data_7HDP
# 
_entry.id   7HDP 
# 
_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   7HDP         pdb_00007hdp 10.2210/pdb7hdp/pdb 
WWPDB D_1001407343 ?            ?                   
# 
_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                        7HDP 
_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-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' 232.282   1   ?                      ? 
? ?                                                                                    
4 non-polymer syn 'CHLORIDE ION'                                                           35.453    1   ?                      ? 
? ?                                                                                    
5 water       nat water                                                                    18.015    423 ?                      ? 
? ?                                                                                    
# 
_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-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' A1A8W 
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 
A1A8W non-polymer         . '(2S)-2-cyclobutyl-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' ? 'C12 H16 N4 O'   232.282 
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 A1A8W 1   202 201  A1A8W LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 105  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 15   HOH   HOH A . 
F 5 HOH   4   304 1289 HOH   HOH A . 
F 5 HOH   5   305 405  HOH   HOH A . 
F 5 HOH   6   306 625  HOH   HOH A . 
F 5 HOH   7   307 196  HOH   HOH A . 
F 5 HOH   8   308 493  HOH   HOH A . 
F 5 HOH   9   309 247  HOH   HOH A . 
F 5 HOH   10  310 153  HOH   HOH A . 
F 5 HOH   11  311 229  HOH   HOH A . 
F 5 HOH   12  312 109  HOH   HOH A . 
F 5 HOH   13  313 209  HOH   HOH A . 
F 5 HOH   14  314 6    HOH   HOH A . 
F 5 HOH   15  315 278  HOH   HOH A . 
F 5 HOH   16  316 281  HOH   HOH A . 
F 5 HOH   17  317 661  HOH   HOH A . 
F 5 HOH   18  318 7    HOH   HOH A . 
F 5 HOH   19  319 136  HOH   HOH A . 
F 5 HOH   20  320 1301 HOH   HOH A . 
F 5 HOH   21  321 124  HOH   HOH A . 
F 5 HOH   22  322 76   HOH   HOH A . 
F 5 HOH   23  323 1275 HOH   HOH A . 
F 5 HOH   24  324 192  HOH   HOH A . 
F 5 HOH   25  325 10   HOH   HOH A . 
F 5 HOH   26  326 1295 HOH   HOH A . 
F 5 HOH   27  327 337  HOH   HOH A . 
F 5 HOH   28  328 15   HOH   HOH A . 
F 5 HOH   29  329 225  HOH   HOH A . 
F 5 HOH   30  330 236  HOH   HOH A . 
F 5 HOH   31  331 18   HOH   HOH A . 
F 5 HOH   32  332 8    HOH   HOH A . 
F 5 HOH   33  333 140  HOH   HOH A . 
F 5 HOH   34  334 164  HOH   HOH A . 
F 5 HOH   35  335 21   HOH   HOH A . 
F 5 HOH   36  336 630  HOH   HOH A . 
F 5 HOH   37  337 86   HOH   HOH A . 
F 5 HOH   38  338 469  HOH   HOH A . 
F 5 HOH   39  339 151  HOH   HOH A . 
F 5 HOH   40  340 17   HOH   HOH A . 
F 5 HOH   41  341 1283 HOH   HOH A . 
F 5 HOH   42  342 320  HOH   HOH A . 
F 5 HOH   43  343 662  HOH   HOH A . 
F 5 HOH   44  344 165  HOH   HOH A . 
F 5 HOH   45  345 1300 HOH   HOH A . 
F 5 HOH   46  346 296  HOH   HOH A . 
F 5 HOH   47  347 393  HOH   HOH A . 
F 5 HOH   48  348 964  HOH   HOH A . 
F 5 HOH   49  349 241  HOH   HOH A . 
F 5 HOH   50  350 155  HOH   HOH A . 
F 5 HOH   51  351 33   HOH   HOH A . 
F 5 HOH   52  352 93   HOH   HOH A . 
F 5 HOH   53  353 396  HOH   HOH A . 
F 5 HOH   54  354 42   HOH   HOH A . 
F 5 HOH   55  355 57   HOH   HOH A . 
F 5 HOH   56  356 39   HOH   HOH A . 
F 5 HOH   57  357 92   HOH   HOH A . 
F 5 HOH   58  358 354  HOH   HOH A . 
F 5 HOH   59  359 139  HOH   HOH A . 
F 5 HOH   60  360 66   HOH   HOH A . 
F 5 HOH   61  361 409  HOH   HOH A . 
F 5 HOH   62  362 169  HOH   HOH A . 
F 5 HOH   63  363 5    HOH   HOH A . 
F 5 HOH   64  364 2    HOH   HOH A . 
F 5 HOH   65  365 36   HOH   HOH A . 
F 5 HOH   66  366 102  HOH   HOH A . 
F 5 HOH   67  367 45   HOH   HOH A . 
F 5 HOH   68  368 19   HOH   HOH A . 
F 5 HOH   69  369 26   HOH   HOH A . 
F 5 HOH   70  370 159  HOH   HOH A . 
F 5 HOH   71  371 81   HOH   HOH A . 
F 5 HOH   72  372 162  HOH   HOH A . 
F 5 HOH   73  373 138  HOH   HOH A . 
F 5 HOH   74  374 46   HOH   HOH A . 
F 5 HOH   75  375 1290 HOH   HOH A . 
F 5 HOH   76  376 1310 HOH   HOH A . 
F 5 HOH   77  377 115  HOH   HOH A . 
F 5 HOH   78  378 4    HOH   HOH A . 
F 5 HOH   79  379 218  HOH   HOH A . 
F 5 HOH   80  380 186  HOH   HOH A . 
F 5 HOH   81  381 56   HOH   HOH A . 
F 5 HOH   82  382 1308 HOH   HOH A . 
F 5 HOH   83  383 35   HOH   HOH A . 
F 5 HOH   84  384 49   HOH   HOH A . 
F 5 HOH   85  385 939  HOH   HOH A . 
F 5 HOH   86  386 27   HOH   HOH A . 
F 5 HOH   87  387 366  HOH   HOH A . 
F 5 HOH   88  388 140  HOH   HOH A . 
F 5 HOH   89  389 70   HOH   HOH A . 
F 5 HOH   90  390 134  HOH   HOH A . 
F 5 HOH   91  391 154  HOH   HOH A . 
F 5 HOH   92  392 6    HOH   HOH A . 
F 5 HOH   93  393 85   HOH   HOH A . 
F 5 HOH   94  394 58   HOH   HOH A . 
F 5 HOH   95  395 34   HOH   HOH A . 
F 5 HOH   96  396 116  HOH   HOH A . 
F 5 HOH   97  397 461  HOH   HOH A . 
F 5 HOH   98  398 83   HOH   HOH A . 
F 5 HOH   99  399 74   HOH   HOH A . 
F 5 HOH   100 400 148  HOH   HOH A . 
F 5 HOH   101 401 96   HOH   HOH A . 
F 5 HOH   102 402 67   HOH   HOH A . 
F 5 HOH   103 403 12   HOH   HOH A . 
F 5 HOH   104 404 132  HOH   HOH A . 
F 5 HOH   105 405 78   HOH   HOH A . 
F 5 HOH   106 406 351  HOH   HOH A . 
F 5 HOH   107 407 121  HOH   HOH A . 
F 5 HOH   108 408 199  HOH   HOH A . 
F 5 HOH   109 409 1315 HOH   HOH A . 
F 5 HOH   110 410 303  HOH   HOH A . 
F 5 HOH   111 411 195  HOH   HOH A . 
F 5 HOH   112 412 3    HOH   HOH A . 
F 5 HOH   113 413 68   HOH   HOH A . 
F 5 HOH   114 414 1313 HOH   HOH A . 
F 5 HOH   115 415 25   HOH   HOH A . 
F 5 HOH   116 416 123  HOH   HOH A . 
F 5 HOH   117 417 53   HOH   HOH A . 
F 5 HOH   118 418 122  HOH   HOH A . 
F 5 HOH   119 419 1068 HOH   HOH A . 
F 5 HOH   120 420 125  HOH   HOH A . 
F 5 HOH   121 421 333  HOH   HOH A . 
F 5 HOH   122 422 156  HOH   HOH A . 
F 5 HOH   123 423 95   HOH   HOH A . 
F 5 HOH   124 424 1279 HOH   HOH A . 
F 5 HOH   125 425 4    HOH   HOH A . 
F 5 HOH   126 426 24   HOH   HOH A . 
F 5 HOH   127 427 51   HOH   HOH A . 
F 5 HOH   128 428 582  HOH   HOH A . 
F 5 HOH   129 429 397  HOH   HOH A . 
F 5 HOH   130 430 381  HOH   HOH A . 
F 5 HOH   131 431 1309 HOH   HOH A . 
F 5 HOH   132 432 7    HOH   HOH A . 
F 5 HOH   133 433 1296 HOH   HOH A . 
F 5 HOH   134 434 16   HOH   HOH A . 
F 5 HOH   135 435 1222 HOH   HOH A . 
F 5 HOH   136 436 71   HOH   HOH A . 
F 5 HOH   137 437 73   HOH   HOH A . 
F 5 HOH   138 438 1286 HOH   HOH A . 
F 5 HOH   139 439 1094 HOH   HOH A . 
F 5 HOH   140 440 212  HOH   HOH A . 
F 5 HOH   141 441 1189 HOH   HOH A . 
F 5 HOH   142 442 40   HOH   HOH A . 
F 5 HOH   143 443 80   HOH   HOH A . 
F 5 HOH   144 444 94   HOH   HOH A . 
F 5 HOH   145 445 1238 HOH   HOH A . 
F 5 HOH   146 446 8    HOH   HOH A . 
F 5 HOH   147 447 952  HOH   HOH A . 
F 5 HOH   148 448 79   HOH   HOH A . 
F 5 HOH   149 449 944  HOH   HOH A . 
F 5 HOH   150 450 97   HOH   HOH A . 
F 5 HOH   151 451 104  HOH   HOH A . 
F 5 HOH   152 452 576  HOH   HOH A . 
F 5 HOH   153 453 188  HOH   HOH A . 
F 5 HOH   154 454 1119 HOH   HOH A . 
F 5 HOH   155 455 330  HOH   HOH A . 
F 5 HOH   156 456 107  HOH   HOH A . 
F 5 HOH   157 457 509  HOH   HOH A . 
F 5 HOH   158 458 1134 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   162 462 756  HOH   HOH A . 
F 5 HOH   163 463 361  HOH   HOH A . 
F 5 HOH   164 464 126  HOH   HOH A . 
F 5 HOH   165 465 63   HOH   HOH A . 
F 5 HOH   166 466 319  HOH   HOH A . 
F 5 HOH   167 467 556  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 1307 HOH   HOH A . 
F 5 HOH   171 471 250  HOH   HOH A . 
F 5 HOH   172 472 342  HOH   HOH A . 
F 5 HOH   173 473 267  HOH   HOH A . 
F 5 HOH   174 474 1276 HOH   HOH A . 
F 5 HOH   175 475 370  HOH   HOH A . 
F 5 HOH   176 476 3    HOH   HOH A . 
F 5 HOH   177 477 224  HOH   HOH A . 
F 5 HOH   178 478 1306 HOH   HOH A . 
F 5 HOH   179 479 1287 HOH   HOH A . 
F 5 HOH   180 480 326  HOH   HOH A . 
F 5 HOH   181 481 695  HOH   HOH A . 
F 5 HOH   182 482 135  HOH   HOH A . 
F 5 HOH   183 483 5    HOH   HOH A . 
F 5 HOH   184 484 202  HOH   HOH A . 
F 5 HOH   185 485 674  HOH   HOH A . 
F 5 HOH   186 486 2    HOH   HOH A . 
F 5 HOH   187 487 919  HOH   HOH A . 
F 5 HOH   188 488 318  HOH   HOH A . 
F 5 HOH   189 489 521  HOH   HOH A . 
F 5 HOH   190 490 309  HOH   HOH A . 
F 5 HOH   191 491 1299 HOH   HOH A . 
F 5 HOH   192 492 11   HOH   HOH A . 
F 5 HOH   193 493 331  HOH   HOH A . 
F 5 HOH   194 494 711  HOH   HOH A . 
F 5 HOH   195 495 805  HOH   HOH A . 
F 5 HOH   196 496 1314 HOH   HOH A . 
F 5 HOH   197 497 315  HOH   HOH A . 
F 5 HOH   198 498 941  HOH   HOH A . 
F 5 HOH   199 499 356  HOH   HOH A . 
F 5 HOH   200 500 263  HOH   HOH A . 
F 5 HOH   201 501 152  HOH   HOH A . 
F 5 HOH   202 502 208  HOH   HOH A . 
F 5 HOH   203 503 1071 HOH   HOH A . 
F 5 HOH   204 504 1284 HOH   HOH A . 
F 5 HOH   205 505 180  HOH   HOH A . 
F 5 HOH   206 506 350  HOH   HOH A . 
F 5 HOH   207 507 14   HOH   HOH A . 
F 5 HOH   208 508 363  HOH   HOH A . 
F 5 HOH   209 509 371  HOH   HOH A . 
F 5 HOH   210 510 313  HOH   HOH A . 
F 5 HOH   211 511 9    HOH   HOH A . 
F 5 HOH   212 512 12   HOH   HOH A . 
F 5 HOH   213 513 185  HOH   HOH A . 
F 5 HOH   214 514 429  HOH   HOH A . 
F 5 HOH   215 515 70   HOH   HOH A . 
F 5 HOH   216 516 376  HOH   HOH A . 
F 5 HOH   217 517 772  HOH   HOH A . 
F 5 HOH   218 518 13   HOH   HOH A . 
F 5 HOH   219 519 1074 HOH   HOH A . 
F 5 HOH   220 520 346  HOH   HOH A . 
F 5 HOH   221 521 1292 HOH   HOH A . 
F 5 HOH   222 522 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   203 900  HOH   HOH B . 
G 5 HOH   4   204 240  HOH   HOH B . 
G 5 HOH   5   205 364  HOH   HOH B . 
G 5 HOH   6   206 358  HOH   HOH B . 
G 5 HOH   7   207 531  HOH   HOH B . 
G 5 HOH   8   208 758  HOH   HOH B . 
G 5 HOH   9   209 1249 HOH   HOH B . 
G 5 HOH   10  210 398  HOH   HOH B . 
G 5 HOH   11  211 50   HOH   HOH B . 
G 5 HOH   12  212 654  HOH   HOH B . 
G 5 HOH   13  213 120  HOH   HOH B . 
G 5 HOH   14  214 452  HOH   HOH B . 
G 5 HOH   15  215 264  HOH   HOH B . 
G 5 HOH   16  216 743  HOH   HOH B . 
G 5 HOH   17  217 232  HOH   HOH B . 
G 5 HOH   18  218 353  HOH   HOH B . 
G 5 HOH   19  219 1140 HOH   HOH B . 
G 5 HOH   20  220 332  HOH   HOH B . 
G 5 HOH   21  221 444  HOH   HOH B . 
G 5 HOH   22  222 205  HOH   HOH B . 
G 5 HOH   23  223 343  HOH   HOH B . 
G 5 HOH   24  224 131  HOH   HOH B . 
G 5 HOH   25  225 82   HOH   HOH B . 
G 5 HOH   26  226 172  HOH   HOH B . 
G 5 HOH   27  227 60   HOH   HOH B . 
G 5 HOH   28  228 54   HOH   HOH B . 
G 5 HOH   29  229 723  HOH   HOH B . 
G 5 HOH   30  230 75   HOH   HOH B . 
G 5 HOH   31  231 1278 HOH   HOH B . 
G 5 HOH   32  232 276  HOH   HOH B . 
G 5 HOH   33  233 1312 HOH   HOH B . 
G 5 HOH   34  234 282  HOH   HOH B . 
G 5 HOH   35  235 110  HOH   HOH B . 
G 5 HOH   36  236 127  HOH   HOH B . 
G 5 HOH   37  237 166  HOH   HOH B . 
G 5 HOH   38  238 272  HOH   HOH B . 
G 5 HOH   39  239 1    HOH   HOH B . 
G 5 HOH   40  240 325  HOH   HOH B . 
G 5 HOH   41  241 30   HOH   HOH B . 
G 5 HOH   42  242 69   HOH   HOH B . 
G 5 HOH   43  243 128  HOH   HOH B . 
G 5 HOH   44  244 300  HOH   HOH B . 
G 5 HOH   45  245 133  HOH   HOH B . 
G 5 HOH   46  246 9    HOH   HOH B . 
G 5 HOH   47  247 231  HOH   HOH B . 
G 5 HOH   48  248 129  HOH   HOH B . 
G 5 HOH   49  249 41   HOH   HOH B . 
G 5 HOH   50  250 14   HOH   HOH B . 
G 5 HOH   51  251 144  HOH   HOH B . 
G 5 HOH   52  252 271  HOH   HOH B . 
G 5 HOH   53  253 181  HOH   HOH B . 
G 5 HOH   54  254 31   HOH   HOH B . 
G 5 HOH   55  255 143  HOH   HOH B . 
G 5 HOH   56  256 52   HOH   HOH B . 
G 5 HOH   57  257 72   HOH   HOH B . 
G 5 HOH   58  258 391  HOH   HOH B . 
G 5 HOH   59  259 347  HOH   HOH B . 
G 5 HOH   60  260 221  HOH   HOH B . 
G 5 HOH   61  261 47   HOH   HOH B . 
G 5 HOH   62  262 62   HOH   HOH B . 
G 5 HOH   63  263 10   HOH   HOH B . 
G 5 HOH   64  264 150  HOH   HOH B . 
G 5 HOH   65  265 103  HOH   HOH B . 
G 5 HOH   66  266 1277 HOH   HOH B . 
G 5 HOH   67  267 252  HOH   HOH B . 
G 5 HOH   68  268 59   HOH   HOH B . 
G 5 HOH   69  269 243  HOH   HOH B . 
G 5 HOH   70  270 61   HOH   HOH B . 
G 5 HOH   71  271 302  HOH   HOH B . 
G 5 HOH   72  272 287  HOH   HOH B . 
G 5 HOH   73  273 117  HOH   HOH B . 
G 5 HOH   74  274 11   HOH   HOH B . 
G 5 HOH   75  275 242  HOH   HOH B . 
G 5 HOH   76  276 114  HOH   HOH B . 
G 5 HOH   77  277 20   HOH   HOH B . 
G 5 HOH   78  278 84   HOH   HOH B . 
G 5 HOH   79  279 77   HOH   HOH B . 
G 5 HOH   80  280 43   HOH   HOH B . 
G 5 HOH   81  281 175  HOH   HOH B . 
G 5 HOH   82  282 147  HOH   HOH B . 
G 5 HOH   83  283 1106 HOH   HOH B . 
G 5 HOH   84  284 216  HOH   HOH B . 
G 5 HOH   85  285 387  HOH   HOH B . 
G 5 HOH   86  286 22   HOH   HOH B . 
G 5 HOH   87  287 235  HOH   HOH B . 
G 5 HOH   88  288 1305 HOH   HOH B . 
G 5 HOH   89  289 99   HOH   HOH B . 
G 5 HOH   90  290 416  HOH   HOH B . 
G 5 HOH   91  291 89   HOH   HOH B . 
G 5 HOH   92  292 1066 HOH   HOH B . 
G 5 HOH   93  293 220  HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 106  HOH   HOH B . 
G 5 HOH   96  296 13   HOH   HOH B . 
G 5 HOH   97  297 88   HOH   HOH B . 
G 5 HOH   98  298 160  HOH   HOH B . 
G 5 HOH   99  299 112  HOH   HOH B . 
G 5 HOH   100 300 32   HOH   HOH B . 
G 5 HOH   101 301 297  HOH   HOH B . 
G 5 HOH   102 302 341  HOH   HOH B . 
G 5 HOH   103 303 311  HOH   HOH B . 
G 5 HOH   104 304 316  HOH   HOH B . 
G 5 HOH   105 305 299  HOH   HOH B . 
G 5 HOH   106 306 38   HOH   HOH B . 
G 5 HOH   107 307 142  HOH   HOH B . 
G 5 HOH   108 308 1285 HOH   HOH B . 
G 5 HOH   109 309 101  HOH   HOH B . 
G 5 HOH   110 310 118  HOH   HOH B . 
G 5 HOH   111 311 635  HOH   HOH B . 
G 5 HOH   112 312 215  HOH   HOH B . 
G 5 HOH   113 313 37   HOH   HOH B . 
G 5 HOH   114 314 704  HOH   HOH B . 
G 5 HOH   115 315 177  HOH   HOH B . 
G 5 HOH   116 316 23   HOH   HOH B . 
G 5 HOH   117 317 170  HOH   HOH B . 
G 5 HOH   118 318 48   HOH   HOH B . 
G 5 HOH   119 319 445  HOH   HOH B . 
G 5 HOH   120 320 91   HOH   HOH B . 
G 5 HOH   121 321 1274 HOH   HOH B . 
G 5 HOH   122 322 44   HOH   HOH B . 
G 5 HOH   123 323 28   HOH   HOH B . 
G 5 HOH   124 324 161  HOH   HOH B . 
G 5 HOH   125 325 1291 HOH   HOH B . 
G 5 HOH   126 326 197  HOH   HOH B . 
G 5 HOH   127 327 100  HOH   HOH B . 
G 5 HOH   128 328 1294 HOH   HOH B . 
G 5 HOH   129 329 182  HOH   HOH B . 
G 5 HOH   130 330 29   HOH   HOH B . 
G 5 HOH   131 331 55   HOH   HOH B . 
G 5 HOH   132 332 1126 HOH   HOH B . 
G 5 HOH   133 333 98   HOH   HOH B . 
G 5 HOH   134 334 717  HOH   HOH B . 
G 5 HOH   135 335 334  HOH   HOH B . 
G 5 HOH   136 336 141  HOH   HOH B . 
G 5 HOH   137 337 207  HOH   HOH B . 
G 5 HOH   138 338 65   HOH   HOH B . 
G 5 HOH   139 339 234  HOH   HOH B . 
G 5 HOH   140 340 1293 HOH   HOH B . 
G 5 HOH   141 341 619  HOH   HOH B . 
G 5 HOH   142 342 339  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 960  HOH   HOH B . 
G 5 HOH   145 345 178  HOH   HOH B . 
G 5 HOH   146 346 90   HOH   HOH B . 
G 5 HOH   147 347 463  HOH   HOH B . 
G 5 HOH   148 348 87   HOH   HOH B . 
G 5 HOH   149 349 1280 HOH   HOH B . 
G 5 HOH   150 350 191  HOH   HOH B . 
G 5 HOH   151 351 623  HOH   HOH B . 
G 5 HOH   152 352 1046 HOH   HOH B . 
G 5 HOH   153 353 335  HOH   HOH B . 
G 5 HOH   154 354 1304 HOH   HOH B . 
G 5 HOH   155 355 304  HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 290  HOH   HOH B . 
G 5 HOH   158 358 541  HOH   HOH B . 
G 5 HOH   159 359 1077 HOH   HOH B . 
G 5 HOH   160 360 479  HOH   HOH B . 
G 5 HOH   161 361 389  HOH   HOH B . 
G 5 HOH   162 362 718  HOH   HOH B . 
G 5 HOH   163 363 1072 HOH   HOH B . 
G 5 HOH   164 364 283  HOH   HOH B . 
G 5 HOH   165 365 1316 HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 291  HOH   HOH B . 
G 5 HOH   168 368 340  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 615  HOH   HOH B . 
G 5 HOH   171 371 1303 HOH   HOH B . 
G 5 HOH   172 372 667  HOH   HOH B . 
G 5 HOH   173 373 190  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 1173 HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 183  HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 1163 HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 176  HOH   HOH B . 
G 5 HOH   184 384 424  HOH   HOH B . 
G 5 HOH   185 385 981  HOH   HOH B . 
G 5 HOH   186 386 491  HOH   HOH B . 
G 5 HOH   187 387 470  HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 1298 HOH   HOH B . 
G 5 HOH   190 390 265  HOH   HOH B . 
G 5 HOH   191 391 184  HOH   HOH B . 
G 5 HOH   192 392 360  HOH   HOH B . 
G 5 HOH   193 393 410  HOH   HOH B . 
G 5 HOH   194 394 355  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           7HDP 
_cell.length_a           88.806 
_cell.length_b           88.806 
_cell.length_c           39.518 
_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                         7HDP 
_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          7HDP 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.71 
_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                     7HDP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165516 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.100 
_reflns.B_iso_Wilson_estimate        11.750 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1053476 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33755 7519 ? 1.062 ? ? ? 4.500 ? 0.900  ? ? ? ? ? ? 91.500 1.200 0.545 0.697 
1 2 5.480 44.400 ? 7501  1096 ? 0.027 ? ? ? 6.800 ? 52.500 ? ? ? ? ? ? 99.900 0.029 0.011 0.999 
# 
_refine.entry_id                                 7HDP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4900 
_refine.ls_number_reflns_obs                     165434 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1455 
_refine.ls_R_factor_R_work                       0.1448 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1590 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7976 
_refine.ls_number_reflns_R_work                  157458 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.7859 
_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                            0.1000 
_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                                67.730 
_refine.B_iso_min                                7.950 
_refine.pdbx_overall_phase_error                 18.2100 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.number_atoms_solvent             423 
_refine_hist.number_atoms_total               3006 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.91 
_refine_hist.pdbx_B_iso_mean_solvent          29.78 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 89.0000  4727 . 0.4014 0.3741 . 243 0.0000 4970 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 97.0000  5113 . 0.3236 0.3263 . 227 0.0000 5340 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5246 . 0.2829 0.2693 . 248 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5179 . 0.2468 0.2503 . 282 0.0000 5461 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5201 . 0.2305 0.2463 . 321 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5252 . 0.2137 0.2432 . 249 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5285 . 0.1942 0.2185 . 266 0.0000 5551 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5210 . 0.1753 0.1889 . 257 0.0000 5467 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5252 . 0.1681 0.1850 . 278 0.0000 5530 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5273 . 0.1509 0.1665 . 237 0.0000 5510 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5277 . 0.1438 0.1575 . 260 0.0000 5537 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5273 . 0.1345 0.1576 . 268 0.0000 5541 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5194 . 0.1286 0.1674 . 293 0.0000 5487 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5283 . 0.1244 0.1497 . 235 0.0000 5518 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5233 . 0.1256 0.1347 . 260 0.0000 5493 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5278 . 0.1249 0.1491 . 275 0.0000 5553 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5250 . 0.1256 0.1475 . 290 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5236 . 0.1319 0.1451 . 273 0.0000 5509 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5294 . 0.1285 0.1618 . 245 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5223 . 0.1281 0.1579 . 266 0.0000 5489 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5335 . 0.1232 0.1285 . 253 0.0000 5588 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5225 . 0.1181 0.1239 . 280 0.0000 5505 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5289 . 0.1182 0.1345 . 261 0.0000 5550 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5318 . 0.1256 0.1511 . 272 0.0000 5590 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5284 . 0.1351 0.1397 . 250 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5276 . 0.1343 0.1359 . 281 0.0000 5557 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5306 . 0.1387 0.1440 . 285 0.0000 5591 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5311 . 0.1372 0.1449 . 291 0.0000 5602 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5345 . 0.1491 0.1672 . 260 0.0000 5605 . 'X-RAY DIFFRACTION' 
3.1100 44.4000 30 100.0000 5490 . 0.1505 0.1707 . 270 0.0000 5760 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDP 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003638' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDP 
_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 7HDP A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDP 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 7HDP SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDP MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDP SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDP 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                   7HDP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    167 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.60 
# 
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  ? ? 55.84   -133.35 
2 1 SER A 128 ? B 70.32   -8.12   
3 1 ASP A 157 ? B 177.90  153.27  
4 1 PHE A 168 ? B -148.43 -49.31  
5 1 HIS B 86  ? ? 57.34   -127.86 
# 
_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 520 ? 5.89 . 
2 1 O ? A HOH 521 ? 5.95 . 
3 1 O ? A HOH 522 ? 7.55 . 
4 1 O ? B HOH 401 ? 6.33 . 
# 
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 
A1A8W N2   N  Y N 1   
A1A8W C3   C  Y N 2   
A1A8W C6   C  Y N 3   
A1A8W C9   C  N N 4   
A1A8W C12  C  N N 5   
A1A8W C1   C  N N 6   
A1A8W C10  C  N N 7   
A1A8W C11  C  N N 8   
A1A8W C2   C  N S 9   
A1A8W C4   C  Y N 10  
A1A8W C5   C  Y N 11  
A1A8W C7   C  Y N 12  
A1A8W C8   C  Y N 13  
A1A8W N1   N  N N 14  
A1A8W N3   N  Y N 15  
A1A8W N4   N  Y N 16  
A1A8W O1   O  N N 17  
A1A8W H10  H  N N 18  
A1A8W H15  H  N N 19  
A1A8W H16  H  N N 20  
A1A8W H4   H  N N 21  
A1A8W H3   H  N N 22  
A1A8W H11  H  N N 23  
A1A8W H12  H  N N 24  
A1A8W H14  H  N N 25  
A1A8W H13  H  N N 26  
A1A8W H1   H  N N 27  
A1A8W H6   H  N N 28  
A1A8W H7   H  N N 29  
A1A8W H8   H  N N 30  
A1A8W H5   H  N N 31  
A1A8W H9   H  N N 32  
A1A8W H2   H  N N 33  
ALA   N    N  N N 34  
ALA   CA   C  N S 35  
ALA   C    C  N N 36  
ALA   O    O  N N 37  
ALA   CB   C  N N 38  
ALA   OXT  O  N N 39  
ALA   H    H  N N 40  
ALA   H2   H  N N 41  
ALA   HA   H  N N 42  
ALA   HB1  H  N N 43  
ALA   HB2  H  N N 44  
ALA   HB3  H  N N 45  
ALA   HXT  H  N N 46  
ARG   N    N  N N 47  
ARG   CA   C  N S 48  
ARG   C    C  N N 49  
ARG   O    O  N N 50  
ARG   CB   C  N N 51  
ARG   CG   C  N N 52  
ARG   CD   C  N N 53  
ARG   NE   N  N N 54  
ARG   CZ   C  N N 55  
ARG   NH1  N  N N 56  
ARG   NH2  N  N N 57  
ARG   OXT  O  N N 58  
ARG   H    H  N N 59  
ARG   H2   H  N N 60  
ARG   HA   H  N N 61  
ARG   HB2  H  N N 62  
ARG   HB3  H  N N 63  
ARG   HG2  H  N N 64  
ARG   HG3  H  N N 65  
ARG   HD2  H  N N 66  
ARG   HD3  H  N N 67  
ARG   HE   H  N N 68  
ARG   HH11 H  N N 69  
ARG   HH12 H  N N 70  
ARG   HH21 H  N N 71  
ARG   HH22 H  N N 72  
ARG   HXT  H  N N 73  
ASN   N    N  N N 74  
ASN   CA   C  N S 75  
ASN   C    C  N N 76  
ASN   O    O  N N 77  
ASN   CB   C  N N 78  
ASN   CG   C  N N 79  
ASN   OD1  O  N N 80  
ASN   ND2  N  N N 81  
ASN   OXT  O  N N 82  
ASN   H    H  N N 83  
ASN   H2   H  N N 84  
ASN   HA   H  N N 85  
ASN   HB2  H  N N 86  
ASN   HB3  H  N N 87  
ASN   HD21 H  N N 88  
ASN   HD22 H  N N 89  
ASN   HXT  H  N N 90  
ASP   N    N  N N 91  
ASP   CA   C  N S 92  
ASP   C    C  N N 93  
ASP   O    O  N N 94  
ASP   CB   C  N N 95  
ASP   CG   C  N N 96  
ASP   OD1  O  N N 97  
ASP   OD2  O  N N 98  
ASP   OXT  O  N N 99  
ASP   H    H  N N 100 
ASP   H2   H  N N 101 
ASP   HA   H  N N 102 
ASP   HB2  H  N N 103 
ASP   HB3  H  N N 104 
ASP   HD2  H  N N 105 
ASP   HXT  H  N N 106 
CL    CL   CL N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
GLN   N    N  N N 122 
GLN   CA   C  N S 123 
GLN   C    C  N N 124 
GLN   O    O  N N 125 
GLN   CB   C  N N 126 
GLN   CG   C  N N 127 
GLN   CD   C  N N 128 
GLN   OE1  O  N N 129 
GLN   NE2  N  N N 130 
GLN   OXT  O  N N 131 
GLN   H    H  N N 132 
GLN   H2   H  N N 133 
GLN   HA   H  N N 134 
GLN   HB2  H  N N 135 
GLN   HB3  H  N N 136 
GLN   HG2  H  N N 137 
GLN   HG3  H  N N 138 
GLN   HE21 H  N N 139 
GLN   HE22 H  N N 140 
GLN   HXT  H  N N 141 
GLU   N    N  N N 142 
GLU   CA   C  N S 143 
GLU   C    C  N N 144 
GLU   O    O  N N 145 
GLU   CB   C  N N 146 
GLU   CG   C  N N 147 
GLU   CD   C  N N 148 
GLU   OE1  O  N N 149 
GLU   OE2  O  N N 150 
GLU   OXT  O  N N 151 
GLU   H    H  N N 152 
GLU   H2   H  N N 153 
GLU   HA   H  N N 154 
GLU   HB2  H  N N 155 
GLU   HB3  H  N N 156 
GLU   HG2  H  N N 157 
GLU   HG3  H  N N 158 
GLU   HE2  H  N N 159 
GLU   HXT  H  N N 160 
GLY   N    N  N N 161 
GLY   CA   C  N N 162 
GLY   C    C  N N 163 
GLY   O    O  N N 164 
GLY   OXT  O  N N 165 
GLY   H    H  N N 166 
GLY   H2   H  N N 167 
GLY   HA2  H  N N 168 
GLY   HA3  H  N N 169 
GLY   HXT  H  N N 170 
HIS   N    N  N N 171 
HIS   CA   C  N S 172 
HIS   C    C  N N 173 
HIS   O    O  N N 174 
HIS   CB   C  N N 175 
HIS   CG   C  Y N 176 
HIS   ND1  N  Y N 177 
HIS   CD2  C  Y N 178 
HIS   CE1  C  Y N 179 
HIS   NE2  N  Y N 180 
HIS   OXT  O  N N 181 
HIS   H    H  N N 182 
HIS   H2   H  N N 183 
HIS   HA   H  N N 184 
HIS   HB2  H  N N 185 
HIS   HB3  H  N N 186 
HIS   HD1  H  N N 187 
HIS   HD2  H  N N 188 
HIS   HE1  H  N N 189 
HIS   HE2  H  N N 190 
HIS   HXT  H  N N 191 
HOH   O    O  N N 192 
HOH   H1   H  N N 193 
HOH   H2   H  N N 194 
ILE   N    N  N N 195 
ILE   CA   C  N S 196 
ILE   C    C  N N 197 
ILE   O    O  N N 198 
ILE   CB   C  N S 199 
ILE   CG1  C  N N 200 
ILE   CG2  C  N N 201 
ILE   CD1  C  N N 202 
ILE   OXT  O  N N 203 
ILE   H    H  N N 204 
ILE   H2   H  N N 205 
ILE   HA   H  N N 206 
ILE   HB   H  N N 207 
ILE   HG12 H  N N 208 
ILE   HG13 H  N N 209 
ILE   HG21 H  N N 210 
ILE   HG22 H  N N 211 
ILE   HG23 H  N N 212 
ILE   HD11 H  N N 213 
ILE   HD12 H  N N 214 
ILE   HD13 H  N N 215 
ILE   HXT  H  N N 216 
LEU   N    N  N N 217 
LEU   CA   C  N S 218 
LEU   C    C  N N 219 
LEU   O    O  N N 220 
LEU   CB   C  N N 221 
LEU   CG   C  N N 222 
LEU   CD1  C  N N 223 
LEU   CD2  C  N N 224 
LEU   OXT  O  N N 225 
LEU   H    H  N N 226 
LEU   H2   H  N N 227 
LEU   HA   H  N N 228 
LEU   HB2  H  N N 229 
LEU   HB3  H  N N 230 
LEU   HG   H  N N 231 
LEU   HD11 H  N N 232 
LEU   HD12 H  N N 233 
LEU   HD13 H  N N 234 
LEU   HD21 H  N N 235 
LEU   HD22 H  N N 236 
LEU   HD23 H  N N 237 
LEU   HXT  H  N N 238 
LYS   N    N  N N 239 
LYS   CA   C  N S 240 
LYS   C    C  N N 241 
LYS   O    O  N N 242 
LYS   CB   C  N N 243 
LYS   CG   C  N N 244 
LYS   CD   C  N N 245 
LYS   CE   C  N N 246 
LYS   NZ   N  N N 247 
LYS   OXT  O  N N 248 
LYS   H    H  N N 249 
LYS   H2   H  N N 250 
LYS   HA   H  N N 251 
LYS   HB2  H  N N 252 
LYS   HB3  H  N N 253 
LYS   HG2  H  N N 254 
LYS   HG3  H  N N 255 
LYS   HD2  H  N N 256 
LYS   HD3  H  N N 257 
LYS   HE2  H  N N 258 
LYS   HE3  H  N N 259 
LYS   HZ1  H  N N 260 
LYS   HZ2  H  N N 261 
LYS   HZ3  H  N N 262 
LYS   HXT  H  N N 263 
MET   N    N  N N 264 
MET   CA   C  N S 265 
MET   C    C  N N 266 
MET   O    O  N N 267 
MET   CB   C  N N 268 
MET   CG   C  N N 269 
MET   SD   S  N N 270 
MET   CE   C  N N 271 
MET   OXT  O  N N 272 
MET   H    H  N N 273 
MET   H2   H  N N 274 
MET   HA   H  N N 275 
MET   HB2  H  N N 276 
MET   HB3  H  N N 277 
MET   HG2  H  N N 278 
MET   HG3  H  N N 279 
MET   HE1  H  N N 280 
MET   HE2  H  N N 281 
MET   HE3  H  N N 282 
MET   HXT  H  N N 283 
PHE   N    N  N N 284 
PHE   CA   C  N S 285 
PHE   C    C  N N 286 
PHE   O    O  N N 287 
PHE   CB   C  N N 288 
PHE   CG   C  Y N 289 
PHE   CD1  C  Y N 290 
PHE   CD2  C  Y N 291 
PHE   CE1  C  Y N 292 
PHE   CE2  C  Y N 293 
PHE   CZ   C  Y N 294 
PHE   OXT  O  N N 295 
PHE   H    H  N N 296 
PHE   H2   H  N N 297 
PHE   HA   H  N N 298 
PHE   HB2  H  N N 299 
PHE   HB3  H  N N 300 
PHE   HD1  H  N N 301 
PHE   HD2  H  N N 302 
PHE   HE1  H  N N 303 
PHE   HE2  H  N N 304 
PHE   HZ   H  N N 305 
PHE   HXT  H  N N 306 
PRO   N    N  N N 307 
PRO   CA   C  N S 308 
PRO   C    C  N N 309 
PRO   O    O  N N 310 
PRO   CB   C  N N 311 
PRO   CG   C  N N 312 
PRO   CD   C  N N 313 
PRO   OXT  O  N N 314 
PRO   H    H  N N 315 
PRO   HA   H  N N 316 
PRO   HB2  H  N N 317 
PRO   HB3  H  N N 318 
PRO   HG2  H  N N 319 
PRO   HG3  H  N N 320 
PRO   HD2  H  N N 321 
PRO   HD3  H  N N 322 
PRO   HXT  H  N N 323 
SER   N    N  N N 324 
SER   CA   C  N S 325 
SER   C    C  N N 326 
SER   O    O  N N 327 
SER   CB   C  N N 328 
SER   OG   O  N N 329 
SER   OXT  O  N N 330 
SER   H    H  N N 331 
SER   H2   H  N N 332 
SER   HA   H  N N 333 
SER   HB2  H  N N 334 
SER   HB3  H  N N 335 
SER   HG   H  N N 336 
SER   HXT  H  N N 337 
TFA   C1   C  N N 338 
TFA   C2   C  N N 339 
TFA   O    O  N N 340 
TFA   F1   F  N N 341 
TFA   F2   F  N N 342 
TFA   F3   F  N N 343 
TFA   OXT  O  N N 344 
TFA   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TYR   N    N  N N 363 
TYR   CA   C  N S 364 
TYR   C    C  N N 365 
TYR   O    O  N N 366 
TYR   CB   C  N N 367 
TYR   CG   C  Y N 368 
TYR   CD1  C  Y N 369 
TYR   CD2  C  Y N 370 
TYR   CE1  C  Y N 371 
TYR   CE2  C  Y N 372 
TYR   CZ   C  Y N 373 
TYR   OH   O  N N 374 
TYR   OXT  O  N N 375 
TYR   H    H  N N 376 
TYR   H2   H  N N 377 
TYR   HA   H  N N 378 
TYR   HB2  H  N N 379 
TYR   HB3  H  N N 380 
TYR   HD1  H  N N 381 
TYR   HD2  H  N N 382 
TYR   HE1  H  N N 383 
TYR   HE2  H  N N 384 
TYR   HH   H  N N 385 
TYR   HXT  H  N N 386 
VAL   N    N  N N 387 
VAL   CA   C  N S 388 
VAL   C    C  N N 389 
VAL   O    O  N N 390 
VAL   CB   C  N N 391 
VAL   CG1  C  N N 392 
VAL   CG2  C  N N 393 
VAL   OXT  O  N N 394 
VAL   H    H  N N 395 
VAL   H2   H  N N 396 
VAL   HA   H  N N 397 
VAL   HB   H  N N 398 
VAL   HG11 H  N N 399 
VAL   HG12 H  N N 400 
VAL   HG13 H  N N 401 
VAL   HG21 H  N N 402 
VAL   HG22 H  N N 403 
VAL   HG23 H  N N 404 
VAL   HXT  H  N N 405 
# 
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 
A1A8W C1  O1   sing N N 1   
A1A8W C1  C2   sing N N 2   
A1A8W C12 C9   sing N N 3   
A1A8W C12 C11  sing N N 4   
A1A8W C9  C2   sing N N 5   
A1A8W C9  C10  sing N N 6   
A1A8W C2  N1   sing N N 7   
A1A8W C11 C10  sing N N 8   
A1A8W N1  C3   sing N N 9   
A1A8W C3  C6   doub Y N 10  
A1A8W C3  N2   sing Y N 11  
A1A8W C7  C6   sing Y N 12  
A1A8W C7  C8   doub Y N 13  
A1A8W C6  C5   sing Y N 14  
A1A8W N2  C4   doub Y N 15  
A1A8W C8  N4   sing Y N 16  
A1A8W C5  N4   sing Y N 17  
A1A8W C5  N3   doub Y N 18  
A1A8W C4  N3   sing Y N 19  
A1A8W C9  H10  sing N N 20  
A1A8W C12 H15  sing N N 21  
A1A8W C12 H16  sing N N 22  
A1A8W C1  H4   sing N N 23  
A1A8W C1  H3   sing N N 24  
A1A8W C10 H11  sing N N 25  
A1A8W C10 H12  sing N N 26  
A1A8W C11 H14  sing N N 27  
A1A8W C11 H13  sing N N 28  
A1A8W C2  H1   sing N N 29  
A1A8W C4  H6   sing N N 30  
A1A8W C7  H7   sing N N 31  
A1A8W C8  H8   sing N N 32  
A1A8W N1  H5   sing N N 33  
A1A8W N4  H9   sing N N 34  
A1A8W O1  H2   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
TFA   C1  C2   sing N N 325 
TFA   C1  O    doub N N 326 
TFA   C1  OXT  sing N N 327 
TFA   C2  F1   sing N N 328 
TFA   C2  F2   sing N N 329 
TFA   C2  F3   sing N N 330 
TFA   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TYR   N   CA   sing N N 348 
TYR   N   H    sing N N 349 
TYR   N   H2   sing N N 350 
TYR   CA  C    sing N N 351 
TYR   CA  CB   sing N N 352 
TYR   CA  HA   sing N N 353 
TYR   C   O    doub N N 354 
TYR   C   OXT  sing N N 355 
TYR   CB  CG   sing N N 356 
TYR   CB  HB2  sing N N 357 
TYR   CB  HB3  sing N N 358 
TYR   CG  CD1  doub Y N 359 
TYR   CG  CD2  sing Y N 360 
TYR   CD1 CE1  sing Y N 361 
TYR   CD1 HD1  sing N N 362 
TYR   CD2 CE2  doub Y N 363 
TYR   CD2 HD2  sing N N 364 
TYR   CE1 CZ   doub Y N 365 
TYR   CE1 HE1  sing N N 366 
TYR   CE2 CZ   sing Y N 367 
TYR   CE2 HE2  sing N N 368 
TYR   CZ  OH   sing N N 369 
TYR   OH  HH   sing N N 370 
TYR   OXT HXT  sing N N 371 
VAL   N   CA   sing N N 372 
VAL   N   H    sing N N 373 
VAL   N   H2   sing N N 374 
VAL   CA  C    sing N N 375 
VAL   CA  CB   sing N N 376 
VAL   CA  HA   sing N N 377 
VAL   C   O    doub N N 378 
VAL   C   OXT  sing N N 379 
VAL   CB  CG1  sing N N 380 
VAL   CB  CG2  sing N N 381 
VAL   CB  HB   sing N N 382 
VAL   CG1 HG11 sing N N 383 
VAL   CG1 HG12 sing N N 384 
VAL   CG1 HG13 sing N N 385 
VAL   CG2 HG21 sing N N 386 
VAL   CG2 HG22 sing N N 387 
VAL   CG2 HG23 sing N N 388 
VAL   OXT HXT  sing N N 389 
# 
_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                    7HDP 
_atom_sites.fract_transf_matrix[1][1]   0.011261 
_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]   0.011261 
_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]   0.025305 
_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    A VAL   A 1 3   ? 19.664 -16.232 22.246  0.74 53.89 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.577 -16.217 22.325  0.26 52.87 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.692 -15.160 22.417  0.74 53.51 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.636 -15.117 22.497  0.26 52.63 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.338 -13.810 22.125  0.74 52.22 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.310 -13.790 22.170  0.26 51.69 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.453 -13.537 22.572  0.74 52.70 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.418 -13.516 22.632  0.26 52.09 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.064 -15.193 23.825  0.74 54.09 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.046 -15.102 23.921  0.26 53.08 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.047 -14.072 23.984  0.74 54.21 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.048 -13.962 24.071  0.26 53.18 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.412 -16.543 24.083  0.74 54.22 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.388 -16.436 24.239  0.26 53.18 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.975 -15.283 21.779  0.74 64.35 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.899 -15.233 21.880  0.26 63.30 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.760 -15.064 24.489  0.74 65.04 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.761 -14.960 24.560  0.26 63.84 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.542 -14.219 24.799  0.74 65.19 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.565 -14.075 24.904  0.26 63.95 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.514 -13.224 24.035  0.74 65.19 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.527 -13.119 24.080  0.26 63.95 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.450 -14.078 23.220  0.74 65.19 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.429 -13.985 23.325  0.26 63.95 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.964 -16.519 24.943  0.74 65.20 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.954 -16.375 25.104  0.26 63.96 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.768 -16.721 23.380  0.74 65.20 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.732 -16.635 23.553  0.26 63.96 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.097 -17.229 24.086  0.74 65.20 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.068 -17.128 24.258  0.26 63.96 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.636 -12.971 21.366  1.00 50.08 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.099 -11.629 21.032  1.00 46.04 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.965 -10.637 21.278  1.00 42.41 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.852 -11.014 21.659  1.00 42.27 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.651 -11.548 19.600  1.00 45.29 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.627 -11.920 18.551  1.00 44.48 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.510 -11.403 18.543  1.00 44.13 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.005 -12.824 17.652  1.00 44.33 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.870 -13.164 21.024  0.74 60.23 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.886 -13.176 20.996  0.26 60.23 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.824 -11.401 21.626  1.00 55.38 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.942 -10.637 19.426  1.00 54.48 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.402 -12.155 19.516  1.00 54.48 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.463 -13.070 17.032  1.00 53.33 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.795 -13.165 17.691  1.00 53.33 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.253 -9.354  21.057  1.00 38.68 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.352 -8.275  21.443  1.00 34.86 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.462 -7.786  20.303  1.00 29.78 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.752 -6.789  20.472  1.00 30.35 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.141 -7.108  22.043  1.00 36.26 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.005 -6.524  21.086  1.00 37.00 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 18.975 -9.084  20.674  1.00 46.55 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.767 -8.605  22.139  1.00 41.98 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.517 -6.434  22.359  1.00 43.65 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.673 -7.434  22.788  1.00 43.65 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.427 -5.883  21.434  1.00 44.54 ?  5   SER   A HG   1 
ATOM   57   N  N    A PHE   A 1 6   ? 16.454 -8.466  19.159  0.74 26.13 ?  6   PHE   A N    1 
ATOM   58   N  N    B PHE   A 1 6   ? 16.511 -8.441  19.145  0.26 27.30 ?  6   PHE   A N    1 
ATOM   59   C  CA   A PHE   A 1 6   ? 15.531 -8.093  18.093  0.74 22.63 ?  6   PHE   A CA   1 
ATOM   60   C  CA   B PHE   A 1 6   ? 15.645 -8.085  18.027  0.26 24.70 ?  6   PHE   A CA   1 
ATOM   61   C  C    A PHE   A 1 6   ? 14.099 -8.450  18.485  0.74 22.40 ?  6   PHE   A C    1 
ATOM   62   C  C    B PHE   A 1 6   ? 14.211 -8.448  18.386  0.26 23.78 ?  6   PHE   A C    1 
ATOM   63   O  O    A PHE   A 1 6   ? 13.849 -9.496  19.088  0.74 23.25 ?  6   PHE   A O    1 
ATOM   64   O  O    B PHE   A 1 6   ? 13.848 -9.629  18.409  0.26 23.36 ?  6   PHE   A O    1 
ATOM   65   C  CB   A PHE   A 1 6   ? 15.913 -8.795  16.792  0.74 20.43 ?  6   PHE   A CB   1 
ATOM   66   C  CB   B PHE   A 1 6   ? 16.096 -8.823  16.770  0.26 23.28 ?  6   PHE   A CB   1 
ATOM   67   C  CG   A PHE   A 1 6   ? 17.193 -8.284  16.181  0.74 18.96 ?  6   PHE   A CG   1 
ATOM   68   C  CG   B PHE   A 1 6   ? 17.371 -8.291  16.177  0.26 22.05 ?  6   PHE   A CG   1 
ATOM   69   C  CD1  A PHE   A 1 6   ? 17.204 -7.111  15.444  0.74 18.46 ?  6   PHE   A CD1  1 
ATOM   70   C  CD1  B PHE   A 1 6   ? 17.402 -7.042  15.581  0.26 21.50 ?  6   PHE   A CD1  1 
ATOM   71   C  CD2  A PHE   A 1 6   ? 18.377 -8.980  16.340  0.74 19.43 ?  6   PHE   A CD2  1 
ATOM   72   C  CD2  B PHE   A 1 6   ? 18.536 -9.043  16.204  0.26 21.74 ?  6   PHE   A CD2  1 
ATOM   73   C  CE1  A PHE   A 1 6   ? 18.377 -6.639  14.880  0.74 18.28 ?  6   PHE   A CE1  1 
ATOM   74   C  CE1  B PHE   A 1 6   ? 18.569 -6.547  15.030  0.26 21.25 ?  6   PHE   A CE1  1 
ATOM   75   C  CE2  A PHE   A 1 6   ? 19.548 -8.517  15.777  0.74 19.32 ?  6   PHE   A CE2  1 
ATOM   76   C  CE2  B PHE   A 1 6   ? 19.707 -8.554  15.653  0.26 21.50 ?  6   PHE   A CE2  1 
ATOM   77   C  CZ   A PHE   A 1 6   ? 19.548 -7.343  15.047  0.74 18.72 ?  6   PHE   A CZ   1 
ATOM   78   C  CZ   B PHE   A 1 6   ? 19.723 -7.304  15.066  0.26 21.32 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 16.968 -9.133  18.979  0.74 31.50 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 17.040 -9.100  18.982  0.26 32.90 ?  6   PHE   A H    1 
ATOM   81   H  HA   A PHE   A 1 6   ? 15.578 -7.139  17.951  0.74 27.29 ?  6   PHE   A HA   1 
ATOM   82   H  HA   B PHE   A 1 6   ? 15.697 -7.131  17.864  0.26 29.78 ?  6   PHE   A HA   1 
ATOM   83   H  HB2  A PHE   A 1 6   ? 16.025 -9.744  16.969  0.74 24.66 ?  6   PHE   A HB2  1 
ATOM   84   H  HB2  B PHE   A 1 6   ? 16.239 -9.757  16.990  0.26 28.08 ?  6   PHE   A HB2  1 
ATOM   85   H  HB3  A PHE   A 1 6   ? 15.200 -8.665  16.148  0.74 24.66 ?  6   PHE   A HB3  1 
ATOM   86   H  HB3  B PHE   A 1 6   ? 15.403 -8.746  16.097  0.26 28.08 ?  6   PHE   A HB3  1 
ATOM   87   H  HD1  A PHE   A 1 6   ? 16.412 -6.635  15.329  0.74 22.29 ?  6   PHE   A HD1  1 
ATOM   88   H  HD1  B PHE   A 1 6   ? 16.628 -6.528  15.555  0.26 25.95 ?  6   PHE   A HD1  1 
ATOM   89   H  HD2  A PHE   A 1 6   ? 18.382 -9.770  16.834  0.74 23.46 ?  6   PHE   A HD2  1 
ATOM   90   H  HD2  B PHE   A 1 6   ? 18.531 -9.885  16.598  0.26 26.22 ?  6   PHE   A HD2  1 
ATOM   91   H  HE1  A PHE   A 1 6   ? 18.370 -5.851  14.387  0.74 22.08 ?  6   PHE   A HE1  1 
ATOM   92   H  HE1  B PHE   A 1 6   ? 18.577 -5.705  14.635  0.26 25.64 ?  6   PHE   A HE1  1 
ATOM   93   H  HE2  A PHE   A 1 6   ? 20.340 -8.990  15.894  0.74 23.33 ?  6   PHE   A HE2  1 
ATOM   94   H  HE2  B PHE   A 1 6   ? 20.484 -9.065  15.679  0.26 25.94 ?  6   PHE   A HE2  1 
ATOM   95   H  HZ   A PHE   A 1 6   ? 20.335 -7.027  14.669  0.74 22.61 ?  6   PHE   A HZ   1 
ATOM   96   H  HZ   B PHE   A 1 6   ? 20.510 -6.972  14.695  0.26 25.72 ?  6   PHE   A HZ   1 
ATOM   97   N  N    A SER   A 1 7   ? 13.152 -7.578  18.133  0.74 21.16 ?  7   SER   A N    1 
ATOM   98   N  N    B SER   A 1 7   ? 13.395 -7.438  18.670  0.26 23.27 ?  7   SER   A N    1 
ATOM   99   C  CA   A SER   A 1 7   ? 11.780 -7.688  18.619  0.74 21.16 ?  7   SER   A CA   1 
ATOM   100  C  CA   B SER   A 1 7   ? 12.038 -7.639  19.150  0.26 23.03 ?  7   SER   A CA   1 
ATOM   101  C  C    A SER   A 1 7   ? 10.777 -7.433  17.500  0.74 18.99 ?  7   SER   A C    1 
ATOM   102  C  C    B SER   A 1 7   ? 11.032 -7.242  18.078  0.26 21.72 ?  7   SER   A C    1 
ATOM   103  O  O    A SER   A 1 7   ? 10.975 -6.548  16.665  0.74 19.00 ?  7   SER   A O    1 
ATOM   104  O  O    B SER   A 1 7   ? 11.257 -6.306  17.305  0.26 21.70 ?  7   SER   A O    1 
ATOM   105  C  CB   A SER   A 1 7   ? 11.539 -6.680  19.752  0.74 23.38 ?  7   SER   A CB   1 
ATOM   106  C  CB   B SER   A 1 7   ? 11.791 -6.819  20.420  0.26 23.91 ?  7   SER   A CB   1 
ATOM   107  O  OG   A SER   A 1 7   ? 10.188 -6.697  20.176  0.74 24.93 ?  7   SER   A OG   1 
ATOM   108  O  OG   B SER   A 1 7   ? 10.514 -7.094  20.967  0.26 24.50 ?  7   SER   A OG   1 
ATOM   109  H  H    A SER   A 1 7   ? 13.288 -6.917  17.603  0.74 25.54 ?  7   SER   A H    1 
ATOM   110  H  H    B SER   A 1 7   ? 13.613 -6.609  18.588  0.26 28.07 ?  7   SER   A H    1 
ATOM   111  H  HA   A SER   A 1 7   ? 11.632 -8.580  18.966  0.74 25.54 ?  7   SER   A HA   1 
ATOM   112  H  HA   B SER   A 1 7   ? 11.906 -8.575  19.361  0.26 27.77 ?  7   SER   A HA   1 
ATOM   113  H  HB2  A SER   A 1 7   ? 12.112 -6.909  20.504  0.74 28.20 ?  7   SER   A HB2  1 
ATOM   114  H  HB2  B SER   A 1 7   ? 12.470 -7.044  21.077  0.26 28.83 ?  7   SER   A HB2  1 
ATOM   115  H  HB3  A SER   A 1 7   ? 11.757 -5.790  19.434  0.74 28.20 ?  7   SER   A HB3  1 
ATOM   116  H  HB3  B SER   A 1 7   ? 11.844 -5.875  20.201  0.26 28.83 ?  7   SER   A HB3  1 
ATOM   117  H  HG   A SER   A 1 7   ? 10.077 -6.144  20.799  0.74 30.05 ?  7   SER   A HG   1 
ATOM   118  H  HG   B SER   A 1 7   ? 10.395 -6.637  21.661  0.26 29.54 ?  7   SER   A HG   1 
ATOM   119  N  N    A GLY   A 1 8   ? 9.686  -8.202  17.502  0.74 17.25 ?  8   GLY   A N    1 
ATOM   120  N  N    B GLY   A 1 8   ? 9.919  -7.972  18.037  0.26 20.55 ?  8   GLY   A N    1 
ATOM   121  C  CA   A GLY   A 1 8   ? 8.598  -7.980  16.571  0.74 16.29 ?  8   GLY   A CA   1 
ATOM   122  C  CA   B GLY   A 1 8   ? 8.838  -7.661  17.126  0.26 19.15 ?  8   GLY   A CA   1 
ATOM   123  C  C    A GLY   A 1 8   ? 8.820  -8.489  15.166  0.74 15.04 ?  8   GLY   A C    1 
ATOM   124  C  C    B GLY   A 1 8   ? 8.987  -8.200  15.722  0.26 17.85 ?  8   GLY   A C    1 
ATOM   125  O  O    A GLY   A 1 8   ? 8.075  -8.104  14.258  0.74 15.48 ?  8   GLY   A O    1 
ATOM   126  O  O    B GLY   A 1 8   ? 8.204  -7.813  14.848  0.26 17.83 ?  8   GLY   A O    1 
ATOM   127  H  H    A GLY   A 1 8   ? 9.560  -8.851  18.043  0.74 20.84 ?  8   GLY   A H    1 
ATOM   128  H  H    B GLY   A 1 8   ? 9.770  -8.655  18.536  0.26 24.80 ?  8   GLY   A H    1 
ATOM   129  H  HA2  A GLY   A 1 8   ? 7.799  -8.407  16.926  0.74 19.69 ?  8   GLY   A HA2  1 
ATOM   130  H  HA2  B GLY   A 1 8   ? 8.013  -8.017  17.485  0.26 23.12 ?  8   GLY   A HA2  1 
ATOM   131  H  HA3  A GLY   A 1 8   ? 8.422  -7.030  16.511  0.74 19.69 ?  8   GLY   A HA3  1 
ATOM   132  H  HA3  B GLY   A 1 8   ? 8.748  -6.697  17.064  0.26 23.12 ?  8   GLY   A HA3  1 
ATOM   133  N  N    A TYR   A 1 9   ? 9.812  -9.352  14.952  0.74 13.94 ?  9   TYR   A N    1 
ATOM   134  N  N    B TYR   A 1 9   ? 9.951  -9.081  15.473  0.26 16.75 ?  9   TYR   A N    1 
ATOM   135  C  CA   A TYR   A 1 9   ? 10.080 -9.903  13.633  0.74 12.61 ?  9   TYR   A CA   1 
ATOM   136  C  CA   B TYR   A 1 9   ? 10.173 -9.600  14.131  0.26 15.74 ?  9   TYR   A CA   1 
ATOM   137  C  C    A TYR   A 1 9   ? 9.220  -11.129 13.364  0.74 12.10 ?  9   TYR   A C    1 
ATOM   138  C  C    B TYR   A 1 9   ? 9.269  -10.794 13.845  0.26 15.04 ?  9   TYR   A C    1 
ATOM   139  O  O    A TYR   A 1 9   ? 8.960  -11.942 14.257  0.74 13.29 ?  9   TYR   A O    1 
ATOM   140  O  O    B TYR   A 1 9   ? 8.864  -11.529 14.750  0.26 15.40 ?  9   TYR   A O    1 
ATOM   141  C  CB   A TYR   A 1 9   ? 11.559 -10.287 13.485  0.74 13.11 ?  9   TYR   A CB   1 
ATOM   142  C  CB   B TYR   A 1 9   ? 11.634 -10.013 13.940  0.26 15.86 ?  9   TYR   A CB   1 
ATOM   143  C  CG   A TYR   A 1 9   ? 12.467 -9.090  13.323  0.74 13.72 ?  9   TYR   A CG   1 
ATOM   144  C  CG   B TYR   A 1 9   ? 12.567 -8.851  13.682  0.26 15.74 ?  9   TYR   A CG   1 
ATOM   145  C  CD1  A TYR   A 1 9   ? 12.805 -8.308  14.415  0.74 14.62 ?  9   TYR   A CD1  1 
ATOM   146  C  CD1  B TYR   A 1 9   ? 12.914 -7.975  14.700  0.26 16.13 ?  9   TYR   A CD1  1 
ATOM   147  C  CD2  A TYR   A 1 9   ? 12.961 -8.727  12.075  0.74 13.60 ?  9   TYR   A CD2  1 
ATOM   148  C  CD2  B TYR   A 1 9   ? 13.096 -8.629  12.416  0.26 15.50 ?  9   TYR   A CD2  1 
ATOM   149  C  CE1  A TYR   A 1 9   ? 13.611 -7.198  14.277  0.74 15.45 ?  9   TYR   A CE1  1 
ATOM   150  C  CE1  B TYR   A 1 9   ? 13.761 -6.909  14.468  0.26 16.33 ?  9   TYR   A CE1  1 
ATOM   151  C  CE2  A TYR   A 1 9   ? 13.771 -7.619  11.925  0.74 14.12 ?  9   TYR   A CE2  1 
ATOM   152  C  CE2  B TYR   A 1 9   ? 13.942 -7.564  12.173  0.26 15.69 ?  9   TYR   A CE2  1 
ATOM   153  C  CZ   A TYR   A 1 9   ? 14.085 -6.854  13.027  0.74 15.41 ?  9   TYR   A CZ   1 
ATOM   154  C  CZ   B TYR   A 1 9   ? 14.271 -6.708  13.203  0.26 16.36 ?  9   TYR   A CZ   1 
ATOM   155  O  OH   A TYR   A 1 9   ? 14.884 -5.749  12.876  0.74 16.83 ?  9   TYR   A OH   1 
ATOM   156  O  OH   B TYR   A 1 9   ? 15.114 -5.648  12.967  0.26 17.11 ?  9   TYR   A OH   1 
ATOM   157  H  H    A TYR   A 1 9   ? 10.337 -9.646  15.563  0.74 16.87 ?  9   TYR   A H    1 
ATOM   158  H  H    B TYR   A 1 9   ? 10.495 -9.394  16.065  0.26 20.24 ?  9   TYR   A H    1 
ATOM   159  H  HA   A TYR   A 1 9   ? 9.873  -9.240  12.960  0.74 15.27 ?  9   TYR   A HA   1 
ATOM   160  H  HA   B TYR   A 1 9   ? 9.972  -8.902  13.486  0.26 19.02 ?  9   TYR   A HA   1 
ATOM   161  H  HB2  A TYR   A 1 9   ? 11.842 -10.777 14.274  0.74 15.87 ?  9   TYR   A HB2  1 
ATOM   162  H  HB2  B TYR   A 1 9   ? 11.943 -10.476 14.733  0.26 19.18 ?  9   TYR   A HB2  1 
ATOM   163  H  HB3  A TYR   A 1 9   ? 11.657 -10.847 12.697  0.74 15.87 ?  9   TYR   A HB3  1 
ATOM   164  H  HB3  B TYR   A 1 9   ? 11.684 -10.607 13.176  0.26 19.18 ?  9   TYR   A HB3  1 
ATOM   165  H  HD1  A TYR   A 1 9   ? 12.473 -8.536  15.258  0.74 17.69 ?  9   TYR   A HD1  1 
ATOM   166  H  HD1  B TYR   A 1 9   ? 12.569 -8.108  15.553  0.26 19.50 ?  9   TYR   A HD1  1 
ATOM   167  H  HD2  A TYR   A 1 9   ? 12.736 -9.239  11.328  0.74 16.46 ?  9   TYR   A HD2  1 
ATOM   168  H  HD2  B TYR   A 1 9   ? 12.876 -9.204  11.720  0.26 18.74 ?  9   TYR   A HD2  1 
ATOM   169  H  HE1  A TYR   A 1 9   ? 13.829 -6.685  15.021  0.74 18.69 ?  9   TYR   A HE1  1 
ATOM   170  H  HE1  B TYR   A 1 9   ? 13.984 -6.331  15.160  0.26 19.74 ?  9   TYR   A HE1  1 
ATOM   171  H  HE2  A TYR   A 1 9   ? 14.094 -7.387  11.084  0.74 17.09 ?  9   TYR   A HE2  1 
ATOM   172  H  HE2  B TYR   A 1 9   ? 14.292 -7.428  11.321  0.26 18.96 ?  9   TYR   A HE2  1 
ATOM   173  H  HH   A TYR   A 1 9   ? 15.022 -5.389  13.621  0.74 20.33 ?  9   TYR   A HH   1 
ATOM   174  H  HH   B TYR   A 1 9   ? 15.231 -5.213  13.676  0.26 20.67 ?  9   TYR   A HH   1 
ATOM   175  N  N    A LEU   A 1 10  ? 8.805  -11.266 12.113  0.74 11.92 ?  10  LEU   A N    1 
ATOM   176  N  N    B LEU   A 1 10  ? 8.952  -10.966 12.565  0.26 14.70 ?  10  LEU   A N    1 
ATOM   177  C  CA   A LEU   A 1 10  ? 8.211  -12.495 11.617  0.74 11.66 ?  10  LEU   A CA   1 
ATOM   178  C  CA   B LEU   A 1 10  ? 8.220  -12.120 12.065  0.26 14.84 ?  10  LEU   A CA   1 
ATOM   179  C  C    A LEU   A 1 10  ? 9.332  -13.435 11.178  0.74 11.63 ?  10  LEU   A C    1 
ATOM   180  C  C    B LEU   A 1 10  ? 9.238  -13.116 11.523  0.26 13.63 ?  10  LEU   A C    1 
ATOM   181  O  O    A LEU   A 1 10  ? 10.284 -13.012 10.518  0.74 12.08 ?  10  LEU   A O    1 
ATOM   182  O  O    B LEU   A 1 10  ? 10.105 -12.748 10.723  0.26 13.27 ?  10  LEU   A O    1 
ATOM   183  C  CB   A LEU   A 1 10  ? 7.322  -12.162 10.422  0.74 12.58 ?  10  LEU   A CB   1 
ATOM   184  C  CB   B LEU   A 1 10  ? 7.278  -11.679 10.944  0.26 16.25 ?  10  LEU   A CB   1 
ATOM   185  C  CG   A LEU   A 1 10  ? 6.599  -13.335 9.771   0.74 14.45 ?  10  LEU   A CG   1 
ATOM   186  C  CG   B LEU   A 1 10  ? 6.196  -12.658 10.507  0.26 17.91 ?  10  LEU   A CG   1 
ATOM   187  C  CD1  A LEU   A 1 10  ? 5.561  -13.914 10.715  0.74 15.98 ?  10  LEU   A CD1  1 
ATOM   188  C  CD1  B LEU   A 1 10  ? 4.886  -12.286 11.176  0.26 18.55 ?  10  LEU   A CD1  1 
ATOM   189  C  CD2  A LEU   A 1 10  ? 5.967  -12.935 8.438   0.74 16.40 ?  10  LEU   A CD2  1 
ATOM   190  C  CD2  B LEU   A 1 10  ? 6.065  -12.645 8.996   0.26 18.54 ?  10  LEU   A CD2  1 
ATOM   191  H  H    A LEU   A 1 10  ? 8.867  -10.655 11.510  0.74 14.44 ?  10  LEU   A H    1 
ATOM   192  H  H    B LEU   A 1 10  ? 9.158  -10.406 11.943  0.26 17.78 ?  10  LEU   A H    1 
ATOM   193  H  HA   A LEU   A 1 10  ? 7.682  -12.924 12.312  0.74 14.13 ?  10  LEU   A HA   1 
ATOM   194  H  HA   B LEU   A 1 10  ? 7.697  -12.531 12.777  0.26 17.95 ?  10  LEU   A HA   1 
ATOM   195  H  HB2  A LEU   A 1 10  ? 6.647  -11.536 10.715  0.74 15.24 ?  10  LEU   A HB2  1 
ATOM   196  H  HB2  B LEU   A 1 10  ? 6.819  -10.867 11.228  0.26 19.65 ?  10  LEU   A HB2  1 
ATOM   197  H  HB3  A LEU   A 1 10  ? 7.875  -11.754 9.740   0.74 15.24 ?  10  LEU   A HB3  1 
ATOM   198  H  HB3  B LEU   A 1 10  ? 7.811  -11.480 10.160  0.26 19.65 ?  10  LEU   A HB3  1 
ATOM   199  H  HG   A LEU   A 1 10  ? 7.243  -14.037 9.586   0.74 17.48 ?  10  LEU   A HG   1 
ATOM   200  H  HG   B LEU   A 1 10  ? 6.440  -13.554 10.788  0.26 21.63 ?  10  LEU   A HG   1 
ATOM   201  H  HD11 A LEU   A 1 10  ? 5.143  -14.685 10.295  0.74 19.31 ?  10  LEU   A HD11 1 
ATOM   202  H  HD11 B LEU   A 1 10  ? 4.217  -12.950 10.957  0.26 22.40 ?  10  LEU   A HD11 1 
ATOM   203  H  HD12 A LEU   A 1 10  ? 5.994  -14.187 11.540  0.74 19.31 ?  10  LEU   A HD12 1 
ATOM   204  H  HD12 B LEU   A 1 10  ? 5.024  -12.254 12.135  0.26 22.40 ?  10  LEU   A HD12 1 
ATOM   205  H  HD13 A LEU   A 1 10  ? 4.891  -13.239 10.904  0.74 19.31 ?  10  LEU   A HD13 1 
ATOM   206  H  HD13 B LEU   A 1 10  ? 4.606  -11.412 10.855  0.26 22.40 ?  10  LEU   A HD13 1 
ATOM   207  H  HD21 A LEU   A 1 10  ? 5.517  -13.708 8.060   0.74 19.82 ?  10  LEU   A HD21 1 
ATOM   208  H  HD21 B LEU   A 1 10  ? 5.352  -13.247 8.736   0.26 22.39 ?  10  LEU   A HD21 1 
ATOM   209  H  HD22 A LEU   A 1 10  ? 5.328  -12.224 8.595   0.74 19.82 ?  10  LEU   A HD22 1 
ATOM   210  H  HD22 B LEU   A 1 10  ? 5.861  -11.742 8.706   0.26 22.39 ?  10  LEU   A HD22 1 
ATOM   211  H  HD23 A LEU   A 1 10  ? 6.665  -12.632 7.839   0.74 19.82 ?  10  LEU   A HD23 1 
ATOM   212  H  HD23 B LEU   A 1 10  ? 6.904  -12.937 8.606   0.26 22.39 ?  10  LEU   A HD23 1 
ATOM   213  N  N    A LYS   A 1 11  ? 9.228  -14.709 11.559  0.74 11.81 ?  11  LYS   A N    1 
ATOM   214  N  N    B LYS   A 1 11  ? 9.150  -14.364 11.970  0.26 13.17 ?  11  LYS   A N    1 
ATOM   215  C  CA   A LYS   A 1 11  ? 10.232 -15.712 11.220  0.74 11.86 ?  11  LYS   A CA   1 
ATOM   216  C  CA   B LYS   A 1 11  ? 10.106 -15.384 11.557  0.26 12.54 ?  11  LYS   A CA   1 
ATOM   217  C  C    A LYS   A 1 11  ? 9.885  -16.304 9.861   0.74 11.89 ?  11  LYS   A C    1 
ATOM   218  C  C    B LYS   A 1 11  ? 9.710  -15.929 10.189  0.26 11.72 ?  11  LYS   A C    1 
ATOM   219  O  O    A LYS   A 1 11  ? 8.814  -16.892 9.701   0.74 13.73 ?  11  LYS   A O    1 
ATOM   220  O  O    B LYS   A 1 11  ? 8.590  -16.422 10.013  0.26 11.51 ?  11  LYS   A O    1 
ATOM   221  C  CB   A LYS   A 1 11  ? 10.271 -16.794 12.301  0.74 11.99 ?  11  LYS   A CB   1 
ATOM   222  C  CB   B LYS   A 1 11  ? 10.153 -16.503 12.595  0.26 12.67 ?  11  LYS   A CB   1 
ATOM   223  C  CG   A LYS   A 1 11  ? 11.284 -17.908 12.088  0.74 12.36 ?  11  LYS   A CG   1 
ATOM   224  C  CG   B LYS   A 1 11  ? 11.223 -17.560 12.348  0.26 12.75 ?  11  LYS   A CG   1 
ATOM   225  C  CD   A LYS   A 1 11  ? 11.387 -18.751 13.365  0.74 13.14 ?  11  LYS   A CD   1 
ATOM   226  C  CD   B LYS   A 1 11  ? 11.296 -18.542 13.513  0.26 13.06 ?  11  LYS   A CD   1 
ATOM   227  C  CE   A LYS   A 1 11  ? 12.365 -19.908 13.248  0.74 13.16 ?  11  LYS   A CE   1 
ATOM   228  C  CE   B LYS   A 1 11  ? 12.343 -19.627 13.290  0.26 13.09 ?  11  LYS   A CE   1 
ATOM   229  N  NZ   A LYS   A 1 11  ? 13.733 -19.440 12.922  0.74 13.41 ?  11  LYS   A NZ   1 
ATOM   230  N  NZ   B LYS   A 1 11  ? 13.732 -19.089 13.295  0.26 12.97 ?  11  LYS   A NZ   1 
ATOM   231  H  H    A LYS   A 1 11  ? 8.568  -15.032 12.012  0.74 14.31 ?  11  LYS   A H    1 
ATOM   232  H  H    B LYS   A 1 11  ? 8.545  -14.639 12.515  0.26 15.94 ?  11  LYS   A H    1 
ATOM   233  H  HA   A LYS   A 1 11  ? 11.106 -15.299 11.161  0.74 14.37 ?  11  LYS   A HA   1 
ATOM   234  H  HA   B LYS   A 1 11  ? 10.985 -14.985 11.485  0.26 15.19 ?  11  LYS   A HA   1 
ATOM   235  H  HB2  A LYS   A 1 11  ? 10.491 -16.371 13.147  0.74 14.53 ?  11  LYS   A HB2  1 
ATOM   236  H  HB2  B LYS   A 1 11  ? 10.326 -16.105 13.462  0.26 15.35 ?  11  LYS   A HB2  1 
ATOM   237  H  HB3  A LYS   A 1 11  ? 9.400  -17.207 12.360  0.74 14.53 ?  11  LYS   A HB3  1 
ATOM   238  H  HB3  B LYS   A 1 11  ? 9.295  -16.949 12.604  0.26 15.35 ?  11  LYS   A HB3  1 
ATOM   239  H  HG2  A LYS   A 1 11  ? 10.991 -18.484 11.362  0.74 14.97 ?  11  LYS   A HG2  1 
ATOM   240  H  HG2  B LYS   A 1 11  ? 11.005 -18.054 11.543  0.26 15.45 ?  11  LYS   A HG2  1 
ATOM   241  H  HG3  A LYS   A 1 11  ? 12.156 -17.532 11.895  0.74 14.97 ?  11  LYS   A HG3  1 
ATOM   242  H  HG3  B LYS   A 1 11  ? 12.086 -17.128 12.256  0.26 15.45 ?  11  LYS   A HG3  1 
ATOM   243  H  HD2  A LYS   A 1 11  ? 11.681 -18.182 14.093  0.74 15.91 ?  11  LYS   A HD2  1 
ATOM   244  H  HD2  B LYS   A 1 11  ? 11.529 -18.060 14.322  0.26 15.81 ?  11  LYS   A HD2  1 
ATOM   245  H  HD3  A LYS   A 1 11  ? 10.512 -19.120 13.568  0.74 15.91 ?  11  LYS   A HD3  1 
ATOM   246  H  HD3  B LYS   A 1 11  ? 10.434 -18.973 13.619  0.26 15.81 ?  11  LYS   A HD3  1 
ATOM   247  H  HE2  A LYS   A 1 11  ? 12.403 -20.382 14.094  0.74 15.93 ?  11  LYS   A HE2  1 
ATOM   248  H  HE2  B LYS   A 1 11  ? 12.276 -20.286 13.999  0.26 15.85 ?  11  LYS   A HE2  1 
ATOM   249  H  HE3  A LYS   A 1 11  ? 12.074 -20.504 12.543  0.74 15.93 ?  11  LYS   A HE3  1 
ATOM   250  H  HE3  B LYS   A 1 11  ? 12.188 -20.048 12.430  0.26 15.85 ?  11  LYS   A HE3  1 
ATOM   251  H  HZ1  A LYS   A 1 11  ? 14.283 -20.136 12.844  0.74 16.23 ?  11  LYS   A HZ1  1 
ATOM   252  H  HZ1  B LYS   A 1 11  ? 14.315 -19.748 13.158  0.26 15.70 ?  11  LYS   A HZ1  1 
ATOM   253  H  HZ2  A LYS   A 1 11  ? 13.726 -18.991 12.154  0.74 16.23 ?  11  LYS   A HZ2  1 
ATOM   254  H  HZ2  B LYS   A 1 11  ? 13.826 -18.483 12.649  0.26 15.70 ?  11  LYS   A HZ2  1 
ATOM   255  H  HZ3  A LYS   A 1 11  ? 14.035 -18.905 13.566  0.74 16.23 ?  11  LYS   A HZ3  1 
ATOM   256  H  HZ3  B LYS   A 1 11  ? 13.908 -18.706 14.078  0.26 15.70 ?  11  LYS   A HZ3  1 
ATOM   257  N  N    A LEU   A 1 12  ? 10.781 -16.160 8.883   0.74 11.02 ?  12  LEU   A N    1 
ATOM   258  N  N    B LEU   A 1 12  ? 10.616 -15.822 9.216   0.26 11.91 ?  12  LEU   A N    1 
ATOM   259  C  CA   A LEU   A 1 12  ? 10.525 -16.743 7.569   0.74 11.17 ?  12  LEU   A CA   1 
ATOM   260  C  CA   B LEU   A 1 12  ? 10.369 -16.330 7.869   0.26 12.09 ?  12  LEU   A CA   1 
ATOM   261  C  C    A LEU   A 1 12  ? 11.119 -18.139 7.425   0.74 11.31 ?  12  LEU   A C    1 
ATOM   262  C  C    B LEU   A 1 12  ? 10.934 -17.728 7.656   0.26 11.91 ?  12  LEU   A C    1 
ATOM   263  O  O    A LEU   A 1 12  ? 10.494 -19.014 6.814   0.74 11.73 ?  12  LEU   A O    1 
ATOM   264  O  O    B LEU   A 1 12  ? 10.249 -18.598 7.109   0.26 12.00 ?  12  LEU   A O    1 
ATOM   265  C  CB   A LEU   A 1 12  ? 11.069 -15.847 6.450   0.74 11.62 ?  12  LEU   A CB   1 
ATOM   266  C  CB   B LEU   A 1 12  ? 10.938 -15.370 6.813   0.26 12.97 ?  12  LEU   A CB   1 
ATOM   267  C  CG   A LEU   A 1 12  ? 10.426 -14.467 6.302   0.74 12.68 ?  12  LEU   A CG   1 
ATOM   268  C  CG   B LEU   A 1 12  ? 10.195 -14.044 6.641   0.26 13.86 ?  12  LEU   A CG   1 
ATOM   269  C  CD1  A LEU   A 1 12  ? 11.146 -13.672 5.234   0.74 13.38 ?  12  LEU   A CD1  1 
ATOM   270  C  CD1  B LEU   A 1 12  ? 10.659 -13.304 5.391   0.26 14.45 ?  12  LEU   A CD1  1 
ATOM   271  C  CD2  A LEU   A 1 12  ? 8.944  -14.598 5.965   0.74 13.52 ?  12  LEU   A CD2  1 
ATOM   272  C  CD2  B LEU   A 1 12  ? 8.696  -14.281 6.590   0.26 14.28 ?  12  LEU   A CD2  1 
ATOM   273  H  H    A LEU   A 1 12  ? 11.534 -15.737 8.950   0.74 13.37 ?  12  LEU   A H    1 
ATOM   274  H  H    B LEU   A 1 12  ? 11.385 -15.442 9.310   0.26 14.43 ?  12  LEU   A H    1 
ATOM   275  H  HA   A LEU   A 1 12  ? 9.568  -16.824 7.450   0.74 13.54 ?  12  LEU   A HA   1 
ATOM   276  H  HA   B LEU   A 1 12  ? 9.411  -16.390 7.740   0.26 14.65 ?  12  LEU   A HA   1 
ATOM   277  H  HB2  A LEU   A 1 12  ? 12.012 -15.713 6.602   0.74 14.09 ?  12  LEU   A HB2  1 
ATOM   278  H  HB2  B LEU   A 1 12  ? 11.854 -15.157 7.051   0.26 15.71 ?  12  LEU   A HB2  1 
ATOM   279  H  HB3  A LEU   A 1 12  ? 10.941 -16.316 5.607   0.74 14.09 ?  12  LEU   A HB3  1 
ATOM   280  H  HB3  B LEU   A 1 12  ? 10.925 -15.819 5.953   0.26 15.71 ?  12  LEU   A HB3  1 
ATOM   281  H  HG   A LEU   A 1 12  ? 10.502 -13.991 7.142   0.74 15.36 ?  12  LEU   A HG   1 
ATOM   282  H  HG   B LEU   A 1 12  ? 10.381 -13.478 7.407   0.26 16.77 ?  12  LEU   A HG   1 
ATOM   283  H  HD11 A LEU   A 1 12  ? 10.730 -12.803 5.153   0.74 16.20 ?  12  LEU   A HD11 1 
ATOM   284  H  HD11 B LEU   A 1 12  ? 10.175 -12.463 5.325   0.26 17.48 ?  12  LEU   A HD11 1 
ATOM   285  H  HD12 A LEU   A 1 12  ? 12.077 -13.573 5.494   0.74 16.20 ?  12  LEU   A HD12 1 
ATOM   286  H  HD12 B LEU   A 1 12  ? 11.609 -13.134 5.457   0.26 17.48 ?  12  LEU   A HD12 1 
ATOM   287  H  HD13 A LEU   A 1 12  ? 11.089 -14.150 4.392   0.74 16.20 ?  12  LEU   A HD13 1 
ATOM   288  H  HD13 B LEU   A 1 12  ? 10.471 -13.853 4.612   0.26 17.48 ?  12  LEU   A HD13 1 
ATOM   289  H  HD21 A LEU   A 1 12  ? 8.586  -13.721 5.758   0.74 16.37 ?  12  LEU   A HD21 1 
ATOM   290  H  HD21 B LEU   A 1 12  ? 8.265  -13.506 6.203   0.26 17.28 ?  12  LEU   A HD21 1 
ATOM   291  H  HD22 A LEU   A 1 12  ? 8.841  -15.187 5.200   0.74 16.37 ?  12  LEU   A HD22 1 
ATOM   292  H  HD22 B LEU   A 1 12  ? 8.520  -15.066 6.047   0.26 17.28 ?  12  LEU   A HD22 1 
ATOM   293  H  HD23 A LEU   A 1 12  ? 8.474  -14.972 6.730   0.74 16.37 ?  12  LEU   A HD23 1 
ATOM   294  H  HD23 B LEU   A 1 12  ? 8.368  -14.427 7.493   0.26 17.28 ?  12  LEU   A HD23 1 
ATOM   295  N  N    A THR   A 1 13  ? 12.325 -18.348 7.949   0.74 11.51 ?  13  THR   A N    1 
ATOM   296  N  N    B THR   A 1 13  ? 12.178 -17.958 8.062   0.26 11.93 ?  13  THR   A N    1 
ATOM   297  C  CA   A THR   A 1 13  ? 13.024 -19.626 7.866   0.74 11.74 ?  13  THR   A CA   1 
ATOM   298  C  CA   B THR   A 1 13  ? 12.802 -19.266 7.947   0.26 12.11 ?  13  THR   A CA   1 
ATOM   299  C  C    A THR   A 1 13  ? 13.795 -19.835 9.164   0.74 12.26 ?  13  THR   A C    1 
ATOM   300  C  C    B THR   A 1 13  ? 13.582 -19.542 9.228   0.26 12.47 ?  13  THR   A C    1 
ATOM   301  O  O    A THR   A 1 13  ? 13.713 -19.035 10.100  0.74 12.28 ?  13  THR   A O    1 
ATOM   302  O  O    B THR   A 1 13  ? 13.451 -18.839 10.234  0.26 12.93 ?  13  THR   A O    1 
ATOM   303  C  CB   A THR   A 1 13  ? 14.008 -19.666 6.690   0.74 12.71 ?  13  THR   A CB   1 
ATOM   304  C  CB   B THR   A 1 13  ? 13.725 -19.338 6.722   0.26 12.23 ?  13  THR   A CB   1 
ATOM   305  O  OG1  A THR   A 1 13  ? 15.069 -18.743 6.947   0.74 13.08 ?  13  THR   A OG1  1 
ATOM   306  O  OG1  B THR   A 1 13  ? 14.806 -18.415 6.888   0.26 12.27 ?  13  THR   A OG1  1 
ATOM   307  C  CG2  A THR   A 1 13  ? 13.340 -19.315 5.369   0.74 13.75 ?  13  THR   A CG2  1 
ATOM   308  C  CG2  B THR   A 1 13  ? 12.980 -19.009 5.436   0.26 12.35 ?  13  THR   A CG2  1 
ATOM   309  H  H    A THR   A 1 13  ? 12.778 -17.746 8.359   0.74 13.96 ?  13  THR   A H    1 
ATOM   310  H  H    B THR   A 1 13  ? 12.686 -17.355 8.401   0.26 14.45 ?  13  THR   A H    1 
ATOM   311  H  HA   A THR   A 1 13  ? 12.387 -20.349 7.759   0.74 14.23 ?  13  THR   A HA   1 
ATOM   312  H  HA   B THR   A 1 13  ? 12.109 -19.941 7.850   0.26 14.67 ?  13  THR   A HA   1 
ATOM   313  H  HB   A THR   A 1 13  ? 14.378 -20.564 6.605   0.74 15.40 ?  13  THR   A HB   1 
ATOM   314  H  HB   B THR   A 1 13  ? 14.082 -20.235 6.645   0.26 14.81 ?  13  THR   A HB   1 
ATOM   315  H  HG1  A THR   A 1 13  ? 15.721 -19.145 7.293   0.74 15.84 ?  13  THR   A HG1  1 
ATOM   316  H  HG1  B THR   A 1 13  ? 15.411 -18.762 7.355   0.26 14.86 ?  13  THR   A HG1  1 
ATOM   317  H  HG21 A THR   A 1 13  ? 13.959 -19.467 4.632   0.74 16.65 ?  13  THR   A HG21 1 
ATOM   318  H  HG21 B THR   A 1 13  ? 13.576 -19.117 4.675   0.26 14.96 ?  13  THR   A HG21 1 
ATOM   319  H  HG22 A THR   A 1 13  ? 12.558 -19.873 5.235   0.74 16.65 ?  13  THR   A HG22 1 
ATOM   320  H  HG22 B THR   A 1 13  ? 12.224 -19.607 5.328   0.26 14.96 ?  13  THR   A HG22 1 
ATOM   321  H  HG23 A THR   A 1 13  ? 13.073 -18.386 5.369   0.74 16.65 ?  13  THR   A HG23 1 
ATOM   322  H  HG23 B THR   A 1 13  ? 12.662 -18.096 5.458   0.26 14.96 ?  13  THR   A HG23 1 
ATOM   323  N  N    A ASP   A 1 14  ? 14.595 -20.903 9.201   0.74 13.03 ?  14  ASP   A N    1 
ATOM   324  N  N    B ASP   A 1 14  ? 14.406 -20.587 9.168   0.26 12.85 ?  14  ASP   A N    1 
ATOM   325  C  CA   A ASP   A 1 14  ? 15.444 -21.147 10.360  0.74 14.25 ?  14  ASP   A CA   1 
ATOM   326  C  CA   B ASP   A 1 14  ? 15.256 -20.963 10.291  0.26 13.33 ?  14  ASP   A CA   1 
ATOM   327  C  C    A ASP   A 1 14  ? 16.243 -19.904 10.746  0.74 14.01 ?  14  ASP   A C    1 
ATOM   328  C  C    B ASP   A 1 14  ? 16.206 -19.842 10.701  0.26 12.50 ?  14  ASP   A C    1 
ATOM   329  O  O    A ASP   A 1 14  ? 16.393 -19.598 11.935  0.74 14.97 ?  14  ASP   A O    1 
ATOM   330  O  O    B ASP   A 1 14  ? 16.648 -19.801 11.855  0.26 12.57 ?  14  ASP   A O    1 
ATOM   331  C  CB   A ASP   A 1 14  ? 16.394 -22.308 10.072  0.74 16.95 ?  14  ASP   A CB   1 
ATOM   332  C  CB   B ASP   A 1 14  ? 16.075 -22.188 9.900   0.26 14.69 ?  14  ASP   A CB   1 
ATOM   333  C  CG   A ASP   A 1 14  ? 17.323 -22.582 11.228  0.74 21.21 ?  14  ASP   A CG   1 
ATOM   334  C  CG   B ASP   A 1 14  ? 17.016 -22.637 11.002  0.26 16.26 ?  14  ASP   A CG   1 
ATOM   335  O  OD1  A ASP   A 1 14  ? 16.824 -22.929 12.318  0.74 22.76 ?  14  ASP   A OD1  1 
ATOM   336  O  OD1  B ASP   A 1 14  ? 16.531 -23.189 12.014  0.26 16.70 ?  14  ASP   A OD1  1 
ATOM   337  O  OD2  A ASP   A 1 14  ? 18.548 -22.431 11.049  0.74 24.11 -1 14  ASP   A OD2  1 
ATOM   338  O  OD2  B ASP   A 1 14  ? 18.238 -22.432 10.855  0.26 17.56 -1 14  ASP   A OD2  1 
ATOM   339  H  H    A ASP   A 1 14  ? 14.672 -21.492 8.572   0.74 15.78 ?  14  ASP   A H    1 
ATOM   340  H  H    B ASP   A 1 14  ? 14.468 -21.098 8.488   0.26 15.56 ?  14  ASP   A H    1 
ATOM   341  H  HA   A ASP   A 1 14  ? 14.893 -21.399 11.115  0.74 17.24 ?  14  ASP   A HA   1 
ATOM   342  H  HA   B ASP   A 1 14  ? 14.693 -21.193 11.050  0.26 16.14 ?  14  ASP   A HA   1 
ATOM   343  H  HB2  A ASP   A 1 14  ? 15.867 -23.114 9.887   0.74 20.48 ?  14  ASP   A HB2  1 
ATOM   344  H  HB2  B ASP   A 1 14  ? 15.465 -22.913 9.686   0.26 17.77 ?  14  ASP   A HB2  1 
ATOM   345  H  HB3  A ASP   A 1 14  ? 16.943 -22.098 9.304   0.74 20.48 ?  14  ASP   A HB3  1 
ATOM   346  H  HB3  B ASP   A 1 14  ? 16.605 -21.964 9.115   0.26 17.77 ?  14  ASP   A HB3  1 
ATOM   347  N  N    A ASN   A 1 15  ? 16.750 -19.163 9.755   0.74 12.95 ?  15  ASN   A N    1 
ATOM   348  N  N    B ASN   A 1 15  ? 16.552 -18.939 9.774   0.26 11.75 ?  15  ASN   A N    1 
ATOM   349  C  CA   A ASN   A 1 15  ? 17.732 -18.113 10.011  0.74 13.50 ?  15  ASN   A CA   1 
ATOM   350  C  CA   B ASN   A 1 15  ? 17.556 -17.920 10.065  0.26 11.85 ?  15  ASN   A CA   1 
ATOM   351  C  C    A ASN   A 1 15  ? 17.345 -16.720 9.520   0.74 13.72 ?  15  ASN   A C    1 
ATOM   352  C  C    B ASN   A 1 15  ? 17.214 -16.533 9.532   0.26 12.12 ?  15  ASN   A C    1 
ATOM   353  O  O    A ASN   A 1 15  ? 18.082 -15.772 9.815   0.74 14.81 ?  15  ASN   A O    1 
ATOM   354  O  O    B ASN   A 1 15  ? 18.065 -15.637 9.612   0.26 13.17 ?  15  ASN   A O    1 
ATOM   355  C  CB   A ASN   A 1 15  ? 19.102 -18.496 9.416   0.74 13.49 ?  15  ASN   A CB   1 
ATOM   356  C  CB   B ASN   A 1 15  ? 18.929 -18.330 9.515   0.26 11.70 ?  15  ASN   A CB   1 
ATOM   357  C  CG   A ASN   A 1 15  ? 19.078 -18.573 7.906   0.74 14.13 ?  15  ASN   A CG   1 
ATOM   358  C  CG   B ASN   A 1 15  ? 18.934 -18.489 8.007   0.26 11.72 ?  15  ASN   A CG   1 
ATOM   359  O  OD1  A ASN   A 1 15  ? 18.402 -19.429 7.328   0.74 14.61 ?  15  ASN   A OD1  1 
ATOM   360  O  OD1  B ASN   A 1 15  ? 18.117 -19.223 7.448   0.26 11.84 ?  15  ASN   A OD1  1 
ATOM   361  N  ND2  A ASN   A 1 15  ? 19.819 -17.676 7.254   0.74 14.60 ?  15  ASN   A ND2  1 
ATOM   362  N  ND2  B ASN   A 1 15  ? 19.848 -17.789 7.337   0.26 11.75 ?  15  ASN   A ND2  1 
ATOM   363  H  H    A ASN   A 1 15  ? 16.552 -19.263 8.929   0.74 15.68 ?  15  ASN   A H    1 
ATOM   364  H  H    B ASN   A 1 15  ? 16.225 -18.901 8.984   0.26 14.24 ?  15  ASN   A H    1 
ATOM   365  H  HA   A ASN   A 1 15  ? 17.862 -18.049 10.966  0.74 16.34 ?  15  ASN   A HA   1 
ATOM   366  H  HA   B ASN   A 1 15  ? 17.637 -17.836 11.027  0.26 14.36 ?  15  ASN   A HA   1 
ATOM   367  H  HB2  A ASN   A 1 15  ? 19.762 -17.824 9.675   0.74 16.32 ?  15  ASN   A HB2  1 
ATOM   368  H  HB2  B ASN   A 1 15  ? 19.574 -17.644 9.748   0.26 14.18 ?  15  ASN   A HB2  1 
ATOM   369  H  HB3  A ASN   A 1 15  ? 19.376 -19.365 9.759   0.74 16.32 ?  15  ASN   A HB3  1 
ATOM   370  H  HB3  B ASN   A 1 15  ? 19.177 -19.175 9.903   0.26 14.18 ?  15  ASN   A HB3  1 
ATOM   371  H  HD21 A ASN   A 1 15  ? 19.832 -17.679 6.394   0.74 17.65 ?  15  ASN   A HD21 1 
ATOM   372  H  HD21 B ASN   A 1 15  ? 19.885 -17.841 6.478   0.26 14.24 ?  15  ASN   A HD21 1 
ATOM   373  H  HD22 A ASN   A 1 15  ? 20.279 -17.091 7.688   0.74 17.65 ?  15  ASN   A HD22 1 
ATOM   374  H  HD22 B ASN   A 1 15  ? 20.402 -17.284 7.759   0.26 14.24 ?  15  ASN   A HD22 1 
ATOM   375  N  N    A VAL   A 1 16  ? 16.233 -16.559 8.795   0.74 12.87 ?  16  VAL   A N    1 
ATOM   376  N  N    B VAL   A 1 16  ? 16.015 -16.314 8.998   0.26 11.42 ?  16  VAL   A N    1 
ATOM   377  C  CA   A VAL   A 1 16  ? 15.831 -15.273 8.226   0.74 12.58 ?  16  VAL   A CA   1 
ATOM   378  C  CA   B VAL   A 1 16  ? 15.641 -15.041 8.393   0.26 11.40 ?  16  VAL   A CA   1 
ATOM   379  C  C    A VAL   A 1 16  ? 14.546 -14.787 8.887   0.74 12.20 ?  16  VAL   A C    1 
ATOM   380  C  C    B VAL   A 1 16  ? 14.398 -14.512 9.099   0.26 11.12 ?  16  VAL   A C    1 
ATOM   381  O  O    A VAL   A 1 16  ? 13.558 -15.527 8.986   0.74 12.11 ?  16  VAL   A O    1 
ATOM   382  O  O    B VAL   A 1 16  ? 13.382 -15.211 9.189   0.26 10.98 ?  16  VAL   A O    1 
ATOM   383  C  CB   A VAL   A 1 16  ? 15.669 -15.337 6.698   0.74 13.15 ?  16  VAL   A CB   1 
ATOM   384  C  CB   B VAL   A 1 16  ? 15.416 -15.181 6.876   0.26 11.78 ?  16  VAL   A CB   1 
ATOM   385  C  CG1  A VAL   A 1 16  ? 15.220 -13.979 6.153   0.74 14.00 ?  16  VAL   A CG1  1 
ATOM   386  C  CG1  B VAL   A 1 16  ? 14.999 -13.850 6.261   0.26 12.18 ?  16  VAL   A CG1  1 
ATOM   387  C  CG2  A VAL   A 1 16  ? 16.962 -15.774 6.041   0.74 14.15 ?  16  VAL   A CG2  1 
ATOM   388  C  CG2  B VAL   A 1 16  ? 16.675 -15.715 6.197   0.26 12.19 ?  16  VAL   A CG2  1 
ATOM   389  H  H    A VAL   A 1 16  ? 15.697 -17.209 8.612   0.74 15.59 ?  16  VAL   A H    1 
ATOM   390  H  H    B VAL   A 1 16  ? 15.385 -16.899 8.976   0.26 13.84 ?  16  VAL   A H    1 
ATOM   391  H  HA   A VAL   A 1 16  ? 16.528 -14.631 8.417   0.74 15.24 ?  16  VAL   A HA   1 
ATOM   392  H  HA   B VAL   A 1 16  ? 16.352 -14.397 8.529   0.26 13.82 ?  16  VAL   A HA   1 
ATOM   393  H  HB   A VAL   A 1 16  ? 14.986 -15.992 6.481   0.74 15.91 ?  16  VAL   A HB   1 
ATOM   394  H  HB   B VAL   A 1 16  ? 14.701 -15.818 6.720   0.26 14.28 ?  16  VAL   A HB   1 
ATOM   395  H  HG11 A VAL   A 1 16  ? 15.317 -13.982 5.189   0.74 16.94 ?  16  VAL   A HG11 1 
ATOM   396  H  HG11 B VAL   A 1 16  ? 15.034 -13.927 5.294   0.26 14.76 ?  16  VAL   A HG11 1 
ATOM   397  H  HG12 A VAL   A 1 16  ? 14.288 -13.835 6.390   0.74 16.94 ?  16  VAL   A HG12 1 
ATOM   398  H  HG12 B VAL   A 1 16  ? 14.094 -13.641 6.541   0.26 14.76 ?  16  VAL   A HG12 1 
ATOM   399  H  HG13 A VAL   A 1 16  ? 15.772 -13.286 6.541   0.74 16.94 ?  16  VAL   A HG13 1 
ATOM   400  H  HG13 B VAL   A 1 16  ? 15.609 -13.159 6.560   0.26 14.76 ?  16  VAL   A HG13 1 
ATOM   401  H  HG21 A VAL   A 1 16  ? 16.866 -15.700 5.080   0.74 17.12 ?  16  VAL   A HG21 1 
ATOM   402  H  HG21 B VAL   A 1 16  ? 16.531 -15.746 5.239   0.26 14.77 ?  16  VAL   A HG21 1 
ATOM   403  H  HG22 A VAL   A 1 16  ? 17.680 -15.202 6.348   0.74 17.12 ?  16  VAL   A HG22 1 
ATOM   404  H  HG22 B VAL   A 1 16  ? 17.419 -15.126 6.400   0.26 14.77 ?  16  VAL   A HG22 1 
ATOM   405  H  HG23 A VAL   A 1 16  ? 17.145 -16.694 6.287   0.74 17.12 ?  16  VAL   A HG23 1 
ATOM   406  H  HG23 B VAL   A 1 16  ? 16.862 -16.607 6.532   0.26 14.77 ?  16  VAL   A HG23 1 
ATOM   407  N  N    A TYR   A 1 17  ? 14.556 -13.514 9.275   0.74 11.95 ?  17  TYR   A N    1 
ATOM   408  N  N    B TYR   A 1 17  ? 14.487 -13.275 9.590   0.26 10.93 ?  17  TYR   A N    1 
ATOM   409  C  CA   A TYR   A 1 17  ? 13.474 -12.834 9.970   0.74 11.69 ?  17  TYR   A CA   1 
ATOM   410  C  CA   B TYR   A 1 17  ? 13.421 -12.607 10.321  0.26 10.62 ?  17  TYR   A CA   1 
ATOM   411  C  C    A TYR   A 1 17  ? 13.200 -11.510 9.262   0.74 11.70 ?  17  TYR   A C    1 
ATOM   412  C  C    B TYR   A 1 17  ? 13.172 -11.255 9.673   0.26 10.38 ?  17  TYR   A C    1 
ATOM   413  O  O    A TYR   A 1 17  ? 14.101 -10.947 8.636   0.74 11.43 ?  17  TYR   A O    1 
ATOM   414  O  O    B TYR   A 1 17  ? 14.094 -10.649 9.123   0.26 10.26 ?  17  TYR   A O    1 
ATOM   415  C  CB   A TYR   A 1 17  ? 13.902 -12.561 11.411  0.74 12.51 ?  17  TYR   A CB   1 
ATOM   416  C  CB   B TYR   A 1 17  ? 13.826 -12.391 11.780  0.26 11.51 ?  17  TYR   A CB   1 
ATOM   417  C  CG   A TYR   A 1 17  ? 14.091 -13.815 12.240  0.74 13.65 ?  17  TYR   A CG   1 
ATOM   418  C  CG   B TYR   A 1 17  ? 14.083 -13.672 12.539  0.26 12.38 ?  17  TYR   A CG   1 
ATOM   419  C  CD1  A TYR   A 1 17  ? 15.265 -14.562 12.178  0.74 15.02 ?  17  TYR   A CD1  1 
ATOM   420  C  CD1  B TYR   A 1 17  ? 15.265 -14.385 12.370  0.26 13.13 ?  17  TYR   A CD1  1 
ATOM   421  C  CD2  A TYR   A 1 17  ? 13.081 -14.263 13.077  0.74 13.88 ?  17  TYR   A CD2  1 
ATOM   422  C  CD2  B TYR   A 1 17  ? 13.141 -14.169 13.428  0.26 12.95 ?  17  TYR   A CD2  1 
ATOM   423  C  CE1  A TYR   A 1 17  ? 15.420 -15.724 12.932  0.74 15.48 ?  17  TYR   A CE1  1 
ATOM   424  C  CE1  B TYR   A 1 17  ? 15.497 -15.562 13.064  0.26 13.93 ?  17  TYR   A CE1  1 
ATOM   425  C  CE2  A TYR   A 1 17  ? 13.226 -15.418 13.834  0.74 14.88 ?  17  TYR   A CE2  1 
ATOM   426  C  CE2  B TYR   A 1 17  ? 13.364 -15.343 14.127  0.26 13.70 ?  17  TYR   A CE2  1 
ATOM   427  C  CZ   A TYR   A 1 17  ? 14.396 -16.144 13.761  0.74 15.32 ?  17  TYR   A CZ   1 
ATOM   428  C  CZ   B TYR   A 1 17  ? 14.544 -16.035 13.943  0.26 14.19 ?  17  TYR   A CZ   1 
ATOM   429  O  OH   A TYR   A 1 17  ? 14.532 -17.289 14.518  0.74 16.12 ?  17  TYR   A OH   1 
ATOM   430  O  OH   B TYR   A 1 17  ? 14.769 -17.201 14.639  0.26 14.81 ?  17  TYR   A OH   1 
ATOM   431  H  H    A TYR   A 1 17  ? 15.230 -13.000 9.125   0.74 14.48 ?  17  TYR   A H    1 
ATOM   432  H  H    B TYR   A 1 17  ? 15.185 -12.774 9.495   0.26 13.26 ?  17  TYR   A H    1 
ATOM   433  H  HA   A TYR   A 1 17  ? 12.677 -13.394 9.960   0.74 14.17 ?  17  TYR   A HA   1 
ATOM   434  H  HA   B TYR   A 1 17  ? 12.604 -13.122 10.283  0.26 12.88 ?  17  TYR   A HA   1 
ATOM   435  H  HB2  A TYR   A 1 17  ? 14.746 -12.086 11.397  0.74 15.15 ?  17  TYR   A HB2  1 
ATOM   436  H  HB2  B TYR   A 1 17  ? 14.639 -11.865 11.795  0.26 13.96 ?  17  TYR   A HB2  1 
ATOM   437  H  HB3  A TYR   A 1 17  ? 13.222 -12.026 11.834  0.74 15.15 ?  17  TYR   A HB3  1 
ATOM   438  H  HB3  B TYR   A 1 17  ? 13.116 -11.911 12.233  0.26 13.96 ?  17  TYR   A HB3  1 
ATOM   439  H  HD1  A TYR   A 1 17  ? 15.958 -14.284 11.616  0.74 18.16 ?  17  TYR   A HD1  1 
ATOM   440  H  HD1  B TYR   A 1 17  ? 15.909 -14.070 11.774  0.26 15.90 ?  17  TYR   A HD1  1 
ATOM   441  H  HD2  A TYR   A 1 17  ? 12.289 -13.785 13.132  0.74 16.80 ?  17  TYR   A HD2  1 
ATOM   442  H  HD2  B TYR   A 1 17  ? 12.344 -13.703 13.552  0.26 15.68 ?  17  TYR   A HD2  1 
ATOM   443  H  HE1  A TYR   A 1 17  ? 16.218 -16.210 12.884  0.74 18.72 ?  17  TYR   A HE1  1 
ATOM   444  H  HE1  B TYR   A 1 17  ? 16.292 -16.030 12.940  0.26 16.86 ?  17  TYR   A HE1  1 
ATOM   445  H  HE2  A TYR   A 1 17  ? 12.539 -15.695 14.394  0.74 17.99 ?  17  TYR   A HE2  1 
ATOM   446  H  HE2  B TYR   A 1 17  ? 12.722 -15.659 14.718  0.26 16.59 ?  17  TYR   A HE2  1 
ATOM   447  H  HH   A TYR   A 1 17  ? 13.791 -17.497 14.847  0.74 19.49 ?  17  TYR   A HH   1 
ATOM   448  H  HH   B TYR   A 1 17  ? 15.519 -17.518 14.436  0.26 17.92 ?  17  TYR   A HH   1 
ATOM   449  N  N    A ILE   A 1 18  ? 11.969 -10.994 9.363   0.74 11.88 ?  18  ILE   A N    1 
ATOM   450  N  N    B ILE   A 1 18  ? 11.931 -10.770 9.741   0.26 10.24 ?  18  ILE   A N    1 
ATOM   451  C  CA   A ILE   A 1 18  ? 11.584 -9.801  8.605   0.74 11.66 ?  18  ILE   A CA   1 
ATOM   452  C  CA   B ILE   A 1 18  ? 11.554 -9.549  9.035   0.26 10.26 ?  18  ILE   A CA   1 
ATOM   453  C  C    A ILE   A 1 18  ? 10.615 -8.936  9.409   0.74 11.91 ?  18  ILE   A C    1 
ATOM   454  C  C    B ILE   A 1 18  ? 10.657 -8.688  9.916   0.26 10.31 ?  18  ILE   A C    1 
ATOM   455  O  O    A ILE   A 1 18  ? 9.788  -9.444  10.169  0.74 12.37 ?  18  ILE   A O    1 
ATOM   456  O  O    B ILE   A 1 18  ? 9.810  -9.202  10.655  0.26 10.44 ?  18  ILE   A O    1 
ATOM   457  C  CB   A ILE   A 1 18  ? 11.027 -10.205 7.219   0.74 11.37 ?  18  ILE   A CB   1 
ATOM   458  C  CB   B ILE   A 1 18  ? 10.898 -9.860  7.673   0.26 10.12 ?  18  ILE   A CB   1 
ATOM   459  C  CG1  A ILE   A 1 18  ? 10.977 -9.005  6.280   0.74 11.66 ?  18  ILE   A CG1  1 
ATOM   460  C  CG1  B ILE   A 1 18  ? 10.792 -8.592  6.822   0.26 11.16 ?  18  ILE   A CG1  1 
ATOM   461  C  CG2  A ILE   A 1 18  ? 9.677  -10.916 7.352   0.74 11.43 ?  18  ILE   A CG2  1 
ATOM   462  C  CG2  B ILE   A 1 18  ? 9.533  -10.506 7.863   0.26 10.20 ?  18  ILE   A CG2  1 
ATOM   463  C  CD1  A ILE   A 1 18  ? 10.727 -9.389  4.848   0.74 13.38 ?  18  ILE   A CD1  1 
ATOM   464  C  CD1  B ILE   A 1 18  ? 10.371 -8.860  5.391   0.26 12.12 ?  18  ILE   A CD1  1 
ATOM   465  H  H    A ILE   A 1 18  ? 11.349 -11.333 9.858   0.74 14.40 ?  18  ILE   A H    1 
ATOM   466  H  H    B ILE   A 1 18  ? 11.287 -11.130 10.188  0.26 12.43 ?  18  ILE   A H    1 
ATOM   467  H  HA   A ILE   A 1 18  ? 12.387 -9.284  8.451   0.74 14.13 ?  18  ILE   A HA   1 
ATOM   468  H  HA   B ILE   A 1 18  ? 12.355 -9.036  8.860   0.26 12.45 ?  18  ILE   A HA   1 
ATOM   469  H  HB   A ILE   A 1 18  ? 11.647 -10.849 6.832   0.74 13.79 ?  18  ILE   A HB   1 
ATOM   470  H  HB   B ILE   A 1 18  ? 11.468 -10.484 7.208   0.26 12.29 ?  18  ILE   A HB   1 
ATOM   471  H  HG12 A ILE   A 1 18  ? 10.268 -8.415  6.562   0.74 14.14 ?  18  ILE   A HG12 1 
ATOM   472  H  HG12 B ILE   A 1 18  ? 10.135 -7.996  7.218   0.26 13.54 ?  18  ILE   A HG12 1 
ATOM   473  H  HG13 A ILE   A 1 18  ? 11.832 -8.544  6.318   0.74 14.14 ?  18  ILE   A HG13 1 
ATOM   474  H  HG13 B ILE   A 1 18  ? 11.658 -8.153  6.798   0.26 13.54 ?  18  ILE   A HG13 1 
ATOM   475  H  HG21 A ILE   A 1 18  ? 9.425  -11.286 6.488   0.74 13.86 ?  18  ILE   A HG21 1 
ATOM   476  H  HG21 B ILE   A 1 18  ? 9.229  -10.854 7.009   0.26 12.38 ?  18  ILE   A HG21 1 
ATOM   477  H  HG22 A ILE   A 1 18  ? 9.756  -11.634 8.002   0.74 13.86 ?  18  ILE   A HG22 1 
ATOM   478  H  HG22 B ILE   A 1 18  ? 9.613  -11.227 8.505   0.26 12.38 ?  18  ILE   A HG22 1 
ATOM   479  H  HG23 A ILE   A 1 18  ? 9.008  -10.280 7.645   0.74 13.86 ?  18  ILE   A HG23 1 
ATOM   480  H  HG23 B ILE   A 1 18  ? 8.906  -9.840  8.189   0.26 12.38 ?  18  ILE   A HG23 1 
ATOM   481  H  HD11 A ILE   A 1 18  ? 10.774 -8.591  4.293   0.74 16.20 ?  18  ILE   A HD11 1 
ATOM   482  H  HD11 B ILE   A 1 18  ? 10.396 -8.028  4.892   0.26 14.69 ?  18  ILE   A HD11 1 
ATOM   483  H  HD12 A ILE   A 1 18  ? 11.400 -10.026 4.562   0.74 16.20 ?  18  ILE   A HD12 1 
ATOM   484  H  HD12 B ILE   A 1 18  ? 10.985 -9.500  4.997   0.26 14.69 ?  18  ILE   A HD12 1 
ATOM   485  H  HD13 A ILE   A 1 18  ? 9.844  -9.786  4.774   0.74 16.20 ?  18  ILE   A HD13 1 
ATOM   486  H  HD13 B ILE   A 1 18  ? 9.470  -9.220  5.388   0.26 14.69 ?  18  ILE   A HD13 1 
ATOM   487  N  N    A LYS   A 1 19  ? 10.706 -7.614  9.214   0.74 11.33 ?  19  LYS   A N    1 
ATOM   488  N  N    B LYS   A 1 19  ? 10.852 -7.369  9.830   0.26 10.91 ?  19  LYS   A N    1 
ATOM   489  C  CA   A LYS   A 1 19  ? 9.882  -6.651  9.942   0.74 12.20 ?  19  LYS   A CA   1 
ATOM   490  C  CA   B LYS   A 1 19  ? 10.097 -6.409  10.621  0.26 12.19 ?  19  LYS   A CA   1 
ATOM   491  C  C    A LYS   A 1 19  ? 9.701  -5.393  9.099   0.74 12.25 ?  19  LYS   A C    1 
ATOM   492  C  C    B LYS   A 1 19  ? 9.846  -5.175  9.773   0.26 12.73 ?  19  LYS   A C    1 
ATOM   493  O  O    A LYS   A 1 19  ? 10.604 -5.001  8.355   0.74 12.16 ?  19  LYS   A O    1 
ATOM   494  O  O    B LYS   A 1 19  ? 10.704 -4.771  8.984   0.26 12.79 ?  19  LYS   A O    1 
ATOM   495  C  CB   A LYS   A 1 19  ? 10.574 -6.274  11.261  0.74 13.89 ?  19  LYS   A CB   1 
ATOM   496  C  CB   B LYS   A 1 19  ? 10.878 -6.010  11.880  0.26 12.77 ?  19  LYS   A CB   1 
ATOM   497  C  CG   A LYS   A 1 19  ? 9.815  -5.323  12.174  0.74 15.55 ?  19  LYS   A CG   1 
ATOM   498  C  CG   B LYS   A 1 19  ? 10.168 -5.062  12.833  0.26 13.69 ?  19  LYS   A CG   1 
ATOM   499  C  CD   A LYS   A 1 19  ? 10.669 -5.043  13.404  0.74 17.27 ?  19  LYS   A CD   1 
ATOM   500  C  CD   B LYS   A 1 19  ? 11.089 -4.727  14.000  0.26 14.31 ?  19  LYS   A CD   1 
ATOM   501  C  CE   A LYS   A 1 19  ? 10.000 -4.105  14.385  0.74 18.49 ?  19  LYS   A CE   1 
ATOM   502  C  CE   B LYS   A 1 19  ? 10.402 -3.888  15.061  0.26 14.86 ?  19  LYS   A CE   1 
ATOM   503  N  NZ   A LYS   A 1 19  ? 10.887 -3.841  15.553  0.74 18.99 ?  19  LYS   A NZ   1 
ATOM   504  N  NZ   B LYS   A 1 19  ? 11.275 -3.727  16.258  0.26 15.12 ?  19  LYS   A NZ   1 
ATOM   505  H  H    A LYS   A 1 19  ? 11.252 -7.261  8.657   0.74 13.74 ?  19  LYS   A H    1 
ATOM   506  H  H    B LYS   A 1 19  ? 11.436 -6.990  9.307   0.26 13.23 ?  19  LYS   A H    1 
ATOM   507  H  HA   A LYS   A 1 19  ? 9.014  -7.049  10.139  0.74 14.78 ?  19  LYS   A HA   1 
ATOM   508  H  HA   B LYS   A 1 19  ? 9.248  -6.787  10.884  0.26 14.77 ?  19  LYS   A HA   1 
ATOM   509  H  HB2  A LYS   A 1 19  ? 10.731 -7.088  11.766  0.74 16.81 ?  19  LYS   A HB2  1 
ATOM   510  H  HB2  B LYS   A 1 19  ? 11.079 -6.812  12.382  0.26 15.46 ?  19  LYS   A HB2  1 
ATOM   511  H  HB3  A LYS   A 1 19  ? 11.420 -5.859  11.047  0.74 16.81 ?  19  LYS   A HB3  1 
ATOM   512  H  HB3  B LYS   A 1 19  ? 11.705 -5.579  11.612  0.26 15.46 ?  19  LYS   A HB3  1 
ATOM   513  H  HG2  A LYS   A 1 19  ? 9.648  -4.485  11.711  0.74 18.80 ?  19  LYS   A HG2  1 
ATOM   514  H  HG2  B LYS   A 1 19  ? 9.945  -4.237  12.375  0.26 16.56 ?  19  LYS   A HG2  1 
ATOM   515  H  HG3  A LYS   A 1 19  ? 8.980  -5.730  12.458  0.74 18.80 ?  19  LYS   A HG3  1 
ATOM   516  H  HG3  B LYS   A 1 19  ? 9.370  -5.486  13.185  0.26 16.56 ?  19  LYS   A HG3  1 
ATOM   517  H  HD2  A LYS   A 1 19  ? 10.847 -5.881  13.861  0.74 20.86 ?  19  LYS   A HD2  1 
ATOM   518  H  HD2  B LYS   A 1 19  ? 11.382 -5.552  14.418  0.26 17.32 ?  19  LYS   A HD2  1 
ATOM   519  H  HD3  A LYS   A 1 19  ? 11.505 -4.638  13.121  0.74 20.86 ?  19  LYS   A HD3  1 
ATOM   520  H  HD3  B LYS   A 1 19  ? 11.853 -4.231  13.669  0.26 17.32 ?  19  LYS   A HD3  1 
ATOM   521  H  HE2  A LYS   A 1 19  ? 9.813  -3.261  13.945  0.74 22.33 ?  19  LYS   A HE2  1 
ATOM   522  H  HE2  B LYS   A 1 19  ? 10.212 -3.008  14.702  0.26 17.97 ?  19  LYS   A HE2  1 
ATOM   523  H  HE3  A LYS   A 1 19  ? 9.180  -4.508  14.707  0.74 22.33 ?  19  LYS   A HE3  1 
ATOM   524  H  HE3  B LYS   A 1 19  ? 9.583  -4.326  15.338  0.26 17.97 ?  19  LYS   A HE3  1 
ATOM   525  H  HZ1  A LYS   A 1 19  ? 10.477 -3.302  16.129  0.74 22.93 ?  19  LYS   A HZ1  1 
ATOM   526  H  HZ1  B LYS   A 1 19  ? 10.861 -3.234  16.873  0.26 18.29 ?  19  LYS   A HZ1  1 
ATOM   527  H  HZ2  A LYS   A 1 19  ? 11.086 -4.606  15.962  0.74 22.93 ?  19  LYS   A HZ2  1 
ATOM   528  H  HZ2  B LYS   A 1 19  ? 11.463 -4.524  16.607  0.26 18.29 ?  19  LYS   A HZ2  1 
ATOM   529  H  HZ3  A LYS   A 1 19  ? 11.640 -3.454  15.281  0.74 22.93 ?  19  LYS   A HZ3  1 
ATOM   530  H  HZ3  B LYS   A 1 19  ? 12.035 -3.325  16.029  0.26 18.29 ?  19  LYS   A HZ3  1 
ATOM   531  N  N    A ASN   A 1 20  ? 8.527  -4.764  9.211   0.74 13.11 ?  20  ASN   A N    1 
ATOM   532  N  N    B ASN   A 1 20  ? 8.667  -4.583  9.933   0.26 13.86 ?  20  ASN   A N    1 
ATOM   533  C  CA   A ASN   A 1 20  ? 8.302  -3.441  8.628   0.74 14.55 ?  20  ASN   A CA   1 
ATOM   534  C  CA   B ASN   A 1 20  ? 8.335  -3.330  9.264   0.26 15.40 ?  20  ASN   A CA   1 
ATOM   535  C  C    A ASN   A 1 20  ? 8.911  -2.416  9.579   0.74 15.74 ?  20  ASN   A C    1 
ATOM   536  C  C    B ASN   A 1 20  ? 8.957  -2.198  10.068  0.26 15.91 ?  20  ASN   A C    1 
ATOM   537  O  O    A ASN   A 1 20  ? 8.372  -2.170  10.662  0.74 17.30 ?  20  ASN   A O    1 
ATOM   538  O  O    B ASN   A 1 20  ? 8.395  -1.748  11.070  0.26 16.55 ?  20  ASN   A O    1 
ATOM   539  C  CB   A ASN   A 1 20  ? 6.804  -3.210  8.416   0.74 15.53 ?  20  ASN   A CB   1 
ATOM   540  C  CB   B ASN   A 1 20  ? 6.824  -3.170  9.173   0.26 16.56 ?  20  ASN   A CB   1 
ATOM   541  C  CG   A ASN   A 1 20  ? 6.462  -1.782  8.002   0.74 17.00 ?  20  ASN   A CG   1 
ATOM   542  C  CG   B ASN   A 1 20  ? 6.413  -1.812  8.649   0.26 17.80 ?  20  ASN   A CG   1 
ATOM   543  O  OD1  A ASN   A 1 20  ? 5.435  -1.244  8.417   0.74 18.93 ?  20  ASN   A OD1  1 
ATOM   544  O  OD1  B ASN   A 1 20  ? 5.784  -1.025  9.356   0.26 18.37 ?  20  ASN   A OD1  1 
ATOM   545  N  ND2  A ASN   A 1 20  ? 7.303  -1.173  7.174   0.74 17.18 ?  20  ASN   A ND2  1 
ATOM   546  N  ND2  B ASN   A 1 20  ? 6.774  -1.525  7.406   0.26 18.21 ?  20  ASN   A ND2  1 
ATOM   547  H  H    A ASN   A 1 20  ? 7.843  -5.094  9.620   0.74 15.87 ?  20  ASN   A H    1 
ATOM   548  H  H    B ASN   A 1 20  ? 8.038  -4.891  10.427  0.26 16.78 ?  20  ASN   A H    1 
ATOM   549  H  HA   A ASN   A 1 20  ? 8.753  -3.390  7.771   0.74 17.60 ?  20  ASN   A HA   1 
ATOM   550  H  HA   B ASN   A 1 20  ? 8.711  -3.322  8.370   0.26 18.62 ?  20  ASN   A HA   1 
ATOM   551  H  HB2  A ASN   A 1 20  ? 6.489  -3.800  7.715   0.74 18.77 ?  20  ASN   A HB2  1 
ATOM   552  H  HB2  B ASN   A 1 20  ? 6.473  -3.847  8.573   0.26 20.01 ?  20  ASN   A HB2  1 
ATOM   553  H  HB3  A ASN   A 1 20  ? 6.338  -3.409  9.243   0.74 18.77 ?  20  ASN   A HB3  1 
ATOM   554  H  HB3  B ASN   A 1 20  ? 6.442  -3.282  10.058  0.26 20.01 ?  20  ASN   A HB3  1 
ATOM   555  H  HD21 A ASN   A 1 20  ? 7.143  -0.368  6.924   0.74 20.75 ?  20  ASN   A HD21 1 
ATOM   556  H  HD21 B ASN   A 1 20  ? 6.562  -0.768  7.062   0.26 21.99 ?  20  ASN   A HD21 1 
ATOM   557  H  HD22 A ASN   A 1 20  ? 8.002  -1.584  6.893   0.74 20.75 ?  20  ASN   A HD22 1 
ATOM   558  H  HD22 B ASN   A 1 20  ? 7.222  -2.098  6.945   0.26 21.99 ?  20  ASN   A HD22 1 
ATOM   559  N  N    A ALA   A 1 21  ? 10.054 -1.843  9.204   0.74 15.79 ?  21  ALA   A N    1 
ATOM   560  N  N    B ALA   A 1 21  ? 10.127 -1.735  9.633   0.26 15.95 ?  21  ALA   A N    1 
ATOM   561  C  CA   A ALA   A 1 21  ? 10.749 -0.953  10.125  0.74 16.25 ?  21  ALA   A CA   1 
ATOM   562  C  CA   B ALA   A 1 21  ? 10.827 -0.679  10.347  0.26 15.85 ?  21  ALA   A CA   1 
ATOM   563  C  C    A ALA   A 1 21  ? 11.718 -0.062  9.372   0.74 15.92 ?  21  ALA   A C    1 
ATOM   564  C  C    B ALA   A 1 21  ? 11.918 -0.116  9.452   0.26 15.45 ?  21  ALA   A C    1 
ATOM   565  O  O    A ALA   A 1 21  ? 12.186 -0.402  8.281   0.74 15.83 ?  21  ALA   A O    1 
ATOM   566  O  O    B ALA   A 1 21  ? 12.517 -0.849  8.664   0.26 15.58 ?  21  ALA   A O    1 
ATOM   567  C  CB   A ALA   A 1 21  ? 11.504 -1.738  11.200  0.74 17.35 ?  21  ALA   A CB   1 
ATOM   568  C  CB   B ALA   A 1 21  ? 11.443 -1.220  11.644  0.26 16.42 ?  21  ALA   A CB   1 
ATOM   569  H  H    A ALA   A 1 21  ? 10.435 -1.953  8.440   0.74 19.09 ?  21  ALA   A H    1 
ATOM   570  H  H    B ALA   A 1 21  ? 10.537 -2.017  8.931   0.26 19.28 ?  21  ALA   A H    1 
ATOM   571  H  HA   A ALA   A 1 21  ? 10.091 -0.390  10.565  0.74 19.64 ?  21  ALA   A HA   1 
ATOM   572  H  HA   B ALA   A 1 21  ? 10.208 0.033   10.572  0.26 19.17 ?  21  ALA   A HA   1 
ATOM   573  H  HB1  A ALA   A 1 21  ? 11.934 -1.109  11.797  0.74 20.96 ?  21  ALA   A HB1  1 
ATOM   574  H  HB1  B ALA   A 1 21  ? 11.920 -0.505  12.093  0.26 19.84 ?  21  ALA   A HB1  1 
ATOM   575  H  HB2  A ALA   A 1 21  ? 10.869 -2.284  11.693  0.74 20.96 ?  21  ALA   A HB2  1 
ATOM   576  H  HB2  B ALA   A 1 21  ? 10.734 -1.555  12.218  0.26 19.84 ?  21  ALA   A HB2  1 
ATOM   577  H  HB3  A ALA   A 1 21  ? 12.163 -2.301  10.772  0.74 20.96 ?  21  ALA   A HB3  1 
ATOM   578  H  HB3  B ALA   A 1 21  ? 12.056 -1.940  11.426  0.26 19.84 ?  21  ALA   A HB3  1 
ATOM   579  N  N    A ASP   A 1 22  ? 12.007 1.087   9.990   0.74 16.24 ?  22  ASP   A N    1 
ATOM   580  N  N    B ASP   A 1 22  ? 12.143 1.191   9.560   0.26 14.98 ?  22  ASP   A N    1 
ATOM   581  C  CA   A ASP   A 1 22  ? 13.054 2.004   9.548   0.74 16.43 ?  22  ASP   A CA   1 
ATOM   582  C  CA   B ASP   A 1 22  ? 13.335 1.804   8.989   0.26 14.72 ?  22  ASP   A CA   1 
ATOM   583  C  C    A ASP   A 1 22  ? 14.378 1.507   10.118  0.74 15.07 ?  22  ASP   A C    1 
ATOM   584  C  C    B ASP   A 1 22  ? 14.567 1.176   9.629   0.26 13.88 ?  22  ASP   A C    1 
ATOM   585  O  O    A ASP   A 1 22  ? 14.568 1.493   11.339  0.74 15.65 ?  22  ASP   A O    1 
ATOM   586  O  O    B ASP   A 1 22  ? 14.664 1.086   10.856  0.26 13.84 ?  22  ASP   A O    1 
ATOM   587  C  CB   A ASP   A 1 22  ? 12.725 3.407   10.056  0.74 18.64 ?  22  ASP   A CB   1 
ATOM   588  C  CB   B ASP   A 1 22  ? 13.294 3.308   9.276   0.26 15.60 ?  22  ASP   A CB   1 
ATOM   589  C  CG   A ASP   A 1 22  ? 13.732 4.456   9.609   0.74 21.14 ?  22  ASP   A CG   1 
ATOM   590  C  CG   B ASP   A 1 22  ? 14.404 4.085   8.591   0.26 16.20 ?  22  ASP   A CG   1 
ATOM   591  O  OD1  A ASP   A 1 22  ? 14.857 4.104   9.205   0.74 21.51 ?  22  ASP   A OD1  1 
ATOM   592  O  OD1  B ASP   A 1 22  ? 15.330 3.464   8.033   0.26 16.18 ?  22  ASP   A OD1  1 
ATOM   593  O  OD2  A ASP   A 1 22  ? 13.399 5.657   9.676   0.74 23.06 -1 22  ASP   A OD2  1 
ATOM   594  O  OD2  B ASP   A 1 22  ? 14.346 5.333   8.619   0.26 16.63 -1 22  ASP   A OD2  1 
ATOM   595  H  H    A ASP   A 1 22  ? 11.579 1.372   10.688  0.74 19.63 ?  22  ASP   A H    1 
ATOM   596  H  H    B ASP   A 1 22  ? 11.609 1.742   9.949   0.26 18.12 ?  22  ASP   A H    1 
ATOM   597  H  HA   A ASP   A 1 22  ? 13.101 2.011   8.581   0.74 19.86 ?  22  ASP   A HA   1 
ATOM   598  H  HA   B ASP   A 1 22  ? 13.368 1.655   8.031   0.26 17.80 ?  22  ASP   A HA   1 
ATOM   599  H  HB2  A ASP   A 1 22  ? 11.848 3.664   9.723   0.74 22.51 ?  22  ASP   A HB2  1 
ATOM   600  H  HB2  B ASP   A 1 22  ? 12.447 3.665   8.974   0.26 18.87 ?  22  ASP   A HB2  1 
ATOM   601  H  HB3  A ASP   A 1 22  ? 12.711 3.392   11.028  0.74 22.51 ?  22  ASP   A HB3  1 
ATOM   602  H  HB3  B ASP   A 1 22  ? 13.397 3.442   10.227  0.26 18.87 ?  22  ASP   A HB3  1 
ATOM   603  N  N    A ILE   A 1 23  ? 15.293 1.092   9.235   0.74 14.37 ?  23  ILE   A N    1 
ATOM   604  N  N    B ILE   A 1 23  ? 15.506 0.721   8.793   0.26 13.55 ?  23  ILE   A N    1 
ATOM   605  C  CA   A ILE   A 1 23  ? 16.547 0.483   9.674   0.74 13.76 ?  23  ILE   A CA   1 
ATOM   606  C  CA   B ILE   A 1 23  ? 16.714 0.085   9.316   0.26 13.14 ?  23  ILE   A CA   1 
ATOM   607  C  C    A ILE   A 1 23  ? 17.344 1.431   10.558  0.74 13.76 ?  23  ILE   A C    1 
ATOM   608  C  C    B ILE   A 1 23  ? 17.470 1.040   10.227  0.26 13.61 ?  23  ILE   A C    1 
ATOM   609  O  O    A ILE   A 1 23  ? 18.068 0.989   11.459  0.74 14.17 ?  23  ILE   A O    1 
ATOM   610  O  O    B ILE   A 1 23  ? 18.107 0.614   11.198  0.26 13.75 ?  23  ILE   A O    1 
ATOM   611  C  CB   A ILE   A 1 23  ? 17.358 -0.023  8.460   0.74 13.46 ?  23  ILE   A CB   1 
ATOM   612  C  CB   B ILE   A 1 23  ? 17.605 -0.469  8.180   0.26 12.35 ?  23  ILE   A CB   1 
ATOM   613  C  CG1  A ILE   A 1 23  ? 18.507 -0.926  8.917   0.74 13.38 ?  23  ILE   A CG1  1 
ATOM   614  C  CG1  B ILE   A 1 23  ? 18.675 -1.397  8.766   0.26 11.74 ?  23  ILE   A CG1  1 
ATOM   615  C  CG2  A ILE   A 1 23  ? 17.857 1.141   7.610   0.74 13.56 ?  23  ILE   A CG2  1 
ATOM   616  C  CG2  B ILE   A 1 23  ? 18.250 0.662   7.380   0.26 12.32 ?  23  ILE   A CG2  1 
ATOM   617  C  CD1  A ILE   A 1 23  ? 19.208 -1.642  7.781   0.74 13.68 ?  23  ILE   A CD1  1 
ATOM   618  C  CD1  B ILE   A 1 23  ? 19.624 -1.991  7.744   0.26 11.42 ?  23  ILE   A CD1  1 
ATOM   619  H  H    A ILE   A 1 23  ? 15.202 1.152   8.387   0.74 17.38 ?  23  ILE   A H    1 
ATOM   620  H  H    B ILE   A 1 23  ? 15.468 0.765   7.943   0.26 16.40 ?  23  ILE   A H    1 
ATOM   621  H  HA   A ILE   A 1 23  ? 16.334 -0.289  10.213  0.74 16.66 ?  23  ILE   A HA   1 
ATOM   622  H  HA   B ILE   A 1 23  ? 16.440 -0.672  9.852   0.26 15.91 ?  23  ILE   A HA   1 
ATOM   623  H  HB   A ILE   A 1 23  ? 16.764 -0.555  7.909   0.74 16.30 ?  23  ILE   A HB   1 
ATOM   624  H  HB   B ILE   A 1 23  ? 17.049 -0.989  7.579   0.26 14.96 ?  23  ILE   A HB   1 
ATOM   625  H  HG12 A ILE   A 1 23  ? 19.168 -0.385  9.376   0.74 16.19 ?  23  ILE   A HG12 1 
ATOM   626  H  HG12 B ILE   A 1 23  ? 19.208 -0.898  9.403   0.26 14.23 ?  23  ILE   A HG12 1 
ATOM   627  H  HG13 A ILE   A 1 23  ? 18.156 -1.599  9.519   0.74 16.19 ?  23  ILE   A HG13 1 
ATOM   628  H  HG13 B ILE   A 1 23  ? 18.233 -2.134  9.217   0.26 14.23 ?  23  ILE   A HG13 1 
ATOM   629  H  HG21 A ILE   A 1 23  ? 18.216 0.796   6.777   0.74 16.41 ?  23  ILE   A HG21 1 
ATOM   630  H  HG21 B ILE   A 1 23  ? 18.629 0.294   6.563   0.26 14.93 ?  23  ILE   A HG21 1 
ATOM   631  H  HG22 A ILE   A 1 23  ? 17.111 1.737   7.422   0.74 16.41 ?  23  ILE   A HG22 1 
ATOM   632  H  HG22 B ILE   A 1 23  ? 17.572 1.318   7.160   0.26 14.93 ?  23  ILE   A HG22 1 
ATOM   633  H  HG23 A ILE   A 1 23  ? 18.545 1.620   8.095   0.74 16.41 ?  23  ILE   A HG23 1 
ATOM   634  H  HG23 B ILE   A 1 23  ? 18.949 1.070   7.913   0.26 14.93 ?  23  ILE   A HG23 1 
ATOM   635  H  HD11 A ILE   A 1 23  ? 19.873 -2.241  8.151   0.74 16.56 ?  23  ILE   A HD11 1 
ATOM   636  H  HD11 B ILE   A 1 23  ? 20.177 -2.660  8.181   0.26 13.84 ?  23  ILE   A HD11 1 
ATOM   637  H  HD12 A ILE   A 1 23  ? 18.550 -2.148  7.277   0.74 16.56 ?  23  ILE   A HD12 1 
ATOM   638  H  HD12 B ILE   A 1 23  ? 19.107 -2.402  7.035   0.26 13.84 ?  23  ILE   A HD12 1 
ATOM   639  H  HD13 A ILE   A 1 23  ? 19.632 -0.986  7.208   0.74 16.56 ?  23  ILE   A HD13 1 
ATOM   640  H  HD13 B ILE   A 1 23  ? 20.183 -1.286  7.384   0.26 13.84 ?  23  ILE   A HD13 1 
ATOM   641  N  N    A VAL   A 1 24  ? 17.222 2.740   10.328  0.74 14.61 ?  24  VAL   A N    1 
ATOM   642  N  N    B VAL   A 1 24  ? 17.408 2.340   9.939   0.26 14.41 ?  24  VAL   A N    1 
ATOM   643  C  CA   A VAL   A 1 24  ? 17.907 3.709   11.180  0.74 15.72 ?  24  VAL   A CA   1 
ATOM   644  C  CA   B VAL   A 1 24  ? 18.040 3.327   10.809  0.26 15.46 ?  24  VAL   A CA   1 
ATOM   645  C  C    A VAL   A 1 24  ? 17.381 3.624   12.606  0.74 16.38 ?  24  VAL   A C    1 
ATOM   646  C  C    B VAL   A 1 24  ? 17.384 3.321   12.182  0.26 16.21 ?  24  VAL   A C    1 
ATOM   647  O  O    A VAL   A 1 24  ? 18.153 3.536   13.571  0.74 16.83 ?  24  VAL   A O    1 
ATOM   648  O  O    B VAL   A 1 24  ? 18.065 3.398   13.213  0.26 16.71 ?  24  VAL   A O    1 
ATOM   649  C  CB   A VAL   A 1 24  ? 17.759 5.128   10.602  0.74 16.83 ?  24  VAL   A CB   1 
ATOM   650  C  CB   B VAL   A 1 24  ? 17.993 4.717   10.151  0.26 15.87 ?  24  VAL   A CB   1 
ATOM   651  C  CG1  A VAL   A 1 24  ? 18.252 6.174   11.597  0.74 17.69 ?  24  VAL   A CG1  1 
ATOM   652  C  CG1  B VAL   A 1 24  ? 18.635 5.752   11.054  0.26 16.35 ?  24  VAL   A CG1  1 
ATOM   653  C  CG2  A VAL   A 1 24  ? 18.507 5.241   9.280   0.74 17.69 ?  24  VAL   A CG2  1 
ATOM   654  C  CG2  B VAL   A 1 24  ? 18.680 4.675   8.798   0.26 15.87 ?  24  VAL   A CG2  1 
ATOM   655  H  H    A VAL   A 1 24  ? 16.753 3.089   9.696   0.74 17.67 ?  24  VAL   A H    1 
ATOM   656  H  H    B VAL   A 1 24  ? 17.009 2.671   9.257   0.26 17.44 ?  24  VAL   A H    1 
ATOM   657  H  HA   A VAL   A 1 24  ? 18.852 3.500   11.199  0.74 19.01 ?  24  VAL   A HA   1 
ATOM   658  H  HA   B VAL   A 1 24  ? 18.970 3.087   10.930  0.26 18.70 ?  24  VAL   A HA   1 
ATOM   659  H  HB   A VAL   A 1 24  ? 16.823 5.305   10.422  0.74 20.34 ?  24  VAL   A HB   1 
ATOM   660  H  HB   B VAL   A 1 24  ? 17.068 4.971   10.011  0.26 19.18 ?  24  VAL   A HB   1 
ATOM   661  H  HG11 A VAL   A 1 24  ? 18.412 7.007   11.126  0.74 21.36 ?  24  VAL   A HG11 1 
ATOM   662  H  HG11 B VAL   A 1 24  ? 18.766 6.568   10.550  0.26 19.76 ?  24  VAL   A HG11 1 
ATOM   663  H  HG12 A VAL   A 1 24  ? 17.573 6.306   12.276  0.74 21.36 ?  24  VAL   A HG12 1 
ATOM   664  H  HG12 B VAL   A 1 24  ? 18.050 5.919   11.810  0.26 19.76 ?  24  VAL   A HG12 1 
ATOM   665  H  HG13 A VAL   A 1 24  ? 19.074 5.860   12.002  0.74 21.36 ?  24  VAL   A HG13 1 
ATOM   666  H  HG13 B VAL   A 1 24  ? 19.489 5.412   11.363  0.26 19.76 ?  24  VAL   A HG13 1 
ATOM   667  H  HG21 A VAL   A 1 24  ? 18.272 6.079   8.850   0.74 21.37 ?  24  VAL   A HG21 1 
ATOM   668  H  HG21 B VAL   A 1 24  ? 18.750 5.578   8.453   0.26 19.18 ?  24  VAL   A HG21 1 
ATOM   669  H  HG22 A VAL   A 1 24  ? 19.463 5.220   9.453   0.74 21.37 ?  24  VAL   A HG22 1 
ATOM   670  H  HG22 B VAL   A 1 24  ? 19.566 4.294   8.907   0.26 19.18 ?  24  VAL   A HG22 1 
ATOM   671  H  HG23 A VAL   A 1 24  ? 18.260 4.497   8.707   0.74 21.37 ?  24  VAL   A HG23 1 
ATOM   672  H  HG23 B VAL   A 1 24  ? 18.158 4.127   8.193   0.26 19.18 ?  24  VAL   A HG23 1 
ATOM   673  N  N    A GLU   A 1 25  ? 16.055 3.653   12.758  0.74 17.34 ?  25  GLU   A N    1 
ATOM   674  N  N    B GLU   A 1 25  ? 16.052 3.221   12.222  0.26 16.85 ?  25  GLU   A N    1 
ATOM   675  C  CA   A GLU   A 1 25  ? 15.463 3.586   14.089  0.74 18.75 ?  25  GLU   A CA   1 
ATOM   676  C  CA   B GLU   A 1 25  ? 15.355 3.165   13.503  0.26 17.80 ?  25  GLU   A CA   1 
ATOM   677  C  C    A GLU   A 1 25  ? 15.703 2.226   14.731  0.74 17.81 ?  25  GLU   A C    1 
ATOM   678  C  C    B GLU   A 1 25  ? 15.631 1.854   14.230  0.26 17.73 ?  25  GLU   A C    1 
ATOM   679  O  O    A GLU   A 1 25  ? 15.931 2.139   15.942  0.74 18.56 ?  25  GLU   A O    1 
ATOM   680  O  O    B GLU   A 1 25  ? 15.791 1.842   15.456  0.26 17.63 ?  25  GLU   A O    1 
ATOM   681  C  CB   A GLU   A 1 25  ? 13.970 3.916   14.015  0.74 21.18 ?  25  GLU   A CB   1 
ATOM   682  C  CB   B GLU   A 1 25  ? 13.856 3.386   13.299  0.26 19.00 ?  25  GLU   A CB   1 
ATOM   683  C  CG   A GLU   A 1 25  ? 13.699 5.369   13.652  0.74 24.20 ?  25  GLU   A CG   1 
ATOM   684  C  CG   B GLU   A 1 25  ? 13.517 4.780   12.789  0.26 20.51 ?  25  GLU   A CG   1 
ATOM   685  C  CD   A GLU   A 1 25  ? 14.477 6.340   14.520  0.74 26.79 ?  25  GLU   A CD   1 
ATOM   686  C  CD   B GLU   A 1 25  ? 13.990 5.875   13.726  0.26 21.87 ?  25  GLU   A CD   1 
ATOM   687  O  OE1  A GLU   A 1 25  ? 14.566 6.110   15.746  0.74 27.54 ?  25  GLU   A OE1  1 
ATOM   688  O  OE1  B GLU   A 1 25  ? 13.949 5.663   14.956  0.26 22.44 ?  25  GLU   A OE1  1 
ATOM   689  O  OE2  A GLU   A 1 25  ? 15.021 7.319   13.971  0.74 28.02 -1 25  GLU   A OE2  1 
ATOM   690  O  OE2  B GLU   A 1 25  ? 14.412 6.942   13.231  0.26 22.56 -1 25  GLU   A OE2  1 
ATOM   691  H  H    A GLU   A 1 25  ? 15.487 3.720   12.113  0.74 20.94 ?  25  GLU   A H    1 
ATOM   692  H  H    B GLU   A 1 25  ? 15.539 3.187   11.531  0.26 20.36 ?  25  GLU   A H    1 
ATOM   693  H  HA   A GLU   A 1 25  ? 15.890 4.247   14.654  0.74 22.64 ?  25  GLU   A HA   1 
ATOM   694  H  HA   B GLU   A 1 25  ? 15.685 3.878   14.065  0.26 21.50 ?  25  GLU   A HA   1 
ATOM   695  H  HB2  A GLU   A 1 25  ? 13.551 3.362   13.335  0.74 25.56 ?  25  GLU   A HB2  1 
ATOM   696  H  HB2  B GLU   A 1 25  ? 13.526 2.743   12.649  0.26 22.94 ?  25  GLU   A HB2  1 
ATOM   697  H  HB3  A GLU   A 1 25  ? 13.559 3.747   14.877  0.74 25.56 ?  25  GLU   A HB3  1 
ATOM   698  H  HB3  B GLU   A 1 25  ? 13.400 3.259   14.146  0.26 22.94 ?  25  GLU   A HB3  1 
ATOM   699  H  HG2  A GLU   A 1 25  ? 13.967 5.524   12.734  0.74 29.18 ?  25  GLU   A HG2  1 
ATOM   700  H  HG2  B GLU   A 1 25  ? 13.953 4.917   11.934  0.26 24.75 ?  25  GLU   A HG2  1 
ATOM   701  H  HG3  A GLU   A 1 25  ? 12.752 5.555   13.759  0.74 29.18 ?  25  GLU   A HG3  1 
ATOM   702  H  HG3  B GLU   A 1 25  ? 12.556 4.856   12.692  0.26 24.75 ?  25  GLU   A HG3  1 
ATOM   703  N  N    A GLU   A 1 26  ? 15.681 1.157   13.933  0.74 17.20 ?  26  GLU   A N    1 
ATOM   704  N  N    B GLU   A 1 26  ? 15.692 0.739   13.496  0.26 17.70 ?  26  GLU   A N    1 
ATOM   705  C  CA   A GLU   A 1 26  ? 15.974 -0.168  14.469  0.74 17.14 ?  26  GLU   A CA   1 
ATOM   706  C  CA   B GLU   A 1 26  ? 16.077 -0.525  14.118  0.26 18.07 ?  26  GLU   A CA   1 
ATOM   707  C  C    A GLU   A 1 26  ? 17.400 -0.236  15.003  0.74 16.14 ?  26  GLU   A C    1 
ATOM   708  C  C    B GLU   A 1 26  ? 17.489 -0.464  14.680  0.26 18.06 ?  26  GLU   A C    1 
ATOM   709  O  O    A GLU   A 1 26  ? 17.640 -0.732  16.109  0.74 16.00 ?  26  GLU   A O    1 
ATOM   710  O  O    B GLU   A 1 26  ? 17.791 -1.129  15.677  0.26 17.76 ?  26  GLU   A O    1 
ATOM   711  C  CB   A GLU   A 1 26  ? 15.766 -1.226  13.387  0.74 18.89 ?  26  GLU   A CB   1 
ATOM   712  C  CB   B GLU   A 1 26  ? 15.970 -1.672  13.110  0.26 18.40 ?  26  GLU   A CB   1 
ATOM   713  C  CG   A GLU   A 1 26  ? 14.341 -1.706  13.227  0.74 22.22 ?  26  GLU   A CG   1 
ATOM   714  C  CG   B GLU   A 1 26  ? 14.569 -2.212  12.923  0.26 18.48 ?  26  GLU   A CG   1 
ATOM   715  C  CD   A GLU   A 1 26  ? 13.835 -2.481  14.429  0.74 24.53 ?  26  GLU   A CD   1 
ATOM   716  C  CD   B GLU   A 1 26  ? 13.969 -2.755  14.204  0.26 18.27 ?  26  GLU   A CD   1 
ATOM   717  O  OE1  A GLU   A 1 26  ? 14.428 -3.526  14.775  0.74 25.24 ?  26  GLU   A OE1  1 
ATOM   718  O  OE1  B GLU   A 1 26  ? 14.376 -3.852  14.660  0.26 18.29 ?  26  GLU   A OE1  1 
ATOM   719  O  OE2  A GLU   A 1 26  ? 12.841 -2.029  15.028  0.74 26.11 -1 26  GLU   A OE2  1 
ATOM   720  O  OE2  B GLU   A 1 26  ? 13.077 -2.083  14.754  0.26 17.64 -1 26  GLU   A OE2  1 
ATOM   721  H  H    A GLU   A 1 26  ? 15.505 1.181   13.092  0.74 20.78 ?  26  GLU   A H    1 
ATOM   722  H  H    B GLU   A 1 26  ? 15.516 0.687   12.656  0.26 21.38 ?  26  GLU   A H    1 
ATOM   723  H  HA   A GLU   A 1 26  ? 15.366 -0.351  15.198  0.74 20.71 ?  26  GLU   A HA   1 
ATOM   724  H  HA   B GLU   A 1 26  ? 15.478 -0.710  14.855  0.26 21.82 ?  26  GLU   A HA   1 
ATOM   725  H  HB2  A GLU   A 1 26  ? 16.045 -0.852  12.533  0.74 22.81 ?  26  GLU   A HB2  1 
ATOM   726  H  HB2  B GLU   A 1 26  ? 16.279 -1.358  12.244  0.26 22.22 ?  26  GLU   A HB2  1 
ATOM   727  H  HB3  A GLU   A 1 26  ? 16.317 -1.992  13.599  0.74 22.81 ?  26  GLU   A HB3  1 
ATOM   728  H  HB3  B GLU   A 1 26  ? 16.528 -2.407  13.408  0.26 22.22 ?  26  GLU   A HB3  1 
ATOM   729  H  HG2  A GLU   A 1 26  ? 13.759 -0.942  13.128  0.74 26.81 ?  26  GLU   A HG2  1 
ATOM   730  H  HG2  B GLU   A 1 26  ? 14.004 -1.500  12.582  0.26 22.31 ?  26  GLU   A HG2  1 
ATOM   731  H  HG3  A GLU   A 1 26  ? 14.287 -2.271  12.439  0.74 26.81 ?  26  GLU   A HG3  1 
ATOM   732  H  HG3  B GLU   A 1 26  ? 14.591 -2.950  12.300  0.26 22.31 ?  26  GLU   A HG3  1 
ATOM   733  N  N    A ALA   A 1 27  ? 18.367 0.252   14.222  0.74 15.40 ?  27  ALA   A N    1 
ATOM   734  N  N    B ALA   A 1 27  ? 18.366 0.324   14.060  0.26 18.30 ?  27  ALA   A N    1 
ATOM   735  C  CA   A ALA   A 1 27  ? 19.757 0.208   14.667  0.74 15.73 ?  27  ALA   A CA   1 
ATOM   736  C  CA   B ALA   A 1 27  ? 19.755 0.368   14.506  0.26 18.95 ?  27  ALA   A CA   1 
ATOM   737  C  C    A ALA   A 1 27  ? 19.954 1.029   15.937  0.74 17.31 ?  27  ALA   A C    1 
ATOM   738  C  C    B ALA   A 1 27  ? 19.886 1.117   15.827  0.26 20.51 ?  27  ALA   A C    1 
ATOM   739  O  O    A ALA   A 1 27  ? 20.631 0.588   16.873  0.74 17.51 ?  27  ALA   A O    1 
ATOM   740  O  O    B ALA   A 1 27  ? 20.571 0.656   16.748  0.26 20.46 ?  27  ALA   A O    1 
ATOM   741  C  CB   A ALA   A 1 27  ? 20.688 0.691   13.551  0.74 15.30 ?  27  ALA   A CB   1 
ATOM   742  C  CB   B ALA   A 1 27  ? 20.629 1.010   13.429  0.26 18.42 ?  27  ALA   A CB   1 
ATOM   743  H  H    A ALA   A 1 27  ? 18.247 0.603   13.448  0.74 18.62 ?  27  ALA   A H    1 
ATOM   744  H  H    B ALA   A 1 27  ? 18.182 0.835   13.391  0.26 22.10 ?  27  ALA   A H    1 
ATOM   745  H  HA   A ALA   A 1 27  ? 19.990 -0.711  14.869  0.74 19.01 ?  27  ALA   A HA   1 
ATOM   746  H  HA   B ALA   A 1 27  ? 20.067 -0.539  14.642  0.26 22.88 ?  27  ALA   A HA   1 
ATOM   747  H  HB1  A ALA   A 1 27  ? 21.607 0.651   13.868  0.74 18.50 ?  27  ALA   A HB1  1 
ATOM   748  H  HB1  B ALA   A 1 27  ? 21.549 1.007   13.733  0.26 22.24 ?  27  ALA   A HB1  1 
ATOM   749  H  HB2  A ALA   A 1 27  ? 20.583 0.109   12.780  0.74 18.50 ?  27  ALA   A HB2  1 
ATOM   750  H  HB2  B ALA   A 1 27  ? 20.548 0.496   12.610  0.26 22.24 ?  27  ALA   A HB2  1 
ATOM   751  H  HB3  A ALA   A 1 27  ? 20.459 1.600   13.316  0.74 18.50 ?  27  ALA   A HB3  1 
ATOM   752  H  HB3  B ALA   A 1 27  ? 20.329 1.920   13.279  0.26 22.24 ?  27  ALA   A HB3  1 
ATOM   753  N  N    A LYS   A 1 28  ? 19.356 2.220   15.999  0.74 19.68 ?  28  LYS   A N    1 
ATOM   754  N  N    B LYS   A 1 28  ? 19.229 2.273   15.944  0.26 22.49 ?  28  LYS   A N    1 
ATOM   755  C  CA   A LYS   A 1 28  ? 19.496 3.047   17.193  0.74 22.73 ?  28  LYS   A CA   1 
ATOM   756  C  CA   B LYS   A 1 28  ? 19.385 3.084   17.148  0.26 24.72 ?  28  LYS   A CA   1 
ATOM   757  C  C    A LYS   A 1 28  ? 18.936 2.349   18.426  0.74 23.74 ?  28  LYS   A C    1 
ATOM   758  C  C    B LYS   A 1 28  ? 18.826 2.388   18.383  0.26 25.66 ?  28  LYS   A C    1 
ATOM   759  O  O    A LYS   A 1 28  ? 19.483 2.487   19.526  0.74 24.99 ?  28  LYS   A O    1 
ATOM   760  O  O    B LYS   A 1 28  ? 19.308 2.626   19.496  0.26 26.00 ?  28  LYS   A O    1 
ATOM   761  C  CB   A LYS   A 1 28  ? 18.840 4.412   16.978  0.74 25.21 ?  28  LYS   A CB   1 
ATOM   762  C  CB   B LYS   A 1 28  ? 18.726 4.450   16.960  0.26 26.17 ?  28  LYS   A CB   1 
ATOM   763  C  CG   A LYS   A 1 28  ? 19.678 5.345   16.120  0.74 27.69 ?  28  LYS   A CG   1 
ATOM   764  C  CG   B LYS   A 1 28  ? 19.508 5.381   16.048  0.26 27.62 ?  28  LYS   A CG   1 
ATOM   765  C  CD   A LYS   A 1 28  ? 19.191 6.781   16.191  0.74 30.44 ?  28  LYS   A CD   1 
ATOM   766  C  CD   B LYS   A 1 28  ? 19.022 6.819   16.149  0.26 29.16 ?  28  LYS   A CD   1 
ATOM   767  C  CE   A LYS   A 1 28  ? 17.904 6.964   15.418  0.74 32.37 ?  28  LYS   A CE   1 
ATOM   768  C  CE   B LYS   A 1 28  ? 17.699 7.019   15.433  0.26 30.27 ?  28  LYS   A CE   1 
ATOM   769  N  NZ   A LYS   A 1 28  ? 17.502 8.396   15.365  0.74 33.56 ?  28  LYS   A NZ   1 
ATOM   770  N  NZ   B LYS   A 1 28  ? 17.347 8.464   15.331  0.26 30.95 ?  28  LYS   A NZ   1 
ATOM   771  H  H    A LYS   A 1 28  ? 18.883 2.566   15.376  0.74 23.75 ?  28  LYS   A H    1 
ATOM   772  H  H    B LYS   A 1 28  ? 18.699 2.603   15.354  0.26 27.13 ?  28  LYS   A H    1 
ATOM   773  H  HA   A LYS   A 1 28  ? 20.437 3.200   17.363  0.74 27.42 ?  28  LYS   A HA   1 
ATOM   774  H  HA   B LYS   A 1 28  ? 20.331 3.232   17.296  0.26 29.81 ?  28  LYS   A HA   1 
ATOM   775  H  HB2  A LYS   A 1 28  ? 17.988 4.288   16.534  0.74 30.39 ?  28  LYS   A HB2  1 
ATOM   776  H  HB2  B LYS   A 1 28  ? 17.846 4.323   16.573  0.26 31.54 ?  28  LYS   A HB2  1 
ATOM   777  H  HB3  A LYS   A 1 28  ? 18.708 4.841   17.838  0.74 30.39 ?  28  LYS   A HB3  1 
ATOM   778  H  HB3  B LYS   A 1 28  ? 18.646 4.878   17.827  0.26 31.54 ?  28  LYS   A HB3  1 
ATOM   779  H  HG2  A LYS   A 1 28  ? 20.597 5.324   16.429  0.74 33.37 ?  28  LYS   A HG2  1 
ATOM   780  H  HG2  B LYS   A 1 28  ? 20.445 5.360   16.299  0.26 33.29 ?  28  LYS   A HG2  1 
ATOM   781  H  HG3  A LYS   A 1 28  ? 19.630 5.056   15.196  0.74 33.37 ?  28  LYS   A HG3  1 
ATOM   782  H  HG3  B LYS   A 1 28  ? 19.401 5.090   15.129  0.26 33.29 ?  28  LYS   A HG3  1 
ATOM   783  H  HD2  A LYS   A 1 28  ? 19.028 7.020   17.117  0.74 36.66 ?  28  LYS   A HD2  1 
ATOM   784  H  HD2  B LYS   A 1 28  ? 18.899 7.050   17.084  0.26 35.14 ?  28  LYS   A HD2  1 
ATOM   785  H  HD3  A LYS   A 1 28  ? 19.863 7.366   15.807  0.74 36.66 ?  28  LYS   A HD3  1 
ATOM   786  H  HD3  B LYS   A 1 28  ? 19.678 7.407   15.744  0.26 35.14 ?  28  LYS   A HD3  1 
ATOM   787  H  HE2  A LYS   A 1 28  ? 18.030 6.648   14.509  0.74 38.98 ?  28  LYS   A HE2  1 
ATOM   788  H  HE2  B LYS   A 1 28  ? 17.763 6.658   14.535  0.26 36.46 ?  28  LYS   A HE2  1 
ATOM   789  H  HE3  A LYS   A 1 28  ? 17.196 6.464   15.853  0.74 38.98 ?  28  LYS   A HE3  1 
ATOM   790  H  HE3  B LYS   A 1 28  ? 16.996 6.569   15.927  0.26 36.46 ?  28  LYS   A HE3  1 
ATOM   791  H  HZ1  A LYS   A 1 28  ? 16.745 8.482   14.907  0.74 40.42 ?  28  LYS   A HZ1  1 
ATOM   792  H  HZ1  B LYS   A 1 28  ? 16.571 8.559   14.908  0.26 37.28 ?  28  LYS   A HZ1  1 
ATOM   793  H  HZ2  A LYS   A 1 28  ? 17.380 8.708   16.189  0.74 40.42 ?  28  LYS   A HZ2  1 
ATOM   794  H  HZ2  B LYS   A 1 28  ? 17.280 8.818   16.145  0.26 37.28 ?  28  LYS   A HZ2  1 
ATOM   795  H  HZ3  A LYS   A 1 28  ? 18.138 8.875   14.966  0.74 40.42 ?  28  LYS   A HZ3  1 
ATOM   796  H  HZ3  B LYS   A 1 28  ? 17.979 8.899   14.878  0.26 37.28 ?  28  LYS   A HZ3  1 
ATOM   797  N  N    A LYS   A 1 29  ? 17.854 1.585   18.263  0.74 24.18 ?  29  LYS   A N    1 
ATOM   798  N  N    B LYS   A 1 29  ? 17.817 1.533   18.213  0.26 26.46 ?  29  LYS   A N    1 
ATOM   799  C  CA   A LYS   A 1 29  ? 17.259 0.878   19.394  0.74 25.99 ?  29  LYS   A CA   1 
ATOM   800  C  CA   B LYS   A 1 29  ? 17.210 0.858   19.356  0.26 27.41 ?  29  LYS   A CA   1 
ATOM   801  C  C    A LYS   A 1 29  ? 18.082 -0.346  19.781  0.74 25.69 ?  29  LYS   A C    1 
ATOM   802  C  C    B LYS   A 1 29  ? 18.016 -0.368  19.775  0.26 26.25 ?  29  LYS   A C    1 
ATOM   803  O  O    A LYS   A 1 29  ? 18.416 -0.532  20.957  0.74 26.59 ?  29  LYS   A O    1 
ATOM   804  O  O    B LYS   A 1 29  ? 18.284 -0.569  20.964  0.26 26.58 ?  29  LYS   A O    1 
ATOM   805  C  CB   A LYS   A 1 29  ? 15.827 0.460   19.051  0.74 28.54 ?  29  LYS   A CB   1 
ATOM   806  C  CB   B LYS   A 1 29  ? 15.775 0.455   19.011  0.26 29.39 ?  29  LYS   A CB   1 
ATOM   807  C  CG   A LYS   A 1 29  ? 15.090 -0.240  20.186  0.74 31.42 ?  29  LYS   A CG   1 
ATOM   808  C  CG   B LYS   A 1 29  ? 14.997 -0.162  20.163  0.26 31.27 ?  29  LYS   A CG   1 
ATOM   809  C  CD   A LYS   A 1 29  ? 14.776 0.722   21.320  0.74 34.06 ?  29  LYS   A CD   1 
ATOM   810  C  CD   B LYS   A 1 29  ? 14.657 0.871   21.225  0.26 32.86 ?  29  LYS   A CD   1 
ATOM   811  C  CE   A LYS   A 1 29  ? 13.902 0.067   22.377  0.74 35.89 ?  29  LYS   A CE   1 
ATOM   812  C  CE   B LYS   A 1 29  ? 13.753 0.284   22.299  0.26 33.97 ?  29  LYS   A CE   1 
ATOM   813  N  NZ   A LYS   A 1 29  ? 13.481 1.037   23.424  0.74 36.93 ?  29  LYS   A NZ   1 
ATOM   814  N  NZ   B LYS   A 1 29  ? 13.401 1.289   23.339  0.26 34.59 ?  29  LYS   A NZ   1 
ATOM   815  H  H    A LYS   A 1 29  ? 17.447 1.462   17.517  0.74 29.16 ?  29  LYS   A H    1 
ATOM   816  H  H    B LYS   A 1 29  ? 17.464 1.336   17.454  0.26 31.89 ?  29  LYS   A H    1 
ATOM   817  H  HA   A LYS   A 1 29  ? 17.222 1.471   20.161  0.74 31.33 ?  29  LYS   A HA   1 
ATOM   818  H  HA   B LYS   A 1 29  ? 17.180 1.470   20.106  0.26 33.04 ?  29  LYS   A HA   1 
ATOM   819  H  HB2  A LYS   A 1 29  ? 15.317 1.250   18.817  0.74 34.39 ?  29  LYS   A HB2  1 
ATOM   820  H  HB2  B LYS   A 1 29  ? 15.293 1.245   18.722  0.26 35.41 ?  29  LYS   A HB2  1 
ATOM   821  H  HB3  A LYS   A 1 29  ? 15.851 -0.151  18.299  0.74 34.39 ?  29  LYS   A HB3  1 
ATOM   822  H  HB3  B LYS   A 1 29  ? 15.799 -0.195  18.291  0.26 35.41 ?  29  LYS   A HB3  1 
ATOM   823  H  HG2  A LYS   A 1 29  ? 14.251 -0.595  19.853  0.74 37.84 ?  29  LYS   A HG2  1 
ATOM   824  H  HG2  B LYS   A 1 29  ? 14.167 -0.532  19.824  0.26 37.67 ?  29  LYS   A HG2  1 
ATOM   825  H  HG3  A LYS   A 1 29  ? 15.637 -0.960  20.541  0.74 37.84 ?  29  LYS   A HG3  1 
ATOM   826  H  HG3  B LYS   A 1 29  ? 15.528 -0.861  20.577  0.26 37.67 ?  29  LYS   A HG3  1 
ATOM   827  H  HD2  A LYS   A 1 29  ? 15.604 1.003   21.741  0.74 41.01 ?  29  LYS   A HD2  1 
ATOM   828  H  HD2  B LYS   A 1 29  ? 15.474 1.177   21.649  0.26 39.57 ?  29  LYS   A HD2  1 
ATOM   829  H  HD3  A LYS   A 1 29  ? 14.302 1.491   20.965  0.74 41.01 ?  29  LYS   A HD3  1 
ATOM   830  H  HD3  B LYS   A 1 29  ? 14.193 1.616   20.811  0.26 39.57 ?  29  LYS   A HD3  1 
ATOM   831  H  HE2  A LYS   A 1 29  ? 13.104 -0.290  21.955  0.74 43.21 ?  29  LYS   A HE2  1 
ATOM   832  H  HE2  B LYS   A 1 29  ? 12.931 -0.029  21.889  0.26 40.91 ?  29  LYS   A HE2  1 
ATOM   833  H  HE3  A LYS   A 1 29  ? 14.401 -0.646  22.807  0.74 43.21 ?  29  LYS   A HE3  1 
ATOM   834  H  HE3  B LYS   A 1 29  ? 14.211 -0.454  22.733  0.26 40.91 ?  29  LYS   A HE3  1 
ATOM   835  H  HZ1  A LYS   A 1 29  ? 12.971 0.629   24.029  0.74 44.46 ?  29  LYS   A HZ1  1 
ATOM   836  H  HZ1  B LYS   A 1 29  ? 12.873 0.920   23.953  0.26 41.65 ?  29  LYS   A HZ1  1 
ATOM   837  H  HZ2  A LYS   A 1 29  ? 14.197 1.376   23.830  0.74 44.46 ?  29  LYS   A HZ2  1 
ATOM   838  H  HZ2  B LYS   A 1 29  ? 14.140 1.588   23.735  0.26 41.65 ?  29  LYS   A HZ2  1 
ATOM   839  H  HZ3  A LYS   A 1 29  ? 13.017 1.700   23.054  0.74 44.46 ?  29  LYS   A HZ3  1 
ATOM   840  H  HZ3  B LYS   A 1 29  ? 12.974 1.975   22.966  0.26 41.65 ?  29  LYS   A HZ3  1 
ATOM   841  N  N    . VAL   A 1 30  ? 18.399 -1.201  18.808  1.00 24.66 ?  30  VAL   A N    1 
ATOM   842  C  CA   . VAL   A 1 30  ? 19.056 -2.468  19.120  1.00 23.35 ?  30  VAL   A CA   1 
ATOM   843  C  C    . VAL   A 1 30  ? 20.560 -2.310  19.331  1.00 22.13 ?  30  VAL   A C    1 
ATOM   844  O  O    . VAL   A 1 30  ? 21.157 -3.036  20.133  1.00 22.60 ?  30  VAL   A O    1 
ATOM   845  C  CB   . VAL   A 1 30  ? 18.755 -3.476  17.996  1.00 23.81 ?  30  VAL   A CB   1 
ATOM   846  C  CG1  . VAL   A 1 30  ? 19.530 -4.772  18.204  1.00 24.22 ?  30  VAL   A CG1  1 
ATOM   847  C  CG2  . VAL   A 1 30  ? 17.256 -3.747  17.904  1.00 24.35 ?  30  VAL   A CG2  1 
ATOM   848  H  H    A VAL   A 1 30  ? 18.231 -1.081  17.973  0.74 29.74 ?  30  VAL   A H    1 
ATOM   849  H  H    B VAL   A 1 30  ? 18.275 -1.064  17.969  0.26 29.74 ?  30  VAL   A H    1 
ATOM   850  H  HA   . VAL   A 1 30  ? 18.669 -2.822  19.936  1.00 28.16 ?  30  VAL   A HA   1 
ATOM   851  H  HB   . VAL   A 1 30  ? 19.038 -3.097  17.150  1.00 28.72 ?  30  VAL   A HB   1 
ATOM   852  H  HG11 . VAL   A 1 30  ? 19.149 -5.462  17.637  1.00 29.21 ?  30  VAL   A HG11 1 
ATOM   853  H  HG12 . VAL   A 1 30  ? 20.459 -4.629  17.969  1.00 29.21 ?  30  VAL   A HG12 1 
ATOM   854  H  HG13 . VAL   A 1 30  ? 19.457 -5.036  19.135  1.00 29.21 ?  30  VAL   A HG13 1 
ATOM   855  H  HG21 . VAL   A 1 30  ? 17.097 -4.422  17.224  1.00 29.36 ?  30  VAL   A HG21 1 
ATOM   856  H  HG22 . VAL   A 1 30  ? 16.939 -4.065  18.764  1.00 29.36 ?  30  VAL   A HG22 1 
ATOM   857  H  HG23 . VAL   A 1 30  ? 16.799 -2.926  17.665  1.00 29.36 ?  30  VAL   A HG23 1 
ATOM   858  N  N    A LYS   A 1 31  ? 21.196 -1.377  18.631  0.74 21.13 ?  31  LYS   A N    1 
ATOM   859  N  N    B LYS   A 1 31  ? 21.188 -1.368  18.635  0.26 22.46 ?  31  LYS   A N    1 
ATOM   860  C  CA   A LYS   A 1 31  ? 22.650 -1.272  18.588  0.74 21.91 ?  31  LYS   A CA   1 
ATOM   861  C  CA   B LYS   A 1 31  ? 22.640 -1.265  18.573  0.26 23.25 ?  31  LYS   A CA   1 
ATOM   862  C  C    A LYS   A 1 31  ? 23.267 -2.633  18.250  0.74 19.62 ?  31  LYS   A C    1 
ATOM   863  C  C    B LYS   A 1 31  ? 23.257 -2.629  18.251  0.26 20.83 ?  31  LYS   A C    1 
ATOM   864  O  O    A LYS   A 1 31  ? 24.039 -3.186  19.041  0.74 20.35 ?  31  LYS   A O    1 
ATOM   865  O  O    B LYS   A 1 31  ? 24.019 -3.178  19.052  0.26 21.28 ?  31  LYS   A O    1 
ATOM   866  C  CB   A LYS   A 1 31  ? 23.219 -0.722  19.887  0.74 26.50 ?  31  LYS   A CB   1 
ATOM   867  C  CB   B LYS   A 1 31  ? 23.225 -0.687  19.854  0.26 26.63 ?  31  LYS   A CB   1 
ATOM   868  C  CG   A LYS   A 1 31  ? 22.548 0.553   20.369  0.74 31.37 ?  31  LYS   A CG   1 
ATOM   869  C  CG   B LYS   A 1 31  ? 22.558 0.598   20.311  0.26 29.84 ?  31  LYS   A CG   1 
ATOM   870  C  CD   A LYS   A 1 31  ? 23.571 1.607   20.764  0.74 35.07 ?  31  LYS   A CD   1 
ATOM   871  C  CD   B LYS   A 1 31  ? 23.562 1.557   20.928  0.26 32.30 ?  31  LYS   A CD   1 
ATOM   872  C  CE   A LYS   A 1 31  ? 22.965 2.646   21.694  0.74 37.45 ?  31  LYS   A CE   1 
ATOM   873  C  CE   B LYS   A 1 31  ? 22.874 2.599   21.795  0.26 33.89 ?  31  LYS   A CE   1 
ATOM   874  N  NZ   A LYS   A 1 31  ? 21.747 3.281   21.122  0.74 38.71 ?  31  LYS   A NZ   1 
ATOM   875  N  NZ   B LYS   A 1 31  ? 21.750 3.284   21.097  0.26 34.75 ?  31  LYS   A NZ   1 
ATOM   876  H  H    A LYS   A 1 31  ? 20.794 -0.780  18.162  0.74 25.49 ?  31  LYS   A H    1 
ATOM   877  H  H    B LYS   A 1 31  ? 20.780 -0.763  18.182  0.26 27.09 ?  31  LYS   A H    1 
ATOM   878  H  HA   A LYS   A 1 31  ? 22.885 -0.657  17.882  0.74 26.44 ?  31  LYS   A HA   1 
ATOM   879  H  HA   B LYS   A 1 31  ? 22.866 -0.663  17.854  0.26 28.04 ?  31  LYS   A HA   1 
ATOM   880  H  HB2  A LYS   A 1 31  ? 23.119 -1.390  20.580  0.74 31.94 ?  31  LYS   A HB2  1 
ATOM   881  H  HB2  B LYS   A 1 31  ? 23.132 -1.339  20.562  0.26 32.09 ?  31  LYS   A HB2  1 
ATOM   882  H  HB3  A LYS   A 1 31  ? 24.161 -0.527  19.752  0.74 31.94 ?  31  LYS   A HB3  1 
ATOM   883  H  HB3  B LYS   A 1 31  ? 24.165 -0.495  19.706  0.26 32.09 ?  31  LYS   A HB3  1 
ATOM   884  H  HG2  A LYS   A 1 31  ? 21.997 0.915   19.658  0.74 37.78 ?  31  LYS   A HG2  1 
ATOM   885  H  HG2  B LYS   A 1 31  ? 22.149 1.035   19.548  0.26 35.94 ?  31  LYS   A HG2  1 
ATOM   886  H  HG3  A LYS   A 1 31  ? 22.004 0.353   21.147  0.74 37.78 ?  31  LYS   A HG3  1 
ATOM   887  H  HG3  B LYS   A 1 31  ? 21.887 0.390   20.979  0.26 35.94 ?  31  LYS   A HG3  1 
ATOM   888  H  HD2  A LYS   A 1 31  ? 24.311 1.181   21.225  0.74 42.23 ?  31  LYS   A HD2  1 
ATOM   889  H  HD2  B LYS   A 1 31  ? 24.182 1.058   21.483  0.26 38.90 ?  31  LYS   A HD2  1 
ATOM   890  H  HD3  A LYS   A 1 31  ? 23.889 2.060   19.966  0.74 42.23 ?  31  LYS   A HD3  1 
ATOM   891  H  HD3  B LYS   A 1 31  ? 24.042 2.016   20.220  0.26 38.90 ?  31  LYS   A HD3  1 
ATOM   892  H  HE2  A LYS   A 1 31  ? 22.717 2.218   22.528  0.74 45.08 ?  31  LYS   A HE2  1 
ATOM   893  H  HE2  B LYS   A 1 31  ? 22.514 2.164   22.582  0.26 40.80 ?  31  LYS   A HE2  1 
ATOM   894  H  HE3  A LYS   A 1 31  ? 23.618 3.344   21.859  0.74 45.08 ?  31  LYS   A HE3  1 
ATOM   895  H  HE3  B LYS   A 1 31  ? 23.522 3.273   22.055  0.26 40.80 ?  31  LYS   A HE3  1 
ATOM   896  H  HZ1  A LYS   A 1 31  ? 21.436 3.900   21.681  0.74 46.59 ?  31  LYS   A HZ1  1 
ATOM   897  H  HZ1  B LYS   A 1 31  ? 21.401 3.911   21.624  0.26 41.84 ?  31  LYS   A HZ1  1 
ATOM   898  H  HZ2  A LYS   A 1 31  ? 21.942 3.666   20.344  0.74 46.59 ?  31  LYS   A HZ2  1 
ATOM   899  H  HZ2  B LYS   A 1 31  ? 22.043 3.665   20.349  0.26 41.84 ?  31  LYS   A HZ2  1 
ATOM   900  H  HZ3  A LYS   A 1 31  ? 21.117 2.667   20.990  0.74 46.59 ?  31  LYS   A HZ3  1 
ATOM   901  H  HZ3  B LYS   A 1 31  ? 21.114 2.695   20.891  0.26 41.84 ?  31  LYS   A HZ3  1 
ATOM   902  N  N    . PRO   A 1 32  ? 22.945 -3.194  17.089  1.00 18.16 ?  32  PRO   A N    1 
ATOM   903  C  CA   . PRO   A 1 32  ? 23.423 -4.536  16.764  1.00 17.68 ?  32  PRO   A CA   1 
ATOM   904  C  C    . PRO   A 1 32  ? 24.924 -4.548  16.552  1.00 17.52 ?  32  PRO   A C    1 
ATOM   905  O  O    . PRO   A 1 32  ? 25.566 -3.517  16.341  1.00 17.30 ?  32  PRO   A O    1 
ATOM   906  C  CB   . PRO   A 1 32  ? 22.696 -4.849  15.453  1.00 17.72 ?  32  PRO   A CB   1 
ATOM   907  C  CG   . PRO   A 1 32  ? 22.540 -3.503  14.812  1.00 16.76 ?  32  PRO   A CG   1 
ATOM   908  C  CD   . PRO   A 1 32  ? 22.229 -2.581  15.958  1.00 17.01 ?  32  PRO   A CD   1 
ATOM   909  H  HA   . PRO   A 1 32  ? 23.174 -5.175  17.450  1.00 21.36 ?  32  PRO   A HA   1 
ATOM   910  H  HB2  . PRO   A 1 32  ? 23.238 -5.441  14.904  1.00 21.40 ?  32  PRO   A HB2  1 
ATOM   911  H  HB3  . PRO   A 1 32  ? 21.831 -5.251  15.641  1.00 21.40 ?  32  PRO   A HB3  1 
ATOM   912  H  HG2  . PRO   A 1 32  ? 23.368 -3.258  14.374  1.00 20.26 ?  32  PRO   A HG2  1 
ATOM   913  H  HG3  . PRO   A 1 32  ? 21.807 -3.533  14.176  1.00 20.26 ?  32  PRO   A HG3  1 
ATOM   914  H  HD2  . PRO   A 1 32  ? 22.578 -1.697  15.767  1.00 20.55 ?  32  PRO   A HD2  1 
ATOM   915  H  HD3  . PRO   A 1 32  ? 21.278 -2.566  16.123  1.00 20.55 ?  32  PRO   A HD3  1 
ATOM   916  N  N    . THR   A 1 33  ? 25.477 -5.758  16.583  1.00 17.26 ?  33  THR   A N    1 
ATOM   917  C  CA   . THR   A 1 33  ? 26.889 -5.919  16.267  1.00 17.36 ?  33  THR   A CA   1 
ATOM   918  C  C    . THR   A 1 33  ? 27.188 -5.454  14.849  1.00 15.75 ?  33  THR   A C    1 
ATOM   919  O  O    . THR   A 1 33  ? 28.219 -4.810  14.603  1.00 15.91 ?  33  THR   A O    1 
ATOM   920  C  CB   . THR   A 1 33  ? 27.296 -7.379  16.461  1.00 19.07 ?  33  THR   A CB   1 
ATOM   921  O  OG1  . THR   A 1 33  ? 26.986 -7.781  17.797  1.00 20.86 ?  33  THR   A OG1  1 
ATOM   922  C  CG2  . THR   A 1 33  ? 28.783 -7.560  16.215  1.00 20.04 ?  33  THR   A CG2  1 
ATOM   923  H  H    . THR   A 1 33  ? 25.062 -6.486  16.775  1.00 20.86 ?  33  THR   A H    1 
ATOM   924  H  HA   . THR   A 1 33  ? 27.412 -5.380  16.878  1.00 20.97 ?  33  THR   A HA   1 
ATOM   925  H  HB   . THR   A 1 33  ? 26.808 -7.939  15.834  1.00 23.02 ?  33  THR   A HB   1 
ATOM   926  H  HG1  . THR   A 1 33  ? 27.408 -7.307  18.350  1.00 25.17 ?  33  THR   A HG1  1 
ATOM   927  H  HG21 . THR   A 1 33  ? 29.057 -8.445  16.500  1.00 24.19 ?  33  THR   A HG21 1 
ATOM   928  H  HG22 . THR   A 1 33  ? 28.978 -7.458  15.271  1.00 24.19 ?  33  THR   A HG22 1 
ATOM   929  H  HG23 . THR   A 1 33  ? 29.281 -6.898  16.717  1.00 24.19 ?  33  THR   A HG23 1 
ATOM   930  N  N    . VAL   A 1 34  ? 26.300 -5.770  13.905  1.00 14.15 ?  34  VAL   A N    1 
ATOM   931  C  CA   . VAL   A 1 34  ? 26.497 -5.444  12.497  1.00 12.93 ?  34  VAL   A CA   1 
ATOM   932  C  C    . VAL   A 1 34  ? 25.198 -4.889  11.925  1.00 12.14 ?  34  VAL   A C    1 
ATOM   933  O  O    . VAL   A 1 34  ? 24.160 -5.562  11.966  1.00 12.85 ?  34  VAL   A O    1 
ATOM   934  C  CB   . VAL   A 1 34  ? 26.946 -6.660  11.667  1.00 13.34 ?  34  VAL   A CB   1 
ATOM   935  C  CG1  . VAL   A 1 34  ? 27.138 -6.271  10.211  1.00 13.45 ?  34  VAL   A CG1  1 
ATOM   936  C  CG2  . VAL   A 1 34  ? 28.222 -7.270  12.243  1.00 14.64 ?  34  VAL   A CG2  1 
ATOM   937  H  H    . VAL   A 1 34  ? 25.563 -6.187  14.060  1.00 17.12 ?  34  VAL   A H    1 
ATOM   938  H  HA   . VAL   A 1 34  ? 27.177 -4.756  12.417  1.00 15.66 ?  34  VAL   A HA   1 
ATOM   939  H  HB   . VAL   A 1 34  ? 26.251 -7.337  11.711  1.00 16.15 ?  34  VAL   A HB   1 
ATOM   940  H  HG11 . VAL   A 1 34  ? 27.621 -6.983  9.760   1.00 16.28 ?  34  VAL   A HG11 1 
ATOM   941  H  HG12 . VAL   A 1 34  ? 26.271 -6.149  9.798   1.00 16.28 ?  34  VAL   A HG12 1 
ATOM   942  H  HG13 . VAL   A 1 34  ? 27.650 -5.449  10.169  1.00 16.28 ?  34  VAL   A HG13 1 
ATOM   943  H  HG21 . VAL   A 1 34  ? 28.504 -8.003  11.674  1.00 17.71 ?  34  VAL   A HG21 1 
ATOM   944  H  HG22 . VAL   A 1 34  ? 28.912 -6.589  12.273  1.00 17.71 ?  34  VAL   A HG22 1 
ATOM   945  H  HG23 . VAL   A 1 34  ? 28.042 -7.599  13.139  1.00 17.71 ?  34  VAL   A HG23 1 
ATOM   946  N  N    . VAL   A 1 35  ? 25.262 -3.678  11.370  1.00 11.49 ?  35  VAL   A N    1 
ATOM   947  C  CA   . VAL   A 1 35  ? 24.232 -3.163  10.477  1.00 10.90 ?  35  VAL   A CA   1 
ATOM   948  C  C    . VAL   A 1 35  ? 24.785 -3.175  9.060   1.00 10.31 ?  35  VAL   A C    1 
ATOM   949  O  O    . VAL   A 1 35  ? 25.931 -2.772  8.827   1.00 11.22 ?  35  VAL   A O    1 
ATOM   950  C  CB   . VAL   A 1 35  ? 23.706 -1.767  10.879  1.00 11.70 ?  35  VAL   A CB   1 
ATOM   951  C  CG1  . VAL   A 1 35  ? 24.774 -0.680  10.745  1.00 12.49 ?  35  VAL   A CG1  1 
ATOM   952  C  CG2  . VAL   A 1 35  ? 22.467 -1.417  10.049  1.00 12.21 ?  35  VAL   A CG2  1 
ATOM   953  H  H    . VAL   A 1 35  ? 25.907 -3.124  11.494  1.00 13.93 ?  35  VAL   A H    1 
ATOM   954  H  HA   . VAL   A 1 35  ? 23.474 -3.773  10.497  1.00 13.22 ?  35  VAL   A HA   1 
ATOM   955  H  HB   . VAL   A 1 35  ? 23.426 -1.794  11.803  1.00 14.19 ?  35  VAL   A HB   1 
ATOM   956  H  HG11 . VAL   A 1 35  ? 24.428 0.151   11.107  1.00 15.13 ?  35  VAL   A HG11 1 
ATOM   957  H  HG12 . VAL   A 1 35  ? 25.561 -0.954  11.240  1.00 15.13 ?  35  VAL   A HG12 1 
ATOM   958  H  HG13 . VAL   A 1 35  ? 24.997 -0.563  9.807   1.00 15.13 ?  35  VAL   A HG13 1 
ATOM   959  H  HG21 . VAL   A 1 35  ? 22.113 -0.567  10.349  1.00 14.79 ?  35  VAL   A HG21 1 
ATOM   960  H  HG22 . VAL   A 1 35  ? 22.722 -1.353  9.110   1.00 14.79 ?  35  VAL   A HG22 1 
ATOM   961  H  HG23 . VAL   A 1 35  ? 21.803 -2.114  10.160  1.00 14.79 ?  35  VAL   A HG23 1 
ATOM   962  N  N    . VAL   A 1 36  ? 23.971 -3.634  8.112   1.00 9.93  ?  36  VAL   A N    1 
ATOM   963  C  CA   . VAL   A 1 36  ? 24.349 -3.647  6.707   1.00 9.72  ?  36  VAL   A CA   1 
ATOM   964  C  C    . VAL   A 1 36  ? 23.888 -2.357  6.045   1.00 9.94  ?  36  VAL   A C    1 
ATOM   965  O  O    . VAL   A 1 36  ? 22.727 -1.955  6.184   1.00 10.69 ?  36  VAL   A O    1 
ATOM   966  C  CB   . VAL   A 1 36  ? 23.745 -4.861  5.987   1.00 9.94  ?  36  VAL   A CB   1 
ATOM   967  C  CG1  . VAL   A 1 36  ? 24.008 -4.792  4.503   1.00 10.58 ?  36  VAL   A CG1  1 
ATOM   968  C  CG2  . VAL   A 1 36  ? 24.289 -6.160  6.565   1.00 10.88 ?  36  VAL   A CG2  1 
ATOM   969  H  H    . VAL   A 1 36  ? 23.180 -3.950  8.262   1.00 12.05 ?  36  VAL   A H    1 
ATOM   970  H  HA   . VAL   A 1 36  ? 25.317 -3.705  6.635   1.00 11.80 ?  36  VAL   A HA   1 
ATOM   971  H  HB   . VAL   A 1 36  ? 22.783 -4.856  6.117   1.00 12.07 ?  36  VAL   A HB   1 
ATOM   972  H  HG11 . VAL   A 1 36  ? 23.867 -5.667  4.112   1.00 12.84 ?  36  VAL   A HG11 1 
ATOM   973  H  HG12 . VAL   A 1 36  ? 23.396 -4.151  4.097   1.00 12.84 ?  36  VAL   A HG12 1 
ATOM   974  H  HG13 . VAL   A 1 36  ? 24.924 -4.509  4.355   1.00 12.84 ?  36  VAL   A HG13 1 
ATOM   975  H  HG21 . VAL   A 1 36  ? 23.896 -6.910  6.088   1.00 13.20 ?  36  VAL   A HG21 1 
ATOM   976  H  HG22 . VAL   A 1 36  ? 25.253 -6.174  6.461   1.00 13.20 ?  36  VAL   A HG22 1 
ATOM   977  H  HG23 . VAL   A 1 36  ? 24.057 -6.212  7.506   1.00 13.20 ?  36  VAL   A HG23 1 
ATOM   978  N  N    . ASN   A 1 37  ? 24.804 -1.723  5.308   1.00 9.38  ?  37  ASN   A N    1 
ATOM   979  C  CA   . ASN   A 1 37  ? 24.477 -0.602  4.442   1.00 9.12  ?  37  ASN   A CA   1 
ATOM   980  C  C    . ASN   A 1 37  ? 24.340 -1.075  3.005   1.00 9.07  ?  37  ASN   A C    1 
ATOM   981  O  O    . ASN   A 1 37  ? 25.125 -1.907  2.531   1.00 9.89  ?  37  ASN   A O    1 
ATOM   982  C  CB   . ASN   A 1 37  ? 25.558 0.472   4.512   1.00 9.31  ?  37  ASN   A CB   1 
ATOM   983  C  CG   . ASN   A 1 37  ? 25.233 1.675   3.662   1.00 9.60  ?  37  ASN   A CG   1 
ATOM   984  O  OD1  . ASN   A 1 37  ? 24.059 2.010   3.480   1.00 10.31 ?  37  ASN   A OD1  1 
ATOM   985  N  ND2  . ASN   A 1 37  ? 26.264 2.332   3.140   1.00 9.93  ?  37  ASN   A ND2  1 
ATOM   986  H  H    . ASN   A 1 37  ? 25.643 -1.925  5.305   1.00 11.39 ?  37  ASN   A H    1 
ATOM   987  H  HA   . ASN   A 1 37  ? 23.640 -0.209  4.724   1.00 11.08 ?  37  ASN   A HA   1 
ATOM   988  H  HB2  . ASN   A 1 37  ? 25.651 0.769   5.432   1.00 11.31 ?  37  ASN   A HB2  1 
ATOM   989  H  HB3  . ASN   A 1 37  ? 26.400 0.097   4.201   1.00 11.31 ?  37  ASN   A HB3  1 
ATOM   990  H  HD21 . ASN   A 1 37  ? 26.126 3.022   2.646   1.00 12.06 ?  37  ASN   A HD21 1 
ATOM   991  H  HD22 . ASN   A 1 37  ? 27.062 2.070   3.291   1.00 12.06 ?  37  ASN   A HD22 1 
ATOM   992  N  N    A ALA   A 1 38  ? 23.326 -0.533  2.325   0.74 9.66  ?  38  ALA   A N    1 
ATOM   993  N  N    B ALA   A 1 38  ? 23.329 -0.549  2.311   0.26 9.28  ?  38  ALA   A N    1 
ATOM   994  C  CA   A ALA   A 1 38  ? 23.131 -0.677  0.883   0.74 9.82  ?  38  ALA   A CA   1 
ATOM   995  C  CA   B ALA   A 1 38  ? 23.163 -0.795  0.878   0.26 9.55  ?  38  ALA   A CA   1 
ATOM   996  C  C    A ALA   A 1 38  ? 24.045 0.322   0.172   0.74 9.62  ?  38  ALA   A C    1 
ATOM   997  C  C    B ALA   A 1 38  ? 24.020 0.220   0.122   0.26 9.45  ?  38  ALA   A C    1 
ATOM   998  O  O    A ALA   A 1 38  ? 23.640 1.425   -0.208  0.74 9.69  ?  38  ALA   A O    1 
ATOM   999  O  O    B ALA   A 1 38  ? 23.540 1.211   -0.436  0.26 9.22  ?  38  ALA   A O    1 
ATOM   1000 C  CB   A ALA   A 1 38  ? 21.669 -0.429  0.531   0.74 10.85 ?  38  ALA   A CB   1 
ATOM   1001 C  CB   B ALA   A 1 38  ? 21.694 -0.717  0.485   0.26 10.10 ?  38  ALA   A CB   1 
ATOM   1002 H  H    A ALA   A 1 38  ? 22.721 -0.044  2.698   0.74 11.73 ?  38  ALA   A H    1 
ATOM   1003 H  H    B ALA   A 1 38  ? 22.720 -0.041  2.652   0.26 11.27 ?  38  ALA   A H    1 
ATOM   1004 H  HA   A ALA   A 1 38  ? 23.373 -1.572  0.606   0.74 11.93 ?  38  ALA   A HA   1 
ATOM   1005 H  HA   B ALA   A 1 38  ? 23.485 -1.688  0.669   0.26 11.60 ?  38  ALA   A HA   1 
ATOM   1006 H  HB1  A ALA   A 1 38  ? 21.552 -0.530  -0.426  0.74 13.16 ?  38  ALA   A HB1  1 
ATOM   1007 H  HB1  B ALA   A 1 38  ? 21.611 -0.918  -0.459  0.26 12.26 ?  38  ALA   A HB1  1 
ATOM   1008 H  HB2  A ALA   A 1 38  ? 21.117 -1.073  1.003   0.74 13.16 ?  38  ALA   A HB2  1 
ATOM   1009 H  HB2  B ALA   A 1 38  ? 21.189 -1.363  1.006   0.26 12.26 ?  38  ALA   A HB2  1 
ATOM   1010 H  HB3  A ALA   A 1 38  ? 21.427 0.472   0.800   0.74 13.16 ?  38  ALA   A HB3  1 
ATOM   1011 H  HB3  B ALA   A 1 38  ? 21.369 0.177   0.661   0.26 12.26 ?  38  ALA   A HB3  1 
ATOM   1012 N  N    A ALA   A 1 39  ? 25.304 -0.076  -0.003  0.74 9.86  ?  39  ALA   A N    1 
ATOM   1013 N  N    B ALA   A 1 39  ? 25.321 -0.050  0.108   0.26 9.81  ?  39  ALA   A N    1 
ATOM   1014 C  CA   A ALA   A 1 39  ? 26.357 0.805   -0.483  0.74 9.73  ?  39  ALA   A CA   1 
ATOM   1015 C  CA   B ALA   A 1 39  ? 26.307 0.885   -0.404  0.26 10.02 ?  39  ALA   A CA   1 
ATOM   1016 C  C    A ALA   A 1 39  ? 26.472 0.773   -2.007  0.74 9.75  ?  39  ALA   A C    1 
ATOM   1017 C  C    B ALA   A 1 39  ? 26.461 0.751   -1.915  0.26 9.61  ?  39  ALA   A C    1 
ATOM   1018 O  O    A ALA   A 1 39  ? 25.955 -0.119  -2.688  0.74 10.08 ?  39  ALA   A O    1 
ATOM   1019 O  O    B ALA   A 1 39  ? 26.110 -0.269  -2.515  0.26 9.37  ?  39  ALA   A O    1 
ATOM   1020 C  CB   A ALA   A 1 39  ? 27.686 0.397   0.159   0.74 10.07 ?  39  ALA   A CB   1 
ATOM   1021 C  CB   B ALA   A 1 39  ? 27.656 0.626   0.265   0.26 10.42 ?  39  ALA   A CB   1 
ATOM   1022 H  H    A ALA   A 1 39  ? 25.576 -0.876  0.168   0.74 11.98 ?  39  ALA   A H    1 
ATOM   1023 H  H    B ALA   A 1 39  ? 25.658 -0.786  0.394   0.26 11.91 ?  39  ALA   A H    1 
ATOM   1024 H  HA   A ALA   A 1 39  ? 26.152 1.717   -0.208  0.74 11.81 ?  39  ALA   A HA   1 
ATOM   1025 H  HA   B ALA   A 1 39  ? 26.029 1.790   -0.202  0.26 12.17 ?  39  ALA   A HA   1 
ATOM   1026 H  HB1  A ALA   A 1 39  ? 28.381 0.993   -0.162  0.74 12.23 ?  39  ALA   A HB1  1 
ATOM   1027 H  HB1  B ALA   A 1 39  ? 28.304 1.255   -0.083  0.26 12.65 ?  39  ALA   A HB1  1 
ATOM   1028 H  HB2  A ALA   A 1 39  ? 27.609 0.474   1.126   0.74 12.23 ?  39  ALA   A HB2  1 
ATOM   1029 H  HB2  B ALA   A 1 39  ? 27.558 0.744   1.223   0.26 12.65 ?  39  ALA   A HB2  1 
ATOM   1030 H  HB3  A ALA   A 1 39  ? 27.886 -0.515  -0.086  0.74 12.23 ?  39  ALA   A HB3  1 
ATOM   1031 H  HB3  B ALA   A 1 39  ? 27.935 -0.283  0.071   0.26 12.65 ?  39  ALA   A HB3  1 
ATOM   1032 N  N    A ASN   A 1 40  ? 27.186 1.765   -2.537  0.74 10.03 ?  40  ASN   A N    1 
ATOM   1033 N  N    B ASN   A 1 40  ? 27.000 1.804   -2.526  0.26 9.70  ?  40  ASN   A N    1 
ATOM   1034 C  CA   A ASN   A 1 40  ? 27.731 1.719   -3.886  0.74 9.92  ?  40  ASN   A CA   1 
ATOM   1035 C  CA   B ASN   A 1 40  ? 27.460 1.763   -3.906  0.26 9.93  ?  40  ASN   A CA   1 
ATOM   1036 C  C    A ASN   A 1 40  ? 29.256 1.616   -3.808  0.74 9.01  ?  40  ASN   A C    1 
ATOM   1037 C  C    B ASN   A 1 40  ? 28.984 1.634   -3.930  0.26 9.92  ?  40  ASN   A C    1 
ATOM   1038 O  O    A ASN   A 1 40  ? 29.849 1.721   -2.731  0.74 9.60  ?  40  ASN   A O    1 
ATOM   1039 O  O    B ASN   A 1 40  ? 29.652 1.710   -2.898  0.26 10.10 ?  40  ASN   A O    1 
ATOM   1040 C  CB   A ASN   A 1 40  ? 27.242 2.894   -4.751  0.74 10.67 ?  40  ASN   A CB   1 
ATOM   1041 C  CB   B ASN   A 1 40  ? 26.993 3.004   -4.678  0.26 10.83 ?  40  ASN   A CB   1 
ATOM   1042 C  CG   A ASN   A 1 40  ? 27.608 4.252   -4.185  0.74 11.32 ?  40  ASN   A CG   1 
ATOM   1043 C  CG   B ASN   A 1 40  ? 27.393 4.297   -4.001  0.26 11.73 ?  40  ASN   A CG   1 
ATOM   1044 O  OD1  A ASN   A 1 40  ? 28.775 4.510   -3.865  0.74 12.44 ?  40  ASN   A OD1  1 
ATOM   1045 O  OD1  B ASN   A 1 40  ? 28.579 4.611   -3.887  0.26 12.58 ?  40  ASN   A OD1  1 
ATOM   1046 N  ND2  A ASN   A 1 40  ? 26.604 5.135   -4.064  0.74 11.56 ?  40  ASN   A ND2  1 
ATOM   1047 N  ND2  B ASN   A 1 40  ? 26.401 5.063   -3.556  0.26 11.96 ?  40  ASN   A ND2  1 
ATOM   1048 H  H    A ASN   A 1 40  ? 27.379 2.484   -2.115  0.74 12.18 ?  40  ASN   A H    1 
ATOM   1049 H  H    B ASN   A 1 40  ? 27.112 2.571   -2.149  0.26 11.79 ?  40  ASN   A H    1 
ATOM   1050 H  HA   A ASN   A 1 40  ? 27.423 0.904   -4.309  0.74 12.05 ?  40  ASN   A HA   1 
ATOM   1051 H  HA   B ASN   A 1 40  ? 27.083 0.982   -4.345  0.26 12.05 ?  40  ASN   A HA   1 
ATOM   1052 H  HB2  A ASN   A 1 40  ? 27.638 2.816   -5.634  0.74 12.95 ?  40  ASN   A HB2  1 
ATOM   1053 H  HB2  B ASN   A 1 40  ? 27.387 2.993   -5.564  0.26 13.13 ?  40  ASN   A HB2  1 
ATOM   1054 H  HB3  A ASN   A 1 40  ? 26.276 2.843   -4.818  0.74 12.95 ?  40  ASN   A HB3  1 
ATOM   1055 H  HB3  B ASN   A 1 40  ? 26.023 2.987   -4.749  0.26 13.13 ?  40  ASN   A HB3  1 
ATOM   1056 H  HD21 A ASN   A 1 40  ? 26.756 5.923   -3.752  0.74 14.02 ?  40  ASN   A HD21 1 
ATOM   1057 H  HD21 B ASN   A 1 40  ? 26.576 5.807   -3.165  0.26 14.50 ?  40  ASN   A HD21 1 
ATOM   1058 H  HD22 A ASN   A 1 40  ? 25.804 4.913   -4.294  0.74 14.02 ?  40  ASN   A HD22 1 
ATOM   1059 H  HD22 B ASN   A 1 40  ? 25.583 4.811   -3.657  0.26 14.50 ?  40  ASN   A HD22 1 
ATOM   1060 N  N    A VAL   A 1 41  ? 29.885 1.371   -4.960  0.74 9.46  ?  41  VAL   A N    1 
ATOM   1061 N  N    B VAL   A 1 41  ? 29.534 1.430   -5.131  0.26 10.07 ?  41  VAL   A N    1 
ATOM   1062 C  CA   A VAL   A 1 41  ? 31.311 1.056   -4.976  0.74 10.14 ?  41  VAL   A CA   1 
ATOM   1063 C  CA   B VAL   A 1 41  ? 30.961 1.116   -5.240  0.26 10.20 ?  41  VAL   A CA   1 
ATOM   1064 C  C    A VAL   A 1 41  ? 32.167 2.210   -4.496  0.74 10.17 ?  41  VAL   A C    1 
ATOM   1065 C  C    B VAL   A 1 41  ? 31.835 2.255   -4.736  0.26 10.31 ?  41  VAL   A C    1 
ATOM   1066 O  O    A VAL   A 1 41  ? 33.309 1.992   -4.079  0.74 10.53 ?  41  VAL   A O    1 
ATOM   1067 O  O    B VAL   A 1 41  ? 32.977 2.026   -4.317  0.26 10.20 ?  41  VAL   A O    1 
ATOM   1068 C  CB   A VAL   A 1 41  ? 31.800 0.559   -6.358  0.74 10.34 ?  41  VAL   A CB   1 
ATOM   1069 C  CB   B VAL   A 1 41  ? 31.348 0.710   -6.677  0.26 10.74 ?  41  VAL   A CB   1 
ATOM   1070 C  CG1  A VAL   A 1 41  ? 31.117 -0.750  -6.732  0.74 11.34 ?  41  VAL   A CG1  1 
ATOM   1071 C  CG1  B VAL   A 1 41  ? 30.701 -0.614  -7.051  0.26 11.14 ?  41  VAL   A CG1  1 
ATOM   1072 C  CG2  A VAL   A 1 41  ? 31.633 1.621   -7.448  0.74 10.44 ?  41  VAL   A CG2  1 
ATOM   1073 C  CG2  B VAL   A 1 41  ? 30.989 1.811   -7.671  0.26 11.26 ?  41  VAL   A CG2  1 
ATOM   1074 H  H    A VAL   A 1 41  ? 29.516 1.373   -5.733  0.74 11.49 ?  41  VAL   A H    1 
ATOM   1075 H  H    B VAL   A 1 41  ? 29.108 1.458   -5.877  0.26 12.22 ?  41  VAL   A H    1 
ATOM   1076 H  HA   A VAL   A 1 41  ? 31.467 0.329   -4.355  0.74 12.31 ?  41  VAL   A HA   1 
ATOM   1077 H  HA   B VAL   A 1 41  ? 31.136 0.351   -4.673  0.26 12.38 ?  41  VAL   A HA   1 
ATOM   1078 H  HB   A VAL   A 1 41  ? 32.748 0.367   -6.293  0.74 12.54 ?  41  VAL   A HB   1 
ATOM   1079 H  HB   B VAL   A 1 41  ? 32.309 0.585   -6.709  0.26 13.03 ?  41  VAL   A HB   1 
ATOM   1080 H  HG11 A VAL   A 1 41  ? 31.456 -1.057  -7.587  0.74 13.75 ?  41  VAL   A HG11 1 
ATOM   1081 H  HG11 B VAL   A 1 41  ? 30.918 -0.821  -7.972  0.26 13.51 ?  41  VAL   A HG11 1 
ATOM   1082 H  HG12 A VAL   A 1 41  ? 31.300 -1.413  -6.046  0.74 13.75 ?  41  VAL   A HG12 1 
ATOM   1083 H  HG12 B VAL   A 1 41  ? 31.045 -1.309  -6.466  0.26 13.51 ?  41  VAL   A HG12 1 
ATOM   1084 H  HG13 A VAL   A 1 41  ? 30.157 -0.601  -6.794  0.74 13.75 ?  41  VAL   A HG13 1 
ATOM   1085 H  HG13 B VAL   A 1 41  ? 29.742 -0.543  -6.945  0.26 13.51 ?  41  VAL   A HG13 1 
ATOM   1086 H  HG21 A VAL   A 1 41  ? 31.887 1.235   -8.304  0.74 12.67 ?  41  VAL   A HG21 1 
ATOM   1087 H  HG21 B VAL   A 1 41  ? 31.280 1.539   -8.555  0.26 13.66 ?  41  VAL   A HG21 1 
ATOM   1088 H  HG22 A VAL   A 1 41  ? 30.708 1.903   -7.475  0.74 12.67 ?  41  VAL   A HG22 1 
ATOM   1089 H  HG22 B VAL   A 1 41  ? 30.029 1.944   -7.666  0.26 13.66 ?  41  VAL   A HG22 1 
ATOM   1090 H  HG23 A VAL   A 1 41  ? 32.208 2.373   -7.243  0.74 12.67 ?  41  VAL   A HG23 1 
ATOM   1091 H  HG23 B VAL   A 1 41  ? 31.439 2.630   -7.412  0.26 13.66 ?  41  VAL   A HG23 1 
ATOM   1092 N  N    A TYR   A 1 42  ? 31.656 3.441   -4.570  0.74 10.26 ?  42  TYR   A N    1 
ATOM   1093 N  N    B TYR   A 1 42  ? 31.343 3.491   -4.793  0.26 10.11 ?  42  TYR   A N    1 
ATOM   1094 C  CA   A TYR   A 1 42  ? 32.390 4.629   -4.149  0.74 10.56 ?  42  TYR   A CA   1 
ATOM   1095 C  CA   B TYR   A 1 42  ? 32.119 4.655   -4.378  0.26 10.33 ?  42  TYR   A CA   1 
ATOM   1096 C  C    A TYR   A 1 42  ? 32.115 5.006   -2.704  0.74 10.31 ?  42  TYR   A C    1 
ATOM   1097 C  C    B TYR   A 1 42  ? 31.892 5.036   -2.921  0.26 10.26 ?  42  TYR   A C    1 
ATOM   1098 O  O    A TYR   A 1 42  ? 32.680 5.994   -2.212  0.74 10.80 ?  42  TYR   A O    1 
ATOM   1099 O  O    B TYR   A 1 42  ? 32.479 6.020   -2.454  0.26 10.61 ?  42  TYR   A O    1 
ATOM   1100 C  CB   A TYR   A 1 42  ? 32.051 5.819   -5.070  0.74 11.20 ?  42  TYR   A CB   1 
ATOM   1101 C  CB   B TYR   A 1 42  ? 31.796 5.854   -5.277  0.26 10.67 ?  42  TYR   A CB   1 
ATOM   1102 C  CG   A TYR   A 1 42  ? 32.237 5.498   -6.538  0.74 11.92 ?  42  TYR   A CG   1 
ATOM   1103 C  CG   B TYR   A 1 42  ? 31.972 5.568   -6.749  0.26 11.20 ?  42  TYR   A CG   1 
ATOM   1104 C  CD1  A TYR   A 1 42  ? 33.501 5.296   -7.065  0.74 12.75 ?  42  TYR   A CD1  1 
ATOM   1105 C  CD1  B TYR   A 1 42  ? 33.231 5.358   -7.290  0.26 11.20 ?  42  TYR   A CD1  1 
ATOM   1106 C  CD2  A TYR   A 1 42  ? 31.150 5.360   -7.391  0.74 13.25 ?  42  TYR   A CD2  1 
ATOM   1107 C  CD2  B TYR   A 1 42  ? 30.876 5.507   -7.597  0.26 12.14 ?  42  TYR   A CD2  1 
ATOM   1108 C  CE1  A TYR   A 1 42  ? 33.684 4.975   -8.400  0.74 13.16 ?  42  TYR   A CE1  1 
ATOM   1109 C  CE1  B TYR   A 1 42  ? 33.395 5.090   -8.636  0.26 11.88 ?  42  TYR   A CE1  1 
ATOM   1110 C  CE2  A TYR   A 1 42  ? 31.325 5.045   -8.731  0.74 14.11 ?  42  TYR   A CE2  1 
ATOM   1111 C  CE2  B TYR   A 1 42  ? 31.029 5.245   -8.941  0.26 12.92 ?  42  TYR   A CE2  1 
ATOM   1112 C  CZ   A TYR   A 1 42  ? 32.595 4.855   -9.227  0.74 13.86 ?  42  TYR   A CZ   1 
ATOM   1113 C  CZ   B TYR   A 1 42  ? 32.288 5.038   -9.456  0.26 12.65 ?  42  TYR   A CZ   1 
ATOM   1114 O  OH   A TYR   A 1 42  ? 32.774 4.538   -10.553 0.74 15.35 ?  42  TYR   A OH   1 
ATOM   1115 O  OH   B TYR   A 1 42  ? 32.433 4.778   -10.798 0.26 13.12 ?  42  TYR   A OH   1 
ATOM   1116 H  H    A TYR   A 1 42  ? 30.875 3.618   -4.875  0.74 12.45 ?  42  TYR   A H    1 
ATOM   1117 H  H    B TYR   A 1 42  ? 30.554 3.684   -5.083  0.26 12.28 ?  42  TYR   A H    1 
ATOM   1118 H  HA   A TYR   A 1 42  ? 33.343 4.463   -4.236  0.74 12.82 ?  42  TYR   A HA   1 
ATOM   1119 H  HA   B TYR   A 1 42  ? 33.059 4.456   -4.490  0.26 12.54 ?  42  TYR   A HA   1 
ATOM   1120 H  HB2  A TYR   A 1 42  ? 31.124 6.073   -4.933  0.74 13.59 ?  42  TYR   A HB2  1 
ATOM   1121 H  HB2  B TYR   A 1 42  ? 30.873 6.118   -5.137  0.26 12.95 ?  42  TYR   A HB2  1 
ATOM   1122 H  HB3  A TYR   A 1 42  ? 32.631 6.570   -4.851  0.74 13.59 ?  42  TYR   A HB3  1 
ATOM   1123 H  HB3  B TYR   A 1 42  ? 32.387 6.589   -5.048  0.26 12.95 ?  42  TYR   A HB3  1 
ATOM   1124 H  HD1  A TYR   A 1 42  ? 34.248 5.375   -6.512  0.74 15.44 ?  42  TYR   A HD1  1 
ATOM   1125 H  HD1  B TYR   A 1 42  ? 33.978 5.393   -6.735  0.26 13.58 ?  42  TYR   A HD1  1 
ATOM   1126 H  HD2  A TYR   A 1 42  ? 30.290 5.492   -7.059  0.74 16.04 ?  42  TYR   A HD2  1 
ATOM   1127 H  HD2  B TYR   A 1 42  ? 30.023 5.647   -7.253  0.26 14.71 ?  42  TYR   A HD2  1 
ATOM   1128 H  HE1  A TYR   A 1 42  ? 34.542 4.850   -8.741  0.74 15.93 ?  42  TYR   A HE1  1 
ATOM   1129 H  HE1  B TYR   A 1 42  ? 34.247 4.950   -8.984  0.26 14.39 ?  42  TYR   A HE1  1 
ATOM   1130 H  HE2  A TYR   A 1 42  ? 30.583 4.967   -9.293  0.74 17.08 ?  42  TYR   A HE2  1 
ATOM   1131 H  HE2  B TYR   A 1 42  ? 30.285 5.206   -9.496  0.26 15.64 ?  42  TYR   A HE2  1 
ATOM   1132 H  HH   A TYR   A 1 42  ? 33.593 4.443   -10.721 0.74 18.56 ?  42  TYR   A HH   1 
ATOM   1133 H  HH   B TYR   A 1 42  ? 31.684 4.772   -11.172 0.26 15.89 ?  42  TYR   A HH   1 
ATOM   1134 N  N    A LEU   A 1 43  ? 31.263 4.240   -2.022  0.74 10.08 ?  43  LEU   A N    1 
ATOM   1135 N  N    B LEU   A 1 43  ? 31.063 4.284   -2.200  0.26 10.10 ?  43  LEU   A N    1 
ATOM   1136 C  CA   A LEU   A 1 43  ? 30.808 4.577   -0.677  0.74 9.81  ?  43  LEU   A CA   1 
ATOM   1137 C  CA   B LEU   A 1 43  ? 30.672 4.620   -0.831  0.26 10.15 ?  43  LEU   A CA   1 
ATOM   1138 C  C    A LEU   A 1 43  ? 30.333 6.027   -0.586  0.74 9.82  ?  43  LEU   A C    1 
ATOM   1139 C  C    B LEU   A 1 43  ? 30.179 6.062   -0.722  0.26 10.36 ?  43  LEU   A C    1 
ATOM   1140 O  O    A LEU   A 1 43  ? 30.604 6.731   0.390   0.74 11.19 ?  43  LEU   A O    1 
ATOM   1141 O  O    B LEU   A 1 43  ? 30.416 6.752   0.271   0.26 10.36 ?  43  LEU   A O    1 
ATOM   1142 C  CB   A LEU   A 1 43  ? 31.849 4.262   0.395   0.74 10.06 ?  43  LEU   A CB   1 
ATOM   1143 C  CB   B LEU   A 1 43  ? 31.779 4.320   0.182   0.26 10.20 ?  43  LEU   A CB   1 
ATOM   1144 C  CG   A LEU   A 1 43  ? 32.361 2.821   0.482   0.74 10.39 ?  43  LEU   A CG   1 
ATOM   1145 C  CG   B LEU   A 1 43  ? 32.226 2.858   0.305   0.26 10.31 ?  43  LEU   A CG   1 
ATOM   1146 C  CD1  A LEU   A 1 43  ? 33.404 2.716   1.584   0.74 11.41 ?  43  LEU   A CD1  1 
ATOM   1147 C  CD1  B LEU   A 1 43  ? 33.270 2.713   1.403   0.26 10.48 ?  43  LEU   A CD1  1 
ATOM   1148 C  CD2  A LEU   A 1 43  ? 31.231 1.830   0.719   0.74 10.73 ?  43  LEU   A CD2  1 
ATOM   1149 C  CD2  B LEU   A 1 43  ? 31.039 1.930   0.560   0.26 10.41 ?  43  LEU   A CD2  1 
ATOM   1150 H  H    A LEU   A 1 43  ? 30.931 3.501   -2.324  0.74 12.24 ?  43  LEU   A H    1 
ATOM   1151 H  H    B LEU   A 1 43  ? 30.707 3.559   -2.489  0.26 12.26 ?  43  LEU   A H    1 
ATOM   1152 H  HA   A LEU   A 1 43  ? 30.035 4.019   -0.486  0.74 11.91 ?  43  LEU   A HA   1 
ATOM   1153 H  HA   B LEU   A 1 43  ? 29.922 4.056   -0.600  0.26 12.32 ?  43  LEU   A HA   1 
ATOM   1154 H  HB2  A LEU   A 1 43  ? 32.616 4.834   0.244   0.74 12.21 ?  43  LEU   A HB2  1 
ATOM   1155 H  HB2  B LEU   A 1 43  ? 32.559 4.840   -0.056  0.26 12.38 ?  43  LEU   A HB2  1 
ATOM   1156 H  HB3  A LEU   A 1 43  ? 31.456 4.475   1.257   0.74 12.21 ?  43  LEU   A HB3  1 
ATOM   1157 H  HB3  B LEU   A 1 43  ? 31.464 4.596   1.058   0.26 12.38 ?  43  LEU   A HB3  1 
ATOM   1158 H  HG   A LEU   A 1 43  ? 32.793 2.591   -0.356  0.74 12.61 ?  43  LEU   A HG   1 
ATOM   1159 H  HG   B LEU   A 1 43  ? 32.638 2.589   -0.529  0.26 12.52 ?  43  LEU   A HG   1 
ATOM   1160 H  HD11 A LEU   A 1 43  ? 33.724 1.801   1.630   0.74 13.83 ?  43  LEU   A HD11 1 
ATOM   1161 H  HD11 B LEU   A 1 43  ? 33.541 1.783   1.461   0.26 12.71 ?  43  LEU   A HD11 1 
ATOM   1162 H  HD12 A LEU   A 1 43  ? 34.140 3.314   1.383   0.74 13.83 ?  43  LEU   A HD12 1 
ATOM   1163 H  HD12 B LEU   A 1 43  ? 34.037 3.267   1.186   0.26 12.71 ?  43  LEU   A HD12 1 
ATOM   1164 H  HD13 A LEU   A 1 43  ? 32.996 2.966   2.428   0.74 13.83 ?  43  LEU   A HD13 1 
ATOM   1165 H  HD13 B LEU   A 1 43  ? 32.885 2.998   2.247   0.26 12.71 ?  43  LEU   A HD13 1 
ATOM   1166 H  HD21 A LEU   A 1 43  ? 31.610 0.946   0.842   0.74 13.01 ?  43  LEU   A HD21 1 
ATOM   1167 H  HD21 B LEU   A 1 43  ? 31.372 1.050   0.796   0.26 12.64 ?  43  LEU   A HD21 1 
ATOM   1168 H  HD22 A LEU   A 1 43  ? 30.743 2.096   1.512   0.74 13.01 ?  43  LEU   A HD22 1 
ATOM   1169 H  HD22 B LEU   A 1 43  ? 30.507 2.289   1.287   0.26 12.64 ?  43  LEU   A HD22 1 
ATOM   1170 H  HD23 A LEU   A 1 43  ? 30.643 1.835   -0.052  0.74 13.01 ?  43  LEU   A HD23 1 
ATOM   1171 H  HD23 B LEU   A 1 43  ? 30.503 1.876   -0.247  0.26 12.64 ?  43  LEU   A HD23 1 
ATOM   1172 N  N    A LYS   A 1 44  ? 29.601 6.470   -1.614  0.74 10.10 ?  44  LYS   A N    1 
ATOM   1173 N  N    B LYS   A 1 44  ? 29.468 6.513   -1.754  0.26 10.69 ?  44  LYS   A N    1 
ATOM   1174 C  CA   A LYS   A 1 44  ? 28.952 7.777   -1.615  0.74 10.57 ?  44  LYS   A CA   1 
ATOM   1175 C  CA   B LYS   A 1 44  ? 28.820 7.824   -1.754  0.26 11.18 ?  44  LYS   A CA   1 
ATOM   1176 C  C    A LYS   A 1 44  ? 27.516 7.579   -1.140  0.74 10.07 ?  44  LYS   A C    1 
ATOM   1177 C  C    B LYS   A 1 44  ? 27.423 7.645   -1.180  0.26 10.23 ?  44  LYS   A C    1 
ATOM   1178 O  O    A LYS   A 1 44  ? 26.673 7.038   -1.867  0.74 10.94 ?  44  LYS   A O    1 
ATOM   1179 O  O    B LYS   A 1 44  ? 26.504 7.205   -1.875  0.26 10.31 ?  44  LYS   A O    1 
ATOM   1180 C  CB   A LYS   A 1 44  ? 29.014 8.419   -2.996  0.74 12.50 ?  44  LYS   A CB   1 
ATOM   1181 C  CB   B LYS   A 1 44  ? 28.774 8.392   -3.168  0.26 13.44 ?  44  LYS   A CB   1 
ATOM   1182 C  CG   A LYS   A 1 44  ? 30.411 8.871   -3.406  0.74 15.55 ?  44  LYS   A CG   1 
ATOM   1183 C  CG   B LYS   A 1 44  ? 30.104 8.937   -3.666  0.26 15.99 ?  44  LYS   A CG   1 
ATOM   1184 C  CD   A LYS   A 1 44  ? 31.051 9.816   -2.391  0.74 20.81 ?  44  LYS   A CD   1 
ATOM   1185 C  CD   B LYS   A 1 44  ? 30.872 9.619   -2.544  0.26 18.77 ?  44  LYS   A CD   1 
ATOM   1186 C  CE   A LYS   A 1 44  ? 32.381 10.343  -2.897  0.74 24.13 ?  44  LYS   A CE   1 
ATOM   1187 C  CE   B LYS   A 1 44  ? 31.948 10.537  -3.076  0.26 20.49 ?  44  LYS   A CE   1 
ATOM   1188 N  NZ   A LYS   A 1 44  ? 33.200 10.938  -1.809  0.74 25.94 ?  44  LYS   A NZ   1 
ATOM   1189 N  NZ   B LYS   A 1 44  ? 32.794 11.073  -1.978  0.26 21.64 ?  44  LYS   A NZ   1 
ATOM   1190 H  H    A LYS   A 1 44  ? 29.466 6.016   -2.339  0.74 12.26 ?  44  LYS   A H    1 
ATOM   1191 H  H    B LYS   A 1 44  ? 29.343 6.070   -2.479  0.26 12.97 ?  44  LYS   A H    1 
ATOM   1192 H  HA   A LYS   A 1 44  ? 29.398 8.351   -0.973  0.74 12.83 ?  44  LYS   A HA   1 
ATOM   1193 H  HA   B LYS   A 1 44  ? 29.290 8.422   -1.156  0.26 13.56 ?  44  LYS   A HA   1 
ATOM   1194 H  HB2  A LYS   A 1 44  ? 28.707 7.782   -3.653  0.74 15.14 ?  44  LYS   A HB2  1 
ATOM   1195 H  HB2  B LYS   A 1 44  ? 28.500 7.687   -3.780  0.26 16.27 ?  44  LYS   A HB2  1 
ATOM   1196 H  HB3  A LYS   A 1 44  ? 28.442 9.203   -2.998  0.74 15.14 ?  44  LYS   A HB3  1 
ATOM   1197 H  HB3  B LYS   A 1 44  ? 28.130 9.116   -3.198  0.26 16.27 ?  44  LYS   A HB3  1 
ATOM   1198 H  HG2  A LYS   A 1 44  ? 30.988 8.094   -3.493  0.74 18.80 ?  44  LYS   A HG2  1 
ATOM   1199 H  HG2  B LYS   A 1 44  ? 30.644 8.207   -4.009  0.26 19.33 ?  44  LYS   A HG2  1 
ATOM   1200 H  HG3  A LYS   A 1 44  ? 30.361 9.341   -4.255  0.74 18.80 ?  44  LYS   A HG3  1 
ATOM   1201 H  HG3  B LYS   A 1 44  ? 29.943 9.593   -4.364  0.26 19.33 ?  44  LYS   A HG3  1 
ATOM   1202 H  HD2  A LYS   A 1 44  ? 30.455 10.565  -2.232  0.74 25.11 ?  44  LYS   A HD2  1 
ATOM   1203 H  HD2  B LYS   A 1 44  ? 30.255 10.149  -2.011  0.26 22.67 ?  44  LYS   A HD2  1 
ATOM   1204 H  HD3  A LYS   A 1 44  ? 31.214 9.334   -1.563  0.74 25.11 ?  44  LYS   A HD3  1 
ATOM   1205 H  HD3  B LYS   A 1 44  ? 31.293 8.938   -1.987  0.26 22.67 ?  44  LYS   A HD3  1 
ATOM   1206 H  HE2  A LYS   A 1 44  ? 32.883 9.611   -3.288  0.74 29.10 ?  44  LYS   A HE2  1 
ATOM   1207 H  HE2  B LYS   A 1 44  ? 32.514 10.042  -3.686  0.26 24.72 ?  44  LYS   A HE2  1 
ATOM   1208 H  HE3  A LYS   A 1 44  ? 32.215 11.028  -3.563  0.74 29.10 ?  44  LYS   A HE3  1 
ATOM   1209 H  HE3  B LYS   A 1 44  ? 31.529 11.283  -3.532  0.26 24.72 ?  44  LYS   A HE3  1 
ATOM   1210 H  HZ1  A LYS   A 1 44  ? 33.970 11.237  -2.138  0.74 31.27 ?  44  LYS   A HZ1  1 
ATOM   1211 H  HZ1  B LYS   A 1 44  ? 33.419 11.610  -2.313  0.26 26.11 ?  44  LYS   A HZ1  1 
ATOM   1212 H  HZ2  A LYS   A 1 44  ? 32.760 11.620  -1.438  0.74 31.27 ?  44  LYS   A HZ2  1 
ATOM   1213 H  HZ2  B LYS   A 1 44  ? 32.293 11.532  -1.404  0.26 26.11 ?  44  LYS   A HZ2  1 
ATOM   1214 H  HZ3  A LYS   A 1 44  ? 33.366 10.329  -1.184  0.74 31.27 ?  44  LYS   A HZ3  1 
ATOM   1215 H  HZ3  B LYS   A 1 44  ? 33.190 10.403  -1.545  0.26 26.11 ?  44  LYS   A HZ3  1 
ATOM   1216 N  N    . HIS   A 1 45  ? 27.257 7.982   0.098   1.00 9.97  ?  45  HIS   A N    1 
ATOM   1217 C  CA   . HIS   A 1 45  ? 26.023 7.642   0.800   1.00 10.06 ?  45  HIS   A CA   1 
ATOM   1218 C  C    . HIS   A 1 45  ? 25.000 8.767   0.635   1.00 10.80 ?  45  HIS   A C    1 
ATOM   1219 O  O    . HIS   A 1 45  ? 24.706 9.527   1.557   1.00 12.57 ?  45  HIS   A O    1 
ATOM   1220 C  CB   . HIS   A 1 45  ? 26.324 7.388   2.267   1.00 9.86  ?  45  HIS   A CB   1 
ATOM   1221 C  CG   . HIS   A 1 45  ? 27.439 6.424   2.498   1.00 9.63  ?  45  HIS   A CG   1 
ATOM   1222 N  ND1  . HIS   A 1 45  ? 27.429 5.133   2.008   1.00 10.06 ?  45  HIS   A ND1  1 
ATOM   1223 C  CD2  . HIS   A 1 45  ? 28.604 6.578   3.170   1.00 9.89  ?  45  HIS   A CD2  1 
ATOM   1224 C  CE1  . HIS   A 1 45  ? 28.551 4.539   2.378   1.00 9.77  ?  45  HIS   A CE1  1 
ATOM   1225 N  NE2  . HIS   A 1 45  ? 29.280 5.391   3.083   1.00 9.81  ?  45  HIS   A NE2  1 
ATOM   1226 H  H    A HIS   A 1 45  ? 27.792 8.466   0.565   0.74 12.11 ?  45  HIS   A H    1 
ATOM   1227 H  H    B HIS   A 1 45  ? 27.837 8.396   0.578   0.26 12.11 ?  45  HIS   A H    1 
ATOM   1228 H  HA   . HIS   A 1 45  ? 25.645 6.831   0.418   1.00 12.22 ?  45  HIS   A HA   1 
ATOM   1229 H  HB2  . HIS   A 1 45  ? 26.557 8.231   2.687   1.00 11.97 ?  45  HIS   A HB2  1 
ATOM   1230 H  HB3  . HIS   A 1 45  ? 25.522 7.027   2.690   1.00 11.97 ?  45  HIS   A HB3  1 
ATOM   1231 H  HD2  . HIS   A 1 45  ? 28.897 7.353   3.605   1.00 12.00 ?  45  HIS   A HD2  1 
ATOM   1232 H  HE1  . HIS   A 1 45  ? 28.781 3.660   2.189   1.00 11.86 ?  45  HIS   A HE1  1 
ATOM   1233 H  HE2  . HIS   A 1 45  ? 30.051 5.225   3.428   1.00 11.91 ?  45  HIS   A HE2  1 
ATOM   1234 N  N    A GLY   A 1 46  ? 24.403 8.823   -0.551  0.74 11.72 ?  46  GLY   A N    1 
ATOM   1235 N  N    B GLY   A 1 46  ? 24.478 8.891   -0.583  0.26 11.07 ?  46  GLY   A N    1 
ATOM   1236 C  CA   A GLY   A 1 46  ? 23.564 9.956   -0.888  0.74 12.55 ?  46  GLY   A CA   1 
ATOM   1237 C  CA   B GLY   A 1 46  ? 23.694 10.066  -0.932  0.26 11.24 ?  46  GLY   A CA   1 
ATOM   1238 C  C    A GLY   A 1 46  ? 22.086 9.798   -0.600  0.74 12.30 ?  46  GLY   A C    1 
ATOM   1239 C  C    B GLY   A 1 46  ? 22.220 9.996   -0.582  0.26 11.12 ?  46  GLY   A C    1 
ATOM   1240 O  O    A GLY   A 1 46  ? 21.421 10.775  -0.233  0.74 13.63 ?  46  GLY   A O    1 
ATOM   1241 O  O    B GLY   A 1 46  ? 21.590 11.021  -0.301  0.26 11.69 ?  46  GLY   A O    1 
ATOM   1242 H  H    A GLY   A 1 46  ? 24.464 8.230   -1.166  0.74 14.20 ?  46  GLY   A H    1 
ATOM   1243 H  H    B GLY   A 1 46  ? 24.563 8.319   -1.217  0.26 13.43 ?  46  GLY   A H    1 
ATOM   1244 H  HA2  A GLY   A 1 46  ? 23.866 10.736  -0.393  0.74 15.20 ?  46  GLY   A HA2  1 
ATOM   1245 H  HA2  B GLY   A 1 46  ? 24.080 10.842  -0.487  0.26 13.63 ?  46  GLY   A HA2  1 
ATOM   1246 H  HA3  A GLY   A 1 46  ? 23.654 10.149  -1.830  0.74 15.20 ?  46  GLY   A HA3  1 
ATOM   1247 H  HA3  B GLY   A 1 46  ? 23.758 10.213  -1.887  0.26 13.63 ?  46  GLY   A HA3  1 
ATOM   1248 N  N    A GLY   A 1 47  ? 21.549 8.593   -0.779  0.74 12.06 ?  47  GLY   A N    1 
ATOM   1249 N  N    B GLY   A 1 47  ? 21.654 8.799   -0.623  0.26 10.94 ?  47  GLY   A N    1 
ATOM   1250 C  CA   A GLY   A 1 47  ? 20.117 8.391   -0.720  0.74 12.01 ?  47  GLY   A CA   1 
ATOM   1251 C  CA   B GLY   A 1 47  ? 20.241 8.617   -0.366  0.26 11.02 ?  47  GLY   A CA   1 
ATOM   1252 C  C    A GLY   A 1 47  ? 19.787 6.965   -0.337  0.74 11.60 ?  47  GLY   A C    1 
ATOM   1253 C  C    B GLY   A 1 47  ? 19.937 7.155   -0.121  0.26 10.96 ?  47  GLY   A C    1 
ATOM   1254 O  O    A GLY   A 1 47  ? 20.674 6.140   -0.108  0.74 11.76 ?  47  GLY   A O    1 
ATOM   1255 O  O    B GLY   A 1 47  ? 20.837 6.316   -0.057  0.26 11.26 ?  47  GLY   A O    1 
ATOM   1256 H  H    A GLY   A 1 47  ? 22.001 7.867   -0.905  0.74 14.62 ?  47  GLY   A H    1 
ATOM   1257 H  H    B GLY   A 1 47  ? 22.073 8.079   -0.794  0.26 13.27 ?  47  GLY   A H    1 
ATOM   1258 H  HA2  A GLY   A 1 47  ? 19.720 8.984   -0.064  0.74 14.55 ?  47  GLY   A HA2  1 
ATOM   1259 H  HA2  B GLY   A 1 47  ? 19.968 9.143   0.407   0.26 13.36 ?  47  GLY   A HA2  1 
ATOM   1260 H  HA3  A GLY   A 1 47  ? 19.728 8.575   -1.587  0.74 14.55 ?  47  GLY   A HA3  1 
ATOM   1261 H  HA3  B GLY   A 1 47  ? 19.733 8.918   -1.136  0.26 13.36 ?  47  GLY   A HA3  1 
ATOM   1262 N  N    A GLY   A 1 48  ? 18.492 6.669   -0.283  0.74 11.72 ?  48  GLY   A N    1 
ATOM   1263 N  N    B GLY   A 1 48  ? 18.647 6.855   0.016   0.26 11.38 ?  48  GLY   A N    1 
ATOM   1264 C  CA   A GLY   A 1 48  ? 18.078 5.353   0.144   0.74 11.98 ?  48  GLY   A CA   1 
ATOM   1265 C  CA   B GLY   A 1 48  ? 18.242 5.483   0.263   0.26 11.51 ?  48  GLY   A CA   1 
ATOM   1266 C  C    A GLY   A 1 48  ? 18.582 5.067   1.542   0.74 11.28 ?  48  GLY   A C    1 
ATOM   1267 C  C    B GLY   A 1 48  ? 18.680 5.012   1.640   0.26 11.12 ?  48  GLY   A C    1 
ATOM   1268 O  O    A GLY   A 1 48  ? 18.778 5.977   2.362   0.74 11.66 ?  48  GLY   A O    1 
ATOM   1269 O  O    B GLY   A 1 48  ? 18.719 5.778   2.610   0.26 11.49 ?  48  GLY   A O    1 
ATOM   1270 H  H    A GLY   A 1 48  ? 17.843 7.204   -0.472  0.74 14.20 ?  48  GLY   A H    1 
ATOM   1271 H  H    B GLY   A 1 48  ? 18.003 7.423   -0.027  0.26 13.79 ?  48  GLY   A H    1 
ATOM   1272 H  HA2  A GLY   A 1 48  ? 17.111 5.280   0.140   0.74 14.52 ?  48  GLY   A HA2  1 
ATOM   1273 H  HA2  B GLY   A 1 48  ? 17.279 5.411   0.202   0.26 13.95 ?  48  GLY   A HA2  1 
ATOM   1274 H  HA3  A GLY   A 1 48  ? 18.445 4.679   -0.450  0.74 14.52 ?  48  GLY   A HA3  1 
ATOM   1275 H  HA3  B GLY   A 1 48  ? 18.641 4.901   -0.404  0.26 13.95 ?  48  GLY   A HA3  1 
ATOM   1276 N  N    A VAL   A 1 49  ? 18.802 3.780   1.815   0.74 10.58 ?  49  VAL   A N    1 
ATOM   1277 N  N    B VAL   A 1 49  ? 19.009 3.720   1.725   0.26 10.67 ?  49  VAL   A N    1 
ATOM   1278 C  CA   A VAL   A 1 49  ? 19.315 3.355   3.113   0.74 10.80 ?  49  VAL   A CA   1 
ATOM   1279 C  CA   B VAL   A 1 49  ? 19.566 3.177   2.961   0.26 10.10 ?  49  VAL   A CA   1 
ATOM   1280 C  C    A VAL   A 1 49  ? 20.624 4.067   3.439   0.74 10.04 ?  49  VAL   A C    1 
ATOM   1281 C  C    B VAL   A 1 49  ? 20.820 3.944   3.353   0.26 9.26  ?  49  VAL   A C    1 
ATOM   1282 O  O    A VAL   A 1 49  ? 20.834 4.512   4.572   0.74 10.36 ?  49  VAL   A O    1 
ATOM   1283 O  O    B VAL   A 1 49  ? 21.003 4.319   4.516   0.26 8.93  ?  49  VAL   A O    1 
ATOM   1284 C  CB   A VAL   A 1 49  ? 19.481 1.823   3.133   0.74 11.34 ?  49  VAL   A CB   1 
ATOM   1285 C  CB   B VAL   A 1 49  ? 19.867 1.676   2.803   0.26 9.74  ?  49  VAL   A CB   1 
ATOM   1286 C  CG1  A VAL   A 1 49  ? 20.286 1.378   4.350   0.74 11.37 ?  49  VAL   A CG1  1 
ATOM   1287 C  CG1  B VAL   A 1 49  ? 20.715 1.188   3.974   0.26 9.37  ?  49  VAL   A CG1  1 
ATOM   1288 C  CG2  A VAL   A 1 49  ? 18.118 1.137   3.104   0.74 13.07 ?  49  VAL   A CG2  1 
ATOM   1289 C  CG2  B VAL   A 1 49  ? 18.590 0.869   2.695   0.26 9.82  ?  49  VAL   A CG2  1 
ATOM   1290 H  H    A VAL   A 1 49  ? 18.659 3.132   1.270   0.74 12.84 ?  49  VAL   A H    1 
ATOM   1291 H  H    B VAL   A 1 49  ? 18.928 3.145   1.092   0.26 12.94 ?  49  VAL   A H    1 
ATOM   1292 H  HA   A VAL   A 1 49  ? 18.678 3.588   3.804   0.74 13.10 ?  49  VAL   A HA   1 
ATOM   1293 H  HA   B VAL   A 1 49  ? 18.919 3.277   3.675   0.26 12.26 ?  49  VAL   A HA   1 
ATOM   1294 H  HB   A VAL   A 1 49  ? 19.972 1.545   2.342   0.74 13.75 ?  49  VAL   A HB   1 
ATOM   1295 H  HB   B VAL   A 1 49  ? 20.380 1.543   1.992   0.26 11.83 ?  49  VAL   A HB   1 
ATOM   1296 H  HG11 A VAL   A 1 49  ? 20.141 0.432   4.496   0.74 13.78 ?  49  VAL   A HG11 1 
ATOM   1297 H  HG11 B VAL   A 1 49  ? 20.645 0.224   4.035   0.26 11.38 ?  49  VAL   A HG11 1 
ATOM   1298 H  HG12 A VAL   A 1 49  ? 21.228 1.547   4.190   0.74 13.78 ?  49  VAL   A HG12 1 
ATOM   1299 H  HG12 B VAL   A 1 49  ? 21.643 1.439   3.826   0.26 11.38 ?  49  VAL   A HG12 1 
ATOM   1300 H  HG13 A VAL   A 1 49  ? 19.985 1.881   5.125   0.74 13.78 ?  49  VAL   A HG13 1 
ATOM   1301 H  HG13 B VAL   A 1 49  ? 20.390 1.593   4.793   0.26 11.38 ?  49  VAL   A HG13 1 
ATOM   1302 H  HG21 A VAL   A 1 49  ? 18.247 0.176   3.117   0.74 15.82 ?  49  VAL   A HG21 1 
ATOM   1303 H  HG21 B VAL   A 1 49  ? 18.818 -0.047  2.468   0.26 11.92 ?  49  VAL   A HG21 1 
ATOM   1304 H  HG22 A VAL   A 1 49  ? 17.612 1.415   3.884   0.74 15.82 ?  49  VAL   A HG22 1 
ATOM   1305 H  HG22 B VAL   A 1 49  ? 18.131 0.895   3.547   0.26 11.92 ?  49  VAL   A HG22 1 
ATOM   1306 H  HG23 A VAL   A 1 49  ? 17.654 1.400   2.295   0.74 15.82 ?  49  VAL   A HG23 1 
ATOM   1307 H  HG23 B VAL   A 1 49  ? 18.037 1.255   2.001   0.26 11.92 ?  49  VAL   A HG23 1 
ATOM   1308 N  N    A ALA   A 1 50  ? 21.541 4.133   2.469   0.74 9.60  ?  50  ALA   A N    1 
ATOM   1309 N  N    B ALA   A 1 50  ? 21.718 4.157   2.389   0.26 8.99  ?  50  ALA   A N    1 
ATOM   1310 C  CA   A ALA   A 1 50  ? 22.864 4.694   2.735   0.74 9.46  ?  50  ALA   A CA   1 
ATOM   1311 C  CA   B ALA   A 1 50  ? 23.012 4.755   2.698   0.26 9.17  ?  50  ALA   A CA   1 
ATOM   1312 C  C    A ALA   A 1 50  ? 22.769 6.153   3.155   0.74 9.46  ?  50  ALA   A C    1 
ATOM   1313 C  C    B ALA   A 1 50  ? 22.864 6.205   3.135   0.26 9.26  ?  50  ALA   A C    1 
ATOM   1314 O  O    A ALA   A 1 50  ? 23.394 6.572   4.136   0.74 9.83  ?  50  ALA   A O    1 
ATOM   1315 O  O    B ALA   A 1 50  ? 23.499 6.634   4.105   0.26 9.42  ?  50  ALA   A O    1 
ATOM   1316 C  CB   A ALA   A 1 50  ? 23.740 4.561   1.493   0.74 9.58  ?  50  ALA   A CB   1 
ATOM   1317 C  CB   B ALA   A 1 50  ? 23.934 4.652   1.484   0.26 9.36  ?  50  ALA   A CB   1 
ATOM   1318 H  H    A ALA   A 1 50  ? 21.422 3.870   1.657   0.74 11.66 ?  50  ALA   A H    1 
ATOM   1319 H  H    B ALA   A 1 50  ? 21.598 3.967   1.559   0.26 10.93 ?  50  ALA   A H    1 
ATOM   1320 H  HA   A ALA   A 1 50  ? 23.281 4.202   3.457   0.74 11.49 ?  50  ALA   A HA   1 
ATOM   1321 H  HA   B ALA   A 1 50  ? 23.420 4.267   3.426   0.26 11.14 ?  50  ALA   A HA   1 
ATOM   1322 H  HB1  A ALA   A 1 50  ? 24.615 4.938   1.682   0.74 11.64 ?  50  ALA   A HB1  1 
ATOM   1323 H  HB1  B ALA   A 1 50  ? 24.791 5.049   1.703   0.26 11.37 ?  50  ALA   A HB1  1 
ATOM   1324 H  HB2  A ALA   A 1 50  ? 23.826 3.624   1.264   0.74 11.64 ?  50  ALA   A HB2  1 
ATOM   1325 H  HB2  B ALA   A 1 50  ? 24.051 3.716   1.254   0.26 11.37 ?  50  ALA   A HB2  1 
ATOM   1326 H  HB3  A ALA   A 1 50  ? 23.326 5.046   0.760   0.74 11.64 ?  50  ALA   A HB3  1 
ATOM   1327 H  HB3  B ALA   A 1 50  ? 23.531 5.126   0.738   0.26 11.37 ?  50  ALA   A HB3  1 
ATOM   1328 N  N    A GLY   A 1 51  ? 21.994 6.948   2.419   0.74 9.72  ?  51  GLY   A N    1 
ATOM   1329 N  N    B GLY   A 1 51  ? 22.035 6.976   2.433   0.26 9.52  ?  51  GLY   A N    1 
ATOM   1330 C  CA   A GLY   A 1 51  ? 21.836 8.339   2.800   0.74 10.40 ?  51  GLY   A CA   1 
ATOM   1331 C  CA   B GLY   A 1 51  ? 21.843 8.363   2.818   0.26 9.92  ?  51  GLY   A CA   1 
ATOM   1332 C  C    A GLY   A 1 51  ? 21.236 8.485   4.183   0.74 10.25 ?  51  GLY   A C    1 
ATOM   1333 C  C    B GLY   A 1 51  ? 21.222 8.499   4.193   0.26 10.01 ?  51  GLY   A C    1 
ATOM   1334 O  O    A GLY   A 1 51  ? 21.627 9.370   4.950   0.74 10.97 ?  51  GLY   A O    1 
ATOM   1335 O  O    B GLY   A 1 51  ? 21.590 9.387   4.966   0.26 10.24 ?  51  GLY   A O    1 
ATOM   1336 H  H    A GLY   A 1 51  ? 21.571 6.709   1.707   0.74 11.80 ?  51  GLY   A H    1 
ATOM   1337 H  H    B GLY   A 1 51  ? 21.587 6.722   1.745   0.26 11.56 ?  51  GLY   A H    1 
ATOM   1338 H  HA2  A GLY   A 1 51  ? 22.697 8.781   2.787   0.74 12.62 ?  51  GLY   A HA2  1 
ATOM   1339 H  HA2  B GLY   A 1 51  ? 22.698 8.818   2.823   0.26 12.04 ?  51  GLY   A HA2  1 
ATOM   1340 H  HA3  A GLY   A 1 51  ? 21.251 8.783   2.164   0.74 12.62 ?  51  GLY   A HA3  1 
ATOM   1341 H  HA3  B GLY   A 1 51  ? 21.264 8.802   2.176   0.26 12.04 ?  51  GLY   A HA3  1 
ATOM   1342 N  N    . ALA   A 1 52  ? 20.274 7.617   4.518   1.00 10.29 ?  52  ALA   A N    1 
ATOM   1343 C  CA   . ALA   A 1 52  ? 19.630 7.675   5.827   1.00 11.07 ?  52  ALA   A CA   1 
ATOM   1344 C  C    . ALA   A 1 52  ? 20.585 7.262   6.947   1.00 10.35 ?  52  ALA   A C    1 
ATOM   1345 O  O    . ALA   A 1 52  ? 20.659 7.926   7.987   1.00 11.35 ?  52  ALA   A O    1 
ATOM   1346 C  CB   . ALA   A 1 52  ? 18.372 6.803   5.819   1.00 12.56 ?  52  ALA   A CB   1 
ATOM   1347 H  H    A ALA   A 1 52  ? 19.990 6.981   4.008   0.74 12.49 ?  52  ALA   A H    1 
ATOM   1348 H  H    B ALA   A 1 52  ? 20.002 6.975   4.009   0.26 12.49 ?  52  ALA   A H    1 
ATOM   1349 H  HA   . ALA   A 1 52  ? 19.353 8.583   5.993   1.00 13.42 ?  52  ALA   A HA   1 
ATOM   1350 H  HB1  . ALA   A 1 52  ? 17.938 6.866   6.687   1.00 15.22 ?  52  ALA   A HB1  1 
ATOM   1351 H  HB2  . ALA   A 1 52  ? 17.768 7.125   5.129   1.00 15.22 ?  52  ALA   A HB2  1 
ATOM   1352 H  HB3  . ALA   A 1 52  ? 18.618 5.883   5.639   1.00 15.22 ?  52  ALA   A HB3  1 
ATOM   1353 N  N    A LEU   A 1 53  ? 21.320 6.161   6.768   0.74 10.01 ?  53  LEU   A N    1 
ATOM   1354 N  N    B LEU   A 1 53  ? 21.326 6.165   6.746   0.26 10.12 ?  53  LEU   A N    1 
ATOM   1355 C  CA   A LEU   A 1 53  ? 22.297 5.772   7.784   0.74 10.32 ?  53  LEU   A CA   1 
ATOM   1356 C  CA   B LEU   A 1 53  ? 22.290 5.722   7.749   0.26 10.21 ?  53  LEU   A CA   1 
ATOM   1357 C  C    A LEU   A 1 53  ? 23.338 6.867   7.968   0.74 9.62  ?  53  LEU   A C    1 
ATOM   1358 C  C    B LEU   A 1 53  ? 23.355 6.782   7.988   0.26 10.19 ?  53  LEU   A C    1 
ATOM   1359 O  O    A LEU   A 1 53  ? 23.641 7.274   9.093   0.74 10.44 ?  53  LEU   A O    1 
ATOM   1360 O  O    B LEU   A 1 53  ? 23.762 7.018   9.131   0.26 10.61 ?  53  LEU   A O    1 
ATOM   1361 C  CB   A LEU   A 1 53  ? 22.972 4.447   7.414   0.74 10.77 ?  53  LEU   A CB   1 
ATOM   1362 C  CB   B LEU   A 1 53  ? 22.955 4.416   7.308   0.26 10.09 ?  53  LEU   A CB   1 
ATOM   1363 C  CG   A LEU   A 1 53  ? 22.084 3.199   7.438   0.74 11.86 ?  53  LEU   A CG   1 
ATOM   1364 C  CG   B LEU   A 1 53  ? 22.225 3.080   7.475   0.26 9.89  ?  53  LEU   A CG   1 
ATOM   1365 C  CD1  A LEU   A 1 53  ? 22.831 2.001   6.880   0.74 12.62 ?  53  LEU   A CD1  1 
ATOM   1366 C  CD1  B LEU   A 1 53  ? 23.029 1.976   6.803   0.26 10.39 ?  53  LEU   A CD1  1 
ATOM   1367 C  CD2  A LEU   A 1 53  ? 21.569 2.905   8.843   0.74 12.95 ?  53  LEU   A CD2  1 
ATOM   1368 C  CD2  B LEU   A 1 53  ? 22.000 2.743   8.938   0.26 9.68  ?  53  LEU   A CD2  1 
ATOM   1369 H  H    A LEU   A 1 53  ? 21.272 5.635   6.084   0.74 12.16 ?  53  LEU   A H    1 
ATOM   1370 H  H    B LEU   A 1 53  ? 21.291 5.670   6.042   0.26 12.28 ?  53  LEU   A H    1 
ATOM   1371 H  HA   A LEU   A 1 53  ? 21.838 5.646   8.627   0.74 12.52 ?  53  LEU   A HA   1 
ATOM   1372 H  HA   B LEU   A 1 53  ? 21.830 5.565   8.587   0.26 12.39 ?  53  LEU   A HA   1 
ATOM   1373 H  HB2  A LEU   A 1 53  ? 23.329 4.526   6.514   0.74 13.06 ?  53  LEU   A HB2  1 
ATOM   1374 H  HB2  B LEU   A 1 53  ? 23.155 4.497   6.363   0.26 12.24 ?  53  LEU   A HB2  1 
ATOM   1375 H  HB3  A LEU   A 1 53  ? 23.699 4.291   8.035   0.74 13.06 ?  53  LEU   A HB3  1 
ATOM   1376 H  HB3  B LEU   A 1 53  ? 23.785 4.331   7.797   0.26 12.24 ?  53  LEU   A HB3  1 
ATOM   1377 H  HG   A LEU   A 1 53  ? 21.315 3.351   6.865   0.74 14.37 ?  53  LEU   A HG   1 
ATOM   1378 H  HG   B LEU   A 1 53  ? 21.361 3.126   7.036   0.26 12.01 ?  53  LEU   A HG   1 
ATOM   1379 H  HD11 A LEU   A 1 53  ? 22.248 1.225   6.904   0.74 15.28 ?  53  LEU   A HD11 1 
ATOM   1380 H  HD11 B LEU   A 1 53  ? 22.564 1.131   6.917   0.26 12.61 ?  53  LEU   A HD11 1 
ATOM   1381 H  HD12 A LEU   A 1 53  ? 23.092 2.188   5.964   0.74 15.28 ?  53  LEU   A HD12 1 
ATOM   1382 H  HD12 B LEU   A 1 53  ? 23.118 2.178   5.859   0.26 12.61 ?  53  LEU   A HD12 1 
ATOM   1383 H  HD13 A LEU   A 1 53  ? 23.619 1.840   7.422   0.74 15.28 ?  53  LEU   A HD13 1 
ATOM   1384 H  HD13 B LEU   A 1 53  ? 23.905 1.928   7.216   0.26 12.61 ?  53  LEU   A HD13 1 
ATOM   1385 H  HD21 A LEU   A 1 53  ? 21.083 2.066   8.834   0.74 15.68 ?  53  LEU   A HD21 1 
ATOM   1386 H  HD21 B LEU   A 1 53  ? 21.419 1.968   8.999   0.26 11.76 ?  53  LEU   A HD21 1 
ATOM   1387 H  HD22 A LEU   A 1 53  ? 22.322 2.846   9.450   0.74 15.68 ?  53  LEU   A HD22 1 
ATOM   1388 H  HD22 B LEU   A 1 53  ? 22.853 2.551   9.353   0.26 11.76 ?  53  LEU   A HD22 1 
ATOM   1389 H  HD23 A LEU   A 1 53  ? 20.978 3.624   9.118   0.74 15.68 ?  53  LEU   A HD23 1 
ATOM   1390 H  HD23 B LEU   A 1 53  ? 21.582 3.501   9.376   0.26 11.76 ?  53  LEU   A HD23 1 
ATOM   1391 N  N    A ASN   A 1 54  ? 23.883 7.370   6.865   0.74 9.33  ?  54  ASN   A N    1 
ATOM   1392 N  N    B ASN   A 1 54  ? 23.829 7.425   6.922   0.26 10.08 ?  54  ASN   A N    1 
ATOM   1393 C  CA   A ASN   A 1 54  ? 24.925 8.378   6.987   0.74 9.38  ?  54  ASN   A CA   1 
ATOM   1394 C  CA   B ASN   A 1 54  ? 24.889 8.413   7.084   0.26 10.11 ?  54  ASN   A CA   1 
ATOM   1395 C  C    A ASN   A 1 54  ? 24.409 9.630   7.696   0.74 10.03 ?  54  ASN   A C    1 
ATOM   1396 C  C    B ASN   A 1 54  ? 24.378 9.647   7.816   0.26 10.17 ?  54  ASN   A C    1 
ATOM   1397 O  O    A ASN   A 1 54  ? 25.108 10.204  8.539   0.74 10.49 ?  54  ASN   A O    1 
ATOM   1398 O  O    B ASN   A 1 54  ? 25.030 10.149  8.740   0.26 10.11 ?  54  ASN   A O    1 
ATOM   1399 C  CB   A ASN   A 1 54  ? 25.489 8.730   5.623   0.74 9.79  ?  54  ASN   A CB   1 
ATOM   1400 C  CB   B ASN   A 1 54  ? 25.475 8.792   5.728   0.26 10.00 ?  54  ASN   A CB   1 
ATOM   1401 C  CG   A ASN   A 1 54  ? 26.507 9.829   5.722   0.74 10.16 ?  54  ASN   A CG   1 
ATOM   1402 C  CG   B ASN   A 1 54  ? 26.485 9.917   5.839   0.26 9.82  ?  54  ASN   A CG   1 
ATOM   1403 O  OD1  A ASN   A 1 54  ? 27.497 9.699   6.459   0.74 10.30 ?  54  ASN   A OD1  1 
ATOM   1404 O  OD1  B ASN   A 1 54  ? 27.560 9.747   6.419   0.26 9.98  ?  54  ASN   A OD1  1 
ATOM   1405 N  ND2  A ASN   A 1 54  ? 26.268 10.935  5.027   0.74 10.49 ?  54  ASN   A ND2  1 
ATOM   1406 N  ND2  B ASN   A 1 54  ? 26.139 11.079  5.300   0.26 9.58  ?  54  ASN   A ND2  1 
ATOM   1407 H  H    A ASN   A 1 54  ? 23.672 7.145   6.062   0.74 11.33 ?  54  ASN   A H    1 
ATOM   1408 H  H    B ASN   A 1 54  ? 23.555 7.312   6.113   0.26 12.24 ?  54  ASN   A H    1 
ATOM   1409 H  HA   A ASN   A 1 54  ? 25.642 8.016   7.522   0.74 11.40 ?  54  ASN   A HA   1 
ATOM   1410 H  HA   B ASN   A 1 54  ? 25.598 8.025   7.615   0.26 12.28 ?  54  ASN   A HA   1 
ATOM   1411 H  HB2  A ASN   A 1 54  ? 25.924 7.941   5.250   0.74 11.89 ?  54  ASN   A HB2  1 
ATOM   1412 H  HB2  B ASN   A 1 54  ? 25.923 8.016   5.349   0.26 12.14 ?  54  ASN   A HB2  1 
ATOM   1413 H  HB3  A ASN   A 1 54  ? 24.774 9.022   5.042   0.74 11.89 ?  54  ASN   A HB3  1 
ATOM   1414 H  HB3  B ASN   A 1 54  ? 24.759 9.080   5.140   0.26 12.14 ?  54  ASN   A HB3  1 
ATOM   1415 H  HD21 A ASN   A 1 54  ? 26.820 11.587  5.060   0.74 12.72 ?  54  ASN   A HD21 1 
ATOM   1416 H  HD21 B ASN   A 1 54  ? 26.678 11.745  5.342   0.26 11.64 ?  54  ASN   A HD21 1 
ATOM   1417 H  HD22 A ASN   A 1 54  ? 25.560 10.986  4.540   0.74 12.72 ?  54  ASN   A HD22 1 
ATOM   1418 H  HD22 B ASN   A 1 54  ? 25.379 11.162  4.905   0.26 11.64 ?  54  ASN   A HD22 1 
ATOM   1419 N  N    A LYS   A 1 55  ? 23.187 10.066  7.369   0.74 10.29 ?  55  LYS   A N    1 
ATOM   1420 N  N    B LYS   A 1 55  ? 23.204 10.148  7.420   0.26 10.42 ?  55  LYS   A N    1 
ATOM   1421 C  CA   A LYS   A 1 55  ? 22.598 11.221  8.042   0.74 10.92 ?  55  LYS   A CA   1 
ATOM   1422 C  CA   B LYS   A 1 55  ? 22.628 11.300  8.103   0.26 11.19 ?  55  LYS   A CA   1 
ATOM   1423 C  C    A LYS   A 1 55  ? 22.529 11.001  9.547   0.74 11.07 ?  55  LYS   A C    1 
ATOM   1424 C  C    B LYS   A 1 55  ? 22.483 11.032  9.595   0.26 11.28 ?  55  LYS   A C    1 
ATOM   1425 O  O    A LYS   A 1 55  ? 22.831 11.907  10.333  0.74 11.81 ?  55  LYS   A O    1 
ATOM   1426 O  O    B LYS   A 1 55  ? 22.698 11.930  10.418  0.26 11.32 ?  55  LYS   A O    1 
ATOM   1427 C  CB   A LYS   A 1 55  ? 21.209 11.490  7.458   0.74 11.49 ?  55  LYS   A CB   1 
ATOM   1428 C  CB   B LYS   A 1 55  ? 21.281 11.661  7.473   0.26 12.05 ?  55  LYS   A CB   1 
ATOM   1429 C  CG   A LYS   A 1 55  ? 20.459 12.655  8.084   0.74 13.02 ?  55  LYS   A CG   1 
ATOM   1430 C  CG   B LYS   A 1 55  ? 20.579 12.842  8.130   0.26 13.12 ?  55  LYS   A CG   1 
ATOM   1431 C  CD   A LYS   A 1 55  ? 19.122 12.859  7.378   0.74 14.21 ?  55  LYS   A CD   1 
ATOM   1432 C  CD   B LYS   A 1 55  ? 19.267 13.169  7.429   0.26 14.05 ?  55  LYS   A CD   1 
ATOM   1433 C  CE   A LYS   A 1 55  ? 18.272 13.939  8.032   0.74 15.78 ?  55  LYS   A CE   1 
ATOM   1434 C  CE   B LYS   A 1 55  ? 18.502 14.272  8.152   0.26 15.28 ?  55  LYS   A CE   1 
ATOM   1435 N  NZ   A LYS   A 1 55  ? 16.949 14.069  7.361   0.74 16.21 ?  55  LYS   A NZ   1 
ATOM   1436 N  NZ   B LYS   A 1 55  ? 17.215 14.596  7.474   0.26 15.94 ?  55  LYS   A NZ   1 
ATOM   1437 H  H    A LYS   A 1 55  ? 22.675 9.705   6.773   0.74 12.49 ?  55  LYS   A H    1 
ATOM   1438 H  H    B LYS   A 1 55  ? 22.726 9.840   6.773   0.26 12.65 ?  55  LYS   A H    1 
ATOM   1439 H  HA   A LYS   A 1 55  ? 23.149 11.997  7.877   0.74 13.25 ?  55  LYS   A HA   1 
ATOM   1440 H  HA   B LYS   A 1 55  ? 23.219 12.059  7.993   0.26 13.57 ?  55  LYS   A HA   1 
ATOM   1441 H  HB2  A LYS   A 1 55  ? 21.301 11.681  6.513   0.74 13.93 ?  55  LYS   A HB2  1 
ATOM   1442 H  HB2  B LYS   A 1 55  ? 21.425 11.889  6.540   0.26 14.61 ?  55  LYS   A HB2  1 
ATOM   1443 H  HB3  A LYS   A 1 55  ? 20.660 10.698  7.578   0.74 13.93 ?  55  LYS   A HB3  1 
ATOM   1444 H  HB3  B LYS   A 1 55  ? 20.690 10.896  7.535   0.26 14.61 ?  55  LYS   A HB3  1 
ATOM   1445 H  HG2  A LYS   A 1 55  ? 20.283 12.467  9.020   0.74 15.76 ?  55  LYS   A HG2  1 
ATOM   1446 H  HG2  B LYS   A 1 55  ? 20.379 12.625  9.054   0.26 15.89 ?  55  LYS   A HG2  1 
ATOM   1447 H  HG3  A LYS   A 1 55  ? 20.981 13.466  7.991   0.74 15.76 ?  55  LYS   A HG3  1 
ATOM   1448 H  HG3  B LYS   A 1 55  ? 21.151 13.623  8.083   0.26 15.89 ?  55  LYS   A HG3  1 
ATOM   1449 H  HD2  A LYS   A 1 55  ? 19.286 13.118  6.458   0.74 17.19 ?  55  LYS   A HD2  1 
ATOM   1450 H  HD2  B LYS   A 1 55  ? 19.454 13.471  6.526   0.26 17.00 ?  55  LYS   A HD2  1 
ATOM   1451 H  HD3  A LYS   A 1 55  ? 18.621 12.026  7.402   0.74 17.19 ?  55  LYS   A HD3  1 
ATOM   1452 H  HD3  B LYS   A 1 55  ? 18.709 12.376  7.408   0.26 17.00 ?  55  LYS   A HD3  1 
ATOM   1453 H  HE2  A LYS   A 1 55  ? 18.124 13.709  8.963   0.74 19.07 ?  55  LYS   A HE2  1 
ATOM   1454 H  HE2  B LYS   A 1 55  ? 18.303 13.981  9.057   0.26 18.48 ?  55  LYS   A HE2  1 
ATOM   1455 H  HE3  A LYS   A 1 55  ? 18.735 14.790  7.968   0.74 19.07 ?  55  LYS   A HE3  1 
ATOM   1456 H  HE3  B LYS   A 1 55  ? 19.044 15.076  8.172   0.26 18.48 ?  55  LYS   A HE3  1 
ATOM   1457 H  HZ1  A LYS   A 1 55  ? 16.373 14.472  7.906   0.74 19.59 ?  55  LYS   A HZ1  1 
ATOM   1458 H  HZ1  B LYS   A 1 55  ? 16.781 15.226  7.929   0.26 19.27 ?  55  LYS   A HZ1  1 
ATOM   1459 H  HZ2  A LYS   A 1 55  ? 17.031 14.555  6.619   0.74 19.59 ?  55  LYS   A HZ2  1 
ATOM   1460 H  HZ2  B LYS   A 1 55  ? 17.371 14.891  6.649   0.26 19.27 ?  55  LYS   A HZ2  1 
ATOM   1461 H  HZ3  A LYS   A 1 55  ? 16.634 13.265  7.151   0.74 19.59 ?  55  LYS   A HZ3  1 
ATOM   1462 H  HZ3  B LYS   A 1 55  ? 16.703 13.869  7.429   0.26 19.27 ?  55  LYS   A HZ3  1 
ATOM   1463 N  N    . ALA   A 1 56  ? 22.128 9.799   9.967   1.00 11.52 ?  56  ALA   A N    1 
ATOM   1464 C  CA   . ALA   A 1 56  ? 22.005 9.476   11.382  1.00 12.35 ?  56  ALA   A CA   1 
ATOM   1465 C  C    . ALA   A 1 56  ? 23.348 9.504   12.107  1.00 12.28 ?  56  ALA   A C    1 
ATOM   1466 O  O    . ALA   A 1 56  ? 23.368 9.694   13.326  1.00 13.35 ?  56  ALA   A O    1 
ATOM   1467 C  CB   . ALA   A 1 56  ? 21.308 8.122   11.560  1.00 13.23 ?  56  ALA   A CB   1 
ATOM   1468 H  H    A ALA   A 1 56  ? 21.920 9.151   9.443   0.74 13.96 ?  56  ALA   A H    1 
ATOM   1469 H  H    B ALA   A 1 56  ? 21.955 9.150   9.431   0.26 13.96 ?  56  ALA   A H    1 
ATOM   1470 H  HA   . ALA   A 1 56  ? 21.449 10.139  11.805  1.00 14.96 ?  56  ALA   A HA   1 
ATOM   1471 H  HB1  . ALA   A 1 56  ? 21.238 7.922   12.509  1.00 16.01 ?  56  ALA   A HB1  1 
ATOM   1472 H  HB2  . ALA   A 1 56  ? 20.422 8.172   11.169  1.00 16.01 ?  56  ALA   A HB2  1 
ATOM   1473 H  HB3  . ALA   A 1 56  ? 21.827 7.433   11.117  1.00 16.01 ?  56  ALA   A HB3  1 
ATOM   1474 N  N    . THR   A 1 57  ? 24.462 9.319   11.390  1.00 11.22 ?  57  THR   A N    1 
ATOM   1475 C  CA   . THR   A 1 57  ? 25.805 9.447   11.964  1.00 11.43 ?  57  THR   A CA   1 
ATOM   1476 C  C    . THR   A 1 57  ? 26.357 10.866  11.885  1.00 11.70 ?  57  THR   A C    1 
ATOM   1477 O  O    . THR   A 1 57  ? 27.542 11.076  12.177  1.00 12.33 ?  57  THR   A O    1 
ATOM   1478 C  CB   . THR   A 1 57  ? 26.817 8.499   11.291  1.00 11.34 ?  57  THR   A CB   1 
ATOM   1479 O  OG1  . THR   A 1 57  ? 27.199 9.000   9.998   1.00 11.03 ?  57  THR   A OG1  1 
ATOM   1480 C  CG2  . THR   A 1 57  ? 26.289 7.075   11.184  1.00 11.20 ?  57  THR   A CG2  1 
ATOM   1481 H  H    . THR   A 1 57  ? 24.468 9.095   10.558  1.00 13.61 ?  57  THR   A H    1 
ATOM   1482 H  HA   . THR   A 1 57  ? 25.764 9.187   12.903  1.00 13.85 ?  57  THR   A HA   1 
ATOM   1483 H  HB   . THR   A 1 57  ? 27.617 8.460   11.847  1.00 13.74 ?  57  THR   A HB   1 
ATOM   1484 H  HG1  . THR   A 1 57  ? 26.520 9.072   9.509   1.00 13.37 ?  57  THR   A HG1  1 
ATOM   1485 H  HG21 . THR   A 1 57  ? 26.904 6.524   10.666  1.00 13.58 ?  57  THR   A HG21 1 
ATOM   1486 H  HG22 . THR   A 1 57  ? 26.192 6.682   12.066  1.00 13.58 ?  57  THR   A HG22 1 
ATOM   1487 H  HG23 . THR   A 1 57  ? 25.426 7.065   10.743  1.00 13.58 ?  57  THR   A HG23 1 
ATOM   1488 N  N    . ASN   A 1 58  ? 25.541 11.841  11.482  1.00 12.17 ?  58  ASN   A N    1 
ATOM   1489 C  CA   . ASN   A 1 58  ? 26.004 13.221  11.379  1.00 12.88 ?  58  ASN   A CA   1 
ATOM   1490 C  C    . ASN   A 1 58  ? 27.155 13.344  10.372  1.00 11.69 ?  58  ASN   A C    1 
ATOM   1491 O  O    . ASN   A 1 58  ? 28.049 14.178  10.528  1.00 12.48 ?  58  ASN   A O    1 
ATOM   1492 C  CB   . ASN   A 1 58  ? 26.372 13.768  12.771  1.00 15.53 ?  58  ASN   A CB   1 
ATOM   1493 C  CG   . ASN   A 1 58  ? 26.765 15.228  12.759  1.00 19.77 ?  58  ASN   A CG   1 
ATOM   1494 O  OD1  . ASN   A 1 58  ? 26.127 16.041  12.103  1.00 21.43 ?  58  ASN   A OD1  1 
ATOM   1495 N  ND2  . ASN   A 1 58  ? 27.821 15.573  13.500  1.00 21.22 ?  58  ASN   A ND2  1 
ATOM   1496 H  H    . ASN   A 1 58  ? 24.718 11.717  11.257  1.00 14.74 ?  58  ASN   A H    1 
ATOM   1497 H  HA   . ASN   A 1 58  ? 25.270 13.750  11.045  1.00 15.60 ?  58  ASN   A HA   1 
ATOM   1498 H  HB2  . ASN   A 1 58  ? 25.599 13.671  13.360  1.00 18.77 ?  58  ASN   A HB2  1 
ATOM   1499 H  HB3  . ASN   A 1 58  ? 27.117 13.269  13.128  1.00 18.77 ?  58  ASN   A HB3  1 
ATOM   1500 H  HD21 . ASN   A 1 58  ? 28.076 16.396  13.526  1.00 25.61 ?  58  ASN   A HD21 1 
ATOM   1501 H  HD22 . ASN   A 1 58  ? 28.236 14.977  13.950  1.00 25.61 ?  58  ASN   A HD22 1 
ATOM   1502 N  N    . ASN   A 1 59  ? 27.135 12.525  9.318   1.00 10.90 ?  59  ASN   A N    1 
ATOM   1503 C  CA   . ASN   A 1 59  ? 28.114 12.503  8.222   1.00 10.78 ?  59  ASN   A CA   1 
ATOM   1504 C  C    . ASN   A 1 59  ? 29.430 11.820  8.608   1.00 10.59 ?  59  ASN   A C    1 
ATOM   1505 O  O    . ASN   A 1 59  ? 30.349 11.778  7.781   1.00 10.76 ?  59  ASN   A O    1 
ATOM   1506 C  CB   . ASN   A 1 59  ? 28.407 13.889  7.616   1.00 10.97 ?  59  ASN   A CB   1 
ATOM   1507 C  CG   . ASN   A 1 59  ? 28.766 13.817  6.151   1.00 11.05 ?  59  ASN   A CG   1 
ATOM   1508 O  OD1  . ASN   A 1 59  ? 28.061 13.192  5.358   1.00 11.38 ?  59  ASN   A OD1  1 
ATOM   1509 N  ND2  . ASN   A 1 59  ? 29.852 14.481  5.772   1.00 11.78 ?  59  ASN   A ND2  1 
ATOM   1510 H  H    . ASN   A 1 59  ? 26.521 11.928  9.207   1.00 13.22 ?  59  ASN   A H    1 
ATOM   1511 H  HA   . ASN   A 1 59  ? 27.732 11.972  7.511   1.00 13.07 ?  59  ASN   A HA   1 
ATOM   1512 H  HB2  . ASN   A 1 59  ? 27.620 14.449  7.701   1.00 13.30 ?  59  ASN   A HB2  1 
ATOM   1513 H  HB3  . ASN   A 1 59  ? 29.154 14.293  8.084   1.00 13.30 ?  59  ASN   A HB3  1 
ATOM   1514 H  HD21 . ASN   A 1 59  ? 30.105 14.470  4.946   1.00 14.28 ?  59  ASN   A HD21 1 
ATOM   1515 H  HD22 . ASN   A 1 59  ? 30.327 14.908  6.352   1.00 14.28 ?  59  ASN   A HD22 1 
ATOM   1516 N  N    . ALA   A 1 60  ? 29.556 11.276  9.817   1.00 10.58 ?  60  ALA   A N    1 
ATOM   1517 C  CA   . ALA   A 1 60  ? 30.792 10.592  10.178  1.00 10.73 ?  60  ALA   A CA   1 
ATOM   1518 C  C    . ALA   A 1 60  ? 31.017 9.356   9.318   1.00 10.43 ?  60  ALA   A C    1 
ATOM   1519 O  O    . ALA   A 1 60  ? 32.164 9.035   8.983   1.00 10.99 ?  60  ALA   A O    1 
ATOM   1520 C  CB   . ALA   A 1 60  ? 30.783 10.233  11.661  1.00 11.69 ?  60  ALA   A CB   1 
ATOM   1521 H  H    . ALA   A 1 60  ? 28.958 11.283  10.430  1.00 12.84 ?  60  ALA   A H    1 
ATOM   1522 H  HA   . ALA   A 1 60  ? 31.538 11.195  10.023  1.00 13.02 ?  60  ALA   A HA   1 
ATOM   1523 H  HB1  . ALA   A 1 60  ? 31.610 9.782   11.881  1.00 14.16 ?  60  ALA   A HB1  1 
ATOM   1524 H  HB2  . ALA   A 1 60  ? 30.701 11.050  12.179  1.00 14.16 ?  60  ALA   A HB2  1 
ATOM   1525 H  HB3  . ALA   A 1 60  ? 30.027 9.652   11.837  1.00 14.16 ?  60  ALA   A HB3  1 
ATOM   1526 N  N    . MET   A 1 61  ? 29.943 8.661   8.935   1.00 10.11 ?  61  MET   A N    1 
ATOM   1527 C  CA   . MET   A 1 61  ? 30.082 7.526   8.028   1.00 10.13 ?  61  MET   A CA   1 
ATOM   1528 C  C    . MET   A 1 61  ? 30.717 7.950   6.706   1.00 10.09 ?  61  MET   A C    1 
ATOM   1529 O  O    . MET   A 1 61  ? 31.611 7.266   6.192   1.00 10.38 ?  61  MET   A O    1 
ATOM   1530 C  CB   . MET   A 1 61  ? 28.719 6.861   7.812   1.00 10.14 ?  61  MET   A CB   1 
ATOM   1531 C  CG   . MET   A 1 61  ? 28.731 5.692   6.840   1.00 10.62 ?  61  MET   A CG   1 
ATOM   1532 S  SD   . MET   A 1 61  ? 27.112 4.944   6.640   1.00 11.63 ?  61  MET   A SD   1 
ATOM   1533 C  CE   . MET   A 1 61  ? 26.981 4.062   8.199   1.00 13.12 ?  61  MET   A CE   1 
ATOM   1534 H  H    . MET   A 1 61  ? 29.137 8.830   9.176   1.00 12.27 ?  61  MET   A H    1 
ATOM   1535 H  HA   . MET   A 1 61  ? 30.660 6.871   8.447   1.00 12.29 ?  61  MET   A HA   1 
ATOM   1536 H  HB2  . MET   A 1 61  ? 28.401 6.532   8.664   1.00 12.30 ?  61  MET   A HB2  1 
ATOM   1537 H  HB3  . MET   A 1 61  ? 28.105 7.523   7.464   1.00 12.30 ?  61  MET   A HB3  1 
ATOM   1538 H  HG2  . MET   A 1 61  ? 29.020 5.995   5.968   1.00 12.88 ?  61  MET   A HG2  1 
ATOM   1539 H  HG3  . MET   A 1 61  ? 29.333 5.005   7.172   1.00 12.88 ?  61  MET   A HG3  1 
ATOM   1540 H  HE1  . MET   A 1 61  ? 26.141 3.577   8.221   1.00 15.89 ?  61  MET   A HE1  1 
ATOM   1541 H  HE2  . MET   A 1 61  ? 27.723 3.444   8.276   1.00 15.89 ?  61  MET   A HE2  1 
ATOM   1542 H  HE3  . MET   A 1 61  ? 27.008 4.702   8.932   1.00 15.89 ?  61  MET   A HE3  1 
ATOM   1543 N  N    . GLN   A 1 62  ? 30.273 9.079   6.146   1.00 10.11 ?  62  GLN   A N    1 
ATOM   1544 C  CA   . GLN   A 1 62  ? 30.834 9.550   4.884   1.00 10.14 ?  62  GLN   A CA   1 
ATOM   1545 C  C    . GLN   A 1 62  ? 32.303 9.929   5.032   1.00 10.24 ?  62  GLN   A C    1 
ATOM   1546 O  O    . GLN   A 1 62  ? 33.117 9.613   4.159   1.00 10.60 ?  62  GLN   A O    1 
ATOM   1547 C  CB   . GLN   A 1 62  ? 30.031 10.736  4.354   1.00 10.21 ?  62  GLN   A CB   1 
ATOM   1548 C  CG   . GLN   A 1 62  ? 30.407 11.098  2.929   1.00 10.39 ?  62  GLN   A CG   1 
ATOM   1549 C  CD   . GLN   A 1 62  ? 30.083 9.968   1.982   1.00 10.50 ?  62  GLN   A CD   1 
ATOM   1550 O  OE1  . GLN   A 1 62  ? 28.902 9.660   1.771   1.00 11.15 ?  62  GLN   A OE1  1 
ATOM   1551 N  NE2  . GLN   A 1 62  ? 31.103 9.298   1.461   1.00 11.21 ?  62  GLN   A NE2  1 
ATOM   1552 H  H    . GLN   A 1 62  ? 29.650 9.571   6.471   1.00 12.28 ?  62  GLN   A H    1 
ATOM   1553 H  HA   . GLN   A 1 62  ? 30.781 8.831   4.235   1.00 12.31 ?  62  GLN   A HA   1 
ATOM   1554 H  HB2  . GLN   A 1 62  ? 29.088 10.515  4.373   1.00 12.39 ?  62  GLN   A HB2  1 
ATOM   1555 H  HB3  . GLN   A 1 62  ? 30.203 11.510  4.917   1.00 12.39 ?  62  GLN   A HB3  1 
ATOM   1556 H  HG2  . GLN   A 1 62  ? 29.899 11.876  2.653   1.00 12.60 ?  62  GLN   A HG2  1 
ATOM   1557 H  HG3  . GLN   A 1 62  ? 31.357 11.278  2.878   1.00 12.60 ?  62  GLN   A HG3  1 
ATOM   1558 H  HE21 . GLN   A 1 62  ? 31.909 9.531   1.649   1.00 13.59 ?  62  GLN   A HE21 1 
ATOM   1559 H  HE22 . GLN   A 1 62  ? 30.957 8.641   0.928   1.00 13.59 ?  62  GLN   A HE22 1 
ATOM   1560 N  N    . VAL   A 1 63  ? 32.661 10.615  6.119   1.00 10.67 ?  63  VAL   A N    1 
ATOM   1561 C  CA   . VAL   A 1 63  ? 34.056 11.009  6.332   1.00 11.40 ?  63  VAL   A CA   1 
ATOM   1562 C  C    . VAL   A 1 63  ? 34.955 9.776   6.397   1.00 10.70 ?  63  VAL   A C    1 
ATOM   1563 O  O    . VAL   A 1 63  ? 36.009 9.709   5.746   1.00 11.40 ?  63  VAL   A O    1 
ATOM   1564 C  CB   . VAL   A 1 63  ? 34.168 11.890  7.591   1.00 12.96 ?  63  VAL   A CB   1 
ATOM   1565 C  CG1  . VAL   A 1 63  ? 35.613 12.135  7.952   1.00 14.47 ?  63  VAL   A CG1  1 
ATOM   1566 C  CG2  . VAL   A 1 63  ? 33.444 13.218  7.370   1.00 13.21 ?  63  VAL   A CG2  1 
ATOM   1567 H  H    . VAL   A 1 63  ? 32.117 10.864  6.743   1.00 12.94 ?  63  VAL   A H    1 
ATOM   1568 H  HA   . VAL   A 1 63  ? 34.338 11.542  5.577   1.00 13.82 ?  63  VAL   A HA   1 
ATOM   1569 H  HB   . VAL   A 1 63  ? 33.745 11.438  8.338   1.00 15.69 ?  63  VAL   A HB   1 
ATOM   1570 H  HG11 . VAL   A 1 63  ? 35.656 12.868  8.584   1.00 17.50 ?  63  VAL   A HG11 1 
ATOM   1571 H  HG12 . VAL   A 1 63  ? 35.980 11.331  8.348   1.00 17.50 ?  63  VAL   A HG12 1 
ATOM   1572 H  HG13 . VAL   A 1 63  ? 36.100 12.365  7.145   1.00 17.50 ?  63  VAL   A HG13 1 
ATOM   1573 H  HG21 . VAL   A 1 63  ? 33.535 13.765  8.167   1.00 15.99 ?  63  VAL   A HG21 1 
ATOM   1574 H  HG22 . VAL   A 1 63  ? 33.845 13.674  6.612   1.00 15.99 ?  63  VAL   A HG22 1 
ATOM   1575 H  HG23 . VAL   A 1 63  ? 32.508 13.044  7.193   1.00 15.99 ?  63  VAL   A HG23 1 
ATOM   1576 N  N    . GLU   A 1 64  ? 34.535 8.769   7.168   1.00 10.80 ?  64  GLU   A N    1 
ATOM   1577 C  CA   . GLU   A 1 64  ? 35.299 7.531   7.266   1.00 10.99 ?  64  GLU   A CA   1 
ATOM   1578 C  C    . GLU   A 1 64  ? 35.390 6.839   5.913   1.00 10.51 ?  64  GLU   A C    1 
ATOM   1579 O  O    . GLU   A 1 64  ? 36.439 6.293   5.542   1.00 11.13 ?  64  GLU   A O    1 
ATOM   1580 C  CB   . GLU   A 1 64  ? 34.612 6.619   8.285   1.00 11.49 ?  64  GLU   A CB   1 
ATOM   1581 C  CG   . GLU   A 1 64  ? 35.257 5.265   8.435   1.00 11.83 ?  64  GLU   A CG   1 
ATOM   1582 C  CD   . GLU   A 1 64  ? 34.375 4.270   9.168   1.00 12.58 ?  64  GLU   A CD   1 
ATOM   1583 O  OE1  . GLU   A 1 64  ? 33.138 4.360   9.032   1.00 13.38 ?  64  GLU   A OE1  1 
ATOM   1584 O  OE2  . GLU   A 1 64  ? 34.932 3.380   9.855   1.00 12.88 -1 64  GLU   A OE2  1 
ATOM   1585 H  H    . GLU   A 1 64  ? 33.806 8.773   7.628   1.00 13.10 ?  64  GLU   A H    1 
ATOM   1586 H  HA   . GLU   A 1 64  ? 36.197 7.734   7.580   1.00 13.33 ?  64  GLU   A HA   1 
ATOM   1587 H  HB2  . GLU   A 1 64  ? 34.639 7.059   9.157   1.00 13.93 ?  64  GLU   A HB2  1 
ATOM   1588 H  HB3  . GLU   A 1 64  ? 33.693 6.494   8.014   1.00 13.93 ?  64  GLU   A HB3  1 
ATOM   1589 H  HG2  . GLU   A 1 64  ? 35.449 4.896   7.555   1.00 14.34 ?  64  GLU   A HG2  1 
ATOM   1590 H  HG3  . GLU   A 1 64  ? 36.083 5.361   8.933   1.00 14.34 ?  64  GLU   A HG3  1 
ATOM   1591 N  N    . SER   A 1 65  ? 34.274 6.825   5.179   1.00 10.31 ?  65  SER   A N    1 
ATOM   1592 C  CA   . SER   A 1 65  ? 34.220 6.167   3.879   1.00 10.20 ?  65  SER   A CA   1 
ATOM   1593 C  C    . SER   A 1 65  ? 35.141 6.836   2.867   1.00 10.56 ?  65  SER   A C    1 
ATOM   1594 O  O    . SER   A 1 65  ? 35.778 6.157   2.053   1.00 11.11 ?  65  SER   A O    1 
ATOM   1595 C  CB   . SER   A 1 65  ? 32.788 6.172   3.347   1.00 10.41 ?  65  SER   A CB   1 
ATOM   1596 O  OG   . SER   A 1 65  ? 31.937 5.360   4.146   1.00 10.78 ?  65  SER   A OG   1 
ATOM   1597 H  H    . SER   A 1 65  ? 33.537 7.195   5.415   1.00 12.51 ?  65  SER   A H    1 
ATOM   1598 H  HA   . SER   A 1 65  ? 34.506 5.248   3.974   1.00 12.39 ?  65  SER   A HA   1 
ATOM   1599 H  HB2  . SER   A 1 65  ? 32.451 7.078   3.353   1.00 12.64 ?  65  SER   A HB2  1 
ATOM   1600 H  HB3  . SER   A 1 65  ? 32.792 5.824   2.442   1.00 12.64 ?  65  SER   A HB3  1 
ATOM   1601 H  HG   . SER   A 1 65  ? 31.932 5.649   4.940   1.00 13.07 ?  65  SER   A HG   1 
ATOM   1602 N  N    . ASP   A 1 66  ? 35.217 8.170   2.887   1.00 10.59 ?  66  ASP   A N    1 
ATOM   1603 C  CA   . ASP   A 1 66  ? 36.077 8.867   1.936   1.00 11.64 ?  66  ASP   A CA   1 
ATOM   1604 C  C    . ASP   A 1 66  ? 37.541 8.514   2.171   1.00 11.52 ?  66  ASP   A C    1 
ATOM   1605 O  O    . ASP   A 1 66  ? 38.311 8.342   1.219   1.00 12.34 ?  66  ASP   A O    1 
ATOM   1606 C  CB   . ASP   A 1 66  ? 35.856 10.374  2.046   1.00 12.84 ?  66  ASP   A CB   1 
ATOM   1607 C  CG   . ASP   A 1 66  ? 34.524 10.837  1.443   1.00 14.50 ?  66  ASP   A CG   1 
ATOM   1608 O  OD1  . ASP   A 1 66  ? 33.809 10.040  0.790   1.00 14.60 ?  66  ASP   A OD1  1 
ATOM   1609 O  OD2  . ASP   A 1 66  ? 34.217 12.036  1.611   1.00 17.52 -1 66  ASP   A OD2  1 
ATOM   1610 H  H    . ASP   A 1 66  ? 34.782 8.684   3.427   1.00 12.85 ?  66  ASP   A H    1 
ATOM   1611 H  HA   . ASP   A 1 66  ? 35.836 8.595   1.037   1.00 14.11 ?  66  ASP   A HA   1 
ATOM   1612 H  HB2  . ASP   A 1 66  ? 35.856 10.625  2.983   1.00 15.55 ?  66  ASP   A HB2  1 
ATOM   1613 H  HB3  . ASP   A 1 66  ? 36.576 10.830  1.581   1.00 15.55 ?  66  ASP   A HB3  1 
ATOM   1614 N  N    . ASP   A 1 67  ? 37.941 8.386   3.436   1.00 11.58 ?  67  ASP   A N    1 
ATOM   1615 C  CA   . ASP   A 1 67  ? 39.297 7.940   3.733   1.00 12.25 ?  67  ASP   A CA   1 
ATOM   1616 C  C    . ASP   A 1 67  ? 39.517 6.503   3.271   1.00 12.08 ?  67  ASP   A C    1 
ATOM   1617 O  O    . ASP   A 1 67  ? 40.578 6.175   2.726   1.00 12.93 ?  67  ASP   A O    1 
ATOM   1618 C  CB   . ASP   A 1 67  ? 39.565 8.073   5.228   1.00 13.44 ?  67  ASP   A CB   1 
ATOM   1619 C  CG   . ASP   A 1 67  ? 40.859 7.412   5.648   1.00 14.59 ?  67  ASP   A CG   1 
ATOM   1620 O  OD1  . ASP   A 1 67  ? 41.935 8.045   5.510   1.00 17.14 ?  67  ASP   A OD1  1 
ATOM   1621 O  OD2  . ASP   A 1 67  ? 40.806 6.250   6.114   1.00 14.61 -1 67  ASP   A OD2  1 
ATOM   1622 H  H    . ASP   A 1 67  ? 37.456 8.545   4.124   1.00 14.04 ?  67  ASP   A H    1 
ATOM   1623 H  HA   . ASP   A 1 67  ? 39.926 8.505   3.255   1.00 14.84 ?  67  ASP   A HA   1 
ATOM   1624 H  HB2  . ASP   A 1 67  ? 39.622 9.009   5.451   1.00 16.27 ?  67  ASP   A HB2  1 
ATOM   1625 H  HB3  . ASP   A 1 67  ? 38.844 7.648   5.713   1.00 16.27 ?  67  ASP   A HB3  1 
ATOM   1626 N  N    . TYR   A 1 68  ? 38.522 5.629   3.468   1.00 11.67 ?  68  TYR   A N    1 
ATOM   1627 C  CA   . TYR   A 1 68  ? 38.640 4.248   2.996   1.00 11.88 ?  68  TYR   A CA   1 
ATOM   1628 C  C    . TYR   A 1 68  ? 38.877 4.196   1.488   1.00 11.61 ?  68  TYR   A C    1 
ATOM   1629 O  O    . TYR   A 1 68  ? 39.754 3.464   1.010   1.00 12.18 ?  68  TYR   A O    1 
ATOM   1630 C  CB   . TYR   A 1 68  ? 37.390 3.426   3.373   1.00 12.08 ?  68  TYR   A CB   1 
ATOM   1631 C  CG   . TYR   A 1 68  ? 37.416 2.034   2.747   1.00 13.61 ?  68  TYR   A CG   1 
ATOM   1632 C  CD1  . TYR   A 1 68  ? 36.958 1.836   1.444   1.00 15.26 ?  68  TYR   A CD1  1 
ATOM   1633 C  CD2  . TYR   A 1 68  ? 37.947 0.949   3.422   1.00 15.13 ?  68  TYR   A CD2  1 
ATOM   1634 C  CE1  . TYR   A 1 68  ? 37.026 0.617   0.834   1.00 16.76 ?  68  TYR   A CE1  1 
ATOM   1635 C  CE2  . TYR   A 1 68  ? 38.008 -0.314  2.811   1.00 16.14 ?  68  TYR   A CE2  1 
ATOM   1636 C  CZ   . TYR   A 1 68  ? 37.553 -0.451  1.518   1.00 16.99 ?  68  TYR   A CZ   1 
ATOM   1637 O  OH   . TYR   A 1 68  ? 37.629 -1.665  0.895   1.00 18.19 ?  68  TYR   A OH   1 
ATOM   1638 H  H    . TYR   A 1 68  ? 37.781 5.807   3.869   1.00 14.14 ?  68  TYR   A H    1 
ATOM   1639 H  HA   . TYR   A 1 68  ? 39.402 3.835   3.431   1.00 14.39 ?  68  TYR   A HA   1 
ATOM   1640 H  HB2  . TYR   A 1 68  ? 37.353 3.322   4.336   1.00 14.64 ?  68  TYR   A HB2  1 
ATOM   1641 H  HB3  . TYR   A 1 68  ? 36.597 3.887   3.055   1.00 14.64 ?  68  TYR   A HB3  1 
ATOM   1642 H  HD1  . TYR   A 1 68  ? 36.614 2.563   0.971   1.00 18.45 ?  68  TYR   A HD1  1 
ATOM   1643 H  HD2  . TYR   A 1 68  ? 38.274 1.058   4.282   1.00 18.29 ?  68  TYR   A HD2  1 
ATOM   1644 H  HE1  . TYR   A 1 68  ? 36.706 0.511   -0.035  1.00 20.26 ?  68  TYR   A HE1  1 
ATOM   1645 H  HE2  . TYR   A 1 68  ? 38.369 -1.043  3.256   1.00 19.51 ?  68  TYR   A HE2  1 
ATOM   1646 H  HH   . TYR   A 1 68  ? 37.955 -2.238  1.420   1.00 21.97 ?  68  TYR   A HH   1 
ATOM   1647 N  N    . ILE   A 1 69  ? 38.085 4.950   0.717   1.00 11.29 ?  69  ILE   A N    1 
ATOM   1648 C  CA   . ILE   A 1 69  ? 38.227 4.942   -0.739  1.00 11.45 ?  69  ILE   A CA   1 
ATOM   1649 C  C    . ILE   A 1 69  ? 39.562 5.550   -1.165  1.00 11.24 ?  69  ILE   A C    1 
ATOM   1650 O  O    . ILE   A 1 69  ? 40.208 5.065   -2.102  1.00 11.81 ?  69  ILE   A O    1 
ATOM   1651 C  CB   . ILE   A 1 69  ? 37.035 5.652   -1.411  1.00 12.37 ?  69  ILE   A CB   1 
ATOM   1652 C  CG1  . ILE   A 1 69  ? 35.718 4.925   -1.134  1.00 12.90 ?  69  ILE   A CG1  1 
ATOM   1653 C  CG2  . ILE   A 1 69  ? 37.271 5.826   -2.918  1.00 13.91 ?  69  ILE   A CG2  1 
ATOM   1654 C  CD1  . ILE   A 1 69  ? 35.556 3.633   -1.900  1.00 13.56 ?  69  ILE   A CD1  1 
ATOM   1655 H  H    . ILE   A 1 69  ? 37.475 5.475   1.013   1.00 13.69 ?  69  ILE   A H    1 
ATOM   1656 H  HA   . ILE   A 1 69  ? 38.224 4.022   -1.038  1.00 13.88 ?  69  ILE   A HA   1 
ATOM   1657 H  HB   . ILE   A 1 69  ? 36.966 6.535   -1.023  1.00 14.98 ?  69  ILE   A HB   1 
ATOM   1658 H  HG12 . ILE   A 1 69  ? 35.671 4.718   -0.186  1.00 15.62 ?  69  ILE   A HG12 1 
ATOM   1659 H  HG13 . ILE   A 1 69  ? 34.984 5.511   -1.376  1.00 15.62 ?  69  ILE   A HG13 1 
ATOM   1660 H  HG21 . ILE   A 1 69  ? 36.426 6.044   -3.348  1.00 16.83 ?  69  ILE   A HG21 1 
ATOM   1661 H  HG22 . ILE   A 1 69  ? 37.902 6.555   -3.061  1.00 16.83 ?  69  ILE   A HG22 1 
ATOM   1662 H  HG23 . ILE   A 1 69  ? 37.626 5.005   -3.287  1.00 16.83 ?  69  ILE   A HG23 1 
ATOM   1663 H  HD11 . ILE   A 1 69  ? 34.766 3.177   -1.574  1.00 16.42 ?  69  ILE   A HD11 1 
ATOM   1664 H  HD12 . ILE   A 1 69  ? 35.454 3.838   -2.842  1.00 16.42 ?  69  ILE   A HD12 1 
ATOM   1665 H  HD13 . ILE   A 1 69  ? 36.339 3.083   -1.760  1.00 16.42 ?  69  ILE   A HD13 1 
ATOM   1666 N  N    . ALA   A 1 70  ? 39.980 6.632   -0.512  1.00 11.68 ?  70  ALA   A N    1 
ATOM   1667 C  CA   . ALA   A 1 70  ? 41.258 7.239   -0.868  1.00 12.67 ?  70  ALA   A CA   1 
ATOM   1668 C  C    . ALA   A 1 70  ? 42.407 6.253   -0.695  1.00 12.97 ?  70  ALA   A C    1 
ATOM   1669 O  O    . ALA   A 1 70  ? 43.374 6.285   -1.459  1.00 14.84 ?  70  ALA   A O    1 
ATOM   1670 C  CB   . ALA   A 1 70  ? 41.497 8.495   -0.031  1.00 13.28 ?  70  ALA   A CB   1 
ATOM   1671 H  H    . ALA   A 1 70  ? 39.554 7.028   0.116   1.00 14.16 ?  70  ALA   A H    1 
ATOM   1672 H  HA   . ALA   A 1 70  ? 41.231 7.511   -1.801  1.00 15.35 ?  70  ALA   A HA   1 
ATOM   1673 H  HB1  . ALA   A 1 70  ? 42.355 8.883   -0.281  1.00 16.07 ?  70  ALA   A HB1  1 
ATOM   1674 H  HB2  . ALA   A 1 70  ? 40.789 9.132   -0.197  1.00 16.07 ?  70  ALA   A HB2  1 
ATOM   1675 H  HB3  . ALA   A 1 70  ? 41.513 8.251   0.908   1.00 16.07 ?  70  ALA   A HB3  1 
ATOM   1676 N  N    . THR   A 1 71  ? 42.306 5.358   0.283   1.00 12.50 ?  71  THR   A N    1 
ATOM   1677 C  CA   . THR   A 1 71  ? 43.358 4.380   0.533   1.00 14.06 ?  71  THR   A CA   1 
ATOM   1678 C  C    . THR   A 1 71  ? 43.241 3.156   -0.366  1.00 14.05 ?  71  THR   A C    1 
ATOM   1679 O  O    . THR   A 1 71  ? 44.256 2.649   -0.865  1.00 16.02 ?  71  THR   A O    1 
ATOM   1680 C  CB   . THR   A 1 71  ? 43.285 3.930   1.987   1.00 16.13 ?  71  THR   A CB   1 
ATOM   1681 O  OG1  . THR   A 1 71  ? 43.544 5.052   2.834   1.00 17.39 ?  71  THR   A OG1  1 
ATOM   1682 C  CG2  . THR   A 1 71  ? 44.283 2.810   2.273   1.00 17.63 ?  71  THR   A CG2  1 
ATOM   1683 H  H    . THR   A 1 71  ? 41.629 5.286   0.806   1.00 15.15 ?  71  THR   A H    1 
ATOM   1684 H  HA   . THR   A 1 71  ? 44.222 4.788   0.376   1.00 17.02 ?  71  THR   A HA   1 
ATOM   1685 H  HB   . THR   A 1 71  ? 42.393 3.585   2.165   1.00 19.50 ?  71  THR   A HB   1 
ATOM   1686 H  HG1  . THR   A 1 71  ? 42.961 5.643   2.704   1.00 21.00 ?  71  THR   A HG1  1 
ATOM   1687 H  HG21 . THR   A 1 71  ? 44.429 2.735   3.230   1.00 21.29 ?  71  THR   A HG21 1 
ATOM   1688 H  HG22 . THR   A 1 71  ? 43.951 1.963   1.939   1.00 21.29 ?  71  THR   A HG22 1 
ATOM   1689 H  HG23 . THR   A 1 71  ? 45.134 3.007   1.844   1.00 21.29 ?  71  THR   A HG23 1 
ATOM   1690 N  N    . ASN   A 1 72  ? 42.018 2.647   -0.557  1.00 13.15 ?  72  ASN   A N    1 
ATOM   1691 C  CA   . ASN   A 1 72  ? 41.804 1.322   -1.122  1.00 13.54 ?  72  ASN   A CA   1 
ATOM   1692 C  C    . ASN   A 1 72  ? 41.179 1.313   -2.504  1.00 13.64 ?  72  ASN   A C    1 
ATOM   1693 O  O    . ASN   A 1 72  ? 41.181 0.256   -3.150  1.00 14.86 ?  72  ASN   A O    1 
ATOM   1694 C  CB   . ASN   A 1 72  ? 40.914 0.495   -0.185  1.00 13.99 ?  72  ASN   A CB   1 
ATOM   1695 C  CG   . ASN   A 1 72  ? 41.518 0.351   1.186   1.00 15.04 ?  72  ASN   A CG   1 
ATOM   1696 O  OD1  . ASN   A 1 72  ? 41.060 0.953   2.154   1.00 16.75 ?  72  ASN   A OD1  1 
ATOM   1697 N  ND2  . ASN   A 1 72  ? 42.574 -0.430  1.273   1.00 15.71 ?  72  ASN   A ND2  1 
ATOM   1698 H  H    . ASN   A 1 72  ? 41.286 3.062   -0.366  1.00 15.92 ?  72  ASN   A H    1 
ATOM   1699 H  HA   . ASN   A 1 72  ? 42.660 0.874   -1.194  1.00 16.39 ?  72  ASN   A HA   1 
ATOM   1700 H  HB2  . ASN   A 1 72  ? 40.054 0.927   -0.099  1.00 16.93 ?  72  ASN   A HB2  1 
ATOM   1701 H  HB3  . ASN   A 1 72  ? 40.804 -0.396  -0.565  1.00 16.93 ?  72  ASN   A HB3  1 
ATOM   1702 H  HD21 . ASN   A 1 72  ? 42.962 -0.540  2.034   1.00 18.99 ?  72  ASN   A HD21 1 
ATOM   1703 H  HD22 . ASN   A 1 72  ? 42.882 -0.826  0.575   1.00 18.99 ?  72  ASN   A HD22 1 
ATOM   1704 N  N    . GLY   A 1 73  ? 40.625 2.427   -2.963  1.00 12.98 ?  73  GLY   A N    1 
ATOM   1705 C  CA   . GLY   A 1 73  ? 39.888 2.438   -4.199  1.00 12.75 ?  73  GLY   A CA   1 
ATOM   1706 C  C    . GLY   A 1 73  ? 38.496 1.860   -4.028  1.00 12.37 ?  73  GLY   A C    1 
ATOM   1707 O  O    . GLY   A 1 73  ? 38.110 1.405   -2.944  1.00 12.96 ?  73  GLY   A O    1 
ATOM   1708 H  H    . GLY   A 1 73  ? 40.672 3.199   -2.576  1.00 15.71 ?  73  GLY   A H    1 
ATOM   1709 H  HA2  . GLY   A 1 73  ? 39.811 3.353   -4.521  1.00 15.44 ?  73  GLY   A HA2  1 
ATOM   1710 H  HA3  . GLY   A 1 73  ? 40.363 1.918   -4.866  1.00 15.44 ?  73  GLY   A HA3  1 
ATOM   1711 N  N    . PRO   A 1 74  ? 37.718 1.875   -5.110  1.00 12.78 ?  74  PRO   A N    1 
ATOM   1712 C  CA   . PRO   A 1 74  ? 36.322 1.440   -5.030  1.00 12.88 ?  74  PRO   A CA   1 
ATOM   1713 C  C    . PRO   A 1 74  ? 36.178 -0.041  -4.711  1.00 12.20 ?  74  PRO   A C    1 
ATOM   1714 O  O    . PRO   A 1 74  ? 37.045 -0.869  -4.997  1.00 13.07 ?  74  PRO   A O    1 
ATOM   1715 C  CB   . PRO   A 1 74  ? 35.773 1.743   -6.430  1.00 14.55 ?  74  PRO   A CB   1 
ATOM   1716 C  CG   . PRO   A 1 74  ? 36.730 2.714   -7.038  1.00 17.16 ?  74  PRO   A CG   1 
ATOM   1717 C  CD   . PRO   A 1 74  ? 38.065 2.380   -6.449  1.00 14.79 ?  74  PRO   A CD   1 
ATOM   1718 H  HA   . PRO   A 1 74  ? 35.838 1.963   -4.371  1.00 15.60 ?  74  PRO   A HA   1 
ATOM   1719 H  HB2  . PRO   A 1 74  ? 35.735 0.926   -6.951  1.00 17.60 ?  74  PRO   A HB2  1 
ATOM   1720 H  HB3  . PRO   A 1 74  ? 34.888 2.140   -6.355  1.00 17.60 ?  74  PRO   A HB3  1 
ATOM   1721 H  HG2  . PRO   A 1 74  ? 36.744 2.599   -8.001  1.00 20.73 ?  74  PRO   A HG2  1 
ATOM   1722 H  HG3  . PRO   A 1 74  ? 36.472 3.617   -6.805  1.00 20.73 ?  74  PRO   A HG3  1 
ATOM   1723 H  HD2  . PRO   A 1 74  ? 38.508 1.688   -6.971  1.00 17.89 ?  74  PRO   A HD2  1 
ATOM   1724 H  HD3  . PRO   A 1 74  ? 38.615 3.180   -6.390  1.00 17.89 ?  74  PRO   A HD3  1 
ATOM   1725 N  N    . LEU   A 1 75  ? 35.034 -0.368  -4.124  1.00 11.33 ?  75  LEU   A N    1 
ATOM   1726 C  CA   . LEU   A 1 75  ? 34.633 -1.757  -3.976  1.00 10.95 ?  75  LEU   A CA   1 
ATOM   1727 C  C    . LEU   A 1 75  ? 34.249 -2.337  -5.334  1.00 11.62 ?  75  LEU   A C    1 
ATOM   1728 O  O    . LEU   A 1 75  ? 34.128 -1.625  -6.335  1.00 13.06 ?  75  LEU   A O    1 
ATOM   1729 C  CB   . LEU   A 1 75  ? 33.447 -1.875  -3.020  1.00 11.43 ?  75  LEU   A CB   1 
ATOM   1730 C  CG   . LEU   A 1 75  ? 33.661 -1.467  -1.565  1.00 13.14 ?  75  LEU   A CG   1 
ATOM   1731 C  CD1  . LEU   A 1 75  ? 32.383 -1.680  -0.771  1.00 14.98 ?  75  LEU   A CD1  1 
ATOM   1732 C  CD2  . LEU   A 1 75  ? 34.816 -2.174  -0.905  1.00 16.31 ?  75  LEU   A CD2  1 
ATOM   1733 H  H    . LEU   A 1 75  ? 34.479 0.200   -3.794  1.00 13.74 ?  75  LEU   A H    1 
ATOM   1734 H  HA   . LEU   A 1 75  ? 35.373 -2.271  -3.622  1.00 13.28 ?  75  LEU   A HA   1 
ATOM   1735 H  HB2  . LEU   A 1 75  ? 32.728 -1.327  -3.365  1.00 13.86 ?  75  LEU   A HB2  1 
ATOM   1736 H  HB3  . LEU   A 1 75  ? 33.164 -2.805  -3.015  1.00 13.86 ?  75  LEU   A HB3  1 
ATOM   1737 H  HG   . LEU   A 1 75  ? 33.867 -0.519  -1.546  1.00 15.91 ?  75  LEU   A HG   1 
ATOM   1738 H  HD11 . LEU   A 1 75  ? 32.541 -1.413  0.148   1.00 18.11 ?  75  LEU   A HD11 1 
ATOM   1739 H  HD12 . LEU   A 1 75  ? 31.685 -1.135  -1.162  1.00 18.11 ?  75  LEU   A HD12 1 
ATOM   1740 H  HD13 . LEU   A 1 75  ? 32.144 -2.616  -0.811  1.00 18.11 ?  75  LEU   A HD13 1 
ATOM   1741 H  HD21 . LEU   A 1 75  ? 34.873 -1.895  0.024   1.00 19.72 ?  75  LEU   A HD21 1 
ATOM   1742 H  HD22 . LEU   A 1 75  ? 34.679 -3.132  -0.955  1.00 19.72 ?  75  LEU   A HD22 1 
ATOM   1743 H  HD23 . LEU   A 1 75  ? 35.645 -1.938  -1.364  1.00 19.72 ?  75  LEU   A HD23 1 
ATOM   1744 N  N    . LYS   A 1 76  ? 34.069 -3.656  -5.353  1.00 11.98 ?  76  LYS   A N    1 
ATOM   1745 C  CA   . LYS   A 1 76  ? 33.467 -4.368  -6.472  1.00 12.53 ?  76  LYS   A CA   1 
ATOM   1746 C  C    . LYS   A 1 76  ? 31.956 -4.451  -6.273  1.00 11.19 ?  76  LYS   A C    1 
ATOM   1747 O  O    . LYS   A 1 76  ? 31.476 -4.571  -5.149  1.00 11.37 ?  76  LYS   A O    1 
ATOM   1748 C  CB   . LYS   A 1 76  ? 34.011 -5.806  -6.533  1.00 14.42 ?  76  LYS   A CB   1 
ATOM   1749 C  CG   . LYS   A 1 76  ? 35.525 -5.914  -6.718  1.00 15.62 ?  76  LYS   A CG   1 
ATOM   1750 C  CD   . LYS   A 1 76  ? 36.047 -7.319  -6.503  1.00 16.78 ?  76  LYS   A CD   1 
ATOM   1751 C  CE   . LYS   A 1 76  ? 37.547 -7.379  -6.709  1.00 19.29 ?  76  LYS   A CE   1 
ATOM   1752 N  NZ   . LYS   A 1 76  ? 38.076 -8.741  -6.500  1.00 20.02 ?  76  LYS   A NZ   1 
ATOM   1753 H  H    . LYS   A 1 76  ? 34.297 -4.172  -4.703  1.00 14.51 ?  76  LYS   A H    1 
ATOM   1754 H  HA   . LYS   A 1 76  ? 33.662 -3.916  -7.307  1.00 15.17 ?  76  LYS   A HA   1 
ATOM   1755 H  HB2  . LYS   A 1 76  ? 33.782 -6.258  -5.707  1.00 17.44 ?  76  LYS   A HB2  1 
ATOM   1756 H  HB3  . LYS   A 1 76  ? 33.591 -6.260  -7.281  1.00 17.44 ?  76  LYS   A HB3  1 
ATOM   1757 H  HG2  . LYS   A 1 76  ? 35.753 -5.643  -7.622  1.00 18.88 ?  76  LYS   A HG2  1 
ATOM   1758 H  HG3  . LYS   A 1 76  ? 35.964 -5.330  -6.078  1.00 18.88 ?  76  LYS   A HG3  1 
ATOM   1759 H  HD2  . LYS   A 1 76  ? 35.850 -7.601  -5.595  1.00 20.28 ?  76  LYS   A HD2  1 
ATOM   1760 H  HD3  . LYS   A 1 76  ? 35.627 -7.919  -7.140  1.00 20.28 ?  76  LYS   A HD3  1 
ATOM   1761 H  HE2  . LYS   A 1 76  ? 37.755 -7.107  -7.615  1.00 23.29 ?  76  LYS   A HE2  1 
ATOM   1762 H  HE3  . LYS   A 1 76  ? 37.978 -6.786  -6.073  1.00 23.29 ?  76  LYS   A HE3  1 
ATOM   1763 H  HZ1  . LYS   A 1 76  ? 38.956 -8.755  -6.626  1.00 24.17 ?  76  LYS   A HZ1  1 
ATOM   1764 H  HZ2  . LYS   A 1 76  ? 37.899 -9.018  -5.671  1.00 24.17 ?  76  LYS   A HZ2  1 
ATOM   1765 H  HZ3  . LYS   A 1 76  ? 37.696 -9.310  -7.075  1.00 24.17 ?  76  LYS   A HZ3  1 
ATOM   1766 N  N    . VAL   A 1 77  ? 31.204 -4.421  -7.378  1.00 11.68 ?  77  VAL   A N    1 
ATOM   1767 C  CA   . VAL   A 1 77  ? 29.798 -4.811  -7.297  1.00 11.65 ?  77  VAL   A CA   1 
ATOM   1768 C  C    . VAL   A 1 77  ? 29.734 -6.264  -6.856  1.00 11.32 ?  77  VAL   A C    1 
ATOM   1769 O  O    . VAL   A 1 77  ? 30.398 -7.133  -7.433  1.00 11.89 ?  77  VAL   A O    1 
ATOM   1770 C  CB   . VAL   A 1 77  ? 29.077 -4.595  -8.636  1.00 12.70 ?  77  VAL   A CB   1 
ATOM   1771 C  CG1  . VAL   A 1 77  ? 27.617 -5.040  -8.529  1.00 13.55 ?  77  VAL   A CG1  1 
ATOM   1772 C  CG2  . VAL   A 1 77  ? 29.157 -3.140  -9.059  1.00 14.01 ?  77  VAL   A CG2  1 
ATOM   1773 H  H    . VAL   A 1 77  ? 31.480 -4.178  -8.155  1.00 14.15 ?  77  VAL   A H    1 
ATOM   1774 H  HA   . VAL   A 1 77  ? 29.360 -4.267  -6.625  1.00 14.12 ?  77  VAL   A HA   1 
ATOM   1775 H  HB   . VAL   A 1 77  ? 29.510 -5.128  -9.320  1.00 15.38 ?  77  VAL   A HB   1 
ATOM   1776 H  HG11 . VAL   A 1 77  ? 27.141 -4.733  -9.313  1.00 16.40 ?  77  VAL   A HG11 1 
ATOM   1777 H  HG12 . VAL   A 1 77  ? 27.588 -6.007  -8.478  1.00 16.40 ?  77  VAL   A HG12 1 
ATOM   1778 H  HG13 . VAL   A 1 77  ? 27.232 -4.650  -7.730  1.00 16.40 ?  77  VAL   A HG13 1 
ATOM   1779 H  HG21 . VAL   A 1 77  ? 28.651 -3.023  -9.878  1.00 16.95 ?  77  VAL   A HG21 1 
ATOM   1780 H  HG22 . VAL   A 1 77  ? 28.779 -2.588  -8.355  1.00 16.95 ?  77  VAL   A HG22 1 
ATOM   1781 H  HG23 . VAL   A 1 77  ? 30.085 -2.901  -9.205  1.00 16.95 ?  77  VAL   A HG23 1 
ATOM   1782 N  N    . GLY   A 1 78  ? 28.951 -6.533  -5.810  1.00 11.17 ?  78  GLY   A N    1 
ATOM   1783 C  CA   . GLY   A 1 78  ? 28.930 -7.824  -5.155  1.00 11.20 ?  78  GLY   A CA   1 
ATOM   1784 C  C    . GLY   A 1 78  ? 29.842 -7.916  -3.951  1.00 10.81 ?  78  GLY   A C    1 
ATOM   1785 O  O    . GLY   A 1 78  ? 29.788 -8.922  -3.228  1.00 11.54 ?  78  GLY   A O    1 
ATOM   1786 H  H    . GLY   A 1 78  ? 28.405 -5.960  -5.464  1.00 13.55 ?  78  GLY   A H    1 
ATOM   1787 H  HA2  . GLY   A 1 78  ? 28.026 -8.017  -4.869  1.00 13.58 ?  78  GLY   A HA2  1 
ATOM   1788 H  HA3  . GLY   A 1 78  ? 29.196 -8.503  -5.797  1.00 13.58 ?  78  GLY   A HA3  1 
ATOM   1789 N  N    . GLY   A 1 79  ? 30.696 -6.911  -3.730  1.00 10.87 ?  79  GLY   A N    1 
ATOM   1790 C  CA   . GLY   A 1 79  ? 31.657 -6.925  -2.649  1.00 11.30 ?  79  GLY   A CA   1 
ATOM   1791 C  C    . GLY   A 1 79  ? 31.211 -6.123  -1.438  1.00 10.58 ?  79  GLY   A C    1 
ATOM   1792 O  O    . GLY   A 1 79  ? 30.090 -5.615  -1.359  1.00 11.08 ?  79  GLY   A O    1 
ATOM   1793 H  H    . GLY   A 1 79  ? 30.737 -6.200  -4.211  1.00 13.19 ?  79  GLY   A H    1 
ATOM   1794 H  HA2  . GLY   A 1 79  ? 31.808 -7.852  -2.374  1.00 13.70 ?  79  GLY   A HA2  1 
ATOM   1795 H  HA3  . GLY   A 1 79  ? 32.499 -6.569  -2.964  1.00 13.70 ?  79  GLY   A HA3  1 
ATOM   1796 N  N    . SER   A 1 80  ? 32.118 -6.028  -0.466  1.00 11.32 ?  80  SER   A N    1 
ATOM   1797 C  CA   . SER   A 1 80  ? 31.796 -5.403  0.807   1.00 10.77 ?  80  SER   A CA   1 
ATOM   1798 C  C    . SER   A 1 80  ? 33.071 -4.950  1.502   1.00 10.70 ?  80  SER   A C    1 
ATOM   1799 O  O    . SER   A 1 80  ? 34.184 -5.381  1.173   1.00 12.23 ?  80  SER   A O    1 
ATOM   1800 C  CB   . SER   A 1 80  ? 31.034 -6.366  1.729   1.00 11.78 ?  80  SER   A CB   1 
ATOM   1801 O  OG   . SER   A 1 80  ? 31.872 -7.408  2.210   1.00 13.44 ?  80  SER   A OG   1 
ATOM   1802 H  H    . SER   A 1 80  ? 32.931 -6.303  -0.530  1.00 13.72 ?  80  SER   A H    1 
ATOM   1803 H  HA   . SER   A 1 80  ? 31.240 -4.623  0.630   1.00 13.07 ?  80  SER   A HA   1 
ATOM   1804 H  HB2  . SER   A 1 80  ? 30.688 -5.860  2.479   1.00 14.28 ?  80  SER   A HB2  1 
ATOM   1805 H  HB3  . SER   A 1 80  ? 30.299 -6.753  1.226   1.00 14.28 ?  80  SER   A HB3  1 
ATOM   1806 H  HG   . SER   A 1 80  ? 32.174 -7.843  1.559   1.00 16.27 ?  80  SER   A HG   1 
ATOM   1807 N  N    . CYS   A 1 81  ? 32.883 -4.101  2.510   1.00 10.53 ?  81  CYS   A N    1 
ATOM   1808 C  CA   . CYS   A 1 81  ? 33.937 -3.810  3.470   1.00 10.70 ?  81  CYS   A CA   1 
ATOM   1809 C  C    . CYS   A 1 81  ? 33.292 -3.575  4.829   1.00 10.49 ?  81  CYS   A C    1 
ATOM   1810 O  O    . CYS   A 1 81  ? 32.124 -3.180  4.917   1.00 11.74 ?  81  CYS   A O    1 
ATOM   1811 C  CB   . CYS   A 1 81  ? 34.804 -2.618  3.042   1.00 11.34 ?  81  CYS   A CB   1 
ATOM   1812 S  SG   . CYS   A 1 81  ? 33.908 -1.049  3.071   1.00 11.43 ?  81  CYS   A SG   1 
ATOM   1813 H  H    . CYS   A 1 81  ? 32.140 -3.688  2.665   1.00 12.78 ?  81  CYS   A H    1 
ATOM   1814 H  HA   . CYS   A 1 81  ? 34.511 -4.584  3.543   1.00 12.98 ?  81  CYS   A HA   1 
ATOM   1815 H  HB2  . CYS   A 1 81  ? 35.561 -2.552  3.648   1.00 13.74 ?  81  CYS   A HB2  1 
ATOM   1816 H  HB3  . CYS   A 1 81  ? 35.123 -2.775  2.136   1.00 13.74 ?  81  CYS   A HB3  1 
ATOM   1817 H  HG   . CYS   A 1 81  ? 34.648 -0.170  2.727   1.00 13.85 ?  81  CYS   A HG   1 
ATOM   1818 N  N    . VAL   A 1 82  ? 34.058 -3.842  5.886   1.00 10.86 ?  82  VAL   A N    1 
ATOM   1819 C  CA   . VAL   A 1 82  ? 33.634 -3.599  7.258   1.00 11.19 ?  82  VAL   A CA   1 
ATOM   1820 C  C    . VAL   A 1 82  ? 34.232 -2.281  7.727   1.00 11.47 ?  82  VAL   A C    1 
ATOM   1821 O  O    . VAL   A 1 82  ? 35.457 -2.103  7.708   1.00 12.14 ?  82  VAL   A O    1 
ATOM   1822 C  CB   . VAL   A 1 82  ? 34.058 -4.737  8.197   1.00 12.64 ?  82  VAL   A CB   1 
ATOM   1823 C  CG1  . VAL   A 1 82  ? 33.609 -4.434  9.617   1.00 14.09 ?  82  VAL   A CG1  1 
ATOM   1824 C  CG2  . VAL   A 1 82  ? 33.502 -6.070  7.726   1.00 13.86 ?  82  VAL   A CG2  1 
ATOM   1825 H  H    . VAL   A 1 82  ? 34.852 -4.182  5.827   1.00 13.18 ?  82  VAL   A H    1 
ATOM   1826 H  HA   . VAL   A 1 82  ? 32.665 -3.522  7.282   1.00 13.57 ?  82  VAL   A HA   1 
ATOM   1827 H  HB   . VAL   A 1 82  ? 35.024 -4.794  8.197   1.00 15.31 ?  82  VAL   A HB   1 
ATOM   1828 H  HG11 . VAL   A 1 82  ? 33.689 -5.241  10.149  1.00 17.05 ?  82  VAL   A HG11 1 
ATOM   1829 H  HG12 . VAL   A 1 82  ? 34.171 -3.737  9.990   1.00 17.05 ?  82  VAL   A HG12 1 
ATOM   1830 H  HG13 . VAL   A 1 82  ? 32.683 -4.140  9.602   1.00 17.05 ?  82  VAL   A HG13 1 
ATOM   1831 H  HG21 . VAL   A 1 82  ? 33.757 -6.757  8.362   1.00 16.77 ?  82  VAL   A HG21 1 
ATOM   1832 H  HG22 . VAL   A 1 82  ? 32.536 -6.010  7.672   1.00 16.77 ?  82  VAL   A HG22 1 
ATOM   1833 H  HG23 . VAL   A 1 82  ? 33.872 -6.275  6.853   1.00 16.77 ?  82  VAL   A HG23 1 
ATOM   1834 N  N    . LEU   A 1 83  ? 33.372 -1.359  8.147   1.00 11.05 ?  83  LEU   A N    1 
ATOM   1835 C  CA   . LEU   A 1 83  ? 33.791 -0.091  8.723   1.00 11.00 ?  83  LEU   A CA   1 
ATOM   1836 C  C    . LEU   A 1 83  ? 33.073 0.090   10.056  1.00 11.08 ?  83  LEU   A C    1 
ATOM   1837 O  O    . LEU   A 1 83  ? 32.353 -0.800  10.524  1.00 11.82 ?  83  LEU   A O    1 
ATOM   1838 C  CB   . LEU   A 1 83  ? 33.538 1.065   7.743   1.00 11.55 ?  83  LEU   A CB   1 
ATOM   1839 C  CG   . LEU   A 1 83  ? 34.443 1.067   6.504   1.00 12.04 ?  83  LEU   A CG   1 
ATOM   1840 C  CD1  . LEU   A 1 83  ? 33.999 2.111   5.506   1.00 12.62 ?  83  LEU   A CD1  1 
ATOM   1841 C  CD2  . LEU   A 1 83  ? 35.914 1.301   6.887   1.00 12.70 ?  83  LEU   A CD2  1 
ATOM   1842 H  H    . LEU   A 1 83  ? 32.515 -1.449  8.103   1.00 13.40 ?  83  LEU   A H    1 
ATOM   1843 H  HA   . LEU   A 1 83  ? 34.742 -0.120  8.899   1.00 13.34 ?  83  LEU   A HA   1 
ATOM   1844 H  HB2  . LEU   A 1 83  ? 32.623 1.018   7.425   1.00 14.00 ?  83  LEU   A HB2  1 
ATOM   1845 H  HB3  . LEU   A 1 83  ? 33.680 1.907   8.201   1.00 14.00 ?  83  LEU   A HB3  1 
ATOM   1846 H  HG   . LEU   A 1 83  ? 34.389 0.201   6.071   1.00 14.59 ?  83  LEU   A HG   1 
ATOM   1847 H  HD11 . LEU   A 1 83  ? 34.590 2.083   4.735   1.00 15.28 ?  83  LEU   A HD11 1 
ATOM   1848 H  HD12 . LEU   A 1 83  ? 33.090 1.916   5.234   1.00 15.28 ?  83  LEU   A HD12 1 
ATOM   1849 H  HD13 . LEU   A 1 83  ? 34.043 2.984   5.924   1.00 15.28 ?  83  LEU   A HD13 1 
ATOM   1850 H  HD21 . LEU   A 1 83  ? 36.436 1.445   6.078   1.00 15.37 ?  83  LEU   A HD21 1 
ATOM   1851 H  HD22 . LEU   A 1 83  ? 35.973 2.088   7.455   1.00 15.37 ?  83  LEU   A HD22 1 
ATOM   1852 H  HD23 . LEU   A 1 83  ? 36.251 0.526   7.361   1.00 15.37 ?  83  LEU   A HD23 1 
ATOM   1853 N  N    . SER   A 1 84  ? 33.283 1.244   10.684  1.00 11.89 ?  84  SER   A N    1 
ATOM   1854 C  CA   . SER   A 1 84  ? 32.633 1.507   11.958  1.00 11.92 ?  84  SER   A CA   1 
ATOM   1855 C  C    . SER   A 1 84  ? 31.115 1.579   11.808  1.00 11.84 ?  84  SER   A C    1 
ATOM   1856 O  O    . SER   A 1 84  ? 30.585 2.046   10.799  1.00 11.91 ?  84  SER   A O    1 
ATOM   1857 C  CB   . SER   A 1 84  ? 33.116 2.837   12.522  1.00 12.82 ?  84  SER   A CB   1 
ATOM   1858 O  OG   . SER   A 1 84  ? 32.504 3.104   13.768  1.00 13.53 ?  84  SER   A OG   1 
ATOM   1859 H  H    . SER   A 1 84  ? 33.785 1.886   10.390  1.00 14.41 ?  84  SER   A H    1 
ATOM   1860 H  HA   . SER   A 1 84  ? 32.859 0.804   12.582  1.00 14.44 ?  84  SER   A HA   1 
ATOM   1861 H  HB2  . SER   A 1 84  ? 34.077 2.806   12.635  1.00 15.52 ?  84  SER   A HB2  1 
ATOM   1862 H  HB3  . SER   A 1 84  ? 32.881 3.548   11.898  1.00 15.52 ?  84  SER   A HB3  1 
ATOM   1863 H  HG   . SER   A 1 84  ? 32.779 3.840   14.069  1.00 16.37 ?  84  SER   A HG   1 
ATOM   1864 N  N    . GLY   A 1 85  ? 30.411 1.160   12.857  1.00 12.55 ?  85  GLY   A N    1 
ATOM   1865 C  CA   . GLY   A 1 85  ? 28.987 1.396   12.956  1.00 13.13 ?  85  GLY   A CA   1 
ATOM   1866 C  C    . GLY   A 1 85  ? 28.619 2.713   13.602  1.00 12.72 ?  85  GLY   A C    1 
ATOM   1867 O  O    . GLY   A 1 85  ? 27.428 3.030   13.709  1.00 13.37 ?  85  GLY   A O    1 
ATOM   1868 H  H    . GLY   A 1 85  ? 30.746 0.728   13.525  1.00 15.19 ?  85  GLY   A H    1 
ATOM   1869 H  HA2  . GLY   A 1 85  ? 28.603 1.373   12.066  1.00 15.90 ?  85  GLY   A HA2  1 
ATOM   1870 H  HA3  . GLY   A 1 85  ? 28.585 0.688   13.477  1.00 15.90 ?  85  GLY   A HA3  1 
ATOM   1871 N  N    . HIS   A 1 86  ? 29.607 3.491   14.039  1.00 12.51 ?  86  HIS   A N    1 
ATOM   1872 C  CA   . HIS   A 1 86  ? 29.381 4.831   14.595  1.00 13.21 ?  86  HIS   A CA   1 
ATOM   1873 C  C    . HIS   A 1 86  ? 28.397 4.713   15.752  1.00 14.07 ?  86  HIS   A C    1 
ATOM   1874 O  O    . HIS   A 1 86  ? 28.584 3.841   16.616  1.00 15.04 ?  86  HIS   A O    1 
ATOM   1875 C  CB   . HIS   A 1 86  ? 29.005 5.811   13.487  1.00 13.08 ?  86  HIS   A CB   1 
ATOM   1876 C  CG   . HIS   A 1 86  ? 30.060 5.912   12.446  1.00 12.86 ?  86  HIS   A CG   1 
ATOM   1877 N  ND1  . HIS   A 1 86  ? 31.149 6.750   12.573  1.00 13.86 ?  86  HIS   A ND1  1 
ATOM   1878 C  CD2  . HIS   A 1 86  ? 30.242 5.219   11.300  1.00 12.74 ?  86  HIS   A CD2  1 
ATOM   1879 C  CE1  . HIS   A 1 86  ? 31.941 6.583   11.529  1.00 13.53 ?  86  HIS   A CE1  1 
ATOM   1880 N  NE2  . HIS   A 1 86  ? 31.421 5.653   10.750  1.00 13.13 ?  86  HIS   A NE2  1 
ATOM   1881 H  H    . HIS   A 1 86  ? 30.432 3.270   14.027  1.00 15.15 ?  86  HIS   A H    1 
ATOM   1882 H  HA   . HIS   A 1 86  ? 30.217 5.150   14.965  1.00 15.99 ?  86  HIS   A HA   1 
ATOM   1883 H  HB2  . HIS   A 1 86  ? 28.182 5.520   13.059  1.00 15.83 ?  86  HIS   A HB2  1 
ATOM   1884 H  HB3  . HIS   A 1 86  ? 28.876 6.701   13.867  1.00 15.83 ?  86  HIS   A HB3  1 
ATOM   1885 H  HD2  . HIS   A 1 86  ? 29.680 4.557   10.952  1.00 15.43 ?  86  HIS   A HD2  1 
ATOM   1886 H  HE1  . HIS   A 1 86  ? 32.731 7.042   11.359  1.00 16.38 ?  86  HIS   A HE1  1 
ATOM   1887 H  HE2  . HIS   A 1 86  ? 31.754 5.375   9.999   1.00 15.89 ?  86  HIS   A HE2  1 
ATOM   1888 N  N    . ASN   A 1 87  ? 27.382 5.562   15.823  1.00 14.92 ?  87  ASN   A N    1 
ATOM   1889 C  CA   . ASN   A 1 87  ? 26.403 5.552   16.894  1.00 15.75 ?  87  ASN   A CA   1 
ATOM   1890 C  C    . ASN   A 1 87  ? 25.281 4.554   16.659  1.00 17.04 ?  87  ASN   A C    1 
ATOM   1891 O  O    . ASN   A 1 87  ? 24.363 4.483   17.479  1.00 18.98 ?  87  ASN   A O    1 
ATOM   1892 C  CB   . ASN   A 1 87  ? 25.804 6.957   17.055  1.00 16.53 ?  87  ASN   A CB   1 
ATOM   1893 C  CG   . ASN   A 1 87  ? 25.304 7.537   15.737  1.00 17.53 ?  87  ASN   A CG   1 
ATOM   1894 O  OD1  . ASN   A 1 87  ? 25.951 7.414   14.701  1.00 18.10 ?  87  ASN   A OD1  1 
ATOM   1895 N  ND2  . ASN   A 1 87  ? 24.150 8.173   15.775  1.00 18.49 ?  87  ASN   A ND2  1 
ATOM   1896 H  H    . ASN   A 1 87  ? 27.235 6.179   15.245  1.00 18.05 ?  87  ASN   A H    1 
ATOM   1897 H  HA   . ASN   A 1 87  ? 26.836 5.315   17.734  1.00 19.04 ?  87  ASN   A HA   1 
ATOM   1898 H  HB2  . ASN   A 1 87  ? 25.051 6.911   17.673  1.00 19.98 ?  87  ASN   A HB2  1 
ATOM   1899 H  HB3  . ASN   A 1 87  ? 26.483 7.549   17.410  1.00 19.98 ?  87  ASN   A HB3  1 
ATOM   1900 H  HD21 . ASN   A 1 87  ? 23.829 8.512   15.055  1.00 22.33 ?  87  ASN   A HD21 1 
ATOM   1901 H  HD22 . ASN   A 1 87  ? 23.724 8.251   16.518  1.00 22.33 ?  87  ASN   A HD22 1 
ATOM   1902 N  N    . LEU   A 1 88  ? 25.333 3.777   15.581  1.00 15.96 ?  88  LEU   A N    1 
ATOM   1903 C  CA   . LEU   A 1 88  ? 24.220 2.916   15.193  1.00 15.80 ?  88  LEU   A CA   1 
ATOM   1904 C  C    . LEU   A 1 88  ? 24.436 1.438   15.490  1.00 15.31 ?  88  LEU   A C    1 
ATOM   1905 O  O    . LEU   A 1 88  ? 23.457 0.703   15.660  1.00 16.25 ?  88  LEU   A O    1 
ATOM   1906 C  CB   . LEU   A 1 88  ? 23.956 3.071   13.695  1.00 16.14 ?  88  LEU   A CB   1 
ATOM   1907 C  CG   . LEU   A 1 88  ? 23.674 4.494   13.211  1.00 17.82 ?  88  LEU   A CG   1 
ATOM   1908 C  CD1  . LEU   A 1 88  ? 23.511 4.514   11.705  1.00 18.06 ?  88  LEU   A CD1  1 
ATOM   1909 C  CD2  . LEU   A 1 88  ? 22.438 5.065   13.892  1.00 19.42 ?  88  LEU   A CD2  1 
ATOM   1910 H  H    . LEU   A 1 88  ? 26.010 3.737   15.057  1.00 19.29 ?  88  LEU   A H    1 
ATOM   1911 H  HA   . LEU   A 1 88  ? 23.426 3.201   15.668  1.00 19.10 ?  88  LEU   A HA   1 
ATOM   1912 H  HB2  . LEU   A 1 88  ? 24.726 2.749   13.209  1.00 19.51 ?  88  LEU   A HB2  1 
ATOM   1913 H  HB3  . LEU   A 1 88  ? 23.180 2.534   13.466  1.00 19.51 ?  88  LEU   A HB3  1 
ATOM   1914 H  HG   . LEU   A 1 88  ? 24.428 5.060   13.436  1.00 21.52 ?  88  LEU   A HG   1 
ATOM   1915 H  HD11 . LEU   A 1 88  ? 23.347 5.427   11.416  1.00 21.81 ?  88  LEU   A HD11 1 
ATOM   1916 H  HD12 . LEU   A 1 88  ? 24.324 4.180   11.294  1.00 21.81 ?  88  LEU   A HD12 1 
ATOM   1917 H  HD13 . LEU   A 1 88  ? 22.761 3.951   11.459  1.00 21.81 ?  88  LEU   A HD13 1 
ATOM   1918 H  HD21 . LEU   A 1 88  ? 22.223 5.919   13.485  1.00 23.44 ?  88  LEU   A HD21 1 
ATOM   1919 H  HD22 . LEU   A 1 88  ? 21.703 4.446   13.777  1.00 23.44 ?  88  LEU   A HD22 1 
ATOM   1920 H  HD23 . LEU   A 1 88  ? 22.629 5.185   14.835  1.00 23.44 ?  88  LEU   A HD23 1 
ATOM   1921 N  N    . ALA   A 1 89  ? 25.685 0.989   15.524  1.00 14.64 ?  89  ALA   A N    1 
ATOM   1922 C  CA   . ALA   A 1 89  ? 26.026 -0.422  15.626  1.00 14.37 ?  89  ALA   A CA   1 
ATOM   1923 C  C    . ALA   A 1 89  ? 27.508 -0.487  15.948  1.00 14.72 ?  89  ALA   A C    1 
ATOM   1924 O  O    . ALA   A 1 89  ? 28.222 0.509   15.831  1.00 15.24 ?  89  ALA   A O    1 
ATOM   1925 C  CB   . ALA   A 1 89  ? 25.753 -1.136  14.304  1.00 13.78 ?  89  ALA   A CB   1 
ATOM   1926 H  H    . ALA   A 1 89  ? 26.374 1.505   15.478  1.00 17.71 ?  89  ALA   A H    1 
ATOM   1927 H  HA   . ALA   A 1 89  ? 25.517 -0.838  16.337  1.00 17.38 ?  89  ALA   A HA   1 
ATOM   1928 H  HB1  . ALA   A 1 89  ? 25.999 -2.070  14.394  1.00 16.68 ?  89  ALA   A HB1  1 
ATOM   1929 H  HB2  . ALA   A 1 89  ? 24.807 -1.064  14.093  1.00 16.68 ?  89  ALA   A HB2  1 
ATOM   1930 H  HB3  . ALA   A 1 89  ? 26.279 -0.722  13.604  1.00 16.68 ?  89  ALA   A HB3  1 
ATOM   1931 N  N    . LYS   A 1 90  ? 27.983 -1.667  16.336  1.00 15.45 ?  90  LYS   A N    1 
ATOM   1932 C  CA   . LYS   A 1 90  ? 29.427 -1.818  16.491  1.00 16.19 ?  90  LYS   A CA   1 
ATOM   1933 C  C    . LYS   A 1 90  ? 30.134 -1.634  15.150  1.00 15.02 ?  90  LYS   A C    1 
ATOM   1934 O  O    . LYS   A 1 90  ? 31.072 -0.827  15.026  1.00 16.31 ?  90  LYS   A O    1 
ATOM   1935 C  CB   . LYS   A 1 90  ? 29.762 -3.174  17.114  1.00 19.23 ?  90  LYS   A CB   1 
ATOM   1936 C  CG   . LYS   A 1 90  ? 31.243 -3.325  17.442  1.00 24.44 ?  90  LYS   A CG   1 
ATOM   1937 C  CD   . LYS   A 1 90  ? 31.505 -4.581  18.259  1.00 30.09 ?  90  LYS   A CD   1 
ATOM   1938 C  CE   . LYS   A 1 90  ? 32.897 -4.574  18.878  1.00 34.40 ?  90  LYS   A CE   1 
ATOM   1939 N  NZ   . LYS   A 1 90  ? 33.972 -4.882  17.895  1.00 36.93 ?  90  LYS   A NZ   1 
ATOM   1940 H  H    . LYS   A 1 90  ? 27.508 -2.357  16.516  1.00 18.69 ?  90  LYS   A H    1 
ATOM   1941 H  HA   . LYS   A 1 90  ? 29.749 -1.129  17.088  1.00 19.57 ?  90  LYS   A HA   1 
ATOM   1942 H  HB2  . LYS   A 1 90  ? 29.258 -3.273  17.941  1.00 23.21 ?  90  LYS   A HB2  1 
ATOM   1943 H  HB3  . LYS   A 1 90  ? 29.515 -3.878  16.495  1.00 23.21 ?  90  LYS   A HB3  1 
ATOM   1944 H  HG2  . LYS   A 1 90  ? 31.748 -3.386  16.617  1.00 29.47 ?  90  LYS   A HG2  1 
ATOM   1945 H  HG3  . LYS   A 1 90  ? 31.535 -2.558  17.959  1.00 29.47 ?  90  LYS   A HG3  1 
ATOM   1946 H  HD2  . LYS   A 1 90  ? 30.854 -4.638  18.977  1.00 36.25 ?  90  LYS   A HD2  1 
ATOM   1947 H  HD3  . LYS   A 1 90  ? 31.433 -5.358  17.682  1.00 36.25 ?  90  LYS   A HD3  1 
ATOM   1948 H  HE2  . LYS   A 1 90  ? 33.075 -3.695  19.248  1.00 41.43 ?  90  LYS   A HE2  1 
ATOM   1949 H  HE3  . LYS   A 1 90  ? 32.934 -5.242  19.580  1.00 41.43 ?  90  LYS   A HE3  1 
ATOM   1950 H  HZ1  . LYS   A 1 90  ? 34.767 -4.868  18.298  1.00 44.45 ?  90  LYS   A HZ1  1 
ATOM   1951 H  HZ2  . LYS   A 1 90  ? 33.841 -5.690  17.544  1.00 44.45 ?  90  LYS   A HZ2  1 
ATOM   1952 H  HZ3  . LYS   A 1 90  ? 33.969 -4.280  17.241  1.00 44.45 ?  90  LYS   A HZ3  1 
ATOM   1953 N  N    . HIS   A 1 91  ? 29.666 -2.350  14.127  1.00 13.26 ?  91  HIS   A N    1 
ATOM   1954 C  CA   . HIS   A 1 91  ? 30.246 -2.338  12.799  1.00 12.54 ?  91  HIS   A CA   1 
ATOM   1955 C  C    . HIS   A 1 91  ? 29.165 -2.065  11.771  1.00 11.38 ?  91  HIS   A C    1 
ATOM   1956 O  O    . HIS   A 1 91  ? 27.997 -2.419  11.964  1.00 12.16 ?  91  HIS   A O    1 
ATOM   1957 C  CB   . HIS   A 1 91  ? 30.840 -3.707  12.444  1.00 15.01 ?  91  HIS   A CB   1 
ATOM   1958 C  CG   . HIS   A 1 91  ? 31.829 -4.219  13.441  1.00 19.09 ?  91  HIS   A CG   1 
ATOM   1959 N  ND1  . HIS   A 1 91  ? 33.113 -3.729  13.532  1.00 21.18 ?  91  HIS   A ND1  1 
ATOM   1960 C  CD2  . HIS   A 1 91  ? 31.731 -5.192  14.377  1.00 21.01 ?  91  HIS   A CD2  1 
ATOM   1961 C  CE1  . HIS   A 1 91  ? 33.763 -4.372  14.486  1.00 22.19 ?  91  HIS   A CE1  1 
ATOM   1962 N  NE2  . HIS   A 1 91  ? 32.946 -5.266  15.015  1.00 22.41 ?  91  HIS   A NE2  1 
ATOM   1963 H  H    . HIS   A 1 91  ? 28.981 -2.888  14.194  1.00 16.05 ?  91  HIS   A H    1 
ATOM   1964 H  HA   . HIS   A 1 91  ? 30.932 -1.665  12.739  1.00 15.19 ?  91  HIS   A HA   1 
ATOM   1965 H  HB2  . HIS   A 1 91  ? 30.123 -4.360  12.385  1.00 18.15 ?  91  HIS   A HB2  1 
ATOM   1966 H  HB3  . HIS   A 1 91  ? 31.292 -3.640  11.589  1.00 18.15 ?  91  HIS   A HB3  1 
ATOM   1967 H  HD1  . HIS   A 1 91  ? 33.444 -3.101  13.041  1.00 25.56 ?  91  HIS   A HD1  1 
ATOM   1968 H  HD2  . HIS   A 1 91  ? 30.988 -5.713  14.560  1.00 25.35 ?  91  HIS   A HD2  1 
ATOM   1969 H  HE1  . HIS   A 1 91  ? 34.649 -4.217  14.741  1.00 26.77 ?  91  HIS   A HE1  1 
ATOM   1970 N  N    . CYS   A 1 92  ? 29.574 -1.466  10.658  1.00 11.20 ?  92  CYS   A N    1 
ATOM   1971 C  CA   . CYS   A 1 92  ? 28.743 -1.390  9.465   1.00 10.89 ?  92  CYS   A CA   1 
ATOM   1972 C  C    . CYS   A 1 92  ? 29.392 -2.208  8.358   1.00 10.40 ?  92  CYS   A C    1 
ATOM   1973 O  O    . CYS   A 1 92  ? 30.551 -1.957  7.992   1.00 11.19 ?  92  CYS   A O    1 
ATOM   1974 C  CB   . CYS   A 1 92  ? 28.529 0.052   9.003   1.00 11.22 ?  92  CYS   A CB   1 
ATOM   1975 S  SG   . CYS   A 1 92  ? 27.514 0.157   7.489   1.00 10.64 ?  92  CYS   A SG   1 
ATOM   1976 H  H    . CYS   A 1 92  ? 30.339 -1.081  10.572  1.00 13.58 ?  92  CYS   A H    1 
ATOM   1977 H  HA   . CYS   A 1 92  ? 27.873 -1.773  9.658   1.00 13.21 ?  92  CYS   A HA   1 
ATOM   1978 H  HB2  . CYS   A 1 92  ? 28.076 0.552   9.703   1.00 13.61 ?  92  CYS   A HB2  1 
ATOM   1979 H  HB3  . CYS   A 1 92  ? 29.389 0.459   8.811   1.00 13.61 ?  92  CYS   A HB3  1 
ATOM   1980 H  HG   . CYS   A 1 92  ? 27.374 1.310   7.198   1.00 12.91 ?  92  CYS   A HG   1 
ATOM   1981 N  N    . LEU   A 1 93  ? 28.654 -3.196  7.852   1.00 10.32 ?  93  LEU   A N    1 
ATOM   1982 C  CA   . LEU   A 1 93  ? 29.058 -3.954  6.674   1.00 10.14 ?  93  LEU   A CA   1 
ATOM   1983 C  C    . LEU   A 1 93  ? 28.461 -3.260  5.452   1.00 9.54  ?  93  LEU   A C    1 
ATOM   1984 O  O    . LEU   A 1 93  ? 27.245 -3.319  5.228   1.00 9.88  ?  93  LEU   A O    1 
ATOM   1985 C  CB   . LEU   A 1 93  ? 28.572 -5.401  6.779   1.00 10.55 ?  93  LEU   A CB   1 
ATOM   1986 C  CG   . LEU   A 1 93  ? 28.963 -6.305  5.607   1.00 10.74 ?  93  LEU   A CG   1 
ATOM   1987 C  CD1  . LEU   A 1 93  ? 30.469 -6.560  5.588   1.00 11.90 ?  93  LEU   A CD1  1 
ATOM   1988 C  CD2  . LEU   A 1 93  ? 28.191 -7.625  5.654   1.00 11.67 ?  93  LEU   A CD2  1 
ATOM   1989 H  H    . LEU   A 1 93  ? 27.897 -3.445  8.187   1.00 12.52 ?  93  LEU   A H    1 
ATOM   1990 H  HA   . LEU   A 1 93  ? 30.020 -3.945  6.601   1.00 12.31 ?  93  LEU   A HA   1 
ATOM   1991 H  HB2  . LEU   A 1 93  ? 28.947 -5.790  7.587   1.00 12.81 ?  93  LEU   A HB2  1 
ATOM   1992 H  HB3  . LEU   A 1 93  ? 27.607 -5.401  6.838   1.00 12.81 ?  93  LEU   A HB3  1 
ATOM   1993 H  HG   . LEU   A 1 93  ? 28.734 -5.867  4.781   1.00 13.03 ?  93  LEU   A HG   1 
ATOM   1994 H  HD11 . LEU   A 1 93  ? 30.681 -7.177  4.871   1.00 14.42 ?  93  LEU   A HD11 1 
ATOM   1995 H  HD12 . LEU   A 1 93  ? 30.932 -5.720  5.452   1.00 14.42 ?  93  LEU   A HD12 1 
ATOM   1996 H  HD13 . LEU   A 1 93  ? 30.739 -6.948  6.441   1.00 14.42 ?  93  LEU   A HD13 1 
ATOM   1997 H  HD21 . LEU   A 1 93  ? 28.464 -8.178  4.902   1.00 14.15 ?  93  LEU   A HD21 1 
ATOM   1998 H  HD22 . LEU   A 1 93  ? 28.391 -8.084  6.486   1.00 14.15 ?  93  LEU   A HD22 1 
ATOM   1999 H  HD23 . LEU   A 1 93  ? 27.242 -7.438  5.598   1.00 14.15 ?  93  LEU   A HD23 1 
ATOM   2000 N  N    . HIS   A 1 94  ? 29.309 -2.569  4.688   1.00 9.54  ?  94  HIS   A N    1 
ATOM   2001 C  CA   . HIS   A 1 94  ? 28.888 -1.894  3.462   1.00 9.60  ?  94  HIS   A CA   1 
ATOM   2002 C  C    . HIS   A 1 94  ? 28.897 -2.929  2.351   1.00 9.59  ?  94  HIS   A C    1 
ATOM   2003 O  O    . HIS   A 1 94  ? 29.962 -3.441  2.004   1.00 11.07 ?  94  HIS   A O    1 
ATOM   2004 C  CB   . HIS   A 1 94  ? 29.854 -0.754  3.137   1.00 9.43  ?  94  HIS   A CB   1 
ATOM   2005 C  CG   . HIS   A 1 94  ? 29.835 0.343   4.148   1.00 9.56  ?  94  HIS   A CG   1 
ATOM   2006 N  ND1  . HIS   A 1 94  ? 28.952 1.402   4.095   1.00 9.55  ?  94  HIS   A ND1  1 
ATOM   2007 C  CD2  . HIS   A 1 94  ? 30.577 0.518   5.264   1.00 10.26 ?  94  HIS   A CD2  1 
ATOM   2008 C  CE1  . HIS   A 1 94  ? 29.168 2.187   5.135   1.00 9.84  ?  94  HIS   A CE1  1 
ATOM   2009 N  NE2  . HIS   A 1 94  ? 30.144 1.672   5.860   1.00 10.26 ?  94  HIS   A NE2  1 
ATOM   2010 H  H    . HIS   A 1 94  ? 30.145 -2.470  4.863   1.00 11.58 ?  94  HIS   A H    1 
ATOM   2011 H  HA   . HIS   A 1 94  ? 27.987 -1.539  3.564   1.00 11.67 ?  94  HIS   A HA   1 
ATOM   2012 H  HB2  . HIS   A 1 94  ? 30.747 -1.105  3.095   1.00 11.45 ?  94  HIS   A HB2  1 
ATOM   2013 H  HB3  . HIS   A 1 94  ? 29.598 -0.369  2.281   1.00 11.45 ?  94  HIS   A HB3  1 
ATOM   2014 H  HD2  . HIS   A 1 94  ? 31.252 -0.034  5.571   1.00 12.45 ?  94  HIS   A HD2  1 
ATOM   2015 H  HE1  . HIS   A 1 94  ? 28.694 2.970   5.322   1.00 11.95 ?  94  HIS   A HE1  1 
ATOM   2016 H  HE2  . HIS   A 1 94  ? 30.454 2.020   6.580   1.00 12.45 ?  94  HIS   A HE2  1 
ATOM   2017 N  N    . VAL   A 1 95  ? 27.726 -3.259  1.805   1.00 9.05  ?  95  VAL   A N    1 
ATOM   2018 C  CA   . VAL   A 1 95  ? 27.585 -4.293  0.783   1.00 9.29  ?  95  VAL   A CA   1 
ATOM   2019 C  C    . VAL   A 1 95  ? 27.033 -3.657  -0.480  1.00 8.97  ?  95  VAL   A C    1 
ATOM   2020 O  O    . VAL   A 1 95  ? 26.030 -2.934  -0.425  1.00 9.97  ?  95  VAL   A O    1 
ATOM   2021 C  CB   . VAL   A 1 95  ? 26.657 -5.434  1.237   1.00 9.93  ?  95  VAL   A CB   1 
ATOM   2022 C  CG1  . VAL   A 1 95  ? 26.556 -6.480  0.137   1.00 10.61 ?  95  VAL   A CG1  1 
ATOM   2023 C  CG2  . VAL   A 1 95  ? 27.157 -6.049  2.527   1.00 10.38 ?  95  VAL   A CG2  1 
ATOM   2024 H  H    . VAL   A 1 95  ? 26.976 -2.895  2.023   1.00 11.01 ?  95  VAL   A H    1 
ATOM   2025 H  HA   . VAL   A 1 95  ? 28.454 -4.668  0.579   1.00 11.28 ?  95  VAL   A HA   1 
ATOM   2026 H  HB   . VAL   A 1 95  ? 25.772 -5.083  1.393   1.00 12.05 ?  95  VAL   A HB   1 
ATOM   2027 H  HG11 . VAL   A 1 95  ? 26.166 -7.295  0.504   1.00 12.88 ?  95  VAL   A HG11 1 
ATOM   2028 H  HG12 . VAL   A 1 95  ? 25.993 -6.147  -0.580  1.00 12.88 ?  95  VAL   A HG12 1 
ATOM   2029 H  HG13 . VAL   A 1 95  ? 27.445 -6.678  -0.206  1.00 12.88 ?  95  VAL   A HG13 1 
ATOM   2030 H  HG21 . VAL   A 1 95  ? 26.594 -6.811  2.751   1.00 12.60 ?  95  VAL   A HG21 1 
ATOM   2031 H  HG22 . VAL   A 1 95  ? 28.072 -6.337  2.411   1.00 12.60 ?  95  VAL   A HG22 1 
ATOM   2032 H  HG23 . VAL   A 1 95  ? 27.102 -5.384  3.231   1.00 12.60 ?  95  VAL   A HG23 1 
ATOM   2033 N  N    A VAL   A 1 96  ? 27.670 -3.944  -1.614  0.74 9.06  ?  96  VAL   A N    1 
ATOM   2034 N  N    B VAL   A 1 96  ? 27.663 -3.925  -1.617  0.26 9.15  ?  96  VAL   A N    1 
ATOM   2035 C  CA   A VAL   A 1 96  ? 27.265 -3.410  -2.908  0.74 9.76  ?  96  VAL   A CA   1 
ATOM   2036 C  CA   B VAL   A 1 96  ? 27.250 -3.329  -2.883  0.26 9.68  ?  96  VAL   A CA   1 
ATOM   2037 C  C    A VAL   A 1 96  ? 26.460 -4.474  -3.647  0.74 10.08 ?  96  VAL   A C    1 
ATOM   2038 C  C    B VAL   A 1 96  ? 26.450 -4.360  -3.673  0.26 9.86  ?  96  VAL   A C    1 
ATOM   2039 O  O    A VAL   A 1 96  ? 27.019 -5.425  -4.202  0.74 11.14 ?  96  VAL   A O    1 
ATOM   2040 O  O    B VAL   A 1 96  ? 27.013 -5.294  -4.253  0.26 10.23 ?  96  VAL   A O    1 
ATOM   2041 C  CB   A VAL   A 1 96  ? 28.463 -2.951  -3.739  0.74 10.08 ?  96  VAL   A CB   1 
ATOM   2042 C  CB   B VAL   A 1 96  ? 28.440 -2.799  -3.684  0.26 9.92  ?  96  VAL   A CB   1 
ATOM   2043 C  CG1  A VAL   A 1 96  ? 27.967 -2.310  -5.022  0.74 10.77 ?  96  VAL   A CG1  1 
ATOM   2044 C  CG1  B VAL   A 1 96  ? 27.948 -2.172  -4.976  0.26 10.14 ?  96  VAL   A CG1  1 
ATOM   2045 C  CG2  A VAL   A 1 96  ? 29.349 -1.995  -2.946  0.74 10.48 ?  96  VAL   A CG2  1 
ATOM   2046 C  CG2  B VAL   A 1 96  ? 29.225 -1.792  -2.861  0.26 10.19 ?  96  VAL   A CG2  1 
ATOM   2047 H  H    A VAL   A 1 96  ? 28.365 -4.457  -1.655  0.74 11.01 ?  96  VAL   A H    1 
ATOM   2048 H  H    B VAL   A 1 96  ? 28.349 -4.446  -1.680  0.26 11.12 ?  96  VAL   A H    1 
ATOM   2049 H  HA   A VAL   A 1 96  ? 26.694 -2.644  -2.767  0.74 11.85 ?  96  VAL   A HA   1 
ATOM   2050 H  HA   B VAL   A 1 96  ? 26.662 -2.583  -2.695  0.26 11.76 ?  96  VAL   A HA   1 
ATOM   2051 H  HB   A VAL   A 1 96  ? 29.001 -3.721  -3.980  0.74 12.24 ?  96  VAL   A HB   1 
ATOM   2052 H  HB   B VAL   A 1 96  ? 29.028 -3.537  -3.910  0.26 12.05 ?  96  VAL   A HB   1 
ATOM   2053 H  HG11 A VAL   A 1 96  ? 28.714 -1.862  -5.458  0.74 13.06 ?  96  VAL   A HG11 1 
ATOM   2054 H  HG11 B VAL   A 1 96  ? 28.672 -1.658  -5.365  0.26 12.30 ?  96  VAL   A HG11 1 
ATOM   2055 H  HG12 A VAL   A 1 96  ? 27.614 -2.996  -5.606  0.74 13.06 ?  96  VAL   A HG12 1 
ATOM   2056 H  HG12 B VAL   A 1 96  ? 27.675 -2.872  -5.587  0.26 12.30 ?  96  VAL   A HG12 1 
ATOM   2057 H  HG13 A VAL   A 1 96  ? 27.280 -1.663  -4.807  0.74 13.06 ?  96  VAL   A HG13 1 
ATOM   2058 H  HG13 B VAL   A 1 96  ? 27.199 -1.589  -4.778  0.26 12.30 ?  96  VAL   A HG13 1 
ATOM   2059 H  HG21 A VAL   A 1 96  ? 30.050 -1.656  -3.522  0.74 12.72 ?  96  VAL   A HG21 1 
ATOM   2060 H  HG21 B VAL   A 1 96  ? 29.934 -1.423  -3.407  0.26 12.37 ?  96  VAL   A HG21 1 
ATOM   2061 H  HG22 A VAL   A 1 96  ? 28.807 -1.261  -2.615  0.74 12.72 ?  96  VAL   A HG22 1 
ATOM   2062 H  HG22 B VAL   A 1 96  ? 28.625 -1.086  -2.572  0.26 12.37 ?  96  VAL   A HG22 1 
ATOM   2063 H  HG23 A VAL   A 1 96  ? 29.742 -2.475  -2.197  0.74 12.72 ?  96  VAL   A HG23 1 
ATOM   2064 H  HG23 B VAL   A 1 96  ? 29.602 -2.242  -2.088  0.26 12.37 ?  96  VAL   A HG23 1 
ATOM   2065 N  N    A GLY   A 1 97  ? 25.142 -4.312  -3.679  0.74 10.18 ?  97  GLY   A N    1 
ATOM   2066 N  N    B GLY   A 1 97  ? 25.132 -4.181  -3.715  0.26 10.31 ?  97  GLY   A N    1 
ATOM   2067 C  CA   A GLY   A 1 97  ? 24.329 -5.067  -4.597  0.74 10.83 ?  97  GLY   A CA   1 
ATOM   2068 C  CA   B GLY   A 1 97  ? 24.294 -4.966  -4.587  0.26 10.63 ?  97  GLY   A CA   1 
ATOM   2069 C  C    A GLY   A 1 97  ? 24.341 -4.399  -5.957  0.74 10.96 ?  97  GLY   A C    1 
ATOM   2070 C  C    B GLY   A 1 97  ? 24.275 -4.384  -5.988  0.26 10.74 ?  97  GLY   A C    1 
ATOM   2071 O  O    A GLY   A 1 97  ? 24.668 -3.215  -6.077  0.74 11.76 ?  97  GLY   A O    1 
ATOM   2072 O  O    B GLY   A 1 97  ? 24.451 -3.178  -6.181  0.26 10.87 ?  97  GLY   A O    1 
ATOM   2073 H  H    A GLY   A 1 97  ? 24.703 -3.769  -3.173  0.74 12.35 ?  97  GLY   A H    1 
ATOM   2074 H  H    B GLY   A 1 97  ? 24.699 -3.607  -3.237  0.26 12.51 ?  97  GLY   A H    1 
ATOM   2075 H  HA2  A GLY   A 1 97  ? 24.680 -5.964  -4.682  0.74 13.13 ?  97  GLY   A HA2  1 
ATOM   2076 H  HA2  B GLY   A 1 97  ? 24.631 -5.874  -4.619  0.26 12.90 ?  97  GLY   A HA2  1 
ATOM   2077 H  HA3  A GLY   A 1 97  ? 23.417 -5.111  -4.272  0.74 13.13 ?  97  GLY   A HA3  1 
ATOM   2078 H  HA3  B GLY   A 1 97  ? 23.385 -4.983  -4.242  0.26 12.90 ?  97  GLY   A HA3  1 
ATOM   2079 N  N    A PRO   A 1 98  ? 23.983 -5.134  -7.007  0.74 11.07 ?  98  PRO   A N    1 
ATOM   2080 N  N    B PRO   A 1 98  ? 24.059 -5.228  -6.995  0.26 10.96 ?  98  PRO   A N    1 
ATOM   2081 C  CA   A PRO   A 1 98  ? 23.866 -4.504  -8.327  0.74 12.03 ?  98  PRO   A CA   1 
ATOM   2082 C  CA   B PRO   A 1 98  ? 24.029 -4.726  -8.373  0.26 11.59 ?  98  PRO   A CA   1 
ATOM   2083 C  C    A PRO   A 1 98  ? 22.750 -3.466  -8.350  0.74 12.09 ?  98  PRO   A C    1 
ATOM   2084 C  C    B PRO   A 1 98  ? 22.907 -3.716  -8.573  0.26 11.82 ?  98  PRO   A C    1 
ATOM   2085 O  O    A PRO   A 1 98  ? 21.678 -3.657  -7.768  0.74 12.09 ?  98  PRO   A O    1 
ATOM   2086 O  O    B PRO   A 1 98  ? 21.823 -3.834  -7.998  0.26 12.23 ?  98  PRO   A O    1 
ATOM   2087 C  CB   A PRO   A 1 98  ? 23.562 -5.687  -9.257  0.74 12.19 ?  98  PRO   A CB   1 
ATOM   2088 C  CB   B PRO   A 1 98  ? 23.799 -5.993  -9.205  0.26 11.57 ?  98  PRO   A CB   1 
ATOM   2089 C  CG   A PRO   A 1 98  ? 22.943 -6.722  -8.365  0.74 12.51 ?  98  PRO   A CG   1 
ATOM   2090 C  CG   B PRO   A 1 98  ? 23.150 -6.955  -8.256  0.26 11.76 ?  98  PRO   A CG   1 
ATOM   2091 C  CD   A PRO   A 1 98  ? 23.665 -6.574  -7.046  0.74 11.71 ?  98  PRO   A CD   1 
ATOM   2092 C  CD   B PRO   A 1 98  ? 23.788 -6.675  -6.929  0.26 11.07 ?  98  PRO   A CD   1 
ATOM   2093 H  HA   A PRO   A 1 98  ? 24.706 -4.096  -8.585  0.74 14.58 ?  98  PRO   A HA   1 
ATOM   2094 H  HA   B PRO   A 1 98  ? 24.881 -4.325  -8.611  0.26 14.05 ?  98  PRO   A HA   1 
ATOM   2095 H  HB2  A PRO   A 1 98  ? 22.938 -5.413  -9.943  0.74 14.77 ?  98  PRO   A HB2  1 
ATOM   2096 H  HB2  B PRO   A 1 98  ? 23.213 -5.791  -9.951  0.26 14.02 ?  98  PRO   A HB2  1 
ATOM   2097 H  HB3  A PRO   A 1 98  ? 24.385 -6.021  -9.648  0.74 14.77 ?  98  PRO   A HB3  1 
ATOM   2098 H  HB3  B PRO   A 1 98  ? 24.650 -6.338  -9.518  0.26 14.02 ?  98  PRO   A HB3  1 
ATOM   2099 H  HG2  A PRO   A 1 98  ? 21.998 -6.544  -8.261  0.74 15.16 ?  98  PRO   A HG2  1 
ATOM   2100 H  HG2  B PRO   A 1 98  ? 22.195 -6.782  -8.222  0.26 14.26 ?  98  PRO   A HG2  1 
ATOM   2101 H  HG3  A PRO   A 1 98  ? 23.091 -7.607  -8.736  0.74 15.16 ?  98  PRO   A HG3  1 
ATOM   2102 H  HG3  B PRO   A 1 98  ? 23.327 -7.863  -8.540  0.26 14.26 ?  98  PRO   A HG3  1 
ATOM   2103 H  HD2  A PRO   A 1 98  ? 23.078 -6.815  -6.307  0.74 14.19 ?  98  PRO   A HD2  1 
ATOM   2104 H  HD2  B PRO   A 1 98  ? 23.173 -6.875  -6.206  0.26 13.43 ?  98  PRO   A HD2  1 
ATOM   2105 H  HD3  A PRO   A 1 98  ? 24.479 -7.102  -7.036  0.74 14.19 ?  98  PRO   A HD3  1 
ATOM   2106 H  HD3  B PRO   A 1 98  ? 24.618 -7.169  -6.838  0.26 13.43 ?  98  PRO   A HD3  1 
ATOM   2107 N  N    A ASN   A 1 99  ? 23.016 -2.351  -9.026  0.74 12.79 ?  99  ASN   A N    1 
ATOM   2108 N  N    B ASN   A 1 99  ? 23.180 -2.712  -9.402  0.26 11.92 ?  99  ASN   A N    1 
ATOM   2109 C  CA   A ASN   A 1 99  ? 22.031 -1.297  -9.247  0.74 14.17 ?  99  ASN   A CA   1 
ATOM   2110 C  CA   B ASN   A 1 99  ? 22.225 -1.650  -9.701  0.26 12.44 ?  99  ASN   A CA   1 
ATOM   2111 C  C    A ASN   A 1 99  ? 21.485 -1.461  -10.661 0.74 15.86 ?  99  ASN   A C    1 
ATOM   2112 C  C    B ASN   A 1 99  ? 21.564 -1.957  -11.037 0.26 13.30 ?  99  ASN   A C    1 
ATOM   2113 O  O    A ASN   A 1 99  ? 22.179 -1.173  -11.645 0.74 16.77 ?  99  ASN   A O    1 
ATOM   2114 O  O    B ASN   A 1 99  ? 22.217 -1.918  -12.086 0.26 13.08 ?  99  ASN   A O    1 
ATOM   2115 C  CB   A ASN   A 1 99  ? 22.669 0.079   -9.064  0.74 14.11 ?  99  ASN   A CB   1 
ATOM   2116 C  CB   B ASN   A 1 99  ? 22.922 -0.295  -9.752  0.26 12.85 ?  99  ASN   A CB   1 
ATOM   2117 C  CG   A ASN   A 1 99  ? 21.646 1.216   -9.048  0.74 14.21 ?  99  ASN   A CG   1 
ATOM   2118 C  CG   B ASN   A 1 99  ? 21.948 0.854   -9.920  0.26 13.38 ?  99  ASN   A CG   1 
ATOM   2119 O  OD1  A ASN   A 1 99  ? 20.639 1.172   -9.753  0.74 14.83 ?  99  ASN   A OD1  1 
ATOM   2120 O  OD1  B ASN   A 1 99  ? 20.946 0.729   -10.620 0.26 13.14 ?  99  ASN   A OD1  1 
ATOM   2121 N  ND2  A ASN   A 1 99  ? 21.914 2.243   -8.248  0.74 14.73 ?  99  ASN   A ND2  1 
ATOM   2122 N  ND2  B ASN   A 1 99  ? 22.239 1.982   -9.273  0.26 14.20 ?  99  ASN   A ND2  1 
ATOM   2123 H  H    A ASN   A 1 99  ? 23.786 -2.177  -9.363  0.74 15.49 ?  99  ASN   A H    1 
ATOM   2124 H  H    B ASN   A 1 99  ? 23.931 -2.620  -9.805  0.26 14.44 ?  99  ASN   A H    1 
ATOM   2125 H  HA   A ASN   A 1 99  ? 21.299 -1.396  -8.611  0.74 17.14 ?  99  ASN   A HA   1 
ATOM   2126 H  HA   B ASN   A 1 99  ? 21.537 -1.629  -9.014  0.26 15.07 ?  99  ASN   A HA   1 
ATOM   2127 H  HB2  A ASN   A 1 99  ? 23.153 0.092   -8.228  0.74 17.08 ?  99  ASN   A HB2  1 
ATOM   2128 H  HB2  B ASN   A 1 99  ? 23.406 -0.158  -8.930  0.26 15.56 ?  99  ASN   A HB2  1 
ATOM   2129 H  HB3  A ASN   A 1 99  ? 23.279 0.234   -9.805  0.74 17.08 ?  99  ASN   A HB3  1 
ATOM   2130 H  HB3  B ASN   A 1 99  ? 23.527 -0.284  -10.507 0.26 15.56 ?  99  ASN   A HB3  1 
ATOM   2131 H  HD21 A ASN   A 1 99  ? 21.369 2.904   -8.204  0.74 17.82 ?  99  ASN   A HD21 1 
ATOM   2132 H  HD21 B ASN   A 1 99  ? 21.719 2.666   -9.328  0.26 17.18 ?  99  ASN   A HD21 1 
ATOM   2133 H  HD22 A ASN   A 1 99  ? 22.631 2.239   -7.774  0.74 17.82 ?  99  ASN   A HD22 1 
ATOM   2134 H  HD22 B ASN   A 1 99  ? 22.952 2.025   -8.793  0.26 17.18 ?  99  ASN   A HD22 1 
ATOM   2135 N  N    A VAL   A 1 100 ? 20.239 -1.934  -10.756 0.74 17.42 ?  100 VAL   A N    1 
ATOM   2136 N  N    B VAL   A 1 100 ? 20.258 -2.223  -10.993 0.26 15.17 ?  100 VAL   A N    1 
ATOM   2137 C  CA   A VAL   A 1 100 ? 19.626 -2.174  -12.060 0.74 19.53 ?  100 VAL   A CA   1 
ATOM   2138 C  CA   B VAL   A 1 100 ? 19.519 -2.596  -12.195 0.26 17.08 ?  100 VAL   A CA   1 
ATOM   2139 C  C    A VAL   A 1 100 ? 19.503 -0.876  -12.844 0.74 20.14 ?  100 VAL   A C    1 
ATOM   2140 C  C    B VAL   A 1 100 ? 19.499 -1.445  -13.186 0.26 17.64 ?  100 VAL   A C    1 
ATOM   2141 O  O    A VAL   A 1 100 ? 19.586 -0.873  -14.078 0.74 20.96 ?  100 VAL   A O    1 
ATOM   2142 O  O    B VAL   A 1 100 ? 19.589 -1.653  -14.402 0.26 17.51 ?  100 VAL   A O    1 
ATOM   2143 C  CB   A VAL   A 1 100 ? 18.276 -2.904  -11.891 0.74 20.99 ?  100 VAL   A CB   1 
ATOM   2144 C  CB   B VAL   A 1 100 ? 18.097 -3.047  -11.818 0.26 18.24 ?  100 VAL   A CB   1 
ATOM   2145 C  CG1  A VAL   A 1 100 ? 17.556 -3.053  -13.229 0.74 21.39 ?  100 VAL   A CG1  1 
ATOM   2146 C  CG1  B VAL   A 1 100 ? 17.419 -3.721  -12.999 0.26 18.46 ?  100 VAL   A CG1  1 
ATOM   2147 C  CG2  A VAL   A 1 100 ? 18.499 -4.272  -11.258 0.74 21.11 ?  100 VAL   A CG2  1 
ATOM   2148 C  CG2  B VAL   A 1 100 ? 18.154 -3.970  -10.620 0.26 18.77 ?  100 VAL   A CG2  1 
ATOM   2149 H  H    A VAL   A 1 100 ? 19.722 -2.121  -10.084 0.74 21.05 ?  100 VAL   A H    1 
ATOM   2150 H  H    B VAL   A 1 100 ? 19.777 -2.181  -10.284 0.26 18.35 ?  100 VAL   A H    1 
ATOM   2151 H  HA   A VAL   A 1 100 ? 20.201 -2.767  -12.565 0.74 23.57 ?  100 VAL   A HA   1 
ATOM   2152 H  HA   B VAL   A 1 100 ? 19.962 -3.334  -12.630 0.26 20.64 ?  100 VAL   A HA   1 
ATOM   2153 H  HB   A VAL   A 1 100 ? 17.702 -2.394  -11.300 0.74 25.33 ?  100 VAL   A HB   1 
ATOM   2154 H  HB   B VAL   A 1 100 ? 17.570 -2.268  -11.575 0.26 22.02 ?  100 VAL   A HB   1 
ATOM   2155 H  HG11 A VAL   A 1 100 ? 16.817 -3.677  -13.126 0.74 25.81 ?  100 VAL   A HG11 1 
ATOM   2156 H  HG11 B VAL   A 1 100 ? 16.543 -4.031  -12.723 0.26 22.29 ?  100 VAL   A HG11 1 
ATOM   2157 H  HG12 A VAL   A 1 100 ? 17.217 -2.188  -13.506 0.74 25.81 ?  100 VAL   A HG12 1 
ATOM   2158 H  HG12 B VAL   A 1 100 ? 17.330 -3.079  -13.722 0.26 22.29 ?  100 VAL   A HG12 1 
ATOM   2159 H  HG13 A VAL   A 1 100 ? 18.181 -3.393  -13.889 0.74 25.81 ?  100 VAL   A HG13 1 
ATOM   2160 H  HG13 B VAL   A 1 100 ? 17.962 -4.471  -13.287 0.26 22.29 ?  100 VAL   A HG13 1 
ATOM   2161 H  HG21 A VAL   A 1 100 ? 17.650 -4.740  -11.198 0.74 25.47 ?  100 VAL   A HG21 1 
ATOM   2162 H  HG21 B VAL   A 1 100 ? 17.347 -4.499  -10.593 0.26 22.67 ?  100 VAL   A HG21 1 
ATOM   2163 H  HG22 A VAL   A 1 100 ? 19.117 -4.779  -11.808 0.74 25.47 ?  100 VAL   A HG22 1 
ATOM   2164 H  HG22 B VAL   A 1 100 ? 18.930 -4.545  -10.709 0.26 22.67 ?  100 VAL   A HG22 1 
ATOM   2165 H  HG23 A VAL   A 1 100 ? 18.871 -4.152  -10.370 0.74 25.47 ?  100 VAL   A HG23 1 
ATOM   2166 H  HG23 B VAL   A 1 100 ? 18.231 -3.434  -9.814  0.26 22.67 ?  100 VAL   A HG23 1 
ATOM   2167 N  N    A ASN   A 1 101 ? 19.315 0.245   -12.155 0.74 20.98 ?  101 ASN   A N    1 
ATOM   2168 N  N    B ASN   A 1 101 ? 19.375 -0.214  -12.682 0.26 18.14 ?  101 ASN   A N    1 
ATOM   2169 C  CA   A ASN   A 1 101 ? 19.255 1.527   -12.847 0.74 22.32 ?  101 ASN   A CA   1 
ATOM   2170 C  CA   B ASN   A 1 101 ? 19.319 0.952   -13.558 0.26 18.45 ?  101 ASN   A CA   1 
ATOM   2171 C  C    A ASN   A 1 101 ? 20.613 1.969   -13.393 0.74 24.74 ?  101 ASN   A C    1 
ATOM   2172 C  C    B ASN   A 1 101 ? 20.641 1.170   -14.280 0.26 19.19 ?  101 ASN   A C    1 
ATOM   2173 O  O    A ASN   A 1 101 ? 20.690 3.038   -14.013 0.74 26.31 ?  101 ASN   A O    1 
ATOM   2174 O  O    B ASN   A 1 101 ? 20.661 1.764   -15.364 0.26 18.94 ?  101 ASN   A O    1 
ATOM   2175 C  CB   A ASN   A 1 101 ? 18.636 2.578   -11.923 0.74 21.85 ?  101 ASN   A CB   1 
ATOM   2176 C  CB   B ASN   A 1 101 ? 18.927 2.189   -12.745 0.26 18.04 ?  101 ASN   A CB   1 
ATOM   2177 C  CG   A ASN   A 1 101 ? 17.258 2.163   -11.416 0.74 21.52 ?  101 ASN   A CG   1 
ATOM   2178 C  CG   B ASN   A 1 101 ? 17.768 1.919   -11.797 0.26 18.08 ?  101 ASN   A CG   1 
ATOM   2179 O  OD1  A ASN   A 1 101 ? 16.423 1.671   -12.180 0.74 21.96 ?  101 ASN   A OD1  1 
ATOM   2180 O  OD1  B ASN   A 1 101 ? 16.789 1.265   -12.161 0.26 18.17 ?  101 ASN   A OD1  1 
ATOM   2181 N  ND2  A ASN   A 1 101 ? 17.024 2.341   -10.121 0.74 21.37 ?  101 ASN   A ND2  1 
ATOM   2182 N  ND2  B ASN   A 1 101 ? 17.883 2.408   -10.568 0.26 18.23 ?  101 ASN   A ND2  1 
ATOM   2183 H  H    A ASN   A 1 101 ? 19.207 0.287   -11.308 0.74 25.32 ?  101 ASN   A H    1 
ATOM   2184 H  H    B ASN   A 1 101 ? 19.322 -0.024  -11.843 0.26 21.91 ?  101 ASN   A H    1 
ATOM   2185 H  HA   A ASN   A 1 101 ? 18.662 1.432   -13.608 0.74 26.93 ?  101 ASN   A HA   1 
ATOM   2186 H  HA   B ASN   A 1 101 ? 18.641 0.821   -14.233 0.26 22.28 ?  101 ASN   A HA   1 
ATOM   2187 H  HB2  A ASN   A 1 101 ? 19.216 2.711   -11.159 0.74 26.36 ?  101 ASN   A HB2  1 
ATOM   2188 H  HB2  B ASN   A 1 101 ? 19.683 2.483   -12.212 0.26 21.79 ?  101 ASN   A HB2  1 
ATOM   2189 H  HB3  A ASN   A 1 101 ? 18.541 3.412   -12.417 0.74 26.36 ?  101 ASN   A HB3  1 
ATOM   2190 H  HB3  B ASN   A 1 101 ? 18.655 2.903   -13.349 0.26 21.79 ?  101 ASN   A HB3  1 
ATOM   2191 H  HD21 A ASN   A 1 101 ? 16.262 2.124   -9.789  0.74 25.79 ?  101 ASN   A HD21 1 
ATOM   2192 H  HD21 B ASN   A 1 101 ? 17.254 2.282   -9.994  0.26 22.01 ?  101 ASN   A HD21 1 
ATOM   2193 H  HD22 A ASN   A 1 101 ? 17.630 2.685   -9.618  0.74 25.79 ?  101 ASN   A HD22 1 
ATOM   2194 H  HD22 B ASN   A 1 101 ? 18.582 2.857   -10.346 0.26 22.01 ?  101 ASN   A HD22 1 
ATOM   2195 N  N    A LYS   A 1 102 ? 21.667 1.169   -13.190 0.74 26.40 ?  102 LYS   A N    1 
ATOM   2196 N  N    B LYS   A 1 102 ? 21.743 0.699   -13.704 0.26 20.46 ?  102 LYS   A N    1 
ATOM   2197 C  CA   A LYS   A 1 102 ? 22.964 1.364   -13.829 0.74 27.78 ?  102 LYS   A CA   1 
ATOM   2198 C  CA   B LYS   A 1 102 ? 23.055 0.780   -14.329 0.26 21.40 ?  102 LYS   A CA   1 
ATOM   2199 C  C    A LYS   A 1 102 ? 23.299 0.268   -14.833 0.74 27.96 ?  102 LYS   A C    1 
ATOM   2200 C  C    B LYS   A 1 102 ? 23.359 -0.432  -15.202 0.26 21.07 ?  102 LYS   A C    1 
ATOM   2201 O  O    A LYS   A 1 102 ? 24.391 0.294   -15.410 0.74 28.36 ?  102 LYS   A O    1 
ATOM   2202 O  O    B LYS   A 1 102 ? 24.483 -0.560  -15.697 0.26 20.74 ?  102 LYS   A O    1 
ATOM   2203 C  CB   A LYS   A 1 102 ? 24.080 1.420   -12.778 0.74 29.21 ?  102 LYS   A CB   1 
ATOM   2204 C  CB   B LYS   A 1 102 ? 24.140 0.918   -13.257 0.26 22.96 ?  102 LYS   A CB   1 
ATOM   2205 C  CG   A LYS   A 1 102 ? 23.969 2.559   -11.785 0.74 30.33 ?  102 LYS   A CG   1 
ATOM   2206 C  CG   B LYS   A 1 102 ? 24.276 2.315   -12.671 0.26 24.39 ?  102 LYS   A CG   1 
ATOM   2207 C  CD   A LYS   A 1 102 ? 25.131 2.525   -10.800 0.74 31.57 ?  102 LYS   A CD   1 
ATOM   2208 C  CD   B LYS   A 1 102 ? 24.965 2.272   -11.315 0.26 25.75 ?  102 LYS   A CD   1 
ATOM   2209 C  CE   A LYS   A 1 102 ? 25.056 3.668   -9.802  0.74 32.54 ?  102 LYS   A CE   1 
ATOM   2210 C  CE   B LYS   A 1 102 ? 25.288 3.662   -10.795 0.26 26.78 ?  102 LYS   A CE   1 
ATOM   2211 N  NZ   A LYS   A 1 102 ? 26.149 3.589   -8.790  0.74 32.99 ?  102 LYS   A NZ   1 
ATOM   2212 N  NZ   B LYS   A 1 102 ? 26.752 3.936   -10.838 0.26 27.34 ?  102 LYS   A NZ   1 
ATOM   2213 H  H    A LYS   A 1 102 ? 21.654 0.481   -12.670 0.74 31.82 ?  102 LYS   A H    1 
ATOM   2214 H  H    B LYS   A 1 102 ? 21.752 0.317   -12.934 0.26 24.69 ?  102 LYS   A H    1 
ATOM   2215 H  HA   A LYS   A 1 102 ? 22.959 2.204   -14.305 0.74 33.48 ?  102 LYS   A HA   1 
ATOM   2216 H  HA   B LYS   A 1 102 ? 23.088 1.578   -14.881 0.26 25.83 ?  102 LYS   A HA   1 
ATOM   2217 H  HB2  A LYS   A 1 102 ? 24.074 0.591   -12.275 0.74 35.19 ?  102 LYS   A HB2  1 
ATOM   2218 H  HB2  B LYS   A 1 102 ? 23.935 0.311   -12.529 0.26 27.69 ?  102 LYS   A HB2  1 
ATOM   2219 H  HB3  A LYS   A 1 102 ? 24.931 1.513   -13.236 0.74 35.19 ?  102 LYS   A HB3  1 
ATOM   2220 H  HB3  B LYS   A 1 102 ? 24.994 0.679   -13.648 0.26 27.69 ?  102 LYS   A HB3  1 
ATOM   2221 H  HG2  A LYS   A 1 102 ? 23.993 3.404   -12.260 0.74 36.54 ?  102 LYS   A HG2  1 
ATOM   2222 H  HG2  B LYS   A 1 102 ? 24.812 2.864   -13.268 0.26 29.41 ?  102 LYS   A HG2  1 
ATOM   2223 H  HG3  A LYS   A 1 102 ? 23.141 2.472   -11.288 0.74 36.54 ?  102 LYS   A HG3  1 
ATOM   2224 H  HG3  B LYS   A 1 102 ? 23.396 2.706   -12.556 0.26 29.41 ?  102 LYS   A HG3  1 
ATOM   2225 H  HD2  A LYS   A 1 102 ? 25.107 1.689   -10.307 0.74 38.02 ?  102 LYS   A HD2  1 
ATOM   2226 H  HD2  B LYS   A 1 102 ? 24.381 1.839   -10.675 0.26 31.05 ?  102 LYS   A HD2  1 
ATOM   2227 H  HD3  A LYS   A 1 102 ? 25.966 2.601   -11.289 0.74 38.02 ?  102 LYS   A HD3  1 
ATOM   2228 H  HD3  B LYS   A 1 102 ? 25.795 1.779   -11.396 0.26 31.05 ?  102 LYS   A HD3  1 
ATOM   2229 H  HE2  A LYS   A 1 102 ? 25.141 4.511   -10.277 0.74 39.19 ?  102 LYS   A HE2  1 
ATOM   2230 H  HE2  B LYS   A 1 102 ? 24.839 4.322   -11.346 0.26 32.28 ?  102 LYS   A HE2  1 
ATOM   2231 H  HE3  A LYS   A 1 102 ? 24.205 3.631   -9.337  0.74 39.19 ?  102 LYS   A HE3  1 
ATOM   2232 H  HE3  B LYS   A 1 102 ? 24.992 3.736   -9.874  0.26 32.28 ?  102 LYS   A HE3  1 
ATOM   2233 H  HZ1  A LYS   A 1 102 ? 26.085 4.267   -8.219  0.74 39.73 ?  102 LYS   A HZ1  1 
ATOM   2234 H  HZ1  B LYS   A 1 102 ? 26.918 4.753   -10.529 0.26 32.95 ?  102 LYS   A HZ1  1 
ATOM   2235 H  HZ2  A LYS   A 1 102 ? 26.090 2.823   -8.340  0.74 39.73 ?  102 LYS   A HZ2  1 
ATOM   2236 H  HZ2  B LYS   A 1 102 ? 27.187 3.343   -10.336 0.26 32.95 ?  102 LYS   A HZ2  1 
ATOM   2237 H  HZ3  A LYS   A 1 102 ? 26.941 3.625   -9.195  0.74 39.73 ?  102 LYS   A HZ3  1 
ATOM   2238 H  HZ3  B LYS   A 1 102 ? 27.048 3.876   -11.675 0.26 32.95 ?  102 LYS   A HZ3  1 
ATOM   2239 N  N    A GLY   A 1 103 ? 22.409 -0.700  -15.042 0.74 28.39 ?  103 GLY   A N    1 
ATOM   2240 N  N    B GLY   A 1 103 ? 22.393 -1.331  -15.387 0.26 21.09 ?  103 GLY   A N    1 
ATOM   2241 C  CA   A GLY   A 1 103 ? 22.671 -1.784  -15.969 0.74 28.26 ?  103 GLY   A CA   1 
ATOM   2242 C  CA   B GLY   A 1 103 ? 22.626 -2.509  -16.196 0.26 20.88 ?  103 GLY   A CA   1 
ATOM   2243 C  C    A GLY   A 1 103 ? 23.513 -2.912  -15.419 0.74 28.11 ?  103 GLY   A C    1 
ATOM   2244 C  C    B GLY   A 1 103 ? 23.504 -3.558  -15.554 0.26 20.34 ?  103 GLY   A C    1 
ATOM   2245 O  O    A GLY   A 1 103 ? 24.109 -3.659  -16.202 0.74 29.09 ?  103 GLY   A O    1 
ATOM   2246 O  O    B GLY   A 1 103 ? 23.950 -4.480  -16.244 0.26 20.34 ?  103 GLY   A O    1 
ATOM   2247 H  H    A GLY   A 1 103 ? 21.647 -0.754  -14.654 0.74 34.21 ?  103 GLY   A H    1 
ATOM   2248 H  H    B GLY   A 1 103 ? 21.601 -1.279  -15.048 0.26 25.45 ?  103 GLY   A H    1 
ATOM   2249 H  HA2  A GLY   A 1 103 ? 21.824 -2.153  -16.275 0.74 34.05 ?  103 GLY   A HA2  1 
ATOM   2250 H  HA2  B GLY   A 1 103 ? 21.777 -2.925  -16.398 0.26 25.20 ?  103 GLY   A HA2  1 
ATOM   2251 H  HA3  A GLY   A 1 103 ? 23.139 -1.434  -16.742 0.74 34.05 ?  103 GLY   A HA3  1 
ATOM   2252 H  HA3  B GLY   A 1 103 ? 23.033 -2.231  -17.034 0.26 25.20 ?  103 GLY   A HA3  1 
ATOM   2253 N  N    A GLU   A 1 104 ? 23.585 -3.065  -14.100 0.74 26.20 ?  104 GLU   A N    1 
ATOM   2254 N  N    B GLU   A 1 104 ? 23.755 -3.454  -14.253 0.26 19.68 ?  104 GLU   A N    1 
ATOM   2255 C  CA   A GLU   A 1 104 ? 24.453 -4.064  -13.492 0.74 24.28 ?  104 GLU   A CA   1 
ATOM   2256 C  CA   B GLU   A 1 104 ? 24.652 -4.385  -13.584 0.26 19.06 ?  104 GLU   A CA   1 
ATOM   2257 C  C    A GLU   A 1 104 ? 23.764 -5.425  -13.400 0.74 24.41 ?  104 GLU   A C    1 
ATOM   2258 C  C    B GLU   A 1 104 ? 23.974 -5.740  -13.398 0.26 19.48 ?  104 GLU   A C    1 
ATOM   2259 O  O    A GLU   A 1 104 ? 22.536 -5.522  -13.311 0.74 24.49 ?  104 GLU   A O    1 
ATOM   2260 O  O    B GLU   A 1 104 ? 22.784 -5.826  -13.083 0.26 19.27 ?  104 GLU   A O    1 
ATOM   2261 C  CB   A GLU   A 1 104 ? 24.943 -3.570  -12.126 0.74 22.34 ?  104 GLU   A CB   1 
ATOM   2262 C  CB   B GLU   A 1 104 ? 25.105 -3.797  -12.246 0.26 18.49 ?  104 GLU   A CB   1 
ATOM   2263 C  CG   A GLU   A 1 104 ? 25.876 -2.359  -12.281 0.74 21.24 ?  104 GLU   A CG   1 
ATOM   2264 C  CG   B GLU   A 1 104 ? 25.869 -2.481  -12.411 0.26 18.44 ?  104 GLU   A CG   1 
ATOM   2265 C  CD   A GLU   A 1 104 ? 26.212 -1.604  -10.998 0.74 20.41 ?  104 GLU   A CD   1 
ATOM   2266 C  CD   B GLU   A 1 104 ? 26.227 -1.810  -11.096 0.26 18.46 ?  104 GLU   A CD   1 
ATOM   2267 O  OE1  A GLU   A 1 104 ? 25.629 -1.880  -9.931  0.74 18.91 ?  104 GLU   A OE1  1 
ATOM   2268 O  OE1  B GLU   A 1 104 ? 25.743 -2.250  -10.034 0.26 18.44 ?  104 GLU   A OE1  1 
ATOM   2269 O  OE2  A GLU   A 1 104 ? 27.076 -0.697  -11.084 0.74 21.42 -1 104 GLU   A OE2  1 
ATOM   2270 O  OE2  B GLU   A 1 104 ? 26.999 -0.828  -11.133 0.26 18.85 -1 104 GLU   A OE2  1 
ATOM   2271 H  H    A GLU   A 1 104 ? 23.144 -2.590  -13.533 0.74 31.58 ?  104 GLU   A H    1 
ATOM   2272 H  H    B GLU   A 1 104 ? 23.415 -2.853  -13.741 0.26 23.76 ?  104 GLU   A H    1 
ATOM   2273 H  HA   A GLU   A 1 104 ? 25.230 -4.173  -14.058 0.74 29.27 ?  104 GLU   A HA   1 
ATOM   2274 H  HA   B GLU   A 1 104 ? 25.442 -4.513  -14.132 0.26 23.01 ?  104 GLU   A HA   1 
ATOM   2275 H  HB2  A GLU   A 1 104 ? 24.181 -3.306  -11.589 0.74 26.95 ?  104 GLU   A HB2  1 
ATOM   2276 H  HB2  B GLU   A 1 104 ? 24.329 -3.621  -11.693 0.26 22.33 ?  104 GLU   A HB2  1 
ATOM   2277 H  HB3  A GLU   A 1 104 ? 25.435 -4.282  -11.690 0.74 26.95 ?  104 GLU   A HB3  1 
ATOM   2278 H  HB3  B GLU   A 1 104 ? 25.695 -4.426  -11.803 0.26 22.33 ?  104 GLU   A HB3  1 
ATOM   2279 H  HG2  A GLU   A 1 104 ? 26.708 -2.665  -12.667 0.74 25.63 ?  104 GLU   A HG2  1 
ATOM   2280 H  HG2  B GLU   A 1 104 ? 26.699 -2.653  -12.884 0.26 22.26 ?  104 GLU   A HG2  1 
ATOM   2281 H  HG3  A GLU   A 1 104 ? 25.451 -1.723  -12.876 0.74 25.63 ?  104 GLU   A HG3  1 
ATOM   2282 H  HG3  B GLU   A 1 104 ? 25.324 -1.860  -12.923 0.26 22.26 ?  104 GLU   A HG3  1 
ATOM   2283 N  N    A ASP   A 1 105 ? 24.579 -6.479  -13.429 0.74 24.87 ?  105 ASP   A N    1 
ATOM   2284 N  N    B ASP   A 1 105 ? 24.751 -6.800  -13.609 0.26 20.63 ?  105 ASP   A N    1 
ATOM   2285 C  CA   A ASP   A 1 105 ? 24.092 -7.847  -13.585 0.74 25.73 ?  105 ASP   A CA   1 
ATOM   2286 C  CA   B ASP   A 1 105 ? 24.240 -8.167  -13.614 0.26 21.96 ?  105 ASP   A CA   1 
ATOM   2287 C  C    A ASP   A 1 105 ? 23.414 -8.327  -12.305 0.74 23.35 ?  105 ASP   A C    1 
ATOM   2288 C  C    B ASP   A 1 105 ? 23.511 -8.482  -12.314 0.26 21.99 ?  105 ASP   A C    1 
ATOM   2289 O  O    A ASP   A 1 105 ? 24.051 -8.417  -11.253 0.74 21.20 ?  105 ASP   A O    1 
ATOM   2290 O  O    B ASP   A 1 105 ? 24.110 -8.464  -11.234 0.26 21.52 ?  105 ASP   A O    1 
ATOM   2291 C  CB   A ASP   A 1 105 ? 25.276 -8.750  -13.929 0.74 28.91 ?  105 ASP   A CB   1 
ATOM   2292 C  CB   B ASP   A 1 105 ? 25.422 -9.119  -13.803 0.26 23.30 ?  105 ASP   A CB   1 
ATOM   2293 C  CG   A ASP   A 1 105 ? 24.868 -10.182 -14.185 0.74 31.62 ?  105 ASP   A CG   1 
ATOM   2294 C  CG   B ASP   A 1 105 ? 25.011 -10.579 -13.818 0.26 24.43 ?  105 ASP   A CG   1 
ATOM   2295 O  OD1  A ASP   A 1 105 ? 23.653 -10.444 -14.293 0.74 32.29 ?  105 ASP   A OD1  1 
ATOM   2296 O  OD1  B ASP   A 1 105 ? 23.800 -10.868 -13.907 0.26 24.44 ?  105 ASP   A OD1  1 
ATOM   2297 O  OD2  A ASP   A 1 105 ? 25.769 -11.045 -14.281 0.74 33.02 -1 105 ASP   A OD2  1 
ATOM   2298 O  OD2  B ASP   A 1 105 ? 25.912 -11.444 -13.734 0.26 25.24 -1 105 ASP   A OD2  1 
ATOM   2299 H  H    A ASP   A 1 105 ? 25.435 -6.424  -13.362 0.74 29.99 ?  105 ASP   A H    1 
ATOM   2300 H  H    B ASP   A 1 105 ? 25.592 -6.746  -13.758 0.26 24.89 ?  105 ASP   A H    1 
ATOM   2301 H  HA   A ASP   A 1 105 ? 23.451 -7.888  -14.310 0.74 31.01 ?  105 ASP   A HA   1 
ATOM   2302 H  HA   B ASP   A 1 105 ? 23.620 -8.281  -14.351 0.26 26.49 ?  105 ASP   A HA   1 
ATOM   2303 H  HB2  A ASP   A 1 105 ? 25.707 -8.416  -14.732 0.74 34.84 ?  105 ASP   A HB2  1 
ATOM   2304 H  HB2  B ASP   A 1 105 ? 25.858 -8.909  -14.645 0.26 28.11 ?  105 ASP   A HB2  1 
ATOM   2305 H  HB3  A ASP   A 1 105 ? 25.905 -8.743  -13.190 0.74 34.84 ?  105 ASP   A HB3  1 
ATOM   2306 H  HB3  B ASP   A 1 105 ? 26.044 -8.996  -13.070 0.26 28.11 ?  105 ASP   A HB3  1 
ATOM   2307 N  N    A ILE   A 1 106 ? 22.126 -8.667  -12.401 0.74 23.17 ?  106 ILE   A N    1 
ATOM   2308 N  N    B ILE   A 1 106 ? 22.216 -8.789  -12.422 0.26 22.48 ?  106 ILE   A N    1 
ATOM   2309 C  CA   A ILE   A 1 106 ? 21.368 -9.075  -11.223 0.74 22.50 ?  106 ILE   A CA   1 
ATOM   2310 C  CA   B ILE   A 1 106 ? 21.429 -9.119  -11.240 0.26 22.93 ?  106 ILE   A CA   1 
ATOM   2311 C  C    A ILE   A 1 106 ? 21.910 -10.359 -10.615 0.74 21.56 ?  106 ILE   A C    1 
ATOM   2312 C  C    B ILE   A 1 106 ? 21.920 -10.401 -10.589 0.26 22.75 ?  106 ILE   A C    1 
ATOM   2313 O  O    A ILE   A 1 106 ? 21.701 -10.609 -9.424  0.74 20.71 ?  106 ILE   A O    1 
ATOM   2314 O  O    B ILE   A 1 106 ? 21.690 -10.615 -9.394  0.26 22.56 ?  106 ILE   A O    1 
ATOM   2315 C  CB   A ILE   A 1 106 ? 19.860 -9.173  -11.554 0.74 23.93 ?  106 ILE   A CB   1 
ATOM   2316 C  CB   B ILE   A 1 106 ? 19.922 -9.180  -11.582 0.26 23.81 ?  106 ILE   A CB   1 
ATOM   2317 C  CG1  A ILE   A 1 106 ? 19.022 -9.259  -10.274 0.74 24.57 ?  106 ILE   A CG1  1 
ATOM   2318 C  CG1  B ILE   A 1 106 ? 19.072 -9.224  -10.308 0.26 24.24 ?  106 ILE   A CG1  1 
ATOM   2319 C  CG2  A ILE   A 1 106 ? 19.580 -10.371 -12.442 0.74 24.55 ?  106 ILE   A CG2  1 
ATOM   2320 C  CG2  B ILE   A 1 106 ? 19.617 -10.393 -12.435 0.26 24.07 ?  106 ILE   A CG2  1 
ATOM   2321 C  CD1  A ILE   A 1 106 ? 19.110 -8.027  -9.396  0.74 24.99 ?  106 ILE   A CD1  1 
ATOM   2322 C  CD1  B ILE   A 1 106 ? 19.258 -8.030  -9.398  0.26 24.44 ?  106 ILE   A CD1  1 
ATOM   2323 H  H    A ILE   A 1 106 ? 21.677 -8.665  -13.129 0.74 27.95 ?  106 ILE   A H    1 
ATOM   2324 H  H    B ILE   A 1 106 ? 21.778 -8.811  -13.160 0.26 27.12 ?  106 ILE   A H    1 
ATOM   2325 H  HA   A ILE   A 1 106 ? 21.474 -8.393  -10.551 0.74 27.14 ?  106 ILE   A HA   1 
ATOM   2326 H  HA   B ILE   A 1 106 ? 21.555 -8.411  -10.596 0.26 27.65 ?  106 ILE   A HA   1 
ATOM   2327 H  HB   A ILE   A 1 106 ? 19.604 -8.371  -12.033 0.74 28.85 ?  106 ILE   A HB   1 
ATOM   2328 H  HB   B ILE   A 1 106 ? 19.687 -8.384  -12.082 0.26 28.71 ?  106 ILE   A HB   1 
ATOM   2329 H  HG12 A ILE   A 1 106 ? 18.091 -9.377  -10.519 0.74 29.62 ?  106 ILE   A HG12 1 
ATOM   2330 H  HG12 B ILE   A 1 106 ? 18.135 -9.255  -10.560 0.26 29.22 ?  106 ILE   A HG12 1 
ATOM   2331 H  HG13 A ILE   A 1 106 ? 19.322 -10.017 -9.750  0.74 29.62 ?  106 ILE   A HG13 1 
ATOM   2332 H  HG13 B ILE   A 1 106 ? 19.301 -10.018 -9.802  0.26 29.22 ?  106 ILE   A HG13 1 
ATOM   2333 H  HG21 A ILE   A 1 106 ? 18.679 -10.296 -12.791 0.74 29.60 ?  106 ILE   A HG21 1 
ATOM   2334 H  HG21 B ILE   A 1 106 ? 18.722 -10.303 -12.797 0.26 29.03 ?  106 ILE   A HG21 1 
ATOM   2335 H  HG22 A ILE   A 1 106 ? 20.219 -10.376 -13.170 0.74 29.60 ?  106 ILE   A HG22 1 
ATOM   2336 H  HG22 B ILE   A 1 106 ? 20.264 -10.439 -13.154 0.26 29.03 ?  106 ILE   A HG22 1 
ATOM   2337 H  HG23 A ILE   A 1 106 ? 19.667 -11.181 -11.916 0.74 29.60 ?  106 ILE   A HG23 1 
ATOM   2338 H  HG23 B ILE   A 1 106 ? 19.673 -11.189 -11.884 0.26 29.03 ?  106 ILE   A HG23 1 
ATOM   2339 H  HD11 A ILE   A 1 106 ? 18.396 -8.053  -8.742  0.74 30.13 ?  106 ILE   A HD11 1 
ATOM   2340 H  HD11 B ILE   A 1 106 ? 18.525 -8.002  -8.765  0.26 29.46 ?  106 ILE   A HD11 1 
ATOM   2341 H  HD12 A ILE   A 1 106 ? 19.970 -8.019  -8.944  0.74 30.13 ?  106 ILE   A HD12 1 
ATOM   2342 H  HD12 B ILE   A 1 106 ? 20.100 -8.121  -8.926  0.26 29.46 ?  106 ILE   A HD12 1 
ATOM   2343 H  HD13 A ILE   A 1 106 ? 19.021 -7.236  -9.951  0.74 30.13 ?  106 ILE   A HD13 1 
ATOM   2344 H  HD13 B ILE   A 1 106 ? 19.262 -7.223  -9.935  0.26 29.46 ?  106 ILE   A HD13 1 
ATOM   2345 N  N    A GLN   A 1 107 ? 22.620 -11.176 -11.403 0.74 22.40 ?  107 GLN   A N    1 
ATOM   2346 N  N    B GLN   A 1 107 ? 22.604 -11.264 -11.346 0.26 22.93 ?  107 GLN   A N    1 
ATOM   2347 C  CA   A GLN   A 1 107 ? 23.234 -12.389 -10.868 0.74 24.76 ?  107 GLN   A CA   1 
ATOM   2348 C  CA   B GLN   A 1 107 ? 23.207 -12.449 -10.750 0.26 23.41 ?  107 GLN   A CA   1 
ATOM   2349 C  C    A GLN   A 1 107 ? 24.204 -12.071 -9.736  0.74 22.13 ?  107 GLN   A C    1 
ATOM   2350 C  C    B GLN   A 1 107 ? 24.239 -12.085 -9.693  0.26 21.15 ?  107 GLN   A C    1 
ATOM   2351 O  O    A GLN   A 1 107 ? 24.429 -12.911 -8.857  0.74 23.46 ?  107 GLN   A O    1 
ATOM   2352 O  O    B GLN   A 1 107 ? 24.553 -12.918 -8.836  0.26 21.65 ?  107 GLN   A O    1 
ATOM   2353 C  CB   A GLN   A 1 107 ? 23.944 -13.151 -11.994 0.74 29.60 ?  107 GLN   A CB   1 
ATOM   2354 C  CB   B GLN   A 1 107 ? 23.838 -13.329 -11.833 0.26 26.11 ?  107 GLN   A CB   1 
ATOM   2355 C  CG   A GLN   A 1 107 ? 23.081 -13.366 -13.235 0.74 34.63 ?  107 GLN   A CG   1 
ATOM   2356 C  CG   B GLN   A 1 107 ? 22.837 -13.870 -12.844 0.26 28.68 ?  107 GLN   A CG   1 
ATOM   2357 C  CD   A GLN   A 1 107 ? 21.802 -14.121 -12.935 0.74 38.83 ?  107 GLN   A CD   1 
ATOM   2358 C  CD   B GLN   A 1 107 ? 21.693 -14.621 -12.191 0.26 30.89 ?  107 GLN   A CD   1 
ATOM   2359 O  OE1  A GLN   A 1 107 ? 21.827 -15.186 -12.318 0.74 40.41 ?  107 GLN   A OE1  1 
ATOM   2360 O  OE1  B GLN   A 1 107 ? 21.893 -15.369 -11.233 0.26 31.59 ?  107 GLN   A OE1  1 
ATOM   2361 N  NE2  A GLN   A 1 107 ? 20.673 -13.568 -13.365 0.74 40.16 ?  107 GLN   A NE2  1 
ATOM   2362 N  NE2  B GLN   A 1 107 ? 20.483 -14.416 -12.701 0.26 31.59 ?  107 GLN   A NE2  1 
ATOM   2363 H  H    A GLN   A 1 107 ? 22.755 -11.053 -12.241 0.74 27.02 ?  107 GLN   A H    1 
ATOM   2364 H  H    B GLN   A 1 107 ? 22.730 -11.184 -12.192 0.26 27.65 ?  107 GLN   A H    1 
ATOM   2365 H  HA   A GLN   A 1 107 ? 22.549 -12.970 -10.510 0.74 29.85 ?  107 GLN   A HA   1 
ATOM   2366 H  HA   B GLN   A 1 107 ? 22.516 -12.964 -10.314 0.26 28.23 ?  107 GLN   A HA   1 
ATOM   2367 H  HB2  A GLN   A 1 107 ? 24.732 -12.655 -12.266 0.74 35.66 ?  107 GLN   A HB2  1 
ATOM   2368 H  HB2  B GLN   A 1 107 ? 24.497 -12.809 -12.319 0.26 31.47 ?  107 GLN   A HB2  1 
ATOM   2369 H  HB3  A GLN   A 1 107 ? 24.207 -14.028 -11.669 0.74 35.66 ?  107 GLN   A HB3  1 
ATOM   2370 H  HB3  B GLN   A 1 107 ? 24.268 -14.088 -11.409 0.26 31.47 ?  107 GLN   A HB3  1 
ATOM   2371 H  HG2  A GLN   A 1 107 ? 22.838 -12.506 -13.613 0.74 41.70 ?  107 GLN   A HG2  1 
ATOM   2372 H  HG2  B GLN   A 1 107 ? 22.463 -13.130 -13.347 0.26 34.55 ?  107 GLN   A HG2  1 
ATOM   2373 H  HG3  A GLN   A 1 107 ? 23.586 -13.877 -13.886 0.74 41.70 ?  107 GLN   A HG3  1 
ATOM   2374 H  HG3  B GLN   A 1 107 ? 23.292 -14.483 -13.443 0.26 34.55 ?  107 GLN   A HG3  1 
ATOM   2375 H  HE21 A GLN   A 1 107 ? 20.693 -12.822 -13.792 0.74 48.33 ?  107 GLN   A HE21 1 
ATOM   2376 H  HE21 B GLN   A 1 107 ? 20.384 -13.883 -13.369 0.26 38.05 ?  107 GLN   A HE21 1 
ATOM   2377 H  HE22 A GLN   A 1 107 ? 19.921 -13.959 -13.219 0.74 48.33 ?  107 GLN   A HE22 1 
ATOM   2378 H  HE22 B GLN   A 1 107 ? 19.800 -14.815 -12.364 0.26 38.05 ?  107 GLN   A HE22 1 
ATOM   2379 N  N    . LEU   A 1 108 ? 24.763 -10.858 -9.722  1.00 18.58 ?  108 LEU   A N    1 
ATOM   2380 C  CA   . LEU   A 1 108 ? 25.676 -10.432 -8.673  1.00 15.59 ?  108 LEU   A CA   1 
ATOM   2381 C  C    . LEU   A 1 108 ? 24.975 -10.253 -7.336  1.00 13.51 ?  108 LEU   A C    1 
ATOM   2382 O  O    . LEU   A 1 108 ? 25.657 -10.087 -6.322  1.00 13.80 ?  108 LEU   A O    1 
ATOM   2383 C  CB   . LEU   A 1 108 ? 26.403 -9.142  -9.081  1.00 15.42 ?  108 LEU   A CB   1 
ATOM   2384 C  CG   . LEU   A 1 108 ? 27.407 -9.334  -10.221 1.00 17.15 ?  108 LEU   A CG   1 
ATOM   2385 C  CD1  . LEU   A 1 108 ? 27.882 -7.998  -10.774 1.00 17.67 ?  108 LEU   A CD1  1 
ATOM   2386 C  CD2  . LEU   A 1 108 ? 28.600 -10.168 -9.767  1.00 18.83 ?  108 LEU   A CD2  1 
ATOM   2387 H  H    A LEU   A 1 108 ? 24.618 -10.260 -10.316 0.74 22.43 ?  108 LEU   A H    1 
ATOM   2388 H  H    B LEU   A 1 108 ? 24.614 -10.276 -10.330 0.26 22.43 ?  108 LEU   A H    1 
ATOM   2389 H  HA   . LEU   A 1 108 ? 26.347 -11.119 -8.548  1.00 18.85 ?  108 LEU   A HA   1 
ATOM   2390 H  HB2  . LEU   A 1 108 ? 25.746 -8.492  -9.374  1.00 18.65 ?  108 LEU   A HB2  1 
ATOM   2391 H  HB3  . LEU   A 1 108 ? 26.887 -8.800  -8.316  1.00 18.65 ?  108 LEU   A HB3  1 
ATOM   2392 H  HG   . LEU   A 1 108 ? 26.973 -9.813  -10.944 1.00 20.72 ?  108 LEU   A HG   1 
ATOM   2393 H  HD11 . LEU   A 1 108 ? 28.487 -8.159  -11.519 1.00 21.35 ?  108 LEU   A HD11 1 
ATOM   2394 H  HD12 . LEU   A 1 108 ? 27.116 -7.488  -11.078 1.00 21.35 ?  108 LEU   A HD12 1 
ATOM   2395 H  HD13 . LEU   A 1 108 ? 28.348 -7.511  -10.075 1.00 21.35 ?  108 LEU   A HD13 1 
ATOM   2396 H  HD21 . LEU   A 1 108 ? 29.286 -10.136 -10.449 1.00 22.73 ?  108 LEU   A HD21 1 
ATOM   2397 H  HD22 . LEU   A 1 108 ? 28.940 -9.801  -8.936  1.00 22.73 ?  108 LEU   A HD22 1 
ATOM   2398 H  HD23 . LEU   A 1 108 ? 28.310 -11.084 -9.629  1.00 22.73 ?  108 LEU   A HD23 1 
ATOM   2399 N  N    . LEU   A 1 109 ? 23.640 -10.307 -7.298  1.00 12.93 ?  109 LEU   A N    1 
ATOM   2400 C  CA   . LEU   A 1 109 ? 22.946 -10.177 -6.023  1.00 12.17 ?  109 LEU   A CA   1 
ATOM   2401 C  C    . LEU   A 1 109 ? 23.289 -11.333 -5.087  1.00 11.50 ?  109 LEU   A C    1 
ATOM   2402 O  O    . LEU   A 1 109 ? 23.425 -11.136 -3.875  1.00 11.95 ?  109 LEU   A O    1 
ATOM   2403 C  CB   . LEU   A 1 109 ? 21.441 -10.098 -6.267  1.00 13.08 ?  109 LEU   A CB   1 
ATOM   2404 C  CG   . LEU   A 1 109 ? 20.556 -9.808  -5.059  1.00 13.31 ?  109 LEU   A CG   1 
ATOM   2405 C  CD1  . LEU   A 1 109 ? 21.007 -8.540  -4.352  1.00 13.56 ?  109 LEU   A CD1  1 
ATOM   2406 C  CD2  . LEU   A 1 109 ? 19.100 -9.678  -5.496  1.00 14.41 ?  109 LEU   A CD2  1 
ATOM   2407 H  H    . LEU   A 1 109 ? 23.125 -10.409 -7.980  1.00 15.66 ?  109 LEU   A H    1 
ATOM   2408 H  HA   . LEU   A 1 109 ? 23.227 -9.352  -5.595  1.00 14.74 ?  109 LEU   A HA   1 
ATOM   2409 H  HB2  . LEU   A 1 109 ? 21.278 -9.394  -6.914  1.00 15.84 ?  109 LEU   A HB2  1 
ATOM   2410 H  HB3  . LEU   A 1 109 ? 21.150 -10.945 -6.634  1.00 15.84 ?  109 LEU   A HB3  1 
ATOM   2411 H  HG   . LEU   A 1 109 ? 20.617 -10.541 -4.430  1.00 16.12 ?  109 LEU   A HG   1 
ATOM   2412 H  HD11 . LEU   A 1 109 ? 20.323 -8.261  -3.724  1.00 16.41 ?  109 LEU   A HD11 1 
ATOM   2413 H  HD12 . LEU   A 1 109 ? 21.837 -8.714  -3.884  1.00 16.41 ?  109 LEU   A HD12 1 
ATOM   2414 H  HD13 . LEU   A 1 109 ? 21.145 -7.841  -5.016  1.00 16.41 ?  109 LEU   A HD13 1 
ATOM   2415 H  HD21 . LEU   A 1 109 ? 18.568 -9.374  -4.743  1.00 17.43 ?  109 LEU   A HD21 1 
ATOM   2416 H  HD22 . LEU   A 1 109 ? 19.042 -9.038  -6.222  1.00 17.43 ?  109 LEU   A HD22 1 
ATOM   2417 H  HD23 . LEU   A 1 109 ? 18.782 -10.546 -5.795  1.00 17.43 ?  109 LEU   A HD23 1 
ATOM   2418 N  N    . LYS   A 1 110 ? 23.434 -12.547 -5.623  1.00 11.48 ?  110 LYS   A N    1 
ATOM   2419 C  CA   . LYS   A 1 110 ? 23.813 -13.668 -4.769  1.00 11.37 ?  110 LYS   A CA   1 
ATOM   2420 C  C    . LYS   A 1 110 ? 25.196 -13.443 -4.163  1.00 11.21 ?  110 LYS   A C    1 
ATOM   2421 O  O    . LYS   A 1 110 ? 25.395 -13.640 -2.961  1.00 11.49 ?  110 LYS   A O    1 
ATOM   2422 C  CB   . LYS   A 1 110 ? 23.733 -14.994 -5.531  1.00 12.29 ?  110 LYS   A CB   1 
ATOM   2423 C  CG   . LYS   A 1 110 ? 23.943 -16.204 -4.626  1.00 12.61 ?  110 LYS   A CG   1 
ATOM   2424 C  CD   . LYS   A 1 110 ? 23.715 -17.524 -5.339  1.00 13.28 ?  110 LYS   A CD   1 
ATOM   2425 C  CE   . LYS   A 1 110 ? 23.814 -18.705 -4.379  1.00 14.17 ?  110 LYS   A CE   1 
ATOM   2426 N  NZ   . LYS   A 1 110 ? 22.625 -18.831 -3.494  1.00 14.42 ?  110 LYS   A NZ   1 
ATOM   2427 H  H    . LYS   A 1 110 ? 23.321 -12.742 -6.451  1.00 13.92 ?  110 LYS   A H    1 
ATOM   2428 H  HA   . LYS   A 1 110 ? 23.177 -13.717 -4.033  1.00 13.79 ?  110 LYS   A HA   1 
ATOM   2429 H  HB2  . LYS   A 1 110 ? 22.854 -15.073 -5.936  1.00 14.89 ?  110 LYS   A HB2  1 
ATOM   2430 H  HB3  . LYS   A 1 110 ? 24.418 -15.007 -6.214  1.00 14.89 ?  110 LYS   A HB3  1 
ATOM   2431 H  HG2  . LYS   A 1 110 ? 24.854 -16.196 -4.293  1.00 15.27 ?  110 LYS   A HG2  1 
ATOM   2432 H  HG3  . LYS   A 1 110 ? 23.321 -16.156 -3.883  1.00 15.27 ?  110 LYS   A HG3  1 
ATOM   2433 H  HD2  . LYS   A 1 110 ? 22.835 -17.529 -5.733  1.00 16.08 ?  110 LYS   A HD2  1 
ATOM   2434 H  HD3  . LYS   A 1 110 ? 24.396 -17.636 -6.024  1.00 16.08 ?  110 LYS   A HD3  1 
ATOM   2435 H  HE2  . LYS   A 1 110 ? 23.898 -19.525 -4.890  1.00 17.14 ?  110 LYS   A HE2  1 
ATOM   2436 H  HE3  . LYS   A 1 110 ? 24.597 -18.590 -3.811  1.00 17.14 ?  110 LYS   A HE3  1 
ATOM   2437 H  HZ1  . LYS   A 1 110 ? 22.715 -19.526 -2.952  1.00 17.45 ?  110 LYS   A HZ1  1 
ATOM   2438 H  HZ2  . LYS   A 1 110 ? 22.528 -18.090 -3.007  1.00 17.45 ?  110 LYS   A HZ2  1 
ATOM   2439 H  HZ3  . LYS   A 1 110 ? 21.891 -18.942 -3.990  1.00 17.45 ?  110 LYS   A HZ3  1 
ATOM   2440 N  N    . SER   A 1 111 ? 26.157 -13.002 -4.981  1.00 11.39 ?  111 SER   A N    1 
ATOM   2441 C  CA   . SER   A 1 111 ? 27.487 -12.693 -4.464  1.00 11.50 ?  111 SER   A CA   1 
ATOM   2442 C  C    . SER   A 1 111 ? 27.420 -11.647 -3.357  1.00 11.07 ?  111 SER   A C    1 
ATOM   2443 O  O    . SER   A 1 111 ? 28.119 -11.751 -2.343  1.00 11.64 ?  111 SER   A O    1 
ATOM   2444 C  CB   . SER   A 1 111 ? 28.379 -12.198 -5.603  1.00 12.68 ?  111 SER   A CB   1 
ATOM   2445 O  OG   . SER   A 1 111 ? 28.479 -13.188 -6.615  1.00 14.67 ?  111 SER   A OG   1 
ATOM   2446 H  H    . SER   A 1 111 ? 26.054 -12.870 -5.822  1.00 13.81 ?  111 SER   A H    1 
ATOM   2447 H  HA   . SER   A 1 111 ? 27.880 -13.499 -4.100  1.00 13.95 ?  111 SER   A HA   1 
ATOM   2448 H  HB2  . SER   A 1 111 ? 27.983 -11.400 -5.991  1.00 15.35 ?  111 SER   A HB2  1 
ATOM   2449 H  HB3  . SER   A 1 111 ? 29.258 -11.995 -5.251  1.00 15.35 ?  111 SER   A HB3  1 
ATOM   2450 H  HG   . SER   A 1 111 ? 28.989 -12.911 -7.232  1.00 17.75 ?  111 SER   A HG   1 
ATOM   2451 N  N    . ALA   A 1 112 ? 26.574 -10.630 -3.534  1.00 11.05 ?  112 ALA   A N    1 
ATOM   2452 C  CA   . ALA   A 1 112 ? 26.431 -9.591  -2.516  1.00 10.91 ?  112 ALA   A CA   1 
ATOM   2453 C  C    . ALA   A 1 112 ? 25.945 -10.183 -1.195  1.00 10.91 ?  112 ALA   A C    1 
ATOM   2454 O  O    . ALA   A 1 112 ? 26.493 -9.893  -0.124  1.00 11.13 ?  112 ALA   A O    1 
ATOM   2455 C  CB   . ALA   A 1 112 ? 25.473 -8.505  -3.011  1.00 11.47 ?  112 ALA   A CB   1 
ATOM   2456 H  H    . ALA   A 1 112 ? 26.078 -10.515 -4.227  1.00 13.41 ?  112 ALA   A H    1 
ATOM   2457 H  HA   . ALA   A 1 112 ? 27.294 -9.172  -2.360  1.00 13.24 ?  112 ALA   A HA   1 
ATOM   2458 H  HB1  . ALA   A 1 112 ? 25.400 -7.809  -2.330  1.00 13.91 ?  112 ALA   A HB1  1 
ATOM   2459 H  HB2  . ALA   A 1 112 ? 25.820 -8.119  -3.831  1.00 13.91 ?  112 ALA   A HB2  1 
ATOM   2460 H  HB3  . ALA   A 1 112 ? 24.601 -8.895  -3.171  1.00 13.91 ?  112 ALA   A HB3  1 
ATOM   2461 N  N    . TYR   A 1 113 ? 24.914 -11.029 -1.249  1.00 10.98 ?  113 TYR   A N    1 
ATOM   2462 C  CA   . TYR   A 1 113 ? 24.403 -11.633 -0.021  1.00 10.68 ?  113 TYR   A CA   1 
ATOM   2463 C  C    . TYR   A 1 113 ? 25.410 -12.585 0.624   1.00 10.65 ?  113 TYR   A C    1 
ATOM   2464 O  O    . TYR   A 1 113 ? 25.370 -12.775 1.843   1.00 11.07 ?  113 TYR   A O    1 
ATOM   2465 C  CB   . TYR   A 1 113 ? 23.087 -12.362 -0.290  1.00 11.27 ?  113 TYR   A CB   1 
ATOM   2466 C  CG   . TYR   A 1 113 ? 21.872 -11.466 -0.205  1.00 10.99 ?  113 TYR   A CG   1 
ATOM   2467 C  CD1  . TYR   A 1 113 ? 21.508 -10.869 0.999   1.00 11.00 ?  113 TYR   A CD1  1 
ATOM   2468 C  CD2  . TYR   A 1 113 ? 21.065 -11.241 -1.315  1.00 11.16 ?  113 TYR   A CD2  1 
ATOM   2469 C  CE1  . TYR   A 1 113 ? 20.383 -10.072 1.095   1.00 11.29 ?  113 TYR   A CE1  1 
ATOM   2470 C  CE2  . TYR   A 1 113 ? 19.918 -10.440 -1.223  1.00 11.35 ?  113 TYR   A CE2  1 
ATOM   2471 C  CZ   . TYR   A 1 113 ? 19.588 -9.867  -0.016  1.00 11.12 ?  113 TYR   A CZ   1 
ATOM   2472 O  OH   . TYR   A 1 113 ? 18.463 -9.073  0.107   1.00 11.63 ?  113 TYR   A OH   1 
ATOM   2473 H  H    . TYR   A 1 113 ? 24.510 -11.263 -1.970  1.00 13.32 ?  113 TYR   A H    1 
ATOM   2474 H  HA   . TYR   A 1 113 ? 24.227 -10.928 0.615   1.00 12.95 ?  113 TYR   A HA   1 
ATOM   2475 H  HB2  . TYR   A 1 113 ? 23.114 -12.737 -1.182  1.00 13.67 ?  113 TYR   A HB2  1 
ATOM   2476 H  HB3  . TYR   A 1 113 ? 22.986 -13.069 0.365   1.00 13.67 ?  113 TYR   A HB3  1 
ATOM   2477 H  HD1  . TYR   A 1 113 ? 22.032 -11.016 1.754   1.00 13.35 ?  113 TYR   A HD1  1 
ATOM   2478 H  HD2  . TYR   A 1 113 ? 21.278 -11.641 -2.124  1.00 13.53 ?  113 TYR   A HD2  1 
ATOM   2479 H  HE1  . TYR   A 1 113 ? 20.155 -9.684  1.909   1.00 13.68 ?  113 TYR   A HE1  1 
ATOM   2480 H  HE2  . TYR   A 1 113 ? 19.380 -10.295 -1.967  1.00 13.76 ?  113 TYR   A HE2  1 
ATOM   2481 H  HH   . TYR   A 1 113 ? 18.071 -9.029  -0.639  1.00 14.09 ?  113 TYR   A HH   1 
ATOM   2482 N  N    . GLU   A 1 114 ? 26.313 -13.196 -0.157  1.00 10.77 ?  114 GLU   A N    1 
ATOM   2483 C  CA   . GLU   A 1 114 ? 27.301 -14.096 0.442   1.00 11.01 ?  114 GLU   A CA   1 
ATOM   2484 C  C    . GLU   A 1 114 ? 28.148 -13.386 1.491   1.00 10.78 ?  114 GLU   A C    1 
ATOM   2485 O  O    . GLU   A 1 114 ? 28.623 -14.019 2.442   1.00 11.31 ?  114 GLU   A O    1 
ATOM   2486 C  CB   . GLU   A 1 114 ? 28.170 -14.740 -0.646  1.00 11.17 ?  114 GLU   A CB   1 
ATOM   2487 C  CG   . GLU   A 1 114 ? 27.412 -15.796 -1.426  1.00 11.70 ?  114 GLU   A CG   1 
ATOM   2488 C  CD   . GLU   A 1 114 ? 28.121 -16.325 -2.667  1.00 12.19 ?  114 GLU   A CD   1 
ATOM   2489 O  OE1  . GLU   A 1 114 ? 29.078 -15.691 -3.162  1.00 12.24 ?  114 GLU   A OE1  1 
ATOM   2490 O  OE2  . GLU   A 1 114 ? 27.674 -17.385 -3.161  1.00 13.01 -1 114 GLU   A OE2  1 
ATOM   2491 H  H    . GLU   A 1 114 ? 26.375 -13.099 -1.017  1.00 13.06 ?  114 GLU   A H    1 
ATOM   2492 H  HA   . GLU   A 1 114 ? 26.822 -14.808 0.887   1.00 13.35 ?  114 GLU   A HA   1 
ATOM   2493 H  HB2  . GLU   A 1 114 ? 28.459 -14.059 -1.274  1.00 13.55 ?  114 GLU   A HB2  1 
ATOM   2494 H  HB3  . GLU   A 1 114 ? 28.933 -15.166 -0.235  1.00 13.55 ?  114 GLU   A HB3  1 
ATOM   2495 H  HG2  . GLU   A 1 114 ? 27.247 -16.552 -0.843  1.00 14.18 ?  114 GLU   A HG2  1 
ATOM   2496 H  HG3  . GLU   A 1 114 ? 26.562 -15.419 -1.714  1.00 14.18 ?  114 GLU   A HG3  1 
ATOM   2497 N  N    . ASN   A 1 115 ? 28.331 -12.068 1.357   1.00 10.52 ?  115 ASN   A N    1 
ATOM   2498 C  CA   . ASN   A 1 115 ? 29.097 -11.337 2.362   1.00 10.92 ?  115 ASN   A CA   1 
ATOM   2499 C  C    . ASN   A 1 115 ? 28.480 -11.469 3.749   1.00 10.69 ?  115 ASN   A C    1 
ATOM   2500 O  O    . ASN   A 1 115 ? 29.194 -11.401 4.756   1.00 11.14 ?  115 ASN   A O    1 
ATOM   2501 C  CB   . ASN   A 1 115 ? 29.203 -9.861  1.981   1.00 11.23 ?  115 ASN   A CB   1 
ATOM   2502 C  CG   . ASN   A 1 115 ? 30.002 -9.644  0.723   1.00 11.70 ?  115 ASN   A CG   1 
ATOM   2503 O  OD1  . ASN   A 1 115 ? 31.221 -9.746  0.739   1.00 15.20 ?  115 ASN   A OD1  1 
ATOM   2504 N  ND2  . ASN   A 1 115 ? 29.327 -9.341  -0.371  1.00 11.46 ?  115 ASN   A ND2  1 
ATOM   2505 H  H    . ASN   A 1 115 ? 28.020 -11.580 0.713   1.00 12.77 ?  115 ASN   A H    1 
ATOM   2506 H  HA   . ASN   A 1 115 ? 29.989 -11.703 2.399   1.00 13.25 ?  115 ASN   A HA   1 
ATOM   2507 H  HB2  . ASN   A 1 115 ? 28.310 -9.503  1.848   1.00 13.62 ?  115 ASN   A HB2  1 
ATOM   2508 H  HB3  . ASN   A 1 115 ? 29.641 -9.383  2.708   1.00 13.62 ?  115 ASN   A HB3  1 
ATOM   2509 H  HD21 . ASN   A 1 115 ? 29.744 -9.205  -1.110  1.00 13.90 ?  115 ASN   A HD21 1 
ATOM   2510 H  HD22 . ASN   A 1 115 ? 28.466 -9.297  -0.350  1.00 13.90 ?  115 ASN   A HD22 1 
ATOM   2511 N  N    . PHE   A 1 116 ? 27.152 -11.638 3.828   1.00 10.91 ?  116 PHE   A N    1 
ATOM   2512 C  CA   . PHE   A 1 116 ? 26.503 -11.736 5.133   1.00 10.88 ?  116 PHE   A CA   1 
ATOM   2513 C  C    . PHE   A 1 116 ? 26.983 -12.967 5.904   1.00 11.12 ?  116 PHE   A C    1 
ATOM   2514 O  O    . PHE   A 1 116 ? 26.905 -12.986 7.132   1.00 11.55 ?  116 PHE   A O    1 
ATOM   2515 C  CB   . PHE   A 1 116 ? 24.975 -11.863 5.007   1.00 11.11 ?  116 PHE   A CB   1 
ATOM   2516 C  CG   . PHE   A 1 116 ? 24.220 -10.617 4.541   1.00 10.90 ?  116 PHE   A CG   1 
ATOM   2517 C  CD1  . PHE   A 1 116 ? 24.794 -9.593  3.798   1.00 10.80 ?  116 PHE   A CD1  1 
ATOM   2518 C  CD2  . PHE   A 1 116 ? 22.860 -10.520 4.845   1.00 11.37 ?  116 PHE   A CD2  1 
ATOM   2519 C  CE1  . PHE   A 1 116 ? 24.031 -8.515  3.380   1.00 11.11 ?  116 PHE   A CE1  1 
ATOM   2520 C  CE2  . PHE   A 1 116 ? 22.101 -9.442  4.434   1.00 11.41 ?  116 PHE   A CE2  1 
ATOM   2521 C  CZ   . PHE   A 1 116 ? 22.678 -8.441  3.700   1.00 10.93 ?  116 PHE   A CZ   1 
ATOM   2522 H  H    . PHE   A 1 116 ? 26.614 -11.679 3.154   1.00 13.23 ?  116 PHE   A H    1 
ATOM   2523 H  HA   . PHE   A 1 116 ? 26.700 -10.944 5.659   1.00 13.19 ?  116 PHE   A HA   1 
ATOM   2524 H  HB2  . PHE   A 1 116 ? 24.780 -12.572 4.375   1.00 13.47 ?  116 PHE   A HB2  1 
ATOM   2525 H  HB3  . PHE   A 1 116 ? 24.619 -12.110 5.879   1.00 13.47 ?  116 PHE   A HB3  1 
ATOM   2526 H  HD1  . PHE   A 1 116 ? 25.691 -9.648  3.579   1.00 13.10 ?  116 PHE   A HD1  1 
ATOM   2527 H  HD2  . PHE   A 1 116 ? 22.448 -11.205 5.337   1.00 13.78 ?  116 PHE   A HD2  1 
ATOM   2528 H  HE1  . PHE   A 1 116 ? 24.431 -7.837  2.892   1.00 13.47 ?  116 PHE   A HE1  1 
ATOM   2529 H  HE2  . PHE   A 1 116 ? 21.194 -9.402  4.652   1.00 13.83 ?  116 PHE   A HE2  1 
ATOM   2530 H  HZ   . PHE   A 1 116 ? 22.175 -7.711  3.429   1.00 13.26 ?  116 PHE   A HZ   1 
ATOM   2531 N  N    . ASN   A 1 117 ? 27.427 -14.018 5.201   1.00 11.21 ?  117 ASN   A N    1 
ATOM   2532 C  CA   . ASN   A 1 117 ? 27.795 -15.264 5.869   1.00 11.53 ?  117 ASN   A CA   1 
ATOM   2533 C  C    . ASN   A 1 117 ? 29.053 -15.142 6.708   1.00 12.15 ?  117 ASN   A C    1 
ATOM   2534 O  O    . ASN   A 1 117 ? 29.350 -16.065 7.476   1.00 12.93 ?  117 ASN   A O    1 
ATOM   2535 C  CB   . ASN   A 1 117 ? 27.913 -16.393 4.849   1.00 11.73 ?  117 ASN   A CB   1 
ATOM   2536 C  CG   . ASN   A 1 117 ? 26.557 -16.777 4.307   1.00 11.71 ?  117 ASN   A CG   1 
ATOM   2537 O  OD1  . ASN   A 1 117 ? 25.579 -16.803 5.055   1.00 12.46 ?  117 ASN   A OD1  1 
ATOM   2538 N  ND2  . ASN   A 1 117 ? 26.473 -17.032 3.015   1.00 11.64 ?  117 ASN   A ND2  1 
ATOM   2539 H  H    . ASN   A 1 117 ? 27.501 -14.033 4.341   1.00 13.59 ?  117 ASN   A H    1 
ATOM   2540 H  HA   . ASN   A 1 117 ? 27.070 -15.497 6.470   1.00 13.98 ?  117 ASN   A HA   1 
ATOM   2541 H  HB2  . ASN   A 1 117 ? 28.465 -16.096 4.107   1.00 14.22 ?  117 ASN   A HB2  1 
ATOM   2542 H  HB3  . ASN   A 1 117 ? 28.299 -17.166 5.276   1.00 14.22 ?  117 ASN   A HB3  1 
ATOM   2543 H  HD21 . ASN   A 1 117 ? 25.719 -17.246 2.672   1.00 14.11 ?  117 ASN   A HD21 1 
ATOM   2544 H  HD22 . ASN   A 1 117 ? 27.178 -16.989 2.524   1.00 14.11 ?  117 ASN   A HD22 1 
ATOM   2545 N  N    . GLN   A 1 118 ? 29.782 -14.030 6.593   1.00 12.22 ?  118 GLN   A N    1 
ATOM   2546 C  CA   . GLN   A 1 118 ? 30.960 -13.795 7.416   1.00 12.74 ?  118 GLN   A CA   1 
ATOM   2547 C  C    . GLN   A 1 118 ? 30.616 -13.219 8.785   1.00 12.77 ?  118 GLN   A C    1 
ATOM   2548 O  O    . GLN   A 1 118 ? 31.529 -12.931 9.568   1.00 14.08 ?  118 GLN   A O    1 
ATOM   2549 C  CB   . GLN   A 1 118 ? 31.953 -12.895 6.676   1.00 12.98 ?  118 GLN   A CB   1 
ATOM   2550 C  CG   . GLN   A 1 118 ? 32.417 -13.474 5.350   1.00 13.00 ?  118 GLN   A CG   1 
ATOM   2551 C  CD   . GLN   A 1 118 ? 33.261 -14.727 5.523   1.00 13.17 ?  118 GLN   A CD   1 
ATOM   2552 O  OE1  . GLN   A 1 118 ? 34.125 -14.790 6.406   1.00 13.82 ?  118 GLN   A OE1  1 
ATOM   2553 N  NE2  . GLN   A 1 118 ? 33.014 -15.731 4.682   1.00 13.38 ?  118 GLN   A NE2  1 
ATOM   2554 H  H    . GLN   A 1 118 ? 29.600 -13.385 6.043   1.00 14.81 ?  118 GLN   A H    1 
ATOM   2555 H  HA   . GLN   A 1 118 ? 31.388 -14.649 7.563   1.00 15.43 ?  118 GLN   A HA   1 
ATOM   2556 H  HB2  . GLN   A 1 118 ? 31.530 -12.041 6.501   1.00 15.72 ?  118 GLN   A HB2  1 
ATOM   2557 H  HB3  . GLN   A 1 118 ? 32.732 -12.771 7.239   1.00 15.72 ?  118 GLN   A HB3  1 
ATOM   2558 H  HG2  . GLN   A 1 118 ? 31.641 -13.701 4.810   1.00 15.75 ?  118 GLN   A HG2  1 
ATOM   2559 H  HG3  . GLN   A 1 118 ? 32.957 -12.814 4.889   1.00 15.75 ?  118 GLN   A HG3  1 
ATOM   2560 H  HE21 . GLN   A 1 118 ? 32.395 -15.650 4.082   1.00 16.19 ?  118 GLN   A HE21 1 
ATOM   2561 H  HE22 . GLN   A 1 118 ? 33.455 -16.464 4.740   1.00 16.19 ?  118 GLN   A HE22 1 
ATOM   2562 N  N    . HIS   A 1 119 ? 29.328 -13.066 9.097   1.00 12.30 ?  119 HIS   A N    1 
ATOM   2563 C  CA   . HIS   A 1 119 ? 28.867 -12.456 10.339  1.00 12.66 ?  119 HIS   A CA   1 
ATOM   2564 C  C    . HIS   A 1 119 ? 27.731 -13.283 10.914  1.00 12.84 ?  119 HIS   A C    1 
ATOM   2565 O  O    . HIS   A 1 119 ? 26.785 -13.623 10.196  1.00 13.50 ?  119 HIS   A O    1 
ATOM   2566 C  CB   . HIS   A 1 119 ? 28.407 -11.026 10.057  1.00 12.98 ?  119 HIS   A CB   1 
ATOM   2567 C  CG   . HIS   A 1 119 ? 29.486 -10.214 9.439   1.00 14.11 ?  119 HIS   A CG   1 
ATOM   2568 N  ND1  . HIS   A 1 119 ? 30.464 -9.609  10.191  1.00 16.61 ?  119 HIS   A ND1  1 
ATOM   2569 C  CD2  . HIS   A 1 119 ? 29.823 -10.022 8.144   1.00 15.24 ?  119 HIS   A CD2  1 
ATOM   2570 C  CE1  . HIS   A 1 119 ? 31.330 -9.025  9.383   1.00 16.70 ?  119 HIS   A CE1  1 
ATOM   2571 N  NE2  . HIS   A 1 119 ? 30.971 -9.268  8.135   1.00 16.63 ?  119 HIS   A NE2  1 
ATOM   2572 H  H    . HIS   A 1 119 ? 28.678 -13.328 8.590   1.00 14.90 ?  119 HIS   A H    1 
ATOM   2573 H  HA   . HIS   A 1 119 ? 29.595 -12.437 10.979  1.00 15.34 ?  119 HIS   A HA   1 
ATOM   2574 H  HB2  . HIS   A 1 119 ? 27.652 -11.052 9.449   1.00 15.72 ?  119 HIS   A HB2  1 
ATOM   2575 H  HB3  . HIS   A 1 119 ? 28.151 -10.610 10.894  1.00 15.72 ?  119 HIS   A HB3  1 
ATOM   2576 H  HD1  . HIS   A 1 119 ? 30.497 -9.601  11.047  1.00 20.07 ?  119 HIS   A HD1  1 
ATOM   2577 H  HD2  . HIS   A 1 119 ? 29.354 -10.330 7.399   1.00 18.43 ?  119 HIS   A HD2  1 
ATOM   2578 H  HE1  . HIS   A 1 119 ? 32.067 -8.527  9.645   1.00 20.18 ?  119 HIS   A HE1  1 
ATOM   2579 N  N    . GLU   A 1 120 ? 27.813 -13.581 12.212  1.00 13.87 ?  120 GLU   A N    1 
ATOM   2580 C  CA   . GLU   A 1 120 ? 26.858 -14.509 12.817  1.00 16.34 ?  120 GLU   A CA   1 
ATOM   2581 C  C    . GLU   A 1 120 ? 25.440 -13.949 12.873  1.00 14.64 ?  120 GLU   A C    1 
ATOM   2582 O  O    . GLU   A 1 120 ? 24.470 -14.715 12.760  1.00 14.85 ?  120 GLU   A O    1 
ATOM   2583 C  CB   . GLU   A 1 120 ? 27.325 -14.900 14.222  1.00 22.03 ?  120 GLU   A CB   1 
ATOM   2584 C  CG   . GLU   A 1 120 ? 28.538 -15.816 14.244  1.00 29.98 ?  120 GLU   A CG   1 
ATOM   2585 C  CD   . GLU   A 1 120 ? 28.683 -16.561 15.558  1.00 37.43 ?  120 GLU   A CD   1 
ATOM   2586 O  OE1  . GLU   A 1 120 ? 28.300 -16.002 16.608  1.00 39.37 ?  120 GLU   A OE1  1 
ATOM   2587 O  OE2  . GLU   A 1 120 ? 29.178 -17.708 15.540  1.00 41.79 -1 120 GLU   A OE2  1 
ATOM   2588 H  H    . GLU   A 1 120 ? 28.409 -13.271 12.757  1.00 16.78 ?  120 GLU   A H    1 
ATOM   2589 H  HA   . GLU   A 1 120 ? 26.836 -15.319 12.291  1.00 19.75 ?  120 GLU   A HA   1 
ATOM   2590 H  HB2  . GLU   A 1 120 ? 27.561 -14.102 14.719  1.00 26.58 ?  120 GLU   A HB2  1 
ATOM   2591 H  HB3  . GLU   A 1 120 ? 26.605 -15.368 14.679  1.00 26.58 ?  120 GLU   A HB3  1 
ATOM   2592 H  HG2  . GLU   A 1 120 ? 28.464 -16.462 13.524  1.00 36.11 ?  120 GLU   A HG2  1 
ATOM   2593 H  HG3  . GLU   A 1 120 ? 29.342 -15.288 14.139  1.00 36.11 ?  120 GLU   A HG3  1 
ATOM   2594 N  N    . VAL   A 1 121 ? 25.303 -12.637 13.082  1.00 14.07 ?  121 VAL   A N    1 
ATOM   2595 C  CA   . VAL   A 1 121 ? 24.008 -11.972 13.201  1.00 13.79 ?  121 VAL   A CA   1 
ATOM   2596 C  C    . VAL   A 1 121 ? 24.119 -10.591 12.562  1.00 12.53 ?  121 VAL   A C    1 
ATOM   2597 O  O    . VAL   A 1 121 ? 25.087 -9.862  12.809  1.00 13.34 ?  121 VAL   A O    1 
ATOM   2598 C  CB   . VAL   A 1 121 ? 23.568 -11.820 14.675  1.00 16.84 ?  121 VAL   A CB   1 
ATOM   2599 C  CG1  . VAL   A 1 121 ? 22.167 -11.214 14.764  1.00 17.50 ?  121 VAL   A CG1  1 
ATOM   2600 C  CG2  . VAL   A 1 121 ? 23.607 -13.145 15.419  1.00 18.79 ?  121 VAL   A CG2  1 
ATOM   2601 H  H    . VAL   A 1 121 ? 25.967 -12.094 13.163  1.00 17.03 ?  121 VAL   A H    1 
ATOM   2602 H  HA   . VAL   A 1 121 ? 23.334 -12.489 12.731  1.00 16.69 ?  121 VAL   A HA   1 
ATOM   2603 H  HB   . VAL   A 1 121 ? 24.175 -11.215 15.123  1.00 20.35 ?  121 VAL   A HB   1 
ATOM   2604 H  HG11 . VAL   A 1 121 ? 21.861 -11.254 15.687  1.00 21.14 ?  121 VAL   A HG11 1 
ATOM   2605 H  HG12 . VAL   A 1 121 ? 22.197 -10.292 14.469  1.00 21.14 ?  121 VAL   A HG12 1 
ATOM   2606 H  HG13 . VAL   A 1 121 ? 21.562 -11.724 14.200  1.00 21.14 ?  121 VAL   A HG13 1 
ATOM   2607 H  HG21 . VAL   A 1 121 ? 23.254 -13.016 16.319  1.00 22.69 ?  121 VAL   A HG21 1 
ATOM   2608 H  HG22 . VAL   A 1 121 ? 23.058 -13.794 14.948  1.00 22.69 ?  121 VAL   A HG22 1 
ATOM   2609 H  HG23 . VAL   A 1 121 ? 24.521 -13.458 15.469  1.00 22.69 ?  121 VAL   A HG23 1 
ATOM   2610 N  N    . LEU   A 1 122 ? 23.107 -10.209 11.776  1.00 12.02 ?  122 LEU   A N    1 
ATOM   2611 C  CA   . LEU   A 1 122 ? 23.109 -8.915  11.096  1.00 11.94 ?  122 LEU   A CA   1 
ATOM   2612 C  C    . LEU   A 1 122 ? 21.709 -8.325  11.065  1.00 11.77 ?  122 LEU   A C    1 
ATOM   2613 O  O    . LEU   A 1 122 ? 20.720 -9.044  10.927  1.00 12.88 ?  122 LEU   A O    1 
ATOM   2614 C  CB   . LEU   A 1 122 ? 23.528 -9.021  9.627   1.00 13.25 ?  122 LEU   A CB   1 
ATOM   2615 C  CG   . LEU   A 1 122 ? 24.747 -9.861  9.279   1.00 13.61 ?  122 LEU   A CG   1 
ATOM   2616 C  CD1  . LEU   A 1 122 ? 24.349 -11.311 9.062   1.00 14.31 ?  122 LEU   A CD1  1 
ATOM   2617 C  CD2  . LEU   A 1 122 ? 25.431 -9.300  8.047   1.00 12.82 ?  122 LEU   A CD2  1 
ATOM   2618 H  H    . LEU   A 1 122 ? 22.403 -10.684 11.613  1.00 14.56 ?  122 LEU   A H    1 
ATOM   2619 H  HA   . LEU   A 1 122 ? 23.708 -8.301  11.551  1.00 14.47 ?  122 LEU   A HA   1 
ATOM   2620 H  HB2  . LEU   A 1 122 ? 22.789 -9.393  9.128   1.00 16.04 ?  122 LEU   A HB2  1 
ATOM   2621 H  HB3  . LEU   A 1 122 ? 23.717 -8.129  9.302   1.00 16.04 ?  122 LEU   A HB3  1 
ATOM   2622 H  HG   . LEU   A 1 122 ? 25.386 -9.840  10.010  1.00 16.47 ?  122 LEU   A HG   1 
ATOM   2623 H  HD11 . LEU   A 1 122 ? 25.127 -11.828 8.799   1.00 17.32 ?  122 LEU   A HD11 1 
ATOM   2624 H  HD12 . LEU   A 1 122 ? 23.985 -11.670 9.890   1.00 17.32 ?  122 LEU   A HD12 1 
ATOM   2625 H  HD13 . LEU   A 1 122 ? 23.674 -11.356 8.364   1.00 17.32 ?  122 LEU   A HD13 1 
ATOM   2626 H  HD21 . LEU   A 1 122 ? 26.184 -9.872  7.805   1.00 15.52 ?  122 LEU   A HD21 1 
ATOM   2627 H  HD22 . LEU   A 1 122 ? 24.798 -9.270  7.315   1.00 15.52 ?  122 LEU   A HD22 1 
ATOM   2628 H  HD23 . LEU   A 1 122 ? 25.754 -8.407  8.245   1.00 15.52 ?  122 LEU   A HD23 1 
ATOM   2629 N  N    . LEU   A 1 123 ? 21.646 -6.998  11.162  1.00 11.56 ?  123 LEU   A N    1 
ATOM   2630 C  CA   . LEU   A 1 123 ? 20.475 -6.205  10.793  1.00 11.34 ?  123 LEU   A CA   1 
ATOM   2631 C  C    . LEU   A 1 123 ? 20.726 -5.679  9.389   1.00 10.65 ?  123 LEU   A C    1 
ATOM   2632 O  O    . LEU   A 1 123 ? 21.774 -5.078  9.146   1.00 11.47 ?  123 LEU   A O    1 
ATOM   2633 C  CB   . LEU   A 1 123 ? 20.342 -5.024  11.755  1.00 11.85 ?  123 LEU   A CB   1 
ATOM   2634 C  CG   . LEU   A 1 123 ? 19.294 -3.963  11.412  1.00 12.67 ?  123 LEU   A CG   1 
ATOM   2635 C  CD1  . LEU   A 1 123 ? 17.893 -4.560  11.416  1.00 13.47 ?  123 LEU   A CD1  1 
ATOM   2636 C  CD2  . LEU   A 1 123 ? 19.385 -2.785  12.383  1.00 13.39 ?  123 LEU   A CD2  1 
ATOM   2637 H  H    . LEU   A 1 123 ? 22.302 -6.513  11.442  1.00 14.01 ?  123 LEU   A H    1 
ATOM   2638 H  HA   . LEU   A 1 123 ? 19.670 -6.745  10.808  1.00 13.75 ?  123 LEU   A HA   1 
ATOM   2639 H  HB2  . LEU   A 1 123 ? 20.106 -5.377  12.632  1.00 14.36 ?  123 LEU   A HB2  1 
ATOM   2640 H  HB3  . LEU   A 1 123 ? 21.193 -4.575  11.810  1.00 14.36 ?  123 LEU   A HB3  1 
ATOM   2641 H  HG   . LEU   A 1 123 ? 19.462 -3.619  10.521  1.00 15.34 ?  123 LEU   A HG   1 
ATOM   2642 H  HD11 . LEU   A 1 123 ? 17.247 -3.862  11.234  1.00 16.31 ?  123 LEU   A HD11 1 
ATOM   2643 H  HD12 . LEU   A 1 123 ? 17.842 -5.245  10.730  1.00 16.31 ?  123 LEU   A HD12 1 
ATOM   2644 H  HD13 . LEU   A 1 123 ? 17.721 -4.953  12.287  1.00 16.31 ?  123 LEU   A HD13 1 
ATOM   2645 H  HD21 . LEU   A 1 123 ? 18.712 -2.126  12.149  1.00 16.21 ?  123 LEU   A HD21 1 
ATOM   2646 H  HD22 . LEU   A 1 123 ? 19.225 -3.111  13.286  1.00 16.21 ?  123 LEU   A HD22 1 
ATOM   2647 H  HD23 . LEU   A 1 123 ? 20.268 -2.397  12.323  1.00 16.21 ?  123 LEU   A HD23 1 
ATOM   2648 N  N    A ALA   A 1 124 ? 19.759 -5.847  8.482   0.74 10.38 ?  124 ALA   A N    1 
ATOM   2649 N  N    B ALA   A 1 124 ? 19.814 -5.939  8.464   0.26 10.48 ?  124 ALA   A N    1 
ATOM   2650 C  CA   A ALA   A 1 124 ? 20.034 -5.557  7.082   0.74 10.39 ?  124 ALA   A CA   1 
ATOM   2651 C  CA   B ALA   A 1 124 ? 20.096 -5.683  7.061   0.26 10.60 ?  124 ALA   A CA   1 
ATOM   2652 C  C    A ALA   A 1 124 ? 18.795 -5.123  6.310   0.74 10.49 ?  124 ALA   A C    1 
ATOM   2653 C  C    B ALA   A 1 124 ? 18.863 -5.153  6.350   0.26 10.63 ?  124 ALA   A C    1 
ATOM   2654 O  O    A ALA   A 1 124 ? 17.667 -5.507  6.658   0.74 11.04 ?  124 ALA   A O    1 
ATOM   2655 O  O    B ALA   A 1 124 ? 17.730 -5.379  6.792   0.26 10.85 ?  124 ALA   A O    1 
ATOM   2656 C  CB   A ALA   A 1 124 ? 20.640 -6.775  6.379   0.74 11.02 ?  124 ALA   A CB   1 
ATOM   2657 C  CB   B ALA   A 1 124 ? 20.586 -6.951  6.348   0.26 10.91 ?  124 ALA   A CB   1 
ATOM   2658 H  H    A ALA   A 1 124 ? 18.957 -6.118  8.649   0.74 12.59 ?  124 ALA   A H    1 
ATOM   2659 H  H    B ALA   A 1 124 ? 19.032 -6.265  8.618   0.26 12.71 ?  124 ALA   A H    1 
ATOM   2660 H  HA   A ALA   A 1 124 ? 20.684 -4.840  7.043   0.74 12.61 ?  124 ALA   A HA   1 
ATOM   2661 H  HA   B ALA   A 1 124 ? 20.795 -5.016  7.003   0.26 12.86 ?  124 ALA   A HA   1 
ATOM   2662 H  HB1  A ALA   A 1 124 ? 20.818 -6.555  5.448   0.74 13.36 ?  124 ALA   A HB1  1 
ATOM   2663 H  HB1  B ALA   A 1 124 ? 20.768 -6.744  5.416   0.26 13.23 ?  124 ALA   A HB1  1 
ATOM   2664 H  HB2  A ALA   A 1 124 ? 21.477 -7.011  6.820   0.74 13.36 ?  124 ALA   A HB2  1 
ATOM   2665 H  HB2  B ALA   A 1 124 ? 21.401 -7.263  6.778   0.26 13.23 ?  124 ALA   A HB2  1 
ATOM   2666 H  HB3  A ALA   A 1 124 ? 20.023 -7.518  6.431   0.74 13.36 ?  124 ALA   A HB3  1 
ATOM   2667 H  HB3  B ALA   A 1 124 ? 19.901 -7.636  6.406   0.26 13.23 ?  124 ALA   A HB3  1 
ATOM   2668 N  N    A PRO   A 1 125 ? 18.985 -4.370  5.227   0.74 10.35 ?  125 PRO   A N    1 
ATOM   2669 N  N    B PRO   A 1 125 ? 19.056 -4.437  5.240   0.26 10.48 ?  125 PRO   A N    1 
ATOM   2670 C  CA   A PRO   A 1 125 ? 17.932 -4.138  4.239   0.74 10.59 ?  125 PRO   A CA   1 
ATOM   2671 C  CA   B PRO   A 1 125 ? 17.933 -4.083  4.372   0.26 10.63 ?  125 PRO   A CA   1 
ATOM   2672 C  C    A PRO   A 1 125 ? 17.986 -5.214  3.159   0.74 10.33 ?  125 PRO   A C    1 
ATOM   2673 C  C    B PRO   A 1 125 ? 17.874 -5.061  3.212   0.26 10.80 ?  125 PRO   A C    1 
ATOM   2674 O  O    A PRO   A 1 125 ? 18.957 -5.965  3.045   0.74 10.72 ?  125 PRO   A O    1 
ATOM   2675 O  O    B PRO   A 1 125 ? 18.748 -5.927  3.096   0.26 10.99 ?  125 PRO   A O    1 
ATOM   2676 C  CB   A PRO   A 1 125 ? 18.371 -2.800  3.633   0.74 10.57 ?  125 PRO   A CB   1 
ATOM   2677 C  CB   B PRO   A 1 125 ? 18.331 -2.690  3.882   0.26 10.59 ?  125 PRO   A CB   1 
ATOM   2678 C  CG   A PRO   A 1 125 ? 19.884 -2.958  3.561   0.74 10.91 ?  125 PRO   A CG   1 
ATOM   2679 C  CG   B PRO   A 1 125 ? 19.836 -2.813  3.721   0.26 10.88 ?  125 PRO   A CG   1 
ATOM   2680 C  CD   A PRO   A 1 125 ? 20.246 -3.703  4.837   0.74 10.82 ?  125 PRO   A CD   1 
ATOM   2681 C  CD   B PRO   A 1 125 ? 20.310 -3.822  4.765   0.26 10.57 ?  125 PRO   A CD   1 
ATOM   2682 H  HA   A PRO   A 1 125 ? 17.049 -4.079  4.641   0.74 12.85 ?  125 PRO   A HA   1 
ATOM   2683 H  HA   B PRO   A 1 125 ? 17.091 -4.051  4.860   0.26 12.89 ?  125 PRO   A HA   1 
ATOM   2684 H  HB2  A PRO   A 1 125 ? 17.979 -2.692  2.748   0.74 12.83 ?  125 PRO   A HB2  1 
ATOM   2685 H  HB2  B PRO   A 1 125 ? 17.899 -2.499  3.033   0.26 12.85 ?  125 PRO   A HB2  1 
ATOM   2686 H  HB3  A PRO   A 1 125 ? 18.114 -2.072  4.219   0.74 12.83 ?  125 PRO   A HB3  1 
ATOM   2687 H  HB3  B PRO   A 1 125 ? 18.101 -2.020  4.547   0.26 12.85 ?  125 PRO   A HB3  1 
ATOM   2688 H  HG2  A PRO   A 1 125 ? 20.126 -3.479  2.777   0.74 13.23 ?  125 PRO   A HG2  1 
ATOM   2689 H  HG2  B PRO   A 1 125 ? 20.038 -3.129  2.827   0.26 13.20 ?  125 PRO   A HG2  1 
ATOM   2690 H  HG3  A PRO   A 1 125 ? 20.304 -2.084  3.536   0.74 13.23 ?  125 PRO   A HG3  1 
ATOM   2691 H  HG3  B PRO   A 1 125 ? 20.248 -1.949  3.875   0.26 13.20 ?  125 PRO   A HG3  1 
ATOM   2692 H  HD2  A PRO   A 1 125 ? 20.941 -4.353  4.664   0.74 13.13 ?  125 PRO   A HD2  1 
ATOM   2693 H  HD2  B PRO   A 1 125 ? 20.885 -4.488  4.352   0.26 12.82 ?  125 PRO   A HD2  1 
ATOM   2694 H  HD3  A PRO   A 1 125 ? 20.514 -3.071  5.527   0.74 13.13 ?  125 PRO   A HD3  1 
ATOM   2695 H  HD3  B PRO   A 1 125 ? 20.762 -3.365  5.492   0.26 12.82 ?  125 PRO   A HD3  1 
ATOM   2696 N  N    A LEU   A 1 126 ? 16.933 -5.253  2.345   0.74 10.29 ?  126 LEU   A N    1 
ATOM   2697 N  N    B LEU   A 1 126 ? 16.876 -4.936  2.342   0.26 11.05 ?  126 LEU   A N    1 
ATOM   2698 C  CA   A LEU   A 1 126 ? 16.951 -6.072  1.141   0.74 10.90 ?  126 LEU   A CA   1 
ATOM   2699 C  CA   B LEU   A 1 126 ? 16.826 -5.752  1.132   0.26 10.97 ?  126 LEU   A CA   1 
ATOM   2700 C  C    A LEU   A 1 126 ? 17.880 -5.454  0.098   0.74 11.02 ?  126 LEU   A C    1 
ATOM   2701 C  C    B LEU   A 1 126 ? 17.784 -5.171  0.097   0.26 10.40 ?  126 LEU   A C    1 
ATOM   2702 O  O    A LEU   A 1 126 ? 17.646 -4.343  -0.387  0.74 12.18 ?  126 LEU   A O    1 
ATOM   2703 O  O    B LEU   A 1 126 ? 17.557 -4.075  -0.423  0.26 10.92 ?  126 LEU   A O    1 
ATOM   2704 C  CB   A LEU   A 1 126 ? 15.541 -6.222  0.586   0.74 11.41 ?  126 LEU   A CB   1 
ATOM   2705 C  CB   B LEU   A 1 126 ? 15.408 -5.784  0.575   0.26 11.70 ?  126 LEU   A CB   1 
ATOM   2706 C  CG   A LEU   A 1 126 ? 14.638 -7.166  1.379   0.74 12.02 ?  126 LEU   A CG   1 
ATOM   2707 C  CG   B LEU   A 1 126 ? 14.388 -6.633  1.328   0.26 11.94 ?  126 LEU   A CG   1 
ATOM   2708 C  CD1  A LEU   A 1 126 ? 13.215 -7.041  0.886   0.74 13.33 ?  126 LEU   A CD1  1 
ATOM   2709 C  CD1  B LEU   A 1 126 ? 13.009 -6.446  0.721   0.26 12.13 ?  126 LEU   A CD1  1 
ATOM   2710 C  CD2  A LEU   A 1 126 ? 15.123 -8.611  1.259   0.74 11.97 ?  126 LEU   A CD2  1 
ATOM   2711 C  CD2  B LEU   A 1 126 ? 14.779 -8.099  1.307   0.26 11.98 ?  126 LEU   A CD2  1 
ATOM   2712 H  H    A LEU   A 1 126 ? 16.206 -4.811  2.461   0.74 12.49 ?  126 LEU   A H    1 
ATOM   2713 H  H    B LEU   A 1 126 ? 16.207 -4.395  2.442   0.26 13.40 ?  126 LEU   A H    1 
ATOM   2714 H  HA   A LEU   A 1 126 ? 17.289 -6.951  1.355   0.74 13.22 ?  126 LEU   A HA   1 
ATOM   2715 H  HA   B LEU   A 1 126 ? 17.107 -6.655  1.350   0.26 13.30 ?  126 LEU   A HA   1 
ATOM   2716 H  HB2  A LEU   A 1 126 ? 15.112 -5.350  0.580   0.74 13.84 ?  126 LEU   A HB2  1 
ATOM   2717 H  HB2  B LEU   A 1 126 ? 15.072 -4.875  0.557   0.26 14.19 ?  126 LEU   A HB2  1 
ATOM   2718 H  HB3  A LEU   A 1 126 ? 15.593 -6.562  -0.321  0.74 13.84 ?  126 LEU   A HB3  1 
ATOM   2719 H  HB3  B LEU   A 1 126 ? 15.458 -6.128  -0.329  0.26 14.19 ?  126 LEU   A HB3  1 
ATOM   2720 H  HG   A LEU   A 1 126 ? 14.656 -6.917  2.315   0.74 14.57 ?  126 LEU   A HG   1 
ATOM   2721 H  HG   B LEU   A 1 126 ? 14.350 -6.341  2.253   0.26 14.47 ?  126 LEU   A HG   1 
ATOM   2722 H  HD11 A LEU   A 1 126 ? 12.650 -7.648  1.391   0.74 16.13 ?  126 LEU   A HD11 1 
ATOM   2723 H  HD11 B LEU   A 1 126 ? 12.459 -7.210  0.954   0.26 14.70 ?  126 LEU   A HD11 1 
ATOM   2724 H  HD12 A LEU   A 1 126 ? 12.914 -6.128  1.013   0.74 16.13 ?  126 LEU   A HD12 1 
ATOM   2725 H  HD12 B LEU   A 1 126 ? 12.613 -5.632  1.070   0.26 14.70 ?  126 LEU   A HD12 1 
ATOM   2726 H  HD13 A LEU   A 1 126 ? 13.184 -7.271  -0.057  0.74 16.13 ?  126 LEU   A HD13 1 
ATOM   2727 H  HD13 B LEU   A 1 126 ? 13.094 -6.386  -0.244  0.26 14.70 ?  126 LEU   A HD13 1 
ATOM   2728 H  HD21 A LEU   A 1 126 ? 14.454 -9.204  1.626   0.74 14.50 ?  126 LEU   A HD21 1 
ATOM   2729 H  HD21 B LEU   A 1 126 ? 14.060 -8.622  1.693   0.26 14.51 ?  126 LEU   A HD21 1 
ATOM   2730 H  HD22 A LEU   A 1 126 ? 15.273 -8.817  0.322   0.74 14.50 ?  126 LEU   A HD22 1 
ATOM   2731 H  HD22 B LEU   A 1 126 ? 14.929 -8.368  0.387   0.26 14.51 ?  126 LEU   A HD22 1 
ATOM   2732 H  HD23 A LEU   A 1 126 ? 15.957 -8.706  1.751   0.74 14.50 ?  126 LEU   A HD23 1 
ATOM   2733 H  HD23 B LEU   A 1 126 ? 15.589 -8.215  1.824   0.26 14.51 ?  126 LEU   A HD23 1 
ATOM   2734 N  N    A LEU   A 1 127 ? 18.929 -6.187  -0.254  0.74 10.74 ?  127 LEU   A N    1 
ATOM   2735 N  N    B LEU   A 1 127 ? 18.842 -5.908  -0.227  0.26 9.84  ?  127 LEU   A N    1 
ATOM   2736 C  CA   A LEU   A 1 127 ? 19.917 -5.689  -1.196  0.74 10.41 ?  127 LEU   A CA   1 
ATOM   2737 C  CA   B LEU   A 1 127 ? 19.837 -5.391  -1.155  0.26 9.88  ?  127 LEU   A CA   1 
ATOM   2738 C  C    A LEU   A 1 127 ? 19.298 -5.503  -2.570  0.74 10.09 ?  127 LEU   A C    1 
ATOM   2739 C  C    B LEU   A 1 127 ? 19.289 -5.331  -2.579  0.26 10.16 ?  127 LEU   A C    1 
ATOM   2740 O  O    A LEU   A 1 127 ? 18.465 -6.298  -3.016  0.74 10.65 ?  127 LEU   A O    1 
ATOM   2741 O  O    B LEU   A 1 127 ? 18.453 -6.141  -2.990  0.26 10.29 ?  127 LEU   A O    1 
ATOM   2742 C  CB   A LEU   A 1 127 ? 21.088 -6.665  -1.290  0.74 11.11 ?  127 LEU   A CB   1 
ATOM   2743 C  CB   B LEU   A 1 127 ? 21.096 -6.256  -1.131  0.26 9.91  ?  127 LEU   A CB   1 
ATOM   2744 C  CG   A LEU   A 1 127 ? 21.886 -6.887  -0.008  0.74 11.75 ?  127 LEU   A CG   1 
ATOM   2745 C  CG   B LEU   A 1 127 ? 21.883 -6.265  0.183   0.26 10.17 ?  127 LEU   A CG   1 
ATOM   2746 C  CD1  A LEU   A 1 127 ? 22.983 -7.891  -0.274  0.74 12.23 ?  127 LEU   A CD1  1 
ATOM   2747 C  CD1  B LEU   A 1 127 ? 23.062 -7.220  0.090   0.26 10.48 ?  127 LEU   A CD1  1 
ATOM   2748 C  CD2  A LEU   A 1 127 ? 22.475 -5.588  0.495   0.74 12.47 ?  127 LEU   A CD2  1 
ATOM   2749 C  CD2  B LEU   A 1 127 ? 22.349 -4.857  0.558   0.26 10.40 ?  127 LEU   A CD2  1 
ATOM   2750 H  H    A LEU   A 1 127 ? 19.090 -6.975  0.046   0.74 13.03 ?  127 LEU   A H    1 
ATOM   2751 H  H    B LEU   A 1 127 ? 19.004 -6.695  0.084   0.26 11.94 ?  127 LEU   A H    1 
ATOM   2752 H  HA   A LEU   A 1 127 ? 20.253 -4.834  -0.892  0.74 12.64 ?  127 LEU   A HA   1 
ATOM   2753 H  HA   B LEU   A 1 127 ? 20.078 -4.490  -0.878  0.26 12.00 ?  127 LEU   A HA   1 
ATOM   2754 H  HB2  A LEU   A 1 127 ? 20.740 -7.529  -1.566  0.74 13.48 ?  127 LEU   A HB2  1 
ATOM   2755 H  HB2  B LEU   A 1 127 ? 20.836 -7.170  -1.325  0.26 12.03 ?  127 LEU   A HB2  1 
ATOM   2756 H  HB3  A LEU   A 1 127 ? 21.705 -6.337  -1.960  0.74 13.48 ?  127 LEU   A HB3  1 
ATOM   2757 H  HB3  B LEU   A 1 127 ? 21.690 -5.934  -1.827  0.26 12.03 ?  127 LEU   A HB3  1 
ATOM   2758 H  HG   A LEU   A 1 127 ? 21.299 -7.246  0.679   0.74 14.24 ?  127 LEU   A HG   1 
ATOM   2759 H  HG   B LEU   A 1 127 ? 21.300 -6.583  0.890   0.26 12.34 ?  127 LEU   A HG   1 
ATOM   2760 H  HD11 A LEU   A 1 127 ? 23.468 -8.053  0.551   0.74 14.81 ?  127 LEU   A HD11 1 
ATOM   2761 H  HD11 B LEU   A 1 127 ? 23.561 -7.183  0.920   0.26 12.72 ?  127 LEU   A HD11 1 
ATOM   2762 H  HD12 A LEU   A 1 127 ? 22.585 -8.718  -0.591  0.74 14.81 ?  127 LEU   A HD12 1 
ATOM   2763 H  HD12 B LEU   A 1 127 ? 22.729 -8.119  -0.057  0.26 12.72 ?  127 LEU   A HD12 1 
ATOM   2764 H  HD13 A LEU   A 1 127 ? 23.581 -7.532  -0.946  0.74 14.81 ?  127 LEU   A HD13 1 
ATOM   2765 H  HD13 B LEU   A 1 127 ? 23.627 -6.951  -0.650  0.26 12.72 ?  127 LEU   A HD13 1 
ATOM   2766 H  HD21 A LEU   A 1 127 ? 23.088 -5.777  1.220   0.74 15.10 ?  127 LEU   A HD21 1 
ATOM   2767 H  HD21 B LEU   A 1 127 ? 22.964 -4.920  1.305   0.26 12.62 ?  127 LEU   A HD21 1 
ATOM   2768 H  HD22 A LEU   A 1 127 ? 22.952 -5.156  -0.236  0.74 15.10 ?  127 LEU   A HD22 1 
ATOM   2769 H  HD22 B LEU   A 1 127 ? 22.793 -4.458  -0.206  0.26 12.62 ?  127 LEU   A HD22 1 
ATOM   2770 H  HD23 A LEU   A 1 127 ? 21.760 -5.011  0.804   0.74 15.10 ?  127 LEU   A HD23 1 
ATOM   2771 H  HD23 B LEU   A 1 127 ? 21.577 -4.325  0.808   0.26 12.62 ?  127 LEU   A HD23 1 
ATOM   2772 N  N    A SER   A 1 128 ? 19.726 -4.441  -3.241  0.74 10.56 ?  128 SER   A N    1 
ATOM   2773 N  N    B SER   A 1 128 ? 19.781 -4.344  -3.327  0.26 10.45 ?  128 SER   A N    1 
ATOM   2774 C  CA   A SER   A 1 128 ? 19.318 -4.045  -4.581  0.74 10.97 ?  128 SER   A CA   1 
ATOM   2775 C  CA   B SER   A 1 128 ? 19.455 -4.117  -4.733  0.26 10.15 ?  128 SER   A CA   1 
ATOM   2776 C  C    A SER   A 1 128 ? 17.858 -3.602  -4.669  0.74 11.44 ?  128 SER   A C    1 
ATOM   2777 C  C    B SER   A 1 128 ? 18.031 -3.624  -4.976  0.26 9.79  ?  128 SER   A C    1 
ATOM   2778 O  O    A SER   A 1 128 ? 17.399 -3.284  -5.766  0.74 12.61 ?  128 SER   A O    1 
ATOM   2779 O  O    B SER   A 1 128 ? 17.698 -3.245  -6.103  0.26 9.75  ?  128 SER   A O    1 
ATOM   2780 C  CB   A SER   A 1 128 ? 19.657 -5.085  -5.661  0.74 11.25 ?  128 SER   A CB   1 
ATOM   2781 C  CB   B SER   A 1 128 ? 19.762 -5.349  -5.588  0.26 10.31 ?  128 SER   A CB   1 
ATOM   2782 O  OG   A SER   A 1 128 ? 21.064 -5.290  -5.741  0.74 11.55 ?  128 SER   A OG   1 
ATOM   2783 O  OG   B SER   A 1 128 ? 21.164 -5.539  -5.705  0.26 10.31 ?  128 SER   A OG   1 
ATOM   2784 H  H    A SER   A 1 128 ? 20.310 -3.892  -2.915  0.74 12.81 ?  128 SER   A H    1 
ATOM   2785 H  H    B SER   A 1 128 ? 20.349 -3.774  -3.025  0.26 12.68 ?  128 SER   A H    1 
ATOM   2786 H  HA   A SER   A 1 128 ? 19.836 -3.261  -4.808  0.74 13.30 ?  128 SER   A HA   1 
ATOM   2787 H  HA   B SER   A 1 128 ? 20.039 -3.412  -5.046  0.26 12.32 ?  128 SER   A HA   1 
ATOM   2788 H  HB2  A SER   A 1 128 ? 19.217 -5.921  -5.442  0.74 13.64 ?  128 SER   A HB2  1 
ATOM   2789 H  HB2  B SER   A 1 128 ? 19.365 -6.129  -5.180  0.26 12.51 ?  128 SER   A HB2  1 
ATOM   2790 H  HB3  A SER   A 1 128 ? 19.339 -4.760  -6.521  0.74 13.64 ?  128 SER   A HB3  1 
ATOM   2791 H  HB3  B SER   A 1 128 ? 19.382 -5.211  -6.475  0.26 12.51 ?  128 SER   A HB3  1 
ATOM   2792 H  HG   A SER   A 1 128 ? 21.446 -4.564  -5.909  0.74 14.00 ?  128 SER   A HG   1 
ATOM   2793 H  HG   B SER   A 1 128 ? 21.509 -4.862  -6.068  0.26 12.51 ?  128 SER   A HG   1 
ATOM   2794 N  N    A ALA   A 1 129 ? 17.131 -3.538  -3.553  0.74 11.97 ?  129 ALA   A N    1 
ATOM   2795 N  N    B ALA   A 1 129 ? 17.192 -3.609  -3.941  0.26 10.00 ?  129 ALA   A N    1 
ATOM   2796 C  CA   A ALA   A 1 129 ? 15.758 -3.057  -3.548  0.74 12.24 ?  129 ALA   A CA   1 
ATOM   2797 C  CA   B ALA   A 1 129 ? 15.840 -3.083  -4.051  0.26 10.32 ?  129 ALA   A CA   1 
ATOM   2798 C  C    A ALA   A 1 129 ? 15.738 -1.528  -3.522  0.74 11.83 ?  129 ALA   A C    1 
ATOM   2799 C  C    B ALA   A 1 129 ? 15.863 -1.577  -3.778  0.26 10.85 ?  129 ALA   A C    1 
ATOM   2800 O  O    A ALA   A 1 129 ? 16.774 -0.859  -3.592  0.74 11.81 ?  129 ALA   A O    1 
ATOM   2801 O  O    B ALA   A 1 129 ? 16.924 -0.947  -3.741  0.26 10.83 ?  129 ALA   A O    1 
ATOM   2802 C  CB   A ALA   A 1 129 ? 14.987 -3.659  -2.372  0.74 13.22 ?  129 ALA   A CB   1 
ATOM   2803 C  CB   B ALA   A 1 129 ? 14.896 -3.857  -3.129  0.26 10.17 ?  129 ALA   A CB   1 
ATOM   2804 H  H    A ALA   A 1 129 ? 17.419 -3.769  -2.777  0.74 14.51 ?  129 ALA   A H    1 
ATOM   2805 H  H    B ALA   A 1 129 ? 17.383 -3.901  -3.155  0.26 12.14 ?  129 ALA   A H    1 
ATOM   2806 H  HA   A ALA   A 1 129 ? 15.324 -3.343  -4.364  0.74 14.83 ?  129 ALA   A HA   1 
ATOM   2807 H  HA   B ALA   A 1 129 ? 15.532 -3.210  -4.958  0.26 12.52 ?  129 ALA   A HA   1 
ATOM   2808 H  HB1  A ALA   A 1 129 ? 14.073 -3.332  -2.393  0.74 16.00 ?  129 ALA   A HB1  1 
ATOM   2809 H  HB1  B ALA   A 1 129 ? 14.005 -3.479  -3.205  0.26 12.34 ?  129 ALA   A HB1  1 
ATOM   2810 H  HB2  A ALA   A 1 129 ? 14.996 -4.624  -2.450  0.74 16.00 ?  129 ALA   A HB2  1 
ATOM   2811 H  HB2  B ALA   A 1 129 ? 14.886 -4.786  -3.401  0.26 12.34 ?  129 ALA   A HB2  1 
ATOM   2812 H  HB3  A ALA   A 1 129 ? 15.414 -3.389  -1.543  0.74 16.00 ?  129 ALA   A HB3  1 
ATOM   2813 H  HB3  B ALA   A 1 129 ? 15.211 -3.780  -2.216  0.26 12.34 ?  129 ALA   A HB3  1 
ATOM   2814 N  N    A GLY   A 1 130 ? 14.537 -0.966  -3.447  0.74 12.57 ?  130 GLY   A N    1 
ATOM   2815 N  N    B GLY   A 1 130 ? 14.690 -0.977  -3.605  0.26 11.44 ?  130 GLY   A N    1 
ATOM   2816 C  CA   A GLY   A 1 130 ? 14.414 0.480   -3.426  0.74 12.83 ?  130 GLY   A CA   1 
ATOM   2817 C  CA   B GLY   A 1 130 ? 14.646 0.451   -3.338  0.26 11.87 ?  130 GLY   A CA   1 
ATOM   2818 C  C    A GLY   A 1 130 ? 15.060 1.106   -4.645  0.74 12.31 ?  130 GLY   A C    1 
ATOM   2819 C  C    B GLY   A 1 130 ? 15.162 1.221   -4.536  0.26 12.16 ?  130 GLY   A C    1 
ATOM   2820 O  O    A GLY   A 1 130 ? 14.872 0.650   -5.776  0.74 12.33 ?  130 GLY   A O    1 
ATOM   2821 O  O    B GLY   A 1 130 ? 14.814 0.923   -5.683  0.26 12.33 ?  130 GLY   A O    1 
ATOM   2822 H  H    A GLY   A 1 130 ? 13.791 -1.395  -3.411  0.74 15.22 ?  130 GLY   A H    1 
ATOM   2823 H  H    B GLY   A 1 130 ? 13.924 -1.362  -3.648  0.26 13.87 ?  130 GLY   A H    1 
ATOM   2824 H  HA2  A GLY   A 1 130 ? 13.474 0.727   -3.410  0.74 15.54 ?  130 GLY   A HA2  1 
ATOM   2825 H  HA2  B GLY   A 1 130 ? 13.734 0.726   -3.144  0.26 14.38 ?  130 GLY   A HA2  1 
ATOM   2826 H  HA3  A GLY   A 1 130 ? 14.842 0.834   -2.636  0.74 15.54 ?  130 GLY   A HA3  1 
ATOM   2827 H  HA3  B GLY   A 1 130 ? 15.203 0.664   -2.576  0.26 14.38 ?  130 GLY   A HA3  1 
ATOM   2828 N  N    A ILE   A 1 131 ? 15.835 2.173   -4.415  0.74 12.47 ?  131 ILE   A N    1 
ATOM   2829 N  N    B ILE   A 1 131 ? 16.022 2.211   -4.277  0.26 12.37 ?  131 ILE   A N    1 
ATOM   2830 C  CA   A ILE   A 1 131 ? 16.418 2.948   -5.511  0.74 12.39 ?  131 ILE   A CA   1 
ATOM   2831 C  CA   B ILE   A 1 131 ? 16.565 3.033   -5.354  0.26 12.42 ?  131 ILE   A CA   1 
ATOM   2832 C  C    A ILE   A 1 131 ? 17.463 2.185   -6.317  0.74 12.26 ?  131 ILE   A C    1 
ATOM   2833 C  C    B ILE   A 1 131 ? 17.506 2.261   -6.265  0.26 12.28 ?  131 ILE   A C    1 
ATOM   2834 O  O    A ILE   A 1 131 ? 17.911 2.697   -7.352  0.74 13.25 ?  131 ILE   A O    1 
ATOM   2835 O  O    B ILE   A 1 131 ? 17.835 2.751   -7.352  0.26 12.50 ?  131 ILE   A O    1 
ATOM   2836 C  CB   A ILE   A 1 131 ? 16.951 4.323   -5.047  0.74 13.26 ?  131 ILE   A CB   1 
ATOM   2837 C  CB   B ILE   A 1 131 ? 17.262 4.304   -4.816  0.26 12.77 ?  131 ILE   A CB   1 
ATOM   2838 C  CG1  A ILE   A 1 131 ? 18.189 4.174   -4.155  0.74 14.40 ?  131 ILE   A CG1  1 
ATOM   2839 C  CG1  B ILE   A 1 131 ? 18.500 3.952   -3.984  0.26 13.04 ?  131 ILE   A CG1  1 
ATOM   2840 C  CG2  A ILE   A 1 131 ? 15.853 5.115   -4.338  0.74 13.73 ?  131 ILE   A CG2  1 
ATOM   2841 C  CG2  B ILE   A 1 131 ? 16.290 5.134   -3.996  0.26 12.89 ?  131 ILE   A CG2  1 
ATOM   2842 C  CD1  A ILE   A 1 131 ? 18.809 5.506   -3.745  0.74 15.75 ?  131 ILE   A CD1  1 
ATOM   2843 C  CD1  B ILE   A 1 131 ? 19.254 5.173   -3.461  0.26 13.14 ?  131 ILE   A CD1  1 
ATOM   2844 H  H    A ILE   A 1 131 ? 16.016 2.477   -3.626  0.74 15.10 ?  131 ILE   A H    1 
ATOM   2845 H  H    B ILE   A 1 131 ? 16.313 2.416   -3.494  0.26 14.99 ?  131 ILE   A H    1 
ATOM   2846 H  HA   A ILE   A 1 131 ? 15.706 3.138   -6.128  0.74 15.00 ?  131 ILE   A HA   1 
ATOM   2847 H  HA   B ILE   A 1 131 ? 15.823 3.336   -5.899  0.26 15.04 ?  131 ILE   A HA   1 
ATOM   2848 H  HB   A ILE   A 1 131 ? 17.211 4.820   -5.834  0.74 16.05 ?  131 ILE   A HB   1 
ATOM   2849 H  HB   B ILE   A 1 131 ? 17.546 4.837   -5.575  0.26 15.46 ?  131 ILE   A HB   1 
ATOM   2850 H  HG12 A ILE   A 1 131 ? 17.945 3.701   -3.345  0.74 17.42 ?  131 ILE   A HG12 1 
ATOM   2851 H  HG12 B ILE   A 1 131 ? 18.224 3.427   -3.219  0.26 15.79 ?  131 ILE   A HG12 1 
ATOM   2852 H  HG13 A ILE   A 1 131 ? 18.871 3.675   -4.634  0.74 17.42 ?  131 ILE   A HG13 1 
ATOM   2853 H  HG13 B ILE   A 1 131 ? 19.116 3.444   -4.532  0.26 15.79 ?  131 ILE   A HG13 1 
ATOM   2854 H  HG21 A ILE   A 1 131 ? 16.159 6.022   -4.189  0.74 16.61 ?  131 ILE   A HG21 1 
ATOM   2855 H  HG21 B ILE   A 1 131 ? 16.680 6.007   -3.832  0.26 15.60 ?  131 ILE   A HG21 1 
ATOM   2856 H  HG22 A ILE   A 1 131 ? 15.061 5.120   -4.896  0.74 16.61 ?  131 ILE   A HG22 1 
ATOM   2857 H  HG22 B ILE   A 1 131 ? 15.463 5.230   -4.493  0.26 15.60 ?  131 ILE   A HG22 1 
ATOM   2858 H  HG23 A ILE   A 1 131 ? 15.654 4.689   -3.487  0.74 16.61 ?  131 ILE   A HG23 1 
ATOM   2859 H  HG23 B ILE   A 1 131 ? 16.121 4.681   -3.156  0.26 15.60 ?  131 ILE   A HG23 1 
ATOM   2860 H  HD11 A ILE   A 1 131 ? 19.655 5.340   -3.299  0.74 19.03 ?  131 ILE   A HD11 1 
ATOM   2861 H  HD11 B ILE   A 1 131 ? 20.093 4.884   -3.069  0.26 15.90 ?  131 ILE   A HD11 1 
ATOM   2862 H  HD12 A ILE   A 1 131 ? 18.955 6.045   -4.538  0.74 19.03 ?  131 ILE   A HD12 1 
ATOM   2863 H  HD12 B ILE   A 1 131 ? 19.428 5.780   -4.200  0.26 15.90 ?  131 ILE   A HD12 1 
ATOM   2864 H  HD13 A ILE   A 1 131 ? 18.204 5.966   -3.141  0.74 19.03 ?  131 ILE   A HD13 1 
ATOM   2865 H  HD13 B ILE   A 1 131 ? 18.713 5.621   -2.790  0.26 15.90 ?  131 ILE   A HD13 1 
ATOM   2866 N  N    A PHE   A 1 132 ? 17.870 0.981   -5.885  0.74 11.73 ?  132 PHE   A N    1 
ATOM   2867 N  N    B PHE   A 1 132 ? 17.948 1.065   -5.858  0.26 12.18 ?  132 PHE   A N    1 
ATOM   2868 C  CA   A PHE   A 1 132 ? 18.736 0.149   -6.717  0.74 11.88 ?  132 PHE   A CA   1 
ATOM   2869 C  CA   B PHE   A 1 132 ? 18.880 0.295   -6.676  0.26 12.35 ?  132 PHE   A CA   1 
ATOM   2870 C  C    A PHE   A 1 132 ? 17.967 -0.608  -7.802  0.74 12.45 ?  132 PHE   A C    1 
ATOM   2871 C  C    B PHE   A 1 132 ? 18.209 -0.421  -7.849  0.26 12.89 ?  132 PHE   A C    1 
ATOM   2872 O  O    A PHE   A 1 132 ? 18.596 -1.248  -8.651  0.74 12.96 ?  132 PHE   A O    1 
ATOM   2873 O  O    B PHE   A 1 132 ? 18.914 -0.877  -8.756  0.26 13.26 ?  132 PHE   A O    1 
ATOM   2874 C  CB   A PHE   A 1 132 ? 19.557 -0.831  -5.865  0.74 11.29 ?  132 PHE   A CB   1 
ATOM   2875 C  CB   B PHE   A 1 132 ? 19.675 -0.693  -5.816  0.26 11.57 ?  132 PHE   A CB   1 
ATOM   2876 C  CG   A PHE   A 1 132 ? 20.786 -0.226  -5.206  0.74 11.18 ?  132 PHE   A CG   1 
ATOM   2877 C  CG   B PHE   A 1 132 ? 20.871 -0.082  -5.123  0.26 11.14 ?  132 PHE   A CG   1 
ATOM   2878 C  CD1  A PHE   A 1 132 ? 20.676 0.823   -4.311  0.74 12.03 ?  132 PHE   A CD1  1 
ATOM   2879 C  CD1  B PHE   A 1 132 ? 20.706 0.797   -4.063  0.26 11.43 ?  132 PHE   A CD1  1 
ATOM   2880 C  CD2  A PHE   A 1 132 ? 22.046 -0.767  -5.436  0.74 11.63 ?  132 PHE   A CD2  1 
ATOM   2881 C  CD2  B PHE   A 1 132 ? 22.161 -0.406  -5.520  0.26 11.00 ?  132 PHE   A CD2  1 
ATOM   2882 C  CE1  A PHE   A 1 132 ? 21.804 1.349   -3.692  0.74 12.52 ?  132 PHE   A CE1  1 
ATOM   2883 C  CE1  B PHE   A 1 132 ? 21.803 1.351   -3.423  0.26 11.57 ?  132 PHE   A CE1  1 
ATOM   2884 C  CE2  A PHE   A 1 132 ? 23.173 -0.248  -4.817  0.74 11.99 ?  132 PHE   A CE2  1 
ATOM   2885 C  CE2  B PHE   A 1 132 ? 23.261 0.146   -4.883  0.26 11.34 ?  132 PHE   A CE2  1 
ATOM   2886 C  CZ   A PHE   A 1 132 ? 23.047 0.812   -3.942  0.74 12.22 ?  132 PHE   A CZ   1 
ATOM   2887 C  CZ   B PHE   A 1 132 ? 23.079 1.024   -3.832  0.26 11.53 ?  132 PHE   A CZ   1 
ATOM   2888 H  H    A PHE   A 1 132 ? 17.660 0.629   -5.119  0.74 14.22 ?  132 PHE   A H    1 
ATOM   2889 H  H    B PHE   A 1 132 ? 17.732 0.688   -5.112  0.26 14.75 ?  132 PHE   A H    1 
ATOM   2890 H  HA   A PHE   A 1 132 ? 19.370 0.731   -7.157  0.74 14.39 ?  132 PHE   A HA   1 
ATOM   2891 H  HA   B PHE   A 1 132 ? 19.518 0.920   -7.047  0.26 14.96 ?  132 PHE   A HA   1 
ATOM   2892 H  HB2  A PHE   A 1 132 ? 18.993 -1.180  -5.157  0.74 13.69 ?  132 PHE   A HB2  1 
ATOM   2893 H  HB2  B PHE   A 1 132 ? 19.092 -1.054  -5.133  0.26 14.03 ?  132 PHE   A HB2  1 
ATOM   2894 H  HB3  A PHE   A 1 132 ? 19.859 -1.562  -6.430  0.74 13.69 ?  132 PHE   A HB3  1 
ATOM   2895 H  HB3  B PHE   A 1 132 ? 19.999 -1.408  -6.386  0.26 14.03 ?  132 PHE   A HB3  1 
ATOM   2896 H  HD1  A PHE   A 1 132 ? 19.844 1.192   -4.129  0.74 14.58 ?  132 PHE   A HD1  1 
ATOM   2897 H  HD1  B PHE   A 1 132 ? 19.850 1.025   -3.782  0.26 13.86 ?  132 PHE   A HD1  1 
ATOM   2898 H  HD2  A PHE   A 1 132 ? 22.141 -1.483  -6.023  0.74 14.09 ?  132 PHE   A HD2  1 
ATOM   2899 H  HD2  B PHE   A 1 132 ? 22.290 -0.996  -6.228  0.26 13.34 ?  132 PHE   A HD2  1 
ATOM   2900 H  HE1  A PHE   A 1 132 ? 21.722 2.064   -3.099  0.74 15.16 ?  132 PHE   A HE1  1 
ATOM   2901 H  HE1  B PHE   A 1 132 ? 21.680 1.944   -2.716  0.26 14.02 ?  132 PHE   A HE1  1 
ATOM   2902 H  HE2  A PHE   A 1 132 ? 24.015 -0.610  -4.992  0.74 14.53 ?  132 PHE   A HE2  1 
ATOM   2903 H  HE2  B PHE   A 1 132 ? 24.121 -0.076  -5.162  0.26 13.75 ?  132 PHE   A HE2  1 
ATOM   2904 H  HZ   A PHE   A 1 132 ? 23.802 1.171   -3.528  0.74 14.81 ?  132 PHE   A HZ   1 
ATOM   2905 H  HZ   B PHE   A 1 132 ? 23.818 1.396   -3.405  0.26 13.98 ?  132 PHE   A HZ   1 
ATOM   2906 N  N    A GLY   A 1 133 ? 16.632 -0.572  -7.788  0.74 12.62 ?  133 GLY   A N    1 
ATOM   2907 N  N    B GLY   A 1 133 ? 16.879 -0.547  -7.855  0.26 13.05 ?  133 GLY   A N    1 
ATOM   2908 C  CA   A GLY   A 1 133 ? 15.838 -0.937  -8.946  0.74 13.43 ?  133 GLY   A CA   1 
ATOM   2909 C  CA   B GLY   A 1 133 ? 16.135 -0.896  -9.050  0.26 13.18 ?  133 GLY   A CA   1 
ATOM   2910 C  C    A GLY   A 1 133 ? 15.543 -2.409  -9.168  0.74 13.66 ?  133 GLY   A C    1 
ATOM   2911 C  C    B GLY   A 1 133 ? 15.491 -2.271  -9.062  0.26 13.11 ?  133 GLY   A C    1 
ATOM   2912 O  O    A GLY   A 1 133 ? 14.917 -2.735  -10.183 0.74 14.54 ?  133 GLY   A O    1 
ATOM   2913 O  O    B GLY   A 1 133 ? 14.597 -2.503  -9.886  0.26 12.96 ?  133 GLY   A O    1 
ATOM   2914 H  H    A GLY   A 1 133 ? 16.164 -0.335  -7.106  0.74 15.28 ?  133 GLY   A H    1 
ATOM   2915 H  H    B GLY   A 1 133 ? 16.384 -0.434  -7.161  0.26 15.80 ?  133 GLY   A H    1 
ATOM   2916 H  HA2  A GLY   A 1 133 ? 14.986 -0.479  -8.887  0.74 16.26 ?  133 GLY   A HA2  1 
ATOM   2917 H  HA2  B GLY   A 1 133 ? 15.432 -0.245  -9.189  0.26 15.96 ?  133 GLY   A HA2  1 
ATOM   2918 H  HA3  A GLY   A 1 133 ? 16.290 -0.617  -9.740  0.74 16.26 ?  133 GLY   A HA3  1 
ATOM   2919 H  HA3  B GLY   A 1 133 ? 16.729 -0.848  -9.814  0.26 15.96 ?  133 GLY   A HA3  1 
ATOM   2920 N  N    A ALA   A 1 134 ? 15.960 -3.309  -8.279  0.74 13.21 ?  134 ALA   A N    1 
ATOM   2921 N  N    B ALA   A 1 134 ? 15.906 -3.188  -8.194  0.26 13.11 ?  134 ALA   A N    1 
ATOM   2922 C  CA   A ALA   A 1 134 ? 15.633 -4.717  -8.446  0.74 13.50 ?  134 ALA   A CA   1 
ATOM   2923 C  CA   B ALA   A 1 134 ? 15.448 -4.566  -8.299  0.26 13.14 ?  134 ALA   A CA   1 
ATOM   2924 C  C    A ALA   A 1 134 ? 14.275 -5.028  -7.817  0.74 13.56 ?  134 ALA   A C    1 
ATOM   2925 C  C    B ALA   A 1 134 ? 14.140 -4.786  -7.546  0.26 12.83 ?  134 ALA   A C    1 
ATOM   2926 O  O    A ALA   A 1 134 ? 13.712 -4.237  -7.057  0.74 14.81 ?  134 ALA   A O    1 
ATOM   2927 O  O    B ALA   A 1 134 ? 13.760 -4.019  -6.658  0.26 13.02 ?  134 ALA   A O    1 
ATOM   2928 C  CB   A ALA   A 1 134 ? 16.727 -5.606  -7.854  0.74 14.40 ?  134 ALA   A CB   1 
ATOM   2929 C  CB   B ALA   A 1 134 ? 16.503 -5.537  -7.776  0.26 13.46 ?  134 ALA   A CB   1 
ATOM   2930 H  H    A ALA   A 1 134 ? 16.443 -3.125  -7.583  0.74 16.00 ?  134 ALA   A H    1 
ATOM   2931 H  H    B ALA   A 1 134 ? 16.452 -3.036  -7.546  0.26 15.88 ?  134 ALA   A H    1 
ATOM   2932 H  HA   A ALA   A 1 134 ? 15.580 -4.909  -9.395  0.74 16.34 ?  134 ALA   A HA   1 
ATOM   2933 H  HA   B ALA   A 1 134 ? 15.288 -4.766  -9.233  0.26 15.91 ?  134 ALA   A HA   1 
ATOM   2934 H  HB1  A ALA   A 1 134 ? 16.489 -6.533  -7.997  0.74 17.42 ?  134 ALA   A HB1  1 
ATOM   2935 H  HB1  B ALA   A 1 134 ? 16.171 -6.441  -7.881  0.26 16.29 ?  134 ALA   A HB1  1 
ATOM   2936 H  HB2  A ALA   A 1 134 ? 17.571 -5.409  -8.297  0.74 17.42 ?  134 ALA   A HB2  1 
ATOM   2937 H  HB2  B ALA   A 1 134 ? 17.315 -5.419  -8.290  0.26 16.29 ?  134 ALA   A HB2  1 
ATOM   2938 H  HB3  A ALA   A 1 134 ? 16.805 -5.423  -6.905  0.74 17.42 ?  134 ALA   A HB3  1 
ATOM   2939 H  HB3  B ALA   A 1 134 ? 16.668 -5.348  -6.841  0.26 16.29 ?  134 ALA   A HB3  1 
ATOM   2940 N  N    A ASP   A 1 135 ? 13.751 -6.204  -8.150  0.74 13.97 ?  135 ASP   A N    1 
ATOM   2941 N  N    B ASP   A 1 135 ? 13.455 -5.863  -7.920  0.26 12.97 ?  135 ASP   A N    1 
ATOM   2942 C  CA   A ASP   A 1 135 ? 12.483 -6.673  -7.593  0.74 14.90 ?  135 ASP   A CA   1 
ATOM   2943 C  CA   B ASP   A 1 135 ? 12.217 -6.262  -7.267  0.26 13.28 ?  135 ASP   A CA   1 
ATOM   2944 C  C    A ASP   A 1 135 ? 12.707 -7.114  -6.152  0.74 14.30 ?  135 ASP   A C    1 
ATOM   2945 C  C    B ASP   A 1 135 ? 12.529 -6.758  -5.861  0.26 12.84 ?  135 ASP   A C    1 
ATOM   2946 O  O    A ASP   A 1 135 ? 13.503 -8.030  -5.917  0.74 14.10 ?  135 ASP   A O    1 
ATOM   2947 O  O    B ASP   A 1 135 ? 13.246 -7.757  -5.711  0.26 12.64 ?  135 ASP   A O    1 
ATOM   2948 C  CB   A ASP   A 1 135 ? 11.998 -7.857  -8.426  0.74 17.08 ?  135 ASP   A CB   1 
ATOM   2949 C  CB   B ASP   A 1 135 ? 11.560 -7.378  -8.069  0.26 13.95 ?  135 ASP   A CB   1 
ATOM   2950 C  CG   A ASP   A 1 135 ? 10.705 -8.480  -7.901  0.74 19.40 ?  135 ASP   A CG   1 
ATOM   2951 C  CG   B ASP   A 1 135 ? 10.150 -7.691  -7.598  0.26 14.79 ?  135 ASP   A CG   1 
ATOM   2952 O  OD1  A ASP   A 1 135 ? 10.149 -8.002  -6.892  0.74 19.45 ?  135 ASP   A OD1  1 
ATOM   2953 O  OD1  B ASP   A 1 135 ? 9.828  -7.391  -6.427  0.26 14.90 ?  135 ASP   A OD1  1 
ATOM   2954 O  OD2  A ASP   A 1 135 ? 10.240 -9.463  -8.518  0.74 22.11 -1 135 ASP   A OD2  1 
ATOM   2955 O  OD2  B ASP   A 1 135 ? 9.372  -8.256  -8.396  0.26 15.52 -1 135 ASP   A OD2  1 
ATOM   2956 H  H    A ASP   A 1 135 ? 14.117 -6.755  -8.702  0.74 16.91 ?  135 ASP   A H    1 
ATOM   2957 H  H    B ASP   A 1 135 ? 13.688 -6.380  -8.560  0.26 15.70 ?  135 ASP   A H    1 
ATOM   2958 H  HA   A ASP   A 1 135 ? 11.827 -5.963  -7.636  0.74 18.02 ?  135 ASP   A HA   1 
ATOM   2959 H  HA   B ASP   A 1 135 ? 11.608 -5.507  -7.233  0.26 16.08 ?  135 ASP   A HA   1 
ATOM   2960 H  HB2  A ASP   A 1 135 ? 11.839 -7.557  -9.332  0.74 20.63 ?  135 ASP   A HB2  1 
ATOM   2961 H  HB2  B ASP   A 1 135 ? 11.543 -7.119  -9.004  0.26 16.88 ?  135 ASP   A HB2  1 
ATOM   2962 H  HB3  A ASP   A 1 135 ? 12.679 -8.544  -8.417  0.74 20.63 ?  135 ASP   A HB3  1 
ATOM   2963 H  HB3  B ASP   A 1 135 ? 12.072 -8.189  -7.955  0.26 16.88 ?  135 ASP   A HB3  1 
ATOM   2964 N  N    A PRO   A 1 136 ? 12.054 -6.496  -5.165  0.74 13.96 ?  136 PRO   A N    1 
ATOM   2965 N  N    B PRO   A 1 136 ? 12.026 -6.103  -4.814  0.26 12.62 ?  136 PRO   A N    1 
ATOM   2966 C  CA   A PRO   A 1 136 ? 12.295 -6.904  -3.768  0.74 13.81 ?  136 PRO   A CA   1 
ATOM   2967 C  CA   B PRO   A 1 136 ? 12.324 -6.560  -3.448  0.26 12.80 ?  136 PRO   A CA   1 
ATOM   2968 C  C    A PRO   A 1 136 ? 11.877 -8.331  -3.454  0.74 12.96 ?  136 PRO   A C    1 
ATOM   2969 C  C    B PRO   A 1 136 ? 11.850 -7.974  -3.158  0.26 12.53 ?  136 PRO   A C    1 
ATOM   2970 O  O    A PRO   A 1 136 ? 12.478 -8.965  -2.579  0.74 12.76 ?  136 PRO   A O    1 
ATOM   2971 O  O    B PRO   A 1 136 ? 12.430 -8.649  -2.297  0.26 12.14 ?  136 PRO   A O    1 
ATOM   2972 C  CB   A PRO   A 1 136 ? 11.500 -5.869  -2.959  0.74 14.70 ?  136 PRO   A CB   1 
ATOM   2973 C  CB   B PRO   A 1 136 ? 11.632 -5.506  -2.569  0.26 13.13 ?  136 PRO   A CB   1 
ATOM   2974 C  CG   A PRO   A 1 136 ? 10.465 -5.346  -3.913  0.74 15.47 ?  136 PRO   A CG   1 
ATOM   2975 C  CG   B PRO   A 1 136 ? 10.612 -4.864  -3.472  0.26 13.22 ?  136 PRO   A CG   1 
ATOM   2976 C  CD   A PRO   A 1 136 ? 11.101 -5.377  -5.266  0.74 14.80 ?  136 PRO   A CD   1 
ATOM   2977 C  CD   B PRO   A 1 136 ? 11.212 -4.879  -4.826  0.26 12.81 ?  136 PRO   A CD   1 
ATOM   2978 H  HA   A PRO   A 1 136 ? 13.239 -6.806  -3.557  0.74 16.71 ?  136 PRO   A HA   1 
ATOM   2979 H  HA   B PRO   A 1 136 ? 13.277 -6.516  -3.287  0.26 15.50 ?  136 PRO   A HA   1 
ATOM   2980 H  HB2  A PRO   A 1 136 ? 11.082 -6.302  -2.200  0.74 17.78 ?  136 PRO   A HB2  1 
ATOM   2981 H  HB2  B PRO   A 1 136 ? 11.204 -5.929  -1.813  0.26 15.90 ?  136 PRO   A HB2  1 
ATOM   2982 H  HB3  A PRO   A 1 136 ? 12.094 -5.160  -2.668  0.74 17.78 ?  136 PRO   A HB3  1 
ATOM   2983 H  HB3  B PRO   A 1 136 ? 12.284 -4.846  -2.271  0.26 15.90 ?  136 PRO   A HB3  1 
ATOM   2984 H  HG2  A PRO   A 1 136 ? 9.687  -5.917  -3.890  0.74 18.70 ?  136 PRO   A HG2  1 
ATOM   2985 H  HG2  B PRO   A 1 136 ? 9.791  -5.382  -3.459  0.26 16.01 ?  136 PRO   A HG2  1 
ATOM   2986 H  HG3  A PRO   A 1 136 ? 10.236 -4.437  -3.670  0.74 18.70 ?  136 PRO   A HG3  1 
ATOM   2987 H  HG3  B PRO   A 1 136 ? 10.444 -3.951  -3.190  0.26 16.01 ?  136 PRO   A HG3  1 
ATOM   2988 H  HD2  A PRO   A 1 136 ? 10.430 -5.565  -5.946  0.74 17.90 ?  136 PRO   A HD2  1 
ATOM   2989 H  HD2  B PRO   A 1 136 ? 10.514 -4.936  -5.500  0.26 15.52 ?  136 PRO   A HD2  1 
ATOM   2990 H  HD3  A PRO   A 1 136 ? 11.567 -4.548  -5.448  0.74 17.90 ?  136 PRO   A HD3  1 
ATOM   2991 H  HD3  B PRO   A 1 136 ? 11.776 -4.101  -4.963  0.26 15.52 ?  136 PRO   A HD3  1 
ATOM   2992 N  N    A ILE   A 1 137 ? 10.851 -8.854  -4.126  0.74 13.06 ?  137 ILE   A N    1 
ATOM   2993 N  N    B ILE   A 1 137 ? 10.810 -8.447  -3.849  0.26 12.77 ?  137 ILE   A N    1 
ATOM   2994 C  CA   A ILE   A 1 137 ? 10.481 -10.254 -3.924  0.74 13.33 ?  137 ILE   A CA   1 
ATOM   2995 C  CA   B ILE   A 1 137 ? 10.398 -9.840  -3.704  0.26 13.11 ?  137 ILE   A CA   1 
ATOM   2996 C  C    A ILE   A 1 137 ? 11.641 -11.163 -4.314  0.74 12.85 ?  137 ILE   A C    1 
ATOM   2997 C  C    B ILE   A 1 137 ? 11.528 -10.768 -4.136  0.26 12.93 ?  137 ILE   A C    1 
ATOM   2998 O  O    A ILE   A 1 137 ? 11.962 -12.132 -3.611  0.74 13.18 ?  137 ILE   A O    1 
ATOM   2999 O  O    B ILE   A 1 137 ? 11.797 -11.791 -3.495  0.26 13.19 ?  137 ILE   A O    1 
ATOM   3000 C  CB   A ILE   A 1 137 ? 9.193  -10.585 -4.702  0.74 14.54 ?  137 ILE   A CB   1 
ATOM   3001 C  CB   B ILE   A 1 137 ? 9.104  -10.093 -4.502  0.26 13.66 ?  137 ILE   A CB   1 
ATOM   3002 C  CG1  A ILE   A 1 137 ? 8.011  -9.744  -4.197  0.74 16.52 ?  137 ILE   A CG1  1 
ATOM   3003 C  CG1  B ILE   A 1 137 ? 7.983  -9.170  -4.005  0.26 14.45 ?  137 ILE   A CG1  1 
ATOM   3004 C  CG2  A ILE   A 1 137 ? 8.884  -12.075 -4.594  0.74 15.05 ?  137 ILE   A CG2  1 
ATOM   3005 C  CG2  B ILE   A 1 137 ? 8.698  -11.559 -4.415  0.26 13.69 ?  137 ILE   A CG2  1 
ATOM   3006 C  CD1  A ILE   A 1 137 ? 6.736  -9.933  -4.994  0.74 18.07 ?  137 ILE   A CD1  1 
ATOM   3007 C  CD1  B ILE   A 1 137 ? 6.720  -9.226  -4.838  0.26 14.77 ?  137 ILE   A CD1  1 
ATOM   3008 H  H    A ILE   A 1 137 ? 10.364 -8.433  -4.689  0.74 15.81 ?  137 ILE   A H    1 
ATOM   3009 H  H    B ILE   A 1 137 ? 10.335 -7.980  -4.397  0.26 15.47 ?  137 ILE   A H    1 
ATOM   3010 H  HA   A ILE   A 1 137 ? 10.306 -10.402 -2.985  0.74 16.14 ?  137 ILE   A HA   1 
ATOM   3011 H  HA   B ILE   A 1 137 ? 10.204 -10.010 -2.768  0.26 15.88 ?  137 ILE   A HA   1 
ATOM   3012 H  HB   A ILE   A 1 137 ? 9.337  -10.378 -5.636  0.74 17.58 ?  137 ILE   A HB   1 
ATOM   3013 H  HB   B ILE   A 1 137 ? 9.275  -9.879  -5.431  0.26 16.53 ?  137 ILE   A HB   1 
ATOM   3014 H  HG12 A ILE   A 1 137 ? 7.830  -9.981  -3.274  0.74 19.96 ?  137 ILE   A HG12 1 
ATOM   3015 H  HG12 B ILE   A 1 137 ? 7.748  -9.420  -3.099  0.26 17.48 ?  137 ILE   A HG12 1 
ATOM   3016 H  HG13 A ILE   A 1 137 ? 8.259  -8.804  -4.248  0.74 19.96 ?  137 ILE   A HG13 1 
ATOM   3017 H  HG13 B ILE   A 1 137 ? 8.296  -8.250  -4.019  0.26 17.48 ?  137 ILE   A HG13 1 
ATOM   3018 H  HG21 A ILE   A 1 137 ? 7.985  -12.249 -4.915  0.74 18.20 ?  137 ILE   A HG21 1 
ATOM   3019 H  HG21 B ILE   A 1 137 ? 7.814  -11.667 -4.798  0.26 16.57 ?  137 ILE   A HG21 1 
ATOM   3020 H  HG22 A ILE   A 1 137 ? 9.519  -12.569 -5.133  0.74 18.20 ?  137 ILE   A HG22 1 
ATOM   3021 H  HG22 B ILE   A 1 137 ? 9.338  -12.092 -4.910  0.26 16.57 ?  137 ILE   A HG22 1 
ATOM   3022 H  HG23 A ILE   A 1 137 ? 8.956  -12.342 -3.666  0.74 18.20 ?  137 ILE   A HG23 1 
ATOM   3023 H  HG23 B ILE   A 1 137 ? 8.690  -11.828 -3.484  0.26 16.57 ?  137 ILE   A HG23 1 
ATOM   3024 H  HD11 A ILE   A 1 137 ? 6.032  -10.226 -4.397  0.74 21.83 ?  137 ILE   A HD11 1 
ATOM   3025 H  HD11 B ILE   A 1 137 ? 6.253  -8.379  -4.762  0.26 17.86 ?  137 ILE   A HD11 1 
ATOM   3026 H  HD12 A ILE   A 1 137 ? 6.504  -9.087  -5.400  0.74 21.83 ?  137 ILE   A HD12 1 
ATOM   3027 H  HD12 B ILE   A 1 137 ? 6.960  -9.386  -5.764  0.26 17.86 ?  137 ILE   A HD12 1 
ATOM   3028 H  HD13 A ILE   A 1 137 ? 6.885  -10.595 -5.686  0.74 21.83 ?  137 ILE   A HD13 1 
ATOM   3029 H  HD13 B ILE   A 1 137 ? 6.159  -9.947  -4.513  0.26 17.86 ?  137 ILE   A HD13 1 
ATOM   3030 N  N    A HIS   A 1 138 ? 12.288 -10.863 -5.442  0.74 12.59 ?  138 HIS   A N    1 
ATOM   3031 N  N    B HIS   A 1 138 ? 12.210 -10.418 -5.228  0.26 12.74 ?  138 HIS   A N    1 
ATOM   3032 C  CA   A HIS   A 1 138 ? 13.460 -11.626 -5.855  0.74 12.93 ?  138 HIS   A CA   1 
ATOM   3033 C  CA   B HIS   A 1 138 ? 13.349 -11.208 -5.683  0.26 12.10 ?  138 HIS   A CA   1 
ATOM   3034 C  C    A HIS   A 1 138 ? 14.597 -11.482 -4.852  0.74 12.60 ?  138 HIS   A C    1 
ATOM   3035 C  C    B HIS   A 1 138 ? 14.521 -11.101 -4.712  0.26 11.39 ?  138 HIS   A C    1 
ATOM   3036 O  O    A HIS   A 1 138 ? 15.247 -12.472 -4.495  0.74 13.22 ?  138 HIS   A O    1 
ATOM   3037 O  O    B HIS   A 1 138 ? 15.226 -12.090 -4.470  0.26 11.47 ?  138 HIS   A O    1 
ATOM   3038 C  CB   A HIS   A 1 138 ? 13.899 -11.192 -7.251  0.74 13.76 ?  138 HIS   A CB   1 
ATOM   3039 C  CB   B HIS   A 1 138 ? 13.753 -10.760 -7.088  0.26 12.21 ?  138 HIS   A CB   1 
ATOM   3040 C  CG   A HIS   A 1 138 ? 15.170 -11.840 -7.699  0.74 14.58 ?  138 HIS   A CG   1 
ATOM   3041 C  CG   B HIS   A 1 138 ? 15.015 -11.392 -7.588  0.26 12.78 ?  138 HIS   A CG   1 
ATOM   3042 N  ND1  A HIS   A 1 138 ? 15.277 -13.198 -7.910  0.74 15.83 ?  138 HIS   A ND1  1 
ATOM   3043 N  ND1  B HIS   A 1 138 ? 15.093 -12.719 -7.951  0.26 13.46 ?  138 HIS   A ND1  1 
ATOM   3044 C  CD2  A HIS   A 1 138 ? 16.395 -11.322 -7.948  0.74 14.95 ?  138 HIS   A CD2  1 
ATOM   3045 C  CD2  B HIS   A 1 138 ? 16.250 -10.875 -7.786  0.26 12.84 ?  138 HIS   A CD2  1 
ATOM   3046 C  CE1  A HIS   A 1 138 ? 16.509 -13.485 -8.288  0.74 16.31 ?  138 HIS   A CE1  1 
ATOM   3047 C  CE1  B HIS   A 1 138 ? 16.323 -12.992 -8.351  0.26 13.61 ?  138 HIS   A CE1  1 
ATOM   3048 N  NE2  A HIS   A 1 138 ? 17.209 -12.365 -8.318  0.74 15.56 ?  138 HIS   A NE2  1 
ATOM   3049 N  NE2  B HIS   A 1 138 ? 17.045 -11.890 -8.261  0.26 13.27 ?  138 HIS   A NE2  1 
ATOM   3050 H  H    A HIS   A 1 138 ? 12.073 -10.221 -5.980  0.74 15.25 ?  138 HIS   A H    1 
ATOM   3051 H  H    B HIS   A 1 138 ? 12.023 -9.734  -5.720  0.26 15.43 ?  138 HIS   A H    1 
ATOM   3052 H  HA   A HIS   A 1 138 ? 13.220 -12.561 -5.903  0.74 15.65 ?  138 HIS   A HA   1 
ATOM   3053 H  HA   B HIS   A 1 138 ? 13.081 -12.135 -5.728  0.26 14.66 ?  138 HIS   A HA   1 
ATOM   3054 H  HB2  A HIS   A 1 138 ? 13.201 -11.429 -7.888  0.74 16.65 ?  138 HIS   A HB2  1 
ATOM   3055 H  HB2  B HIS   A 1 138 ? 13.038 -10.992 -7.704  0.26 14.80 ?  138 HIS   A HB2  1 
ATOM   3056 H  HB3  A HIS   A 1 138 ? 14.034 -10.232 -7.258  0.74 16.65 ?  138 HIS   A HB3  1 
ATOM   3057 H  HB3  B HIS   A 1 138 ? 13.880 -9.798  -7.085  0.26 14.80 ?  138 HIS   A HB3  1 
ATOM   3058 H  HD1  A HIS   A 1 138 ? 14.634 -13.767 -7.822  0.74 19.14 ?  138 HIS   A HD1  1 
ATOM   3059 H  HD1  B HIS   A 1 138 ? 14.441 -13.281 -7.921  0.26 16.30 ?  138 HIS   A HD1  1 
ATOM   3060 H  HD2  A HIS   A 1 138 ? 16.633 -10.426 -7.886  0.74 18.08 ?  138 HIS   A HD2  1 
ATOM   3061 H  HD2  B HIS   A 1 138 ? 16.509 -9.995  -7.629  0.26 15.55 ?  138 HIS   A HD2  1 
ATOM   3062 H  HE1  A HIS   A 1 138 ? 16.828 -14.331 -8.492  0.74 19.71 ?  138 HIS   A HE1  1 
ATOM   3063 H  HE1  B HIS   A 1 138 ? 16.625 -13.820 -8.645  0.26 16.47 ?  138 HIS   A HE1  1 
ATOM   3064 N  N    A SER   A 1 139 ? 14.852 -10.260 -4.384  0.74 12.04 ?  139 SER   A N    1 
ATOM   3065 N  N    B SER   A 1 139 ? 14.742 -9.911  -4.144  0.26 10.98 ?  139 SER   A N    1 
ATOM   3066 C  CA   A SER   A 1 139 ? 15.924 -10.064 -3.417  0.74 11.68 ?  139 SER   A CA   1 
ATOM   3067 C  CA   B SER   A 1 139 ? 15.812 -9.739  -3.166  0.26 11.07 ?  139 SER   A CA   1 
ATOM   3068 C  C    A SER   A 1 139 ? 15.698 -10.881 -2.151  0.74 11.72 ?  139 SER   A C    1 
ATOM   3069 C  C    B SER   A 1 139 ? 15.611 -10.645 -1.957  0.26 11.16 ?  139 SER   A C    1 
ATOM   3070 O  O    A SER   A 1 139 ? 16.636 -11.496 -1.629  0.74 11.25 ?  139 SER   A O    1 
ATOM   3071 O  O    B SER   A 1 139 ? 16.587 -11.153 -1.390  0.26 11.30 ?  139 SER   A O    1 
ATOM   3072 C  CB   A SER   A 1 139 ? 16.068 -8.581  -3.085  0.74 11.26 ?  139 SER   A CB   1 
ATOM   3073 C  CB   B SER   A 1 139 ? 15.895 -8.267  -2.745  0.26 11.10 ?  139 SER   A CB   1 
ATOM   3074 O  OG   A SER   A 1 139 ? 17.143 -8.406  -2.180  0.74 11.15 ?  139 SER   A OG   1 
ATOM   3075 O  OG   B SER   A 1 139 ? 16.934 -8.050  -1.803  0.26 11.46 ?  139 SER   A OG   1 
ATOM   3076 H  H    A SER   A 1 139 ? 14.435 -9.547  -4.605  0.74 14.59 ?  139 SER   A H    1 
ATOM   3077 H  H    B SER   A 1 139 ? 14.292 -9.194  -4.304  0.26 13.31 ?  139 SER   A H    1 
ATOM   3078 H  HA   A SER   A 1 139 ? 16.765 -10.358 -3.809  0.74 14.16 ?  139 SER   A HA   1 
ATOM   3079 H  HA   B SER   A 1 139 ? 16.657 -9.975  -3.574  0.26 13.42 ?  139 SER   A HA   1 
ATOM   3080 H  HB2  A SER   A 1 139 ? 16.257 -8.084  -3.896  0.74 13.65 ?  139 SER   A HB2  1 
ATOM   3081 H  HB2  B SER   A 1 139 ? 16.063 -7.721  -3.534  0.26 13.46 ?  139 SER   A HB2  1 
ATOM   3082 H  HB3  A SER   A 1 139 ? 15.253 -8.262  -2.673  0.74 13.65 ?  139 SER   A HB3  1 
ATOM   3083 H  HB3  B SER   A 1 139 ? 15.058 -8.002  -2.338  0.26 13.46 ?  139 SER   A HB3  1 
ATOM   3084 H  HG   A SER   A 1 139 ? 17.235 -7.591  -1.984  0.74 13.52 ?  139 SER   A HG   1 
ATOM   3085 H  HG   B SER   A 1 139 ? 16.975 -7.228  -1.599  0.26 13.89 ?  139 SER   A HG   1 
ATOM   3086 N  N    A LEU   A 1 140 ? 14.468 -10.888 -1.631  0.74 12.07 ?  140 LEU   A N    1 
ATOM   3087 N  N    B LEU   A 1 140 ? 14.359 -10.873 -1.558  0.26 11.29 ?  140 LEU   A N    1 
ATOM   3088 C  CA   A LEU   A 1 140 ? 14.185 -11.692 -0.445  0.74 12.30 ?  140 LEU   A CA   1 
ATOM   3089 C  CA   B LEU   A 1 140 ? 14.104 -11.716 -0.395  0.26 11.41 ?  140 LEU   A CA   1 
ATOM   3090 C  C    A LEU   A 1 140 ? 14.440 -13.170 -0.715  0.74 12.40 ?  140 LEU   A C    1 
ATOM   3091 C  C    B LEU   A 1 140 ? 14.402 -13.182 -0.696  0.26 11.94 ?  140 LEU   A C    1 
ATOM   3092 O  O    A LEU   A 1 140 ? 14.989 -13.882 0.136   0.74 13.07 ?  140 LEU   A O    1 
ATOM   3093 O  O    B LEU   A 1 140 ? 14.958 -13.895 0.148   0.26 12.05 ?  140 LEU   A O    1 
ATOM   3094 C  CB   A LEU   A 1 140 ? 12.743 -11.467 0.008   0.74 12.91 ?  140 LEU   A CB   1 
ATOM   3095 C  CB   B LEU   A 1 140 ? 12.659 -11.531 0.067   0.26 11.44 ?  140 LEU   A CB   1 
ATOM   3096 C  CG   A LEU   A 1 140 ? 12.266 -12.358 1.155   0.74 13.50 ?  140 LEU   A CG   1 
ATOM   3097 C  CG   B LEU   A 1 140 ? 12.230 -12.308 1.311   0.26 11.51 ?  140 LEU   A CG   1 
ATOM   3098 C  CD1  A LEU   A 1 140 ? 13.164 -12.228 2.380   0.74 13.93 ?  140 LEU   A CD1  1 
ATOM   3099 C  CD1  B LEU   A 1 140 ? 13.126 -11.983 2.490   0.26 11.33 ?  140 LEU   A CD1  1 
ATOM   3100 C  CD2  A LEU   A 1 140 ? 10.803 -12.047 1.503   0.74 14.20 ?  140 LEU   A CD2  1 
ATOM   3101 C  CD2  B LEU   A 1 140 ? 10.775 -12.009 1.645   0.26 11.94 ?  140 LEU   A CD2  1 
ATOM   3102 H  H    A LEU   A 1 140 ? 13.799 -10.443 -1.933  0.74 14.62 ?  140 LEU   A H    1 
ATOM   3103 H  H    B LEU   A 1 140 ? 13.654 -10.554 -1.937  0.26 13.69 ?  140 LEU   A H    1 
ATOM   3104 H  HA   A LEU   A 1 140 ? 14.770 -11.417 0.276   0.74 14.90 ?  140 LEU   A HA   1 
ATOM   3105 H  HA   B LEU   A 1 140 ? 14.687 -11.433 0.326   0.26 13.84 ?  140 LEU   A HA   1 
ATOM   3106 H  HB2  A LEU   A 1 140 ? 12.650 -10.551 0.301   0.74 15.63 ?  140 LEU   A HB2  1 
ATOM   3107 H  HB2  B LEU   A 1 140 ? 12.519 -10.591 0.256   0.26 13.86 ?  140 LEU   A HB2  1 
ATOM   3108 H  HB3  A LEU   A 1 140 ? 12.154 -11.631 -0.745  0.74 15.63 ?  140 LEU   A HB3  1 
ATOM   3109 H  HB3  B LEU   A 1 140 ? 12.075 -11.804 -0.656  0.26 13.86 ?  140 LEU   A HB3  1 
ATOM   3110 H  HG   A LEU   A 1 140 ? 12.292 -13.286 0.868   0.74 16.34 ?  140 LEU   A HG   1 
ATOM   3111 H  HG   B LEU   A 1 140 ? 12.303 -13.258 1.130   0.26 13.95 ?  140 LEU   A HG   1 
ATOM   3112 H  HD11 A LEU   A 1 140 ? 12.775 -12.731 3.114   0.74 16.86 ?  140 LEU   A HD11 1 
ATOM   3113 H  HD11 B LEU   A 1 140 ? 12.752 -12.387 3.287   0.26 13.74 ?  140 LEU   A HD11 1 
ATOM   3114 H  HD12 A LEU   A 1 140 ? 14.041 -12.588 2.165   0.74 16.86 ?  140 LEU   A HD12 1 
ATOM   3115 H  HD12 B LEU   A 1 140 ? 14.010 -12.343 2.319   0.26 13.74 ?  140 LEU   A HD12 1 
ATOM   3116 H  HD13 A LEU   A 1 140 ? 13.238 -11.294 2.620   0.74 16.86 ?  140 LEU   A HD13 1 
ATOM   3117 H  HD13 B LEU   A 1 140 ? 13.171 -11.021 2.593   0.26 13.74 ?  140 LEU   A HD13 1 
ATOM   3118 H  HD21 A LEU   A 1 140 ? 10.520 -12.626 2.233   0.74 17.18 ?  140 LEU   A HD21 1 
ATOM   3119 H  HD21 B LEU   A 1 140 ? 10.479 -12.625 2.334   0.26 14.47 ?  140 LEU   A HD21 1 
ATOM   3120 H  HD22 A LEU   A 1 140 ? 10.731 -11.120 1.773   0.74 17.18 ?  140 LEU   A HD22 1 
ATOM   3121 H  HD22 B LEU   A 1 140 ? 10.706 -11.097 1.965   0.26 14.47 ?  140 LEU   A HD22 1 
ATOM   3122 H  HD23 A LEU   A 1 140 ? 10.248 -12.211 0.724   0.74 17.18 ?  140 LEU   A HD23 1 
ATOM   3123 H  HD23 B LEU   A 1 140 ? 10.237 -12.124 0.846   0.26 14.47 ?  140 LEU   A HD23 1 
ATOM   3124 N  N    . ARG   A 1 141 ? 14.041 -13.648 -1.895  1.00 12.63 ?  141 ARG   A N    1 
ATOM   3125 C  CA   . ARG   A 1 141 ? 14.283 -15.040 -2.256  1.00 13.64 ?  141 ARG   A CA   1 
ATOM   3126 C  C    . ARG   A 1 141 ? 15.779 -15.344 -2.279  1.00 12.95 ?  141 ARG   A C    1 
ATOM   3127 O  O    . ARG   A 1 141 ? 16.229 -16.362 -1.737  1.00 13.29 ?  141 ARG   A O    1 
ATOM   3128 C  CB   . ARG   A 1 141 ? 13.645 -15.314 -3.621  1.00 15.14 ?  141 ARG   A CB   1 
ATOM   3129 C  CG   . ARG   A 1 141 ? 13.637 -16.763 -4.060  1.00 18.20 ?  141 ARG   A CG   1 
ATOM   3130 C  CD   . ARG   A 1 141 ? 12.607 -17.534 -3.297  1.00 20.86 ?  141 ARG   A CD   1 
ATOM   3131 N  NE   . ARG   A 1 141 ? 13.222 -18.334 -2.252  1.00 22.01 ?  141 ARG   A NE   1 
ATOM   3132 C  CZ   . ARG   A 1 141 ? 12.550 -18.906 -1.261  1.00 23.19 ?  141 ARG   A CZ   1 
ATOM   3133 N  NH1  . ARG   A 1 141 ? 11.262 -18.666 -1.069  1.00 22.55 ?  141 ARG   A NH1  1 
ATOM   3134 N  NH2  . ARG   A 1 141 ? 13.188 -19.728 -0.433  1.00 24.42 ?  141 ARG   A NH2  1 
ATOM   3135 H  H    A ARG   A 1 141 ? 13.632 -13.188 -2.497  0.74 15.30 ?  141 ARG   A H    1 
ATOM   3136 H  H    B ARG   A 1 141 ? 13.652 -13.182 -2.505  0.26 15.30 ?  141 ARG   A H    1 
ATOM   3137 H  HA   . ARG   A 1 141 ? 13.867 -15.620 -1.604  1.00 16.51 ?  141 ARG   A HA   1 
ATOM   3138 H  HB2  . ARG   A 1 141 ? 12.725 -15.006 -3.600  1.00 18.31 ?  141 ARG   A HB2  1 
ATOM   3139 H  HB3  . ARG   A 1 141 ? 14.133 -14.813 -4.293  1.00 18.31 ?  141 ARG   A HB3  1 
ATOM   3140 H  HG2  . ARG   A 1 141 ? 13.421 -16.816 -5.007  1.00 21.98 ?  141 ARG   A HG2  1 
ATOM   3141 H  HG3  . ARG   A 1 141 ? 14.507 -17.162 -3.893  1.00 21.98 ?  141 ARG   A HG3  1 
ATOM   3142 H  HD2  . ARG   A 1 141 ? 11.988 -16.920 -2.869  1.00 25.17 ?  141 ARG   A HD2  1 
ATOM   3143 H  HD3  . ARG   A 1 141 ? 12.122 -18.121 -3.905  1.00 25.17 ?  141 ARG   A HD3  1 
ATOM   3144 H  HE   . ARG   A 1 141 ? 14.044 -18.557 -2.351  1.00 26.55 ?  141 ARG   A HE   1 
ATOM   3145 H  HH11 . ARG   A 1 141 ? 10.831 -18.150 -1.606  1.00 27.20 ?  141 ARG   A HH11 1 
ATOM   3146 H  HH12 . ARG   A 1 141 ? 10.844 -19.045 -0.417  1.00 27.20 ?  141 ARG   A HH12 1 
ATOM   3147 H  HH21 . ARG   A 1 141 ? 14.021 -19.894 -0.549  1.00 29.44 ?  141 ARG   A HH21 1 
ATOM   3148 H  HH22 . ARG   A 1 141 ? 12.763 -20.096 0.221   1.00 29.44 ?  141 ARG   A HH22 1 
ATOM   3149 N  N    . VAL   A 1 142 ? 16.569 -14.475 -2.912  1.00 12.27 ?  142 VAL   A N    1 
ATOM   3150 C  CA   . VAL   A 1 142 ? 18.015 -14.687 -2.943  1.00 12.13 ?  142 VAL   A CA   1 
ATOM   3151 C  C    . VAL   A 1 142 ? 18.587 -14.666 -1.534  1.00 11.63 ?  142 VAL   A C    1 
ATOM   3152 O  O    . VAL   A 1 142 ? 19.448 -15.483 -1.189  1.00 12.22 ?  142 VAL   A O    1 
ATOM   3153 C  CB   . VAL   A 1 142 ? 18.710 -13.672 -3.866  1.00 12.61 ?  142 VAL   A CB   1 
ATOM   3154 C  CG1  . VAL   A 1 142 ? 20.218 -13.879 -3.827  1.00 12.55 ?  142 VAL   A CG1  1 
ATOM   3155 C  CG2  . VAL   A 1 142 ? 18.211 -13.814 -5.291  1.00 13.64 ?  142 VAL   A CG2  1 
ATOM   3156 H  H    . VAL   A 1 142 ? 16.302 -13.758 -3.318  1.00 14.86 ?  142 VAL   A H    1 
ATOM   3157 H  HA   . VAL   A 1 142 ? 18.186 -15.561 -3.312  1.00 14.69 ?  142 VAL   A HA   1 
ATOM   3158 H  HB   . VAL   A 1 142 ? 18.524 -12.764 -3.564  1.00 15.27 ?  142 VAL   A HB   1 
ATOM   3159 H  HG11 . VAL   A 1 142 ? 20.626 -13.397 -4.565  1.00 15.20 ?  142 VAL   A HG11 1 
ATOM   3160 H  HG12 . VAL   A 1 142 ? 20.568 -13.542 -2.985  1.00 15.20 ?  142 VAL   A HG12 1 
ATOM   3161 H  HG13 . VAL   A 1 142 ? 20.408 -14.826 -3.909  1.00 15.20 ?  142 VAL   A HG13 1 
ATOM   3162 H  HG21 . VAL   A 1 142 ? 18.677 -13.174 -5.853  1.00 16.50 ?  142 VAL   A HG21 1 
ATOM   3163 H  HG22 . VAL   A 1 142 ? 18.400 -14.716 -5.593  1.00 16.50 ?  142 VAL   A HG22 1 
ATOM   3164 H  HG23 . VAL   A 1 142 ? 17.262 -13.645 -5.307  1.00 16.50 ?  142 VAL   A HG23 1 
ATOM   3165 N  N    . CYS   A 1 143 ? 18.115 -13.744 -0.694  1.00 11.79 ?  143 CYS   A N    1 
ATOM   3166 C  CA   . CYS   A 1 143 ? 18.576 -13.695 0.688   1.00 12.12 ?  143 CYS   A CA   1 
ATOM   3167 C  C    . CYS   A 1 143 ? 18.348 -15.034 1.380   1.00 12.02 ?  143 CYS   A C    1 
ATOM   3168 O  O    . CYS   A 1 143 ? 19.268 -15.623 1.953   1.00 12.09 ?  143 CYS   A O    1 
ATOM   3169 C  CB   . CYS   A 1 143 ? 17.844 -12.580 1.432   1.00 12.47 ?  143 CYS   A CB   1 
ATOM   3170 S  SG   . CYS   A 1 143 ? 18.344 -12.403 3.157   1.00 12.71 ?  143 CYS   A SG   1 
ATOM   3171 H  H    . CYS   A 1 143 ? 17.530 -13.151 -0.897  1.00 14.29 ?  143 CYS   A H    1 
ATOM   3172 H  HA   . CYS   A 1 143 ? 19.525 -13.508 0.705   1.00 14.68 ?  143 CYS   A HA   1 
ATOM   3173 H  HB2  . CYS   A 1 143 ? 18.015 -11.739 0.980   1.00 15.10 ?  143 CYS   A HB2  1 
ATOM   3174 H  HB3  . CYS   A 1 143 ? 16.895 -12.769 1.419   1.00 15.10 ?  143 CYS   A HB3  1 
ATOM   3175 H  HG   . CYS   A 1 143 ? 17.767 -11.468 3.634   1.00 15.39 ?  143 CYS   A HG   1 
ATOM   3176 N  N    . VAL   A 1 144 ? 17.117 -15.536 1.325   1.00 12.63 ?  144 VAL   A N    1 
ATOM   3177 C  CA   . VAL   A 1 144 ? 16.781 -16.774 2.022   1.00 13.80 ?  144 VAL   A CA   1 
ATOM   3178 C  C    . VAL   A 1 144 ? 17.601 -17.942 1.495   1.00 13.61 ?  144 VAL   A C    1 
ATOM   3179 O  O    . VAL   A 1 144 ? 17.961 -18.855 2.250   1.00 14.42 ?  144 VAL   A O    1 
ATOM   3180 C  CB   . VAL   A 1 144 ? 15.266 -17.027 1.899   1.00 16.58 ?  144 VAL   A CB   1 
ATOM   3181 C  CG1  . VAL   A 1 144 ? 14.910 -18.461 2.236   1.00 18.35 ?  144 VAL   A CG1  1 
ATOM   3182 C  CG2  . VAL   A 1 144 ? 14.510 -16.028 2.774   1.00 16.63 ?  144 VAL   A CG2  1 
ATOM   3183 H  H    . VAL   A 1 144 ? 16.456 -15.178 0.898   1.00 15.30 ?  144 VAL   A H    1 
ATOM   3184 H  HA   . VAL   A 1 144 ? 16.978 -16.670 2.961   1.00 16.70 ?  144 VAL   A HA   1 
ATOM   3185 H  HB   . VAL   A 1 144 ? 14.993 -16.865 0.978   1.00 20.04 ?  144 VAL   A HB   1 
ATOM   3186 H  HG11 . VAL   A 1 144 ? 13.954 -18.517 2.422   1.00 22.16 ?  144 VAL   A HG11 1 
ATOM   3187 H  HG12 . VAL   A 1 144 ? 15.126 -19.031 1.482   1.00 22.16 ?  144 VAL   A HG12 1 
ATOM   3188 H  HG13 . VAL   A 1 144 ? 15.409 -18.736 3.018   1.00 22.16 ?  144 VAL   A HG13 1 
ATOM   3189 H  HG21 . VAL   A 1 144 ? 13.552 -16.190 2.697   1.00 20.09 ?  144 VAL   A HG21 1 
ATOM   3190 H  HG22 . VAL   A 1 144 ? 14.785 -16.138 3.697   1.00 20.09 ?  144 VAL   A HG22 1 
ATOM   3191 H  HG23 . VAL   A 1 144 ? 14.709 -15.123 2.478   1.00 20.09 ?  144 VAL   A HG23 1 
ATOM   3192 N  N    . ASP   A 1 145 ? 17.867 -17.963 0.191   1.00 13.72 ?  145 ASP   A N    1 
ATOM   3193 C  CA   . ASP   A 1 145 ? 18.578 -19.068 -0.441  1.00 14.25 ?  145 ASP   A CA   1 
ATOM   3194 C  C    . ASP   A 1 145 ? 20.099 -18.920 -0.400  1.00 14.03 ?  145 ASP   A C    1 
ATOM   3195 O  O    . ASP   A 1 145 ? 20.804 -19.815 -0.883  1.00 15.85 ?  145 ASP   A O    1 
ATOM   3196 C  CB   . ASP   A 1 145 ? 18.129 -19.209 -1.898  1.00 15.81 ?  145 ASP   A CB   1 
ATOM   3197 C  CG   . ASP   A 1 145 ? 16.684 -19.656 -2.030  1.00 17.81 ?  145 ASP   A CG   1 
ATOM   3198 O  OD1  . ASP   A 1 145 ? 16.121 -20.209 -1.060  1.00 18.29 ?  145 ASP   A OD1  1 
ATOM   3199 O  OD2  . ASP   A 1 145 ? 16.113 -19.448 -3.116  1.00 19.39 -1 145 ASP   A OD2  1 
ATOM   3200 H  H    . ASP   A 1 145 ? 17.628 -17.344 -0.361  1.00 16.61 ?  145 ASP   A H    1 
ATOM   3201 H  HA   . ASP   A 1 145 ? 18.343 -19.890 0.018   1.00 17.24 ?  145 ASP   A HA   1 
ATOM   3202 H  HB2  . ASP   A 1 145 ? 18.226 -18.350 -2.340  1.00 19.11 ?  145 ASP   A HB2  1 
ATOM   3203 H  HB3  . ASP   A 1 145 ? 18.683 -19.872 -2.334  1.00 19.11 ?  145 ASP   A HB3  1 
ATOM   3204 N  N    . THR   A 1 146 ? 20.623 -17.830 0.150   1.00 12.40 ?  146 THR   A N    1 
ATOM   3205 C  CA   . THR   A 1 146 ? 22.063 -17.578 0.168   1.00 12.04 ?  146 THR   A CA   1 
ATOM   3206 C  C    . THR   A 1 146 ? 22.621 -17.390 1.566   1.00 12.14 ?  146 THR   A C    1 
ATOM   3207 O  O    . THR   A 1 146 ? 23.701 -17.916 1.874   1.00 13.06 ?  146 THR   A O    1 
ATOM   3208 C  CB   . THR   A 1 146 ? 22.385 -16.327 -0.672  1.00 12.21 ?  146 THR   A CB   1 
ATOM   3209 O  OG1  . THR   A 1 146 ? 21.856 -16.493 -1.987  1.00 12.72 ?  146 THR   A OG1  1 
ATOM   3210 C  CG2  . THR   A 1 146 ? 23.885 -16.097 -0.772  1.00 12.70 ?  146 THR   A CG2  1 
ATOM   3211 H  H    . THR   A 1 146 ? 20.158 -17.206 0.518   1.00 15.03 ?  146 THR   A H    1 
ATOM   3212 H  HA   . THR   A 1 146 ? 22.523 -18.325 -0.233  1.00 14.59 ?  146 THR   A HA   1 
ATOM   3213 H  HB   . THR   A 1 146 ? 21.984 -15.543 -0.259  1.00 14.79 ?  146 THR   A HB   1 
ATOM   3214 H  HG1  . THR   A 1 146 ? 21.019 -16.568 -1.954  1.00 15.41 ?  146 THR   A HG1  1 
ATOM   3215 H  HG21 . THR   A 1 146 ? 24.071 -15.424 -1.445  1.00 15.38 ?  146 THR   A HG21 1 
ATOM   3216 H  HG22 . THR   A 1 146 ? 24.232 -15.792 0.080   1.00 15.38 ?  146 THR   A HG22 1 
ATOM   3217 H  HG23 . THR   A 1 146 ? 24.327 -16.922 -1.021  1.00 15.38 ?  146 THR   A HG23 1 
ATOM   3218 N  N    . VAL   A 1 147 ? 21.939 -16.614 2.402   1.00 12.20 ?  147 VAL   A N    1 
ATOM   3219 C  CA   . VAL   A 1 147 ? 22.428 -16.313 3.739   1.00 12.21 ?  147 VAL   A CA   1 
ATOM   3220 C  C    . VAL   A 1 147 ? 22.114 -17.485 4.657   1.00 12.57 ?  147 VAL   A C    1 
ATOM   3221 O  O    . VAL   A 1 147 ? 20.972 -17.961 4.710   1.00 13.26 ?  147 VAL   A O    1 
ATOM   3222 C  CB   . VAL   A 1 147 ? 21.803 -15.008 4.257   1.00 12.21 ?  147 VAL   A CB   1 
ATOM   3223 C  CG1  . VAL   A 1 147 ? 22.326 -14.693 5.640   1.00 13.09 ?  147 VAL   A CG1  1 
ATOM   3224 C  CG2  . VAL   A 1 147 ? 22.080 -13.864 3.288   1.00 12.45 ?  147 VAL   A CG2  1 
ATOM   3225 H  H    . VAL   A 1 147 ? 21.177 -16.251 2.221   1.00 14.77 ?  147 VAL   A H    1 
ATOM   3226 H  HA   . VAL   A 1 147 ? 23.388 -16.199 3.708   1.00 14.79 ?  147 VAL   A HA   1 
ATOM   3227 H  HB   . VAL   A 1 147 ? 20.844 -15.121 4.319   1.00 14.79 ?  147 VAL   A HB   1 
ATOM   3228 H  HG11 . VAL   A 1 147 ? 22.075 -13.790 5.875   1.00 15.85 ?  147 VAL   A HG11 1 
ATOM   3229 H  HG12 . VAL   A 1 147 ? 21.928 -15.319 6.276   1.00 15.85 ?  147 VAL   A HG12 1 
ATOM   3230 H  HG13 . VAL   A 1 147 ? 23.288 -14.789 5.646   1.00 15.85 ?  147 VAL   A HG13 1 
ATOM   3231 H  HG21 . VAL   A 1 147 ? 21.755 -13.039 3.681   1.00 15.08 ?  147 VAL   A HG21 1 
ATOM   3232 H  HG22 . VAL   A 1 147 ? 23.034 -13.809 3.135   1.00 15.08 ?  147 VAL   A HG22 1 
ATOM   3233 H  HG23 . VAL   A 1 147 ? 21.616 -14.042 2.456   1.00 15.08 ?  147 VAL   A HG23 1 
ATOM   3234 N  N    . ARG   A 1 148 ? 23.137 -17.949 5.378   1.00 12.75 ?  148 ARG   A N    1 
ATOM   3235 C  CA   . ARG   A 1 148 ? 23.007 -19.026 6.346   1.00 13.12 ?  148 ARG   A CA   1 
ATOM   3236 C  C    . ARG   A 1 148 ? 23.128 -18.554 7.783   1.00 13.27 ?  148 ARG   A C    1 
ATOM   3237 O  O    . ARG   A 1 148 ? 22.721 -19.282 8.696   1.00 14.82 ?  148 ARG   A O    1 
ATOM   3238 C  CB   . ARG   A 1 148 ? 24.050 -20.122 6.073   1.00 13.62 ?  148 ARG   A CB   1 
ATOM   3239 C  CG   . ARG   A 1 148 ? 23.896 -20.760 4.705   1.00 14.96 ?  148 ARG   A CG   1 
ATOM   3240 C  CD   . ARG   A 1 148 ? 24.985 -21.794 4.423   1.00 15.82 ?  148 ARG   A CD   1 
ATOM   3241 N  NE   . ARG   A 1 148 ? 26.321 -21.211 4.456   1.00 15.54 ?  148 ARG   A NE   1 
ATOM   3242 C  CZ   . ARG   A 1 148 ? 26.837 -20.476 3.480   1.00 14.93 ?  148 ARG   A CZ   1 
ATOM   3243 N  NH1  . ARG   A 1 148 ? 26.169 -20.247 2.362   1.00 15.31 ?  148 ARG   A NH1  1 
ATOM   3244 N  NH2  . ARG   A 1 148 ? 28.052 -19.950 3.632   1.00 15.34 ?  148 ARG   A NH2  1 
ATOM   3245 H  H    . ARG   A 1 148 ? 23.943 -17.645 5.305   1.00 15.44 ?  148 ARG   A H    1 
ATOM   3246 H  HA   . ARG   A 1 148 ? 22.135 -19.423 6.246   1.00 15.89 ?  148 ARG   A HA   1 
ATOM   3247 H  HB2  . ARG   A 1 148 ? 24.937 -19.745 6.126   1.00 16.48 ?  148 ARG   A HB2  1 
ATOM   3248 H  HB3  . ARG   A 1 148 ? 23.945 -20.827 6.734   1.00 16.48 ?  148 ARG   A HB3  1 
ATOM   3249 H  HG2  . ARG   A 1 148 ? 23.033 -21.199 4.656   1.00 18.09 ?  148 ARG   A HG2  1 
ATOM   3250 H  HG3  . ARG   A 1 148 ? 23.953 -20.062 4.030   1.00 18.09 ?  148 ARG   A HG3  1 
ATOM   3251 H  HD2  . ARG   A 1 148 ? 24.941 -22.486 5.097   1.00 19.12 ?  148 ARG   A HD2  1 
ATOM   3252 H  HD3  . ARG   A 1 148 ? 24.839 -22.171 3.542   1.00 19.12 ?  148 ARG   A HD3  1 
ATOM   3253 H  HE   . ARG   A 1 148 ? 26.817 -21.382 5.134   1.00 18.79 ?  148 ARG   A HE   1 
ATOM   3254 H  HH11 . ARG   A 1 148 ? 25.381 -20.569 2.254   1.00 18.52 ?  148 ARG   A HH11 1 
ATOM   3255 H  HH12 . ARG   A 1 148 ? 26.522 -19.759 1.745   1.00 18.52 ?  148 ARG   A HH12 1 
ATOM   3256 H  HH21 . ARG   A 1 148 ? 28.491 -20.087 4.357   1.00 18.55 ?  148 ARG   A HH21 1 
ATOM   3257 H  HH22 . ARG   A 1 148 ? 28.393 -19.466 3.007   1.00 18.55 ?  148 ARG   A HH22 1 
ATOM   3258 N  N    . THR   A 1 149 ? 23.678 -17.360 7.997   1.00 13.29 ?  149 THR   A N    1 
ATOM   3259 C  CA   . THR   A 1 149 ? 23.751 -16.758 9.314   1.00 13.50 ?  149 THR   A CA   1 
ATOM   3260 C  C    . THR   A 1 149 ? 22.424 -16.064 9.618   1.00 13.10 ?  149 THR   A C    1 
ATOM   3261 O  O    . THR   A 1 149 ? 21.491 -16.065 8.806   1.00 13.74 ?  149 THR   A O    1 
ATOM   3262 C  CB   . THR   A 1 149 ? 24.953 -15.822 9.371   1.00 13.63 ?  149 THR   A CB   1 
ATOM   3263 O  OG1  . THR   A 1 149 ? 24.825 -14.893 8.296   1.00 13.66 ?  149 THR   A OG1  1 
ATOM   3264 C  CG2  . THR   A 1 149 ? 26.266 -16.619 9.239   1.00 14.42 ?  149 THR   A CG2  1 
ATOM   3265 H  H    . THR   A 1 149 ? 24.029 -16.869 7.377   1.00 16.08 ?  149 THR   A H    1 
ATOM   3266 H  HA   . THR   A 1 149 ? 23.878 -17.459 9.972   1.00 16.34 ?  149 THR   A HA   1 
ATOM   3267 H  HB   . THR   A 1 149 ? 24.949 -15.347 10.216  1.00 16.50 ?  149 THR   A HB   1 
ATOM   3268 H  HG1  . THR   A 1 149 ? 25.474 -14.361 8.294   1.00 16.54 ?  149 THR   A HG1  1 
ATOM   3269 H  HG21 . THR   A 1 149 ? 27.023 -16.021 9.299   1.00 17.45 ?  149 THR   A HG21 1 
ATOM   3270 H  HG22 . THR   A 1 149 ? 26.326 -17.280 9.948   1.00 17.45 ?  149 THR   A HG22 1 
ATOM   3271 H  HG23 . THR   A 1 149 ? 26.291 -17.078 8.382   1.00 17.45 ?  149 THR   A HG23 1 
ATOM   3272 N  N    . ASN   A 1 150 ? 22.301 -15.519 10.821  1.00 13.25 ?  150 ASN   A N    1 
ATOM   3273 C  CA   . ASN   A 1 150 ? 21.016 -15.009 11.303  1.00 13.73 ?  150 ASN   A CA   1 
ATOM   3274 C  C    . ASN   A 1 150 ? 20.833 -13.571 10.841  1.00 12.84 ?  150 ASN   A C    1 
ATOM   3275 O  O    . ASN   A 1 150 ? 21.580 -12.676 11.257  1.00 14.36 ?  150 ASN   A O    1 
ATOM   3276 C  CB   . ASN   A 1 150 ? 20.958 -15.114 12.821  1.00 16.03 ?  150 ASN   A CB   1 
ATOM   3277 C  CG   . ASN   A 1 150 ? 20.854 -16.541 13.287  1.00 20.08 ?  150 ASN   A CG   1 
ATOM   3278 O  OD1  . ASN   A 1 150 ? 20.266 -17.376 12.603  1.00 21.24 ?  150 ASN   A OD1  1 
ATOM   3279 N  ND2  . ASN   A 1 150 ? 21.443 -16.838 14.443  1.00 22.48 ?  150 ASN   A ND2  1 
ATOM   3280 H  H    . ASN   A 1 150 ? 22.944 -15.432 11.382  1.00 16.05 ?  150 ASN   A H    1 
ATOM   3281 H  HA   . ASN   A 1 150 ? 20.296 -15.548 10.933  1.00 16.61 ?  150 ASN   A HA   1 
ATOM   3282 H  HB2  . ASN   A 1 150 ? 21.763 -14.733 13.199  1.00 19.38 ?  150 ASN   A HB2  1 
ATOM   3283 H  HB3  . ASN   A 1 150 ? 20.176 -14.644 13.146  1.00 19.38 ?  150 ASN   A HB3  1 
ATOM   3284 H  HD21 . ASN   A 1 150 ? 21.419 -17.644 14.755  1.00 27.11 ?  150 ASN   A HD21 1 
ATOM   3285 H  HD22 . ASN   A 1 150 ? 21.848 -16.224 14.892  1.00 27.11 ?  150 ASN   A HD22 1 
ATOM   3286 N  N    . VAL   A 1 151 ? 19.845 -13.343 9.982   1.00 12.44 ?  151 VAL   A N    1 
ATOM   3287 C  CA   . VAL   A 1 151 ? 19.631 -12.037 9.377   1.00 12.50 ?  151 VAL   A CA   1 
ATOM   3288 C  C    . VAL   A 1 151 ? 18.242 -11.521 9.739   1.00 12.31 ?  151 VAL   A C    1 
ATOM   3289 O  O    . VAL   A 1 151 ? 17.233 -12.231 9.594   1.00 13.72 ?  151 VAL   A O    1 
ATOM   3290 C  CB   . VAL   A 1 151 ? 19.920 -12.040 7.860   1.00 13.88 ?  151 VAL   A CB   1 
ATOM   3291 C  CG1  . VAL   A 1 151 ? 19.100 -13.078 7.121   1.00 14.86 ?  151 VAL   A CG1  1 
ATOM   3292 C  CG2  . VAL   A 1 151 ? 19.726 -10.642 7.262   1.00 14.17 ?  151 VAL   A CG2  1 
ATOM   3293 H  H    . VAL   A 1 151 ? 19.276 -13.939 9.729   1.00 15.06 ?  151 VAL   A H    1 
ATOM   3294 H  HA   . VAL   A 1 151 ? 20.274 -11.422 9.767   1.00 15.14 ?  151 VAL   A HA   1 
ATOM   3295 H  HB   . VAL   A 1 151 ? 20.854 -12.273 7.726   1.00 16.80 ?  151 VAL   A HB   1 
ATOM   3296 H  HG11 . VAL   A 1 151 ? 19.294 -13.030 6.170   1.00 17.97 ?  151 VAL   A HG11 1 
ATOM   3297 H  HG12 . VAL   A 1 151 ? 19.333 -13.965 7.453   1.00 17.97 ?  151 VAL   A HG12 1 
ATOM   3298 H  HG13 . VAL   A 1 151 ? 18.156 -12.913 7.272   1.00 17.97 ?  151 VAL   A HG13 1 
ATOM   3299 H  HG21 . VAL   A 1 151 ? 20.032 -10.650 6.337   1.00 17.14 ?  151 VAL   A HG21 1 
ATOM   3300 H  HG22 . VAL   A 1 151 ? 18.786 -10.411 7.292   1.00 17.14 ?  151 VAL   A HG22 1 
ATOM   3301 H  HG23 . VAL   A 1 151 ? 20.245 -10.005 7.773   1.00 17.14 ?  151 VAL   A HG23 1 
ATOM   3302 N  N    . TYR   A 1 152 ? 18.224 -10.277 10.219  1.00 12.55 ?  152 TYR   A N    1 
ATOM   3303 C  CA   . TYR   A 1 152 ? 17.030 -9.546  10.606  1.00 12.17 ?  152 TYR   A CA   1 
ATOM   3304 C  C    . TYR   A 1 152 ? 16.835 -8.443  9.577   1.00 11.87 ?  152 TYR   A C    1 
ATOM   3305 O  O    . TYR   A 1 152 ? 17.611 -7.480  9.533   1.00 12.21 ?  152 TYR   A O    1 
ATOM   3306 C  CB   . TYR   A 1 152 ? 17.205 -9.004  12.021  1.00 13.24 ?  152 TYR   A CB   1 
ATOM   3307 C  CG   . TYR   A 1 152 ? 17.157 -10.125 13.021  1.00 13.74 ?  152 TYR   A CG   1 
ATOM   3308 C  CD1  . TYR   A 1 152 ? 18.282 -10.894 13.295  1.00 15.37 ?  152 TYR   A CD1  1 
ATOM   3309 C  CD2  . TYR   A 1 152 ? 15.971 -10.459 13.653  1.00 14.16 ?  152 TYR   A CD2  1 
ATOM   3310 C  CE1  . TYR   A 1 152 ? 18.234 -11.949 14.185  1.00 16.68 ?  152 TYR   A CE1  1 
ATOM   3311 C  CE2  . TYR   A 1 152 ? 15.910 -11.522 14.546  1.00 15.89 ?  152 TYR   A CE2  1 
ATOM   3312 C  CZ   . TYR   A 1 152 ? 17.049 -12.258 14.808  1.00 16.74 ?  152 TYR   A CZ   1 
ATOM   3313 O  OH   . TYR   A 1 152 ? 17.008 -13.319 15.692  1.00 19.14 ?  152 TYR   A OH   1 
ATOM   3314 H  H    . TYR   A 1 152 ? 18.945 -9.803  10.317  1.00 15.20 ?  152 TYR   A H    1 
ATOM   3315 H  HA   . TYR   A 1 152 ? 16.266 -10.142 10.587  1.00 14.74 ?  152 TYR   A HA   1 
ATOM   3316 H  HB2  . TYR   A 1 152 ? 18.068 -8.571  12.094  1.00 16.03 ?  152 TYR   A HB2  1 
ATOM   3317 H  HB3  . TYR   A 1 152 ? 16.494 -8.382  12.220  1.00 16.03 ?  152 TYR   A HB3  1 
ATOM   3318 H  HD1  . TYR   A 1 152 ? 19.084 -10.689 12.868  1.00 18.58 ?  152 TYR   A HD1  1 
ATOM   3319 H  HD2  . TYR   A 1 152 ? 15.198 -9.966  13.474  1.00 17.14 ?  152 TYR   A HD2  1 
ATOM   3320 H  HE1  . TYR   A 1 152 ? 18.999 -12.443 14.360  1.00 20.16 ?  152 TYR   A HE1  1 
ATOM   3321 H  HE2  . TYR   A 1 152 ? 15.108 -11.727 14.973  1.00 19.21 ?  152 TYR   A HE2  1 
ATOM   3322 H  HH   . TYR   A 1 152 ? 16.235 -13.391 16.008  1.00 23.10 ?  152 TYR   A HH   1 
ATOM   3323 N  N    . LEU   A 1 153 ? 15.822 -8.607  8.732   1.00 12.07 ?  153 LEU   A N    1 
ATOM   3324 C  CA   . LEU   A 1 153 ? 15.562 -7.706  7.620   1.00 11.99 ?  153 LEU   A CA   1 
ATOM   3325 C  C    . LEU   A 1 153 ? 14.566 -6.633  8.027   1.00 12.40 ?  153 LEU   A C    1 
ATOM   3326 O  O    . LEU   A 1 153 ? 13.461 -6.941  8.487   1.00 13.64 ?  153 LEU   A O    1 
ATOM   3327 C  CB   . LEU   A 1 153 ? 14.999 -8.484  6.433   1.00 12.01 ?  153 LEU   A CB   1 
ATOM   3328 C  CG   . LEU   A 1 153 ? 15.943 -9.488  5.779   1.00 12.12 ?  153 LEU   A CG   1 
ATOM   3329 C  CD1  . LEU   A 1 153 ? 15.165 -10.390 4.837   1.00 12.85 ?  153 LEU   A CD1  1 
ATOM   3330 C  CD2  . LEU   A 1 153 ? 17.060 -8.769  5.034   1.00 12.83 ?  153 LEU   A CD2  1 
ATOM   3331 H  H    . LEU   A 1 153 ? 15.247 -9.255  8.794   1.00 14.62 ?  153 LEU   A H    1 
ATOM   3332 H  HA   . LEU   A 1 153 ? 16.388 -7.287  7.360   1.00 14.52 ?  153 LEU   A HA   1 
ATOM   3333 H  HB2  . LEU   A 1 153 ? 14.216 -8.974  6.736   1.00 14.56 ?  153 LEU   A HB2  1 
ATOM   3334 H  HB3  . LEU   A 1 153 ? 14.735 -7.845  5.755   1.00 14.56 ?  153 LEU   A HB3  1 
ATOM   3335 H  HG   . LEU   A 1 153 ? 16.351 -10.038 6.472   1.00 14.69 ?  153 LEU   A HG   1 
ATOM   3336 H  HD11 . LEU   A 1 153 ? 15.756 -11.078 4.504   1.00 15.56 ?  153 LEU   A HD11 1 
ATOM   3337 H  HD12 . LEU   A 1 153 ? 14.428 -10.786 5.324   1.00 15.56 ?  153 LEU   A HD12 1 
ATOM   3338 H  HD13 . LEU   A 1 153 ? 14.829 -9.852  4.104   1.00 15.56 ?  153 LEU   A HD13 1 
ATOM   3339 H  HD21 . LEU   A 1 153 ? 17.626 -9.432  4.616   1.00 15.54 ?  153 LEU   A HD21 1 
ATOM   3340 H  HD22 . LEU   A 1 153 ? 16.659 -8.197  4.363   1.00 15.54 ?  153 LEU   A HD22 1 
ATOM   3341 H  HD23 . LEU   A 1 153 ? 17.569 -8.241  5.664   1.00 15.54 ?  153 LEU   A HD23 1 
ATOM   3342 N  N    A ALA   A 1 154 ? 14.933 -5.380  7.779   0.74 12.38 ?  154 ALA   A N    1 
ATOM   3343 N  N    B ALA   A 1 154 ? 14.975 -5.374  7.906   0.26 12.01 ?  154 ALA   A N    1 
ATOM   3344 C  CA   A ALA   A 1 154 ? 14.055 -4.232  7.958   0.74 12.64 ?  154 ALA   A CA   1 
ATOM   3345 C  CA   B ALA   A 1 154 ? 14.140 -4.227  8.238   0.26 12.00 ?  154 ALA   A CA   1 
ATOM   3346 C  C    A ALA   A 1 154 ? 13.570 -3.765  6.590   0.74 12.19 ?  154 ALA   A C    1 
ATOM   3347 C  C    B ALA   A 1 154 ? 13.691 -3.594  6.931   0.26 11.88 ?  154 ALA   A C    1 
ATOM   3348 O  O    A ALA   A 1 154 ? 14.382 -3.408  5.730   0.74 12.80 ?  154 ALA   A O    1 
ATOM   3349 O  O    B ALA   A 1 154 ? 14.528 -3.189  6.118   0.26 11.54 ?  154 ALA   A O    1 
ATOM   3350 C  CB   A ALA   A 1 154 ? 14.809 -3.102  8.657   0.74 13.00 ?  154 ALA   A CB   1 
ATOM   3351 C  CB   B ALA   A 1 154 ? 14.917 -3.215  9.080   0.26 11.91 ?  154 ALA   A CB   1 
ATOM   3352 H  H    A ALA   A 1 154 ? 15.716 -5.166  7.491   0.74 14.99 ?  154 ALA   A H    1 
ATOM   3353 H  H    B ALA   A 1 154 ? 15.753 -5.151  7.613   0.26 14.55 ?  154 ALA   A H    1 
ATOM   3354 H  HA   A ALA   A 1 154 ? 13.288 -4.483  8.499   0.74 15.31 ?  154 ALA   A HA   1 
ATOM   3355 H  HA   B ALA   A 1 154 ? 13.357 -4.510  8.735   0.26 14.55 ?  154 ALA   A HA   1 
ATOM   3356 H  HB1  A ALA   A 1 154 ? 14.212 -2.347  8.766   0.74 15.74 ?  154 ALA   A HB1  1 
ATOM   3357 H  HB1  B ALA   A 1 154 ? 14.339 -2.464  9.292   0.26 14.44 ?  154 ALA   A HB1  1 
ATOM   3358 H  HB2  A ALA   A 1 154 ? 15.116 -3.414  9.521   0.74 15.74 ?  154 ALA   A HB2  1 
ATOM   3359 H  HB2  B ALA   A 1 154 ? 15.211 -3.645  9.898   0.26 14.44 ?  154 ALA   A HB2  1 
ATOM   3360 H  HB3  A ALA   A 1 154 ? 15.569 -2.847  8.108   0.74 15.74 ?  154 ALA   A HB3  1 
ATOM   3361 H  HB3  B ALA   A 1 154 ? 15.686 -2.906  8.575   0.26 14.44 ?  154 ALA   A HB3  1 
ATOM   3362 N  N    A VAL   A 1 155 ? 12.254 -3.768  6.395   0.54 11.16 ?  155 VAL   A N    1 
ATOM   3363 N  N    B VAL   A 1 155 ? 12.380 -3.518  6.722   0.26 12.14 ?  155 VAL   A N    1 
ATOM   3364 C  CA   A VAL   A 1 155 ? 11.612 -3.321  5.160   0.54 12.69 ?  155 VAL   A CA   1 
ATOM   3365 C  CA   B VAL   A 1 155 ? 11.812 -3.004  5.481   0.26 13.57 ?  155 VAL   A CA   1 
ATOM   3366 C  CA   T VAL   A 1 155 ? 11.636 -3.320  5.285   0.20 12.97 ?  155 VAL   A CA   1 
ATOM   3367 C  C    A VAL   A 1 155 ? 10.878 -2.024  5.477   0.54 13.71 ?  155 VAL   A C    1 
ATOM   3368 C  C    B VAL   A 1 155 ? 11.037 -1.735  5.809   0.26 15.37 ?  155 VAL   A C    1 
ATOM   3369 C  C    T VAL   A 1 155 ? 11.026 -1.954  5.599   0.20 12.91 ?  155 VAL   A C    1 
ATOM   3370 O  O    A VAL   A 1 155 ? 9.888  -2.034  6.217   0.54 14.23 ?  155 VAL   A O    1 
ATOM   3371 O  O    B VAL   A 1 155 ? 10.105 -1.762  6.622   0.26 15.21 ?  155 VAL   A O    1 
ATOM   3372 O  O    T VAL   A 1 155 ? 10.207 -1.822  6.508   0.20 12.66 ?  155 VAL   A O    1 
ATOM   3373 C  CB   A VAL   A 1 155 ? 10.644 -4.384  4.617   0.54 13.40 ?  155 VAL   A CB   1 
ATOM   3374 C  CB   B VAL   A 1 155 ? 10.933 -4.051  4.780   0.26 13.45 ?  155 VAL   A CB   1 
ATOM   3375 C  CB   T VAL   A 1 155 ? 10.597 -4.317  4.727   0.20 13.08 ?  155 VAL   A CB   1 
ATOM   3376 C  CG1  A VAL   A 1 155 ? 9.949  -3.886  3.355   0.54 14.08 ?  155 VAL   A CG1  1 
ATOM   3377 C  CG1  B VAL   A 1 155 ? 10.342 -3.483  3.500   0.26 13.24 ?  155 VAL   A CG1  1 
ATOM   3378 C  CG1  T VAL   A 1 155 ? 9.897  -3.732  3.512   0.20 13.31 ?  155 VAL   A CG1  1 
ATOM   3379 C  CG2  A VAL   A 1 155 ? 11.377 -5.695  4.344   0.54 14.29 ?  155 VAL   A CG2  1 
ATOM   3380 C  CG2  B VAL   A 1 155 ? 11.760 -5.295  4.472   0.26 13.54 ?  155 VAL   A CG2  1 
ATOM   3381 C  CG2  T VAL   A 1 155 ? 11.267 -5.643  4.372   0.20 13.28 ?  155 VAL   A CG2  1 
ATOM   3382 H  H    A VAL   A 1 155 ? 11.692 -4.067  6.977   0.54 13.53 ?  155 VAL   A H    1 
ATOM   3383 H  H    B VAL   A 1 155 ? 11.786 -3.755  7.300   0.26 14.71 ?  155 VAL   A H    1 
ATOM   3384 H  HA   A VAL   A 1 155 ? 12.287 -3.148  4.486   0.54 15.37 ?  155 VAL   A HA   1 
ATOM   3385 H  HA   B VAL   A 1 155 ? 12.532 -2.768  4.876   0.26 16.42 ?  155 VAL   A HA   1 
ATOM   3386 H  HB   A VAL   A 1 155 ? 9.961  -4.563  5.284   0.54 16.22 ?  155 VAL   A HB   1 
ATOM   3387 H  HB   B VAL   A 1 155 ? 10.207 -4.310  5.366   0.26 16.28 ?  155 VAL   A HB   1 
ATOM   3388 H  HB   T VAL   A 1 155 ? 9.928  -4.494  5.406   0.20 15.83 ?  155 VAL   A HB   1 
ATOM   3389 H  HG11 A VAL   A 1 155 ? 9.475  -4.625  2.941   0.54 17.03 ?  155 VAL   A HG11 1 
ATOM   3390 H  HG11 B VAL   A 1 155 ? 9.721  -4.127  3.130   0.26 16.03 ?  155 VAL   A HG11 1 
ATOM   3391 H  HG11 T VAL   A 1 155 ? 9.402  -4.436  3.065   0.20 16.11 ?  155 VAL   A HG11 1 
ATOM   3392 H  HG12 A VAL   A 1 155 ? 9.321  -3.186  3.594   0.54 17.03 ?  155 VAL   A HG12 1 
ATOM   3393 H  HG12 B VAL   A 1 155 ? 9.877  -2.653  3.691   0.26 16.03 ?  155 VAL   A HG12 1 
ATOM   3394 H  HG12 T VAL   A 1 155 ? 9.291  -3.034  3.801   0.20 16.11 ?  155 VAL   A HG12 1 
ATOM   3395 H  HG13 A VAL   A 1 155 ? 10.617 -3.539  2.744   0.54 17.03 ?  155 VAL   A HG13 1 
ATOM   3396 H  HG13 B VAL   A 1 155 ? 11.063 -3.325  2.872   0.26 16.03 ?  155 VAL   A HG13 1 
ATOM   3397 H  HG13 T VAL   A 1 155 ? 10.565 -3.367  2.911   0.20 16.11 ?  155 VAL   A HG13 1 
ATOM   3398 H  HG21 A VAL   A 1 155 ? 10.763 -6.321  3.929   0.54 17.29 ?  155 VAL   A HG21 1 
ATOM   3399 H  HG21 B VAL   A 1 155 ? 11.208 -5.931  3.990   0.26 16.39 ?  155 VAL   A HG21 1 
ATOM   3400 H  HG21 T VAL   A 1 155 ? 10.598 -6.256  4.029   0.20 16.08 ?  155 VAL   A HG21 1 
ATOM   3401 H  HG22 A VAL   A 1 155 ? 12.123 -5.520  3.749   0.54 17.29 ?  155 VAL   A HG22 1 
ATOM   3402 H  HG22 B VAL   A 1 155 ? 12.522 -5.041  3.927   0.26 16.39 ?  155 VAL   A HG22 1 
ATOM   3403 H  HG22 T VAL   A 1 155 ? 11.945 -5.483  3.695   0.20 16.08 ?  155 VAL   A HG22 1 
ATOM   3404 H  HG23 A VAL   A 1 155 ? 11.702 -6.058  5.183   0.54 17.29 ?  155 VAL   A HG23 1 
ATOM   3405 H  HG23 B VAL   A 1 155 ? 12.066 -5.688  5.304   0.26 16.39 ?  155 VAL   A HG23 1 
ATOM   3406 H  HG23 T VAL   A 1 155 ? 11.677 -6.014  5.169   0.20 16.08 ?  155 VAL   A HG23 1 
ATOM   3407 N  N    A PHE   A 1 156 ? 11.347 -0.908  4.907   0.54 15.21 ?  156 PHE   A N    1 
ATOM   3408 N  N    B PHE   A 1 156 ? 11.432 -0.625  5.185   0.26 17.23 ?  156 PHE   A N    1 
ATOM   3409 N  N    T PHE   A 1 156 ? 11.445 -0.937  4.841   0.20 13.26 ?  156 PHE   A N    1 
ATOM   3410 C  CA   A PHE   A 1 156 ? 10.820 0.403   5.293   0.54 16.95 ?  156 PHE   A CA   1 
ATOM   3411 C  CA   B PHE   A 1 156 ? 10.858 0.691   5.479   0.26 19.43 ?  156 PHE   A CA   1 
ATOM   3412 C  CA   T PHE   A 1 156 ? 11.016 0.432   5.120   0.20 13.55 ?  156 PHE   A CA   1 
ATOM   3413 C  C    A PHE   A 1 156 ? 9.357  0.570   4.898   0.54 16.87 ?  156 PHE   A C    1 
ATOM   3414 C  C    B PHE   A 1 156 ? 9.743  1.025   4.484   0.26 20.65 ?  156 PHE   A C    1 
ATOM   3415 C  C    T PHE   A 1 156 ? 9.558  0.657   4.734   0.20 14.12 ?  156 PHE   A C    1 
ATOM   3416 O  O    A PHE   A 1 156 ? 8.552  1.100   5.677   0.54 17.65 ?  156 PHE   A O    1 
ATOM   3417 O  O    B PHE   A 1 156 ? 9.839  1.938   3.662   0.26 21.17 ?  156 PHE   A O    1 
ATOM   3418 O  O    T PHE   A 1 156 ? 8.809  1.313   5.468   0.20 14.53 ?  156 PHE   A O    1 
ATOM   3419 C  CB   A PHE   A 1 156 ? 11.666 1.517   4.675   0.54 17.97 ?  156 PHE   A CB   1 
ATOM   3420 C  CB   B PHE   A 1 156 ? 11.961 1.748   5.501   0.26 20.22 ?  156 PHE   A CB   1 
ATOM   3421 C  CB   T PHE   A 1 156 ? 11.920 1.412   4.371   0.20 12.84 ?  156 PHE   A CB   1 
ATOM   3422 C  CG   A PHE   A 1 156 ? 11.163 2.903   4.996   0.54 19.70 ?  156 PHE   A CG   1 
ATOM   3423 C  CG   B PHE   A 1 156 ? 11.464 3.158   5.674   0.26 20.88 ?  156 PHE   A CG   1 
ATOM   3424 C  CG   T PHE   A 1 156 ? 11.552 2.860   4.568   0.20 12.74 ?  156 PHE   A CG   1 
ATOM   3425 C  CD1  A PHE   A 1 156 ? 11.095 3.329   6.313   0.54 20.40 ?  156 PHE   A CD1  1 
ATOM   3426 C  CD1  B PHE   A 1 156 ? 10.576 3.486   6.686   0.26 20.94 ?  156 PHE   A CD1  1 
ATOM   3427 C  CD1  T PHE   A 1 156 ? 11.892 3.521   5.739   0.20 13.31 ?  156 PHE   A CD1  1 
ATOM   3428 C  CD2  A PHE   A 1 156 ? 10.760 3.769   3.991   0.54 20.67 ?  156 PHE   A CD2  1 
ATOM   3429 C  CD2  B PHE   A 1 156 ? 11.907 4.162   4.829   0.26 21.04 ?  156 PHE   A CD2  1 
ATOM   3430 C  CD2  T PHE   A 1 156 ? 10.878 3.560   3.579   0.20 13.04 ?  156 PHE   A CD2  1 
ATOM   3431 C  CE1  A PHE   A 1 156 ? 10.636 4.592   6.622   0.54 21.18 ?  156 PHE   A CE1  1 
ATOM   3432 C  CE1  B PHE   A 1 156 ? 10.126 4.789   6.837   0.26 21.02 ?  156 PHE   A CE1  1 
ATOM   3433 C  CE1  T PHE   A 1 156 ? 11.557 4.848   5.926   0.20 13.65 ?  156 PHE   A CE1  1 
ATOM   3434 C  CE2  A PHE   A 1 156 ? 10.295 5.036   4.296   0.54 21.61 ?  156 PHE   A CE2  1 
ATOM   3435 C  CE2  B PHE   A 1 156 ? 11.464 5.464   4.976   0.26 20.93 ?  156 PHE   A CE2  1 
ATOM   3436 C  CE2  T PHE   A 1 156 ? 10.544 4.889   3.758   0.20 13.58 ?  156 PHE   A CE2  1 
ATOM   3437 C  CZ   A PHE   A 1 156 ? 10.237 5.447   5.613   0.54 21.87 ?  156 PHE   A CZ   1 
ATOM   3438 C  CZ   B PHE   A 1 156 ? 10.576 5.779   5.982   0.26 21.02 ?  156 PHE   A CZ   1 
ATOM   3439 C  CZ   T PHE   A 1 156 ? 10.883 5.534   4.934   0.20 13.49 ?  156 PHE   A CZ   1 
ATOM   3440 H  H    A PHE   A 1 156 ? 11.964 -0.898  4.307   0.54 18.39 ?  156 PHE   A H    1 
ATOM   3441 H  H    B PHE   A 1 156 ? 12.057 -0.607  4.590   0.26 20.81 ?  156 PHE   A H    1 
ATOM   3442 H  H    T PHE   A 1 156 ? 11.984 -1.020  4.177   0.20 16.06 ?  156 PHE   A H    1 
ATOM   3443 H  HA   A PHE   A 1 156 ? 10.883 0.481   6.257   0.54 20.49 ?  156 PHE   A HA   1 
ATOM   3444 H  HA   B PHE   A 1 156 ? 10.465 0.665   6.362   0.26 23.46 ?  156 PHE   A HA   1 
ATOM   3445 H  HA   T PHE   A 1 156 ? 11.110 0.596   6.072   0.20 16.39 ?  156 PHE   A HA   1 
ATOM   3446 H  HB2  A PHE   A 1 156 ? 12.579 1.439   5.011   0.54 21.71 ?  156 PHE   A HB2  1 
ATOM   3447 H  HB2  B PHE   A 1 156 ? 12.570 1.548   6.226   0.26 24.40 ?  156 PHE   A HB2  1 
ATOM   3448 H  HB2  T PHE   A 1 156 ? 12.831 1.289   4.681   0.20 15.55 ?  156 PHE   A HB2  1 
ATOM   3449 H  HB3  A PHE   A 1 156 ? 11.667 1.409   3.711   0.54 21.71 ?  156 PHE   A HB3  1 
ATOM   3450 H  HB3  B PHE   A 1 156 ? 12.442 1.712   4.663   0.26 24.40 ?  156 PHE   A HB3  1 
ATOM   3451 H  HB3  T PHE   A 1 156 ? 11.866 1.216   3.423   0.20 15.55 ?  156 PHE   A HB3  1 
ATOM   3452 H  HD1  A PHE   A 1 156 ? 11.367 2.752   6.999   0.54 24.62 ?  156 PHE   A HD1  1 
ATOM   3453 H  HD1  B PHE   A 1 156 ? 10.270 2.825   7.264   0.26 25.27 ?  156 PHE   A HD1  1 
ATOM   3454 H  HD1  T PHE   A 1 156 ? 12.341 3.056   6.415   0.20 16.12 ?  156 PHE   A HD1  1 
ATOM   3455 H  HD2  A PHE   A 1 156 ? 10.802 3.487   3.105   0.54 24.94 ?  156 PHE   A HD2  1 
ATOM   3456 H  HD2  B PHE   A 1 156 ? 12.507 3.957   4.149   0.26 25.38 ?  156 PHE   A HD2  1 
ATOM   3457 H  HD2  T PHE   A 1 156 ? 10.647 3.124   2.792   0.20 15.78 ?  156 PHE   A HD2  1 
ATOM   3458 H  HE1  A PHE   A 1 156 ? 10.598 4.865   7.512   0.54 25.56 ?  156 PHE   A HE1  1 
ATOM   3459 H  HE1  B PHE   A 1 156 ? 9.526  4.999   7.516   0.26 25.37 ?  156 PHE   A HE1  1 
ATOM   3460 H  HE1  T PHE   A 1 156 ? 11.784 5.276   6.720   0.20 16.52 ?  156 PHE   A HE1  1 
ATOM   3461 H  HE2  A PHE   A 1 156 ? 10.031 5.605   3.616   0.54 26.07 ?  156 PHE   A HE2  1 
ATOM   3462 H  HE2  B PHE   A 1 156 ? 11.768 6.127   4.398   0.26 25.26 ?  156 PHE   A HE2  1 
ATOM   3463 H  HE2  T PHE   A 1 156 ? 10.088 5.345   3.093   0.20 16.44 ?  156 PHE   A HE2  1 
ATOM   3464 H  HZ   A PHE   A 1 156 ? 9.929  6.296   5.823   0.54 26.39 ?  156 PHE   A HZ   1 
ATOM   3465 H  HZ   B PHE   A 1 156 ? 10.275 6.655   6.081   0.26 25.37 ?  156 PHE   A HZ   1 
ATOM   3466 H  HZ   T PHE   A 1 156 ? 10.656 6.424   5.059   0.20 16.33 ?  156 PHE   A HZ   1 
ATOM   3467 N  N    A ASP   A 1 157 ? 9.002  0.141   3.693   0.54 16.87 ?  157 ASP   A N    1 
ATOM   3468 N  N    B ASP   A 1 157 ? 8.664  0.247   4.588   0.26 20.99 ?  157 ASP   A N    1 
ATOM   3469 N  N    T ASP   A 1 157 ? 9.144  0.132   3.586   0.20 14.55 ?  157 ASP   A N    1 
ATOM   3470 C  CA   A ASP   A 1 157 ? 7.680  0.397   3.133   0.54 18.02 ?  157 ASP   A CA   1 
ATOM   3471 C  CA   B ASP   A 1 157 ? 7.414  0.475   3.867   0.26 21.46 ?  157 ASP   A CA   1 
ATOM   3472 C  CA   T ASP   A 1 157 ? 7.826  0.399   3.026   0.20 15.13 ?  157 ASP   A CA   1 
ATOM   3473 C  C    A ASP   A 1 157 ? 6.693  -0.627  3.681   0.54 18.02 ?  157 ASP   A C    1 
ATOM   3474 C  C    B ASP   A 1 157 ? 6.446  -0.652  4.210   0.26 21.26 ?  157 ASP   A C    1 
ATOM   3475 C  C    T ASP   A 1 157 ? 6.817  -0.586  3.606   0.20 16.08 ?  157 ASP   A C    1 
ATOM   3476 O  O    A ASP   A 1 157 ? 6.821  -1.828  3.411   0.54 17.18 ?  157 ASP   A O    1 
ATOM   3477 O  O    B ASP   A 1 157 ? 6.879  -1.763  4.532   0.26 21.72 ?  157 ASP   A O    1 
ATOM   3478 O  O    T ASP   A 1 157 ? 6.964  -1.802  3.438   0.20 15.82 ?  157 ASP   A O    1 
ATOM   3479 C  CB   A ASP   A 1 157 ? 7.763  0.313   1.613   0.54 19.49 ?  157 ASP   A CB   1 
ATOM   3480 C  CB   B ASP   A 1 157 ? 7.634  0.517   2.354   0.26 22.02 ?  157 ASP   A CB   1 
ATOM   3481 C  CB   T ASP   A 1 157 ? 7.900  0.254   1.508   0.20 14.81 ?  157 ASP   A CB   1 
ATOM   3482 C  CG   A ASP   A 1 157 ? 6.499  0.802   0.933   0.54 21.11 ?  157 ASP   A CG   1 
ATOM   3483 C  CG   B ASP   A 1 157 ? 6.443  1.066   1.608   0.26 22.54 ?  157 ASP   A CG   1 
ATOM   3484 C  CG   T ASP   A 1 157 ? 6.756  0.933   0.799   0.20 14.24 ?  157 ASP   A CG   1 
ATOM   3485 O  OD1  A ASP   A 1 157 ? 6.216  2.017   0.980   0.54 22.82 ?  157 ASP   A OD1  1 
ATOM   3486 O  OD1  B ASP   A 1 157 ? 5.395  0.388   1.585   0.26 22.25 ?  157 ASP   A OD1  1 
ATOM   3487 O  OD1  T ASP   A 1 157 ? 5.634  0.393   0.849   0.20 14.29 ?  157 ASP   A OD1  1 
ATOM   3488 O  OD2  A ASP   A 1 157 ? 5.777  -0.041  0.359   0.54 20.93 -1 157 ASP   A OD2  1 
ATOM   3489 O  OD2  B ASP   A 1 157 ? 6.555  2.179   1.053   0.26 23.20 -1 157 ASP   A OD2  1 
ATOM   3490 O  OD2  T ASP   A 1 157 ? 6.981  2.005   0.196   0.20 13.41 -1 157 ASP   A OD2  1 
ATOM   3491 H  H    A ASP   A 1 157 ? 9.523  -0.314  3.172   0.54 20.38 ?  157 ASP   A H    1 
ATOM   3492 H  H    B ASP   A 1 157 ? 8.635  -0.442  5.094   0.26 25.33 ?  157 ASP   A H    1 
ATOM   3493 H  H    T ASP   A 1 157 ? 9.626  -0.388  3.098   0.20 17.60 ?  157 ASP   A H    1 
ATOM   3494 H  HA   A ASP   A 1 157 ? 7.390  1.283   3.390   0.54 21.76 ?  157 ASP   A HA   1 
ATOM   3495 H  HA   B ASP   A 1 157 ? 7.030  1.326   4.148   0.26 25.90 ?  157 ASP   A HA   1 
ATOM   3496 H  HA   T ASP   A 1 157 ? 7.551  1.303   3.246   0.20 18.29 ?  157 ASP   A HA   1 
ATOM   3497 H  HB2  A ASP   A 1 157 ? 8.540  0.822   1.319   0.54 23.53 ?  157 ASP   A HB2  1 
ATOM   3498 H  HB2  B ASP   A 1 157 ? 8.389  1.074   2.139   0.26 26.56 ?  157 ASP   A HB2  1 
ATOM   3499 H  HB2  T ASP   A 1 157 ? 8.719  0.651   1.192   0.20 17.91 ?  157 ASP   A HB2  1 
ATOM   3500 H  HB3  A ASP   A 1 157 ? 7.877  -0.615  1.359   0.54 23.53 ?  157 ASP   A HB3  1 
ATOM   3501 H  HB3  B ASP   A 1 157 ? 7.776  -0.386  2.034   0.26 26.56 ?  157 ASP   A HB3  1 
ATOM   3502 H  HB3  T ASP   A 1 157 ? 7.885  -0.691  1.287   0.20 17.91 ?  157 ASP   A HB3  1 
ATOM   3503 N  N    A LYS   A 1 158 ? 5.710  -0.160  4.462   0.54 19.60 ?  158 LYS   A N    1 
ATOM   3504 N  N    B LYS   A 1 158 ? 5.140  -0.393  4.131   0.26 20.30 ?  158 LYS   A N    1 
ATOM   3505 N  N    T LYS   A 1 158 ? 5.791  -0.062  4.283   0.20 17.55 ?  158 LYS   A N    1 
ATOM   3506 C  CA   A LYS   A 1 158 ? 4.728  -1.076  5.039   0.54 20.67 ?  158 LYS   A CA   1 
ATOM   3507 C  CA   B LYS   A 1 158 ? 4.130  -1.356  4.563   0.26 19.54 ?  158 LYS   A CA   1 
ATOM   3508 C  CA   T LYS   A 1 158 ? 4.803  -0.935  4.911   0.20 19.06 ?  158 LYS   A CA   1 
ATOM   3509 C  C    A LYS   A 1 158 ? 3.978  -1.823  3.949   0.54 19.94 ?  158 LYS   A C    1 
ATOM   3510 C  C    B LYS   A 1 158 ? 3.591  -2.214  3.420   0.26 17.31 ?  158 LYS   A C    1 
ATOM   3511 C  C    T LYS   A 1 158 ? 4.040  -1.743  3.868   0.20 19.19 ?  158 LYS   A C    1 
ATOM   3512 O  O    A LYS   A 1 158 ? 3.765  -3.037  4.049   0.54 20.05 ?  158 LYS   A O    1 
ATOM   3513 O  O    B LYS   A 1 158 ? 3.562  -3.445  3.530   0.26 16.51 ?  158 LYS   A O    1 
ATOM   3514 O  O    T LYS   A 1 158 ? 3.818  -2.946  4.047   0.20 19.28 ?  158 LYS   A O    1 
ATOM   3515 C  CB   A LYS   A 1 158 ? 3.752  -0.321  5.947   0.54 22.83 ?  158 LYS   A CB   1 
ATOM   3516 C  CB   B LYS   A 1 158 ? 2.979  -0.633  5.284   0.26 21.07 ?  158 LYS   A CB   1 
ATOM   3517 C  CB   T LYS   A 1 158 ? 3.840  -0.118  5.776   0.20 20.62 ?  158 LYS   A CB   1 
ATOM   3518 C  CG   A LYS   A 1 158 ? 2.507  -1.123  6.370   0.54 25.05 ?  158 LYS   A CG   1 
ATOM   3519 C  CG   B LYS   A 1 158 ? 1.982  -1.561  5.979   0.26 22.42 ?  158 LYS   A CG   1 
ATOM   3520 C  CG   T LYS   A 1 158 ? 2.614  -0.893  6.262   0.20 22.10 ?  158 LYS   A CG   1 
ATOM   3521 C  CD   A LYS   A 1 158 ? 2.844  -2.415  7.127   0.54 26.79 ?  158 LYS   A CD   1 
ATOM   3522 C  CD   B LYS   A 1 158 ? 2.637  -2.397  7.074   0.26 23.60 ?  158 LYS   A CD   1 
ATOM   3523 C  CD   T LYS   A 1 158 ? 2.995  -2.097  7.116   0.20 23.46 ?  158 LYS   A CD   1 
ATOM   3524 C  CE   A LYS   A 1 158 ? 1.578  -3.103  7.649   0.54 27.86 ?  158 LYS   A CE   1 
ATOM   3525 C  CE   B LYS   A 1 158 ? 1.590  -3.009  7.998   0.26 24.36 ?  158 LYS   A CE   1 
ATOM   3526 C  CE   T LYS   A 1 158 ? 1.767  -2.911  7.509   0.20 24.44 ?  158 LYS   A CE   1 
ATOM   3527 N  NZ   A LYS   A 1 158 ? 1.845  -4.446  8.247   0.54 28.43 ?  158 LYS   A NZ   1 
ATOM   3528 N  NZ   B LYS   A 1 158 ? 1.774  -4.474  8.209   0.26 24.78 ?  158 LYS   A NZ   1 
ATOM   3529 N  NZ   T LYS   A 1 158 ? 2.117  -4.120  8.308   0.20 24.93 ?  158 LYS   A NZ   1 
ATOM   3530 H  H    A LYS   A 1 158 ? 5.602  0.663   4.672   0.54 23.66 ?  158 LYS   A H    1 
ATOM   3531 H  H    B LYS   A 1 158 ? 4.814  0.339   3.824   0.26 24.50 ?  158 LYS   A H    1 
ATOM   3532 H  H    T LYS   A 1 158 ? 5.647  0.778   4.391   0.20 21.20 ?  158 LYS   A H    1 
ATOM   3533 H  HA   A LYS   A 1 158 ? 5.189  -1.732  5.585   0.54 24.95 ?  158 LYS   A HA   1 
ATOM   3534 H  HA   B LYS   A 1 158 ? 4.535  -1.954  5.207   0.26 23.59 ?  158 LYS   A HA   1 
ATOM   3535 H  HA   T LYS   A 1 158 ? 5.261  -1.561  5.492   0.20 23.01 ?  158 LYS   A HA   1 
ATOM   3536 H  HB2  A LYS   A 1 158 ? 4.219  -0.055  6.756   0.54 27.53 ?  158 LYS   A HB2  1 
ATOM   3537 H  HB2  B LYS   A 1 158 ? 3.351  -0.048  5.966   0.26 25.42 ?  158 LYS   A HB2  1 
ATOM   3538 H  HB2  T LYS   A 1 158 ? 4.316  0.196   6.563   0.20 24.88 ?  158 LYS   A HB2  1 
ATOM   3539 H  HB3  A LYS   A 1 158 ? 3.444  0.470   5.479   0.54 27.53 ?  158 LYS   A HB3  1 
ATOM   3540 H  HB3  B LYS   A 1 158 ? 2.483  -0.105  4.640   0.26 25.42 ?  158 LYS   A HB3  1 
ATOM   3541 H  HB3  T LYS   A 1 158 ? 3.522  0.640   5.263   0.20 24.88 ?  158 LYS   A HB3  1 
ATOM   3542 H  HG2  A LYS   A 1 158 ? 1.968  -0.572  6.957   0.54 30.20 ?  158 LYS   A HG2  1 
ATOM   3543 H  HG2  B LYS   A 1 158 ? 1.280  -1.029  6.387   0.26 27.05 ?  158 LYS   A HG2  1 
ATOM   3544 H  HG2  T LYS   A 1 158 ? 2.068  -0.306  6.806   0.20 26.66 ?  158 LYS   A HG2  1 
ATOM   3545 H  HG3  A LYS   A 1 158 ? 1.991  -1.361  5.583   0.54 30.20 ?  158 LYS   A HG3  1 
ATOM   3546 H  HG3  B LYS   A 1 158 ? 1.600  -2.168  5.325   0.26 27.05 ?  158 LYS   A HG3  1 
ATOM   3547 H  HG3  T LYS   A 1 158 ? 2.100  -1.208  5.501   0.20 26.66 ?  158 LYS   A HG3  1 
ATOM   3548 H  HD2  A LYS   A 1 158 ? 3.303  -3.028  6.533   0.54 32.29 ?  158 LYS   A HD2  1 
ATOM   3549 H  HD2  B LYS   A 1 158 ? 3.147  -3.117  6.669   0.26 28.46 ?  158 LYS   A HD2  1 
ATOM   3550 H  HD2  T LYS   A 1 158 ? 3.591  -2.675  6.615   0.20 28.29 ?  158 LYS   A HD2  1 
ATOM   3551 H  HD3  A LYS   A 1 158 ? 3.403  -2.202  7.890   0.54 32.29 ?  158 LYS   A HD3  1 
ATOM   3552 H  HD3  B LYS   A 1 158 ? 3.221  -1.831  7.606   0.26 28.46 ?  158 LYS   A HD3  1 
ATOM   3553 H  HD3  T LYS   A 1 158 ? 3.429  -1.790  7.928   0.20 28.29 ?  158 LYS   A HD3  1 
ATOM   3554 H  HE2  A LYS   A 1 158 ? 1.175  -2.546  8.334   0.54 33.57 ?  158 LYS   A HE2  1 
ATOM   3555 H  HE2  B LYS   A 1 158 ? 1.643  -2.575  8.864   0.26 29.38 ?  158 LYS   A HE2  1 
ATOM   3556 H  HE2  T LYS   A 1 158 ? 1.175  -2.358  8.044   0.20 29.47 ?  158 LYS   A HE2  1 
ATOM   3557 H  HE3  A LYS   A 1 158 ? 0.960  -3.222  6.913   0.54 33.57 ?  158 LYS   A HE3  1 
ATOM   3558 H  HE3  B LYS   A 1 158 ? 0.712  -2.871  7.612   0.26 29.38 ?  158 LYS   A HE3  1 
ATOM   3559 H  HE3  T LYS   A 1 158 ? 1.310  -3.205  6.705   0.20 29.47 ?  158 LYS   A HE3  1 
ATOM   3560 H  HZ1  A LYS   A 1 158 ? 1.084  -4.808  8.535   0.54 34.25 ?  158 LYS   A HZ1  1 
ATOM   3561 H  HZ1  B LYS   A 1 158 ? 1.140  -4.784  8.753   0.26 29.88 ?  158 LYS   A HZ1  1 
ATOM   3562 H  HZ1  T LYS   A 1 158 ? 1.379  -4.571  8.519   0.20 30.06 ?  158 LYS   A HZ1  1 
ATOM   3563 H  HZ2  A LYS   A 1 158 ? 2.207  -4.985  7.637   0.54 34.25 ?  158 LYS   A HZ2  1 
ATOM   3564 H  HZ2  B LYS   A 1 158 ? 1.721  -4.902  7.431   0.26 29.88 ?  158 LYS   A HZ2  1 
ATOM   3565 H  HZ2  T LYS   A 1 158 ? 2.654  -4.651  7.836   0.20 30.06 ?  158 LYS   A HZ2  1 
ATOM   3566 H  HZ3  A LYS   A 1 158 ? 2.407  -4.370  8.933   0.54 34.25 ?  158 LYS   A HZ3  1 
ATOM   3567 H  HZ3  B LYS   A 1 158 ? 2.570  -4.632  8.573   0.26 29.88 ?  158 LYS   A HZ3  1 
ATOM   3568 H  HZ3  T LYS   A 1 158 ? 2.533  -3.881  9.057   0.20 30.06 ?  158 LYS   A HZ3  1 
ATOM   3569 N  N    A ASN   A 1 159 ? 3.571  -1.118  2.894   0.54 19.91 ?  159 ASN   A N    1 
ATOM   3570 N  N    B ASN   A 1 159 ? 3.165  -1.589  2.318   0.26 16.58 ?  159 ASN   A N    1 
ATOM   3571 N  N    T ASN   A 1 159 ? 3.627  -1.104  2.780   0.20 19.43 ?  159 ASN   A N    1 
ATOM   3572 C  CA   A ASN   A 1 159 ? 2.895  -1.796  1.798   0.54 19.71 ?  159 ASN   A CA   1 
ATOM   3573 C  CA   B ASN   A 1 159 ? 2.567  -2.340  1.215   0.26 16.25 ?  159 ASN   A CA   1 
ATOM   3574 C  CA   T ASN   A 1 159 ? 2.888  -1.798  1.733   0.20 19.59 ?  159 ASN   A CA   1 
ATOM   3575 C  C    A ASN   A 1 159 ? 3.791  -2.863  1.180   0.54 18.48 ?  159 ASN   A C    1 
ATOM   3576 C  C    B ASN   A 1 159 ? 3.479  -3.473  0.757   0.26 15.37 ?  159 ASN   A C    1 
ATOM   3577 C  C    T ASN   A 1 159 ? 3.728  -2.897  1.093   0.20 19.19 ?  159 ASN   A C    1 
ATOM   3578 O  O    A ASN   A 1 159 ? 3.337  -3.975  0.895   0.54 17.94 ?  159 ASN   A O    1 
ATOM   3579 O  O    B ASN   A 1 159 ? 3.054  -4.632  0.648   0.26 15.39 ?  159 ASN   A O    1 
ATOM   3580 O  O    T ASN   A 1 159 ? 3.205  -3.945  0.722   0.20 19.18 ?  159 ASN   A O    1 
ATOM   3581 C  CB   A ASN   A 1 159 ? 2.409  -0.776  0.767   0.54 21.22 ?  159 ASN   A CB   1 
ATOM   3582 C  CB   B ASN   A 1 159 ? 2.245  -1.394  0.052   0.26 17.20 ?  159 ASN   A CB   1 
ATOM   3583 C  CB   T ASN   A 1 159 ? 2.395  -0.812  0.671   0.20 20.31 ?  159 ASN   A CB   1 
ATOM   3584 C  CG   A ASN   A 1 159 ? 1.200  0.005   1.252   0.54 22.97 ?  159 ASN   A CG   1 
ATOM   3585 C  CG   B ASN   A 1 159 ? 0.811  -0.890  0.083   0.26 18.26 ?  159 ASN   A CG   1 
ATOM   3586 C  CG   T ASN   A 1 159 ? 1.204  0.002   1.144   0.20 21.05 ?  159 ASN   A CG   1 
ATOM   3587 O  OD1  A ASN   A 1 159 ? 0.382  -0.514  2.009   0.54 23.94 ?  159 ASN   A OD1  1 
ATOM   3588 O  OD1  B ASN   A 1 159 ? 0.187  -0.818  1.142   0.26 19.00 ?  159 ASN   A OD1  1 
ATOM   3589 O  OD1  T ASN   A 1 159 ? 0.390  -0.473  1.935   0.20 21.45 ?  159 ASN   A OD1  1 
ATOM   3590 N  ND2  A ASN   A 1 159 ? 1.083  1.256   0.822   0.54 23.88 ?  159 ASN   A ND2  1 
ATOM   3591 N  ND2  B ASN   A 1 159 ? 0.280  -0.541  -1.087  0.26 18.58 ?  159 ASN   A ND2  1 
ATOM   3592 N  ND2  T ASN   A 1 159 ? 1.097  1.233   0.662   0.20 21.41 ?  159 ASN   A ND2  1 
ATOM   3593 H  H    A ASN   A 1 159 ? 3.678  -0.272  2.795   0.54 24.03 ?  159 ASN   A H    1 
ATOM   3594 H  H    B ASN   A 1 159 ? 3.216  -0.739  2.189   0.26 20.04 ?  159 ASN   A H    1 
ATOM   3595 H  H    T ASN   A 1 159 ? 3.757  -0.270  2.628   0.20 23.46 ?  159 ASN   A H    1 
ATOM   3596 H  HA   A ASN   A 1 159 ? 2.110  -2.244  2.152   0.54 23.79 ?  159 ASN   A HA   1 
ATOM   3597 H  HA   B ASN   A 1 159 ? 1.735  -2.730  1.513   0.26 19.64 ?  159 ASN   A HA   1 
ATOM   3598 H  HA   T ASN   A 1 159 ? 2.111  -2.220  2.128   0.20 23.64 ?  159 ASN   A HA   1 
ATOM   3599 H  HB2  A ASN   A 1 159 ? 3.114  -0.140  0.587   0.54 25.60 ?  159 ASN   A HB2  1 
ATOM   3600 H  HB2  B ASN   A 1 159 ? 2.833  -0.617  0.095   0.26 20.78 ?  159 ASN   A HB2  1 
ATOM   3601 H  HB2  T ASN   A 1 159 ? 3.110  -0.198  0.451   0.20 24.52 ?  159 ASN   A HB2  1 
ATOM   3602 H  HB3  A ASN   A 1 159 ? 2.159  -1.242  -0.047  0.54 25.60 ?  159 ASN   A HB3  1 
ATOM   3603 H  HB3  B ASN   A 1 159 ? 2.374  -1.856  -0.786  0.26 20.78 ?  159 ASN   A HB3  1 
ATOM   3604 H  HB3  T ASN   A 1 159 ? 2.128  -1.310  -0.121  0.20 24.52 ?  159 ASN   A HB3  1 
ATOM   3605 H  HD21 A ASN   A 1 159 ? 0.411  1.734   1.066   0.54 28.80 ?  159 ASN   A HD21 1 
ATOM   3606 H  HD21 B ASN   A 1 159 ? -0.528 -0.243  -1.127  0.26 22.43 ?  159 ASN   A HD21 1 
ATOM   3607 H  HD21 T ASN   A 1 159 ? 0.437  1.729   0.900   0.20 25.84 ?  159 ASN   A HD21 1 
ATOM   3608 H  HD22 A ASN   A 1 159 ? 1.680  1.586   0.301   0.54 28.80 ?  159 ASN   A HD22 1 
ATOM   3609 H  HD22 B ASN   A 1 159 ? 0.744  -0.610  -1.809  0.26 22.43 ?  159 ASN   A HD22 1 
ATOM   3610 H  HD22 T ASN   A 1 159 ? 1.687  1.531   0.115   0.20 25.84 ?  159 ASN   A HD22 1 
ATOM   3611 N  N    A LEU   A 1 160 ? 5.077  -2.568  1.004   0.54 17.45 ?  160 LEU   A N    1 
ATOM   3612 N  N    B LEU   A 1 160 ? 4.750  -3.160  0.497   0.26 15.15 ?  160 LEU   A N    1 
ATOM   3613 N  N    T LEU   A 1 160 ? 5.028  -2.663  0.968   0.20 18.74 ?  160 LEU   A N    1 
ATOM   3614 C  CA   A LEU   A 1 160 ? 5.966  -3.595  0.467   0.54 16.57 ?  160 LEU   A CA   1 
ATOM   3615 C  CA   B LEU   A 1 160 ? 5.641  -4.180  -0.039  0.26 15.85 ?  160 LEU   A CA   1 
ATOM   3616 C  CA   T LEU   A 1 160 ? 5.921  -3.673  0.413   0.20 18.35 ?  160 LEU   A CA   1 
ATOM   3617 C  C    A LEU   A 1 160 ? 6.133  -4.752  1.445   0.54 15.92 ?  160 LEU   A C    1 
ATOM   3618 C  C    B LEU   A 1 160 ? 6.066  -5.174  1.040   0.26 15.65 ?  160 LEU   A C    1 
ATOM   3619 O  O    A LEU   A 1 160 ? 6.140  -5.918  1.037   0.54 16.04 ?  160 LEU   A O    1 
ATOM   3620 O  O    B LEU   A 1 160 ? 6.226  -6.367  0.758   0.26 15.78 ?  160 LEU   A O    1 
ATOM   3621 C  CB   A LEU   A 1 160 ? 7.317  -2.999  0.091   0.54 16.49 ?  160 LEU   A CB   1 
ATOM   3622 C  CB   B LEU   A 1 160 ? 6.832  -3.516  -0.720  0.26 16.98 ?  160 LEU   A CB   1 
ATOM   3623 C  CB   T LEU   A 1 160 ? 7.292  -3.076  0.106   0.20 18.04 ?  160 LEU   A CB   1 
ATOM   3624 C  CG   A LEU   A 1 160 ? 8.323  -4.055  -0.369  0.54 17.79 ?  160 LEU   A CG   1 
ATOM   3625 C  CG   B LEU   A 1 160 ? 8.181  -3.549  -0.031  0.26 18.33 ?  160 LEU   A CG   1 
ATOM   3626 C  CG   T LEU   A 1 160 ? 8.351  -4.089  -0.325  0.20 18.14 ?  160 LEU   A CG   1 
ATOM   3627 C  CD1  A LEU   A 1 160 ? 7.815  -4.798  -1.589  0.54 18.66 ?  160 LEU   A CD1  1 
ATOM   3628 C  CD1  B LEU   A 1 160 ? 8.923  -4.762  -0.507  0.26 18.81 ?  160 LEU   A CD1  1 
ATOM   3629 C  CD1  T LEU   A 1 160 ? 7.907  -4.840  -1.565  0.20 18.26 ?  160 LEU   A CD1  1 
ATOM   3630 C  CD2  A LEU   A 1 160 ? 9.657  -3.406  -0.654  0.54 18.06 ?  160 LEU   A CD2  1 
ATOM   3631 C  CD2  B LEU   A 1 160 ? 8.905  -2.292  -0.398  0.26 18.76 ?  160 LEU   A CD2  1 
ATOM   3632 C  CD2  T LEU   A 1 160 ? 9.675  -3.391  -0.566  0.20 18.10 ?  160 LEU   A CD2  1 
ATOM   3633 H  H    A LEU   A 1 160 ? 5.447  -1.810  1.194   0.54 21.08 ?  160 LEU   A H    1 
ATOM   3634 H  H    B LEU   A 1 160 ? 5.112  -2.381  0.620   0.26 18.33 ?  160 LEU   A H    1 
ATOM   3635 H  H    T LEU   A 1 160 ? 5.418  -1.930  1.198   0.20 22.63 ?  160 LEU   A H    1 
ATOM   3636 H  HA   A LEU   A 1 160 ? 5.564  -3.940  -0.342  0.54 20.03 ?  160 LEU   A HA   1 
ATOM   3637 H  HA   B LEU   A 1 160 ? 5.160  -4.669  -0.720  0.26 19.16 ?  160 LEU   A HA   1 
ATOM   3638 H  HB2  A LEU   A 1 160 ? 7.202  -2.344  -0.625  0.54 19.93 ?  160 LEU   A HB2  1 
ATOM   3639 H  HB2  B LEU   A 1 160 ? 6.952  -3.940  -1.585  0.26 20.52 ?  160 LEU   A HB2  1 
ATOM   3640 H  HB2  T LEU   A 1 160 ? 7.197  -2.413  -0.601  0.20 21.79 ?  160 LEU   A HB2  1 
ATOM   3641 H  HB3  A LEU   A 1 160 ? 7.692  -2.570  0.873   0.54 19.93 ?  160 LEU   A HB3  1 
ATOM   3642 H  HB3  B LEU   A 1 160 ? 6.614  -2.583  -0.857  0.26 20.52 ?  160 LEU   A HB3  1 
ATOM   3643 H  HB3  T LEU   A 1 160 ? 7.625  -2.655  0.911   0.20 21.79 ?  160 LEU   A HB3  1 
ATOM   3644 H  HG   A LEU   A 1 160 ? 8.461  -4.696  0.343   0.54 21.49 ?  160 LEU   A HG   1 
ATOM   3645 H  HG   B LEU   A 1 160 ? 8.084  -3.584  0.935   0.26 22.14 ?  160 LEU   A HG   1 
ATOM   3646 H  HG   T LEU   A 1 160 ? 8.480  -4.732  0.390   0.20 21.91 ?  160 LEU   A HG   1 
ATOM   3647 H  HD11 A LEU   A 1 160 ? 8.526  -5.358  -1.931  0.54 22.53 ?  160 LEU   A HD11 1 
ATOM   3648 H  HD11 B LEU   A 1 160 ? 9.581  -5.014  0.154   0.26 22.71 ?  160 LEU   A HD11 1 
ATOM   3649 H  HD11 T LEU   A 1 160 ? 8.637  -5.399  -1.871  0.20 22.06 ?  160 LEU   A HD11 1 
ATOM   3650 H  HD12 A LEU   A 1 160 ? 7.056  -5.346  -1.333  0.54 22.53 ?  160 LEU   A HD12 1 
ATOM   3651 H  HD12 B LEU   A 1 160 ? 8.291  -5.482  -0.653  0.26 22.71 ?  160 LEU   A HD12 1 
ATOM   3652 H  HD12 T LEU   A 1 160 ? 7.139  -5.388  -1.343  0.20 22.06 ?  160 LEU   A HD12 1 
ATOM   3653 H  HD13 A LEU   A 1 160 ? 7.547  -4.153  -2.263  0.54 22.53 ?  160 LEU   A HD13 1 
ATOM   3654 H  HD13 B LEU   A 1 160 ? 9.357  -4.535  -1.339  0.26 22.71 ?  160 LEU   A HD13 1 
ATOM   3655 H  HD13 T LEU   A 1 160 ? 7.670  -4.198  -2.253  0.20 22.06 ?  160 LEU   A HD13 1 
ATOM   3656 H  HD21 A LEU   A 1 160 ? 10.285 -4.090  -0.939  0.54 21.82 ?  160 LEU   A HD21 1 
ATOM   3657 H  HD21 B LEU   A 1 160 ? 9.852  -2.443  -0.290  0.26 22.65 ?  160 LEU   A HD21 1 
ATOM   3658 H  HD21 T LEU   A 1 160 ? 10.334 -4.050  -0.835  0.20 21.86 ?  160 LEU   A HD21 1 
ATOM   3659 H  HD22 A LEU   A 1 160 ? 9.547  -2.747  -1.357  0.54 21.82 ?  160 LEU   A HD22 1 
ATOM   3660 H  HD22 B LEU   A 1 160 ? 8.707  -2.076  -1.323  0.26 22.65 ?  160 LEU   A HD22 1 
ATOM   3661 H  HD22 T LEU   A 1 160 ? 9.560  -2.732  -1.268  0.20 21.86 ?  160 LEU   A HD22 1 
ATOM   3662 H  HD23 A LEU   A 1 160 ? 9.982  -2.977  0.154   0.54 21.82 ?  160 LEU   A HD23 1 
ATOM   3663 H  HD23 B LEU   A 1 160 ? 8.604  -1.575  0.181   0.26 22.65 ?  160 LEU   A HD23 1 
ATOM   3664 H  HD23 T LEU   A 1 160 ? 9.958  -2.956  0.254   0.20 21.86 ?  160 LEU   A HD23 1 
ATOM   3665 N  N    A TYR   A 1 161 ? 6.280  -4.454  2.736   0.74 15.99 ?  161 TYR   A N    1 
ATOM   3666 N  N    B TYR   A 1 161 ? 6.246  -4.702  2.277   0.26 15.73 ?  161 TYR   A N    1 
ATOM   3667 C  CA   A TYR   A 1 161 ? 6.396  -5.514  3.731   0.74 15.93 ?  161 TYR   A CA   1 
ATOM   3668 C  CA   B TYR   A 1 161 ? 6.477  -5.615  3.392   0.26 16.25 ?  161 TYR   A CA   1 
ATOM   3669 C  C    A TYR   A 1 161 ? 5.234  -6.496  3.635   0.74 17.33 ?  161 TYR   A C    1 
ATOM   3670 C  C    B TYR   A 1 161 ? 5.336  -6.614  3.525   0.26 16.65 ?  161 TYR   A C    1 
ATOM   3671 O  O    A TYR   A 1 161 ? 5.433  -7.715  3.585   0.74 17.05 ?  161 TYR   A O    1 
ATOM   3672 O  O    B TYR   A 1 161 ? 5.564  -7.794  3.817   0.26 16.64 ?  161 TYR   A O    1 
ATOM   3673 C  CB   A TYR   A 1 161 ? 6.469  -4.908  5.128   0.74 15.57 ?  161 TYR   A CB   1 
ATOM   3674 C  CB   B TYR   A 1 161 ? 6.658  -4.825  4.690   0.26 16.36 ?  161 TYR   A CB   1 
ATOM   3675 C  CG   A TYR   A 1 161 ? 6.377  -5.944  6.208   0.74 15.06 ?  161 TYR   A CG   1 
ATOM   3676 C  CG   B TYR   A 1 161 ? 6.507  -5.655  5.948   0.26 16.71 ?  161 TYR   A CG   1 
ATOM   3677 C  CD1  A TYR   A 1 161 ? 7.499  -6.654  6.606   0.74 14.94 ?  161 TYR   A CD1  1 
ATOM   3678 C  CD1  B TYR   A 1 161 ? 7.595  -6.318  6.502   0.26 17.05 ?  161 TYR   A CD1  1 
ATOM   3679 C  CD2  A TYR   A 1 161 ? 5.167  -6.218  6.829   0.74 14.95 ?  161 TYR   A CD2  1 
ATOM   3680 C  CD2  B TYR   A 1 161 ? 5.277  -5.772  6.584   0.26 17.00 ?  161 TYR   A CD2  1 
ATOM   3681 C  CE1  A TYR   A 1 161 ? 7.420  -7.611  7.583   0.74 14.50 ?  161 TYR   A CE1  1 
ATOM   3682 C  CE1  B TYR   A 1 161 ? 7.460  -7.078  7.651   0.26 17.43 ?  161 TYR   A CE1  1 
ATOM   3683 C  CE2  A TYR   A 1 161 ? 5.081  -7.170  7.811   0.74 14.56 ?  161 TYR   A CE2  1 
ATOM   3684 C  CE2  B TYR   A 1 161 ? 5.133  -6.531  7.730   0.26 17.40 ?  161 TYR   A CE2  1 
ATOM   3685 C  CZ   A TYR   A 1 161 ? 6.211  -7.867  8.182   0.74 14.59 ?  161 TYR   A CZ   1 
ATOM   3686 C  CZ   B TYR   A 1 161 ? 6.227  -7.180  8.260   0.26 17.95 ?  161 TYR   A CZ   1 
ATOM   3687 O  OH   A TYR   A 1 161 ? 6.145  -8.819  9.163   0.74 15.15 ?  161 TYR   A OH   1 
ATOM   3688 O  OH   B TYR   A 1 161 ? 6.086  -7.935  9.402   0.26 19.00 ?  161 TYR   A OH   1 
ATOM   3689 H  H    A TYR   A 1 161 ? 6.311  -3.653  3.054   0.74 19.33 ?  161 TYR   A H    1 
ATOM   3690 H  H    B TYR   A 1 161 ? 6.244  -3.870  2.489   0.26 19.02 ?  161 TYR   A H    1 
ATOM   3691 H  HA   A TYR   A 1 161 ? 7.213  -6.002  3.572   0.74 19.26 ?  161 TYR   A HA   1 
ATOM   3692 H  HA   B TYR   A 1 161 ? 7.289  -6.115  3.232   0.26 19.64 ?  161 TYR   A HA   1 
ATOM   3693 H  HB2  A TYR   A 1 161 ? 7.315  -4.445  5.227   0.74 18.83 ?  161 TYR   A HB2  1 
ATOM   3694 H  HB2  B TYR   A 1 161 ? 7.548  -4.438  4.697   0.26 19.77 ?  161 TYR   A HB2  1 
ATOM   3695 H  HB3  A TYR   A 1 161 ? 5.733  -4.286  5.245   0.74 18.83 ?  161 TYR   A HB3  1 
ATOM   3696 H  HB3  B TYR   A 1 161 ? 5.995  -4.119  4.720   0.26 19.77 ?  161 TYR   A HB3  1 
ATOM   3697 H  HD1  A TYR   A 1 161 ? 8.314  -6.487  6.197   0.74 18.07 ?  161 TYR   A HD1  1 
ATOM   3698 H  HD1  B TYR   A 1 161 ? 8.427  -6.251  6.094   0.26 20.60 ?  161 TYR   A HD1  1 
ATOM   3699 H  HD2  A TYR   A 1 161 ? 4.400  -5.757  6.579   0.74 18.08 ?  161 TYR   A HD2  1 
ATOM   3700 H  HD2  B TYR   A 1 161 ? 4.535  -5.334  6.230   0.26 20.54 ?  161 TYR   A HD2  1 
ATOM   3701 H  HE1  A TYR   A 1 161 ? 8.178  -8.086  7.841   0.74 17.54 ?  161 TYR   A HE1  1 
ATOM   3702 H  HE1  B TYR   A 1 161 ? 8.196  -7.517  8.013   0.26 21.06 ?  161 TYR   A HE1  1 
ATOM   3703 H  HE2  A TYR   A 1 161 ? 4.258  -7.356  8.223   0.74 17.61 ?  161 TYR   A HE2  1 
ATOM   3704 H  HE2  B TYR   A 1 161 ? 4.302  -6.597  8.143   0.26 21.02 ?  161 TYR   A HE2  1 
ATOM   3705 H  HH   A TYR   A 1 161 ? 6.894  -9.173  9.292   0.74 18.32 ?  161 TYR   A HH   1 
ATOM   3706 H  HH   B TYR   A 1 161 ? 6.823  -8.271  9.617   0.26 22.95 ?  161 TYR   A HH   1 
ATOM   3707 N  N    A ASP   A 1 162 ? 4.003  -5.981  3.617   0.74 18.22 ?  162 ASP   A N    1 
ATOM   3708 N  N    B ASP   A 1 162 ? 4.098  -6.162  3.319   0.26 17.00 ?  162 ASP   A N    1 
ATOM   3709 C  CA   A ASP   A 1 162 ? 2.844  -6.866  3.542   0.74 19.30 ?  162 ASP   A CA   1 
ATOM   3710 C  CA   B ASP   A 1 162 ? 2.973  -7.088  3.384   0.26 17.69 ?  162 ASP   A CA   1 
ATOM   3711 C  C    A ASP   A 1 162 ? 2.891  -7.729  2.288   0.74 19.27 ?  162 ASP   A C    1 
ATOM   3712 C  C    B ASP   A 1 162 ? 2.951  -8.017  2.176   0.26 17.75 ?  162 ASP   A C    1 
ATOM   3713 O  O    A ASP   A 1 162 ? 2.527  -8.911  2.324   0.74 19.86 ?  162 ASP   A O    1 
ATOM   3714 O  O    B ASP   A 1 162 ? 2.623  -9.202  2.306   0.26 17.79 ?  162 ASP   A O    1 
ATOM   3715 C  CB   A ASP   A 1 162 ? 1.545  -6.056  3.584   0.74 20.76 ?  162 ASP   A CB   1 
ATOM   3716 C  CB   B ASP   A 1 162 ? 1.657  -6.325  3.525   0.26 18.47 ?  162 ASP   A CB   1 
ATOM   3717 C  CG   A ASP   A 1 162 ? 1.244  -5.488  4.957   0.74 22.32 ?  162 ASP   A CG   1 
ATOM   3718 C  CG   B ASP   A 1 162 ? 1.484  -5.704  4.895   0.26 19.28 ?  162 ASP   A CG   1 
ATOM   3719 O  OD1  A ASP   A 1 162 ? 1.918  -5.846  5.941   0.74 23.12 ?  162 ASP   A OD1  1 
ATOM   3720 O  OD1  B ASP   A 1 162 ? 1.859  -6.352  5.896   0.26 19.49 ?  162 ASP   A OD1  1 
ATOM   3721 O  OD2  A ASP   A 1 162 ? 0.309  -4.669  5.047   0.74 22.78 -1 162 ASP   A OD2  1 
ATOM   3722 O  OD2  B ASP   A 1 162 ? 0.965  -4.571  4.970   0.26 19.89 -1 162 ASP   A OD2  1 
ATOM   3723 H  H    A ASP   A 1 162 ? 3.811  -5.141  3.644   0.74 22.01 ?  162 ASP   A H    1 
ATOM   3724 H  H    B ASP   A 1 162 ? 3.891  -5.343  3.153   0.26 20.54 ?  162 ASP   A H    1 
ATOM   3725 H  HA   A ASP   A 1 162 ? 2.845  -7.459  4.306   0.74 23.30 ?  162 ASP   A HA   1 
ATOM   3726 H  HA   B ASP   A 1 162 ? 3.083  -7.637  4.171   0.26 21.36 ?  162 ASP   A HA   1 
ATOM   3727 H  HB2  A ASP   A 1 162 ? 1.610  -5.310  2.972   0.74 25.05 ?  162 ASP   A HB2  1 
ATOM   3728 H  HB2  B ASP   A 1 162 ? 1.626  -5.621  2.862   0.26 22.30 ?  162 ASP   A HB2  1 
ATOM   3729 H  HB3  A ASP   A 1 162 ? 0.801  -6.629  3.335   0.74 25.05 ?  162 ASP   A HB3  1 
ATOM   3730 H  HB3  B ASP   A 1 162 ? 0.925  -6.943  3.400   0.26 22.30 ?  162 ASP   A HB3  1 
ATOM   3731 N  N    A LYS   A 1 163 ? 3.341  -7.159  1.167   0.74 19.86 ?  163 LYS   A N    1 
ATOM   3732 N  N    B LYS   A 1 163 ? 3.297  -7.503  0.993   0.26 18.13 ?  163 LYS   A N    1 
ATOM   3733 C  CA   A LYS   A 1 163 ? 3.410  -7.935  -0.067  0.74 20.33 ?  163 LYS   A CA   1 
ATOM   3734 C  CA   B LYS   A 1 163 ? 3.514  -8.383  -0.149  0.26 18.54 ?  163 LYS   A CA   1 
ATOM   3735 C  C    A LYS   A 1 163 ? 4.479  -9.021  0.008   0.74 19.47 ?  163 LYS   A C    1 
ATOM   3736 C  C    B LYS   A 1 163 ? 4.663  -9.346  0.124   0.26 17.83 ?  163 LYS   A C    1 
ATOM   3737 O  O    A LYS   A 1 163 ? 4.299  -10.111 -0.544  0.74 19.56 ?  163 LYS   A O    1 
ATOM   3738 O  O    B LYS   A 1 163 ? 4.562  -10.546 -0.159  0.26 17.92 ?  163 LYS   A O    1 
ATOM   3739 C  CB   A LYS   A 1 163 ? 3.663  -7.013  -1.260  0.74 22.90 ?  163 LYS   A CB   1 
ATOM   3740 C  CB   B LYS   A 1 163 ? 3.798  -7.555  -1.401  0.26 20.14 ?  163 LYS   A CB   1 
ATOM   3741 C  CG   A LYS   A 1 163 ? 3.748  -7.747  -2.590  0.74 25.79 ?  163 LYS   A CG   1 
ATOM   3742 C  CG   B LYS   A 1 163 ? 2.566  -6.940  -2.059  0.26 21.85 ?  163 LYS   A CG   1 
ATOM   3743 C  CD   A LYS   A 1 163 ? 4.170  -6.816  -3.710  0.74 28.98 ?  163 LYS   A CD   1 
ATOM   3744 C  CD   B LYS   A 1 163 ? 2.942  -6.179  -3.327  0.26 23.36 ?  163 LYS   A CD   1 
ATOM   3745 C  CE   A LYS   A 1 163 ? 4.101  -7.509  -5.061  0.74 31.50 ?  163 LYS   A CE   1 
ATOM   3746 C  CE   B LYS   A 1 163 ? 3.729  -7.054  -4.299  0.26 24.60 ?  163 LYS   A CE   1 
ATOM   3747 N  NZ   A LYS   A 1 163 ? 4.759  -6.715  -6.136  0.74 32.64 ?  163 LYS   A NZ   1 
ATOM   3748 N  NZ   B LYS   A 1 163 ? 4.221  -6.298  -5.474  0.26 25.16 ?  163 LYS   A NZ   1 
ATOM   3749 H  H    A LYS   A 1 163 ? 3.605  -6.338  1.100   0.74 23.97 ?  163 LYS   A H    1 
ATOM   3750 H  H    B LYS   A 1 163 ? 3.411  -6.670  0.826   0.26 21.89 ?  163 LYS   A H    1 
ATOM   3751 H  HA   A LYS   A 1 163 ? 2.554  -8.366  -0.206  0.74 24.54 ?  163 LYS   A HA   1 
ATOM   3752 H  HA   B LYS   A 1 163 ? 2.718  -8.906  -0.316  0.26 22.38 ?  163 LYS   A HA   1 
ATOM   3753 H  HB2  A LYS   A 1 163 ? 2.935  -6.372  -1.323  0.74 27.62 ?  163 LYS   A HB2  1 
ATOM   3754 H  HB2  B LYS   A 1 163 ? 4.401  -6.825  -1.184  0.26 24.31 ?  163 LYS   A HB2  1 
ATOM   3755 H  HB3  A LYS   A 1 163 ? 4.500  -6.545  -1.124  0.74 27.62 ?  163 LYS   A HB3  1 
ATOM   3756 H  HB3  B LYS   A 1 163 ? 4.218  -8.147  -2.040  0.26 24.31 ?  163 LYS   A HB3  1 
ATOM   3757 H  HG2  A LYS   A 1 163 ? 4.406  -8.458  -2.529  0.74 31.09 ?  163 LYS   A HG2  1 
ATOM   3758 H  HG2  B LYS   A 1 163 ? 1.943  -7.643  -2.300  0.26 26.35 ?  163 LYS   A HG2  1 
ATOM   3759 H  HG3  A LYS   A 1 163 ? 2.877  -8.114  -2.809  0.74 31.09 ?  163 LYS   A HG3  1 
ATOM   3760 H  HG3  B LYS   A 1 163 ? 2.148  -6.316  -1.443  0.26 26.35 ?  163 LYS   A HG3  1 
ATOM   3761 H  HD2  A LYS   A 1 163 ? 3.576  -6.050  -3.730  0.74 34.92 ?  163 LYS   A HD2  1 
ATOM   3762 H  HD2  B LYS   A 1 163 ? 2.132  -5.882  -3.775  0.26 28.17 ?  163 LYS   A HD2  1 
ATOM   3763 H  HD3  A LYS   A 1 163 ? 5.084  -6.529  -3.560  0.74 34.92 ?  163 LYS   A HD3  1 
ATOM   3764 H  HD3  B LYS   A 1 163 ? 3.492  -5.416  -3.090  0.26 28.17 ?  163 LYS   A HD3  1 
ATOM   3765 H  HE2  A LYS   A 1 163 ? 4.538  -8.372  -5.001  0.74 37.94 ?  163 LYS   A HE2  1 
ATOM   3766 H  HE2  B LYS   A 1 163 ? 4.515  -7.412  -3.858  0.26 29.66 ?  163 LYS   A HE2  1 
ATOM   3767 H  HE3  A LYS   A 1 163 ? 3.171  -7.628  -5.306  0.74 37.94 ?  163 LYS   A HE3  1 
ATOM   3768 H  HE3  B LYS   A 1 163 ? 3.159  -7.780  -4.602  0.26 29.66 ?  163 LYS   A HE3  1 
ATOM   3769 H  HZ1  A LYS   A 1 163 ? 4.702  -7.147  -6.912  0.74 39.30 ?  163 LYS   A HZ1  1 
ATOM   3770 H  HZ1  B LYS   A 1 163 ? 4.677  -6.841  -6.011  0.26 30.33 ?  163 LYS   A HZ1  1 
ATOM   3771 H  HZ2  A LYS   A 1 163 ? 4.360  -5.924  -6.216  0.74 39.30 ?  163 LYS   A HZ2  1 
ATOM   3772 H  HZ2  B LYS   A 1 163 ? 3.537  -5.952  -5.919  0.26 30.33 ?  163 LYS   A HZ2  1 
ATOM   3773 H  HZ3  A LYS   A 1 163 ? 5.617  -6.587  -5.938  0.74 39.30 ?  163 LYS   A HZ3  1 
ATOM   3774 H  HZ3  B LYS   A 1 163 ? 4.759  -5.640  -5.206  0.26 30.33 ?  163 LYS   A HZ3  1 
ATOM   3775 N  N    A LEU   A 1 164 ? 5.611  -8.736  0.658   0.74 17.86 ?  164 LEU   A N    1 
ATOM   3776 N  N    B LEU   A 1 164 ? 5.763  -8.833  0.681   0.26 16.94 ?  164 LEU   A N    1 
ATOM   3777 C  CA   A LEU   A 1 164 ? 6.683  -9.728  0.746   0.74 16.59 ?  164 LEU   A CA   1 
ATOM   3778 C  CA   B LEU   A 1 164 ? 6.880  -9.687  1.070   0.26 15.92 ?  164 LEU   A CA   1 
ATOM   3779 C  C    A LEU   A 1 164 ? 6.261  -10.925 1.590   0.74 16.55 ?  164 LEU   A C    1 
ATOM   3780 C  C    B LEU   A 1 164 ? 6.407  -10.793 1.999   0.26 15.80 ?  164 LEU   A C    1 
ATOM   3781 O  O    A LEU   A 1 164 ? 6.571  -12.074 1.255   0.74 16.91 ?  164 LEU   A O    1 
ATOM   3782 O  O    B LEU   A 1 164 ? 6.709  -11.973 1.790   0.26 15.79 ?  164 LEU   A O    1 
ATOM   3783 C  CB   A LEU   A 1 164 ? 7.936  -9.085  1.334   0.74 15.94 ?  164 LEU   A CB   1 
ATOM   3784 C  CB   B LEU   A 1 164 ? 7.949  -8.851  1.774   0.26 15.21 ?  164 LEU   A CB   1 
ATOM   3785 C  CG   A LEU   A 1 164 ? 8.661  -8.086  0.431   0.74 15.51 ?  164 LEU   A CG   1 
ATOM   3786 C  CG   B LEU   A 1 164 ? 8.887  -7.957  0.966   0.26 14.95 ?  164 LEU   A CG   1 
ATOM   3787 C  CD1  A LEU   A 1 164 ? 9.578  -7.174  1.243   0.74 14.60 ?  164 LEU   A CD1  1 
ATOM   3788 C  CD1  B LEU   A 1 164 ? 9.721  -7.130  1.932   0.26 14.97 ?  164 LEU   A CD1  1 
ATOM   3789 C  CD2  A LEU   A 1 164 ? 9.458  -8.816  -0.635  0.74 15.93 ?  164 LEU   A CD2  1 
ATOM   3790 C  CD2  B LEU   A 1 164 ? 9.786  -8.761  0.037   0.26 14.49 ?  164 LEU   A CD2  1 
ATOM   3791 H  H    A LEU   A 1 164 ? 5.782  -7.985  1.052   0.74 21.57 ?  164 LEU   A H    1 
ATOM   3792 H  H    B LEU   A 1 164 ? 5.875  -8.002  0.857   0.26 20.47 ?  164 LEU   A H    1 
ATOM   3793 H  HA   A LEU   A 1 164 ? 6.892  -10.043 -0.145  0.74 20.05 ?  164 LEU   A HA   1 
ATOM   3794 H  HA   B LEU   A 1 164 ? 7.275  -10.095 0.283   0.26 19.25 ?  164 LEU   A HA   1 
ATOM   3795 H  HB2  A LEU   A 1 164 ? 7.691  -8.616  2.143   0.74 19.26 ?  164 LEU   A HB2  1 
ATOM   3796 H  HB2  B LEU   A 1 164 ? 7.497  -8.267  2.400   0.26 18.39 ?  164 LEU   A HB2  1 
ATOM   3797 H  HB3  A LEU   A 1 164 ? 8.568  -9.790  1.546   0.74 19.26 ?  164 LEU   A HB3  1 
ATOM   3798 H  HB3  B LEU   A 1 164 ? 8.517  -9.460  2.268   0.26 18.39 ?  164 LEU   A HB3  1 
ATOM   3799 H  HG   A LEU   A 1 164 ? 8.007  -7.528  -0.014  0.74 18.75 ?  164 LEU   A HG   1 
ATOM   3800 H  HG   B LEU   A 1 164 ? 8.363  -7.350  0.426   0.26 18.08 ?  164 LEU   A HG   1 
ATOM   3801 H  HD11 A LEU   A 1 164 ? 10.020 -6.554  0.644   0.74 17.67 ?  164 LEU   A HD11 1 
ATOM   3802 H  HD11 B LEU   A 1 164 ? 10.404 -6.661  1.436   0.26 18.11 ?  164 LEU   A HD11 1 
ATOM   3803 H  HD12 A LEU   A 1 164 ? 9.042  -6.685  1.890   0.74 17.67 ?  164 LEU   A HD12 1 
ATOM   3804 H  HD12 B LEU   A 1 164 ? 9.149  -6.490  2.381   0.26 18.11 ?  164 LEU   A HD12 1 
ATOM   3805 H  HD13 A LEU   A 1 164 ? 10.236 -7.717  1.705   0.74 17.67 ?  164 LEU   A HD13 1 
ATOM   3806 H  HD13 B LEU   A 1 164 ? 10.129 -7.722  2.584   0.26 18.11 ?  164 LEU   A HD13 1 
ATOM   3807 H  HD21 A LEU   A 1 164 ? 9.920  -8.163  -1.188  0.74 19.26 ?  164 LEU   A HD21 1 
ATOM   3808 H  HD21 B LEU   A 1 164 ? 10.353 -8.149  -0.462  0.26 17.53 ?  164 LEU   A HD21 1 
ATOM   3809 H  HD22 A LEU   A 1 164 ? 10.105 -9.399  -0.207  0.74 19.26 ?  164 LEU   A HD22 1 
ATOM   3810 H  HD22 B LEU   A 1 164 ? 10.336 -9.359  0.566   0.26 17.53 ?  164 LEU   A HD22 1 
ATOM   3811 H  HD23 A LEU   A 1 164 ? 8.851  -9.338  -1.182  0.74 19.26 ?  164 LEU   A HD23 1 
ATOM   3812 H  HD23 B LEU   A 1 164 ? 9.233  -9.270  -0.575  0.26 17.53 ?  164 LEU   A HD23 1 
ATOM   3813 N  N    A VAL   A 1 165 ? 5.563  -10.671 2.693   0.74 15.87 ?  165 VAL   A N    1 
ATOM   3814 N  N    B VAL   A 1 165 ? 5.669  -10.425 3.047   0.26 15.73 ?  165 VAL   A N    1 
ATOM   3815 C  CA   A VAL   A 1 165 ? 5.104  -11.749 3.563   0.74 15.53 ?  165 VAL   A CA   1 
ATOM   3816 C  CA   B VAL   A 1 165 ? 5.157  -11.434 3.967   0.26 16.02 ?  165 VAL   A CA   1 
ATOM   3817 C  C    A VAL   A 1 165 ? 4.082  -12.616 2.839   0.74 15.52 ?  165 VAL   A C    1 
ATOM   3818 C  C    B VAL   A 1 165 ? 4.046  -12.246 3.311   0.26 15.86 ?  165 VAL   A C    1 
ATOM   3819 O  O    A VAL   A 1 165 ? 4.190  -13.848 2.810   0.74 15.49 ?  165 VAL   A O    1 
ATOM   3820 O  O    B VAL   A 1 165 ? 4.067  -13.482 3.336   0.26 15.59 ?  165 VAL   A O    1 
ATOM   3821 C  CB   A VAL   A 1 165 ? 4.525  -11.150 4.858   0.74 16.05 ?  165 VAL   A CB   1 
ATOM   3822 C  CB   B VAL   A 1 165 ? 4.709  -10.797 5.294   0.26 16.49 ?  165 VAL   A CB   1 
ATOM   3823 C  CG1  A VAL   A 1 165 ? 3.783  -12.203 5.672   0.74 16.41 ?  165 VAL   A CG1  1 
ATOM   3824 C  CG1  B VAL   A 1 165 ? 3.953  -11.817 6.136   0.26 16.72 ?  165 VAL   A CG1  1 
ATOM   3825 C  CG2  A VAL   A 1 165 ? 5.629  -10.491 5.681   0.74 16.32 ?  165 VAL   A CG2  1 
ATOM   3826 C  CG2  B VAL   A 1 165 ? 5.917  -10.277 6.053   0.26 16.76 ?  165 VAL   A CG2  1 
ATOM   3827 H  H    A VAL   A 1 165 ? 5.333  -9.892  2.956   0.74 19.18 ?  165 VAL   A H    1 
ATOM   3828 H  H    B VAL   A 1 165 ? 5.465  -9.608  3.246   0.26 19.02 ?  165 VAL   A H    1 
ATOM   3829 H  HA   A VAL   A 1 165 ? 5.858  -12.314 3.804   0.74 18.77 ?  165 VAL   A HA   1 
ATOM   3830 H  HA   B VAL   A 1 165 ? 5.878  -12.042 4.173   0.26 19.37 ?  165 VAL   A HA   1 
ATOM   3831 H  HB   A VAL   A 1 165 ? 3.889  -10.461 4.621   0.74 19.40 ?  165 VAL   A HB   1 
ATOM   3832 H  HB   B VAL   A 1 165 ? 4.116  -10.049 5.115   0.26 19.93 ?  165 VAL   A HB   1 
ATOM   3833 H  HG11 A VAL   A 1 165 ? 3.662  -11.871 6.577   0.74 19.83 ?  165 VAL   A HG11 1 
ATOM   3834 H  HG11 B VAL   A 1 165 ? 3.915  -11.503 7.053   0.26 20.20 ?  165 VAL   A HG11 1 
ATOM   3835 H  HG12 A VAL   A 1 165 ? 2.916  -12.364 5.266   0.74 19.83 ?  165 VAL   A HG12 1 
ATOM   3836 H  HG12 B VAL   A 1 165 ? 3.054  -11.919 5.785   0.26 20.20 ?  165 VAL   A HG12 1 
ATOM   3837 H  HG13 A VAL   A 1 165 ? 4.303  -13.018 5.687   0.74 19.83 ?  165 VAL   A HG13 1 
ATOM   3838 H  HG13 B VAL   A 1 165 ? 4.423  -12.666 6.099   0.26 20.20 ?  165 VAL   A HG13 1 
ATOM   3839 H  HG21 A VAL   A 1 165 ? 5.245  -10.122 6.494   0.74 19.73 ?  165 VAL   A HG21 1 
ATOM   3840 H  HG21 B VAL   A 1 165 ? 5.622  -9.882  6.887   0.26 20.26 ?  165 VAL   A HG21 1 
ATOM   3841 H  HG22 A VAL   A 1 165 ? 6.301  -11.154 5.907   0.74 19.73 ?  165 VAL   A HG22 1 
ATOM   3842 H  HG22 B VAL   A 1 165 ? 6.518  -11.018 6.233   0.26 20.26 ?  165 VAL   A HG22 1 
ATOM   3843 H  HG23 A VAL   A 1 165 ? 6.034  -9.778  5.158   0.74 19.73 ?  165 VAL   A HG23 1 
ATOM   3844 H  HG23 B VAL   A 1 165 ? 6.368  -9.611  5.511   0.26 20.26 ?  165 VAL   A HG23 1 
ATOM   3845 N  N    A SER   A 1 166 ? 3.074  -11.980 2.243   0.74 16.36 ?  166 SER   A N    1 
ATOM   3846 N  N    B SER   A 1 166 ? 3.065  -11.568 2.705   0.26 15.98 ?  166 SER   A N    1 
ATOM   3847 C  CA   A SER   A 1 166 ? 1.956  -12.715 1.664   0.74 17.74 ?  166 SER   A CA   1 
ATOM   3848 C  CA   B SER   A 1 166 ? 1.906  -12.294 2.192   0.26 16.32 ?  166 SER   A CA   1 
ATOM   3849 C  C    A SER   A 1 166 ? 2.386  -13.547 0.469   0.74 18.57 ?  166 SER   A C    1 
ATOM   3850 C  C    B SER   A 1 166 ? 2.304  -13.330 1.151   0.26 17.28 ?  166 SER   A C    1 
ATOM   3851 O  O    A SER   A 1 166 ? 1.755  -14.571 0.175   0.74 20.07 ?  166 SER   A O    1 
ATOM   3852 O  O    B SER   A 1 166 ? 1.702  -14.407 1.091   0.26 17.77 ?  166 SER   A O    1 
ATOM   3853 C  CB   A SER   A 1 166 ? 0.852  -11.746 1.229   0.74 18.93 ?  166 SER   A CB   1 
ATOM   3854 C  CB   B SER   A 1 166 ? 0.845  -11.339 1.633   0.26 15.96 ?  166 SER   A CB   1 
ATOM   3855 O  OG   A SER   A 1 166 ? 0.268  -11.060 2.331   0.74 20.75 ?  166 SER   A OG   1 
ATOM   3856 O  OG   B SER   A 1 166 ? 1.184  -10.884 0.335   0.26 15.96 ?  166 SER   A OG   1 
ATOM   3857 H  H    A SER   A 1 166 ? 3.007  -11.142 2.171   0.74 19.78 ?  166 SER   A H    1 
ATOM   3858 H  H    B SER   A 1 166 ? 3.044  -10.714 2.583   0.26 19.32 ?  166 SER   A H    1 
ATOM   3859 H  HA   A SER   A 1 166 ? 1.577  -13.324 2.325   0.74 21.43 ?  166 SER   A HA   1 
ATOM   3860 H  HA   B SER   A 1 166 ? 1.497  -12.768 2.927   0.26 19.73 ?  166 SER   A HA   1 
ATOM   3861 H  HB2  A SER   A 1 166 ? 1.233  -11.098 0.619   0.74 22.86 ?  166 SER   A HB2  1 
ATOM   3862 H  HB2  B SER   A 1 166 ? -0.007 -11.811 1.583   0.26 19.30 ?  166 SER   A HB2  1 
ATOM   3863 H  HB3  A SER   A 1 166 ? 0.152  -12.248 0.775   0.74 22.86 ?  166 SER   A HB3  1 
ATOM   3864 H  HB3  B SER   A 1 166 ? 0.752  -10.575 2.226   0.26 19.30 ?  166 SER   A HB3  1 
ATOM   3865 H  HG   A SER   A 1 166 ? 0.868  -10.618 2.731   0.74 25.05 ?  166 SER   A HG   1 
ATOM   3866 H  HG   B SER   A 1 166 ? 0.589  -10.362 0.049   0.26 19.29 ?  166 SER   A HG   1 
ATOM   3867 N  N    A SER   A 1 167 ? 3.431  -13.122 -0.238  0.74 17.79 ?  167 SER   A N    1 
ATOM   3868 N  N    B SER   A 1 167 ? 3.317  -13.045 0.342   0.26 18.21 ?  167 SER   A N    1 
ATOM   3869 C  CA   A SER   A 1 167 ? 3.929  -13.845 -1.395  0.74 18.65 ?  167 SER   A CA   1 
ATOM   3870 C  CA   B SER   A 1 167 ? 3.766  -13.969 -0.696  0.26 18.78 ?  167 SER   A CA   1 
ATOM   3871 C  C    A SER   A 1 167 ? 5.074  -14.780 -1.050  0.74 18.85 ?  167 SER   A C    1 
ATOM   3872 C  C    B SER   A 1 167 ? 5.162  -14.460 -0.322  0.26 18.48 ?  167 SER   A C    1 
ATOM   3873 O  O    A SER   A 1 167 ? 5.563  -15.486 -1.936  0.74 19.17 ?  167 SER   A O    1 
ATOM   3874 O  O    B SER   A 1 167 ? 6.159  -13.784 -0.590  0.26 19.55 ?  167 SER   A O    1 
ATOM   3875 C  CB   A SER   A 1 167 ? 4.377  -12.860 -2.484  0.74 19.18 ?  167 SER   A CB   1 
ATOM   3876 C  CB   B SER   A 1 167 ? 3.745  -13.299 -2.067  0.26 19.78 ?  167 SER   A CB   1 
ATOM   3877 O  OG   A SER   A 1 167 ? 5.423  -12.021 -2.015  0.74 19.23 ?  167 SER   A OG   1 
ATOM   3878 O  OG   B SER   A 1 167 ? 4.544  -12.131 -2.080  0.26 20.45 ?  167 SER   A OG   1 
ATOM   3879 H  H    A SER   A 1 167 ? 3.858  -12.398 -0.070  0.74 21.49 ?  167 SER   A H    1 
ATOM   3880 H  H    B SER   A 1 167 ? 3.771  -12.312 0.380   0.26 21.99 ?  167 SER   A H    1 
ATOM   3881 H  HA   A SER   A 1 167 ? 3.211  -14.380 -1.765  0.74 22.52 ?  167 SER   A HA   1 
ATOM   3882 H  HA   B SER   A 1 167 ? 3.173  -14.733 -0.725  0.26 22.68 ?  167 SER   A HA   1 
ATOM   3883 H  HB2  A SER   A 1 167 ? 4.696  -13.361 -3.252  0.74 23.16 ?  167 SER   A HB2  1 
ATOM   3884 H  HB2  B SER   A 1 167 ? 4.087  -13.924 -2.724  0.26 23.88 ?  167 SER   A HB2  1 
ATOM   3885 H  HB3  A SER   A 1 167 ? 3.616  -12.312 -2.746  0.74 23.16 ?  167 SER   A HB3  1 
ATOM   3886 H  HB3  B SER   A 1 167 ? 2.827  -13.063 -2.286  0.26 23.88 ?  167 SER   A HB3  1 
ATOM   3887 H  HG   A SER   A 1 167 ? 5.147  -11.564 -1.362  0.74 23.21 ?  167 SER   A HG   1 
ATOM   3888 H  HG   B SER   A 1 167 ? 4.224  -11.559 -1.554  0.26 24.68 ?  167 SER   A HG   1 
ATOM   3889 N  N    A PHE   A 1 168 ? 5.517  -14.808 0.205   0.74 18.76 ?  168 PHE   A N    1 
ATOM   3890 N  N    B PHE   A 1 168 ? 5.228  -15.638 0.301   0.26 16.86 ?  168 PHE   A N    1 
ATOM   3891 C  CA   A PHE   A 1 168 ? 6.688  -15.605 0.536   0.74 19.25 ?  168 PHE   A CA   1 
ATOM   3892 C  CA   B PHE   A 1 168 ? 6.511  -16.214 0.686   0.26 15.75 ?  168 PHE   A CA   1 
ATOM   3893 C  C    A PHE   A 1 168 ? 6.369  -17.085 0.414   0.74 21.10 ?  168 PHE   A C    1 
ATOM   3894 C  C    B PHE   A 1 168 ? 6.518  -17.737 0.657   0.26 15.19 ?  168 PHE   A C    1 
ATOM   3895 O  O    A PHE   A 1 168 ? 5.371  -17.567 0.961   0.74 22.51 ?  168 PHE   A O    1 
ATOM   3896 O  O    B PHE   A 1 168 ? 7.438  -18.335 0.090   0.26 14.09 ?  168 PHE   A O    1 
ATOM   3897 C  CB   A PHE   A 1 168 ? 7.199  -15.318 1.945   0.74 18.40 ?  168 PHE   A CB   1 
ATOM   3898 C  CB   B PHE   A 1 168 ? 6.944  -15.721 2.069   0.26 16.09 ?  168 PHE   A CB   1 
ATOM   3899 C  CG   A PHE   A 1 168 ? 8.466  -16.064 2.265   0.74 17.22 ?  168 PHE   A CG   1 
ATOM   3900 C  CG   B PHE   A 1 168 ? 8.246  -16.312 2.539   0.26 16.34 ?  168 PHE   A CG   1 
ATOM   3901 C  CD1  A PHE   A 1 168 ? 9.649  -15.709 1.647   0.74 17.14 ?  168 PHE   A CD1  1 
ATOM   3902 C  CD1  B PHE   A 1 168 ? 9.448  -15.886 2.002   0.26 16.62 ?  168 PHE   A CD1  1 
ATOM   3903 C  CD2  A PHE   A 1 168 ? 8.475  -17.144 3.137   0.74 16.64 ?  168 PHE   A CD2  1 
ATOM   3904 C  CD2  B PHE   A 1 168 ? 8.267  -17.295 3.516   0.26 16.68 ?  168 PHE   A CD2  1 
ATOM   3905 C  CE1  A PHE   A 1 168 ? 10.818 -16.392 1.907   0.74 16.38 ?  168 PHE   A CE1  1 
ATOM   3906 C  CE1  B PHE   A 1 168 ? 10.645 -16.426 2.430   0.26 16.85 ?  168 PHE   A CE1  1 
ATOM   3907 C  CE2  A PHE   A 1 168 ? 9.654  -17.829 3.403   0.74 16.62 ?  168 PHE   A CE2  1 
ATOM   3908 C  CE2  B PHE   A 1 168 ? 9.461  -17.836 3.949   0.26 16.94 ?  168 PHE   A CE2  1 
ATOM   3909 C  CZ   A PHE   A 1 168 ? 10.822 -17.449 2.784   0.74 16.14 ?  168 PHE   A CZ   1 
ATOM   3910 C  CZ   B PHE   A 1 168 ? 10.651 -17.402 3.404   0.26 16.99 ?  168 PHE   A CZ   1 
ATOM   3911 H  H    A PHE   A 1 168 ? 5.168  -14.381 0.863   0.74 22.65 ?  168 PHE   A H    1 
ATOM   3912 H  H    B PHE   A 1 168 ? 4.547  -16.120 0.505   0.26 20.37 ?  168 PHE   A H    1 
ATOM   3913 H  HA   A PHE   A 1 168 ? 7.400  -15.396 -0.090  0.74 23.24 ?  168 PHE   A HA   1 
ATOM   3914 H  HA   B PHE   A 1 168 ? 7.181  -15.921 0.052   0.26 19.04 ?  168 PHE   A HA   1 
ATOM   3915 H  HB2  A PHE   A 1 168 ? 7.379  -14.370 2.029   0.74 22.22 ?  168 PHE   A HB2  1 
ATOM   3916 H  HB2  B PHE   A 1 168 ? 7.053  -14.759 2.035   0.26 19.45 ?  168 PHE   A HB2  1 
ATOM   3917 H  HB3  A PHE   A 1 168 ? 6.521  -15.586 2.586   0.74 22.22 ?  168 PHE   A HB3  1 
ATOM   3918 H  HB3  B PHE   A 1 168 ? 6.263  -15.957 2.715   0.26 19.45 ?  168 PHE   A HB3  1 
ATOM   3919 H  HD1  A PHE   A 1 168 ? 9.662  -14.996 1.053   0.74 20.71 ?  168 PHE   A HD1  1 
ATOM   3920 H  HD1  B PHE   A 1 168 ? 9.453  -15.229 1.345   0.26 20.09 ?  168 PHE   A HD1  1 
ATOM   3921 H  HD2  A PHE   A 1 168 ? 7.687  -17.404 3.558   0.74 20.11 ?  168 PHE   A HD2  1 
ATOM   3922 H  HD2  B PHE   A 1 168 ? 7.468  -17.591 3.887   0.26 20.15 ?  168 PHE   A HD2  1 
ATOM   3923 H  HE1  A PHE   A 1 168 ? 11.613 -16.138 1.492   0.74 19.79 ?  168 PHE   A HE1  1 
ATOM   3924 H  HE1  B PHE   A 1 168 ? 11.448 -16.132 2.063   0.26 20.36 ?  168 PHE   A HE1  1 
ATOM   3925 H  HE2  A PHE   A 1 168 ? 9.650  -18.548 3.996   0.74 20.08 ?  168 PHE   A HE2  1 
ATOM   3926 H  HE2  B PHE   A 1 168 ? 9.463  -18.495 4.606   0.26 20.47 ?  168 PHE   A HE2  1 
ATOM   3927 H  HZ   A PHE   A 1 168 ? 11.612 -17.910 2.961   0.74 19.50 ?  168 PHE   A HZ   1 
ATOM   3928 H  HZ   B PHE   A 1 168 ? 11.456 -17.764 3.693   0.26 20.53 ?  168 PHE   A HZ   1 
ATOM   3929 N  N    A LEU   A 1 169 ? 7.239  -17.809 -0.282  0.74 23.09 ?  169 LEU   A N    1 
ATOM   3930 N  N    B LEU   A 1 169 ? 5.527  -18.378 1.269   0.26 15.92 ?  169 LEU   A N    1 
ATOM   3931 C  CA   A LEU   A 1 169 ? 7.060  -19.240 -0.448  0.74 25.88 ?  169 LEU   A CA   1 
ATOM   3932 C  CA   B LEU   A 1 169 ? 5.545  -19.832 1.400   0.26 16.92 ?  169 LEU   A CA   1 
ATOM   3933 C  C    A LEU   A 1 169 ? 7.911  -19.978 0.573   0.74 26.30 ?  169 LEU   A C    1 
ATOM   3934 C  C    B LEU   A 1 169 ? 4.985  -20.514 0.154   0.26 17.84 ?  169 LEU   A C    1 
ATOM   3935 O  O    A LEU   A 1 169 ? 7.383  -20.444 1.586   0.74 26.68 ?  169 LEU   A O    1 
ATOM   3936 O  O    B LEU   A 1 169 ? 4.083  -19.998 -0.506  0.26 18.15 ?  169 LEU   A O    1 
ATOM   3937 C  CB   A LEU   A 1 169 ? 7.408  -19.668 -1.878  0.74 27.31 ?  169 LEU   A CB   1 
ATOM   3938 C  CB   B LEU   A 1 169 ? 4.764  -20.280 2.639   0.26 16.99 ?  169 LEU   A CB   1 
ATOM   3939 C  CG   A LEU   A 1 169 ? 7.079  -21.119 -2.250  0.74 28.58 ?  169 LEU   A CG   1 
ATOM   3940 C  CG   B LEU   A 1 169 ? 4.982  -21.744 3.031   0.26 17.11 ?  169 LEU   A CG   1 
ATOM   3941 C  CD1  A LEU   A 1 169 ? 5.649  -21.467 -1.869  0.74 29.15 ?  169 LEU   A CD1  1 
ATOM   3942 C  CD1  B LEU   A 1 169 ? 6.437  -21.978 3.412   0.26 17.58 ?  169 LEU   A CD1  1 
ATOM   3943 C  CD2  A LEU   A 1 169 ? 7.304  -21.358 -3.737  0.74 28.77 ?  169 LEU   A CD2  1 
ATOM   3944 C  CD2  B LEU   A 1 169 ? 4.056  -22.155 4.165   0.26 17.20 ?  169 LEU   A CD2  1 
ATOM   3945 O  OXT  A LEU   A 1 169 ? 9.127  -20.108 0.426   0.74 25.57 -1 169 LEU   A OXT  1 
ATOM   3946 O  OXT  B LEU   A 1 169 ? 5.426  -21.604 -0.216  0.26 18.58 -1 169 LEU   A OXT  1 
ATOM   3947 H  H    A LEU   A 1 169 ? 7.947  -17.496 -0.662  0.74 27.85 ?  169 LEU   A H    1 
ATOM   3948 H  H    B LEU   A 1 169 ? 4.836  -17.999 1.610   0.26 19.25 ?  169 LEU   A H    1 
ATOM   3949 H  HA   A LEU   A 1 169 ? 6.139  -19.465 -0.274  0.74 31.20 ?  169 LEU   A HA   1 
ATOM   3950 H  HA   B LEU   A 1 169 ? 6.464  -20.117 1.510   0.26 20.45 ?  169 LEU   A HA   1 
ATOM   3951 H  HB2  A LEU   A 1 169 ? 6.918  -19.099 -2.492  0.74 32.91 ?  169 LEU   A HB2  1 
ATOM   3952 H  HB2  B LEU   A 1 169 ? 5.037  -19.733 3.393   0.26 20.53 ?  169 LEU   A HB2  1 
ATOM   3953 H  HB3  A LEU   A 1 169 ? 8.359  -19.547 -2.015  0.74 32.91 ?  169 LEU   A HB3  1 
ATOM   3954 H  HB3  B LEU   A 1 169 ? 3.817  -20.160 2.473   0.26 20.53 ?  169 LEU   A HB3  1 
ATOM   3955 H  HG   A LEU   A 1 169 ? 7.671  -21.713 -1.762  0.74 34.44 ?  169 LEU   A HG   1 
ATOM   3956 H  HG   B LEU   A 1 169 ? 4.783  -22.308 2.268   0.26 20.67 ?  169 LEU   A HG   1 
ATOM   3957 H  HD11 A LEU   A 1 169 ? 5.398  -22.297 -2.303  0.74 35.12 ?  169 LEU   A HD11 1 
ATOM   3958 H  HD11 B LEU   A 1 169 ? 6.510  -22.828 3.872   0.26 21.24 ?  169 LEU   A HD11 1 
ATOM   3959 H  HD12 A LEU   A 1 169 ? 5.593  -21.568 -0.906  0.74 35.12 ?  169 LEU   A HD12 1 
ATOM   3960 H  HD12 B LEU   A 1 169 ? 6.979  -21.991 2.607   0.26 21.24 ?  169 LEU   A HD12 1 
ATOM   3961 H  HD13 A LEU   A 1 169 ? 5.062  -20.751 -2.163  0.74 35.12 ?  169 LEU   A HD13 1 
ATOM   3962 H  HD13 B LEU   A 1 169 ? 6.730  -21.260 3.997   0.26 21.24 ?  169 LEU   A HD13 1 
ATOM   3963 H  HD21 A LEU   A 1 169 ? 7.097  -22.284 -3.944  0.74 34.67 ?  169 LEU   A HD21 1 
ATOM   3964 H  HD21 B LEU   A 1 169 ? 4.216  -23.087 4.381   0.26 20.78 ?  169 LEU   A HD21 1 
ATOM   3965 H  HD22 A LEU   A 1 169 ? 6.721  -20.770 -4.243  0.74 34.67 ?  169 LEU   A HD22 1 
ATOM   3966 H  HD22 B LEU   A 1 169 ? 4.240  -21.600 4.939   0.26 20.78 ?  169 LEU   A HD22 1 
ATOM   3967 H  HD23 A LEU   A 1 169 ? 8.231  -21.171 -3.951  0.74 34.67 ?  169 LEU   A HD23 1 
ATOM   3968 H  HD23 B LEU   A 1 169 ? 3.138  -22.034 3.880   0.26 20.78 ?  169 LEU   A HD23 1 
ATOM   3969 N  N    A SER   B 1 1   ? 50.805 -9.259  -23.765 0.74 28.16 ?  1   SER   B N    1 
ATOM   3970 N  N    B SER   B 1 1   ? 50.759 -9.271  -23.757 0.26 25.84 ?  1   SER   B N    1 
ATOM   3971 C  CA   A SER   B 1 1   ? 51.303 -10.295 -22.839 0.74 28.26 ?  1   SER   B CA   1 
ATOM   3972 C  CA   B SER   B 1 1   ? 51.259 -10.264 -22.782 0.26 25.82 ?  1   SER   B CA   1 
ATOM   3973 C  C    A SER   B 1 1   ? 50.232 -11.341 -22.568 0.74 26.98 ?  1   SER   B C    1 
ATOM   3974 C  C    B SER   B 1 1   ? 50.202 -11.327 -22.522 0.26 25.35 ?  1   SER   B C    1 
ATOM   3975 O  O    A SER   B 1 1   ? 49.033 -11.126 -22.801 0.74 26.77 ?  1   SER   B O    1 
ATOM   3976 O  O    B SER   B 1 1   ? 49.026 -11.154 -22.854 0.26 25.17 ?  1   SER   B O    1 
ATOM   3977 C  CB   A SER   B 1 1   ? 51.753 -9.677  -21.520 0.74 29.15 ?  1   SER   B CB   1 
ATOM   3978 C  CB   B SER   B 1 1   ? 51.643 -9.586  -21.472 0.26 26.00 ?  1   SER   B CB   1 
ATOM   3979 O  OG   A SER   B 1 1   ? 50.638 -9.344  -20.715 0.74 30.89 ?  1   SER   B OG   1 
ATOM   3980 O  OG   B SER   B 1 1   ? 50.546 -9.569  -20.578 0.26 26.60 ?  1   SER   B OG   1 
ATOM   3981 H  H1   A SER   B 1 1   ? 50.734 -9.607  -24.579 0.74 33.93 ?  1   SER   B H1   1 
ATOM   3982 H  H1   B SER   B 1 1   ? 51.453 -8.873  -24.143 0.26 31.15 ?  1   SER   B H1   1 
ATOM   3983 H  H2   A SER   B 1 1   ? 50.013 -8.978  -23.485 0.74 33.93 ?  1   SER   B H2   1 
ATOM   3984 H  H2   B SER   B 1 1   ? 50.272 -9.688  -24.371 0.26 31.15 ?  1   SER   B H2   1 
ATOM   3985 H  H3   A SER   B 1 1   ? 51.381 -8.584  -23.776 0.74 33.93 ?  1   SER   B H3   1 
ATOM   3986 H  H3   B SER   B 1 1   ? 50.264 -8.672  -23.331 0.26 31.15 ?  1   SER   B H3   1 
ATOM   3987 H  HA   A SER   B 1 1   ? 52.064 -10.727 -23.252 0.74 34.05 ?  1   SER   B HA   1 
ATOM   3988 H  HA   B SER   B 1 1   ? 52.044 -10.687 -23.155 0.26 31.13 ?  1   SER   B HA   1 
ATOM   3989 H  HB2  A SER   B 1 1   ? 52.305 -10.321 -21.050 0.74 35.12 ?  1   SER   B HB2  1 
ATOM   3990 H  HB2  B SER   B 1 1   ? 52.378 -10.077 -21.076 0.26 31.34 ?  1   SER   B HB2  1 
ATOM   3991 H  HB3  A SER   B 1 1   ? 52.261 -8.873  -21.703 0.74 35.12 ?  1   SER   B HB3  1 
ATOM   3992 H  HB3  B SER   B 1 1   ? 51.914 -8.672  -21.655 0.26 31.34 ?  1   SER   B HB3  1 
ATOM   3993 H  HG   A SER   B 1 1   ? 50.891 -8.879  -20.062 0.74 37.21 ?  1   SER   B HG   1 
ATOM   3994 H  HG   B SER   B 1 1   ? 50.665 -8.976  -19.997 0.26 32.06 ?  1   SER   B HG   1 
ATOM   3995 N  N    A MET   B 1 2   ? 50.686 -12.474 -22.053 0.74 25.86 ?  2   MET   B N    1 
ATOM   3996 N  N    B MET   B 1 2   ? 50.633 -12.424 -21.911 0.26 24.93 ?  2   MET   B N    1 
ATOM   3997 C  CA   A MET   B 1 2   ? 49.866 -13.664 -21.883 0.74 25.79 ?  2   MET   B CA   1 
ATOM   3998 C  CA   B MET   B 1 2   ? 49.811 -13.615 -21.738 0.26 24.60 ?  2   MET   B CA   1 
ATOM   3999 C  C    A MET   B 1 2   ? 49.619 -13.862 -20.395 0.74 23.38 ?  2   MET   B C    1 
ATOM   4000 C  C    B MET   B 1 2   ? 49.542 -13.813 -20.254 0.26 23.05 ?  2   MET   B C    1 
ATOM   4001 O  O    A MET   B 1 2   ? 50.555 -14.129 -19.636 0.74 23.66 ?  2   MET   B O    1 
ATOM   4002 O  O    B MET   B 1 2   ? 50.439 -14.205 -19.500 0.26 23.40 ?  2   MET   B O    1 
ATOM   4003 C  CB   A MET   B 1 2   ? 50.597 -14.861 -22.478 0.74 29.65 ?  2   MET   B CB   1 
ATOM   4004 C  CB   B MET   B 1 2   ? 50.550 -14.812 -22.316 0.26 26.11 ?  2   MET   B CB   1 
ATOM   4005 C  CG   A MET   B 1 2   ? 49.756 -16.116 -22.626 0.74 33.20 ?  2   MET   B CG   1 
ATOM   4006 C  CG   B MET   B 1 2   ? 49.663 -15.968 -22.753 0.26 27.35 ?  2   MET   B CG   1 
ATOM   4007 S  SD   A MET   B 1 2   ? 50.600 -17.345 -23.640 0.74 36.53 ?  2   MET   B SD   1 
ATOM   4008 S  SD   B MET   B 1 2   ? 50.549 -17.064 -23.868 0.26 28.43 ?  2   MET   B SD   1 
ATOM   4009 C  CE   A MET   B 1 2   ? 51.119 -16.308 -25.001 0.74 36.84 ?  2   MET   B CE   1 
ATOM   4010 C  CE   B MET   B 1 2   ? 51.439 -15.863 -24.843 0.26 28.73 ?  2   MET   B CE   1 
ATOM   4011 H  H    A MET   B 1 2   ? 51.496 -12.584 -21.783 0.74 31.17 ?  2   MET   B H    1 
ATOM   4012 H  H    B MET   B 1 2   ? 51.426 -12.510 -21.588 0.26 30.06 ?  2   MET   B H    1 
ATOM   4013 H  HA   A MET   B 1 2   ? 49.023 -13.561 -22.347 0.74 31.08 ?  2   MET   B HA   1 
ATOM   4014 H  HA   B MET   B 1 2   ? 48.979 -13.515 -22.227 0.26 29.66 ?  2   MET   B HA   1 
ATOM   4015 H  HB2  A MET   B 1 2   ? 50.911 -14.584 -23.348 0.74 35.72 ?  2   MET   B HB2  1 
ATOM   4016 H  HB2  B MET   B 1 2   ? 51.053 -14.463 -23.062 0.26 31.47 ?  2   MET   B HB2  1 
ATOM   4017 H  HB3  A MET   B 1 2   ? 51.351 -15.092 -21.919 0.74 35.72 ?  2   MET   B HB3  1 
ATOM   4018 H  HB3  B MET   B 1 2   ? 51.161 -15.172 -21.663 0.26 31.47 ?  2   MET   B HB3  1 
ATOM   4019 H  HG2  A MET   B 1 2   ? 49.595 -16.499 -21.745 0.74 39.98 ?  2   MET   B HG2  1 
ATOM   4020 H  HG2  B MET   B 1 2   ? 49.392 -16.480 -21.970 0.26 32.96 ?  2   MET   B HG2  1 
ATOM   4021 H  HG3  A MET   B 1 2   ? 48.915 -15.898 -23.056 0.74 39.98 ?  2   MET   B HG3  1 
ATOM   4022 H  HG3  B MET   B 1 2   ? 48.883 -15.635 -23.219 0.26 32.96 ?  2   MET   B HG3  1 
ATOM   4023 H  HE1  A MET   B 1 2   ? 51.270 -16.863 -25.768 0.74 44.35 ?  2   MET   B HE1  1 
ATOM   4024 H  HE1  B MET   B 1 2   ? 51.672 -16.281 -25.662 0.26 34.61 ?  2   MET   B HE1  1 
ATOM   4025 H  HE2  A MET   B 1 2   ? 50.414 -15.663 -25.184 0.74 44.35 ?  2   MET   B HE2  1 
ATOM   4026 H  HE2  B MET   B 1 2   ? 50.862 -15.095 -25.014 0.26 34.61 ?  2   MET   B HE2  1 
ATOM   4027 H  HE3  A MET   B 1 2   ? 51.937 -15.839 -24.757 0.74 44.35 ?  2   MET   B HE3  1 
ATOM   4028 H  HE3  B MET   B 1 2   ? 52.242 -15.580 -24.363 0.26 34.61 ?  2   MET   B HE3  1 
ATOM   4029 N  N    A VAL   B 1 3   ? 48.365 -13.709 -19.980 0.74 20.81 ?  3   VAL   B N    1 
ATOM   4030 N  N    B VAL   B 1 3   ? 48.311 -13.538 -19.838 0.26 21.15 ?  3   VAL   B N    1 
ATOM   4031 C  CA   A VAL   B 1 3   ? 47.950 -13.950 -18.605 0.74 19.78 ?  3   VAL   B CA   1 
ATOM   4032 C  CA   B VAL   B 1 3   ? 47.869 -13.803 -18.476 0.26 19.57 ?  3   VAL   B CA   1 
ATOM   4033 C  C    A VAL   B 1 3   ? 46.713 -14.838 -18.624 0.74 18.09 ?  3   VAL   B C    1 
ATOM   4034 C  C    B VAL   B 1 3   ? 46.617 -14.664 -18.518 0.26 17.77 ?  3   VAL   B C    1 
ATOM   4035 O  O    A VAL   B 1 3   ? 45.999 -14.931 -19.625 0.74 18.44 ?  3   VAL   B O    1 
ATOM   4036 O  O    B VAL   B 1 3   ? 45.795 -14.560 -19.433 0.26 17.66 ?  3   VAL   B O    1 
ATOM   4037 C  CB   A VAL   B 1 3   ? 47.669 -12.637 -17.840 0.74 21.40 ?  3   VAL   B CB   1 
ATOM   4038 C  CB   B VAL   B 1 3   ? 47.602 -12.512 -17.672 0.26 20.03 ?  3   VAL   B CB   1 
ATOM   4039 C  CG1  A VAL   B 1 3   ? 48.937 -11.786 -17.746 0.74 22.10 ?  3   VAL   B CG1  1 
ATOM   4040 C  CG1  B VAL   B 1 3   ? 48.871 -11.684 -17.552 0.26 20.29 ?  3   VAL   B CG1  1 
ATOM   4041 C  CG2  A VAL   B 1 3   ? 46.544 -11.863 -18.510 0.74 22.05 ?  3   VAL   B CG2  1 
ATOM   4042 C  CG2  B VAL   B 1 3   ? 46.480 -11.711 -18.312 0.26 20.19 ?  3   VAL   B CG2  1 
ATOM   4043 H  H    A VAL   B 1 3   ? 47.720 -13.467 -20.492 0.74 25.11 ?  3   VAL   B H    1 
ATOM   4044 H  H    B VAL   B 1 3   ? 47.711 -13.186 -20.343 0.26 25.52 ?  3   VAL   B H    1 
ATOM   4045 H  HA   A VAL   B 1 3   ? 48.655 -14.426 -18.135 0.74 23.87 ?  3   VAL   B HA   1 
ATOM   4046 H  HA   B VAL   B 1 3   ? 48.564 -14.301 -18.020 0.26 23.62 ?  3   VAL   B HA   1 
ATOM   4047 H  HB   A VAL   B 1 3   ? 47.388 -12.855 -16.937 0.74 25.83 ?  3   VAL   B HB   1 
ATOM   4048 H  HB   B VAL   B 1 3   ? 47.320 -12.763 -16.779 0.26 24.18 ?  3   VAL   B HB   1 
ATOM   4049 H  HG11 A VAL   B 1 3   ? 48.734 -10.978 -17.251 0.74 26.66 ?  3   VAL   B HG11 1 
ATOM   4050 H  HG11 B VAL   B 1 3   ? 48.677 -10.892 -17.028 0.26 24.49 ?  3   VAL   B HG11 1 
ATOM   4051 H  HG12 A VAL   B 1 3   ? 49.622 -12.295 -17.285 0.74 26.66 ?  3   VAL   B HG12 1 
ATOM   4052 H  HG12 B VAL   B 1 3   ? 49.553 -12.215 -17.112 0.26 24.49 ?  3   VAL   B HG12 1 
ATOM   4053 H  HG13 A VAL   B 1 3   ? 49.232 -11.564 -18.641 0.74 26.66 ?  3   VAL   B HG13 1 
ATOM   4054 H  HG13 B VAL   B 1 3   ? 49.168 -11.431 -18.440 0.26 24.49 ?  3   VAL   B HG13 1 
ATOM   4055 H  HG21 A VAL   B 1 3   ? 46.481 -10.987 -18.104 0.74 26.61 ?  3   VAL   B HG21 1 
ATOM   4056 H  HG21 B VAL   B 1 3   ? 46.427 -10.848 -17.877 0.26 24.36 ?  3   VAL   B HG21 1 
ATOM   4057 H  HG22 A VAL   B 1 3   ? 46.739 -11.778 -19.456 0.74 26.61 ?  3   VAL   B HG22 1 
ATOM   4058 H  HG22 B VAL   B 1 3   ? 46.671 -11.598 -19.256 0.26 24.36 ?  3   VAL   B HG22 1 
ATOM   4059 H  HG23 A VAL   B 1 3   ? 45.711 -12.347 -18.387 0.74 26.61 ?  3   VAL   B HG23 1 
ATOM   4060 H  HG23 B VAL   B 1 3   ? 45.643 -12.191 -18.200 0.26 24.36 ?  3   VAL   B HG23 1 
ATOM   4061 N  N    . ASN   B 1 4   ? 46.467 -15.504 -17.497 1.00 16.33 ?  4   ASN   B N    1 
ATOM   4062 C  CA   . ASN   B 1 4   ? 45.328 -16.413 -17.383 1.00 15.39 ?  4   ASN   B CA   1 
ATOM   4063 C  C    . ASN   B 1 4   ? 45.270 -17.381 -18.565 1.00 15.94 ?  4   ASN   B C    1 
ATOM   4064 O  O    . ASN   B 1 4   ? 44.209 -17.636 -19.129 1.00 16.67 ?  4   ASN   B O    1 
ATOM   4065 C  CB   . ASN   B 1 4   ? 44.010 -15.647 -17.221 1.00 14.88 ?  4   ASN   B CB   1 
ATOM   4066 C  CG   . ASN   B 1 4   ? 43.968 -14.835 -15.938 1.00 14.33 ?  4   ASN   B CG   1 
ATOM   4067 O  OD1  . ASN   B 1 4   ? 44.255 -15.348 -14.857 1.00 14.20 ?  4   ASN   B OD1  1 
ATOM   4068 N  ND2  . ASN   B 1 4   ? 43.620 -13.557 -16.054 1.00 15.28 ?  4   ASN   B ND2  1 
ATOM   4069 H  H    A ASN   B 1 4   ? 46.948 -15.450 -16.788 0.74 19.73 ?  4   ASN   B H    1 
ATOM   4070 H  H    B ASN   B 1 4   ? 47.016 -15.554 -16.838 0.26 19.73 ?  4   ASN   B H    1 
ATOM   4071 H  HA   . ASN   B 1 4   ? 45.450 -16.946 -16.583 1.00 18.60 ?  4   ASN   B HA   1 
ATOM   4072 H  HB2  . ASN   B 1 4   ? 43.901 -15.037 -17.967 1.00 18.00 ?  4   ASN   B HB2  1 
ATOM   4073 H  HB3  . ASN   B 1 4   ? 43.276 -16.281 -17.199 1.00 18.00 ?  4   ASN   B HB3  1 
ATOM   4074 H  HD21 . ASN   B 1 4   ? 43.588 -13.052 -15.356 1.00 18.47 ?  4   ASN   B HD21 1 
ATOM   4075 H  HD22 . ASN   B 1 4   ? 43.433 -13.226 -16.827 1.00 18.47 ?  4   ASN   B HD22 1 
ATOM   4076 N  N    . SER   B 1 5   ? 46.426 -17.921 -18.947 1.00 17.33 ?  5   SER   B N    1 
ATOM   4077 C  CA   . SER   B 1 5   ? 46.515 -18.840 -20.081 1.00 19.66 ?  5   SER   B CA   1 
ATOM   4078 C  C    . SER   B 1 5   ? 46.498 -20.272 -19.558 1.00 21.17 ?  5   SER   B C    1 
ATOM   4079 O  O    . SER   B 1 5   ? 47.511 -20.963 -19.511 1.00 23.16 ?  5   SER   B O    1 
ATOM   4080 C  CB   . SER   B 1 5   ? 47.772 -18.555 -20.902 1.00 21.25 ?  5   SER   B CB   1 
ATOM   4081 O  OG   . SER   B 1 5   ? 48.943 -18.702 -20.116 1.00 23.70 ?  5   SER   B OG   1 
ATOM   4082 H  H    . SER   B 1 5   ? 47.180 -17.775 -18.561 1.00 20.93 ?  5   SER   B H    1 
ATOM   4083 H  HA   . SER   B 1 5   ? 45.747 -18.719 -20.660 1.00 23.74 ?  5   SER   B HA   1 
ATOM   4084 H  HB2  . SER   B 1 5   ? 47.811 -19.176 -21.651 1.00 25.64 ?  5   SER   B HB2  1 
ATOM   4085 H  HB3  . SER   B 1 5   ? 47.724 -17.646 -21.238 1.00 25.64 ?  5   SER   B HB3  1 
ATOM   4086 H  HG   . SER   B 1 5   ? 49.006 -19.493 -19.841 1.00 28.58 ?  5   SER   B HG   1 
ATOM   4087 N  N    . PHE   B 1 6   ? 45.309 -20.697 -19.140 1.00 21.64 ?  6   PHE   B N    1 
ATOM   4088 C  CA   . PHE   B 1 6   ? 45.120 -22.036 -18.605 1.00 21.49 ?  6   PHE   B CA   1 
ATOM   4089 C  C    . PHE   B 1 6   ? 45.039 -23.027 -19.755 1.00 24.93 ?  6   PHE   B C    1 
ATOM   4090 O  O    . PHE   B 1 6   ? 44.352 -22.775 -20.749 1.00 26.79 ?  6   PHE   B O    1 
ATOM   4091 C  CB   . PHE   B 1 6   ? 43.837 -22.090 -17.779 1.00 19.30 ?  6   PHE   B CB   1 
ATOM   4092 C  CG   . PHE   B 1 6   ? 43.867 -21.230 -16.548 1.00 17.06 ?  6   PHE   B CG   1 
ATOM   4093 C  CD1  . PHE   B 1 6   ? 44.381 -21.720 -15.363 1.00 15.89 ?  6   PHE   B CD1  1 
ATOM   4094 C  CD2  . PHE   B 1 6   ? 43.380 -19.930 -16.578 1.00 16.23 ?  6   PHE   B CD2  1 
ATOM   4095 C  CE1  . PHE   B 1 6   ? 44.399 -20.934 -14.222 1.00 15.27 ?  6   PHE   B CE1  1 
ATOM   4096 C  CE2  . PHE   B 1 6   ? 43.406 -19.135 -15.448 1.00 16.65 ?  6   PHE   B CE2  1 
ATOM   4097 C  CZ   . PHE   B 1 6   ? 43.921 -19.628 -14.269 1.00 15.63 ?  6   PHE   B CZ   1 
ATOM   4098 H  H    . PHE   B 1 6   ? 44.587 -20.229 -19.166 1.00 26.11 ?  6   PHE   B H    1 
ATOM   4099 H  HA   . PHE   B 1 6   ? 45.869 -22.276 -18.039 1.00 25.93 ?  6   PHE   B HA   1 
ATOM   4100 H  HB2  . PHE   B 1 6   ? 43.097 -21.793 -18.332 1.00 23.31 ?  6   PHE   B HB2  1 
ATOM   4101 H  HB3  . PHE   B 1 6   ? 43.685 -23.007 -17.497 1.00 23.31 ?  6   PHE   B HB3  1 
ATOM   4102 H  HD1  . PHE   B 1 6   ? 44.714 -22.589 -15.328 1.00 19.21 ?  6   PHE   B HD1  1 
ATOM   4103 H  HD2  . PHE   B 1 6   ? 43.031 -19.594 -17.370 1.00 19.62 ?  6   PHE   B HD2  1 
ATOM   4104 H  HE1  . PHE   B 1 6   ? 44.760 -21.267 -13.430 1.00 18.46 ?  6   PHE   B HE1  1 
ATOM   4105 H  HE2  . PHE   B 1 6   ? 43.073 -18.267 -15.483 1.00 20.12 ?  6   PHE   B HE2  1 
ATOM   4106 H  HZ   . PHE   B 1 6   ? 43.937 -19.098 -13.506 1.00 18.90 ?  6   PHE   B HZ   1 
ATOM   4107 N  N    . SER   B 1 7   ? 45.751 -24.146 -19.625 1.00 26.23 ?  7   SER   B N    1 
ATOM   4108 C  CA   . SER   B 1 7   ? 45.837 -25.134 -20.690 1.00 29.05 ?  7   SER   B CA   1 
ATOM   4109 C  C    . SER   B 1 7   ? 45.780 -26.536 -20.105 1.00 27.58 ?  7   SER   B C    1 
ATOM   4110 O  O    . SER   B 1 7   ? 46.376 -26.809 -19.059 1.00 28.27 ?  7   SER   B O    1 
ATOM   4111 C  CB   . SER   B 1 7   ? 47.133 -24.964 -21.493 1.00 32.71 ?  7   SER   B CB   1 
ATOM   4112 O  OG   . SER   B 1 7   ? 47.119 -25.764 -22.662 1.00 34.75 ?  7   SER   B OG   1 
ATOM   4113 H  H    . SER   B 1 7   ? 46.202 -24.354 -18.919 1.00 31.62 ?  7   SER   B H    1 
ATOM   4114 H  HA   . SER   B 1 7   ? 45.087 -25.028 -21.290 1.00 35.00 ?  7   SER   B HA   1 
ATOM   4115 H  HB2  . SER   B 1 7   ? 47.224 -24.031 -21.746 1.00 39.39 ?  7   SER   B HB2  1 
ATOM   4116 H  HB3  . SER   B 1 7   ? 47.885 -25.231 -20.942 1.00 39.39 ?  7   SER   B HB3  1 
ATOM   4117 H  HG   . SER   B 1 7   ? 47.832 -25.652 -23.094 1.00 41.84 ?  7   SER   B HG   1 
ATOM   4118 N  N    . GLY   B 1 8   ? 45.057 -27.422 -20.788 1.00 26.91 ?  8   GLY   B N    1 
ATOM   4119 C  CA   . GLY   B 1 8   ? 45.014 -28.815 -20.402 1.00 25.99 ?  8   GLY   B CA   1 
ATOM   4120 C  C    . GLY   B 1 8   ? 44.071 -29.139 -19.273 1.00 24.55 ?  8   GLY   B C    1 
ATOM   4121 O  O    . GLY   B 1 8   ? 44.216 -30.198 -18.649 1.00 25.81 ?  8   GLY   B O    1 
ATOM   4122 H  H    . GLY   B 1 8   ? 44.585 -27.232 -21.478 1.00 32.43 ?  8   GLY   B H    1 
ATOM   4123 H  HA2  . GLY   B 1 8   ? 44.749 -29.345 -21.168 1.00 31.33 ?  8   GLY   B HA2  1 
ATOM   4124 H  HA3  . GLY   B 1 8   ? 45.897 -29.096 -20.128 1.00 31.33 ?  8   GLY   B HA3  1 
ATOM   4125 N  N    . TYR   B 1 9   ? 43.089 -28.282 -19.000 1.00 22.62 ?  9   TYR   B N    1 
ATOM   4126 C  CA   . TYR   B 1 9   ? 42.135 -28.553 -17.938 1.00 20.64 ?  9   TYR   B CA   1 
ATOM   4127 C  C    . TYR   B 1 9   ? 40.952 -29.348 -18.455 1.00 20.06 ?  9   TYR   B C    1 
ATOM   4128 O  O    . TYR   B 1 9   ? 40.531 -29.212 -19.607 1.00 21.89 ?  9   TYR   B O    1 
ATOM   4129 C  CB   . TYR   B 1 9   ? 41.625 -27.265 -17.296 1.00 19.75 ?  9   TYR   B CB   1 
ATOM   4130 C  CG   . TYR   B 1 9   ? 42.651 -26.638 -16.384 1.00 19.04 ?  9   TYR   B CG   1 
ATOM   4131 C  CD1  . TYR   B 1 9   ? 43.749 -25.971 -16.906 1.00 19.42 ?  9   TYR   B CD1  1 
ATOM   4132 C  CD2  . TYR   B 1 9   ? 42.538 -26.735 -15.007 1.00 18.41 ?  9   TYR   B CD2  1 
ATOM   4133 C  CE1  . TYR   B 1 9   ? 44.704 -25.410 -16.080 1.00 19.47 ?  9   TYR   B CE1  1 
ATOM   4134 C  CE2  . TYR   B 1 9   ? 43.487 -26.175 -14.170 1.00 18.52 ?  9   TYR   B CE2  1 
ATOM   4135 C  CZ   . TYR   B 1 9   ? 44.569 -25.510 -14.714 1.00 19.22 ?  9   TYR   B CZ   1 
ATOM   4136 O  OH   . TYR   B 1 9   ? 45.517 -24.960 -13.889 1.00 19.72 ?  9   TYR   B OH   1 
ATOM   4137 H  H    . TYR   B 1 9   ? 42.939 -27.548 -19.425 1.00 27.29 ?  9   TYR   B H    1 
ATOM   4138 H  HA   . TYR   B 1 9   ? 42.561 -29.077 -17.248 1.00 24.91 ?  9   TYR   B HA   1 
ATOM   4139 H  HB2  . TYR   B 1 9   ? 41.395 -26.623 -17.989 1.00 23.84 ?  9   TYR   B HB2  1 
ATOM   4140 H  HB3  . TYR   B 1 9   ? 40.843 -27.478 -16.766 1.00 23.84 ?  9   TYR   B HB3  1 
ATOM   4141 H  HD1  . TYR   B 1 9   ? 43.842 -25.903 -17.830 1.00 23.44 ?  9   TYR   B HD1  1 
ATOM   4142 H  HD2  . TYR   B 1 9   ? 41.804 -27.187 -14.640 1.00 22.23 ?  9   TYR   B HD2  1 
ATOM   4143 H  HE1  . TYR   B 1 9   ? 45.427 -24.968 -16.445 1.00 23.50 ?  9   TYR   B HE1  1 
ATOM   4144 H  HE2  . TYR   B 1 9   ? 43.385 -26.253 -13.248 1.00 22.36 ?  9   TYR   B HE2  1 
ATOM   4145 H  HH   . TYR   B 1 9   ? 46.105 -24.592 -14.350 1.00 23.81 ?  9   TYR   B HH   1 
ATOM   4146 N  N    . LEU   B 1 10  ? 40.425 -30.194 -17.578 1.00 18.36 ?  10  LEU   B N    1 
ATOM   4147 C  CA   . LEU   B 1 10  ? 39.216 -30.951 -17.844 1.00 18.24 ?  10  LEU   B CA   1 
ATOM   4148 C  C    . LEU   B 1 10  ? 38.030 -30.186 -17.271 1.00 17.80 ?  10  LEU   B C    1 
ATOM   4149 O  O    . LEU   B 1 10  ? 38.052 -29.771 -16.108 1.00 17.59 ?  10  LEU   B O    1 
ATOM   4150 C  CB   . LEU   B 1 10  ? 39.323 -32.322 -17.181 1.00 19.16 ?  10  LEU   B CB   1 
ATOM   4151 C  CG   . LEU   B 1 10  ? 38.181 -33.282 -17.498 1.00 20.89 ?  10  LEU   B CG   1 
ATOM   4152 C  CD1  . LEU   B 1 10  ? 38.294 -33.784 -18.931 1.00 22.17 ?  10  LEU   B CD1  1 
ATOM   4153 C  CD2  . LEU   B 1 10  ? 38.154 -34.439 -16.514 1.00 21.99 ?  10  LEU   B CD2  1 
ATOM   4154 H  H    . LEU   B 1 10  ? 40.752 -30.352 -16.795 1.00 22.18 ?  10  LEU   B H    1 
ATOM   4155 H  HA   . LEU   B 1 10  ? 39.090 -31.071 -18.797 1.00 22.02 ?  10  LEU   B HA   1 
ATOM   4156 H  HB2  . LEU   B 1 10  ? 40.146 -32.748 -17.473 1.00 23.13 ?  10  LEU   B HB2  1 
ATOM   4157 H  HB3  . LEU   B 1 10  ? 39.344 -32.207 -16.217 1.00 23.13 ?  10  LEU   B HB3  1 
ATOM   4158 H  HG   . LEU   B 1 10  ? 37.338 -32.809 -17.416 1.00 25.21 ?  10  LEU   B HG   1 
ATOM   4159 H  HD11 . LEU   B 1 10  ? 37.595 -34.436 -19.093 1.00 26.74 ?  10  LEU   B HD11 1 
ATOM   4160 H  HD12 . LEU   B 1 10  ? 38.190 -33.031 -19.535 1.00 26.74 ?  10  LEU   B HD12 1 
ATOM   4161 H  HD13 . LEU   B 1 10  ? 39.164 -34.191 -19.054 1.00 26.74 ?  10  LEU   B HD13 1 
ATOM   4162 H  HD21 . LEU   B 1 10  ? 37.420 -35.030 -16.745 1.00 26.53 ?  10  LEU   B HD21 1 
ATOM   4163 H  HD22 . LEU   B 1 10  ? 38.995 -34.914 -16.566 1.00 26.53 ?  10  LEU   B HD22 1 
ATOM   4164 H  HD23 . LEU   B 1 10  ? 38.024 -34.084 -15.620 1.00 26.53 ?  10  LEU   B HD23 1 
ATOM   4165 N  N    . LYS   B 1 11  ? 37.002 -30.001 -18.092 1.00 19.10 ?  11  LYS   B N    1 
ATOM   4166 C  CA   . LYS   B 1 11  ? 35.804 -29.289 -17.677 1.00 21.17 ?  11  LYS   B CA   1 
ATOM   4167 C  C    . LYS   B 1 11  ? 34.934 -30.217 -16.835 1.00 20.02 ?  11  LYS   B C    1 
ATOM   4168 O  O    . LYS   B 1 11  ? 34.564 -31.307 -17.284 1.00 21.59 ?  11  LYS   B O    1 
ATOM   4169 C  CB   . LYS   B 1 11  ? 35.054 -28.823 -18.924 1.00 25.18 ?  11  LYS   B CB   1 
ATOM   4170 C  CG   . LYS   B 1 11  ? 33.898 -27.878 -18.673 1.00 28.73 ?  11  LYS   B CG   1 
ATOM   4171 C  CD   . LYS   B 1 11  ? 33.154 -27.594 -19.972 1.00 31.72 ?  11  LYS   B CD   1 
ATOM   4172 C  CE   . LYS   B 1 11  ? 32.145 -26.471 -19.808 1.00 33.86 ?  11  LYS   B CE   1 
ATOM   4173 N  NZ   . LYS   B 1 11  ? 32.813 -25.154 -19.627 1.00 35.03 ?  11  LYS   B NZ   1 
ATOM   4174 H  H    . LYS   B 1 11  ? 36.970 -30.284 -18.905 1.00 23.06 ?  11  LYS   B H    1 
ATOM   4175 H  HA   . LYS   B 1 11  ? 36.046 -28.513 -17.147 1.00 25.55 ?  11  LYS   B HA   1 
ATOM   4176 H  HB2  . LYS   B 1 11  ? 35.681 -28.362 -19.506 1.00 30.36 ?  11  LYS   B HB2  1 
ATOM   4177 H  HB3  . LYS   B 1 11  ? 34.699 -29.600 -19.381 1.00 30.36 ?  11  LYS   B HB3  1 
ATOM   4178 H  HG2  . LYS   B 1 11  ? 33.277 -28.284 -18.049 1.00 34.62 ?  11  LYS   B HG2  1 
ATOM   4179 H  HG3  . LYS   B 1 11  ? 34.234 -27.039 -18.323 1.00 34.62 ?  11  LYS   B HG3  1 
ATOM   4180 H  HD2  . LYS   B 1 11  ? 33.793 -27.332 -20.655 1.00 38.20 ?  11  LYS   B HD2  1 
ATOM   4181 H  HD3  . LYS   B 1 11  ? 32.679 -28.393 -20.249 1.00 38.20 ?  11  LYS   B HD3  1 
ATOM   4182 H  HE2  . LYS   B 1 11  ? 31.588 -26.424 -20.601 1.00 40.77 ?  11  LYS   B HE2  1 
ATOM   4183 H  HE3  . LYS   B 1 11  ? 31.600 -26.650 -19.026 1.00 40.77 ?  11  LYS   B HE3  1 
ATOM   4184 H  HZ1  . LYS   B 1 11  ? 32.202 -24.512 -19.549 1.00 42.18 ?  11  LYS   B HZ1  1 
ATOM   4185 H  HZ2  . LYS   B 1 11  ? 33.316 -25.166 -18.894 1.00 42.18 ?  11  LYS   B HZ2  1 
ATOM   4186 H  HZ3  . LYS   B 1 11  ? 33.330 -24.977 -20.331 1.00 42.18 ?  11  LYS   B HZ3  1 
ATOM   4187 N  N    . LEU   B 1 12  ? 34.603 -29.788 -15.616 1.00 18.38 ?  12  LEU   B N    1 
ATOM   4188 C  CA   . LEU   B 1 12  ? 33.651 -30.498 -14.768 1.00 17.76 ?  12  LEU   B CA   1 
ATOM   4189 C  C    . LEU   B 1 12  ? 32.260 -29.891 -14.851 1.00 17.17 ?  12  LEU   B C    1 
ATOM   4190 O  O    . LEU   B 1 12  ? 31.273 -30.608 -15.014 1.00 17.67 ?  12  LEU   B O    1 
ATOM   4191 C  CB   . LEU   B 1 12  ? 34.122 -30.515 -13.308 1.00 17.35 ?  12  LEU   B CB   1 
ATOM   4192 C  CG   . LEU   B 1 12  ? 35.466 -31.191 -13.040 1.00 17.04 ?  12  LEU   B CG   1 
ATOM   4193 C  CD1  . LEU   B 1 12  ? 35.819 -31.140 -11.560 1.00 16.95 ?  12  LEU   B CD1  1 
ATOM   4194 C  CD2  . LEU   B 1 12  ? 35.474 -32.625 -13.548 1.00 17.59 ?  12  LEU   B CD2  1 
ATOM   4195 H  H    . LEU   B 1 12  ? 34.917 -29.073 -15.254 1.00 22.20 ?  12  LEU   B H    1 
ATOM   4196 H  HA   . LEU   B 1 12  ? 33.582 -31.416 -15.073 1.00 21.46 ?  12  LEU   B HA   1 
ATOM   4197 H  HB2  . LEU   B 1 12  ? 34.189 -29.599 -13.001 1.00 20.97 ?  12  LEU   B HB2  1 
ATOM   4198 H  HB3  . LEU   B 1 12  ? 33.453 -30.982 -12.780 1.00 20.97 ?  12  LEU   B HB3  1 
ATOM   4199 H  HG   . LEU   B 1 12  ? 36.153 -30.704 -13.519 1.00 20.58 ?  12  LEU   B HG   1 
ATOM   4200 H  HD11 . LEU   B 1 12  ? 36.681 -31.572 -11.426 1.00 20.49 ?  12  LEU   B HD11 1 
ATOM   4201 H  HD12 . LEU   B 1 12  ? 35.872 -30.213 -11.275 1.00 20.49 ?  12  LEU   B HD12 1 
ATOM   4202 H  HD13 . LEU   B 1 12  ? 35.138 -31.604 -11.051 1.00 20.49 ?  12  LEU   B HD13 1 
ATOM   4203 H  HD21 . LEU   B 1 12  ? 36.284 -33.061 -13.243 1.00 21.24 ?  12  LEU   B HD21 1 
ATOM   4204 H  HD22 . LEU   B 1 12  ? 34.696 -33.086 -13.200 1.00 21.24 ?  12  LEU   B HD22 1 
ATOM   4205 H  HD23 . LEU   B 1 12  ? 35.448 -32.614 -14.518 1.00 21.24 ?  12  LEU   B HD23 1 
ATOM   4206 N  N    . THR   B 1 13  ? 32.171 -28.573 -14.739 1.00 17.19 ?  13  THR   B N    1 
ATOM   4207 C  CA   . THR   B 1 13  ? 30.947 -27.822 -14.947 1.00 17.43 ?  13  THR   B CA   1 
ATOM   4208 C  C    . THR   B 1 13  ? 31.285 -26.626 -15.831 1.00 19.60 ?  13  THR   B C    1 
ATOM   4209 O  O    . THR   B 1 13  ? 32.432 -26.439 -16.256 1.00 20.50 ?  13  THR   B O    1 
ATOM   4210 C  CB   . THR   B 1 13  ? 30.349 -27.342 -13.620 1.00 16.98 ?  13  THR   B CB   1 
ATOM   4211 O  OG1  . THR   B 1 13  ? 31.198 -26.324 -13.075 1.00 16.98 ?  13  THR   B OG1  1 
ATOM   4212 C  CG2  . THR   B 1 13  ? 30.220 -28.494 -12.624 1.00 17.39 ?  13  THR   B CG2  1 
ATOM   4213 H  H    . THR   B 1 13  ? 32.836 -28.073 -14.529 1.00 20.77 ?  13  THR   B H    1 
ATOM   4214 H  HA   . THR   B 1 13  ? 30.288 -28.377 -15.393 1.00 21.05 ?  13  THR   B HA   1 
ATOM   4215 H  HB   . THR   B 1 13  ? 29.458 -26.973 -13.774 1.00 20.52 ?  13  THR   B HB   1 
ATOM   4216 H  HG1  . THR   B 1 13  ? 30.895 -25.560 -13.271 1.00 20.52 ?  13  THR   B HG1  1 
ATOM   4217 H  HG21 . THR   B 1 13  ? 29.729 -28.205 -11.837 1.00 21.01 ?  13  THR   B HG21 1 
ATOM   4218 H  HG22 . THR   B 1 13  ? 29.747 -29.235 -13.033 1.00 21.01 ?  13  THR   B HG22 1 
ATOM   4219 H  HG23 . THR   B 1 13  ? 31.100 -28.795 -12.351 1.00 21.01 ?  13  THR   B HG23 1 
ATOM   4220 N  N    A ASP   B 1 14  ? 30.277 -25.796 -16.094 0.74 20.62 ?  14  ASP   B N    1 
ATOM   4221 N  N    B ASP   B 1 14  ? 30.279 -25.789 -16.092 0.26 20.35 ?  14  ASP   B N    1 
ATOM   4222 C  CA   A ASP   B 1 14  ? 30.492 -24.640 -16.956 0.74 22.10 ?  14  ASP   B CA   1 
ATOM   4223 C  CA   B ASP   B 1 14  ? 30.485 -24.635 -16.961 0.26 21.22 ?  14  ASP   B CA   1 
ATOM   4224 C  C    A ASP   B 1 14  ? 31.583 -23.723 -16.419 0.74 20.26 ?  14  ASP   B C    1 
ATOM   4225 C  C    B ASP   B 1 14  ? 31.500 -23.648 -16.401 0.26 19.49 ?  14  ASP   B C    1 
ATOM   4226 O  O    A ASP   B 1 14  ? 32.236 -23.022 -17.202 0.74 21.60 ?  14  ASP   B O    1 
ATOM   4227 O  O    B ASP   B 1 14  ? 32.000 -22.806 -17.156 0.26 19.73 ?  14  ASP   B O    1 
ATOM   4228 C  CB   A ASP   B 1 14  ? 29.189 -23.860 -17.130 0.74 25.74 ?  14  ASP   B CB   1 
ATOM   4229 C  CB   B ASP   B 1 14  ? 29.164 -23.906 -17.209 0.26 23.78 ?  14  ASP   B CB   1 
ATOM   4230 C  CG   A ASP   B 1 14  ? 28.220 -24.538 -18.076 0.74 29.42 ?  14  ASP   B CG   1 
ATOM   4231 C  CG   B ASP   B 1 14  ? 28.269 -24.638 -18.191 0.26 26.07 ?  14  ASP   B CG   1 
ATOM   4232 O  OD1  A ASP   B 1 14  ? 28.613 -25.511 -18.759 0.74 30.67 ?  14  ASP   B OD1  1 
ATOM   4233 O  OD1  B ASP   B 1 14  ? 28.803 -25.327 -19.085 0.26 26.85 ?  14  ASP   B OD1  1 
ATOM   4234 O  OD2  A ASP   B 1 14  ? 27.053 -24.099 -18.132 0.74 30.93 -1 14  ASP   B OD2  1 
ATOM   4235 O  OD2  B ASP   B 1 14  ? 27.031 -24.526 -18.069 0.26 26.86 -1 14  ASP   B OD2  1 
ATOM   4236 H  H    A ASP   B 1 14  ? 29.477 -25.873 -15.784 0.74 24.89 ?  14  ASP   B H    1 
ATOM   4237 H  H    B ASP   B 1 14  ? 29.481 -25.865 -15.782 0.26 24.56 ?  14  ASP   B H    1 
ATOM   4238 H  HA   A ASP   B 1 14  ? 30.776 -24.947 -17.827 0.74 26.67 ?  14  ASP   B HA   1 
ATOM   4239 H  HA   B ASP   B 1 14  ? 30.818 -24.945 -17.816 0.26 25.61 ?  14  ASP   B HA   1 
ATOM   4240 H  HB2  A ASP   B 1 14  ? 28.745 -23.785 -16.273 0.74 31.03 ?  14  ASP   B HB2  1 
ATOM   4241 H  HB2  B ASP   B 1 14  ? 28.686 -23.826 -16.370 0.26 28.67 ?  14  ASP   B HB2  1 
ATOM   4242 H  HB3  A ASP   B 1 14  ? 29.391 -22.979 -17.480 0.74 31.03 ?  14  ASP   B HB3  1 
ATOM   4243 H  HB3  B ASP   B 1 14  ? 29.358 -23.020 -17.563 0.26 28.67 ?  14  ASP   B HB3  1 
ATOM   4244 N  N    . ASN   B 1 15  ? 31.800 -23.712 -15.101 1.00 17.86 ?  15  ASN   B N    1 
ATOM   4245 C  CA   . ASN   B 1 15  ? 32.762 -22.794 -14.496 1.00 15.52 ?  15  ASN   B CA   1 
ATOM   4246 C  C    . ASN   B 1 15  ? 33.857 -23.451 -13.664 1.00 14.33 ?  15  ASN   B C    1 
ATOM   4247 O  O    . ASN   B 1 15  ? 34.715 -22.728 -13.146 1.00 14.54 ?  15  ASN   B O    1 
ATOM   4248 C  CB   . ASN   B 1 15  ? 32.048 -21.739 -13.635 1.00 15.65 ?  15  ASN   B CB   1 
ATOM   4249 C  CG   . ASN   B 1 15  ? 31.431 -22.337 -12.393 1.00 15.20 ?  15  ASN   B CG   1 
ATOM   4250 O  OD1  . ASN   B 1 15  ? 30.488 -23.130 -12.480 1.00 16.77 ?  15  ASN   B OD1  1 
ATOM   4251 N  ND2  . ASN   B 1 15  ? 31.960 -21.987 -11.235 1.00 14.40 ?  15  ASN   B ND2  1 
ATOM   4252 H  H    A ASN   B 1 15  ? 31.395 -24.219 -14.534 0.74 21.57 ?  15  ASN   B H    1 
ATOM   4253 H  H    B ASN   B 1 15  ? 31.439 -24.259 -14.543 0.26 21.57 ?  15  ASN   B H    1 
ATOM   4254 H  HA   . ASN   B 1 15  ? 33.207 -22.308 -15.200 1.00 18.77 ?  15  ASN   B HA   1 
ATOM   4255 H  HB2  . ASN   B 1 15  ? 32.690 -21.059 -13.359 1.00 18.92 ?  15  ASN   B HB2  1 
ATOM   4256 H  HB3  . ASN   B 1 15  ? 31.336 -21.321 -14.152 1.00 18.92 ?  15  ASN   B HB3  1 
ATOM   4257 H  HD21 . ASN   B 1 15  ? 31.643 -22.298 -10.497 1.00 17.42 ?  15  ASN   B HD21 1 
ATOM   4258 H  HD22 . ASN   B 1 15  ? 32.630 -21.437 -11.207 1.00 17.42 ?  15  ASN   B HD22 1 
ATOM   4259 N  N    . VAL   B 1 16  ? 33.864 -24.774 -13.513 1.00 13.93 ?  16  VAL   B N    1 
ATOM   4260 C  CA   . VAL   B 1 16  ? 34.868 -25.464 -12.710 1.00 13.55 ?  16  VAL   B CA   1 
ATOM   4261 C  C    . VAL   B 1 16  ? 35.658 -26.400 -13.609 1.00 14.04 ?  16  VAL   B C    1 
ATOM   4262 O  O    . VAL   B 1 16  ? 35.080 -27.280 -14.267 1.00 14.80 ?  16  VAL   B O    1 
ATOM   4263 C  CB   . VAL   B 1 16  ? 34.245 -26.231 -11.531 1.00 14.09 ?  16  VAL   B CB   1 
ATOM   4264 C  CG1  . VAL   B 1 16  ? 35.332 -26.962 -10.751 1.00 13.93 ?  16  VAL   B CG1  1 
ATOM   4265 C  CG2  . VAL   B 1 16  ? 33.449 -25.285 -10.630 1.00 14.90 ?  16  VAL   B CG2  1 
ATOM   4266 H  H    . VAL   B 1 16  ? 33.277 -25.300 -13.866 1.00 16.86 ?  16  VAL   B H    1 
ATOM   4267 H  HA   . VAL   B 1 16  ? 35.479 -24.807 -12.342 1.00 16.40 ?  16  VAL   B HA   1 
ATOM   4268 H  HB   . VAL   B 1 16  ? 33.630 -26.898 -11.879 1.00 17.05 ?  16  VAL   B HB   1 
ATOM   4269 H  HG11 . VAL   B 1 16  ? 34.967 -27.251 -9.901  1.00 16.85 ?  16  VAL   B HG11 1 
ATOM   4270 H  HG12 . VAL   B 1 16  ? 35.628 -27.729 -11.263 1.00 16.85 ?  16  VAL   B HG12 1 
ATOM   4271 H  HG13 . VAL   B 1 16  ? 36.072 -26.352 -10.603 1.00 16.85 ?  16  VAL   B HG13 1 
ATOM   4272 H  HG21 . VAL   B 1 16  ? 33.112 -25.786 -9.869  1.00 18.02 ?  16  VAL   B HG21 1 
ATOM   4273 H  HG22 . VAL   B 1 16  ? 34.031 -24.575 -10.329 1.00 18.02 ?  16  VAL   B HG22 1 
ATOM   4274 H  HG23 . VAL   B 1 16  ? 32.708 -24.918 -11.137 1.00 18.02 ?  16  VAL   B HG23 1 
ATOM   4275 N  N    . TYR   B 1 17  ? 36.983 -26.231 -13.589 1.00 14.35 ?  17  TYR   B N    1 
ATOM   4276 C  CA   . TYR   B 1 17  ? 37.931 -26.984 -14.397 1.00 14.78 ?  17  TYR   B CA   1 
ATOM   4277 C  C    . TYR   B 1 17  ? 38.984 -27.589 -13.480 1.00 13.64 ?  17  TYR   B C    1 
ATOM   4278 O  O    . TYR   B 1 17  ? 39.259 -27.059 -12.401 1.00 14.04 ?  17  TYR   B O    1 
ATOM   4279 C  CB   . TYR   B 1 17  ? 38.634 -26.067 -15.404 1.00 17.41 ?  17  TYR   B CB   1 
ATOM   4280 C  CG   . TYR   B 1 17  ? 37.706 -25.300 -16.313 1.00 20.76 ?  17  TYR   B CG   1 
ATOM   4281 C  CD1  . TYR   B 1 17  ? 37.140 -24.098 -15.910 1.00 22.36 ?  17  TYR   B CD1  1 
ATOM   4282 C  CD2  . TYR   B 1 17  ? 37.399 -25.777 -17.579 1.00 22.71 ?  17  TYR   B CD2  1 
ATOM   4283 C  CE1  . TYR   B 1 17  ? 36.289 -23.391 -16.744 1.00 24.01 ?  17  TYR   B CE1  1 
ATOM   4284 C  CE2  . TYR   B 1 17  ? 36.552 -25.080 -18.421 1.00 24.31 ?  17  TYR   B CE2  1 
ATOM   4285 C  CZ   . TYR   B 1 17  ? 35.999 -23.889 -17.997 1.00 25.06 ?  17  TYR   B CZ   1 
ATOM   4286 O  OH   . TYR   B 1 17  ? 35.159 -23.192 -18.833 1.00 26.37 ?  17  TYR   B OH   1 
ATOM   4287 H  H    . TYR   B 1 17  ? 37.375 -25.645 -13.087 1.00 17.36 ?  17  TYR   B H    1 
ATOM   4288 H  HA   . TYR   B 1 17  ? 37.465 -27.694 -14.875 1.00 17.87 ?  17  TYR   B HA   1 
ATOM   4289 H  HB2  . TYR   B 1 17  ? 39.174 -25.428 -14.920 1.00 21.03 ?  17  TYR   B HB2  1 
ATOM   4290 H  HB3  . TYR   B 1 17  ? 39.193 -26.615 -15.969 1.00 21.03 ?  17  TYR   B HB3  1 
ATOM   4291 H  HD1  . TYR   B 1 17  ? 37.333 -23.760 -15.066 1.00 26.98 ?  17  TYR   B HD1  1 
ATOM   4292 H  HD2  . TYR   B 1 17  ? 37.766 -26.581 -17.868 1.00 27.40 ?  17  TYR   B HD2  1 
ATOM   4293 H  HE1  . TYR   B 1 17  ? 35.917 -22.585 -16.463 1.00 28.95 ?  17  TYR   B HE1  1 
ATOM   4294 H  HE2  . TYR   B 1 17  ? 36.352 -25.412 -19.268 1.00 29.31 ?  17  TYR   B HE2  1 
ATOM   4295 H  HH   . TYR   B 1 17  ? 35.066 -23.601 -19.561 1.00 31.78 ?  17  TYR   B HH   1 
ATOM   4296 N  N    . ILE   B 1 18  ? 39.594 -28.696 -13.910 1.00 14.00 ?  18  ILE   B N    1 
ATOM   4297 C  CA   . ILE   B 1 18  ? 40.523 -29.420 -13.050 1.00 13.95 ?  18  ILE   B CA   1 
ATOM   4298 C  C    . ILE   B 1 18  ? 41.681 -29.974 -13.871 1.00 14.25 ?  18  ILE   B C    1 
ATOM   4299 O  O    . ILE   B 1 18  ? 41.519 -30.367 -15.031 1.00 15.50 ?  18  ILE   B O    1 
ATOM   4300 C  CB   . ILE   B 1 18  ? 39.776 -30.520 -12.250 1.00 14.23 ?  18  ILE   B CB   1 
ATOM   4301 C  CG1  . ILE   B 1 18  ? 40.637 -31.067 -11.110 1.00 14.57 ?  18  ILE   B CG1  1 
ATOM   4302 C  CG2  . ILE   B 1 18  ? 39.282 -31.642 -13.176 1.00 14.76 ?  18  ILE   B CG2  1 
ATOM   4303 C  CD1  . ILE   B 1 18  ? 39.837 -31.887 -10.103 1.00 15.91 ?  18  ILE   B CD1  1 
ATOM   4304 H  H    . ILE   B 1 18  ? 39.479 -29.048 -14.685 1.00 16.94 ?  18  ILE   B H    1 
ATOM   4305 H  HA   . ILE   B 1 18  ? 40.882 -28.802 -12.398 1.00 16.88 ?  18  ILE   B HA   1 
ATOM   4306 H  HB   . ILE   B 1 18  ? 38.988 -30.122 -11.844 1.00 17.21 ?  18  ILE   B HB   1 
ATOM   4307 H  HG12 . ILE   B 1 18  ? 41.327 -31.638 -11.476 1.00 17.62 ?  18  ILE   B HG12 1 
ATOM   4308 H  HG13 . ILE   B 1 18  ? 41.035 -30.322 -10.633 1.00 17.62 ?  18  ILE   B HG13 1 
ATOM   4309 H  HG21 . ILE   B 1 18  ? 38.686 -32.225 -12.679 1.00 17.85 ?  18  ILE   B HG21 1 
ATOM   4310 H  HG22 . ILE   B 1 18  ? 38.807 -31.240 -13.920 1.00 17.85 ?  18  ILE   B HG22 1 
ATOM   4311 H  HG23 . ILE   B 1 18  ? 40.044 -32.142 -13.499 1.00 17.85 ?  18  ILE   B HG23 1 
ATOM   4312 H  HD11 . ILE   B 1 18  ? 40.424 -32.164 -9.380  1.00 19.23 ?  18  ILE   B HD11 1 
ATOM   4313 H  HD12 . ILE   B 1 18  ? 39.115 -31.343 -9.750  1.00 19.23 ?  18  ILE   B HD12 1 
ATOM   4314 H  HD13 . ILE   B 1 18  ? 39.473 -32.670 -10.548 1.00 19.23 ?  18  ILE   B HD13 1 
ATOM   4315 N  N    . LYS   B 1 19  ? 42.859 -30.014 -13.247 1.00 14.74 ?  19  LYS   B N    1 
ATOM   4316 C  CA   . LYS   B 1 19  ? 44.069 -30.481 -13.906 1.00 15.66 ?  19  LYS   B CA   1 
ATOM   4317 C  C    . LYS   B 1 19  ? 44.976 -31.155 -12.886 1.00 15.58 ?  19  LYS   B C    1 
ATOM   4318 O  O    . LYS   B 1 19  ? 45.061 -30.726 -11.733 1.00 14.96 ?  19  LYS   B O    1 
ATOM   4319 C  CB   . LYS   B 1 19  ? 44.822 -29.310 -14.553 1.00 17.13 ?  19  LYS   B CB   1 
ATOM   4320 C  CG   . LYS   B 1 19  ? 46.018 -29.712 -15.398 1.00 19.06 ?  19  LYS   B CG   1 
ATOM   4321 C  CD   . LYS   B 1 19  ? 46.758 -28.483 -15.913 1.00 20.72 ?  19  LYS   B CD   1 
ATOM   4322 C  CE   . LYS   B 1 19  ? 47.897 -28.860 -16.841 1.00 22.39 ?  19  LYS   B CE   1 
ATOM   4323 N  NZ   . LYS   B 1 19  ? 48.670 -27.671 -17.290 1.00 23.43 ?  19  LYS   B NZ   1 
ATOM   4324 H  H    . LYS   B 1 19  ? 42.972 -29.769 -12.425 1.00 17.82 ?  19  LYS   B H    1 
ATOM   4325 H  HA   . LYS   B 1 19  ? 43.829 -31.123 -14.593 1.00 18.93 ?  19  LYS   B HA   1 
ATOM   4326 H  HB2  . LYS   B 1 19  ? 44.202 -28.831 -15.125 1.00 20.70 ?  19  LYS   B HB2  1 
ATOM   4327 H  HB3  . LYS   B 1 19  ? 45.133 -28.721 -13.846 1.00 20.70 ?  19  LYS   B HB3  1 
ATOM   4328 H  HG2  . LYS   B 1 19  ? 46.625 -30.240 -14.859 1.00 23.02 ?  19  LYS   B HG2  1 
ATOM   4329 H  HG3  . LYS   B 1 19  ? 45.704 -30.229 -16.159 1.00 23.02 ?  19  LYS   B HG3  1 
ATOM   4330 H  HD2  . LYS   B 1 19  ? 46.136 -27.920 -16.402 1.00 25.01 ?  19  LYS   B HD2  1 
ATOM   4331 H  HD3  . LYS   B 1 19  ? 47.126 -27.997 -15.158 1.00 25.01 ?  19  LYS   B HD3  1 
ATOM   4332 H  HE2  . LYS   B 1 19  ? 48.500 -29.459 -16.374 1.00 27.01 ?  19  LYS   B HE2  1 
ATOM   4333 H  HE3  . LYS   B 1 19  ? 47.531 -29.302 -17.625 1.00 27.01 ?  19  LYS   B HE3  1 
ATOM   4334 H  HZ1  . LYS   B 1 19  ? 49.285 -27.916 -17.886 1.00 28.25 ?  19  LYS   B HZ1  1 
ATOM   4335 H  HZ2  . LYS   B 1 19  ? 48.124 -27.077 -17.667 1.00 28.25 ?  19  LYS   B HZ2  1 
ATOM   4336 H  HZ3  . LYS   B 1 19  ? 49.076 -27.292 -16.596 1.00 28.25 ?  19  LYS   B HZ3  1 
ATOM   4337 N  N    . ASN   B 1 20  ? 45.664 -32.208 -13.322 1.00 16.71 ?  20  ASN   B N    1 
ATOM   4338 C  CA   . ASN   B 1 20  ? 46.688 -32.847 -12.500 1.00 17.92 ?  20  ASN   B CA   1 
ATOM   4339 C  C    . ASN   B 1 20  ? 47.967 -32.039 -12.685 1.00 18.21 ?  20  ASN   B C    1 
ATOM   4340 O  O    . ASN   B 1 20  ? 48.625 -32.130 -13.725 1.00 20.09 ?  20  ASN   B O    1 
ATOM   4341 C  CB   . ASN   B 1 20  ? 46.856 -34.305 -12.926 1.00 19.56 ?  20  ASN   B CB   1 
ATOM   4342 C  CG   . ASN   B 1 20  ? 48.029 -35.007 -12.246 1.00 20.90 ?  20  ASN   B CG   1 
ATOM   4343 O  OD1  . ASN   B 1 20  ? 48.704 -35.841 -12.862 1.00 23.14 ?  20  ASN   B OD1  1 
ATOM   4344 N  ND2  . ASN   B 1 20  ? 48.264 -34.697 -10.978 1.00 20.48 ?  20  ASN   B ND2  1 
ATOM   4345 H  H    . ASN   B 1 20  ? 45.551 -32.571 -14.093 1.00 20.19 ?  20  ASN   B H    1 
ATOM   4346 H  HA   . ASN   B 1 20  ? 46.412 -32.822 -11.569 1.00 21.65 ?  20  ASN   B HA   1 
ATOM   4347 H  HB2  . ASN   B 1 20  ? 46.043 -34.794 -12.703 1.00 23.61 ?  20  ASN   B HB2  1 
ATOM   4348 H  HB3  . ASN   B 1 20  ? 47.001 -34.335 -13.883 1.00 23.61 ?  20  ASN   B HB3  1 
ATOM   4349 H  HD21 . ASN   B 1 20  ? 48.917 -35.066 -10.561 1.00 24.72 ?  20  ASN   B HD21 1 
ATOM   4350 H  HD22 . ASN   B 1 20  ? 47.772 -34.114 -10.572 1.00 24.72 ?  20  ASN   B HD22 1 
ATOM   4351 N  N    . ALA   B 1 21  ? 48.315 -31.224 -11.688 1.00 17.38 ?  21  ALA   B N    1 
ATOM   4352 C  CA   . ALA   B 1 21  ? 49.445 -30.321 -11.839 1.00 18.07 ?  21  ALA   B CA   1 
ATOM   4353 C  C    . ALA   B 1 21  ? 49.902 -29.811 -10.481 1.00 17.05 ?  21  ALA   B C    1 
ATOM   4354 O  O    . ALA   B 1 21  ? 49.160 -29.834 -9.494  1.00 16.87 ?  21  ALA   B O    1 
ATOM   4355 C  CB   . ALA   B 1 21  ? 49.087 -29.153 -12.756 1.00 19.47 ?  21  ALA   B CB   1 
ATOM   4356 H  H    . ALA   B 1 21  ? 47.912 -31.179 -10.925 1.00 21.00 ?  21  ALA   B H    1 
ATOM   4357 H  HA   . ALA   B 1 21  ? 50.179 -30.815 -12.241 1.00 21.82 ?  21  ALA   B HA   1 
ATOM   4358 H  HB1  . ALA   B 1 21  ? 49.888 -28.639 -12.913 1.00 23.51 ?  21  ALA   B HB1  1 
ATOM   4359 H  HB2  . ALA   B 1 21  ? 48.750 -29.512 -13.592 1.00 23.51 ?  21  ALA   B HB2  1 
ATOM   4360 H  HB3  . ALA   B 1 21  ? 48.409 -28.617 -12.325 1.00 23.51 ?  21  ALA   B HB3  1 
ATOM   4361 N  N    . ASP   B 1 22  ? 51.154 -29.354 -10.466 1.00 16.27 ?  22  ASP   B N    1 
ATOM   4362 C  CA   . ASP   B 1 22  ? 51.769 -28.662 -9.339  1.00 15.60 ?  22  ASP   B CA   1 
ATOM   4363 C  C    . ASP   B 1 22  ? 51.365 -27.189 -9.417  1.00 14.17 ?  22  ASP   B C    1 
ATOM   4364 O  O    . ASP   B 1 22  ? 51.673 -26.514 -10.404 1.00 14.39 ?  22  ASP   B O    1 
ATOM   4365 C  CB   . ASP   B 1 22  ? 53.286 -28.846 -9.491  1.00 16.99 ?  22  ASP   B CB   1 
ATOM   4366 C  CG   . ASP   B 1 22  ? 54.116 -28.083 -8.464  1.00 18.59 ?  22  ASP   B CG   1 
ATOM   4367 O  OD1  . ASP   B 1 22  ? 53.744 -26.970 -8.063  1.00 18.55 ?  22  ASP   B OD1  1 
ATOM   4368 O  OD2  . ASP   B 1 22  ? 55.199 -28.588 -8.088  1.00 20.67 -1 22  ASP   B OD2  1 
ATOM   4369 H  H    . ASP   B 1 22  ? 51.691 -29.438 -11.137 1.00 19.66 ?  22  ASP   B H    1 
ATOM   4370 H  HA   . ASP   B 1 22  ? 51.473 -29.046 -8.498  1.00 18.86 ?  22  ASP   B HA   1 
ATOM   4371 H  HB2  . ASP   B 1 22  ? 53.499 -29.785 -9.409  1.00 20.53 ?  22  ASP   B HB2  1 
ATOM   4372 H  HB3  . ASP   B 1 22  ? 53.552 -28.520 -10.366 1.00 20.53 ?  22  ASP   B HB3  1 
ATOM   4373 N  N    . ILE   B 1 23  ? 50.653 -26.698 -8.393  1.00 13.62 ?  23  ILE   B N    1 
ATOM   4374 C  CA   . ILE   B 1 23  ? 50.058 -25.358 -8.456  1.00 12.81 ?  23  ILE   B CA   1 
ATOM   4375 C  C    . ILE   B 1 23  ? 51.113 -24.267 -8.594  1.00 12.59 ?  23  ILE   B C    1 
ATOM   4376 O  O    . ILE   B 1 23  ? 50.847 -23.222 -9.195  1.00 12.20 ?  23  ILE   B O    1 
ATOM   4377 C  CB   . ILE   B 1 23  ? 49.121 -25.115 -7.258  1.00 13.20 ?  23  ILE   B CB   1 
ATOM   4378 C  CG1  . ILE   B 1 23  ? 48.295 -23.844 -7.464  1.00 14.02 ?  23  ILE   B CG1  1 
ATOM   4379 C  CG2  . ILE   B 1 23  ? 49.895 -25.070 -5.954  1.00 14.34 ?  23  ILE   B CG2  1 
ATOM   4380 C  CD1  . ILE   B 1 23  ? 47.160 -23.689 -6.473  1.00 14.88 ?  23  ILE   B CD1  1 
ATOM   4381 H  H    . ILE   B 1 23  ? 50.504 -27.120 -7.660  1.00 16.48 ?  23  ILE   B H    1 
ATOM   4382 H  HA   . ILE   B 1 23  ? 49.511 -25.317 -9.252  1.00 15.52 ?  23  ILE   B HA   1 
ATOM   4383 H  HB   . ILE   B 1 23  ? 48.501 -25.861 -7.212  1.00 15.98 ?  23  ILE   B HB   1 
ATOM   4384 H  HG12 . ILE   B 1 23  ? 48.881 -23.071 -7.368  1.00 16.96 ?  23  ILE   B HG12 1 
ATOM   4385 H  HG13 . ILE   B 1 23  ? 47.916 -23.853 -8.359  1.00 16.96 ?  23  ILE   B HG13 1 
ATOM   4386 H  HG21 . ILE   B 1 23  ? 49.270 -25.066 -5.214  1.00 17.35 ?  23  ILE   B HG21 1 
ATOM   4387 H  HG22 . ILE   B 1 23  ? 50.465 -25.854 -5.900  1.00 17.35 ?  23  ILE   B HG22 1 
ATOM   4388 H  HG23 . ILE   B 1 23  ? 50.438 -24.267 -5.936  1.00 17.35 ?  23  ILE   B HG23 1 
ATOM   4389 H  HD11 . ILE   B 1 23  ? 46.644 -22.903 -6.705  1.00 18.00 ?  23  ILE   B HD11 1 
ATOM   4390 H  HD12 . ILE   B 1 23  ? 46.598 -24.481 -6.522  1.00 18.00 ?  23  ILE   B HD12 1 
ATOM   4391 H  HD13 . ILE   B 1 23  ? 47.529 -23.599 -5.584  1.00 18.00 ?  23  ILE   B HD13 1 
ATOM   4392 N  N    . VAL   B 1 24  ? 52.312 -24.477 -8.043  1.00 12.84 ?  24  VAL   B N    1 
ATOM   4393 C  CA   . VAL   B 1 24  ? 53.389 -23.499 -8.210  1.00 13.36 ?  24  VAL   B CA   1 
ATOM   4394 C  C    . VAL   B 1 24  ? 53.842 -23.453 -9.663  1.00 13.58 ?  24  VAL   B C    1 
ATOM   4395 O  O    . VAL   B 1 24  ? 53.990 -22.375 -10.256 1.00 13.91 ?  24  VAL   B O    1 
ATOM   4396 C  CB   . VAL   B 1 24  ? 54.566 -23.817 -7.267  1.00 14.29 ?  24  VAL   B CB   1 
ATOM   4397 C  CG1  . VAL   B 1 24  ? 55.770 -22.945 -7.602  1.00 14.99 ?  24  VAL   B CG1  1 
ATOM   4398 C  CG2  . VAL   B 1 24  ? 54.158 -23.613 -5.827  1.00 15.41 ?  24  VAL   B CG2  1 
ATOM   4399 H  H    . VAL   B 1 24  ? 52.524 -25.162 -7.572  1.00 15.55 ?  24  VAL   B H    1 
ATOM   4400 H  HA   . VAL   B 1 24  ? 53.057 -22.622 -7.976  1.00 16.17 ?  24  VAL   B HA   1 
ATOM   4401 H  HB   . VAL   B 1 24  ? 54.827 -24.746 -7.374  1.00 17.29 ?  24  VAL   B HB   1 
ATOM   4402 H  HG11 . VAL   B 1 24  ? 56.368 -22.931 -6.839  1.00 18.12 ?  24  VAL   B HG11 1 
ATOM   4403 H  HG12 . VAL   B 1 24  ? 56.222 -23.315 -8.372  1.00 18.12 ?  24  VAL   B HG12 1 
ATOM   4404 H  HG13 . VAL   B 1 24  ? 55.459 -22.046 -7.793  1.00 18.12 ?  24  VAL   B HG13 1 
ATOM   4405 H  HG21 . VAL   B 1 24  ? 54.891 -23.868 -5.248  1.00 18.63 ?  24  VAL   B HG21 1 
ATOM   4406 H  HG22 . VAL   B 1 24  ? 53.940 -22.676 -5.693  1.00 18.63 ?  24  VAL   B HG22 1 
ATOM   4407 H  HG23 . VAL   B 1 24  ? 53.380 -24.163 -5.639  1.00 18.63 ?  24  VAL   B HG23 1 
ATOM   4408 N  N    . GLU   B 1 25  ? 54.100 -24.625 -10.250 1.00 14.72 ?  25  GLU   B N    1 
ATOM   4409 C  CA   . GLU   B 1 25  ? 54.490 -24.663 -11.654 1.00 16.21 ?  25  GLU   B CA   1 
ATOM   4410 C  C    . GLU   B 1 25  ? 53.380 -24.117 -12.537 1.00 15.06 ?  25  GLU   B C    1 
ATOM   4411 O  O    . GLU   B 1 25  ? 53.645 -23.403 -13.514 1.00 15.99 ?  25  GLU   B O    1 
ATOM   4412 C  CB   . GLU   B 1 25  ? 54.875 -26.087 -12.051 1.00 20.44 ?  25  GLU   B CB   1 
ATOM   4413 C  CG   . GLU   B 1 25  ? 56.177 -26.543 -11.408 1.00 25.86 ?  25  GLU   B CG   1 
ATOM   4414 C  CD   . GLU   B 1 25  ? 57.282 -25.497 -11.479 1.00 30.83 ?  25  GLU   B CD   1 
ATOM   4415 O  OE1  . GLU   B 1 25  ? 57.681 -25.119 -12.601 1.00 32.80 ?  25  GLU   B OE1  1 
ATOM   4416 O  OE2  . GLU   B 1 25  ? 57.736 -25.032 -10.408 1.00 32.66 -1 25  GLU   B OE2  1 
ATOM   4417 H  H    . GLU   B 1 25  ? 54.051 -25.394 -9.864  1.00 17.80 ?  25  GLU   B H    1 
ATOM   4418 H  HA   . GLU   B 1 25  ? 55.250 -24.081 -11.780 1.00 19.59 ?  25  GLU   B HA   1 
ATOM   4419 H  HB2  . GLU   B 1 25  ? 54.173 -26.698 -11.767 1.00 24.67 ?  25  GLU   B HB2  1 
ATOM   4420 H  HB3  . GLU   B 1 25  ? 54.979 -26.130 -13.014 1.00 24.67 ?  25  GLU   B HB3  1 
ATOM   4421 H  HG2  . GLU   B 1 25  ? 56.024 -26.715 -10.472 1.00 31.17 ?  25  GLU   B HG2  1 
ATOM   4422 H  HG3  . GLU   B 1 25  ? 56.484 -27.344 -11.858 1.00 31.17 ?  25  GLU   B HG3  1 
ATOM   4423 N  N    A GLU   B 1 26  ? 52.128 -24.426 -12.197 0.74 14.17 ?  26  GLU   B N    1 
ATOM   4424 N  N    B GLU   B 1 26  ? 52.126 -24.430 -12.201 0.26 14.68 ?  26  GLU   B N    1 
ATOM   4425 C  CA   A GLU   B 1 26  ? 51.001 -23.903 -12.959 0.74 14.71 ?  26  GLU   B CA   1 
ATOM   4426 C  CA   B GLU   B 1 26  ? 50.999 -23.901 -12.963 0.26 14.90 ?  26  GLU   B CA   1 
ATOM   4427 C  C    A GLU   B 1 26  ? 50.951 -22.385 -12.886 0.74 13.84 ?  26  GLU   B C    1 
ATOM   4428 C  C    B GLU   B 1 26  ? 50.958 -22.382 -12.888 0.26 13.86 ?  26  GLU   B C    1 
ATOM   4429 O  O    A GLU   B 1 26  ? 50.752 -21.711 -13.900 0.74 14.97 ?  26  GLU   B O    1 
ATOM   4430 O  O    B GLU   B 1 26  ? 50.786 -21.703 -13.906 0.26 14.27 ?  26  GLU   B O    1 
ATOM   4431 C  CB   A GLU   B 1 26  ? 49.690 -24.488 -12.431 0.74 16.74 ?  26  GLU   B CB   1 
ATOM   4432 C  CB   B GLU   B 1 26  ? 49.688 -24.489 -12.441 0.26 16.39 ?  26  GLU   B CB   1 
ATOM   4433 C  CG   A GLU   B 1 26  ? 49.282 -25.790 -13.073 0.74 20.07 ?  26  GLU   B CG   1 
ATOM   4434 C  CG   B GLU   B 1 26  ? 49.271 -25.774 -13.122 0.26 18.39 ?  26  GLU   B CG   1 
ATOM   4435 C  CD   A GLU   B 1 26  ? 49.025 -25.649 -14.571 0.74 22.08 ?  26  GLU   B CD   1 
ATOM   4436 C  CD   B GLU   B 1 26  ? 48.998 -25.597 -14.608 0.26 19.78 ?  26  GLU   B CD   1 
ATOM   4437 O  OE1  A GLU   B 1 26  ? 48.086 -24.931 -14.977 0.74 22.33 ?  26  GLU   B OE1  1 
ATOM   4438 O  OE1  B GLU   B 1 26  ? 48.037 -24.885 -14.969 0.26 20.15 ?  26  GLU   B OE1  1 
ATOM   4439 O  OE2  A GLU   B 1 26  ? 49.769 -26.267 -15.346 0.74 23.95 -1 26  GLU   B OE2  1 
ATOM   4440 O  OE2  B GLU   B 1 26  ? 49.748 -26.174 -15.417 0.26 20.89 -1 26  GLU   B OE2  1 
ATOM   4441 H  H    A GLU   B 1 26  ? 51.904 -24.937 -11.539 0.74 17.15 ?  26  GLU   B H    1 
ATOM   4442 H  H    B GLU   B 1 26  ? 51.904 -24.940 -11.543 0.26 17.76 ?  26  GLU   B H    1 
ATOM   4443 H  HA   A GLU   B 1 26  ? 51.099 -24.156 -13.889 0.74 17.80 ?  26  GLU   B HA   1 
ATOM   4444 H  HA   B GLU   B 1 26  ? 51.100 -24.152 -13.892 0.26 18.02 ?  26  GLU   B HA   1 
ATOM   4445 H  HB2  A GLU   B 1 26  ? 49.780 -24.641 -11.478 0.74 20.23 ?  26  GLU   B HB2  1 
ATOM   4446 H  HB2  B GLU   B 1 26  ? 49.782 -24.676 -11.492 0.26 19.81 ?  26  GLU   B HB2  1 
ATOM   4447 H  HB3  A GLU   B 1 26  ? 48.978 -23.846 -12.592 0.74 20.23 ?  26  GLU   B HB3  1 
ATOM   4448 H  HB3  B GLU   B 1 26  ? 48.978 -23.841 -12.575 0.26 19.81 ?  26  GLU   B HB3  1 
ATOM   4449 H  HG2  A GLU   B 1 26  ? 49.993 -26.435 -12.932 0.74 24.22 ?  26  GLU   B HG2  1 
ATOM   4450 H  HG2  B GLU   B 1 26  ? 49.979 -26.424 -13.006 0.26 22.21 ?  26  GLU   B HG2  1 
ATOM   4451 H  HG3  A GLU   B 1 26  ? 48.463 -26.101 -12.658 0.74 24.22 ?  26  GLU   B HG3  1 
ATOM   4452 H  HG3  B GLU   B 1 26  ? 48.452 -26.091 -12.715 0.26 22.21 ?  26  GLU   B HG3  1 
ATOM   4453 N  N    . ALA   B 1 27  ? 51.102 -21.831 -11.682 1.00 12.93 ?  27  ALA   B N    1 
ATOM   4454 C  CA   . ALA   B 1 27  ? 51.068 -20.382 -11.532 1.00 13.31 ?  27  ALA   B CA   1 
ATOM   4455 C  C    . ALA   B 1 27  ? 52.140 -19.722 -12.389 1.00 14.21 ?  27  ALA   B C    1 
ATOM   4456 O  O    . ALA   B 1 27  ? 51.880 -18.721 -13.071 1.00 14.86 ?  27  ALA   B O    1 
ATOM   4457 C  CB   . ALA   B 1 27  ? 51.228 -20.008 -10.059 1.00 13.42 ?  27  ALA   B CB   1 
ATOM   4458 H  H    A ALA   B 1 27  ? 51.211 -22.268 -10.949 0.74 15.65 ?  27  ALA   B H    1 
ATOM   4459 H  H    B ALA   B 1 27  ? 51.212 -22.268 -10.949 0.26 15.65 ?  27  ALA   B H    1 
ATOM   4460 H  HA   . ALA   B 1 27  ? 50.208 -20.051 -11.827 1.00 16.12 ?  27  ALA   B HA   1 
ATOM   4461 H  HB1  . ALA   B 1 27  ? 51.199 -19.042 -9.971  1.00 16.25 ?  27  ALA   B HB1  1 
ATOM   4462 H  HB2  . ALA   B 1 27  ? 50.498 -20.405 -9.551  1.00 16.25 ?  27  ALA   B HB2  1 
ATOM   4463 H  HB3  . ALA   B 1 27  ? 52.075 -20.346 -9.733  1.00 16.25 ?  27  ALA   B HB3  1 
ATOM   4464 N  N    . LYS   B 1 28  ? 53.354 -20.276 -12.382 1.00 15.79 ?  28  LYS   B N    1 
ATOM   4465 C  CA   . LYS   B 1 28  ? 54.429 -19.666 -13.154 1.00 17.90 ?  28  LYS   B CA   1 
ATOM   4466 C  C    . LYS   B 1 28  ? 54.170 -19.750 -14.652 1.00 18.72 ?  28  LYS   B C    1 
ATOM   4467 O  O    . LYS   B 1 28  ? 54.580 -18.852 -15.398 1.00 19.69 ?  28  LYS   B O    1 
ATOM   4468 C  CB   . LYS   B 1 28  ? 55.782 -20.272 -12.767 1.00 20.64 ?  28  LYS   B CB   1 
ATOM   4469 C  CG   . LYS   B 1 28  ? 56.196 -19.905 -11.346 1.00 23.91 ?  28  LYS   B CG   1 
ATOM   4470 C  CD   . LYS   B 1 28  ? 57.633 -20.277 -11.017 1.00 28.36 ?  28  LYS   B CD   1 
ATOM   4471 C  CE   . LYS   B 1 28  ? 57.762 -21.732 -10.638 1.00 31.84 ?  28  LYS   B CE   1 
ATOM   4472 N  NZ   . LYS   B 1 28  ? 59.114 -22.031 -10.088 1.00 33.31 ?  28  LYS   B NZ   1 
ATOM   4473 H  H    . LYS   B 1 28  ? 53.577 -20.986 -11.947 1.00 19.08 ?  28  LYS   B H    1 
ATOM   4474 H  HA   . LYS   B 1 28  ? 54.467 -18.727 -12.935 1.00 21.62 ?  28  LYS   B HA   1 
ATOM   4475 H  HB2  . LYS   B 1 28  ? 55.729 -21.237 -12.825 1.00 24.90 ?  28  LYS   B HB2  1 
ATOM   4476 H  HB3  . LYS   B 1 28  ? 56.464 -19.938 -13.374 1.00 24.90 ?  28  LYS   B HB3  1 
ATOM   4477 H  HG2  . LYS   B 1 28  ? 56.100 -18.944 -11.233 1.00 28.83 ?  28  LYS   B HG2  1 
ATOM   4478 H  HG3  . LYS   B 1 28  ? 55.615 -20.368 -10.724 1.00 28.83 ?  28  LYS   B HG3  1 
ATOM   4479 H  HD2  . LYS   B 1 28  ? 58.189 -20.112 -11.795 1.00 34.17 ?  28  LYS   B HD2  1 
ATOM   4480 H  HD3  . LYS   B 1 28  ? 57.935 -19.736 -10.270 1.00 34.17 ?  28  LYS   B HD3  1 
ATOM   4481 H  HE2  . LYS   B 1 28  ? 57.103 -21.946 -9.958  1.00 38.35 ?  28  LYS   B HE2  1 
ATOM   4482 H  HE3  . LYS   B 1 28  ? 57.624 -22.283 -11.424 1.00 38.35 ?  28  LYS   B HE3  1 
ATOM   4483 H  HZ1  . LYS   B 1 28  ? 59.171 -22.891 -9.869  1.00 40.11 ?  28  LYS   B HZ1  1 
ATOM   4484 H  HZ2  . LYS   B 1 28  ? 59.737 -21.844 -10.695 1.00 40.11 ?  28  LYS   B HZ2  1 
ATOM   4485 H  HZ3  . LYS   B 1 28  ? 59.262 -21.538 -9.361  1.00 40.11 ?  28  LYS   B HZ3  1 
ATOM   4486 N  N    . LYS   B 1 29  ? 53.461 -20.784 -15.107 1.00 20.02 ?  29  LYS   B N    1 
ATOM   4487 C  CA   . LYS   B 1 29  ? 53.183 -20.931 -16.531 1.00 23.05 ?  29  LYS   B CA   1 
ATOM   4488 C  C    . LYS   B 1 29  ? 51.927 -20.182 -16.972 1.00 21.65 ?  29  LYS   B C    1 
ATOM   4489 O  O    . LYS   B 1 29  ? 51.915 -19.587 -18.055 1.00 22.79 ?  29  LYS   B O    1 
ATOM   4490 C  CB   . LYS   B 1 29  ? 53.059 -22.413 -16.888 1.00 28.03 ?  29  LYS   B CB   1 
ATOM   4491 C  CG   . LYS   B 1 29  ? 52.931 -22.685 -18.378 1.00 32.70 ?  29  LYS   B CG   1 
ATOM   4492 C  CD   . LYS   B 1 29  ? 53.190 -24.154 -18.697 1.00 36.50 ?  29  LYS   B CD   1 
ATOM   4493 C  CE   . LYS   B 1 29  ? 52.102 -25.059 -18.140 1.00 39.10 ?  29  LYS   B CE   1 
ATOM   4494 N  NZ   . LYS   B 1 29  ? 52.378 -26.498 -18.424 1.00 40.41 ?  29  LYS   B NZ   1 
ATOM   4495 H  H    . LYS   B 1 29  ? 53.120 -21.410 -14.609 1.00 24.16 ?  29  LYS   B H    1 
ATOM   4496 H  HA   . LYS   B 1 29  ? 53.930 -20.570 -17.025 1.00 27.80 ?  29  LYS   B HA   1 
ATOM   4497 H  HB2  . LYS   B 1 29  ? 53.855 -22.872 -16.574 1.00 33.78 ?  29  LYS   B HB2  1 
ATOM   4498 H  HB3  . LYS   B 1 29  ? 52.276 -22.775 -16.453 1.00 33.78 ?  29  LYS   B HB3  1 
ATOM   4499 H  HG2  . LYS   B 1 29  ? 52.031 -22.463 -18.665 1.00 39.38 ?  29  LYS   B HG2  1 
ATOM   4500 H  HG3  . LYS   B 1 29  ? 53.580 -22.147 -18.860 1.00 39.38 ?  29  LYS   B HG3  1 
ATOM   4501 H  HD2  . LYS   B 1 29  ? 53.219 -24.272 -19.659 1.00 43.94 ?  29  LYS   B HD2  1 
ATOM   4502 H  HD3  . LYS   B 1 29  ? 54.036 -24.422 -18.302 1.00 43.94 ?  29  LYS   B HD3  1 
ATOM   4503 H  HE2  . LYS   B 1 29  ? 52.050 -24.946 -17.178 1.00 47.06 ?  29  LYS   B HE2  1 
ATOM   4504 H  HE3  . LYS   B 1 29  ? 51.253 -24.827 -18.550 1.00 47.06 ?  29  LYS   B HE3  1 
ATOM   4505 H  HZ1  . LYS   B 1 29  ? 51.727 -27.005 -18.089 1.00 48.63 ?  29  LYS   B HZ1  1 
ATOM   4506 H  HZ2  . LYS   B 1 29  ? 52.425 -26.632 -19.303 1.00 48.63 ?  29  LYS   B HZ2  1 
ATOM   4507 H  HZ3  . LYS   B 1 29  ? 53.151 -26.739 -18.053 1.00 48.63 ?  29  LYS   B HZ3  1 
ATOM   4508 N  N    . VAL   B 1 30  ? 50.871 -20.210 -16.153 1.00 19.72 ?  30  VAL   B N    1 
ATOM   4509 C  CA   . VAL   B 1 30  ? 49.582 -19.620 -16.522 1.00 19.88 ?  30  VAL   B CA   1 
ATOM   4510 C  C    . VAL   B 1 30  ? 49.586 -18.104 -16.379 1.00 18.67 ?  30  VAL   B C    1 
ATOM   4511 O  O    . VAL   B 1 30  ? 48.844 -17.402 -17.083 1.00 19.48 ?  30  VAL   B O    1 
ATOM   4512 C  CB   . VAL   B 1 30  ? 48.477 -20.237 -15.641 1.00 20.79 ?  30  VAL   B CB   1 
ATOM   4513 C  CG1  . VAL   B 1 30  ? 47.193 -19.427 -15.721 1.00 21.22 ?  30  VAL   B CG1  1 
ATOM   4514 C  CG2  . VAL   B 1 30  ? 48.229 -21.690 -16.030 1.00 21.48 ?  30  VAL   B CG2  1 
ATOM   4515 H  H    . VAL   B 1 30  ? 50.868 -20.586 -15.373 1.00 23.80 ?  30  VAL   B H    1 
ATOM   4516 H  HA   . VAL   B 1 30  ? 49.381 -19.850 -17.441 1.00 24.00 ?  30  VAL   B HA   1 
ATOM   4517 H  HB   . VAL   B 1 30  ? 48.768 -20.234 -14.715 1.00 25.09 ?  30  VAL   B HB   1 
ATOM   4518 H  HG11 . VAL   B 1 30  ? 46.450 -20.008 -15.491 1.00 25.60 ?  30  VAL   B HG11 1 
ATOM   4519 H  HG12 . VAL   B 1 30  ? 47.239 -18.693 -15.092 1.00 25.60 ?  30  VAL   B HG12 1 
ATOM   4520 H  HG13 . VAL   B 1 30  ? 47.078 -19.101 -16.622 1.00 25.60 ?  30  VAL   B HG13 1 
ATOM   4521 H  HG21 . VAL   B 1 30  ? 47.540 -22.064 -15.451 1.00 25.92 ?  30  VAL   B HG21 1 
ATOM   4522 H  HG22 . VAL   B 1 30  ? 47.929 -21.724 -16.954 1.00 25.92 ?  30  VAL   B HG22 1 
ATOM   4523 H  HG23 . VAL   B 1 30  ? 49.050 -22.192 -15.929 1.00 25.92 ?  30  VAL   B HG23 1 
ATOM   4524 N  N    . LYS   B 1 31  ? 50.370 -17.591 -15.444 1.00 18.09 ?  31  LYS   B N    1 
ATOM   4525 C  CA   . LYS   B 1 31  ? 50.398 -16.182 -15.082 1.00 18.52 ?  31  LYS   B CA   1 
ATOM   4526 C  C    . LYS   B 1 31  ? 48.997 -15.709 -14.696 1.00 16.30 ?  31  LYS   B C    1 
ATOM   4527 O  O    . LYS   B 1 31  ? 48.458 -14.788 -15.322 1.00 17.23 ?  31  LYS   B O    1 
ATOM   4528 C  CB   . LYS   B 1 31  ? 51.032 -15.364 -16.212 1.00 21.52 ?  31  LYS   B CB   1 
ATOM   4529 C  CG   . LYS   B 1 31  ? 52.465 -15.801 -16.525 1.00 24.69 ?  31  LYS   B CG   1 
ATOM   4530 C  CD   . LYS   B 1 31  ? 53.038 -15.041 -17.701 1.00 27.99 ?  31  LYS   B CD   1 
ATOM   4531 C  CE   . LYS   B 1 31  ? 54.514 -15.314 -17.865 1.00 30.41 ?  31  LYS   B CE   1 
ATOM   4532 N  NZ   . LYS   B 1 31  ? 55.259 -14.954 -16.627 1.00 31.56 ?  31  LYS   B NZ   1 
ATOM   4533 H  H    . LYS   B 1 31  ? 50.915 -18.073 -14.990 1.00 21.85 ?  31  LYS   B H    1 
ATOM   4534 H  HA   . LYS   B 1 31  ? 50.953 -16.088 -14.306 1.00 22.36 ?  31  LYS   B HA   1 
ATOM   4535 H  HB2  . LYS   B 1 31  ? 50.506 -15.469 -17.020 1.00 25.96 ?  31  LYS   B HB2  1 
ATOM   4536 H  HB3  . LYS   B 1 31  ? 51.055 -14.434 -15.946 1.00 25.96 ?  31  LYS   B HB3  1 
ATOM   4537 H  HG2  . LYS   B 1 31  ? 53.020 -15.636 -15.747 1.00 29.77 ?  31  LYS   B HG2  1 
ATOM   4538 H  HG3  . LYS   B 1 31  ? 52.473 -16.749 -16.743 1.00 29.77 ?  31  LYS   B HG3  1 
ATOM   4539 H  HD2  . LYS   B 1 31  ? 52.582 -15.322 -18.509 1.00 33.72 ?  31  LYS   B HD2  1 
ATOM   4540 H  HD3  . LYS   B 1 31  ? 52.915 -14.093 -17.553 1.00 33.72 ?  31  LYS   B HD3  1 
ATOM   4541 H  HE2  . LYS   B 1 31  ? 54.652 -16.259 -18.043 1.00 36.64 ?  31  LYS   B HE2  1 
ATOM   4542 H  HE3  . LYS   B 1 31  ? 54.859 -14.779 -18.597 1.00 36.64 ?  31  LYS   B HE3  1 
ATOM   4543 H  HZ1  . LYS   B 1 31  ? 56.133 -14.958 -16.786 1.00 38.01 ?  31  LYS   B HZ1  1 
ATOM   4544 H  HZ2  . LYS   B 1 31  ? 55.016 -14.143 -16.353 1.00 38.01 ?  31  LYS   B HZ2  1 
ATOM   4545 H  HZ3  . LYS   B 1 31  ? 55.079 -15.542 -15.983 1.00 38.01 ?  31  LYS   B HZ3  1 
ATOM   4546 N  N    . PRO   B 1 32  ? 48.385 -16.305 -13.667 1.00 14.26 ?  32  PRO   B N    1 
ATOM   4547 C  CA   . PRO   B 1 32  ? 47.008 -15.942 -13.308 1.00 13.34 ?  32  PRO   B CA   1 
ATOM   4548 C  C    . PRO   B 1 32  ? 46.931 -14.596 -12.605 1.00 13.42 ?  32  PRO   B C    1 
ATOM   4549 O  O    . PRO   B 1 32  ? 47.855 -14.179 -11.901 1.00 14.71 ?  32  PRO   B O    1 
ATOM   4550 C  CB   . PRO   B 1 32  ? 46.606 -17.057 -12.336 1.00 13.56 ?  32  PRO   B CB   1 
ATOM   4551 C  CG   . PRO   B 1 32  ? 47.901 -17.392 -11.651 1.00 14.00 ?  32  PRO   B CG   1 
ATOM   4552 C  CD   . PRO   B 1 32  ? 48.952 -17.295 -12.730 1.00 14.15 ?  32  PRO   B CD   1 
ATOM   4553 H  HA   . PRO   B 1 32  ? 46.424 -15.955 -14.086 1.00 16.15 ?  32  PRO   B HA   1 
ATOM   4554 H  HB2  . PRO   B 1 32  ? 45.951 -16.725 -11.698 1.00 16.41 ?  32  PRO   B HB2  1 
ATOM   4555 H  HB3  . PRO   B 1 32  ? 46.263 -17.822 -12.821 1.00 16.41 ?  32  PRO   B HB3  1 
ATOM   4556 H  HG2  . PRO   B 1 32  ? 48.074 -16.747 -10.942 1.00 16.94 ?  32  PRO   B HG2  1 
ATOM   4557 H  HG3  . PRO   B 1 32  ? 47.860 -18.291 -11.288 1.00 16.94 ?  32  PRO   B HG3  1 
ATOM   4558 H  HD2  . PRO   B 1 32  ? 49.783 -16.971 -12.364 1.00 17.12 ?  32  PRO   B HD2  1 
ATOM   4559 H  HD3  . PRO   B 1 32  ? 49.054 -18.150 -13.171 1.00 17.12 ?  32  PRO   B HD3  1 
ATOM   4560 N  N    . THR   B 1 33  ? 45.784 -13.935 -12.776 1.00 13.05 ?  33  THR   B N    1 
ATOM   4561 C  CA   . THR   B 1 33  ? 45.488 -12.760 -11.967 1.00 13.41 ?  33  THR   B CA   1 
ATOM   4562 C  C    . THR   B 1 33  ? 45.441 -13.112 -10.485 1.00 12.99 ?  33  THR   B C    1 
ATOM   4563 O  O    . THR   B 1 33  ? 45.917 -12.334 -9.644  1.00 13.94 ?  33  THR   B O    1 
ATOM   4564 C  CB   . THR   B 1 33  ? 44.172 -12.120 -12.418 1.00 13.96 ?  33  THR   B CB   1 
ATOM   4565 O  OG1  . THR   B 1 33  ? 44.215 -11.875 -13.824 1.00 13.89 ?  33  THR   B OG1  1 
ATOM   4566 C  CG2  . THR   B 1 33  ? 43.929 -10.816 -11.682 1.00 15.15 ?  33  THR   B CG2  1 
ATOM   4567 H  H    . THR   B 1 33  ? 45.165 -14.151 -13.340 1.00 15.80 ?  33  THR   B H    1 
ATOM   4568 H  HA   . THR   B 1 33  ? 46.192 -12.112 -12.093 1.00 16.23 ?  33  THR   B HA   1 
ATOM   4569 H  HB   . THR   B 1 33  ? 43.435 -12.724 -12.223 1.00 16.90 ?  33  THR   B HB   1 
ATOM   4570 H  HG1  . THR   B 1 33  ? 43.501 -11.504 -14.076 1.00 16.81 ?  33  THR   B HG1  1 
ATOM   4571 H  HG21 . THR   B 1 33  ? 43.173 -10.352 -12.070 1.00 18.32 ?  33  THR   B HG21 1 
ATOM   4572 H  HG22 . THR   B 1 33  ? 43.746 -10.989 -10.745 1.00 18.32 ?  33  THR   B HG22 1 
ATOM   4573 H  HG23 . THR   B 1 33  ? 44.715 -10.249 -11.749 1.00 18.32 ?  33  THR   B HG23 1 
ATOM   4574 N  N    . VAL   B 1 34  ? 44.889 -14.283 -10.145 1.00 12.23 ?  34  VAL   B N    1 
ATOM   4575 C  CA   . VAL   B 1 34  ? 44.687 -14.680 -8.753  1.00 11.89 ?  34  VAL   B CA   1 
ATOM   4576 C  C    . VAL   B 1 34  ? 45.119 -16.129 -8.585  1.00 10.86 ?  34  VAL   B C    1 
ATOM   4577 O  O    . VAL   B 1 34  ? 44.593 -17.019 -9.265  1.00 11.47 ?  34  VAL   B O    1 
ATOM   4578 C  CB   . VAL   B 1 34  ? 43.218 -14.539 -8.310  1.00 12.70 ?  34  VAL   B CB   1 
ATOM   4579 C  CG1  . VAL   B 1 34  ? 43.052 -14.982 -6.863  1.00 13.16 ?  34  VAL   B CG1  1 
ATOM   4580 C  CG2  . VAL   B 1 34  ? 42.717 -13.121 -8.504  1.00 13.59 ?  34  VAL   B CG2  1 
ATOM   4581 H  H    . VAL   B 1 34  ? 44.630 -14.878 -10.711 1.00 14.82 ?  34  VAL   B H    1 
ATOM   4582 H  HA   . VAL   B 1 34  ? 45.236 -14.126 -8.173  1.00 14.41 ?  34  VAL   B HA   1 
ATOM   4583 H  HB   . VAL   B 1 34  ? 42.671 -15.121 -8.862  1.00 15.38 ?  34  VAL   B HB   1 
ATOM   4584 H  HG11 . VAL   B 1 34  ? 42.193 -14.669 -6.533  1.00 15.93 ?  34  VAL   B HG11 1 
ATOM   4585 H  HG12 . VAL   B 1 34  ? 43.083 -15.952 -6.820  1.00 15.93 ?  34  VAL   B HG12 1 
ATOM   4586 H  HG13 . VAL   B 1 34  ? 43.767 -14.603 -6.331  1.00 15.93 ?  34  VAL   B HG13 1 
ATOM   4587 H  HG21 . VAL   B 1 34  ? 41.796 -13.064 -8.196  1.00 16.45 ?  34  VAL   B HG21 1 
ATOM   4588 H  HG22 . VAL   B 1 34  ? 43.273 -12.514 -7.994  1.00 16.45 ?  34  VAL   B HG22 1 
ATOM   4589 H  HG23 . VAL   B 1 34  ? 42.759 -12.895 -9.449  1.00 16.45 ?  34  VAL   B HG23 1 
ATOM   4590 N  N    . VAL   B 1 35  ? 46.028 -16.378 -7.645  1.00 10.33 ?  35  VAL   B N    1 
ATOM   4591 C  CA   . VAL   B 1 35  ? 46.259 -17.721 -7.127  1.00 10.03 ?  35  VAL   B CA   1 
ATOM   4592 C  C    . VAL   B 1 35  ? 45.724 -17.776 -5.706  1.00 9.82  ?  35  VAL   B C    1 
ATOM   4593 O  O    . VAL   B 1 35  ? 45.946 -16.850 -4.918  1.00 10.29 ?  35  VAL   B O    1 
ATOM   4594 C  CB   . VAL   B 1 35  ? 47.740 -18.147 -7.212  1.00 10.95 ?  35  VAL   B CB   1 
ATOM   4595 C  CG1  . VAL   B 1 35  ? 48.640 -17.307 -6.295  1.00 11.83 ?  35  VAL   B CG1  1 
ATOM   4596 C  CG2  . VAL   B 1 35  ? 47.880 -19.638 -6.890  1.00 11.54 ?  35  VAL   B CG2  1 
ATOM   4597 H  H    . VAL   B 1 35  ? 46.530 -15.777 -7.287  1.00 12.54 ?  35  VAL   B H    1 
ATOM   4598 H  HA   . VAL   B 1 35  ? 45.738 -18.350 -7.653  1.00 12.18 ?  35  VAL   B HA   1 
ATOM   4599 H  HB   . VAL   B 1 35  ? 48.045 -18.024 -8.125  1.00 13.28 ?  35  VAL   B HB   1 
ATOM   4600 H  HG11 . VAL   B 1 35  ? 49.563 -17.533 -6.480  1.00 14.33 ?  35  VAL   B HG11 1 
ATOM   4601 H  HG12 . VAL   B 1 35  ? 48.474 -16.376 -6.470  1.00 14.33 ?  35  VAL   B HG12 1 
ATOM   4602 H  HG13 . VAL   B 1 35  ? 48.424 -17.523 -5.372  1.00 14.33 ?  35  VAL   B HG13 1 
ATOM   4603 H  HG21 . VAL   B 1 35  ? 48.799 -19.909 -7.006  1.00 13.99 ?  35  VAL   B HG21 1 
ATOM   4604 H  HG22 . VAL   B 1 35  ? 47.599 -19.795 -5.972  1.00 13.99 ?  35  VAL   B HG22 1 
ATOM   4605 H  HG23 . VAL   B 1 35  ? 47.306 -20.152 -7.492  1.00 13.99 ?  35  VAL   B HG23 1 
ATOM   4606 N  N    . VAL   B 1 36  ? 45.000 -18.849 -5.388  1.00 9.79  ?  36  VAL   B N    1 
ATOM   4607 C  CA   . VAL   B 1 36  ? 44.454 -19.052 -4.057  1.00 9.71  ?  36  VAL   B CA   1 
ATOM   4608 C  C    . VAL   B 1 36  ? 45.463 -19.814 -3.204  1.00 9.42  ?  36  VAL   B C    1 
ATOM   4609 O  O    . VAL   B 1 36  ? 46.008 -20.844 -3.626  1.00 10.65 ?  36  VAL   B O    1 
ATOM   4610 C  CB   . VAL   B 1 36  ? 43.115 -19.811 -4.130  1.00 10.14 ?  36  VAL   B CB   1 
ATOM   4611 C  CG1  . VAL   B 1 36  ? 42.617 -20.182 -2.737  1.00 10.94 ?  36  VAL   B CG1  1 
ATOM   4612 C  CG2  . VAL   B 1 36  ? 42.081 -18.972 -4.858  1.00 10.73 ?  36  VAL   B CG2  1 
ATOM   4613 H  H    . VAL   B 1 36  ? 44.813 -19.480 -5.941  1.00 11.89 ?  36  VAL   B H    1 
ATOM   4614 H  HA   . VAL   B 1 36  ? 44.290 -18.191 -3.641  1.00 11.79 ?  36  VAL   B HA   1 
ATOM   4615 H  HB   . VAL   B 1 36  ? 43.240 -20.631 -4.632  1.00 12.31 ?  36  VAL   B HB   1 
ATOM   4616 H  HG11 . VAL   B 1 36  ? 41.679 -20.416 -2.790  1.00 13.27 ?  36  VAL   B HG11 1 
ATOM   4617 H  HG12 . VAL   B 1 36  ? 43.130 -20.932 -2.405  1.00 13.27 ?  36  VAL   B HG12 1 
ATOM   4618 H  HG13 . VAL   B 1 36  ? 42.731 -19.414 -2.150  1.00 13.27 ?  36  VAL   B HG13 1 
ATOM   4619 H  HG21 . VAL   B 1 36  ? 41.239 -19.450 -4.882  1.00 13.02 ?  36  VAL   B HG21 1 
ATOM   4620 H  HG22 . VAL   B 1 36  ? 41.968 -18.128 -4.388  1.00 13.02 ?  36  VAL   B HG22 1 
ATOM   4621 H  HG23 . VAL   B 1 36  ? 42.390 -18.801 -5.764  1.00 13.02 ?  36  VAL   B HG23 1 
ATOM   4622 N  N    . ASN   B 1 37  ? 45.679 -19.325 -1.986  1.00 9.75  ?  37  ASN   B N    1 
ATOM   4623 C  CA   . ASN   B 1 37  ? 46.434 -20.045 -0.975  1.00 10.06 ?  37  ASN   B CA   1 
ATOM   4624 C  C    . ASN   B 1 37  ? 45.489 -20.718 0.009   1.00 10.03 ?  37  ASN   B C    1 
ATOM   4625 O  O    . ASN   B 1 37  ? 44.476 -20.143 0.417   1.00 10.73 ?  37  ASN   B O    1 
ATOM   4626 C  CB   . ASN   B 1 37  ? 47.364 -19.098 -0.215  1.00 10.11 ?  37  ASN   B CB   1 
ATOM   4627 C  CG   . ASN   B 1 37  ? 48.215 -19.814 0.798   1.00 10.49 ?  37  ASN   B CG   1 
ATOM   4628 O  OD1  . ASN   B 1 37  ? 48.555 -20.990 0.619   1.00 11.02 ?  37  ASN   B OD1  1 
ATOM   4629 N  ND2  . ASN   B 1 37  ? 48.568 -19.114 1.871   1.00 10.71 ?  37  ASN   B ND2  1 
ATOM   4630 H  H    . ASN   B 1 37  ? 45.393 -18.559 -1.717  1.00 11.84 ?  37  ASN   B H    1 
ATOM   4631 H  HA   . ASN   B 1 37  ? 46.970 -20.733 -1.393  1.00 12.21 ?  37  ASN   B HA   1 
ATOM   4632 H  HB2  . ASN   B 1 37  ? 47.957 -18.668 -0.850  1.00 12.28 ?  37  ASN   B HB2  1 
ATOM   4633 H  HB3  . ASN   B 1 37  ? 46.836 -18.437 0.254   1.00 12.28 ?  37  ASN   B HB3  1 
ATOM   4634 H  HD21 . ASN   B 1 37  ? 49.065 -19.473 2.474   1.00 12.99 ?  37  ASN   B HD21 1 
ATOM   4635 H  HD22 . ASN   B 1 37  ? 48.321 -18.300 1.953   1.00 12.99 ?  37  ASN   B HD22 1 
ATOM   4636 N  N    . ALA   B 1 38  ? 45.840 -21.950 0.384   1.00 10.21 ?  38  ALA   B N    1 
ATOM   4637 C  CA   . ALA   B 1 38  ? 45.184 -22.694 1.460   1.00 10.56 ?  38  ALA   B CA   1 
ATOM   4638 C  C    . ALA   B 1 38  ? 45.766 -22.206 2.785   1.00 10.43 ?  38  ALA   B C    1 
ATOM   4639 O  O    . ALA   B 1 38  ? 46.671 -22.812 3.370   1.00 11.58 ?  38  ALA   B O    1 
ATOM   4640 C  CB   . ALA   B 1 38  ? 45.406 -24.190 1.278   1.00 11.86 ?  38  ALA   B CB   1 
ATOM   4641 H  H    . ALA   B 1 38  ? 46.488 -22.389 0.028   1.00 12.39 ?  38  ALA   B H    1 
ATOM   4642 H  HA   . ALA   B 1 38  ? 44.228 -22.517 1.454   1.00 12.81 ?  38  ALA   B HA   1 
ATOM   4643 H  HB1  . ALA   B 1 38  ? 44.956 -24.668 2.003   1.00 14.37 ?  38  ALA   B HB1  1 
ATOM   4644 H  HB2  . ALA   B 1 38  ? 45.028 -24.465 0.428   1.00 14.37 ?  38  ALA   B HB2  1 
ATOM   4645 H  HB3  . ALA   B 1 38  ? 46.352 -24.378 1.301   1.00 14.37 ?  38  ALA   B HB3  1 
ATOM   4646 N  N    . ALA   B 1 39  ? 45.245 -21.066 3.244   1.00 10.35 ?  39  ALA   B N    1 
ATOM   4647 C  CA   . ALA   B 1 39  ? 45.797 -20.329 4.368   1.00 10.84 ?  39  ALA   B CA   1 
ATOM   4648 C  C    . ALA   B 1 39  ? 45.186 -20.773 5.695   1.00 10.72 ?  39  ALA   B C    1 
ATOM   4649 O  O    . ALA   B 1 39  ? 44.157 -21.449 5.749   1.00 11.86 ?  39  ALA   B O    1 
ATOM   4650 C  CB   . ALA   B 1 39  ? 45.552 -18.830 4.170   1.00 11.45 ?  39  ALA   B CB   1 
ATOM   4651 H  H    . ALA   B 1 39  ? 44.545 -20.696 2.905   1.00 12.57 ?  39  ALA   B H    1 
ATOM   4652 H  HA   . ALA   B 1 39  ? 46.751 -20.477 4.406   1.00 13.15 ?  39  ALA   B HA   1 
ATOM   4653 H  HB1  . ALA   B 1 39  ? 45.925 -18.347 4.924   1.00 13.88 ?  39  ALA   B HB1  1 
ATOM   4654 H  HB2  . ALA   B 1 39  ? 45.984 -18.543 3.349   1.00 13.88 ?  39  ALA   B HB2  1 
ATOM   4655 H  HB3  . ALA   B 1 39  ? 44.597 -18.667 4.113   1.00 13.88 ?  39  ALA   B HB3  1 
ATOM   4656 N  N    . ASN   B 1 40  ? 45.829 -20.346 6.780   1.00 11.36 ?  40  ASN   B N    1 
ATOM   4657 C  CA   . ASN   B 1 40  ? 45.266 -20.395 8.119   1.00 12.32 ?  40  ASN   B CA   1 
ATOM   4658 C  C    . ASN   B 1 40  ? 45.087 -18.968 8.645   1.00 11.81 ?  40  ASN   B C    1 
ATOM   4659 O  O    . ASN   B 1 40  ? 45.493 -17.988 8.013   1.00 11.95 ?  40  ASN   B O    1 
ATOM   4660 C  CB   . ASN   B 1 40  ? 46.114 -21.274 9.055   1.00 13.06 ?  40  ASN   B CB   1 
ATOM   4661 C  CG   . ASN   B 1 40  ? 47.569 -20.871 9.083   1.00 14.32 ?  40  ASN   B CG   1 
ATOM   4662 O  OD1  . ASN   B 1 40  ? 47.891 -19.688 9.143   1.00 15.90 ?  40  ASN   B OD1  1 
ATOM   4663 N  ND2  . ASN   B 1 40  ? 48.457 -21.853 9.048   1.00 14.41 ?  40  ASN   B ND2  1 
ATOM   4664 H  H    . ASN   B 1 40  ? 46.622 -20.012 6.754   1.00 13.77 ?  40  ASN   B H    1 
ATOM   4665 H  HA   . ASN   B 1 40  ? 44.384 -20.790 8.069   1.00 14.93 ?  40  ASN   B HA   1 
ATOM   4666 H  HB2  . ASN   B 1 40  ? 45.764 -21.199 9.955   1.00 15.81 ?  40  ASN   B HB2  1 
ATOM   4667 H  HB3  . ASN   B 1 40  ? 46.060 -22.193 8.752   1.00 15.81 ?  40  ASN   B HB3  1 
ATOM   4668 H  HD21 . ASN   B 1 40  ? 49.295 -21.676 9.060   1.00 17.44 ?  40  ASN   B HD21 1 
ATOM   4669 H  HD22 . ASN   B 1 40  ? 48.188 -22.671 9.002   1.00 17.44 ?  40  ASN   B HD22 1 
ATOM   4670 N  N    . VAL   B 1 41  ? 44.443 -18.840 9.808   1.00 12.39 ?  41  VAL   B N    1 
ATOM   4671 C  CA   . VAL   B 1 41  ? 43.983 -17.520 10.251  1.00 13.10 ?  41  VAL   B CA   1 
ATOM   4672 C  C    . VAL   B 1 41  ? 45.132 -16.567 10.549  1.00 12.58 ?  41  VAL   B C    1 
ATOM   4673 O  O    . VAL   B 1 41  ? 44.950 -15.347 10.466  1.00 12.82 ?  41  VAL   B O    1 
ATOM   4674 C  CB   . VAL   B 1 41  ? 43.009 -17.598 11.442  1.00 14.56 ?  41  VAL   B CB   1 
ATOM   4675 C  CG1  . VAL   B 1 41  ? 41.705 -18.267 11.031  1.00 14.92 ?  41  VAL   B CG1  1 
ATOM   4676 C  CG2  . VAL   B 1 41  ? 43.655 -18.291 12.636  1.00 15.60 ?  41  VAL   B CG2  1 
ATOM   4677 H  H    . VAL   B 1 41  ? 44.269 -19.482 10.340  1.00 15.01 ?  41  VAL   B H    1 
ATOM   4678 H  HA   . VAL   B 1 41  ? 43.486 -17.124 9.521   1.00 15.86 ?  41  VAL   B HA   1 
ATOM   4679 H  HB   . VAL   B 1 41  ? 42.790 -16.695 11.718  1.00 17.61 ?  41  VAL   B HB   1 
ATOM   4680 H  HG11 . VAL   B 1 41  ? 41.100 -18.273 11.791  1.00 18.04 ?  41  VAL   B HG11 1 
ATOM   4681 H  HG12 . VAL   B 1 41  ? 41.311 -17.768 10.299  1.00 18.04 ?  41  VAL   B HG12 1 
ATOM   4682 H  HG13 . VAL   B 1 41  ? 41.891 -19.176 10.751  1.00 18.04 ?  41  VAL   B HG13 1 
ATOM   4683 H  HG21 . VAL   B 1 41  ? 43.019 -18.321 13.367  1.00 18.86 ?  41  VAL   B HG21 1 
ATOM   4684 H  HG22 . VAL   B 1 41  ? 43.907 -19.194 12.382  1.00 18.86 ?  41  VAL   B HG22 1 
ATOM   4685 H  HG23 . VAL   B 1 41  ? 44.443 -17.792 12.903  1.00 18.86 ?  41  VAL   B HG23 1 
ATOM   4686 N  N    . TYR   B 1 42  ? 46.302 -17.081 10.930  1.00 12.90 ?  42  TYR   B N    1 
ATOM   4687 C  CA   . TYR   B 1 42  ? 47.454 -16.230 11.195  1.00 13.46 ?  42  TYR   B CA   1 
ATOM   4688 C  C    . TYR   B 1 42  ? 48.420 -16.161 10.015  1.00 12.80 ?  42  TYR   B C    1 
ATOM   4689 O  O    . TYR   B 1 42  ? 49.512 -15.595 10.149  1.00 14.00 ?  42  TYR   B O    1 
ATOM   4690 C  CB   . TYR   B 1 42  ? 48.153 -16.641 12.499  1.00 15.36 ?  42  TYR   B CB   1 
ATOM   4691 C  CG   . TYR   B 1 42  ? 47.548 -15.964 13.725  1.00 15.60 ?  42  TYR   B CG   1 
ATOM   4692 C  CD1  . TYR   B 1 42  ? 47.761 -14.610 13.964  1.00 14.72 ?  42  TYR   B CD1  1 
ATOM   4693 C  CD2  . TYR   B 1 42  ? 46.762 -16.666 14.627  1.00 17.10 ?  42  TYR   B CD2  1 
ATOM   4694 C  CE1  . TYR   B 1 42  ? 47.216 -13.976 15.064  1.00 15.63 ?  42  TYR   B CE1  1 
ATOM   4695 C  CE2  . TYR   B 1 42  ? 46.214 -16.038 15.738  1.00 17.30 ?  42  TYR   B CE2  1 
ATOM   4696 C  CZ   . TYR   B 1 42  ? 46.444 -14.689 15.950  1.00 17.69 ?  42  TYR   B CZ   1 
ATOM   4697 O  OH   . TYR   B 1 42  ? 45.905 -14.049 17.050  1.00 20.72 ?  42  TYR   B OH   1 
ATOM   4698 H  H    . TYR   B 1 42  ? 46.453 -17.926 11.027  1.00 15.62 ?  42  TYR   B H    1 
ATOM   4699 H  HA   . TYR   B 1 42  ? 47.127 -15.332 11.331  1.00 16.30 ?  42  TYR   B HA   1 
ATOM   4700 H  HB2  . TYR   B 1 42  ? 48.070 -17.599 12.616  1.00 18.57 ?  42  TYR   B HB2  1 
ATOM   4701 H  HB3  . TYR   B 1 42  ? 49.088 -16.390 12.448  1.00 18.57 ?  42  TYR   B HB3  1 
ATOM   4702 H  HD1  . TYR   B 1 42  ? 48.286 -14.121 13.363  1.00 17.80 ?  42  TYR   B HD1  1 
ATOM   4703 H  HD2  . TYR   B 1 42  ? 46.603 -17.573 14.484  1.00 20.66 ?  42  TYR   B HD2  1 
ATOM   4704 H  HE1  . TYR   B 1 42  ? 47.377 -13.070 15.202  1.00 18.89 ?  42  TYR   B HE1  1 
ATOM   4705 H  HE2  . TYR   B 1 42  ? 45.688 -16.525 16.331  1.00 20.90 ?  42  TYR   B HE2  1 
ATOM   4706 H  HH   . TYR   B 1 42  ? 46.130 -13.246 17.041  1.00 25.00 ?  42  TYR   B HH   1 
ATOM   4707 N  N    . LEU   B 1 43  ? 48.020 -16.678 8.855   1.00 11.87 ?  43  LEU   B N    1 
ATOM   4708 C  CA   . LEU   B 1 43  ? 48.831 -16.614 7.643   1.00 11.58 ?  43  LEU   B CA   1 
ATOM   4709 C  C    . LEU   B 1 43  ? 50.242 -17.126 7.901   1.00 11.87 ?  43  LEU   B C    1 
ATOM   4710 O  O    . LEU   B 1 43  ? 51.228 -16.531 7.457   1.00 12.75 ?  43  LEU   B O    1 
ATOM   4711 C  CB   . LEU   B 1 43  ? 48.856 -15.211 7.032   1.00 11.63 ?  43  LEU   B CB   1 
ATOM   4712 C  CG   . LEU   B 1 43  ? 47.496 -14.598 6.673   1.00 11.99 ?  43  LEU   B CG   1 
ATOM   4713 C  CD1  . LEU   B 1 43  ? 47.701 -13.203 6.084   1.00 13.30 ?  43  LEU   B CD1  1 
ATOM   4714 C  CD2  . LEU   B 1 43  ? 46.716 -15.484 5.711   1.00 12.20 ?  43  LEU   B CD2  1 
ATOM   4715 H  H    . LEU   B 1 43  ? 47.272 -17.084 8.743   1.00 14.38 ?  43  LEU   B H    1 
ATOM   4716 H  HA   . LEU   B 1 43  ? 48.430 -17.207 6.982   1.00 14.03 ?  43  LEU   B HA   1 
ATOM   4717 H  HB2  . LEU   B 1 43  ? 49.287 -14.615 7.659   1.00 14.10 ?  43  LEU   B HB2  1 
ATOM   4718 H  HB3  . LEU   B 1 43  ? 49.376 -15.249 6.212   1.00 14.10 ?  43  LEU   B HB3  1 
ATOM   4719 H  HG   . LEU   B 1 43  ? 46.973 -14.500 7.482   1.00 14.53 ?  43  LEU   B HG   1 
ATOM   4720 H  HD11 . LEU   B 1 43  ? 46.837 -12.822 5.863   1.00 16.11 ?  43  LEU   B HD11 1 
ATOM   4721 H  HD12 . LEU   B 1 43  ? 48.149 -12.645 6.741   1.00 16.11 ?  43  LEU   B HD12 1 
ATOM   4722 H  HD13 . LEU   B 1 43  ? 48.247 -13.273 5.285   1.00 16.11 ?  43  LEU   B HD13 1 
ATOM   4723 H  HD21 . LEU   B 1 43  ? 45.912 -15.013 5.432   1.00 14.78 ?  43  LEU   B HD21 1 
ATOM   4724 H  HD22 . LEU   B 1 43  ? 47.269 -15.679 4.941   1.00 14.78 ?  43  LEU   B HD22 1 
ATOM   4725 H  HD23 . LEU   B 1 43  ? 46.475 -16.305 6.166   1.00 14.78 ?  43  LEU   B HD23 1 
ATOM   4726 N  N    . LYS   B 1 44  ? 50.338 -18.245 8.619   1.00 11.87 ?  44  LYS   B N    1 
ATOM   4727 C  CA   . LYS   B 1 44  ? 51.603 -18.926 8.860   1.00 12.66 ?  44  LYS   B CA   1 
ATOM   4728 C  C    . LYS   B 1 44  ? 51.723 -20.046 7.835   1.00 12.06 ?  44  LYS   B C    1 
ATOM   4729 O  O    . LYS   B 1 44  ? 51.026 -21.061 7.923   1.00 13.41 ?  44  LYS   B O    1 
ATOM   4730 C  CB   . LYS   B 1 44  ? 51.658 -19.438 10.299  1.00 14.32 ?  44  LYS   B CB   1 
ATOM   4731 C  CG   . LYS   B 1 44  ? 51.846 -18.326 11.321  1.00 17.02 ?  44  LYS   B CG   1 
ATOM   4732 C  CD   . LYS   B 1 44  ? 53.050 -17.465 10.928  1.00 20.32 ?  44  LYS   B CD   1 
ATOM   4733 C  CE   . LYS   B 1 44  ? 53.542 -16.591 12.047  1.00 23.08 ?  44  LYS   B CE   1 
ATOM   4734 N  NZ   . LYS   B 1 44  ? 54.721 -15.783 11.653  1.00 24.33 ?  44  LYS   B NZ   1 
ATOM   4735 H  H    . LYS   B 1 44  ? 49.663 -18.634 8.986   1.00 14.39 ?  44  LYS   B H    1 
ATOM   4736 H  HA   . LYS   B 1 44  ? 52.333 -18.311 8.700   1.00 15.33 ?  44  LYS   B HA   1 
ATOM   4737 H  HB2  . LYS   B 1 44  ? 50.818 -19.889 10.504  1.00 17.33 ?  44  LYS   B HB2  1 
ATOM   4738 H  HB3  . LYS   B 1 44  ? 52.393 -20.056 10.388  1.00 17.33 ?  44  LYS   B HB3  1 
ATOM   4739 H  HG2  . LYS   B 1 44  ? 51.056 -17.769 11.347  1.00 20.57 ?  44  LYS   B HG2  1 
ATOM   4740 H  HG3  . LYS   B 1 44  ? 52.018 -18.719 12.194  1.00 20.57 ?  44  LYS   B HG3  1 
ATOM   4741 H  HD2  . LYS   B 1 44  ? 53.772 -18.054 10.641  1.00 24.53 ?  44  LYS   B HD2  1 
ATOM   4742 H  HD3  . LYS   B 1 44  ? 52.788 -16.887 10.194  1.00 24.53 ?  44  LYS   B HD3  1 
ATOM   4743 H  HE2  . LYS   B 1 44  ? 52.840 -15.971 12.267  1.00 27.84 ?  44  LYS   B HE2  1 
ATOM   4744 H  HE3  . LYS   B 1 44  ? 53.776 -17.143 12.811  1.00 27.84 ?  44  LYS   B HE3  1 
ATOM   4745 H  HZ1  . LYS   B 1 44  ? 54.980 -15.275 12.336  1.00 29.34 ?  44  LYS   B HZ1  1 
ATOM   4746 H  HZ2  . LYS   B 1 44  ? 55.393 -16.313 11.413  1.00 29.34 ?  44  LYS   B HZ2  1 
ATOM   4747 H  HZ3  . LYS   B 1 44  ? 54.510 -15.254 10.966  1.00 29.34 ?  44  LYS   B HZ3  1 
ATOM   4748 N  N    . HIS   B 1 45  ? 52.578 -19.830 6.837   1.00 11.85 ?  45  HIS   B N    1 
ATOM   4749 C  CA   . HIS   B 1 45  ? 52.595 -20.657 5.632   1.00 11.91 ?  45  HIS   B CA   1 
ATOM   4750 C  C    . HIS   B 1 45  ? 53.606 -21.787 5.795   1.00 14.21 ?  45  HIS   B C    1 
ATOM   4751 O  O    . HIS   B 1 45  ? 54.664 -21.815 5.174   1.00 16.35 ?  45  HIS   B O    1 
ATOM   4752 C  CB   . HIS   B 1 45  ? 52.918 -19.802 4.419   1.00 12.03 ?  45  HIS   B CB   1 
ATOM   4753 C  CG   . HIS   B 1 45  ? 52.047 -18.600 4.304   1.00 11.76 ?  45  HIS   B CG   1 
ATOM   4754 N  ND1  . HIS   B 1 45  ? 50.669 -18.677 4.257   1.00 11.82 ?  45  HIS   B ND1  1 
ATOM   4755 C  CD2  . HIS   B 1 45  ? 52.365 -17.285 4.237   1.00 12.37 ?  45  HIS   B CD2  1 
ATOM   4756 C  CE1  . HIS   B 1 45  ? 50.185 -17.452 4.156   1.00 11.48 ?  45  HIS   B CE1  1 
ATOM   4757 N  NE2  . HIS   B 1 45  ? 51.188 -16.591 4.139   1.00 12.28 ?  45  HIS   B NE2  1 
ATOM   4758 H  H    . HIS   B 1 45  ? 53.150 -19.188 6.827   1.00 14.36 ?  45  HIS   B H    1 
ATOM   4759 H  HA   . HIS   B 1 45  ? 51.713 -21.046 5.499   1.00 14.43 ?  45  HIS   B HA   1 
ATOM   4760 H  HB2  . HIS   B 1 45  ? 53.837 -19.503 4.481   1.00 14.58 ?  45  HIS   B HB2  1 
ATOM   4761 H  HB3  . HIS   B 1 45  ? 52.798 -20.339 3.617   1.00 14.58 ?  45  HIS   B HB3  1 
ATOM   4762 H  HD2  . HIS   B 1 45  ? 53.222 -16.921 4.253   1.00 14.98 ?  45  HIS   B HD2  1 
ATOM   4763 H  HE1  . HIS   B 1 45  ? 49.284 -17.231 4.094   1.00 13.92 ?  45  HIS   B HE1  1 
ATOM   4764 H  HE2  . HIS   B 1 45  ? 51.112 -15.734 4.086   1.00 14.88 ?  45  HIS   B HE2  1 
ATOM   4765 N  N    A GLY   B 1 46  ? 53.238 -22.750 6.635   0.74 15.14 ?  46  GLY   B N    1 
ATOM   4766 N  N    B GLY   B 1 46  ? 53.247 -22.735 6.652   0.26 14.90 ?  46  GLY   B N    1 
ATOM   4767 C  CA   A GLY   B 1 46  ? 54.156 -23.807 7.021   0.74 16.78 ?  46  GLY   B CA   1 
ATOM   4768 C  CA   B GLY   B 1 46  ? 54.159 -23.804 6.998   0.26 15.88 ?  46  GLY   B CA   1 
ATOM   4769 C  C    A GLY   B 1 46  ? 54.214 -25.030 6.125   0.74 18.32 ?  46  GLY   B C    1 
ATOM   4770 C  C    B GLY   B 1 46  ? 54.198 -24.947 6.005   0.26 16.91 ?  46  GLY   B C    1 
ATOM   4771 O  O    A GLY   B 1 46  ? 55.299 -25.473 5.737   0.74 21.14 ?  46  GLY   B O    1 
ATOM   4772 O  O    B GLY   B 1 46  ? 55.241 -25.223 5.404   0.26 17.43 ?  46  GLY   B O    1 
ATOM   4773 H  H    A GLY   B 1 46  ? 52.460 -22.795 7.012   0.74 18.31 ?  46  GLY   B H    1 
ATOM   4774 H  H    B GLY   B 1 46  ? 52.480 -22.773 7.050   0.26 18.02 ?  46  GLY   B H    1 
ATOM   4775 H  HA2  A GLY   B 1 46  ? 55.047 -23.432 7.075   0.74 20.28 ?  46  GLY   B HA2  1 
ATOM   4776 H  HA2  B GLY   B 1 46  ? 55.053 -23.438 7.071   0.26 19.19 ?  46  GLY   B HA2  1 
ATOM   4777 H  HA3  A GLY   B 1 46  ? 53.910 -24.117 7.907   0.74 20.28 ?  46  GLY   B HA3  1 
ATOM   4778 H  HA3  B GLY   B 1 46  ? 53.908 -24.160 7.865   0.26 19.19 ?  46  GLY   B HA3  1 
ATOM   4779 N  N    . GLY   B 1 47  ? 53.061 -25.614 5.808   1.00 17.58 ?  47  GLY   B N    1 
ATOM   4780 C  CA   . GLY   B 1 47  ? 53.015 -26.879 5.103   1.00 15.43 ?  47  GLY   B CA   1 
ATOM   4781 C  C    . GLY   B 1 47  ? 52.099 -26.859 3.895   1.00 13.66 ?  47  GLY   B C    1 
ATOM   4782 O  O    . GLY   B 1 47  ? 51.447 -25.858 3.597   1.00 13.70 ?  47  GLY   B O    1 
ATOM   4783 H  H    A GLY   B 1 47  ? 52.286 -25.304 6.017   0.74 21.24 ?  47  GLY   B H    1 
ATOM   4784 H  H    B GLY   B 1 47  ? 52.291 -25.344 6.084   0.26 21.24 ?  47  GLY   B H    1 
ATOM   4785 H  HA2  . GLY   B 1 47  ? 53.907 -27.119 4.804   1.00 18.66 ?  47  GLY   B HA2  1 
ATOM   4786 H  HA3  . GLY   B 1 47  ? 52.707 -27.570 5.713   1.00 18.66 ?  47  GLY   B HA3  1 
ATOM   4787 N  N    . GLY   B 1 48  ? 52.048 -28.004 3.215   1.00 12.78 ?  48  GLY   B N    1 
ATOM   4788 C  CA   . GLY   B 1 48  ? 51.125 -28.150 2.106   1.00 12.70 ?  48  GLY   B CA   1 
ATOM   4789 C  C    . GLY   B 1 48  ? 51.264 -27.041 1.090   1.00 12.06 ?  48  GLY   B C    1 
ATOM   4790 O  O    . GLY   B 1 48  ? 52.365 -26.574 0.781   1.00 12.66 ?  48  GLY   B O    1 
ATOM   4791 H  H    . GLY   B 1 48  ? 52.536 -28.689 3.371   1.00 15.48 ?  48  GLY   B H    1 
ATOM   4792 H  HA2  . GLY   B 1 48  ? 51.285 -28.999 1.662   1.00 15.39 ?  48  GLY   B HA2  1 
ATOM   4793 H  HA3  . GLY   B 1 48  ? 50.214 -28.145 2.436   1.00 15.39 ?  48  GLY   B HA3  1 
ATOM   4794 N  N    . VAL   B 1 49  ? 50.119 -26.608 0.562   1.00 12.16 ?  49  VAL   B N    1 
ATOM   4795 C  CA   . VAL   B 1 49  ? 50.101 -25.584 -0.479  1.00 12.07 ?  49  VAL   B CA   1 
ATOM   4796 C  C    . VAL   B 1 49  ? 50.762 -24.298 0.009   1.00 11.32 ?  49  VAL   B C    1 
ATOM   4797 O  O    . VAL   B 1 49  ? 51.549 -23.677 -0.714  1.00 11.84 ?  49  VAL   B O    1 
ATOM   4798 C  CB   . VAL   B 1 49  ? 48.657 -25.332 -0.957  1.00 13.29 ?  49  VAL   B CB   1 
ATOM   4799 C  CG1  . VAL   B 1 49  ? 48.581 -24.087 -1.834  1.00 13.27 ?  49  VAL   B CG1  1 
ATOM   4800 C  CG2  . VAL   B 1 49  ? 48.112 -26.549 -1.704  1.00 14.91 ?  49  VAL   B CG2  1 
ATOM   4801 H  H    . VAL   B 1 49  ? 49.331 -26.887 0.790   1.00 14.73 ?  49  VAL   B H    1 
ATOM   4802 H  HA   . VAL   B 1 49  ? 50.605 -25.904 -1.242  1.00 14.63 ?  49  VAL   B HA   1 
ATOM   4803 H  HB   . VAL   B 1 49  ? 48.088 -25.184 -0.188  1.00 16.09 ?  49  VAL   B HB   1 
ATOM   4804 H  HG11 . VAL   B 1 49  ? 47.746 -24.100 -2.333  1.00 16.07 ?  49  VAL   B HG11 1 
ATOM   4805 H  HG12 . VAL   B 1 49  ? 48.609 -23.298 -1.269  1.00 16.07 ?  49  VAL   B HG12 1 
ATOM   4806 H  HG13 . VAL   B 1 49  ? 49.329 -24.084 -2.449  1.00 16.07 ?  49  VAL   B HG13 1 
ATOM   4807 H  HG21 . VAL   B 1 49  ? 47.203 -26.368 -1.994  1.00 18.03 ?  49  VAL   B HG21 1 
ATOM   4808 H  HG22 . VAL   B 1 49  ? 48.674 -26.726 -2.477  1.00 18.03 ?  49  VAL   B HG22 1 
ATOM   4809 H  HG23 . VAL   B 1 49  ? 48.121 -27.315 -1.108  1.00 18.03 ?  49  VAL   B HG23 1 
ATOM   4810 N  N    . ALA   B 1 50  ? 50.414 -23.850 1.216   1.00 10.97 ?  50  ALA   B N    1 
ATOM   4811 C  CA   . ALA   B 1 50  ? 50.936 -22.574 1.694   1.00 10.78 ?  50  ALA   B CA   1 
ATOM   4812 C  C    . ALA   B 1 50  ? 52.455 -22.608 1.796   1.00 11.16 ?  50  ALA   B C    1 
ATOM   4813 O  O    . ALA   B 1 50  ? 53.135 -21.641 1.429   1.00 11.18 ?  50  ALA   B O    1 
ATOM   4814 C  CB   . ALA   B 1 50  ? 50.314 -22.216 3.043   1.00 11.06 ?  50  ALA   B CB   1 
ATOM   4815 H  H    . ALA   B 1 50  ? 49.888 -24.257 1.764   1.00 13.30 ?  50  ALA   B H    1 
ATOM   4816 H  HA   . ALA   B 1 50  ? 50.702 -21.881 1.066   1.00 13.08 ?  50  ALA   B HA   1 
ATOM   4817 H  HB1  . ALA   B 1 50  ? 50.676 -21.365 3.342   1.00 13.41 ?  50  ALA   B HB1  1 
ATOM   4818 H  HB2  . ALA   B 1 50  ? 49.352 -22.145 2.939   1.00 13.41 ?  50  ALA   B HB2  1 
ATOM   4819 H  HB3  . ALA   B 1 50  ? 50.527 -22.908 3.688   1.00 13.41 ?  50  ALA   B HB3  1 
ATOM   4820 N  N    . GLY   B 1 51  ? 53.005 -23.701 2.315   1.00 11.66 ?  51  GLY   B N    1 
ATOM   4821 C  CA   . GLY   B 1 51  ? 54.449 -23.810 2.386   1.00 12.38 ?  51  GLY   B CA   1 
ATOM   4822 C  C    . GLY   B 1 51  ? 55.097 -23.755 1.018   1.00 12.02 ?  51  GLY   B C    1 
ATOM   4823 O  O    . GLY   B 1 51  ? 56.139 -23.116 0.838   1.00 12.94 ?  51  GLY   B O    1 
ATOM   4824 H  H    . GLY   B 1 51  ? 52.574 -24.380 2.625   1.00 14.13 ?  51  GLY   B H    1 
ATOM   4825 H  HA2  . GLY   B 1 51  ? 54.804 -23.085 2.923   1.00 14.99 ?  51  GLY   B HA2  1 
ATOM   4826 H  HA3  . GLY   B 1 51  ? 54.691 -24.651 2.810   1.00 14.99 ?  51  GLY   B HA3  1 
ATOM   4827 N  N    . ALA   B 1 52  ? 54.488 -24.416 0.034   1.00 11.81 ?  52  ALA   B N    1 
ATOM   4828 C  CA   . ALA   B 1 52  ? 55.049 -24.424 -1.309  1.00 12.11 ?  52  ALA   B CA   1 
ATOM   4829 C  C    . ALA   B 1 52  ? 54.973 -23.048 -1.961  1.00 11.60 ?  52  ALA   B C    1 
ATOM   4830 O  O    . ALA   B 1 52  ? 55.946 -22.597 -2.585  1.00 12.39 ?  52  ALA   B O    1 
ATOM   4831 C  CB   . ALA   B 1 52  ? 54.350 -25.468 -2.168  1.00 12.92 ?  52  ALA   B CB   1 
ATOM   4832 H  H    . ALA   B 1 52  ? 53.744 -24.848 0.117   1.00 14.32 ?  52  ALA   B H    1 
ATOM   4833 H  HA   . ALA   B 1 52  ? 55.982 -24.667 -1.246  1.00 14.68 ?  52  ALA   B HA   1 
ATOM   4834 H  HB1  . ALA   B 1 52  ? 54.746 -25.459 -3.055  1.00 15.65 ?  52  ALA   B HB1  1 
ATOM   4835 H  HB2  . ALA   B 1 52  ? 54.476 -26.342 -1.762  1.00 15.65 ?  52  ALA   B HB2  1 
ATOM   4836 H  HB3  . ALA   B 1 52  ? 53.408 -25.259 -2.222  1.00 15.65 ?  52  ALA   B HB3  1 
ATOM   4837 N  N    . LEU   B 1 53  ? 53.829 -22.369 -1.843  1.00 11.22 ?  53  LEU   B N    1 
ATOM   4838 C  CA   . LEU   B 1 53  ? 53.721 -21.028 -2.408  1.00 11.40 ?  53  LEU   B CA   1 
ATOM   4839 C  C    . LEU   B 1 53  ? 54.732 -20.092 -1.760  1.00 11.24 ?  53  LEU   B C    1 
ATOM   4840 O  O    . LEU   B 1 53  ? 55.436 -19.345 -2.447  1.00 12.04 ?  53  LEU   B O    1 
ATOM   4841 C  CB   . LEU   B 1 53  ? 52.296 -20.491 -2.238  1.00 11.84 ?  53  LEU   B CB   1 
ATOM   4842 C  CG   . LEU   B 1 53  ? 51.159 -21.211 -2.970  1.00 12.23 ?  53  LEU   B CG   1 
ATOM   4843 C  CD1  . LEU   B 1 53  ? 49.813 -20.611 -2.605  1.00 13.53 ?  53  LEU   B CD1  1 
ATOM   4844 C  CD2  . LEU   B 1 53  ? 51.349 -21.191 -4.482  1.00 14.15 ?  53  LEU   B CD2  1 
ATOM   4845 H  H    . LEU   B 1 53  ? 53.120 -22.651 -1.449  1.00 13.61 ?  53  LEU   B H    1 
ATOM   4846 H  HA   . LEU   B 1 53  ? 53.923 -21.070 -3.362  1.00 13.82 ?  53  LEU   B HA   1 
ATOM   4847 H  HB2  . LEU   B 1 53  ? 52.086 -20.518 -1.298  1.00 14.35 ?  53  LEU   B HB2  1 
ATOM   4848 H  HB3  . LEU   B 1 53  ? 52.290 -19.574 -2.546  1.00 14.35 ?  53  LEU   B HB3  1 
ATOM   4849 H  HG   . LEU   B 1 53  ? 51.142 -22.138 -2.691  1.00 14.82 ?  53  LEU   B HG   1 
ATOM   4850 H  HD11 . LEU   B 1 53  ? 49.110 -21.090 -3.078  1.00 16.38 ?  53  LEU   B HD11 1 
ATOM   4851 H  HD12 . LEU   B 1 53  ? 49.676 -20.701 -1.645  1.00 16.38 ?  53  LEU   B HD12 1 
ATOM   4852 H  HD13 . LEU   B 1 53  ? 49.799 -19.676 -2.853  1.00 16.38 ?  53  LEU   B HD13 1 
ATOM   4853 H  HD21 . LEU   B 1 53  ? 50.645 -21.718 -4.897  1.00 17.12 ?  53  LEU   B HD21 1 
ATOM   4854 H  HD22 . LEU   B 1 53  ? 51.297 -20.275 -4.796  1.00 17.12 ?  53  LEU   B HD22 1 
ATOM   4855 H  HD23 . LEU   B 1 53  ? 52.213 -21.570 -4.698  1.00 17.12 ?  53  LEU   B HD23 1 
ATOM   4856 N  N    . ASN   B 1 54  ? 54.822 -20.120 -0.433  1.00 10.98 ?  54  ASN   B N    1 
ATOM   4857 C  CA   . ASN   B 1 54  ? 55.738 -19.209 0.237   1.00 11.70 ?  54  ASN   B CA   1 
ATOM   4858 C  C    . ASN   B 1 54  ? 57.180 -19.489 -0.164  1.00 12.16 ?  54  ASN   B C    1 
ATOM   4859 O  O    . ASN   B 1 54  ? 57.956 -18.554 -0.408  1.00 12.88 ?  54  ASN   B O    1 
ATOM   4860 C  CB   . ASN   B 1 54  ? 55.578 -19.286 1.750   1.00 12.52 ?  54  ASN   B CB   1 
ATOM   4861 C  CG   . ASN   B 1 54  ? 56.552 -18.365 2.458   1.00 12.63 ?  54  ASN   B CG   1 
ATOM   4862 O  OD1  . ASN   B 1 54  ? 56.566 -17.156 2.211   1.00 12.87 ?  54  ASN   B OD1  1 
ATOM   4863 N  ND2  . ASN   B 1 54  ? 57.398 -18.931 3.312   1.00 13.99 ?  54  ASN   B ND2  1 
ATOM   4864 H  H    . ASN   B 1 54  ? 54.376 -20.642 0.085   1.00 13.31 ?  54  ASN   B H    1 
ATOM   4865 H  HA   . ASN   B 1 54  ? 55.525 -18.304 -0.034  1.00 14.18 ?  54  ASN   B HA   1 
ATOM   4866 H  HB2  . ASN   B 1 54  ? 54.676 -19.017 1.993   1.00 15.17 ?  54  ASN   B HB2  1 
ATOM   4867 H  HB3  . ASN   B 1 54  ? 55.748 -20.193 2.048   1.00 15.17 ?  54  ASN   B HB3  1 
ATOM   4868 H  HD21 . ASN   B 1 54  ? 57.977 -18.451 3.732   1.00 16.93 ?  54  ASN   B HD21 1 
ATOM   4869 H  HD22 . ASN   B 1 54  ? 57.369 -19.781 3.450   1.00 16.93 ?  54  ASN   B HD22 1 
ATOM   4870 N  N    . LYS   B 1 55  ? 57.564 -20.767 -0.225  1.00 12.79 ?  55  LYS   B N    1 
ATOM   4871 C  CA   . LYS   B 1 55  ? 58.916 -21.113 -0.645  1.00 13.86 ?  55  LYS   B CA   1 
ATOM   4872 C  C    . LYS   B 1 55  ? 59.210 -20.571 -2.037  1.00 13.46 ?  55  LYS   B C    1 
ATOM   4873 O  O    . LYS   B 1 55  ? 60.311 -20.073 -2.296  1.00 14.29 ?  55  LYS   B O    1 
ATOM   4874 C  CB   . LYS   B 1 55  ? 59.106 -22.631 -0.600  1.00 15.49 ?  55  LYS   B CB   1 
ATOM   4875 C  CG   . LYS   B 1 55  ? 60.484 -23.094 -1.036  1.00 19.44 ?  55  LYS   B CG   1 
ATOM   4876 C  CD   . LYS   B 1 55  ? 60.659 -24.592 -0.853  1.00 23.06 ?  55  LYS   B CD   1 
ATOM   4877 C  CE   . LYS   B 1 55  ? 60.649 -24.988 0.620   1.00 26.14 ?  55  LYS   B CE   1 
ATOM   4878 N  NZ   . LYS   B 1 55  ? 61.064 -26.395 0.828   1.00 27.69 ?  55  LYS   B NZ   1 
ATOM   4879 H  H    . LYS   B 1 55  ? 57.062 -21.438 -0.034  1.00 15.49 ?  55  LYS   B H    1 
ATOM   4880 H  HA   . LYS   B 1 55  ? 59.549 -20.713 -0.031  1.00 16.77 ?  55  LYS   B HA   1 
ATOM   4881 H  HB2  . LYS   B 1 55  ? 58.961 -22.928 0.313   1.00 18.73 ?  55  LYS   B HB2  1 
ATOM   4882 H  HB3  . LYS   B 1 55  ? 58.454 -23.047 -1.185  1.00 18.73 ?  55  LYS   B HB3  1 
ATOM   4883 H  HG2  . LYS   B 1 55  ? 60.608 -22.889 -1.975  1.00 23.47 ?  55  LYS   B HG2  1 
ATOM   4884 H  HG3  . LYS   B 1 55  ? 61.155 -22.642 -0.501  1.00 23.47 ?  55  LYS   B HG3  1 
ATOM   4885 H  HD2  . LYS   B 1 55  ? 59.933 -25.059 -1.296  1.00 27.82 ?  55  LYS   B HD2  1 
ATOM   4886 H  HD3  . LYS   B 1 55  ? 61.511 -24.865 -1.231  1.00 27.82 ?  55  LYS   B HD3  1 
ATOM   4887 H  HE2  . LYS   B 1 55  ? 61.262 -24.409 1.104   1.00 31.51 ?  55  LYS   B HE2  1 
ATOM   4888 H  HE3  . LYS   B 1 55  ? 59.748 -24.880 0.968   1.00 31.51 ?  55  LYS   B HE3  1 
ATOM   4889 H  HZ1  . LYS   B 1 55  ? 61.024 -26.595 1.694   1.00 33.37 ?  55  LYS   B HZ1  1 
ATOM   4890 H  HZ2  . LYS   B 1 55  ? 60.520 -26.938 0.379   1.00 33.37 ?  55  LYS   B HZ2  1 
ATOM   4891 H  HZ3  . LYS   B 1 55  ? 61.895 -26.511 0.539   1.00 33.37 ?  55  LYS   B HZ3  1 
ATOM   4892 N  N    . ALA   B 1 56  ? 58.240 -20.659 -2.951  1.00 13.05 ?  56  ALA   B N    1 
ATOM   4893 C  CA   . ALA   B 1 56  ? 58.464 -20.157 -4.301  1.00 13.87 ?  56  ALA   B CA   1 
ATOM   4894 C  C    . ALA   B 1 56  ? 58.747 -18.663 -4.300  1.00 13.61 ?  56  ALA   B C    1 
ATOM   4895 O  O    . ALA   B 1 56  ? 59.470 -18.167 -5.172  1.00 14.81 ?  56  ALA   B O    1 
ATOM   4896 C  CB   . ALA   B 1 56  ? 57.262 -20.480 -5.190  1.00 14.89 ?  56  ALA   B CB   1 
ATOM   4897 H  H    . ALA   B 1 56  ? 57.455 -20.991 -2.814  1.00 15.80 ?  56  ALA   B H    1 
ATOM   4898 H  HA   . ALA   B 1 56  ? 59.236 -20.601 -4.677  1.00 16.79 ?  56  ALA   B HA   1 
ATOM   4899 H  HB1  . ALA   B 1 56  ? 57.430 -20.144 -6.086  1.00 18.01 ?  56  ALA   B HB1  1 
ATOM   4900 H  HB2  . ALA   B 1 56  ? 57.141 -21.444 -5.220  1.00 18.01 ?  56  ALA   B HB2  1 
ATOM   4901 H  HB3  . ALA   B 1 56  ? 56.470 -20.060 -4.824  1.00 18.01 ?  56  ALA   B HB3  1 
ATOM   4902 N  N    . THR   B 1 57  ? 58.182 -17.928 -3.341  1.00 13.29 ?  57  THR   B N    1 
ATOM   4903 C  CA   . THR   B 1 57  ? 58.419 -16.492 -3.226  1.00 13.42 ?  57  THR   B CA   1 
ATOM   4904 C  C    . THR   B 1 57  ? 59.668 -16.163 -2.417  1.00 14.36 ?  57  THR   B C    1 
ATOM   4905 O  O    . THR   B 1 57  ? 59.905 -14.987 -2.111  1.00 14.81 ?  57  THR   B O    1 
ATOM   4906 C  CB   . THR   B 1 57  ? 57.217 -15.762 -2.596  1.00 12.59 ?  57  THR   B CB   1 
ATOM   4907 O  OG1  . THR   B 1 57  ? 57.191 -15.971 -1.177  1.00 13.02 ?  57  THR   B OG1  1 
ATOM   4908 C  CG2  . THR   B 1 57  ? 55.903 -16.184 -3.237  1.00 12.49 ?  57  THR   B CG2  1 
ATOM   4909 H  H    . THR   B 1 57  ? 57.637 -18.238 -2.747  1.00 16.09 ?  57  THR   B H    1 
ATOM   4910 H  HA   . THR   B 1 57  ? 58.540 -16.131 -4.119  1.00 16.25 ?  57  THR   B HA   1 
ATOM   4911 H  HB   . THR   B 1 57  ? 57.324 -14.812 -2.766  1.00 15.25 ?  57  THR   B HB   1 
ATOM   4912 H  HG1  . THR   B 1 57  ? 57.121 -16.791 -1.013  1.00 15.76 ?  57  THR   B HG1  1 
ATOM   4913 H  HG21 . THR   B 1 57  ? 55.179 -15.639 -2.899  1.00 15.13 ?  57  THR   B HG21 1 
ATOM   4914 H  HG22 . THR   B 1 57  ? 55.954 -16.081 -4.202  1.00 15.13 ?  57  THR   B HG22 1 
ATOM   4915 H  HG23 . THR   B 1 57  ? 55.719 -17.115 -3.034  1.00 15.13 ?  57  THR   B HG23 1 
ATOM   4916 N  N    . ASN   B 1 58  ? 60.463 -17.166 -2.055  1.00 15.09 ?  58  ASN   B N    1 
ATOM   4917 C  CA   . ASN   B 1 58  ? 61.661 -16.949 -1.248  1.00 18.11 ?  58  ASN   B CA   1 
ATOM   4918 C  C    . ASN   B 1 58  ? 61.324 -16.236 0.063   1.00 15.52 ?  58  ASN   B C    1 
ATOM   4919 O  O    . ASN   B 1 58  ? 62.065 -15.364 0.531   1.00 16.09 ?  58  ASN   B O    1 
ATOM   4920 C  CB   . ASN   B 1 58  ? 62.748 -16.205 -2.030  1.00 26.61 ?  58  ASN   B CB   1 
ATOM   4921 C  CG   . ASN   B 1 58  ? 64.120 -16.351 -1.400  1.00 36.22 ?  58  ASN   B CG   1 
ATOM   4922 O  OD1  . ASN   B 1 58  ? 64.414 -17.354 -0.751  1.00 38.82 ?  58  ASN   B OD1  1 
ATOM   4923 N  ND2  . ASN   B 1 58  ? 64.967 -15.347 -1.588  1.00 42.38 ?  58  ASN   B ND2  1 
ATOM   4924 H  H    . ASN   B 1 58  ? 60.327 -17.993 -2.265  1.00 18.25 ?  58  ASN   B H    1 
ATOM   4925 H  HA   . ASN   B 1 58  ? 62.023 -17.821 -1.023  1.00 21.87 ?  58  ASN   B HA   1 
ATOM   4926 H  HB2  . ASN   B 1 58  ? 62.791 -16.562 -2.934  1.00 32.08 ?  58  ASN   B HB2  1 
ATOM   4927 H  HB3  . ASN   B 1 58  ? 62.529 -15.262 -2.057  1.00 32.08 ?  58  ASN   B HB3  1 
ATOM   4928 H  HD21 . ASN   B 1 58  ? 65.758 -15.383 -1.251  1.00 50.99 ?  58  ASN   B HD21 1 
ATOM   4929 H  HD22 . ASN   B 1 58  ? 64.725 -14.661 -2.046  1.00 50.99 ?  58  ASN   B HD22 1 
ATOM   4930 N  N    . ASN   B 1 59  ? 60.201 -16.623 0.669   1.00 14.48 ?  59  ASN   B N    1 
ATOM   4931 C  CA   . ASN   B 1 59  ? 59.727 -16.149 1.970   1.00 14.51 ?  59  ASN   B CA   1 
ATOM   4932 C  C    . ASN   B 1 59  ? 59.129 -14.743 1.913   1.00 13.65 ?  59  ASN   B C    1 
ATOM   4933 O  O    . ASN   B 1 59  ? 58.694 -14.241 2.957   1.00 13.77 ?  59  ASN   B O    1 
ATOM   4934 C  CB   . ASN   B 1 59  ? 60.799 -16.206 3.074   1.00 15.55 ?  59  ASN   B CB   1 
ATOM   4935 C  CG   . ASN   B 1 59  ? 60.209 -16.384 4.457   1.00 16.55 ?  59  ASN   B CG   1 
ATOM   4936 O  OD1  . ASN   B 1 59  ? 59.386 -17.272 4.685   1.00 16.75 ?  59  ASN   B OD1  1 
ATOM   4937 N  ND2  . ASN   B 1 59  ? 60.627 -15.537 5.391   1.00 17.26 ?  59  ASN   B ND2  1 
ATOM   4938 H  H    . ASN   B 1 59  ? 59.669 -17.211 0.328   1.00 17.52 ?  59  ASN   B H    1 
ATOM   4939 H  HA   . ASN   B 1 59  ? 59.018 -16.745 2.252   1.00 17.55 ?  59  ASN   B HA   1 
ATOM   4940 H  HB2  . ASN   B 1 59  ? 61.391 -16.958 2.913   1.00 18.80 ?  59  ASN   B HB2  1 
ATOM   4941 H  HB3  . ASN   B 1 59  ? 61.302 -15.380 3.077   1.00 18.80 ?  59  ASN   B HB3  1 
ATOM   4942 H  HD21 . ASN   B 1 59  ? 60.320 -15.596 6.195   1.00 20.85 ?  59  ASN   B HD21 1 
ATOM   4943 H  HD22 . ASN   B 1 59  ? 61.199 -14.929 5.195   1.00 20.85 ?  59  ASN   B HD22 1 
ATOM   4944 N  N    . ALA   B 1 60  ? 59.070 -14.098 0.744   1.00 13.46 ?  60  ALA   B N    1 
ATOM   4945 C  CA   . ALA   B 1 60  ? 58.476 -12.764 0.672   1.00 13.45 ?  60  ALA   B CA   1 
ATOM   4946 C  C    . ALA   B 1 60  ? 57.007 -12.789 1.073   1.00 12.68 ?  60  ALA   B C    1 
ATOM   4947 O  O    . ALA   B 1 60  ? 56.502 -11.836 1.682   1.00 13.36 ?  60  ALA   B O    1 
ATOM   4948 C  CB   . ALA   B 1 60  ? 58.634 -12.187 -0.734  1.00 14.76 ?  60  ALA   B CB   1 
ATOM   4949 H  H    . ALA   B 1 60  ? 59.361 -14.411 -0.003  1.00 16.30 ?  60  ALA   B H    1 
ATOM   4950 H  HA   . ALA   B 1 60  ? 58.943 -12.184 1.291   1.00 16.28 ?  60  ALA   B HA   1 
ATOM   4951 H  HB1  . ALA   B 1 60  ? 58.237 -11.305 -0.757  1.00 17.85 ?  60  ALA   B HB1  1 
ATOM   4952 H  HB2  . ALA   B 1 60  ? 59.582 -12.131 -0.947  1.00 17.85 ?  60  ALA   B HB2  1 
ATOM   4953 H  HB3  . ALA   B 1 60  ? 58.190 -12.772 -1.368  1.00 17.85 ?  60  ALA   B HB3  1 
ATOM   4954 N  N    . MET   B 1 61  ? 56.299 -13.866 0.725   1.00 12.10 ?  61  MET   B N    1 
ATOM   4955 C  CA   . MET   B 1 61  ? 54.903 -13.988 1.119   1.00 11.57 ?  61  MET   B CA   1 
ATOM   4956 C  C    . MET   B 1 61  ? 54.764 -13.996 2.640   1.00 11.89 ?  61  MET   B C    1 
ATOM   4957 O  O    . MET   B 1 61  ? 53.864 -13.346 3.189   1.00 11.62 ?  61  MET   B O    1 
ATOM   4958 C  CB   . MET   B 1 61  ? 54.320 -15.254 0.487   1.00 11.54 ?  61  MET   B CB   1 
ATOM   4959 C  CG   . MET   B 1 61  ? 52.881 -15.551 0.910   1.00 11.46 ?  61  MET   B CG   1 
ATOM   4960 S  SD   . MET   B 1 61  ? 52.228 -17.047 0.148   1.00 12.15 ?  61  MET   B SD   1 
ATOM   4961 C  CE   . MET   B 1 61  ? 51.974 -16.469 -1.529  1.00 13.49 ?  61  MET   B CE   1 
ATOM   4962 H  H    . MET   B 1 61  ? 56.606 -14.534 0.266   1.00 14.66 ?  61  MET   B H    1 
ATOM   4963 H  HA   . MET   B 1 61  ? 54.414 -13.233 0.758   1.00 14.03 ?  61  MET   B HA   1 
ATOM   4964 H  HB2  . MET   B 1 61  ? 54.327 -15.155 -0.483  1.00 13.99 ?  61  MET   B HB2  1 
ATOM   4965 H  HB3  . MET   B 1 61  ? 54.867 -16.013 0.738   1.00 13.99 ?  61  MET   B HB3  1 
ATOM   4966 H  HG2  . MET   B 1 61  ? 52.850 -15.674 1.872   1.00 13.90 ?  61  MET   B HG2  1 
ATOM   4967 H  HG3  . MET   B 1 61  ? 52.313 -14.809 0.650   1.00 13.90 ?  61  MET   B HG3  1 
ATOM   4968 H  HE1  . MET   B 1 61  ? 51.587 -17.184 -2.056  1.00 16.33 ?  61  MET   B HE1  1 
ATOM   4969 H  HE2  . MET   B 1 61  ? 51.376 -15.705 -1.515  1.00 16.33 ?  61  MET   B HE2  1 
ATOM   4970 H  HE3  . MET   B 1 61  ? 52.831 -16.207 -1.907  1.00 16.33 ?  61  MET   B HE3  1 
ATOM   4971 N  N    . GLN   B 1 62  ? 55.643 -14.715 3.343   1.00 11.77 ?  62  GLN   B N    1 
ATOM   4972 C  CA   . GLN   B 1 62  ? 55.534 -14.768 4.798   1.00 12.23 ?  62  GLN   B CA   1 
ATOM   4973 C  C    . GLN   B 1 62  ? 55.818 -13.411 5.428   1.00 12.50 ?  62  GLN   B C    1 
ATOM   4974 O  O    . GLN   B 1 62  ? 55.133 -13.003 6.373   1.00 13.00 ?  62  GLN   B O    1 
ATOM   4975 C  CB   . GLN   B 1 62  ? 56.481 -15.826 5.369   1.00 12.50 ?  62  GLN   B CB   1 
ATOM   4976 C  CG   . GLN   B 1 62  ? 56.260 -16.090 6.848   1.00 12.67 ?  62  GLN   B CG   1 
ATOM   4977 C  CD   . GLN   B 1 62  ? 54.883 -16.682 7.094   1.00 12.54 ?  62  GLN   B CD   1 
ATOM   4978 O  OE1  . GLN   B 1 62  ? 54.622 -17.836 6.741   1.00 12.88 ?  62  GLN   B OE1  1 
ATOM   4979 N  NE2  . GLN   B 1 62  ? 53.973 -15.884 7.650   1.00 13.12 ?  62  GLN   B NE2  1 
ATOM   4980 H  H    . GLN   B 1 62  ? 56.293 -15.173 3.005   1.00 14.26 ?  62  GLN   B H    1 
ATOM   4981 H  HA   . GLN   B 1 62  ? 54.628 -15.022 5.029   1.00 14.81 ?  62  GLN   B HA   1 
ATOM   4982 H  HB2  . GLN   B 1 62  ? 56.348 -16.664 4.894   1.00 15.14 ?  62  GLN   B HB2  1 
ATOM   4983 H  HB3  . GLN   B 1 62  ? 57.398 -15.527 5.254   1.00 15.14 ?  62  GLN   B HB3  1 
ATOM   4984 H  HG2  . GLN   B 1 62  ? 56.922 -16.723 7.164   1.00 15.35 ?  62  GLN   B HG2  1 
ATOM   4985 H  HG3  . GLN   B 1 62  ? 56.327 -15.257 7.339   1.00 15.35 ?  62  GLN   B HG3  1 
ATOM   4986 H  HE21 . GLN   B 1 62  ? 54.182 -15.079 7.869   1.00 15.88 ?  62  GLN   B HE21 1 
ATOM   4987 H  HE22 . GLN   B 1 62  ? 53.179 -16.178 7.801   1.00 15.88 ?  62  GLN   B HE22 1 
ATOM   4988 N  N    . VAL   B 1 63  ? 56.836 -12.705 4.938   1.00 12.93 ?  63  VAL   B N    1 
ATOM   4989 C  CA   . VAL   B 1 63  ? 57.144 -11.386 5.486   1.00 13.67 ?  63  VAL   B CA   1 
ATOM   4990 C  C    . VAL   B 1 63  ? 55.953 -10.449 5.305   1.00 13.08 ?  63  VAL   B C    1 
ATOM   4991 O  O    . VAL   B 1 63  ? 55.540 -9.745  6.237   1.00 13.72 ?  63  VAL   B O    1 
ATOM   4992 C  CB   . VAL   B 1 63  ? 58.436 -10.835 4.858   1.00 14.90 ?  63  VAL   B CB   1 
ATOM   4993 C  CG1  . VAL   B 1 63  ? 58.676 -9.404  5.306   1.00 15.35 ?  63  VAL   B CG1  1 
ATOM   4994 C  CG2  . VAL   B 1 63  ? 59.611 -11.718 5.250   1.00 15.56 ?  63  VAL   B CG2  1 
ATOM   4995 H  H    . VAL   B 1 63  ? 57.346 -12.960 4.290   1.00 15.65 ?  63  VAL   B H    1 
ATOM   4996 H  HA   . VAL   B 1 63  ? 57.301 -11.483 6.433   1.00 16.54 ?  63  VAL   B HA   1 
ATOM   4997 H  HB   . VAL   B 1 63  ? 58.363 -10.849 3.890   1.00 18.02 ?  63  VAL   B HB   1 
ATOM   4998 H  HG11 . VAL   B 1 63  ? 59.594 -9.163  5.108   1.00 18.56 ?  63  VAL   B HG11 1 
ATOM   4999 H  HG12 . VAL   B 1 63  ? 58.069 -8.819  4.832   1.00 18.56 ?  63  VAL   B HG12 1 
ATOM   5000 H  HG13 . VAL   B 1 63  ? 58.520 -9.347  6.262   1.00 18.56 ?  63  VAL   B HG13 1 
ATOM   5001 H  HG21 . VAL   B 1 63  ? 60.426 -11.350 4.875   1.00 18.82 ?  63  VAL   B HG21 1 
ATOM   5002 H  HG22 . VAL   B 1 63  ? 59.678 -11.743 6.220   1.00 18.82 ?  63  VAL   B HG22 1 
ATOM   5003 H  HG23 . VAL   B 1 63  ? 59.466 -12.615 4.908   1.00 18.82 ?  63  VAL   B HG23 1 
ATOM   5004 N  N    . GLU   B 1 64  ? 55.379 -10.436 4.101   1.00 12.71 ?  64  GLU   B N    1 
ATOM   5005 C  CA   . GLU   B 1 64  ? 54.211 -9.600  3.832   1.00 12.40 ?  64  GLU   B CA   1 
ATOM   5006 C  C    . GLU   B 1 64  ? 53.030 -10.002 4.709   1.00 12.01 ?  64  GLU   B C    1 
ATOM   5007 O  O    . GLU   B 1 64  ? 52.283 -9.141  5.205   1.00 12.62 ?  64  GLU   B O    1 
ATOM   5008 C  CB   . GLU   B 1 64  ? 53.848 -9.739  2.354   1.00 12.45 ?  64  GLU   B CB   1 
ATOM   5009 C  CG   . GLU   B 1 64  ? 52.580 -9.017  1.927   1.00 12.76 ?  64  GLU   B CG   1 
ATOM   5010 C  CD   . GLU   B 1 64  ? 52.049 -9.517  0.590   1.00 13.37 ?  64  GLU   B CD   1 
ATOM   5011 O  OE1  . GLU   B 1 64  ? 52.227 -10.725 0.272   1.00 14.32 ?  64  GLU   B OE1  1 
ATOM   5012 O  OE2  . GLU   B 1 64  ? 51.423 -8.703  -0.130  1.00 14.11 -1 64  GLU   B OE2  1 
ATOM   5013 H  H    . GLU   B 1 64  ? 55.648 -10.897 3.423   1.00 15.40 ?  64  GLU   B H    1 
ATOM   5014 H  HA   . GLU   B 1 64  ? 54.427 -8.673  4.013   1.00 15.02 ?  64  GLU   B HA   1 
ATOM   5015 H  HB2  . GLU   B 1 64  ? 54.573 -9.372  1.820   1.00 15.09 ?  64  GLU   B HB2  1 
ATOM   5016 H  HB3  . GLU   B 1 64  ? 53.732 -10.674 2.148   1.00 15.09 ?  64  GLU   B HB3  1 
ATOM   5017 H  HG2  . GLU   B 1 64  ? 51.876 -9.156  2.587   1.00 15.46 ?  64  GLU   B HG2  1 
ATOM   5018 H  HG3  . GLU   B 1 64  ? 52.759 -8.066  1.843   1.00 15.46 ?  64  GLU   B HG3  1 
ATOM   5019 N  N    . SER   B 1 65  ? 52.845 -11.309 4.898   1.00 11.70 ?  65  SER   B N    1 
ATOM   5020 C  CA   . SER   B 1 65  ? 51.738 -11.815 5.701   1.00 11.75 ?  65  SER   B CA   1 
ATOM   5021 C  C    . SER   B 1 65  ? 51.873 -11.417 7.164   1.00 11.80 ?  65  SER   B C    1 
ATOM   5022 O  O    . SER   B 1 65  ? 50.875 -11.047 7.799   1.00 12.47 ?  65  SER   B O    1 
ATOM   5023 C  CB   . SER   B 1 65  ? 51.653 -13.336 5.571   1.00 12.03 ?  65  SER   B CB   1 
ATOM   5024 O  OG   . SER   B 1 65  ? 51.307 -13.732 4.250   1.00 12.23 ?  65  SER   B OG   1 
ATOM   5025 H  H    . SER   B 1 65  ? 53.351 -11.930 4.572   1.00 14.18 ?  65  SER   B H    1 
ATOM   5026 H  HA   . SER   B 1 65  ? 50.908 -11.444 5.366   1.00 14.24 ?  65  SER   B HA   1 
ATOM   5027 H  HB2  . SER   B 1 65  ? 52.510 -13.722 5.795   1.00 14.58 ?  65  SER   B HB2  1 
ATOM   5028 H  HB3  . SER   B 1 65  ? 50.972 -13.665 6.184   1.00 14.58 ?  65  SER   B HB3  1 
ATOM   5029 H  HG   . SER   B 1 65  ? 51.879 -13.445 3.704   1.00 14.82 ?  65  SER   B HG   1 
ATOM   5030 N  N    . ASP   B 1 66  ? 53.081 -11.519 7.730   1.00 12.35 ?  66  ASP   B N    1 
ATOM   5031 C  CA   . ASP   B 1 66  ? 53.270 -11.121 9.123   1.00 12.60 ?  66  ASP   B CA   1 
ATOM   5032 C  C    . ASP   B 1 66  ? 52.958 -9.641  9.317   1.00 12.67 ?  66  ASP   B C    1 
ATOM   5033 O  O    . ASP   B 1 66  ? 52.377 -9.249  10.337  1.00 13.29 ?  66  ASP   B O    1 
ATOM   5034 C  CB   . ASP   B 1 66  ? 54.696 -11.436 9.579   1.00 13.62 ?  66  ASP   B CB   1 
ATOM   5035 C  CG   . ASP   B 1 66  ? 54.956 -12.932 9.741   1.00 15.67 ?  66  ASP   B CG   1 
ATOM   5036 O  OD1  . ASP   B 1 66  ? 54.003 -13.740 9.667   1.00 16.45 ?  66  ASP   B OD1  1 
ATOM   5037 O  OD2  . ASP   B 1 66  ? 56.133 -13.302 9.958   1.00 18.36 -1 66  ASP   B OD2  1 
ATOM   5038 H  H    . ASP   B 1 66  ? 53.783 -11.821 7.341   1.00 14.96 ?  66  ASP   B H    1 
ATOM   5039 H  HA   . ASP   B 1 66  ? 52.662 -11.624 9.687   1.00 15.27 ?  66  ASP   B HA   1 
ATOM   5040 H  HB2  . ASP   B 1 66  ? 55.321 -11.093 8.920   1.00 16.49 ?  66  ASP   B HB2  1 
ATOM   5041 H  HB3  . ASP   B 1 66  ? 54.856 -11.005 10.437  1.00 16.49 ?  66  ASP   B HB3  1 
ATOM   5042 N  N    . ASP   B 1 67  ? 53.331 -8.801  8.351   1.00 12.36 ?  67  ASP   B N    1 
ATOM   5043 C  CA   . ASP   B 1 67  ? 52.986 -7.387  8.434   1.00 12.91 ?  67  ASP   B CA   1 
ATOM   5044 C  C    . ASP   B 1 67  ? 51.475 -7.180  8.353   1.00 13.02 ?  67  ASP   B C    1 
ATOM   5045 O  O    . ASP   B 1 67  ? 50.912 -6.374  9.104   1.00 13.77 ?  67  ASP   B O    1 
ATOM   5046 C  CB   . ASP   B 1 67  ? 53.706 -6.616  7.334   1.00 14.32 ?  67  ASP   B CB   1 
ATOM   5047 C  CG   . ASP   B 1 67  ? 53.284 -5.174  7.285   1.00 15.85 ?  67  ASP   B CG   1 
ATOM   5048 O  OD1  . ASP   B 1 67  ? 53.786 -4.359  8.096   1.00 17.22 ?  67  ASP   B OD1  1 
ATOM   5049 O  OD2  . ASP   B 1 67  ? 52.419 -4.875  6.449   1.00 16.84 -1 67  ASP   B OD2  1 
ATOM   5050 H  H    . ASP   B 1 67  ? 53.790 -9.022  7.657   1.00 14.97 ?  67  ASP   B H    1 
ATOM   5051 H  HA   . ASP   B 1 67  ? 53.290 -7.038  9.286   1.00 15.64 ?  67  ASP   B HA   1 
ATOM   5052 H  HB2  . ASP   B 1 67  ? 54.663 -6.646  7.493   1.00 17.32 ?  67  ASP   B HB2  1 
ATOM   5053 H  HB3  . ASP   B 1 67  ? 53.503 -7.024  6.474   1.00 17.32 ?  67  ASP   B HB3  1 
ATOM   5054 N  N    . TYR   B 1 68  ? 50.797 -7.913  7.462   1.00 12.85 ?  68  TYR   B N    1 
ATOM   5055 C  CA   . TYR   B 1 68  ? 49.340 -7.835  7.390   1.00 13.56 ?  68  TYR   B CA   1 
ATOM   5056 C  C    . TYR   B 1 68  ? 48.705 -8.172  8.736   1.00 13.20 ?  68  TYR   B C    1 
ATOM   5057 O  O    . TYR   B 1 68  ? 47.770 -7.493  9.179   1.00 14.02 ?  68  TYR   B O    1 
ATOM   5058 C  CB   . TYR   B 1 68  ? 48.805 -8.768  6.298   1.00 14.39 ?  68  TYR   B CB   1 
ATOM   5059 C  CG   . TYR   B 1 68  ? 47.300 -8.921  6.360   1.00 15.33 ?  68  TYR   B CG   1 
ATOM   5060 C  CD1  . TYR   B 1 68  ? 46.713 -9.875  7.188   1.00 16.25 ?  68  TYR   B CD1  1 
ATOM   5061 C  CD2  . TYR   B 1 68  ? 46.468 -8.089  5.631   1.00 16.31 ?  68  TYR   B CD2  1 
ATOM   5062 C  CE1  . TYR   B 1 68  ? 45.346 -9.999  7.277   1.00 17.30 ?  68  TYR   B CE1  1 
ATOM   5063 C  CE2  . TYR   B 1 68  ? 45.087 -8.218  5.707   1.00 16.94 ?  68  TYR   B CE2  1 
ATOM   5064 C  CZ   . TYR   B 1 68  ? 44.545 -9.169  6.534   1.00 17.48 ?  68  TYR   B CZ   1 
ATOM   5065 O  OH   . TYR   B 1 68  ? 43.178 -9.284  6.622   1.00 18.71 ?  68  TYR   B OH   1 
ATOM   5066 H  H    . TYR   B 1 68  ? 51.156 -8.468  6.903   1.00 15.56 ?  68  TYR   B H    1 
ATOM   5067 H  HA   . TYR   B 1 68  ? 49.092 -6.929  7.161   1.00 16.41 ?  68  TYR   B HA   1 
ATOM   5068 H  HB2  . TYR   B 1 68  ? 49.032 -8.402  5.431   1.00 17.41 ?  68  TYR   B HB2  1 
ATOM   5069 H  HB3  . TYR   B 1 68  ? 49.202 -9.646  6.407   1.00 17.41 ?  68  TYR   B HB3  1 
ATOM   5070 H  HD1  . TYR   B 1 68  ? 47.253 -10.445 7.692   1.00 19.64 ?  68  TYR   B HD1  1 
ATOM   5071 H  HD2  . TYR   B 1 68  ? 46.840 -7.440  5.085   1.00 19.71 ?  68  TYR   B HD2  1 
ATOM   5072 H  HE1  . TYR   B 1 68  ? 44.961 -10.654 7.822   1.00 20.90 ?  68  TYR   B HE1  1 
ATOM   5073 H  HE2  . TYR   B 1 68  ? 44.533 -7.654  5.217   1.00 20.47 ?  68  TYR   B HE2  1 
ATOM   5074 H  HH   . TYR   B 1 68  ? 42.794 -8.729  6.112   1.00 22.60 ?  68  TYR   B HH   1 
ATOM   5075 N  N    . ILE   B 1 69  ? 49.183 -9.239  9.386   1.00 12.97 ?  69  ILE   B N    1 
ATOM   5076 C  CA   . ILE   B 1 69  ? 48.624 -9.665  10.666  1.00 13.60 ?  69  ILE   B CA   1 
ATOM   5077 C  C    . ILE   B 1 69  ? 48.882 -8.624  11.748  1.00 13.25 ?  69  ILE   B C    1 
ATOM   5078 O  O    . ILE   B 1 69  ? 48.015 -8.355  12.587  1.00 13.56 ?  69  ILE   B O    1 
ATOM   5079 C  CB   . ILE   B 1 69  ? 49.198 -11.041 11.054  1.00 14.36 ?  69  ILE   B CB   1 
ATOM   5080 C  CG1  . ILE   B 1 69  ? 48.668 -12.139 10.127  1.00 14.80 ?  69  ILE   B CG1  1 
ATOM   5081 C  CG2  . ILE   B 1 69  ? 48.912 -11.359 12.516  1.00 15.25 ?  69  ILE   B CG2  1 
ATOM   5082 C  CD1  . ILE   B 1 69  ? 47.193 -12.461 10.308  1.00 15.07 ?  69  ILE   B CD1  1 
ATOM   5083 H  H    . ILE   B 1 69  ? 49.834 -9.724  9.111   1.00 15.70 ?  69  ILE   B H    1 
ATOM   5084 H  HA   . ILE   B 1 69  ? 47.665 -9.759  10.570  1.00 16.46 ?  69  ILE   B HA   1 
ATOM   5085 H  HB   . ILE   B 1 69  ? 50.162 -11.000 10.944  1.00 17.37 ?  69  ILE   B HB   1 
ATOM   5086 H  HG12 . ILE   B 1 69  ? 48.798 -11.854 9.208   1.00 17.90 ?  69  ILE   B HG12 1 
ATOM   5087 H  HG13 . ILE   B 1 69  ? 49.172 -12.951 10.291  1.00 17.90 ?  69  ILE   B HG13 1 
ATOM   5088 H  HG21 . ILE   B 1 69  ? 49.042 -12.309 12.660  1.00 18.44 ?  69  ILE   B HG21 1 
ATOM   5089 H  HG22 . ILE   B 1 69  ? 49.526 -10.857 13.078  1.00 18.44 ?  69  ILE   B HG22 1 
ATOM   5090 H  HG23 . ILE   B 1 69  ? 47.997 -11.116 12.721  1.00 18.44 ?  69  ILE   B HG23 1 
ATOM   5091 H  HD11 . ILE   B 1 69  ? 46.949 -13.154 9.676   1.00 18.23 ?  69  ILE   B HD11 1 
ATOM   5092 H  HD12 . ILE   B 1 69  ? 47.047 -12.775 11.213  1.00 18.23 ?  69  ILE   B HD12 1 
ATOM   5093 H  HD13 . ILE   B 1 69  ? 46.670 -11.663 10.143  1.00 18.23 ?  69  ILE   B HD13 1 
ATOM   5094 N  N    . ALA   B 1 70  ? 50.079 -8.038  11.769  1.00 13.30 ?  70  ALA   B N    1 
ATOM   5095 C  CA   . ALA   B 1 70  ? 50.360 -7.003  12.757  1.00 13.15 ?  70  ALA   B CA   1 
ATOM   5096 C  C    . ALA   B 1 70  ? 49.362 -5.858  12.646  1.00 13.44 ?  70  ALA   B C    1 
ATOM   5097 O  O    . ALA   B 1 70  ? 48.920 -5.311  13.659  1.00 13.80 ?  70  ALA   B O    1 
ATOM   5098 C  CB   . ALA   B 1 70  ? 51.789 -6.492  12.585  1.00 13.82 ?  70  ALA   B CB   1 
ATOM   5099 H  H    . ALA   B 1 70  ? 50.720 -8.219  11.236  1.00 16.10 ?  70  ALA   B H    1 
ATOM   5100 H  HA   . ALA   B 1 70  ? 50.284 -7.382  13.646  1.00 15.92 ?  70  ALA   B HA   1 
ATOM   5101 H  HB1  . ALA   B 1 70  ? 51.975 -5.831  13.270  1.00 16.73 ?  70  ALA   B HB1  1 
ATOM   5102 H  HB2  . ALA   B 1 70  ? 52.405 -7.239  12.675  1.00 16.73 ?  70  ALA   B HB2  1 
ATOM   5103 H  HB3  . ALA   B 1 70  ? 51.882 -6.095  11.705  1.00 16.73 ?  70  ALA   B HB3  1 
ATOM   5104 N  N    . THR   B 1 71  ? 48.986 -5.495  11.423  1.00 13.65 ?  71  THR   B N    1 
ATOM   5105 C  CA   . THR   B 1 71  ? 48.098 -4.357  11.212  1.00 14.61 ?  71  THR   B CA   1 
ATOM   5106 C  C    . THR   B 1 71  ? 46.631 -4.720  11.418  1.00 15.30 ?  71  THR   B C    1 
ATOM   5107 O  O    . THR   B 1 71  ? 45.854 -3.902  11.932  1.00 16.86 ?  71  THR   B O    1 
ATOM   5108 C  CB   . THR   B 1 71  ? 48.318 -3.798  9.804   1.00 16.45 ?  71  THR   B CB   1 
ATOM   5109 O  OG1  . THR   B 1 71  ? 49.640 -3.254  9.707   1.00 18.47 ?  71  THR   B OG1  1 
ATOM   5110 C  CG2  . THR   B 1 71  ? 47.294 -2.718  9.468   1.00 17.23 ?  71  THR   B CG2  1 
ATOM   5111 H  H    . THR   B 1 71  ? 49.231 -5.890  10.700  1.00 16.52 ?  71  THR   B H    1 
ATOM   5112 H  HA   . THR   B 1 71  ? 48.325 -3.659  11.844  1.00 17.67 ?  71  THR   B HA   1 
ATOM   5113 H  HB   . THR   B 1 71  ? 48.231 -4.510  9.153   1.00 19.88 ?  71  THR   B HB   1 
ATOM   5114 H  HG1  . THR   B 1 71  ? 49.770 -2.927  8.939   1.00 22.31 ?  71  THR   B HG1  1 
ATOM   5115 H  HG21 . THR   B 1 71  ? 47.602 -2.193  8.710   1.00 20.82 ?  71  THR   B HG21 1 
ATOM   5116 H  HG22 . THR   B 1 71  ? 46.444 -3.122  9.245   1.00 20.82 ?  71  THR   B HG22 1 
ATOM   5117 H  HG23 . THR   B 1 71  ? 47.177 -2.126  10.228  1.00 20.82 ?  71  THR   B HG23 1 
ATOM   5118 N  N    . ASN   B 1 72  ? 46.232 -5.933  11.022  1.00 14.94 ?  72  ASN   B N    1 
ATOM   5119 C  CA   . ASN   B 1 72  ? 44.827 -6.290  10.896  1.00 15.42 ?  72  ASN   B CA   1 
ATOM   5120 C  C    . ASN   B 1 72  ? 44.356 -7.387  11.840  1.00 15.98 ?  72  ASN   B C    1 
ATOM   5121 O  O    . ASN   B 1 72  ? 43.141 -7.548  12.003  1.00 17.12 ?  72  ASN   B O    1 
ATOM   5122 C  CB   . ASN   B 1 72  ? 44.516 -6.718  9.452   1.00 16.16 ?  72  ASN   B CB   1 
ATOM   5123 C  CG   . ASN   B 1 72  ? 44.795 -5.620  8.452   1.00 17.19 ?  72  ASN   B CG   1 
ATOM   5124 O  OD1  . ASN   B 1 72  ? 45.814 -5.634  7.758   1.00 18.32 ?  72  ASN   B OD1  1 
ATOM   5125 N  ND2  . ASN   B 1 72  ? 43.912 -4.641  8.398   1.00 18.55 ?  72  ASN   B ND2  1 
ATOM   5126 H  H    . ASN   B 1 72  ? 46.770 -6.578  10.817  1.00 18.07 ?  72  ASN   B H    1 
ATOM   5127 H  HA   . ASN   B 1 72  ? 44.297 -5.503  11.079  1.00 18.65 ?  72  ASN   B HA   1 
ATOM   5128 H  HB2  . ASN   B 1 72  ? 45.072 -7.482  9.217   1.00 19.54 ?  72  ASN   B HB2  1 
ATOM   5129 H  HB3  . ASN   B 1 72  ? 43.581 -6.956  9.382   1.00 19.54 ?  72  ASN   B HB3  1 
ATOM   5130 H  HD21 . ASN   B 1 72  ? 44.018 -3.988  7.845   1.00 22.40 ?  72  ASN   B HD21 1 
ATOM   5131 H  HD22 . ASN   B 1 72  ? 43.212 -4.662  8.901   1.00 22.40 ?  72  ASN   B HD22 1 
ATOM   5132 N  N    . GLY   B 1 73  ? 45.259 -8.135  12.465  1.00 15.41 ?  73  GLY   B N    1 
ATOM   5133 C  CA   . GLY   B 1 73  ? 44.862 -9.276  13.254  1.00 14.96 ?  73  GLY   B CA   1 
ATOM   5134 C  C    . GLY   B 1 73  ? 44.500 -10.461 12.386  1.00 13.75 ?  73  GLY   B C    1 
ATOM   5135 O  O    . GLY   B 1 73  ? 44.497 -10.382 11.155  1.00 13.57 ?  73  GLY   B O    1 
ATOM   5136 H  H    . GLY   B 1 73  ? 46.110 -7.999  12.443  1.00 18.63 ?  73  GLY   B H    1 
ATOM   5137 H  HA2  . GLY   B 1 73  ? 45.590 -9.533  13.843  1.00 18.09 ?  73  GLY   B HA2  1 
ATOM   5138 H  HA3  . GLY   B 1 73  ? 44.093 -9.045  13.797  1.00 18.09 ?  73  GLY   B HA3  1 
ATOM   5139 N  N    . PRO   B 1 74  ? 44.186 -11.586 13.024  1.00 13.88 ?  74  PRO   B N    1 
ATOM   5140 C  CA   . PRO   B 1 74  ? 43.936 -12.820 12.278  1.00 13.44 ?  74  PRO   B CA   1 
ATOM   5141 C  C    . PRO   B 1 74  ? 42.634 -12.767 11.492  1.00 12.97 ?  74  PRO   B C    1 
ATOM   5142 O  O    . PRO   B 1 74  ? 41.692 -12.035 11.816  1.00 14.21 ?  74  PRO   B O    1 
ATOM   5143 C  CB   . PRO   B 1 74  ? 43.868 -13.885 13.380  1.00 14.73 ?  74  PRO   B CB   1 
ATOM   5144 C  CG   . PRO   B 1 74  ? 43.419 -13.136 14.590  1.00 16.15 ?  74  PRO   B CG   1 
ATOM   5145 C  CD   . PRO   B 1 74  ? 44.072 -11.785 14.478  1.00 15.62 ?  74  PRO   B CD   1 
ATOM   5146 H  HA   . PRO   B 1 74  ? 44.678 -13.013 11.679  1.00 16.27 ?  74  PRO   B HA   1 
ATOM   5147 H  HB2  . PRO   B 1 74  ? 43.226 -14.568 13.134  1.00 17.82 ?  74  PRO   B HB2  1 
ATOM   5148 H  HB3  . PRO   B 1 74  ? 44.749 -14.270 13.517  1.00 17.82 ?  74  PRO   B HB3  1 
ATOM   5149 H  HG2  . PRO   B 1 74  ? 42.453 -13.051 14.581  1.00 19.52 ?  74  PRO   B HG2  1 
ATOM   5150 H  HG3  . PRO   B 1 74  ? 43.717 -13.597 15.388  1.00 19.52 ?  74  PRO   B HG3  1 
ATOM   5151 H  HD2  . PRO   B 1 74  ? 43.505 -11.102 14.877  1.00 18.88 ?  74  PRO   B HD2  1 
ATOM   5152 H  HD3  . PRO   B 1 74  ? 44.951 -11.797 14.888  1.00 18.88 ?  74  PRO   B HD3  1 
ATOM   5153 N  N    . LEU   B 1 75  ? 42.602 -13.577 10.438  1.00 12.30 ?  75  LEU   B N    1 
ATOM   5154 C  CA   . LEU   B 1 75  ? 41.392 -13.798 9.668   1.00 12.52 ?  75  LEU   B CA   1 
ATOM   5155 C  C    . LEU   B 1 75  ? 40.414 -14.655 10.468  1.00 12.97 ?  75  LEU   B C    1 
ATOM   5156 O  O    . LEU   B 1 75  ? 40.754 -15.225 11.505  1.00 13.93 ?  75  LEU   B O    1 
ATOM   5157 C  CB   . LEU   B 1 75  ? 41.723 -14.517 8.360   1.00 12.62 ?  75  LEU   B CB   1 
ATOM   5158 C  CG   . LEU   B 1 75  ? 42.568 -13.772 7.322   1.00 14.40 ?  75  LEU   B CG   1 
ATOM   5159 C  CD1  . LEU   B 1 75  ? 42.766 -14.611 6.061   1.00 15.74 ?  75  LEU   B CD1  1 
ATOM   5160 C  CD2  . LEU   B 1 75  ? 41.975 -12.433 6.978   1.00 17.50 ?  75  LEU   B CD2  1 
ATOM   5161 H  H    . LEU   B 1 75  ? 43.281 -14.019 10.141  1.00 14.90 ?  75  LEU   B H    1 
ATOM   5162 H  HA   . LEU   B 1 75  ? 40.968 -12.954 9.464   1.00 15.16 ?  75  LEU   B HA   1 
ATOM   5163 H  HB2  . LEU   B 1 75  ? 42.201 -15.334 8.576   1.00 15.29 ?  75  LEU   B HB2  1 
ATOM   5164 H  HB3  . LEU   B 1 75  ? 40.887 -14.750 7.923   1.00 15.29 ?  75  LEU   B HB3  1 
ATOM   5165 H  HG   . LEU   B 1 75  ? 43.447 -13.615 7.700   1.00 17.42 ?  75  LEU   B HG   1 
ATOM   5166 H  HD11 . LEU   B 1 75  ? 43.311 -14.111 5.427   1.00 19.03 ?  75  LEU   B HD11 1 
ATOM   5167 H  HD12 . LEU   B 1 75  ? 43.217 -15.440 6.293   1.00 19.03 ?  75  LEU   B HD12 1 
ATOM   5168 H  HD13 . LEU   B 1 75  ? 41.902 -14.806 5.666   1.00 19.03 ?  75  LEU   B HD13 1 
ATOM   5169 H  HD21 . LEU   B 1 75  ? 42.481 -12.040 6.250   1.00 21.14 ?  75  LEU   B HD21 1 
ATOM   5170 H  HD22 . LEU   B 1 75  ? 41.052 -12.557 6.712   1.00 21.14 ?  75  LEU   B HD22 1 
ATOM   5171 H  HD23 . LEU   B 1 75  ? 42.022 -11.860 7.760   1.00 21.14 ?  75  LEU   B HD23 1 
ATOM   5172 N  N    . LYS   B 1 76  ? 39.182 -14.740 9.966   1.00 14.36 ?  76  LYS   B N    1 
ATOM   5173 C  CA   . LYS   B 1 76  ? 38.200 -15.703 10.443  1.00 15.63 ?  76  LYS   B CA   1 
ATOM   5174 C  C    . LYS   B 1 76  ? 38.294 -16.975 9.604   1.00 14.11 ?  76  LYS   B C    1 
ATOM   5175 O  O    . LYS   B 1 76  ? 38.565 -16.917 8.404   1.00 13.82 ?  76  LYS   B O    1 
ATOM   5176 C  CB   . LYS   B 1 76  ? 36.779 -15.140 10.274  1.00 17.75 ?  76  LYS   B CB   1 
ATOM   5177 C  CG   . LYS   B 1 76  ? 36.502 -13.753 10.880  1.00 19.68 ?  76  LYS   B CG   1 
ATOM   5178 C  CD   . LYS   B 1 76  ? 35.091 -13.238 10.528  1.00 20.85 ?  76  LYS   B CD   1 
ATOM   5179 C  CE   . LYS   B 1 76  ? 34.823 -11.862 11.122  1.00 22.62 ?  76  LYS   B CE   1 
ATOM   5180 N  NZ   . LYS   B 1 76  ? 33.521 -11.277 10.688  1.00 23.11 ?  76  LYS   B NZ   1 
ATOM   5181 H  H    . LYS   B 1 76  ? 38.892 -14.244 9.329   1.00 17.38 ?  76  LYS   B H    1 
ATOM   5182 H  HA   . LYS   B 1 76  ? 38.357 -15.924 11.375  1.00 18.90 ?  76  LYS   B HA   1 
ATOM   5183 H  HB2  . LYS   B 1 76  ? 36.590 -15.082 9.325   1.00 21.44 ?  76  LYS   B HB2  1 
ATOM   5184 H  HB3  . LYS   B 1 76  ? 36.158 -15.761 10.686  1.00 21.44 ?  76  LYS   B HB3  1 
ATOM   5185 H  HG2  . LYS   B 1 76  ? 36.577 -13.808 11.846  1.00 23.75 ?  76  LYS   B HG2  1 
ATOM   5186 H  HG3  . LYS   B 1 76  ? 37.155 -13.121 10.533  1.00 23.75 ?  76  LYS   B HG3  1 
ATOM   5187 H  HD2  . LYS   B 1 76  ? 35.009 -13.174 9.563   1.00 25.17 ?  76  LYS   B HD2  1 
ATOM   5188 H  HD3  . LYS   B 1 76  ? 34.432 -13.855 10.879  1.00 25.17 ?  76  LYS   B HD3  1 
ATOM   5189 H  HE2  . LYS   B 1 76  ? 34.811 -11.937 12.088  1.00 27.28 ?  76  LYS   B HE2  1 
ATOM   5190 H  HE3  . LYS   B 1 76  ? 35.530 -11.259 10.845  1.00 27.28 ?  76  LYS   B HE3  1 
ATOM   5191 H  HZ1  . LYS   B 1 76  ? 33.408 -10.474 11.059  1.00 27.87 ?  76  LYS   B HZ1  1 
ATOM   5192 H  HZ2  . LYS   B 1 76  ? 33.505 -11.187 9.802   1.00 27.87 ?  76  LYS   B HZ2  1 
ATOM   5193 H  HZ3  . LYS   B 1 76  ? 32.849 -11.805 10.936  1.00 27.87 ?  76  LYS   B HZ3  1 
ATOM   5194 N  N    . VAL   B 1 77  ? 38.047 -18.129 10.235  1.00 14.66 ?  77  VAL   B N    1 
ATOM   5195 C  CA   . VAL   B 1 77  ? 37.837 -19.344 9.454   1.00 14.74 ?  77  VAL   B CA   1 
ATOM   5196 C  C    . VAL   B 1 77  ? 36.645 -19.114 8.538   1.00 13.62 ?  77  VAL   B C    1 
ATOM   5197 O  O    . VAL   B 1 77  ? 35.580 -18.669 8.983   1.00 13.90 ?  77  VAL   B O    1 
ATOM   5198 C  CB   . VAL   B 1 77  ? 37.632 -20.558 10.371  1.00 16.56 ?  77  VAL   B CB   1 
ATOM   5199 C  CG1  . VAL   B 1 77  ? 37.351 -21.797 9.533   1.00 17.18 ?  77  VAL   B CG1  1 
ATOM   5200 C  CG2  . VAL   B 1 77  ? 38.858 -20.777 11.257  1.00 18.03 ?  77  VAL   B CG2  1 
ATOM   5201 H  H    . VAL   B 1 77  ? 37.990 -18.230 11.083  1.00 17.73 ?  77  VAL   B H    1 
ATOM   5202 H  HA   . VAL   B 1 77  ? 38.611 -19.509 8.898   1.00 17.83 ?  77  VAL   B HA   1 
ATOM   5203 H  HB   . VAL   B 1 77  ? 36.861 -20.400 10.942  1.00 20.02 ?  77  VAL   B HB   1 
ATOM   5204 H  HG11 . VAL   B 1 77  ? 37.405 -22.579 10.103  1.00 20.76 ?  77  VAL   B HG11 1 
ATOM   5205 H  HG12 . VAL   B 1 77  ? 36.457 -21.730 9.153   1.00 20.76 ?  77  VAL   B HG12 1 
ATOM   5206 H  HG13 . VAL   B 1 77  ? 38.008 -21.855 8.825   1.00 20.76 ?  77  VAL   B HG13 1 
ATOM   5207 H  HG21 . VAL   B 1 77  ? 38.717 -21.573 11.788  1.00 21.77 ?  77  VAL   B HG21 1 
ATOM   5208 H  HG22 . VAL   B 1 77  ? 39.634 -20.882 10.690  1.00 21.77 ?  77  VAL   B HG22 1 
ATOM   5209 H  HG23 . VAL   B 1 77  ? 38.965 -20.005 11.833  1.00 21.77 ?  77  VAL   B HG23 1 
ATOM   5210 N  N    . GLY   B 1 78  ? 36.825 -19.394 7.248   1.00 12.91 ?  78  GLY   B N    1 
ATOM   5211 C  CA   . GLY   B 1 78  ? 35.846 -19.067 6.239   1.00 12.66 ?  78  GLY   B CA   1 
ATOM   5212 C  C    . GLY   B 1 78  ? 36.089 -17.749 5.540   1.00 12.37 ?  78  GLY   B C    1 
ATOM   5213 O  O    . GLY   B 1 78  ? 35.404 -17.461 4.552   1.00 12.78 ?  78  GLY   B O    1 
ATOM   5214 H  H    . GLY   B 1 78  ? 37.518 -19.791 6.931   1.00 15.64 ?  78  GLY   B H    1 
ATOM   5215 H  HA2  . GLY   B 1 78  ? 35.833 -19.759 5.564   1.00 15.34 ?  78  GLY   B HA2  1 
ATOM   5216 H  HA3  . GLY   B 1 78  ? 34.964 -19.027 6.647   1.00 15.34 ?  78  GLY   B HA3  1 
ATOM   5217 N  N    . GLY   B 1 79  ? 37.041 -16.944 6.024   1.00 12.37 ?  79  GLY   B N    1 
ATOM   5218 C  CA   . GLY   B 1 79  ? 37.338 -15.650 5.447   1.00 11.94 ?  79  GLY   B CA   1 
ATOM   5219 C  C    . GLY   B 1 79  ? 38.573 -15.674 4.553   1.00 11.52 ?  79  GLY   B C    1 
ATOM   5220 O  O    . GLY   B 1 79  ? 39.186 -16.711 4.306   1.00 11.89 ?  79  GLY   B O    1 
ATOM   5221 H  H    . GLY   B 1 79  ? 37.539 -17.137 6.697   1.00 14.98 ?  79  GLY   B H    1 
ATOM   5222 H  HA2  . GLY   B 1 79  ? 36.584 -15.348 4.917   1.00 14.47 ?  79  GLY   B HA2  1 
ATOM   5223 H  HA3  . GLY   B 1 79  ? 37.494 -15.007 6.155   1.00 14.47 ?  79  GLY   B HA3  1 
ATOM   5224 N  N    . SER   B 1 80  ? 38.941 -14.481 4.077   1.00 11.50 ?  80  SER   B N    1 
ATOM   5225 C  CA   . SER   B 1 80  ? 40.047 -14.348 3.137   1.00 11.23 ?  80  SER   B CA   1 
ATOM   5226 C  C    . SER   B 1 80  ? 40.630 -12.941 3.192   1.00 11.12 ?  80  SER   B C    1 
ATOM   5227 O  O    . SER   B 1 80  ? 40.012 -12.002 3.700   1.00 12.16 ?  80  SER   B O    1 
ATOM   5228 C  CB   . SER   B 1 80  ? 39.599 -14.640 1.700   1.00 11.76 ?  80  SER   B CB   1 
ATOM   5229 O  OG   . SER   B 1 80  ? 38.763 -13.612 1.197   1.00 12.85 ?  80  SER   B OG   1 
ATOM   5230 H  H    . SER   B 1 80  ? 38.574 -13.737 4.289   1.00 13.94 ?  80  SER   B H    1 
ATOM   5231 H  HA   . SER   B 1 80  ? 40.740 -14.978 3.379   1.00 13.61 ?  80  SER   B HA   1 
ATOM   5232 H  HB2  . SER   B 1 80  ? 40.382 -14.705 1.131   1.00 14.25 ?  80  SER   B HB2  1 
ATOM   5233 H  HB3  . SER   B 1 80  ? 39.109 -15.476 1.685   1.00 14.25 ?  80  SER   B HB3  1 
ATOM   5234 H  HG   . SER   B 1 80  ? 38.073 -13.542 1.679   1.00 15.56 ?  80  SER   B HG   1 
ATOM   5235 N  N    . CYS   B 1 81  ? 41.823 -12.804 2.615   1.00 10.98 ?  81  CYS   B N    1 
ATOM   5236 C  CA   . CYS   B 1 81  ? 42.366 -11.492 2.295   1.00 11.02 ?  81  CYS   B CA   1 
ATOM   5237 C  C    . CYS   B 1 81  ? 43.132 -11.577 0.984   1.00 10.23 ?  81  CYS   B C    1 
ATOM   5238 O  O    . CYS   B 1 81  ? 43.645 -12.640 0.609   1.00 11.45 ?  81  CYS   B O    1 
ATOM   5239 C  CB   . CYS   B 1 81  ? 43.260 -10.931 3.412   1.00 11.98 ?  81  CYS   B CB   1 
ATOM   5240 S  SG   . CYS   B 1 81  ? 44.781 -11.872 3.671   1.00 12.18 ?  81  CYS   B SG   1 
ATOM   5241 H  H    . CYS   B 1 81  ? 42.340 -13.459 2.390   1.00 13.32 ?  81  CYS   B H    1 
ATOM   5242 H  HA   . CYS   B 1 81  ? 41.630 -10.873 2.168   1.00 13.37 ?  81  CYS   B HA   1 
ATOM   5243 H  HB2  . CYS   B 1 81  ? 43.509 -10.021 3.188   1.00 14.52 ?  81  CYS   B HB2  1 
ATOM   5244 H  HB3  . CYS   B 1 81  ? 42.757 -10.935 4.245   1.00 14.52 ?  81  CYS   B HB3  1 
ATOM   5245 H  HG   . CYS   B 1 81  ? 45.405 -11.362 4.568   1.00 14.76 ?  81  CYS   B HG   1 
ATOM   5246 N  N    . VAL   B 1 82  ? 43.237 -10.430 0.311   1.00 10.84 ?  82  VAL   B N    1 
ATOM   5247 C  CA   . VAL   B 1 82  ? 44.004 -10.303 -0.926  1.00 11.07 ?  82  VAL   B CA   1 
ATOM   5248 C  C    . VAL   B 1 82  ? 45.348 -9.662  -0.606  1.00 11.50 ?  82  VAL   B C    1 
ATOM   5249 O  O    . VAL   B 1 82  ? 45.402 -8.545  -0.072  1.00 12.34 ?  82  VAL   B O    1 
ATOM   5250 C  CB   . VAL   B 1 82  ? 43.258 -9.464  -1.975  1.00 12.11 ?  82  VAL   B CB   1 
ATOM   5251 C  CG1  . VAL   B 1 82  ? 44.109 -9.323  -3.233  1.00 13.39 ?  82  VAL   B CG1  1 
ATOM   5252 C  CG2  . VAL   B 1 82  ? 41.901 -10.062 -2.293  1.00 13.16 ?  82  VAL   B CG2  1 
ATOM   5253 H  H    . VAL   B 1 82  ? 42.856 -9.692  0.552   1.00 13.15 ?  82  VAL   B H    1 
ATOM   5254 H  HA   . VAL   B 1 82  ? 44.163 -11.182 -1.297  1.00 13.43 ?  82  VAL   B HA   1 
ATOM   5255 H  HB   . VAL   B 1 82  ? 43.110 -8.577  -1.622  1.00 14.67 ?  82  VAL   B HB   1 
ATOM   5256 H  HG11 . VAL   B 1 82  ? 43.552 -9.012  -3.963  1.00 16.21 ?  82  VAL   B HG11 1 
ATOM   5257 H  HG12 . VAL   B 1 82  ? 44.819 -8.678  -3.066  1.00 16.21 ?  82  VAL   B HG12 1 
ATOM   5258 H  HG13 . VAL   B 1 82  ? 44.495 -10.184 -3.456  1.00 16.21 ?  82  VAL   B HG13 1 
ATOM   5259 H  HG21 . VAL   B 1 82  ? 41.470 -9.533  -2.985  1.00 15.94 ?  82  VAL   B HG21 1 
ATOM   5260 H  HG22 . VAL   B 1 82  ? 42.016 -10.976 -2.603  1.00 15.94 ?  82  VAL   B HG22 1 
ATOM   5261 H  HG23 . VAL   B 1 82  ? 41.354 -10.056 -1.490  1.00 15.94 ?  82  VAL   B HG23 1 
ATOM   5262 N  N    . LEU   B 1 83  ? 46.428 -10.353 -0.967  1.00 11.04 ?  83  LEU   B N    1 
ATOM   5263 C  CA   . LEU   B 1 83  ? 47.785 -9.839  -0.851  1.00 10.88 ?  83  LEU   B CA   1 
ATOM   5264 C  C    . LEU   B 1 83  ? 48.485 -9.986  -2.203  1.00 10.78 ?  83  LEU   B C    1 
ATOM   5265 O  O    . LEU   B 1 83  ? 47.881 -10.404 -3.193  1.00 10.87 ?  83  LEU   B O    1 
ATOM   5266 C  CB   . LEU   B 1 83  ? 48.537 -10.521 0.301   1.00 11.51 ?  83  LEU   B CB   1 
ATOM   5267 C  CG   . LEU   B 1 83  ? 48.028 -10.154 1.700   1.00 12.77 ?  83  LEU   B CG   1 
ATOM   5268 C  CD1  . LEU   B 1 83  ? 48.646 -11.021 2.780   1.00 13.37 ?  83  LEU   B CD1  1 
ATOM   5269 C  CD2  . LEU   B 1 83  ? 48.247 -8.669  2.016   1.00 13.67 ?  83  LEU   B CD2  1 
ATOM   5270 H  H    . LEU   B 1 83  ? 46.387 -11.152 -1.292  1.00 13.39 ?  83  LEU   B H    1 
ATOM   5271 H  HA   . LEU   B 1 83  ? 47.734 -8.895  -0.653  1.00 13.20 ?  83  LEU   B HA   1 
ATOM   5272 H  HB2  . LEU   B 1 83  ? 48.455 -11.482 0.201   1.00 13.96 ?  83  LEU   B HB2  1 
ATOM   5273 H  HB3  . LEU   B 1 83  ? 49.471 -10.266 0.250   1.00 13.96 ?  83  LEU   B HB3  1 
ATOM   5274 H  HG   . LEU   B 1 83  ? 47.075 -10.310 1.720   1.00 15.47 ?  83  LEU   B HG   1 
ATOM   5275 H  HD11 . LEU   B 1 83  ? 48.285 -10.756 3.642   1.00 16.19 ?  83  LEU   B HD11 1 
ATOM   5276 H  HD12 . LEU   B 1 83  ? 48.424 -11.951 2.604   1.00 16.19 ?  83  LEU   B HD12 1 
ATOM   5277 H  HD13 . LEU   B 1 83  ? 49.608 -10.905 2.774   1.00 16.19 ?  83  LEU   B HD13 1 
ATOM   5278 H  HD21 . LEU   B 1 83  ? 48.053 -8.515  2.953   1.00 16.54 ?  83  LEU   B HD21 1 
ATOM   5279 H  HD22 . LEU   B 1 83  ? 49.170 -8.437  1.826   1.00 16.54 ?  83  LEU   B HD22 1 
ATOM   5280 H  HD23 . LEU   B 1 83  ? 47.653 -8.138  1.463   1.00 16.54 ?  83  LEU   B HD23 1 
ATOM   5281 N  N    . SER   B 1 84  ? 49.762 -9.614  -2.261  1.00 11.88 ?  84  SER   B N    1 
ATOM   5282 C  CA   . SER   B 1 84  ? 50.496 -9.731  -3.512  1.00 12.15 ?  84  SER   B CA   1 
ATOM   5283 C  C    . SER   B 1 84  ? 50.652 -11.192 -3.920  1.00 11.34 ?  84  SER   B C    1 
ATOM   5284 O  O    . SER   B 1 84  ? 50.767 -12.087 -3.084  1.00 11.23 ?  84  SER   B O    1 
ATOM   5285 C  CB   . SER   B 1 84  ? 51.891 -9.126  -3.368  1.00 13.95 ?  84  SER   B CB   1 
ATOM   5286 O  OG   . SER   B 1 84  ? 52.636 -9.338  -4.550  1.00 15.35 ?  84  SER   B OG   1 
ATOM   5287 H  H    . SER   B 1 84  ? 50.206 -9.277  -1.606  1.00 14.40 ?  84  SER   B H    1 
ATOM   5288 H  HA   . SER   B 1 84  ? 50.022 -9.262  -4.217  1.00 14.73 ?  84  SER   B HA   1 
ATOM   5289 H  HB2  . SER   B 1 84  ? 51.806 -8.170  -3.207  1.00 16.88 ?  84  SER   B HB2  1 
ATOM   5290 H  HB3  . SER   B 1 84  ? 52.345 -9.548  -2.624  1.00 16.88 ?  84  SER   B HB3  1 
ATOM   5291 H  HG   . SER   B 1 84  ? 53.404 -8.996  -4.469  1.00 18.56 ?  84  SER   B HG   1 
ATOM   5292 N  N    . GLY   B 1 85  ? 50.713 -11.417 -5.223  1.00 12.36 ?  85  GLY   B N    1 
ATOM   5293 C  CA   . GLY   B 1 85  ? 51.066 -12.709 -5.758  1.00 13.05 ?  85  GLY   B CA   1 
ATOM   5294 C  C    . GLY   B 1 85  ? 52.538 -12.899 -6.062  1.00 12.49 ?  85  GLY   B C    1 
ATOM   5295 O  O    . GLY   B 1 85  ? 52.915 -13.977 -6.524  1.00 12.68 ?  85  GLY   B O    1 
ATOM   5296 H  H    . GLY   B 1 85  ? 50.563 -10.826 -5.822  1.00 14.97 ?  85  GLY   B H    1 
ATOM   5297 H  HA2  . GLY   B 1 85  ? 50.804 -13.399 -5.126  1.00 15.80 ?  85  GLY   B HA2  1 
ATOM   5298 H  HA3  . GLY   B 1 85  ? 50.578 -12.857 -6.579  1.00 15.80 ?  85  GLY   B HA3  1 
ATOM   5299 N  N    . HIS   B 1 86  ? 53.390 -11.901 -5.834  1.00 12.44 ?  86  HIS   B N    1 
ATOM   5300 C  CA   . HIS   B 1 86  ? 54.853 -12.067 -5.919  1.00 12.18 ?  86  HIS   B CA   1 
ATOM   5301 C  C    . HIS   B 1 86  ? 55.226 -12.575 -7.311  1.00 12.38 ?  86  HIS   B C    1 
ATOM   5302 O  O    . HIS   B 1 86  ? 54.836 -11.956 -8.312  1.00 13.12 ?  86  HIS   B O    1 
ATOM   5303 C  CB   . HIS   B 1 86  ? 55.341 -12.911 -4.743  1.00 12.59 ?  86  HIS   B CB   1 
ATOM   5304 C  CG   . HIS   B 1 86  ? 55.026 -12.306 -3.416  1.00 12.54 ?  86  HIS   B CG   1 
ATOM   5305 N  ND1  . HIS   B 1 86  ? 55.854 -11.392 -2.803  1.00 13.96 ?  86  HIS   B ND1  1 
ATOM   5306 C  CD2  . HIS   B 1 86  ? 53.952 -12.452 -2.602  1.00 12.84 ?  86  HIS   B CD2  1 
ATOM   5307 C  CE1  . HIS   B 1 86  ? 55.302 -11.000 -1.669  1.00 13.74 ?  86  HIS   B CE1  1 
ATOM   5308 N  NE2  . HIS   B 1 86  ? 54.145 -11.623 -1.525  1.00 13.07 ?  86  HIS   B NE2  1 
ATOM   5309 H  H    . HIS   B 1 86  ? 53.148 -11.105 -5.623  1.00 15.06 ?  86  HIS   B H    1 
ATOM   5310 H  HA   . HIS   B 1 86  ? 55.260 -11.195 -5.821  1.00 14.76 ?  86  HIS   B HA   1 
ATOM   5311 H  HB2  . HIS   B 1 86  ? 54.921 -13.783 -4.781  1.00 15.25 ?  86  HIS   B HB2  1 
ATOM   5312 H  HB3  . HIS   B 1 86  ? 56.306 -13.007 -4.801  1.00 15.25 ?  86  HIS   B HB3  1 
ATOM   5313 H  HD2  . HIS   B 1 86  ? 53.211 -12.993 -2.756  1.00 15.55 ?  86  HIS   B HD2  1 
ATOM   5314 H  HE1  . HIS   B 1 86  ? 55.673 -10.400 -1.063  1.00 16.63 ?  86  HIS   B HE1  1 
ATOM   5315 H  HE2  . HIS   B 1 86  ? 53.611 -11.541 -0.855  1.00 15.82 ?  86  HIS   B HE2  1 
ATOM   5316 N  N    . ASN   B 1 87  ? 55.993 -13.659 -7.423  1.00 12.75 ?  87  ASN   B N    1 
ATOM   5317 C  CA   . ASN   B 1 87  ? 56.389 -14.230 -8.701  1.00 13.63 ?  87  ASN   B CA   1 
ATOM   5318 C  C    . ASN   B 1 87  ? 55.404 -15.273 -9.204  1.00 13.36 ?  87  ASN   B C    1 
ATOM   5319 O  O    . ASN   B 1 87  ? 55.720 -15.990 -10.160 1.00 15.22 ?  87  ASN   B O    1 
ATOM   5320 C  CB   . ASN   B 1 87  ? 57.784 -14.859 -8.586  1.00 15.55 ?  87  ASN   B CB   1 
ATOM   5321 C  CG   . ASN   B 1 87  ? 57.845 -15.973 -7.541  1.00 16.25 ?  87  ASN   B CG   1 
ATOM   5322 O  OD1  . ASN   B 1 87  ? 57.206 -15.893 -6.487  1.00 15.49 ?  87  ASN   B OD1  1 
ATOM   5323 N  ND2  . ASN   B 1 87  ? 58.592 -17.036 -7.848  1.00 18.53 ?  87  ASN   B ND2  1 
ATOM   5324 H  H    . ASN   B 1 87  ? 56.300 -14.095 -6.749  1.00 15.45 ?  87  ASN   B H    1 
ATOM   5325 H  HA   . ASN   B 1 87  ? 56.430 -13.525 -9.359  1.00 16.49 ?  87  ASN   B HA   1 
ATOM   5326 H  HB2  . ASN   B 1 87  ? 58.030 -15.238 -9.446  1.00 18.80 ?  87  ASN   B HB2  1 
ATOM   5327 H  HB3  . ASN   B 1 87  ? 58.418 -14.174 -8.331  1.00 18.80 ?  87  ASN   B HB3  1 
ATOM   5328 H  HD21 . ASN   B 1 87  ? 58.659 -17.687 -7.294  1.00 22.37 ?  87  ASN   B HD21 1 
ATOM   5329 H  HD22 . ASN   B 1 87  ? 59.019 -17.061 -8.596  1.00 22.37 ?  87  ASN   B HD22 1 
ATOM   5330 N  N    . LEU   B 1 88  ? 54.222 -15.373 -8.587  1.00 12.43 ?  88  LEU   B N    1 
ATOM   5331 C  CA   . LEU   B 1 88  ? 53.245 -16.406 -8.914  1.00 12.64 ?  88  LEU   B CA   1 
ATOM   5332 C  C    . LEU   B 1 88  ? 52.009 -15.893 -9.631  1.00 12.40 ?  88  LEU   B C    1 
ATOM   5333 O  O    . LEU   B 1 88  ? 51.406 -16.641 -10.411 1.00 14.08 ?  88  LEU   B O    1 
ATOM   5334 C  CB   . LEU   B 1 88  ? 52.779 -17.099 -7.631  1.00 13.46 ?  88  LEU   B CB   1 
ATOM   5335 C  CG   . LEU   B 1 88  ? 53.900 -17.745 -6.827  1.00 15.64 ?  88  LEU   B CG   1 
ATOM   5336 C  CD1  . LEU   B 1 88  ? 53.400 -18.123 -5.443  1.00 16.95 ?  88  LEU   B CD1  1 
ATOM   5337 C  CD2  . LEU   B 1 88  ? 54.435 -18.956 -7.566  1.00 18.80 ?  88  LEU   B CD2  1 
ATOM   5338 H  H    . LEU   B 1 88  ? 53.956 -14.839 -7.959  1.00 15.06 ?  88  LEU   B H    1 
ATOM   5339 H  HA   . LEU   B 1 88  ? 53.660 -17.066 -9.480  1.00 15.30 ?  88  LEU   B HA   1 
ATOM   5340 H  HB2  . LEU   B 1 88  ? 52.343 -16.448 -7.060  1.00 16.29 ?  88  LEU   B HB2  1 
ATOM   5341 H  HB3  . LEU   B 1 88  ? 52.146 -17.798 -7.869  1.00 16.29 ?  88  LEU   B HB3  1 
ATOM   5342 H  HG   . LEU   B 1 88  ? 54.623 -17.109 -6.723  1.00 18.90 ?  88  LEU   B HG   1 
ATOM   5343 H  HD11 . LEU   B 1 88  ? 54.087 -18.633 -4.988  1.00 20.48 ?  88  LEU   B HD11 1 
ATOM   5344 H  HD12 . LEU   B 1 88  ? 53.202 -17.313 -4.947  1.00 20.48 ?  88  LEU   B HD12 1 
ATOM   5345 H  HD13 . LEU   B 1 88  ? 52.597 -18.658 -5.536  1.00 20.48 ?  88  LEU   B HD13 1 
ATOM   5346 H  HD21 . LEU   B 1 88  ? 55.087 -19.404 -7.004  1.00 22.70 ?  88  LEU   B HD21 1 
ATOM   5347 H  HD22 . LEU   B 1 88  ? 53.701 -19.557 -7.764  1.00 22.70 ?  88  LEU   B HD22 1 
ATOM   5348 H  HD23 . LEU   B 1 88  ? 54.856 -18.664 -8.390  1.00 22.70 ?  88  LEU   B HD23 1 
ATOM   5349 N  N    . ALA   B 1 89  ? 51.609 -14.655 -9.371  1.00 11.79 ?  89  ALA   B N    1 
ATOM   5350 C  CA   . ALA   B 1 89  ? 50.314 -14.160 -9.813  1.00 11.11 ?  89  ALA   B CA   1 
ATOM   5351 C  C    . ALA   B 1 89  ? 50.284 -12.670 -9.529  1.00 11.79 ?  89  ALA   B C    1 
ATOM   5352 O  O    . ALA   B 1 89  ? 51.127 -12.151 -8.795  1.00 12.44 ?  89  ALA   B O    1 
ATOM   5353 C  CB   . ALA   B 1 89  ? 49.183 -14.844 -9.052  1.00 11.36 ?  89  ALA   B CB   1 
ATOM   5354 H  H    . ALA   B 1 89  ? 52.064 -14.071 -8.928  1.00 14.29 ?  89  ALA   B H    1 
ATOM   5355 H  HA   . ALA   B 1 89  ? 50.196 -14.307 -10.767 1.00 13.47 ?  89  ALA   B HA   1 
ATOM   5356 H  HB1  . ALA   B 1 89  ? 48.332 -14.510 -9.380  1.00 13.78 ?  89  ALA   B HB1  1 
ATOM   5357 H  HB2  . ALA   B 1 89  ? 49.240 -15.801 -9.202  1.00 13.78 ?  89  ALA   B HB2  1 
ATOM   5358 H  HB3  . ALA   B 1 89  ? 49.275 -14.648 -8.110  1.00 13.78 ?  89  ALA   B HB3  1 
ATOM   5359 N  N    . LYS   B 1 90  ? 49.292 -11.980 -10.089 1.00 12.70 ?  90  LYS   B N    1 
ATOM   5360 C  CA   . LYS   B 1 90  ? 49.109 -10.592 -9.686  1.00 12.68 ?  90  LYS   B CA   1 
ATOM   5361 C  C    . LYS   B 1 90  ? 48.791 -10.518 -8.198  1.00 12.38 ?  90  LYS   B C    1 
ATOM   5362 O  O    . LYS   B 1 90  ? 49.432 -9.764  -7.449  1.00 13.44 ?  90  LYS   B O    1 
ATOM   5363 C  CB   . LYS   B 1 90  ? 48.033 -9.928  -10.543 1.00 14.06 ?  90  LYS   B CB   1 
ATOM   5364 C  CG   . LYS   B 1 90  ? 47.736 -8.487  -10.166 1.00 14.75 ?  90  LYS   B CG   1 
ATOM   5365 C  CD   . LYS   B 1 90  ? 48.950 -7.597  -10.224 1.00 17.36 ?  90  LYS   B CD   1 
ATOM   5366 C  CE   . LYS   B 1 90  ? 48.505 -6.175  -9.982  1.00 19.32 ?  90  LYS   B CE   1 
ATOM   5367 N  NZ   . LYS   B 1 90  ? 49.651 -5.242  -9.862  1.00 19.29 ?  90  LYS   B NZ   1 
ATOM   5368 H  H    . LYS   B 1 90  ? 48.739 -12.279 -10.678 1.00 15.39 ?  90  LYS   B H    1 
ATOM   5369 H  HA   . LYS   B 1 90  ? 49.935 -10.116 -9.833  1.00 15.35 ?  90  LYS   B HA   1 
ATOM   5370 H  HB2  . LYS   B 1 90  ? 48.327 -9.930  -11.471 1.00 17.01 ?  90  LYS   B HB2  1 
ATOM   5371 H  HB3  . LYS   B 1 90  ? 47.207 -10.428 -10.464 1.00 17.01 ?  90  LYS   B HB3  1 
ATOM   5372 H  HG2  . LYS   B 1 90  ? 47.075 -8.129  -10.781 1.00 17.85 ?  90  LYS   B HG2  1 
ATOM   5373 H  HG3  . LYS   B 1 90  ? 47.386 -8.461  -9.260  1.00 17.85 ?  90  LYS   B HG3  1 
ATOM   5374 H  HD2  . LYS   B 1 90  ? 49.580 -7.849  -9.529  1.00 20.97 ?  90  LYS   B HD2  1 
ATOM   5375 H  HD3  . LYS   B 1 90  ? 49.363 -7.654  -11.100 1.00 20.97 ?  90  LYS   B HD3  1 
ATOM   5376 H  HE2  . LYS   B 1 90  ? 47.959 -5.874  -10.728 1.00 23.32 ?  90  LYS   B HE2  1 
ATOM   5377 H  HE3  . LYS   B 1 90  ? 47.998 -6.125  -9.158  1.00 23.32 ?  90  LYS   B HE3  1 
ATOM   5378 H  HZ1  . LYS   B 1 90  ? 49.360 -4.409  -9.723  1.00 23.29 ?  90  LYS   B HZ1  1 
ATOM   5379 H  HZ2  . LYS   B 1 90  ? 50.171 -5.481  -9.181  1.00 23.29 ?  90  LYS   B HZ2  1 
ATOM   5380 H  HZ3  . LYS   B 1 90  ? 50.135 -5.252  -10.611 1.00 23.29 ?  90  LYS   B HZ3  1 
ATOM   5381 N  N    . HIS   B 1 91  ? 47.829 -11.331 -7.750  1.00 11.05 ?  91  HIS   B N    1 
ATOM   5382 C  CA   . HIS   B 1 91  ? 47.362 -11.355 -6.376  1.00 10.93 ?  91  HIS   B CA   1 
ATOM   5383 C  C    . HIS   B 1 91  ? 47.362 -12.782 -5.856  1.00 10.48 ?  91  HIS   B C    1 
ATOM   5384 O  O    . HIS   B 1 91  ? 47.130 -13.734 -6.608  1.00 11.06 ?  91  HIS   B O    1 
ATOM   5385 C  CB   . HIS   B 1 91  ? 45.910 -10.873 -6.267  1.00 12.67 ?  91  HIS   B CB   1 
ATOM   5386 C  CG   . HIS   B 1 91  ? 45.703 -9.466  -6.708  1.00 15.66 ?  91  HIS   B CG   1 
ATOM   5387 N  ND1  . HIS   B 1 91  ? 46.314 -8.392  -6.097  1.00 18.19 ?  91  HIS   B ND1  1 
ATOM   5388 C  CD2  . HIS   B 1 91  ? 44.919 -8.951  -7.680  1.00 18.10 ?  91  HIS   B CD2  1 
ATOM   5389 C  CE1  . HIS   B 1 91  ? 45.932 -7.273  -6.690  1.00 19.26 ?  91  HIS   B CE1  1 
ATOM   5390 N  NE2  . HIS   B 1 91  ? 45.080 -7.586  -7.651  1.00 19.49 ?  91  HIS   B NE2  1 
ATOM   5391 H  H    . HIS   B 1 91  ? 47.415 -11.897 -8.252  1.00 13.39 ?  91  HIS   B H    1 
ATOM   5392 H  HA   . HIS   B 1 91  ? 47.933 -10.797 -5.814  1.00 13.26 ?  91  HIS   B HA   1 
ATOM   5393 H  HB2  . HIS   B 1 91  ? 45.350 -11.439 -6.817  1.00 15.34 ?  91  HIS   B HB2  1 
ATOM   5394 H  HB3  . HIS   B 1 91  ? 45.628 -10.936 -5.338  1.00 15.34 ?  91  HIS   B HB3  1 
ATOM   5395 H  HD1  . HIS   B 1 91  ? 46.866 -8.443  -5.436  1.00 21.96 ?  91  HIS   B HD1  1 
ATOM   5396 H  HD2  . HIS   B 1 91  ? 44.377 -9.421  -8.267  1.00 21.86 ?  91  HIS   B HD2  1 
ATOM   5397 H  HE1  . HIS   B 1 91  ? 46.214 -6.414  -6.462  1.00 23.25 ?  91  HIS   B HE1  1 
ATOM   5398 N  N    . CYS   B 1 92  ? 47.555 -12.914 -4.554  1.00 10.25 ?  92  CYS   B N    1 
ATOM   5399 C  CA   . CYS   B 1 92  ? 47.251 -14.146 -3.842  1.00 10.15 ?  92  CYS   B CA   1 
ATOM   5400 C  C    . CYS   B 1 92  ? 46.029 -13.910 -2.962  1.00 9.67  ?  92  CYS   B C    1 
ATOM   5401 O  O    . CYS   B 1 92  ? 46.028 -13.009 -2.112  1.00 10.94 ?  92  CYS   B O    1 
ATOM   5402 C  CB   . CYS   B 1 92  ? 48.424 -14.602 -2.981  1.00 10.64 ?  92  CYS   B CB   1 
ATOM   5403 S  SG   . CYS   B 1 92  ? 48.070 -16.141 -2.091  1.00 10.62 ?  92  CYS   B SG   1 
ATOM   5404 H  H    . CYS   B 1 92  ? 47.886 -12.294 -4.048  1.00 12.44 ?  92  CYS   B H    1 
ATOM   5405 H  HA   . CYS   B 1 92  ? 47.053 -14.845 -4.483  1.00 12.32 ?  92  CYS   B HA   1 
ATOM   5406 H  HB2  . CYS   B 1 92  ? 49.196 -14.745 -3.544  1.00 12.91 ?  92  CYS   B HB2  1 
ATOM   5407 H  HB3  . CYS   B 1 92  ? 48.614 -13.911 -2.322  1.00 12.91 ?  92  CYS   B HB3  1 
ATOM   5408 H  HG   . CYS   B 1 92  ? 49.038 -16.453 -1.457  1.00 12.89 ?  92  CYS   B HG   1 
ATOM   5409 N  N    . LEU   B 1 93  ? 44.991 -14.716 -3.174  1.00 9.78  ?  93  LEU   B N    1 
ATOM   5410 C  CA   . LEU   B 1 93  ? 43.815 -14.723 -2.315  1.00 9.99  ?  93  LEU   B CA   1 
ATOM   5411 C  C    . LEU   B 1 93  ? 44.035 -15.786 -1.246  1.00 9.51  ?  93  LEU   B C    1 
ATOM   5412 O  O    . LEU   B 1 93  ? 43.989 -16.988 -1.534  1.00 10.37 ?  93  LEU   B O    1 
ATOM   5413 C  CB   . LEU   B 1 93  ? 42.557 -15.009 -3.128  1.00 10.28 ?  93  LEU   B CB   1 
ATOM   5414 C  CG   . LEU   B 1 93  ? 41.257 -15.027 -2.318  1.00 11.24 ?  93  LEU   B CG   1 
ATOM   5415 C  CD1  . LEU   B 1 93  ? 40.898 -13.639 -1.832  1.00 11.58 ?  93  LEU   B CD1  1 
ATOM   5416 C  CD2  . LEU   B 1 93  ? 40.127 -15.621 -3.140  1.00 11.50 ?  93  LEU   B CD2  1 
ATOM   5417 H  H    . LEU   B 1 93  ? 44.949 -15.291 -3.824  1.00 11.88 ?  93  LEU   B H    1 
ATOM   5418 H  HA   . LEU   B 1 93  ? 43.726 -13.860 -1.888  1.00 12.12 ?  93  LEU   B HA   1 
ATOM   5419 H  HB2  . LEU   B 1 93  ? 42.465 -14.317 -3.806  1.00 12.47 ?  93  LEU   B HB2  1 
ATOM   5420 H  HB3  . LEU   B 1 93  ? 42.648 -15.870 -3.553  1.00 12.47 ?  93  LEU   B HB3  1 
ATOM   5421 H  HG   . LEU   B 1 93  ? 41.379 -15.587 -1.539  1.00 13.63 ?  93  LEU   B HG   1 
ATOM   5422 H  HD11 . LEU   B 1 93  ? 40.046 -13.675 -1.375  1.00 14.03 ?  93  LEU   B HD11 1 
ATOM   5423 H  HD12 . LEU   B 1 93  ? 41.589 -13.327 -1.230  1.00 14.03 ?  93  LEU   B HD12 1 
ATOM   5424 H  HD13 . LEU   B 1 93  ? 40.837 -13.044 -2.600  1.00 14.03 ?  93  LEU   B HD13 1 
ATOM   5425 H  HD21 . LEU   B 1 93  ? 39.313 -15.619 -2.609  1.00 13.94 ?  93  LEU   B HD21 1 
ATOM   5426 H  HD22 . LEU   B 1 93  ? 39.998 -15.088 -3.940  1.00 13.94 ?  93  LEU   B HD22 1 
ATOM   5427 H  HD23 . LEU   B 1 93  ? 40.357 -16.533 -3.384  1.00 13.94 ?  93  LEU   B HD23 1 
ATOM   5428 N  N    . HIS   B 1 94  ? 44.307 -15.350 -0.024  1.00 9.73  ?  94  HIS   B N    1 
ATOM   5429 C  CA   . HIS   B 1 94  ? 44.534 -16.255 1.095   1.00 9.64  ?  94  HIS   B CA   1 
ATOM   5430 C  C    . HIS   B 1 94  ? 43.175 -16.611 1.678   1.00 10.16 ?  94  HIS   B C    1 
ATOM   5431 O  O    . HIS   B 1 94  ? 42.504 -15.742 2.233   1.00 11.37 ?  94  HIS   B O    1 
ATOM   5432 C  CB   . HIS   B 1 94  ? 45.408 -15.580 2.150   1.00 9.94  ?  94  HIS   B CB   1 
ATOM   5433 C  CG   . HIS   B 1 94  ? 46.790 -15.281 1.677   1.00 10.35 ?  94  HIS   B CG   1 
ATOM   5434 N  ND1  . HIS   B 1 94  ? 47.818 -16.195 1.766   1.00 10.52 ?  94  HIS   B ND1  1 
ATOM   5435 C  CD2  . HIS   B 1 94  ? 47.298 -14.176 1.078   1.00 10.40 ?  94  HIS   B CD2  1 
ATOM   5436 C  CE1  . HIS   B 1 94  ? 48.909 -15.645 1.258   1.00 10.32 ?  94  HIS   B CE1  1 
ATOM   5437 N  NE2  . HIS   B 1 94  ? 48.621 -14.424 0.833   1.00 10.64 ?  94  HIS   B NE2  1 
ATOM   5438 H  H    . HIS   B 1 94  ? 44.366 -14.513 0.183   1.00 11.81 ?  94  HIS   B H    1 
ATOM   5439 H  HA   . HIS   B 1 94  ? 44.972 -17.061 0.781   1.00 11.71 ?  94  HIS   B HA   1 
ATOM   5440 H  HB2  . HIS   B 1 94  ? 44.993 -14.744 2.406   1.00 12.07 ?  94  HIS   B HB2  1 
ATOM   5441 H  HB3  . HIS   B 1 94  ? 45.475 -16.169 2.914   1.00 12.07 ?  94  HIS   B HB3  1 
ATOM   5442 H  HD2  . HIS   B 1 94  ? 46.841 -13.394 0.875   1.00 12.62 ?  94  HIS   B HD2  1 
ATOM   5443 H  HE1  . HIS   B 1 94  ? 49.740 -16.062 1.201   1.00 12.52 ?  94  HIS   B HE1  1 
ATOM   5444 H  HE2  . HIS   B 1 94  ? 49.177 -13.887 0.461   1.00 12.91 ?  94  HIS   B HE2  1 
ATOM   5445 N  N    . VAL   B 1 95  ? 42.746 -17.869 1.531   1.00 9.97  ?  95  VAL   B N    1 
ATOM   5446 C  CA   . VAL   B 1 95  ? 41.418 -18.309 1.960   1.00 10.22 ?  95  VAL   B CA   1 
ATOM   5447 C  C    . VAL   B 1 95  ? 41.581 -19.346 3.057   1.00 10.59 ?  95  VAL   B C    1 
ATOM   5448 O  O    . VAL   B 1 95  ? 42.357 -20.297 2.904   1.00 11.14 ?  95  VAL   B O    1 
ATOM   5449 C  CB   . VAL   B 1 95  ? 40.592 -18.903 0.801   1.00 10.50 ?  95  VAL   B CB   1 
ATOM   5450 C  CG1  . VAL   B 1 95  ? 39.211 -19.345 1.288   1.00 11.58 ?  95  VAL   B CG1  1 
ATOM   5451 C  CG2  . VAL   B 1 95  ? 40.478 -17.923 -0.339  1.00 10.56 ?  95  VAL   B CG2  1 
ATOM   5452 H  H    . VAL   B 1 95  ? 43.216 -18.498 1.172   1.00 12.10 ?  95  VAL   B H    1 
ATOM   5453 H  HA   . VAL   B 1 95  ? 40.930 -17.557 2.325   1.00 12.40 ?  95  VAL   B HA   1 
ATOM   5454 H  HB   . VAL   B 1 95  ? 41.044 -19.686 0.465   1.00 12.73 ?  95  VAL   B HB   1 
ATOM   5455 H  HG11 . VAL   B 1 95  ? 38.646 -19.536 0.518   1.00 14.04 ?  95  VAL   B HG11 1 
ATOM   5456 H  HG12 . VAL   B 1 95  ? 39.301 -20.146 1.829   1.00 14.04 ?  95  VAL   B HG12 1 
ATOM   5457 H  HG13 . VAL   B 1 95  ? 38.810 -18.634 1.814   1.00 14.04 ?  95  VAL   B HG13 1 
ATOM   5458 H  HG21 . VAL   B 1 95  ? 39.900 -18.303 -1.020  1.00 12.82 ?  95  VAL   B HG21 1 
ATOM   5459 H  HG22 . VAL   B 1 95  ? 40.093 -17.097 -0.003  1.00 12.82 ?  95  VAL   B HG22 1 
ATOM   5460 H  HG23 . VAL   B 1 95  ? 41.358 -17.761 -0.698  1.00 12.82 ?  95  VAL   B HG23 1 
ATOM   5461 N  N    . VAL   B 1 96  ? 40.850 -19.172 4.151   1.00 10.99 ?  96  VAL   B N    1 
ATOM   5462 C  CA   . VAL   B 1 96  ? 40.932 -20.083 5.292   1.00 11.32 ?  96  VAL   B CA   1 
ATOM   5463 C  C    . VAL   B 1 96  ? 39.741 -21.040 5.248   1.00 11.88 ?  96  VAL   B C    1 
ATOM   5464 O  O    . VAL   B 1 96  ? 38.622 -20.684 5.631   1.00 12.45 ?  96  VAL   B O    1 
ATOM   5465 C  CB   . VAL   B 1 96  ? 40.986 -19.333 6.625   1.00 12.04 ?  96  VAL   B CB   1 
ATOM   5466 C  CG1  . VAL   B 1 96  ? 41.157 -20.326 7.770   1.00 12.82 ?  96  VAL   B CG1  1 
ATOM   5467 C  CG2  . VAL   B 1 96  ? 42.100 -18.303 6.626   1.00 12.62 ?  96  VAL   B CG2  1 
ATOM   5468 H  H    . VAL   B 1 96  ? 40.287 -18.534 4.260   1.00 13.33 ?  96  VAL   B H    1 
ATOM   5469 H  HA   . VAL   B 1 96  ? 41.739 -20.616 5.217   1.00 13.72 ?  96  VAL   B HA   1 
ATOM   5470 H  HB   . VAL   B 1 96  ? 40.144 -18.870 6.759   1.00 14.58 ?  96  VAL   B HB   1 
ATOM   5471 H  HG11 . VAL   B 1 96  ? 41.348 -19.835 8.586   1.00 15.52 ?  96  VAL   B HG11 1 
ATOM   5472 H  HG12 . VAL   B 1 96  ? 40.340 -20.837 7.879   1.00 15.52 ?  96  VAL   B HG12 1 
ATOM   5473 H  HG13 . VAL   B 1 96  ? 41.896 -20.921 7.566   1.00 15.52 ?  96  VAL   B HG13 1 
ATOM   5474 H  HG21 . VAL   B 1 96  ? 42.153 -17.894 7.505   1.00 15.29 ?  96  VAL   B HG21 1 
ATOM   5475 H  HG22 . VAL   B 1 96  ? 42.938 -18.740 6.413   1.00 15.29 ?  96  VAL   B HG22 1 
ATOM   5476 H  HG23 . VAL   B 1 96  ? 41.903 -17.623 5.960   1.00 15.29 ?  96  VAL   B HG23 1 
ATOM   5477 N  N    . GLY   B 1 97  ? 39.977 -22.272 4.805   1.00 11.73 ?  97  GLY   B N    1 
ATOM   5478 C  CA   . GLY   B 1 97  ? 39.007 -23.331 4.958   1.00 12.66 ?  97  GLY   B CA   1 
ATOM   5479 C  C    . GLY   B 1 97  ? 39.135 -23.949 6.332   1.00 13.59 ?  97  GLY   B C    1 
ATOM   5480 O  O    . GLY   B 1 97  ? 40.174 -23.818 6.993   1.00 13.98 ?  97  GLY   B O    1 
ATOM   5481 H  H    . GLY   B 1 97  ? 40.704 -22.513 4.407   1.00 14.22 ?  97  GLY   B H    1 
ATOM   5482 H  HA2  . GLY   B 1 97  ? 38.111 -22.964 4.843   1.00 15.34 ?  97  GLY   B HA2  1 
ATOM   5483 H  HA3  . GLY   B 1 97  ? 39.150 -24.012 4.282   1.00 15.34 ?  97  GLY   B HA3  1 
ATOM   5484 N  N    . PRO   B 1 98  ? 38.085 -24.631 6.795   1.00 14.47 ?  98  PRO   B N    1 
ATOM   5485 C  CA   . PRO   B 1 98  ? 38.176 -25.323 8.084   1.00 15.38 ?  98  PRO   B CA   1 
ATOM   5486 C  C    . PRO   B 1 98  ? 39.201 -26.445 8.047   1.00 14.99 ?  98  PRO   B C    1 
ATOM   5487 O  O    . PRO   B 1 98  ? 39.315 -27.180 7.066   1.00 15.20 ?  98  PRO   B O    1 
ATOM   5488 C  CB   . PRO   B 1 98  ? 36.758 -25.864 8.294   1.00 15.47 ?  98  PRO   B CB   1 
ATOM   5489 C  CG   . PRO   B 1 98  ? 36.190 -25.989 6.930   1.00 15.33 ?  98  PRO   B CG   1 
ATOM   5490 C  CD   . PRO   B 1 98  ? 36.764 -24.818 6.166   1.00 14.57 ?  98  PRO   B CD   1 
ATOM   5491 H  HA   . PRO   B 1 98  ? 38.400 -24.698 8.785   1.00 18.60 ?  98  PRO   B HA   1 
ATOM   5492 H  HB2  . PRO   B 1 98  ? 36.803 -26.731 8.730   1.00 18.71 ?  98  PRO   B HB2  1 
ATOM   5493 H  HB3  . PRO   B 1 98  ? 36.246 -25.238 8.825   1.00 18.71 ?  98  PRO   B HB3  1 
ATOM   5494 H  HG2  . PRO   B 1 98  ? 36.470 -26.832 6.535   1.00 18.54 ?  98  PRO   B HG2  1 
ATOM   5495 H  HG3  . PRO   B 1 98  ? 35.223 -25.936 6.974   1.00 18.54 ?  98  PRO   B HG3  1 
ATOM   5496 H  HD2  . PRO   B 1 98  ? 36.853 -25.042 5.222   1.00 17.62 ?  98  PRO   B HD2  1 
ATOM   5497 H  HD3  . PRO   B 1 98  ? 36.215 -24.028 6.292   1.00 17.62 ?  98  PRO   B HD3  1 
ATOM   5498 N  N    . ASN   B 1 99  ? 39.954 -26.565 9.131   1.00 15.92 ?  99  ASN   B N    1 
ATOM   5499 C  CA   . ASN   B 1 99  ? 40.932 -27.636 9.297   1.00 17.05 ?  99  ASN   B CA   1 
ATOM   5500 C  C    . ASN   B 1 99  ? 40.304 -28.715 10.175  1.00 19.92 ?  99  ASN   B C    1 
ATOM   5501 O  O    . ASN   B 1 99  ? 40.227 -28.568 11.397  1.00 20.49 ?  99  ASN   B O    1 
ATOM   5502 C  CB   . ASN   B 1 99  ? 42.205 -27.082 9.921   1.00 17.18 ?  99  ASN   B CB   1 
ATOM   5503 C  CG   . ASN   B 1 99  ? 43.337 -28.086 9.923   1.00 17.94 ?  99  ASN   B CG   1 
ATOM   5504 O  OD1  . ASN   B 1 99  ? 43.116 -29.277 10.086  1.00 18.74 ?  99  ASN   B OD1  1 
ATOM   5505 N  ND2  . ASN   B 1 99  ? 44.553 -27.609 9.740   1.00 17.91 ?  99  ASN   B ND2  1 
ATOM   5506 H  H    . ASN   B 1 99  ? 39.914 -26.027 9.797   1.00 19.25 ?  99  ASN   B H    1 
ATOM   5507 H  HA   . ASN   B 1 99  ? 41.142 -28.029 8.437   1.00 20.61 ?  99  ASN   B HA   1 
ATOM   5508 H  HB2  . ASN   B 1 99  ? 42.486 -26.309 9.419   1.00 20.76 ?  99  ASN   B HB2  1 
ATOM   5509 H  HB3  . ASN   B 1 99  ? 42.017 -26.838 10.843  1.00 20.76 ?  99  ASN   B HB3  1 
ATOM   5510 H  HD21 . ASN   B 1 99  ? 45.224 -28.143 9.730   1.00 21.63 ?  99  ASN   B HD21 1 
ATOM   5511 H  HD22 . ASN   B 1 99  ? 44.665 -26.766 9.632   1.00 21.63 ?  99  ASN   B HD22 1 
ATOM   5512 N  N    A VAL   B 1 100 ? 39.841 -29.799 9.547   0.74 21.82 ?  100 VAL   B N    1 
ATOM   5513 N  N    B VAL   B 1 100 ? 39.849 -29.800 9.540   0.26 21.91 ?  100 VAL   B N    1 
ATOM   5514 C  CA   A VAL   B 1 100 ? 39.224 -30.888 10.303  0.74 24.50 ?  100 VAL   B CA   1 
ATOM   5515 C  CA   B VAL   B 1 100 ? 39.228 -30.901 10.272  0.26 24.08 ?  100 VAL   B CA   1 
ATOM   5516 C  C    A VAL   B 1 100 ? 40.235 -31.538 11.237  0.74 24.84 ?  100 VAL   B C    1 
ATOM   5517 C  C    B VAL   B 1 100 ? 40.228 -31.559 11.214  0.26 24.78 ?  100 VAL   B C    1 
ATOM   5518 O  O    A VAL   B 1 100 ? 39.876 -32.012 12.322  0.74 25.42 ?  100 VAL   B O    1 
ATOM   5519 O  O    B VAL   B 1 100 ? 39.853 -32.052 12.285  0.26 25.00 ?  100 VAL   B O    1 
ATOM   5520 C  CB   A VAL   B 1 100 ? 38.576 -31.908 9.344   0.74 26.92 ?  100 VAL   B CB   1 
ATOM   5521 C  CB   B VAL   B 1 100 ? 38.605 -31.907 9.281   0.26 25.52 ?  100 VAL   B CB   1 
ATOM   5522 C  CG1  A VAL   B 1 100 ? 38.098 -33.135 10.110  0.74 27.98 ?  100 VAL   B CG1  1 
ATOM   5523 C  CG1  B VAL   B 1 100 ? 38.102 -33.144 10.010  0.26 26.08 ?  100 VAL   B CG1  1 
ATOM   5524 C  CG2  A VAL   B 1 100 ? 37.417 -31.265 8.600   0.74 27.55 ?  100 VAL   B CG2  1 
ATOM   5525 C  CG2  B VAL   B 1 100 ? 37.472 -31.249 8.505   0.26 26.01 ?  100 VAL   B CG2  1 
ATOM   5526 H  H    A VAL   B 1 100 ? 39.869 -29.924 8.697   0.74 26.32 ?  100 VAL   B H    1 
ATOM   5527 H  H    B VAL   B 1 100 ? 39.887 -29.918 8.689   0.26 26.43 ?  100 VAL   B H    1 
ATOM   5528 H  HA   A VAL   B 1 100 ? 38.511 -30.520 10.849  0.74 29.55 ?  100 VAL   B HA   1 
ATOM   5529 H  HA   B VAL   B 1 100 ? 38.506 -30.547 10.813  0.26 29.04 ?  100 VAL   B HA   1 
ATOM   5530 H  HB   A VAL   B 1 100 ? 39.233 -32.198 8.693   0.74 32.44 ?  100 VAL   B HB   1 
ATOM   5531 H  HB   B VAL   B 1 100 ? 39.280 -32.189 8.644   0.26 30.76 ?  100 VAL   B HB   1 
ATOM   5532 H  HG11 A VAL   B 1 100 ? 37.498 -33.648 9.543   0.74 33.72 ?  100 VAL   B HG11 1 
ATOM   5533 H  HG11 B VAL   B 1 100 ? 37.524 -33.648 9.413   0.26 31.44 ?  100 VAL   B HG11 1 
ATOM   5534 H  HG12 A VAL   B 1 100 ? 38.862 -33.681 10.354  0.74 33.72 ?  100 VAL   B HG12 1 
ATOM   5535 H  HG12 B VAL   B 1 100 ? 38.859 -33.690 10.271  0.26 31.44 ?  100 VAL   B HG12 1 
ATOM   5536 H  HG13 A VAL   B 1 100 ? 37.626 -32.849 10.908  0.74 33.72 ?  100 VAL   B HG13 1 
ATOM   5537 H  HG13 B VAL   B 1 100 ? 37.603 -32.868 10.794  0.26 31.44 ?  100 VAL   B HG13 1 
ATOM   5538 H  HG21 A VAL   B 1 100 ? 37.025 -31.921 8.001   0.74 33.20 ?  100 VAL   B HG21 1 
ATOM   5539 H  HG21 B VAL   B 1 100 ? 37.082 -31.900 7.900   0.26 31.35 ?  100 VAL   B HG21 1 
ATOM   5540 H  HG22 A VAL   B 1 100 ? 36.754 -30.969 9.244   0.74 33.20 ?  100 VAL   B HG22 1 
ATOM   5541 H  HG22 B VAL   B 1 100 ? 36.800 -30.937 9.132   0.26 31.35 ?  100 VAL   B HG22 1 
ATOM   5542 H  HG23 A VAL   B 1 100 ? 37.748 -30.510 8.093   0.74 33.20 ?  100 VAL   B HG23 1 
ATOM   5543 H  HG23 B VAL   B 1 100 ? 37.827 -30.501 8.001   0.26 31.35 ?  100 VAL   B HG23 1 
ATOM   5544 N  N    . ASN   B 1 101 ? 41.508 -31.589 10.834  1.00 25.37 ?  101 ASN   B N    1 
ATOM   5545 C  CA   . ASN   B 1 101 ? 42.546 -32.131 11.710  1.00 27.28 ?  101 ASN   B CA   1 
ATOM   5546 C  C    . ASN   B 1 101 ? 42.750 -31.292 12.967  1.00 29.60 ?  101 ASN   B C    1 
ATOM   5547 O  O    . ASN   B 1 101 ? 43.395 -31.763 13.913  1.00 30.70 ?  101 ASN   B O    1 
ATOM   5548 C  CB   . ASN   B 1 101 ? 43.869 -32.265 10.949  1.00 27.18 ?  101 ASN   B CB   1 
ATOM   5549 C  CG   . ASN   B 1 101 ? 43.861 -33.420 9.968   1.00 26.96 ?  101 ASN   B CG   1 
ATOM   5550 O  OD1  . ASN   B 1 101 ? 43.193 -34.424 10.188  1.00 27.62 ?  101 ASN   B OD1  1 
ATOM   5551 N  ND2  . ASN   B 1 101 ? 44.602 -33.279 8.875   1.00 26.51 ?  101 ASN   B ND2  1 
ATOM   5552 H  H    A ASN   B 1 101 ? 41.782 -31.338 10.060  0.74 30.58 ?  101 ASN   B H    1 
ATOM   5553 H  H    B ASN   B 1 101 ? 41.792 -31.316 10.071  0.26 30.58 ?  101 ASN   B H    1 
ATOM   5554 H  HA   . ASN   B 1 101 ? 42.281 -33.013 11.996  1.00 32.88 ?  101 ASN   B HA   1 
ATOM   5555 H  HB2  . ASN   B 1 101 ? 44.040 -31.452 10.450  1.00 32.76 ?  101 ASN   B HB2  1 
ATOM   5556 H  HB3  . ASN   B 1 101 ? 44.584 -32.419 11.587  1.00 32.76 ?  101 ASN   B HB3  1 
ATOM   5557 H  HD21 . ASN   B 1 101 ? 44.629 -33.909 8.289   1.00 31.96 ?  101 ASN   B HD21 1 
ATOM   5558 H  HD22 . ASN   B 1 101 ? 45.052 -32.558 8.752   1.00 31.96 ?  101 ASN   B HD22 1 
ATOM   5559 N  N    . LYS   B 1 102 ? 42.232 -30.062 12.991  1.00 32.30 ?  102 LYS   B N    1 
ATOM   5560 C  CA   . LYS   B 1 102 ? 42.215 -29.226 14.185  1.00 35.46 ?  102 LYS   B CA   1 
ATOM   5561 C  C    . LYS   B 1 102 ? 40.833 -29.158 14.824  1.00 34.65 ?  102 LYS   B C    1 
ATOM   5562 O  O    . LYS   B 1 102 ? 40.617 -28.340 15.723  1.00 35.15 ?  102 LYS   B O    1 
ATOM   5563 C  CB   . LYS   B 1 102 ? 42.682 -27.806 13.857  1.00 39.49 ?  102 LYS   B CB   1 
ATOM   5564 C  CG   . LYS   B 1 102 ? 44.146 -27.673 13.476  1.00 43.16 ?  102 LYS   B CG   1 
ATOM   5565 C  CD   . LYS   B 1 102 ? 44.419 -26.270 12.957  1.00 46.47 ?  102 LYS   B CD   1 
ATOM   5566 C  CE   . LYS   B 1 102 ? 45.902 -25.974 12.836  1.00 48.95 ?  102 LYS   B CE   1 
ATOM   5567 N  NZ   . LYS   B 1 102 ? 46.128 -24.584 12.344  1.00 50.32 ?  102 LYS   B NZ   1 
ATOM   5568 H  H    . LYS   B 1 102 ? 41.869 -29.679 12.309  1.00 38.90 ?  102 LYS   B H    1 
ATOM   5569 H  HA   . LYS   B 1 102 ? 42.831 -29.595 14.836  1.00 42.70 ?  102 LYS   B HA   1 
ATOM   5570 H  HB2  . LYS   B 1 102 ? 42.157 -27.470 13.116  1.00 47.53 ?  102 LYS   B HB2  1 
ATOM   5571 H  HB3  . LYS   B 1 102 ? 42.535 -27.244 14.637  1.00 47.53 ?  102 LYS   B HB3  1 
ATOM   5572 H  HG2  . LYS   B 1 102 ? 44.703 -27.827 14.256  1.00 51.94 ?  102 LYS   B HG2  1 
ATOM   5573 H  HG3  . LYS   B 1 102 ? 44.358 -28.309 12.775  1.00 51.94 ?  102 LYS   B HG3  1 
ATOM   5574 H  HD2  . LYS   B 1 102 ? 44.022 -26.175 12.076  1.00 55.90 ?  102 LYS   B HD2  1 
ATOM   5575 H  HD3  . LYS   B 1 102 ? 44.031 -25.624 13.568  1.00 55.90 ?  102 LYS   B HD3  1 
ATOM   5576 H  HE2  . LYS   B 1 102 ? 46.320 -26.061 13.708  1.00 58.88 ?  102 LYS   B HE2  1 
ATOM   5577 H  HE3  . LYS   B 1 102 ? 46.305 -26.591 12.206  1.00 58.88 ?  102 LYS   B HE3  1 
ATOM   5578 H  HZ1  . LYS   B 1 102 ? 47.000 -24.422 12.278  1.00 60.53 ?  102 LYS   B HZ1  1 
ATOM   5579 H  HZ2  . LYS   B 1 102 ? 45.752 -24.481 11.543  1.00 60.53 ?  102 LYS   B HZ2  1 
ATOM   5580 H  HZ3  . LYS   B 1 102 ? 45.766 -23.999 12.909  1.00 60.53 ?  102 LYS   B HZ3  1 
ATOM   5581 N  N    . GLY   B 1 103 ? 39.889 -29.977 14.365  1.00 33.63 ?  103 GLY   B N    1 
ATOM   5582 C  CA   . GLY   B 1 103 ? 38.566 -30.019 14.953  1.00 32.87 ?  103 GLY   B CA   1 
ATOM   5583 C  C    . GLY   B 1 103 ? 37.612 -28.945 14.484  1.00 31.56 ?  103 GLY   B C    1 
ATOM   5584 O  O    . GLY   B 1 103 ? 36.518 -28.825 15.048  1.00 31.95 ?  103 GLY   B O    1 
ATOM   5585 H  H    . GLY   B 1 103 ? 39.994 -30.517 13.705  1.00 40.50 ?  103 GLY   B H    1 
ATOM   5586 H  HA2  . GLY   B 1 103 ? 38.161 -30.876 14.755  1.00 39.58 ?  103 GLY   B HA2  1 
ATOM   5587 H  HA3  . GLY   B 1 103 ? 38.648 -29.942 15.918  1.00 39.58 ?  103 GLY   B HA3  1 
ATOM   5588 N  N    A GLU   B 1 104 ? 37.988 -28.158 13.480  0.74 30.30 ?  104 GLU   B N    1 
ATOM   5589 N  N    B GLU   B 1 104 ? 37.972 -28.175 13.464  0.26 30.82 ?  104 GLU   B N    1 
ATOM   5590 C  CA   A GLU   B 1 104 ? 37.149 -27.062 13.025  0.74 28.90 ?  104 GLU   B CA   1 
ATOM   5591 C  CA   B GLU   B 1 104 ? 37.111 -27.100 12.995  0.26 29.90 ?  104 GLU   B CA   1 
ATOM   5592 C  C    A GLU   B 1 104 ? 35.965 -27.590 12.216  0.74 29.25 ?  104 GLU   B C    1 
ATOM   5593 C  C    B GLU   B 1 104 ? 35.956 -27.653 12.165  0.26 29.94 ?  104 GLU   B C    1 
ATOM   5594 O  O    A GLU   B 1 104 ? 36.006 -28.680 11.637  0.74 29.92 ?  104 GLU   B O    1 
ATOM   5595 O  O    B GLU   B 1 104 ? 36.045 -28.729 11.567  0.26 30.12 ?  104 GLU   B O    1 
ATOM   5596 C  CB   A GLU   B 1 104 ? 37.980 -26.062 12.216  0.74 27.63 ?  104 GLU   B CB   1 
ATOM   5597 C  CB   B GLU   B 1 104 ? 37.926 -26.081 12.198  0.26 28.99 ?  104 GLU   B CB   1 
ATOM   5598 C  CG   A GLU   B 1 104 ? 39.079 -25.412 13.051  0.74 26.32 ?  104 GLU   B CG   1 
ATOM   5599 C  CG   B GLU   B 1 104 ? 39.014 -25.421 13.036  0.26 28.17 ?  104 GLU   B CG   1 
ATOM   5600 C  CD   A GLU   B 1 104 ? 40.025 -24.539 12.251  0.74 24.92 ?  104 GLU   B CD   1 
ATOM   5601 C  CD   B GLU   B 1 104 ? 39.968 -24.574 12.218  0.26 27.45 ?  104 GLU   B CD   1 
ATOM   5602 O  OE1  A GLU   B 1 104 ? 40.014 -24.598 11.005  0.74 23.22 ?  104 GLU   B OE1  1 
ATOM   5603 O  OE1  B GLU   B 1 104 ? 39.888 -24.606 10.972  0.26 26.94 ?  104 GLU   B OE1  1 
ATOM   5604 O  OE2  A GLU   B 1 104 ? 40.789 -23.786 12.888  0.74 24.95 -1 104 GLU   B OE2  1 
ATOM   5605 O  OE2  B GLU   B 1 104 ? 40.804 -23.874 12.827  0.26 27.32 -1 104 GLU   B OE2  1 
ATOM   5606 H  H    A GLU   B 1 104 ? 38.728 -28.239 13.048  0.74 36.50 ?  104 GLU   B H    1 
ATOM   5607 H  H    B GLU   B 1 104 ? 38.712 -28.251 13.031  0.26 37.13 ?  104 GLU   B H    1 
ATOM   5608 H  HA   A GLU   B 1 104 ? 36.799 -26.594 13.800  0.74 34.82 ?  104 GLU   B HA   1 
ATOM   5609 H  HA   B GLU   B 1 104 ? 36.735 -26.644 13.761  0.26 36.02 ?  104 GLU   B HA   1 
ATOM   5610 H  HB2  A GLU   B 1 104 ? 38.399 -26.523 11.474  0.74 33.30 ?  104 GLU   B HB2  1 
ATOM   5611 H  HB2  B GLU   B 1 104 ? 38.352 -26.527 11.450  0.26 34.93 ?  104 GLU   B HB2  1 
ATOM   5612 H  HB3  A GLU   B 1 104 ? 37.398 -25.358 11.887  0.74 33.30 ?  104 GLU   B HB3  1 
ATOM   5613 H  HB3  B GLU   B 1 104 ? 37.332 -25.384 11.875  0.26 34.93 ?  104 GLU   B HB3  1 
ATOM   5614 H  HG2  A GLU   B 1 104 ? 38.673 -24.850 13.729  0.74 31.73 ?  104 GLU   B HG2  1 
ATOM   5615 H  HG2  B GLU   B 1 104 ? 38.597 -24.846 13.698  0.26 33.95 ?  104 GLU   B HG2  1 
ATOM   5616 H  HG3  A GLU   B 1 104 ? 39.610 -26.105 13.473  0.74 31.73 ?  104 GLU   B HG3  1 
ATOM   5617 H  HG3  B GLU   B 1 104 ? 39.532 -26.111 13.482  0.26 33.95 ?  104 GLU   B HG3  1 
ATOM   5618 N  N    A ASP   B 1 105 ? 34.896 -26.797 12.189  0.74 28.88 ?  105 ASP   B N    1 
ATOM   5619 N  N    B ASP   B 1 105 ? 34.860 -26.896 12.140  0.26 29.67 ?  105 ASP   B N    1 
ATOM   5620 C  CA   A ASP   B 1 105 ? 33.622 -27.255 11.646  0.74 29.48 ?  105 ASP   B CA   1 
ATOM   5621 C  CA   B ASP   B 1 105 ? 33.605 -27.375 11.573  0.26 29.65 ?  105 ASP   B CA   1 
ATOM   5622 C  C    A ASP   B 1 105 ? 33.678 -27.311 10.123  0.74 27.58 ?  105 ASP   B C    1 
ATOM   5623 C  C    B ASP   B 1 105 ? 33.684 -27.390 10.050  0.26 28.68 ?  105 ASP   B C    1 
ATOM   5624 O  O    A ASP   B 1 105 ? 33.847 -26.282 9.461   0.74 26.51 ?  105 ASP   B O    1 
ATOM   5625 O  O    B ASP   B 1 105 ? 33.910 -26.353 9.419   0.26 28.37 ?  105 ASP   B O    1 
ATOM   5626 C  CB   A ASP   B 1 105 ? 32.506 -26.317 12.101  0.74 32.48 ?  105 ASP   B CB   1 
ATOM   5627 C  CB   B ASP   B 1 105 ? 32.456 -26.481 12.039  0.26 30.56 ?  105 ASP   B CB   1 
ATOM   5628 C  CG   A ASP   B 1 105 ? 31.132 -26.793 11.672  0.74 35.10 ?  105 ASP   B CG   1 
ATOM   5629 C  CG   B ASP   B 1 105 ? 31.094 -27.059 11.700  0.26 31.42 ?  105 ASP   B CG   1 
ATOM   5630 O  OD1  A ASP   B 1 105 ? 31.030 -27.901 11.104  0.74 35.30 ?  105 ASP   B OD1  1 
ATOM   5631 O  OD1  B ASP   B 1 105 ? 31.041 -28.091 10.998  0.26 31.60 ?  105 ASP   B OD1  1 
ATOM   5632 O  OD2  A ASP   B 1 105 ? 30.149 -26.054 11.900  0.74 36.66 -1 105 ASP   B OD2  1 
ATOM   5633 O  OD2  B ASP   B 1 105 ? 30.075 -26.487 12.143  0.26 31.73 -1 105 ASP   B OD2  1 
ATOM   5634 H  H    A ASP   B 1 105 ? 34.883 -25.987 12.483  0.74 34.79 ?  105 ASP   B H    1 
ATOM   5635 H  H    B ASP   B 1 105 ? 34.822 -26.097 12.442  0.26 35.75 ?  105 ASP   B H    1 
ATOM   5636 H  HA   A ASP   B 1 105 ? 33.431 -28.145 11.981  0.74 35.51 ?  105 ASP   B HA   1 
ATOM   5637 H  HA   B ASP   B 1 105 ? 33.427 -28.277 11.880  0.26 35.72 ?  105 ASP   B HA   1 
ATOM   5638 H  HB2  A ASP   B 1 105 ? 32.528 -26.248 13.070  0.74 39.12 ?  105 ASP   B HB2  1 
ATOM   5639 H  HB2  B ASP   B 1 105 ? 32.504 -26.376 13.004  0.26 36.81 ?  105 ASP   B HB2  1 
ATOM   5640 H  HB3  A ASP   B 1 105 ? 32.645 -25.445 11.704  0.74 39.12 ?  105 ASP   B HB3  1 
ATOM   5641 H  HB3  B ASP   B 1 105 ? 32.532 -25.612 11.611  0.26 36.81 ?  105 ASP   B HB3  1 
ATOM   5642 N  N    A ILE   B 1 106 ? 33.505 -28.515 9.570   0.74 27.19 ?  106 ILE   B N    1 
ATOM   5643 N  N    B ILE   B 1 106 ? 33.488 -28.574 9.463   0.26 27.99 ?  106 ILE   B N    1 
ATOM   5644 C  CA   A ILE   B 1 106 ? 33.504 -28.703 8.123   0.74 26.28 ?  106 ILE   B CA   1 
ATOM   5645 C  CA   B ILE   B 1 106 ? 33.503 -28.722 8.013   0.26 27.38 ?  106 ILE   B CA   1 
ATOM   5646 C  C    A ILE   B 1 106 ? 32.412 -27.881 7.446   0.74 24.83 ?  106 ILE   B C    1 
ATOM   5647 C  C    B ILE   B 1 106 ? 32.406 -27.898 7.349   0.26 26.69 ?  106 ILE   B C    1 
ATOM   5648 O  O    A ILE   B 1 106 ? 32.521 -27.568 6.255   0.74 24.00 ?  106 ILE   B O    1 
ATOM   5649 O  O    B ILE   B 1 106 ? 32.491 -27.604 6.152   0.26 26.44 ?  106 ILE   B O    1 
ATOM   5650 C  CB   A ILE   B 1 106 ? 33.397 -30.211 7.796   0.74 27.19 ?  106 ILE   B CB   1 
ATOM   5651 C  CB   B ILE   B 1 106 ? 33.407 -30.221 7.645   0.26 27.58 ?  106 ILE   B CB   1 
ATOM   5652 C  CG1  A ILE   B 1 106 ? 33.657 -30.474 6.311   0.74 27.61 ?  106 ILE   B CG1  1 
ATOM   5653 C  CG1  B ILE   B 1 106 ? 33.683 -30.442 6.155   0.26 27.62 ?  106 ILE   B CG1  1 
ATOM   5654 C  CG2  A ILE   B 1 106 ? 32.032 -30.756 8.203   0.74 27.71 ?  106 ILE   B CG2  1 
ATOM   5655 C  CG2  B ILE   B 1 106 ? 32.040 -30.778 8.017   0.26 27.80 ?  106 ILE   B CG2  1 
ATOM   5656 C  CD1  A ILE   B 1 106 ? 35.025 -30.029 5.850   0.74 27.62 ?  106 ILE   B CD1  1 
ATOM   5657 C  CD1  B ILE   B 1 106 ? 35.044 -29.961 5.712   0.26 27.60 ?  106 ILE   B CD1  1 
ATOM   5658 H  H    A ILE   B 1 106 ? 33.390 -29.238 10.019  0.74 32.77 ?  106 ILE   B H    1 
ATOM   5659 H  H    B ILE   B 1 106 ? 33.355 -29.307 9.888   0.26 33.73 ?  106 ILE   B H    1 
ATOM   5660 H  HA   A ILE   B 1 106 ? 34.351 -28.390 7.783   0.74 31.67 ?  106 ILE   B HA   1 
ATOM   5661 H  HA   B ILE   B 1 106 ? 34.349 -28.390 7.685   0.26 33.00 ?  106 ILE   B HA   1 
ATOM   5662 H  HB   A ILE   B 1 106 ? 34.071 -30.683 8.309   0.74 32.77 ?  106 ILE   B HB   1 
ATOM   5663 H  HB   B ILE   B 1 106 ? 34.078 -30.703 8.152   0.26 33.24 ?  106 ILE   B HB   1 
ATOM   5664 H  HG12 A ILE   B 1 106 ? 33.588 -31.429 6.146   0.74 33.27 ?  106 ILE   B HG12 1 
ATOM   5665 H  HG12 B ILE   B 1 106 ? 33.632 -31.394 5.966   0.26 33.28 ?  106 ILE   B HG12 1 
ATOM   5666 H  HG13 A ILE   B 1 106 ? 32.996 -30.002 5.785   0.74 33.27 ?  106 ILE   B HG13 1 
ATOM   5667 H  HG13 B ILE   B 1 106 ? 33.016 -29.970 5.636   0.26 33.28 ?  106 ILE   B HG13 1 
ATOM   5668 H  HG21 A ILE   B 1 106 ? 32.040 -31.723 8.121   0.74 33.40 ?  106 ILE   B HG21 1 
ATOM   5669 H  HG21 B ILE   B 1 106 ? 32.057 -31.744 7.924   0.26 33.51 ?  106 ILE   B HG21 1 
ATOM   5670 H  HG22 A ILE   B 1 106 ? 31.853 -30.506 9.124   0.74 33.40 ?  106 ILE   B HG22 1 
ATOM   5671 H  HG22 B ILE   B 1 106 ? 31.842 -30.539 8.936   0.26 33.51 ?  106 ILE   B HG22 1 
ATOM   5672 H  HG23 A ILE   B 1 106 ? 31.352 -30.382 7.622   0.74 33.40 ?  106 ILE   B HG23 1 
ATOM   5673 H  HG23 B ILE   B 1 106 ? 31.370 -30.402 7.425   0.26 33.51 ?  106 ILE   B HG23 1 
ATOM   5674 H  HD11 A ILE   B 1 106 ? 35.218 -30.440 4.994   0.74 33.28 ?  106 ILE   B HD11 1 
ATOM   5675 H  HD11 B ILE   B 1 106 ? 35.249 -30.352 4.850   0.26 33.26 ?  106 ILE   B HD11 1 
ATOM   5676 H  HD12 A ILE   B 1 106 ? 35.029 -29.062 5.760   0.74 33.28 ?  106 ILE   B HD12 1 
ATOM   5677 H  HD12 B ILE   B 1 106 ? 35.029 -28.994 5.641   0.26 33.26 ?  106 ILE   B HD12 1 
ATOM   5678 H  HD13 A ILE   B 1 106 ? 35.685 -30.304 6.506   0.74 33.28 ?  106 ILE   B HD13 1 
ATOM   5679 H  HD13 B ILE   B 1 106 ? 35.704 -30.237 6.367   0.26 33.26 ?  106 ILE   B HD13 1 
ATOM   5680 N  N    A GLN   B 1 107 ? 31.362 -27.507 8.180   0.74 25.21 ?  107 GLN   B N    1 
ATOM   5681 N  N    B GLN   B 1 107 ? 31.371 -27.515 8.101   0.26 26.52 ?  107 GLN   B N    1 
ATOM   5682 C  CA   A GLN   B 1 107 ? 30.288 -26.706 7.601   0.74 25.47 ?  107 GLN   B CA   1 
ATOM   5683 C  CA   B GLN   B 1 107 ? 30.293 -26.708 7.539   0.26 26.30 ?  107 GLN   B CA   1 
ATOM   5684 C  C    A GLN   B 1 107 ? 30.778 -25.357 7.086   0.74 23.03 ?  107 GLN   B C    1 
ATOM   5685 C  C    B GLN   B 1 107 ? 30.774 -25.337 7.077   0.26 23.66 ?  107 GLN   B C    1 
ATOM   5686 O  O    A GLN   B 1 107 ? 30.138 -24.781 6.202   0.74 23.41 ?  107 GLN   B O    1 
ATOM   5687 O  O    B GLN   B 1 107 ? 30.118 -24.719 6.233   0.26 23.84 ?  107 GLN   B O    1 
ATOM   5688 C  CB   A GLN   B 1 107 ? 29.174 -26.505 8.633   0.74 29.37 ?  107 GLN   B CB   1 
ATOM   5689 C  CB   B GLN   B 1 107 ? 29.168 -26.562 8.567   0.26 28.93 ?  107 GLN   B CB   1 
ATOM   5690 C  CG   A GLN   B 1 107 ? 27.850 -26.013 8.056   0.74 33.28 ?  107 GLN   B CG   1 
ATOM   5691 C  CG   B GLN   B 1 107 ? 27.838 -26.085 7.992   0.26 31.36 ?  107 GLN   B CG   1 
ATOM   5692 C  CD   A GLN   B 1 107 ? 27.774 -24.500 7.950   0.74 36.35 ?  107 GLN   B CD   1 
ATOM   5693 C  CD   B GLN   B 1 107 ? 27.712 -24.573 7.965   0.26 33.31 ?  107 GLN   B CD   1 
ATOM   5694 O  OE1  A GLN   B 1 107 ? 28.606 -23.783 8.509   0.74 37.46 ?  107 GLN   B OE1  1 
ATOM   5695 O  OE1  B GLN   B 1 107 ? 28.518 -23.859 8.563   0.26 33.99 ?  107 GLN   B OE1  1 
ATOM   5696 N  NE2  A GLN   B 1 107 ? 26.767 -24.006 7.233   0.74 37.35 ?  107 GLN   B NE2  1 
ATOM   5697 N  NE2  B GLN   B 1 107 ? 26.693 -24.078 7.271   0.26 33.97 ?  107 GLN   B NE2  1 
ATOM   5698 H  H    A GLN   B 1 107 ? 31.250 -27.701 9.006   0.74 30.39 ?  107 GLN   B H    1 
ATOM   5699 H  H    B GLN   B 1 107 ? 31.268 -27.714 8.929   0.26 31.96 ?  107 GLN   B H    1 
ATOM   5700 H  HA   A GLN   B 1 107 ? 29.909 -27.190 6.850   0.74 30.70 ?  107 GLN   B HA   1 
ATOM   5701 H  HA   B GLN   B 1 107 ? 29.928 -27.170 6.769   0.26 31.70 ?  107 GLN   B HA   1 
ATOM   5702 H  HB2  A GLN   B 1 107 ? 29.003 -27.352 9.069   0.74 35.39 ?  107 GLN   B HB2  1 
ATOM   5703 H  HB2  B GLN   B 1 107 ? 29.013 -27.425 8.978   0.26 34.86 ?  107 GLN   B HB2  1 
ATOM   5704 H  HB3  A GLN   B 1 107 ? 29.472 -25.855 9.289   0.74 35.39 ?  107 GLN   B HB3  1 
ATOM   5705 H  HB3  B GLN   B 1 107 ? 29.444 -25.924 9.243   0.26 34.86 ?  107 GLN   B HB3  1 
ATOM   5706 H  HG2  A GLN   B 1 107 ? 27.735 -26.377 7.165   0.74 40.08 ?  107 GLN   B HG2  1 
ATOM   5707 H  HG2  B GLN   B 1 107 ? 27.753 -26.407 7.081   0.26 37.78 ?  107 GLN   B HG2  1 
ATOM   5708 H  HG3  A GLN   B 1 107 ? 27.125 -26.312 8.631   0.74 40.08 ?  107 GLN   B HG3  1 
ATOM   5709 H  HG3  B GLN   B 1 107 ? 27.114 -26.439 8.535   0.26 37.78 ?  107 GLN   B HG3  1 
ATOM   5710 H  HE21 A GLN   B 1 107 ? 26.205 -24.538 6.856   0.74 44.96 ?  107 GLN   B HE21 1 
ATOM   5711 H  HE21 B GLN   B 1 107 ? 26.150 -24.607 6.865   0.26 40.91 ?  107 GLN   B HE21 1 
ATOM   5712 H  HE22 A GLN   B 1 107 ? 26.676 -23.155 7.146   0.74 44.96 ?  107 GLN   B HE22 1 
ATOM   5713 H  HE22 B GLN   B 1 107 ? 26.576 -23.227 7.228   0.26 40.91 ?  107 GLN   B HE22 1 
ATOM   5714 N  N    . LEU   B 1 108 ? 31.902 -24.850 7.601   1.00 21.11 ?  108 LEU   B N    1 
ATOM   5715 C  CA   . LEU   B 1 108 ? 32.447 -23.554 7.189   1.00 18.56 ?  108 LEU   B CA   1 
ATOM   5716 C  C    . LEU   B 1 108 ? 33.091 -23.580 5.813   1.00 16.25 ?  108 LEU   B C    1 
ATOM   5717 O  O    . LEU   B 1 108 ? 33.521 -22.523 5.322   1.00 15.67 ?  108 LEU   B O    1 
ATOM   5718 C  CB   . LEU   B 1 108 ? 33.453 -23.057 8.226   1.00 19.16 ?  108 LEU   B CB   1 
ATOM   5719 C  CG   . LEU   B 1 108 ? 32.824 -22.573 9.531   1.00 20.60 ?  108 LEU   B CG   1 
ATOM   5720 C  CD1  . LEU   B 1 108 ? 33.846 -22.523 10.652  1.00 21.18 ?  108 LEU   B CD1  1 
ATOM   5721 C  CD2  . LEU   B 1 108 ? 32.205 -21.204 9.321   1.00 21.56 ?  108 LEU   B CD2  1 
ATOM   5722 H  H    A LEU   B 1 108 ? 32.365 -25.240 8.207   0.74 25.47 ?  108 LEU   B H    1 
ATOM   5723 H  H    B LEU   B 1 108 ? 32.363 -25.247 8.204   0.26 25.47 ?  108 LEU   B H    1 
ATOM   5724 H  HA   . LEU   B 1 108 ? 31.721 -22.915 7.154   1.00 22.42 ?  108 LEU   B HA   1 
ATOM   5725 H  HB2  . LEU   B 1 108 ? 34.059 -23.780 8.444   1.00 23.14 ?  108 LEU   B HB2  1 
ATOM   5726 H  HB3  . LEU   B 1 108 ? 33.948 -22.315 7.847   1.00 23.14 ?  108 LEU   B HB3  1 
ATOM   5727 H  HG   . LEU   B 1 108 ? 32.116 -23.185 9.793   1.00 24.86 ?  108 LEU   B HG   1 
ATOM   5728 H  HD11 . LEU   B 1 108 ? 33.404 -22.248 11.472  1.00 25.55 ?  108 LEU   B HD11 1 
ATOM   5729 H  HD12 . LEU   B 1 108 ? 34.234 -23.404 10.765  1.00 25.55 ?  108 LEU   B HD12 1 
ATOM   5730 H  HD13 . LEU   B 1 108 ? 34.537 -21.883 10.420  1.00 25.55 ?  108 LEU   B HD13 1 
ATOM   5731 H  HD21 . LEU   B 1 108 ? 31.863 -20.879 10.169  1.00 26.01 ?  108 LEU   B HD21 1 
ATOM   5732 H  HD22 . LEU   B 1 108 ? 32.884 -20.600 8.984   1.00 26.01 ?  108 LEU   B HD22 1 
ATOM   5733 H  HD23 . LEU   B 1 108 ? 31.480 -21.278 8.680   1.00 26.01 ?  108 LEU   B HD23 1 
ATOM   5734 N  N    . LEU   B 1 109 ? 33.152 -24.749 5.183   1.00 15.30 ?  109 LEU   B N    1 
ATOM   5735 C  CA   . LEU   B 1 109 ? 33.779 -24.861 3.874   1.00 14.34 ?  109 LEU   B CA   1 
ATOM   5736 C  C    . LEU   B 1 109 ? 33.012 -24.075 2.815   1.00 13.77 ?  109 LEU   B C    1 
ATOM   5737 O  O    . LEU   B 1 109 ? 33.626 -23.475 1.925   1.00 13.21 ?  109 LEU   B O    1 
ATOM   5738 C  CB   . LEU   B 1 109 ? 33.888 -26.337 3.499   1.00 14.32 ?  109 LEU   B CB   1 
ATOM   5739 C  CG   . LEU   B 1 109 ? 34.670 -26.676 2.234   1.00 14.20 ?  109 LEU   B CG   1 
ATOM   5740 C  CD1  . LEU   B 1 109 ? 36.053 -26.023 2.239   1.00 13.79 ?  109 LEU   B CD1  1 
ATOM   5741 C  CD2  . LEU   B 1 109 ? 34.791 -28.184 2.088   1.00 15.04 ?  109 LEU   B CD2  1 
ATOM   5742 H  H    . LEU   B 1 109 ? 32.849 -25.491 5.492   1.00 18.50 ?  109 LEU   B H    1 
ATOM   5743 H  HA   . LEU   B 1 109 ? 34.675 -24.502 3.921   1.00 17.34 ?  109 LEU   B HA   1 
ATOM   5744 H  HB2  . LEU   B 1 109 ? 34.322 -26.807 4.230   1.00 17.32 ?  109 LEU   B HB2  1 
ATOM   5745 H  HB3  . LEU   B 1 109 ? 32.993 -26.693 3.382   1.00 17.32 ?  109 LEU   B HB3  1 
ATOM   5746 H  HG   . LEU   B 1 109 ? 34.181 -26.348 1.460   1.00 17.18 ?  109 LEU   B HG   1 
ATOM   5747 H  HD11 . LEU   B 1 109 ? 36.578 -26.391 1.511   1.00 16.69 ?  109 LEU   B HD11 1 
ATOM   5748 H  HD12 . LEU   B 1 109 ? 35.947 -25.068 2.121   1.00 16.69 ?  109 LEU   B HD12 1 
ATOM   5749 H  HD13 . LEU   B 1 109 ? 36.484 -26.212 3.086   1.00 16.69 ?  109 LEU   B HD13 1 
ATOM   5750 H  HD21 . LEU   B 1 109 ? 35.348 -28.386 1.319   1.00 18.19 ?  109 LEU   B HD21 1 
ATOM   5751 H  HD22 . LEU   B 1 109 ? 35.191 -28.549 2.891   1.00 18.19 ?  109 LEU   B HD22 1 
ATOM   5752 H  HD23 . LEU   B 1 109 ? 33.904 -28.564 1.959   1.00 18.19 ?  109 LEU   B HD23 1 
ATOM   5753 N  N    . LYS   B 1 110 ? 31.677 -24.040 2.896   1.00 13.39 ?  110 LYS   B N    1 
ATOM   5754 C  CA   . LYS   B 1 110 ? 30.924 -23.283 1.899   1.00 13.30 ?  110 LYS   B CA   1 
ATOM   5755 C  C    . LYS   B 1 110 ? 31.260 -21.794 1.984   1.00 12.80 ?  110 LYS   B C    1 
ATOM   5756 O  O    . LYS   B 1 110 ? 31.518 -21.145 0.964   1.00 12.65 ?  110 LYS   B O    1 
ATOM   5757 C  CB   . LYS   B 1 110 ? 29.420 -23.535 2.043   1.00 13.61 ?  110 LYS   B CB   1 
ATOM   5758 C  CG   . LYS   B 1 110 ? 28.614 -22.926 0.899   1.00 13.93 ?  110 LYS   B CG   1 
ATOM   5759 C  CD   . LYS   B 1 110 ? 27.150 -23.358 0.931   1.00 14.22 ?  110 LYS   B CD   1 
ATOM   5760 C  CE   . LYS   B 1 110 ? 26.378 -22.821 -0.277  1.00 14.95 ?  110 LYS   B CE   1 
ATOM   5761 N  NZ   . LYS   B 1 110 ? 26.712 -23.523 -1.546  1.00 15.35 ?  110 LYS   B NZ   1 
ATOM   5762 H  H    . LYS   B 1 110 ? 31.205 -24.442 3.489   1.00 16.21 ?  110 LYS   B H    1 
ATOM   5763 H  HA   . LYS   B 1 110 ? 31.188 -23.589 1.016   1.00 16.10 ?  110 LYS   B HA   1 
ATOM   5764 H  HB2  . LYS   B 1 110 ? 29.260 -24.496 2.046   1.00 16.47 ?  110 LYS   B HB2  1 
ATOM   5765 H  HB3  . LYS   B 1 110 ? 29.110 -23.146 2.873   1.00 16.47 ?  110 LYS   B HB3  1 
ATOM   5766 H  HG2  . LYS   B 1 110 ? 28.638 -21.961 0.968   1.00 16.85 ?  110 LYS   B HG2  1 
ATOM   5767 H  HG3  . LYS   B 1 110 ? 28.989 -23.213 0.052   1.00 16.85 ?  110 LYS   B HG3  1 
ATOM   5768 H  HD2  . LYS   B 1 110 ? 27.097 -24.332 0.917   1.00 17.20 ?  110 LYS   B HD2  1 
ATOM   5769 H  HD3  . LYS   B 1 110 ? 26.727 -23.019 1.738   1.00 17.20 ?  110 LYS   B HD3  1 
ATOM   5770 H  HE2  . LYS   B 1 110 ? 25.426 -22.931 -0.120  1.00 18.08 ?  110 LYS   B HE2  1 
ATOM   5771 H  HE3  . LYS   B 1 110 ? 26.589 -21.883 -0.390  1.00 18.08 ?  110 LYS   B HE3  1 
ATOM   5772 H  HZ1  . LYS   B 1 110 ? 26.247 -23.179 -2.218  1.00 18.56 ?  110 LYS   B HZ1  1 
ATOM   5773 H  HZ2  . LYS   B 1 110 ? 27.583 -23.435 -1.720  1.00 18.56 ?  110 LYS   B HZ2  1 
ATOM   5774 H  HZ3  . LYS   B 1 110 ? 26.522 -24.391 -1.474  1.00 18.56 ?  110 LYS   B HZ3  1 
ATOM   5775 N  N    . SER   B 1 111 ? 31.289 -21.247 3.204   1.00 13.29 ?  111 SER   B N    1 
ATOM   5776 C  CA   . SER   B 1 111 ? 31.674 -19.848 3.380   1.00 13.00 ?  111 SER   B CA   1 
ATOM   5777 C  C    . SER   B 1 111 ? 33.053 -19.584 2.790   1.00 12.45 ?  111 SER   B C    1 
ATOM   5778 O  O    . SER   B 1 111 ? 33.279 -18.550 2.141   1.00 12.64 ?  111 SER   B O    1 
ATOM   5779 C  CB   . SER   B 1 111 ? 31.667 -19.485 4.865   1.00 14.04 ?  111 SER   B CB   1 
ATOM   5780 O  OG   . SER   B 1 111 ? 30.360 -19.482 5.396   1.00 15.75 ?  111 SER   B OG   1 
ATOM   5781 H  H    . SER   B 1 111 ? 31.102 -21.665 3.933   1.00 16.09 ?  111 SER   B H    1 
ATOM   5782 H  HA   . SER   B 1 111 ? 31.038 -19.283 2.924   1.00 15.74 ?  111 SER   B HA   1 
ATOM   5783 H  HB2  . SER   B 1 111 ? 32.195 -20.141 5.352   1.00 16.99 ?  111 SER   B HB2  1 
ATOM   5784 H  HB3  . SER   B 1 111 ? 32.051 -18.606 4.975   1.00 16.99 ?  111 SER   B HB3  1 
ATOM   5785 H  HG   . SER   B 1 111 ? 30.379 -19.279 6.216   1.00 19.05 ?  111 SER   B HG   1 
ATOM   5786 N  N    . ALA   B 1 112 ? 33.989 -20.508 3.008   1.00 12.53 ?  112 ALA   B N    1 
ATOM   5787 C  CA   . ALA   B 1 112 ? 35.333 -20.334 2.468   1.00 12.46 ?  112 ALA   B CA   1 
ATOM   5788 C  C    . ALA   B 1 112 ? 35.302 -20.238 0.944   1.00 11.75 ?  112 ALA   B C    1 
ATOM   5789 O  O    . ALA   B 1 112 ? 35.928 -19.349 0.352   1.00 11.92 ?  112 ALA   B O    1 
ATOM   5790 C  CB   . ALA   B 1 112 ? 36.238 -21.473 2.946   1.00 12.98 ?  112 ALA   B CB   1 
ATOM   5791 H  H    . ALA   B 1 112 ? 33.872 -21.236 3.462   1.00 15.18 ?  112 ALA   B H    1 
ATOM   5792 H  HA   . ALA   B 1 112 ? 35.696 -19.504 2.812   1.00 15.09 ?  112 ALA   B HA   1 
ATOM   5793 H  HB1  . ALA   B 1 112 ? 37.128 -21.335 2.586   1.00 15.72 ?  112 ALA   B HB1  1 
ATOM   5794 H  HB2  . ALA   B 1 112 ? 36.273 -21.459 3.919   1.00 15.72 ?  112 ALA   B HB2  1 
ATOM   5795 H  HB3  . ALA   B 1 112 ? 35.878 -22.314 2.640   1.00 15.72 ?  112 ALA   B HB3  1 
ATOM   5796 N  N    . TYR   B 1 113 ? 34.576 -21.146 0.286   1.00 11.64 ?  113 TYR   B N    1 
ATOM   5797 C  CA   . TYR   B 1 113 ? 34.497 -21.100 -1.170  1.00 11.40 ?  113 TYR   B CA   1 
ATOM   5798 C  C    . TYR   B 1 113 ? 33.791 -19.847 -1.683  1.00 10.97 ?  113 TYR   B C    1 
ATOM   5799 O  O    . TYR   B 1 113 ? 34.058 -19.415 -2.811  1.00 11.40 ?  113 TYR   B O    1 
ATOM   5800 C  CB   . TYR   B 1 113 ? 33.824 -22.361 -1.717  1.00 11.66 ?  113 TYR   B CB   1 
ATOM   5801 C  CG   . TYR   B 1 113 ? 34.785 -23.510 -1.973  1.00 11.96 ?  113 TYR   B CG   1 
ATOM   5802 C  CD1  . TYR   B 1 113 ? 35.788 -23.402 -2.927  1.00 12.65 ?  113 TYR   B CD1  1 
ATOM   5803 C  CD2  . TYR   B 1 113 ? 34.678 -24.704 -1.279  1.00 12.23 ?  113 TYR   B CD2  1 
ATOM   5804 C  CE1  . TYR   B 1 113 ? 36.667 -24.433 -3.175  1.00 12.70 ?  113 TYR   B CE1  1 
ATOM   5805 C  CE2  . TYR   B 1 113 ? 35.551 -25.756 -1.523  1.00 12.52 ?  113 TYR   B CE2  1 
ATOM   5806 C  CZ   . TYR   B 1 113 ? 36.539 -25.617 -2.476  1.00 12.70 ?  113 TYR   B CZ   1 
ATOM   5807 O  OH   . TYR   B 1 113 ? 37.420 -26.636 -2.747  1.00 13.50 ?  113 TYR   B OH   1 
ATOM   5808 H  H    . TYR   B 1 113 ? 34.114 -21.777 0.659   1.00 14.11 ?  113 TYR   B H    1 
ATOM   5809 H  HA   . TYR   B 1 113 ? 35.398 -21.084 -1.509  1.00 13.82 ?  113 TYR   B HA   1 
ATOM   5810 H  HB2  . TYR   B 1 113 ? 33.161 -22.673 -1.075  1.00 14.14 ?  113 TYR   B HB2  1 
ATOM   5811 H  HB3  . TYR   B 1 113 ? 33.386 -22.145 -2.555  1.00 14.14 ?  113 TYR   B HB3  1 
ATOM   5812 H  HD1  . TYR   B 1 113 ? 35.880 -22.605 -3.404  1.00 15.32 ?  113 TYR   B HD1  1 
ATOM   5813 H  HD2  . TYR   B 1 113 ? 34.003 -24.805 -0.650  1.00 14.82 ?  113 TYR   B HD2  1 
ATOM   5814 H  HE1  . TYR   B 1 113 ? 37.335 -24.338 -3.822  1.00 15.38 ?  113 TYR   B HE1  1 
ATOM   5815 H  HE2  . TYR   B 1 113 ? 35.457 -26.556 -1.061  1.00 15.17 ?  113 TYR   B HE2  1 
ATOM   5816 H  HH   . TYR   B 1 113 ? 37.236 -27.306 -2.278  1.00 16.34 ?  113 TYR   B HH   1 
ATOM   5817 N  N    . GLU   B 1 114 ? 32.865 -19.276 -0.903  1.00 11.22 ?  114 GLU   B N    1 
ATOM   5818 C  CA   . GLU   B 1 114 ? 32.181 -18.068 -1.359  1.00 11.27 ?  114 GLU   B CA   1 
ATOM   5819 C  C    . GLU   B 1 114 ? 33.164 -16.945 -1.658  1.00 11.07 ?  114 GLU   B C    1 
ATOM   5820 O  O    . GLU   B 1 114 ? 32.882 -16.084 -2.498  1.00 11.54 ?  114 GLU   B O    1 
ATOM   5821 C  CB   . GLU   B 1 114 ? 31.120 -17.639 -0.340  1.00 11.76 ?  114 GLU   B CB   1 
ATOM   5822 C  CG   . GLU   B 1 114 ? 29.902 -18.553 -0.412  1.00 12.01 ?  114 GLU   B CG   1 
ATOM   5823 C  CD   . GLU   B 1 114 ? 28.881 -18.369 0.699   1.00 12.13 ?  114 GLU   B CD   1 
ATOM   5824 O  OE1  . GLU   B 1 114 ? 29.168 -17.753 1.743   1.00 12.57 ?  114 GLU   B OE1  1 
ATOM   5825 O  OE2  . GLU   B 1 114 ? 27.758 -18.907 0.533   1.00 13.04 -1 114 GLU   B OE2  1 
ATOM   5826 H  H    . GLU   B 1 114 ? 32.612 -19.572 -0.132  1.00 13.60 ?  114 GLU   B H    1 
ATOM   5827 H  HA   . GLU   B 1 114 ? 31.724 -18.271 -2.183  1.00 13.67 ?  114 GLU   B HA   1 
ATOM   5828 H  HB2  . GLU   B 1 114 ? 31.489 -17.698 0.557   1.00 14.25 ?  114 GLU   B HB2  1 
ATOM   5829 H  HB3  . GLU   B 1 114 ? 30.835 -16.737 -0.531  1.00 14.25 ?  114 GLU   B HB3  1 
ATOM   5830 H  HG2  . GLU   B 1 114 ? 29.451 -18.391 -1.253  1.00 14.55 ?  114 GLU   B HG2  1 
ATOM   5831 H  HG3  . GLU   B 1 114 ? 30.208 -19.474 -0.378  1.00 14.55 ?  114 GLU   B HG3  1 
ATOM   5832 N  N    . ASN   B 1 115 ? 34.327 -16.932 -1.000  1.00 11.19 ?  115 ASN   B N    1 
ATOM   5833 C  CA   . ASN   B 1 115 ? 35.320 -15.902 -1.302  1.00 11.02 ?  115 ASN   B CA   1 
ATOM   5834 C  C    . ASN   B 1 115 ? 35.725 -15.925 -2.770  1.00 10.63 ?  115 ASN   B C    1 
ATOM   5835 O  O    . ASN   B 1 115 ? 36.119 -14.887 -3.325  1.00 11.43 ?  115 ASN   B O    1 
ATOM   5836 C  CB   . ASN   B 1 115 ? 36.559 -16.079 -0.418  1.00 11.54 ?  115 ASN   B CB   1 
ATOM   5837 C  CG   . ASN   B 1 115 ? 36.291 -15.815 1.044   1.00 12.06 ?  115 ASN   B CG   1 
ATOM   5838 O  OD1  . ASN   B 1 115 ? 36.301 -14.667 1.487   1.00 13.92 ?  115 ASN   B OD1  1 
ATOM   5839 N  ND2  . ASN   B 1 115 ? 36.119 -16.882 1.819   1.00 12.02 ?  115 ASN   B ND2  1 
ATOM   5840 H  H    . ASN   B 1 115 ? 34.561 -17.489 -0.380  1.00 13.56 ?  115 ASN   B H    1 
ATOM   5841 H  HA   . ASN   B 1 115 ? 34.944 -15.032 -1.109  1.00 13.36 ?  115 ASN   B HA   1 
ATOM   5842 H  HB2  . ASN   B 1 115 ? 36.887 -16.988 -0.505  1.00 13.99 ?  115 ASN   B HB2  1 
ATOM   5843 H  HB3  . ASN   B 1 115 ? 37.246 -15.455 -0.708  1.00 13.99 ?  115 ASN   B HB3  1 
ATOM   5844 H  HD21 . ASN   B 1 115 ? 35.974 -16.782 2.663   1.00 14.56 ?  115 ASN   B HD21 1 
ATOM   5845 H  HD22 . ASN   B 1 115 ? 36.136 -17.672 1.480   1.00 14.56 ?  115 ASN   B HD22 1 
ATOM   5846 N  N    . PHE   B 1 116 ? 35.696 -17.105 -3.402  1.00 10.50 ?  116 PHE   B N    1 
ATOM   5847 C  CA   . PHE   B 1 116 ? 36.132 -17.200 -4.790  1.00 10.98 ?  116 PHE   B CA   1 
ATOM   5848 C  C    . PHE   B 1 116 ? 35.228 -16.378 -5.703  1.00 10.87 ?  116 PHE   B C    1 
ATOM   5849 O  O    . PHE   B 1 116 ? 35.659 -15.947 -6.779  1.00 11.26 ?  116 PHE   B O    1 
ATOM   5850 C  CB   . PHE   B 1 116 ? 36.103 -18.646 -5.311  1.00 10.70 ?  116 PHE   B CB   1 
ATOM   5851 C  CG   . PHE   B 1 116 ? 37.170 -19.599 -4.757  1.00 10.55 ?  116 PHE   B CG   1 
ATOM   5852 C  CD1  . PHE   B 1 116 ? 37.823 -19.408 -3.549  1.00 11.43 ?  116 PHE   B CD1  1 
ATOM   5853 C  CD2  . PHE   B 1 116 ? 37.473 -20.737 -5.490  1.00 10.79 ?  116 PHE   B CD2  1 
ATOM   5854 C  CE1  . PHE   B 1 116 ? 38.753 -20.349 -3.090  1.00 11.48 ?  116 PHE   B CE1  1 
ATOM   5855 C  CE2  . PHE   B 1 116 ? 38.397 -21.672 -5.042  1.00 10.88 ?  116 PHE   B CE2  1 
ATOM   5856 C  CZ   . PHE   B 1 116 ? 39.034 -21.482 -3.848  1.00 11.01 ?  116 PHE   B CZ   1 
ATOM   5857 H  H    . PHE   B 1 116 ? 35.431 -17.850 -3.051  1.00 12.74 ?  116 PHE   B H    1 
ATOM   5858 H  HA   . PHE   B 1 116 ? 37.037 -16.867 -4.867  1.00 13.32 ?  116 PHE   B HA   1 
ATOM   5859 H  HB2  . PHE   B 1 116 ? 35.233 -19.028 -5.096  1.00 12.99 ?  116 PHE   B HB2  1 
ATOM   5860 H  HB3  . PHE   B 1 116 ? 36.209 -18.624 -6.273  1.00 12.99 ?  116 PHE   B HB3  1 
ATOM   5861 H  HD1  . PHE   B 1 116 ? 37.621 -18.658 -3.032  1.00 13.86 ?  116 PHE   B HD1  1 
ATOM   5862 H  HD2  . PHE   B 1 116 ? 37.035 -20.891 -6.294  1.00 13.09 ?  116 PHE   B HD2  1 
ATOM   5863 H  HE1  . PHE   B 1 116 ? 39.187 -20.205 -2.279  1.00 13.92 ?  116 PHE   B HE1  1 
ATOM   5864 H  HE2  . PHE   B 1 116 ? 38.584 -22.425 -5.553  1.00 13.20 ?  116 PHE   B HE2  1 
ATOM   5865 H  HZ   . PHE   B 1 116 ? 39.666 -22.093 -3.547  1.00 13.36 ?  116 PHE   B HZ   1 
ATOM   5866 N  N    . ASN   B 1 117 ? 33.961 -16.176 -5.316  1.00 10.98 ?  117 ASN   B N    1 
ATOM   5867 C  CA   . ASN   B 1 117 ? 33.016 -15.476 -6.184  1.00 11.34 ?  117 ASN   B CA   1 
ATOM   5868 C  C    . ASN   B 1 117 ? 33.330 -13.994 -6.340  1.00 11.65 ?  117 ASN   B C    1 
ATOM   5869 O  O    . ASN   B 1 117 ? 32.727 -13.341 -7.196  1.00 12.70 ?  117 ASN   B O    1 
ATOM   5870 C  CB   . ASN   B 1 117 ? 31.590 -15.692 -5.690  1.00 11.49 ?  117 ASN   B CB   1 
ATOM   5871 C  CG   . ASN   B 1 117 ? 31.136 -17.097 -5.942  1.00 11.76 ?  117 ASN   B CG   1 
ATOM   5872 O  OD1  . ASN   B 1 117 ? 31.494 -17.693 -6.961  1.00 12.69 ?  117 ASN   B OD1  1 
ATOM   5873 N  ND2  . ASN   B 1 117 ? 30.392 -17.667 -5.003  1.00 12.03 ?  117 ASN   B ND2  1 
ATOM   5874 H  H    . ASN   B 1 117 ? 33.637 -16.430 -4.556  1.00 13.32 ?  117 ASN   B H    1 
ATOM   5875 H  HA   . ASN   B 1 117 ? 33.074 -15.875 -7.060  1.00 13.75 ?  117 ASN   B HA   1 
ATOM   5876 H  HB2  . ASN   B 1 117 ? 31.550 -15.526 -4.731  1.00 13.93 ?  117 ASN   B HB2  1 
ATOM   5877 H  HB3  . ASN   B 1 117 ? 30.994 -15.084 -6.156  1.00 13.93 ?  117 ASN   B HB3  1 
ATOM   5878 H  HD21 . ASN   B 1 117 ? 30.107 -18.473 -5.107  1.00 14.57 ?  117 ASN   B HD21 1 
ATOM   5879 H  HD22 . ASN   B 1 117 ? 30.169 -17.223 -4.300  1.00 14.57 ?  117 ASN   B HD22 1 
ATOM   5880 N  N    . GLN   B 1 118 ? 34.266 -13.464 -5.563  1.00 11.48 ?  118 GLN   B N    1 
ATOM   5881 C  CA   . GLN   B 1 118 ? 34.692 -12.077 -5.707  1.00 12.16 ?  118 GLN   B CA   1 
ATOM   5882 C  C    . GLN   B 1 118 ? 35.762 -11.891 -6.779  1.00 12.14 ?  118 GLN   B C    1 
ATOM   5883 O  O    . GLN   B 1 118 ? 36.231 -10.763 -6.968  1.00 13.57 ?  118 GLN   B O    1 
ATOM   5884 C  CB   . GLN   B 1 118 ? 35.167 -11.534 -4.355  1.00 12.43 ?  118 GLN   B CB   1 
ATOM   5885 C  CG   . GLN   B 1 118 ? 34.083 -11.582 -3.287  1.00 12.55 ?  118 GLN   B CG   1 
ATOM   5886 C  CD   . GLN   B 1 118 ? 32.914 -10.675 -3.612  1.00 12.74 ?  118 GLN   B CD   1 
ATOM   5887 O  OE1  . GLN   B 1 118 ? 33.101 -9.534  -4.049  1.00 13.41 ?  118 GLN   B OE1  1 
ATOM   5888 N  NE2  . GLN   B 1 118 ? 31.698 -11.172 -3.411  1.00 13.23 ?  118 GLN   B NE2  1 
ATOM   5889 H  H    . GLN   B 1 118 ? 34.684 -13.886 -4.939  1.00 13.92 ?  118 GLN   B H    1 
ATOM   5890 H  HA   . GLN   B 1 118 ? 33.926 -11.550 -5.983  1.00 14.74 ?  118 GLN   B HA   1 
ATOM   5891 H  HB2  . GLN   B 1 118 ? 35.918 -12.054 -4.046  1.00 15.05 ?  118 GLN   B HB2  1 
ATOM   5892 H  HB3  . GLN   B 1 118 ? 35.431 -10.601 -4.464  1.00 15.05 ?  118 GLN   B HB3  1 
ATOM   5893 H  HG2  . GLN   B 1 118 ? 33.750 -12.491 -3.216  1.00 15.20 ?  118 GLN   B HG2  1 
ATOM   5894 H  HG3  . GLN   B 1 118 ? 34.459 -11.298 -2.439  1.00 15.20 ?  118 GLN   B HG3  1 
ATOM   5895 H  HE21 . GLN   B 1 118 ? 31.605 -11.971 -3.102  1.00 16.02 ?  118 GLN   B HE21 1 
ATOM   5896 H  HE22 . GLN   B 1 118 ? 31.008 -10.693 -3.580  1.00 16.02 ?  118 GLN   B HE22 1 
ATOM   5897 N  N    . HIS   B 1 119 ? 36.115 -12.950 -7.510  1.00 11.45 ?  119 HIS   B N    1 
ATOM   5898 C  CA   . HIS   B 1 119 ? 37.159 -12.901 -8.526  1.00 11.79 ?  119 HIS   B CA   1 
ATOM   5899 C  C    . HIS   B 1 119 ? 36.681 -13.633 -9.765  1.00 11.56 ?  119 HIS   B C    1 
ATOM   5900 O  O    . HIS   B 1 119 ? 36.167 -14.747 -9.663  1.00 12.45 ?  119 HIS   B O    1 
ATOM   5901 C  CB   . HIS   B 1 119 ? 38.437 -13.532 -7.977  1.00 12.41 ?  119 HIS   B CB   1 
ATOM   5902 C  CG   . HIS   B 1 119 ? 38.921 -12.830 -6.754  1.00 13.52 ?  119 HIS   B CG   1 
ATOM   5903 N  ND1  . HIS   B 1 119 ? 39.714 -11.704 -6.814  1.00 14.94 ?  119 HIS   B ND1  1 
ATOM   5904 C  CD2  . HIS   B 1 119 ? 38.627 -13.019 -5.448  1.00 14.78 ?  119 HIS   B CD2  1 
ATOM   5905 C  CE1  . HIS   B 1 119 ? 39.928 -11.262 -5.589  1.00 16.12 ?  119 HIS   B CE1  1 
ATOM   5906 N  NE2  . HIS   B 1 119 ? 39.271 -12.033 -4.743  1.00 16.29 ?  119 HIS   B NE2  1 
ATOM   5907 H  H    . HIS   B 1 119 ? 35.743 -13.729 -7.440  1.00 13.88 ?  119 HIS   B H    1 
ATOM   5908 H  HA   . HIS   B 1 119 ? 37.339 -11.977 -8.763  1.00 14.29 ?  119 HIS   B HA   1 
ATOM   5909 H  HB2  . HIS   B 1 119 ? 38.265 -14.458 -7.751  1.00 15.04 ?  119 HIS   B HB2  1 
ATOM   5910 H  HB3  . HIS   B 1 119 ? 39.133 -13.477 -8.654  1.00 15.04 ?  119 HIS   B HB3  1 
ATOM   5911 H  HD2  . HIS   B 1 119 ? 38.096 -13.696 -5.093  1.00 17.88 ?  119 HIS   B HD2  1 
ATOM   5912 H  HE1  . HIS   B 1 119 ? 40.458 -10.533 -5.359  1.00 19.49 ?  119 HIS   B HE1  1 
ATOM   5913 H  HE2  . HIS   B 1 119 ? 39.276 -11.954 -3.885  1.00 19.68 ?  119 HIS   B HE2  1 
ATOM   5914 N  N    . GLU   B 1 120 ? 36.838 -13.015 -10.935 1.00 12.11 ?  120 GLU   B N    1 
ATOM   5915 C  CA   . GLU   B 1 120 ? 36.247 -13.599 -12.136 1.00 13.89 ?  120 GLU   B CA   1 
ATOM   5916 C  C    . GLU   B 1 120 ? 36.923 -14.900 -12.553 1.00 12.77 ?  120 GLU   B C    1 
ATOM   5917 O  O    . GLU   B 1 120 ? 36.260 -15.775 -13.124 1.00 12.98 ?  120 GLU   B O    1 
ATOM   5918 C  CB   . GLU   B 1 120 ? 36.258 -12.591 -13.282 1.00 18.81 ?  120 GLU   B CB   1 
ATOM   5919 C  CG   . GLU   B 1 120 ? 35.308 -11.426 -13.063 1.00 25.35 ?  120 GLU   B CG   1 
ATOM   5920 C  CD   . GLU   B 1 120 ? 35.152 -10.549 -14.289 1.00 31.60 ?  120 GLU   B CD   1 
ATOM   5921 O  OE1  . GLU   B 1 120 ? 36.142 -10.376 -15.031 1.00 33.94 ?  120 GLU   B OE1  1 
ATOM   5922 O  OE2  . GLU   B 1 120 ? 34.036 -10.032 -14.508 1.00 34.37 -1 120 GLU   B OE2  1 
ATOM   5923 H  H    . GLU   B 1 120 ? 37.265 -12.277 -11.059 1.00 14.68 ?  120 GLU   B H    1 
ATOM   5924 H  HA   . GLU   B 1 120 ? 35.322 -13.806 -11.947 1.00 16.81 ?  120 GLU   B HA   1 
ATOM   5925 H  HB2  . GLU   B 1 120 ? 37.148 -12.228 -13.383 1.00 22.71 ?  120 GLU   B HB2  1 
ATOM   5926 H  HB3  . GLU   B 1 120 ? 35.987 -13.040 -14.100 1.00 22.71 ?  120 GLU   B HB3  1 
ATOM   5927 H  HG2  . GLU   B 1 120 ? 34.429 -11.769 -12.830 1.00 30.56 ?  120 GLU   B HG2  1 
ATOM   5928 H  HG3  . GLU   B 1 120 ? 35.646 -10.868 -12.348 1.00 30.56 ?  120 GLU   B HG3  1 
ATOM   5929 N  N    . VAL   B 1 121 ? 38.224 -15.043 -12.294 1.00 12.22 ?  121 VAL   B N    1 
ATOM   5930 C  CA   . VAL   B 1 121 ? 38.970 -16.254 -12.636 1.00 12.08 ?  121 VAL   B CA   1 
ATOM   5931 C  C    . VAL   B 1 121 ? 40.079 -16.456 -11.611 1.00 11.56 ?  121 VAL   B C    1 
ATOM   5932 O  O    . VAL   B 1 121 ? 40.757 -15.497 -11.218 1.00 12.20 ?  121 VAL   B O    1 
ATOM   5933 C  CB   . VAL   B 1 121 ? 39.490 -16.212 -14.093 1.00 14.10 ?  121 VAL   B CB   1 
ATOM   5934 C  CG1  . VAL   B 1 121 ? 40.361 -14.982 -14.344 1.00 15.31 ?  121 VAL   B CG1  1 
ATOM   5935 C  CG2  . VAL   B 1 121 ? 40.231 -17.499 -14.442 1.00 15.19 ?  121 VAL   B CG2  1 
ATOM   5936 H  H    . VAL   B 1 121 ? 38.709 -14.435 -11.925 1.00 14.80 ?  121 VAL   B H    1 
ATOM   5937 H  HA   . VAL   B 1 121 ? 38.363 -17.005 -12.572 1.00 14.64 ?  121 VAL   B HA   1 
ATOM   5938 H  HB   . VAL   B 1 121 ? 38.725 -16.152 -14.692 1.00 17.06 ?  121 VAL   B HB   1 
ATOM   5939 H  HG11 . VAL   B 1 121 ? 40.674 -14.998 -15.263 1.00 18.51 ?  121 VAL   B HG11 1 
ATOM   5940 H  HG12 . VAL   B 1 121 ? 39.832 -14.184 -14.190 1.00 18.51 ?  121 VAL   B HG12 1 
ATOM   5941 H  HG13 . VAL   B 1 121 ? 41.117 -15.002 -13.737 1.00 18.51 ?  121 VAL   B HG13 1 
ATOM   5942 H  HG21 . VAL   B 1 121 ? 40.440 -17.499 -15.392 1.00 18.37 ?  121 VAL   B HG21 1 
ATOM   5943 H  HG22 . VAL   B 1 121 ? 41.053 -17.543 -13.927 1.00 18.37 ?  121 VAL   B HG22 1 
ATOM   5944 H  HG23 . VAL   B 1 121 ? 39.667 -18.259 -14.231 1.00 18.37 ?  121 VAL   B HG23 1 
ATOM   5945 N  N    . LEU   B 1 122 ? 40.260 -17.711 -11.178 1.00 11.26 ?  122 LEU   B N    1 
ATOM   5946 C  CA   . LEU   B 1 122 ? 41.242 -18.062 -10.156 1.00 10.93 ?  122 LEU   B CA   1 
ATOM   5947 C  C    . LEU   B 1 122 ? 41.899 -19.392 -10.484 1.00 10.64 ?  122 LEU   B C    1 
ATOM   5948 O  O    . LEU   B 1 122 ? 41.240 -20.312 -10.983 1.00 11.88 ?  122 LEU   B O    1 
ATOM   5949 C  CB   . LEU   B 1 122 ? 40.588 -18.291 -8.781  1.00 12.42 ?  122 LEU   B CB   1 
ATOM   5950 C  CG   . LEU   B 1 122 ? 39.558 -17.260 -8.300  1.00 12.61 ?  122 LEU   B CG   1 
ATOM   5951 C  CD1  . LEU   B 1 122 ? 38.153 -17.604 -8.775  1.00 13.44 ?  122 LEU   B CD1  1 
ATOM   5952 C  CD2  . LEU   B 1 122 ? 39.599 -17.143 -6.788  1.00 12.43 ?  122 LEU   B CD2  1 
ATOM   5953 H  H    . LEU   B 1 122 ? 39.817 -18.389 -11.470 1.00 13.65 ?  122 LEU   B H    1 
ATOM   5954 H  HA   . LEU   B 1 122 ? 41.917 -17.367 -10.079 1.00 13.25 ?  122 LEU   B HA   1 
ATOM   5955 H  HB2  . LEU   B 1 122 ? 40.137 -19.146 -8.802  1.00 15.05 ?  122 LEU   B HB2  1 
ATOM   5956 H  HB3  . LEU   B 1 122 ? 41.290 -18.314 -8.114  1.00 15.05 ?  122 LEU   B HB3  1 
ATOM   5957 H  HG   . LEU   B 1 122 ? 39.788 -16.390 -8.665  1.00 15.27 ?  122 LEU   B HG   1 
ATOM   5958 H  HD11 . LEU   B 1 122 ? 37.530 -16.952 -8.409  1.00 16.27 ?  122 LEU   B HD11 1 
ATOM   5959 H  HD12 . LEU   B 1 122 ? 38.131 -17.564 -9.745  1.00 16.27 ?  122 LEU   B HD12 1 
ATOM   5960 H  HD13 . LEU   B 1 122 ? 37.923 -18.489 -8.470  1.00 16.27 ?  122 LEU   B HD13 1 
ATOM   5961 H  HD21 . LEU   B 1 122 ? 38.924 -16.510 -6.494  1.00 15.06 ?  122 LEU   B HD21 1 
ATOM   5962 H  HD22 . LEU   B 1 122 ? 39.428 -18.013 -6.395  1.00 15.06 ?  122 LEU   B HD22 1 
ATOM   5963 H  HD23 . LEU   B 1 122 ? 40.480 -16.828 -6.517  1.00 15.06 ?  122 LEU   B HD23 1 
ATOM   5964 N  N    . LEU   B 1 123 ? 43.185 -19.500 -10.126 1.00 10.46 ?  123 LEU   B N    1 
ATOM   5965 C  CA   . LEU   B 1 123 ? 43.897 -20.769 -10.003 1.00 10.46 ?  123 LEU   B CA   1 
ATOM   5966 C  C    . LEU   B 1 123 ? 43.873 -21.161 -8.531  1.00 10.24 ?  123 LEU   B C    1 
ATOM   5967 O  O    . LEU   B 1 123 ? 44.222 -20.336 -7.678  1.00 10.82 ?  123 LEU   B O    1 
ATOM   5968 C  CB   . LEU   B 1 123 ? 45.345 -20.589 -10.465 1.00 11.19 ?  123 LEU   B CB   1 
ATOM   5969 C  CG   . LEU   B 1 123 ? 46.290 -21.773 -10.218 1.00 11.50 ?  123 LEU   B CG   1 
ATOM   5970 C  CD1  . LEU   B 1 123 ? 45.874 -23.025 -10.993 1.00 11.99 ?  123 LEU   B CD1  1 
ATOM   5971 C  CD2  . LEU   B 1 123 ? 47.706 -21.375 -10.578 1.00 12.55 ?  123 LEU   B CD2  1 
ATOM   5972 H  H    . LEU   B 1 123 ? 43.682 -18.818 -9.934  1.00 12.70 ?  123 LEU   B H    1 
ATOM   5973 H  HA   . LEU   B 1 123 ? 43.458 -21.456 -10.532 1.00 12.69 ?  123 LEU   B HA   1 
ATOM   5974 H  HB2  . LEU   B 1 123 ? 45.335 -20.424 -11.419 1.00 13.56 ?  123 LEU   B HB2  1 
ATOM   5975 H  HB3  . LEU   B 1 123 ? 45.714 -19.824 -10.005 1.00 13.56 ?  123 LEU   B HB3  1 
ATOM   5976 H  HG   . LEU   B 1 123 ? 46.280 -21.995 -9.273  1.00 13.94 ?  123 LEU   B HG   1 
ATOM   5977 H  HD11 . LEU   B 1 123 ? 46.509 -23.732 -10.809 1.00 14.52 ?  123 LEU   B HD11 1 
ATOM   5978 H  HD12 . LEU   B 1 123 ? 44.986 -23.290 -10.705 1.00 14.52 ?  123 LEU   B HD12 1 
ATOM   5979 H  HD13 . LEU   B 1 123 ? 45.867 -22.818 -11.939 1.00 14.52 ?  123 LEU   B HD13 1 
ATOM   5980 H  HD21 . LEU   B 1 123 ? 48.295 -22.129 -10.420 1.00 15.20 ?  123 LEU   B HD21 1 
ATOM   5981 H  HD22 . LEU   B 1 123 ? 47.733 -21.123 -11.514 1.00 15.20 ?  123 LEU   B HD22 1 
ATOM   5982 H  HD23 . LEU   B 1 123 ? 47.972 -20.624 -10.025 1.00 15.20 ?  123 LEU   B HD23 1 
ATOM   5983 N  N    . ALA   B 1 124 ? 43.436 -22.390 -8.222  1.00 10.43 ?  124 ALA   B N    1 
ATOM   5984 C  CA   . ALA   B 1 124 ? 43.177 -22.710 -6.827  1.00 10.54 ?  124 ALA   B CA   1 
ATOM   5985 C  C    . ALA   B 1 124 ? 43.449 -24.169 -6.494  1.00 10.35 ?  124 ALA   B C    1 
ATOM   5986 O  O    . ALA   B 1 124 ? 43.310 -25.050 -7.358  1.00 10.94 ?  124 ALA   B O    1 
ATOM   5987 C  CB   . ALA   B 1 124 ? 41.718 -22.399 -6.458  1.00 11.07 ?  124 ALA   B CB   1 
ATOM   5988 H  H    . ALA   B 1 124 ? 43.269 -23.028 -8.782  1.00 12.66 ?  124 ALA   B H    1 
ATOM   5989 H  HA   . ALA   B 1 124 ? 43.745 -22.155 -6.276  1.00 12.79 ?  124 ALA   B HA   1 
ATOM   5990 H  HB1  . ALA   B 1 124 ? 41.565 -22.616 -5.525  1.00 13.42 ?  124 ALA   B HB1  1 
ATOM   5991 H  HB2  . ALA   B 1 124 ? 41.547 -21.452 -6.606  1.00 13.42 ?  124 ALA   B HB2  1 
ATOM   5992 H  HB3  . ALA   B 1 124 ? 41.125 -22.926 -7.019  1.00 13.42 ?  124 ALA   B HB3  1 
ATOM   5993 N  N    . PRO   B 1 125 ? 43.751 -24.458 -5.232  1.00 10.62 ?  125 PRO   B N    1 
ATOM   5994 C  CA   . PRO   B 1 125 ? 43.685 -25.823 -4.708  1.00 11.18 ?  125 PRO   B CA   1 
ATOM   5995 C  C    . PRO   B 1 125 ? 42.285 -26.098 -4.160  1.00 11.23 ?  125 PRO   B C    1 
ATOM   5996 O  O    . PRO   B 1 125 ? 41.490 -25.179 -3.950  1.00 11.80 ?  125 PRO   B O    1 
ATOM   5997 C  CB   . PRO   B 1 125 ? 44.668 -25.750 -3.535  1.00 12.12 ?  125 PRO   B CB   1 
ATOM   5998 C  CG   . PRO   B 1 125 ? 44.421 -24.368 -2.971  1.00 12.04 ?  125 PRO   B CG   1 
ATOM   5999 C  CD   . PRO   B 1 125 ? 44.083 -23.490 -4.172  1.00 11.04 ?  125 PRO   B CD   1 
ATOM   6000 H  HA   . PRO   B 1 125 ? 43.961 -26.494 -5.355  1.00 13.56 ?  125 PRO   B HA   1 
ATOM   6001 H  HB2  . PRO   B 1 125 ? 44.458 -26.434 -2.876  1.00 14.68 ?  125 PRO   B HB2  1 
ATOM   6002 H  HB3  . PRO   B 1 125 ? 45.579 -25.839 -3.850  1.00 14.68 ?  125 PRO   B HB3  1 
ATOM   6003 H  HG2  . PRO   B 1 125 ? 43.676 -24.390 -2.348  1.00 14.59 ?  125 PRO   B HG2  1 
ATOM   6004 H  HG3  . PRO   B 1 125 ? 45.224 -24.044 -2.524  1.00 14.59 ?  125 PRO   B HG3  1 
ATOM   6005 H  HD2  . PRO   B 1 125 ? 43.321 -22.926 -3.981  1.00 13.39 ?  125 PRO   B HD2  1 
ATOM   6006 H  HD3  . PRO   B 1 125 ? 44.861 -22.958 -4.428  1.00 13.39 ?  125 PRO   B HD3  1 
ATOM   6007 N  N    . LEU   B 1 126 ? 42.017 -27.377 -3.880  1.00 12.03 ?  126 LEU   B N    1 
ATOM   6008 C  CA   . LEU   B 1 126 ? 40.796 -27.743 -3.166  1.00 12.62 ?  126 LEU   B CA   1 
ATOM   6009 C  C    . LEU   B 1 126 ? 40.913 -27.343 -1.702  1.00 12.80 ?  126 LEU   B C    1 
ATOM   6010 O  O    . LEU   B 1 126 ? 41.805 -27.803 -0.986  1.00 14.48 ?  126 LEU   B O    1 
ATOM   6011 C  CB   . LEU   B 1 126 ? 40.541 -29.240 -3.279  1.00 13.83 ?  126 LEU   B CB   1 
ATOM   6012 C  CG   . LEU   B 1 126 ? 40.011 -29.725 -4.629  1.00 14.78 ?  126 LEU   B CG   1 
ATOM   6013 C  CD1  . LEU   B 1 126 ? 40.054 -31.232 -4.703  1.00 16.53 ?  126 LEU   B CD1  1 
ATOM   6014 C  CD2  . LEU   B 1 126 ? 38.593 -29.237 -4.878  1.00 15.23 ?  126 LEU   B CD2  1 
ATOM   6015 H  H    . LEU   B 1 126 ? 42.524 -28.042 -4.081  1.00 14.57 ?  126 LEU   B H    1 
ATOM   6016 H  HA   . LEU   B 1 126 ? 40.044 -27.268 -3.556  1.00 15.28 ?  126 LEU   B HA   1 
ATOM   6017 H  HB2  . LEU   B 1 126 ? 41.373 -29.701 -3.111  1.00 16.74 ?  126 LEU   B HB2  1 
ATOM   6018 H  HB3  . LEU   B 1 126 ? 39.887 -29.485 -2.608  1.00 16.74 ?  126 LEU   B HB3  1 
ATOM   6019 H  HG   . LEU   B 1 126 ? 40.577 -29.374 -5.335  1.00 17.87 ?  126 LEU   B HG   1 
ATOM   6020 H  HD11 . LEU   B 1 126 ? 39.713 -31.515 -5.566  1.00 19.98 ?  126 LEU   B HD11 1 
ATOM   6021 H  HD12 . LEU   B 1 126 ? 40.967 -31.529 -4.591  1.00 19.98 ?  126 LEU   B HD12 1 
ATOM   6022 H  HD13 . LEU   B 1 126 ? 39.495 -31.596 -3.995  1.00 19.98 ?  126 LEU   B HD13 1 
ATOM   6023 H  HD21 . LEU   B 1 126 ? 38.255 -29.646 -5.691  1.00 18.42 ?  126 LEU   B HD21 1 
ATOM   6024 H  HD22 . LEU   B 1 126 ? 38.034 -29.487 -4.126  1.00 18.42 ?  126 LEU   B HD22 1 
ATOM   6025 H  HD23 . LEU   B 1 126 ? 38.600 -28.270 -4.976  1.00 18.42 ?  126 LEU   B HD23 1 
ATOM   6026 N  N    . LEU   B 1 127 ? 39.987 -26.508 -1.246  1.00 12.47 ?  127 LEU   B N    1 
ATOM   6027 C  CA   . LEU   B 1 127 ? 40.046 -26.014 0.118   1.00 13.07 ?  127 LEU   B CA   1 
ATOM   6028 C  C    . LEU   B 1 127 ? 39.769 -27.133 1.112   1.00 12.62 ?  127 LEU   B C    1 
ATOM   6029 O  O    . LEU   B 1 127 ? 38.951 -28.030 0.881   1.00 13.17 ?  127 LEU   B O    1 
ATOM   6030 C  CB   . LEU   B 1 127 ? 39.032 -24.888 0.335   1.00 13.56 ?  127 LEU   B CB   1 
ATOM   6031 C  CG   . LEU   B 1 127 ? 39.210 -23.627 -0.507  1.00 14.12 ?  127 LEU   B CG   1 
ATOM   6032 C  CD1  . LEU   B 1 127 ? 38.084 -22.656 -0.191  1.00 14.33 ?  127 LEU   B CD1  1 
ATOM   6033 C  CD2  . LEU   B 1 127 ? 40.563 -22.978 -0.268  1.00 14.90 ?  127 LEU   B CD2  1 
ATOM   6034 H  H    . LEU   B 1 127 ? 39.317 -26.205 -1.705  1.00 15.11 ?  127 LEU   B H    1 
ATOM   6035 H  HA   . LEU   B 1 127 ? 40.932 -25.660 0.291   1.00 15.82 ?  127 LEU   B HA   1 
ATOM   6036 H  HB2  . LEU   B 1 127 ? 38.146 -25.237 0.146   1.00 16.41 ?  127 LEU   B HB2  1 
ATOM   6037 H  HB3  . LEU   B 1 127 ? 39.074 -24.618 1.266   1.00 16.41 ?  127 LEU   B HB3  1 
ATOM   6038 H  HG   . LEU   B 1 127 ? 39.139 -23.855 -1.444  1.00 17.09 ?  127 LEU   B HG   1 
ATOM   6039 H  HD11 . LEU   B 1 127 ? 38.200 -21.847 -0.719  1.00 17.33 ?  127 LEU   B HD11 1 
ATOM   6040 H  HD12 . LEU   B 1 127 ? 37.231 -23.066 -0.406  1.00 17.33 ?  127 LEU   B HD12 1 
ATOM   6041 H  HD13 . LEU   B 1 127 ? 38.110 -22.431 0.755   1.00 17.33 ?  127 LEU   B HD13 1 
ATOM   6042 H  HD21 . LEU   B 1 127 ? 40.598 -22.131 -0.741  1.00 18.02 ?  127 LEU   B HD21 1 
ATOM   6043 H  HD22 . LEU   B 1 127 ? 40.678 -22.827 0.684   1.00 18.02 ?  127 LEU   B HD22 1 
ATOM   6044 H  HD23 . LEU   B 1 127 ? 41.255 -23.570 -0.596  1.00 18.02 ?  127 LEU   B HD23 1 
ATOM   6045 N  N    . SER   B 1 128 ? 40.449 -27.048 2.245   1.00 12.71 ?  128 SER   B N    1 
ATOM   6046 C  CA   . SER   B 1 128 ? 40.333 -27.966 3.365   1.00 13.41 ?  128 SER   B CA   1 
ATOM   6047 C  C    . SER   B 1 128 ? 40.827 -29.374 3.046   1.00 14.53 ?  128 SER   B C    1 
ATOM   6048 O  O    . SER   B 1 128 ? 40.731 -30.256 3.901   1.00 15.85 ?  128 SER   B O    1 
ATOM   6049 C  CB   . SER   B 1 128 ? 38.933 -27.970 3.992   1.00 13.60 ?  128 SER   B CB   1 
ATOM   6050 O  OG   . SER   B 1 128 ? 38.634 -26.694 4.549   1.00 14.23 ?  128 SER   B OG   1 
ATOM   6051 H  H    . SER   B 1 128 ? 41.019 -26.423 2.395   1.00 15.40 ?  128 SER   B H    1 
ATOM   6052 H  HA   . SER   B 1 128 ? 40.922 -27.638 4.051   1.00 16.23 ?  128 SER   B HA   1 
ATOM   6053 H  HB2  . SER   B 1 128 ? 38.274 -28.190 3.310   1.00 16.46 ?  128 SER   B HB2  1 
ATOM   6054 H  HB3  . SER   B 1 128 ? 38.904 -28.648 4.697   1.00 16.46 ?  128 SER   B HB3  1 
ATOM   6055 H  HG   . SER   B 1 128 ? 39.201 -26.509 5.140   1.00 17.21 ?  128 SER   B HG   1 
ATOM   6056 N  N    . ALA   B 1 129 ? 41.407 -29.598 1.866   1.00 15.39 ?  129 ALA   B N    1 
ATOM   6057 C  CA   . ALA   B 1 129 ? 41.950 -30.898 1.507   1.00 16.46 ?  129 ALA   B CA   1 
ATOM   6058 C  C    . ALA   B 1 129 ? 43.340 -31.081 2.104   1.00 15.63 ?  129 ALA   B C    1 
ATOM   6059 O  O    . ALA   B 1 129 ? 43.900 -30.183 2.750   1.00 15.43 ?  129 ALA   B O    1 
ATOM   6060 C  CB   . ALA   B 1 129 ? 42.000 -31.054 -0.011  1.00 18.42 ?  129 ALA   B CB   1 
ATOM   6061 H  H    . ALA   B 1 129 ? 41.497 -29.003 1.247   1.00 18.60 ?  129 ALA   B H    1 
ATOM   6062 H  HA   . ALA   B 1 129 ? 41.378 -31.591 1.860   1.00 19.89 ?  129 ALA   B HA   1 
ATOM   6063 H  HB1  . ALA   B 1 129 ? 42.356 -31.932 -0.228  1.00 22.25 ?  129 ALA   B HB1  1 
ATOM   6064 H  HB2  . ALA   B 1 129 ? 41.104 -30.965 -0.367  1.00 22.25 ?  129 ALA   B HB2  1 
ATOM   6065 H  HB3  . ALA   B 1 129 ? 42.575 -30.366 -0.383  1.00 22.25 ?  129 ALA   B HB3  1 
ATOM   6066 N  N    . GLY   B 1 130 ? 43.904 -32.265 1.869   1.00 15.41 ?  130 GLY   B N    1 
ATOM   6067 C  CA   . GLY   B 1 130 ? 45.292 -32.499 2.221   1.00 15.78 ?  130 GLY   B CA   1 
ATOM   6068 C  C    . GLY   B 1 130 ? 45.506 -32.405 3.713   1.00 16.01 ?  130 GLY   B C    1 
ATOM   6069 O  O    . GLY   B 1 130 ? 44.806 -33.047 4.510   1.00 16.76 ?  130 GLY   B O    1 
ATOM   6070 H  H    . GLY   B 1 130 ? 43.512 -32.935 1.500   1.00 18.63 ?  130 GLY   B H    1 
ATOM   6071 H  HA2  . GLY   B 1 130 ? 45.559 -33.386 1.924   1.00 19.08 ?  130 GLY   B HA2  1 
ATOM   6072 H  HA3  . GLY   B 1 130 ? 45.859 -31.846 1.782   1.00 19.08 ?  130 GLY   B HA3  1 
ATOM   6073 N  N    . ILE   B 1 131 ? 46.482 -31.576 4.099   1.00 16.25 ?  131 ILE   B N    1 
ATOM   6074 C  CA   . ILE   B 1 131 ? 46.842 -31.446 5.503   1.00 17.11 ?  131 ILE   B CA   1 
ATOM   6075 C  C    . ILE   B 1 131 ? 45.726 -30.843 6.336   1.00 16.42 ?  131 ILE   B C    1 
ATOM   6076 O  O    . ILE   B 1 131 ? 45.797 -30.907 7.566   1.00 17.87 ?  131 ILE   B O    1 
ATOM   6077 C  CB   . ILE   B 1 131 ? 48.172 -30.684 5.699   1.00 18.93 ?  131 ILE   B CB   1 
ATOM   6078 C  CG1  . ILE   B 1 131 ? 48.014 -29.199 5.334   1.00 20.11 ?  131 ILE   B CG1  1 
ATOM   6079 C  CG2  . ILE   B 1 131 ? 49.286 -31.334 4.879   1.00 19.92 ?  131 ILE   B CG2  1 
ATOM   6080 C  CD1  . ILE   B 1 131 ? 49.237 -28.354 5.634   1.00 21.19 ?  131 ILE   B CD1  1 
ATOM   6081 H  H    . ILE   B 1 131 ? 46.943 -31.078 3.568   1.00 19.64 ?  131 ILE   B H    1 
ATOM   6082 H  HA   . ILE   B 1 131 ? 46.979 -32.336 5.850   1.00 20.68 ?  131 ILE   B HA   1 
ATOM   6083 H  HB   . ILE   B 1 131 ? 48.411 -30.739 6.637   1.00 22.86 ?  131 ILE   B HB   1 
ATOM   6084 H  HG12 . ILE   B 1 131 ? 47.827 -29.133 4.386   1.00 24.28 ?  131 ILE   B HG12 1 
ATOM   6085 H  HG13 . ILE   B 1 131 ? 47.271 -28.825 5.839   1.00 24.28 ?  131 ILE   B HG13 1 
ATOM   6086 H  HG21 . ILE   B 1 131 ? 50.130 -30.935 5.130   1.00 24.04 ?  131 ILE   B HG21 1 
ATOM   6087 H  HG22 . ILE   B 1 131 ? 49.293 -32.283 5.064   1.00 24.04 ?  131 ILE   B HG22 1 
ATOM   6088 H  HG23 . ILE   B 1 131 ? 49.109 -31.179 3.938   1.00 24.04 ?  131 ILE   B HG23 1 
ATOM   6089 H  HD11 . ILE   B 1 131 ? 49.021 -27.424 5.469   1.00 25.57 ?  131 ILE   B HD11 1 
ATOM   6090 H  HD12 . ILE   B 1 131 ? 49.482 -28.478 6.565   1.00 25.57 ?  131 ILE   B HD12 1 
ATOM   6091 H  HD13 . ILE   B 1 131 ? 49.962 -28.637 5.059   1.00 25.57 ?  131 ILE   B HD13 1 
ATOM   6092 N  N    . PHE   B 1 132 ? 44.695 -30.267 5.703   1.00 15.16 ?  132 PHE   B N    1 
ATOM   6093 C  CA   . PHE   B 1 132 ? 43.536 -29.758 6.430   1.00 15.55 ?  132 PHE   B CA   1 
ATOM   6094 C  C    . PHE   B 1 132 ? 42.511 -30.844 6.761   1.00 16.99 ?  132 PHE   B C    1 
ATOM   6095 O  O    . PHE   B 1 132 ? 41.606 -30.589 7.561   1.00 18.55 ?  132 PHE   B O    1 
ATOM   6096 C  CB   . PHE   B 1 132 ? 42.857 -28.623 5.649   1.00 14.55 ?  132 PHE   B CB   1 
ATOM   6097 C  CG   . PHE   B 1 132 ? 43.555 -27.281 5.763   1.00 14.57 ?  132 PHE   B CG   1 
ATOM   6098 C  CD1  . PHE   B 1 132 ? 44.853 -27.103 5.305   1.00 15.58 ?  132 PHE   B CD1  1 
ATOM   6099 C  CD2  . PHE   B 1 132 ? 42.882 -26.180 6.280   1.00 14.08 ?  132 PHE   B CD2  1 
ATOM   6100 C  CE1  . PHE   B 1 132 ? 45.477 -25.865 5.399   1.00 15.92 ?  132 PHE   B CE1  1 
ATOM   6101 C  CE2  . PHE   B 1 132 ? 43.495 -24.939 6.366   1.00 14.33 ?  132 PHE   B CE2  1 
ATOM   6102 C  CZ   . PHE   B 1 132 ? 44.792 -24.785 5.928   1.00 15.39 ?  132 PHE   B CZ   1 
ATOM   6103 H  H    . PHE   B 1 132 ? 44.643 -30.158 4.850   1.00 18.33 ?  132 PHE   B H    1 
ATOM   6104 H  HA   . PHE   B 1 132 ? 43.843 -29.384 7.269   1.00 18.80 ?  132 PHE   B HA   1 
ATOM   6105 H  HB2  . PHE   B 1 132 ? 42.840 -28.863 4.712   1.00 17.61 ?  132 PHE   B HB2  1 
ATOM   6106 H  HB3  . PHE   B 1 132 ? 41.951 -28.515 5.980   1.00 17.61 ?  132 PHE   B HB3  1 
ATOM   6107 H  HD1  . PHE   B 1 132 ? 45.316 -27.829 4.954   1.00 18.84 ?  132 PHE   B HD1  1 
ATOM   6108 H  HD2  . PHE   B 1 132 ? 42.006 -26.278 6.580   1.00 17.04 ?  132 PHE   B HD2  1 
ATOM   6109 H  HE1  . PHE   B 1 132 ? 46.350 -25.762 5.102   1.00 19.24 ?  132 PHE   B HE1  1 
ATOM   6110 H  HE2  . PHE   B 1 132 ? 43.035 -24.212 6.729   1.00 17.33 ?  132 PHE   B HE2  1 
ATOM   6111 H  HZ   . PHE   B 1 132 ? 45.206 -23.952 5.993   1.00 18.60 ?  132 PHE   B HZ   1 
ATOM   6112 N  N    . GLY   B 1 133 ? 42.613 -32.039 6.165   1.00 16.83 ?  133 GLY   B N    1 
ATOM   6113 C  CA   . GLY   B 1 133 ? 41.893 -33.199 6.661   1.00 17.72 ?  133 GLY   B CA   1 
ATOM   6114 C  C    . GLY   B 1 133 ? 40.497 -33.457 6.125   1.00 17.93 ?  133 GLY   B C    1 
ATOM   6115 O  O    . GLY   B 1 133 ? 39.907 -34.475 6.497   1.00 19.64 ?  133 GLY   B O    1 
ATOM   6116 H  H    . GLY   B 1 133 ? 43.101 -32.197 5.471   1.00 20.33 ?  133 GLY   B H    1 
ATOM   6117 H  HA2  . GLY   B 1 133 ? 42.425 -33.987 6.478   1.00 21.40 ?  133 GLY   B HA2  1 
ATOM   6118 H  HA3  . GLY   B 1 133 ? 41.815 -33.114 7.623   1.00 21.40 ?  133 GLY   B HA3  1 
ATOM   6119 N  N    . ALA   B 1 134 ? 39.936 -32.591 5.289   1.00 16.98 ?  134 ALA   B N    1 
ATOM   6120 C  CA   . ALA   B 1 134 ? 38.614 -32.876 4.751   1.00 16.96 ?  134 ALA   B CA   1 
ATOM   6121 C  C    . ALA   B 1 134 ? 38.704 -33.873 3.602   1.00 17.02 ?  134 ALA   B C    1 
ATOM   6122 O  O    . ALA   B 1 134 ? 39.760 -34.067 2.990   1.00 17.97 ?  134 ALA   B O    1 
ATOM   6123 C  CB   . ALA   B 1 134 ? 37.935 -31.597 4.265   1.00 17.39 ?  134 ALA   B CB   1 
ATOM   6124 H  H    . ALA   B 1 134 ? 40.285 -31.843 5.029   1.00 20.52 ?  134 ALA   B H    1 
ATOM   6125 H  HA   . ALA   B 1 134 ? 38.063 -33.260 5.452   1.00 20.49 ?  134 ALA   B HA   1 
ATOM   6126 H  HB1  . ALA   B 1 134 ? 37.050 -31.818 3.932   1.00 21.01 ?  134 ALA   B HB1  1 
ATOM   6127 H  HB2  . ALA   B 1 134 ? 37.863 -30.975 5.006   1.00 21.01 ?  134 ALA   B HB2  1 
ATOM   6128 H  HB3  . ALA   B 1 134 ? 38.467 -31.207 3.555   1.00 21.01 ?  134 ALA   B HB3  1 
ATOM   6129 N  N    . ASP   B 1 135 ? 37.570 -34.502 3.314   1.00 17.17 ?  135 ASP   B N    1 
ATOM   6130 C  CA   . ASP   B 1 135 ? 37.468 -35.391 2.169   1.00 17.90 ?  135 ASP   B CA   1 
ATOM   6131 C  C    . ASP   B 1 135 ? 37.572 -34.555 0.901   1.00 16.86 ?  135 ASP   B C    1 
ATOM   6132 O  O    . ASP   B 1 135 ? 36.722 -33.680 0.679   1.00 16.72 ?  135 ASP   B O    1 
ATOM   6133 C  CB   . ASP   B 1 135 ? 36.123 -36.113 2.221   1.00 19.89 ?  135 ASP   B CB   1 
ATOM   6134 C  CG   . ASP   B 1 135 ? 35.948 -37.116 1.097   1.00 21.80 ?  135 ASP   B CG   1 
ATOM   6135 O  OD1  . ASP   B 1 135 ? 36.814 -37.177 0.198   1.00 21.44 ?  135 ASP   B OD1  1 
ATOM   6136 O  OD2  . ASP   B 1 135 ? 34.945 -37.866 1.127   1.00 24.64 -1 135 ASP   B OD2  1 
ATOM   6137 H  H    . ASP   B 1 135 ? 36.840 -34.425 3.767   1.00 20.75 ?  135 ASP   B H    1 
ATOM   6138 H  HA   . ASP   B 1 135 ? 38.179 -36.052 2.201   1.00 21.62 ?  135 ASP   B HA   1 
ATOM   6139 H  HB2  . ASP   B 1 135 ? 36.053 -36.589 3.063   1.00 24.01 ?  135 ASP   B HB2  1 
ATOM   6140 H  HB3  . ASP   B 1 135 ? 35.413 -35.460 2.146   1.00 24.01 ?  135 ASP   B HB3  1 
ATOM   6141 N  N    . PRO   B 1 136 ? 38.580 -34.769 0.053   1.00 16.93 ?  136 PRO   B N    1 
ATOM   6142 C  CA   . PRO   B 1 136 ? 38.678 -33.951 -1.166  1.00 16.08 ?  136 PRO   B CA   1 
ATOM   6143 C  C    . PRO   B 1 136 ? 37.486 -34.103 -2.091  1.00 15.67 ?  136 PRO   B C    1 
ATOM   6144 O  O    . PRO   B 1 136 ? 37.164 -33.156 -2.815  1.00 15.07 ?  136 PRO   B O    1 
ATOM   6145 C  CB   . PRO   B 1 136 ? 39.989 -34.426 -1.809  1.00 17.21 ?  136 PRO   B CB   1 
ATOM   6146 C  CG   . PRO   B 1 136 ? 40.189 -35.810 -1.267  1.00 18.37 ?  136 PRO   B CG   1 
ATOM   6147 C  CD   . PRO   B 1 136 ? 39.655 -35.772 0.133   1.00 17.90 ?  136 PRO   B CD   1 
ATOM   6148 H  HA   . PRO   B 1 136 ? 38.766 -33.018 -0.930  1.00 19.44 ?  136 PRO   B HA   1 
ATOM   6149 H  HB2  . PRO   B 1 136 ? 39.897 -34.445 -2.776  1.00 20.79 ?  136 PRO   B HB2  1 
ATOM   6150 H  HB3  . PRO   B 1 136 ? 40.714 -33.842 -1.543  1.00 20.79 ?  136 PRO   B HB3  1 
ATOM   6151 H  HG2  . PRO   B 1 136 ? 39.694 -36.452 -1.803  1.00 22.18 ?  136 PRO   B HG2  1 
ATOM   6152 H  HG3  . PRO   B 1 136 ? 41.136 -36.031 -1.264  1.00 22.18 ?  136 PRO   B HG3  1 
ATOM   6153 H  HD2  . PRO   B 1 136 ? 39.295 -36.638 0.385   1.00 21.62 ?  136 PRO   B HD2  1 
ATOM   6154 H  HD3  . PRO   B 1 136 ? 40.341 -35.477 0.755   1.00 21.62 ?  136 PRO   B HD3  1 
ATOM   6155 N  N    . ILE   B 1 137 ? 36.827 -35.267 -2.098  1.00 15.98 ?  137 ILE   B N    1 
ATOM   6156 C  CA   . ILE   B 1 137 ? 35.607 -35.432 -2.885  1.00 16.27 ?  137 ILE   B CA   1 
ATOM   6157 C  C    . ILE   B 1 137 ? 34.537 -34.459 -2.404  1.00 16.01 ?  137 ILE   B C    1 
ATOM   6158 O  O    . ILE   B 1 137 ? 33.819 -33.848 -3.205  1.00 15.64 ?  137 ILE   B O    1 
ATOM   6159 C  CB   . ILE   B 1 137 ? 35.132 -36.899 -2.819  1.00 18.38 ?  137 ILE   B CB   1 
ATOM   6160 C  CG1  . ILE   B 1 137 ? 36.127 -37.811 -3.541  1.00 20.78 ?  137 ILE   B CG1  1 
ATOM   6161 C  CG2  . ILE   B 1 137 ? 33.726 -37.044 -3.404  1.00 18.71 ?  137 ILE   B CG2  1 
ATOM   6162 C  CD1  . ILE   B 1 137 ? 35.800 -39.287 -3.436  1.00 23.01 ?  137 ILE   B CD1  1 
ATOM   6163 H  H    . ILE   B 1 137 ? 37.063 -35.969 -1.666  1.00 19.31 ?  137 ILE   B H    1 
ATOM   6164 H  HA   . ILE   B 1 137 ? 35.798 -35.228 -3.816  1.00 19.67 ?  137 ILE   B HA   1 
ATOM   6165 H  HB   . ILE   B 1 137 ? 35.096 -37.164 -1.892  1.00 22.19 ?  137 ILE   B HB   1 
ATOM   6166 H  HG12 . ILE   B 1 137 ? 36.140 -37.583 -4.484  1.00 25.07 ?  137 ILE   B HG12 1 
ATOM   6167 H  HG13 . ILE   B 1 137 ? 37.006 -37.679 -3.157  1.00 25.07 ?  137 ILE   B HG13 1 
ATOM   6168 H  HG21 . ILE   B 1 137 ? 33.473 -37.983 -3.421  1.00 22.59 ?  137 ILE   B HG21 1 
ATOM   6169 H  HG22 . ILE   B 1 137 ? 33.092 -36.561 -2.851  1.00 22.59 ?  137 ILE   B HG22 1 
ATOM   6170 H  HG23 . ILE   B 1 137 ? 33.715 -36.689 -4.306  1.00 22.59 ?  137 ILE   B HG23 1 
ATOM   6171 H  HD11 . ILE   B 1 137 ? 36.474 -39.783 -3.922  1.00 27.75 ?  137 ILE   B HD11 1 
ATOM   6172 H  HD12 . ILE   B 1 137 ? 35.803 -39.551 -2.501  1.00 27.75 ?  137 ILE   B HD12 1 
ATOM   6173 H  HD13 . ILE   B 1 137 ? 34.930 -39.462 -3.827  1.00 27.75 ?  137 ILE   B HD13 1 
ATOM   6174 N  N    . HIS   B 1 138 ? 34.408 -34.308 -1.090  1.00 16.07 ?  138 HIS   B N    1 
ATOM   6175 C  CA   . HIS   B 1 138 ? 33.460 -33.341 -0.553  1.00 16.25 ?  138 HIS   B CA   1 
ATOM   6176 C  C    . HIS   B 1 138 ? 33.879 -31.913 -0.876  1.00 15.45 ?  138 HIS   B C    1 
ATOM   6177 O  O    . HIS   B 1 138 ? 33.031 -31.069 -1.185  1.00 15.92 ?  138 HIS   B O    1 
ATOM   6178 C  CB   . HIS   B 1 138 ? 33.338 -33.519 0.952   1.00 17.56 ?  138 HIS   B CB   1 
ATOM   6179 C  CG   . HIS   B 1 138 ? 32.411 -32.535 1.590   1.00 18.86 ?  138 HIS   B CG   1 
ATOM   6180 N  ND1  . HIS   B 1 138 ? 31.069 -32.471 1.283   1.00 20.09 ?  138 HIS   B ND1  1 
ATOM   6181 C  CD2  . HIS   B 1 138 ? 32.638 -31.554 2.495   1.00 19.56 ?  138 HIS   B CD2  1 
ATOM   6182 C  CE1  . HIS   B 1 138 ? 30.506 -31.503 1.982   1.00 20.15 ?  138 HIS   B CE1  1 
ATOM   6183 N  NE2  . HIS   B 1 138 ? 31.435 -30.933 2.729   1.00 19.73 ?  138 HIS   B NE2  1 
ATOM   6184 H  H    . HIS   B 1 138 ? 34.850 -34.748 -0.502  1.00 19.43 ?  138 HIS   B H    1 
ATOM   6185 H  HA   . HIS   B 1 138 ? 32.586 -33.502 -0.952  1.00 19.65 ?  138 HIS   B HA   1 
ATOM   6186 H  HB2  . HIS   B 1 138 ? 32.995 -34.408 1.137   1.00 21.22 ?  138 HIS   B HB2  1 
ATOM   6187 H  HB3  . HIS   B 1 138 ? 34.210 -33.407 1.353   1.00 21.22 ?  138 HIS   B HB3  1 
ATOM   6188 H  HD1  . HIS   B 1 138 ? 30.660 -32.987 0.727   1.00 24.24 ?  138 HIS   B HD1  1 
ATOM   6189 H  HD2  . HIS   B 1 138 ? 33.445 -31.345 2.896   1.00 23.61 ?  138 HIS   B HD2  1 
ATOM   6190 H  HE1  . HIS   B 1 138 ? 29.601 -31.272 1.960   1.00 24.32 ?  138 HIS   B HE1  1 
ATOM   6191 N  N    . SER   B 1 139 ? 35.174 -31.614 -0.802  1.00 15.11 ?  139 SER   B N    1 
ATOM   6192 C  CA   . SER   B 1 139 ? 35.613 -30.264 -1.121  1.00 14.28 ?  139 SER   B CA   1 
ATOM   6193 C  C    . SER   B 1 139 ? 35.283 -29.916 -2.564  1.00 13.51 ?  139 SER   B C    1 
ATOM   6194 O  O    . SER   B 1 139 ? 34.832 -28.801 -2.846  1.00 13.60 ?  139 SER   B O    1 
ATOM   6195 C  CB   . SER   B 1 139 ? 37.104 -30.121 -0.843  1.00 14.81 ?  139 SER   B CB   1 
ATOM   6196 O  OG   . SER   B 1 139 ? 37.513 -28.794 -1.106  1.00 14.75 ?  139 SER   B OG   1 
ATOM   6197 H  H    . SER   B 1 139 ? 35.794 -32.159 -0.587  1.00 18.27 ?  139 SER   B H    1 
ATOM   6198 H  HA   . SER   B 1 139 ? 35.132 -29.640 -0.558  1.00 17.28 ?  139 SER   B HA   1 
ATOM   6199 H  HB2  . SER   B 1 139 ? 37.267 -30.328 0.090   1.00 17.91 ?  139 SER   B HB2  1 
ATOM   6200 H  HB3  . SER   B 1 139 ? 37.596 -30.722 -1.416  1.00 17.91 ?  139 SER   B HB3  1 
ATOM   6201 H  HG   . SER   B 1 139 ? 38.336 -28.708 -0.941  1.00 17.84 ?  139 SER   B HG   1 
ATOM   6202 N  N    . LEU   B 1 140 ? 35.468 -30.861 -3.487  1.00 13.29 ?  140 LEU   B N    1 
ATOM   6203 C  CA   . LEU   B 1 140 ? 35.098 -30.617 -4.874  1.00 13.29 ?  140 LEU   B CA   1 
ATOM   6204 C  C    . LEU   B 1 140 ? 33.595 -30.388 -5.003  1.00 13.68 ?  140 LEU   B C    1 
ATOM   6205 O  O    . LEU   B 1 140 ? 33.158 -29.497 -5.738  1.00 13.62 ?  140 LEU   B O    1 
ATOM   6206 C  CB   . LEU   B 1 140 ? 35.565 -31.781 -5.747  1.00 13.47 ?  140 LEU   B CB   1 
ATOM   6207 C  CG   . LEU   B 1 140 ? 35.206 -31.680 -7.220  1.00 13.80 ?  140 LEU   B CG   1 
ATOM   6208 C  CD1  . LEU   B 1 140 ? 35.770 -30.400 -7.808  1.00 14.68 ?  140 LEU   B CD1  1 
ATOM   6209 C  CD2  . LEU   B 1 140 ? 35.694 -32.906 -7.965  1.00 15.15 ?  140 LEU   B CD2  1 
ATOM   6210 H  H    . LEU   B 1 140 ? 35.801 -31.637 -3.340  1.00 16.08 ?  140 LEU   B H    1 
ATOM   6211 H  HA   . LEU   B 1 140 ? 35.552 -29.816 -5.183  1.00 16.08 ?  140 LEU   B HA   1 
ATOM   6212 H  HB2  . LEU   B 1 140 ? 36.532 -31.846 -5.691  1.00 16.31 ?  140 LEU   B HB2  1 
ATOM   6213 H  HB3  . LEU   B 1 140 ? 35.166 -32.600 -5.415  1.00 16.31 ?  140 LEU   B HB3  1 
ATOM   6214 H  HG   . LEU   B 1 140 ? 34.243 -31.638 -7.307  1.00 16.71 ?  140 LEU   B HG   1 
ATOM   6215 H  HD11 . LEU   B 1 140 ? 35.680 -30.433 -8.771  1.00 17.76 ?  140 LEU   B HD11 1 
ATOM   6216 H  HD12 . LEU   B 1 140 ? 35.274 -29.643 -7.454  1.00 17.76 ?  140 LEU   B HD12 1 
ATOM   6217 H  HD13 . LEU   B 1 140 ? 36.705 -30.327 -7.564  1.00 17.76 ?  140 LEU   B HD13 1 
ATOM   6218 H  HD21 . LEU   B 1 140 ? 35.450 -32.814 -8.900  1.00 18.32 ?  140 LEU   B HD21 1 
ATOM   6219 H  HD22 . LEU   B 1 140 ? 36.651 -32.968 -7.872  1.00 18.32 ?  140 LEU   B HD22 1 
ATOM   6220 H  HD23 . LEU   B 1 140 ? 35.263 -33.685 -7.585  1.00 18.32 ?  140 LEU   B HD23 1 
ATOM   6221 N  N    . ARG   B 1 141 ? 32.793 -31.183 -4.290  1.00 13.65 ?  141 ARG   B N    1 
ATOM   6222 C  CA   . ARG   B 1 141 ? 31.344 -31.002 -4.265  1.00 14.55 ?  141 ARG   B CA   1 
ATOM   6223 C  C    . ARG   B 1 141 ? 30.970 -29.589 -3.842  1.00 14.37 ?  141 ARG   B C    1 
ATOM   6224 O  O    . ARG   B 1 141 ? 30.166 -28.914 -4.503  1.00 14.55 ?  141 ARG   B O    1 
ATOM   6225 C  CB   . ARG   B 1 141 ? 30.760 -32.027 -3.281  1.00 15.74 ?  141 ARG   B CB   1 
ATOM   6226 C  CG   . ARG   B 1 141 ? 29.285 -31.922 -2.974  1.00 17.61 ?  141 ARG   B CG   1 
ATOM   6227 C  CD   . ARG   B 1 141 ? 28.498 -32.560 -4.048  1.00 19.35 ?  141 ARG   B CD   1 
ATOM   6228 N  NE   . ARG   B 1 141 ? 28.235 -31.647 -5.148  1.00 19.77 ?  141 ARG   B NE   1 
ATOM   6229 C  CZ   . ARG   B 1 141 ? 28.210 -31.998 -6.426  1.00 19.15 ?  141 ARG   B CZ   1 
ATOM   6230 N  NH1  . ARG   B 1 141 ? 28.613 -33.194 -6.824  1.00 18.77 ?  141 ARG   B NH1  1 
ATOM   6231 N  NH2  . ARG   B 1 141 ? 27.771 -31.126 -7.328  1.00 20.01 ?  141 ARG   B NH2  1 
ATOM   6232 H  H    . ARG   B 1 141 ? 33.073 -31.836 -3.811  1.00 16.51 ?  141 ARG   B H    1 
ATOM   6233 H  HA   . ARG   B 1 141 ? 30.977 -31.167 -5.142  1.00 17.60 ?  141 ARG   B HA   1 
ATOM   6234 H  HB2  . ARG   B 1 141 ? 30.927 -32.914 -3.636  1.00 19.03 ?  141 ARG   B HB2  1 
ATOM   6235 H  HB3  . ARG   B 1 141 ? 31.231 -31.936 -2.437  1.00 19.03 ?  141 ARG   B HB3  1 
ATOM   6236 H  HG2  . ARG   B 1 141 ? 29.103 -32.372 -2.138  1.00 21.28 ?  141 ARG   B HG2  1 
ATOM   6237 H  HG3  . ARG   B 1 141 ? 29.026 -30.985 -2.912  1.00 21.28 ?  141 ARG   B HG3  1 
ATOM   6238 H  HD2  . ARG   B 1 141 ? 28.991 -33.328 -4.388  1.00 23.36 ?  141 ARG   B HD2  1 
ATOM   6239 H  HD3  . ARG   B 1 141 ? 27.654 -32.856 -3.684  1.00 23.36 ?  141 ARG   B HD3  1 
ATOM   6240 H  HE   . ARG   B 1 141 ? 28.067 -30.827 -4.953  1.00 23.86 ?  141 ARG   B HE   1 
ATOM   6241 H  HH11 . ARG   B 1 141 ? 28.885 -33.776 -6.253  1.00 22.66 ?  141 ARG   B HH11 1 
ATOM   6242 H  HH12 . ARG   B 1 141 ? 28.594 -33.393 -7.658  1.00 22.66 ?  141 ARG   B HH12 1 
ATOM   6243 H  HH21 . ARG   B 1 141 ? 27.516 -30.342 -7.082  1.00 24.15 ?  141 ARG   B HH21 1 
ATOM   6244 H  HH22 . ARG   B 1 141 ? 27.772 -31.335 -8.163  1.00 24.15 ?  141 ARG   B HH22 1 
ATOM   6245 N  N    . VAL   B 1 142 ? 31.513 -29.142 -2.712  1.00 13.96 ?  142 VAL   B N    1 
ATOM   6246 C  CA   . VAL   B 1 142 ? 31.178 -27.810 -2.228  1.00 13.76 ?  142 VAL   B CA   1 
ATOM   6247 C  C    . VAL   B 1 142 ? 31.652 -26.751 -3.216  1.00 13.57 ?  142 VAL   B C    1 
ATOM   6248 O  O    . VAL   B 1 142 ? 30.952 -25.765 -3.473  1.00 14.10 ?  142 VAL   B O    1 
ATOM   6249 C  CB   . VAL   B 1 142 ? 31.723 -27.581 -0.805  1.00 14.47 ?  142 VAL   B CB   1 
ATOM   6250 C  CG1  . VAL   B 1 142 ? 31.410 -26.161 -0.341  1.00 14.11 ?  142 VAL   B CG1  1 
ATOM   6251 C  CG2  . VAL   B 1 142 ? 31.134 -28.596 0.161   1.00 15.32 ?  142 VAL   B CG2  1 
ATOM   6252 H  H    . VAL   B 1 142 ? 32.070 -29.579 -2.217  1.00 16.89 ?  142 VAL   B H    1 
ATOM   6253 H  HA   . VAL   B 1 142 ? 30.218 -27.739 -2.174  1.00 16.66 ?  142 VAL   B HA   1 
ATOM   6254 H  HB   . VAL   B 1 142 ? 32.688 -27.691 -0.807  1.00 17.50 ?  142 VAL   B HB   1 
ATOM   6255 H  HG11 . VAL   B 1 142 ? 31.588 -26.094 0.608   1.00 17.07 ?  142 VAL   B HG11 1 
ATOM   6256 H  HG12 . VAL   B 1 142 ? 31.975 -25.537 -0.827  1.00 17.07 ?  142 VAL   B HG12 1 
ATOM   6257 H  HG13 . VAL   B 1 142 ? 30.477 -25.971 -0.519  1.00 17.07 ?  142 VAL   B HG13 1 
ATOM   6258 H  HG21 . VAL   B 1 142 ? 31.457 -28.407 1.056   1.00 18.52 ?  142 VAL   B HG21 1 
ATOM   6259 H  HG22 . VAL   B 1 142 ? 30.166 -28.525 0.138   1.00 18.52 ?  142 VAL   B HG22 1 
ATOM   6260 H  HG23 . VAL   B 1 142 ? 31.407 -29.485 -0.110  1.00 18.52 ?  142 VAL   B HG23 1 
ATOM   6261 N  N    . CYS   B 1 143 ? 32.835 -26.946 -3.800  1.00 13.05 ?  143 CYS   B N    1 
ATOM   6262 C  CA   . CYS   B 1 143 ? 33.330 -26.008 -4.804  1.00 13.23 ?  143 CYS   B CA   1 
ATOM   6263 C  C    . CYS   B 1 143 ? 32.329 -25.863 -5.945  1.00 13.07 ?  143 CYS   B C    1 
ATOM   6264 O  O    . CYS   B 1 143 ? 31.928 -24.751 -6.307  1.00 13.21 ?  143 CYS   B O    1 
ATOM   6265 C  CB   . CYS   B 1 143 ? 34.688 -26.489 -5.329  1.00 13.51 ?  143 CYS   B CB   1 
ATOM   6266 S  SG   . CYS   B 1 143 ? 35.438 -25.396 -6.553  1.00 13.72 ?  143 CYS   B SG   1 
ATOM   6267 H  H    . CYS   B 1 143 ? 33.365 -27.599 -3.637  1.00 15.80 ?  143 CYS   B H    1 
ATOM   6268 H  HA   . CYS   B 1 143 ? 33.457 -25.134 -4.401  1.00 16.01 ?  143 CYS   B HA   1 
ATOM   6269 H  HB2  . CYS   B 1 143 ? 35.308 -26.564 -4.586  1.00 16.36 ?  143 CYS   B HB2  1 
ATOM   6270 H  HB3  . CYS   B 1 143 ? 34.573 -27.357 -5.740  1.00 16.36 ?  143 CYS   B HB3  1 
ATOM   6271 H  HG   . CYS   B 1 143 ? 36.520 -25.831 -6.863  1.00 16.60 ?  143 CYS   B HG   1 
ATOM   6272 N  N    . VAL   B 1 144 ? 31.923 -26.986 -6.534  1.00 13.56 ?  144 VAL   B N    1 
ATOM   6273 C  CA   . VAL   B 1 144 ? 31.014 -26.936 -7.674  1.00 14.51 ?  144 VAL   B CA   1 
ATOM   6274 C  C    . VAL   B 1 144 ? 29.675 -26.316 -7.297  1.00 14.59 ?  144 VAL   B C    1 
ATOM   6275 O  O    . VAL   B 1 144 ? 29.059 -25.606 -8.102  1.00 16.01 ?  144 VAL   B O    1 
ATOM   6276 C  CB   . VAL   B 1 144 ? 30.848 -28.350 -8.243  1.00 16.86 ?  144 VAL   B CB   1 
ATOM   6277 C  CG1  . VAL   B 1 144 ? 29.561 -28.478 -9.058  1.00 19.05 ?  144 VAL   B CG1  1 
ATOM   6278 C  CG2  . VAL   B 1 144 ? 32.084 -28.741 -9.049  1.00 17.14 ?  144 VAL   B CG2  1 
ATOM   6279 H  H    . VAL   B 1 144 ? 32.160 -27.778 -6.302  1.00 16.42 ?  144 VAL   B H    1 
ATOM   6280 H  HA   . VAL   B 1 144 ? 31.396 -26.382 -8.368  1.00 17.55 ?  144 VAL   B HA   1 
ATOM   6281 H  HB   . VAL   B 1 144 ? 30.779 -28.972 -7.499  1.00 20.37 ?  144 VAL   B HB   1 
ATOM   6282 H  HG11 . VAL   B 1 144 ? 29.626 -29.272 -9.617  1.00 23.00 ?  144 VAL   B HG11 1 
ATOM   6283 H  HG12 . VAL   B 1 144 ? 28.808 -28.570 -8.453  1.00 23.00 ?  144 VAL   B HG12 1 
ATOM   6284 H  HG13 . VAL   B 1 144 ? 29.455 -27.694 -9.613  1.00 23.00 ?  144 VAL   B HG13 1 
ATOM   6285 H  HG21 . VAL   B 1 144 ? 31.963 -29.640 -9.393  1.00 20.71 ?  144 VAL   B HG21 1 
ATOM   6286 H  HG22 . VAL   B 1 144 ? 32.186 -28.116 -9.785  1.00 20.71 ?  144 VAL   B HG22 1 
ATOM   6287 H  HG23 . VAL   B 1 144 ? 32.859 -28.705 -8.472  1.00 20.71 ?  144 VAL   B HG23 1 
ATOM   6288 N  N    . ASP   B 1 145 ? 29.207 -26.562 -6.078  1.00 14.77 ?  145 ASP   B N    1 
ATOM   6289 C  CA   . ASP   B 1 145 ? 27.898 -26.091 -5.650  1.00 15.59 ?  145 ASP   B CA   1 
ATOM   6290 C  C    . ASP   B 1 145 ? 27.929 -24.665 -5.109  1.00 15.12 ?  145 ASP   B C    1 
ATOM   6291 O  O    . ASP   B 1 145 ? 26.869 -24.127 -4.771  1.00 16.89 ?  145 ASP   B O    1 
ATOM   6292 C  CB   . ASP   B 1 145 ? 27.309 -27.013 -4.572  1.00 17.33 ?  145 ASP   B CB   1 
ATOM   6293 C  CG   . ASP   B 1 145 ? 26.955 -28.392 -5.084  1.00 18.91 ?  145 ASP   B CG   1 
ATOM   6294 O  OD1  . ASP   B 1 145 ? 26.855 -28.578 -6.313  1.00 19.43 ?  145 ASP   B OD1  1 
ATOM   6295 O  OD2  . ASP   B 1 145 ? 26.766 -29.285 -4.234  1.00 21.00 -1 145 ASP   B OD2  1 
ATOM   6296 H  H    . ASP   B 1 145 ? 29.641 -26.984 -5.469  1.00 17.86 ?  145 ASP   B H    1 
ATOM   6297 H  HA   . ASP   B 1 145 ? 27.303 -26.088 -6.412  1.00 18.85 ?  145 ASP   B HA   1 
ATOM   6298 H  HB2  . ASP   B 1 145 ? 27.951 -27.124 -3.866  1.00 20.93 ?  145 ASP   B HB2  1 
ATOM   6299 H  HB3  . ASP   B 1 145 ? 26.493 -26.609 -4.232  1.00 20.93 ?  145 ASP   B HB3  1 
ATOM   6300 N  N    . THR   B 1 146 ? 29.108 -24.049 -5.003  1.00 13.49 ?  146 THR   B N    1 
ATOM   6301 C  CA   . THR   B 1 146 ? 29.242 -22.726 -4.400  1.00 12.78 ?  146 THR   B CA   1 
ATOM   6302 C  C    . THR   B 1 146 ? 29.872 -21.699 -5.323  1.00 12.74 ?  146 THR   B C    1 
ATOM   6303 O  O    . THR   B 1 146 ? 29.416 -20.541 -5.372  1.00 13.07 ?  146 THR   B O    1 
ATOM   6304 C  CB   . THR   B 1 146 ? 30.069 -22.830 -3.111  1.00 13.21 ?  146 THR   B CB   1 
ATOM   6305 O  OG1  . THR   B 1 146 ? 29.494 -23.822 -2.251  1.00 13.61 ?  146 THR   B OG1  1 
ATOM   6306 C  CG2  . THR   B 1 146 ? 30.142 -21.490 -2.396  1.00 13.60 ?  146 THR   B CG2  1 
ATOM   6307 H  H    . THR   B 1 146 ? 29.859 -24.377 -5.277  1.00 16.33 ?  146 THR   B H    1 
ATOM   6308 H  HA   . THR   B 1 146 ? 28.367 -22.396 -4.161  1.00 15.48 ?  146 THR   B HA   1 
ATOM   6309 H  HB   . THR   B 1 146 ? 30.978 -23.088 -3.335  1.00 15.99 ?  146 THR   B HB   1 
ATOM   6310 H  HG1  . THR   B 1 146 ? 29.530 -24.579 -2.628  1.00 16.47 ?  146 THR   B HG1  1 
ATOM   6311 H  HG21 . THR   B 1 146 ? 30.490 -21.610 -1.501  1.00 16.46 ?  146 THR   B HG21 1 
ATOM   6312 H  HG22 . THR   B 1 146 ? 30.728 -20.884 -2.882  1.00 16.46 ?  146 THR   B HG22 1 
ATOM   6313 H  HG23 . THR   B 1 146 ? 29.258 -21.096 -2.343  1.00 16.46 ?  146 THR   B HG23 1 
ATOM   6314 N  N    . VAL   B 1 147 ? 30.933 -22.076 -6.026  1.00 12.75 ?  147 VAL   B N    1 
ATOM   6315 C  CA   . VAL   B 1 147 ? 31.658 -21.132 -6.861  1.00 12.32 ?  147 VAL   B CA   1 
ATOM   6316 C  C    . VAL   B 1 147 ? 30.926 -20.999 -8.183  1.00 12.53 ?  147 VAL   B C    1 
ATOM   6317 O  O    . VAL   B 1 147 ? 30.555 -22.001 -8.808  1.00 13.68 ?  147 VAL   B O    1 
ATOM   6318 C  CB   . VAL   B 1 147 ? 33.113 -21.587 -7.063  1.00 12.50 ?  147 VAL   B CB   1 
ATOM   6319 C  CG1  . VAL   B 1 147 ? 33.872 -20.562 -7.886  1.00 12.67 ?  147 VAL   B CG1  1 
ATOM   6320 C  CG2  . VAL   B 1 147 ? 33.792 -21.802 -5.725  1.00 12.61 ?  147 VAL   B CG2  1 
ATOM   6321 H  H    . VAL   B 1 147 ? 31.250 -22.881 -6.048  1.00 15.44 ?  147 VAL   B H    1 
ATOM   6322 H  HA   . VAL   B 1 147 ? 31.672 -20.268 -6.432  1.00 14.92 ?  147 VAL   B HA   1 
ATOM   6323 H  HB   . VAL   B 1 147 ? 33.127 -22.430 -7.549  1.00 15.14 ?  147 VAL   B HB   1 
ATOM   6324 H  HG11 . VAL   B 1 147 ? 34.818 -20.778 -7.871  1.00 15.35 ?  147 VAL   B HG11 1 
ATOM   6325 H  HG12 . VAL   B 1 147 ? 33.546 -20.578 -8.800  1.00 15.35 ?  147 VAL   B HG12 1 
ATOM   6326 H  HG13 . VAL   B 1 147 ? 33.731 -19.682 -7.500  1.00 15.35 ?  147 VAL   B HG13 1 
ATOM   6327 H  HG21 . VAL   B 1 147 ? 34.733 -21.998 -5.873  1.00 15.27 ?  147 VAL   B HG21 1 
ATOM   6328 H  HG22 . VAL   B 1 147 ? 33.703 -20.996 -5.194  1.00 15.27 ?  147 VAL   B HG22 1 
ATOM   6329 H  HG23 . VAL   B 1 147 ? 33.369 -22.547 -5.271  1.00 15.27 ?  147 VAL   B HG23 1 
ATOM   6330 N  N    . ARG   B 1 148 ? 30.717 -19.752 -8.605  1.00 12.27 ?  148 ARG   B N    1 
ATOM   6331 C  CA   . ARG   B 1 148 ? 30.091 -19.439 -9.879  1.00 12.67 ?  148 ARG   B CA   1 
ATOM   6332 C  C    . ARG   B 1 148 ? 31.044 -18.764 -10.852 1.00 12.72 ?  148 ARG   B C    1 
ATOM   6333 O  O    . ARG   B 1 148 ? 30.757 -18.740 -12.051 1.00 14.12 ?  148 ARG   B O    1 
ATOM   6334 C  CB   . ARG   B 1 148 ? 28.851 -18.557 -9.662  1.00 13.11 ?  148 ARG   B CB   1 
ATOM   6335 C  CG   . ARG   B 1 148 ? 27.783 -19.265 -8.840  1.00 13.83 ?  148 ARG   B CG   1 
ATOM   6336 C  CD   . ARG   B 1 148 ? 26.571 -18.378 -8.534  1.00 14.80 ?  148 ARG   B CD   1 
ATOM   6337 N  NE   . ARG   B 1 148 ? 26.947 -17.174 -7.804  1.00 14.68 ?  148 ARG   B NE   1 
ATOM   6338 C  CZ   . ARG   B 1 148 ? 27.249 -17.136 -6.513  1.00 13.75 ?  148 ARG   B CZ   1 
ATOM   6339 N  NH1  . ARG   B 1 148 ? 27.185 -18.220 -5.753  1.00 13.92 ?  148 ARG   B NH1  1 
ATOM   6340 N  NH2  . ARG   B 1 148 ? 27.649 -15.985 -5.973  1.00 13.72 ?  148 ARG   B NH2  1 
ATOM   6341 H  H    . ARG   B 1 148 ? 30.940 -19.051 -8.153  1.00 14.87 ?  148 ARG   B H    1 
ATOM   6342 H  HA   . ARG   B 1 148 ? 29.799 -20.264 -10.291 1.00 15.34 ?  148 ARG   B HA   1 
ATOM   6343 H  HB2  . ARG   B 1 148 ? 29.112 -17.752 -9.191  1.00 15.87 ?  148 ARG   B HB2  1 
ATOM   6344 H  HB3  . ARG   B 1 148 ? 28.469 -18.333 -10.525 1.00 15.87 ?  148 ARG   B HB3  1 
ATOM   6345 H  HG2  . ARG   B 1 148 ? 27.469 -20.041 -9.334  1.00 16.74 ?  148 ARG   B HG2  1 
ATOM   6346 H  HG3  . ARG   B 1 148 ? 28.169 -19.547 -7.996  1.00 16.74 ?  148 ARG   B HG3  1 
ATOM   6347 H  HD2  . ARG   B 1 148 ? 26.155 -18.110 -9.367  1.00 17.90 ?  148 ARG   B HD2  1 
ATOM   6348 H  HD3  . ARG   B 1 148 ? 25.940 -18.878 -7.991  1.00 17.90 ?  148 ARG   B HD3  1 
ATOM   6349 H  HE   . ARG   B 1 148 ? 26.997 -16.441 -8.245  1.00 17.75 ?  148 ARG   B HE   1 
ATOM   6350 H  HH11 . ARG   B 1 148 ? 26.927 -18.972 -6.086  1.00 16.84 ?  148 ARG   B HH11 1 
ATOM   6351 H  HH12 . ARG   B 1 148 ? 27.378 -18.172 -4.915  1.00 16.84 ?  148 ARG   B HH12 1 
ATOM   6352 H  HH21 . ARG   B 1 148 ? 27.703 -15.281 -6.460  1.00 16.61 ?  148 ARG   B HH21 1 
ATOM   6353 H  HH22 . ARG   B 1 148 ? 27.846 -15.948 -5.137  1.00 16.61 ?  148 ARG   B HH22 1 
ATOM   6354 N  N    . THR   B 1 149 ? 32.151 -18.210 -10.363 1.00 12.56 ?  149 THR   B N    1 
ATOM   6355 C  CA   . THR   B 1 149 ? 33.197 -17.650 -11.204 1.00 12.74 ?  149 THR   B CA   1 
ATOM   6356 C  C    . THR   B 1 149 ? 34.079 -18.788 -11.719 1.00 12.51 ?  149 THR   B C    1 
ATOM   6357 O  O    . THR   B 1 149 ? 33.886 -19.957 -11.380 1.00 12.97 ?  149 THR   B O    1 
ATOM   6358 C  CB   . THR   B 1 149 ? 33.966 -16.596 -10.414 1.00 12.81 ?  149 THR   B CB   1 
ATOM   6359 O  OG1  . THR   B 1 149 ? 34.419 -17.191 -9.197  1.00 12.60 ?  149 THR   B OG1  1 
ATOM   6360 C  CG2  . THR   B 1 149 ? 33.075 -15.382 -10.117 1.00 13.47 ?  149 THR   B CG2  1 
ATOM   6361 H  H    . THR   B 1 149 ? 32.315 -18.139 -9.522  1.00 15.21 ?  149 THR   B H    1 
ATOM   6362 H  HA   . THR   B 1 149 ? 32.791 -17.210 -11.967 1.00 15.43 ?  149 THR   B HA   1 
ATOM   6363 H  HB   . THR   B 1 149 ? 34.732 -16.306 -10.924 1.00 15.52 ?  149 THR   B HB   1 
ATOM   6364 H  HG1  . THR   B 1 149 ? 34.832 -16.618 -8.731  1.00 15.26 ?  149 THR   B HG1  1 
ATOM   6365 H  HG21 . THR   B 1 149 ? 33.580 -14.713 -9.622  1.00 16.31 ?  149 THR   B HG21 1 
ATOM   6366 H  HG22 . THR   B 1 149 ? 32.768 -14.985 -10.949 1.00 16.31 ?  149 THR   B HG22 1 
ATOM   6367 H  HG23 . THR   B 1 149 ? 32.307 -15.646 -9.591  1.00 16.31 ?  149 THR   B HG23 1 
ATOM   6368 N  N    . ASN   B 1 150 ? 35.042 -18.465 -12.572 1.00 12.44 ?  150 ASN   B N    1 
ATOM   6369 C  CA   . ASN   B 1 150 ? 35.808 -19.488 -13.275 1.00 12.82 ?  150 ASN   B CA   1 
ATOM   6370 C  C    . ASN   B 1 150 ? 36.971 -19.939 -12.400 1.00 12.49 ?  150 ASN   B C    1 
ATOM   6371 O  O    . ASN   B 1 150 ? 37.901 -19.168 -12.148 1.00 13.04 ?  150 ASN   B O    1 
ATOM   6372 C  CB   . ASN   B 1 150 ? 36.276 -18.953 -14.622 1.00 14.66 ?  150 ASN   B CB   1 
ATOM   6373 C  CG   . ASN   B 1 150 ? 35.130 -18.748 -15.571 1.00 17.51 ?  150 ASN   B CG   1 
ATOM   6374 O  OD1  . ASN   B 1 150 ? 34.236 -19.579 -15.645 1.00 18.34 ?  150 ASN   B OD1  1 
ATOM   6375 N  ND2  . ASN   B 1 150 ? 35.125 -17.627 -16.275 1.00 19.12 ?  150 ASN   B ND2  1 
ATOM   6376 H  H    . ASN   B 1 150 ? 35.279 -17.656 -12.755 1.00 15.07 ?  150 ASN   B H    1 
ATOM   6377 H  HA   . ASN   B 1 150 ? 35.232 -20.254 -13.438 1.00 15.52 ?  150 ASN   B HA   1 
ATOM   6378 H  HB2  . ASN   B 1 150 ? 36.711 -18.096 -14.488 1.00 17.74 ?  150 ASN   B HB2  1 
ATOM   6379 H  HB3  . ASN   B 1 150 ? 36.888 -19.584 -15.020 1.00 17.74 ?  150 ASN   B HB3  1 
ATOM   6380 H  HD21 . ASN   B 1 150 ? 34.486 -17.465 -16.830 1.00 23.08 ?  150 ASN   B HD21 1 
ATOM   6381 H  HD22 . ASN   B 1 150 ? 35.768 -17.061 -16.189 1.00 23.08 ?  150 ASN   B HD22 1 
ATOM   6382 N  N    . VAL   B 1 151 ? 36.924 -21.186 -11.938 1.00 12.14 ?  151 VAL   B N    1 
ATOM   6383 C  CA   . VAL   B 1 151 ? 37.942 -21.718 -11.046 1.00 12.36 ?  151 VAL   B CA   1 
ATOM   6384 C  C    . VAL   B 1 151 ? 38.653 -22.886 -11.720 1.00 12.18 ?  151 VAL   B C    1 
ATOM   6385 O  O    . VAL   B 1 151 ? 38.016 -23.825 -12.222 1.00 13.16 ?  151 VAL   B O    1 
ATOM   6386 C  CB   . VAL   B 1 151 ? 37.386 -22.058 -9.647  1.00 13.71 ?  151 VAL   B CB   1 
ATOM   6387 C  CG1  . VAL   B 1 151 ? 36.211 -23.040 -9.724  1.00 14.69 ?  151 VAL   B CG1  1 
ATOM   6388 C  CG2  . VAL   B 1 151 ? 38.499 -22.561 -8.740  1.00 13.91 ?  151 VAL   B CG2  1 
ATOM   6389 H  H    . VAL   B 1 151 ? 36.300 -21.748 -12.137 1.00 14.71 ?  151 VAL   B H    1 
ATOM   6390 H  HA   . VAL   B 1 151 ? 38.606 -21.022 -10.913 1.00 14.98 ?  151 VAL   B HA   1 
ATOM   6391 H  HB   . VAL   B 1 151 ? 37.047 -21.239 -9.250  1.00 16.60 ?  151 VAL   B HB   1 
ATOM   6392 H  HG11 . VAL   B 1 151 ? 35.899 -23.233 -8.825  1.00 17.77 ?  151 VAL   B HG11 1 
ATOM   6393 H  HG12 . VAL   B 1 151 ? 35.492 -22.636 -10.240 1.00 17.77 ?  151 VAL   B HG12 1 
ATOM   6394 H  HG13 . VAL   B 1 151 ? 36.505 -23.857 -10.154 1.00 17.77 ?  151 VAL   B HG13 1 
ATOM   6395 H  HG21 . VAL   B 1 151 ? 38.160 -22.631 -7.832  1.00 16.84 ?  151 VAL   B HG21 1 
ATOM   6396 H  HG22 . VAL   B 1 151 ? 38.791 -23.435 -9.048  1.00 16.84 ?  151 VAL   B HG22 1 
ATOM   6397 H  HG23 . VAL   B 1 151 ? 39.240 -21.936 -8.766  1.00 16.84 ?  151 VAL   B HG23 1 
ATOM   6398 N  N    . TYR   B 1 152 ? 39.983 -22.796 -11.740 1.00 11.55 ?  152 TYR   B N    1 
ATOM   6399 C  CA   . TYR   B 1 152 ? 40.887 -23.779 -12.319 1.00 11.97 ?  152 TYR   B CA   1 
ATOM   6400 C  C    . TYR   B 1 152 ? 41.610 -24.454 -11.158 1.00 11.41 ?  152 TYR   B C    1 
ATOM   6401 O  O    . TYR   B 1 152 ? 42.460 -23.839 -10.506 1.00 11.96 ?  152 TYR   B O    1 
ATOM   6402 C  CB   . TYR   B 1 152 ? 41.852 -23.075 -13.275 1.00 12.75 ?  152 TYR   B CB   1 
ATOM   6403 C  CG   . TYR   B 1 152 ? 41.170 -22.611 -14.542 1.00 13.45 ?  152 TYR   B CG   1 
ATOM   6404 C  CD1  . TYR   B 1 152 ? 40.498 -21.390 -14.604 1.00 13.74 ?  152 TYR   B CD1  1 
ATOM   6405 C  CD2  . TYR   B 1 152 ? 41.170 -23.414 -15.669 1.00 14.62 ?  152 TYR   B CD2  1 
ATOM   6406 C  CE1  . TYR   B 1 152 ? 39.860 -20.987 -15.762 1.00 15.02 ?  152 TYR   B CE1  1 
ATOM   6407 C  CE2  . TYR   B 1 152 ? 40.534 -23.023 -16.828 1.00 15.61 ?  152 TYR   B CE2  1 
ATOM   6408 C  CZ   . TYR   B 1 152 ? 39.884 -21.808 -16.873 1.00 15.93 ?  152 TYR   B CZ   1 
ATOM   6409 O  OH   . TYR   B 1 152 ? 39.255 -21.433 -18.036 1.00 18.32 ?  152 TYR   B OH   1 
ATOM   6410 H  H    . TYR   B 1 152 ? 40.415 -22.129 -11.391 1.00 14.01 ?  152 TYR   B H    1 
ATOM   6411 H  HA   . TYR   B 1 152 ? 40.377 -24.444 -12.811 1.00 14.50 ?  152 TYR   B HA   1 
ATOM   6412 H  HB2  . TYR   B 1 152 ? 42.225 -22.298 -12.827 1.00 15.44 ?  152 TYR   B HB2  1 
ATOM   6413 H  HB3  . TYR   B 1 152 ? 42.562 -23.689 -13.518 1.00 15.44 ?  152 TYR   B HB3  1 
ATOM   6414 H  HD1  . TYR   B 1 152 ? 40.477 -20.836 -13.854 1.00 16.63 ?  152 TYR   B HD1  1 
ATOM   6415 H  HD2  . TYR   B 1 152 ? 41.607 -24.235 -15.643 1.00 17.68 ?  152 TYR   B HD2  1 
ATOM   6416 H  HE1  . TYR   B 1 152 ? 39.417 -20.169 -15.795 1.00 18.17 ?  152 TYR   B HE1  1 
ATOM   6417 H  HE2  . TYR   B 1 152 ? 40.553 -23.573 -17.576 1.00 18.87 ?  152 TYR   B HE2  1 
ATOM   6418 H  HH   . TYR   B 1 152 ? 39.358 -22.027 -18.622 1.00 22.13 ?  152 TYR   B HH   1 
ATOM   6419 N  N    . LEU   B 1 153 ? 41.246 -25.710 -10.890 1.00 11.66 ?  153 LEU   B N    1 
ATOM   6420 C  CA   . LEU   B 1 153 ? 41.751 -26.463 -9.752  1.00 11.31 ?  153 LEU   B CA   1 
ATOM   6421 C  C    . LEU   B 1 153 ? 42.985 -27.262 -10.148 1.00 11.52 ?  153 LEU   B C    1 
ATOM   6422 O  O    . LEU   B 1 153 ? 42.969 -27.991 -11.143 1.00 12.85 ?  153 LEU   B O    1 
ATOM   6423 C  CB   . LEU   B 1 153 ? 40.672 -27.425 -9.241  1.00 11.74 ?  153 LEU   B CB   1 
ATOM   6424 C  CG   . LEU   B 1 153 ? 39.419 -26.766 -8.663  1.00 12.56 ?  153 LEU   B CG   1 
ATOM   6425 C  CD1  . LEU   B 1 153 ? 38.309 -27.792 -8.497  1.00 13.50 ?  153 LEU   B CD1  1 
ATOM   6426 C  CD2  . LEU   B 1 153 ? 39.725 -26.107 -7.333  1.00 13.18 ?  153 LEU   B CD2  1 
ATOM   6427 H  H    . LEU   B 1 153 ? 40.679 -26.159 -11.370 1.00 14.14 ?  153 LEU   B H    1 
ATOM   6428 H  HA   . LEU   B 1 153 ? 41.981 -25.851 -9.041  1.00 13.71 ?  153 LEU   B HA   1 
ATOM   6429 H  HB2  . LEU   B 1 153 ? 40.387 -27.991 -9.972  1.00 14.22 ?  153 LEU   B HB2  1 
ATOM   6430 H  HB3  . LEU   B 1 153 ? 41.056 -27.972 -8.537  1.00 14.22 ?  153 LEU   B HB3  1 
ATOM   6431 H  HG   . LEU   B 1 153 ? 39.103 -26.076 -9.272  1.00 15.22 ?  153 LEU   B HG   1 
ATOM   6432 H  HD11 . LEU   B 1 153 ? 37.502 -27.335 -8.198  1.00 16.34 ?  153 LEU   B HD11 1 
ATOM   6433 H  HD12 . LEU   B 1 153 ? 38.149 -28.218 -9.348  1.00 16.34 ?  153 LEU   B HD12 1 
ATOM   6434 H  HD13 . LEU   B 1 153 ? 38.583 -28.442 -7.837  1.00 16.34 ?  153 LEU   B HD13 1 
ATOM   6435 H  HD21 . LEU   B 1 153 ? 38.913 -25.740 -6.957  1.00 15.96 ?  153 LEU   B HD21 1 
ATOM   6436 H  HD22 . LEU   B 1 153 ? 40.101 -26.769 -6.731  1.00 15.96 ?  153 LEU   B HD22 1 
ATOM   6437 H  HD23 . LEU   B 1 153 ? 40.373 -25.393 -7.476  1.00 15.96 ?  153 LEU   B HD23 1 
ATOM   6438 N  N    . ALA   B 1 154 ? 44.037 -27.152 -9.344  1.00 11.65 ?  154 ALA   B N    1 
ATOM   6439 C  CA   . ALA   B 1 154 ? 45.262 -27.918 -9.530  1.00 12.97 ?  154 ALA   B CA   1 
ATOM   6440 C  C    . ALA   B 1 154 ? 45.329 -28.995 -8.455  1.00 13.61 ?  154 ALA   B C    1 
ATOM   6441 O  O    . ALA   B 1 154 ? 45.258 -28.694 -7.257  1.00 14.71 ?  154 ALA   B O    1 
ATOM   6442 C  CB   . ALA   B 1 154 ? 46.488 -27.009 -9.469  1.00 13.81 ?  154 ALA   B CB   1 
ATOM   6443 H  H    . ALA   B 1 154 ? 44.058 -26.624 -8.663  1.00 14.12 ?  154 ALA   B H    1 
ATOM   6444 H  HA   . ALA   B 1 154 ? 45.246 -28.347 -10.395 1.00 15.71 ?  154 ALA   B HA   1 
ATOM   6445 H  HB1  . ALA   B 1 154 ? 47.288 -27.544 -9.595  1.00 16.72 ?  154 ALA   B HB1  1 
ATOM   6446 H  HB2  . ALA   B 1 154 ? 46.426 -26.341 -10.173 1.00 16.72 ?  154 ALA   B HB2  1 
ATOM   6447 H  HB3  . ALA   B 1 154 ? 46.519 -26.568 -8.603  1.00 16.72 ?  154 ALA   B HB3  1 
ATOM   6448 N  N    . VAL   B 1 155 ? 45.448 -30.243 -8.886  1.00 12.89 ?  155 VAL   B N    1 
ATOM   6449 C  CA   . VAL   B 1 155 ? 45.556 -31.388 -7.992  1.00 12.90 ?  155 VAL   B CA   1 
ATOM   6450 C  C    . VAL   B 1 155 ? 46.897 -32.057 -8.273  1.00 12.76 ?  155 VAL   B C    1 
ATOM   6451 O  O    . VAL   B 1 155 ? 47.131 -32.550 -9.384  1.00 14.84 ?  155 VAL   B O    1 
ATOM   6452 C  CB   . VAL   B 1 155 ? 44.397 -32.381 -8.188  1.00 14.24 ?  155 VAL   B CB   1 
ATOM   6453 C  CG1  . VAL   B 1 155 ? 44.577 -33.579 -7.272  1.00 14.31 ?  155 VAL   B CG1  1 
ATOM   6454 C  CG2  . VAL   B 1 155 ? 43.051 -31.692 -7.944  1.00 14.96 ?  155 VAL   B CG2  1 
ATOM   6455 H  H    . VAL   B 1 155 ? 45.482 -30.460 -9.720  1.00 15.60 ?  155 VAL   B H    1 
ATOM   6456 H  HA   . VAL   B 1 155 ? 45.549 -31.086 -7.071  1.00 15.62 ?  155 VAL   B HA   1 
ATOM   6457 H  HB   . VAL   B 1 155 ? 44.406 -32.697 -9.105  1.00 17.23 ?  155 VAL   B HB   1 
ATOM   6458 H  HG11 . VAL   B 1 155 ? 43.749 -34.085 -7.243  1.00 17.31 ?  155 VAL   B HG11 1 
ATOM   6459 H  HG12 . VAL   B 1 155 ? 45.291 -34.143 -7.616  1.00 17.31 ?  155 VAL   B HG12 1 
ATOM   6460 H  HG13 . VAL   B 1 155 ? 44.803 -33.270 -6.380  1.00 17.31 ?  155 VAL   B HG13 1 
ATOM   6461 H  HG21 . VAL   B 1 155 ? 42.340 -32.349 -8.034  1.00 18.09 ?  155 VAL   B HG21 1 
ATOM   6462 H  HG22 . VAL   B 1 155 ? 43.042 -31.320 -7.048  1.00 18.09 ?  155 VAL   B HG22 1 
ATOM   6463 H  HG23 . VAL   B 1 155 ? 42.929 -30.986 -8.598  1.00 18.09 ?  155 VAL   B HG23 1 
ATOM   6464 N  N    . PHE   B 1 156 ? 47.760 -32.103 -7.258  1.00 13.39 ?  156 PHE   B N    1 
ATOM   6465 C  CA   . PHE   B 1 156 ? 49.138 -32.558 -7.460  1.00 14.59 ?  156 PHE   B CA   1 
ATOM   6466 C  C    . PHE   B 1 156 ? 49.235 -34.058 -7.745  1.00 15.63 ?  156 PHE   B C    1 
ATOM   6467 O  O    . PHE   B 1 156 ? 49.960 -34.484 -8.655  1.00 17.51 ?  156 PHE   B O    1 
ATOM   6468 C  CB   . PHE   B 1 156 ? 49.970 -32.188 -6.234  1.00 14.74 ?  156 PHE   B CB   1 
ATOM   6469 C  CG   . PHE   B 1 156 ? 51.391 -32.653 -6.293  1.00 15.29 ?  156 PHE   B CG   1 
ATOM   6470 C  CD1  . PHE   B 1 156 ? 52.275 -32.112 -7.207  1.00 16.85 ?  156 PHE   B CD1  1 
ATOM   6471 C  CD2  . PHE   B 1 156 ? 51.847 -33.612 -5.414  1.00 15.65 ?  156 PHE   B CD2  1 
ATOM   6472 C  CE1  . PHE   B 1 156 ? 53.591 -32.523 -7.252  1.00 17.56 ?  156 PHE   B CE1  1 
ATOM   6473 C  CE2  . PHE   B 1 156 ? 53.165 -34.030 -5.455  1.00 17.05 ?  156 PHE   B CE2  1 
ATOM   6474 C  CZ   . PHE   B 1 156 ? 54.029 -33.486 -6.379  1.00 17.43 ?  156 PHE   B CZ   1 
ATOM   6475 H  H    . PHE   B 1 156 ? 47.572 -31.885 -6.448  1.00 16.21 ?  156 PHE   B H    1 
ATOM   6476 H  HA   . PHE   B 1 156 ? 49.506 -32.087 -8.219  1.00 17.65 ?  156 PHE   B HA   1 
ATOM   6477 H  HB2  . PHE   B 1 156 ? 49.979 -31.221 -6.148  1.00 17.82 ?  156 PHE   B HB2  1 
ATOM   6478 H  HB3  . PHE   B 1 156 ? 49.561 -32.582 -5.447  1.00 17.82 ?  156 PHE   B HB3  1 
ATOM   6479 H  HD1  . PHE   B 1 156 ? 51.978 -31.456 -7.799  1.00 20.36 ?  156 PHE   B HD1  1 
ATOM   6480 H  HD2  . PHE   B 1 156 ? 51.259 -33.984 -4.794  1.00 18.92 ?  156 PHE   B HD2  1 
ATOM   6481 H  HE1  . PHE   B 1 156 ? 54.175 -32.153 -7.875  1.00 21.21 ?  156 PHE   B HE1  1 
ATOM   6482 H  HE2  . PHE   B 1 156 ? 53.460 -34.688 -4.864  1.00 20.60 ?  156 PHE   B HE2  1 
ATOM   6483 H  HZ   . PHE   B 1 156 ? 54.915 -33.771 -6.406  1.00 21.06 ?  156 PHE   B HZ   1 
ATOM   6484 N  N    . ASP   B 1 157 ? 48.563 -34.877 -6.949  1.00 16.05 ?  157 ASP   B N    1 
ATOM   6485 C  CA   . ASP   B 1 157 ? 48.708 -36.325 -7.042  1.00 17.22 ?  157 ASP   B CA   1 
ATOM   6486 C  C    . ASP   B 1 157 ? 47.794 -36.872 -8.134  1.00 17.23 ?  157 ASP   B C    1 
ATOM   6487 O  O    . ASP   B 1 157 ? 46.569 -36.743 -8.045  1.00 16.50 ?  157 ASP   B O    1 
ATOM   6488 C  CB   . ASP   B 1 157 ? 48.347 -36.941 -5.695  1.00 18.73 ?  157 ASP   B CB   1 
ATOM   6489 C  CG   . ASP   B 1 157 ? 48.500 -38.450 -5.678  1.00 20.75 ?  157 ASP   B CG   1 
ATOM   6490 O  OD1  . ASP   B 1 157 ? 48.823 -39.056 -6.729  1.00 21.21 ?  157 ASP   B OD1  1 
ATOM   6491 O  OD2  . ASP   B 1 157 ? 48.308 -39.030 -4.592  1.00 22.72 -1 157 ASP   B OD2  1 
ATOM   6492 H  H    . ASP   B 1 157 ? 48.016 -34.622 -6.346  1.00 19.40 ?  157 ASP   B H    1 
ATOM   6493 H  HA   . ASP   B 1 157 ? 49.628 -36.559 -7.253  1.00 20.81 ?  157 ASP   B HA   1 
ATOM   6494 H  HB2  . ASP   B 1 157 ? 48.915 -36.558 -5.011  1.00 22.62 ?  157 ASP   B HB2  1 
ATOM   6495 H  HB3  . ASP   B 1 157 ? 47.414 -36.733 -5.498  1.00 22.62 ?  157 ASP   B HB3  1 
ATOM   6496 N  N    A LYS   B 1 158 ? 48.392 -37.490 -9.159  0.74 18.09 ?  158 LYS   B N    1 
ATOM   6497 N  N    B LYS   B 1 158 ? 48.392 -37.513 -9.143  0.26 17.67 ?  158 LYS   B N    1 
ATOM   6498 C  CA   A LYS   B 1 158 ? 47.617 -38.103 -10.240 0.74 19.11 ?  158 LYS   B CA   1 
ATOM   6499 C  CA   B LYS   B 1 158 ? 47.616 -38.096 -10.236 0.26 18.38 ?  158 LYS   B CA   1 
ATOM   6500 C  C    A LYS   B 1 158 ? 46.553 -39.062 -9.708  0.74 18.91 ?  158 LYS   B C    1 
ATOM   6501 C  C    B LYS   B 1 158 ? 46.560 -39.069 -9.718  0.26 18.34 ?  158 LYS   B C    1 
ATOM   6502 O  O    A LYS   B 1 158 ? 45.445 -39.142 -10.254 0.74 19.21 ?  158 LYS   B O    1 
ATOM   6503 O  O    B LYS   B 1 158 ? 45.460 -39.156 -10.276 0.26 18.15 ?  158 LYS   B O    1 
ATOM   6504 C  CB   A LYS   B 1 158 ? 48.566 -38.831 -11.202 0.74 20.89 ?  158 LYS   B CB   1 
ATOM   6505 C  CB   B LYS   B 1 158 ? 48.564 -38.789 -11.221 0.26 19.55 ?  158 LYS   B CB   1 
ATOM   6506 C  CG   A LYS   B 1 158 ? 47.890 -39.751 -12.211 0.74 23.02 ?  158 LYS   B CG   1 
ATOM   6507 C  CG   B LYS   B 1 158 ? 47.892 -39.679 -12.261 0.26 20.97 ?  158 LYS   B CG   1 
ATOM   6508 C  CD   A LYS   B 1 158 ? 47.030 -38.984 -13.192 0.74 24.97 ?  158 LYS   B CD   1 
ATOM   6509 C  CD   B LYS   B 1 158 ? 47.005 -38.888 -13.204 0.26 22.39 ?  158 LYS   B CD   1 
ATOM   6510 C  CE   A LYS   B 1 158 ? 46.434 -39.913 -14.235 0.74 26.49 ?  158 LYS   B CE   1 
ATOM   6511 C  CE   B LYS   B 1 158 ? 46.435 -39.783 -14.294 0.26 23.50 ?  158 LYS   B CE   1 
ATOM   6512 N  NZ   A LYS   B 1 158 ? 45.359 -39.247 -15.023 0.74 26.80 ?  158 LYS   B NZ   1 
ATOM   6513 N  NZ   B LYS   B 1 158 ? 45.400 -39.090 -15.110 0.26 23.96 ?  158 LYS   B NZ   1 
ATOM   6514 H  H    A LYS   B 1 158 ? 49.247 -37.571 -9.250  0.74 21.85 ?  158 LYS   B H    1 
ATOM   6515 H  H    B LYS   B 1 158 ? 49.243 -37.627 -9.215  0.26 21.35 ?  158 LYS   B H    1 
ATOM   6516 H  HA   A LYS   B 1 158 ? 47.171 -37.405 -10.743 0.74 23.08 ?  158 LYS   B HA   1 
ATOM   6517 H  HA   B LYS   B 1 158 ? 47.161 -37.386 -10.715 0.26 22.20 ?  158 LYS   B HA   1 
ATOM   6518 H  HB2  A LYS   B 1 158 ? 49.066 -38.167 -11.709 0.74 25.21 ?  158 LYS   B HB2  1 
ATOM   6519 H  HB2  B LYS   B 1 158 ? 49.060 -38.107 -11.705 0.26 23.60 ?  158 LYS   B HB2  1 
ATOM   6520 H  HB3  A LYS   B 1 158 ? 49.184 -39.370 -10.684 0.74 25.21 ?  158 LYS   B HB3  1 
ATOM   6521 H  HB3  B LYS   B 1 158 ? 49.182 -39.343 -10.721 0.26 23.60 ?  158 LYS   B HB3  1 
ATOM   6522 H  HG2  A LYS   B 1 158 ? 48.575 -40.214 -12.719 0.74 27.77 ?  158 LYS   B HG2  1 
ATOM   6523 H  HG2  B LYS   B 1 158 ? 48.579 -40.112 -12.792 0.26 25.30 ?  158 LYS   B HG2  1 
ATOM   6524 H  HG3  A LYS   B 1 158 ? 47.333 -40.400 -11.752 0.74 27.77 ?  158 LYS   B HG3  1 
ATOM   6525 H  HG3  B LYS   B 1 158 ? 47.349 -40.352 -11.820 0.26 25.30 ?  158 LYS   B HG3  1 
ATOM   6526 H  HD2  A LYS   B 1 158 ? 46.303 -38.552 -12.716 0.74 30.11 ?  158 LYS   B HD2  1 
ATOM   6527 H  HD2  B LYS   B 1 158 ? 46.268 -38.504 -12.706 0.26 27.01 ?  158 LYS   B HD2  1 
ATOM   6528 H  HD3  A LYS   B 1 158 ? 47.573 -38.322 -13.649 0.74 30.11 ?  158 LYS   B HD3  1 
ATOM   6529 H  HD3  B LYS   B 1 158 ? 47.529 -38.189 -13.626 0.26 27.01 ?  158 LYS   B HD3  1 
ATOM   6530 H  HE2  A LYS   B 1 158 ? 47.129 -40.191 -14.850 0.74 31.93 ?  158 LYS   B HE2  1 
ATOM   6531 H  HE2  B LYS   B 1 158 ? 47.152 -40.058 -14.887 0.26 28.34 ?  158 LYS   B HE2  1 
ATOM   6532 H  HE3  A LYS   B 1 158 ? 46.050 -40.687 -13.793 0.74 31.93 ?  158 LYS   B HE3  1 
ATOM   6533 H  HE3  B LYS   B 1 158 ? 46.026 -40.562 -13.884 0.26 28.34 ?  158 LYS   B HE3  1 
ATOM   6534 H  HZ1  A LYS   B 1 158 ? 45.026 -39.812 -15.625 0.74 32.30 ?  158 LYS   B HZ1  1 
ATOM   6535 H  HZ1  B LYS   B 1 158 ? 45.087 -39.640 -15.736 0.26 28.89 ?  158 LYS   B HZ1  1 
ATOM   6536 H  HZ2  A LYS   B 1 158 ? 44.703 -38.982 -14.481 0.74 32.30 ?  158 LYS   B HZ2  1 
ATOM   6537 H  HZ2  B LYS   B 1 158 ? 44.725 -38.832 -14.589 0.26 28.89 ?  158 LYS   B HZ2  1 
ATOM   6538 H  HZ3  A LYS   B 1 158 ? 45.688 -38.535 -15.445 0.74 32.30 ?  158 LYS   B HZ3  1 
ATOM   6539 H  HZ3  B LYS   B 1 158 ? 45.752 -38.374 -15.504 0.26 28.89 ?  158 LYS   B HZ3  1 
ATOM   6540 N  N    . ASN   B 1 159 ? 46.876 -39.817 -8.657  1.00 18.91 ?  159 ASN   B N    1 
ATOM   6541 C  CA   . ASN   B 1 159 ? 45.923 -40.801 -8.144  1.00 19.80 ?  159 ASN   B CA   1 
ATOM   6542 C  C    . ASN   B 1 159 ? 44.725 -40.131 -7.468  1.00 18.97 ?  159 ASN   B C    1 
ATOM   6543 O  O    . ASN   B 1 159 ? 43.589 -40.618 -7.576  1.00 19.52 ?  159 ASN   B O    1 
ATOM   6544 C  CB   . ASN   B 1 159 ? 46.634 -41.778 -7.210  1.00 21.34 ?  159 ASN   B CB   1 
ATOM   6545 C  CG   . ASN   B 1 159 ? 47.658 -42.623 -7.934  1.00 23.60 ?  159 ASN   B CG   1 
ATOM   6546 O  OD1  . ASN   B 1 159 ? 47.404 -43.119 -9.039  1.00 24.48 ?  159 ASN   B OD1  1 
ATOM   6547 N  ND2  . ASN   B 1 159 ? 48.825 -42.799 -7.316  1.00 24.26 ?  159 ASN   B ND2  1 
ATOM   6548 H  H    A ASN   B 1 159 ? 47.622 -39.773 -8.235  0.74 22.83 ?  159 ASN   B H    1 
ATOM   6549 H  H    B ASN   B 1 159 ? 47.620 -39.769 -8.232  0.26 22.83 ?  159 ASN   B H    1 
ATOM   6550 H  HA   . ASN   B 1 159 ? 45.586 -41.310 -8.896  1.00 23.90 ?  159 ASN   B HA   1 
ATOM   6551 H  HB2  . ASN   B 1 159 ? 47.092 -41.280 -6.516  1.00 25.75 ?  159 ASN   B HB2  1 
ATOM   6552 H  HB3  . ASN   B 1 159 ? 45.981 -42.375 -6.824  1.00 25.75 ?  159 ASN   B HB3  1 
ATOM   6553 H  HD21 . ASN   B 1 159 ? 49.446 -43.276 -7.685  1.00 29.25 ?  159 ASN   B HD21 1 
ATOM   6554 H  HD22 . ASN   B 1 159 ? 48.961 -42.457 -6.538  1.00 29.25 ?  159 ASN   B HD22 1 
ATOM   6555 N  N    . LEU   B 1 160 ? 44.943 -39.003 -6.782  1.00 17.90 ?  160 LEU   B N    1 
ATOM   6556 C  CA   . LEU   B 1 160 ? 43.811 -38.263 -6.238  1.00 17.08 ?  160 LEU   B CA   1 
ATOM   6557 C  C    . LEU   B 1 160 ? 43.020 -37.597 -7.352  1.00 16.52 ?  160 LEU   B C    1 
ATOM   6558 O  O    . LEU   B 1 160 ? 41.783 -37.595 -7.328  1.00 16.26 ?  160 LEU   B O    1 
ATOM   6559 C  CB   . LEU   B 1 160 ? 44.277 -37.232 -5.214  1.00 16.59 ?  160 LEU   B CB   1 
ATOM   6560 C  CG   . LEU   B 1 160 ? 43.149 -36.338 -4.687  1.00 16.36 ?  160 LEU   B CG   1 
ATOM   6561 C  CD1  . LEU   B 1 160 ? 42.035 -37.184 -4.077  1.00 17.18 ?  160 LEU   B CD1  1 
ATOM   6562 C  CD2  . LEU   B 1 160 ? 43.681 -35.346 -3.672  1.00 16.51 ?  160 LEU   B CD2  1 
ATOM   6563 H  H    . LEU   B 1 160 ? 45.718 -38.659 -6.622  1.00 21.63 ?  160 LEU   B H    1 
ATOM   6564 H  HA   . LEU   B 1 160 ? 43.225 -38.891 -5.791  1.00 20.64 ?  160 LEU   B HA   1 
ATOM   6565 H  HB2  . LEU   B 1 160 ? 44.669 -37.702 -4.458  1.00 20.05 ?  160 LEU   B HB2  1 
ATOM   6566 H  HB3  . LEU   B 1 160 ? 44.947 -36.663 -5.626  1.00 20.05 ?  160 LEU   B HB3  1 
ATOM   6567 H  HG   . LEU   B 1 160 ? 42.774 -35.838 -5.426  1.00 19.78 ?  160 LEU   B HG   1 
ATOM   6568 H  HD11 . LEU   B 1 160 ? 41.416 -36.602 -3.617  1.00 20.76 ?  160 LEU   B HD11 1 
ATOM   6569 H  HD12 . LEU   B 1 160 ? 41.573 -37.667 -4.783  1.00 20.76 ?  160 LEU   B HD12 1 
ATOM   6570 H  HD13 . LEU   B 1 160 ? 42.423 -37.817 -3.448  1.00 20.76 ?  160 LEU   B HD13 1 
ATOM   6571 H  HD21 . LEU   B 1 160 ? 42.950 -34.783 -3.379  1.00 19.96 ?  160 LEU   B HD21 1 
ATOM   6572 H  HD22 . LEU   B 1 160 ? 44.050 -35.834 -2.921  1.00 19.96 ?  160 LEU   B HD22 1 
ATOM   6573 H  HD23 . LEU   B 1 160 ? 44.369 -34.809 -4.092  1.00 19.96 ?  160 LEU   B HD23 1 
ATOM   6574 N  N    . TYR   B 1 161 ? 43.717 -37.028 -8.337  1.00 16.72 ?  161 TYR   B N    1 
ATOM   6575 C  CA   . TYR   B 1 161 ? 43.044 -36.461 -9.500  1.00 16.63 ?  161 TYR   B CA   1 
ATOM   6576 C  C    . TYR   B 1 161 ? 42.096 -37.481 -10.122 1.00 16.54 ?  161 TYR   B C    1 
ATOM   6577 O  O    . TYR   B 1 161 ? 40.926 -37.182 -10.386 1.00 16.58 ?  161 TYR   B O    1 
ATOM   6578 C  CB   . TYR   B 1 161 ? 44.086 -35.984 -10.519 1.00 17.23 ?  161 TYR   B CB   1 
ATOM   6579 C  CG   . TYR   B 1 161 ? 43.509 -35.516 -11.836 1.00 17.79 ?  161 TYR   B CG   1 
ATOM   6580 C  CD1  . TYR   B 1 161 ? 43.115 -34.195 -12.006 1.00 17.83 ?  161 TYR   B CD1  1 
ATOM   6581 C  CD2  . TYR   B 1 161 ? 43.340 -36.394 -12.902 1.00 18.32 ?  161 TYR   B CD2  1 
ATOM   6582 C  CE1  . TYR   B 1 161 ? 42.586 -33.758 -13.195 1.00 18.94 ?  161 TYR   B CE1  1 
ATOM   6583 C  CE2  . TYR   B 1 161 ? 42.802 -35.964 -14.097 1.00 19.35 ?  161 TYR   B CE2  1 
ATOM   6584 C  CZ   . TYR   B 1 161 ? 42.430 -34.643 -14.238 1.00 19.57 ?  161 TYR   B CZ   1 
ATOM   6585 O  OH   . TYR   B 1 161 ? 41.892 -34.205 -15.422 1.00 21.33 ?  161 TYR   B OH   1 
ATOM   6586 H  H    . TYR   B 1 161 ? 44.573 -36.969 -8.361  1.00 20.20 ?  161 TYR   B H    1 
ATOM   6587 H  HA   . TYR   B 1 161 ? 42.519 -35.697 -9.225  1.00 20.10 ?  161 TYR   B HA   1 
ATOM   6588 H  HB2  . TYR   B 1 161 ? 44.576 -35.238 -10.134 1.00 20.82 ?  161 TYR   B HB2  1 
ATOM   6589 H  HB3  . TYR   B 1 161 ? 44.696 -36.711 -10.710 1.00 20.82 ?  161 TYR   B HB3  1 
ATOM   6590 H  HD1  . TYR   B 1 161 ? 43.222 -33.587 -11.309 1.00 21.54 ?  161 TYR   B HD1  1 
ATOM   6591 H  HD2  . TYR   B 1 161 ? 43.587 -37.284 -12.812 1.00 22.12 ?  161 TYR   B HD2  1 
ATOM   6592 H  HE1  . TYR   B 1 161 ? 42.335 -32.863 -13.293 1.00 22.87 ?  161 TYR   B HE1  1 
ATOM   6593 H  HE2  . TYR   B 1 161 ? 42.694 -36.555 -14.806 1.00 23.36 ?  161 TYR   B HE2  1 
ATOM   6594 H  HH   . TYR   B 1 161 ? 41.856 -34.839 -15.973 1.00 25.74 ?  161 TYR   B HH   1 
ATOM   6595 N  N    . ASP   B 1 162 ? 42.587 -38.704 -10.342 1.00 16.77 ?  162 ASP   B N    1 
ATOM   6596 C  CA   . ASP   B 1 162 ? 41.758 -39.737 -10.958 1.00 17.39 ?  162 ASP   B CA   1 
ATOM   6597 C  C    . ASP   B 1 162 ? 40.554 -40.077 -10.089 1.00 16.81 ?  162 ASP   B C    1 
ATOM   6598 O  O    . ASP   B 1 162 ? 39.449 -40.289 -10.602 1.00 17.35 ?  162 ASP   B O    1 
ATOM   6599 C  CB   . ASP   B 1 162 ? 42.585 -41.001 -11.216 1.00 18.82 ?  162 ASP   B CB   1 
ATOM   6600 C  CG   . ASP   B 1 162 ? 43.595 -40.836 -12.335 1.00 20.34 ?  162 ASP   B CG   1 
ATOM   6601 O  OD1  . ASP   B 1 162 ? 43.471 -39.896 -13.142 1.00 20.64 ?  162 ASP   B OD1  1 
ATOM   6602 O  OD2  . ASP   B 1 162 ? 44.505 -41.686 -12.427 1.00 22.02 -1 162 ASP   B OD2  1 
ATOM   6603 H  H    . ASP   B 1 162 ? 43.384 -38.956 -10.146 1.00 20.27 ?  162 ASP   B H    1 
ATOM   6604 H  HA   . ASP   B 1 162 ? 41.431 -39.416 -11.809 1.00 21.01 ?  162 ASP   B HA   1 
ATOM   6605 H  HB2  . ASP   B 1 162 ? 43.078 -41.231 -10.416 1.00 22.73 ?  162 ASP   B HB2  1 
ATOM   6606 H  HB3  . ASP   B 1 162 ? 41.989 -41.725 -11.461 1.00 22.73 ?  162 ASP   B HB3  1 
ATOM   6607 N  N    A LYS   B 1 163 ? 40.750 -40.154 -8.770  0.74 16.11 ?  163 LYS   B N    1 
ATOM   6608 N  N    B LYS   B 1 163 ? 40.745 -40.137 -8.768  0.26 17.14 ?  163 LYS   B N    1 
ATOM   6609 C  CA   A LYS   B 1 163 ? 39.625 -40.424 -7.881  0.74 16.77 ?  163 LYS   B CA   1 
ATOM   6610 C  CA   B LYS   B 1 163 ? 39.623 -40.422 -7.879  0.26 17.90 ?  163 LYS   B CA   1 
ATOM   6611 C  C    A LYS   B 1 163 ? 38.585 -39.310 -7.952  0.74 15.65 ?  163 LYS   B C    1 
ATOM   6612 C  C    B LYS   B 1 163 ? 38.586 -39.306 -7.921  0.26 16.18 ?  163 LYS   B C    1 
ATOM   6613 O  O    A LYS   B 1 163 ? 37.374 -39.577 -7.965  0.74 16.35 ?  163 LYS   B O    1 
ATOM   6614 O  O    B LYS   B 1 163 ? 37.377 -39.569 -7.878  0.26 16.30 ?  163 LYS   B O    1 
ATOM   6615 C  CB   A LYS   B 1 163 ? 40.110 -40.604 -6.444  0.74 19.48 ?  163 LYS   B CB   1 
ATOM   6616 C  CB   B LYS   B 1 163 ? 40.123 -40.626 -6.450  0.26 20.62 ?  163 LYS   B CB   1 
ATOM   6617 C  CG   A LYS   B 1 163 ? 39.037 -41.162 -5.529  0.74 24.07 ?  163 LYS   B CG   1 
ATOM   6618 C  CG   B LYS   B 1 163 ? 39.048 -41.117 -5.501  0.26 23.58 ?  163 LYS   B CG   1 
ATOM   6619 C  CD   A LYS   B 1 163 ? 39.457 -41.185 -4.072  0.74 28.25 ?  163 LYS   B CD   1 
ATOM   6620 C  CD   B LYS   B 1 163 ? 39.566 -41.285 -4.085  0.26 26.47 ?  163 LYS   B CD   1 
ATOM   6621 C  CE   A LYS   B 1 163 ? 38.385 -41.861 -3.229  0.74 31.03 ?  163 LYS   B CE   1 
ATOM   6622 C  CE   B LYS   B 1 163 ? 38.510 -41.939 -3.209  0.26 28.73 ?  163 LYS   B CE   1 
ATOM   6623 N  NZ   A LYS   B 1 163 ? 38.491 -41.520 -1.784  0.74 32.75 ?  163 LYS   B NZ   1 
ATOM   6624 N  NZ   B LYS   B 1 163 ? 38.717 -41.659 -1.763  0.26 29.61 ?  163 LYS   B NZ   1 
ATOM   6625 H  H    A LYS   B 1 163 ? 41.509 -40.054 -8.377  0.74 19.48 ?  163 LYS   B H    1 
ATOM   6626 H  H    B LYS   B 1 163 ? 41.500 -40.022 -8.372  0.26 20.71 ?  163 LYS   B H    1 
ATOM   6627 H  HA   A LYS   B 1 163 ? 39.199 -41.247 -8.159  0.74 20.27 ?  163 LYS   B HA   1 
ATOM   6628 H  HA   B LYS   B 1 163 ? 39.193 -41.242 -8.165  0.26 21.61 ?  163 LYS   B HA   1 
ATOM   6629 H  HB2  A LYS   B 1 163 ? 40.859 -41.221 -6.439  0.74 23.51 ?  163 LYS   B HB2  1 
ATOM   6630 H  HB2  B LYS   B 1 163 ? 40.836 -41.283 -6.456  0.26 24.88 ?  163 LYS   B HB2  1 
ATOM   6631 H  HB3  A LYS   B 1 163 ? 40.385 -39.744 -6.091  0.74 23.51 ?  163 LYS   B HB3  1 
ATOM   6632 H  HB3  B LYS   B 1 163 ? 40.456 -39.781 -6.109  0.26 24.88 ?  163 LYS   B HB3  1 
ATOM   6633 H  HG2  A LYS   B 1 163 ? 38.239 -40.617 -5.601  0.74 29.02 ?  163 LYS   B HG2  1 
ATOM   6634 H  HG2  B LYS   B 1 163 ? 38.322 -40.474 -5.480  0.26 28.44 ?  163 LYS   B HG2  1 
ATOM   6635 H  HG3  A LYS   B 1 163 ? 38.837 -42.076 -5.796  0.74 29.02 ?  163 LYS   B HG3  1 
ATOM   6636 H  HG3  B LYS   B 1 163 ? 38.723 -41.978 -5.807  0.26 28.44 ?  163 LYS   B HG3  1 
ATOM   6637 H  HD2  A LYS   B 1 163 ? 40.283 -41.688 -3.979  0.74 34.04 ?  163 LYS   B HD2  1 
ATOM   6638 H  HD2  B LYS   B 1 163 ? 40.354 -41.852 -4.093  0.26 31.90 ?  163 LYS   B HD2  1 
ATOM   6639 H  HD3  A LYS   B 1 163 ? 39.575 -40.277 -3.754  0.74 34.04 ?  163 LYS   B HD3  1 
ATOM   6640 H  HD3  B LYS   B 1 163 ? 39.779 -40.415 -3.712  0.26 31.90 ?  163 LYS   B HD3  1 
ATOM   6641 H  HE2  A LYS   B 1 163 ? 37.509 -41.588 -3.545  0.74 37.38 ?  163 LYS   B HE2  1 
ATOM   6642 H  HE2  B LYS   B 1 163 ? 37.636 -41.604 -3.462  0.26 34.62 ?  163 LYS   B HE2  1 
ATOM   6643 H  HE3  A LYS   B 1 163 ? 38.478 -42.822 -3.316  0.74 37.38 ?  163 LYS   B HE3  1 
ATOM   6644 H  HE3  B LYS   B 1 163 ? 38.546 -42.900 -3.338  0.26 34.62 ?  163 LYS   B HE3  1 
ATOM   6645 H  HZ1  A LYS   B 1 163 ? 37.847 -41.931 -1.328  0.74 39.44 ?  163 LYS   B HZ1  1 
ATOM   6646 H  HZ1  B LYS   B 1 163 ? 38.081 -42.056 -1.284  0.26 35.67 ?  163 LYS   B HZ1  1 
ATOM   6647 H  HZ2  A LYS   B 1 163 ? 39.281 -41.779 -1.469  0.74 39.44 ?  163 LYS   B HZ2  1 
ATOM   6648 H  HZ2  B LYS   B 1 163 ? 39.510 -41.967 -1.505  0.26 35.67 ?  163 LYS   B HZ2  1 
ATOM   6649 H  HZ3  A LYS   B 1 163 ? 38.408 -40.641 -1.673  0.74 39.44 ?  163 LYS   B HZ3  1 
ATOM   6650 H  HZ3  B LYS   B 1 163 ? 38.684 -40.782 -1.617  0.26 35.67 ?  163 LYS   B HZ3  1 
ATOM   6651 N  N    . LEU   B 1 164 ? 39.041 -38.054 -7.996  1.00 14.79 ?  164 LEU   B N    1 
ATOM   6652 C  CA   . LEU   B 1 164 ? 38.123 -36.920 -8.049  1.00 14.41 ?  164 LEU   B CA   1 
ATOM   6653 C  C    . LEU   B 1 164 ? 37.343 -36.901 -9.358  1.00 14.81 ?  164 LEU   B C    1 
ATOM   6654 O  O    . LEU   B 1 164 ? 36.119 -36.705 -9.362  1.00 15.89 ?  164 LEU   B O    1 
ATOM   6655 C  CB   . LEU   B 1 164 ? 38.917 -35.624 -7.882  1.00 13.85 ?  164 LEU   B CB   1 
ATOM   6656 C  CG   . LEU   B 1 164 ? 39.450 -35.338 -6.481  1.00 14.80 ?  164 LEU   B CG   1 
ATOM   6657 C  CD1  . LEU   B 1 164 ? 40.536 -34.277 -6.552  1.00 14.66 ?  164 LEU   B CD1  1 
ATOM   6658 C  CD2  . LEU   B 1 164 ? 38.342 -34.893 -5.547  1.00 16.68 ?  164 LEU   B CD2  1 
ATOM   6659 H  H    A LEU   B 1 164 ? 39.875 -37.835 -7.994  0.74 17.89 ?  164 LEU   B H    1 
ATOM   6660 H  H    B LEU   B 1 164 ? 39.875 -37.837 -8.018  0.26 17.89 ?  164 LEU   B H    1 
ATOM   6661 H  HA   . LEU   B 1 164 ? 37.491 -36.985 -7.324  1.00 17.44 ?  164 LEU   B HA   1 
ATOM   6662 H  HB2  . LEU   B 1 164 ? 39.683 -35.653 -8.480  1.00 16.75 ?  164 LEU   B HB2  1 
ATOM   6663 H  HB3  . LEU   B 1 164 ? 38.348 -34.881 -8.129  1.00 16.75 ?  164 LEU   B HB3  1 
ATOM   6664 H  HG   . LEU   B 1 164 ? 39.850 -36.142 -6.120  1.00 17.91 ?  164 LEU   B HG   1 
ATOM   6665 H  HD11 . LEU   B 1 164 ? 40.861 -34.089 -5.655  1.00 17.74 ?  164 LEU   B HD11 1 
ATOM   6666 H  HD12 . LEU   B 1 164 ? 41.269 -34.602 -7.102  1.00 17.74 ?  164 LEU   B HD12 1 
ATOM   6667 H  HD13 . LEU   B 1 164 ? 40.169 -33.467 -6.943  1.00 17.74 ?  164 LEU   B HD13 1 
ATOM   6668 H  HD21 . LEU   B 1 164 ? 38.720 -34.683 -4.679  1.00 20.16 ?  164 LEU   B HD21 1 
ATOM   6669 H  HD22 . LEU   B 1 164 ? 37.908 -34.108 -5.918  1.00 20.16 ?  164 LEU   B HD22 1 
ATOM   6670 H  HD23 . LEU   B 1 164 ? 37.697 -35.614 -5.460  1.00 20.16 ?  164 LEU   B HD23 1 
ATOM   6671 N  N    . VAL   B 1 165 ? 38.036 -37.077 -10.485 1.00 16.26 ?  165 VAL   B N    1 
ATOM   6672 C  CA   . VAL   B 1 165 ? 37.379 -37.015 -11.786 1.00 17.79 ?  165 VAL   B CA   1 
ATOM   6673 C  C    . VAL   B 1 165 ? 36.453 -38.212 -11.969 1.00 19.44 ?  165 VAL   B C    1 
ATOM   6674 O  O    . VAL   B 1 165 ? 35.289 -38.070 -12.365 1.00 20.74 ?  165 VAL   B O    1 
ATOM   6675 C  CB   . VAL   B 1 165 ? 38.425 -36.932 -12.913 1.00 18.64 ?  165 VAL   B CB   1 
ATOM   6676 C  CG1  . VAL   B 1 165 ? 37.760 -37.042 -14.265 1.00 19.59 ?  165 VAL   B CG1  1 
ATOM   6677 C  CG2  . VAL   B 1 165 ? 39.217 -35.641 -12.815 1.00 18.60 ?  165 VAL   B CG2  1 
ATOM   6678 H  H    . VAL   B 1 165 ? 38.886 -37.230 -10.523 1.00 19.66 ?  165 VAL   B H    1 
ATOM   6679 H  HA   . VAL   B 1 165 ? 36.842 -36.212 -11.830 1.00 21.49 ?  165 VAL   B HA   1 
ATOM   6680 H  HB   . VAL   B 1 165 ? 39.055 -37.665 -12.823 1.00 22.50 ?  165 VAL   B HB   1 
ATOM   6681 H  HG11 . VAL   B 1 165 ? 38.375 -36.734 -14.947 1.00 23.64 ?  165 VAL   B HG11 1 
ATOM   6682 H  HG12 . VAL   B 1 165 ? 37.532 -37.972 -14.425 1.00 23.64 ?  165 VAL   B HG12 1 
ATOM   6683 H  HG13 . VAL   B 1 165 ? 36.960 -36.498 -14.266 1.00 23.64 ?  165 VAL   B HG13 1 
ATOM   6684 H  HG21 . VAL   B 1 165 ? 39.857 -35.601 -13.545 1.00 22.46 ?  165 VAL   B HG21 1 
ATOM   6685 H  HG22 . VAL   B 1 165 ? 38.605 -34.888 -12.876 1.00 22.46 ?  165 VAL   B HG22 1 
ATOM   6686 H  HG23 . VAL   B 1 165 ? 39.686 -35.615 -11.966 1.00 22.46 ?  165 VAL   B HG23 1 
ATOM   6687 N  N    . SER   B 1 166 ? 36.965 -39.413 -11.682 1.00 20.30 ?  166 SER   B N    1 
ATOM   6688 C  CA   . SER   B 1 166 ? 36.208 -40.624 -11.965 1.00 21.28 ?  166 SER   B CA   1 
ATOM   6689 C  C    . SER   B 1 166 ? 34.950 -40.709 -11.116 1.00 21.49 ?  166 SER   B C    1 
ATOM   6690 O  O    . SER   B 1 166 ? 33.977 -41.327 -11.541 1.00 22.90 ?  166 SER   B O    1 
ATOM   6691 C  CB   . SER   B 1 166 ? 37.073 -41.880 -11.792 1.00 22.25 ?  166 SER   B CB   1 
ATOM   6692 O  OG   . SER   B 1 166 ? 37.443 -42.081 -10.438 1.00 22.44 ?  166 SER   B OG   1 
ATOM   6693 H  H    . SER   B 1 166 ? 37.739 -39.548 -11.329 1.00 24.50 ?  166 SER   B H    1 
ATOM   6694 H  HA   . SER   B 1 166 ? 35.929 -40.601 -12.894 1.00 25.68 ?  166 SER   B HA   1 
ATOM   6695 H  HB2  . SER   B 1 166 ? 36.568 -42.652 -12.093 1.00 26.84 ?  166 SER   B HB2  1 
ATOM   6696 H  HB3  . SER   B 1 166 ? 37.875 -41.785 -12.334 1.00 26.84 ?  166 SER   B HB3  1 
ATOM   6697 H  HG   . SER   B 1 166 ? 37.901 -41.425 -10.171 1.00 27.07 ?  166 SER   B HG   1 
ATOM   6698 N  N    . SER   B 1 167 ? 34.934 -40.099 -9.934  1.00 19.88 ?  167 SER   B N    1 
ATOM   6699 C  CA   . SER   B 1 167 ? 33.780 -40.160 -9.044  1.00 19.43 ?  167 SER   B CA   1 
ATOM   6700 C  C    . SER   B 1 167 ? 32.860 -38.943 -9.142  1.00 19.03 ?  167 SER   B C    1 
ATOM   6701 O  O    . SER   B 1 167 ? 31.782 -38.949 -8.537  1.00 19.59 ?  167 SER   B O    1 
ATOM   6702 C  CB   . SER   B 1 167 ? 34.232 -40.341 -7.589  1.00 19.62 ?  167 SER   B CB   1 
ATOM   6703 O  OG   . SER   B 1 167 ? 34.908 -39.183 -7.120  1.00 19.60 ?  167 SER   B OG   1 
ATOM   6704 H  H    . SER   B 1 167 ? 35.585 -39.640 -9.627  1.00 24.00 ?  167 SER   B H    1 
ATOM   6705 H  HA   . SER   B 1 167 ? 33.252 -40.939 -9.281  1.00 23.45 ?  167 SER   B HA   1 
ATOM   6706 H  HB2  . SER   B 1 167 ? 33.452 -40.503 -7.036  1.00 23.69 ?  167 SER   B HB2  1 
ATOM   6707 H  HB3  . SER   B 1 167 ? 34.829 -41.112 -7.542  1.00 23.69 ?  167 SER   B HB3  1 
ATOM   6708 H  HG   . SER   B 1 167 ? 35.593 -39.053 -7.591  1.00 23.66 ?  167 SER   B HG   1 
ATOM   6709 N  N    . PHE   B 1 168 ? 33.239 -37.905 -9.889  1.00 18.70 ?  168 PHE   B N    1 
ATOM   6710 C  CA   . PHE   B 1 168 ? 32.405 -36.704 -9.956  1.00 18.02 ?  168 PHE   B CA   1 
ATOM   6711 C  C    . PHE   B 1 168 ? 31.094 -36.966 -10.691 1.00 15.82 ?  168 PHE   B C    1 
ATOM   6712 O  O    . PHE   B 1 168 ? 30.052 -36.372 -10.351 1.00 16.73 ?  168 PHE   B O    1 
ATOM   6713 C  CB   . PHE   B 1 168 ? 33.167 -35.566 -10.629 1.00 18.66 ?  168 PHE   B CB   1 
ATOM   6714 C  CG   . PHE   B 1 168 ? 32.362 -34.312 -10.761 1.00 18.59 ?  168 PHE   B CG   1 
ATOM   6715 C  CD1  . PHE   B 1 168 ? 32.019 -33.579 -9.634  1.00 19.64 ?  168 PHE   B CD1  1 
ATOM   6716 C  CD2  . PHE   B 1 168 ? 31.925 -33.879 -11.995 1.00 18.15 ?  168 PHE   B CD2  1 
ATOM   6717 C  CE1  . PHE   B 1 168 ? 31.258 -32.431 -9.735  1.00 20.03 ?  168 PHE   B CE1  1 
ATOM   6718 C  CE2  . PHE   B 1 168 ? 31.180 -32.715 -12.110 1.00 19.03 ?  168 PHE   B CE2  1 
ATOM   6719 C  CZ   . PHE   B 1 168 ? 30.838 -31.992 -10.976 1.00 19.37 ?  168 PHE   B CZ   1 
ATOM   6720 H  H    . PHE   B 1 168 ? 33.960 -37.868 -10.354 1.00 22.58 ?  168 PHE   B H    1 
ATOM   6721 H  HA   . PHE   B 1 168 ? 32.178 -36.426 -9.059  1.00 21.76 ?  168 PHE   B HA   1 
ATOM   6722 H  HB2  . PHE   B 1 168 ? 33.951 -35.361 -10.099 1.00 22.53 ?  168 PHE   B HB2  1 
ATOM   6723 H  HB3  . PHE   B 1 168 ? 33.428 -35.842 -11.520 1.00 22.53 ?  168 PHE   B HB3  1 
ATOM   6724 H  HD1  . PHE   B 1 168 ? 32.295 -33.875 -8.796  1.00 23.71 ?  168 PHE   B HD1  1 
ATOM   6725 H  HD2  . PHE   B 1 168 ? 32.151 -34.352 -12.759 1.00 21.92 ?  168 PHE   B HD2  1 
ATOM   6726 H  HE1  . PHE   B 1 168 ? 31.036 -31.951 -8.971  1.00 24.18 ?  168 PHE   B HE1  1 
ATOM   6727 H  HE2  . PHE   B 1 168 ? 30.891 -32.426 -12.949 1.00 22.98 ?  168 PHE   B HE2  1 
ATOM   6728 H  HZ   . PHE   B 1 168 ? 30.328 -31.217 -11.054 1.00 23.38 ?  168 PHE   B HZ   1 
ATOM   6729 N  N    . LEU   B 1 169 ? 31.128 -37.846 -11.690 1.00 16.20 ?  169 LEU   B N    1 
ATOM   6730 C  CA   . LEU   B 1 169 ? 29.953 -38.158 -12.492 1.00 18.29 ?  169 LEU   B CA   1 
ATOM   6731 C  C    . LEU   B 1 169 ? 29.960 -39.601 -12.988 1.00 20.95 ?  169 LEU   B C    1 
ATOM   6732 O  O    . LEU   B 1 169 ? 29.076 -40.018 -13.737 1.00 23.43 ?  169 LEU   B O    1 
ATOM   6733 C  CB   . LEU   B 1 169 ? 29.875 -37.216 -13.692 1.00 19.88 ?  169 LEU   B CB   1 
ATOM   6734 C  CG   . LEU   B 1 169 ? 28.611 -36.364 -13.805 1.00 22.69 ?  169 LEU   B CG   1 
ATOM   6735 C  CD1  . LEU   B 1 169 ? 28.553 -35.724 -15.176 1.00 23.55 ?  169 LEU   B CD1  1 
ATOM   6736 C  CD2  . LEU   B 1 169 ? 27.358 -37.182 -13.538 1.00 22.80 ?  169 LEU   B CD2  1 
ATOM   6737 O  OXT  . LEU   B 1 169 ? 30.858 -40.373 -12.664 1.00 21.89 -1 169 LEU   B OXT  1 
ATOM   6738 H  H    . LEU   B 1 169 ? 31.833 -38.279 -11.936 1.00 19.58 ?  169 LEU   B H    1 
ATOM   6739 H  HA   . LEU   B 1 169 ? 29.167 -38.021 -11.945 1.00 22.09 ?  169 LEU   B HA   1 
ATOM   6740 H  HB2  . LEU   B 1 169 ? 30.626 -36.603 -13.656 1.00 24.00 ?  169 LEU   B HB2  1 
ATOM   6741 H  HB3  . LEU   B 1 169 ? 29.930 -37.743 -14.505 1.00 24.00 ?  169 LEU   B HB3  1 
ATOM   6742 H  HG   . LEU   B 1 169 ? 28.647 -35.650 -13.147 1.00 27.36 ?  169 LEU   B HG   1 
ATOM   6743 H  HD11 . LEU   B 1 169 ? 27.763 -35.162 -15.229 1.00 28.40 ?  169 LEU   B HD11 1 
ATOM   6744 H  HD12 . LEU   B 1 169 ? 29.350 -35.188 -15.305 1.00 28.40 ?  169 LEU   B HD12 1 
ATOM   6745 H  HD13 . LEU   B 1 169 ? 28.508 -36.423 -15.845 1.00 28.40 ?  169 LEU   B HD13 1 
ATOM   6746 H  HD21 . LEU   B 1 169 ? 26.602 -36.759 -13.970 1.00 27.50 ?  169 LEU   B HD21 1 
ATOM   6747 H  HD22 . LEU   B 1 169 ? 27.486 -38.077 -13.895 1.00 27.50 ?  169 LEU   B HD22 1 
ATOM   6748 H  HD23 . LEU   B 1 169 ? 27.212 -37.227 -12.581 1.00 27.50 ?  169 LEU   B HD23 1 
HETATM 6749 C  C1   T TFA   C 2 .   ? 12.108 -1.293  1.439   0.20 9.58  ?  201 TFA   A C1   1 
HETATM 6750 C  C2   T TFA   C 2 .   ? 12.743 -1.716  0.086   0.20 11.61 ?  201 TFA   A C2   1 
HETATM 6751 O  O    T TFA   C 2 .   ? 12.830 -1.556  2.409   0.20 8.23  ?  201 TFA   A O    1 
HETATM 6752 F  F1   T TFA   C 2 .   ? 12.826 -3.054  0.023   0.20 12.49 ?  201 TFA   A F1   1 
HETATM 6753 F  F2   T TFA   C 2 .   ? 12.043 -1.322  -0.990  0.20 11.99 ?  201 TFA   A F2   1 
HETATM 6754 F  F3   T TFA   C 2 .   ? 13.973 -1.233  -0.088  0.20 12.24 ?  201 TFA   A F3   1 
HETATM 6755 O  OXT  T TFA   C 2 .   ? 10.991 -0.766  1.373   0.20 9.88  ?  201 TFA   A OXT  1 
HETATM 6756 N  N2   B A1A8W D 3 .   ? 15.110 -0.465  3.833   0.26 13.38 ?  202 A1A8W A N2   1 
HETATM 6757 C  C3   B A1A8W D 3 .   ? 15.364 0.616   3.039   0.26 13.37 ?  202 A1A8W A C3   1 
HETATM 6758 C  C6   B A1A8W D 3 .   ? 15.526 1.922   3.587   0.26 12.58 ?  202 A1A8W A C6   1 
HETATM 6759 C  C9   B A1A8W D 3 .   ? 13.582 -0.528  0.279   0.26 16.19 ?  202 A1A8W A C9   1 
HETATM 6760 C  C12  B A1A8W D 3 .   ? 12.676 -1.753  0.212   0.26 16.94 ?  202 A1A8W A C12  1 
HETATM 6761 C  C1   B A1A8W D 3 .   ? 15.976 -1.166  -0.302  0.26 14.10 ?  202 A1A8W A C1   1 
HETATM 6762 C  C10  B A1A8W D 3 .   ? 12.646 0.181   1.295   0.26 16.92 ?  202 A1A8W A C10  1 
HETATM 6763 C  C11  B A1A8W D 3 .   ? 11.586 -0.934  1.056   0.26 17.14 ?  202 A1A8W A C11  1 
HETATM 6764 C  C2   B A1A8W D 3 .   ? 15.017 -0.794  0.866   0.26 14.57 ?  202 A1A8W A C2   1 
HETATM 6765 C  C4   B A1A8W D 3 .   ? 15.026 -0.257  5.195   0.26 13.18 ?  202 A1A8W A C4   1 
HETATM 6766 C  C5   B A1A8W D 3 .   ? 15.404 1.922   5.019   0.26 12.08 ?  202 A1A8W A C5   1 
HETATM 6767 C  C7   B A1A8W D 3 .   ? 15.792 3.302   3.232   0.26 12.29 ?  202 A1A8W A C7   1 
HETATM 6768 C  C8   B A1A8W D 3 .   ? 15.819 4.073   4.410   0.26 11.74 ?  202 A1A8W A C8   1 
HETATM 6769 N  N1   B A1A8W D 3 .   ? 15.456 0.396   1.602   0.26 14.14 ?  202 A1A8W A N1   1 
HETATM 6770 N  N3   B A1A8W D 3 .   ? 15.157 0.906   5.892   0.26 12.70 ?  202 A1A8W A N3   1 
HETATM 6771 N  N4   B A1A8W D 3 .   ? 15.594 3.246   5.514   0.26 11.29 ?  202 A1A8W A N4   1 
HETATM 6772 O  O1   B A1A8W D 3 .   ? 17.181 -1.703  0.265   0.26 13.49 ?  202 A1A8W A O1   1 
HETATM 6773 H  H10  B A1A8W D 3 .   ? 13.576 0.037   -0.701  0.26 19.57 ?  202 A1A8W A H10  1 
HETATM 6774 H  H15  B A1A8W D 3 .   ? 13.137 -2.629  0.674   0.26 20.46 ?  202 A1A8W A H15  1 
HETATM 6775 H  H16  B A1A8W D 3 .   ? 12.385 -2.033  -0.805  0.26 20.46 ?  202 A1A8W A H16  1 
HETATM 6776 H  H4   B A1A8W D 3 .   ? 15.507 -1.901  -1.008  0.26 17.07 ?  202 A1A8W A H4   1 
HETATM 6777 H  H3   B A1A8W D 3 .   ? 16.203 -0.259  -0.899  0.26 17.07 ?  202 A1A8W A H3   1 
HETATM 6778 H  H11  B A1A8W D 3 .   ? 12.345 1.193   1.026   0.26 20.45 ?  202 A1A8W A H11  1 
HETATM 6779 H  H12  B A1A8W D 3 .   ? 13.035 0.249   2.290   0.26 20.45 ?  202 A1A8W A H12  1 
HETATM 6780 H  H14  B A1A8W D 3 .   ? 11.201 -1.416  1.963   0.26 20.70 ?  202 A1A8W A H14  1 
HETATM 6781 H  H13  B A1A8W D 3 .   ? 10.710 -0.600  0.509   0.26 20.70 ?  202 A1A8W A H13  1 
HETATM 6782 H  H1   B A1A8W D 3 .   ? 14.937 -1.654  1.559   0.26 17.63 ?  202 A1A8W A H1   1 
HETATM 6783 H  H6   B A1A8W D 3 .   ? 14.815 -1.103  5.893   0.26 15.95 ?  202 A1A8W A H6   1 
HETATM 6784 H  H7   B A1A8W D 3 .   ? 15.954 3.756   2.274   0.26 14.89 ?  202 A1A8W A H7   1 
HETATM 6785 H  H8   B A1A8W D 3 .   ? 15.977 5.125   4.655   0.26 14.23 ?  202 A1A8W A H8   1 
HETATM 6786 H  H5   B A1A8W D 3 .   ? 15.859 1.125   1.043   0.26 17.10 ?  202 A1A8W A H5   1 
HETATM 6787 H  H9   B A1A8W D 3 .   ? 15.552 3.548   6.470   0.26 13.69 ?  202 A1A8W A H9   1 
HETATM 6788 H  H2   B A1A8W D 3 .   ? 17.674 -2.109  -0.453  0.26 16.33 ?  202 A1A8W A H2   1 
HETATM 6789 CL CL   B CL    E 4 .   ? 15.851 2.637   -1.033  0.26 12.36 ?  203 CL    A CL   1 
HETATM 6790 O  O    . HOH   F 5 .   ? 7.947  -12.582 -0.863  1.00 22.68 ?  301 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 14.760 -4.718  20.484  1.00 43.94 ?  302 HOH   A O    1 
HETATM 6792 O  O    B HOH   F 5 .   ? 5.342  4.042   0.416   0.26 30.24 ?  303 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 18.641 -2.415  -16.435 1.00 45.65 ?  304 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 8.879  -12.077 17.133  1.00 45.57 ?  305 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 34.308 -1.854  12.488  1.00 35.41 ?  306 HOH   A O    1 
HETATM 6796 O  O    A HOH   F 5 .   ? 4.692  3.908   0.583   0.74 22.14 ?  307 HOH   A O    1 
HETATM 6797 O  O    . HOH   F 5 .   ? 7.617  -6.322  -6.612  1.00 38.00 ?  308 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 0.646  -4.601  0.078   1.00 33.24 ?  309 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 17.139 -18.019 15.017  1.00 26.21 ?  310 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 11.996 0.347   14.744  1.00 33.87 ?  311 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 28.922 0.436   -9.755  1.00 21.35 ?  312 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 15.105 -12.246 18.623  1.00 38.29 ?  313 HOH   A O    1 
HETATM 6803 O  O    B HOH   F 5 .   ? 13.560 -1.026  -6.746  0.26 25.51 ?  314 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 16.188 16.639  8.646   1.00 30.82 ?  315 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 30.937 6.215   -12.317 1.00 27.15 ?  316 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 9.202  -10.091 19.333  1.00 40.13 ?  317 HOH   A O    1 
HETATM 6807 O  O    B HOH   F 5 .   ? 22.581 5.579   -1.820  0.26 16.89 ?  318 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 14.702 -13.940 16.689  1.00 25.34 ?  319 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 11.753 -10.843 -10.103 1.00 43.34 ?  320 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 30.237 -13.335 -8.521  1.00 21.57 ?  321 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 42.425 10.567  5.128   1.00 19.40 ?  322 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 14.444 -24.683 11.571  1.00 36.62 ?  323 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 14.106 -4.526  -11.894 1.00 31.60 ?  324 HOH   A O    1 
HETATM 6814 O  O    B HOH   F 5 .   ? 14.843 -3.026  3.423   0.26 16.17 ?  325 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 28.207 -6.300  19.582  1.00 41.60 ?  326 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 18.923 -21.978 6.955   1.00 32.04 ?  327 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 26.504 -19.336 -1.804  1.00 13.88 ?  328 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 34.004 -1.011  -8.917  1.00 26.70 ?  329 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 36.191 -5.117  -0.554  1.00 30.05 ?  330 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 22.698 12.500  1.622   1.00 14.51 ?  331 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 27.911 0.822   -7.164  1.00 13.64 ?  332 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 31.031 -18.118 7.790   1.00 19.42 ?  333 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 37.518 2.808   10.214  1.00 28.99 ?  334 HOH   A O    1 
HETATM 6824 O  O    A HOH   F 5 .   ? 14.636 -3.658  3.071   0.74 13.95 ?  335 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 18.695 -19.384 13.539  1.00 34.33 ?  336 HOH   A O    1 
HETATM 6826 O  O    A HOH   F 5 .   ? 6.949  -8.163  11.823  0.74 18.18 ?  337 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 38.265 10.122  7.141   1.00 38.50 ?  338 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 19.894 -12.550 -8.895  1.00 24.77 ?  339 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 21.262 -2.347  -2.297  1.00 15.08 ?  340 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 15.063 3.997   17.688  1.00 43.32 ?  341 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 20.633 -19.740 -5.063  1.00 26.14 ?  342 HOH   A O    1 
HETATM 6832 O  O    A HOH   F 5 .   ? 8.196  -21.403 3.973   0.74 37.43 ?  343 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 44.316 7.139   6.401   1.00 25.71 ?  344 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 22.310 5.355   19.000  1.00 41.79 ?  345 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 15.494 11.854  7.904   1.00 37.67 ?  346 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 3.563  -9.456  9.665   1.00 30.90 ?  347 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 28.361 -0.149  -13.404 1.00 34.41 ?  348 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 27.320 13.790  2.822   1.00 31.24 ?  349 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 13.546 -15.248 -7.494  1.00 25.37 ?  350 HOH   A O    1 
HETATM 6840 O  O    A HOH   F 5 .   ? 14.273 0.571   6.771   0.74 18.79 ?  351 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 26.833 11.417  1.637   1.00 15.89 ?  352 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 22.205 -19.263 11.366  1.00 34.75 ?  353 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 38.552 4.990   6.967   1.00 15.04 ?  354 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 9.894  -21.415 5.682   1.00 17.95 ?  355 HOH   A O    1 
HETATM 6845 O  O    A HOH   F 5 .   ? 13.310 -1.446  -6.552  0.74 15.33 ?  356 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 39.763 -1.040  -5.187  1.00 20.64 ?  357 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 42.545 4.274   5.367   1.00 29.78 ?  358 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 17.146 -17.819 -5.060  1.00 25.96 ?  359 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 35.789 -12.656 6.835   1.00 15.50 ?  360 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? -0.410 -2.919  3.057   1.00 38.03 ?  361 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 14.354 -21.221 -4.247  1.00 28.86 ?  362 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 30.797 3.089   8.267   1.00 11.75 ?  363 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 24.022 -2.111  -2.111  1.00 10.44 ?  364 HOH   A O    1 
HETATM 6854 O  O    A HOH   F 5 .   ? 17.496 -1.718  0.415   0.74 18.55 ?  365 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 31.678 8.243   14.825  1.00 23.70 ?  366 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 33.638 -7.155  4.310   1.00 16.39 ?  367 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 31.097 -13.944 -2.475  1.00 13.53 ?  368 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 25.705 -0.812  -7.385  1.00 15.21 ?  369 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 43.948 8.453   -3.073  1.00 25.99 ?  370 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 31.888 -9.332  -6.669  1.00 22.43 ?  371 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 37.323 12.008  4.940   1.00 30.61 ?  372 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 21.911 -21.919 8.439   1.00 27.66 ?  373 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 27.456 -10.603 14.054  1.00 17.35 ?  374 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? -0.664 -8.451  2.136   1.00 45.41 ?  375 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 28.559 -10.656 -14.051 1.00 40.09 ?  376 HOH   A O    1 
HETATM 6866 O  O    A HOH   F 5 .   ? 11.066 -0.386  1.904   0.54 22.90 ?  377 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 18.917 -0.727  -1.679  1.00 13.37 ?  378 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 43.358 7.825   2.670   1.00 25.60 ?  379 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 16.537 -22.075 0.970   1.00 27.74 ?  380 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 18.542 9.435   8.996   1.00 21.36 ?  381 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 27.427 -6.110  -14.000 1.00 35.55 ?  382 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 24.197 -7.765  14.424  1.00 16.92 ?  383 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 17.002 -19.281 4.884   1.00 14.88 ?  384 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 37.255 -2.825  9.725   1.00 40.18 ?  385 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 24.403 3.584   -1.829  1.00 14.10 ?  386 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 21.174 10.224  14.995  1.00 35.46 ?  387 HOH   A O    1 
HETATM 6877 O  O    T HOH   F 5 .   ? 15.407 -0.426  2.358   0.20 9.51  ?  388 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 11.668 -10.736 17.015  1.00 24.48 ?  389 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 31.812 -7.303  -9.862  1.00 21.32 ?  390 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 24.706 -17.522 12.711  1.00 23.66 ?  391 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 21.347 3.071   -0.321  1.00 12.81 ?  392 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 24.584 1.984   -7.068  1.00 20.03 ?  393 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 32.778 -9.255  5.951   1.00 19.88 ?  394 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 14.080 -23.050 7.417   1.00 17.66 ?  395 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 37.581 -2.018  5.823   1.00 26.08 ?  396 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 22.652 -11.907 21.810  1.00 45.21 ?  397 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 30.656 1.898   16.689  1.00 21.34 ?  398 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 15.214 -21.551 14.215  1.00 18.01 ?  399 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 13.933 -4.941  17.383  1.00 26.42 ?  400 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 15.161 -8.073  -9.785  1.00 22.40 ?  401 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 20.547 -20.015 2.770   1.00 18.13 ?  402 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 23.463 11.379  4.066   1.00 11.96 ?  403 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 10.943 1.738   12.568  1.00 25.44 ?  404 HOH   A O    1 
HETATM 6894 O  O    A HOH   F 5 .   ? 20.098 4.534   -7.576  0.74 17.88 ?  405 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 6.699  -3.300  12.783  1.00 28.91 ?  406 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 30.056 -10.084 12.990  1.00 21.65 ?  407 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 23.924 -15.721 -9.186  1.00 36.07 ?  408 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 27.297 2.344   18.712  1.00 32.20 ?  409 HOH   A O    1 
HETATM 6899 O  O    A HOH   F 5 .   ? 15.799 -0.948  5.242   0.74 18.27 ?  410 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 14.540 -0.537  -12.136 1.00 25.04 ?  411 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 26.934 4.158   -0.662  1.00 12.31 ?  412 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 38.083 -1.318  -1.943  1.00 18.66 ?  413 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 15.850 2.109   24.700  1.00 43.30 ?  414 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 23.937 -20.273 -1.348  1.00 16.10 ?  415 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 30.322 -12.908 13.510  1.00 20.01 ?  416 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 35.097 -5.222  -3.123  1.00 17.62 ?  417 HOH   A O    1 
HETATM 6907 O  O    A HOH   F 5 .   ? 24.091 3.954   -4.945  0.74 20.04 ?  418 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 40.923 -8.234  -6.859  1.00 35.66 ?  419 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 32.690 -4.291  -9.888  1.00 28.23 ?  420 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 21.742 -13.852 -8.186  1.00 43.89 ?  421 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 32.533 -10.656 3.194   1.00 30.83 ?  422 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 36.735 -4.944  5.371   1.00 24.18 ?  423 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 44.953 -0.574  2.996   1.00 41.07 ?  424 HOH   A O    1 
HETATM 6914 O  O    B HOH   F 5 .   ? 11.890 -1.755  -3.115  0.26 12.12 ?  425 HOH   A O    1 
HETATM 6915 O  O    A HOH   F 5 .   ? 6.466  -5.608  11.151  0.74 18.38 ?  426 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 10.388 -13.735 -1.693  1.00 16.53 ?  427 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 16.225 -14.172 20.135  1.00 53.16 ?  428 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 41.607 1.557   5.013   1.00 37.33 ?  429 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 5.335  2.780   5.051   1.00 30.17 ?  430 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 10.389 -22.225 -1.248  1.00 50.90 ?  431 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 15.974 6.888   2.975   1.00 17.79 ?  432 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 19.406 -11.074 24.030  1.00 67.73 ?  433 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 18.848 1.965   -0.701  1.00 12.76 ?  434 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 22.576 8.176   18.348  1.00 43.84 ?  435 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 23.510 -7.995  17.070  1.00 21.31 ?  436 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 37.757 -8.838  -3.492  1.00 23.80 ?  437 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 21.292 -9.236  21.317  1.00 47.68 ?  438 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? -1.371 -4.890  7.587   1.00 41.75 ?  439 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 27.079 -3.183  19.344  1.00 36.43 ?  440 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 20.577 -17.743 24.782  1.00 51.98 ?  441 HOH   A O    1 
HETATM 6931 O  O    A HOH   F 5 .   ? 16.257 2.941   -1.471  0.74 14.69 ?  442 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 23.346 -20.924 1.321   1.00 18.54 ?  443 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 34.415 -8.086  -0.541  1.00 28.73 ?  444 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 18.489 4.891   -15.133 1.00 47.49 ?  445 HOH   A O    1 
HETATM 6935 O  O    B HOH   F 5 .   ? 23.253 7.894   -3.240  0.26 22.03 ?  446 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 9.467  -16.325 -2.003  1.00 44.81 ?  447 HOH   A O    1 
HETATM 6937 O  O    A HOH   F 5 .   ? 14.027 -0.343  3.433   0.54 31.92 ?  448 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 18.391 -16.032 16.347  1.00 36.36 ?  449 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 30.588 14.779  2.747   1.00 18.72 ?  450 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 31.351 -12.799 0.004   1.00 19.31 ?  451 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 21.517 -14.742 17.930  1.00 51.05 ?  452 HOH   A O    1 
HETATM 6942 O  O    A HOH   F 5 .   ? 23.198 7.508   -3.267  0.74 28.83 ?  453 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 27.730 6.997   -6.505  1.00 35.21 ?  454 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 29.890 -16.061 10.728  1.00 34.90 ?  455 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 25.422 8.259   -4.859  1.00 27.51 ?  456 HOH   A O    1 
HETATM 6946 O  O    . HOH   F 5 .   ? 32.463 -15.889 10.849  1.00 31.94 ?  457 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 29.786 -1.986  -12.758 1.00 45.29 ?  458 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 24.799 5.596   20.704  1.00 52.39 ?  459 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 19.881 -17.346 -5.088  1.00 23.96 ?  460 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 23.193 -22.317 -3.359  1.00 36.01 ?  461 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 24.608 14.615  7.794   1.00 34.85 ?  462 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 26.886 11.618  -1.290  1.00 30.63 ?  463 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 15.714 -21.510 3.674   1.00 22.95 ?  464 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 23.472 13.722  5.488   1.00 18.27 ?  465 HOH   A O    1 
HETATM 6955 O  O    . HOH   F 5 .   ? 18.736 10.853  11.235  1.00 30.65 ?  466 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 39.625 -7.003  -3.499  1.00 45.82 ?  467 HOH   A O    1 
HETATM 6957 O  O    A HOH   F 5 .   ? 21.964 5.260   -5.866  0.74 28.74 ?  468 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 27.498 -11.409 16.544  1.00 36.14 ?  469 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 12.314 1.583   17.298  1.00 38.54 ?  470 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 25.844 10.782  -3.712  1.00 23.94 ?  471 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 11.029 -15.048 -6.101  1.00 33.42 ?  472 HOH   A O    1 
HETATM 6962 O  O    . HOH   F 5 .   ? 14.009 -10.337 -10.917 1.00 32.06 ?  473 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 11.979 -13.422 16.371  1.00 52.69 ?  474 HOH   A O    1 
HETATM 6964 O  O    . HOH   F 5 .   ? 18.106 -16.234 -8.861  1.00 40.42 ?  475 HOH   A O    1 
HETATM 6965 O  O    B HOH   F 5 .   ? 11.279 0.499   -2.080  0.26 19.14 ?  476 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 15.722 -17.128 -7.002  1.00 29.33 ?  477 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 35.160 7.462   12.234  1.00 43.86 ?  478 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 28.838 9.028   17.488  1.00 35.87 ?  479 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 20.531 -16.065 -7.375  1.00 28.73 ?  480 HOH   A O    1 
HETATM 6970 O  O    . HOH   F 5 .   ? 17.406 -18.740 19.830  1.00 50.02 ?  481 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 23.144 11.839  -4.063  1.00 18.93 ?  482 HOH   A O    1 
HETATM 6972 O  O    B HOH   F 5 .   ? 10.603 -1.501  -5.666  0.26 17.27 ?  483 HOH   A O    1 
HETATM 6973 O  O    . HOH   F 5 .   ? 16.827 -20.546 16.130  1.00 28.68 ?  484 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 41.023 -3.978  -0.374  1.00 35.33 ?  485 HOH   A O    1 
HETATM 6975 O  O    B HOH   F 5 .   ? 12.588 2.469   -0.702  0.26 17.32 ?  486 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 30.904 0.757   19.110  1.00 38.65 ?  487 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 44.496 10.443  -1.644  1.00 31.30 ?  488 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 28.566 -4.686  -12.305 1.00 36.36 ?  489 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 41.722 9.344   -4.035  1.00 29.46 ?  490 HOH   A O    1 
HETATM 6980 O  O    . HOH   F 5 .   ? 23.235 -12.862 19.303  1.00 44.04 ?  491 HOH   A O    1 
HETATM 6981 O  O    B HOH   F 5 .   ? 9.143  2.013   -2.451  0.26 18.85 ?  492 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 39.167 2.447   7.500   1.00 30.78 ?  493 HOH   A O    1 
HETATM 6983 O  O    . HOH   F 5 .   ? 15.972 -6.807  -11.874 1.00 42.50 ?  494 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 18.451 -23.196 1.923   1.00 41.62 ?  495 HOH   A O    1 
HETATM 6985 O  O    . HOH   F 5 .   ? 28.711 -7.955  -15.301 1.00 46.76 ?  496 HOH   A O    1 
HETATM 6986 O  O    . HOH   F 5 .   ? 31.471 -0.578  -10.594 1.00 28.71 ?  497 HOH   A O    1 
HETATM 6987 O  O    . HOH   F 5 .   ? 13.942 -25.283 8.915   1.00 32.41 ?  498 HOH   A O    1 
HETATM 6988 O  O    . HOH   F 5 .   ? 30.717 5.820   -14.756 1.00 34.92 ?  499 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 40.536 -0.250  -7.860  1.00 32.41 ?  500 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 20.043 -22.361 4.202   1.00 28.69 ?  501 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 16.188 -23.396 5.726   1.00 26.63 ?  502 HOH   A O    1 
HETATM 6992 O  O    . HOH   F 5 .   ? 30.729 -5.847  -11.869 1.00 45.29 ?  503 HOH   A O    1 
HETATM 6993 O  O    . HOH   F 5 .   ? 8.074  -3.111  -5.808  1.00 48.60 ?  504 HOH   A O    1 
HETATM 6994 O  O    . HOH   F 5 .   ? 37.402 -6.636  7.583   1.00 25.80 ?  505 HOH   A O    1 
HETATM 6995 O  O    . HOH   F 5 .   ? 23.221 -23.800 1.574   1.00 31.09 ?  506 HOH   A O    1 
HETATM 6996 O  O    B HOH   F 5 .   ? 5.902  6.822   1.319   0.26 29.07 ?  507 HOH   A O    1 
HETATM 6997 O  O    . HOH   F 5 .   ? 39.511 -0.004  6.583   1.00 30.27 ?  508 HOH   A O    1 
HETATM 6998 O  O    . HOH   F 5 .   ? 29.008 14.444  0.857   1.00 45.66 ?  509 HOH   A O    1 
HETATM 6999 O  O    . HOH   F 5 .   ? 38.041 13.937  6.693   1.00 44.38 ?  510 HOH   A O    1 
HETATM 7000 O  O    B HOH   F 5 .   ? 15.065 8.303   4.882   0.26 27.59 ?  511 HOH   A O    1 
HETATM 7001 O  O    B HOH   F 5 .   ? 9.863  1.137   -5.351  0.26 18.32 ?  512 HOH   A O    1 
HETATM 7002 O  O    . HOH   F 5 .   ? 22.031 -24.017 4.489   1.00 25.68 ?  513 HOH   A O    1 
HETATM 7003 O  O    . HOH   F 5 .   ? 36.476 -6.509  10.147  1.00 43.77 ?  514 HOH   A O    1 
HETATM 7004 O  O    T HOH   F 5 .   ? 11.923 -2.157  -3.682  0.20 7.95  ?  515 HOH   A O    1 
HETATM 7005 O  O    A HOH   F 5 .   ? 14.846 8.648   4.855   0.74 42.86 ?  516 HOH   A O    1 
HETATM 7006 O  O    . HOH   F 5 .   ? 17.355 -6.698  -14.273 1.00 41.31 ?  517 HOH   A O    1 
HETATM 7007 O  O    B HOH   F 5 .   ? 8.448  7.298   2.020   0.26 29.95 ?  518 HOH   A O    1 
HETATM 7008 O  O    . HOH   F 5 .   ? 24.080 9.003   -7.262  1.00 35.31 ?  519 HOH   A O    1 
HETATM 7009 O  O    . HOH   F 5 .   ? 16.356 -21.092 18.760  1.00 37.29 ?  520 HOH   A O    1 
HETATM 7010 O  O    . HOH   F 5 .   ? 15.872 -12.253 27.394  1.00 42.60 ?  521 HOH   A O    1 
HETATM 7011 O  O    . HOH   F 5 .   ? 14.706 -22.735 19.833  1.00 34.60 ?  522 HOH   A O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 29.855 -22.430 5.508   1.00 20.30 ?  201 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 41.750 -35.972 -17.165 1.00 31.45 ?  202 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 49.403 -22.681 -19.755 1.00 48.25 ?  203 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 27.740 -29.194 -1.846  1.00 35.78 ?  204 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 59.184 -18.714 6.828   1.00 35.74 ?  205 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 48.122 -6.906  15.539  1.00 31.72 ?  206 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 52.975 -13.474 -20.330 1.00 34.59 ?  207 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 41.419 -7.762  5.451   1.00 39.52 ?  208 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 38.037 -39.455 -0.169  1.00 39.17 ?  209 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 27.905 -41.873 -15.160 1.00 35.92 ?  210 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 30.227 -41.026 -8.113  1.00 16.76 ?  211 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 47.440 -7.397  -3.931  1.00 38.99 ?  212 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 54.539 -9.374  -8.760  1.00 19.12 ?  213 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 57.757 -24.489 5.041   1.00 36.77 ?  214 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 58.239 -12.956 8.391   1.00 31.48 ?  215 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 56.402 -19.728 7.255   1.00 31.27 ?  216 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 29.943 -26.295 4.034   1.00 27.61 ?  217 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 50.241 -3.377  7.127   1.00 34.45 ?  218 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 57.201 -26.897 -7.680  1.00 38.75 ?  219 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 56.696 -30.768 -7.775  1.00 32.63 ?  220 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 44.428 -7.250  2.047   1.00 33.57 ?  221 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 30.942 -28.764 4.316   1.00 27.79 ?  222 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 55.427 -16.540 -14.350 1.00 33.03 ?  223 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 50.830 -6.105  0.126   1.00 25.96 ?  224 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 41.532 -39.204 -14.871 1.00 22.11 ?  225 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 34.923 -24.633 13.803  1.00 33.85 ?  226 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 51.729 -6.474  4.381   1.00 19.54 ?  227 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 57.450 -16.269 -12.219 1.00 18.39 ?  228 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 45.150 -34.980 6.842   1.00 40.79 ?  229 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 34.551 -36.393 -7.177  1.00 18.26 ?  230 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 37.099 -19.793 -18.137 1.00 38.87 ?  231 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 29.826 -34.167 -0.428  1.00 34.15 ?  232 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 48.585 -36.533 -15.483 1.00 41.94 ?  233 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 36.030 -43.327 -8.476  1.00 33.49 ?  234 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 35.123 -8.005  -3.038  1.00 17.49 ?  235 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 41.409 -9.615  13.046  1.00 22.10 ?  236 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 44.955 -43.576 -10.508 1.00 27.21 ?  237 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 39.337 -10.888 6.105   1.00 26.01 ?  238 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 50.763 -12.971 -0.493  1.00 11.83 ?  239 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 46.451 -1.555  13.214  1.00 26.88 ?  240 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 39.534 -11.128 0.330   1.00 16.46 ?  241 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 32.828 -43.808 -11.328 1.00 20.26 ?  242 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 40.636 -16.062 14.114  1.00 23.39 ?  243 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 25.430 -25.935 -1.300  1.00 32.57 ?  244 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 44.535 -27.772 -0.715  1.00 22.01 ?  245 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 42.663 -22.862 3.838   1.00 11.57 ?  246 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 51.603 -13.844 11.000  1.00 27.10 ?  247 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 43.096 -43.252 -8.205  1.00 28.74 ?  248 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 38.537 -11.040 -2.279  1.00 18.54 ?  249 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 42.600 -25.373 2.659   1.00 15.10 ?  250 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 34.285 -18.463 11.410  1.00 24.65 ?  251 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 31.793 -17.927 -14.479 1.00 30.65 ?  252 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 28.406 -19.706 -13.152 1.00 23.48 ?  253 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 40.348 -12.773 -11.527 1.00 15.06 ?  254 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 43.196 -32.401 -17.086 1.00 23.41 ?  255 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 57.667 -24.399 -3.819  1.00 21.39 ?  256 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 41.907 -23.524 9.272   1.00 17.69 ?  257 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 50.994 -39.993 -8.204  1.00 33.21 ?  258 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 38.949 -11.952 12.326  1.00 34.16 ?  259 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 30.572 -42.250 -10.618 1.00 29.10 ?  260 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 29.735 -25.230 -10.787 1.00 16.48 ?  261 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 33.536 -16.995 8.064   1.00 19.27 ?  262 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 30.881 -15.734 2.662   1.00 13.67 ?  263 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 58.245 -10.668 -4.078  1.00 19.63 ?  264 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 27.137 -31.842 -9.966  1.00 19.74 ?  265 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 34.951 -33.333 -19.188 1.00 31.87 ?  266 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 48.032 -24.557 -17.761 1.00 30.23 ?  267 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 48.034 -22.768 5.828   1.00 17.05 ?  268 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 28.493 -30.909 -14.708 1.00 29.28 ?  269 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 57.533 -9.231  1.423   1.00 19.21 ?  270 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 49.777 -0.476  10.177  1.00 30.01 ?  271 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 46.892 -29.563 9.792   1.00 30.42 ?  272 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 42.405 -9.917  9.317   1.00 20.02 ?  273 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 43.390 -15.804 -12.196 1.00 14.31 ?  274 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 56.169 -23.591 -14.770 1.00 26.93 ?  275 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 46.644 -31.277 -4.789  1.00 22.83 ?  276 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 49.347 -28.714 -6.889  1.00 15.30 ?  277 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 56.977 -8.638  8.415   1.00 18.93 ?  278 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 28.273 -34.363 -9.412  1.00 19.82 ?  279 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 27.974 -22.894 -7.983  1.00 16.94 ?  280 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 34.492 -12.765 2.607   1.00 24.02 ?  281 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 42.426 -34.714 3.782   1.00 25.25 ?  282 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 57.176 -12.080 12.319  1.00 35.87 ?  283 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 59.814 -15.295 8.126   1.00 31.37 ?  284 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 42.336 -9.990  -14.893 1.00 37.58 ?  285 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 48.442 -25.055 3.102   1.00 13.25 ?  286 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 27.598 -26.724 -15.637 1.00 32.17 ?  287 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 41.181 -5.511  11.495  1.00 42.23 ?  288 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 45.369 -33.393 -15.923 1.00 24.05 ?  289 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 42.875 -20.296 -20.754 1.00 35.96 ?  290 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 47.091 -34.002 -4.622  1.00 17.64 ?  291 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 36.844 -12.763 -1.504  1.00 25.98 ?  292 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 50.026 -24.643 5.805   1.00 33.12 ?  293 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 51.249 -37.608 -9.611  1.00 24.95 ?  294 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 33.520 -15.312 -13.944 1.00 20.63 ?  295 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 48.728 -20.021 5.940   1.00 13.65 ?  296 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 52.559 -10.400 12.994  1.00 21.18 ?  297 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 42.708 -12.326 -18.524 1.00 30.05 ?  298 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 44.658 -27.474 2.017   1.00 15.24 ?  299 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 40.271 -10.862 -9.543  1.00 16.79 ?  300 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 35.101 -33.566 4.551   1.00 29.33 ?  301 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 43.569 -15.381 18.180  1.00 28.81 ?  302 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 37.542 -18.099 13.108  1.00 31.55 ?  303 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 52.631 -35.664 -8.616  1.00 28.71 ?  304 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 45.935 -40.423 -3.612  1.00 28.38 ?  305 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 25.962 -21.490 -3.507  1.00 16.37 ?  306 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 44.070 -29.364 -4.667  1.00 22.42 ?  307 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 51.724 -5.971  -7.922  1.00 46.32 ?  308 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 53.503 -30.202 4.500   1.00 18.41 ?  309 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 52.538 -29.262 -13.052 1.00 24.85 ?  310 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 37.327 -35.664 7.246   1.00 33.22 ?  311 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 53.142 -16.084 -12.751 1.00 27.32 ?  312 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 37.885 -10.255 -10.770 1.00 16.90 ?  313 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 62.856 -20.181 -0.794  1.00 37.82 ?  314 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 37.151 -30.624 -20.985 1.00 31.29 ?  315 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 43.250 -21.405 10.692  1.00 15.84 ?  316 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 62.752 -13.573 4.744   1.00 26.06 ?  317 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 32.826 -34.591 -5.903  1.00 16.91 ?  318 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 45.725 -36.292 -16.070 1.00 35.27 ?  319 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 41.773 -8.056  1.376   1.00 23.42 ?  320 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 51.414 -33.002 -10.801 1.00 38.74 ?  321 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 38.365 -12.729 7.915   1.00 17.87 ?  322 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 26.364 -21.056 -6.237  1.00 16.41 ?  323 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 59.952 -17.217 -10.508 1.00 33.40 ?  324 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 48.131 -32.632 -16.636 1.00 42.40 ?  325 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 53.676 -12.561 -22.228 1.00 34.14 ?  326 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 44.647 -24.599 9.558   1.00 20.39 ?  327 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 44.172 -1.740  7.594   1.00 45.90 ?  328 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 38.413 -9.374  -13.306 1.00 26.75 ?  329 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 36.754 -12.402 4.278   1.00 17.86 ?  330 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 43.123 -34.630 0.121   1.00 20.06 ?  331 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 41.228 -24.487 15.818  1.00 43.28 ?  332 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 47.212 -24.495 8.179   1.00 27.07 ?  333 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 33.660 -31.187 11.060  1.00 33.94 ?  334 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 27.874 -14.776 -9.483  1.00 34.95 ?  335 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 57.615 -22.002 3.309   1.00 29.75 ?  336 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 48.618 -11.975 -14.037 1.00 26.22 ?  337 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 47.505 -27.446 2.013   1.00 14.67 ?  338 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 42.851 -43.504 -14.364 1.00 41.19 ?  339 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 37.017 -15.140 -16.527 1.00 39.91 ?  340 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 46.825 -19.892 12.292  1.00 30.40 ?  341 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 39.535 -23.591 -20.357 1.00 35.53 ?  342 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 28.897 -42.944 -12.360 1.00 36.49 ?  343 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 38.486 -12.234 -16.285 1.00 42.74 ?  344 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 37.058 -45.237 -9.697  1.00 36.74 ?  345 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 33.036 -14.689 1.054   1.00 19.09 ?  346 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 39.832 -44.300 -11.197 1.00 39.23 ?  347 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 34.551 -10.330 7.631   1.00 22.80 ?  348 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 44.211 -37.398 -17.782 1.00 32.06 ?  349 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 40.428 -43.504 -9.085  1.00 25.63 ?  350 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 33.736 -9.511  -8.876  1.00 31.98 ?  351 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 62.579 -20.123 -4.811  1.00 42.44 ?  352 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 27.784 -26.589 -0.548  1.00 29.37 ?  353 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 38.581 -22.326 15.037  1.00 39.18 ?  354 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 55.672 -8.257  10.782  1.00 24.99 ?  355 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 23.253 -23.669 6.804   1.00 35.15 ?  356 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 56.631 -7.301  3.074   1.00 26.44 ?  357 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 36.086 -8.559  -9.733  1.00 33.64 ?  358 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 34.104 -7.773  11.446  1.00 37.87 ?  359 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 43.224 -12.703 -21.222 1.00 40.83 ?  360 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 61.542 -19.917 1.692   1.00 35.69 ?  361 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 56.942 -21.585 -16.380 1.00 40.09 ?  362 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 27.177 -25.968 -11.370 1.00 33.38 ?  363 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 40.259 -8.807  9.877   1.00 36.10 ?  364 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 54.241 -5.763  2.968   1.00 35.14 ?  365 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 32.536 -23.643 14.074  1.00 38.15 ?  366 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 40.170 -11.374 -13.970 1.00 32.02 ?  367 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 36.174 -8.665  8.973   1.00 36.97 ?  368 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 58.984 -10.440 9.157   1.00 39.00 ?  369 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 48.398 -26.467 8.780   1.00 39.49 ?  370 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 41.822 -10.067 -17.459 1.00 56.40 ?  371 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 39.889 -7.018  7.834   1.00 38.28 ?  372 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 56.048 -7.819  -0.637  1.00 33.61 ?  373 HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 52.092 -12.897 13.334  1.00 30.76 ?  374 HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 63.051 -12.393 6.939   1.00 36.56 ?  375 HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 38.055 -10.590 10.059  1.00 29.10 ?  376 HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 41.870 -6.759  -4.903  1.00 45.53 ?  377 HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 42.676 -17.145 -23.157 1.00 43.64 ?  378 HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 36.566 -22.830 13.296  1.00 26.13 ?  379 HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 40.161 -7.642  3.188   1.00 35.05 ?  380 HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 44.068 -5.598  -3.544  1.00 41.90 ?  381 HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 39.673 -14.059 15.676  1.00 46.61 ?  382 HOH   B O    1 
HETATM 7194 O  O    . HOH   G 5 .   ? 52.875 -29.910 7.196   1.00 23.42 ?  383 HOH   B O    1 
HETATM 7195 O  O    . HOH   G 5 .   ? 60.520 -22.292 2.845   1.00 47.35 ?  384 HOH   B O    1 
HETATM 7196 O  O    . HOH   G 5 .   ? 25.826 -18.880 -11.894 1.00 36.95 ?  385 HOH   B O    1 
HETATM 7197 O  O    . HOH   G 5 .   ? 46.824 -5.343  2.869   1.00 38.66 ?  386 HOH   B O    1 
HETATM 7198 O  O    . HOH   G 5 .   ? 35.443 -33.733 7.357   1.00 40.09 ?  387 HOH   B O    1 
HETATM 7199 O  O    . HOH   G 5 .   ? 23.949 -20.903 -7.666  1.00 28.11 ?  388 HOH   B O    1 
HETATM 7200 O  O    . HOH   G 5 .   ? 40.958 -9.777  15.788  1.00 46.11 ?  389 HOH   B O    1 
HETATM 7201 O  O    . HOH   G 5 .   ? 35.300 -20.317 13.293  1.00 31.63 ?  390 HOH   B O    1 
HETATM 7202 O  O    . HOH   G 5 .   ? 40.732 -6.632  -0.866  1.00 24.83 ?  391 HOH   B O    1 
HETATM 7203 O  O    . HOH   G 5 .   ? 44.110 -31.728 -3.773  1.00 34.67 ?  392 HOH   B O    1 
HETATM 7204 O  O    . HOH   G 5 .   ? 27.951 -27.072 2.215   1.00 30.37 ?  393 HOH   B O    1 
HETATM 7205 O  O    . HOH   G 5 .   ? 26.651 -28.010 -13.426 1.00 34.68 ?  394 HOH   B O    1 
HETATM 7206 O  O    . HOH   G 5 .   ? 24.605 -20.593 -10.504 1.00 38.44 ?  395 HOH   B O    1 
HETATM 7207 O  O    . HOH   G 5 .   ? 50.665 -30.855 8.694   1.00 28.66 ?  396 HOH   B O    1 
HETATM 7208 O  O    . HOH   G 5 .   ? 26.863 -30.689 -12.657 1.00 28.57 ?  397 HOH   B O    1 
HETATM 7209 O  O    . HOH   G 5 .   ? 34.400 -33.490 9.655   1.00 34.50 ?  398 HOH   B O    1 
HETATM 7210 O  O    . HOH   G 5 .   ? 57.718 -6.520  -2.362  1.00 34.57 ?  399 HOH   B O    1 
HETATM 7211 O  O    . HOH   G 5 .   ? 45.752 -20.158 15.210  1.00 50.14 ?  400 HOH   B O    1 
HETATM 7212 O  O    . HOH   G 5 .   ? 40.908 -11.751 -22.316 1.00 40.45 ?  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   A VAL   A 3   ? 0.6659 0.6660 0.7156 0.0031  -0.0341 0.0756  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6624 0.6625 0.6841 -0.0009 -0.0228 0.0502  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6638 0.6639 0.7053 0.0019  -0.0328 0.0752  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6604 0.6607 0.6788 -0.0017 -0.0230 0.0519  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6507 0.6529 0.6804 -0.0037 -0.0333 0.0768  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6491 0.6512 0.6638 -0.0058 -0.0273 0.0633  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6533 0.6553 0.6938 -0.0023 -0.0356 0.0797  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6520 0.6535 0.6735 -0.0050 -0.0282 0.0636  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6724 0.6707 0.7120 0.0051  -0.0305 0.0733  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6671 0.6663 0.6833 0.0008  -0.0192 0.0439  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6752 0.6726 0.7118 0.0065  -0.0298 0.0727  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6692 0.6680 0.6833 0.0016  -0.0179 0.0412  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6748 0.6728 0.7123 0.0061  -0.0296 0.0729  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6691 0.6681 0.6835 0.0015  -0.0179 0.0414  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6325 0.6375 0.6327 -0.0112 -0.0302 0.0748  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5957 0.6063 0.5471 -0.0252 -0.0292 0.0822  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5448 0.5697 0.4969 -0.0397 -0.0199 0.0631  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5466 0.5715 0.4879 -0.0408 -0.0222 0.0669  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.6056 0.6088 0.5063 -0.0253 -0.0373 0.1072  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.6127 0.6096 0.4678 -0.0263 -0.0452 0.1305  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.6167 0.6093 0.4506 -0.0271 -0.0500 0.1402  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.6142 0.6100 0.4600 -0.0258 -0.0472 0.1403  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4888 0.5264 0.4543 -0.0545 -0.0085 0.0396  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4306 0.4815 0.4126 -0.0683 0.0051  0.0145  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3656 0.4248 0.3411 -0.0767 0.0208  -0.0008 5   SER   A C   
49   O  O   . SER   A 5   ? 0.3726 0.4346 0.3461 -0.0668 0.0230  -0.0085 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4384 0.4926 0.4467 -0.0726 0.0046  0.0057  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4427 0.4982 0.4648 -0.0754 0.0054  0.0007  5   SER   A OG  
57   N  N   A PHE   A 6   ? 0.3131 0.3893 0.2905 -0.1012 0.0339  0.0013  6   PHE   A N   
58   N  N   B PHE   A 6   ? 0.3396 0.3912 0.3064 -0.0714 0.0208  -0.0039 6   PHE   A N   
59   C  CA  A PHE   A 6   ? 0.2675 0.3523 0.2399 -0.1181 0.0416  0.0181  6   PHE   A CA  
60   C  CA  B PHE   A 6   ? 0.3142 0.3558 0.2685 -0.0647 0.0196  -0.0011 6   PHE   A CA  
61   C  C   A PHE   A 6   ? 0.2612 0.3514 0.2385 -0.1212 0.0524  0.0153  6   PHE   A C   
62   C  C   B PHE   A 6   ? 0.3052 0.3412 0.2569 -0.0590 0.0226  -0.0021 6   PHE   A C   
63   O  O   A PHE   A 6   ? 0.2667 0.3570 0.2598 -0.1214 0.0594  0.0223  6   PHE   A O   
64   O  O   B PHE   A 6   ? 0.3049 0.3404 0.2424 -0.0631 0.0211  0.0015  6   PHE   A O   
65   C  CB  A PHE   A 6   ? 0.2442 0.3210 0.2110 -0.1150 0.0311  0.0367  6   PHE   A CB  
66   C  CB  B PHE   A 6   ? 0.3008 0.3361 0.2477 -0.0606 0.0139  0.0024  6   PHE   A CB  
67   C  CG  A PHE   A 6   ? 0.2263 0.2969 0.1974 -0.1065 0.0168  0.0381  6   PHE   A CG  
68   C  CG  B PHE   A 6   ? 0.2883 0.3185 0.2311 -0.0572 0.0090  0.0052  6   PHE   A CG  
69   C  CD1 A PHE   A 6   ? 0.2189 0.2869 0.1957 -0.0971 0.0088  0.0357  6   PHE   A CD1 
70   C  CD1 B PHE   A 6   ? 0.2826 0.3107 0.2237 -0.0552 0.0061  0.0069  6   PHE   A CD1 
71   C  CD2 A PHE   A 6   ? 0.2330 0.2931 0.2123 -0.0884 0.0150  0.0369  6   PHE   A CD2 
72   C  CD2 B PHE   A 6   ? 0.2855 0.3118 0.2286 -0.0527 0.0087  0.0064  6   PHE   A CD2 
73   C  CE1 A PHE   A 6   ? 0.2146 0.2815 0.1985 -0.0944 0.0142  0.0380  6   PHE   A CE1 
74   C  CE1 B PHE   A 6   ? 0.2796 0.3062 0.2217 -0.0544 0.0065  0.0082  6   PHE   A CE1 
75   C  CE2 A PHE   A 6   ? 0.2285 0.2871 0.2187 -0.0843 0.0162  0.0313  6   PHE   A CE2 
76   C  CE2 B PHE   A 6   ? 0.2824 0.3071 0.2273 -0.0514 0.0085  0.0067  6   PHE   A CE2 
77   C  CZ  A PHE   A 6   ? 0.2211 0.2810 0.2093 -0.0895 0.0156  0.0322  6   PHE   A CZ  
78   C  CZ  B PHE   A 6   ? 0.2803 0.3051 0.2247 -0.0525 0.0067  0.0070  6   PHE   A CZ  
97   N  N   A SER   A 7   ? 0.2486 0.3428 0.2127 -0.1201 0.0552  0.0073  7   SER   A N   
98   N  N   B SER   A 7   ? 0.2964 0.3273 0.2606 -0.0485 0.0248  -0.0068 7   SER   A N   
99   C  CA  A SER   A 7   ? 0.2485 0.3376 0.2180 -0.1075 0.0501  -0.0100 7   SER   A CA  
100  C  CA  B SER   A 7   ? 0.2900 0.3148 0.2701 -0.0371 0.0231  -0.0111 7   SER   A CA  
101  C  C   A SER   A 7   ? 0.2337 0.3000 0.1879 -0.1023 0.0532  -0.0120 7   SER   A C   
102  C  C   B SER   A 7   ? 0.2775 0.2955 0.2521 -0.0322 0.0281  -0.0120 7   SER   A C   
103  O  O   A SER   A 7   ? 0.2462 0.2902 0.1853 -0.1123 0.0513  -0.0103 7   SER   A O   
104  O  O   B SER   A 7   ? 0.2795 0.2959 0.2489 -0.0311 0.0242  -0.0124 7   SER   A O   
105  C  CB  A SER   A 7   ? 0.2703 0.3657 0.2524 -0.0918 0.0466  -0.0125 7   SER   A CB  
106  C  CB  B SER   A 7   ? 0.2950 0.3211 0.2924 -0.0316 0.0181  -0.0105 7   SER   A CB  
107  O  OG  A SER   A 7   ? 0.2879 0.3818 0.2775 -0.0818 0.0420  -0.0141 7   SER   A OG  
108  O  OG  B SER   A 7   ? 0.2979 0.3240 0.3089 -0.0282 0.0132  -0.0068 7   SER   A OG  
119  N  N   A GLY   A 8   ? 0.2096 0.2713 0.1747 -0.0883 0.0474  -0.0228 8   GLY   A N   
120  N  N   B GLY   A 8   ? 0.2650 0.2782 0.2374 -0.0295 0.0355  -0.0127 8   GLY   A N   
121  C  CA  A GLY   A 8   ? 0.1916 0.2432 0.1842 -0.0687 0.0449  -0.0243 8   GLY   A CA  
122  C  CA  B GLY   A 8   ? 0.2499 0.2582 0.2193 -0.0282 0.0389  -0.0129 8   GLY   A CA  
123  C  C   A GLY   A 8   ? 0.1716 0.2212 0.1787 -0.0487 0.0362  -0.0193 8   GLY   A C   
124  C  C   B GLY   A 8   ? 0.2352 0.2390 0.2039 -0.0272 0.0418  -0.0123 8   GLY   A C   
125  O  O   A GLY   A 8   ? 0.1751 0.2218 0.1914 -0.0260 0.0366  -0.0371 8   GLY   A O   
126  O  O   B GLY   A 8   ? 0.2342 0.2389 0.2043 -0.0267 0.0447  -0.0185 8   GLY   A O   
133  N  N   A TYR   A 9   ? 0.1513 0.2042 0.1741 -0.0412 0.0305  0.0036  9   TYR   A N   
134  N  N   B TYR   A 9   ? 0.2211 0.2215 0.1938 -0.0237 0.0378  -0.0069 9   TYR   A N   
135  C  CA  A TYR   A 9   ? 0.1414 0.1811 0.1567 -0.0402 0.0189  0.0095  9   TYR   A CA  
136  C  CA  B TYR   A 9   ? 0.2094 0.2045 0.1841 -0.0193 0.0391  -0.0020 9   TYR   A CA  
137  C  C   A TYR   A 9   ? 0.1474 0.1594 0.1529 -0.0282 0.0282  0.0235  9   TYR   A C   
138  C  C   B TYR   A 9   ? 0.2060 0.1888 0.1766 -0.0135 0.0438  -0.0014 9   TYR   A C   
139  O  O   A TYR   A 9   ? 0.1703 0.1667 0.1678 -0.0249 0.0258  0.0162  9   TYR   A O   
140  O  O   B TYR   A 9   ? 0.2077 0.1896 0.1880 -0.0106 0.0470  -0.0003 9   TYR   A O   
141  C  CB  A TYR   A 9   ? 0.1393 0.1996 0.1590 -0.0309 0.0162  0.0022  9   TYR   A CB  
142  C  CB  B TYR   A 9   ? 0.2027 0.2074 0.1926 -0.0214 0.0322  -0.0019 9   TYR   A CB  
143  C  CG  A TYR   A 9   ? 0.1372 0.2104 0.1735 -0.0234 0.0256  -0.0025 9   TYR   A CG  
144  C  CG  B TYR   A 9   ? 0.1962 0.2102 0.1918 -0.0241 0.0272  -0.0002 9   TYR   A CG  
145  C  CD1 A TYR   A 9   ? 0.1422 0.2231 0.1902 -0.0359 0.0342  -0.0138 9   TYR   A CD1 
146  C  CD1 B TYR   A 9   ? 0.1972 0.2147 0.2012 -0.0288 0.0252  -0.0017 9   TYR   A CD1 
147  C  CD2 A TYR   A 9   ? 0.1333 0.2069 0.1766 -0.0137 0.0149  0.0130  9   TYR   A CD2 
148  C  CD2 B TYR   A 9   ? 0.1934 0.2095 0.1861 -0.0235 0.0221  0.0041  9   TYR   A CD2 
149  C  CE1 A TYR   A 9   ? 0.1456 0.2273 0.2143 -0.0407 0.0416  -0.0140 9   TYR   A CE1 
150  C  CE1 B TYR   A 9   ? 0.1976 0.2166 0.2064 -0.0316 0.0242  -0.0018 9   TYR   A CE1 
151  C  CE2 A TYR   A 9   ? 0.1372 0.2145 0.1849 -0.0184 0.0252  0.0047  9   TYR   A CE2 
152  C  CE2 B TYR   A 9   ? 0.1942 0.2121 0.1897 -0.0250 0.0236  0.0040  9   TYR   A CE2 
153  C  CZ  A TYR   A 9   ? 0.1407 0.2270 0.2178 -0.0395 0.0478  -0.0063 9   TYR   A CZ  
154  C  CZ  B TYR   A 9   ? 0.1982 0.2165 0.2068 -0.0305 0.0278  0.0026  9   TYR   A CZ  
155  O  OH  A TYR   A 9   ? 0.1489 0.2384 0.2520 -0.0592 0.0559  -0.0089 9   TYR   A OH  
156  O  OH  B TYR   A 9   ? 0.2047 0.2219 0.2236 -0.0354 0.0292  0.0047  9   TYR   A OH  
175  N  N   A LEU   A 10  ? 0.1437 0.1473 0.1618 -0.0299 0.0143  0.0224  10  LEU   A N   
176  N  N   B LEU   A 10  ? 0.2049 0.1799 0.1735 -0.0126 0.0397  -0.0036 10  LEU   A N   
177  C  CA  A LEU   A 10  ? 0.1320 0.1410 0.1701 -0.0273 0.0116  0.0299  10  LEU   A CA  
178  C  CA  B LEU   A 10  ? 0.2043 0.1790 0.1805 -0.0132 0.0359  -0.0046 10  LEU   A CA  
179  C  C   A LEU   A 10  ? 0.1268 0.1349 0.1801 -0.0262 0.0118  0.0356  10  LEU   A C   
180  C  C   B LEU   A 10  ? 0.1907 0.1651 0.1621 -0.0146 0.0297  0.0018  10  LEU   A C   
181  O  O   A LEU   A 10  ? 0.1329 0.1349 0.1913 -0.0176 0.0246  0.0453  10  LEU   A O   
182  O  O   B LEU   A 10  ? 0.1885 0.1612 0.1547 -0.0164 0.0381  0.0116  10  LEU   A O   
183  C  CB  A LEU   A 10  ? 0.1354 0.1448 0.1978 -0.0229 0.0074  0.0403  10  LEU   A CB  
184  C  CB  B LEU   A 10  ? 0.2187 0.1927 0.2061 -0.0179 0.0340  -0.0087 10  LEU   A CB  
185  C  CG  A LEU   A 10  ? 0.1516 0.1597 0.2376 -0.0108 -0.0179 0.0503  10  LEU   A CG  
186  C  CG  B LEU   A 10  ? 0.2341 0.2072 0.2392 -0.0222 0.0287  -0.0129 10  LEU   A CG  
187  C  CD1 A LEU   A 10  ? 0.1665 0.1733 0.2673 -0.0228 -0.0119 0.0511  10  LEU   A CD1 
188  C  CD1 B LEU   A 10  ? 0.2396 0.2113 0.2538 -0.0240 0.0297  -0.0148 10  LEU   A CD1 
189  C  CD2 A LEU   A 10  ? 0.1785 0.1882 0.2565 -0.0058 -0.0182 0.0327  10  LEU   A CD2 
190  C  CD2 B LEU   A 10  ? 0.2400 0.2121 0.2523 -0.0217 0.0293  -0.0235 10  LEU   A CD2 
213  N  N   A LYS   A 11  ? 0.1311 0.1393 0.1782 -0.0274 0.0209  0.0372  11  LYS   A N   
214  N  N   B LYS   A 11  ? 0.1842 0.1567 0.1594 -0.0181 0.0126  -0.0018 11  LYS   A N   
215  C  CA  A LYS   A 11  ? 0.1356 0.1377 0.1773 -0.0330 0.0190  0.0335  11  LYS   A CA  
216  C  CA  B LYS   A 11  ? 0.1781 0.1487 0.1498 -0.0172 0.0062  0.0004  11  LYS   A CA  
217  C  C   A LYS   A 11  ? 0.1297 0.1457 0.1762 -0.0266 0.0242  0.0240  11  LYS   A C   
218  C  C   B LYS   A 11  ? 0.1625 0.1371 0.1457 -0.0175 0.0069  -0.0065 11  LYS   A C   
219  O  O   A LYS   A 11  ? 0.1387 0.1742 0.2089 -0.0499 0.0268  0.0095  11  LYS   A O   
220  O  O   B LYS   A 11  ? 0.1555 0.1302 0.1517 -0.0174 0.0081  -0.0212 11  LYS   A O   
221  C  CB  A LYS   A 11  ? 0.1480 0.1349 0.1726 -0.0343 0.0169  0.0261  11  LYS   A CB  
222  C  CB  B LYS   A 11  ? 0.1869 0.1466 0.1481 -0.0181 -0.0001 0.0030  11  LYS   A CB  
223  C  CG  A LYS   A 11  ? 0.1638 0.1308 0.1751 -0.0331 0.0189  0.0290  11  LYS   A CG  
224  C  CG  B LYS   A 11  ? 0.1953 0.1481 0.1412 -0.0181 -0.0035 0.0091  11  LYS   A CG  
225  C  CD  A LYS   A 11  ? 0.1801 0.1357 0.1835 -0.0303 0.0107  0.0315  11  LYS   A CD  
226  C  CD  B LYS   A 11  ? 0.2002 0.1545 0.1414 -0.0172 -0.0030 0.0113  11  LYS   A CD  
227  C  CE  A LYS   A 11  ? 0.1890 0.1320 0.1790 -0.0287 0.0096  0.0365  11  LYS   A CE  
228  C  CE  B LYS   A 11  ? 0.2041 0.1584 0.1349 -0.0137 0.0005  0.0138  11  LYS   A CE  
229  N  NZ  A LYS   A 11  ? 0.1881 0.1305 0.1909 -0.0180 -0.0035 0.0233  11  LYS   A NZ  
230  N  NZ  B LYS   A 11  ? 0.2038 0.1593 0.1296 -0.0086 0.0001  0.0171  11  LYS   A NZ  
257  N  N   A LEU   A 12  ? 0.1242 0.1342 0.1603 -0.0228 0.0206  0.0234  12  LEU   A N   
258  N  N   B LEU   A 12  ? 0.1548 0.1441 0.1536 -0.0025 0.0105  -0.0078 12  LEU   A N   
259  C  CA  A LEU   A 12  ? 0.1231 0.1403 0.1609 -0.0174 0.0098  0.0316  12  LEU   A CA  
260  C  CA  B LEU   A 12  ? 0.1500 0.1507 0.1589 0.0075  0.0220  -0.0026 12  LEU   A CA  
261  C  C   A LEU   A 12  ? 0.1281 0.1321 0.1693 -0.0221 0.0142  0.0337  12  LEU   A C   
262  C  C   B LEU   A 12  ? 0.1464 0.1498 0.1563 0.0095  0.0257  0.0010  12  LEU   A C   
263  O  O   A LEU   A 12  ? 0.1320 0.1320 0.1817 -0.0153 0.0140  0.0130  12  LEU   A O   
264  O  O   B LEU   A 12  ? 0.1490 0.1522 0.1549 0.0124  0.0218  -0.0016 12  LEU   A O   
265  C  CB  A LEU   A 12  ? 0.1277 0.1434 0.1705 -0.0097 0.0056  0.0283  12  LEU   A CB  
266  C  CB  B LEU   A 12  ? 0.1551 0.1605 0.1774 0.0124  0.0299  0.0010  12  LEU   A CB  
267  C  CG  A LEU   A 12  ? 0.1332 0.1557 0.1930 -0.0008 0.0181  0.0291  12  LEU   A CG  
268  C  CG  B LEU   A 12  ? 0.1580 0.1665 0.2021 0.0192  0.0403  0.0034  12  LEU   A CG  
269  C  CD1 A LEU   A 12  ? 0.1428 0.1631 0.2027 0.0105  0.0278  0.0421  12  LEU   A CD1 
270  C  CD1 B LEU   A 12  ? 0.1585 0.1731 0.2174 0.0258  0.0470  0.0032  12  LEU   A CD1 
271  C  CD2 A LEU   A 12  ? 0.1377 0.1653 0.2108 -0.0046 0.0256  0.0298  12  LEU   A CD2 
272  C  CD2 B LEU   A 12  ? 0.1589 0.1711 0.2126 0.0211  0.0434  -0.0045 12  LEU   A CD2 
295  N  N   A THR   A 13  ? 0.1259 0.1288 0.1828 -0.0192 0.0056  0.0287  13  THR   A N   
296  N  N   B THR   A 13  ? 0.1440 0.1463 0.1629 0.0063  0.0216  0.0094  13  THR   A N   
297  C  CA  A THR   A 13  ? 0.1276 0.1298 0.1889 -0.0166 0.0144  0.0311  13  THR   A CA  
298  C  CA  B THR   A 13  ? 0.1420 0.1492 0.1688 -0.0018 0.0263  0.0204  13  THR   A CA  
299  C  C   A THR   A 13  ? 0.1288 0.1355 0.2015 -0.0209 0.0043  0.0386  13  THR   A C   
300  C  C   B THR   A 13  ? 0.1500 0.1532 0.1705 -0.0093 0.0255  0.0228  13  THR   A C   
301  O  O   A THR   A 13  ? 0.1312 0.1390 0.1964 -0.0173 0.0059  0.0369  13  THR   A O   
302  O  O   B THR   A 13  ? 0.1598 0.1567 0.1747 -0.0119 0.0229  0.0264  13  THR   A O   
303  C  CB  A THR   A 13  ? 0.1331 0.1432 0.2068 -0.0090 0.0060  0.0335  13  THR   A CB  
304  C  CB  B THR   A 13  ? 0.1343 0.1514 0.1788 -0.0004 0.0298  0.0257  13  THR   A CB  
305  O  OG1 A THR   A 13  ? 0.1359 0.1414 0.2197 -0.0143 -0.0081 0.0412  13  THR   A OG1 
306  O  OG1 B THR   A 13  ? 0.1247 0.1515 0.1899 -0.0054 0.0389  0.0372  13  THR   A OG1 
307  C  CG2 A THR   A 13  ? 0.1399 0.1630 0.2197 -0.0096 0.0204  0.0234  13  THR   A CG2 
308  C  CG2 B THR   A 13  ? 0.1331 0.1542 0.1819 0.0080  0.0298  0.0213  13  THR   A CG2 
323  N  N   A ASP   A 14  ? 0.1342 0.1392 0.2217 -0.0272 -0.0009 0.0534  14  ASP   A N   
324  N  N   B ASP   A 14  ? 0.1503 0.1556 0.1824 -0.0138 0.0167  0.0260  14  ASP   A N   
325  C  CA  A ASP   A 14  ? 0.1410 0.1522 0.2483 -0.0212 -0.0090 0.0751  14  ASP   A CA  
326  C  CA  B ASP   A 14  ? 0.1520 0.1603 0.1942 -0.0167 0.0080  0.0373  14  ASP   A CA  
327  C  C   A ASP   A 14  ? 0.1457 0.1567 0.2300 -0.0233 -0.0108 0.0648  14  ASP   A C   
328  C  C   B ASP   A 14  ? 0.1466 0.1539 0.1746 -0.0119 -0.0014 0.0448  14  ASP   A C   
329  O  O   A ASP   A 14  ? 0.1559 0.1714 0.2414 -0.0379 -0.0115 0.0689  14  ASP   A O   
330  O  O   B ASP   A 14  ? 0.1480 0.1576 0.1719 -0.0087 -0.0070 0.0471  14  ASP   A O   
331  C  CB  A ASP   A 14  ? 0.1588 0.1799 0.3053 -0.0242 -0.0130 0.0959  14  ASP   A CB  
332  C  CB  B ASP   A 14  ? 0.1585 0.1730 0.2267 -0.0245 0.0041  0.0420  14  ASP   A CB  
333  C  CG  A ASP   A 14  ? 0.1834 0.2381 0.3843 -0.0250 -0.0122 0.0923  14  ASP   A CG  
334  C  CG  B ASP   A 14  ? 0.1601 0.1961 0.2615 -0.0329 0.0043  0.0404  14  ASP   A CG  
335  O  OD1 A ASP   A 14  ? 0.1986 0.2586 0.4077 -0.0135 -0.0328 0.0914  14  ASP   A OD1 
336  O  OD1 B ASP   A 14  ? 0.1626 0.1989 0.2729 -0.0396 0.0084  0.0426  14  ASP   A OD1 
337  O  OD2 A ASP   A 14  ? 0.2052 0.2779 0.4332 -0.0172 -0.0139 0.0729  14  ASP   A OD2 
338  O  OD2 B ASP   A 14  ? 0.1637 0.2178 0.2855 -0.0279 -0.0062 0.0313  14  ASP   A OD2 
347  N  N   A ASN   A 15  ? 0.1312 0.1379 0.2230 -0.0209 -0.0030 0.0604  15  ASN   A N   
348  N  N   B ASN   A 15  ? 0.1357 0.1417 0.1691 -0.0132 -0.0006 0.0546  15  ASN   A N   
349  C  CA  A ASN   A 15  ? 0.1318 0.1402 0.2409 -0.0178 -0.0093 0.0467  15  ASN   A CA  
350  C  CA  B ASN   A 15  ? 0.1328 0.1404 0.1770 -0.0120 -0.0020 0.0500  15  ASN   A CA  
351  C  C   A ASN   A 15  ? 0.1301 0.1387 0.2523 -0.0183 -0.0025 0.0448  15  ASN   A C   
352  C  C   B ASN   A 15  ? 0.1305 0.1405 0.1893 -0.0159 0.0038  0.0437  15  ASN   A C   
353  O  O   A ASN   A 15  ? 0.1344 0.1439 0.2846 -0.0231 -0.0218 0.0540  15  ASN   A O   
354  O  O   B ASN   A 15  ? 0.1373 0.1467 0.2166 -0.0206 -0.0050 0.0364  15  ASN   A O   
355  C  CB  A ASN   A 15  ? 0.1278 0.1433 0.2412 -0.0141 -0.0036 0.0374  15  ASN   A CB  
356  C  CB  B ASN   A 15  ? 0.1323 0.1402 0.1721 -0.0082 -0.0037 0.0519  15  ASN   A CB  
357  C  CG  A ASN   A 15  ? 0.1323 0.1520 0.2528 -0.0121 -0.0005 0.0251  15  ASN   A CG  
358  C  CG  B ASN   A 15  ? 0.1297 0.1421 0.1735 -0.0053 0.0052  0.0433  15  ASN   A CG  
359  O  OD1 A ASN   A 15  ? 0.1376 0.1553 0.2621 -0.0214 0.0005  0.0209  15  ASN   A OD1 
360  O  OD1 B ASN   A 15  ? 0.1282 0.1379 0.1840 -0.0063 0.0148  0.0492  15  ASN   A OD1 
361  N  ND2 A ASN   A 15  ? 0.1360 0.1658 0.2527 -0.0192 0.0088  0.0276  15  ASN   A ND2 
362  N  ND2 B ASN   A 15  ? 0.1309 0.1476 0.1679 -0.0101 0.0073  0.0412  15  ASN   A ND2 
375  N  N   A VAL   A 16  ? 0.1285 0.1334 0.2272 -0.0104 0.0014  0.0388  16  VAL   A N   
376  N  N   B VAL   A 16  ? 0.1244 0.1353 0.1741 -0.0115 0.0113  0.0436  16  VAL   A N   
377  C  CA  A VAL   A 16  ? 0.1226 0.1363 0.2192 -0.0119 0.0062  0.0398  16  VAL   A CA  
378  C  CA  B VAL   A 16  ? 0.1270 0.1390 0.1671 -0.0078 0.0179  0.0397  16  VAL   A CA  
379  C  C   A VAL   A 16  ? 0.1234 0.1328 0.2075 -0.0163 0.0015  0.0359  16  VAL   A C   
380  C  C   B VAL   A 16  ? 0.1221 0.1429 0.1573 -0.0085 0.0189  0.0359  16  VAL   A C   
381  O  O   A VAL   A 16  ? 0.1176 0.1262 0.2162 -0.0187 0.0112  0.0239  16  VAL   A O   
382  O  O   B VAL   A 16  ? 0.1174 0.1401 0.1598 -0.0047 0.0302  0.0336  16  VAL   A O   
383  C  CB  A VAL   A 16  ? 0.1281 0.1571 0.2143 0.0057  0.0298  0.0537  16  VAL   A CB  
384  C  CB  B VAL   A 16  ? 0.1370 0.1457 0.1648 0.0032  0.0318  0.0371  16  VAL   A CB  
385  C  CG1 A VAL   A 16  ? 0.1410 0.1685 0.2224 0.0144  0.0249  0.0507  16  VAL   A CG1 
386  C  CG1 B VAL   A 16  ? 0.1439 0.1490 0.1699 0.0089  0.0308  0.0365  16  VAL   A CG1 
387  C  CG2 A VAL   A 16  ? 0.1372 0.1750 0.2253 0.0113  0.0422  0.0545  16  VAL   A CG2 
388  C  CG2 B VAL   A 16  ? 0.1388 0.1530 0.1713 0.0081  0.0382  0.0353  16  VAL   A CG2 
407  N  N   A TYR   A 17  ? 0.1247 0.1303 0.1991 -0.0139 0.0108  0.0368  17  TYR   A N   
408  N  N   B TYR   A 17  ? 0.1261 0.1423 0.1470 -0.0137 0.0096  0.0290  17  TYR   A N   
409  C  CA  A TYR   A 17  ? 0.1288 0.1360 0.1794 -0.0218 0.0100  0.0379  17  TYR   A CA  
410  C  CA  B TYR   A 17  ? 0.1307 0.1422 0.1304 -0.0196 0.0007  0.0214  17  TYR   A CA  
411  C  C   A TYR   A 17  ? 0.1344 0.1290 0.1810 -0.0216 0.0096  0.0237  17  TYR   A C   
412  C  C   B TYR   A 17  ? 0.1311 0.1435 0.1196 -0.0219 0.0047  0.0169  17  TYR   A C   
413  O  O   A TYR   A 17  ? 0.1308 0.1235 0.1800 -0.0181 0.0187  0.0313  17  TYR   A O   
414  O  O   B TYR   A 17  ? 0.1296 0.1447 0.1156 -0.0256 0.0024  0.0131  17  TYR   A O   
415  C  CB  A TYR   A 17  ? 0.1503 0.1405 0.1844 -0.0280 0.0035  0.0406  17  TYR   A CB  
416  C  CB  B TYR   A 17  ? 0.1482 0.1455 0.1437 -0.0181 -0.0029 0.0222  17  TYR   A CB  
417  C  CG  A TYR   A 17  ? 0.1757 0.1541 0.1888 -0.0385 -0.0116 0.0405  17  TYR   A CG  
418  C  CG  B TYR   A 17  ? 0.1668 0.1531 0.1505 -0.0131 -0.0078 0.0192  17  TYR   A CG  
419  C  CD1 A TYR   A 17  ? 0.1929 0.1634 0.2142 -0.0292 -0.0216 0.0434  17  TYR   A CD1 
420  C  CD1 B TYR   A 17  ? 0.1779 0.1575 0.1635 -0.0035 -0.0097 0.0220  17  TYR   A CD1 
421  C  CD2 A TYR   A 17  ? 0.1917 0.1620 0.1738 -0.0564 -0.0134 0.0449  17  TYR   A CD2 
422  C  CD2 B TYR   A 17  ? 0.1778 0.1623 0.1519 -0.0143 -0.0081 0.0124  17  TYR   A CD2 
423  C  CE1 A TYR   A 17  ? 0.2057 0.1637 0.2189 -0.0388 -0.0340 0.0450  17  TYR   A CE1 
424  C  CE1 B TYR   A 17  ? 0.1873 0.1644 0.1777 -0.0019 -0.0128 0.0232  17  TYR   A CE1 
425  C  CE2 A TYR   A 17  ? 0.2100 0.1633 0.1921 -0.0602 -0.0310 0.0321  17  TYR   A CE2 
426  C  CE2 B TYR   A 17  ? 0.1890 0.1687 0.1629 -0.0108 -0.0123 0.0103  17  TYR   A CE2 
427  C  CZ  A TYR   A 17  ? 0.2170 0.1629 0.2024 -0.0540 -0.0424 0.0468  17  TYR   A CZ  
428  C  CZ  B TYR   A 17  ? 0.1927 0.1713 0.1751 -0.0058 -0.0156 0.0186  17  TYR   A CZ  
429  O  OH  A TYR   A 17  ? 0.2344 0.1649 0.2134 -0.0518 -0.0436 0.0443  17  TYR   A OH  
430  O  OH  B TYR   A 17  ? 0.1985 0.1771 0.1873 -0.0020 -0.0121 0.0196  17  TYR   A OH  
449  N  N   A ILE   A 18  ? 0.1362 0.1328 0.1825 -0.0198 0.0134  0.0371  18  ILE   A N   
450  N  N   B ILE   A 18  ? 0.1261 0.1449 0.1182 -0.0249 0.0176  0.0158  18  ILE   A N   
451  C  CA  A ILE   A 18  ? 0.1372 0.1298 0.1759 -0.0144 0.0159  0.0242  18  ILE   A CA  
452  C  CA  B ILE   A 18  ? 0.1257 0.1479 0.1162 -0.0183 0.0251  0.0091  18  ILE   A CA  
453  C  C   A ILE   A 18  ? 0.1382 0.1397 0.1748 -0.0241 0.0189  0.0222  18  ILE   A C   
454  C  C   B ILE   A 18  ? 0.1282 0.1589 0.1046 -0.0207 0.0236  0.0042  18  ILE   A C   
455  O  O   A ILE   A 18  ? 0.1377 0.1550 0.1771 -0.0308 0.0247  0.0270  18  ILE   A O   
456  O  O   B ILE   A 18  ? 0.1243 0.1621 0.1103 -0.0253 0.0315  0.0064  18  ILE   A O   
457  C  CB  A ILE   A 18  ? 0.1432 0.1285 0.1605 0.0011  0.0191  0.0361  18  ILE   A CB  
458  C  CB  B ILE   A 18  ? 0.1283 0.1404 0.1159 -0.0071 0.0371  0.0101  18  ILE   A CB  
459  C  CG1 A ILE   A 18  ? 0.1481 0.1343 0.1607 0.0136  0.0157  0.0293  18  ILE   A CG1 
460  C  CG1 B ILE   A 18  ? 0.1410 0.1491 0.1340 -0.0084 0.0446  0.0157  18  ILE   A CG1 
461  C  CG2 A ILE   A 18  ? 0.1418 0.1335 0.1591 0.0036  0.0146  0.0247  18  ILE   A CG2 
462  C  CG2 B ILE   A 18  ? 0.1304 0.1429 0.1141 -0.0082 0.0390  0.0086  18  ILE   A CG2 
463  C  CD1 A ILE   A 18  ? 0.1752 0.1563 0.1770 0.0204  0.0135  0.0295  18  ILE   A CD1 
464  C  CD1 B ILE   A 18  ? 0.1483 0.1575 0.1547 -0.0063 0.0456  0.0101  18  ILE   A CD1 
487  N  N   A LYS   A 19  ? 0.1317 0.1431 0.1558 -0.0221 0.0305  0.0181  19  LYS   A N   
488  N  N   B LYS   A 19  ? 0.1358 0.1683 0.1104 -0.0152 0.0286  -0.0034 19  LYS   A N   
489  C  CA  A LYS   A 19  ? 0.1456 0.1580 0.1597 -0.0186 0.0342  0.0234  19  LYS   A CA  
490  C  CA  B LYS   A 19  ? 0.1521 0.1814 0.1298 -0.0075 0.0264  -0.0132 19  LYS   A CA  
491  C  C   A LYS   A 19  ? 0.1382 0.1477 0.1794 -0.0093 0.0333  0.0289  19  LYS   A C   
492  C  C   B LYS   A 19  ? 0.1623 0.1862 0.1353 0.0017  0.0270  -0.0166 19  LYS   A C   
493  O  O   A LYS   A 19  ? 0.1361 0.1443 0.1816 -0.0054 0.0274  0.0365  19  LYS   A O   
494  O  O   B LYS   A 19  ? 0.1640 0.1838 0.1383 -0.0003 0.0263  -0.0137 19  LYS   A O   
495  C  CB  A LYS   A 19  ? 0.1685 0.1870 0.1724 -0.0235 0.0293  0.0192  19  LYS   A CB  
496  C  CB  B LYS   A 19  ? 0.1526 0.1884 0.1440 -0.0087 0.0305  -0.0230 19  LYS   A CB  
497  C  CG  A LYS   A 19  ? 0.1978 0.2114 0.1817 -0.0246 0.0222  0.0078  19  LYS   A CG  
498  C  CG  B LYS   A 19  ? 0.1642 0.1976 0.1582 -0.0087 0.0270  -0.0222 19  LYS   A CG  
499  C  CD  A LYS   A 19  ? 0.2262 0.2336 0.1962 -0.0315 0.0130  0.0045  19  LYS   A CD  
500  C  CD  B LYS   A 19  ? 0.1740 0.2041 0.1657 -0.0136 0.0211  -0.0171 19  LYS   A CD  
501  C  CE  A LYS   A 19  ? 0.2488 0.2463 0.2075 -0.0417 0.0100  0.0020  19  LYS   A CE  
502  C  CE  B LYS   A 19  ? 0.1791 0.2103 0.1753 -0.0190 0.0148  -0.0133 19  LYS   A CE  
503  N  NZ  A LYS   A 19  ? 0.2619 0.2570 0.2025 -0.0509 0.0180  -0.0042 19  LYS   A NZ  
504  N  NZ  B LYS   A 19  ? 0.1824 0.2140 0.1782 -0.0258 0.0191  -0.0104 19  LYS   A NZ  
531  N  N   A ASN   A 20  ? 0.1426 0.1544 0.2010 -0.0112 0.0400  0.0338  20  ASN   A N   
532  N  N   B ASN   A 20  ? 0.1760 0.1976 0.1531 0.0082  0.0271  -0.0202 20  ASN   A N   
533  C  CA  A ASN   A 20  ? 0.1599 0.1708 0.2221 0.0156  0.0566  0.0254  20  ASN   A CA  
534  C  CA  B ASN   A 20  ? 0.1899 0.2115 0.1835 0.0100  0.0230  -0.0226 20  ASN   A CA  
535  C  C   A ASN   A 20  ? 0.1811 0.1723 0.2446 0.0044  0.0724  0.0076  20  ASN   A C   
536  C  C   B ASN   A 20  ? 0.1975 0.2091 0.1980 0.0022  0.0283  -0.0265 20  ASN   A C   
537  O  O   A ASN   A 20  ? 0.2067 0.1836 0.2671 -0.0187 0.0773  -0.0163 20  ASN   A O   
538  O  O   B ASN   A 20  ? 0.2074 0.2150 0.2065 -0.0052 0.0291  -0.0370 20  ASN   A O   
539  C  CB  A ASN   A 20  ? 0.1629 0.1894 0.2376 0.0283  0.0599  0.0448  20  ASN   A CB  
540  C  CB  B ASN   A 20  ? 0.1998 0.2267 0.2025 0.0163  0.0151  -0.0223 20  ASN   A CB  
541  C  CG  A ASN   A 20  ? 0.1715 0.2029 0.2715 0.0395  0.0659  0.0586  20  ASN   A CG  
542  C  CG  B ASN   A 20  ? 0.2104 0.2394 0.2263 0.0221  0.0072  -0.0177 20  ASN   A CG  
543  O  OD1 A ASN   A 20  ? 0.1993 0.2157 0.3044 0.0533  0.0756  0.0451  20  ASN   A OD1 
544  O  OD1 B ASN   A 20  ? 0.2178 0.2446 0.2355 0.0228  -0.0036 -0.0203 20  ASN   A OD1 
545  N  ND2 A ASN   A 20  ? 0.1608 0.1988 0.2930 0.0361  0.0536  0.0767  20  ASN   A ND2 
546  N  ND2 B ASN   A 20  ? 0.2136 0.2427 0.2355 0.0261  0.0061  -0.0117 20  ASN   A ND2 
559  N  N   A ALA   A 21  ? 0.1803 0.1700 0.2497 0.0058  0.0625  0.0133  21  ALA   A N   
560  N  N   B ALA   A 21  ? 0.1975 0.2012 0.2074 -0.0011 0.0257  -0.0191 21  ALA   A N   
561  C  CA  A ALA   A 21  ? 0.1851 0.1715 0.2609 -0.0004 0.0562  0.0187  21  ALA   A CA  
562  C  CA  B ALA   A 21  ? 0.1973 0.1935 0.2116 -0.0072 0.0331  -0.0104 21  ALA   A CA  
563  C  C   A ALA   A 21  ? 0.1677 0.1697 0.2676 -0.0024 0.0521  0.0381  21  ALA   A C   
564  C  C   B ALA   A 21  ? 0.1912 0.1863 0.2096 -0.0054 0.0483  0.0015  21  ALA   A C   
565  O  O   A ALA   A 21  ? 0.1627 0.1727 0.2661 0.0040  0.0413  0.0479  21  ALA   A O   
566  O  O   B ALA   A 21  ? 0.1948 0.1817 0.2153 0.0039  0.0505  -0.0008 21  ALA   A O   
567  C  CB  A ALA   A 21  ? 0.2040 0.1838 0.2715 -0.0055 0.0460  0.0152  21  ALA   A CB  
568  C  CB  B ALA   A 21  ? 0.2027 0.1929 0.2283 -0.0106 0.0278  -0.0123 21  ALA   A CB  
579  N  N   A ASP   A 22  ? 0.1699 0.1679 0.2794 -0.0056 0.0482  0.0430  22  ASP   A N   
580  N  N   B ASP   A 22  ? 0.1848 0.1820 0.2025 -0.0106 0.0569  0.0134  22  ASP   A N   
581  C  CA  A ASP   A 22  ? 0.1770 0.1747 0.2725 -0.0040 0.0399  0.0419  22  ASP   A CA  
582  C  CA  B ASP   A 22  ? 0.1814 0.1786 0.1992 -0.0135 0.0524  0.0150  22  ASP   A CA  
583  C  C   A ASP   A 22  ? 0.1667 0.1840 0.2219 -0.0073 0.0426  0.0367  22  ASP   A C   
584  C  C   B ASP   A 22  ? 0.1690 0.1771 0.1813 -0.0199 0.0558  0.0043  22  ASP   A C   
585  O  O   A ASP   A 22  ? 0.1715 0.1943 0.2291 -0.0113 0.0459  0.0219  22  ASP   A O   
586  O  O   B ASP   A 22  ? 0.1628 0.1792 0.1840 -0.0289 0.0553  -0.0088 22  ASP   A O   
587  C  CB  A ASP   A 22  ? 0.2013 0.1772 0.3298 -0.0104 0.0246  0.0352  22  ASP   A CB  
588  C  CB  B ASP   A 22  ? 0.1914 0.1794 0.2222 -0.0101 0.0411  0.0169  22  ASP   A CB  
589  C  CG  A ASP   A 22  ? 0.2252 0.1882 0.3899 -0.0157 -0.0044 0.0439  22  ASP   A CG  
590  C  CG  B ASP   A 22  ? 0.1975 0.1788 0.2391 -0.0121 0.0289  0.0158  22  ASP   A CG  
591  O  OD1 A ASP   A 22  ? 0.2220 0.1858 0.4096 -0.0353 -0.0188 0.0576  22  ASP   A OD1 
592  O  OD1 B ASP   A 22  ? 0.2005 0.1751 0.2390 -0.0116 0.0320  0.0137  22  ASP   A OD1 
593  O  OD2 A ASP   A 22  ? 0.2490 0.2003 0.4269 -0.0064 -0.0081 0.0345  22  ASP   A OD2 
594  O  OD2 B ASP   A 22  ? 0.1979 0.1828 0.2514 -0.0156 0.0201  0.0103  22  ASP   A OD2 
603  N  N   A ILE   A 23  ? 0.1640 0.1828 0.1990 -0.0069 0.0402  0.0281  23  ILE   A N   
604  N  N   B ILE   A 23  ? 0.1667 0.1740 0.1741 -0.0184 0.0489  0.0046  23  ILE   A N   
605  C  CA  A ILE   A 23  ? 0.1635 0.1747 0.1846 -0.0136 0.0370  0.0259  23  ILE   A CA  
606  C  CA  B ILE   A 23  ? 0.1660 0.1739 0.1592 -0.0188 0.0329  0.0026  23  ILE   A CA  
607  C  C   A ILE   A 23  ? 0.1610 0.1790 0.1828 -0.0147 0.0574  0.0165  23  ILE   A C   
608  C  C   B ILE   A 23  ? 0.1716 0.1801 0.1656 -0.0268 0.0355  -0.0063 23  ILE   A C   
609  O  O   A ILE   A 23  ? 0.1715 0.1793 0.1875 -0.0071 0.0482  0.0043  23  ILE   A O   
610  O  O   B ILE   A 23  ? 0.1707 0.1805 0.1711 -0.0257 0.0322  -0.0077 23  ILE   A O   
611  C  CB  A ILE   A 23  ? 0.1758 0.1723 0.1635 -0.0082 0.0296  0.0243  23  ILE   A CB  
612  C  CB  B ILE   A 23  ? 0.1632 0.1648 0.1413 -0.0120 0.0150  0.0095  23  ILE   A CB  
613  C  CG1 A ILE   A 23  ? 0.1787 0.1721 0.1575 -0.0059 0.0247  0.0160  23  ILE   A CG1 
614  C  CG1 B ILE   A 23  ? 0.1608 0.1582 0.1270 -0.0119 0.0029  0.0053  23  ILE   A CG1 
615  C  CG2 A ILE   A 23  ? 0.1806 0.1730 0.1614 -0.0041 0.0322  0.0286  23  ILE   A CG2 
616  C  CG2 B ILE   A 23  ? 0.1647 0.1634 0.1400 -0.0094 0.0116  0.0140  23  ILE   A CG2 
617  C  CD1 A ILE   A 23  ? 0.1849 0.1741 0.1608 -0.0068 0.0181  0.0031  23  ILE   A CD1 
618  C  CD1 B ILE   A 23  ? 0.1562 0.1548 0.1228 -0.0084 -0.0052 0.0032  23  ILE   A CD1 
641  N  N   A VAL   A 24  ? 0.1678 0.1852 0.2020 -0.0221 0.0548  0.0088  24  VAL   A N   
642  N  N   B VAL   A 24  ? 0.1821 0.1872 0.1782 -0.0319 0.0343  -0.0127 24  VAL   A N   
643  C  CA  A VAL   A 24  ? 0.1861 0.1957 0.2155 -0.0253 0.0553  0.0021  24  VAL   A CA  
644  C  CA  B VAL   A 24  ? 0.1967 0.1952 0.1957 -0.0341 0.0313  -0.0180 24  VAL   A CA  
645  C  C   A VAL   A 24  ? 0.1914 0.2136 0.2174 -0.0328 0.0493  -0.0021 24  VAL   A C   
646  C  C   B VAL   A 24  ? 0.2044 0.2089 0.2028 -0.0339 0.0311  -0.0236 24  VAL   A C   
647  O  O   A VAL   A 24  ? 0.2054 0.2151 0.2189 -0.0282 0.0451  -0.0042 24  VAL   A O   
648  O  O   B VAL   A 24  ? 0.2116 0.2109 0.2125 -0.0303 0.0305  -0.0238 24  VAL   A O   
649  C  CB  A VAL   A 24  ? 0.1942 0.2007 0.2447 -0.0228 0.0614  0.0065  24  VAL   A CB  
650  C  CB  B VAL   A 24  ? 0.2007 0.1946 0.2075 -0.0352 0.0295  -0.0204 24  VAL   A CB  
651  C  CG1 A VAL   A 24  ? 0.1997 0.2110 0.2613 -0.0184 0.0613  -0.0012 24  VAL   A CG1 
652  C  CG1 B VAL   A 24  ? 0.2051 0.1959 0.2201 -0.0348 0.0285  -0.0210 24  VAL   A CG1 
653  C  CG2 A VAL   A 24  ? 0.2092 0.2083 0.2547 -0.0150 0.0741  0.0229  24  VAL   A CG2 
654  C  CG2 B VAL   A 24  ? 0.2034 0.1934 0.2060 -0.0336 0.0303  -0.0258 24  VAL   A CG2 
673  N  N   A GLU   A 25  ? 0.1948 0.2393 0.2246 -0.0414 0.0620  -0.0096 25  GLU   A N   
674  N  N   B GLU   A 25  ? 0.2080 0.2231 0.2090 -0.0349 0.0375  -0.0271 25  GLU   A N   
675  C  CA  A GLU   A 25  ? 0.2126 0.2684 0.2313 -0.0378 0.0702  -0.0185 25  GLU   A CA  
676  C  CA  B GLU   A 25  ? 0.2163 0.2383 0.2218 -0.0387 0.0364  -0.0250 25  GLU   A CA  
677  C  C   A GLU   A 25  ? 0.2001 0.2724 0.2043 -0.0473 0.0721  -0.0197 25  GLU   A C   
678  C  C   B GLU   A 25  ? 0.2181 0.2438 0.2118 -0.0390 0.0438  -0.0268 25  GLU   A C   
679  O  O   A GLU   A 25  ? 0.2062 0.2829 0.2160 -0.0467 0.0613  -0.0209 25  GLU   A O   
680  O  O   B GLU   A 25  ? 0.2172 0.2457 0.2069 -0.0399 0.0513  -0.0348 25  GLU   A O   
681  C  CB  A GLU   A 25  ? 0.2388 0.2967 0.2693 -0.0297 0.0726  -0.0179 25  GLU   A CB  
682  C  CB  B GLU   A 25  ? 0.2234 0.2472 0.2513 -0.0394 0.0330  -0.0230 25  GLU   A CB  
683  C  CG  A GLU   A 25  ? 0.2693 0.3213 0.3289 -0.0291 0.0555  -0.0212 25  GLU   A CG  
684  C  CG  B GLU   A 25  ? 0.2351 0.2567 0.2875 -0.0380 0.0253  -0.0241 25  GLU   A CG  
685  C  CD  A GLU   A 25  ? 0.2909 0.3431 0.3840 -0.0289 0.0375  -0.0229 25  GLU   A CD  
686  C  CD  B GLU   A 25  ? 0.2440 0.2650 0.3219 -0.0357 0.0137  -0.0234 25  GLU   A CD  
687  O  OE1 A GLU   A 25  ? 0.3011 0.3526 0.3928 -0.0243 0.0262  -0.0269 25  GLU   A OE1 
688  O  OE1 B GLU   A 25  ? 0.2474 0.2670 0.3381 -0.0367 0.0050  -0.0244 25  GLU   A OE1 
689  O  OE2 A GLU   A 25  ? 0.2964 0.3503 0.4179 -0.0332 0.0303  -0.0280 25  GLU   A OE2 
690  O  OE2 B GLU   A 25  ? 0.2500 0.2702 0.3371 -0.0310 0.0135  -0.0197 25  GLU   A OE2 
703  N  N   A GLU   A 26  ? 0.1853 0.2668 0.2013 -0.0644 0.0774  -0.0216 26  GLU   A N   
704  N  N   B GLU   A 26  ? 0.2219 0.2446 0.2061 -0.0390 0.0501  -0.0247 26  GLU   A N   
705  C  CA  A GLU   A 26  ? 0.1987 0.2704 0.1821 -0.0770 0.0704  -0.0172 26  GLU   A CA  
706  C  CA  B GLU   A 26  ? 0.2306 0.2463 0.2097 -0.0373 0.0521  -0.0219 26  GLU   A CA  
707  C  C   A GLU   A 26  ? 0.1991 0.2562 0.1580 -0.0782 0.0641  -0.0160 26  GLU   A C   
708  C  C   B GLU   A 26  ? 0.2388 0.2508 0.1967 -0.0310 0.0423  -0.0184 26  GLU   A C   
709  O  O   A GLU   A 26  ? 0.2085 0.2540 0.1454 -0.0841 0.0679  -0.0138 26  GLU   A O   
710  O  O   B GLU   A 26  ? 0.2398 0.2483 0.1866 -0.0316 0.0451  -0.0210 26  GLU   A O   
711  C  CB  A GLU   A 26  ? 0.2203 0.2841 0.2134 -0.0848 0.0661  -0.0100 26  GLU   A CB  
712  C  CB  B GLU   A 26  ? 0.2321 0.2415 0.2254 -0.0468 0.0618  -0.0210 26  GLU   A CB  
713  C  CG  A GLU   A 26  ? 0.2467 0.3090 0.2887 -0.0862 0.0633  -0.0176 26  GLU   A CG  
714  C  CG  B GLU   A 26  ? 0.2313 0.2361 0.2346 -0.0585 0.0840  -0.0253 26  GLU   A CG  
715  C  CD  A GLU   A 26  ? 0.2657 0.3290 0.3371 -0.0907 0.0749  -0.0170 26  GLU   A CD  
716  C  CD  B GLU   A 26  ? 0.2311 0.2295 0.2336 -0.0755 0.1073  -0.0319 26  GLU   A CD  
717  O  OE1 A GLU   A 26  ? 0.2692 0.3527 0.3370 -0.0798 0.0850  -0.0266 26  GLU   A OE1 
718  O  OE1 B GLU   A 26  ? 0.2261 0.2331 0.2356 -0.0770 0.1206  -0.0541 26  GLU   A OE1 
719  O  OE2 A GLU   A 26  ? 0.2888 0.3337 0.3694 -0.0922 0.0727  -0.0120 26  GLU   A OE2 
720  O  OE2 B GLU   A 26  ? 0.2358 0.2245 0.2101 -0.0743 0.1182  -0.0210 26  GLU   A OE2 
733  N  N   A ALA   A 27  ? 0.1819 0.2400 0.1631 -0.0855 0.0613  -0.0065 27  ALA   A N   
734  N  N   B ALA   A 27  ? 0.2455 0.2580 0.1919 -0.0254 0.0343  -0.0115 27  ALA   A N   
735  C  CA  A ALA   A 27  ? 0.1926 0.2454 0.1596 -0.0797 0.0551  -0.0054 27  ALA   A CA  
736  C  CA  B ALA   A 27  ? 0.2581 0.2710 0.1910 -0.0202 0.0262  -0.0085 27  ALA   A CA  
737  C  C   A ALA   A 27  ? 0.2220 0.2619 0.1737 -0.0872 0.0545  -0.0231 27  ALA   A C   
738  C  C   B ALA   A 27  ? 0.2775 0.2913 0.2106 -0.0196 0.0225  -0.0127 27  ALA   A C   
739  O  O   A ALA   A 27  ? 0.2302 0.2564 0.1786 -0.0907 0.0432  -0.0240 27  ALA   A O   
740  O  O   B ALA   A 27  ? 0.2775 0.2898 0.2103 -0.0183 0.0187  -0.0144 27  ALA   A O   
741  C  CB  A ALA   A 27  ? 0.1787 0.2383 0.1643 -0.0781 0.0430  -0.0013 27  ALA   A CB  
742  C  CB  B ALA   A 27  ? 0.2540 0.2666 0.1792 -0.0195 0.0231  -0.0049 27  ALA   A CB  
753  N  N   A LYS   A 28  ? 0.2582 0.2929 0.1966 -0.0803 0.0550  -0.0473 28  LYS   A N   
754  N  N   B LYS   A 28  ? 0.3004 0.3146 0.2396 -0.0206 0.0216  -0.0174 28  LYS   A N   
755  C  CA  A LYS   A 28  ? 0.2976 0.3311 0.2349 -0.0685 0.0589  -0.0603 28  LYS   A CA  
756  C  CA  B LYS   A 28  ? 0.3241 0.3399 0.2754 -0.0218 0.0220  -0.0203 28  LYS   A CA  
757  C  C   A LYS   A 28  ? 0.3156 0.3614 0.2250 -0.0722 0.0811  -0.0435 28  LYS   A C   
758  C  C   B LYS   A 28  ? 0.3376 0.3581 0.2793 -0.0298 0.0310  -0.0160 28  LYS   A C   
759  O  O   A LYS   A 28  ? 0.3226 0.3713 0.2557 -0.0696 0.0668  -0.0432 28  LYS   A O   
760  O  O   B LYS   A 28  ? 0.3407 0.3617 0.2855 -0.0279 0.0276  -0.0175 28  LYS   A O   
761  C  CB  A LYS   A 28  ? 0.3188 0.3434 0.2955 -0.0507 0.0445  -0.0747 28  LYS   A CB  
762  C  CB  B LYS   A 28  ? 0.3349 0.3477 0.3116 -0.0157 0.0151  -0.0238 28  LYS   A CB  
763  C  CG  A LYS   A 28  ? 0.3385 0.3540 0.3596 -0.0358 0.0366  -0.0789 28  LYS   A CG  
764  C  CG  B LYS   A 28  ? 0.3454 0.3545 0.3495 -0.0109 0.0109  -0.0246 28  LYS   A CG  
765  C  CD  A LYS   A 28  ? 0.3557 0.3687 0.4320 -0.0241 0.0255  -0.0762 28  LYS   A CD  
766  C  CD  B LYS   A 28  ? 0.3553 0.3626 0.3902 -0.0074 0.0061  -0.0241 28  LYS   A CD  
767  C  CE  A LYS   A 28  ? 0.3680 0.3792 0.4825 -0.0157 0.0172  -0.0775 28  LYS   A CE  
768  C  CE  B LYS   A 28  ? 0.3625 0.3682 0.4192 -0.0054 0.0029  -0.0247 28  LYS   A CE  
769  N  NZ  A LYS   A 28  ? 0.3762 0.3849 0.5141 -0.0101 0.0149  -0.0817 28  LYS   A NZ  
770  N  NZ  B LYS   A 28  ? 0.3671 0.3714 0.4373 -0.0037 0.0017  -0.0266 28  LYS   A NZ  
797  N  N   A LYS   A 29  ? 0.3238 0.3820 0.2130 -0.0788 0.1174  -0.0207 29  LYS   A N   
798  N  N   B LYS   A 29  ? 0.3472 0.3724 0.2856 -0.0409 0.0449  -0.0086 29  LYS   A N   
799  C  CA  A LYS   A 29  ? 0.3435 0.4050 0.2391 -0.0793 0.1258  -0.0068 29  LYS   A CA  
800  C  CA  B LYS   A 29  ? 0.3575 0.3864 0.2978 -0.0515 0.0571  -0.0027 29  LYS   A CA  
801  C  C   A LYS   A 29  ? 0.3514 0.3982 0.2263 -0.0833 0.1008  0.0018  29  LYS   A C   
802  C  C   B LYS   A 29  ? 0.3539 0.3855 0.2580 -0.0703 0.0697  0.0031  29  LYS   A C   
803  O  O   A LYS   A 29  ? 0.3623 0.4095 0.2385 -0.0765 0.0935  -0.0017 29  LYS   A O   
804  O  O   B LYS   A 29  ? 0.3577 0.3896 0.2627 -0.0680 0.0690  0.0035  29  LYS   A O   
805  C  CB  A LYS   A 29  ? 0.3567 0.4332 0.2945 -0.0722 0.1406  -0.0029 29  LYS   A CB  
806  C  CB  B LYS   A 29  ? 0.3699 0.4001 0.3468 -0.0434 0.0544  -0.0021 29  LYS   A CB  
807  C  CG  A LYS   A 29  ? 0.3742 0.4578 0.3618 -0.0636 0.1392  -0.0012 29  LYS   A CG  
808  C  CG  B LYS   A 29  ? 0.3818 0.4121 0.3943 -0.0363 0.0506  -0.0011 29  LYS   A CG  
809  C  CD  A LYS   A 29  ? 0.3906 0.4779 0.4255 -0.0560 0.1331  -0.0016 29  LYS   A CD  
810  C  CD  B LYS   A 29  ? 0.3917 0.4218 0.4350 -0.0305 0.0472  -0.0001 29  LYS   A CD  
811  C  CE  A LYS   A 29  ? 0.4017 0.4920 0.4699 -0.0508 0.1301  -0.0028 29  LYS   A CE  
812  C  CE  B LYS   A 29  ? 0.3984 0.4285 0.4638 -0.0266 0.0452  -0.0001 29  LYS   A CE  
813  N  NZ  A LYS   A 29  ? 0.4068 0.4995 0.4970 -0.0473 0.1280  -0.0046 29  LYS   A NZ  
814  N  NZ  B LYS   A 29  ? 0.4019 0.4321 0.4804 -0.0244 0.0438  0.0002  29  LYS   A NZ  
841  N  N   . VAL   A 30  ? 0.3444 0.3790 0.2137 -0.0915 0.0844  0.0075  30  VAL   A N   
842  C  CA  . VAL   A 30  ? 0.3388 0.3570 0.1914 -0.1110 0.0533  0.0200  30  VAL   A CA  
843  C  C   . VAL   A 30  ? 0.3420 0.3370 0.1620 -0.1132 0.0393  0.0285  30  VAL   A C   
844  O  O   . VAL   A 30  ? 0.3506 0.3392 0.1690 -0.1151 0.0318  0.0290  30  VAL   A O   
845  C  CB  . VAL   A 30  ? 0.3328 0.3513 0.2207 -0.1256 0.0324  0.0214  30  VAL   A CB  
846  C  CG1 . VAL   A 30  ? 0.3374 0.3496 0.2333 -0.1260 0.0208  0.0257  30  VAL   A CG1 
847  C  CG2 . VAL   A 30  ? 0.3283 0.3520 0.2450 -0.1338 0.0329  0.0191  30  VAL   A CG2 
858  N  N   A LYS   A 31  ? 0.3382 0.3229 0.1416 -0.1158 0.0209  0.0242  31  LYS   A N   
859  N  N   B LYS   A 31  ? 0.3418 0.3289 0.1826 -0.1044 0.0269  0.0248  31  LYS   A N   
860  C  CA  A LYS   A 31  ? 0.3485 0.3212 0.1629 -0.1008 -0.0030 0.0244  31  LYS   A CA  
861  C  CA  B LYS   A 31  ? 0.3445 0.3247 0.2142 -0.0904 0.0106  0.0227  31  LYS   A CA  
862  C  C   A LYS   A 31  ? 0.3218 0.3009 0.1228 -0.0864 -0.0060 0.0615  31  LYS   A C   
863  C  C   B LYS   A 31  ? 0.3208 0.3037 0.1668 -0.0870 0.0025  0.0395  31  LYS   A C   
864  O  O   A LYS   A 31  ? 0.3287 0.3123 0.1322 -0.0826 -0.0211 0.0749  31  LYS   A O   
865  O  O   B LYS   A 31  ? 0.3246 0.3083 0.1757 -0.0857 0.0000  0.0411  31  LYS   A O   
866  C  CB  A LYS   A 31  ? 0.3873 0.3441 0.2755 -0.0907 -0.0213 -0.0037 31  LYS   A CB  
867  C  CB  B LYS   A 31  ? 0.3700 0.3422 0.2996 -0.0780 0.0010  0.0071  31  LYS   A CB  
868  C  CG  A LYS   A 31  ? 0.4267 0.3682 0.3971 -0.0745 -0.0398 -0.0240 31  LYS   A CG  
869  C  CG  B LYS   A 31  ? 0.3932 0.3594 0.3810 -0.0646 -0.0097 -0.0051 31  LYS   A CG  
870  C  CD  A LYS   A 31  ? 0.4575 0.3871 0.4880 -0.0610 -0.0555 -0.0402 31  LYS   A CD  
871  C  CD  B LYS   A 31  ? 0.4111 0.3732 0.4427 -0.0535 -0.0189 -0.0145 31  LYS   A CD  
872  C  CE  A LYS   A 31  ? 0.4775 0.4013 0.5443 -0.0506 -0.0663 -0.0518 31  LYS   A CE  
873  C  CE  B LYS   A 31  ? 0.4225 0.3828 0.4822 -0.0457 -0.0250 -0.0202 31  LYS   A CE  
874  N  NZ  A LYS   A 31  ? 0.4880 0.4078 0.5751 -0.0447 -0.0722 -0.0585 31  LYS   A NZ  
875  N  NZ  B LYS   A 31  ? 0.4284 0.3874 0.5046 -0.0413 -0.0284 -0.0235 31  LYS   A NZ  
902  N  N   . PRO   A 32  ? 0.2900 0.2779 0.1222 -0.0879 -0.0062 0.0470  32  PRO   A N   
903  C  CA  . PRO   A 32  ? 0.2690 0.2569 0.1460 -0.0782 -0.0193 0.0564  32  PRO   A CA  
904  C  C   . PRO   A 32  ? 0.2601 0.2470 0.1587 -0.0654 -0.0276 0.0661  32  PRO   A C   
905  O  O   . PRO   A 32  ? 0.2520 0.2386 0.1666 -0.0682 -0.0387 0.0628  32  PRO   A O   
906  C  CB  . PRO   A 32  ? 0.2598 0.2568 0.1564 -0.0763 -0.0187 0.0460  32  PRO   A CB  
907  C  CG  . PRO   A 32  ? 0.2602 0.2602 0.1164 -0.0733 -0.0248 0.0356  32  PRO   A CG  
908  C  CD  . PRO   A 32  ? 0.2684 0.2651 0.1127 -0.0795 -0.0170 0.0395  32  PRO   A CD  
916  N  N   . THR   A 33  ? 0.2635 0.2408 0.1516 -0.0573 -0.0266 0.0637  33  THR   A N   
917  C  CA  . THR   A 33  ? 0.2593 0.2414 0.1590 -0.0461 -0.0379 0.0617  33  THR   A CA  
918  C  C   . THR   A 33  ? 0.2262 0.2190 0.1534 -0.0507 -0.0363 0.0463  33  THR   A C   
919  O  O   . THR   A 33  ? 0.2242 0.2190 0.1614 -0.0526 -0.0515 0.0459  33  THR   A O   
920  C  CB  . THR   A 33  ? 0.2849 0.2650 0.1745 -0.0372 -0.0417 0.0841  33  THR   A CB  
921  O  OG1 . THR   A 33  ? 0.3085 0.2820 0.2021 -0.0241 -0.0336 0.0942  33  THR   A OG1 
922  C  CG2 . THR   A 33  ? 0.2905 0.2747 0.1964 -0.0329 -0.0487 0.0799  33  THR   A CG2 
930  N  N   . VAL   A 34  ? 0.1991 0.1976 0.1410 -0.0500 -0.0230 0.0443  34  VAL   A N   
931  C  CA  . VAL   A 34  ? 0.1764 0.1812 0.1338 -0.0405 -0.0147 0.0384  34  VAL   A CA  
932  C  C   . VAL   A 34  ? 0.1672 0.1704 0.1237 -0.0339 -0.0073 0.0302  34  VAL   A C   
933  O  O   . VAL   A 34  ? 0.1670 0.1720 0.1492 -0.0393 -0.0079 0.0386  34  VAL   A O   
934  C  CB  . VAL   A 34  ? 0.1757 0.1761 0.1552 -0.0361 -0.0071 0.0273  34  VAL   A CB  
935  C  CG1 . VAL   A 34  ? 0.1819 0.1744 0.1548 -0.0304 0.0029  0.0140  34  VAL   A CG1 
936  C  CG2 . VAL   A 34  ? 0.1828 0.1914 0.1822 -0.0237 -0.0206 0.0315  34  VAL   A CG2 
946  N  N   . VAL   A 35  ? 0.1517 0.1569 0.1279 -0.0344 -0.0115 0.0266  35  VAL   A N   
947  C  CA  . VAL   A 35  ? 0.1411 0.1548 0.1182 -0.0275 -0.0028 0.0185  35  VAL   A CA  
948  C  C   . VAL   A 35  ? 0.1308 0.1402 0.1208 -0.0235 0.0012  0.0224  35  VAL   A C   
949  O  O   . VAL   A 35  ? 0.1273 0.1535 0.1454 -0.0256 0.0112  0.0197  35  VAL   A O   
950  C  CB  . VAL   A 35  ? 0.1463 0.1584 0.1401 -0.0169 0.0052  0.0051  35  VAL   A CB  
951  C  CG1 . VAL   A 35  ? 0.1557 0.1630 0.1558 -0.0107 0.0053  0.0061  35  VAL   A CG1 
952  C  CG2 . VAL   A 35  ? 0.1445 0.1543 0.1650 -0.0141 0.0117  -0.0004 35  VAL   A CG2 
962  N  N   . VAL   A 36  ? 0.1192 0.1390 0.1189 -0.0206 0.0047  0.0226  36  VAL   A N   
963  C  CA  . VAL   A 36  ? 0.1163 0.1278 0.1251 -0.0164 0.0063  0.0147  36  VAL   A CA  
964  C  C   . VAL   A 36  ? 0.1163 0.1277 0.1338 -0.0155 0.0053  0.0121  36  VAL   A C   
965  O  O   . VAL   A 36  ? 0.1245 0.1280 0.1538 -0.0074 0.0196  0.0166  36  VAL   A O   
966  C  CB  . VAL   A 36  ? 0.1188 0.1221 0.1367 -0.0099 0.0030  0.0165  36  VAL   A CB  
967  C  CG1 . VAL   A 36  ? 0.1251 0.1246 0.1524 -0.0191 0.0075  0.0046  36  VAL   A CG1 
968  C  CG2 . VAL   A 36  ? 0.1310 0.1253 0.1570 -0.0106 -0.0080 0.0222  36  VAL   A CG2 
978  N  N   . ASN   A 37  ? 0.1106 0.1216 0.1241 -0.0087 0.0023  0.0159  37  ASN   A N   
979  C  CA  . ASN   A 37  ? 0.1129 0.1167 0.1168 -0.0035 0.0006  0.0166  37  ASN   A CA  
980  C  C   . ASN   A 37  ? 0.1083 0.1151 0.1214 -0.0040 0.0102  0.0243  37  ASN   A C   
981  O  O   . ASN   A 37  ? 0.1232 0.1218 0.1309 0.0052  0.0100  0.0115  37  ASN   A O   
982  C  CB  . ASN   A 37  ? 0.1150 0.1168 0.1220 -0.0040 0.0000  0.0130  37  ASN   A CB  
983  C  CG  . ASN   A 37  ? 0.1133 0.1160 0.1356 -0.0004 0.0035  0.0130  37  ASN   A CG  
984  O  OD1 . ASN   A 37  ? 0.1122 0.1180 0.1614 -0.0025 0.0039  0.0153  37  ASN   A OD1 
985  N  ND2 . ASN   A 37  ? 0.1160 0.1141 0.1474 -0.0049 -0.0009 0.0259  37  ASN   A ND2 
992  N  N   A ALA   A 38  ? 0.1106 0.1216 0.1347 -0.0033 0.0109  0.0170  38  ALA   A N   
993  N  N   B ALA   A 38  ? 0.1100 0.1228 0.1196 -0.0043 0.0032  0.0178  38  ALA   A N   
994  C  CA  A ALA   A 38  ? 0.1199 0.1268 0.1265 -0.0030 0.0041  0.0075  38  ALA   A CA  
995  C  CA  B ALA   A 38  ? 0.1138 0.1299 0.1191 -0.0047 -0.0069 0.0112  38  ALA   A CA  
996  C  C   A ALA   A 38  ? 0.1169 0.1223 0.1265 -0.0038 -0.0010 0.0026  38  ALA   A C   
997  C  C   B ALA   A 38  ? 0.1092 0.1278 0.1220 -0.0030 -0.0128 0.0052  38  ALA   A C   
998  O  O   A ALA   A 38  ? 0.1212 0.1138 0.1333 -0.0027 -0.0056 -0.0000 38  ALA   A O   
999  O  O   B ALA   A 38  ? 0.1029 0.1243 0.1230 -0.0020 -0.0180 0.0089  38  ALA   A O   
1000 C  CB  A ALA   A 38  ? 0.1237 0.1529 0.1356 -0.0169 -0.0023 0.0009  38  ALA   A CB  
1001 C  CB  B ALA   A 38  ? 0.1172 0.1407 0.1259 -0.0094 -0.0108 0.0035  38  ALA   A CB  
1012 N  N   A ALA   A 39  ? 0.1137 0.1214 0.1397 -0.0015 0.0087  0.0154  39  ALA   A N   
1013 N  N   B ALA   A 39  ? 0.1127 0.1288 0.1311 -0.0050 -0.0101 0.0071  39  ALA   A N   
1014 C  CA  A ALA   A 39  ? 0.1196 0.1196 0.1303 -0.0008 0.0062  0.0046  39  ALA   A CA  
1015 C  CA  B ALA   A 39  ? 0.1222 0.1311 0.1274 -0.0064 -0.0033 0.0085  39  ALA   A CA  
1016 C  C   A ALA   A 39  ? 0.1193 0.1185 0.1328 0.0004  0.0020  0.0054  39  ALA   A C   
1017 C  C   B ALA   A 39  ? 0.1228 0.1244 0.1178 -0.0085 0.0045  0.0127  39  ALA   A C   
1018 O  O   A ALA   A 39  ? 0.1292 0.1210 0.1327 -0.0006 -0.0011 0.0080  39  ALA   A O   
1019 O  O   B ALA   A 39  ? 0.1233 0.1214 0.1115 -0.0154 0.0073  0.0223  39  ALA   A O   
1020 C  CB  A ALA   A 39  ? 0.1166 0.1333 0.1328 -0.0023 -0.0067 -0.0057 39  ALA   A CB  
1021 C  CB  B ALA   A 39  ? 0.1273 0.1405 0.1283 -0.0064 -0.0062 -0.0000 39  ALA   A CB  
1032 N  N   A ASN   A 40  ? 0.1204 0.1180 0.1428 -0.0049 0.0169  0.0080  40  ASN   A N   
1033 N  N   B ASN   A 40  ? 0.1268 0.1215 0.1205 -0.0045 0.0115  0.0106  40  ASN   A N   
1034 C  CA  A ASN   A 40  ? 0.1241 0.1156 0.1374 -0.0010 0.0078  0.0083  40  ASN   A CA  
1035 C  CA  B ASN   A 40  ? 0.1324 0.1170 0.1278 -0.0000 0.0028  0.0102  40  ASN   A CA  
1036 C  C   A ASN   A 40  ? 0.1210 0.1047 0.1164 -0.0058 0.0173  0.0125  40  ASN   A C   
1037 C  C   B ASN   A 40  ? 0.1333 0.1168 0.1266 -0.0039 0.0038  0.0157  40  ASN   A C   
1038 O  O   A ASN   A 40  ? 0.1205 0.1158 0.1283 -0.0096 0.0154  0.0136  40  ASN   A O   
1039 O  O   B ASN   A 40  ? 0.1328 0.1209 0.1302 -0.0068 -0.0013 0.0210  40  ASN   A O   
1040 C  CB  A ASN   A 40  ? 0.1372 0.1276 0.1407 0.0030  0.0026  0.0039  40  ASN   A CB  
1041 C  CB  B ASN   A 40  ? 0.1432 0.1192 0.1490 0.0010  -0.0016 0.0089  40  ASN   A CB  
1042 C  CG  A ASN   A 40  ? 0.1428 0.1317 0.1557 0.0059  0.0003  0.0082  40  ASN   A CG  
1043 C  CG  B ASN   A 40  ? 0.1514 0.1243 0.1700 -0.0019 -0.0066 0.0084  40  ASN   A CG  
1044 O  OD1 A ASN   A 40  ? 0.1540 0.1331 0.1855 0.0004  0.0032  0.0105  40  ASN   A OD1 
1045 O  OD1 B ASN   A 40  ? 0.1594 0.1270 0.1916 -0.0051 -0.0118 0.0029  40  ASN   A OD1 
1046 N  ND2 A ASN   A 40  ? 0.1466 0.1389 0.1538 0.0059  0.0127  0.0001  40  ASN   A ND2 
1047 N  ND2 B ASN   A 40  ? 0.1509 0.1331 0.1705 -0.0073 0.0087  0.0059  40  ASN   A ND2 
1060 N  N   A VAL   A 41  ? 0.1251 0.1116 0.1228 -0.0023 0.0143  0.0156  41  VAL   A N   
1061 N  N   B VAL   A 41  ? 0.1359 0.1200 0.1266 -0.0005 0.0088  0.0248  41  VAL   A N   
1062 C  CA  A VAL   A 41  ? 0.1267 0.1198 0.1389 0.0003  0.0155  0.0149  41  VAL   A CA  
1063 C  CA  B VAL   A 41  ? 0.1368 0.1238 0.1269 0.0037  0.0163  0.0271  41  VAL   A CA  
1064 C  C   A VAL   A 41  ? 0.1214 0.1199 0.1450 -0.0003 0.0073  0.0142  41  VAL   A C   
1065 C  C   B VAL   A 41  ? 0.1364 0.1244 0.1311 -0.0004 0.0205  0.0276  41  VAL   A C   
1066 O  O   A VAL   A 41  ? 0.1229 0.1128 0.1644 0.0020  0.0097  0.0073  41  VAL   A O   
1067 O  O   B VAL   A 41  ? 0.1384 0.1148 0.1344 -0.0009 0.0128  0.0264  41  VAL   A O   
1068 C  CB  A VAL   A 41  ? 0.1296 0.1277 0.1354 -0.0001 0.0207  0.0113  41  VAL   A CB  
1069 C  CB  B VAL   A 41  ? 0.1411 0.1310 0.1359 0.0064  0.0245  0.0306  41  VAL   A CB  
1070 C  CG1 A VAL   A 41  ? 0.1420 0.1369 0.1521 0.0056  0.0165  0.0063  41  VAL   A CG1 
1071 C  CG1 B VAL   A 41  ? 0.1483 0.1330 0.1419 0.0050  0.0253  0.0261  41  VAL   A CG1 
1072 C  CG2 A VAL   A 41  ? 0.1413 0.1336 0.1218 -0.0070 0.0342  0.0082  41  VAL   A CG2 
1073 C  CG2 B VAL   A 41  ? 0.1428 0.1379 0.1472 0.0111  0.0171  0.0325  41  VAL   A CG2 
1092 N  N   A TYR   A 42  ? 0.1154 0.1119 0.1625 -0.0051 0.0151  0.0216  42  TYR   A N   
1093 N  N   B TYR   A 42  ? 0.1319 0.1254 0.1270 0.0010  0.0183  0.0362  42  TYR   A N   
1094 C  CA  A TYR   A 42  ? 0.1255 0.1083 0.1675 -0.0081 0.0154  0.0198  42  TYR   A CA  
1095 C  CA  B TYR   A 42  ? 0.1340 0.1310 0.1277 0.0007  0.0159  0.0315  42  TYR   A CA  
1096 C  C   A TYR   A 42  ? 0.1126 0.1092 0.1700 -0.0052 0.0091  0.0232  42  TYR   A C   
1097 C  C   B TYR   A 42  ? 0.1317 0.1351 0.1232 -0.0013 0.0126  0.0349  42  TYR   A C   
1098 O  O   A TYR   A 42  ? 0.1147 0.1131 0.1826 -0.0160 0.0077  0.0046  42  TYR   A O   
1099 O  O   B TYR   A 42  ? 0.1291 0.1413 0.1326 -0.0055 0.0146  0.0287  42  TYR   A O   
1100 C  CB  A TYR   A 42  ? 0.1450 0.1228 0.1579 -0.0100 0.0252  0.0250  42  TYR   A CB  
1101 C  CB  B TYR   A 42  ? 0.1423 0.1340 0.1291 0.0056  0.0087  0.0335  42  TYR   A CB  
1102 C  CG  A TYR   A 42  ? 0.1624 0.1313 0.1592 -0.0032 0.0162  0.0337  42  TYR   A CG  
1103 C  CG  B TYR   A 42  ? 0.1509 0.1396 0.1350 0.0089  0.0036  0.0332  42  TYR   A CG  
1104 C  CD1 A TYR   A 42  ? 0.1718 0.1478 0.1650 -0.0122 0.0212  0.0366  42  TYR   A CD1 
1105 C  CD1 B TYR   A 42  ? 0.1530 0.1410 0.1314 0.0066  0.0035  0.0391  42  TYR   A CD1 
1106 C  CD2 A TYR   A 42  ? 0.1741 0.1531 0.1762 0.0021  0.0086  0.0306  42  TYR   A CD2 
1107 C  CD2 B TYR   A 42  ? 0.1621 0.1520 0.1471 0.0127  0.0035  0.0281  42  TYR   A CD2 
1108 C  CE1 A TYR   A 42  ? 0.1809 0.1572 0.1620 -0.0123 0.0218  0.0317  42  TYR   A CE1 
1109 C  CE1 B TYR   A 42  ? 0.1607 0.1489 0.1417 0.0053  0.0035  0.0289  42  TYR   A CE1 
1110 C  CE2 A TYR   A 42  ? 0.1854 0.1646 0.1862 -0.0061 0.0063  0.0341  42  TYR   A CE2 
1111 C  CE2 B TYR   A 42  ? 0.1716 0.1598 0.1594 0.0092  0.0056  0.0263  42  TYR   A CE2 
1112 C  CZ  A TYR   A 42  ? 0.1929 0.1684 0.1653 -0.0155 0.0178  0.0344  42  TYR   A CZ  
1113 C  CZ  B TYR   A 42  ? 0.1707 0.1587 0.1511 0.0053  0.0080  0.0218  42  TYR   A CZ  
1114 O  OH  A TYR   A 42  ? 0.2096 0.1875 0.1863 -0.0212 0.0143  0.0262  42  TYR   A OH  
1115 O  OH  B TYR   A 42  ? 0.1752 0.1673 0.1562 0.0021  0.0128  0.0179  42  TYR   A OH  
1134 N  N   A LEU   A 43  ? 0.1155 0.1118 0.1558 -0.0089 0.0086  0.0034  43  LEU   A N   
1135 N  N   B LEU   A 43  ? 0.1289 0.1332 0.1216 -0.0006 0.0045  0.0304  43  LEU   A N   
1136 C  CA  A LEU   A 43  ? 0.1109 0.1100 0.1519 -0.0104 0.0095  -0.0014 43  LEU   A CA  
1137 C  CA  B LEU   A 43  ? 0.1340 0.1305 0.1211 0.0002  -0.0023 0.0288  43  LEU   A CA  
1138 C  C   A LEU   A 43  ? 0.1092 0.1154 0.1483 -0.0055 0.0057  -0.0007 43  LEU   A C   
1139 C  C   B LEU   A 43  ? 0.1373 0.1327 0.1236 -0.0014 -0.0078 0.0220  43  LEU   A C   
1140 O  O   A LEU   A 43  ? 0.1286 0.1195 0.1770 0.0028  -0.0047 -0.0022 43  LEU   A O   
1141 O  O   B LEU   A 43  ? 0.1436 0.1336 0.1165 -0.0050 -0.0151 0.0230  43  LEU   A O   
1142 C  CB  A LEU   A 43  ? 0.1180 0.1105 0.1536 -0.0094 0.0046  0.0052  43  LEU   A CB  
1143 C  CB  B LEU   A 43  ? 0.1337 0.1234 0.1305 0.0027  -0.0028 0.0313  43  LEU   A CB  
1144 C  CG  A LEU   A 43  ? 0.1219 0.1141 0.1587 -0.0055 -0.0010 0.0024  43  LEU   A CG  
1145 C  CG  B LEU   A 43  ? 0.1317 0.1218 0.1384 0.0067  -0.0064 0.0285  43  LEU   A CG  
1146 C  CD1 A LEU   A 43  ? 0.1292 0.1199 0.1843 -0.0065 -0.0115 0.0080  43  LEU   A CD1 
1147 C  CD1 B LEU   A 43  ? 0.1327 0.1226 0.1427 0.0090  -0.0121 0.0336  43  LEU   A CD1 
1148 C  CD2 A LEU   A 43  ? 0.1374 0.1133 0.1570 -0.0048 0.0048  0.0085  43  LEU   A CD2 
1149 C  CD2 B LEU   A 43  ? 0.1372 0.1186 0.1399 0.0078  -0.0050 0.0331  43  LEU   A CD2 
1172 N  N   A LYS   A 44  ? 0.1238 0.1124 0.1474 -0.0032 0.0053  0.0113  44  LYS   A N   
1173 N  N   B LYS   A 44  ? 0.1407 0.1332 0.1323 0.0029  -0.0113 0.0198  44  LYS   A N   
1174 C  CA  A LYS   A 44  ? 0.1385 0.1113 0.1517 -0.0067 0.0124  0.0193  44  LYS   A CA  
1175 C  CA  B LYS   A 44  ? 0.1463 0.1355 0.1430 0.0037  -0.0059 0.0178  44  LYS   A CA  
1176 C  C   A LYS   A 44  ? 0.1262 0.1184 0.1380 0.0002  0.0060  0.0099  44  LYS   A C   
1177 C  C   B LYS   A 44  ? 0.1328 0.1258 0.1301 0.0047  -0.0022 0.0124  44  LYS   A C   
1178 O  O   A LYS   A 44  ? 0.1297 0.1328 0.1530 0.0025  0.0028  0.0011  44  LYS   A O   
1179 O  O   B LYS   A 44  ? 0.1371 0.1289 0.1257 0.0070  0.0019  -0.0002 44  LYS   A O   
1180 C  CB  A LYS   A 44  ? 0.1662 0.1305 0.1781 -0.0049 0.0241  0.0340  44  LYS   A CB  
1181 C  CB  B LYS   A 44  ? 0.1668 0.1576 0.1862 0.0062  0.0011  0.0156  44  LYS   A CB  
1182 C  CG  A LYS   A 44  ? 0.1958 0.1576 0.2373 -0.0161 0.0442  0.0446  44  LYS   A CG  
1183 C  CG  B LYS   A 44  ? 0.1854 0.1828 0.2393 0.0072  0.0051  0.0169  44  LYS   A CG  
1184 C  CD  A LYS   A 44  ? 0.2350 0.2069 0.3487 -0.0207 0.0361  0.0312  44  LYS   A CD  
1185 C  CD  B LYS   A 44  ? 0.2053 0.2124 0.2955 0.0002  0.0007  0.0179  44  LYS   A CD  
1186 C  CE  A LYS   A 44  ? 0.2547 0.2400 0.4224 -0.0190 0.0326  0.0269  44  LYS   A CE  
1187 C  CE  B LYS   A 44  ? 0.2139 0.2313 0.3332 -0.0059 -0.0022 0.0229  44  LYS   A CE  
1188 N  NZ  A LYS   A 44  ? 0.2640 0.2634 0.4584 -0.0172 0.0272  0.0253  44  LYS   A NZ  
1189 N  NZ  B LYS   A 44  ? 0.2216 0.2444 0.3563 -0.0140 -0.0017 0.0243  44  LYS   A NZ  
1216 N  N   . HIS   A 45  ? 0.1180 0.1154 0.1455 0.0009  -0.0041 0.0179  45  HIS   A N   
1217 C  CA  . HIS   A 45  ? 0.1155 0.1189 0.1480 -0.0015 -0.0083 0.0139  45  HIS   A CA  
1218 C  C   . HIS   A 45  ? 0.1221 0.1283 0.1598 0.0015  -0.0015 0.0119  45  HIS   A C   
1219 O  O   . HIS   A 45  ? 0.1433 0.1419 0.1925 0.0205  -0.0113 -0.0049 45  HIS   A O   
1220 C  CB  . HIS   A 45  ? 0.1189 0.1132 0.1425 -0.0009 -0.0033 0.0036  45  HIS   A CB  
1221 C  CG  . HIS   A 45  ? 0.1143 0.1160 0.1357 -0.0053 0.0023  0.0121  45  HIS   A CG  
1222 N  ND1 . HIS   A 45  ? 0.1076 0.1249 0.1497 -0.0052 -0.0022 0.0132  45  HIS   A ND1 
1223 C  CD2 . HIS   A 45  ? 0.1144 0.1200 0.1413 -0.0117 -0.0068 0.0198  45  HIS   A CD2 
1224 C  CE1 . HIS   A 45  ? 0.1126 0.1258 0.1327 -0.0088 -0.0051 0.0253  45  HIS   A CE1 
1225 N  NE2 . HIS   A 45  ? 0.1121 0.1288 0.1317 -0.0074 -0.0043 0.0219  45  HIS   A NE2 
1234 N  N   A GLY   A 46  ? 0.1363 0.1346 0.1743 0.0080  -0.0167 0.0150  46  GLY   A N   
1235 N  N   B GLY   A 46  ? 0.1304 0.1342 0.1562 0.0098  -0.0115 0.0137  46  GLY   A N   
1236 C  CA  A GLY   A 46  ? 0.1423 0.1426 0.1918 0.0087  -0.0202 0.0223  46  GLY   A CA  
1237 C  CA  B GLY   A 46  ? 0.1369 0.1354 0.1549 0.0123  -0.0201 0.0198  46  GLY   A CA  
1238 C  C   A GLY   A 46  ? 0.1412 0.1346 0.1914 0.0197  -0.0259 0.0306  46  GLY   A C   
1239 C  C   B GLY   A 46  ? 0.1413 0.1293 0.1517 0.0184  -0.0289 0.0212  46  GLY   A C   
1240 O  O   A GLY   A 46  ? 0.1429 0.1425 0.2326 0.0137  -0.0339 0.0109  46  GLY   A O   
1241 O  O   B GLY   A 46  ? 0.1446 0.1289 0.1707 0.0194  -0.0325 0.0218  46  GLY   A O   
1248 N  N   A GLY   A 47  ? 0.1438 0.1365 0.1781 0.0170  -0.0252 0.0106  47  GLY   A N   
1249 N  N   B GLY   A 47  ? 0.1426 0.1281 0.1450 0.0192  -0.0288 0.0115  47  GLY   A N   
1250 C  CA  A GLY   A 47  ? 0.1431 0.1397 0.1735 0.0161  -0.0425 -0.0027 47  GLY   A CA  
1251 C  CA  B GLY   A 47  ? 0.1458 0.1295 0.1433 0.0210  -0.0376 0.0037  47  GLY   A CA  
1252 C  C   A GLY   A 47  ? 0.1380 0.1312 0.1717 0.0171  -0.0483 -0.0098 47  GLY   A C   
1253 C  C   B GLY   A 47  ? 0.1445 0.1311 0.1409 0.0202  -0.0366 -0.0080 47  GLY   A C   
1254 O  O   A GLY   A 47  ? 0.1381 0.1279 0.1809 0.0178  -0.0401 0.0082  47  GLY   A O   
1255 O  O   B GLY   A 47  ? 0.1468 0.1284 0.1528 0.0240  -0.0302 0.0037  47  GLY   A O   
1262 N  N   A GLY   A 48  ? 0.1361 0.1291 0.1800 0.0159  -0.0573 -0.0108 48  GLY   A N   
1263 N  N   B GLY   A 48  ? 0.1433 0.1346 0.1543 0.0132  -0.0335 -0.0162 48  GLY   A N   
1264 C  CA  A GLY   A 48  ? 0.1324 0.1257 0.1970 0.0066  -0.0492 -0.0130 48  GLY   A CA  
1265 C  CA  B GLY   A 48  ? 0.1415 0.1354 0.1603 0.0104  -0.0157 -0.0175 48  GLY   A CA  
1266 C  C   A GLY   A 48  ? 0.1239 0.1261 0.1785 -0.0012 -0.0223 -0.0127 48  GLY   A C   
1267 C  C   B GLY   A 48  ? 0.1336 0.1366 0.1522 0.0067  0.0065  -0.0116 48  GLY   A C   
1268 O  O   A GLY   A 48  ? 0.1369 0.1214 0.1847 -0.0009 -0.0169 -0.0100 48  GLY   A O   
1269 O  O   B GLY   A 48  ? 0.1437 0.1402 0.1526 0.0018  0.0143  -0.0142 48  GLY   A O   
1276 N  N   A VAL   A 49  ? 0.1104 0.1221 0.1696 -0.0072 -0.0143 -0.0099 49  VAL   A N   
1277 N  N   B VAL   A 49  ? 0.1207 0.1325 0.1521 0.0030  0.0092  -0.0032 49  VAL   A N   
1278 C  CA  A VAL   A 49  ? 0.1247 0.1215 0.1640 -0.0065 0.0151  -0.0085 49  VAL   A CA  
1279 C  CA  B VAL   A 49  ? 0.1113 0.1302 0.1423 0.0012  0.0133  0.0012  49  VAL   A CA  
1280 C  C   A VAL   A 49  ? 0.1221 0.1105 0.1488 0.0013  0.0109  -0.0062 49  VAL   A C   
1281 C  C   B VAL   A 49  ? 0.1092 0.1194 0.1234 0.0023  0.0170  -0.0033 49  VAL   A C   
1282 O  O   A VAL   A 49  ? 0.1302 0.1185 0.1448 -0.0036 0.0156  -0.0032 49  VAL   A O   
1283 O  O   B VAL   A 49  ? 0.1075 0.1135 0.1181 0.0050  0.0181  -0.0053 49  VAL   A O   
1284 C  CB  A VAL   A 49  ? 0.1397 0.1246 0.1666 -0.0097 0.0266  -0.0142 49  VAL   A CB  
1285 C  CB  B VAL   A 49  ? 0.1013 0.1300 0.1389 0.0082  0.0106  0.0011  49  VAL   A CB  
1286 C  CG1 A VAL   A 49  ? 0.1474 0.1165 0.1681 -0.0014 0.0269  -0.0056 49  VAL   A CG1 
1287 C  CG1 B VAL   A 49  ? 0.0922 0.1291 0.1346 0.0209  0.0048  0.0011  49  VAL   A CG1 
1288 C  CG2 A VAL   A 49  ? 0.1529 0.1367 0.2070 -0.0276 0.0284  -0.0087 49  VAL   A CG2 
1289 C  CG2 B VAL   A 49  ? 0.1029 0.1340 0.1362 0.0124  0.0179  0.0019  49  VAL   A CG2 
1308 N  N   A ALA   A 50  ? 0.1157 0.1129 0.1362 -0.0030 -0.0123 0.0073  50  ALA   A N   
1309 N  N   B ALA   A 50  ? 0.1098 0.1183 0.1136 0.0051  0.0086  0.0045  50  ALA   A N   
1310 C  CA  A ALA   A 50  ? 0.1111 0.1097 0.1386 -0.0087 -0.0030 0.0118  50  ALA   A CA  
1311 C  CA  B ALA   A 50  ? 0.1138 0.1168 0.1179 -0.0001 0.0012  0.0050  50  ALA   A CA  
1312 C  C   A ALA   A 50  ? 0.1081 0.1167 0.1347 -0.0117 -0.0040 0.0091  50  ALA   A C   
1313 C  C   B ALA   A 50  ? 0.1136 0.1188 0.1193 -0.0008 -0.0012 0.0001  50  ALA   A C   
1314 O  O   A ALA   A 50  ? 0.1113 0.1168 0.1456 -0.0056 -0.0053 0.0063  50  ALA   A O   
1315 O  O   B ALA   A 50  ? 0.1119 0.1169 0.1291 0.0025  -0.0038 -0.0005 50  ALA   A O   
1316 C  CB  A ALA   A 50  ? 0.1075 0.1178 0.1387 -0.0117 -0.0019 -0.0007 50  ALA   A CB  
1317 C  CB  B ALA   A 50  ? 0.1187 0.1175 0.1195 0.0004  0.0057  -0.0003 50  ALA   A CB  
1328 N  N   A GLY   A 51  ? 0.1152 0.1096 0.1444 0.0028  -0.0127 0.0046  51  GLY   A N   
1329 N  N   B GLY   A 51  ? 0.1175 0.1194 0.1247 0.0028  -0.0079 -0.0058 51  GLY   A N   
1330 C  CA  A GLY   A 51  ? 0.1280 0.1109 0.1561 0.0047  -0.0193 0.0097  51  GLY   A CA  
1331 C  CA  B GLY   A 51  ? 0.1225 0.1226 0.1317 0.0026  -0.0118 -0.0059 51  GLY   A CA  
1332 C  C   A GLY   A 51  ? 0.1177 0.1197 0.1520 0.0059  -0.0106 -0.0053 51  GLY   A C   
1333 C  C   B GLY   A 51  ? 0.1176 0.1267 0.1361 0.0034  -0.0083 -0.0109 51  GLY   A C   
1334 O  O   A GLY   A 51  ? 0.1183 0.1298 0.1689 0.0011  -0.0069 -0.0090 51  GLY   A O   
1335 O  O   B GLY   A 51  ? 0.1185 0.1310 0.1396 0.0030  -0.0089 -0.0120 51  GLY   A O   
1342 N  N   . ALA   A 52  ? 0.1123 0.1298 0.1489 0.0006  -0.0026 -0.0141 52  ALA   A N   
1343 C  CA  . ALA   A 52  ? 0.1129 0.1404 0.1672 -0.0005 0.0030  -0.0110 52  ALA   A CA  
1344 C  C   . ALA   A 52  ? 0.1190 0.1367 0.1375 -0.0082 0.0073  -0.0071 52  ALA   A C   
1345 O  O   . ALA   A 52  ? 0.1283 0.1462 0.1566 -0.0073 0.0056  -0.0148 52  ALA   A O   
1346 C  CB  . ALA   A 52  ? 0.1282 0.1722 0.1770 -0.0075 -0.0000 -0.0067 52  ALA   A CB  
1353 N  N   A LEU   A 53  ? 0.1145 0.1325 0.1334 -0.0076 0.0024  -0.0028 53  LEU   A N   
1354 N  N   B LEU   A 53  ? 0.1177 0.1375 0.1292 -0.0077 0.0019  -0.0029 53  LEU   A N   
1355 C  CA  A LEU   A 53  ? 0.1295 0.1341 0.1284 -0.0077 0.0057  0.0033  53  LEU   A CA  
1356 C  CA  B LEU   A 53  ? 0.1225 0.1391 0.1263 -0.0078 0.0006  -0.0001 53  LEU   A CA  
1357 C  C   A LEU   A 53  ? 0.1229 0.1342 0.1084 0.0020  0.0032  0.0076  53  LEU   A C   
1358 C  C   B LEU   A 53  ? 0.1252 0.1424 0.1196 -0.0059 -0.0019 -0.0017 53  LEU   A C   
1359 O  O   A LEU   A 53  ? 0.1375 0.1411 0.1183 -0.0062 0.0027  0.0056  53  LEU   A O   
1360 O  O   B LEU   A 53  ? 0.1317 0.1424 0.1291 -0.0132 -0.0003 -0.0003 53  LEU   A O   
1361 C  CB  A LEU   A 53  ? 0.1428 0.1354 0.1308 -0.0099 0.0030  0.0101  53  LEU   A CB  
1362 C  CB  B LEU   A 53  ? 0.1222 0.1360 0.1250 -0.0077 -0.0019 0.0029  53  LEU   A CB  
1363 C  CG  A LEU   A 53  ? 0.1632 0.1391 0.1482 -0.0113 0.0037  0.0104  53  LEU   A CG  
1364 C  CG  B LEU   A 53  ? 0.1226 0.1326 0.1205 -0.0089 -0.0067 0.0004  53  LEU   A CG  
1365 C  CD1 A LEU   A 53  ? 0.1766 0.1469 0.1560 -0.0022 0.0119  0.0139  53  LEU   A CD1 
1366 C  CD1 B LEU   A 53  ? 0.1319 0.1367 0.1262 -0.0097 -0.0019 -0.0017 53  LEU   A CD1 
1367 C  CD2 A LEU   A 53  ? 0.1755 0.1541 0.1625 -0.0210 0.0020  0.0101  53  LEU   A CD2 
1368 C  CD2 B LEU   A 53  ? 0.1193 0.1306 0.1179 -0.0087 -0.0056 -0.0011 53  LEU   A CD2 
1391 N  N   A ASN   A 54  ? 0.1135 0.1267 0.1142 -0.0013 -0.0051 0.0080  54  ASN   A N   
1392 N  N   B ASN   A 54  ? 0.1239 0.1442 0.1150 -0.0052 -0.0072 -0.0045 54  ASN   A N   
1393 C  CA  A ASN   A 54  ? 0.1066 0.1211 0.1287 -0.0020 -0.0076 0.0040  54  ASN   A CA  
1394 C  CA  B ASN   A 54  ? 0.1228 0.1454 0.1161 -0.0035 -0.0083 -0.0092 54  ASN   A CA  
1395 C  C   A ASN   A 54  ? 0.1159 0.1254 0.1400 -0.0111 -0.0010 0.0049  54  ASN   A C   
1396 C  C   B ASN   A 54  ? 0.1280 0.1448 0.1137 -0.0070 -0.0024 -0.0112 54  ASN   A C   
1397 O  O   A ASN   A 54  ? 0.1190 0.1336 0.1461 -0.0090 -0.0080 -0.0036 54  ASN   A O   
1398 O  O   B ASN   A 54  ? 0.1275 0.1475 0.1090 -0.0072 0.0023  -0.0178 54  ASN   A O   
1399 C  CB  A ASN   A 54  ? 0.1066 0.1212 0.1442 -0.0096 -0.0133 -0.0015 54  ASN   A CB  
1400 C  CB  B ASN   A 54  ? 0.1186 0.1482 0.1133 0.0015  -0.0075 -0.0134 54  ASN   A CB  
1401 C  CG  A ASN   A 54  ? 0.1107 0.1216 0.1536 -0.0035 -0.0040 0.0026  54  ASN   A CG  
1402 C  CG  B ASN   A 54  ? 0.1155 0.1496 0.1079 0.0063  -0.0024 -0.0158 54  ASN   A CG  
1403 O  OD1 A ASN   A 54  ? 0.1078 0.1231 0.1604 -0.0069 -0.0099 0.0102  54  ASN   A OD1 
1404 O  OD1 B ASN   A 54  ? 0.1141 0.1534 0.1117 0.0046  -0.0071 -0.0210 54  ASN   A OD1 
1405 N  ND2 A ASN   A 54  ? 0.1197 0.1237 0.1550 -0.0099 -0.0065 0.0110  54  ASN   A ND2 
1406 N  ND2 B ASN   A 54  ? 0.1169 0.1479 0.0991 0.0043  0.0026  -0.0115 54  ASN   A ND2 
1419 N  N   A LYS   A 55  ? 0.1150 0.1291 0.1469 -0.0033 -0.0039 -0.0080 55  LYS   A N   
1420 N  N   B LYS   A 55  ? 0.1311 0.1437 0.1213 -0.0030 -0.0055 -0.0132 55  LYS   A N   
1421 C  CA  A LYS   A 55  ? 0.1212 0.1382 0.1558 -0.0009 -0.0107 -0.0187 55  LYS   A CA  
1422 C  CA  B LYS   A 55  ? 0.1376 0.1486 0.1391 0.0011  -0.0064 -0.0136 55  LYS   A CA  
1423 C  C   A LYS   A 55  ? 0.1198 0.1470 0.1538 -0.0039 -0.0017 -0.0231 55  LYS   A C   
1424 C  C   B LYS   A 55  ? 0.1342 0.1502 0.1443 -0.0027 -0.0057 -0.0187 55  LYS   A C   
1425 O  O   A LYS   A 55  ? 0.1273 0.1589 0.1627 -0.0005 -0.0016 -0.0225 55  LYS   A O   
1426 O  O   B LYS   A 55  ? 0.1372 0.1522 0.1405 0.0002  -0.0088 -0.0171 55  LYS   A O   
1427 C  CB  A LYS   A 55  ? 0.1301 0.1420 0.1645 0.0095  -0.0141 -0.0296 55  LYS   A CB  
1428 C  CB  B LYS   A 55  ? 0.1457 0.1547 0.1577 0.0046  -0.0038 -0.0079 55  LYS   A CB  
1429 C  CG  A LYS   A 55  ? 0.1463 0.1679 0.1805 0.0231  -0.0242 -0.0331 55  LYS   A CG  
1430 C  CG  B LYS   A 55  ? 0.1536 0.1653 0.1797 0.0089  -0.0077 -0.0112 55  LYS   A CG  
1431 C  CD  A LYS   A 55  ? 0.1572 0.1886 0.1941 0.0326  -0.0235 -0.0346 55  LYS   A CD  
1432 C  CD  B LYS   A 55  ? 0.1605 0.1731 0.2002 0.0103  -0.0082 -0.0123 55  LYS   A CD  
1433 C  CE  A LYS   A 55  ? 0.1731 0.2102 0.2162 0.0387  -0.0304 -0.0393 55  LYS   A CE  
1434 C  CE  B LYS   A 55  ? 0.1727 0.1840 0.2238 0.0116  -0.0109 -0.0149 55  LYS   A CE  
1435 N  NZ  A LYS   A 55  ? 0.1778 0.2152 0.2227 0.0439  -0.0373 -0.0409 55  LYS   A NZ  
1436 N  NZ  B LYS   A 55  ? 0.1780 0.1916 0.2361 0.0152  -0.0107 -0.0159 55  LYS   A NZ  
1463 N  N   . ALA   A 56  ? 0.1324 0.1521 0.1531 -0.0101 0.0007  -0.0246 56  ALA   A N   
1464 C  CA  . ALA   A 56  ? 0.1449 0.1734 0.1509 -0.0130 0.0073  -0.0219 56  ALA   A CA  
1465 C  C   . ALA   A 56  ? 0.1493 0.1851 0.1321 -0.0112 0.0116  -0.0199 56  ALA   A C   
1466 O  O   . ALA   A 56  ? 0.1501 0.2154 0.1419 0.0015  0.0094  -0.0142 56  ALA   A O   
1467 C  CB  . ALA   A 56  ? 0.1477 0.1914 0.1635 -0.0254 0.0126  -0.0106 56  ALA   A CB  
1474 N  N   . THR   A 57  ? 0.1344 0.1621 0.1299 -0.0085 0.0125  -0.0158 57  THR   A N   
1475 C  CA  . THR   A 57  ? 0.1397 0.1603 0.1341 -0.0148 -0.0006 -0.0111 57  THR   A CA  
1476 C  C   . THR   A 57  ? 0.1417 0.1619 0.1411 -0.0080 -0.0056 -0.0152 57  THR   A C   
1477 O  O   . THR   A 57  ? 0.1347 0.1696 0.1642 -0.0126 -0.0143 -0.0287 57  THR   A O   
1478 C  CB  . THR   A 57  ? 0.1348 0.1602 0.1357 -0.0141 0.0002  -0.0111 57  THR   A CB  
1479 O  OG1 . THR   A 57  ? 0.1240 0.1520 0.1429 -0.0056 -0.0019 -0.0084 57  THR   A OG1 
1480 C  CG2 . THR   A 57  ? 0.1402 0.1613 0.1242 -0.0075 -0.0045 0.0013  57  THR   A CG2 
1488 N  N   . ASN   A 58  ? 0.1418 0.1593 0.1612 -0.0095 0.0006  -0.0267 58  ASN   A N   
1489 C  CA  . ASN   A 58  ? 0.1594 0.1517 0.1782 -0.0122 0.0079  -0.0361 58  ASN   A CA  
1490 C  C   . ASN   A 58  ? 0.1371 0.1395 0.1675 -0.0034 -0.0028 -0.0261 58  ASN   A C   
1491 O  O   . ASN   A 58  ? 0.1407 0.1570 0.1764 -0.0140 -0.0078 -0.0305 58  ASN   A O   
1492 C  CB  . ASN   A 58  ? 0.2054 0.1677 0.2169 -0.0191 0.0355  -0.0513 58  ASN   A CB  
1493 C  CG  . ASN   A 58  ? 0.2568 0.1966 0.2979 -0.0179 0.0459  -0.0411 58  ASN   A CG  
1494 O  OD1 . ASN   A 58  ? 0.2865 0.1890 0.3388 0.0149  0.0836  -0.0275 58  ASN   A OD1 
1495 N  ND2 . ASN   A 58  ? 0.2702 0.2110 0.3251 -0.0241 0.0310  -0.0501 58  ASN   A ND2 
1502 N  N   . ASN   A 59  ? 0.1214 0.1362 0.1563 -0.0065 -0.0110 -0.0162 59  ASN   A N   
1503 C  CA  . ASN   A 59  ? 0.1242 0.1278 0.1574 -0.0028 -0.0107 -0.0089 59  ASN   A CA  
1504 C  C   . ASN   A 59  ? 0.1248 0.1302 0.1474 -0.0042 -0.0082 -0.0045 59  ASN   A C   
1505 O  O   . ASN   A 59  ? 0.1248 0.1300 0.1541 -0.0081 -0.0031 0.0001  59  ASN   A O   
1506 C  CB  . ASN   A 59  ? 0.1313 0.1249 0.1605 0.0029  -0.0221 -0.0148 59  ASN   A CB  
1507 C  CG  . ASN   A 59  ? 0.1258 0.1311 0.1629 0.0006  -0.0277 0.0012  59  ASN   A CG  
1508 O  OD1 . ASN   A 59  ? 0.1396 0.1373 0.1557 -0.0113 -0.0239 0.0057  59  ASN   A OD1 
1509 N  ND2 . ASN   A 59  ? 0.1360 0.1361 0.1756 -0.0102 -0.0161 0.0082  59  ASN   A ND2 
1516 N  N   . ALA   A 60  ? 0.1194 0.1358 0.1468 -0.0028 -0.0053 -0.0034 60  ALA   A N   
1517 C  CA  . ALA   A 60  ? 0.1191 0.1377 0.1509 -0.0027 -0.0171 -0.0040 60  ALA   A CA  
1518 C  C   . ALA   A 60  ? 0.1201 0.1270 0.1494 -0.0025 -0.0137 -0.0058 60  ALA   A C   
1519 O  O   . ALA   A 60  ? 0.1140 0.1284 0.1752 -0.0062 -0.0127 -0.0082 60  ALA   A O   
1520 C  CB  . ALA   A 60  ? 0.1331 0.1519 0.1590 -0.0041 -0.0117 -0.0184 60  ALA   A CB  
1526 N  N   . MET   A 61  ? 0.1160 0.1275 0.1406 -0.0076 -0.0043 -0.0065 61  MET   A N   
1527 C  CA  . MET   A 61  ? 0.1161 0.1255 0.1431 -0.0101 0.0018  0.0004  61  MET   A CA  
1528 C  C   . MET   A 61  ? 0.1115 0.1198 0.1522 -0.0116 -0.0029 -0.0080 61  MET   A C   
1529 O  O   . MET   A 61  ? 0.1149 0.1197 0.1599 -0.0043 0.0060  0.0027  61  MET   A O   
1530 C  CB  . MET   A 61  ? 0.1232 0.1248 0.1372 -0.0087 -0.0047 -0.0021 61  MET   A CB  
1531 C  CG  . MET   A 61  ? 0.1218 0.1313 0.1502 -0.0032 -0.0020 0.0025  61  MET   A CG  
1532 S  SD  . MET   A 61  ? 0.1247 0.1318 0.1854 -0.0119 -0.0035 -0.0140 61  MET   A SD  
1533 C  CE  . MET   A 61  ? 0.1436 0.1406 0.2143 -0.0144 0.0169  -0.0133 61  MET   A CE  
1543 N  N   . GLN   A 62  ? 0.1161 0.1120 0.1562 -0.0097 -0.0065 -0.0020 62  GLN   A N   
1544 C  CA  . GLN   A 62  ? 0.1144 0.1125 0.1584 -0.0040 -0.0061 0.0088  62  GLN   A CA  
1545 C  C   . GLN   A 62  ? 0.1166 0.1082 0.1643 -0.0003 0.0014  0.0019  62  GLN   A C   
1546 O  O   . GLN   A 62  ? 0.1219 0.1197 0.1610 -0.0024 0.0039  0.0022  62  GLN   A O   
1547 C  CB  . GLN   A 62  ? 0.1151 0.1134 0.1594 -0.0062 0.0012  0.0063  62  GLN   A CB  
1548 C  CG  . GLN   A 62  ? 0.1241 0.1132 0.1573 -0.0061 -0.0018 0.0194  62  GLN   A CG  
1549 C  CD  . GLN   A 62  ? 0.1285 0.1176 0.1527 -0.0055 0.0033  0.0129  62  GLN   A CD  
1550 O  OE1 . GLN   A 62  ? 0.1307 0.1311 0.1618 -0.0053 0.0024  0.0024  62  GLN   A OE1 
1551 N  NE2 . GLN   A 62  ? 0.1353 0.1233 0.1672 -0.0001 0.0007  -0.0035 62  GLN   A NE2 
1560 N  N   . VAL   A 63  ? 0.1130 0.1162 0.1762 -0.0067 0.0064  -0.0127 63  VAL   A N   
1561 C  CA  . VAL   A 63  ? 0.1185 0.1261 0.1886 -0.0121 -0.0028 -0.0111 63  VAL   A CA  
1562 C  C   . VAL   A 63  ? 0.1052 0.1259 0.1756 -0.0131 -0.0127 -0.0112 63  VAL   A C   
1563 O  O   . VAL   A 63  ? 0.1084 0.1273 0.1973 -0.0136 -0.0044 -0.0073 63  VAL   A O   
1564 C  CB  . VAL   A 63  ? 0.1312 0.1448 0.2163 -0.0142 -0.0058 -0.0336 63  VAL   A CB  
1565 C  CG1 . VAL   A 63  ? 0.1426 0.1628 0.2444 -0.0122 -0.0157 -0.0522 63  VAL   A CG1 
1566 C  CG2 . VAL   A 63  ? 0.1353 0.1365 0.2301 -0.0133 0.0120  -0.0322 63  VAL   A CG2 
1576 N  N   . GLU   A 64  ? 0.1155 0.1307 0.1642 -0.0053 -0.0032 -0.0057 64  GLU   A N   
1577 C  CA  . GLU   A 64  ? 0.1139 0.1330 0.1707 -0.0077 -0.0093 0.0001  64  GLU   A CA  
1578 C  C   . GLU   A 64  ? 0.1086 0.1247 0.1661 -0.0085 0.0006  0.0040  64  GLU   A C   
1579 O  O   . GLU   A 64  ? 0.1162 0.1307 0.1762 -0.0045 -0.0025 -0.0004 64  GLU   A O   
1580 C  CB  . GLU   A 64  ? 0.1211 0.1421 0.1735 -0.0075 -0.0021 0.0012  64  GLU   A CB  
1581 C  CG  . GLU   A 64  ? 0.1312 0.1436 0.1748 -0.0117 0.0023  0.0014  64  GLU   A CG  
1582 C  CD  . GLU   A 64  ? 0.1418 0.1533 0.1828 -0.0186 0.0045  -0.0001 64  GLU   A CD  
1583 O  OE1 . GLU   A 64  ? 0.1377 0.1625 0.2081 -0.0216 0.0127  0.0047  64  GLU   A OE1 
1584 O  OE2 . GLU   A 64  ? 0.1573 0.1535 0.1785 -0.0259 -0.0095 0.0088  64  GLU   A OE2 
1591 N  N   . SER   A 65  ? 0.1030 0.1250 0.1636 0.0021  0.0008  0.0007  65  SER   A N   
1592 C  CA  . SER   A 65  ? 0.1116 0.1177 0.1584 -0.0057 0.0004  -0.0033 65  SER   A CA  
1593 C  C   . SER   A 65  ? 0.1145 0.1271 0.1594 -0.0053 -0.0062 0.0003  65  SER   A C   
1594 O  O   . SER   A 65  ? 0.1233 0.1300 0.1689 -0.0004 0.0101  -0.0037 65  SER   A O   
1595 C  CB  . SER   A 65  ? 0.1135 0.1205 0.1616 -0.0093 0.0038  0.0120  65  SER   A CB  
1596 O  OG  . SER   A 65  ? 0.1129 0.1331 0.1634 -0.0102 -0.0079 0.0149  65  SER   A OG  
1602 N  N   . ASP   A 66  ? 0.1153 0.1186 0.1684 -0.0067 0.0127  0.0083  66  ASP   A N   
1603 C  CA  . ASP   A 66  ? 0.1250 0.1324 0.1848 -0.0031 0.0113  0.0184  66  ASP   A CA  
1604 C  C   . ASP   A 66  ? 0.1220 0.1302 0.1852 -0.0064 0.0099  0.0171  66  ASP   A C   
1605 O  O   . ASP   A 66  ? 0.1262 0.1422 0.2006 -0.0032 0.0241  0.0197  66  ASP   A O   
1606 C  CB  . ASP   A 66  ? 0.1329 0.1423 0.2126 0.0061  0.0147  0.0307  66  ASP   A CB  
1607 C  CG  . ASP   A 66  ? 0.1563 0.1565 0.2382 0.0007  -0.0004 0.0449  66  ASP   A CG  
1608 O  OD1 . ASP   A 66  ? 0.1573 0.1842 0.2131 -0.0114 -0.0046 0.0484  66  ASP   A OD1 
1609 O  OD2 . ASP   A 66  ? 0.1732 0.1706 0.3218 0.0180  -0.0169 0.0271  66  ASP   A OD2 
1614 N  N   . ASP   A 67  ? 0.1122 0.1341 0.1938 -0.0087 0.0079  0.0209  67  ASP   A N   
1615 C  CA  . ASP   A 67  ? 0.1202 0.1478 0.1974 -0.0058 0.0052  0.0256  67  ASP   A CA  
1616 C  C   . ASP   A 67  ? 0.1227 0.1439 0.1924 0.0009  0.0117  0.0284  67  ASP   A C   
1617 O  O   . ASP   A 67  ? 0.1181 0.1541 0.2189 0.0039  0.0276  0.0360  67  ASP   A O   
1618 C  CB  . ASP   A 67  ? 0.1288 0.1592 0.2227 -0.0047 -0.0094 0.0315  67  ASP   A CB  
1619 C  CG  . ASP   A 67  ? 0.1250 0.1728 0.2568 -0.0100 -0.0265 0.0398  67  ASP   A CG  
1620 O  OD1 . ASP   A 67  ? 0.1287 0.1912 0.3315 -0.0106 -0.0380 0.0473  67  ASP   A OD1 
1621 O  OD2 . ASP   A 67  ? 0.1305 0.1776 0.2469 0.0015  -0.0144 0.0321  67  ASP   A OD2 
1626 N  N   . TYR   A 68  ? 0.1233 0.1324 0.1877 0.0028  0.0154  0.0253  68  TYR   A N   
1627 C  CA  . TYR   A 68  ? 0.1317 0.1333 0.1863 -0.0001 0.0181  0.0228  68  TYR   A CA  
1628 C  C   . TYR   A 68  ? 0.1240 0.1323 0.1849 -0.0004 0.0210  0.0143  68  TYR   A C   
1629 O  O   . TYR   A 68  ? 0.1309 0.1356 0.1962 0.0064  0.0310  0.0213  68  TYR   A O   
1630 C  CB  . TYR   A 68  ? 0.1332 0.1316 0.1943 0.0072  0.0386  0.0244  68  TYR   A CB  
1631 C  CG  . TYR   A 68  ? 0.1379 0.1510 0.2281 0.0037  0.0525  0.0279  68  TYR   A CG  
1632 C  CD1 . TYR   A 68  ? 0.1488 0.1610 0.2700 -0.0211 0.0426  -0.0088 68  TYR   A CD1 
1633 C  CD2 . TYR   A 68  ? 0.1612 0.1478 0.2658 0.0134  0.0535  0.0431  68  TYR   A CD2 
1634 C  CE1 . TYR   A 68  ? 0.1595 0.1677 0.3098 -0.0174 0.0521  -0.0168 68  TYR   A CE1 
1635 C  CE2 . TYR   A 68  ? 0.1636 0.1558 0.2938 0.0032  0.0679  0.0196  68  TYR   A CE2 
1636 C  CZ  . TYR   A 68  ? 0.1640 0.1601 0.3216 -0.0196 0.0545  -0.0118 68  TYR   A CZ  
1637 O  OH  . TYR   A 68  ? 0.1871 0.1578 0.3461 -0.0154 0.0312  -0.0364 68  TYR   A OH  
1647 N  N   . ILE   A 69  ? 0.1176 0.1245 0.1868 -0.0010 0.0143  0.0167  69  ILE   A N   
1648 C  CA  . ILE   A 69  ? 0.1279 0.1305 0.1766 0.0034  0.0113  0.0067  69  ILE   A CA  
1649 C  C   . ILE   A 69  ? 0.1313 0.1296 0.1662 0.0067  0.0179  0.0171  69  ILE   A C   
1650 O  O   . ILE   A 69  ? 0.1371 0.1393 0.1724 -0.0012 0.0201  0.0210  69  ILE   A O   
1651 C  CB  . ILE   A 69  ? 0.1321 0.1548 0.1830 -0.0004 0.0138  0.0011  69  ILE   A CB  
1652 C  CG1 . ILE   A 69  ? 0.1370 0.1638 0.1894 0.0093  0.0120  -0.0183 69  ILE   A CG1 
1653 C  CG2 . ILE   A 69  ? 0.1525 0.1747 0.2012 0.0136  0.0015  -0.0111 69  ILE   A CG2 
1654 C  CD1 . ILE   A 69  ? 0.1359 0.1723 0.2071 -0.0028 0.0089  -0.0174 69  ILE   A CD1 
1666 N  N   . ALA   A 70  ? 0.1363 0.1294 0.1781 -0.0061 0.0180  0.0195  70  ALA   A N   
1667 C  CA  . ALA   A 70  ? 0.1399 0.1455 0.1962 -0.0136 0.0239  0.0247  70  ALA   A CA  
1668 C  C   . ALA   A 70  ? 0.1353 0.1596 0.1978 -0.0109 0.0285  0.0249  70  ALA   A C   
1669 O  O   . ALA   A 70  ? 0.1545 0.1935 0.2159 0.0077  0.0486  0.0384  70  ALA   A O   
1670 C  CB  . ALA   A 70  ? 0.1474 0.1414 0.2157 -0.0171 0.0225  0.0169  70  ALA   A CB  
1676 N  N   . THR   A 71  ? 0.1270 0.1544 0.1937 -0.0043 0.0150  0.0237  71  THR   A N   
1677 C  CA  . THR   A 71  ? 0.1374 0.1740 0.2229 0.0046  0.0198  0.0213  71  THR   A CA  
1678 C  C   . THR   A 71  ? 0.1293 0.1642 0.2404 0.0125  0.0324  0.0239  71  THR   A C   
1679 O  O   . THR   A 71  ? 0.1364 0.1926 0.2799 0.0112  0.0416  -0.0042 71  THR   A O   
1680 C  CB  . THR   A 71  ? 0.1614 0.2014 0.2502 0.0130  -0.0140 0.0340  71  THR   A CB  
1681 O  OG1 . THR   A 71  ? 0.1881 0.2172 0.2554 0.0039  -0.0341 0.0282  71  THR   A OG1 
1682 C  CG2 . THR   A 71  ? 0.1701 0.2203 0.2793 0.0202  -0.0201 0.0454  71  THR   A CG2 
1690 N  N   . ASN   A 72  ? 0.1327 0.1470 0.2200 0.0124  0.0266  0.0264  72  ASN   A N   
1691 C  CA  . ASN   A 72  ? 0.1398 0.1516 0.2232 0.0145  0.0308  0.0235  72  ASN   A CA  
1692 C  C   . ASN   A 72  ? 0.1517 0.1502 0.2162 0.0115  0.0480  0.0143  72  ASN   A C   
1693 O  O   . ASN   A 72  ? 0.1711 0.1499 0.2437 0.0117  0.0437  0.0017  72  ASN   A O   
1694 C  CB  . ASN   A 72  ? 0.1596 0.1552 0.2167 0.0102  0.0315  0.0247  72  ASN   A CB  
1695 C  CG  . ASN   A 72  ? 0.1854 0.1674 0.2186 0.0247  0.0343  0.0288  72  ASN   A CG  
1696 O  OD1 . ASN   A 72  ? 0.2040 0.1985 0.2339 0.0243  0.0351  0.0329  72  ASN   A OD1 
1697 N  ND2 . ASN   A 72  ? 0.2016 0.1696 0.2256 0.0533  0.0188  0.0195  72  ASN   A ND2 
1704 N  N   . GLY   A 73  ? 0.1512 0.1460 0.1959 0.0035  0.0432  0.0071  73  GLY   A N   
1705 C  CA  . GLY   A 73  ? 0.1548 0.1431 0.1867 -0.0090 0.0380  0.0040  73  GLY   A CA  
1706 C  C   . GLY   A 73  ? 0.1540 0.1323 0.1837 -0.0011 0.0477  0.0230  73  GLY   A C   
1707 O  O   . GLY   A 73  ? 0.1526 0.1372 0.2026 0.0100  0.0383  0.0311  73  GLY   A O   
1711 N  N   . PRO   A 74  ? 0.1626 0.1368 0.1859 -0.0141 0.0471  0.0125  74  PRO   A N   
1712 C  CA  . PRO   A 74  ? 0.1578 0.1353 0.1964 -0.0036 0.0424  0.0130  74  PRO   A CA  
1713 C  C   . PRO   A 74  ? 0.1520 0.1216 0.1900 -0.0001 0.0312  0.0067  74  PRO   A C   
1714 O  O   . PRO   A 74  ? 0.1585 0.1274 0.2106 0.0011  0.0371  -0.0035 74  PRO   A O   
1715 C  CB  . PRO   A 74  ? 0.1719 0.1643 0.2167 -0.0002 0.0372  0.0235  74  PRO   A CB  
1716 C  CG  . PRO   A 74  ? 0.1994 0.1983 0.2541 -0.0191 0.0281  0.0109  74  PRO   A CG  
1717 C  CD  . PRO   A 74  ? 0.1808 0.1735 0.2076 -0.0264 0.0331  0.0069  74  PRO   A CD  
1725 N  N   . LEU   A 75  ? 0.1523 0.1138 0.1645 -0.0015 0.0207  0.0068  75  LEU   A N   
1726 C  CA  . LEU   A 75  ? 0.1491 0.1149 0.1521 -0.0016 0.0099  0.0130  75  LEU   A CA  
1727 C  C   . LEU   A 75  ? 0.1621 0.1285 0.1508 0.0038  0.0097  0.0136  75  LEU   A C   
1728 O  O   . LEU   A 75  ? 0.1941 0.1480 0.1543 0.0113  0.0058  0.0083  75  LEU   A O   
1729 C  CB  . LEU   A 75  ? 0.1549 0.1234 0.1560 -0.0098 0.0075  0.0250  75  LEU   A CB  
1730 C  CG  . LEU   A 75  ? 0.1748 0.1560 0.1685 -0.0341 0.0040  0.0179  75  LEU   A CG  
1731 C  CD1 . LEU   A 75  ? 0.1859 0.2049 0.1783 -0.0296 0.0037  0.0032  75  LEU   A CD1 
1732 C  CD2 . LEU   A 75  ? 0.2001 0.1974 0.2223 -0.0099 0.0086  0.0156  75  LEU   A CD2 
1744 N  N   . LYS   A 76  ? 0.1638 0.1273 0.1640 -0.0065 0.0093  0.0014  76  LYS   A N   
1745 C  CA  . LYS   A 76  ? 0.1631 0.1474 0.1654 -0.0108 0.0089  -0.0122 76  LYS   A CA  
1746 C  C   . LYS   A 76  ? 0.1551 0.1335 0.1365 -0.0046 0.0110  0.0015  76  LYS   A C   
1747 O  O   . LYS   A 76  ? 0.1558 0.1299 0.1462 -0.0041 0.0166  0.0142  76  LYS   A O   
1748 C  CB  . LYS   A 76  ? 0.1648 0.1717 0.2113 0.0009  0.0107  -0.0372 76  LYS   A CB  
1749 C  CG  . LYS   A 76  ? 0.1735 0.1660 0.2540 0.0060  0.0088  -0.0329 76  LYS   A CG  
1750 C  CD  . LYS   A 76  ? 0.1808 0.1620 0.2948 0.0071  -0.0059 -0.0311 76  LYS   A CD  
1751 C  CE  . LYS   A 76  ? 0.1991 0.1845 0.3492 -0.0010 -0.0002 -0.0356 76  LYS   A CE  
1752 N  NZ  . LYS   A 76  ? 0.1980 0.1781 0.3847 -0.0163 -0.0025 -0.0471 76  LYS   A NZ  
1766 N  N   . VAL   A 77  ? 0.1664 0.1369 0.1404 -0.0054 0.0258  0.0140  77  VAL   A N   
1767 C  CA  . VAL   A 77  ? 0.1625 0.1387 0.1415 -0.0001 0.0154  0.0121  77  VAL   A CA  
1768 C  C   . VAL   A 77  ? 0.1571 0.1329 0.1399 0.0033  0.0122  0.0016  77  VAL   A C   
1769 O  O   . VAL   A 77  ? 0.1663 0.1365 0.1491 0.0078  0.0305  -0.0072 77  VAL   A O   
1770 C  CB  . VAL   A 77  ? 0.1802 0.1572 0.1452 0.0007  0.0107  0.0155  77  VAL   A CB  
1771 C  CG1 . VAL   A 77  ? 0.1768 0.1733 0.1646 0.0101  0.0006  0.0015  77  VAL   A CG1 
1772 C  CG2 . VAL   A 77  ? 0.2052 0.1667 0.1602 -0.0051 0.0078  0.0203  77  VAL   A CG2 
1782 N  N   . GLY   A 78  ? 0.1507 0.1314 0.1424 0.0019  0.0186  0.0067  78  GLY   A N   
1783 C  CA  . GLY   A 78  ? 0.1489 0.1261 0.1506 -0.0020 0.0244  0.0105  78  GLY   A CA  
1784 C  C   . GLY   A 78  ? 0.1378 0.1204 0.1526 0.0013  0.0229  0.0120  78  GLY   A C   
1785 O  O   . GLY   A 78  ? 0.1345 0.1289 0.1750 0.0001  0.0181  0.0282  78  GLY   A O   
1789 N  N   . GLY   A 79  ? 0.1417 0.1181 0.1533 0.0013  0.0178  0.0119  79  GLY   A N   
1790 C  CA  . GLY   A 79  ? 0.1408 0.1216 0.1669 -0.0021 0.0140  0.0114  79  GLY   A CA  
1791 C  C   . GLY   A 79  ? 0.1291 0.1153 0.1578 -0.0025 0.0127  0.0066  79  GLY   A C   
1792 O  O   . GLY   A 79  ? 0.1287 0.1260 0.1661 0.0147  0.0134  0.0057  79  GLY   A O   
1796 N  N   . SER   A 80  ? 0.1243 0.1308 0.1749 -0.0024 0.0174  -0.0013 80  SER   A N   
1797 C  CA  . SER   A 80  ? 0.1218 0.1264 0.1610 -0.0002 0.0070  0.0036  80  SER   A CA  
1798 C  C   . SER   A 80  ? 0.1174 0.1257 0.1636 -0.0066 0.0075  0.0136  80  SER   A C   
1799 O  O   . SER   A 80  ? 0.1196 0.1509 0.1943 0.0072  0.0136  0.0034  80  SER   A O   
1800 C  CB  . SER   A 80  ? 0.1399 0.1242 0.1836 -0.0052 0.0109  0.0115  80  SER   A CB  
1801 O  OG  . SER   A 80  ? 0.1602 0.1262 0.2243 0.0064  -0.0001 0.0220  80  SER   A OG  
1807 N  N   . CYS   A 81  ? 0.1123 0.1200 0.1679 -0.0049 -0.0033 0.0123  81  CYS   A N   
1808 C  CA  . CYS   A 81  ? 0.1132 0.1330 0.1604 -0.0067 -0.0083 0.0222  81  CYS   A CA  
1809 C  C   . CYS   A 81  ? 0.1149 0.1245 0.1590 -0.0094 -0.0030 0.0267  81  CYS   A C   
1810 O  O   . CYS   A 81  ? 0.1155 0.1547 0.1758 -0.0011 0.0017  0.0382  81  CYS   A O   
1811 C  CB  . CYS   A 81  ? 0.1202 0.1391 0.1714 -0.0113 -0.0029 0.0277  81  CYS   A CB  
1812 S  SG  . CYS   A 81  ? 0.1368 0.1280 0.1694 -0.0139 -0.0005 0.0149  81  CYS   A SG  
1818 N  N   . VAL   A 82  ? 0.1211 0.1342 0.1575 -0.0007 -0.0118 0.0212  82  VAL   A N   
1819 C  CA  . VAL   A 82  ? 0.1324 0.1413 0.1515 -0.0029 -0.0099 0.0254  82  VAL   A CA  
1820 C  C   . VAL   A 82  ? 0.1314 0.1441 0.1603 -0.0006 -0.0098 0.0288  82  VAL   A C   
1821 O  O   . VAL   A 82  ? 0.1229 0.1500 0.1883 -0.0040 -0.0039 0.0052  82  VAL   A O   
1822 C  CB  . VAL   A 82  ? 0.1614 0.1545 0.1645 0.0007  -0.0030 0.0280  82  VAL   A CB  
1823 C  CG1 . VAL   A 82  ? 0.1820 0.1667 0.1868 0.0051  0.0045  0.0299  82  VAL   A CG1 
1824 C  CG2 . VAL   A 82  ? 0.1710 0.1590 0.1967 -0.0028 -0.0022 0.0332  82  VAL   A CG2 
1834 N  N   . LEU   A 83  ? 0.1243 0.1405 0.1550 -0.0123 -0.0126 0.0201  83  LEU   A N   
1835 C  CA  . LEU   A 83  ? 0.1288 0.1422 0.1469 -0.0126 -0.0138 0.0098  83  LEU   A CA  
1836 C  C   . LEU   A 83  ? 0.1326 0.1438 0.1447 -0.0137 -0.0159 0.0217  83  LEU   A C   
1837 O  O   . LEU   A 83  ? 0.1387 0.1440 0.1663 -0.0171 -0.0134 0.0221  83  LEU   A O   
1838 C  CB  . LEU   A 83  ? 0.1357 0.1462 0.1568 -0.0143 -0.0150 0.0124  83  LEU   A CB  
1839 C  CG  . LEU   A 83  ? 0.1448 0.1546 0.1580 -0.0147 -0.0025 0.0078  83  LEU   A CG  
1840 C  CD1 . LEU   A 83  ? 0.1524 0.1584 0.1687 -0.0232 -0.0023 0.0203  83  LEU   A CD1 
1841 C  CD2 . LEU   A 83  ? 0.1434 0.1716 0.1673 -0.0131 0.0098  0.0176  83  LEU   A CD2 
1853 N  N   . SER   A 84  ? 0.1492 0.1505 0.1522 -0.0142 -0.0151 0.0259  84  SER   A N   
1854 C  CA  . SER   A 84  ? 0.1575 0.1576 0.1377 -0.0147 -0.0144 0.0207  84  SER   A CA  
1855 C  C   . SER   A 84  ? 0.1574 0.1552 0.1375 -0.0232 0.0004  0.0141  84  SER   A C   
1856 O  O   . SER   A 84  ? 0.1481 0.1662 0.1381 -0.0177 -0.0101 0.0149  84  SER   A O   
1857 C  CB  . SER   A 84  ? 0.1619 0.1788 0.1463 -0.0129 -0.0117 0.0102  84  SER   A CB  
1858 O  OG  . SER   A 84  ? 0.1647 0.1952 0.1541 -0.0098 -0.0225 -0.0009 84  SER   A OG  
1864 N  N   . GLY   A 85  ? 0.1716 0.1678 0.1373 -0.0238 0.0034  0.0113  85  GLY   A N   
1865 C  CA  . GLY   A 85  ? 0.1713 0.1755 0.1523 -0.0256 0.0115  -0.0010 85  GLY   A CA  
1866 C  C   . GLY   A 85  ? 0.1677 0.1815 0.1341 -0.0216 -0.0002 0.0046  85  GLY   A C   
1867 O  O   . GLY   A 85  ? 0.1676 0.1914 0.1489 -0.0302 0.0103  -0.0082 85  GLY   A O   
1871 N  N   . HIS   A 86  ? 0.1704 0.1759 0.1290 -0.0204 -0.0070 0.0042  86  HIS   A N   
1872 C  CA  . HIS   A 86  ? 0.1880 0.1845 0.1294 -0.0236 -0.0045 0.0037  86  HIS   A CA  
1873 C  C   . HIS   A 86  ? 0.2097 0.2007 0.1242 -0.0272 -0.0095 0.0020  86  HIS   A C   
1874 O  O   . HIS   A 86  ? 0.2197 0.2229 0.1290 -0.0215 0.0016  0.0032  86  HIS   A O   
1875 C  CB  . HIS   A 86  ? 0.1834 0.1734 0.1401 -0.0175 -0.0010 0.0097  86  HIS   A CB  
1876 C  CG  . HIS   A 86  ? 0.1762 0.1723 0.1401 -0.0113 -0.0034 0.0127  86  HIS   A CG  
1877 N  ND1 . HIS   A 86  ? 0.1807 0.1732 0.1729 -0.0205 -0.0030 0.0084  86  HIS   A ND1 
1878 C  CD2 . HIS   A 86  ? 0.1758 0.1708 0.1374 0.0000  0.0053  0.0188  86  HIS   A CD2 
1879 C  CE1 . HIS   A 86  ? 0.1758 0.1705 0.1678 -0.0167 0.0103  0.0146  86  HIS   A CE1 
1880 N  NE2 . HIS   A 86  ? 0.1753 0.1673 0.1561 0.0023  0.0089  0.0239  86  HIS   A NE2 
1888 N  N   . ASN   A 87  ? 0.2239 0.2068 0.1362 -0.0221 0.0134  -0.0073 87  ASN   A N   
1889 C  CA  . ASN   A 87  ? 0.2435 0.2170 0.1379 -0.0187 0.0297  -0.0106 87  ASN   A CA  
1890 C  C   . ASN   A 87  ? 0.2429 0.2320 0.1725 -0.0256 0.0524  -0.0005 87  ASN   A C   
1891 O  O   . ASN   A 87  ? 0.2626 0.2475 0.2109 -0.0371 0.0786  -0.0070 87  ASN   A O   
1892 C  CB  . ASN   A 87  ? 0.2597 0.2199 0.1485 -0.0086 0.0320  -0.0139 87  ASN   A CB  
1893 C  CG  . ASN   A 87  ? 0.2743 0.2314 0.1605 -0.0006 0.0456  -0.0085 87  ASN   A CG  
1894 O  OD1 . ASN   A 87  ? 0.2908 0.2269 0.1700 0.0169  0.0478  -0.0018 87  ASN   A OD1 
1895 N  ND2 . ASN   A 87  ? 0.2761 0.2560 0.1706 -0.0034 0.0481  -0.0037 87  ASN   A ND2 
1902 N  N   . LEU   A 88  ? 0.2155 0.2214 0.1695 -0.0314 0.0336  0.0125  88  LEU   A N   
1903 C  CA  . LEU   A 88  ? 0.1965 0.2206 0.1834 -0.0360 0.0322  0.0200  88  LEU   A CA  
1904 C  C   . LEU   A 88  ? 0.1894 0.2238 0.1685 -0.0381 0.0327  0.0311  88  LEU   A C   
1905 O  O   . LEU   A 88  ? 0.1909 0.2279 0.1985 -0.0369 0.0324  0.0464  88  LEU   A O   
1906 C  CB  . LEU   A 88  ? 0.1971 0.2270 0.1893 -0.0427 0.0019  0.0293  88  LEU   A CB  
1907 C  CG  . LEU   A 88  ? 0.2178 0.2418 0.2176 -0.0438 -0.0073 0.0315  88  LEU   A CG  
1908 C  CD1 . LEU   A 88  ? 0.2298 0.2484 0.2079 -0.0427 -0.0102 0.0291  88  LEU   A CD1 
1909 C  CD2 . LEU   A 88  ? 0.2299 0.2522 0.2556 -0.0397 -0.0051 0.0218  88  LEU   A CD2 
1921 N  N   . ALA   A 89  ? 0.1898 0.2147 0.1517 -0.0356 0.0148  0.0138  89  ALA   A N   
1922 C  CA  . ALA   A 89  ? 0.1945 0.2134 0.1380 -0.0297 0.0047  0.0222  89  ALA   A CA  
1923 C  C   . ALA   A 89  ? 0.2030 0.2133 0.1429 -0.0264 -0.0093 0.0217  89  ALA   A C   
1924 O  O   . ALA   A 89  ? 0.1967 0.2089 0.1733 -0.0329 -0.0145 -0.0040 89  ALA   A O   
1925 C  CB  . ALA   A 89  ? 0.1876 0.2097 0.1264 -0.0233 -0.0001 0.0221  89  ALA   A CB  
1931 N  N   . LYS   A 90  ? 0.2148 0.2281 0.1443 -0.0363 -0.0251 0.0292  90  LYS   A N   
1932 C  CA  . LYS   A 90  ? 0.2273 0.2431 0.1448 -0.0347 -0.0418 0.0305  90  LYS   A CA  
1933 C  C   . LYS   A 90  ? 0.2019 0.2231 0.1455 -0.0325 -0.0355 0.0171  90  LYS   A C   
1934 O  O   . LYS   A 90  ? 0.2054 0.2404 0.1738 -0.0338 -0.0382 0.0061  90  LYS   A O   
1935 C  CB  . LYS   A 90  ? 0.2615 0.2851 0.1839 -0.0353 -0.0475 0.0579  90  LYS   A CB  
1936 C  CG  . LYS   A 90  ? 0.3142 0.3324 0.2821 -0.0339 -0.0425 0.0666  90  LYS   A CG  
1937 C  CD  . LYS   A 90  ? 0.3728 0.3837 0.3869 -0.0360 -0.0252 0.0692  90  LYS   A CD  
1938 C  CE  . LYS   A 90  ? 0.4139 0.4226 0.4707 -0.0369 -0.0127 0.0653  90  LYS   A CE  
1939 N  NZ  . LYS   A 90  ? 0.4386 0.4415 0.5230 -0.0374 -0.0054 0.0624  90  LYS   A NZ  
1953 N  N   . HIS   A 91  ? 0.1839 0.1948 0.1252 -0.0292 -0.0363 0.0247  91  HIS   A N   
1954 C  CA  . HIS   A 91  ? 0.1691 0.1758 0.1315 -0.0184 -0.0306 0.0216  91  HIS   A CA  
1955 C  C   . HIS   A 91  ? 0.1500 0.1599 0.1227 -0.0186 -0.0161 0.0249  91  HIS   A C   
1956 O  O   . HIS   A 91  ? 0.1472 0.1749 0.1401 -0.0232 -0.0066 0.0239  91  HIS   A O   
1957 C  CB  . HIS   A 91  ? 0.1915 0.2061 0.1727 0.0035  -0.0411 0.0236  91  HIS   A CB  
1958 C  CG  . HIS   A 91  ? 0.2324 0.2565 0.2365 0.0156  -0.0705 0.0156  91  HIS   A CG  
1959 N  ND1 . HIS   A 91  ? 0.2440 0.2841 0.2768 0.0212  -0.0811 -0.0012 91  HIS   A ND1 
1960 C  CD2 . HIS   A 91  ? 0.2577 0.2780 0.2626 0.0192  -0.0822 0.0212  91  HIS   A CD2 
1961 C  CE1 . HIS   A 91  ? 0.2574 0.2948 0.2909 0.0245  -0.0834 0.0094  91  HIS   A CE1 
1962 N  NE2 . HIS   A 91  ? 0.2691 0.2936 0.2886 0.0267  -0.0866 0.0148  91  HIS   A NE2 
1970 N  N   . CYS   A 92  ? 0.1384 0.1516 0.1354 -0.0170 -0.0173 0.0240  92  CYS   A N   
1971 C  CA  . CYS   A 92  ? 0.1285 0.1463 0.1390 -0.0118 -0.0052 0.0159  92  CYS   A CA  
1972 C  C   . CYS   A 92  ? 0.1226 0.1405 0.1319 -0.0145 -0.0035 0.0171  92  CYS   A C   
1973 O  O   . CYS   A 92  ? 0.1234 0.1438 0.1580 -0.0187 -0.0042 0.0146  92  CYS   A O   
1974 C  CB  . CYS   A 92  ? 0.1323 0.1480 0.1462 -0.0047 -0.0082 0.0087  92  CYS   A CB  
1975 S  SG  . CYS   A 92  ? 0.1336 0.1355 0.1351 -0.0135 -0.0057 0.0146  92  CYS   A SG  
1981 N  N   . LEU   A 93  ? 0.1240 0.1261 0.1420 -0.0116 0.0032  0.0187  93  LEU   A N   
1982 C  CA  . LEU   A 93  ? 0.1147 0.1262 0.1444 -0.0082 0.0010  0.0144  93  LEU   A CA  
1983 C  C   . LEU   A 93  ? 0.1159 0.1157 0.1307 -0.0029 0.0006  0.0117  93  LEU   A C   
1984 O  O   . LEU   A 93  ? 0.1074 0.1273 0.1405 -0.0035 -0.0003 0.0156  93  LEU   A O   
1985 C  CB  . LEU   A 93  ? 0.1202 0.1291 0.1518 -0.0064 -0.0043 0.0221  93  LEU   A CB  
1986 C  CG  . LEU   A 93  ? 0.1277 0.1261 0.1543 -0.0042 -0.0019 0.0276  93  LEU   A CG  
1987 C  CD1 . LEU   A 93  ? 0.1360 0.1304 0.1856 -0.0020 0.0093  0.0163  93  LEU   A CD1 
1988 C  CD2 . LEU   A 93  ? 0.1400 0.1271 0.1765 -0.0118 -0.0032 0.0228  93  LEU   A CD2 
2000 N  N   . HIS   A 94  ? 0.1120 0.1113 0.1390 -0.0050 0.0034  0.0195  94  HIS   A N   
2001 C  CA  . HIS   A 94  ? 0.1134 0.1156 0.1360 -0.0081 -0.0025 0.0165  94  HIS   A CA  
2002 C  C   . HIS   A 94  ? 0.1057 0.1115 0.1472 -0.0086 0.0013  0.0136  94  HIS   A C   
2003 O  O   . HIS   A 94  ? 0.1094 0.1308 0.1805 -0.0007 0.0011  -0.0051 94  HIS   A O   
2004 C  CB  . HIS   A 94  ? 0.1090 0.1086 0.1406 -0.0077 -0.0026 0.0142  94  HIS   A CB  
2005 C  CG  . HIS   A 94  ? 0.1124 0.1144 0.1363 -0.0081 -0.0038 0.0198  94  HIS   A CG  
2006 N  ND1 . HIS   A 94  ? 0.1113 0.1124 0.1391 -0.0069 -0.0002 0.0171  94  HIS   A ND1 
2007 C  CD2 . HIS   A 94  ? 0.1208 0.1236 0.1454 -0.0106 -0.0078 0.0104  94  HIS   A CD2 
2008 C  CE1 . HIS   A 94  ? 0.1174 0.1194 0.1371 -0.0132 -0.0115 0.0149  94  HIS   A CE1 
2009 N  NE2 . HIS   A 94  ? 0.1252 0.1182 0.1464 -0.0120 -0.0058 0.0077  94  HIS   A NE2 
2017 N  N   . VAL   A 95  ? 0.1068 0.1072 0.1300 -0.0042 0.0063  0.0102  95  VAL   A N   
2018 C  CA  . VAL   A 95  ? 0.1168 0.1092 0.1268 -0.0079 0.0120  0.0102  95  VAL   A CA  
2019 C  C   . VAL   A 95  ? 0.1149 0.1107 0.1154 -0.0138 0.0039  0.0066  95  VAL   A C   
2020 O  O   . VAL   A 95  ? 0.1178 0.1231 0.1381 0.0066  0.0070  0.0076  95  VAL   A O   
2021 C  CB  . VAL   A 95  ? 0.1184 0.1121 0.1466 -0.0103 0.0089  0.0103  95  VAL   A CB  
2022 C  CG1 . VAL   A 95  ? 0.1324 0.1161 0.1547 -0.0199 0.0006  0.0042  95  VAL   A CG1 
2023 C  CG2 . VAL   A 95  ? 0.1225 0.1190 0.1531 -0.0128 0.0063  0.0241  95  VAL   A CG2 
2033 N  N   A VAL   A 96  ? 0.1191 0.1082 0.1169 -0.0061 0.0044  0.0123  96  VAL   A N   
2034 N  N   B VAL   A 96  ? 0.1202 0.1175 0.1100 -0.0085 0.0033  0.0081  96  VAL   A N   
2035 C  CA  A VAL   A 96  ? 0.1255 0.1097 0.1357 -0.0023 0.0074  0.0182  96  VAL   A CA  
2036 C  CA  B VAL   A 96  ? 0.1248 0.1265 0.1166 -0.0039 0.0056  0.0111  96  VAL   A CA  
2037 C  C   A VAL   A 96  ? 0.1295 0.1202 0.1334 -0.0050 0.0128  0.0134  96  VAL   A C   
2038 C  C   B VAL   A 96  ? 0.1274 0.1299 0.1172 0.0001  0.0083  0.0073  96  VAL   A C   
2039 O  O   A VAL   A 96  ? 0.1379 0.1273 0.1580 -0.0074 0.0171  0.0007  96  VAL   A O   
2040 O  O   B VAL   A 96  ? 0.1292 0.1321 0.1272 -0.0012 0.0130  -0.0008 96  VAL   A O   
2041 C  CB  A VAL   A 96  ? 0.1280 0.1129 0.1421 -0.0006 0.0164  0.0154  96  VAL   A CB  
2042 C  CB  B VAL   A 96  ? 0.1260 0.1307 0.1204 -0.0013 0.0093  0.0120  96  VAL   A CB  
2043 C  CG1 A VAL   A 96  ? 0.1456 0.1225 0.1410 0.0008  0.0114  0.0054  96  VAL   A CG1 
2044 C  CG1 B VAL   A 96  ? 0.1300 0.1370 0.1181 0.0001  0.0088  0.0038  96  VAL   A CG1 
2045 C  CG2 A VAL   A 96  ? 0.1241 0.1178 0.1564 -0.0088 0.0185  0.0008  96  VAL   A CG2 
2046 C  CG2 B VAL   A 96  ? 0.1277 0.1333 0.1261 -0.0072 0.0083  0.0169  96  VAL   A CG2 
2065 N  N   A GLY   A 97  ? 0.1285 0.1180 0.1401 -0.0106 0.0096  0.0089  97  GLY   A N   
2066 N  N   B GLY   A 97  ? 0.1312 0.1330 0.1275 0.0006  0.0019  0.0097  97  GLY   A N   
2067 C  CA  A GLY   A 97  ? 0.1357 0.1356 0.1401 -0.0101 -0.0002 0.0148  97  GLY   A CA  
2068 C  CA  B GLY   A 97  ? 0.1372 0.1373 0.1294 0.0031  -0.0024 0.0108  97  GLY   A CA  
2069 C  C   A GLY   A 97  ? 0.1335 0.1511 0.1317 -0.0132 0.0015  0.0121  97  GLY   A C   
2070 C  C   B GLY   A 97  ? 0.1406 0.1416 0.1259 0.0008  -0.0048 0.0101  97  GLY   A C   
2071 O  O   A GLY   A 97  ? 0.1441 0.1472 0.1556 -0.0133 0.0017  0.0172  97  GLY   A O   
2072 O  O   B GLY   A 97  ? 0.1405 0.1441 0.1285 0.0010  -0.0135 0.0108  97  GLY   A O   
2079 N  N   A PRO   A 98  ? 0.1434 0.1606 0.1166 -0.0075 -0.0035 0.0155  98  PRO   A N   
2080 N  N   B PRO   A 98  ? 0.1506 0.1394 0.1265 -0.0014 -0.0003 0.0127  98  PRO   A N   
2081 C  CA  A PRO   A 98  ? 0.1556 0.1816 0.1198 -0.0083 0.0024  0.0055  98  PRO   A CA  
2082 C  CA  B PRO   A 98  ? 0.1620 0.1437 0.1346 -0.0037 0.0023  0.0055  98  PRO   A CA  
2083 C  C   A PRO   A 98  ? 0.1556 0.1939 0.1099 -0.0175 0.0002  0.0197  98  PRO   A C   
2084 C  C   B PRO   A 98  ? 0.1782 0.1441 0.1267 -0.0051 0.0011  0.0125  98  PRO   A C   
2085 O  O   A PRO   A 98  ? 0.1446 0.1784 0.1365 -0.0094 0.0005  0.0191  98  PRO   A O   
2086 O  O   B PRO   A 98  ? 0.1768 0.1427 0.1452 -0.0051 0.0063  0.0076  98  PRO   A O   
2087 C  CB  A PRO   A 98  ? 0.1638 0.1893 0.1100 0.0021  -0.0089 -0.0056 98  PRO   A CB  
2088 C  CB  B PRO   A 98  ? 0.1610 0.1418 0.1368 -0.0000 0.0008  0.0041  98  PRO   A CB  
2089 C  CG  A PRO   A 98  ? 0.1600 0.1804 0.1349 0.0029  -0.0089 -0.0132 98  PRO   A CG  
2090 C  CG  B PRO   A 98  ? 0.1628 0.1429 0.1412 -0.0025 0.0027  0.0072  98  PRO   A CG  
2091 C  CD  A PRO   A 98  ? 0.1496 0.1650 0.1303 -0.0031 -0.0055 0.0015  98  PRO   A CD  
2092 C  CD  B PRO   A 98  ? 0.1541 0.1369 0.1297 -0.0010 0.0031  0.0120  98  PRO   A CD  
2107 N  N   A ASN   A 99  ? 0.1609 0.2175 0.1076 -0.0203 0.0020  0.0360  99  ASN   A N   
2108 N  N   B ASN   A 99  ? 0.1989 0.1446 0.1094 -0.0050 -0.0040 0.0230  99  ASN   A N   
2109 C  CA  A ASN   A 99  ? 0.1838 0.2391 0.1154 -0.0240 -0.0010 0.0488  99  ASN   A CA  
2110 C  CA  B ASN   A 99  ? 0.2215 0.1458 0.1053 -0.0035 -0.0061 0.0381  99  ASN   A CA  
2111 C  C   A ASN   A 99  ? 0.2061 0.2752 0.1212 -0.0466 -0.0058 0.0589  99  ASN   A C   
2112 C  C   B ASN   A 99  ? 0.2329 0.1522 0.1201 -0.0068 -0.0193 0.0376  99  ASN   A C   
2113 O  O   A ASN   A 99  ? 0.2148 0.2949 0.1277 -0.0401 -0.0148 0.0440  99  ASN   A O   
2114 O  O   B ASN   A 99  ? 0.2354 0.1365 0.1250 -0.0037 -0.0289 0.0197  99  ASN   A O   
2115 C  CB  A ASN   A 99  ? 0.1782 0.2297 0.1284 -0.0185 -0.0012 0.0468  99  ASN   A CB  
2116 C  CB  B ASN   A 99  ? 0.2308 0.1431 0.1144 0.0022  -0.0019 0.0421  99  ASN   A CB  
2117 C  CG  A ASN   A 99  ? 0.1735 0.2212 0.1451 -0.0106 -0.0096 0.0352  99  ASN   A CG  
2118 C  CG  B ASN   A 99  ? 0.2389 0.1477 0.1217 0.0031  0.0015  0.0454  99  ASN   A CG  
2119 O  OD1 A ASN   A 99  ? 0.1826 0.2340 0.1469 -0.0001 -0.0108 0.0184  99  ASN   A OD1 
2120 O  OD1 B ASN   A 99  ? 0.2413 0.1549 0.1029 0.0013  0.0028  0.0411  99  ASN   A OD1 
2121 N  ND2 A ASN   A 99  ? 0.1792 0.2154 0.1651 -0.0042 -0.0083 0.0482  99  ASN   A ND2 
2122 N  ND2 B ASN   A 99  ? 0.2422 0.1490 0.1484 0.0117  -0.0039 0.0366  99  ASN   A ND2 
2135 N  N   A VAL   A 100 ? 0.2272 0.2957 0.1391 -0.0671 -0.0307 0.0569  100 VAL   A N   
2136 N  N   B VAL   A 100 ? 0.2411 0.1815 0.1539 -0.0102 -0.0220 0.0441  100 VAL   A N   
2137 C  CA  A VAL   A 100 ? 0.2531 0.3199 0.1690 -0.0788 -0.0475 0.0566  100 VAL   A CA  
2138 C  CA  B VAL   A 100 ? 0.2486 0.2075 0.1929 -0.0118 -0.0203 0.0367  100 VAL   A CA  
2139 C  C   A VAL   A 100 ? 0.2638 0.3351 0.1665 -0.0814 -0.0573 0.0845  100 VAL   A C   
2140 C  C   B VAL   A 100 ? 0.2525 0.2184 0.1994 -0.0105 -0.0257 0.0335  100 VAL   A C   
2141 O  O   A VAL   A 100 ? 0.2674 0.3436 0.1853 -0.0804 -0.0343 0.0843  100 VAL   A O   
2142 O  O   B VAL   A 100 ? 0.2520 0.2143 0.1989 -0.0109 -0.0258 0.0223  100 VAL   A O   
2143 C  CB  A VAL   A 100 ? 0.2730 0.3238 0.2007 -0.0863 -0.0483 0.0390  100 VAL   A CB  
2144 C  CB  B VAL   A 100 ? 0.2527 0.2166 0.2236 -0.0085 -0.0154 0.0312  100 VAL   A CB  
2145 C  CG1 A VAL   A 100 ? 0.2737 0.3217 0.2173 -0.0945 -0.0489 0.0369  100 VAL   A CG1 
2146 C  CG1 B VAL   A 100 ? 0.2525 0.2174 0.2314 -0.0090 -0.0131 0.0327  100 VAL   A CG1 
2147 C  CG2 A VAL   A 100 ? 0.2832 0.3251 0.1936 -0.0880 -0.0462 0.0216  100 VAL   A CG2 
2148 C  CG2 B VAL   A 100 ? 0.2563 0.2185 0.2386 -0.0084 -0.0123 0.0263  100 VAL   A CG2 
2167 N  N   A ASN   A 101 ? 0.2755 0.3437 0.1782 -0.0844 -0.0667 0.1142  101 ASN   A N   
2168 N  N   B ASN   A 101 ? 0.2567 0.2276 0.2049 -0.0074 -0.0309 0.0365  101 ASN   A N   
2169 C  CA  A ASN   A 101 ? 0.2978 0.3481 0.2023 -0.0887 -0.0654 0.1332  101 ASN   A CA  
2170 C  CA  B ASN   A 101 ? 0.2635 0.2325 0.2052 -0.0030 -0.0303 0.0409  101 ASN   A CA  
2171 C  C   A ASN   A 101 ? 0.3269 0.3740 0.2391 -0.0896 -0.0324 0.1540  101 ASN   A C   
2172 C  C   B ASN   A 101 ? 0.2756 0.2417 0.2117 -0.0006 -0.0208 0.0504  101 ASN   A C   
2173 O  O   A ASN   A 101 ? 0.3398 0.3791 0.2807 -0.0839 -0.0310 0.1447  101 ASN   A O   
2174 O  O   B ASN   A 101 ? 0.2794 0.2395 0.2009 -0.0007 -0.0253 0.0620  101 ASN   A O   
2175 C  CB  A ASN   A 101 ? 0.2984 0.3297 0.2022 -0.0918 -0.0829 0.1248  101 ASN   A CB  
2176 C  CB  B ASN   A 101 ? 0.2578 0.2280 0.1996 -0.0027 -0.0332 0.0373  101 ASN   A CB  
2177 C  CG  A ASN   A 101 ? 0.3003 0.3126 0.2048 -0.0928 -0.0951 0.0937  101 ASN   A CG  
2178 C  CG  B ASN   A 101 ? 0.2553 0.2267 0.2050 -0.0025 -0.0347 0.0362  101 ASN   A CG  
2179 O  OD1 A ASN   A 101 ? 0.3004 0.3172 0.2167 -0.0788 -0.0941 0.0629  101 ASN   A OD1 
2180 O  OD1 B ASN   A 101 ? 0.2598 0.2270 0.2036 -0.0059 -0.0324 0.0375  101 ASN   A OD1 
2181 N  ND2 A ASN   A 101 ? 0.3034 0.2970 0.2117 -0.1035 -0.0924 0.0948  101 ASN   A ND2 
2182 N  ND2 B ASN   A 101 ? 0.2522 0.2266 0.2138 0.0003  -0.0336 0.0288  101 ASN   A ND2 
2195 N  N   A LYS   A 102 ? 0.3387 0.3991 0.2654 -0.0930 -0.0106 0.1500  102 LYS   A N   
2196 N  N   B LYS   A 102 ? 0.2842 0.2538 0.2393 -0.0015 -0.0026 0.0484  102 LYS   A N   
2197 C  CA  A LYS   A 102 ? 0.3548 0.4226 0.2781 -0.0911 -0.0106 0.1284  102 LYS   A CA  
2198 C  CA  B LYS   A 102 ? 0.2949 0.2647 0.2536 -0.0048 0.0098  0.0458  102 LYS   A CA  
2199 C  C   A LYS   A 102 ? 0.3626 0.4407 0.2592 -0.0829 -0.0130 0.1178  102 LYS   A C   
2200 C  C   B LYS   A 102 ? 0.2969 0.2643 0.2394 -0.0048 0.0053  0.0578  102 LYS   A C   
2201 O  O   A LYS   A 102 ? 0.3673 0.4517 0.2584 -0.0795 -0.0115 0.1088  102 LYS   A O   
2202 O  O   B LYS   A 102 ? 0.2978 0.2601 0.2301 -0.0058 0.0088  0.0699  102 LYS   A O   
2203 C  CB  A LYS   A 102 ? 0.3662 0.4274 0.3162 -0.0938 -0.0168 0.1063  102 LYS   A CB  
2204 C  CB  B LYS   A 102 ? 0.3051 0.2760 0.2912 -0.0074 0.0179  0.0302  102 LYS   A CB  
2205 C  CG  A LYS   A 102 ? 0.3772 0.4307 0.3445 -0.0943 -0.0267 0.0818  102 LYS   A CG  
2206 C  CG  B LYS   A 102 ? 0.3147 0.2856 0.3265 -0.0094 0.0226  0.0166  102 LYS   A CG  
2207 C  CD  A LYS   A 102 ? 0.3900 0.4350 0.3746 -0.0934 -0.0336 0.0560  102 LYS   A CD  
2208 C  CD  B LYS   A 102 ? 0.3238 0.2950 0.3597 -0.0122 0.0288  0.0069  102 LYS   A CD  
2209 C  CE  A LYS   A 102 ? 0.4006 0.4378 0.3981 -0.0910 -0.0367 0.0393  102 LYS   A CE  
2210 C  CE  B LYS   A 102 ? 0.3301 0.3025 0.3850 -0.0137 0.0307  0.0008  102 LYS   A CE  
2211 N  NZ  A LYS   A 102 ? 0.4055 0.4386 0.4093 -0.0916 -0.0362 0.0287  102 LYS   A NZ  
2212 N  NZ  B LYS   A 102 ? 0.3337 0.3070 0.3980 -0.0145 0.0323  -0.0001 102 LYS   A NZ  
2239 N  N   A GLY   A 103 ? 0.3640 0.4496 0.2652 -0.0742 -0.0197 0.0962  103 GLY   A N   
2240 N  N   B GLY   A 103 ? 0.2971 0.2696 0.2346 -0.0045 -0.0041 0.0560  103 GLY   A N   
2241 C  CA  A GLY   A 103 ? 0.3642 0.4532 0.2564 -0.0648 -0.0177 0.0798  103 GLY   A CA  
2242 C  CA  B GLY   A 103 ? 0.2960 0.2712 0.2264 -0.0056 -0.0103 0.0588  103 GLY   A CA  
2243 C  C   A GLY   A 103 ? 0.3583 0.4551 0.2546 -0.0588 -0.0082 0.0626  103 GLY   A C   
2244 C  C   B GLY   A 103 ? 0.2915 0.2689 0.2123 -0.0086 -0.0115 0.0603  103 GLY   A C   
2245 O  O   A GLY   A 103 ? 0.3683 0.4622 0.2748 -0.0551 -0.0062 0.0556  103 GLY   A O   
2246 O  O   B GLY   A 103 ? 0.2945 0.2682 0.2101 -0.0095 -0.0145 0.0682  103 GLY   A O   
2253 N  N   A GLU   A 104 ? 0.3367 0.4444 0.2145 -0.0617 0.0018  0.0533  104 GLU   A N   
2254 N  N   B GLU   A 104 ? 0.2824 0.2651 0.2004 -0.0104 -0.0158 0.0550  104 GLU   A N   
2255 C  CA  A GLU   A 104 ? 0.3112 0.4296 0.1816 -0.0695 0.0102  0.0426  104 GLU   A CA  
2256 C  CA  B GLU   A 104 ? 0.2739 0.2616 0.1886 -0.0142 -0.0201 0.0448  104 GLU   A CA  
2257 C  C   A GLU   A 104 ? 0.3098 0.4360 0.1817 -0.0676 0.0117  0.0178  104 GLU   A C   
2258 C  C   B GLU   A 104 ? 0.2759 0.2663 0.1979 -0.0103 -0.0163 0.0312  104 GLU   A C   
2259 O  O   A GLU   A 104 ? 0.3027 0.4379 0.1899 -0.0709 -0.0030 0.0143  104 GLU   A O   
2260 O  O   B GLU   A 104 ? 0.2726 0.2598 0.1996 -0.0090 -0.0180 0.0354  104 GLU   A O   
2261 C  CB  A GLU   A 104 ? 0.2823 0.4074 0.1591 -0.0793 0.0171  0.0602  104 GLU   A CB  
2262 C  CB  B GLU   A 104 ? 0.2646 0.2563 0.1815 -0.0207 -0.0261 0.0447  104 GLU   A CB  
2263 C  CG  A GLU   A 104 ? 0.2622 0.3894 0.1555 -0.0811 0.0108  0.0712  104 GLU   A CG  
2264 C  CG  B GLU   A 104 ? 0.2602 0.2570 0.1833 -0.0232 -0.0357 0.0429  104 GLU   A CG  
2265 C  CD  A GLU   A 104 ? 0.2417 0.3729 0.1608 -0.0838 0.0118  0.0779  104 GLU   A CD  
2266 C  CD  B GLU   A 104 ? 0.2566 0.2582 0.1865 -0.0233 -0.0443 0.0409  104 GLU   A CD  
2267 O  OE1 A GLU   A 104 ? 0.2261 0.3584 0.1338 -0.0825 0.0069  0.0732  104 GLU   A OE1 
2268 O  OE1 B GLU   A 104 ? 0.2556 0.2584 0.1867 -0.0215 -0.0476 0.0414  104 GLU   A OE1 
2269 O  OE2 A GLU   A 104 ? 0.2499 0.3715 0.1926 -0.0852 0.0182  0.0943  104 GLU   A OE2 
2270 O  OE2 B GLU   A 104 ? 0.2594 0.2593 0.1973 -0.0253 -0.0439 0.0388  104 GLU   A OE2 
2283 N  N   A ASP   A 105 ? 0.3155 0.4392 0.1905 -0.0635 0.0259  -0.0081 105 ASP   A N   
2284 N  N   B ASP   A 105 ? 0.2857 0.2797 0.2184 -0.0110 -0.0103 0.0127  105 ASP   A N   
2285 C  CA  A ASP   A 105 ? 0.3154 0.4397 0.2224 -0.0565 0.0354  -0.0383 105 ASP   A CA  
2286 C  CA  B ASP   A 105 ? 0.2939 0.2932 0.2474 -0.0095 -0.0019 -0.0107 105 ASP   A CA  
2287 C  C   A ASP   A 105 ? 0.2814 0.4195 0.1864 -0.0659 0.0249  -0.0588 105 ASP   A C   
2288 C  C   B ASP   A 105 ? 0.2928 0.2990 0.2435 -0.0164 0.0011  -0.0176 105 ASP   A C   
2289 O  O   A ASP   A 105 ? 0.2605 0.4077 0.1374 -0.0672 0.0249  -0.0821 105 ASP   A O   
2290 O  O   B ASP   A 105 ? 0.2890 0.2992 0.2295 -0.0159 0.0021  -0.0199 105 ASP   A O   
2291 C  CB  A ASP   A 105 ? 0.3450 0.4600 0.2936 -0.0425 0.0505  -0.0469 105 ASP   A CB  
2292 C  CB  B ASP   A 105 ? 0.3022 0.3011 0.2821 -0.0021 0.0025  -0.0255 105 ASP   A CB  
2293 C  CG  A ASP   A 105 ? 0.3695 0.4757 0.3564 -0.0301 0.0564  -0.0567 105 ASP   A CG  
2294 C  CG  B ASP   A 105 ? 0.3097 0.3068 0.3116 0.0052  0.0035  -0.0384 105 ASP   A CG  
2295 O  OD1 A ASP   A 105 ? 0.3759 0.4818 0.3691 -0.0289 0.0576  -0.0684 105 ASP   A OD1 
2296 O  OD1 B ASP   A 105 ? 0.3113 0.3062 0.3109 0.0060  0.0007  -0.0466 105 ASP   A OD1 
2297 O  OD2 A ASP   A 105 ? 0.3814 0.4816 0.3916 -0.0264 0.0597  -0.0511 105 ASP   A OD2 
2298 O  OD2 B ASP   A 105 ? 0.3148 0.3112 0.3329 0.0074  0.0029  -0.0389 105 ASP   A OD2 
2307 N  N   A ILE   A 106 ? 0.2655 0.4065 0.2085 -0.0718 0.0024  -0.0607 106 ILE   A N   
2308 N  N   B ILE   A 106 ? 0.2946 0.3043 0.2553 -0.0231 -0.0007 -0.0214 106 ILE   A N   
2309 C  CA  A ILE   A 106 ? 0.2407 0.3901 0.2240 -0.0822 -0.0201 -0.0718 106 ILE   A CA  
2310 C  CA  B ILE   A 106 ? 0.2941 0.3094 0.2676 -0.0323 -0.0024 -0.0261 106 ILE   A CA  
2311 C  C   A ILE   A 106 ? 0.2286 0.3641 0.2265 -0.1008 -0.0145 -0.0859 106 ILE   A C   
2312 C  C   B ILE   A 106 ? 0.2921 0.3039 0.2683 -0.0418 0.0055  -0.0319 106 ILE   A C   
2313 O  O   A ILE   A 106 ? 0.2075 0.3537 0.2258 -0.1100 -0.0017 -0.0849 106 ILE   A O   
2314 O  O   B ILE   A 106 ? 0.2894 0.3025 0.2653 -0.0425 0.0072  -0.0345 106 ILE   A O   
2315 C  CB  A ILE   A 106 ? 0.2395 0.4015 0.2682 -0.0661 -0.0399 -0.0478 106 ILE   A CB  
2316 C  CB  B ILE   A 106 ? 0.2967 0.3199 0.2880 -0.0304 -0.0106 -0.0185 106 ILE   A CB  
2317 C  CG1 A ILE   A 106 ? 0.2265 0.4032 0.3038 -0.0502 -0.0446 -0.0258 106 ILE   A CG1 
2318 C  CG1 B ILE   A 106 ? 0.2953 0.3237 0.3018 -0.0273 -0.0135 -0.0100 106 ILE   A CG1 
2319 C  CG2 A ILE   A 106 ? 0.2469 0.4057 0.2800 -0.0650 -0.0456 -0.0477 106 ILE   A CG2 
2320 C  CG2 B ILE   A 106 ? 0.2991 0.3233 0.2922 -0.0305 -0.0135 -0.0193 106 ILE   A CG2 
2321 C  CD1 A ILE   A 106 ? 0.2230 0.4019 0.3245 -0.0350 -0.0384 -0.0121 106 ILE   A CD1 
2322 C  CD1 B ILE   A 106 ? 0.2952 0.3245 0.3088 -0.0240 -0.0131 -0.0050 106 ILE   A CD1 
2345 N  N   A GLN   A 107 ? 0.2487 0.3496 0.2528 -0.0981 -0.0014 -0.0960 107 GLN   A N   
2346 N  N   B GLN   A 107 ? 0.2931 0.2983 0.2797 -0.0485 0.0142  -0.0345 107 GLN   A N   
2347 C  CA  A GLN   A 107 ? 0.2775 0.3359 0.3273 -0.0815 0.0195  -0.0900 107 GLN   A CA  
2348 C  CA  B GLN   A 107 ? 0.2936 0.2924 0.3035 -0.0525 0.0228  -0.0384 107 GLN   A CA  
2349 C  C   A GLN   A 107 ? 0.2534 0.2824 0.3052 -0.0689 0.0428  -0.0699 107 GLN   A C   
2350 C  C   B GLN   A 107 ? 0.2623 0.2636 0.2776 -0.0568 0.0363  -0.0471 107 GLN   A C   
2351 O  O   A GLN   A 107 ? 0.2594 0.2773 0.3547 -0.0616 0.0569  -0.0702 107 GLN   A O   
2352 O  O   B GLN   A 107 ? 0.2670 0.2631 0.2926 -0.0556 0.0400  -0.0492 107 GLN   A O   
2353 C  CB  A GLN   A 107 ? 0.3228 0.3725 0.4293 -0.0839 0.0115  -0.0919 107 GLN   A CB  
2354 C  CB  B GLN   A 107 ? 0.3221 0.3140 0.3560 -0.0542 0.0144  -0.0290 107 GLN   A CB  
2355 C  CG  A GLN   A 107 ? 0.3672 0.4092 0.5394 -0.0810 0.0035  -0.0836 107 GLN   A CG  
2356 C  CG  B GLN   A 107 ? 0.3466 0.3326 0.4104 -0.0551 0.0057  -0.0176 107 GLN   A CG  
2357 C  CD  A GLN   A 107 ? 0.4038 0.4363 0.6352 -0.0777 -0.0013 -0.0728 107 GLN   A CD  
2358 C  CD  B GLN   A 107 ? 0.3672 0.3487 0.4576 -0.0538 -0.0014 -0.0061 107 GLN   A CD  
2359 O  OE1 A GLN   A 107 ? 0.4177 0.4452 0.6725 -0.0767 -0.0025 -0.0700 107 GLN   A OE1 
2360 O  OE1 B GLN   A 107 ? 0.3750 0.3550 0.4702 -0.0535 -0.0028 -0.0010 107 GLN   A OE1 
2361 N  NE2 A GLN   A 107 ? 0.4144 0.4447 0.6666 -0.0772 -0.0044 -0.0705 107 GLN   A NE2 
2362 N  NE2 B GLN   A 107 ? 0.3734 0.3540 0.4729 -0.0533 -0.0057 -0.0018 107 GLN   A NE2 
2379 N  N   . LEU   A 108 ? 0.2259 0.2352 0.2448 -0.0618 0.0410  -0.0579 108 LEU   A N   
2380 C  CA  . LEU   A 108 ? 0.1931 0.1867 0.2125 -0.0280 0.0395  -0.0233 108 LEU   A CA  
2381 C  C   . LEU   A 108 ? 0.1640 0.1444 0.2048 -0.0100 0.0368  0.0026  108 LEU   A C   
2382 O  O   . LEU   A 108 ? 0.1585 0.1446 0.2211 -0.0018 0.0422  0.0045  108 LEU   A O   
2383 C  CB  . LEU   A 108 ? 0.1962 0.1954 0.1943 -0.0343 0.0458  -0.0172 108 LEU   A CB  
2384 C  CG  . LEU   A 108 ? 0.2108 0.2219 0.2190 -0.0286 0.0549  -0.0212 108 LEU   A CG  
2385 C  CD1 . LEU   A 108 ? 0.2271 0.2286 0.2157 -0.0353 0.0590  -0.0208 108 LEU   A CD1 
2386 C  CD2 . LEU   A 108 ? 0.2100 0.2439 0.2615 -0.0212 0.0534  -0.0135 108 LEU   A CD2 
2399 N  N   . LEU   A 109 ? 0.1462 0.1436 0.2015 -0.0002 0.0271  0.0110  109 LEU   A N   
2400 C  CA  . LEU   A 109 ? 0.1443 0.1340 0.1841 0.0032  0.0122  0.0137  109 LEU   A CA  
2401 C  C   . LEU   A 109 ? 0.1307 0.1272 0.1790 -0.0087 0.0141  0.0039  109 LEU   A C   
2402 O  O   . LEU   A 109 ? 0.1410 0.1186 0.1945 -0.0049 0.0027  0.0068  109 LEU   A O   
2403 C  CB  . LEU   A 109 ? 0.1507 0.1410 0.2054 0.0115  0.0047  0.0318  109 LEU   A CB  
2404 C  CG  . LEU   A 109 ? 0.1431 0.1467 0.2162 0.0059  0.0103  0.0326  109 LEU   A CG  
2405 C  CD1 . LEU   A 109 ? 0.1489 0.1408 0.2255 0.0039  0.0178  0.0135  109 LEU   A CD1 
2406 C  CD2 . LEU   A 109 ? 0.1417 0.1677 0.2380 0.0008  0.0073  0.0375  109 LEU   A CD2 
2418 N  N   . LYS   A 110 ? 0.1345 0.1260 0.1758 -0.0064 0.0068  0.0019  110 LYS   A N   
2419 C  CA  . LYS   A 110 ? 0.1312 0.1188 0.1821 -0.0105 -0.0005 0.0131  110 LYS   A CA  
2420 C  C   . LYS   A 110 ? 0.1308 0.1161 0.1790 -0.0121 0.0037  -0.0021 110 LYS   A C   
2421 O  O   . LYS   A 110 ? 0.1221 0.1185 0.1960 -0.0097 0.0095  -0.0068 110 LYS   A O   
2422 C  CB  . LYS   A 110 ? 0.1346 0.1270 0.2054 -0.0052 -0.0039 -0.0019 110 LYS   A CB  
2423 C  CG  . LYS   A 110 ? 0.1387 0.1261 0.2144 -0.0055 -0.0055 -0.0063 110 LYS   A CG  
2424 C  CD  . LYS   A 110 ? 0.1415 0.1320 0.2311 -0.0103 -0.0050 -0.0097 110 LYS   A CD  
2425 C  CE  . LYS   A 110 ? 0.1523 0.1396 0.2464 -0.0084 0.0108  -0.0162 110 LYS   A CE  
2426 N  NZ  . LYS   A 110 ? 0.1521 0.1457 0.2501 -0.0177 0.0176  -0.0127 110 LYS   A NZ  
2440 N  N   . SER   A 111 ? 0.1309 0.1199 0.1818 -0.0064 0.0038  0.0012  111 SER   A N   
2441 C  CA  . SER   A 111 ? 0.1260 0.1230 0.1882 -0.0047 0.0111  -0.0030 111 SER   A CA  
2442 C  C   . SER   A 111 ? 0.1210 0.1177 0.1821 -0.0098 0.0095  0.0055  111 SER   A C   
2443 O  O   . SER   A 111 ? 0.1337 0.1144 0.1940 -0.0066 0.0096  0.0070  111 SER   A O   
2444 C  CB  . SER   A 111 ? 0.1458 0.1440 0.1919 -0.0055 0.0162  -0.0079 111 SER   A CB  
2445 O  OG  . SER   A 111 ? 0.1919 0.1662 0.1995 0.0011  0.0260  -0.0159 111 SER   A OG  
2451 N  N   . ALA   A 112 ? 0.1274 0.1090 0.1836 -0.0044 0.0191  0.0063  112 ALA   A N   
2452 C  CA  . ALA   A 112 ? 0.1286 0.1128 0.1732 -0.0047 0.0215  0.0015  112 ALA   A CA  
2453 C  C   . ALA   A 112 ? 0.1237 0.1097 0.1813 -0.0064 0.0138  0.0027  112 ALA   A C   
2454 O  O   . ALA   A 112 ? 0.1244 0.1089 0.1896 -0.0124 0.0170  0.0102  112 ALA   A O   
2455 C  CB  . ALA   A 112 ? 0.1412 0.1190 0.1756 -0.0065 0.0175  0.0052  112 ALA   A CB  
2461 N  N   . TYR   A 113 ? 0.1154 0.1172 0.1846 -0.0037 0.0149  0.0119  113 TYR   A N   
2462 C  CA  . TYR   A 113 ? 0.1132 0.1134 0.1791 -0.0036 0.0130  0.0155  113 TYR   A CA  
2463 C  C   . TYR   A 113 ? 0.1110 0.1143 0.1795 -0.0136 0.0120  0.0096  113 TYR   A C   
2464 O  O   . TYR   A 113 ? 0.1146 0.1182 0.1878 -0.0068 0.0155  0.0087  113 TYR   A O   
2465 C  CB  . TYR   A 113 ? 0.1122 0.1248 0.1913 -0.0050 0.0064  0.0203  113 TYR   A CB  
2466 C  CG  . TYR   A 113 ? 0.1183 0.1219 0.1773 -0.0143 0.0109  0.0195  113 TYR   A CG  
2467 C  CD1 . TYR   A 113 ? 0.1221 0.1264 0.1697 -0.0027 0.0078  0.0259  113 TYR   A CD1 
2468 C  CD2 . TYR   A 113 ? 0.1204 0.1292 0.1743 -0.0156 0.0086  0.0157  113 TYR   A CD2 
2469 C  CE1 . TYR   A 113 ? 0.1262 0.1344 0.1683 -0.0050 0.0073  0.0240  113 TYR   A CE1 
2470 C  CE2 . TYR   A 113 ? 0.1221 0.1341 0.1751 -0.0123 0.0014  0.0214  113 TYR   A CE2 
2471 C  CZ  . TYR   A 113 ? 0.1215 0.1361 0.1649 -0.0008 0.0127  0.0252  113 TYR   A CZ  
2472 O  OH  . TYR   A 113 ? 0.1211 0.1431 0.1777 0.0064  0.0078  0.0261  113 TYR   A OH  
2482 N  N   . GLU   A 114 ? 0.1128 0.1119 0.1845 -0.0063 0.0162  0.0157  114 GLU   A N   
2483 C  CA  . GLU   A 114 ? 0.1199 0.1071 0.1913 0.0010  0.0115  0.0153  114 GLU   A CA  
2484 C  C   . GLU   A 114 ? 0.1160 0.1137 0.1800 -0.0034 0.0140  0.0101  114 GLU   A C   
2485 O  O   . GLU   A 114 ? 0.1266 0.1181 0.1849 -0.0026 0.0021  0.0107  114 GLU   A O   
2486 C  CB  . GLU   A 114 ? 0.1157 0.1126 0.1962 -0.0091 0.0089  0.0153  114 GLU   A CB  
2487 C  CG  . GLU   A 114 ? 0.1268 0.1157 0.2021 -0.0028 0.0116  0.0084  114 GLU   A CG  
2488 C  CD  . GLU   A 114 ? 0.1346 0.1158 0.2129 -0.0061 0.0041  0.0069  114 GLU   A CD  
2489 O  OE1 . GLU   A 114 ? 0.1345 0.1167 0.2140 -0.0110 0.0152  -0.0073 114 GLU   A OE1 
2490 O  OE2 . GLU   A 114 ? 0.1514 0.1219 0.2211 -0.0132 0.0115  -0.0068 114 GLU   A OE2 
2497 N  N   . ASN   A 115 ? 0.1169 0.1137 0.1692 -0.0080 0.0090  0.0076  115 ASN   A N   
2498 C  CA  . ASN   A 115 ? 0.1182 0.1194 0.1774 -0.0085 0.0124  0.0114  115 ASN   A CA  
2499 C  C   . ASN   A 115 ? 0.1227 0.1170 0.1665 -0.0117 0.0036  0.0090  115 ASN   A C   
2500 O  O   . ASN   A 115 ? 0.1219 0.1286 0.1729 -0.0116 0.0095  0.0185  115 ASN   A O   
2501 C  CB  . ASN   A 115 ? 0.1281 0.1286 0.1701 -0.0154 0.0151  0.0048  115 ASN   A CB  
2502 C  CG  . ASN   A 115 ? 0.1246 0.1425 0.1775 -0.0182 0.0226  0.0049  115 ASN   A CG  
2503 O  OD1 . ASN   A 115 ? 0.1311 0.2393 0.2072 -0.0184 0.0297  0.0228  115 ASN   A OD1 
2504 N  ND2 . ASN   A 115 ? 0.1291 0.1281 0.1784 -0.0161 0.0252  0.0140  115 ASN   A ND2 
2511 N  N   . PHE   A 116 ? 0.1159 0.1196 0.1789 -0.0055 0.0115  0.0207  116 PHE   A N   
2512 C  CA  . PHE   A 116 ? 0.1148 0.1281 0.1704 -0.0066 0.0146  0.0158  116 PHE   A CA  
2513 C  C   . PHE   A 116 ? 0.1155 0.1306 0.1762 -0.0132 0.0154  0.0222  116 PHE   A C   
2514 O  O   . PHE   A 116 ? 0.1234 0.1355 0.1798 -0.0006 0.0156  0.0257  116 PHE   A O   
2515 C  CB  . PHE   A 116 ? 0.1193 0.1189 0.1838 -0.0076 0.0189  0.0169  116 PHE   A CB  
2516 C  CG  . PHE   A 116 ? 0.1230 0.1177 0.1735 -0.0088 0.0122  0.0136  116 PHE   A CG  
2517 C  CD1 . PHE   A 116 ? 0.1221 0.1185 0.1697 -0.0096 0.0126  0.0124  116 PHE   A CD1 
2518 C  CD2 . PHE   A 116 ? 0.1256 0.1229 0.1834 -0.0069 0.0162  0.0200  116 PHE   A CD2 
2519 C  CE1 . PHE   A 116 ? 0.1255 0.1146 0.1819 -0.0180 0.0104  0.0076  116 PHE   A CE1 
2520 C  CE2 . PHE   A 116 ? 0.1230 0.1213 0.1891 -0.0080 0.0122  0.0069  116 PHE   A CE2 
2521 C  CZ  . PHE   A 116 ? 0.1271 0.1102 0.1781 -0.0076 0.0048  0.0079  116 PHE   A CZ  
2531 N  N   . ASN   A 117 ? 0.1188 0.1212 0.1858 -0.0073 0.0161  0.0249  117 ASN   A N   
2532 C  CA  . ASN   A 117 ? 0.1202 0.1206 0.1974 -0.0041 0.0156  0.0265  117 ASN   A CA  
2533 C  C   . ASN   A 117 ? 0.1206 0.1327 0.2082 -0.0022 0.0165  0.0249  117 ASN   A C   
2534 O  O   . ASN   A 117 ? 0.1290 0.1409 0.2216 -0.0073 -0.0035 0.0393  117 ASN   A O   
2535 C  CB  . ASN   A 117 ? 0.1196 0.1273 0.1988 -0.0029 0.0068  0.0290  117 ASN   A CB  
2536 C  CG  . ASN   A 117 ? 0.1180 0.1254 0.2013 -0.0022 0.0174  0.0325  117 ASN   A CG  
2537 O  OD1 . ASN   A 117 ? 0.1203 0.1445 0.2087 -0.0118 0.0150  0.0258  117 ASN   A OD1 
2538 N  ND2 . ASN   A 117 ? 0.1159 0.1245 0.2018 0.0007  0.0115  0.0276  117 ASN   A ND2 
2545 N  N   . GLN   A 118 ? 0.1181 0.1311 0.2151 -0.0103 0.0040  0.0333  118 GLN   A N   
2546 C  CA  . GLN   A 118 ? 0.1243 0.1432 0.2167 -0.0096 -0.0015 0.0266  118 GLN   A CA  
2547 C  C   . GLN   A 118 ? 0.1273 0.1508 0.2071 -0.0087 -0.0024 0.0351  118 GLN   A C   
2548 O  O   . GLN   A 118 ? 0.1268 0.1833 0.2250 -0.0040 -0.0123 0.0161  118 GLN   A O   
2549 C  CB  . GLN   A 118 ? 0.1227 0.1442 0.2263 -0.0056 0.0093  0.0316  118 GLN   A CB  
2550 C  CG  . GLN   A 118 ? 0.1233 0.1457 0.2251 -0.0057 0.0090  0.0328  118 GLN   A CG  
2551 C  CD  . GLN   A 118 ? 0.1199 0.1465 0.2339 -0.0026 0.0092  0.0288  118 GLN   A CD  
2552 O  OE1 . GLN   A 118 ? 0.1263 0.1575 0.2413 0.0093  -0.0019 0.0193  118 GLN   A OE1 
2553 N  NE2 . GLN   A 118 ? 0.1307 0.1458 0.2317 0.0018  0.0031  0.0305  118 GLN   A NE2 
2562 N  N   . HIS   A 119 ? 0.1315 0.1459 0.1901 -0.0061 -0.0001 0.0346  119 HIS   A N   
2563 C  CA  . HIS   A 119 ? 0.1422 0.1538 0.1851 -0.0086 -0.0009 0.0380  119 HIS   A CA  
2564 C  C   . HIS   A 119 ? 0.1498 0.1635 0.1745 -0.0118 0.0067  0.0404  119 HIS   A C   
2565 O  O   . HIS   A 119 ? 0.1522 0.1721 0.1886 -0.0291 -0.0021 0.0408  119 HIS   A O   
2566 C  CB  . HIS   A 119 ? 0.1441 0.1474 0.2016 -0.0064 0.0207  0.0343  119 HIS   A CB  
2567 C  CG  . HIS   A 119 ? 0.1454 0.1542 0.2365 -0.0014 0.0113  0.0429  119 HIS   A CG  
2568 N  ND1 . HIS   A 119 ? 0.1601 0.1769 0.2941 -0.0136 0.0109  0.0358  119 HIS   A ND1 
2569 C  CD2 . HIS   A 119 ? 0.1532 0.1667 0.2593 0.0119  0.0286  0.0582  119 HIS   A CD2 
2570 C  CE1 . HIS   A 119 ? 0.1538 0.1739 0.3068 -0.0175 0.0228  0.0520  119 HIS   A CE1 
2571 N  NE2 . HIS   A 119 ? 0.1609 0.1715 0.2994 0.0008  0.0385  0.0645  119 HIS   A NE2 
2579 N  N   . GLU   A 120 ? 0.1582 0.1854 0.1833 -0.0101 -0.0024 0.0615  120 GLU   A N   
2580 C  CA  . GLU   A 120 ? 0.1846 0.2190 0.2173 -0.0003 -0.0058 0.1040  120 GLU   A CA  
2581 C  C   . GLU   A 120 ? 0.1601 0.2030 0.1931 -0.0150 -0.0047 0.0925  120 GLU   A C   
2582 O  O   . GLU   A 120 ? 0.1559 0.1955 0.2128 -0.0186 -0.0086 0.0890  120 GLU   A O   
2583 C  CB  . GLU   A 120 ? 0.2646 0.2931 0.2794 0.0215  -0.0064 0.1532  120 GLU   A CB  
2584 C  CG  . GLU   A 120 ? 0.3635 0.3792 0.3963 0.0346  -0.0052 0.1557  120 GLU   A CG  
2585 C  CD  . GLU   A 120 ? 0.4529 0.4522 0.5173 0.0431  0.0044  0.1399  120 GLU   A CD  
2586 O  OE1 . GLU   A 120 ? 0.4796 0.4720 0.5444 0.0452  0.0077  0.1351  120 GLU   A OE1 
2587 O  OE2 . GLU   A 120 ? 0.5095 0.5095 0.5688 0.0450  0.0092  0.1322  120 GLU   A OE2 
2594 N  N   . VAL   A 121 ? 0.1580 0.2009 0.1758 -0.0172 0.0046  0.0714  121 VAL   A N   
2595 C  CA  . VAL   A 121 ? 0.1656 0.2031 0.1552 -0.0167 0.0145  0.0634  121 VAL   A CA  
2596 C  C   . VAL   A 121 ? 0.1497 0.1870 0.1393 -0.0245 0.0004  0.0434  121 VAL   A C   
2597 O  O   . VAL   A 121 ? 0.1517 0.1877 0.1675 -0.0294 -0.0147 0.0413  121 VAL   A O   
2598 C  CB  . VAL   A 121 ? 0.2049 0.2431 0.1919 -0.0037 0.0206  0.0649  121 VAL   A CB  
2599 C  CG1 . VAL   A 121 ? 0.2096 0.2604 0.1950 -0.0020 0.0323  0.0689  121 VAL   A CG1 
2600 C  CG2 . VAL   A 121 ? 0.2269 0.2565 0.2307 -0.0128 0.0198  0.0536  121 VAL   A CG2 
2610 N  N   . LEU   A 122 ? 0.1407 0.1657 0.1502 -0.0260 0.0044  0.0425  122 LEU   A N   
2611 C  CA  . LEU   A 122 ? 0.1490 0.1513 0.1533 -0.0216 0.0196  0.0351  122 LEU   A CA  
2612 C  C   . LEU   A 122 ? 0.1452 0.1490 0.1531 -0.0269 0.0098  0.0306  122 LEU   A C   
2613 O  O   . LEU   A 122 ? 0.1425 0.1589 0.1879 -0.0291 0.0059  0.0380  122 LEU   A O   
2614 C  CB  . LEU   A 122 ? 0.1644 0.1530 0.1860 -0.0131 0.0125  0.0424  122 LEU   A CB  
2615 C  CG  . LEU   A 122 ? 0.1676 0.1579 0.1916 -0.0096 0.0224  0.0342  122 LEU   A CG  
2616 C  CD1 . LEU   A 122 ? 0.1842 0.1594 0.2002 -0.0108 0.0236  0.0366  122 LEU   A CD1 
2617 C  CD2 . LEU   A 122 ? 0.1567 0.1451 0.1852 -0.0096 0.0345  0.0286  122 LEU   A CD2 
2629 N  N   . LEU   A 123 ? 0.1377 0.1488 0.1528 -0.0252 0.0011  0.0261  123 LEU   A N   
2630 C  CA  . LEU   A 123 ? 0.1392 0.1494 0.1424 -0.0231 0.0039  0.0247  123 LEU   A CA  
2631 C  C   . LEU   A 123 ? 0.1326 0.1418 0.1304 -0.0194 0.0072  0.0311  123 LEU   A C   
2632 O  O   . LEU   A 123 ? 0.1270 0.1533 0.1553 -0.0267 0.0056  0.0330  123 LEU   A O   
2633 C  CB  . LEU   A 123 ? 0.1475 0.1592 0.1435 -0.0268 0.0127  0.0231  123 LEU   A CB  
2634 C  CG  . LEU   A 123 ? 0.1508 0.1743 0.1562 -0.0220 0.0142  0.0137  123 LEU   A CG  
2635 C  CD1 . LEU   A 123 ? 0.1530 0.1855 0.1734 -0.0096 0.0191  0.0096  123 LEU   A CD1 
2636 C  CD2 . LEU   A 123 ? 0.1643 0.1791 0.1653 -0.0212 0.0060  0.0143  123 LEU   A CD2 
2648 N  N   A ALA   A 124 ? 0.1270 0.1307 0.1366 -0.0179 0.0141  0.0260  124 ALA   A N   
2649 N  N   B ALA   A 124 ? 0.1349 0.1403 0.1229 -0.0203 0.0032  0.0244  124 ALA   A N   
2650 C  CA  A ALA   A 124 ? 0.1188 0.1261 0.1500 -0.0143 0.0050  0.0254  124 ALA   A CA  
2651 C  CA  B ALA   A 124 ? 0.1362 0.1405 0.1260 -0.0231 -0.0023 0.0225  124 ALA   A CA  
2652 C  C   A ALA   A 124 ? 0.1133 0.1290 0.1562 -0.0144 0.0127  0.0231  124 ALA   A C   
2653 C  C   B ALA   A 124 ? 0.1388 0.1399 0.1251 -0.0196 -0.0031 0.0180  124 ALA   A C   
2654 O  O   A ALA   A 124 ? 0.1156 0.1334 0.1705 -0.0131 0.0206  0.0331  124 ALA   A O   
2655 O  O   B ALA   A 124 ? 0.1399 0.1420 0.1305 -0.0144 -0.0015 0.0200  124 ALA   A O   
2656 C  CB  A ALA   A 124 ? 0.1173 0.1221 0.1793 -0.0097 0.0015  0.0207  124 ALA   A CB  
2657 C  CB  B ALA   A 124 ? 0.1358 0.1401 0.1385 -0.0247 0.0017  0.0190  124 ALA   A CB  
2668 N  N   A PRO   A 125 ? 0.1105 0.1281 0.1547 -0.0117 0.0083  0.0344  125 PRO   A N   
2669 N  N   B PRO   A 125 ? 0.1401 0.1363 0.1219 -0.0168 -0.0062 0.0190  125 PRO   A N   
2670 C  CA  A PRO   A 125 ? 0.1187 0.1261 0.1575 -0.0059 0.0131  0.0277  125 PRO   A CA  
2671 C  CA  B PRO   A 125 ? 0.1438 0.1371 0.1228 -0.0125 -0.0023 0.0160  125 PRO   A CA  
2672 C  C   A PRO   A 125 ? 0.1095 0.1222 0.1606 -0.0074 0.0099  0.0282  125 PRO   A C   
2673 C  C   B PRO   A 125 ? 0.1414 0.1384 0.1304 -0.0079 0.0017  0.0181  125 PRO   A C   
2674 O  O   A PRO   A 125 ? 0.1139 0.1217 0.1717 0.0010  0.0009  0.0276  125 PRO   A O   
2675 O  O   B PRO   A 125 ? 0.1405 0.1428 0.1342 -0.0059 0.0079  0.0202  125 PRO   A O   
2676 C  CB  A PRO   A 125 ? 0.1328 0.1218 0.1470 -0.0111 0.0179  0.0211  125 PRO   A CB  
2677 C  CB  B PRO   A 125 ? 0.1463 0.1349 0.1214 -0.0154 -0.0013 0.0122  125 PRO   A CB  
2678 C  CG  A PRO   A 125 ? 0.1320 0.1209 0.1616 -0.0142 0.0147  0.0268  125 PRO   A CG  
2679 C  CG  B PRO   A 125 ? 0.1474 0.1341 0.1320 -0.0189 -0.0044 0.0119  125 PRO   A CG  
2680 C  CD  A PRO   A 125 ? 0.1185 0.1345 0.1582 -0.0181 0.0132  0.0323  125 PRO   A CD  
2681 C  CD  B PRO   A 125 ? 0.1415 0.1344 0.1256 -0.0200 -0.0050 0.0153  125 PRO   A CD  
2696 N  N   A LEU   A 126 ? 0.1040 0.1308 0.1563 -0.0005 0.0103  0.0230  126 LEU   A N   
2697 N  N   B LEU   A 126 ? 0.1447 0.1350 0.1401 -0.0052 -0.0030 0.0130  126 LEU   A N   
2698 C  CA  A LEU   A 126 ? 0.1162 0.1291 0.1688 -0.0053 0.0087  0.0267  126 LEU   A CA  
2699 C  CA  B LEU   A 126 ? 0.1449 0.1252 0.1465 -0.0019 0.0049  0.0083  126 LEU   A CA  
2700 C  C   A LEU   A 126 ? 0.1198 0.1266 0.1724 0.0004  0.0055  0.0222  126 LEU   A C   
2701 C  C   B LEU   A 126 ? 0.1392 0.1135 0.1424 0.0050  0.0121  0.0024  126 LEU   A C   
2702 O  O   A LEU   A 126 ? 0.1358 0.1242 0.2027 0.0087  0.0227  0.0334  126 LEU   A O   
2703 O  O   B LEU   A 126 ? 0.1502 0.1084 0.1563 0.0047  0.0203  0.0074  126 LEU   A O   
2704 C  CB  A LEU   A 126 ? 0.1260 0.1294 0.1782 -0.0045 0.0093  0.0188  126 LEU   A CB  
2705 C  CB  B LEU   A 126 ? 0.1499 0.1298 0.1650 -0.0068 0.0069  0.0020  126 LEU   A CB  
2706 C  CG  A LEU   A 126 ? 0.1223 0.1394 0.1951 -0.0055 0.0190  0.0154  126 LEU   A CG  
2707 C  CG  B LEU   A 126 ? 0.1507 0.1273 0.1756 -0.0052 0.0076  -0.0042 126 LEU   A CG  
2708 C  CD1 A LEU   A 126 ? 0.1262 0.1489 0.2312 -0.0120 0.0122  0.0225  126 LEU   A CD1 
2709 C  CD1 B LEU   A 126 ? 0.1537 0.1233 0.1840 -0.0048 0.0026  -0.0130 126 LEU   A CD1 
2710 C  CD2 A LEU   A 126 ? 0.1314 0.1415 0.1819 -0.0131 0.0155  0.0198  126 LEU   A CD2 
2711 C  CD2 B LEU   A 126 ? 0.1468 0.1282 0.1801 -0.0048 0.0018  -0.0001 126 LEU   A CD2 
2734 N  N   A LEU   A 127 ? 0.1212 0.1318 0.1553 -0.0001 0.0074  0.0184  127 LEU   A N   
2735 N  N   B LEU   A 127 ? 0.1285 0.1152 0.1300 0.0058  0.0094  0.0104  127 LEU   A N   
2736 C  CA  A LEU   A 127 ? 0.1197 0.1318 0.1442 -0.0020 0.0005  0.0152  127 LEU   A CA  
2737 C  CA  B LEU   A 127 ? 0.1206 0.1258 0.1291 0.0024  0.0045  0.0181  127 LEU   A CA  
2738 C  C   A LEU   A 127 ? 0.1182 0.1242 0.1410 -0.0030 0.0006  0.0110  127 LEU   A C   
2739 C  C   B LEU   A 127 ? 0.1222 0.1275 0.1363 -0.0028 0.0004  0.0117  127 LEU   A C   
2740 O  O   A LEU   A 127 ? 0.1261 0.1238 0.1548 -0.0120 -0.0030 0.0171  127 LEU   A O   
2741 O  O   B LEU   A 127 ? 0.1247 0.1285 0.1379 -0.0086 0.0108  0.0164  127 LEU   A O   
2742 C  CB  A LEU   A 127 ? 0.1278 0.1412 0.1532 0.0081  0.0037  0.0181  127 LEU   A CB  
2743 C  CB  B LEU   A 127 ? 0.1154 0.1365 0.1246 0.0034  0.0026  0.0145  127 LEU   A CB  
2744 C  CG  A LEU   A 127 ? 0.1343 0.1458 0.1663 0.0110  -0.0018 0.0231  127 LEU   A CG  
2745 C  CG  B LEU   A 127 ? 0.1151 0.1479 0.1233 0.0066  -0.0007 0.0233  127 LEU   A CG  
2746 C  CD1 A LEU   A 127 ? 0.1383 0.1402 0.1862 0.0050  -0.0036 0.0197  127 LEU   A CD1 
2747 C  CD1 B LEU   A 127 ? 0.1156 0.1514 0.1312 0.0080  0.0101  0.0248  127 LEU   A CD1 
2748 C  CD2 A LEU   A 127 ? 0.1441 0.1468 0.1828 0.0194  -0.0036 0.0223  127 LEU   A CD2 
2749 C  CD2 B LEU   A 127 ? 0.1196 0.1571 0.1184 0.0067  -0.0092 0.0160  127 LEU   A CD2 
2772 N  N   A SER   A 128 ? 0.1281 0.1224 0.1508 -0.0098 -0.0034 0.0188  128 SER   A N   
2773 N  N   B SER   A 128 ? 0.1262 0.1275 0.1435 -0.0091 -0.0109 0.0139  128 SER   A N   
2774 C  CA  A SER   A 128 ? 0.1421 0.1316 0.1430 -0.0034 0.0030  0.0178  128 SER   A CA  
2775 C  CA  B SER   A 128 ? 0.1281 0.1269 0.1305 -0.0093 -0.0178 0.0156  128 SER   A CA  
2776 C  C   A SER   A 128 ? 0.1478 0.1366 0.1503 -0.0008 0.0049  0.0187  128 SER   A C   
2777 C  C   B SER   A 128 ? 0.1263 0.1226 0.1233 -0.0094 -0.0300 0.0222  128 SER   A C   
2778 O  O   A SER   A 128 ? 0.1632 0.1529 0.1632 -0.0043 0.0102  0.0152  128 SER   A O   
2779 O  O   B SER   A 128 ? 0.1244 0.1227 0.1232 -0.0079 -0.0321 0.0188  128 SER   A O   
2780 C  CB  A SER   A 128 ? 0.1416 0.1414 0.1445 -0.0064 -0.0005 0.0227  128 SER   A CB  
2781 C  CB  B SER   A 128 ? 0.1291 0.1337 0.1289 -0.0115 -0.0132 0.0187  128 SER   A CB  
2782 O  OG  A SER   A 128 ? 0.1400 0.1479 0.1511 -0.0034 0.0024  0.0095  128 SER   A OG  
2783 O  OG  B SER   A 128 ? 0.1278 0.1383 0.1255 -0.0161 -0.0006 0.0268  128 SER   A OG  
2794 N  N   A ALA   A 129 ? 0.1410 0.1464 0.1676 -0.0024 0.0046  0.0314  129 ALA   A N   
2795 N  N   B ALA   A 129 ? 0.1261 0.1273 0.1263 -0.0066 -0.0310 0.0303  129 ALA   A N   
2796 C  CA  A ALA   A 129 ? 0.1380 0.1505 0.1766 0.0025  0.0066  0.0368  129 ALA   A CA  
2797 C  CA  B ALA   A 129 ? 0.1262 0.1329 0.1330 -0.0065 -0.0288 0.0261  129 ALA   A CA  
2798 C  C   A ALA   A 129 ? 0.1394 0.1431 0.1672 0.0026  -0.0021 0.0210  129 ALA   A C   
2799 C  C   B ALA   A 129 ? 0.1289 0.1383 0.1452 -0.0103 -0.0235 0.0216  129 ALA   A C   
2800 O  O   A ALA   A 129 ? 0.1400 0.1460 0.1626 -0.0030 0.0035  0.0208  129 ALA   A O   
2801 O  O   B ALA   A 129 ? 0.1285 0.1413 0.1415 -0.0162 -0.0203 0.0278  129 ALA   A O   
2802 C  CB  A ALA   A 129 ? 0.1403 0.1722 0.1896 0.0106  0.0109  0.0495  129 ALA   A CB  
2803 C  CB  B ALA   A 129 ? 0.1245 0.1401 0.1216 -0.0045 -0.0332 0.0186  129 ALA   A CB  
2814 N  N   A GLY   A 130 ? 0.1455 0.1410 0.1911 -0.0006 -0.0044 0.0179  130 GLY   A N   
2815 N  N   B GLY   A 130 ? 0.1321 0.1427 0.1599 -0.0097 -0.0169 0.0176  130 GLY   A N   
2816 C  CA  A GLY   A 130 ? 0.1641 0.1405 0.1828 0.0039  -0.0118 0.0156  130 GLY   A CA  
2817 C  CA  B GLY   A 130 ? 0.1399 0.1466 0.1645 -0.0048 -0.0088 0.0133  130 GLY   A CA  
2818 C  C   A GLY   A 130 ? 0.1716 0.1319 0.1642 0.0047  -0.0249 0.0076  130 GLY   A C   
2819 C  C   B GLY   A 130 ? 0.1488 0.1482 0.1652 -0.0021 -0.0057 0.0055  130 GLY   A C   
2820 O  O   A GLY   A 130 ? 0.1758 0.1171 0.1754 0.0081  -0.0302 0.0028  130 GLY   A O   
2821 O  O   B GLY   A 130 ? 0.1555 0.1468 0.1662 0.0007  0.0010  -0.0027 130 GLY   A O   
2828 N  N   A ILE   A 131 ? 0.1834 0.1303 0.1600 -0.0065 -0.0286 0.0111  131 ILE   A N   
2829 N  N   B ILE   A 131 ? 0.1542 0.1473 0.1686 -0.0059 -0.0162 0.0121  131 ILE   A N   
2830 C  CA  A ILE   A 131 ? 0.1947 0.1327 0.1432 -0.0150 -0.0377 0.0115  131 ILE   A CA  
2831 C  CA  B ILE   A 131 ? 0.1613 0.1452 0.1653 -0.0045 -0.0249 0.0146  131 ILE   A CA  
2832 C  C   A ILE   A 131 ? 0.1859 0.1366 0.1434 -0.0202 -0.0256 0.0253  131 ILE   A C   
2833 C  C   B ILE   A 131 ? 0.1595 0.1480 0.1590 -0.0070 -0.0210 0.0210  131 ILE   A C   
2834 O  O   A ILE   A 131 ? 0.1935 0.1407 0.1694 -0.0162 -0.0260 0.0240  131 ILE   A O   
2835 O  O   B ILE   A 131 ? 0.1624 0.1478 0.1647 -0.0039 -0.0193 0.0255  131 ILE   A O   
2836 C  CB  A ILE   A 131 ? 0.2123 0.1477 0.1436 -0.0251 -0.0377 0.0023  131 ILE   A CB  
2837 C  CB  B ILE   A 131 ? 0.1670 0.1482 0.1700 -0.0050 -0.0380 0.0096  131 ILE   A CB  
2838 C  CG1 A ILE   A 131 ? 0.2192 0.1803 0.1475 -0.0281 -0.0431 -0.0015 131 ILE   A CG1 
2839 C  CG1 B ILE   A 131 ? 0.1699 0.1554 0.1702 -0.0012 -0.0496 0.0114  131 ILE   A CG1 
2840 C  CG2 A ILE   A 131 ? 0.2242 0.1373 0.1600 -0.0198 -0.0334 -0.0146 131 ILE   A CG2 
2841 C  CG2 B ILE   A 131 ? 0.1677 0.1474 0.1744 -0.0064 -0.0439 0.0037  131 ILE   A CG2 
2842 C  CD1 A ILE   A 131 ? 0.2236 0.1943 0.1804 -0.0317 -0.0484 -0.0094 131 ILE   A CD1 
2843 C  CD1 B ILE   A 131 ? 0.1722 0.1551 0.1718 -0.0002 -0.0580 0.0090  131 ILE   A CD1 
2866 N  N   A PHE   A 132 ? 0.1726 0.1321 0.1412 -0.0166 -0.0202 0.0232  132 PHE   A N   
2867 N  N   B PHE   A 132 ? 0.1568 0.1494 0.1566 -0.0069 -0.0223 0.0194  132 PHE   A N   
2868 C  CA  A PHE   A 132 ? 0.1729 0.1361 0.1423 -0.0205 -0.0155 0.0159  132 PHE   A CA  
2869 C  CA  B PHE   A 132 ? 0.1610 0.1510 0.1572 -0.0088 -0.0207 0.0134  132 PHE   A CA  
2870 C  C   A PHE   A 132 ? 0.1740 0.1507 0.1483 -0.0230 -0.0189 0.0178  132 PHE   A C   
2871 C  C   B PHE   A 132 ? 0.1682 0.1597 0.1618 -0.0129 -0.0284 0.0157  132 PHE   A C   
2872 O  O   A PHE   A 132 ? 0.1797 0.1595 0.1534 -0.0283 -0.0116 0.0147  132 PHE   A O   
2873 O  O   B PHE   A 132 ? 0.1769 0.1648 0.1621 -0.0191 -0.0325 0.0144  132 PHE   A O   
2874 C  CB  A PHE   A 132 ? 0.1664 0.1296 0.1329 -0.0151 -0.0200 0.0282  132 PHE   A CB  
2875 C  CB  B PHE   A 132 ? 0.1558 0.1421 0.1417 -0.0031 -0.0151 0.0052  132 PHE   A CB  
2876 C  CG  A PHE   A 132 ? 0.1672 0.1292 0.1284 -0.0069 -0.0211 0.0269  132 PHE   A CG  
2877 C  CG  B PHE   A 132 ? 0.1529 0.1403 0.1299 0.0030  -0.0123 -0.0092 132 PHE   A CG  
2878 C  CD1 A PHE   A 132 ? 0.1658 0.1477 0.1437 -0.0021 -0.0117 0.0048  132 PHE   A CD1 
2879 C  CD1 B PHE   A 132 ? 0.1518 0.1468 0.1358 0.0074  -0.0072 -0.0186 132 PHE   A CD1 
2880 C  CD2 A PHE   A 132 ? 0.1665 0.1367 0.1386 -0.0027 -0.0169 0.0129  132 PHE   A CD2 
2881 C  CD2 B PHE   A 132 ? 0.1522 0.1380 0.1277 0.0081  -0.0092 -0.0239 132 PHE   A CD2 
2882 C  CE1 A PHE   A 132 ? 0.1673 0.1539 0.1545 -0.0001 -0.0214 -0.0012 132 PHE   A CE1 
2883 C  CE1 B PHE   A 132 ? 0.1505 0.1503 0.1387 0.0107  -0.0100 -0.0195 132 PHE   A CE1 
2884 C  CE2 A PHE   A 132 ? 0.1640 0.1437 0.1479 0.0029  -0.0199 0.0117  132 PHE   A CE2 
2885 C  CE2 B PHE   A 132 ? 0.1491 0.1437 0.1382 0.0133  -0.0113 -0.0251 132 PHE   A CE2 
2886 C  CZ  A PHE   A 132 ? 0.1619 0.1491 0.1534 -0.0048 -0.0205 0.0054  132 PHE   A CZ  
2887 C  CZ  B PHE   A 132 ? 0.1484 0.1475 0.1423 0.0102  -0.0098 -0.0231 132 PHE   A CZ  
2906 N  N   A GLY   A 133 ? 0.1775 0.1554 0.1466 -0.0178 -0.0322 0.0234  133 GLY   A N   
2907 N  N   B GLY   A 133 ? 0.1706 0.1626 0.1625 -0.0133 -0.0300 0.0121  133 GLY   A N   
2908 C  CA  A GLY   A 133 ? 0.1868 0.1676 0.1560 -0.0179 -0.0374 0.0157  133 GLY   A CA  
2909 C  CA  B GLY   A 133 ? 0.1727 0.1666 0.1615 -0.0119 -0.0240 0.0052  133 GLY   A CA  
2910 C  C   A GLY   A 133 ? 0.1909 0.1734 0.1548 -0.0143 -0.0462 0.0062  133 GLY   A C   
2911 C  C   B GLY   A 133 ? 0.1730 0.1710 0.1540 -0.0061 -0.0196 -0.0082 133 GLY   A C   
2912 O  O   A GLY   A 133 ? 0.2028 0.1849 0.1647 -0.0126 -0.0426 -0.0136 133 GLY   A O   
2913 O  O   B GLY   A 133 ? 0.1732 0.1747 0.1444 -0.0009 -0.0167 -0.0327 133 GLY   A O   
2920 N  N   A ALA   A 134 ? 0.1861 0.1610 0.1551 -0.0168 -0.0421 0.0048  134 ALA   A N   
2921 N  N   B ALA   A 134 ? 0.1740 0.1678 0.1565 -0.0050 -0.0156 -0.0052 134 ALA   A N   
2922 C  CA  A ALA   A 134 ? 0.1784 0.1584 0.1762 -0.0155 -0.0338 -0.0012 134 ALA   A CA  
2923 C  CA  B ALA   A 134 ? 0.1723 0.1634 0.1636 -0.0022 -0.0148 -0.0042 134 ALA   A CA  
2924 C  C   A ALA   A 134 ? 0.1766 0.1652 0.1736 -0.0144 -0.0278 0.0045  134 ALA   A C   
2925 C  C   B ALA   A 134 ? 0.1715 0.1577 0.1584 0.0013  -0.0152 -0.0032 134 ALA   A C   
2926 O  O   A ALA   A 134 ? 0.1959 0.1776 0.1891 -0.0218 -0.0102 0.0009  134 ALA   A O   
2927 O  O   B ALA   A 134 ? 0.1746 0.1585 0.1615 -0.0014 -0.0016 -0.0061 134 ALA   A O   
2928 C  CB  A ALA   A 134 ? 0.1849 0.1548 0.2074 -0.0127 -0.0284 -0.0085 134 ALA   A CB  
2929 C  CB  B ALA   A 134 ? 0.1725 0.1631 0.1758 -0.0024 -0.0160 -0.0051 134 ALA   A CB  
2940 N  N   A ASP   A 135 ? 0.1761 0.1649 0.1899 -0.0168 -0.0290 0.0092  135 ASP   A N   
2941 N  N   B ASP   A 135 ? 0.1746 0.1575 0.1605 -0.0013 -0.0207 -0.0004 135 ASP   A N   
2942 C  CA  A ASP   A 135 ? 0.1764 0.1735 0.2163 -0.0215 -0.0362 0.0129  135 ASP   A CA  
2943 C  CA  B ASP   A 135 ? 0.1748 0.1578 0.1721 -0.0060 -0.0222 -0.0040 135 ASP   A CA  
2944 C  C   A ASP   A 135 ? 0.1632 0.1584 0.2218 -0.0176 -0.0277 0.0280  135 ASP   A C   
2945 C  C   B ASP   A 135 ? 0.1642 0.1509 0.1726 -0.0000 -0.0144 -0.0144 135 ASP   A C   
2946 O  O   A ASP   A 135 ? 0.1553 0.1532 0.2273 -0.0099 -0.0245 0.0375  135 ASP   A O   
2947 O  O   B ASP   A 135 ? 0.1597 0.1471 0.1735 0.0023  -0.0116 -0.0097 135 ASP   A O   
2948 C  CB  A ASP   A 135 ? 0.2003 0.2002 0.2483 -0.0405 -0.0516 0.0004  135 ASP   A CB  
2949 C  CB  B ASP   A 135 ? 0.1820 0.1681 0.1799 -0.0127 -0.0326 -0.0033 135 ASP   A CB  
2950 C  CG  A ASP   A 135 ? 0.2192 0.2287 0.2893 -0.0584 -0.0588 0.0029  135 ASP   A CG  
2951 C  CG  B ASP   A 135 ? 0.1878 0.1791 0.1949 -0.0186 -0.0366 -0.0044 135 ASP   A CG  
2952 O  OD1 A ASP   A 135 ? 0.2141 0.2379 0.2871 -0.0629 -0.0671 0.0222  135 ASP   A OD1 
2953 O  OD1 B ASP   A 135 ? 0.1877 0.1775 0.2010 -0.0177 -0.0398 -0.0042 135 ASP   A OD1 
2954 O  OD2 A ASP   A 135 ? 0.2501 0.2518 0.3383 -0.0607 -0.0386 -0.0016 135 ASP   A OD2 
2955 O  OD2 B ASP   A 135 ? 0.1924 0.1881 0.2092 -0.0254 -0.0376 -0.0063 135 ASP   A OD2 
2964 N  N   A PRO   A 136 ? 0.1542 0.1499 0.2264 -0.0100 -0.0182 0.0374  136 PRO   A N   
2965 N  N   B PRO   A 136 ? 0.1612 0.1445 0.1739 0.0032  -0.0044 -0.0268 136 PRO   A N   
2966 C  CA  A PRO   A 136 ? 0.1458 0.1482 0.2308 -0.0135 -0.0100 0.0240  136 PRO   A CA  
2967 C  CA  B PRO   A 136 ? 0.1579 0.1525 0.1758 -0.0005 0.0028  -0.0308 136 PRO   A CA  
2968 C  C   A PRO   A 136 ? 0.1251 0.1451 0.2222 -0.0028 -0.0020 0.0161  136 PRO   A C   
2969 C  C   B PRO   A 136 ? 0.1526 0.1562 0.1672 0.0036  0.0016  -0.0254 136 PRO   A C   
2970 O  O   A PRO   A 136 ? 0.1186 0.1491 0.2171 -0.0101 0.0039  0.0213  136 PRO   A O   
2971 O  O   B PRO   A 136 ? 0.1520 0.1547 0.1545 0.0103  0.0129  -0.0245 136 PRO   A O   
2972 C  CB  A PRO   A 136 ? 0.1615 0.1478 0.2494 -0.0138 -0.0116 0.0191  136 PRO   A CB  
2973 C  CB  B PRO   A 136 ? 0.1647 0.1500 0.1843 -0.0009 0.0037  -0.0382 136 PRO   A CB  
2974 C  CG  A PRO   A 136 ? 0.1718 0.1537 0.2621 -0.0034 -0.0144 0.0208  136 PRO   A CG  
2975 C  CG  B PRO   A 136 ? 0.1702 0.1470 0.1851 0.0015  -0.0001 -0.0424 136 PRO   A CG  
2976 C  CD  A PRO   A 136 ? 0.1665 0.1500 0.2459 -0.0020 -0.0110 0.0355  136 PRO   A CD  
2977 C  CD  B PRO   A 136 ? 0.1645 0.1432 0.1791 0.0022  0.0012  -0.0342 136 PRO   A CD  
2992 N  N   A ILE   A 137 ? 0.1252 0.1420 0.2289 0.0015  -0.0091 0.0171  137 ILE   A N   
2993 N  N   B ILE   A 137 ? 0.1536 0.1535 0.1783 0.0022  -0.0094 -0.0231 137 ILE   A N   
2994 C  CA  A ILE   A 137 ? 0.1289 0.1459 0.2317 -0.0108 -0.0149 0.0248  137 ILE   A CA  
2995 C  CA  B ILE   A 137 ? 0.1554 0.1572 0.1856 0.0054  -0.0082 -0.0221 137 ILE   A CA  
2996 C  C   A ILE   A 137 ? 0.1307 0.1473 0.2102 -0.0148 -0.0155 0.0251  137 ILE   A C   
2997 C  C   B ILE   A 137 ? 0.1518 0.1565 0.1832 0.0031  0.0031  -0.0158 137 ILE   A C   
2998 O  O   A ILE   A 137 ? 0.1358 0.1467 0.2182 -0.0156 -0.0135 0.0226  137 ILE   A O   
2999 O  O   B ILE   A 137 ? 0.1479 0.1634 0.1899 0.0053  0.0087  -0.0077 137 ILE   A O   
3000 C  CB  A ILE   A 137 ? 0.1356 0.1594 0.2573 -0.0099 -0.0339 0.0279  137 ILE   A CB  
3001 C  CB  B ILE   A 137 ? 0.1610 0.1591 0.1989 0.0102  -0.0191 -0.0189 137 ILE   A CB  
3002 C  CG1 A ILE   A 137 ? 0.1478 0.1820 0.2978 -0.0056 -0.0354 0.0294  137 ILE   A CG1 
3003 C  CG1 B ILE   A 137 ? 0.1686 0.1644 0.2160 0.0139  -0.0312 -0.0172 137 ILE   A CG1 
3004 C  CG2 A ILE   A 137 ? 0.1427 0.1630 0.2662 -0.0174 -0.0373 0.0214  137 ILE   A CG2 
3005 C  CG2 B ILE   A 137 ? 0.1631 0.1560 0.2012 0.0126  -0.0196 -0.0207 137 ILE   A CG2 
3006 C  CD1 A ILE   A 137 ? 0.1660 0.1986 0.3221 0.0035  -0.0304 0.0253  137 ILE   A CD1 
3007 C  CD1 B ILE   A 137 ? 0.1749 0.1639 0.2222 0.0132  -0.0361 -0.0136 137 ILE   A CD1 
3030 N  N   A HIS   A 138 ? 0.1336 0.1516 0.1933 -0.0092 -0.0084 0.0178  138 HIS   A N   
3031 N  N   B HIS   A 138 ? 0.1499 0.1541 0.1801 0.0004  0.0053  -0.0210 138 HIS   A N   
3032 C  CA  A HIS   A 138 ? 0.1411 0.1589 0.1911 -0.0072 -0.0008 0.0147  138 HIS   A CA  
3033 C  CA  B HIS   A 138 ? 0.1486 0.1403 0.1709 -0.0044 0.0010  -0.0208 138 HIS   A CA  
3034 C  C   A HIS   A 138 ? 0.1352 0.1527 0.1911 -0.0026 -0.0015 0.0241  138 HIS   A C   
3035 C  C   B HIS   A 138 ? 0.1418 0.1260 0.1650 -0.0010 -0.0034 -0.0205 138 HIS   A C   
3036 O  O   A HIS   A 138 ? 0.1491 0.1540 0.1992 -0.0092 -0.0023 0.0284  138 HIS   A O   
3037 O  O   B HIS   A 138 ? 0.1449 0.1234 0.1675 0.0001  -0.0006 -0.0228 138 HIS   A O   
3038 C  CB  A HIS   A 138 ? 0.1595 0.1743 0.1888 -0.0067 -0.0133 0.0072  138 HIS   A CB  
3039 C  CB  B HIS   A 138 ? 0.1506 0.1456 0.1679 -0.0000 0.0033  -0.0305 138 HIS   A CB  
3040 C  CG  A HIS   A 138 ? 0.1771 0.1846 0.1924 -0.0139 -0.0110 0.0035  138 HIS   A CG  
3041 C  CG  B HIS   A 138 ? 0.1564 0.1523 0.1770 0.0026  0.0016  -0.0347 138 HIS   A CG  
3042 N  ND1 A HIS   A 138 ? 0.1863 0.1950 0.2201 -0.0124 -0.0059 -0.0038 138 HIS   A ND1 
3043 N  ND1 B HIS   A 138 ? 0.1620 0.1576 0.1920 0.0062  -0.0018 -0.0344 138 HIS   A ND1 
3044 C  CD2 A HIS   A 138 ? 0.1837 0.1927 0.1917 -0.0131 -0.0042 0.0081  138 HIS   A CD2 
3045 C  CD2 B HIS   A 138 ? 0.1567 0.1531 0.1780 0.0059  0.0011  -0.0336 138 HIS   A CD2 
3046 C  CE1 A HIS   A 138 ? 0.1948 0.2044 0.2205 -0.0012 -0.0031 0.0004  138 HIS   A CE1 
3047 C  CE1 B HIS   A 138 ? 0.1636 0.1587 0.1948 0.0092  -0.0023 -0.0289 138 HIS   A CE1 
3048 N  NE2 A HIS   A 138 ? 0.1906 0.2043 0.1964 -0.0030 0.0016  0.0048  138 HIS   A NE2 
3049 N  NE2 B HIS   A 138 ? 0.1604 0.1562 0.1877 0.0085  -0.0003 -0.0325 138 HIS   A NE2 
3064 N  N   A SER   A 139 ? 0.1227 0.1451 0.1896 -0.0003 0.0014  0.0228  139 SER   A N   
3065 N  N   B SER   A 139 ? 0.1370 0.1168 0.1633 -0.0023 -0.0063 -0.0127 139 SER   A N   
3066 C  CA  A SER   A 139 ? 0.1175 0.1399 0.1865 -0.0055 0.0051  0.0288  139 SER   A CA  
3067 C  CA  B SER   A 139 ? 0.1325 0.1214 0.1666 0.0007  0.0014  -0.0107 139 SER   A CA  
3068 C  C   A SER   A 139 ? 0.1162 0.1381 0.1910 -0.0094 0.0108  0.0249  139 SER   A C   
3069 C  C   B SER   A 139 ? 0.1305 0.1233 0.1702 -0.0011 0.0025  -0.0065 139 SER   A C   
3070 O  O   A SER   A 139 ? 0.1110 0.1297 0.1868 -0.0111 0.0082  0.0140  139 SER   A O   
3071 O  O   B SER   A 139 ? 0.1341 0.1117 0.1838 -0.0040 -0.0045 0.0020  139 SER   A O   
3072 C  CB  A SER   A 139 ? 0.1121 0.1391 0.1767 -0.0085 0.0086  0.0155  139 SER   A CB  
3073 C  CB  B SER   A 139 ? 0.1335 0.1168 0.1715 0.0016  0.0012  -0.0140 139 SER   A CB  
3074 O  OG  A SER   A 139 ? 0.1172 0.1328 0.1736 -0.0104 0.0067  0.0199  139 SER   A OG  
3075 O  OG  B SER   A 139 ? 0.1397 0.1146 0.1811 0.0019  0.0024  -0.0186 139 SER   A OG  
3086 N  N   A LEU   A 140 ? 0.1113 0.1507 0.1965 -0.0105 0.0066  0.0414  140 LEU   A N   
3087 N  N   B LEU   A 140 ? 0.1251 0.1388 0.1652 -0.0035 0.0005  0.0074  140 LEU   A N   
3088 C  CA  A LEU   A 140 ? 0.1142 0.1489 0.2043 -0.0140 0.0033  0.0395  140 LEU   A CA  
3089 C  CA  B LEU   A 140 ? 0.1236 0.1467 0.1634 -0.0065 -0.0017 0.0169  140 LEU   A CA  
3090 C  C   A LEU   A 140 ? 0.1093 0.1568 0.2051 -0.0172 0.0003  0.0368  140 LEU   A C   
3091 C  C   B LEU   A 140 ? 0.1211 0.1540 0.1785 -0.0105 -0.0018 0.0251  140 LEU   A C   
3092 O  O   A LEU   A 140 ? 0.1182 0.1559 0.2224 -0.0094 0.0023  0.0372  140 LEU   A O   
3093 O  O   B LEU   A 140 ? 0.1255 0.1543 0.1782 -0.0076 -0.0028 0.0280  140 LEU   A O   
3094 C  CB  A LEU   A 140 ? 0.1196 0.1561 0.2146 -0.0185 0.0049  0.0408  140 LEU   A CB  
3095 C  CB  B LEU   A 140 ? 0.1238 0.1526 0.1582 -0.0069 0.0003  0.0199  140 LEU   A CB  
3096 C  CG  A LEU   A 140 ? 0.1211 0.1728 0.2189 -0.0230 0.0078  0.0456  140 LEU   A CG  
3097 C  CG  B LEU   A 140 ? 0.1245 0.1590 0.1540 -0.0096 0.0022  0.0278  140 LEU   A CG  
3098 C  CD1 A LEU   A 140 ? 0.1272 0.1744 0.2276 -0.0124 0.0005  0.0401  140 LEU   A CD1 
3099 C  CD1 B LEU   A 140 ? 0.1232 0.1574 0.1499 -0.0100 0.0044  0.0297  140 LEU   A CD1 
3100 C  CD2 A LEU   A 140 ? 0.1304 0.1887 0.2203 -0.0207 0.0183  0.0444  140 LEU   A CD2 
3101 C  CD2 B LEU   A 140 ? 0.1278 0.1670 0.1588 -0.0076 0.0053  0.0287  140 LEU   A CD2 
3124 N  N   . ARG   A 141 ? 0.1207 0.1578 0.2014 -0.0147 -0.0004 0.0265  141 ARG   A N   
3125 C  CA  . ARG   A 141 ? 0.1347 0.1703 0.2131 -0.0256 -0.0051 0.0123  141 ARG   A CA  
3126 C  C   . ARG   A 141 ? 0.1328 0.1548 0.2047 -0.0205 -0.0031 0.0152  141 ARG   A C   
3127 O  O   . ARG   A 141 ? 0.1313 0.1525 0.2211 -0.0194 0.0044  0.0133  141 ARG   A O   
3128 C  CB  . ARG   A 141 ? 0.1446 0.1997 0.2308 -0.0315 -0.0081 -0.0093 141 ARG   A CB  
3129 C  CG  . ARG   A 141 ? 0.1823 0.2432 0.2660 -0.0347 0.0092  -0.0171 141 ARG   A CG  
3130 C  CD  . ARG   A 141 ? 0.2160 0.2766 0.3000 -0.0449 0.0127  -0.0231 141 ARG   A CD  
3131 N  NE  . ARG   A 141 ? 0.2091 0.3076 0.3194 -0.0500 -0.0027 -0.0228 141 ARG   A NE  
3132 C  CZ  . ARG   A 141 ? 0.2127 0.3319 0.3366 -0.0711 0.0111  -0.0127 141 ARG   A CZ  
3133 N  NH1 . ARG   A 141 ? 0.2005 0.3344 0.3220 -0.0891 0.0396  -0.0310 141 ARG   A NH1 
3134 N  NH2 . ARG   A 141 ? 0.2178 0.3483 0.3617 -0.0678 -0.0037 0.0000  141 ARG   A NH2 
3149 N  N   . VAL   A 142 ? 0.1269 0.1493 0.1898 -0.0156 -0.0043 0.0086  142 VAL   A N   
3150 C  CA  . VAL   A 142 ? 0.1299 0.1448 0.1860 -0.0134 0.0128  0.0059  142 VAL   A CA  
3151 C  C   . VAL   A 142 ? 0.1167 0.1421 0.1829 -0.0173 0.0083  0.0147  142 VAL   A C   
3152 O  O   . VAL   A 142 ? 0.1218 0.1459 0.1963 -0.0064 0.0076  0.0165  142 VAL   A O   
3153 C  CB  . VAL   A 142 ? 0.1381 0.1548 0.1861 -0.0152 0.0114  0.0087  142 VAL   A CB  
3154 C  CG1 . VAL   A 142 ? 0.1383 0.1477 0.1907 -0.0178 0.0180  0.0083  142 VAL   A CG1 
3155 C  CG2 . VAL   A 142 ? 0.1489 0.1712 0.1980 -0.0054 0.0166  0.0118  142 VAL   A CG2 
3165 N  N   . CYS   A 143 ? 0.1212 0.1418 0.1848 -0.0177 0.0060  0.0167  143 CYS   A N   
3166 C  CA  . CYS   A 143 ? 0.1169 0.1411 0.2025 -0.0168 0.0086  0.0230  143 CYS   A CA  
3167 C  C   . CYS   A 143 ? 0.1129 0.1382 0.2057 -0.0120 0.0053  0.0272  143 CYS   A C   
3168 O  O   . CYS   A 143 ? 0.1159 0.1418 0.2019 -0.0087 0.0062  0.0277  143 CYS   A O   
3169 C  CB  . CYS   A 143 ? 0.1282 0.1433 0.2022 -0.0128 0.0093  0.0297  143 CYS   A CB  
3170 S  SG  . CYS   A 143 ? 0.1450 0.1496 0.1882 0.0002  0.0111  0.0187  143 CYS   A SG  
3176 N  N   . VAL   A 144 ? 0.1171 0.1407 0.2222 -0.0120 0.0100  0.0352  144 VAL   A N   
3177 C  CA  . VAL   A 144 ? 0.1236 0.1488 0.2519 -0.0143 0.0184  0.0408  144 VAL   A CA  
3178 C  C   . VAL   A 144 ? 0.1281 0.1434 0.2457 -0.0253 -0.0097 0.0345  144 VAL   A C   
3179 O  O   . VAL   A 144 ? 0.1472 0.1474 0.2533 -0.0088 -0.0116 0.0376  144 VAL   A O   
3180 C  CB  . VAL   A 144 ? 0.1476 0.1725 0.3100 -0.0031 0.0343  0.0458  144 VAL   A CB  
3181 C  CG1 . VAL   A 144 ? 0.1632 0.1857 0.3483 -0.0156 0.0151  0.0485  144 VAL   A CG1 
3182 C  CG2 . VAL   A 144 ? 0.1298 0.1786 0.3233 -0.0071 0.0444  0.0569  144 VAL   A CG2 
3192 N  N   . ASP   A 145 ? 0.1309 0.1379 0.2526 -0.0167 -0.0020 0.0256  145 ASP   A N   
3193 C  CA  . ASP   A 145 ? 0.1443 0.1410 0.2561 -0.0181 -0.0034 0.0128  145 ASP   A CA  
3194 C  C   . ASP   A 145 ? 0.1453 0.1357 0.2523 -0.0136 -0.0011 0.0022  145 ASP   A C   
3195 O  O   . ASP   A 145 ? 0.1584 0.1436 0.3001 -0.0128 -0.0072 -0.0262 145 ASP   A O   
3196 C  CB  . ASP   A 145 ? 0.1566 0.1718 0.2722 -0.0253 -0.0144 0.0096  145 ASP   A CB  
3197 C  CG  . ASP   A 145 ? 0.1720 0.2088 0.2958 -0.0442 -0.0281 0.0188  145 ASP   A CG  
3198 O  OD1 . ASP   A 145 ? 0.1663 0.2264 0.3024 -0.0553 -0.0194 0.0204  145 ASP   A OD1 
3199 O  OD2 . ASP   A 145 ? 0.1956 0.2333 0.3080 -0.0522 -0.0472 0.0182  145 ASP   A OD2 
3204 N  N   . THR   A 146 ? 0.1295 0.1278 0.2140 -0.0162 0.0026  0.0108  146 THR   A N   
3205 C  CA  . THR   A 146 ? 0.1253 0.1253 0.2068 -0.0103 0.0019  0.0057  146 THR   A CA  
3206 C  C   . THR   A 146 ? 0.1203 0.1230 0.2180 -0.0030 0.0075  0.0153  146 THR   A C   
3207 O  O   . THR   A 146 ? 0.1327 0.1382 0.2253 0.0054  -0.0019 0.0144  146 THR   A O   
3208 C  CB  . THR   A 146 ? 0.1236 0.1311 0.2092 -0.0073 0.0031  0.0150  146 THR   A CB  
3209 O  OG1 . THR   A 146 ? 0.1205 0.1488 0.2141 -0.0020 -0.0005 0.0125  146 THR   A OG1 
3210 C  CG2 . THR   A 146 ? 0.1245 0.1322 0.2259 -0.0060 0.0029  0.0120  146 THR   A CG2 
3218 N  N   . VAL   A 147 ? 0.1199 0.1286 0.2149 -0.0024 0.0114  0.0208  147 VAL   A N   
3219 C  CA  . VAL   A 147 ? 0.1225 0.1318 0.2094 -0.0108 0.0194  0.0277  147 VAL   A CA  
3220 C  C   . VAL   A 147 ? 0.1217 0.1288 0.2270 -0.0121 0.0157  0.0341  147 VAL   A C   
3221 O  O   . VAL   A 147 ? 0.1261 0.1342 0.2437 -0.0172 0.0078  0.0356  147 VAL   A O   
3222 C  CB  . VAL   A 147 ? 0.1353 0.1329 0.1957 -0.0142 0.0172  0.0268  147 VAL   A CB  
3223 C  CG1 . VAL   A 147 ? 0.1591 0.1405 0.1977 -0.0105 0.0163  0.0357  147 VAL   A CG1 
3224 C  CG2 . VAL   A 147 ? 0.1458 0.1321 0.1951 -0.0128 0.0087  0.0243  147 VAL   A CG2 
3234 N  N   . ARG   A 148 ? 0.1230 0.1332 0.2283 -0.0115 0.0179  0.0449  148 ARG   A N   
3235 C  CA  . ARG   A 148 ? 0.1319 0.1373 0.2294 -0.0141 0.0088  0.0520  148 ARG   A CA  
3236 C  C   . ARG   A 148 ? 0.1407 0.1401 0.2235 -0.0169 0.0102  0.0664  148 ARG   A C   
3237 O  O   . ARG   A 148 ? 0.1679 0.1545 0.2406 -0.0234 0.0181  0.0556  148 ARG   A O   
3238 C  CB  . ARG   A 148 ? 0.1375 0.1395 0.2403 -0.0064 0.0205  0.0459  148 ARG   A CB  
3239 C  CG  . ARG   A 148 ? 0.1541 0.1416 0.2728 -0.0113 0.0360  0.0337  148 ARG   A CG  
3240 C  CD  . ARG   A 148 ? 0.1674 0.1386 0.2950 -0.0079 0.0423  0.0503  148 ARG   A CD  
3241 N  NE  . ARG   A 148 ? 0.1600 0.1422 0.2882 0.0061  0.0480  0.0542  148 ARG   A NE  
3242 C  CZ  . ARG   A 148 ? 0.1586 0.1327 0.2759 0.0030  0.0469  0.0450  148 ARG   A CZ  
3243 N  NH1 . ARG   A 148 ? 0.1671 0.1347 0.2801 -0.0110 0.0453  0.0195  148 ARG   A NH1 
3244 N  NH2 . ARG   A 148 ? 0.1510 0.1507 0.2811 0.0138  0.0514  0.0480  148 ARG   A NH2 
3258 N  N   . THR   A 149 ? 0.1381 0.1518 0.2149 -0.0182 -0.0004 0.0562  149 THR   A N   
3259 C  CA  . THR   A 149 ? 0.1442 0.1533 0.2153 -0.0148 -0.0000 0.0555  149 THR   A CA  
3260 C  C   . THR   A 149 ? 0.1399 0.1495 0.2082 -0.0207 0.0011  0.0560  149 THR   A C   
3261 O  O   . THR   A 149 ? 0.1401 0.1630 0.2188 -0.0253 0.0073  0.0506  149 THR   A O   
3262 C  CB  . THR   A 149 ? 0.1407 0.1617 0.2155 -0.0182 0.0050  0.0472  149 THR   A CB  
3263 O  OG1 . THR   A 149 ? 0.1425 0.1494 0.2273 -0.0260 0.0101  0.0348  149 THR   A OG1 
3264 C  CG2 . THR   A 149 ? 0.1449 0.1782 0.2249 -0.0103 -0.0082 0.0367  149 THR   A CG2 
3272 N  N   . ASN   A 150 ? 0.1430 0.1561 0.2045 -0.0140 -0.0029 0.0630  150 ASN   A N   
3273 C  CA  . ASN   A 150 ? 0.1568 0.1660 0.1987 -0.0180 0.0066  0.0551  150 ASN   A CA  
3274 C  C   . ASN   A 150 ? 0.1387 0.1557 0.1935 -0.0220 -0.0017 0.0518  150 ASN   A C   
3275 O  O   . ASN   A 150 ? 0.1491 0.1674 0.2289 -0.0189 -0.0136 0.0438  150 ASN   A O   
3276 C  CB  . ASN   A 150 ? 0.1985 0.1921 0.2184 -0.0275 0.0273  0.0709  150 ASN   A CB  
3277 C  CG  . ASN   A 150 ? 0.2549 0.2237 0.2844 -0.0231 0.0086  0.0720  150 ASN   A CG  
3278 O  OD1 . ASN   A 150 ? 0.2767 0.2297 0.3005 -0.0254 0.0090  0.0855  150 ASN   A OD1 
3279 N  ND2 . ASN   A 150 ? 0.2822 0.2454 0.3265 -0.0138 -0.0052 0.0666  150 ASN   A ND2 
3286 N  N   . VAL   A 151 ? 0.1372 0.1481 0.1873 -0.0219 0.0006  0.0455  151 VAL   A N   
3287 C  CA  . VAL   A 151 ? 0.1421 0.1497 0.1833 -0.0249 0.0005  0.0412  151 VAL   A CA  
3288 C  C   . VAL   A 151 ? 0.1349 0.1407 0.1922 -0.0309 0.0090  0.0449  151 VAL   A C   
3289 O  O   . VAL   A 151 ? 0.1420 0.1520 0.2271 -0.0259 0.0102  0.0356  151 VAL   A O   
3290 C  CB  . VAL   A 151 ? 0.1728 0.1619 0.1926 -0.0111 0.0043  0.0377  151 VAL   A CB  
3291 C  CG1 . VAL   A 151 ? 0.1698 0.1838 0.2110 -0.0096 0.0003  0.0337  151 VAL   A CG1 
3292 C  CG2 . VAL   A 151 ? 0.1840 0.1528 0.2015 -0.0050 0.0205  0.0358  151 VAL   A CG2 
3302 N  N   . TYR   A 152 ? 0.1356 0.1423 0.1989 -0.0282 0.0082  0.0453  152 TYR   A N   
3303 C  CA  . TYR   A 152 ? 0.1371 0.1516 0.1736 -0.0269 0.0038  0.0450  152 TYR   A CA  
3304 C  C   . TYR   A 152 ? 0.1328 0.1459 0.1724 -0.0240 0.0163  0.0409  152 TYR   A C   
3305 O  O   . TYR   A 152 ? 0.1446 0.1433 0.1759 -0.0304 0.0192  0.0379  152 TYR   A O   
3306 C  CB  . TYR   A 152 ? 0.1552 0.1654 0.1824 -0.0226 0.0141  0.0485  152 TYR   A CB  
3307 C  CG  . TYR   A 152 ? 0.1634 0.1866 0.1720 -0.0299 0.0201  0.0549  152 TYR   A CG  
3308 C  CD1 . TYR   A 152 ? 0.1783 0.2105 0.1951 -0.0167 0.0288  0.0571  152 TYR   A CD1 
3309 C  CD2 . TYR   A 152 ? 0.1691 0.1950 0.1741 -0.0417 0.0152  0.0497  152 TYR   A CD2 
3310 C  CE1 . TYR   A 152 ? 0.2121 0.2237 0.1980 -0.0098 0.0146  0.0678  152 TYR   A CE1 
3311 C  CE2 . TYR   A 152 ? 0.1999 0.2129 0.1909 -0.0412 0.0204  0.0562  152 TYR   A CE2 
3312 C  CZ  . TYR   A 152 ? 0.2257 0.2201 0.1901 -0.0274 0.0153  0.0776  152 TYR   A CZ  
3313 O  OH  . TYR   A 152 ? 0.2608 0.2374 0.2289 -0.0219 0.0147  0.0878  152 TYR   A OH  
3323 N  N   . LEU   A 153 ? 0.1307 0.1434 0.1843 -0.0264 0.0228  0.0414  153 LEU   A N   
3324 C  CA  . LEU   A 153 ? 0.1258 0.1374 0.1922 -0.0145 0.0150  0.0416  153 LEU   A CA  
3325 C  C   . LEU   A 153 ? 0.1303 0.1455 0.1952 -0.0120 0.0245  0.0358  153 LEU   A C   
3326 O  O   . LEU   A 153 ? 0.1351 0.1566 0.2266 -0.0141 0.0405  0.0337  153 LEU   A O   
3327 C  CB  . LEU   A 153 ? 0.1225 0.1390 0.1950 -0.0125 0.0119  0.0404  153 LEU   A CB  
3328 C  CG  . LEU   A 153 ? 0.1257 0.1425 0.1925 -0.0143 0.0157  0.0329  153 LEU   A CG  
3329 C  CD1 . LEU   A 153 ? 0.1447 0.1494 0.1943 -0.0117 0.0029  0.0347  153 LEU   A CD1 
3330 C  CD2 . LEU   A 153 ? 0.1378 0.1492 0.2005 -0.0154 0.0191  0.0115  153 LEU   A CD2 
3342 N  N   A ALA   A 154 ? 0.1262 0.1398 0.2042 -0.0091 0.0293  0.0374  154 ALA   A N   
3343 N  N   B ALA   A 154 ? 0.1358 0.1488 0.1716 -0.0074 0.0126  0.0342  154 ALA   A N   
3344 C  CA  A ALA   A 154 ? 0.1343 0.1410 0.2050 -0.0068 0.0314  0.0341  154 ALA   A CA  
3345 C  CA  B ALA   A 154 ? 0.1453 0.1545 0.1563 -0.0040 0.0003  0.0319  154 ALA   A CA  
3346 C  C   A ALA   A 154 ? 0.1289 0.1335 0.2008 -0.0039 0.0280  0.0359  154 ALA   A C   
3347 C  C   B ALA   A 154 ? 0.1499 0.1595 0.1419 -0.0085 -0.0063 0.0296  154 ALA   A C   
3348 O  O   A ALA   A 154 ? 0.1388 0.1496 0.1981 -0.0108 0.0308  0.0317  154 ALA   A O   
3349 O  O   B ALA   A 154 ? 0.1519 0.1619 0.1247 -0.0151 -0.0083 0.0283  154 ALA   A O   
3350 C  CB  A ALA   A 154 ? 0.1458 0.1478 0.2003 0.0029  0.0238  0.0282  154 ALA   A CB  
3351 C  CB  B ALA   A 154 ? 0.1467 0.1522 0.1538 0.0033  -0.0121 0.0329  154 ALA   A CB  
3362 N  N   A VAL   A 155 ? 0.1156 0.1174 0.1910 0.0011  0.0335  0.0469  155 VAL   A N   
3363 N  N   B VAL   A 155 ? 0.1541 0.1597 0.1476 -0.0079 -0.0078 0.0305  155 VAL   A N   
3364 C  CA  A VAL   A 155 ? 0.1339 0.1281 0.2200 -0.0031 0.0255  0.0500  155 VAL   A CA  
3365 C  CA  B VAL   A 155 ? 0.1718 0.1744 0.1693 -0.0054 -0.0199 0.0308  155 VAL   A CA  
3366 C  CA  T VAL   A 155 ? 0.1576 0.1575 0.1776 0.0031  0.0229  0.0368  155 VAL   A CA  
3367 C  C   A VAL   A 155 ? 0.1467 0.1376 0.2365 0.0125  0.0273  0.0571  155 VAL   A C   
3368 C  C   B VAL   A 155 ? 0.1903 0.1934 0.2003 0.0040  -0.0192 0.0365  155 VAL   A C   
3369 C  C   T VAL   A 155 ? 0.1587 0.1570 0.1748 0.0107  0.0250  0.0413  155 VAL   A C   
3370 O  O   A VAL   A 155 ? 0.1441 0.1421 0.2546 0.0172  0.0405  0.0433  155 VAL   A O   
3371 O  O   B VAL   A 155 ? 0.1859 0.1984 0.1935 0.0082  -0.0240 0.0293  155 VAL   A O   
3372 O  O   T VAL   A 155 ? 0.1526 0.1612 0.1674 0.0170  0.0196  0.0398  155 VAL   A O   
3373 C  CB  A VAL   A 155 ? 0.1423 0.1350 0.2317 -0.0059 0.0057  0.0412  155 VAL   A CB  
3374 C  CB  B VAL   A 155 ? 0.1702 0.1731 0.1678 -0.0073 -0.0330 0.0241  155 VAL   A CB  
3375 C  CB  T VAL   A 155 ? 0.1571 0.1594 0.1804 0.0011  0.0180  0.0326  155 VAL   A CB  
3376 C  CG1 A VAL   A 155 ? 0.1503 0.1461 0.2384 -0.0067 -0.0007 0.0445  155 VAL   A CG1 
3377 C  CG1 B VAL   A 155 ? 0.1688 0.1718 0.1624 -0.0131 -0.0418 0.0248  155 VAL   A CG1 
3378 C  CG1 T VAL   A 155 ? 0.1591 0.1624 0.1841 0.0006  0.0157  0.0343  155 VAL   A CG1 
3379 C  CG2 A VAL   A 155 ? 0.1548 0.1425 0.2459 -0.0034 -0.0146 0.0294  155 VAL   A CG2 
3380 C  CG2 B VAL   A 155 ? 0.1710 0.1743 0.1692 -0.0058 -0.0355 0.0216  155 VAL   A CG2 
3381 C  CG2 T VAL   A 155 ? 0.1593 0.1618 0.1835 0.0020  0.0114  0.0274  155 VAL   A CG2 
3407 N  N   A PHE   A 156 ? 0.1672 0.1482 0.2626 0.0153  0.0254  0.0760  156 PHE   A N   
3408 N  N   B PHE   A 156 ? 0.2139 0.2084 0.2323 0.0067  -0.0144 0.0458  156 PHE   A N   
3409 N  N   T PHE   A 156 ? 0.1690 0.1534 0.1815 0.0095  0.0328  0.0507  156 PHE   A N   
3410 C  CA  A PHE   A 156 ? 0.1920 0.1643 0.2879 0.0296  0.0159  0.0734  156 PHE   A CA  
3411 C  CA  B PHE   A 156 ? 0.2405 0.2283 0.2696 0.0068  -0.0078 0.0465  156 PHE   A CA  
3412 C  CA  T PHE   A 156 ? 0.1829 0.1504 0.1813 0.0119  0.0383  0.0546  156 PHE   A CA  
3413 C  C   A PHE   A 156 ? 0.1941 0.1718 0.2751 0.0446  0.0331  0.0840  156 PHE   A C   
3414 C  C   B PHE   A 156 ? 0.2549 0.2422 0.2876 0.0070  -0.0085 0.0491  156 PHE   A C   
3415 C  C   T PHE   A 156 ? 0.1854 0.1633 0.1879 0.0159  0.0468  0.0551  156 PHE   A C   
3416 O  O   A PHE   A 156 ? 0.2057 0.1789 0.2858 0.0364  0.0393  0.0712  156 PHE   A O   
3417 O  O   B PHE   A 156 ? 0.2604 0.2435 0.3003 0.0045  -0.0073 0.0515  156 PHE   A O   
3418 O  O   T PHE   A 156 ? 0.1905 0.1666 0.1948 0.0146  0.0498  0.0434  156 PHE   A O   
3419 C  CB  A PHE   A 156 ? 0.2110 0.1750 0.2968 0.0221  -0.0044 0.0769  156 PHE   A CB  
3420 C  CB  B PHE   A 156 ? 0.2510 0.2369 0.2803 0.0022  0.0002  0.0450  156 PHE   A CB  
3421 C  CB  T PHE   A 156 ? 0.1877 0.1353 0.1651 0.0087  0.0361  0.0606  156 PHE   A CB  
3422 C  CG  A PHE   A 156 ? 0.2342 0.1898 0.3244 0.0263  -0.0152 0.0619  156 PHE   A CG  
3423 C  CG  B PHE   A 156 ? 0.2599 0.2430 0.2902 -0.0001 0.0032  0.0401  156 PHE   A CG  
3424 C  CG  T PHE   A 156 ? 0.1925 0.1314 0.1603 0.0100  0.0353  0.0623  156 PHE   A CG  
3425 C  CD1 A PHE   A 156 ? 0.2411 0.1961 0.3380 0.0347  -0.0038 0.0476  156 PHE   A CD1 
3426 C  CD1 B PHE   A 156 ? 0.2612 0.2423 0.2921 0.0005  0.0038  0.0426  156 PHE   A CD1 
3427 C  CD1 T PHE   A 156 ? 0.1959 0.1323 0.1776 0.0115  0.0270  0.0543  156 PHE   A CD1 
3428 C  CD2 A PHE   A 156 ? 0.2457 0.2024 0.3372 0.0340  -0.0215 0.0626  156 PHE   A CD2 
3429 C  CD2 B PHE   A 156 ? 0.2622 0.2458 0.2913 -0.0045 0.0070  0.0371  156 PHE   A CD2 
3430 C  CD2 T PHE   A 156 ? 0.1955 0.1320 0.1678 0.0114  0.0343  0.0618  156 PHE   A CD2 
3431 C  CE1 A PHE   A 156 ? 0.2515 0.2025 0.3509 0.0366  -0.0004 0.0368  156 PHE   A CE1 
3432 C  CE1 B PHE   A 156 ? 0.2633 0.2423 0.2932 -0.0006 0.0025  0.0414  156 PHE   A CE1 
3433 C  CE1 T PHE   A 156 ? 0.1987 0.1342 0.1857 0.0146  0.0269  0.0433  156 PHE   A CE1 
3434 C  CE2 A PHE   A 156 ? 0.2581 0.2131 0.3500 0.0351  -0.0187 0.0434  156 PHE   A CE2 
3435 C  CE2 B PHE   A 156 ? 0.2624 0.2433 0.2897 -0.0064 0.0062  0.0364  156 PHE   A CE2 
3436 C  CE2 T PHE   A 156 ? 0.1999 0.1358 0.1805 0.0099  0.0316  0.0522  156 PHE   A CE2 
3437 C  CZ  A PHE   A 156 ? 0.2603 0.2125 0.3583 0.0367  -0.0071 0.0318  156 PHE   A CZ  
3438 C  CZ  B PHE   A 156 ? 0.2636 0.2429 0.2923 -0.0026 0.0028  0.0379  156 PHE   A CZ  
3439 C  CZ  T PHE   A 156 ? 0.1975 0.1303 0.1847 0.0093  0.0333  0.0456  156 PHE   A CZ  
3467 N  N   A ASP   A 157 ? 0.1947 0.1900 0.2561 0.0575  0.0343  0.0986  157 ASP   A N   
3468 N  N   B ASP   A 157 ? 0.2601 0.2504 0.2870 0.0089  -0.0166 0.0489  157 ASP   A N   
3469 N  N   T ASP   A 157 ? 0.1829 0.1795 0.1904 0.0228  0.0449  0.0640  157 ASP   A N   
3470 C  CA  A ASP   A 157 ? 0.2068 0.2198 0.2580 0.0617  0.0321  0.1001  157 ASP   A CA  
3471 C  CA  B ASP   A 157 ? 0.2663 0.2609 0.2883 0.0078  -0.0225 0.0514  157 ASP   A CA  
3472 C  CA  T ASP   A 157 ? 0.1833 0.1958 0.1958 0.0309  0.0421  0.0665  157 ASP   A CA  
3473 C  C   A ASP   A 157 ? 0.1831 0.2383 0.2633 0.0634  0.0388  0.1081  157 ASP   A C   
3474 C  C   B ASP   A 157 ? 0.2563 0.2586 0.2928 0.0042  -0.0236 0.0457  157 ASP   A C   
3475 C  C   T ASP   A 157 ? 0.1906 0.2142 0.2064 0.0324  0.0398  0.0664  157 ASP   A C   
3476 O  O   A ASP   A 157 ? 0.1696 0.2318 0.2513 0.0623  0.0384  0.1216  157 ASP   A O   
3477 O  O   B ASP   A 157 ? 0.2601 0.2639 0.3013 0.0051  -0.0206 0.0476  157 ASP   A O   
3478 O  O   T ASP   A 157 ? 0.1848 0.2146 0.2018 0.0351  0.0419  0.0669  157 ASP   A O   
3479 C  CB  A ASP   A 157 ? 0.2365 0.2299 0.2742 0.0694  0.0231  0.0844  157 ASP   A CB  
3480 C  CB  B ASP   A 157 ? 0.2796 0.2705 0.2864 0.0072  -0.0273 0.0553  157 ASP   A CB  
3481 C  CB  T ASP   A 157 ? 0.1757 0.1926 0.1943 0.0391  0.0420  0.0677  157 ASP   A CB  
3482 C  CG  A ASP   A 157 ? 0.2612 0.2380 0.3030 0.0795  0.0069  0.0763  157 ASP   A CG  
3483 C  CG  B ASP   A 157 ? 0.2912 0.2785 0.2867 0.0062  -0.0325 0.0590  157 ASP   A CG  
3484 C  CG  T ASP   A 157 ? 0.1648 0.1855 0.1909 0.0502  0.0381  0.0755  157 ASP   A CG  
3485 O  OD1 A ASP   A 157 ? 0.2851 0.2462 0.3356 0.0748  -0.0079 0.0663  157 ASP   A OD1 
3486 O  OD1 B ASP   A 157 ? 0.2921 0.2767 0.2765 0.0043  -0.0323 0.0679  157 ASP   A OD1 
3487 O  OD1 T ASP   A 157 ? 0.1616 0.1809 0.2004 0.0522  0.0402  0.0634  157 ASP   A OD1 
3488 O  OD2 A ASP   A 157 ? 0.2556 0.2332 0.3066 0.0825  0.0133  0.0817  157 ASP   A OD2 
3489 O  OD2 B ASP   A 157 ? 0.2980 0.2847 0.2988 0.0045  -0.0355 0.0537  157 ASP   A OD2 
3490 O  OD2 T ASP   A 157 ? 0.1529 0.1822 0.1743 0.0561  0.0353  0.0904  157 ASP   A OD2 
3503 N  N   A LYS   A 158 ? 0.1867 0.2652 0.2926 0.0626  0.0444  0.0891  158 LYS   A N   
3504 N  N   B LYS   A 158 ? 0.2433 0.2476 0.2804 -0.0036 -0.0289 0.0401  158 LYS   A N   
3505 N  N   T LYS   A 158 ? 0.2063 0.2328 0.2276 0.0308  0.0337  0.0570  158 LYS   A N   
3506 C  CA  A LYS   A 158 ? 0.1831 0.2883 0.3140 0.0663  0.0489  0.0747  158 LYS   A CA  
3507 C  CA  B LYS   A 158 ? 0.2354 0.2392 0.2680 -0.0126 -0.0191 0.0318  158 LYS   A CA  
3508 C  CA  T LYS   A 158 ? 0.2198 0.2499 0.2545 0.0294  0.0262  0.0451  158 LYS   A CA  
3509 C  C   A LYS   A 158 ? 0.1629 0.2952 0.2994 0.0690  0.0300  0.0733  158 LYS   A C   
3510 C  C   B LYS   A 158 ? 0.2118 0.2182 0.2278 -0.0243 -0.0258 0.0249  158 LYS   A C   
3511 C  C   T LYS   A 158 ? 0.2201 0.2554 0.2536 0.0285  0.0156  0.0383  158 LYS   A C   
3512 O  O   A LYS   A 158 ? 0.1548 0.3052 0.3018 0.0614  0.0396  0.0674  158 LYS   A O   
3513 O  O   B LYS   A 158 ? 0.2042 0.2121 0.2108 -0.0317 -0.0288 0.0307  158 LYS   A O   
3514 O  O   T LYS   A 158 ? 0.2194 0.2585 0.2548 0.0279  0.0146  0.0353  158 LYS   A O   
3515 C  CB  A LYS   A 158 ? 0.2097 0.3027 0.3549 0.0606  0.0730  0.0712  158 LYS   A CB  
3516 C  CB  B LYS   A 158 ? 0.2504 0.2553 0.2948 -0.0090 -0.0031 0.0330  158 LYS   A CB  
3517 C  CB  T LYS   A 158 ? 0.2356 0.2605 0.2873 0.0266  0.0307  0.0402  158 LYS   A CB  
3518 C  CG  A LYS   A 158 ? 0.2368 0.3179 0.3971 0.0544  0.0853  0.0749  158 LYS   A CG  
3519 C  CG  B LYS   A 158 ? 0.2612 0.2701 0.3207 -0.0062 0.0148  0.0367  158 LYS   A CG  
3520 C  CG  T LYS   A 158 ? 0.2504 0.2706 0.3187 0.0244  0.0325  0.0384  158 LYS   A CG  
3521 C  CD  A LYS   A 158 ? 0.2572 0.3300 0.4308 0.0505  0.1018  0.0824  158 LYS   A CD  
3522 C  CD  B LYS   A 158 ? 0.2695 0.2834 0.3438 -0.0042 0.0322  0.0420  158 LYS   A CD  
3523 C  CD  T LYS   A 158 ? 0.2631 0.2791 0.3490 0.0240  0.0333  0.0394  158 LYS   A CD  
3524 C  CE  A LYS   A 158 ? 0.2703 0.3378 0.4506 0.0457  0.1167  0.0925  158 LYS   A CE  
3525 C  CE  B LYS   A 158 ? 0.2737 0.2922 0.3599 -0.0012 0.0449  0.0479  158 LYS   A CE  
3526 C  CE  T LYS   A 158 ? 0.2720 0.2854 0.3712 0.0235  0.0334  0.0417  158 LYS   A CE  
3527 N  NZ  A LYS   A 158 ? 0.2753 0.3419 0.4629 0.0416  0.1249  0.0985  158 LYS   A NZ  
3528 N  NZ  B LYS   A 158 ? 0.2752 0.2963 0.3701 -0.0004 0.0511  0.0516  158 LYS   A NZ  
3529 N  NZ  T LYS   A 158 ? 0.2765 0.2882 0.3827 0.0231  0.0337  0.0431  158 LYS   A NZ  
3569 N  N   A ASN   A 159 ? 0.1612 0.2903 0.3050 0.0624  0.0039  0.0754  159 ASN   A N   
3570 N  N   B ASN   A 159 ? 0.2029 0.2116 0.2156 -0.0227 -0.0268 0.0125  159 ASN   A N   
3571 N  N   T ASN   A 159 ? 0.2230 0.2553 0.2601 0.0237  0.0083  0.0342  159 ASN   A N   
3572 C  CA  A ASN   A 159 ? 0.1604 0.2856 0.3027 0.0518  -0.0188 0.0813  159 ASN   A CA  
3573 C  CA  B ASN   A 159 ? 0.1982 0.2106 0.2085 -0.0182 -0.0226 0.0064  159 ASN   A CA  
3574 C  CA  T ASN   A 159 ? 0.2266 0.2549 0.2627 0.0170  0.0030  0.0325  159 ASN   A CA  
3575 C  C   A ASN   A 159 ? 0.1405 0.2782 0.2834 0.0364  -0.0131 0.0774  159 ASN   A C   
3576 C  C   B ASN   A 159 ? 0.1861 0.2019 0.1961 -0.0261 -0.0245 0.0029  159 ASN   A C   
3577 C  C   T ASN   A 159 ? 0.2244 0.2513 0.2534 0.0121  0.0066  0.0304  159 ASN   A C   
3578 O  O   A ASN   A 159 ? 0.1218 0.2713 0.2884 0.0292  -0.0268 0.0618  159 ASN   A O   
3579 O  O   B ASN   A 159 ? 0.1834 0.2018 0.1997 -0.0330 -0.0278 0.0075  159 ASN   A O   
3580 O  O   T ASN   A 159 ? 0.2245 0.2492 0.2551 0.0093  0.0060  0.0260  159 ASN   A O   
3581 C  CB  A ASN   A 159 ? 0.1827 0.2917 0.3318 0.0499  -0.0293 0.0871  159 ASN   A CB  
3582 C  CB  B ASN   A 159 ? 0.2078 0.2213 0.2245 -0.0065 -0.0149 0.0052  159 ASN   A CB  
3583 C  CB  T ASN   A 159 ? 0.2331 0.2583 0.2804 0.0145  -0.0018 0.0342  159 ASN   A CB  
3584 C  CG  A ASN   A 159 ? 0.2051 0.3024 0.3653 0.0436  -0.0272 0.0835  159 ASN   A CG  
3585 C  CG  B ASN   A 159 ? 0.2157 0.2319 0.2464 -0.0046 -0.0032 0.0015  159 ASN   A CG  
3586 C  CG  T ASN   A 159 ? 0.2395 0.2623 0.2981 0.0119  -0.0036 0.0339  159 ASN   A CG  
3587 O  OD1 A ASN   A 159 ? 0.2165 0.3127 0.3805 0.0387  -0.0193 0.0749  159 ASN   A OD1 
3588 O  OD1 B ASN   A 159 ? 0.2238 0.2406 0.2576 -0.0040 -0.0016 -0.0015 159 ASN   A OD1 
3589 O  OD1 T ASN   A 159 ? 0.2422 0.2662 0.3067 0.0110  -0.0005 0.0301  159 ASN   A OD1 
3590 N  ND2 A ASN   A 159 ? 0.2147 0.3074 0.3855 0.0396  -0.0247 0.0792  159 ASN   A ND2 
3591 N  ND2 B ASN   A 159 ? 0.2158 0.2357 0.2544 -0.0047 -0.0016 0.0039  159 ASN   A ND2 
3592 N  ND2 T ASN   A 159 ? 0.2425 0.2646 0.3065 0.0102  -0.0052 0.0339  159 ASN   A ND2 
3611 N  N   A LEU   A 160 ? 0.1356 0.2720 0.2554 0.0301  -0.0165 0.0956  160 LEU   A N   
3612 N  N   B LEU   A 160 ? 0.1840 0.2000 0.1918 -0.0192 -0.0214 0.0093  160 LEU   A N   
3613 N  N   T LEU   A 160 ? 0.2204 0.2474 0.2443 0.0098  0.0053  0.0342  160 LEU   A N   
3614 C  CA  A LEU   A 160 ? 0.1316 0.2649 0.2331 0.0182  0.0072  0.1083  160 LEU   A CA  
3615 C  CA  B LEU   A 160 ? 0.1919 0.2070 0.2032 -0.0066 -0.0057 0.0163  160 LEU   A CA  
3616 C  CA  T LEU   A 160 ? 0.2176 0.2427 0.2368 0.0068  0.0099  0.0385  160 LEU   A CA  
3617 C  C   A LEU   A 160 ? 0.1268 0.2660 0.2120 0.0163  0.0232  0.1000  160 LEU   A C   
3618 C  C   B LEU   A 160 ? 0.1835 0.2137 0.1974 0.0067  0.0011  0.0291  160 LEU   A C   
3619 O  O   A LEU   A 160 ? 0.1216 0.2672 0.2207 0.0186  0.0230  0.0990  160 LEU   A O   
3620 O  O   B LEU   A 160 ? 0.1816 0.2145 0.2035 0.0114  0.0002  0.0274  160 LEU   A O   
3621 C  CB  A LEU   A 160 ? 0.1389 0.2617 0.2260 0.0156  0.0143  0.1193  160 LEU   A CB  
3622 C  CB  B LEU   A 160 ? 0.2063 0.2130 0.2259 -0.0050 0.0103  0.0097  160 LEU   A CB  
3623 C  CB  T LEU   A 160 ? 0.2156 0.2395 0.2305 0.0061  0.0153  0.0415  160 LEU   A CB  
3624 C  CG  A LEU   A 160 ? 0.1561 0.2654 0.2547 0.0093  0.0241  0.1035  160 LEU   A CG  
3625 C  CG  B LEU   A 160 ? 0.2194 0.2236 0.2534 -0.0044 0.0209  -0.0001 160 LEU   A CG  
3626 C  CG  T LEU   A 160 ? 0.2171 0.2385 0.2336 0.0044  0.0217  0.0394  160 LEU   A CG  
3627 C  CD1 A LEU   A 160 ? 0.1687 0.2726 0.2676 -0.0000 0.0339  0.0959  160 LEU   A CD1 
3628 C  CD1 B LEU   A 160 ? 0.2242 0.2250 0.2653 -0.0041 0.0248  -0.0035 160 LEU   A CD1 
3629 C  CD1 T LEU   A 160 ? 0.2191 0.2407 0.2342 0.0023  0.0246  0.0385  160 LEU   A CD1 
3630 C  CD2 A LEU   A 160 ? 0.1624 0.2650 0.2589 0.0035  0.0280  0.0949  160 LEU   A CD2 
3631 C  CD2 B LEU   A 160 ? 0.2237 0.2284 0.2606 -0.0056 0.0224  -0.0021 160 LEU   A CD2 
3632 C  CD2 T LEU   A 160 ? 0.2177 0.2376 0.2323 0.0022  0.0248  0.0377  160 LEU   A CD2 
3665 N  N   A TYR   A 161 ? 0.1307 0.2585 0.2183 0.0159  0.0292  0.1005  161 TYR   A N   
3666 N  N   B TYR   A 161 ? 0.1813 0.2222 0.1942 0.0162  0.0118  0.0428  161 TYR   A N   
3667 C  CA  A TYR   A 161 ? 0.1311 0.2547 0.2197 0.0110  0.0307  0.0991  161 TYR   A CA  
3668 C  CA  B TYR   A 161 ? 0.1830 0.2315 0.2028 0.0209  0.0197  0.0553  161 TYR   A CA  
3669 C  C   A TYR   A 161 ? 0.1300 0.2824 0.2460 0.0123  0.0234  0.0898  161 TYR   A C   
3670 C  C   B TYR   A 161 ? 0.1803 0.2397 0.2128 0.0215  0.0237  0.0564  161 TYR   A C   
3671 O  O   A TYR   A 161 ? 0.1221 0.2833 0.2424 -0.0004 0.0179  0.0934  161 TYR   A O   
3672 O  O   B TYR   A 161 ? 0.1792 0.2415 0.2114 0.0198  0.0234  0.0563  161 TYR   A O   
3673 C  CB  A TYR   A 161 ? 0.1411 0.2336 0.2170 0.0045  0.0332  0.0945  161 TYR   A CB  
3674 C  CB  B TYR   A 161 ? 0.1883 0.2320 0.2013 0.0254  0.0222  0.0634  161 TYR   A CB  
3675 C  CG  A TYR   A 161 ? 0.1393 0.2141 0.2188 0.0012  0.0228  0.0713  161 TYR   A CG  
3676 C  CG  B TYR   A 161 ? 0.1917 0.2315 0.2117 0.0263  0.0229  0.0640  161 TYR   A CG  
3677 C  CD1 A TYR   A 161 ? 0.1384 0.2023 0.2268 -0.0010 0.0184  0.0586  161 TYR   A CD1 
3678 C  CD1 B TYR   A 161 ? 0.1953 0.2317 0.2208 0.0266  0.0200  0.0606  161 TYR   A CD1 
3679 C  CD2 A TYR   A 161 ? 0.1446 0.2139 0.2096 0.0050  0.0156  0.0683  161 TYR   A CD2 
3680 C  CD2 B TYR   A 161 ? 0.1953 0.2305 0.2200 0.0264  0.0233  0.0667  161 TYR   A CD2 
3681 C  CE1 A TYR   A 161 ? 0.1408 0.1887 0.2213 -0.0020 0.0112  0.0560  161 TYR   A CE1 
3682 C  CE1 B TYR   A 161 ? 0.1980 0.2365 0.2277 0.0277  0.0195  0.0572  161 TYR   A CE1 
3683 C  CE2 A TYR   A 161 ? 0.1436 0.1978 0.2116 0.0010  0.0168  0.0665  161 TYR   A CE2 
3684 C  CE2 B TYR   A 161 ? 0.1989 0.2356 0.2266 0.0242  0.0238  0.0634  161 TYR   A CE2 
3685 C  CZ  A TYR   A 161 ? 0.1506 0.1881 0.2156 -0.0021 0.0052  0.0646  161 TYR   A CZ  
3686 C  CZ  B TYR   A 161 ? 0.2050 0.2401 0.2369 0.0243  0.0208  0.0577  161 TYR   A CZ  
3687 O  OH  A TYR   A 161 ? 0.1590 0.1806 0.2359 -0.0090 -0.0061 0.0741  161 TYR   A OH  
3688 O  OH  B TYR   A 161 ? 0.2136 0.2476 0.2608 0.0218  0.0183  0.0548  161 TYR   A OH  
3707 N  N   A ASP   A 162 ? 0.1287 0.3046 0.2591 0.0163  0.0322  0.0894  162 ASP   A N   
3708 N  N   B ASP   A 162 ? 0.1799 0.2450 0.2210 0.0172  0.0294  0.0610  162 ASP   A N   
3709 C  CA  A ASP   A 162 ? 0.1282 0.3350 0.2700 0.0148  0.0358  0.0740  162 ASP   A CA  
3710 C  CA  B ASP   A 162 ? 0.1852 0.2556 0.2312 0.0077  0.0298  0.0538  162 ASP   A CA  
3711 C  C   A ASP   A 162 ? 0.1211 0.3471 0.2641 0.0074  0.0292  0.0800  162 ASP   A C   
3712 C  C   B ASP   A 162 ? 0.1844 0.2629 0.2271 0.0028  0.0278  0.0543  162 ASP   A C   
3713 O  O   A ASP   A 162 ? 0.1254 0.3491 0.2800 0.0066  0.0266  0.0672  162 ASP   A O   
3714 O  O   B ASP   A 162 ? 0.1835 0.2633 0.2290 -0.0012 0.0303  0.0559  162 ASP   A O   
3715 C  CB  A ASP   A 162 ? 0.1394 0.3523 0.2971 0.0227  0.0427  0.0538  162 ASP   A CB  
3716 C  CB  B ASP   A 162 ? 0.1933 0.2587 0.2497 0.0040  0.0283  0.0456  162 ASP   A CB  
3717 C  CG  A ASP   A 162 ? 0.1536 0.3688 0.3256 0.0268  0.0474  0.0408  162 ASP   A CG  
3718 C  CG  B ASP   A 162 ? 0.2012 0.2627 0.2688 0.0016  0.0261  0.0346  162 ASP   A CG  
3719 O  OD1 A ASP   A 162 ? 0.1683 0.3771 0.3330 0.0166  0.0464  0.0395  162 ASP   A OD1 
3720 O  OD1 B ASP   A 162 ? 0.2064 0.2621 0.2720 -0.0019 0.0293  0.0302  162 ASP   A OD1 
3721 O  OD2 A ASP   A 162 ? 0.1506 0.3746 0.3405 0.0381  0.0566  0.0335  162 ASP   A OD2 
3722 O  OD2 B ASP   A 162 ? 0.2037 0.2668 0.2852 -0.0005 0.0271  0.0261  162 ASP   A OD2 
3731 N  N   A LYS   A 163 ? 0.1315 0.3592 0.2638 0.0013  0.0086  0.0838  163 LYS   A N   
3732 N  N   B LYS   A 163 ? 0.1876 0.2692 0.2319 0.0010  0.0142  0.0497  163 LYS   A N   
3733 C  CA  A LYS   A 163 ? 0.1448 0.3696 0.2581 0.0019  -0.0009 0.0844  163 LYS   A CA  
3734 C  CA  B LYS   A 163 ? 0.1926 0.2758 0.2359 0.0021  0.0087  0.0432  163 LYS   A CA  
3735 C  C   A LYS   A 163 ? 0.1363 0.3593 0.2443 -0.0060 0.0036  0.0858  163 LYS   A C   
3736 C  C   B LYS   A 163 ? 0.1834 0.2701 0.2237 0.0040  0.0038  0.0411  163 LYS   A C   
3737 O  O   A LYS   A 163 ? 0.1295 0.3671 0.2468 -0.0129 -0.0023 0.0877  163 LYS   A O   
3738 O  O   B LYS   A 163 ? 0.1809 0.2744 0.2257 0.0047  -0.0056 0.0445  163 LYS   A O   
3739 C  CB  A LYS   A 163 ? 0.1826 0.3906 0.2969 0.0203  -0.0171 0.0774  163 LYS   A CB  
3740 C  CB  B LYS   A 163 ? 0.2112 0.2894 0.2646 0.0015  0.0073  0.0328  163 LYS   A CB  
3741 C  CG  A LYS   A 163 ? 0.2214 0.4105 0.3480 0.0257  -0.0208 0.0677  163 LYS   A CG  
3742 C  CG  B LYS   A 163 ? 0.2287 0.3024 0.2989 -0.0002 0.0072  0.0233  163 LYS   A CG  
3743 C  CD  A LYS   A 163 ? 0.2637 0.4259 0.4115 0.0309  -0.0183 0.0576  163 LYS   A CD  
3744 C  CD  B LYS   A 163 ? 0.2432 0.3131 0.3313 0.0004  0.0075  0.0146  163 LYS   A CD  
3745 C  CE  A LYS   A 163 ? 0.2994 0.4355 0.4620 0.0342  -0.0103 0.0532  163 LYS   A CE  
3746 C  CE  B LYS   A 163 ? 0.2548 0.3205 0.3593 0.0009  0.0085  0.0082  163 LYS   A CE  
3747 N  NZ  A LYS   A 163 ? 0.3089 0.4409 0.4902 0.0354  -0.0064 0.0530  163 LYS   A NZ  
3748 N  NZ  B LYS   A 163 ? 0.2600 0.3237 0.3722 0.0011  0.0106  0.0061  163 LYS   A NZ  
3775 N  N   A LEU   A 164 ? 0.1228 0.3320 0.2236 -0.0197 0.0088  0.0805  164 LEU   A N   
3776 N  N   B LEU   A 164 ? 0.1727 0.2597 0.2112 -0.0018 0.0092  0.0336  164 LEU   A N   
3777 C  CA  A LEU   A 164 ? 0.1305 0.3039 0.1961 -0.0292 0.0128  0.0759  164 LEU   A CA  
3778 C  CA  B LEU   A 164 ? 0.1647 0.2486 0.1916 -0.0060 0.0136  0.0268  164 LEU   A CA  
3779 C  C   A LEU   A 164 ? 0.1423 0.2986 0.1879 -0.0292 0.0148  0.0654  164 LEU   A C   
3780 C  C   B LEU   A 164 ? 0.1650 0.2495 0.1857 -0.0140 0.0214  0.0225  164 LEU   A C   
3781 O  O   A LEU   A 164 ? 0.1542 0.3042 0.1841 -0.0338 0.0351  0.0549  164 LEU   A O   
3782 O  O   B LEU   A 164 ? 0.1648 0.2528 0.1823 -0.0196 0.0289  0.0222  164 LEU   A O   
3783 C  CB  A LEU   A 164 ? 0.1339 0.2851 0.1865 -0.0313 0.0139  0.0773  164 LEU   A CB  
3784 C  CB  B LEU   A 164 ? 0.1606 0.2376 0.1795 -0.0022 0.0117  0.0213  164 LEU   A CB  
3785 C  CG  A LEU   A 164 ? 0.1388 0.2722 0.1783 -0.0282 0.0046  0.0717  164 LEU   A CG  
3786 C  CG  B LEU   A 164 ? 0.1604 0.2297 0.1781 0.0027  0.0081  0.0178  164 LEU   A CG  
3787 C  CD1 A LEU   A 164 ? 0.1274 0.2657 0.1618 -0.0232 -0.0073 0.0796  164 LEU   A CD1 
3788 C  CD1 B LEU   A 164 ? 0.1590 0.2292 0.1807 0.0041  0.0112  0.0126  164 LEU   A CD1 
3789 C  CD2 A LEU   A 164 ? 0.1541 0.2695 0.1819 -0.0234 0.0121  0.0647  164 LEU   A CD2 
3790 C  CD2 B LEU   A 164 ? 0.1578 0.2241 0.1687 0.0030  0.0062  0.0172  164 LEU   A CD2 
3813 N  N   A VAL   A 165 ? 0.1328 0.2847 0.1853 -0.0298 0.0172  0.0657  165 VAL   A N   
3814 N  N   B VAL   A 165 ? 0.1637 0.2473 0.1868 -0.0177 0.0192  0.0170  165 VAL   A N   
3815 C  CA  A VAL   A 165 ? 0.1432 0.2758 0.1709 -0.0325 0.0212  0.0630  165 VAL   A CA  
3816 C  CA  B VAL   A 165 ? 0.1694 0.2489 0.1904 -0.0150 0.0161  0.0148  165 VAL   A CA  
3817 C  C   A VAL   A 165 ? 0.1348 0.2871 0.1677 -0.0216 0.0298  0.0632  165 VAL   A C   
3818 C  C   B VAL   A 165 ? 0.1671 0.2511 0.1846 -0.0122 0.0224  0.0090  165 VAL   A C   
3819 O  O   A VAL   A 165 ? 0.1337 0.2852 0.1697 -0.0172 0.0356  0.0593  165 VAL   A O   
3820 O  O   B VAL   A 165 ? 0.1659 0.2523 0.1744 -0.0121 0.0294  0.0040  165 VAL   A O   
3821 C  CB  A VAL   A 165 ? 0.1619 0.2628 0.1851 -0.0380 0.0192  0.0524  165 VAL   A CB  
3822 C  CB  B VAL   A 165 ? 0.1765 0.2505 0.1997 -0.0137 0.0068  0.0125  165 VAL   A CB  
3823 C  CG1 A VAL   A 165 ? 0.1687 0.2615 0.1933 -0.0427 0.0207  0.0423  165 VAL   A CG1 
3824 C  CG1 B VAL   A 165 ? 0.1778 0.2521 0.2054 -0.0127 0.0028  0.0094  165 VAL   A CG1 
3825 C  CG2 A VAL   A 165 ? 0.1680 0.2601 0.1921 -0.0365 0.0140  0.0591  165 VAL   A CG2 
3826 C  CG2 B VAL   A 165 ? 0.1801 0.2515 0.2053 -0.0140 0.0027  0.0107  165 VAL   A CG2 
3845 N  N   A SER   A 166 ? 0.1284 0.3026 0.1908 -0.0214 0.0257  0.0550  166 SER   A N   
3846 N  N   B SER   A 166 ? 0.1608 0.2533 0.1931 -0.0104 0.0283  0.0083  166 SER   A N   
3847 C  CA  A SER   A 166 ? 0.1349 0.3256 0.2136 -0.0210 0.0227  0.0436  166 SER   A CA  
3848 C  CA  B SER   A 166 ? 0.1607 0.2581 0.2013 -0.0123 0.0252  0.0123  166 SER   A CA  
3849 C  C   A SER   A 166 ? 0.1383 0.3513 0.2158 -0.0211 0.0116  0.0329  166 SER   A C   
3850 C  C   B SER   A 166 ? 0.1731 0.2689 0.2144 -0.0195 0.0236  0.0115  166 SER   A C   
3851 O  O   A SER   A 166 ? 0.1571 0.3667 0.2387 -0.0359 0.0227  0.0077  166 SER   A O   
3852 O  O   B SER   A 166 ? 0.1810 0.2771 0.2171 -0.0260 0.0267  0.0070  166 SER   A O   
3853 C  CB  A SER   A 166 ? 0.1511 0.3294 0.2388 -0.0170 0.0185  0.0449  166 SER   A CB  
3854 C  CB  B SER   A 166 ? 0.1485 0.2550 0.2029 -0.0002 0.0187  0.0142  166 SER   A CB  
3855 O  OG  A SER   A 166 ? 0.1810 0.3345 0.2731 -0.0208 0.0185  0.0563  166 SER   A OG  
3856 O  OG  B SER   A 166 ? 0.1412 0.2534 0.2117 0.0070  0.0031  0.0228  166 SER   A OG  
3867 N  N   A SER   A 167 ? 0.1404 0.3542 0.1813 -0.0006 0.0064  0.0463  167 SER   A N   
3868 N  N   B SER   A 167 ? 0.1845 0.2712 0.2363 -0.0185 0.0173  0.0167  167 SER   A N   
3869 C  CA  A SER   A 167 ? 0.1618 0.3572 0.1897 0.0065  -0.0072 0.0380  167 SER   A CA  
3870 C  CA  B SER   A 167 ? 0.1888 0.2715 0.2534 -0.0194 0.0208  0.0208  167 SER   A CA  
3871 C  C   A SER   A 167 ? 0.1667 0.3491 0.2003 0.0125  0.0008  0.0350  167 SER   A C   
3872 C  C   B SER   A 167 ? 0.1814 0.2691 0.2517 -0.0167 0.0303  0.0171  167 SER   A C   
3873 O  O   A SER   A 167 ? 0.1766 0.3527 0.1990 0.0147  -0.0028 0.0273  167 SER   A O   
3874 O  O   B SER   A 167 ? 0.1948 0.2763 0.2715 -0.0207 0.0258  0.0144  167 SER   A O   
3875 C  CB  A SER   A 167 ? 0.1628 0.3659 0.2000 0.0019  0.0031  0.0318  167 SER   A CB  
3876 C  CB  B SER   A 167 ? 0.2002 0.2746 0.2769 -0.0201 0.0132  0.0217  167 SER   A CB  
3877 O  OG  A SER   A 167 ? 0.1498 0.3734 0.2073 -0.0070 0.0216  0.0371  167 SER   A OG  
3878 O  OG  B SER   A 167 ? 0.2084 0.2785 0.2902 -0.0190 0.0076  0.0227  167 SER   A OG  
3889 N  N   A PHE   A 168 ? 0.1564 0.3374 0.2190 0.0184  0.0087  0.0410  168 PHE   A N   
3890 N  N   B PHE   A 168 ? 0.1582 0.2594 0.2229 -0.0104 0.0422  0.0180  168 PHE   A N   
3891 C  CA  A PHE   A 168 ? 0.1627 0.3292 0.2395 0.0104  0.0223  0.0407  168 PHE   A CA  
3892 C  CA  B PHE   A 168 ? 0.1452 0.2545 0.1986 -0.0067 0.0452  0.0172  168 PHE   A CA  
3893 C  C   A PHE   A 168 ? 0.1802 0.3358 0.2858 -0.0026 0.0487  0.0370  168 PHE   A C   
3894 C  C   B PHE   A 168 ? 0.1366 0.2523 0.1882 -0.0112 0.0443  0.0170  168 PHE   A C   
3895 O  O   A PHE   A 168 ? 0.1872 0.3404 0.3276 -0.0125 0.0548  0.0473  168 PHE   A O   
3896 O  O   B PHE   A 168 ? 0.1192 0.2496 0.1664 -0.0124 0.0495  0.0160  168 PHE   A O   
3897 C  CB  A PHE   A 168 ? 0.1597 0.3167 0.2228 0.0012  0.0105  0.0392  168 PHE   A CB  
3898 C  CB  B PHE   A 168 ? 0.1548 0.2537 0.2028 -0.0046 0.0417  0.0230  168 PHE   A CB  
3899 C  CG  A PHE   A 168 ? 0.1521 0.3052 0.1971 -0.0060 0.0101  0.0413  168 PHE   A CG  
3900 C  CG  B PHE   A 168 ? 0.1645 0.2507 0.2057 -0.0005 0.0347  0.0336  168 PHE   A CG  
3901 C  CD1 A PHE   A 168 ? 0.1534 0.3052 0.1926 -0.0111 0.0040  0.0494  168 PHE   A CD1 
3902 C  CD1 B PHE   A 168 ? 0.1682 0.2521 0.2114 0.0004  0.0337  0.0390  168 PHE   A CD1 
3903 C  CD2 A PHE   A 168 ? 0.1479 0.2984 0.1860 -0.0072 0.0299  0.0352  168 PHE   A CD2 
3904 C  CD2 B PHE   A 168 ? 0.1728 0.2477 0.2131 0.0010  0.0255  0.0384  168 PHE   A CD2 
3905 C  CE1 A PHE   A 168 ? 0.1444 0.2998 0.1780 -0.0123 0.0046  0.0515  168 PHE   A CE1 
3906 C  CE1 B PHE   A 168 ? 0.1711 0.2517 0.2174 0.0013  0.0261  0.0409  168 PHE   A CE1 
3907 C  CE2 A PHE   A 168 ? 0.1534 0.2933 0.1847 -0.0082 0.0276  0.0441  168 PHE   A CE2 
3908 C  CE2 B PHE   A 168 ? 0.1779 0.2475 0.2182 0.0038  0.0210  0.0424  168 PHE   A CE2 
3909 C  CZ  A PHE   A 168 ? 0.1465 0.2932 0.1734 -0.0108 0.0177  0.0483  168 PHE   A CZ  
3910 C  CZ  B PHE   A 168 ? 0.1771 0.2493 0.2192 0.0037  0.0196  0.0413  168 PHE   A CZ  
3929 N  N   A LEU   A 169 ? 0.2153 0.3404 0.3215 -0.0095 0.0507  0.0153  169 LEU   A N   
3930 N  N   B LEU   A 169 ? 0.1463 0.2536 0.2051 -0.0115 0.0320  0.0213  169 LEU   A N   
3931 C  CA  A LEU   A 169 ? 0.2607 0.3493 0.3735 -0.0124 0.0338  0.0020  169 LEU   A CA  
3932 C  CA  B LEU   A 169 ? 0.1602 0.2593 0.2234 -0.0139 0.0213  0.0177  169 LEU   A CA  
3933 C  C   A LEU   A 169 ? 0.2619 0.3435 0.3938 -0.0153 0.0384  0.0161  169 LEU   A C   
3934 C  C   B LEU   A 169 ? 0.1748 0.2660 0.2372 -0.0078 0.0175  0.0124  169 LEU   A C   
3935 O  O   A LEU   A 169 ? 0.2687 0.3431 0.4019 -0.0131 0.0328  0.0174  169 LEU   A O   
3936 O  O   B LEU   A 169 ? 0.1792 0.2681 0.2422 -0.0043 0.0100  0.0084  169 LEU   A O   
3937 C  CB  A LEU   A 169 ? 0.2923 0.3620 0.3833 -0.0120 0.0251  -0.0184 169 LEU   A CB  
3938 C  CB  B LEU   A 169 ? 0.1621 0.2610 0.2226 -0.0216 0.0159  0.0226  169 LEU   A CB  
3939 C  CG  A LEU   A 169 ? 0.3205 0.3717 0.3936 -0.0144 0.0183  -0.0411 169 LEU   A CG  
3940 C  CG  B LEU   A 169 ? 0.1624 0.2613 0.2263 -0.0285 0.0151  0.0281  169 LEU   A CG  
3941 C  CD1 A LEU   A 169 ? 0.3313 0.3750 0.4013 -0.0145 0.0139  -0.0476 169 LEU   A CD1 
3942 C  CD1 B LEU   A 169 ? 0.1620 0.2642 0.2418 -0.0315 0.0099  0.0285  169 LEU   A CD1 
3943 C  CD2 A LEU   A 169 ? 0.3281 0.3751 0.3901 -0.0170 0.0206  -0.0493 169 LEU   A CD2 
3944 C  CD2 B LEU   A 169 ? 0.1674 0.2615 0.2245 -0.0331 0.0181  0.0320  169 LEU   A CD2 
3945 O  OXT A LEU   A 169 ? 0.2448 0.3405 0.3861 -0.0182 0.0550  0.0199  169 LEU   A OXT 
3946 O  OXT B LEU   A 169 ? 0.1868 0.2708 0.2484 -0.0101 0.0171  0.0134  169 LEU   A OXT 
3969 N  N   A SER   B 1   ? 0.3715 0.3454 0.3528 -0.1132 -0.0729 0.0392  1   SER   B N   
3970 N  N   B SER   B 1   ? 0.3326 0.3184 0.3308 -0.0608 -0.0416 0.0121  1   SER   B N   
3971 C  CA  A SER   B 1   ? 0.3627 0.3497 0.3613 -0.1198 -0.0755 0.0374  1   SER   B CA  
3972 C  CA  B SER   B 1   ? 0.3287 0.3204 0.3320 -0.0624 -0.0411 0.0115  1   SER   B CA  
3973 C  C   A SER   B 1   ? 0.3317 0.3512 0.3421 -0.1251 -0.0830 0.0549  1   SER   B C   
3974 C  C   B SER   B 1   ? 0.3166 0.3231 0.3235 -0.0611 -0.0449 0.0234  1   SER   B C   
3975 O  O   A SER   B 1   ? 0.3411 0.3536 0.3226 -0.1190 -0.0769 0.0530  1   SER   B O   
3976 O  O   B SER   B 1   ? 0.3185 0.3232 0.3145 -0.0605 -0.0462 0.0219  1   SER   B O   
3977 C  CB  A SER   B 1   ? 0.3786 0.3491 0.3797 -0.1193 -0.0641 0.0239  1   SER   B CB  
3978 C  CB  B SER   B 1   ? 0.3336 0.3177 0.3364 -0.0642 -0.0345 0.0004  1   SER   B CB  
3979 O  OG  A SER   B 1   ? 0.3943 0.3583 0.4210 -0.1150 -0.0578 0.0192  1   SER   B OG  
3980 O  OG  B SER   B 1   ? 0.3391 0.3193 0.3522 -0.0654 -0.0314 -0.0054 1   SER   B OG  
3995 N  N   A MET   B 2   ? 0.2983 0.3476 0.3365 -0.1287 -0.0854 0.0909  2   MET   B N   
3996 N  N   B MET   B 2   ? 0.3040 0.3241 0.3193 -0.0583 -0.0445 0.0425  2   MET   B N   
3997 C  CA  A MET   B 2   ? 0.2779 0.3486 0.3532 -0.1078 -0.0887 0.1118  2   MET   B CA  
3998 C  CA  B MET   B 2   ? 0.2923 0.3240 0.3184 -0.0499 -0.0440 0.0582  2   MET   B CA  
3999 C  C   A MET   B 2   ? 0.2394 0.3230 0.3257 -0.0845 -0.1001 0.1388  2   MET   B C   
4000 C  C   B MET   B 2   ? 0.2720 0.3089 0.2950 -0.0459 -0.0411 0.0663  2   MET   B C   
4001 O  O   A MET   B 2   ? 0.2311 0.3359 0.3320 -0.0662 -0.1176 0.1410  2   MET   B O   
4002 O  O   B MET   B 2   ? 0.2736 0.3153 0.3002 -0.0417 -0.0393 0.0640  2   MET   B O   
4003 C  CB  A MET   B 2   ? 0.3096 0.3845 0.4325 -0.0893 -0.0667 0.0884  2   MET   B CB  
4004 C  CB  B MET   B 2   ? 0.3032 0.3397 0.3492 -0.0409 -0.0437 0.0620  2   MET   B CB  
4005 C  CG  A MET   B 2   ? 0.3391 0.4150 0.5074 -0.0698 -0.0436 0.0711  2   MET   B CG  
4006 C  CG  B MET   B 2   ? 0.3122 0.3529 0.3741 -0.0324 -0.0424 0.0695  2   MET   B CG  
4007 S  SD  A MET   B 2   ? 0.3668 0.4419 0.5792 -0.0526 -0.0279 0.0579  2   MET   B SD  
4008 S  SD  B MET   B 2   ? 0.3206 0.3661 0.3935 -0.0244 -0.0437 0.0769  2   MET   B SD  
4009 C  CE  A MET   B 2   ? 0.3711 0.4489 0.5798 -0.0510 -0.0198 0.0582  2   MET   B CE  
4010 C  CE  B MET   B 2   ? 0.3217 0.3684 0.4015 -0.0239 -0.0408 0.0715  2   MET   B CE  
4029 N  N   A VAL   B 3   ? 0.2123 0.2794 0.2991 -0.0874 -0.0869 0.1528  3   VAL   B N   
4030 N  N   B VAL   B 3   ? 0.2498 0.2852 0.2684 -0.0479 -0.0400 0.0751  3   VAL   B N   
4031 C  CA  A VAL   B 3   ? 0.2091 0.2463 0.2961 -0.0773 -0.0772 0.1302  3   VAL   B CA  
4032 C  CA  B VAL   B 3   ? 0.2310 0.2622 0.2502 -0.0468 -0.0405 0.0753  3   VAL   B CA  
4033 C  C   A VAL   B 3   ? 0.1940 0.2348 0.2587 -0.0658 -0.0704 0.1105  3   VAL   B C   
4034 C  C   B VAL   B 3   ? 0.2070 0.2428 0.2255 -0.0490 -0.0475 0.0825  3   VAL   B C   
4035 O  O   A VAL   B 3   ? 0.1912 0.2408 0.2684 -0.0656 -0.0727 0.1154  3   VAL   B O   
4036 O  O   B VAL   B 3   ? 0.2061 0.2478 0.2171 -0.0396 -0.0461 0.0879  3   VAL   B O   
4037 C  CB  A VAL   B 3   ? 0.2270 0.2415 0.3448 -0.0764 -0.0718 0.1090  3   VAL   B CB  
4038 C  CB  B VAL   B 3   ? 0.2375 0.2604 0.2633 -0.0456 -0.0347 0.0668  3   VAL   B CB  
4039 C  CG1 A VAL   B 3   ? 0.2357 0.2349 0.3692 -0.0781 -0.0694 0.1021  3   VAL   B CG1 
4040 C  CG1 B VAL   B 3   ? 0.2406 0.2588 0.2714 -0.0456 -0.0327 0.0623  3   VAL   B CG1 
4041 C  CG2 A VAL   B 3   ? 0.2312 0.2477 0.3590 -0.0712 -0.0584 0.1158  3   VAL   B CG2 
4042 C  CG2 B VAL   B 3   ? 0.2392 0.2612 0.2665 -0.0441 -0.0306 0.0686  3   VAL   B CG2 
4061 N  N   . ASN   B 4   ? 0.1841 0.2155 0.2208 -0.0618 -0.0594 0.0854  4   ASN   B N   
4062 C  CA  . ASN   B 4   ? 0.1839 0.2126 0.1881 -0.0579 -0.0498 0.0505  4   ASN   B CA  
4063 C  C   . ASN   B 4   ? 0.1879 0.2275 0.1903 -0.0597 -0.0369 0.0382  4   ASN   B C   
4064 O  O   . ASN   B 4   ? 0.1892 0.2312 0.2130 -0.0547 -0.0317 0.0208  4   ASN   B O   
4065 C  CB  . ASN   B 4   ? 0.1840 0.2071 0.1743 -0.0487 -0.0570 0.0412  4   ASN   B CB  
4066 C  CG  . ASN   B 4   ? 0.1828 0.1887 0.1731 -0.0462 -0.0510 0.0359  4   ASN   B CG  
4067 O  OD1 . ASN   B 4   ? 0.1885 0.1698 0.1812 -0.0440 -0.0547 0.0318  4   ASN   B OD1 
4068 N  ND2 . ASN   B 4   ? 0.1999 0.1962 0.1842 -0.0313 -0.0317 0.0301  4   ASN   B ND2 
4076 N  N   . SER   B 5   ? 0.2023 0.2471 0.2089 -0.0631 -0.0290 0.0300  5   SER   B N   
4077 C  CA  . SER   B 5   ? 0.2346 0.2798 0.2327 -0.0552 -0.0092 0.0327  5   SER   B CA  
4078 C  C   . SER   B 5   ? 0.2568 0.2879 0.2596 -0.0723 0.0239  0.0337  5   SER   B C   
4079 O  O   . SER   B 5   ? 0.2718 0.2838 0.3243 -0.0659 0.0571  0.0309  5   SER   B O   
4080 C  CB  . SER   B 5   ? 0.2483 0.2995 0.2595 -0.0449 -0.0004 0.0417  5   SER   B CB  
4081 O  OG  . SER   B 5   ? 0.2689 0.3226 0.3089 -0.0318 0.0039  0.0496  5   SER   B OG  
4087 N  N   . PHE   B 6   ? 0.2771 0.3077 0.2374 -0.0805 0.0393  0.0379  6   PHE   B N   
4088 C  CA  . PHE   B 6   ? 0.2904 0.3163 0.2098 -0.0950 0.0452  0.0200  6   PHE   B CA  
4089 C  C   . PHE   B 6   ? 0.3442 0.3537 0.2492 -0.1038 0.0698  -0.0068 6   PHE   B C   
4090 O  O   . PHE   B 6   ? 0.3576 0.3803 0.2801 -0.0967 0.0557  -0.0234 6   PHE   B O   
4091 C  CB  . PHE   B 6   ? 0.2577 0.2907 0.1851 -0.0857 0.0203  0.0176  6   PHE   B CB  
4092 C  CG  . PHE   B 6   ? 0.2236 0.2554 0.1692 -0.0794 -0.0005 0.0195  6   PHE   B CG  
4093 C  CD1 . PHE   B 6   ? 0.2215 0.2264 0.1558 -0.0727 -0.0117 0.0149  6   PHE   B CD1 
4094 C  CD2 . PHE   B 6   ? 0.2016 0.2513 0.1637 -0.0672 -0.0012 0.0434  6   PHE   B CD2 
4095 C  CE1 . PHE   B 6   ? 0.2158 0.2014 0.1629 -0.0663 -0.0141 0.0095  6   PHE   B CE1 
4096 C  CE2 . PHE   B 6   ? 0.2039 0.2348 0.1938 -0.0587 0.0058  0.0344  6   PHE   B CE2 
4097 C  CZ  . PHE   B 6   ? 0.2064 0.2120 0.1756 -0.0579 -0.0003 0.0122  6   PHE   B CZ  
4107 N  N   . SER   B 7   ? 0.3802 0.3492 0.2674 -0.1264 0.1066  -0.0247 7   SER   B N   
4108 C  CA  . SER   B 7   ? 0.4175 0.3693 0.3171 -0.1277 0.1349  -0.0321 7   SER   B CA  
4109 C  C   . SER   B 7   ? 0.4148 0.3416 0.2917 -0.1319 0.1427  -0.0518 7   SER   B C   
4110 O  O   . SER   B 7   ? 0.4232 0.3382 0.3128 -0.1361 0.1338  -0.0600 7   SER   B O   
4111 C  CB  . SER   B 7   ? 0.4441 0.4044 0.3941 -0.1262 0.1555  -0.0198 7   SER   B CB  
4112 O  OG  . SER   B 7   ? 0.4515 0.4134 0.4554 -0.1261 0.1623  -0.0103 7   SER   B OG  
4118 N  N   . GLY   B 8   ? 0.4105 0.3243 0.2877 -0.1168 0.1461  -0.0665 8   GLY   B N   
4119 C  CA  . GLY   B 8   ? 0.3964 0.3036 0.2876 -0.1076 0.1429  -0.0740 8   GLY   B CA  
4120 C  C   . GLY   B 8   ? 0.3749 0.2743 0.2837 -0.1015 0.1352  -0.0691 8   GLY   B C   
4121 O  O   . GLY   B 8   ? 0.3858 0.2827 0.3119 -0.0906 0.1362  -0.0758 8   GLY   B O   
4125 N  N   . TYR   B 9   ? 0.3523 0.2449 0.2623 -0.0904 0.1085  -0.0751 9   TYR   B N   
4126 C  CA  . TYR   B 9   ? 0.3287 0.2160 0.2395 -0.0775 0.0803  -0.0568 9   TYR   B CA  
4127 C  C   . TYR   B 9   ? 0.3231 0.2134 0.2254 -0.0714 0.0513  -0.0443 9   TYR   B C   
4128 O  O   . TYR   B 9   ? 0.3335 0.2326 0.2655 -0.0748 0.0511  -0.0304 9   TYR   B O   
4129 C  CB  . TYR   B 9   ? 0.3161 0.1914 0.2428 -0.0722 0.0739  -0.0536 9   TYR   B CB  
4130 C  CG  . TYR   B 9   ? 0.3034 0.1768 0.2430 -0.0765 0.0647  -0.0524 9   TYR   B CG  
4131 C  CD1 . TYR   B 9   ? 0.3056 0.1765 0.2557 -0.0869 0.0638  -0.0445 9   TYR   B CD1 
4132 C  CD2 . TYR   B 9   ? 0.2886 0.1762 0.2346 -0.0707 0.0580  -0.0556 9   TYR   B CD2 
4133 C  CE1 . TYR   B 9   ? 0.2985 0.1860 0.2551 -0.0902 0.0668  -0.0564 9   TYR   B CE1 
4134 C  CE2 . TYR   B 9   ? 0.2862 0.1766 0.2408 -0.0696 0.0574  -0.0592 9   TYR   B CE2 
4135 C  CZ  . TYR   B 9   ? 0.2884 0.1894 0.2523 -0.0816 0.0631  -0.0660 9   TYR   B CZ  
4136 O  OH  . TYR   B 9   ? 0.2828 0.2001 0.2664 -0.0905 0.0654  -0.0745 9   TYR   B OH  
4146 N  N   . LEU   B 10  ? 0.3044 0.1879 0.2055 -0.0687 0.0263  -0.0437 10  LEU   B N   
4147 C  CA  . LEU   B 10  ? 0.3003 0.1851 0.2075 -0.0788 -0.0079 -0.0386 10  LEU   B CA  
4148 C  C   . LEU   B 10  ? 0.2805 0.1865 0.2092 -0.0747 -0.0255 -0.0374 10  LEU   B C   
4149 O  O   . LEU   B 10  ? 0.2618 0.1896 0.2170 -0.0607 -0.0169 -0.0288 10  LEU   B O   
4150 C  CB  . LEU   B 10  ? 0.3176 0.1823 0.2280 -0.0826 -0.0306 -0.0188 10  LEU   B CB  
4151 C  CG  . LEU   B 10  ? 0.3367 0.1939 0.2632 -0.0736 -0.0578 -0.0073 10  LEU   B CG  
4152 C  CD1 . LEU   B 10  ? 0.3503 0.2055 0.2864 -0.0668 -0.0565 -0.0059 10  LEU   B CD1 
4153 C  CD2 . LEU   B 10  ? 0.3453 0.1978 0.2924 -0.0758 -0.0552 0.0045  10  LEU   B CD2 
4165 N  N   . LYS   B 11  ? 0.2950 0.2150 0.2158 -0.0676 -0.0379 -0.0274 11  LYS   B N   
4166 C  CA  . LYS   B 11  ? 0.3112 0.2413 0.2520 -0.0559 -0.0466 -0.0302 11  LYS   B CA  
4167 C  C   . LYS   B 11  ? 0.2881 0.2195 0.2533 -0.0766 -0.0466 -0.0371 11  LYS   B C   
4168 O  O   . LYS   B 11  ? 0.3036 0.2337 0.2831 -0.0911 -0.0425 -0.0685 11  LYS   B O   
4169 C  CB  . LYS   B 11  ? 0.3473 0.2924 0.3171 -0.0298 -0.0490 -0.0308 11  LYS   B CB  
4170 C  CG  . LYS   B 11  ? 0.3781 0.3271 0.3865 -0.0135 -0.0501 -0.0317 11  LYS   B CG  
4171 C  CD  . LYS   B 11  ? 0.4033 0.3518 0.4500 -0.0038 -0.0495 -0.0335 11  LYS   B CD  
4172 C  CE  . LYS   B 11  ? 0.4214 0.3678 0.4974 -0.0012 -0.0500 -0.0336 11  LYS   B CE  
4173 N  NZ  . LYS   B 11  ? 0.4315 0.3770 0.5226 -0.0004 -0.0524 -0.0314 11  LYS   B NZ  
4187 N  N   . LEU   B 12  ? 0.2507 0.1979 0.2497 -0.0700 -0.0495 -0.0327 12  LEU   B N   
4188 C  CA  . LEU   B 12  ? 0.2333 0.1782 0.2634 -0.0586 -0.0358 -0.0270 12  LEU   B CA  
4189 C  C   . LEU   B 12  ? 0.2209 0.1719 0.2595 -0.0579 -0.0528 -0.0229 12  LEU   B C   
4190 O  O   . LEU   B 12  ? 0.2183 0.1733 0.2799 -0.0620 -0.0685 -0.0186 12  LEU   B O   
4191 C  CB  . LEU   B 12  ? 0.2320 0.1608 0.2666 -0.0436 -0.0235 -0.0304 12  LEU   B CB  
4192 C  CG  . LEU   B 12  ? 0.2311 0.1534 0.2628 -0.0432 -0.0138 -0.0193 12  LEU   B CG  
4193 C  CD1 . LEU   B 12  ? 0.2444 0.1530 0.2467 -0.0287 -0.0115 -0.0003 12  LEU   B CD1 
4194 C  CD2 . LEU   B 12  ? 0.2369 0.1591 0.2722 -0.0420 -0.0053 -0.0216 12  LEU   B CD2 
4206 N  N   . THR   B 13  ? 0.2140 0.1758 0.2635 -0.0589 -0.0528 -0.0299 13  THR   B N   
4207 C  CA  . THR   B 13  ? 0.2144 0.1859 0.2618 -0.0655 -0.0635 -0.0169 13  THR   B CA  
4208 C  C   . THR   B 13  ? 0.2565 0.2090 0.2793 -0.0742 -0.0755 -0.0109 13  THR   B C   
4209 O  O   . THR   B 13  ? 0.2744 0.2113 0.2933 -0.0742 -0.0466 -0.0137 13  THR   B O   
4210 C  CB  . THR   B 13  ? 0.1973 0.1862 0.2618 -0.0581 -0.0582 -0.0130 13  THR   B CB  
4211 O  OG1 . THR   B 13  ? 0.1872 0.1817 0.2763 -0.0532 -0.0427 -0.0125 13  THR   B OG1 
4212 C  CG2 . THR   B 13  ? 0.2049 0.1934 0.2626 -0.0513 -0.0473 -0.0015 13  THR   B CG2 
4220 N  N   A ASP   B 14  ? 0.2699 0.2221 0.2916 -0.0823 -0.1085 -0.0012 14  ASP   B N   
4221 N  N   B ASP   B 14  ? 0.2653 0.2188 0.2891 -0.0732 -0.0806 -0.0053 14  ASP   B N   
4222 C  CA  A ASP   B 14  ? 0.2843 0.2398 0.3158 -0.0803 -0.1169 0.0180  14  ASP   B CA  
4223 C  CA  B ASP   B 14  ? 0.2733 0.2292 0.3038 -0.0699 -0.0794 0.0038  14  ASP   B CA  
4224 C  C   A ASP   B 14  ? 0.2716 0.2185 0.2798 -0.0832 -0.0966 0.0194  14  ASP   B C   
4225 C  C   B ASP   B 14  ? 0.2579 0.2112 0.2714 -0.0712 -0.0824 0.0076  14  ASP   B C   
4226 O  O   A ASP   B 14  ? 0.2990 0.2350 0.2866 -0.0806 -0.0895 0.0319  14  ASP   B O   
4227 O  O   B ASP   B 14  ? 0.2680 0.2156 0.2660 -0.0690 -0.0844 0.0074  14  ASP   B O   
4228 C  CB  A ASP   B 14  ? 0.3058 0.2785 0.3937 -0.0766 -0.1305 0.0192  14  ASP   B CB  
4229 C  CB  B ASP   B 14  ? 0.2930 0.2561 0.3543 -0.0658 -0.0728 0.0049  14  ASP   B CB  
4230 C  CG  A ASP   B 14  ? 0.3329 0.3127 0.4724 -0.0688 -0.1219 0.0069  14  ASP   B CG  
4231 C  CG  B ASP   B 14  ? 0.3118 0.2786 0.4002 -0.0607 -0.0643 0.0014  14  ASP   B CG  
4232 O  OD1 A ASP   B 14  ? 0.3482 0.3242 0.4929 -0.0691 -0.1186 -0.0073 14  ASP   B OD1 
4233 O  OD1 B ASP   B 14  ? 0.3200 0.2878 0.4125 -0.0591 -0.0609 -0.0026 14  ASP   B OD1 
4234 O  OD2 A ASP   B 14  ? 0.3388 0.3271 0.5095 -0.0649 -0.1145 0.0103  14  ASP   B OD2 
4235 O  OD2 B ASP   B 14  ? 0.3170 0.2856 0.4179 -0.0610 -0.0619 0.0022  14  ASP   B OD2 
4244 N  N   . ASN   B 15  ? 0.2322 0.1900 0.2563 -0.0669 -0.0846 0.0167  15  ASN   B N   
4245 C  CA  . ASN   B 15  ? 0.1865 0.1592 0.2441 -0.0430 -0.0589 0.0091  15  ASN   B CA  
4246 C  C   . ASN   B 15  ? 0.1702 0.1461 0.2283 -0.0281 -0.0476 -0.0017 15  ASN   B C   
4247 O  O   . ASN   B 15  ? 0.1676 0.1421 0.2428 -0.0268 -0.0492 -0.0145 15  ASN   B O   
4248 C  CB  . ASN   B 15  ? 0.1786 0.1544 0.2616 -0.0211 -0.0575 0.0082  15  ASN   B CB  
4249 C  CG  . ASN   B 15  ? 0.1612 0.1537 0.2627 -0.0283 -0.0321 0.0104  15  ASN   B CG  
4250 O  OD1 . ASN   B 15  ? 0.1642 0.1794 0.2936 -0.0442 -0.0362 0.0130  15  ASN   B OD1 
4251 N  ND2 . ASN   B 15  ? 0.1650 0.1326 0.2494 -0.0155 -0.0097 -0.0073 15  ASN   B ND2 
4259 N  N   . VAL   B 16  ? 0.1716 0.1412 0.2166 -0.0328 -0.0522 -0.0047 16  VAL   B N   
4260 C  CA  . VAL   B 16  ? 0.1690 0.1418 0.2039 -0.0303 -0.0390 -0.0199 16  VAL   B CA  
4261 C  C   . VAL   B 16  ? 0.1684 0.1544 0.2107 -0.0388 -0.0386 -0.0128 16  VAL   B C   
4262 O  O   . VAL   B 16  ? 0.1712 0.1643 0.2270 -0.0350 -0.0324 -0.0268 16  VAL   B O   
4263 C  CB  . VAL   B 16  ? 0.1708 0.1404 0.2242 -0.0211 -0.0258 -0.0157 16  VAL   B CB  
4264 C  CG1 . VAL   B 16  ? 0.1765 0.1380 0.2146 -0.0105 -0.0285 -0.0054 16  VAL   B CG1 
4265 C  CG2 . VAL   B 16  ? 0.1704 0.1460 0.2498 -0.0117 -0.0135 -0.0180 16  VAL   B CG2 
4275 N  N   . TYR   B 17  ? 0.1761 0.1645 0.2046 -0.0340 -0.0334 -0.0230 17  TYR   B N   
4276 C  CA  . TYR   B 17  ? 0.1841 0.1761 0.2011 -0.0452 -0.0273 0.0001  17  TYR   B CA  
4277 C  C   . TYR   B 17  ? 0.1768 0.1475 0.1942 -0.0460 -0.0189 -0.0115 17  TYR   B C   
4278 O  O   . TYR   B 17  ? 0.1745 0.1566 0.2023 -0.0384 -0.0299 -0.0343 17  TYR   B O   
4279 C  CB  . TYR   B 17  ? 0.2172 0.2232 0.2210 -0.0333 -0.0311 0.0324  17  TYR   B CB  
4280 C  CG  . TYR   B 17  ? 0.2485 0.2745 0.2657 -0.0233 -0.0462 0.0415  17  TYR   B CG  
4281 C  CD1 . TYR   B 17  ? 0.2668 0.2914 0.2915 -0.0164 -0.0562 0.0521  17  TYR   B CD1 
4282 C  CD2 . TYR   B 17  ? 0.2702 0.3001 0.2927 -0.0140 -0.0576 0.0421  17  TYR   B CD2 
4283 C  CE1 . TYR   B 17  ? 0.2860 0.3138 0.3125 -0.0065 -0.0664 0.0497  17  TYR   B CE1 
4284 C  CE2 . TYR   B 17  ? 0.2864 0.3194 0.3179 -0.0025 -0.0705 0.0489  17  TYR   B CE2 
4285 C  CZ  . TYR   B 17  ? 0.2973 0.3285 0.3263 0.0011  -0.0757 0.0514  17  TYR   B CZ  
4286 O  OH  . TYR   B 17  ? 0.3135 0.3439 0.3444 0.0087  -0.0813 0.0543  17  TYR   B OH  
4296 N  N   . ILE   B 18  ? 0.1885 0.1485 0.1950 -0.0367 -0.0085 -0.0131 18  ILE   B N   
4297 C  CA  . ILE   B 18  ? 0.1912 0.1444 0.1943 -0.0405 -0.0087 -0.0224 18  ILE   B CA  
4298 C  C   . ILE   B 18  ? 0.2052 0.1496 0.1867 -0.0524 -0.0071 -0.0335 18  ILE   B C   
4299 O  O   . ILE   B 18  ? 0.2204 0.1679 0.2005 -0.0436 0.0007  -0.0341 18  ILE   B O   
4300 C  CB  . ILE   B 18  ? 0.1922 0.1482 0.2001 -0.0461 -0.0104 -0.0166 18  ILE   B CB  
4301 C  CG1 . ILE   B 18  ? 0.1908 0.1527 0.2099 -0.0419 -0.0026 -0.0094 18  ILE   B CG1 
4302 C  CG2 . ILE   B 18  ? 0.1917 0.1575 0.2116 -0.0489 -0.0182 -0.0096 18  ILE   B CG2 
4303 C  CD1 . ILE   B 18  ? 0.2003 0.1799 0.2241 -0.0372 -0.0215 0.0101  18  ILE   B CD1 
4315 N  N   . LYS   B 19  ? 0.2080 0.1492 0.2027 -0.0325 0.0276  -0.0355 19  LYS   B N   
4316 C  CA  . LYS   B 19  ? 0.2136 0.1549 0.2264 -0.0349 0.0298  -0.0445 19  LYS   B CA  
4317 C  C   . LYS   B 19  ? 0.1967 0.1527 0.2426 -0.0314 0.0302  -0.0504 19  LYS   B C   
4318 O  O   . LYS   B 19  ? 0.1873 0.1566 0.2244 -0.0229 0.0210  -0.0418 19  LYS   B O   
4319 C  CB  . LYS   B 19  ? 0.2415 0.1752 0.2341 -0.0341 0.0396  -0.0358 19  LYS   B CB  
4320 C  CG  . LYS   B 19  ? 0.2706 0.1986 0.2552 -0.0419 0.0499  -0.0367 19  LYS   B CG  
4321 C  CD  . LYS   B 19  ? 0.2977 0.2293 0.2604 -0.0502 0.0606  -0.0330 19  LYS   B CD  
4322 C  CE  . LYS   B 19  ? 0.3217 0.2530 0.2760 -0.0540 0.0582  -0.0327 19  LYS   B CE  
4323 N  NZ  . LYS   B 19  ? 0.3369 0.2689 0.2844 -0.0588 0.0611  -0.0272 19  LYS   B NZ  
4337 N  N   . ASN   B 20  ? 0.1930 0.1665 0.2753 -0.0243 0.0416  -0.0607 20  ASN   B N   
4338 C  CA  . ASN   B 20  ? 0.1974 0.1787 0.3049 -0.0159 0.0390  -0.0824 20  ASN   B CA  
4339 C  C   . ASN   B 20  ? 0.1920 0.1964 0.3037 -0.0217 0.0514  -0.0882 20  ASN   B C   
4340 O  O   . ASN   B 20  ? 0.2109 0.2316 0.3211 -0.0337 0.0553  -0.0913 20  ASN   B O   
4341 C  CB  . ASN   B 20  ? 0.2214 0.1885 0.3332 0.0076  0.0309  -0.0851 20  ASN   B CB  
4342 C  CG  . ASN   B 20  ? 0.2449 0.1971 0.3521 0.0368  0.0298  -0.0938 20  ASN   B CG  
4343 O  OD1 . ASN   B 20  ? 0.2751 0.2271 0.3770 0.0496  0.0296  -0.0909 20  ASN   B OD1 
4344 N  ND2 . ASN   B 20  ? 0.2359 0.1955 0.3468 0.0414  0.0156  -0.0937 20  ASN   B ND2 
4351 N  N   . ALA   B 21  ? 0.1884 0.1774 0.2946 -0.0272 0.0527  -0.0698 21  ALA   B N   
4352 C  CA  . ALA   B 21  ? 0.1977 0.1866 0.3021 -0.0323 0.0404  -0.0541 21  ALA   B CA  
4353 C  C   . ALA   B 21  ? 0.1975 0.1628 0.2876 -0.0235 0.0400  -0.0389 21  ALA   B C   
4354 O  O   . ALA   B 21  ? 0.2051 0.1496 0.2864 -0.0312 0.0322  -0.0283 21  ALA   B O   
4355 C  CB  . ALA   B 21  ? 0.2095 0.2170 0.3133 -0.0439 0.0406  -0.0434 21  ALA   B CB  
4361 N  N   . ASP   B 22  ? 0.1889 0.1529 0.2762 -0.0243 0.0345  -0.0343 22  ASP   B N   
4362 C  CA  . ASP   B 22  ? 0.1845 0.1454 0.2628 -0.0121 0.0245  -0.0274 22  ASP   B CA  
4363 C  C   . ASP   B 22  ? 0.1774 0.1414 0.2195 -0.0204 0.0154  -0.0153 22  ASP   B C   
4364 O  O   . ASP   B 22  ? 0.1783 0.1478 0.2205 -0.0144 0.0077  -0.0082 22  ASP   B O   
4365 C  CB  . ASP   B 22  ? 0.1933 0.1566 0.2957 -0.0059 0.0263  -0.0125 22  ASP   B CB  
4366 C  CG  . ASP   B 22  ? 0.1977 0.1751 0.3336 -0.0020 0.0073  -0.0110 22  ASP   B CG  
4367 O  OD1 . ASP   B 22  ? 0.2090 0.1678 0.3279 -0.0040 -0.0091 -0.0111 22  ASP   B OD1 
4368 O  OD2 . ASP   B 22  ? 0.2049 0.2003 0.3802 0.0048  -0.0089 -0.0218 22  ASP   B OD2 
4373 N  N   . ILE   B 23  ? 0.1767 0.1415 0.1992 -0.0115 0.0048  0.0149  23  ILE   B N   
4374 C  CA  . ILE   B 23  ? 0.1687 0.1367 0.1815 -0.0108 0.0053  0.0093  23  ILE   B CA  
4375 C  C   . ILE   B 23  ? 0.1603 0.1376 0.1803 -0.0081 -0.0089 0.0049  23  ILE   B C   
4376 O  O   . ILE   B 23  ? 0.1499 0.1350 0.1785 -0.0108 -0.0066 0.0075  23  ILE   B O   
4377 C  CB  . ILE   B 23  ? 0.1626 0.1448 0.1942 -0.0212 0.0045  0.0156  23  ILE   B CB  
4378 C  CG1 . ILE   B 23  ? 0.1629 0.1539 0.2158 -0.0166 0.0039  0.0253  23  ILE   B CG1 
4379 C  CG2 . ILE   B 23  ? 0.1725 0.1681 0.2044 -0.0186 0.0019  0.0080  23  ILE   B CG2 
4380 C  CD1 . ILE   B 23  ? 0.1744 0.1646 0.2264 -0.0105 0.0046  0.0234  23  ILE   B CD1 
4392 N  N   . VAL   B 24  ? 0.1630 0.1391 0.1858 -0.0100 -0.0089 0.0058  24  VAL   B N   
4393 C  CA  . VAL   B 24  ? 0.1555 0.1430 0.2090 -0.0074 -0.0171 0.0013  24  VAL   B CA  
4394 C  C   . VAL   B 24  ? 0.1535 0.1442 0.2182 -0.0148 -0.0050 -0.0013 24  VAL   B C   
4395 O  O   . VAL   B 24  ? 0.1512 0.1540 0.2233 -0.0212 -0.0032 0.0089  24  VAL   B O   
4396 C  CB  . VAL   B 24  ? 0.1656 0.1621 0.2154 0.0032  -0.0197 0.0009  24  VAL   B CB  
4397 C  CG1 . VAL   B 24  ? 0.1640 0.1684 0.2370 -0.0073 -0.0190 0.0045  24  VAL   B CG1 
4398 C  CG2 . VAL   B 24  ? 0.1762 0.1918 0.2175 0.0041  -0.0206 -0.0059 24  VAL   B CG2 
4408 N  N   . GLU   B 25  ? 0.1797 0.1567 0.2228 -0.0123 0.0013  -0.0010 25  GLU   B N   
4409 C  CA  . GLU   B 25  ? 0.1903 0.1850 0.2406 -0.0036 0.0156  -0.0040 25  GLU   B CA  
4410 C  C   . GLU   B 25  ? 0.1813 0.1808 0.2100 -0.0168 0.0124  -0.0010 25  GLU   B C   
4411 O  O   . GLU   B 25  ? 0.1858 0.1955 0.2264 -0.0147 0.0191  0.0020  25  GLU   B O   
4412 C  CB  . GLU   B 25  ? 0.2334 0.2335 0.3098 0.0243  0.0278  -0.0057 25  GLU   B CB  
4413 C  CG  . GLU   B 25  ? 0.2760 0.2912 0.4152 0.0339  0.0240  -0.0055 25  GLU   B CG  
4414 C  CD  . GLU   B 25  ? 0.3206 0.3464 0.5045 0.0322  0.0195  -0.0062 25  GLU   B CD  
4415 O  OE1 . GLU   B 25  ? 0.3439 0.3698 0.5327 0.0380  0.0224  -0.0035 25  GLU   B OE1 
4416 O  OE2 . GLU   B 25  ? 0.3408 0.3660 0.5341 0.0310  0.0122  -0.0116 25  GLU   B OE2 
4423 N  N   A GLU   B 26  ? 0.1788 0.1745 0.1852 -0.0344 0.0035  -0.0006 26  GLU   B N   
4424 N  N   B GLU   B 26  ? 0.1823 0.1812 0.1942 -0.0261 0.0080  0.0016  26  GLU   B N   
4425 C  CA  A GLU   B 26  ? 0.1808 0.1897 0.1885 -0.0417 -0.0094 0.0049  26  GLU   B CA  
4426 C  CA  B GLU   B 26  ? 0.1841 0.1878 0.1943 -0.0324 0.0023  0.0058  26  GLU   B CA  
4427 C  C   A GLU   B 26  ? 0.1653 0.1868 0.1738 -0.0300 0.0019  0.0153  26  GLU   B C   
4428 C  C   B GLU   B 26  ? 0.1691 0.1817 0.1758 -0.0281 0.0057  0.0131  26  GLU   B C   
4429 O  O   A GLU   B 26  ? 0.1829 0.2062 0.1796 -0.0251 -0.0044 0.0174  26  GLU   B O   
4430 O  O   B GLU   B 26  ? 0.1764 0.1910 0.1748 -0.0257 0.0021  0.0132  26  GLU   B O   
4431 C  CB  A GLU   B 26  ? 0.2151 0.2105 0.2103 -0.0496 0.0004  0.0133  26  GLU   B CB  
4432 C  CB  B GLU   B 26  ? 0.2046 0.2018 0.2163 -0.0391 0.0049  0.0059  26  GLU   B CB  
4433 C  CG  A GLU   B 26  ? 0.2566 0.2436 0.2623 -0.0524 0.0198  -0.0005 26  GLU   B CG  
4434 C  CG  B GLU   B 26  ? 0.2276 0.2208 0.2503 -0.0446 0.0119  -0.0021 26  GLU   B CG  
4435 C  CD  A GLU   B 26  ? 0.2844 0.2675 0.2869 -0.0641 0.0425  -0.0233 26  GLU   B CD  
4436 C  CD  B GLU   B 26  ? 0.2444 0.2355 0.2716 -0.0538 0.0202  -0.0143 26  GLU   B CD  
4437 O  OE1 A GLU   B 26  ? 0.2994 0.2550 0.2940 -0.0735 0.0731  -0.0215 26  GLU   B OE1 
4438 O  OE1 B GLU   B 26  ? 0.2546 0.2319 0.2792 -0.0604 0.0347  -0.0149 26  GLU   B OE1 
4439 O  OE2 A GLU   B 26  ? 0.2909 0.3007 0.3185 -0.0610 0.0444  -0.0166 26  GLU   B OE2 
4440 O  OE2 B GLU   B 26  ? 0.2478 0.2530 0.2929 -0.0519 0.0195  -0.0123 26  GLU   B OE2 
4453 N  N   . ALA   B 27  ? 0.1529 0.1673 0.1710 -0.0269 0.0093  0.0191  27  ALA   B N   
4454 C  CA  . ALA   B 27  ? 0.1518 0.1633 0.1908 -0.0187 0.0053  0.0282  27  ALA   B CA  
4455 C  C   . ALA   B 27  ? 0.1513 0.1724 0.2163 -0.0174 0.0138  0.0425  27  ALA   B C   
4456 O  O   . ALA   B 27  ? 0.1616 0.1782 0.2249 -0.0044 0.0105  0.0498  27  ALA   B O   
4457 C  CB  . ALA   B 27  ? 0.1665 0.1497 0.1937 -0.0194 0.0030  0.0245  27  ALA   B CB  
4464 N  N   . LYS   B 28  ? 0.1500 0.1931 0.2567 -0.0221 0.0221  0.0564  28  LYS   B N   
4465 C  CA  . LYS   B 28  ? 0.1657 0.2314 0.2828 -0.0119 0.0543  0.0836  28  LYS   B CA  
4466 C  C   . LYS   B 28  ? 0.1935 0.2476 0.2702 -0.0029 0.0684  0.0772  28  LYS   B C   
4467 O  O   . LYS   B 28  ? 0.2162 0.2511 0.2807 -0.0049 0.0633  0.0702  28  LYS   B O   
4468 C  CB  . LYS   B 28  ? 0.1884 0.2668 0.3288 0.0022  0.0793  0.1070  28  LYS   B CB  
4469 C  CG  . LYS   B 28  ? 0.2195 0.3161 0.3728 0.0127  0.0827  0.1162  28  LYS   B CG  
4470 C  CD  . LYS   B 28  ? 0.2716 0.3756 0.4302 0.0200  0.0955  0.1163  28  LYS   B CD  
4471 C  CE  . LYS   B 28  ? 0.3131 0.4211 0.4756 0.0260  0.1015  0.1221  28  LYS   B CE  
4472 N  NZ  . LYS   B 28  ? 0.3312 0.4358 0.4985 0.0314  0.1005  0.1279  28  LYS   B NZ  
4486 N  N   . LYS   B 29  ? 0.2115 0.2752 0.2739 0.0167  0.0709  0.0688  29  LYS   B N   
4487 C  CA  . LYS   B 29  ? 0.2585 0.3129 0.3044 0.0188  0.0690  0.0676  29  LYS   B CA  
4488 C  C   . LYS   B 29  ? 0.2498 0.3120 0.2609 0.0195  0.0526  0.0778  29  LYS   B C   
4489 O  O   . LYS   B 29  ? 0.2688 0.3295 0.2677 0.0260  0.0464  0.0827  29  LYS   B O   
4490 C  CB  . LYS   B 29  ? 0.3203 0.3537 0.3911 0.0155  0.0693  0.0558  29  LYS   B CB  
4491 C  CG  . LYS   B 29  ? 0.3720 0.3871 0.4832 0.0110  0.0704  0.0514  29  LYS   B CG  
4492 C  CD  . LYS   B 29  ? 0.4182 0.4122 0.5564 0.0055  0.0773  0.0455  29  LYS   B CD  
4493 C  CE  . LYS   B 29  ? 0.4514 0.4296 0.6047 0.0008  0.0848  0.0416  29  LYS   B CE  
4494 N  NZ  . LYS   B 29  ? 0.4647 0.4371 0.6335 -0.0013 0.0877  0.0388  29  LYS   B NZ  
4508 N  N   . VAL   B 30  ? 0.2162 0.2923 0.2407 0.0083  0.0364  0.0784  30  VAL   B N   
4509 C  CA  . VAL   B 30  ? 0.2018 0.2794 0.2743 -0.0078 0.0024  0.0775  30  VAL   B CA  
4510 C  C   . VAL   B 30  ? 0.1790 0.2710 0.2593 -0.0101 0.0055  0.0949  30  VAL   B C   
4511 O  O   . VAL   B 30  ? 0.1925 0.2879 0.2597 -0.0037 0.0086  0.1067  30  VAL   B O   
4512 C  CB  . VAL   B 30  ? 0.2042 0.2718 0.3139 -0.0245 -0.0239 0.0731  30  VAL   B CB  
4513 C  CG1 . VAL   B 30  ? 0.2098 0.2780 0.3183 -0.0258 -0.0120 0.0678  30  VAL   B CG1 
4514 C  CG2 . VAL   B 30  ? 0.2151 0.2698 0.3314 -0.0323 -0.0408 0.0640  30  VAL   B CG2 
4524 N  N   . LYS   B 31  ? 0.1691 0.2332 0.2851 -0.0279 0.0016  0.1024  31  LYS   B N   
4525 C  CA  . LYS   B 31  ? 0.1578 0.2245 0.3214 -0.0395 -0.0035 0.1008  31  LYS   B CA  
4526 C  C   . LYS   B 31  ? 0.1531 0.1890 0.2771 -0.0369 -0.0258 0.0858  31  LYS   B C   
4527 O  O   . LYS   B 31  ? 0.1601 0.2044 0.2903 -0.0297 -0.0251 0.1027  31  LYS   B O   
4528 C  CB  . LYS   B 31  ? 0.1733 0.2674 0.3770 -0.0366 0.0239  0.1094  31  LYS   B CB  
4529 C  CG  . LYS   B 31  ? 0.2066 0.3112 0.4203 -0.0329 0.0403  0.1046  31  LYS   B CG  
4530 C  CD  . LYS   B 31  ? 0.2434 0.3562 0.4637 -0.0262 0.0387  0.0885  31  LYS   B CD  
4531 C  CE  . LYS   B 31  ? 0.2699 0.3850 0.5007 -0.0221 0.0300  0.0748  31  LYS   B CE  
4532 N  NZ  . LYS   B 31  ? 0.2860 0.3999 0.5130 -0.0149 0.0200  0.0636  31  LYS   B NZ  
4546 N  N   . PRO   B 32  ? 0.1667 0.1533 0.2217 -0.0374 -0.0428 0.0485  32  PRO   B N   
4547 C  CA  . PRO   B 32  ? 0.1753 0.1494 0.1824 -0.0375 -0.0428 0.0305  32  PRO   B CA  
4548 C  C   . PRO   B 32  ? 0.1848 0.1424 0.1826 -0.0414 -0.0581 0.0320  32  PRO   B C   
4549 O  O   . PRO   B 32  ? 0.1988 0.1452 0.2149 -0.0452 -0.0713 0.0344  32  PRO   B O   
4550 C  CB  . PRO   B 32  ? 0.1896 0.1472 0.1785 -0.0424 -0.0275 0.0217  32  PRO   B CB  
4551 C  CG  . PRO   B 32  ? 0.2051 0.1381 0.1886 -0.0341 -0.0471 0.0213  32  PRO   B CG  
4552 C  CD  . PRO   B 32  ? 0.1914 0.1377 0.2086 -0.0263 -0.0605 0.0261  32  PRO   B CD  
4560 N  N   . THR   B 33  ? 0.1915 0.1313 0.1731 -0.0324 -0.0540 0.0249  33  THR   B N   
4561 C  CA  . THR   B 33  ? 0.1965 0.1366 0.1764 -0.0373 -0.0450 0.0284  33  THR   B CA  
4562 C  C   . THR   B 33  ? 0.1966 0.1274 0.1696 -0.0386 -0.0473 0.0202  33  THR   B C   
4563 O  O   . THR   B 33  ? 0.2149 0.1305 0.1843 -0.0452 -0.0568 0.0201  33  THR   B O   
4564 C  CB  . THR   B 33  ? 0.2023 0.1462 0.1820 -0.0192 -0.0530 0.0252  33  THR   B CB  
4565 O  OG1 . THR   B 33  ? 0.1913 0.1519 0.1846 -0.0246 -0.0466 0.0273  33  THR   B OG1 
4566 C  CG2 . THR   B 33  ? 0.2272 0.1526 0.1959 -0.0120 -0.0552 0.0249  33  THR   B CG2 
4574 N  N   . VAL   B 34  ? 0.1802 0.1251 0.1595 -0.0382 -0.0462 0.0205  34  VAL   B N   
4575 C  CA  . VAL   B 34  ? 0.1690 0.1224 0.1604 -0.0314 -0.0352 0.0107  34  VAL   B CA  
4576 C  C   . VAL   B 34  ? 0.1515 0.1219 0.1393 -0.0281 -0.0230 0.0102  34  VAL   B C   
4577 O  O   . VAL   B 34  ? 0.1663 0.1230 0.1466 -0.0231 -0.0338 0.0069  34  VAL   B O   
4578 C  CB  . VAL   B 34  ? 0.1714 0.1272 0.1839 -0.0101 -0.0260 0.0003  34  VAL   B CB  
4579 C  CG1 . VAL   B 34  ? 0.1687 0.1487 0.1826 -0.0072 -0.0121 -0.0010 34  VAL   B CG1 
4580 C  CG2 . VAL   B 34  ? 0.1749 0.1336 0.2081 -0.0143 -0.0274 0.0071  34  VAL   B CG2 
4590 N  N   . VAL   B 35  ? 0.1380 0.1173 0.1372 -0.0253 -0.0138 0.0083  35  VAL   B N   
4591 C  CA  . VAL   B 35  ? 0.1348 0.1153 0.1311 -0.0220 -0.0113 0.0094  35  VAL   B CA  
4592 C  C   . VAL   B 35  ? 0.1245 0.1132 0.1354 -0.0198 -0.0143 0.0102  35  VAL   B C   
4593 O  O   . VAL   B 35  ? 0.1317 0.1181 0.1412 -0.0254 -0.0027 -0.0034 35  VAL   B O   
4594 C  CB  . VAL   B 35  ? 0.1340 0.1329 0.1491 -0.0186 -0.0020 0.0048  35  VAL   B CB  
4595 C  CG1 . VAL   B 35  ? 0.1304 0.1461 0.1729 -0.0242 -0.0027 0.0006  35  VAL   B CG1 
4596 C  CG2 . VAL   B 35  ? 0.1358 0.1360 0.1669 -0.0108 0.0008  0.0027  35  VAL   B CG2 
4606 N  N   . VAL   B 36  ? 0.1245 0.1158 0.1316 -0.0184 -0.0119 0.0115  36  VAL   B N   
4607 C  CA  . VAL   B 36  ? 0.1253 0.1124 0.1312 -0.0148 -0.0054 0.0094  36  VAL   B CA  
4608 C  C   . VAL   B 36  ? 0.1211 0.1118 0.1251 -0.0150 -0.0006 0.0026  36  VAL   B C   
4609 O  O   . VAL   B 36  ? 0.1297 0.1238 0.1510 -0.0124 -0.0004 -0.0029 36  VAL   B O   
4610 C  CB  . VAL   B 36  ? 0.1278 0.1205 0.1368 -0.0155 -0.0063 0.0045  36  VAL   B CB  
4611 C  CG1 . VAL   B 36  ? 0.1233 0.1337 0.1586 -0.0171 -0.0052 0.0052  36  VAL   B CG1 
4612 C  CG2 . VAL   B 36  ? 0.1314 0.1247 0.1517 -0.0121 -0.0113 0.0047  36  VAL   B CG2 
4622 N  N   . ASN   B 37  ? 0.1241 0.1176 0.1286 -0.0045 -0.0061 0.0066  37  ASN   B N   
4623 C  CA  . ASN   B 37  ? 0.1251 0.1211 0.1359 -0.0013 -0.0143 0.0067  37  ASN   B CA  
4624 C  C   . ASN   B 37  ? 0.1257 0.1216 0.1337 -0.0007 -0.0137 0.0044  37  ASN   B C   
4625 O  O   . ASN   B 37  ? 0.1325 0.1273 0.1479 0.0011  0.0003  0.0112  37  ASN   B O   
4626 C  CB  . ASN   B 37  ? 0.1243 0.1266 0.1332 0.0016  -0.0131 0.0053  37  ASN   B CB  
4627 C  CG  . ASN   B 37  ? 0.1287 0.1211 0.1486 -0.0046 -0.0068 -0.0007 37  ASN   B CG  
4628 O  OD1 . ASN   B 37  ? 0.1375 0.1267 0.1545 0.0060  -0.0138 0.0056  37  ASN   B OD1 
4629 N  ND2 . ASN   B 37  ? 0.1371 0.1188 0.1509 -0.0015 -0.0166 0.0097  37  ASN   B ND2 
4636 N  N   . ALA   B 38  ? 0.1360 0.1171 0.1347 0.0035  -0.0008 0.0095  38  ALA   B N   
4637 C  CA  . ALA   B 38  ? 0.1429 0.1221 0.1361 -0.0010 0.0033  0.0119  38  ALA   B CA  
4638 C  C   . ALA   B 38  ? 0.1347 0.1185 0.1431 -0.0040 0.0001  0.0093  38  ALA   B C   
4639 O  O   . ALA   B 38  ? 0.1475 0.1323 0.1600 0.0045  -0.0044 0.0120  38  ALA   B O   
4640 C  CB  . ALA   B 38  ? 0.1661 0.1277 0.1568 -0.0106 0.0043  0.0106  38  ALA   B CB  
4646 N  N   . ALA   B 39  ? 0.1407 0.1205 0.1322 0.0050  -0.0003 0.0061  39  ALA   B N   
4647 C  CA  . ALA   B 39  ? 0.1469 0.1284 0.1365 0.0046  -0.0052 0.0079  39  ALA   B CA  
4648 C  C   . ALA   B 39  ? 0.1516 0.1314 0.1244 0.0072  -0.0024 0.0067  39  ALA   B C   
4649 O  O   . ALA   B 39  ? 0.1568 0.1392 0.1545 -0.0021 -0.0016 0.0134  39  ALA   B O   
4650 C  CB  . ALA   B 39  ? 0.1440 0.1274 0.1637 -0.0036 0.0062  0.0034  39  ALA   B CB  
4656 N  N   . ASN   B 40  ? 0.1532 0.1544 0.1240 -0.0040 0.0007  -0.0059 40  ASN   B N   
4657 C  CA  . ASN   B 40  ? 0.1621 0.1640 0.1421 -0.0006 -0.0029 -0.0064 40  ASN   B CA  
4658 C  C   . ASN   B 40  ? 0.1667 0.1602 0.1217 0.0088  -0.0069 0.0009  40  ASN   B C   
4659 O  O   . ASN   B 40  ? 0.1607 0.1521 0.1412 0.0067  -0.0094 0.0063  40  ASN   B O   
4660 C  CB  . ASN   B 40  ? 0.1736 0.1616 0.1609 0.0103  -0.0134 0.0106  40  ASN   B CB  
4661 C  CG  . ASN   B 40  ? 0.1766 0.1668 0.2006 0.0035  -0.0247 0.0162  40  ASN   B CG  
4662 O  OD1 . ASN   B 40  ? 0.1711 0.1625 0.2707 0.0048  -0.0325 0.0231  40  ASN   B OD1 
4663 N  ND2 . ASN   B 40  ? 0.1814 0.1676 0.1987 0.0039  -0.0198 0.0187  40  ASN   B ND2 
4670 N  N   . VAL   B 41  ? 0.1729 0.1655 0.1323 0.0129  0.0050  -0.0001 41  VAL   B N   
4671 C  CA  . VAL   B 41  ? 0.1800 0.1744 0.1434 0.0087  0.0059  -0.0103 41  VAL   B CA  
4672 C  C   . VAL   B 41  ? 0.1761 0.1714 0.1303 0.0158  -0.0041 -0.0111 41  VAL   B C   
4673 O  O   . VAL   B 41  ? 0.1746 0.1674 0.1450 0.0098  -0.0140 -0.0098 41  VAL   B O   
4674 C  CB  . VAL   B 41  ? 0.1954 0.1928 0.1648 -0.0030 0.0235  -0.0200 41  VAL   B CB  
4675 C  CG1 . VAL   B 41  ? 0.1933 0.1938 0.1797 -0.0058 0.0279  -0.0205 41  VAL   B CG1 
4676 C  CG2 . VAL   B 41  ? 0.2081 0.2115 0.1732 -0.0120 0.0237  -0.0223 41  VAL   B CG2 
4686 N  N   . TYR   B 42  ? 0.1842 0.1697 0.1361 0.0171  -0.0159 0.0007  42  TYR   B N   
4687 C  CA  . TYR   B 42  ? 0.1850 0.1802 0.1464 0.0179  -0.0213 -0.0144 42  TYR   B CA  
4688 C  C   . TYR   B 42  ? 0.1671 0.1588 0.1605 0.0209  -0.0242 -0.0103 42  TYR   B C   
4689 O  O   . TYR   B 42  ? 0.1709 0.1682 0.1929 0.0138  -0.0244 -0.0171 42  TYR   B O   
4690 C  CB  . TYR   B 42  ? 0.2093 0.2086 0.1658 0.0128  -0.0261 -0.0022 42  TYR   B CB  
4691 C  CG  . TYR   B 42  ? 0.2093 0.2241 0.1593 0.0014  -0.0252 0.0112  42  TYR   B CG  
4692 C  CD1 . TYR   B 42  ? 0.2065 0.2228 0.1299 -0.0054 -0.0147 0.0063  42  TYR   B CD1 
4693 C  CD2 . TYR   B 42  ? 0.2227 0.2355 0.1915 0.0005  -0.0089 0.0199  42  TYR   B CD2 
4694 C  CE1 . TYR   B 42  ? 0.2183 0.2357 0.1397 0.0015  -0.0080 0.0088  42  TYR   B CE1 
4695 C  CE2 . TYR   B 42  ? 0.2291 0.2430 0.1850 0.0049  0.0174  0.0367  42  TYR   B CE2 
4696 C  CZ  . TYR   B 42  ? 0.2391 0.2545 0.1786 0.0191  0.0201  0.0207  42  TYR   B CZ  
4697 O  OH  . TYR   B 42  ? 0.2742 0.2828 0.2302 0.0370  0.0312  0.0264  42  TYR   B OH  
4707 N  N   . LEU   B 43  ? 0.1556 0.1450 0.1502 0.0093  -0.0149 -0.0145 43  LEU   B N   
4708 C  CA  . LEU   B 43  ? 0.1576 0.1452 0.1370 0.0035  -0.0133 -0.0004 43  LEU   B CA  
4709 C  C   . LEU   B 43  ? 0.1627 0.1473 0.1410 0.0051  -0.0112 0.0029  43  LEU   B C   
4710 O  O   . LEU   B 43  ? 0.1607 0.1523 0.1716 0.0083  -0.0179 0.0052  43  LEU   B O   
4711 C  CB  . LEU   B 43  ? 0.1552 0.1395 0.1472 -0.0020 -0.0226 -0.0046 43  LEU   B CB  
4712 C  CG  . LEU   B 43  ? 0.1620 0.1350 0.1587 0.0023  -0.0209 -0.0097 43  LEU   B CG  
4713 C  CD1 . LEU   B 43  ? 0.1715 0.1431 0.1908 0.0019  -0.0402 -0.0071 43  LEU   B CD1 
4714 C  CD2 . LEU   B 43  ? 0.1567 0.1404 0.1666 -0.0095 -0.0243 -0.0037 43  LEU   B CD2 
4726 N  N   . LYS   B 44  ? 0.1571 0.1466 0.1474 0.0093  -0.0112 -0.0039 44  LYS   B N   
4727 C  CA  . LYS   B 44  ? 0.1720 0.1578 0.1512 0.0098  -0.0138 0.0079  44  LYS   B CA  
4728 C  C   . LYS   B 44  ? 0.1594 0.1525 0.1465 0.0121  -0.0158 0.0018  44  LYS   B C   
4729 O  O   . LYS   B 44  ? 0.1816 0.1502 0.1778 0.0016  -0.0068 0.0046  44  LYS   B O   
4730 C  CB  . LYS   B 44  ? 0.2019 0.1764 0.1659 0.0190  -0.0247 0.0041  44  LYS   B CB  
4731 C  CG  . LYS   B 44  ? 0.2423 0.2041 0.2005 0.0098  -0.0511 0.0101  44  LYS   B CG  
4732 C  CD  . LYS   B 44  ? 0.2788 0.2268 0.2665 -0.0049 -0.0597 0.0073  44  LYS   B CD  
4733 C  CE  . LYS   B 44  ? 0.3103 0.2528 0.3139 -0.0125 -0.0662 0.0195  44  LYS   B CE  
4734 N  NZ  . LYS   B 44  ? 0.3215 0.2609 0.3422 -0.0129 -0.0731 0.0334  44  LYS   B NZ  
4748 N  N   . HIS   B 45  ? 0.1485 0.1541 0.1477 0.0062  -0.0143 0.0126  45  HIS   B N   
4749 C  CA  . HIS   B 45  ? 0.1533 0.1488 0.1504 0.0110  -0.0100 -0.0004 45  HIS   B CA  
4750 C  C   . HIS   B 45  ? 0.1806 0.1725 0.1870 0.0158  -0.0180 -0.0062 45  HIS   B C   
4751 O  O   . HIS   B 45  ? 0.1924 0.1986 0.2302 0.0431  0.0021  -0.0024 45  HIS   B O   
4752 C  CB  . HIS   B 45  ? 0.1468 0.1547 0.1556 -0.0020 -0.0078 -0.0013 45  HIS   B CB  
4753 C  CG  . HIS   B 45  ? 0.1505 0.1495 0.1468 -0.0072 -0.0057 -0.0007 45  HIS   B CG  
4754 N  ND1 . HIS   B 45  ? 0.1540 0.1451 0.1499 0.0007  -0.0204 -0.0127 45  HIS   B ND1 
4755 C  CD2 . HIS   B 45  ? 0.1619 0.1485 0.1596 -0.0092 -0.0116 -0.0019 45  HIS   B CD2 
4756 C  CE1 . HIS   B 45  ? 0.1626 0.1331 0.1404 -0.0018 -0.0240 -0.0070 45  HIS   B CE1 
4757 N  NE2 . HIS   B 45  ? 0.1687 0.1412 0.1569 -0.0026 -0.0158 -0.0072 45  HIS   B NE2 
4765 N  N   A GLY   B 46  ? 0.1916 0.1652 0.2185 0.0196  -0.0381 0.0046  46  GLY   B N   
4766 N  N   B GLY   B 46  ? 0.1894 0.1763 0.2005 0.0175  -0.0267 0.0014  46  GLY   B N   
4767 C  CA  A GLY   B 46  ? 0.2047 0.1774 0.2555 0.0175  -0.0441 0.0055  46  GLY   B CA  
4768 C  CA  B GLY   B 46  ? 0.1977 0.1862 0.2194 0.0164  -0.0306 0.0068  46  GLY   B CA  
4769 C  C   A GLY   B 46  ? 0.2039 0.1945 0.2976 0.0256  -0.0394 0.0002  46  GLY   B C   
4770 C  C   B GLY   B 46  ? 0.2012 0.1977 0.2438 0.0200  -0.0296 0.0106  46  GLY   B C   
4771 O  O   A GLY   B 46  ? 0.2089 0.2124 0.3819 0.0287  -0.0223 -0.0250 46  GLY   B O   
4772 O  O   B GLY   B 46  ? 0.2054 0.2046 0.2522 0.0227  -0.0269 0.0219  46  GLY   B O   
4779 N  N   . GLY   B 47  ? 0.2000 0.2036 0.2644 0.0129  -0.0200 -0.0027 47  GLY   B N   
4780 C  CA  . GLY   B 47  ? 0.1863 0.1763 0.2237 0.0028  -0.0190 -0.0017 47  GLY   B CA  
4781 C  C   . GLY   B 47  ? 0.1693 0.1533 0.1964 -0.0004 -0.0064 0.0065  47  GLY   B C   
4782 O  O   . GLY   B 47  ? 0.1802 0.1388 0.2017 -0.0007 -0.0107 0.0107  47  GLY   B O   
4787 N  N   . GLY   B 48  ? 0.1514 0.1441 0.1902 0.0012  -0.0139 0.0179  48  GLY   B N   
4788 C  CA  . GLY   B 48  ? 0.1513 0.1413 0.1901 -0.0027 0.0015  0.0087  48  GLY   B CA  
4789 C  C   . GLY   B 48  ? 0.1434 0.1372 0.1776 -0.0001 0.0093  0.0036  48  GLY   B C   
4790 O  O   . GLY   B 48  ? 0.1398 0.1402 0.2009 0.0018  -0.0112 0.0008  48  GLY   B O   
4794 N  N   . VAL   B 49  ? 0.1462 0.1432 0.1726 0.0125  0.0009  0.0065  49  VAL   B N   
4795 C  CA  . VAL   B 49  ? 0.1479 0.1461 0.1648 0.0099  -0.0134 -0.0011 49  VAL   B CA  
4796 C  C   . VAL   B 49  ? 0.1397 0.1408 0.1497 0.0132  -0.0078 0.0079  49  VAL   B C   
4797 O  O   . VAL   B 49  ? 0.1472 0.1432 0.1593 0.0056  -0.0010 0.0065  49  VAL   B O   
4798 C  CB  . VAL   B 49  ? 0.1516 0.1655 0.1880 0.0030  -0.0223 -0.0021 49  VAL   B CB  
4799 C  CG1 . VAL   B 49  ? 0.1504 0.1693 0.1847 0.0076  -0.0259 0.0023  49  VAL   B CG1 
4800 C  CG2 . VAL   B 49  ? 0.1723 0.1831 0.2111 -0.0044 -0.0368 -0.0064 49  VAL   B CG2 
4810 N  N   . ALA   B 50  ? 0.1331 0.1359 0.1477 0.0029  -0.0029 0.0062  50  ALA   B N   
4811 C  CA  . ALA   B 50  ? 0.1324 0.1268 0.1505 0.0027  -0.0087 0.0063  50  ALA   B CA  
4812 C  C   . ALA   B 50  ? 0.1426 0.1302 0.1514 0.0038  -0.0006 0.0070  50  ALA   B C   
4813 O  O   . ALA   B 50  ? 0.1411 0.1304 0.1531 0.0038  0.0007  -0.0002 50  ALA   B O   
4814 C  CB  . ALA   B 50  ? 0.1392 0.1274 0.1535 0.0023  0.0025  0.0093  50  ALA   B CB  
4820 N  N   . GLY   B 51  ? 0.1388 0.1412 0.1631 0.0096  -0.0130 0.0051  51  GLY   B N   
4821 C  CA  . GLY   B 51  ? 0.1388 0.1503 0.1811 0.0167  -0.0124 0.0021  51  GLY   B CA  
4822 C  C   . GLY   B 51  ? 0.1373 0.1437 0.1757 0.0187  -0.0063 0.0021  51  GLY   B C   
4823 O  O   . GLY   B 51  ? 0.1394 0.1570 0.1954 0.0081  -0.0097 0.0030  51  GLY   B O   
4827 N  N   . ALA   B 52  ? 0.1410 0.1379 0.1700 0.0158  -0.0052 0.0116  52  ALA   B N   
4828 C  CA  . ALA   B 52  ? 0.1452 0.1461 0.1689 0.0141  0.0034  -0.0030 52  ALA   B CA  
4829 C  C   . ALA   B 52  ? 0.1349 0.1463 0.1595 0.0059  -0.0010 -0.0003 52  ALA   B C   
4830 O  O   . ALA   B 52  ? 0.1390 0.1531 0.1787 0.0090  0.0023  0.0015  52  ALA   B O   
4831 C  CB  . ALA   B 52  ? 0.1637 0.1494 0.1779 0.0037  0.0092  -0.0027 52  ALA   B CB  
4837 N  N   . LEU   B 53  ? 0.1303 0.1408 0.1554 0.0171  0.0020  0.0037  53  LEU   B N   
4838 C  CA  . LEU   B 53  ? 0.1350 0.1505 0.1475 0.0130  -0.0059 0.0038  53  LEU   B CA  
4839 C  C   . LEU   B 53  ? 0.1431 0.1384 0.1456 0.0104  0.0030  0.0117  53  LEU   B C   
4840 O  O   . LEU   B 53  ? 0.1492 0.1467 0.1615 0.0026  0.0060  0.0148  53  LEU   B O   
4841 C  CB  . LEU   B 53  ? 0.1329 0.1573 0.1596 0.0098  0.0006  0.0181  53  LEU   B CB  
4842 C  CG  . LEU   B 53  ? 0.1300 0.1679 0.1668 0.0020  -0.0061 0.0237  53  LEU   B CG  
4843 C  CD1 . LEU   B 53  ? 0.1385 0.1865 0.1890 0.0096  -0.0039 0.0022  53  LEU   B CD1 
4844 C  CD2 . LEU   B 53  ? 0.1479 0.1977 0.1921 -0.0094 -0.0176 -0.0050 53  LEU   B CD2 
4856 N  N   . ASN   B 54  ? 0.1395 0.1301 0.1475 0.0044  0.0026  0.0085  54  ASN   B N   
4857 C  CA  . ASN   B 54  ? 0.1429 0.1421 0.1594 0.0032  -0.0047 0.0005  54  ASN   B CA  
4858 C  C   . ASN   B 54  ? 0.1410 0.1444 0.1767 -0.0000 0.0022  -0.0004 54  ASN   B C   
4859 O  O   . ASN   B 54  ? 0.1390 0.1484 0.2019 -0.0037 0.0074  -0.0029 54  ASN   B O   
4860 C  CB  . ASN   B 54  ? 0.1447 0.1553 0.1758 0.0074  0.0002  0.0044  54  ASN   B CB  
4861 C  CG  . ASN   B 54  ? 0.1423 0.1647 0.1729 0.0031  -0.0099 0.0030  54  ASN   B CG  
4862 O  OD1 . ASN   B 54  ? 0.1431 0.1645 0.1814 -0.0008 -0.0109 -0.0145 54  ASN   B OD1 
4863 N  ND2 . ASN   B 54  ? 0.1564 0.1860 0.1893 -0.0007 -0.0288 0.0150  54  ASN   B ND2 
4870 N  N   . LYS   B 55  ? 0.1355 0.1538 0.1967 0.0087  0.0019  -0.0008 55  LYS   B N   
4871 C  CA  . LYS   B 55  ? 0.1420 0.1676 0.2170 0.0143  -0.0015 0.0008  55  LYS   B CA  
4872 C  C   . LYS   B 55  ? 0.1368 0.1659 0.2089 0.0106  0.0068  -0.0080 55  LYS   B C   
4873 O  O   . LYS   B 55  ? 0.1328 0.1839 0.2263 0.0122  0.0104  -0.0103 55  LYS   B O   
4874 C  CB  . LYS   B 55  ? 0.1559 0.1804 0.2523 0.0251  0.0106  0.0114  55  LYS   B CB  
4875 C  CG  . LYS   B 55  ? 0.1957 0.2123 0.3308 0.0352  0.0265  0.0297  55  LYS   B CG  
4876 C  CD  . LYS   B 55  ? 0.2354 0.2392 0.4017 0.0456  0.0424  0.0440  55  LYS   B CD  
4877 C  CE  . LYS   B 55  ? 0.2626 0.2624 0.4681 0.0469  0.0564  0.0528  55  LYS   B CE  
4878 N  NZ  . LYS   B 55  ? 0.2711 0.2781 0.5028 0.0455  0.0471  0.0621  55  LYS   B NZ  
4892 N  N   . ALA   B 56  ? 0.1346 0.1711 0.1903 0.0095  0.0044  -0.0116 56  ALA   B N   
4893 C  CA  . ALA   B 56  ? 0.1485 0.1877 0.1909 0.0056  0.0102  -0.0105 56  ALA   B CA  
4894 C  C   . ALA   B 56  ? 0.1500 0.1825 0.1848 0.0018  0.0167  -0.0018 56  ALA   B C   
4895 O  O   . ALA   B 56  ? 0.1628 0.1935 0.2063 0.0069  0.0340  -0.0017 56  ALA   B O   
4896 C  CB  . ALA   B 56  ? 0.1607 0.2077 0.1974 -0.0055 0.0090  -0.0132 56  ALA   B CB  
4902 N  N   . THR   B 57  ? 0.1405 0.1730 0.1914 -0.0041 0.0190  0.0058  57  THR   B N   
4903 C  CA  . THR   B 57  ? 0.1470 0.1756 0.1874 -0.0061 0.0215  0.0058  57  THR   B CA  
4904 C  C   . THR   B 57  ? 0.1506 0.1834 0.2118 -0.0040 0.0219  0.0058  57  THR   B C   
4905 O  O   . THR   B 57  ? 0.1593 0.1817 0.2217 -0.0209 0.0179  0.0020  57  THR   B O   
4906 C  CB  . THR   B 57  ? 0.1545 0.1588 0.1651 -0.0016 0.0206  0.0093  57  THR   B CB  
4907 O  OG1 . THR   B 57  ? 0.1515 0.1504 0.1926 -0.0026 0.0213  0.0005  57  THR   B OG1 
4908 C  CG2 . THR   B 57  ? 0.1500 0.1632 0.1614 -0.0015 0.0173  0.0050  57  THR   B CG2 
4916 N  N   . ASN   B 58  ? 0.1360 0.2061 0.2313 -0.0090 0.0092  -0.0136 58  ASN   B N   
4917 C  CA  . ASN   B 58  ? 0.1624 0.2525 0.2731 -0.0239 0.0390  -0.0045 58  ASN   B CA  
4918 C  C   . ASN   B 58  ? 0.1396 0.2234 0.2265 -0.0158 0.0049  -0.0031 58  ASN   B C   
4919 O  O   . ASN   B 58  ? 0.1451 0.2278 0.2385 -0.0162 0.0047  -0.0114 58  ASN   B O   
4920 C  CB  . ASN   B 58  ? 0.2676 0.3395 0.4041 -0.0397 0.0806  0.0106  58  ASN   B CB  
4921 C  CG  . ASN   B 58  ? 0.3926 0.4269 0.5568 -0.0424 0.0951  0.0312  58  ASN   B CG  
4922 O  OD1 . ASN   B 58  ? 0.4133 0.4494 0.6124 -0.0435 0.0976  0.0365  58  ASN   B OD1 
4923 N  ND2 . ASN   B 58  ? 0.5008 0.5008 0.6086 -0.0443 0.1008  0.0371  58  ASN   B ND2 
4930 N  N   . ASN   B 59  ? 0.1395 0.2050 0.2057 -0.0116 -0.0021 0.0026  59  ASN   B N   
4931 C  CA  . ASN   B 59  ? 0.1413 0.2027 0.2073 -0.0144 -0.0138 0.0042  59  ASN   B CA  
4932 C  C   . ASN   B 59  ? 0.1363 0.1902 0.1920 -0.0156 -0.0092 -0.0051 59  ASN   B C   
4933 O  O   . ASN   B 59  ? 0.1383 0.1914 0.1934 -0.0157 -0.0119 -0.0015 59  ASN   B O   
4934 C  CB  . ASN   B 59  ? 0.1513 0.2208 0.2188 -0.0030 -0.0272 0.0089  59  ASN   B CB  
4935 C  CG  . ASN   B 59  ? 0.1634 0.2312 0.2341 -0.0001 -0.0388 0.0089  59  ASN   B CG  
4936 O  OD1 . ASN   B 59  ? 0.1647 0.2369 0.2348 0.0007  -0.0189 0.0214  59  ASN   B OD1 
4937 N  ND2 . ASN   B 59  ? 0.1736 0.2417 0.2405 -0.0079 -0.0394 0.0031  59  ASN   B ND2 
4944 N  N   . ALA   B 60  ? 0.1423 0.1758 0.1935 -0.0137 0.0004  -0.0021 60  ALA   B N   
4945 C  CA  . ALA   B 60  ? 0.1486 0.1655 0.1971 -0.0240 -0.0008 0.0075  60  ALA   B CA  
4946 C  C   . ALA   B 60  ? 0.1502 0.1548 0.1767 -0.0173 -0.0082 0.0029  60  ALA   B C   
4947 O  O   . ALA   B 60  ? 0.1556 0.1537 0.1983 -0.0195 0.0006  -0.0095 60  ALA   B O   
4948 C  CB  . ALA   B 60  ? 0.1695 0.1650 0.2261 -0.0170 0.0059  0.0119  60  ALA   B CB  
4954 N  N   . MET   B 61  ? 0.1410 0.1490 0.1698 -0.0093 -0.0007 0.0055  61  MET   B N   
4955 C  CA  . MET   B 61  ? 0.1329 0.1430 0.1639 -0.0077 -0.0110 0.0050  61  MET   B CA  
4956 C  C   . MET   B 61  ? 0.1420 0.1431 0.1668 -0.0120 -0.0106 0.0017  61  MET   B C   
4957 O  O   . MET   B 61  ? 0.1481 0.1380 0.1554 -0.0031 -0.0069 -0.0115 61  MET   B O   
4958 C  CB  . MET   B 61  ? 0.1285 0.1476 0.1624 0.0005  -0.0095 -0.0035 61  MET   B CB  
4959 C  CG  . MET   B 61  ? 0.1316 0.1458 0.1582 -0.0002 -0.0077 0.0027  61  MET   B CG  
4960 S  SD  . MET   B 61  ? 0.1381 0.1457 0.1777 -0.0036 -0.0052 -0.0083 61  MET   B SD  
4961 C  CE  . MET   B 61  ? 0.1465 0.1603 0.2060 0.0034  -0.0024 -0.0211 61  MET   B CE  
4971 N  N   . GLN   B 62  ? 0.1405 0.1478 0.1589 -0.0053 -0.0159 0.0033  62  GLN   B N   
4972 C  CA  . GLN   B 62  ? 0.1429 0.1512 0.1704 -0.0021 -0.0155 -0.0010 62  GLN   B CA  
4973 C  C   . GLN   B 62  ? 0.1412 0.1572 0.1764 -0.0066 -0.0200 -0.0095 62  GLN   B C   
4974 O  O   . GLN   B 62  ? 0.1533 0.1599 0.1807 -0.0016 -0.0279 -0.0114 62  GLN   B O   
4975 C  CB  . GLN   B 62  ? 0.1456 0.1567 0.1728 0.0021  -0.0117 0.0038  62  GLN   B CB  
4976 C  CG  . GLN   B 62  ? 0.1457 0.1612 0.1746 0.0021  -0.0265 -0.0039 62  GLN   B CG  
4977 C  CD  . GLN   B 62  ? 0.1513 0.1576 0.1678 0.0043  -0.0245 0.0027  62  GLN   B CD  
4978 O  OE1 . GLN   B 62  ? 0.1523 0.1533 0.1838 0.0023  -0.0264 -0.0094 62  GLN   B OE1 
4979 N  NE2 . GLN   B 62  ? 0.1518 0.1670 0.1797 0.0040  -0.0178 -0.0090 62  GLN   B NE2 
4988 N  N   . VAL   B 63  ? 0.1405 0.1603 0.1904 -0.0090 -0.0177 -0.0101 63  VAL   B N   
4989 C  CA  . VAL   B 63  ? 0.1538 0.1618 0.2037 -0.0145 -0.0279 -0.0103 63  VAL   B CA  
4990 C  C   . VAL   B 63  ? 0.1561 0.1531 0.1876 -0.0185 -0.0261 -0.0186 63  VAL   B C   
4991 O  O   . VAL   B 63  ? 0.1672 0.1522 0.2018 -0.0151 -0.0435 -0.0165 63  VAL   B O   
4992 C  CB  . VAL   B 63  ? 0.1558 0.1758 0.2344 -0.0164 -0.0269 -0.0107 63  VAL   B CB  
4993 C  CG1 . VAL   B 63  ? 0.1603 0.1844 0.2387 -0.0253 -0.0207 -0.0093 63  VAL   B CG1 
4994 C  CG2 . VAL   B 63  ? 0.1498 0.1935 0.2481 -0.0112 -0.0331 -0.0156 63  VAL   B CG2 
5004 N  N   . GLU   B 64  ? 0.1546 0.1446 0.1839 -0.0155 -0.0218 -0.0096 64  GLU   B N   
5005 C  CA  . GLU   B 64  ? 0.1568 0.1364 0.1779 -0.0134 -0.0223 -0.0010 64  GLU   B CA  
5006 C  C   . GLU   B 64  ? 0.1485 0.1373 0.1704 -0.0088 -0.0235 -0.0081 64  GLU   B C   
5007 O  O   . GLU   B 64  ? 0.1596 0.1463 0.1735 -0.0111 -0.0225 -0.0129 64  GLU   B O   
5008 C  CB  . GLU   B 64  ? 0.1551 0.1464 0.1717 -0.0170 -0.0164 0.0007  64  GLU   B CB  
5009 C  CG  . GLU   B 64  ? 0.1631 0.1513 0.1706 -0.0263 -0.0285 -0.0104 64  GLU   B CG  
5010 C  CD  . GLU   B 64  ? 0.1655 0.1631 0.1793 -0.0346 -0.0277 0.0002  64  GLU   B CD  
5011 O  OE1 . GLU   B 64  ? 0.1681 0.1827 0.1932 -0.0383 -0.0175 -0.0274 64  GLU   B OE1 
5012 O  OE2 . GLU   B 64  ? 0.1772 0.1724 0.1864 -0.0349 -0.0385 -0.0101 64  GLU   B OE2 
5019 N  N   . SER   B 65  ? 0.1503 0.1345 0.1597 -0.0103 -0.0159 -0.0122 65  SER   B N   
5020 C  CA  . SER   B 65  ? 0.1501 0.1324 0.1638 -0.0026 -0.0176 -0.0125 65  SER   B CA  
5021 C  C   . SER   B 65  ? 0.1515 0.1343 0.1627 0.0010  -0.0199 -0.0140 65  SER   B C   
5022 O  O   . SER   B 65  ? 0.1576 0.1451 0.1711 0.0003  -0.0187 -0.0228 65  SER   B O   
5023 C  CB  . SER   B 65  ? 0.1490 0.1419 0.1663 -0.0121 -0.0190 -0.0096 65  SER   B CB  
5024 O  OG  . SER   B 65  ? 0.1508 0.1435 0.1706 -0.0095 -0.0149 -0.0205 65  SER   B OG  
5030 N  N   . ASP   B 66  ? 0.1589 0.1458 0.1645 -0.0010 -0.0262 -0.0134 66  ASP   B N   
5031 C  CA  . ASP   B 66  ? 0.1682 0.1542 0.1565 0.0050  -0.0315 -0.0101 66  ASP   B CA  
5032 C  C   . ASP   B 66  ? 0.1701 0.1573 0.1539 -0.0031 -0.0248 -0.0134 66  ASP   B C   
5033 O  O   . ASP   B 66  ? 0.1776 0.1636 0.1637 0.0048  -0.0258 -0.0167 66  ASP   B O   
5034 C  CB  . ASP   B 66  ? 0.1796 0.1700 0.1680 0.0108  -0.0424 -0.0153 66  ASP   B CB  
5035 C  CG  . ASP   B 66  ? 0.2088 0.1866 0.1998 0.0188  -0.0532 -0.0022 66  ASP   B CG  
5036 O  OD1 . ASP   B 66  ? 0.2341 0.1828 0.2081 0.0088  -0.0514 0.0030  66  ASP   B OD1 
5037 O  OD2 . ASP   B 66  ? 0.2270 0.2089 0.2618 0.0363  -0.0542 -0.0042 66  ASP   B OD2 
5042 N  N   . ASP   B 67  ? 0.1651 0.1512 0.1533 -0.0083 -0.0214 -0.0202 67  ASP   B N   
5043 C  CA  . ASP   B 67  ? 0.1805 0.1458 0.1644 -0.0079 -0.0245 -0.0078 67  ASP   B CA  
5044 C  C   . ASP   B 67  ? 0.1748 0.1438 0.1761 0.0027  -0.0213 -0.0179 67  ASP   B C   
5045 O  O   . ASP   B 67  ? 0.1845 0.1521 0.1865 -0.0004 -0.0117 -0.0205 67  ASP   B O   
5046 C  CB  . ASP   B 67  ? 0.2027 0.1562 0.1851 -0.0199 -0.0332 -0.0099 67  ASP   B CB  
5047 C  CG  . ASP   B 67  ? 0.2416 0.1642 0.1964 -0.0149 -0.0662 -0.0107 67  ASP   B CG  
5048 O  OD1 . ASP   B 67  ? 0.2659 0.1703 0.2179 -0.0133 -0.0671 -0.0109 67  ASP   B OD1 
5049 O  OD2 . ASP   B 67  ? 0.2573 0.1699 0.2127 0.0018  -0.0741 -0.0079 67  ASP   B OD2 
5054 N  N   . TYR   B 68  ? 0.1666 0.1458 0.1759 0.0010  -0.0346 -0.0258 68  TYR   B N   
5055 C  CA  . TYR   B 68  ? 0.1653 0.1631 0.1868 0.0050  -0.0369 -0.0340 68  TYR   B CA  
5056 C  C   . TYR   B 68  ? 0.1586 0.1628 0.1802 0.0004  -0.0327 -0.0424 68  TYR   B C   
5057 O  O   . TYR   B 68  ? 0.1665 0.1748 0.1915 0.0064  -0.0309 -0.0489 68  TYR   B O   
5058 C  CB  . TYR   B 68  ? 0.1685 0.1822 0.1960 0.0065  -0.0433 -0.0442 68  TYR   B CB  
5059 C  CG  . TYR   B 68  ? 0.1823 0.1979 0.2024 0.0115  -0.0383 -0.0628 68  TYR   B CG  
5060 C  CD1 . TYR   B 68  ? 0.1851 0.2024 0.2300 -0.0051 -0.0303 -0.0650 68  TYR   B CD1 
5061 C  CD2 . TYR   B 68  ? 0.1872 0.2216 0.2110 0.0182  -0.0517 -0.0559 68  TYR   B CD2 
5062 C  CE1 . TYR   B 68  ? 0.1885 0.2182 0.2506 -0.0043 -0.0298 -0.0643 68  TYR   B CE1 
5063 C  CE2 . TYR   B 68  ? 0.1907 0.2281 0.2248 0.0169  -0.0403 -0.0667 68  TYR   B CE2 
5064 C  CZ  . TYR   B 68  ? 0.1863 0.2291 0.2488 0.0043  -0.0360 -0.0682 68  TYR   B CZ  
5065 O  OH  . TYR   B 68  ? 0.1796 0.2460 0.2854 0.0053  -0.0289 -0.0477 68  TYR   B OH  
5075 N  N   . ILE   B 69  ? 0.1581 0.1572 0.1775 0.0016  -0.0312 -0.0366 69  ILE   B N   
5076 C  CA  . ILE   B 69  ? 0.1670 0.1615 0.1881 -0.0008 -0.0195 -0.0344 69  ILE   B CA  
5077 C  C   . ILE   B 69  ? 0.1678 0.1586 0.1771 0.0051  -0.0297 -0.0308 69  ILE   B C   
5078 O  O   . ILE   B 69  ? 0.1713 0.1667 0.1773 0.0052  -0.0187 -0.0309 69  ILE   B O   
5079 C  CB  . ILE   B 69  ? 0.1733 0.1664 0.2058 -0.0045 0.0085  -0.0356 69  ILE   B CB  
5080 C  CG1 . ILE   B 69  ? 0.1768 0.1686 0.2168 -0.0033 0.0137  -0.0355 69  ILE   B CG1 
5081 C  CG2 . ILE   B 69  ? 0.1837 0.1754 0.2204 -0.0066 0.0025  -0.0282 69  ILE   B CG2 
5082 C  CD1 . ILE   B 69  ? 0.1741 0.1722 0.2265 -0.0153 0.0117  -0.0299 69  ILE   B CD1 
5094 N  N   . ALA   B 70  ? 0.1679 0.1558 0.1815 0.0045  -0.0380 -0.0254 70  ALA   B N   
5095 C  CA  . ALA   B 70  ? 0.1716 0.1592 0.1690 -0.0018 -0.0420 -0.0203 70  ALA   B CA  
5096 C  C   . ALA   B 70  ? 0.1781 0.1580 0.1746 -0.0035 -0.0407 -0.0282 70  ALA   B C   
5097 O  O   . ALA   B 70  ? 0.1837 0.1574 0.1834 0.0023  -0.0405 -0.0317 70  ALA   B O   
5098 C  CB  . ALA   B 70  ? 0.1737 0.1758 0.1758 -0.0048 -0.0424 -0.0231 70  ALA   B CB  
5104 N  N   . THR   B 71  ? 0.1833 0.1556 0.1798 0.0028  -0.0480 -0.0321 71  THR   B N   
5105 C  CA  . THR   B 71  ? 0.1966 0.1606 0.1980 0.0087  -0.0601 -0.0316 71  THR   B CA  
5106 C  C   . THR   B 71  ? 0.1922 0.1711 0.2179 0.0258  -0.0593 -0.0469 71  THR   B C   
5107 O  O   . THR   B 71  ? 0.2050 0.1800 0.2556 0.0291  -0.0510 -0.0565 71  THR   B O   
5108 C  CB  . THR   B 71  ? 0.2222 0.1831 0.2196 0.0019  -0.0733 -0.0102 71  THR   B CB  
5109 O  OG1 . THR   B 71  ? 0.2389 0.2100 0.2529 -0.0146 -0.0692 0.0095  71  THR   B OG1 
5110 C  CG2 . THR   B 71  ? 0.2416 0.1778 0.2354 0.0073  -0.0625 -0.0018 71  THR   B CG2 
5118 N  N   . ASN   B 72  ? 0.1752 0.1799 0.2126 0.0170  -0.0609 -0.0650 72  ASN   B N   
5119 C  CA  . ASN   B 72  ? 0.1751 0.1891 0.2217 0.0180  -0.0463 -0.0715 72  ASN   B CA  
5120 C  C   . ASN   B 72  ? 0.1782 0.1993 0.2297 0.0042  -0.0291 -0.0686 72  ASN   B C   
5121 O  O   . ASN   B 72  ? 0.1792 0.2144 0.2568 0.0121  -0.0144 -0.0663 72  ASN   B O   
5122 C  CB  . ASN   B 72  ? 0.1846 0.1997 0.2299 0.0152  -0.0547 -0.0583 72  ASN   B CB  
5123 C  CG  . ASN   B 72  ? 0.2018 0.2150 0.2365 0.0312  -0.0524 -0.0345 72  ASN   B CG  
5124 O  OD1 . ASN   B 72  ? 0.2205 0.2291 0.2463 0.0220  -0.0418 -0.0387 72  ASN   B OD1 
5125 N  ND2 . ASN   B 72  ? 0.2130 0.2232 0.2685 0.0421  -0.0420 -0.0057 72  ASN   B ND2 
5132 N  N   . GLY   B 73  ? 0.1807 0.1987 0.2059 -0.0033 -0.0282 -0.0632 73  GLY   B N   
5133 C  CA  . GLY   B 73  ? 0.1774 0.2070 0.1838 -0.0057 -0.0168 -0.0471 73  GLY   B CA  
5134 C  C   . GLY   B 73  ? 0.1719 0.2039 0.1467 0.0027  -0.0165 -0.0377 73  GLY   B C   
5135 O  O   . GLY   B 73  ? 0.1668 0.1824 0.1663 0.0047  -0.0153 -0.0248 73  GLY   B O   
5139 N  N   . PRO   B 74  ? 0.1713 0.2122 0.1437 0.0046  -0.0251 -0.0331 74  PRO   B N   
5140 C  CA  . PRO   B 74  ? 0.1629 0.2130 0.1349 0.0069  -0.0129 -0.0230 74  PRO   B CA  
5141 C  C   . PRO   B 74  ? 0.1527 0.1963 0.1437 0.0032  -0.0118 -0.0142 74  PRO   B C   
5142 O  O   . PRO   B 74  ? 0.1563 0.1940 0.1897 0.0068  -0.0079 -0.0306 74  PRO   B O   
5143 C  CB  . PRO   B 74  ? 0.1822 0.2335 0.1440 0.0018  -0.0111 -0.0166 74  PRO   B CB  
5144 C  CG  . PRO   B 74  ? 0.2011 0.2400 0.1724 0.0037  -0.0102 -0.0120 74  PRO   B CG  
5145 C  CD  . PRO   B 74  ? 0.1971 0.2280 0.1682 0.0055  -0.0123 -0.0231 74  PRO   B CD  
5153 N  N   . LEU   B 75  ? 0.1512 0.1831 0.1330 0.0033  -0.0165 -0.0122 75  LEU   B N   
5154 C  CA  . LEU   B 75  ? 0.1552 0.1825 0.1380 -0.0000 -0.0155 -0.0039 75  LEU   B CA  
5155 C  C   . LEU   B 75  ? 0.1587 0.1923 0.1416 0.0055  -0.0048 -0.0027 75  LEU   B C   
5156 O  O   . LEU   B 75  ? 0.1723 0.2028 0.1540 -0.0021 -0.0050 0.0011  75  LEU   B O   
5157 C  CB  . LEU   B 75  ? 0.1661 0.1868 0.1268 -0.0140 -0.0184 0.0111  75  LEU   B CB  
5158 C  CG  . LEU   B 75  ? 0.1985 0.2021 0.1465 -0.0333 -0.0090 0.0026  75  LEU   B CG  
5159 C  CD1 . LEU   B 75  ? 0.2317 0.2175 0.1487 -0.0364 0.0127  0.0003  75  LEU   B CD1 
5160 C  CD2 . LEU   B 75  ? 0.2337 0.2195 0.2117 -0.0248 0.0013  0.0095  75  LEU   B CD2 
5172 N  N   . LYS   B 76  ? 0.1598 0.2126 0.1733 0.0023  -0.0009 0.0014  76  LYS   B N   
5173 C  CA  . LYS   B 76  ? 0.1717 0.2204 0.2017 -0.0053 0.0174  0.0025  76  LYS   B CA  
5174 C  C   . LYS   B 76  ? 0.1642 0.2054 0.1665 0.0007  0.0081  0.0244  76  LYS   B C   
5175 O  O   . LYS   B 76  ? 0.1646 0.1873 0.1733 -0.0005 0.0044  0.0215  76  LYS   B O   
5176 C  CB  . LYS   B 76  ? 0.1899 0.2267 0.2576 -0.0113 0.0307  -0.0258 76  LYS   B CB  
5177 C  CG  . LYS   B 76  ? 0.1996 0.2495 0.2985 -0.0010 0.0213  -0.0357 76  LYS   B CG  
5178 C  CD  . LYS   B 76  ? 0.1986 0.2613 0.3324 0.0068  0.0106  -0.0534 76  LYS   B CD  
5179 C  CE  . LYS   B 76  ? 0.2016 0.2779 0.3798 0.0075  -0.0040 -0.0629 76  LYS   B CE  
5180 N  NZ  . LYS   B 76  ? 0.2000 0.2841 0.3940 0.0032  -0.0230 -0.0819 76  LYS   B NZ  
5194 N  N   . VAL   B 77  ? 0.1725 0.2162 0.1684 0.0078  0.0188  0.0264  77  VAL   B N   
5195 C  CA  . VAL   B 77  ? 0.1769 0.2038 0.1794 0.0136  0.0229  0.0541  77  VAL   B CA  
5196 C  C   . VAL   B 77  ? 0.1625 0.1810 0.1739 0.0139  0.0276  0.0375  77  VAL   B C   
5197 O  O   . VAL   B 77  ? 0.1668 0.1808 0.1805 0.0256  0.0310  0.0297  77  VAL   B O   
5198 C  CB  . VAL   B 77  ? 0.1913 0.2153 0.2227 0.0159  0.0308  0.0702  77  VAL   B CB  
5199 C  CG1 . VAL   B 77  ? 0.1935 0.2056 0.2538 0.0115  0.0344  0.0857  77  VAL   B CG1 
5200 C  CG2 . VAL   B 77  ? 0.2040 0.2355 0.2454 0.0137  0.0134  0.0720  77  VAL   B CG2 
5210 N  N   . GLY   B 78  ? 0.1559 0.1646 0.1701 0.0064  0.0202  0.0319  78  GLY   B N   
5211 C  CA  . GLY   B 78  ? 0.1529 0.1603 0.1679 0.0067  0.0257  0.0212  78  GLY   B CA  
5212 C  C   . GLY   B 78  ? 0.1470 0.1543 0.1686 0.0099  0.0224  0.0206  78  GLY   B C   
5213 O  O   . GLY   B 78  ? 0.1466 0.1539 0.1850 0.0154  0.0235  0.0225  78  GLY   B O   
5217 N  N   . GLY   B 79  ? 0.1454 0.1588 0.1657 0.0060  0.0140  0.0148  79  GLY   B N   
5218 C  CA  . GLY   B 79  ? 0.1441 0.1493 0.1601 0.0068  0.0085  0.0109  79  GLY   B CA  
5219 C  C   . GLY   B 79  ? 0.1326 0.1428 0.1624 0.0107  0.0111  0.0062  79  GLY   B C   
5220 O  O   . GLY   B 79  ? 0.1438 0.1384 0.1694 0.0093  0.0187  0.0167  79  GLY   B O   
5224 N  N   . SER   B 80  ? 0.1316 0.1363 0.1691 0.0033  0.0171  0.0041  80  SER   B N   
5225 C  CA  . SER   B 80  ? 0.1272 0.1349 0.1644 0.0011  0.0049  0.0059  80  SER   B CA  
5226 C  C   . SER   B 80  ? 0.1362 0.1313 0.1551 0.0093  -0.0016 -0.0005 80  SER   B C   
5227 O  O   . SER   B 80  ? 0.1459 0.1340 0.1821 0.0075  0.0040  -0.0032 80  SER   B O   
5228 C  CB  . SER   B 80  ? 0.1359 0.1407 0.1701 -0.0034 0.0039  0.0099  80  SER   B CB  
5229 O  OG  . SER   B 80  ? 0.1402 0.1508 0.1973 -0.0012 -0.0083 0.0133  80  SER   B OG  
5235 N  N   . CYS   B 81  ? 0.1360 0.1165 0.1648 0.0004  -0.0075 0.0004  81  CYS   B N   
5236 C  CA  . CYS   B 81  ? 0.1372 0.1200 0.1617 0.0063  -0.0104 -0.0025 81  CYS   B CA  
5237 C  C   . CYS   B 81  ? 0.1317 0.1183 0.1385 -0.0029 -0.0131 0.0010  81  CYS   B C   
5238 O  O   . CYS   B 81  ? 0.1566 0.1190 0.1597 0.0031  -0.0003 -0.0023 81  CYS   B O   
5239 C  CB  . CYS   B 81  ? 0.1543 0.1319 0.1690 -0.0061 -0.0120 -0.0037 81  CYS   B CB  
5240 S  SG  . CYS   B 81  ? 0.1532 0.1513 0.1584 -0.0046 -0.0226 -0.0092 81  CYS   B SG  
5246 N  N   . VAL   B 82  ? 0.1378 0.1184 0.1558 -0.0035 -0.0113 0.0002  82  VAL   B N   
5247 C  CA  . VAL   B 82  ? 0.1428 0.1215 0.1565 -0.0064 -0.0095 0.0041  82  VAL   B CA  
5248 C  C   . VAL   B 82  ? 0.1549 0.1145 0.1677 -0.0050 -0.0044 0.0011  82  VAL   B C   
5249 O  O   . VAL   B 82  ? 0.1612 0.1161 0.1916 -0.0063 -0.0044 -0.0110 82  VAL   B O   
5250 C  CB  . VAL   B 82  ? 0.1519 0.1396 0.1685 -0.0039 -0.0111 0.0103  82  VAL   B CB  
5251 C  CG1 . VAL   B 82  ? 0.1716 0.1621 0.1753 -0.0004 -0.0107 0.0165  82  VAL   B CG1 
5252 C  CG2 . VAL   B 82  ? 0.1581 0.1534 0.1887 -0.0063 -0.0289 0.0137  82  VAL   B CG2 
5262 N  N   . LEU   B 83  ? 0.1398 0.1154 0.1644 -0.0150 -0.0208 -0.0098 83  LEU   B N   
5263 C  CA  . LEU   B 83  ? 0.1428 0.1187 0.1520 -0.0137 -0.0214 -0.0015 83  LEU   B CA  
5264 C  C   . LEU   B 83  ? 0.1424 0.1159 0.1511 -0.0190 -0.0196 -0.0021 83  LEU   B C   
5265 O  O   . LEU   B 83  ? 0.1459 0.1263 0.1407 -0.0226 -0.0144 0.0064  83  LEU   B O   
5266 C  CB  . LEU   B 83  ? 0.1504 0.1302 0.1569 -0.0136 -0.0217 -0.0110 83  LEU   B CB  
5267 C  CG  . LEU   B 83  ? 0.1649 0.1531 0.1672 -0.0176 -0.0135 -0.0096 83  LEU   B CG  
5268 C  CD1 . LEU   B 83  ? 0.1749 0.1593 0.1738 -0.0161 -0.0233 -0.0033 83  LEU   B CD1 
5269 C  CD2 . LEU   B 83  ? 0.1869 0.1601 0.1724 -0.0109 -0.0110 -0.0213 83  LEU   B CD2 
5281 N  N   . SER   B 84  ? 0.1473 0.1280 0.1763 -0.0231 -0.0170 -0.0007 84  SER   B N   
5282 C  CA  . SER   B 84  ? 0.1464 0.1513 0.1642 -0.0265 -0.0145 0.0134  84  SER   B CA  
5283 C  C   . SER   B 84  ? 0.1411 0.1635 0.1262 -0.0234 -0.0121 0.0230  84  SER   B C   
5284 O  O   . SER   B 84  ? 0.1465 0.1522 0.1280 -0.0186 -0.0107 0.0028  84  SER   B O   
5285 C  CB  . SER   B 84  ? 0.1650 0.1582 0.2069 -0.0284 0.0053  0.0136  84  SER   B CB  
5286 O  OG  . SER   B 84  ? 0.1660 0.1746 0.2428 -0.0393 0.0104  0.0207  84  SER   B OG  
5292 N  N   . GLY   B 85  ? 0.1452 0.1838 0.1404 -0.0263 -0.0161 0.0236  85  GLY   B N   
5293 C  CA  . GLY   B 85  ? 0.1462 0.1915 0.1581 -0.0355 -0.0016 0.0021  85  GLY   B CA  
5294 C  C   . GLY   B 85  ? 0.1442 0.1761 0.1544 -0.0452 -0.0009 0.0080  85  GLY   B C   
5295 O  O   . GLY   B 85  ? 0.1513 0.1746 0.1558 -0.0511 0.0118  -0.0074 85  GLY   B O   
5299 N  N   . HIS   B 86  ? 0.1410 0.1609 0.1706 -0.0326 -0.0183 0.0136  86  HIS   B N   
5300 C  CA  . HIS   B 86  ? 0.1436 0.1601 0.1590 -0.0333 -0.0176 0.0188  86  HIS   B CA  
5301 C  C   . HIS   B 86  ? 0.1420 0.1770 0.1513 -0.0440 -0.0078 0.0266  86  HIS   B C   
5302 O  O   . HIS   B 86  ? 0.1589 0.1881 0.1515 -0.0328 0.0061  0.0243  86  HIS   B O   
5303 C  CB  . HIS   B 86  ? 0.1553 0.1621 0.1610 -0.0250 -0.0230 0.0067  86  HIS   B CB  
5304 C  CG  . HIS   B 86  ? 0.1541 0.1681 0.1544 -0.0164 -0.0230 0.0161  86  HIS   B CG  
5305 N  ND1 . HIS   B 86  ? 0.1650 0.1916 0.1740 -0.0248 -0.0286 -0.0043 86  HIS   B ND1 
5306 C  CD2 . HIS   B 86  ? 0.1526 0.1671 0.1682 -0.0149 -0.0182 0.0118  86  HIS   B CD2 
5307 C  CE1 . HIS   B 86  ? 0.1698 0.1869 0.1653 -0.0156 -0.0125 -0.0111 86  HIS   B CE1 
5308 N  NE2 . HIS   B 86  ? 0.1648 0.1750 0.1568 -0.0031 -0.0098 0.0064  86  HIS   B NE2 
5316 N  N   . ASN   B 87  ? 0.1448 0.1779 0.1619 -0.0346 -0.0033 0.0234  87  ASN   B N   
5317 C  CA  . ASN   B 87  ? 0.1534 0.1953 0.1690 -0.0356 0.0180  0.0204  87  ASN   B CA  
5318 C  C   . ASN   B 87  ? 0.1678 0.1775 0.1624 -0.0313 0.0277  0.0137  87  ASN   B C   
5319 O  O   . ASN   B 87  ? 0.1927 0.1900 0.1954 -0.0258 0.0474  0.0122  87  ASN   B O   
5320 C  CB  . ASN   B 87  ? 0.1535 0.2308 0.2065 -0.0276 0.0207  0.0178  87  ASN   B CB  
5321 C  CG  . ASN   B 87  ? 0.1569 0.2489 0.2117 0.0050  0.0314  0.0322  87  ASN   B CG  
5322 O  OD1 . ASN   B 87  ? 0.1527 0.2361 0.1997 0.0084  0.0498  0.0450  87  ASN   B OD1 
5323 N  ND2 . ASN   B 87  ? 0.1954 0.2620 0.2465 0.0088  0.0350  0.0328  87  ASN   B ND2 
5330 N  N   . LEU   B 88  ? 0.1584 0.1635 0.1505 -0.0370 0.0116  0.0130  88  LEU   B N   
5331 C  CA  . LEU   B 88  ? 0.1665 0.1614 0.1522 -0.0361 0.0050  0.0030  88  LEU   B CA  
5332 C  C   . LEU   B 88  ? 0.1687 0.1488 0.1535 -0.0367 0.0022  0.0008  88  LEU   B C   
5333 O  O   . LEU   B 88  ? 0.1939 0.1613 0.1796 -0.0240 -0.0246 -0.0098 88  LEU   B O   
5334 C  CB  . LEU   B 88  ? 0.1756 0.1645 0.1713 -0.0426 -0.0088 0.0119  88  LEU   B CB  
5335 C  CG  . LEU   B 88  ? 0.2140 0.1940 0.1862 -0.0364 -0.0209 0.0301  88  LEU   B CG  
5336 C  CD1 . LEU   B 88  ? 0.2276 0.2210 0.1954 -0.0455 -0.0139 0.0430  88  LEU   B CD1 
5337 C  CD2 . LEU   B 88  ? 0.2510 0.2215 0.2418 -0.0008 -0.0417 0.0087  88  LEU   B CD2 
5349 N  N   . ALA   B 89  ? 0.1565 0.1459 0.1457 -0.0376 0.0191  0.0019  89  ALA   B N   
5350 C  CA  . ALA   B 89  ? 0.1526 0.1425 0.1271 -0.0382 0.0031  0.0096  89  ALA   B CA  
5351 C  C   . ALA   B 89  ? 0.1654 0.1505 0.1320 -0.0408 0.0105  0.0029  89  ALA   B C   
5352 O  O   . ALA   B 89  ? 0.1467 0.1595 0.1666 -0.0408 0.0123  -0.0241 89  ALA   B O   
5353 C  CB  . ALA   B 89  ? 0.1457 0.1435 0.1426 -0.0401 0.0065  0.0131  89  ALA   B CB  
5359 N  N   . LYS   B 90  ? 0.1993 0.1379 0.1454 -0.0489 -0.0067 0.0094  90  LYS   B N   
5360 C  CA  . LYS   B 90  ? 0.2108 0.1332 0.1377 -0.0459 -0.0130 0.0079  90  LYS   B CA  
5361 C  C   . LYS   B 90  ? 0.1928 0.1255 0.1521 -0.0432 -0.0131 -0.0019 90  LYS   B C   
5362 O  O   . LYS   B 90  ? 0.2008 0.1425 0.1674 -0.0584 -0.0011 -0.0019 90  LYS   B O   
5363 C  CB  . LYS   B 90  ? 0.2313 0.1438 0.1591 -0.0379 0.0020  0.0177  90  LYS   B CB  
5364 C  CG  . LYS   B 90  ? 0.2337 0.1578 0.1690 -0.0251 0.0309  0.0147  90  LYS   B CG  
5365 C  CD  . LYS   B 90  ? 0.2639 0.1796 0.2160 -0.0174 0.0532  -0.0073 90  LYS   B CD  
5366 C  CE  . LYS   B 90  ? 0.2747 0.1963 0.2630 -0.0252 0.0714  -0.0173 90  LYS   B CE  
5367 N  NZ  . LYS   B 90  ? 0.2830 0.1869 0.2631 -0.0367 0.0878  -0.0177 90  LYS   B NZ  
5381 N  N   . HIS   B 91  ? 0.1677 0.1178 0.1342 -0.0320 -0.0177 0.0079  91  HIS   B N   
5382 C  CA  . HIS   B 91  ? 0.1516 0.1221 0.1416 -0.0291 -0.0199 -0.0004 91  HIS   B CA  
5383 C  C   . HIS   B 91  ? 0.1416 0.1257 0.1309 -0.0270 -0.0002 0.0052  91  HIS   B C   
5384 O  O   . HIS   B 91  ? 0.1566 0.1288 0.1351 -0.0265 -0.0206 0.0047  91  HIS   B O   
5385 C  CB  . HIS   B 91  ? 0.1726 0.1236 0.1851 -0.0104 -0.0115 0.0172  91  HIS   B CB  
5386 C  CG  . HIS   B 91  ? 0.2113 0.1398 0.2438 0.0008  0.0231  0.0264  91  HIS   B CG  
5387 N  ND1 . HIS   B 91  ? 0.2400 0.1496 0.3013 -0.0021 0.0325  0.0116  91  HIS   B ND1 
5388 C  CD2 . HIS   B 91  ? 0.2249 0.1748 0.2879 0.0170  0.0111  0.0559  91  HIS   B CD2 
5389 C  CE1 . HIS   B 91  ? 0.2442 0.1656 0.3219 0.0148  0.0315  0.0184  91  HIS   B CE1 
5390 N  NE2 . HIS   B 91  ? 0.2370 0.1825 0.3211 0.0279  0.0274  0.0580  91  HIS   B NE2 
5398 N  N   . CYS   B 92  ? 0.1344 0.1232 0.1320 -0.0268 -0.0109 0.0016  92  CYS   B N   
5399 C  CA  . CYS   B 92  ? 0.1332 0.1195 0.1330 -0.0214 -0.0080 0.0056  92  CYS   B CA  
5400 C  C   . CYS   B 92  ? 0.1303 0.1129 0.1243 -0.0135 -0.0043 0.0037  92  CYS   B C   
5401 O  O   . CYS   B 92  ? 0.1396 0.1237 0.1523 -0.0190 -0.0046 0.0003  92  CYS   B O   
5402 C  CB  . CYS   B 92  ? 0.1349 0.1281 0.1414 -0.0138 -0.0077 0.0043  92  CYS   B CB  
5403 S  SG  . CYS   B 92  ? 0.1354 0.1291 0.1391 -0.0111 -0.0103 0.0056  92  CYS   B SG  
5409 N  N   . LEU   B 93  ? 0.1204 0.1162 0.1350 -0.0133 -0.0095 -0.0068 93  LEU   B N   
5410 C  CA  . LEU   B 93  ? 0.1228 0.1208 0.1358 -0.0056 -0.0113 0.0065  93  LEU   B CA  
5411 C  C   . LEU   B 93  ? 0.1193 0.1139 0.1280 -0.0054 -0.0134 0.0041  93  LEU   B C   
5412 O  O   . LEU   B 93  ? 0.1292 0.1158 0.1489 -0.0080 -0.0057 0.0044  93  LEU   B O   
5413 C  CB  . LEU   B 93  ? 0.1265 0.1182 0.1458 -0.0021 -0.0051 0.0031  93  LEU   B CB  
5414 C  CG  . LEU   B 93  ? 0.1263 0.1290 0.1719 -0.0042 -0.0051 0.0104  93  LEU   B CG  
5415 C  CD1 . LEU   B 93  ? 0.1347 0.1398 0.1654 0.0015  0.0023  -0.0017 93  LEU   B CD1 
5416 C  CD2 . LEU   B 93  ? 0.1258 0.1281 0.1829 -0.0064 -0.0083 0.0024  93  LEU   B CD2 
5428 N  N   . HIS   B 94  ? 0.1249 0.1130 0.1317 -0.0077 -0.0149 0.0101  94  HIS   B N   
5429 C  CA  . HIS   B 94  ? 0.1242 0.1119 0.1301 -0.0013 -0.0034 0.0055  94  HIS   B CA  
5430 C  C   . HIS   B 94  ? 0.1228 0.1177 0.1455 -0.0044 -0.0074 0.0079  94  HIS   B C   
5431 O  O   . HIS   B 94  ? 0.1259 0.1247 0.1814 -0.0060 0.0182  -0.0043 94  HIS   B O   
5432 C  CB  . HIS   B 94  ? 0.1221 0.1194 0.1361 -0.0027 -0.0043 0.0023  94  HIS   B CB  
5433 C  CG  . HIS   B 94  ? 0.1302 0.1206 0.1425 -0.0038 -0.0203 0.0043  94  HIS   B CG  
5434 N  ND1 . HIS   B 94  ? 0.1333 0.1236 0.1429 -0.0079 -0.0209 0.0009  94  HIS   B ND1 
5435 C  CD2 . HIS   B 94  ? 0.1317 0.1216 0.1419 -0.0013 -0.0188 0.0045  94  HIS   B CD2 
5436 C  CE1 . HIS   B 94  ? 0.1380 0.1220 0.1320 -0.0107 -0.0192 0.0026  94  HIS   B CE1 
5437 N  NE2 . HIS   B 94  ? 0.1339 0.1251 0.1453 -0.0160 -0.0139 0.0039  94  HIS   B NE2 
5445 N  N   . VAL   B 95  ? 0.1173 0.1129 0.1485 -0.0014 -0.0018 0.0062  95  VAL   B N   
5446 C  CA  . VAL   B 95  ? 0.1189 0.1238 0.1454 0.0000  0.0022  0.0143  95  VAL   B CA  
5447 C  C   . VAL   B 95  ? 0.1269 0.1229 0.1527 -0.0024 0.0083  0.0062  95  VAL   B C   
5448 O  O   . VAL   B 95  ? 0.1330 0.1210 0.1694 0.0060  0.0089  0.0189  95  VAL   B O   
5449 C  CB  . VAL   B 95  ? 0.1266 0.1210 0.1512 -0.0022 -0.0075 0.0068  95  VAL   B CB  
5450 C  CG1 . VAL   B 95  ? 0.1327 0.1410 0.1664 -0.0095 0.0015  0.0177  95  VAL   B CG1 
5451 C  CG2 . VAL   B 95  ? 0.1358 0.1178 0.1478 -0.0017 -0.0070 0.0085  95  VAL   B CG2 
5461 N  N   . VAL   B 96  ? 0.1412 0.1296 0.1469 0.0093  0.0048  0.0161  96  VAL   B N   
5462 C  CA  . VAL   B 96  ? 0.1476 0.1359 0.1466 0.0040  0.0039  0.0196  96  VAL   B CA  
5463 C  C   . VAL   B 96  ? 0.1499 0.1401 0.1613 0.0024  0.0097  0.0196  96  VAL   B C   
5464 O  O   . VAL   B 96  ? 0.1510 0.1492 0.1728 -0.0013 0.0170  0.0082  96  VAL   B O   
5465 C  CB  . VAL   B 96  ? 0.1526 0.1595 0.1452 0.0068  0.0046  0.0107  96  VAL   B CB  
5466 C  CG1 . VAL   B 96  ? 0.1484 0.1778 0.1608 0.0182  0.0069  0.0091  96  VAL   B CG1 
5467 C  CG2 . VAL   B 96  ? 0.1590 0.1617 0.1589 0.0048  0.0120  0.0059  96  VAL   B CG2 
5477 N  N   . GLY   B 97  ? 0.1574 0.1353 0.1531 0.0045  0.0109  0.0272  97  GLY   B N   
5478 C  CA  . GLY   B 97  ? 0.1726 0.1427 0.1658 0.0091  0.0154  0.0193  97  GLY   B CA  
5479 C  C   . GLY   B 97  ? 0.1898 0.1561 0.1704 0.0134  0.0122  0.0208  97  GLY   B C   
5480 O  O   . GLY   B 97  ? 0.2023 0.1610 0.1680 0.0068  0.0088  0.0124  97  GLY   B O   
5484 N  N   . PRO   B 98  ? 0.2039 0.1594 0.1867 0.0155  0.0360  0.0389  98  PRO   B N   
5485 C  CA  . PRO   B 98  ? 0.2153 0.1774 0.1918 0.0200  0.0470  0.0354  98  PRO   B CA  
5486 C  C   . PRO   B 98  ? 0.2279 0.1777 0.1638 0.0356  0.0456  0.0518  98  PRO   B C   
5487 O  O   . PRO   B 98  ? 0.2180 0.1737 0.1857 0.0298  0.0526  0.0441  98  PRO   B O   
5488 C  CB  . PRO   B 98  ? 0.2047 0.1833 0.1999 0.0133  0.0576  0.0362  98  PRO   B CB  
5489 C  CG  . PRO   B 98  ? 0.2035 0.1755 0.2036 0.0114  0.0458  0.0465  98  PRO   B CG  
5490 C  CD  . PRO   B 98  ? 0.1916 0.1650 0.1969 0.0159  0.0372  0.0472  98  PRO   B CD  
5498 N  N   . ASN   B 99  ? 0.2405 0.1923 0.1721 0.0519  0.0465  0.0325  99  ASN   B N   
5499 C  CA  . ASN   B 99  ? 0.2603 0.2043 0.1833 0.0576  0.0377  0.0540  99  ASN   B CA  
5500 C  C   . ASN   B 99  ? 0.2910 0.2443 0.2217 0.0533  0.0509  0.0840  99  ASN   B C   
5501 O  O   . ASN   B 99  ? 0.3005 0.2521 0.2258 0.0540  0.0440  0.0870  99  ASN   B O   
5502 C  CB  . ASN   B 99  ? 0.2691 0.2020 0.1818 0.0551  0.0285  0.0438  99  ASN   B CB  
5503 C  CG  . ASN   B 99  ? 0.2725 0.2091 0.2001 0.0506  0.0190  0.0397  99  ASN   B CG  
5504 O  OD1 . ASN   B 99  ? 0.2749 0.2100 0.2272 0.0549  0.0273  0.0437  99  ASN   B OD1 
5505 N  ND2 . ASN   B 99  ? 0.2689 0.2068 0.2046 0.0568  -0.0128 0.0303  99  ASN   B ND2 
5512 N  N   A VAL   B 100 ? 0.3089 0.2588 0.2614 0.0402  0.0592  0.1091  100 VAL   B N   
5513 N  N   B VAL   B 100 ? 0.3139 0.2616 0.2569 0.0447  0.0441  0.0957  100 VAL   B N   
5514 C  CA  A VAL   B 100 ? 0.3372 0.2805 0.3133 0.0266  0.0617  0.1254  100 VAL   B CA  
5515 C  CA  B VAL   B 100 ? 0.3399 0.2803 0.2947 0.0360  0.0368  0.1042  100 VAL   B CA  
5516 C  C   A VAL   B 100 ? 0.3598 0.2882 0.2958 0.0346  0.0599  0.1424  100 VAL   B C   
5517 C  C   B VAL   B 100 ? 0.3598 0.2882 0.2934 0.0394  0.0368  0.1264  100 VAL   B C   
5518 O  O   A VAL   B 100 ? 0.3675 0.3012 0.2972 0.0309  0.0741  0.1365  100 VAL   B O   
5519 O  O   B VAL   B 100 ? 0.3634 0.2937 0.2927 0.0364  0.0391  0.1223  100 VAL   B O   
5520 C  CB  A VAL   B 100 ? 0.3456 0.2956 0.3815 0.0044  0.0607  0.1322  100 VAL   B CB  
5521 C  CB  B VAL   B 100 ? 0.3462 0.2907 0.3327 0.0244  0.0300  0.0951  100 VAL   B CB  
5522 C  CG1 A VAL   B 100 ? 0.3505 0.3026 0.4100 0.0015  0.0599  0.1303  100 VAL   B CG1 
5523 C  CG1 B VAL   B 100 ? 0.3490 0.2946 0.3474 0.0218  0.0283  0.0916  100 VAL   B CG1 
5524 C  CG2 A VAL   B 100 ? 0.3463 0.3002 0.4003 -0.0048 0.0640  0.1402  100 VAL   B CG2 
5525 C  CG2 B VAL   B 100 ? 0.3478 0.2944 0.3459 0.0201  0.0282  0.0929  100 VAL   B CG2 
5544 N  N   . ASN   B 101 ? 0.3749 0.2915 0.2974 0.0465  0.0347  0.1462  101 ASN   B N   
5545 C  CA  . ASN   B 101 ? 0.4124 0.3099 0.3142 0.0560  0.0112  0.1521  101 ASN   B CA  
5546 C  C   . ASN   B 101 ? 0.4561 0.3523 0.3165 0.0572  0.0002  0.1669  101 ASN   B C   
5547 O  O   . ASN   B 101 ? 0.4603 0.3648 0.3415 0.0621  0.0029  0.1415  101 ASN   B O   
5548 C  CB  . ASN   B 101 ? 0.4091 0.2913 0.3323 0.0542  0.0108  0.1308  101 ASN   B CB  
5549 C  CG  . ASN   B 101 ? 0.4044 0.2741 0.3460 0.0565  0.0119  0.1202  101 ASN   B CG  
5550 O  OD1 . ASN   B 101 ? 0.4060 0.2745 0.3689 0.0489  0.0254  0.1103  101 ASN   B OD1 
5551 N  ND2 . ASN   B 101 ? 0.3998 0.2645 0.3431 0.0609  0.0092  0.1103  101 ASN   B ND2 
5559 N  N   . LYS   B 102 ? 0.4939 0.3921 0.3411 0.0462  0.0029  0.1653  102 LYS   B N   
5560 C  CA  . LYS   B 102 ? 0.5295 0.4396 0.3784 0.0309  0.0122  0.1348  102 LYS   B CA  
5561 C  C   . LYS   B 102 ? 0.5222 0.4392 0.3552 0.0294  0.0168  0.1402  102 LYS   B C   
5562 O  O   . LYS   B 102 ? 0.5309 0.4449 0.3597 0.0301  0.0005  0.1408  102 LYS   B O   
5563 C  CB  . LYS   B 102 ? 0.5677 0.4837 0.4492 0.0187  0.0250  0.0871  102 LYS   B CB  
5564 C  CG  . LYS   B 102 ? 0.5985 0.5208 0.5207 0.0087  0.0386  0.0401  102 LYS   B CG  
5565 C  CD  . LYS   B 102 ? 0.6233 0.5509 0.5914 0.0015  0.0520  0.0021  102 LYS   B CD  
5566 C  CE  . LYS   B 102 ? 0.6419 0.5718 0.6463 -0.0041 0.0612  -0.0244 102 LYS   B CE  
5567 N  NZ  . LYS   B 102 ? 0.6510 0.5836 0.6774 -0.0066 0.0646  -0.0387 102 LYS   B NZ  
5581 N  N   . GLY   B 103 ? 0.5021 0.4294 0.3464 0.0258  0.0393  0.1344  103 GLY   B N   
5582 C  CA  . GLY   B 103 ? 0.4794 0.4176 0.3518 0.0246  0.0588  0.1116  103 GLY   B CA  
5583 C  C   . GLY   B 103 ? 0.4521 0.4009 0.3460 0.0223  0.0745  0.0855  103 GLY   B C   
5584 O  O   . GLY   B 103 ? 0.4575 0.4077 0.3487 0.0218  0.0788  0.0880  103 GLY   B O   
5588 N  N   A GLU   B 104 ? 0.4341 0.3855 0.3316 0.0250  0.0940  0.0699  104 GLU   B N   
5589 N  N   B GLU   B 104 ? 0.4350 0.3905 0.3456 0.0176  0.0638  0.0661  104 GLU   B N   
5590 C  CA  A GLU   B 104 ? 0.4144 0.3697 0.3140 0.0313  0.1064  0.0518  104 GLU   B CA  
5591 C  CA  B GLU   B 104 ? 0.4166 0.3789 0.3404 0.0138  0.0519  0.0438  104 GLU   B CA  
5592 C  C   A GLU   B 104 ? 0.4170 0.3717 0.3227 0.0125  0.1471  0.0583  104 GLU   B C   
5593 C  C   B GLU   B 104 ? 0.4105 0.3764 0.3506 0.0076  0.0592  0.0359  104 GLU   B C   
5594 O  O   A GLU   B 104 ? 0.4181 0.3760 0.3429 0.0078  0.1480  0.0557  104 GLU   B O   
5595 O  O   B GLU   B 104 ? 0.4105 0.3773 0.3567 0.0064  0.0597  0.0331  104 GLU   B O   
5596 C  CB  A GLU   B 104 ? 0.3964 0.3495 0.3040 0.0561  0.0670  0.0191  104 GLU   B CB  
5597 C  CB  B GLU   B 104 ? 0.4056 0.3684 0.3274 0.0156  0.0318  0.0264  104 GLU   B CB  
5598 C  CG  A GLU   B 104 ? 0.3797 0.3331 0.2874 0.0785  0.0238  -0.0144 104 GLU   B CG  
5599 C  CG  B GLU   B 104 ? 0.3962 0.3597 0.3145 0.0170  0.0115  0.0085  104 GLU   B CG  
5600 C  CD  A GLU   B 104 ? 0.3654 0.3169 0.2647 0.0970  -0.0132 -0.0332 104 GLU   B CD  
5601 C  CD  B GLU   B 104 ? 0.3891 0.3518 0.3021 0.0174  -0.0049 -0.0040 104 GLU   B CD  
5602 O  OE1 A GLU   B 104 ? 0.3496 0.3019 0.2305 0.1107  -0.0113 -0.0380 104 GLU   B OE1 
5603 O  OE1 B GLU   B 104 ? 0.3848 0.3471 0.2915 0.0166  -0.0066 -0.0065 104 GLU   B OE1 
5604 O  OE2 A GLU   B 104 ? 0.3672 0.3192 0.2617 0.0952  -0.0422 -0.0453 104 GLU   B OE2 
5605 O  OE2 B GLU   B 104 ? 0.3881 0.3505 0.2994 0.0179  -0.0157 -0.0108 104 GLU   B OE2 
5618 N  N   A ASP   B 105 ? 0.4137 0.3696 0.3140 0.0003  0.1805  0.0631  105 ASP   B N   
5619 N  N   B ASP   B 105 ? 0.4030 0.3728 0.3515 0.0028  0.0647  0.0302  105 ASP   B N   
5620 C  CA  A ASP   B 105 ? 0.4150 0.3696 0.3354 -0.0080 0.1988  0.0502  105 ASP   B CA  
5621 C  CA  B ASP   B 105 ? 0.3970 0.3694 0.3601 -0.0014 0.0675  0.0215  105 ASP   B CA  
5622 C  C   A ASP   B 105 ? 0.3995 0.3400 0.3084 -0.0193 0.1961  0.0509  105 ASP   B C   
5623 C  C   B ASP   B 105 ? 0.3884 0.3593 0.3419 -0.0051 0.0673  0.0165  105 ASP   B C   
5624 O  O   A ASP   B 105 ? 0.3828 0.3336 0.2907 -0.0191 0.1849  0.0523  105 ASP   B O   
5625 O  O   B ASP   B 105 ? 0.3877 0.3577 0.3325 -0.0052 0.0690  0.0170  105 ASP   B O   
5626 C  CB  A ASP   B 105 ? 0.4312 0.3949 0.4081 -0.0003 0.2030  0.0279  105 ASP   B CB  
5627 C  CB  B ASP   B 105 ? 0.3986 0.3746 0.3879 -0.0004 0.0693  0.0170  105 ASP   B CB  
5628 C  CG  A ASP   B 105 ? 0.4423 0.4144 0.4768 0.0037  0.2124  0.0135  105 ASP   B CG  
5629 C  CG  B ASP   B 105 ? 0.3997 0.3782 0.4161 -0.0007 0.0726  0.0150  105 ASP   B CG  
5630 O  OD1 A ASP   B 105 ? 0.4402 0.4189 0.4820 -0.0021 0.2310  0.0191  105 ASP   B OD1 
5631 O  OD1 B ASP   B 105 ? 0.3990 0.3795 0.4222 -0.0030 0.0750  0.0157  105 ASP   B OD1 
5632 O  OD2 A ASP   B 105 ? 0.4497 0.4244 0.5189 0.0107  0.2021  0.0004  105 ASP   B OD2 
5633 O  OD2 B ASP   B 105 ? 0.3995 0.3795 0.4266 -0.0005 0.0741  0.0145  105 ASP   B OD2 
5642 N  N   A ILE   B 106 ? 0.3933 0.3160 0.3237 -0.0270 0.1831  0.0494  106 ILE   B N   
5643 N  N   B ILE   B 106 ? 0.3793 0.3500 0.3342 -0.0068 0.0632  0.0129  106 ILE   B N   
5644 C  CA  A ILE   B 106 ? 0.3746 0.2873 0.3364 -0.0405 0.1846  0.0425  106 ILE   B CA  
5645 C  CA  B ILE   B 106 ? 0.3678 0.3405 0.3321 -0.0090 0.0620  0.0080  106 ILE   B CA  
5646 C  C   A ILE   B 106 ? 0.3413 0.2753 0.3269 -0.0339 0.1865  0.0288  106 ILE   B C   
5647 C  C   B ILE   B 106 ? 0.3519 0.3348 0.3273 -0.0057 0.0618  0.0027  106 ILE   B C   
5648 O  O   A ILE   B 106 ? 0.3313 0.2509 0.3299 -0.0344 0.1862  0.0232  106 ILE   B O   
5649 O  O   B ILE   B 106 ? 0.3499 0.3308 0.3239 -0.0067 0.0581  -0.0007 106 ILE   B O   
5650 C  CB  A ILE   B 106 ? 0.3935 0.2790 0.3605 -0.0540 0.1721  0.0481  106 ILE   B CB  
5651 C  CB  B ILE   B 106 ? 0.3724 0.3388 0.3368 -0.0137 0.0601  0.0089  106 ILE   B CB  
5652 C  CG1 A ILE   B 106 ? 0.4020 0.2793 0.3678 -0.0473 0.1607  0.0400  106 ILE   B CG1 
5653 C  CG1 B ILE   B 106 ? 0.3737 0.3372 0.3383 -0.0136 0.0574  0.0088  106 ILE   B CG1 
5654 C  CG2 A ILE   B 106 ? 0.3989 0.2777 0.3764 -0.0657 0.1737  0.0577  106 ILE   B CG2 
5655 C  CG2 B ILE   B 106 ? 0.3745 0.3400 0.3419 -0.0160 0.0610  0.0095  106 ILE   B CG2 
5656 C  CD1 A ILE   B 106 ? 0.4063 0.2801 0.3629 -0.0412 0.1563  0.0380  106 ILE   B CD1 
5657 C  CD1 B ILE   B 106 ? 0.3743 0.3362 0.3382 -0.0128 0.0560  0.0090  106 ILE   B CD1 
5680 N  N   A GLN   B 107 ? 0.3244 0.2929 0.3404 -0.0296 0.1740  0.0266  107 GLN   B N   
5681 N  N   B GLN   B 107 ? 0.3387 0.3338 0.3351 -0.0024 0.0637  0.0020  107 GLN   B N   
5682 C  CA  A GLN   B 107 ? 0.3051 0.3087 0.3540 -0.0276 0.1525  0.0268  107 GLN   B CA  
5683 C  CA  B GLN   B 107 ? 0.3246 0.3304 0.3442 0.0005  0.0651  0.0051  107 GLN   B CA  
5684 C  C   A GLN   B 107 ? 0.2739 0.2851 0.3162 -0.0168 0.1185  0.0130  107 GLN   B C   
5685 C  C   B GLN   B 107 ? 0.2901 0.3011 0.3078 0.0045  0.0766  0.0048  107 GLN   B C   
5686 O  O   A GLN   B 107 ? 0.2656 0.2837 0.3404 -0.0172 0.0927  -0.0079 107 GLN   B O   
5687 O  O   B GLN   B 107 ? 0.2898 0.3042 0.3119 0.0051  0.0675  -0.0025 107 GLN   B O   
5688 C  CB  A GLN   B 107 ? 0.3362 0.3510 0.4288 -0.0233 0.1309  0.0298  107 GLN   B CB  
5689 C  CB  B GLN   B 107 ? 0.3468 0.3552 0.3974 0.0014  0.0524  0.0067  107 GLN   B CB  
5690 C  CG  A GLN   B 107 ? 0.3692 0.3889 0.5066 -0.0145 0.0961  0.0283  107 GLN   B CG  
5691 C  CG  B GLN   B 107 ? 0.3663 0.3761 0.4492 0.0029  0.0385  0.0077  107 GLN   B CG  
5692 C  CD  A GLN   B 107 ? 0.3943 0.4179 0.5688 -0.0100 0.0701  0.0301  107 GLN   B CD  
5693 C  CD  B GLN   B 107 ? 0.3812 0.3920 0.4923 0.0032  0.0275  0.0091  107 GLN   B CD  
5694 O  OE1 A GLN   B 107 ? 0.4033 0.4289 0.5910 -0.0081 0.0652  0.0271  107 GLN   B OE1 
5695 O  OE1 B GLN   B 107 ? 0.3865 0.3979 0.5069 0.0030  0.0257  0.0085  107 GLN   B OE1 
5696 N  NE2 A GLN   B 107 ? 0.4039 0.4269 0.5885 -0.0062 0.0583  0.0348  107 GLN   B NE2 
5697 N  NE2 B GLN   B 107 ? 0.3868 0.3972 0.5068 0.0042  0.0227  0.0109  107 GLN   B NE2 
5714 N  N   . LEU   B 108 ? 0.2542 0.2676 0.2802 0.0113  0.0954  0.0107  108 LEU   B N   
5715 C  CA  . LEU   B 108 ? 0.2259 0.2343 0.2451 0.0291  0.0742  0.0267  108 LEU   B CA  
5716 C  C   . LEU   B 108 ? 0.1901 0.1890 0.2382 0.0267  0.0469  0.0352  108 LEU   B C   
5717 O  O   . LEU   B 108 ? 0.1864 0.1722 0.2368 0.0272  0.0415  0.0310  108 LEU   B O   
5718 C  CB  . LEU   B 108 ? 0.2431 0.2530 0.2320 0.0307  0.0717  0.0356  108 LEU   B CB  
5719 C  CG  . LEU   B 108 ? 0.2578 0.2823 0.2426 0.0346  0.0680  0.0120  108 LEU   B CG  
5720 C  CD1 . LEU   B 108 ? 0.2688 0.2964 0.2394 0.0265  0.0689  0.0165  108 LEU   B CD1 
5721 C  CD2 . LEU   B 108 ? 0.2695 0.2966 0.2530 0.0409  0.0594  -0.0045 108 LEU   B CD2 
5734 N  N   . LEU   B 109 ? 0.1703 0.1691 0.2419 0.0155  0.0445  0.0297  109 LEU   B N   
5735 C  CA  . LEU   B 109 ? 0.1509 0.1419 0.2519 0.0100  0.0435  0.0342  109 LEU   B CA  
5736 C  C   . LEU   B 109 ? 0.1430 0.1332 0.2471 0.0033  0.0358  0.0237  109 LEU   B C   
5737 O  O   . LEU   B 109 ? 0.1388 0.1299 0.2331 0.0041  0.0314  0.0338  109 LEU   B O   
5738 C  CB  . LEU   B 109 ? 0.1587 0.1331 0.2522 0.0083  0.0286  0.0434  109 LEU   B CB  
5739 C  CG  . LEU   B 109 ? 0.1562 0.1340 0.2493 0.0026  0.0236  0.0247  109 LEU   B CG  
5740 C  CD1 . LEU   B 109 ? 0.1539 0.1439 0.2261 0.0121  0.0285  0.0248  109 LEU   B CD1 
5741 C  CD2 . LEU   B 109 ? 0.1681 0.1400 0.2634 0.0030  0.0172  0.0250  109 LEU   B CD2 
5753 N  N   . LYS   B 110 ? 0.1341 0.1329 0.2419 -0.0034 0.0345  0.0223  110 LYS   B N   
5754 C  CA  . LYS   B 110 ? 0.1363 0.1301 0.2387 -0.0010 0.0260  0.0164  110 LYS   B CA  
5755 C  C   . LYS   B 110 ? 0.1349 0.1269 0.2245 -0.0008 0.0281  0.0175  110 LYS   B C   
5756 O  O   . LYS   B 110 ? 0.1297 0.1322 0.2188 -0.0069 0.0220  0.0100  110 LYS   B O   
5757 C  CB  . LYS   B 110 ? 0.1348 0.1290 0.2533 -0.0054 0.0271  0.0105  110 LYS   B CB  
5758 C  CG  . LYS   B 110 ? 0.1358 0.1316 0.2618 -0.0039 0.0184  0.0135  110 LYS   B CG  
5759 C  CD  . LYS   B 110 ? 0.1416 0.1322 0.2665 -0.0069 0.0188  0.0165  110 LYS   B CD  
5760 C  CE  . LYS   B 110 ? 0.1387 0.1431 0.2863 -0.0062 0.0223  0.0100  110 LYS   B CE  
5761 N  NZ  . LYS   B 110 ? 0.1447 0.1584 0.2801 0.0056  0.0102  0.0030  110 LYS   B NZ  
5775 N  N   . SER   B 111 ? 0.1411 0.1304 0.2335 -0.0034 0.0268  0.0132  111 SER   B N   
5776 C  CA  . SER   B 111 ? 0.1452 0.1322 0.2164 -0.0006 0.0217  0.0172  111 SER   B CA  
5777 C  C   . SER   B 111 ? 0.1370 0.1265 0.2096 0.0006  0.0154  0.0078  111 SER   B C   
5778 O  O   . SER   B 111 ? 0.1321 0.1303 0.2179 -0.0031 0.0118  0.0084  111 SER   B O   
5779 C  CB  . SER   B 111 ? 0.1573 0.1532 0.2230 0.0012  0.0390  0.0241  111 SER   B CB  
5780 O  OG  . SER   B 111 ? 0.1740 0.1880 0.2366 0.0071  0.0411  0.0293  111 SER   B OG  
5786 N  N   . ALA   B 112 ? 0.1270 0.1320 0.2173 0.0035  0.0244  0.0165  112 ALA   B N   
5787 C  CA  . ALA   B 112 ? 0.1312 0.1353 0.2070 -0.0025 0.0104  0.0085  112 ALA   B CA  
5788 C  C   . ALA   B 112 ? 0.1244 0.1257 0.1964 -0.0003 0.0097  0.0032  112 ALA   B C   
5789 O  O   . ALA   B 112 ? 0.1247 0.1291 0.1992 -0.0068 0.0138  0.0042  112 ALA   B O   
5790 C  CB  . ALA   B 112 ? 0.1312 0.1436 0.2185 0.0061  0.0109  0.0205  112 ALA   B CB  
5796 N  N   . TYR   B 113 ? 0.1184 0.1160 0.2079 -0.0033 0.0117  0.0119  113 TYR   B N   
5797 C  CA  . TYR   B 113 ? 0.1168 0.1150 0.2014 -0.0039 0.0132  0.0036  113 TYR   B CA  
5798 C  C   . TYR   B 113 ? 0.1152 0.1107 0.1910 -0.0087 0.0096  0.0007  113 TYR   B C   
5799 O  O   . TYR   B 113 ? 0.1244 0.1154 0.1932 -0.0081 0.0038  -0.0001 113 TYR   B O   
5800 C  CB  . TYR   B 113 ? 0.1233 0.1092 0.2107 -0.0045 0.0170  0.0095  113 TYR   B CB  
5801 C  CG  . TYR   B 113 ? 0.1259 0.1106 0.2180 -0.0067 0.0118  0.0142  113 TYR   B CG  
5802 C  CD1 . TYR   B 113 ? 0.1282 0.1157 0.2368 -0.0065 0.0189  0.0152  113 TYR   B CD1 
5803 C  CD2 . TYR   B 113 ? 0.1325 0.1094 0.2228 -0.0044 0.0114  0.0098  113 TYR   B CD2 
5804 C  CE1 . TYR   B 113 ? 0.1282 0.1208 0.2336 -0.0063 0.0236  0.0093  113 TYR   B CE1 
5805 C  CE2 . TYR   B 113 ? 0.1392 0.1083 0.2284 -0.0011 0.0134  0.0158  113 TYR   B CE2 
5806 C  CZ  . TYR   B 113 ? 0.1296 0.1157 0.2372 0.0031  0.0146  0.0161  113 TYR   B CZ  
5807 O  OH  . TYR   B 113 ? 0.1400 0.1110 0.2618 0.0114  0.0234  0.0138  113 TYR   B OH  
5817 N  N   . GLU   B 114 ? 0.1148 0.1050 0.2064 -0.0042 0.0127  0.0074  114 GLU   B N   
5818 C  CA  . GLU   B 114 ? 0.1150 0.1086 0.2048 0.0004  0.0069  0.0020  114 GLU   B CA  
5819 C  C   . GLU   B 114 ? 0.1146 0.1100 0.1958 -0.0047 0.0096  0.0012  114 GLU   B C   
5820 O  O   . GLU   B 114 ? 0.1177 0.1148 0.2059 -0.0027 0.0048  0.0068  114 GLU   B O   
5821 C  CB  . GLU   B 114 ? 0.1166 0.1165 0.2135 -0.0025 0.0111  0.0104  114 GLU   B CB  
5822 C  CG  . GLU   B 114 ? 0.1248 0.1153 0.2161 -0.0025 0.0074  0.0091  114 GLU   B CG  
5823 C  CD  . GLU   B 114 ? 0.1190 0.1162 0.2256 -0.0077 0.0086  0.0062  114 GLU   B CD  
5824 O  OE1 . GLU   B 114 ? 0.1206 0.1323 0.2248 -0.0108 0.0186  0.0119  114 GLU   B OE1 
5825 O  OE2 . GLU   B 114 ? 0.1230 0.1352 0.2372 -0.0151 0.0080  0.0061  114 GLU   B OE2 
5832 N  N   . ASN   B 115 ? 0.1201 0.1068 0.1981 -0.0031 0.0001  0.0063  115 ASN   B N   
5833 C  CA  . ASN   B 115 ? 0.1203 0.1162 0.1821 -0.0079 0.0019  0.0129  115 ASN   B CA  
5834 C  C   . ASN   B 115 ? 0.1133 0.1104 0.1804 -0.0106 -0.0023 0.0025  115 ASN   B C   
5835 O  O   . ASN   B 115 ? 0.1261 0.1160 0.1922 -0.0136 0.0025  0.0064  115 ASN   B O   
5836 C  CB  . ASN   B 115 ? 0.1278 0.1284 0.1822 -0.0124 0.0065  0.0057  115 ASN   B CB  
5837 C  CG  . ASN   B 115 ? 0.1374 0.1314 0.1895 -0.0024 0.0071  0.0019  115 ASN   B CG  
5838 O  OD1 . ASN   B 115 ? 0.1763 0.1430 0.2098 -0.0060 0.0109  -0.0054 115 ASN   B OD1 
5839 N  ND2 . ASN   B 115 ? 0.1315 0.1375 0.1876 -0.0060 0.0092  0.0080  115 ASN   B ND2 
5846 N  N   . PHE   B 116 ? 0.1163 0.1126 0.1701 -0.0089 -0.0003 0.0041  116 PHE   B N   
5847 C  CA  . PHE   B 116 ? 0.1206 0.1161 0.1806 -0.0108 -0.0023 0.0035  116 PHE   B CA  
5848 C  C   . PHE   B 116 ? 0.1222 0.1064 0.1846 -0.0148 -0.0051 0.0047  116 PHE   B C   
5849 O  O   . PHE   B 116 ? 0.1233 0.1171 0.1874 -0.0030 -0.0066 0.0039  116 PHE   B O   
5850 C  CB  . PHE   B 116 ? 0.1198 0.1111 0.1759 -0.0067 -0.0153 0.0074  116 PHE   B CB  
5851 C  CG  . PHE   B 116 ? 0.1134 0.1107 0.1767 -0.0056 -0.0027 0.0078  116 PHE   B CG  
5852 C  CD1 . PHE   B 116 ? 0.1233 0.1196 0.1915 -0.0046 0.0000  0.0050  116 PHE   B CD1 
5853 C  CD2 . PHE   B 116 ? 0.1193 0.1215 0.1691 -0.0027 0.0005  -0.0002 116 PHE   B CD2 
5854 C  CE1 . PHE   B 116 ? 0.1279 0.1257 0.1825 -0.0076 -0.0092 0.0094  116 PHE   B CE1 
5855 C  CE2 . PHE   B 116 ? 0.1232 0.1227 0.1676 -0.0030 0.0002  0.0035  116 PHE   B CE2 
5856 C  CZ  . PHE   B 116 ? 0.1175 0.1289 0.1721 -0.0047 -0.0087 0.0054  116 PHE   B CZ  
5866 N  N   . ASN   B 117 ? 0.1191 0.1120 0.1861 -0.0060 -0.0063 0.0042  117 ASN   B N   
5867 C  CA  . ASN   B 117 ? 0.1281 0.1141 0.1886 -0.0032 -0.0063 0.0001  117 ASN   B CA  
5868 C  C   . ASN   B 117 ? 0.1331 0.1122 0.1974 0.0004  -0.0070 0.0057  117 ASN   B C   
5869 O  O   . ASN   B 117 ? 0.1395 0.1167 0.2264 -0.0093 -0.0282 0.0095  117 ASN   B O   
5870 C  CB  . ASN   B 117 ? 0.1285 0.1153 0.1927 -0.0059 -0.0055 -0.0011 117 ASN   B CB  
5871 C  CG  . ASN   B 117 ? 0.1214 0.1193 0.2060 0.0004  -0.0009 -0.0022 117 ASN   B CG  
5872 O  OD1 . ASN   B 117 ? 0.1432 0.1162 0.2229 -0.0158 0.0055  -0.0043 117 ASN   B OD1 
5873 N  ND2 . ASN   B 117 ? 0.1271 0.1236 0.2062 -0.0048 0.0005  -0.0033 117 ASN   B ND2 
5880 N  N   . GLN   B 118 ? 0.1291 0.1099 0.1972 -0.0093 -0.0190 0.0001  118 GLN   B N   
5881 C  CA  . GLN   B 118 ? 0.1337 0.1162 0.2122 -0.0034 -0.0119 -0.0020 118 GLN   B CA  
5882 C  C   . GLN   B 118 ? 0.1359 0.1145 0.2108 -0.0050 -0.0072 -0.0037 118 GLN   B C   
5883 O  O   . GLN   B 118 ? 0.1569 0.1090 0.2496 -0.0096 0.0029  0.0054  118 GLN   B O   
5884 C  CB  . GLN   B 118 ? 0.1405 0.1159 0.2157 0.0005  -0.0124 0.0009  118 GLN   B CB  
5885 C  CG  . GLN   B 118 ? 0.1494 0.1209 0.2066 0.0022  -0.0058 -0.0076 118 GLN   B CG  
5886 C  CD  . GLN   B 118 ? 0.1517 0.1155 0.2170 -0.0021 -0.0125 -0.0153 118 GLN   B CD  
5887 O  OE1 . GLN   B 118 ? 0.1607 0.1155 0.2334 0.0004  0.0069  0.0013  118 GLN   B OE1 
5888 N  NE2 . GLN   B 118 ? 0.1615 0.1184 0.2228 0.0010  -0.0148 -0.0010 118 GLN   B NE2 
5897 N  N   . HIS   B 119 ? 0.1392 0.1154 0.1805 -0.0092 -0.0124 0.0064  119 HIS   B N   
5898 C  CA  . HIS   B 119 ? 0.1482 0.1285 0.1712 -0.0059 -0.0170 0.0103  119 HIS   B CA  
5899 C  C   . HIS   B 119 ? 0.1505 0.1260 0.1628 -0.0085 -0.0256 0.0055  119 HIS   B C   
5900 O  O   . HIS   B 119 ? 0.1560 0.1248 0.1921 -0.0269 -0.0165 0.0095  119 HIS   B O   
5901 C  CB  . HIS   B 119 ? 0.1504 0.1412 0.1800 -0.0080 -0.0227 0.0031  119 HIS   B CB  
5902 C  CG  . HIS   B 119 ? 0.1554 0.1623 0.1957 0.0049  -0.0345 -0.0143 119 HIS   B CG  
5903 N  ND1 . HIS   B 119 ? 0.1684 0.1767 0.2224 0.0018  -0.0502 -0.0290 119 HIS   B ND1 
5904 C  CD2 . HIS   B 119 ? 0.1771 0.1828 0.2019 0.0335  -0.0446 -0.0174 119 HIS   B CD2 
5905 C  CE1 . HIS   B 119 ? 0.1874 0.1947 0.2305 0.0162  -0.0550 -0.0415 119 HIS   B CE1 
5906 N  NE2 . HIS   B 119 ? 0.1918 0.2045 0.2225 0.0319  -0.0475 -0.0367 119 HIS   B NE2 
5914 N  N   . GLU   B 120 ? 0.1680 0.1306 0.1616 -0.0108 -0.0347 0.0141  120 GLU   B N   
5915 C  CA  . GLU   B 120 ? 0.2009 0.1462 0.1805 -0.0023 -0.0470 0.0313  120 GLU   B CA  
5916 C  C   . GLU   B 120 ? 0.1763 0.1338 0.1751 -0.0140 -0.0374 0.0279  120 GLU   B C   
5917 O  O   . GLU   B 120 ? 0.1656 0.1493 0.1781 -0.0177 -0.0352 0.0102  120 GLU   B O   
5918 C  CB  . GLU   B 120 ? 0.2698 0.1907 0.2541 0.0226  -0.0774 0.0559  120 GLU   B CB  
5919 C  CG  . GLU   B 120 ? 0.3344 0.2725 0.3562 0.0339  -0.0997 0.0757  120 GLU   B CG  
5920 C  CD  . GLU   B 120 ? 0.3862 0.3483 0.4662 0.0379  -0.1058 0.0821  120 GLU   B CD  
5921 O  OE1 . GLU   B 120 ? 0.4080 0.3768 0.5048 0.0337  -0.1031 0.0891  120 GLU   B OE1 
5922 O  OE2 . GLU   B 120 ? 0.4057 0.3803 0.5198 0.0397  -0.1044 0.0744  120 GLU   B OE2 
5929 N  N   . VAL   B 121 ? 0.1642 0.1315 0.1686 -0.0244 -0.0292 0.0239  121 VAL   B N   
5930 C  CA  . VAL   B 121 ? 0.1592 0.1453 0.1544 -0.0202 -0.0246 0.0160  121 VAL   B CA  
5931 C  C   . VAL   B 121 ? 0.1509 0.1333 0.1549 -0.0246 -0.0152 0.0151  121 VAL   B C   
5932 O  O   . VAL   B 121 ? 0.1596 0.1298 0.1742 -0.0331 -0.0239 0.0095  121 VAL   B O   
5933 C  CB  . VAL   B 121 ? 0.1855 0.1812 0.1690 -0.0084 -0.0293 0.0149  121 VAL   B CB  
5934 C  CG1 . VAL   B 121 ? 0.1880 0.1925 0.2012 -0.0195 -0.0175 0.0125  121 VAL   B CG1 
5935 C  CG2 . VAL   B 121 ? 0.2101 0.2038 0.1631 0.0050  -0.0180 0.0009  121 VAL   B CG2 
5945 N  N   . LEU   B 122 ? 0.1438 0.1296 0.1545 -0.0215 -0.0238 0.0120  122 LEU   B N   
5946 C  CA  . LEU   B 122 ? 0.1357 0.1378 0.1417 -0.0203 -0.0221 0.0117  122 LEU   B CA  
5947 C  C   . LEU   B 122 ? 0.1361 0.1241 0.1440 -0.0260 -0.0167 0.0091  122 LEU   B C   
5948 O  O   . LEU   B 122 ? 0.1463 0.1278 0.1772 -0.0328 -0.0225 0.0029  122 LEU   B O   
5949 C  CB  . LEU   B 122 ? 0.1612 0.1404 0.1705 -0.0092 -0.0252 0.0108  122 LEU   B CB  
5950 C  CG  . LEU   B 122 ? 0.1494 0.1493 0.1805 -0.0168 -0.0105 0.0114  122 LEU   B CG  
5951 C  CD1 . LEU   B 122 ? 0.1551 0.1730 0.1825 -0.0195 -0.0151 0.0080  122 LEU   B CD1 
5952 C  CD2 . LEU   B 122 ? 0.1548 0.1544 0.1632 -0.0094 -0.0091 0.0006  122 LEU   B CD2 
5964 N  N   . LEU   B 123 ? 0.1422 0.1155 0.1399 -0.0235 -0.0108 0.0127  123 LEU   B N   
5965 C  CA  . LEU   B 123 ? 0.1393 0.1174 0.1406 -0.0267 -0.0176 -0.0014 123 LEU   B CA  
5966 C  C   . LEU   B 123 ? 0.1340 0.1151 0.1400 -0.0257 -0.0193 0.0042  123 LEU   B C   
5967 O  O   . LEU   B 123 ? 0.1443 0.1189 0.1478 -0.0322 -0.0182 0.0035  123 LEU   B O   
5968 C  CB  . LEU   B 123 ? 0.1449 0.1251 0.1550 -0.0273 -0.0133 -0.0051 123 LEU   B CB  
5969 C  CG  . LEU   B 123 ? 0.1420 0.1287 0.1661 -0.0174 -0.0118 0.0075  123 LEU   B CG  
5970 C  CD1 . LEU   B 123 ? 0.1546 0.1329 0.1679 -0.0172 0.0014  -0.0091 123 LEU   B CD1 
5971 C  CD2 . LEU   B 123 ? 0.1533 0.1370 0.1863 -0.0150 0.0007  0.0182  123 LEU   B CD2 
5983 N  N   . ALA   B 124 ? 0.1321 0.1162 0.1481 -0.0234 -0.0062 -0.0002 124 ALA   B N   
5984 C  CA  . ALA   B 124 ? 0.1267 0.1161 0.1577 -0.0176 -0.0101 -0.0010 124 ALA   B CA  
5985 C  C   . ALA   B 124 ? 0.1213 0.1164 0.1555 -0.0163 -0.0112 0.0007  124 ALA   B C   
5986 O  O   . ALA   B 124 ? 0.1316 0.1148 0.1692 -0.0150 -0.0158 0.0020  124 ALA   B O   
5987 C  CB  . ALA   B 124 ? 0.1327 0.1222 0.1657 -0.0133 0.0010  0.0023  124 ALA   B CB  
5993 N  N   . PRO   B 125 ? 0.1329 0.1198 0.1509 -0.0144 -0.0130 0.0133  125 PRO   B N   
5994 C  CA  . PRO   B 125 ? 0.1391 0.1186 0.1673 -0.0159 -0.0139 0.0229  125 PRO   B CA  
5995 C  C   . PRO   B 125 ? 0.1325 0.1126 0.1816 -0.0160 -0.0069 0.0049  125 PRO   B C   
5996 O  O   . PRO   B 125 ? 0.1399 0.1124 0.1960 -0.0142 -0.0002 0.0118  125 PRO   B O   
5997 C  CB  . PRO   B 125 ? 0.1396 0.1432 0.1777 -0.0188 -0.0207 0.0328  125 PRO   B CB  
5998 C  CG  . PRO   B 125 ? 0.1469 0.1463 0.1644 -0.0280 -0.0161 0.0159  125 PRO   B CG  
5999 C  CD  . PRO   B 125 ? 0.1403 0.1275 0.1517 -0.0279 -0.0090 0.0053  125 PRO   B CD  
6007 N  N   . LEU   B 126 ? 0.1390 0.1102 0.2078 -0.0163 0.0107  0.0161  126 LEU   B N   
6008 C  CA  . LEU   B 126 ? 0.1452 0.1209 0.2133 -0.0127 0.0144  0.0168  126 LEU   B CA  
6009 C  C   . LEU   B 126 ? 0.1394 0.1278 0.2190 0.0008  0.0192  0.0209  126 LEU   B C   
6010 O  O   . LEU   B 126 ? 0.1627 0.1549 0.2326 0.0190  -0.0049 -0.0029 126 LEU   B O   
6011 C  CB  . LEU   B 126 ? 0.1630 0.1219 0.2406 -0.0182 0.0257  0.0129  126 LEU   B CB  
6012 C  CG  . LEU   B 126 ? 0.1809 0.1318 0.2487 -0.0261 0.0255  -0.0095 126 LEU   B CG  
6013 C  CD1 . LEU   B 126 ? 0.1949 0.1398 0.2935 -0.0227 0.0224  -0.0152 126 LEU   B CD1 
6014 C  CD2 . LEU   B 126 ? 0.1876 0.1441 0.2471 -0.0276 0.0227  -0.0089 126 LEU   B CD2 
6026 N  N   . LEU   B 127 ? 0.1362 0.1155 0.2221 -0.0000 0.0189  0.0172  127 LEU   B N   
6027 C  CA  . LEU   B 127 ? 0.1404 0.1313 0.2248 -0.0063 0.0300  0.0194  127 LEU   B CA  
6028 C  C   . LEU   B 127 ? 0.1351 0.1236 0.2208 0.0008  0.0218  0.0197  127 LEU   B C   
6029 O  O   . LEU   B 127 ? 0.1365 0.1279 0.2360 -0.0147 0.0117  0.0269  127 LEU   B O   
6030 C  CB  . LEU   B 127 ? 0.1530 0.1256 0.2366 -0.0018 0.0211  0.0242  127 LEU   B CB  
6031 C  CG  . LEU   B 127 ? 0.1616 0.1294 0.2457 0.0013  0.0231  0.0204  127 LEU   B CG  
6032 C  CD1 . LEU   B 127 ? 0.1713 0.1291 0.2440 0.0018  0.0061  0.0082  127 LEU   B CD1 
6033 C  CD2 . LEU   B 127 ? 0.1678 0.1383 0.2600 -0.0132 0.0225  0.0272  127 LEU   B CD2 
6045 N  N   . SER   B 128 ? 0.1407 0.1250 0.2174 0.0022  0.0081  0.0195  128 SER   B N   
6046 C  CA  . SER   B 128 ? 0.1556 0.1331 0.2206 0.0083  -0.0019 0.0243  128 SER   B CA  
6047 C  C   . SER   B 128 ? 0.1669 0.1390 0.2460 0.0066  -0.0213 0.0219  128 SER   B C   
6048 O  O   . SER   B 128 ? 0.1806 0.1409 0.2808 0.0047  -0.0158 0.0282  128 SER   B O   
6049 C  CB  . SER   B 128 ? 0.1624 0.1310 0.2231 0.0054  0.0076  0.0317  128 SER   B CB  
6050 O  OG  . SER   B 128 ? 0.1676 0.1471 0.2259 0.0099  0.0133  0.0332  128 SER   B OG  
6056 N  N   . ALA   B 129 ? 0.1790 0.1403 0.2652 0.0233  -0.0122 0.0101  129 ALA   B N   
6057 C  CA  . ALA   B 129 ? 0.1936 0.1500 0.2817 0.0307  -0.0094 -0.0014 129 ALA   B CA  
6058 C  C   . ALA   B 129 ? 0.1798 0.1405 0.2734 0.0217  0.0068  0.0074  129 ALA   B C   
6059 O  O   . ALA   B 129 ? 0.1646 0.1474 0.2742 0.0193  0.0011  0.0098  129 ALA   B O   
6060 C  CB  . ALA   B 129 ? 0.2150 0.1740 0.3110 0.0365  0.0064  -0.0101 129 ALA   B CB  
6066 N  N   . GLY   B 130 ? 0.1798 0.1355 0.2700 0.0286  0.0118  0.0025  130 GLY   B N   
6067 C  CA  . GLY   B 130 ? 0.1861 0.1484 0.2651 0.0235  0.0276  0.0000  130 GLY   B CA  
6068 C  C   . GLY   B 130 ? 0.1896 0.1560 0.2628 0.0144  0.0205  0.0070  130 GLY   B C   
6069 O  O   . GLY   B 130 ? 0.2032 0.1627 0.2711 0.0138  0.0158  0.0122  130 GLY   B O   
6073 N  N   . ILE   B 131 ? 0.1824 0.1668 0.2682 0.0300  0.0214  -0.0008 131 ILE   B N   
6074 C  CA  . ILE   B 131 ? 0.1999 0.1823 0.2681 0.0283  0.0077  0.0154  131 ILE   B CA  
6075 C  C   . ILE   B 131 ? 0.2129 0.1749 0.2360 0.0172  0.0047  0.0208  131 ILE   B C   
6076 O  O   . ILE   B 131 ? 0.2426 0.1902 0.2463 0.0214  -0.0094 0.0260  131 ILE   B O   
6077 C  CB  . ILE   B 131 ? 0.1999 0.2174 0.3020 0.0283  -0.0076 0.0239  131 ILE   B CB  
6078 C  CG1 . ILE   B 131 ? 0.2010 0.2388 0.3245 0.0071  -0.0031 0.0273  131 ILE   B CG1 
6079 C  CG2 . ILE   B 131 ? 0.2008 0.2346 0.3213 0.0340  -0.0068 0.0195  131 ILE   B CG2 
6080 C  CD1 . ILE   B 131 ? 0.2076 0.2576 0.3399 -0.0107 -0.0093 0.0294  131 ILE   B CD1 
6092 N  N   . PHE   B 132 ? 0.1961 0.1563 0.2236 0.0141  0.0221  0.0254  132 PHE   B N   
6093 C  CA  . PHE   B 132 ? 0.2095 0.1574 0.2238 0.0061  0.0371  0.0169  132 PHE   B CA  
6094 C  C   . PHE   B 132 ? 0.2283 0.1702 0.2471 0.0093  0.0491  0.0181  132 PHE   B C   
6095 O  O   . PHE   B 132 ? 0.2473 0.1907 0.2670 0.0033  0.0614  0.0241  132 PHE   B O   
6096 C  CB  . PHE   B 132 ? 0.1910 0.1561 0.2060 0.0109  0.0345  0.0229  132 PHE   B CB  
6097 C  CG  . PHE   B 132 ? 0.1863 0.1587 0.2087 0.0147  0.0280  0.0241  132 PHE   B CG  
6098 C  CD1 . PHE   B 132 ? 0.1936 0.1592 0.2392 0.0135  0.0280  0.0177  132 PHE   B CD1 
6099 C  CD2 . PHE   B 132 ? 0.1885 0.1612 0.1852 0.0268  0.0226  0.0284  132 PHE   B CD2 
6100 C  CE1 . PHE   B 132 ? 0.1989 0.1648 0.2412 0.0091  0.0210  0.0179  132 PHE   B CE1 
6101 C  CE2 . PHE   B 132 ? 0.1951 0.1655 0.1837 0.0223  0.0085  0.0239  132 PHE   B CE2 
6102 C  CZ  . PHE   B 132 ? 0.1993 0.1672 0.2181 0.0149  0.0022  0.0295  132 PHE   B CZ  
6112 N  N   . GLY   B 133 ? 0.2248 0.1606 0.2540 0.0039  0.0358  0.0383  133 GLY   B N   
6113 C  CA  . GLY   B 133 ? 0.2350 0.1750 0.2631 -0.0162 0.0329  0.0426  133 GLY   B CA  
6114 C  C   . GLY   B 133 ? 0.2372 0.1826 0.2613 -0.0278 0.0374  0.0463  133 GLY   B C   
6115 O  O   . GLY   B 133 ? 0.2547 0.1922 0.2994 -0.0403 0.0366  0.0543  133 GLY   B O   
6119 N  N   . ALA   B 134 ? 0.2178 0.1822 0.2452 -0.0254 0.0409  0.0335  134 ALA   B N   
6120 C  CA  . ALA   B 134 ? 0.2119 0.1806 0.2520 -0.0185 0.0437  0.0234  134 ALA   B CA  
6121 C  C   . ALA   B 134 ? 0.2167 0.1693 0.2607 -0.0105 0.0391  0.0312  134 ALA   B C   
6122 O  O   . ALA   B 134 ? 0.2194 0.1855 0.2780 0.0003  0.0316  0.0240  134 ALA   B O   
6123 C  CB  . ALA   B 134 ? 0.2107 0.1826 0.2675 -0.0102 0.0363  0.0195  134 ALA   B CB  
6129 N  N   . ASP   B 135 ? 0.2318 0.1608 0.2599 -0.0150 0.0226  0.0355  135 ASP   B N   
6130 C  CA  . ASP   B 135 ? 0.2485 0.1560 0.2756 -0.0179 0.0068  0.0386  135 ASP   B CA  
6131 C  C   . ASP   B 135 ? 0.2310 0.1450 0.2646 -0.0058 0.0067  0.0367  135 ASP   B C   
6132 O  O   . ASP   B 135 ? 0.2243 0.1413 0.2698 -0.0057 0.0082  0.0313  135 ASP   B O   
6133 C  CB  . ASP   B 135 ? 0.2790 0.1708 0.3059 -0.0405 0.0053  0.0412  135 ASP   B CB  
6134 C  CG  . ASP   B 135 ? 0.3060 0.1710 0.3514 -0.0584 0.0048  0.0347  135 ASP   B CG  
6135 O  OD1 . ASP   B 135 ? 0.3132 0.1545 0.3470 -0.0396 -0.0031 0.0316  135 ASP   B OD1 
6136 O  OD2 . ASP   B 135 ? 0.3259 0.2033 0.4069 -0.0728 0.0051  0.0181  135 ASP   B OD2 
6141 N  N   . PRO   B 136 ? 0.2218 0.1474 0.2741 0.0141  -0.0081 0.0305  136 PRO   B N   
6142 C  CA  . PRO   B 136 ? 0.1962 0.1385 0.2764 0.0145  -0.0063 0.0173  136 PRO   B CA  
6143 C  C   . PRO   B 136 ? 0.1762 0.1286 0.2906 0.0137  -0.0066 0.0125  136 PRO   B C   
6144 O  O   . PRO   B 136 ? 0.1570 0.1287 0.2870 0.0097  0.0085  0.0119  136 PRO   B O   
6145 C  CB  . PRO   B 136 ? 0.2057 0.1611 0.2869 0.0273  -0.0157 0.0021  136 PRO   B CB  
6146 C  CG  . PRO   B 136 ? 0.2251 0.1690 0.3037 0.0322  -0.0107 0.0063  136 PRO   B CG  
6147 C  CD  . PRO   B 136 ? 0.2284 0.1615 0.2901 0.0365  -0.0071 0.0155  136 PRO   B CD  
6155 N  N   . ILE   B 137 ? 0.1869 0.1227 0.2974 0.0203  -0.0089 0.0078  137 ILE   B N   
6156 C  CA  . ILE   B 137 ? 0.1930 0.1213 0.3039 -0.0006 0.0010  0.0047  137 ILE   B CA  
6157 C  C   . ILE   B 137 ? 0.1847 0.1278 0.2957 -0.0091 0.0127  0.0153  137 ILE   B C   
6158 O  O   . ILE   B 137 ? 0.1750 0.1252 0.2940 -0.0116 0.0105  0.0133  137 ILE   B O   
6159 C  CB  . ILE   B 137 ? 0.2234 0.1260 0.3489 -0.0024 -0.0018 0.0092  137 ILE   B CB  
6160 C  CG1 . ILE   B 137 ? 0.2490 0.1431 0.3973 0.0030  -0.0002 -0.0088 137 ILE   B CG1 
6161 C  CG2 . ILE   B 137 ? 0.2291 0.1297 0.3520 -0.0305 -0.0048 0.0141  137 ILE   B CG2 
6162 C  CD1 . ILE   B 137 ? 0.2706 0.1707 0.4329 0.0175  -0.0025 -0.0087 137 ILE   B CD1 
6174 N  N   . HIS   B 138 ? 0.1914 0.1276 0.2917 -0.0091 0.0224  0.0156  138 HIS   B N   
6175 C  CA  . HIS   B 138 ? 0.1969 0.1371 0.2836 -0.0071 0.0356  0.0179  138 HIS   B CA  
6176 C  C   . HIS   B 138 ? 0.1786 0.1345 0.2741 -0.0068 0.0351  0.0256  138 HIS   B C   
6177 O  O   . HIS   B 138 ? 0.1670 0.1347 0.3032 -0.0041 0.0354  0.0398  138 HIS   B O   
6178 C  CB  . HIS   B 138 ? 0.2213 0.1513 0.2948 -0.0118 0.0520  0.0135  138 HIS   B CB  
6179 C  CG  . HIS   B 138 ? 0.2452 0.1712 0.3001 -0.0141 0.0717  0.0332  138 HIS   B CG  
6180 N  ND1 . HIS   B 138 ? 0.2531 0.1888 0.3212 -0.0095 0.0832  0.0256  138 HIS   B ND1 
6181 C  CD2 . HIS   B 138 ? 0.2623 0.1823 0.2985 -0.0140 0.0732  0.0315  138 HIS   B CD2 
6182 C  CE1 . HIS   B 138 ? 0.2586 0.1888 0.3181 -0.0104 0.0867  0.0322  138 HIS   B CE1 
6183 N  NE2 . HIS   B 138 ? 0.2681 0.1795 0.3021 -0.0070 0.0828  0.0243  138 HIS   B NE2 
6191 N  N   . SER   B 139 ? 0.1753 0.1243 0.2744 0.0009  0.0313  0.0155  139 SER   B N   
6192 C  CA  . SER   B 139 ? 0.1729 0.1151 0.2545 -0.0046 0.0312  0.0055  139 SER   B CA  
6193 C  C   . SER   B 139 ? 0.1506 0.1092 0.2534 -0.0014 0.0205  0.0085  139 SER   B C   
6194 O  O   . SER   B 139 ? 0.1481 0.1120 0.2567 -0.0026 0.0101  0.0072  139 SER   B O   
6195 C  CB  . SER   B 139 ? 0.1793 0.1172 0.2662 -0.0036 0.0114  0.0034  139 SER   B CB  
6196 O  OG  . SER   B 139 ? 0.1774 0.1164 0.2666 -0.0032 -0.0043 0.0152  139 SER   B OG  
6202 N  N   . LEU   B 140 ? 0.1495 0.1086 0.2466 -0.0087 0.0185  -0.0036 140 LEU   B N   
6203 C  CA  . LEU   B 140 ? 0.1425 0.1100 0.2523 -0.0026 0.0126  -0.0021 140 LEU   B CA  
6204 C  C   . LEU   B 140 ? 0.1401 0.1149 0.2648 -0.0062 0.0066  -0.0008 140 LEU   B C   
6205 O  O   . LEU   B 140 ? 0.1384 0.1227 0.2566 -0.0032 0.0040  0.0033  140 LEU   B O   
6206 C  CB  . LEU   B 140 ? 0.1429 0.1084 0.2605 -0.0112 0.0120  -0.0095 140 LEU   B CB  
6207 C  CG  . LEU   B 140 ? 0.1540 0.1128 0.2577 -0.0124 0.0068  0.0038  140 LEU   B CG  
6208 C  CD1 . LEU   B 140 ? 0.1579 0.1286 0.2713 -0.0128 0.0148  0.0008  140 LEU   B CD1 
6209 C  CD2 . LEU   B 140 ? 0.1719 0.1237 0.2800 -0.0106 0.0021  -0.0058 140 LEU   B CD2 
6221 N  N   . ARG   B 141 ? 0.1306 0.1110 0.2769 -0.0113 0.0103  -0.0020 141 ARG   B N   
6222 C  CA  . ARG   B 141 ? 0.1366 0.1124 0.3038 -0.0170 0.0254  -0.0030 141 ARG   B CA  
6223 C  C   . ARG   B 141 ? 0.1334 0.1171 0.2957 -0.0140 0.0142  0.0013  141 ARG   B C   
6224 O  O   . ARG   B 141 ? 0.1379 0.1166 0.2983 -0.0127 -0.0001 -0.0144 141 ARG   B O   
6225 C  CB  . ARG   B 141 ? 0.1516 0.1270 0.3196 -0.0227 0.0240  -0.0084 141 ARG   B CB  
6226 C  CG  . ARG   B 141 ? 0.1838 0.1514 0.3341 -0.0217 0.0250  -0.0090 141 ARG   B CG  
6227 C  CD  . ARG   B 141 ? 0.2231 0.1754 0.3366 -0.0178 0.0088  -0.0130 141 ARG   B CD  
6228 N  NE  . ARG   B 141 ? 0.2473 0.1772 0.3266 -0.0316 0.0146  -0.0170 141 ARG   B NE  
6229 C  CZ  . ARG   B 141 ? 0.2622 0.1597 0.3059 -0.0277 0.0209  -0.0255 141 ARG   B CZ  
6230 N  NH1 . ARG   B 141 ? 0.2706 0.1478 0.2948 -0.0248 0.0244  -0.0231 141 ARG   B NH1 
6231 N  NH2 . ARG   B 141 ? 0.2751 0.1724 0.3127 -0.0126 0.0123  -0.0168 141 ARG   B NH2 
6245 N  N   . VAL   B 142 ? 0.1390 0.1088 0.2826 -0.0079 0.0180  -0.0037 142 VAL   B N   
6246 C  CA  . VAL   B 142 ? 0.1345 0.1168 0.2717 -0.0055 0.0231  0.0012  142 VAL   B CA  
6247 C  C   . VAL   B 142 ? 0.1326 0.1140 0.2688 -0.0006 0.0143  -0.0045 142 VAL   B C   
6248 O  O   . VAL   B 142 ? 0.1370 0.1119 0.2868 0.0005  0.0208  -0.0055 142 VAL   B O   
6249 C  CB  . VAL   B 142 ? 0.1497 0.1255 0.2744 -0.0028 0.0273  0.0119  142 VAL   B CB  
6250 C  CG1 . VAL   B 142 ? 0.1448 0.1243 0.2669 0.0054  0.0277  0.0098  142 VAL   B CG1 
6251 C  CG2 . VAL   B 142 ? 0.1670 0.1297 0.2852 -0.0003 0.0212  0.0153  142 VAL   B CG2 
6261 N  N   . CYS   B 143 ? 0.1279 0.1138 0.2542 -0.0020 0.0047  0.0039  143 CYS   B N   
6262 C  CA  . CYS   B 143 ? 0.1265 0.1135 0.2626 -0.0081 0.0030  0.0027  143 CYS   B CA  
6263 C  C   . CYS   B 143 ? 0.1206 0.1145 0.2616 -0.0068 0.0082  -0.0030 143 CYS   B C   
6264 O  O   . CYS   B 143 ? 0.1258 0.1170 0.2591 -0.0067 0.0044  -0.0033 143 CYS   B O   
6265 C  CB  . CYS   B 143 ? 0.1362 0.1246 0.2527 -0.0090 0.0066  -0.0042 143 CYS   B CB  
6266 S  SG  . CYS   B 143 ? 0.1349 0.1390 0.2473 -0.0058 0.0059  0.0039  143 CYS   B SG  
6272 N  N   . VAL   B 144 ? 0.1283 0.1157 0.2714 -0.0095 0.0017  -0.0109 144 VAL   B N   
6273 C  CA  . VAL   B 144 ? 0.1348 0.1258 0.2908 -0.0126 -0.0081 -0.0156 144 VAL   B CA  
6274 C  C   . VAL   B 144 ? 0.1314 0.1284 0.2946 -0.0138 -0.0119 -0.0039 144 VAL   B C   
6275 O  O   . VAL   B 144 ? 0.1438 0.1488 0.3156 -0.0053 -0.0102 0.0180  144 VAL   B O   
6276 C  CB  . VAL   B 144 ? 0.1623 0.1405 0.3377 -0.0122 -0.0180 -0.0338 144 VAL   B CB  
6277 C  CG1 . VAL   B 144 ? 0.1868 0.1777 0.3591 -0.0060 -0.0217 -0.0262 144 VAL   B CG1 
6278 C  CG2 . VAL   B 144 ? 0.1814 0.1436 0.3262 -0.0001 -0.0360 -0.0438 144 VAL   B CG2 
6288 N  N   . ASP   B 145 ? 0.1360 0.1206 0.3045 -0.0120 -0.0041 -0.0137 145 ASP   B N   
6289 C  CA  . ASP   B 145 ? 0.1340 0.1281 0.3302 -0.0088 0.0086  -0.0100 145 ASP   B CA  
6290 C  C   . ASP   B 145 ? 0.1300 0.1325 0.3119 -0.0084 0.0137  -0.0076 145 ASP   B C   
6291 O  O   . ASP   B 145 ? 0.1322 0.1447 0.3649 -0.0143 0.0179  -0.0251 145 ASP   B O   
6292 C  CB  . ASP   B 145 ? 0.1460 0.1369 0.3755 -0.0149 0.0220  -0.0062 145 ASP   B CB  
6293 C  CG  . ASP   B 145 ? 0.1598 0.1350 0.4237 -0.0260 0.0323  -0.0102 145 ASP   B CG  
6294 O  OD1 . ASP   B 145 ? 0.1685 0.1403 0.4297 -0.0230 -0.0010 -0.0150 145 ASP   B OD1 
6295 O  OD2 . ASP   B 145 ? 0.1895 0.1444 0.4641 -0.0304 0.0566  -0.0016 145 ASP   B OD2 
6300 N  N   . THR   B 146 ? 0.1209 0.1194 0.2722 -0.0112 0.0077  0.0028  146 THR   B N   
6301 C  CA  . THR   B 146 ? 0.1271 0.1133 0.2453 -0.0076 0.0075  -0.0040 146 THR   B CA  
6302 C  C   . THR   B 146 ? 0.1313 0.1166 0.2360 -0.0079 0.0009  0.0032  146 THR   B C   
6303 O  O   . THR   B 146 ? 0.1365 0.1171 0.2430 -0.0079 -0.0028 0.0025  146 THR   B O   
6304 C  CB  . THR   B 146 ? 0.1357 0.1154 0.2507 -0.0061 0.0202  0.0039  146 THR   B CB  
6305 O  OG1 . THR   B 146 ? 0.1383 0.1131 0.2657 -0.0075 0.0235  0.0140  146 THR   B OG1 
6306 C  CG2 . THR   B 146 ? 0.1451 0.1224 0.2492 -0.0050 0.0146  0.0027  146 THR   B CG2 
6314 N  N   . VAL   B 147 ? 0.1356 0.1203 0.2284 -0.0074 0.0088  0.0087  147 VAL   B N   
6315 C  CA  . VAL   B 147 ? 0.1335 0.1153 0.2192 -0.0120 -0.0037 0.0001  147 VAL   B CA  
6316 C  C   . VAL   B 147 ? 0.1283 0.1170 0.2308 -0.0172 -0.0097 -0.0057 147 VAL   B C   
6317 O  O   . VAL   B 147 ? 0.1409 0.1299 0.2490 -0.0221 -0.0263 -0.0180 147 VAL   B O   
6318 C  CB  . VAL   B 147 ? 0.1399 0.1301 0.2050 -0.0094 -0.0094 -0.0019 147 VAL   B CB  
6319 C  CG1 . VAL   B 147 ? 0.1453 0.1429 0.1934 -0.0185 -0.0044 0.0021  147 VAL   B CG1 
6320 C  CG2 . VAL   B 147 ? 0.1404 0.1298 0.2090 -0.0133 -0.0003 0.0005  147 VAL   B CG2 
6330 N  N   . ARG   B 148 ? 0.1290 0.1170 0.2203 -0.0096 -0.0163 -0.0121 148 ARG   B N   
6331 C  CA  . ARG   B 148 ? 0.1342 0.1312 0.2160 -0.0089 -0.0299 -0.0092 148 ARG   B CA  
6332 C  C   . ARG   B 148 ? 0.1407 0.1402 0.2025 -0.0105 -0.0317 -0.0063 148 ARG   B C   
6333 O  O   . ARG   B 148 ? 0.1607 0.1671 0.2085 -0.0254 -0.0372 0.0030  148 ARG   B O   
6334 C  CB  . ARG   B 148 ? 0.1412 0.1395 0.2175 -0.0063 -0.0308 -0.0201 148 ARG   B CB  
6335 C  CG  . ARG   B 148 ? 0.1427 0.1499 0.2329 -0.0103 -0.0290 -0.0313 148 ARG   B CG  
6336 C  CD  . ARG   B 148 ? 0.1472 0.1660 0.2492 0.0036  -0.0280 -0.0322 148 ARG   B CD  
6337 N  NE  . ARG   B 148 ? 0.1498 0.1653 0.2425 0.0196  -0.0303 -0.0306 148 ARG   B NE  
6338 C  CZ  . ARG   B 148 ? 0.1415 0.1584 0.2225 0.0131  -0.0234 -0.0189 148 ARG   B CZ  
6339 N  NH1 . ARG   B 148 ? 0.1381 0.1650 0.2256 -0.0051 -0.0042 -0.0146 148 ARG   B NH1 
6340 N  NH2 . ARG   B 148 ? 0.1638 0.1403 0.2172 0.0155  -0.0160 -0.0153 148 ARG   B NH2 
6354 N  N   . THR   B 149 ? 0.1429 0.1302 0.2042 -0.0100 -0.0290 -0.0024 149 THR   B N   
6355 C  CA  . THR   B 149 ? 0.1487 0.1333 0.2022 -0.0126 -0.0259 0.0064  149 THR   B CA  
6356 C  C   . THR   B 149 ? 0.1492 0.1330 0.1931 -0.0161 -0.0300 0.0029  149 THR   B C   
6357 O  O   . THR   B 149 ? 0.1524 0.1317 0.2087 -0.0215 -0.0160 0.0045  149 THR   B O   
6358 C  CB  . THR   B 149 ? 0.1522 0.1313 0.2034 -0.0168 -0.0293 0.0008  149 THR   B CB  
6359 O  OG1 . THR   B 149 ? 0.1500 0.1352 0.1937 -0.0248 -0.0253 0.0007  149 THR   B OG1 
6360 C  CG2 . THR   B 149 ? 0.1595 0.1349 0.2176 -0.0098 -0.0175 0.0006  149 THR   B CG2 
6368 N  N   . ASN   B 150 ? 0.1574 0.1313 0.1840 -0.0185 -0.0309 -0.0014 150 ASN   B N   
6369 C  CA  . ASN   B 150 ? 0.1639 0.1486 0.1744 -0.0257 -0.0306 -0.0094 150 ASN   B CA  
6370 C  C   . ASN   B 150 ? 0.1540 0.1399 0.1806 -0.0201 -0.0254 -0.0035 150 ASN   B C   
6371 O  O   . ASN   B 150 ? 0.1621 0.1365 0.1968 -0.0267 -0.0403 -0.0040 150 ASN   B O   
6372 C  CB  . ASN   B 150 ? 0.1854 0.1850 0.1868 -0.0297 -0.0377 0.0068  150 ASN   B CB  
6373 C  CG  . ASN   B 150 ? 0.2123 0.2269 0.2264 -0.0225 -0.0410 0.0230  150 ASN   B CG  
6374 O  OD1 . ASN   B 150 ? 0.2148 0.2429 0.2391 -0.0314 -0.0549 0.0132  150 ASN   B OD1 
6375 N  ND2 . ASN   B 150 ? 0.2267 0.2419 0.2578 -0.0116 -0.0459 0.0621  150 ASN   B ND2 
6382 N  N   . VAL   B 151 ? 0.1440 0.1356 0.1818 -0.0215 -0.0258 -0.0018 151 VAL   B N   
6383 C  CA  . VAL   B 151 ? 0.1429 0.1370 0.1899 -0.0241 -0.0207 -0.0041 151 VAL   B CA  
6384 C  C   . VAL   B 151 ? 0.1489 0.1289 0.1850 -0.0346 -0.0253 -0.0048 151 VAL   B C   
6385 O  O   . VAL   B 151 ? 0.1556 0.1383 0.2062 -0.0283 -0.0185 -0.0089 151 VAL   B O   
6386 C  CB  . VAL   B 151 ? 0.1622 0.1516 0.2072 -0.0109 -0.0168 -0.0027 151 VAL   B CB  
6387 C  CG1 . VAL   B 151 ? 0.1706 0.1555 0.2321 -0.0149 -0.0095 -0.0071 151 VAL   B CG1 
6388 C  CG2 . VAL   B 151 ? 0.1724 0.1685 0.1877 0.0044  -0.0197 0.0098  151 VAL   B CG2 
6398 N  N   . TYR   B 152 ? 0.1439 0.1230 0.1721 -0.0244 -0.0201 -0.0067 152 TYR   B N   
6399 C  CA  . TYR   B 152 ? 0.1482 0.1428 0.1637 -0.0307 -0.0102 -0.0119 152 TYR   B CA  
6400 C  C   . TYR   B 152 ? 0.1464 0.1237 0.1634 -0.0235 -0.0088 -0.0121 152 TYR   B C   
6401 O  O   . TYR   B 152 ? 0.1532 0.1226 0.1784 -0.0273 -0.0152 -0.0036 152 TYR   B O   
6402 C  CB  . TYR   B 152 ? 0.1588 0.1549 0.1708 -0.0299 -0.0119 0.0016  152 TYR   B CB  
6403 C  CG  . TYR   B 152 ? 0.1792 0.1639 0.1679 -0.0403 -0.0164 -0.0001 152 TYR   B CG  
6404 C  CD1 . TYR   B 152 ? 0.1890 0.1751 0.1580 -0.0334 -0.0280 0.0073  152 TYR   B CD1 
6405 C  CD2 . TYR   B 152 ? 0.1997 0.1798 0.1759 -0.0376 -0.0141 -0.0056 152 TYR   B CD2 
6406 C  CE1 . TYR   B 152 ? 0.2074 0.1939 0.1695 -0.0299 -0.0318 0.0219  152 TYR   B CE1 
6407 C  CE2 . TYR   B 152 ? 0.2107 0.2028 0.1796 -0.0370 -0.0217 -0.0099 152 TYR   B CE2 
6408 C  CZ  . TYR   B 152 ? 0.2180 0.2137 0.1737 -0.0342 -0.0398 0.0127  152 TYR   B CZ  
6409 O  OH  . TYR   B 152 ? 0.2430 0.2476 0.2056 -0.0239 -0.0432 0.0154  152 TYR   B OH  
6419 N  N   . LEU   B 153 ? 0.1477 0.1224 0.1730 -0.0302 -0.0109 -0.0076 153 LEU   B N   
6420 C  CA  . LEU   B 153 ? 0.1516 0.1180 0.1601 -0.0202 -0.0049 -0.0089 153 LEU   B CA  
6421 C  C   . LEU   B 153 ? 0.1522 0.1135 0.1720 -0.0257 -0.0044 -0.0146 153 LEU   B C   
6422 O  O   . LEU   B 153 ? 0.1657 0.1376 0.1849 -0.0156 -0.0066 -0.0351 153 LEU   B O   
6423 C  CB  . LEU   B 153 ? 0.1497 0.1163 0.1800 -0.0282 -0.0039 -0.0077 153 LEU   B CB  
6424 C  CG  . LEU   B 153 ? 0.1447 0.1271 0.2055 -0.0256 -0.0030 -0.0028 153 LEU   B CG  
6425 C  CD1 . LEU   B 153 ? 0.1548 0.1414 0.2168 -0.0267 0.0001  0.0051  153 LEU   B CD1 
6426 C  CD2 . LEU   B 153 ? 0.1507 0.1400 0.2102 -0.0328 0.0071  0.0016  153 LEU   B CD2 
6438 N  N   . ALA   B 154 ? 0.1419 0.1200 0.1809 -0.0113 -0.0091 -0.0102 154 ALA   B N   
6439 C  CA  . ALA   B 154 ? 0.1510 0.1321 0.2098 -0.0047 -0.0136 -0.0188 154 ALA   B CA  
6440 C  C   . ALA   B 154 ? 0.1639 0.1368 0.2163 -0.0002 -0.0225 -0.0232 154 ALA   B C   
6441 O  O   . ALA   B 154 ? 0.1945 0.1373 0.2272 0.0035  -0.0076 -0.0085 154 ALA   B O   
6442 C  CB  . ALA   B 154 ? 0.1501 0.1442 0.2305 -0.0079 -0.0103 -0.0295 154 ALA   B CB  
6448 N  N   . VAL   B 155 ? 0.1369 0.1273 0.2254 -0.0035 -0.0043 -0.0186 155 VAL   B N   
6449 C  CA  . VAL   B 155 ? 0.1332 0.1246 0.2324 -0.0026 -0.0083 -0.0110 155 VAL   B CA  
6450 C  C   . VAL   B 155 ? 0.1358 0.1224 0.2265 -0.0017 -0.0110 -0.0202 155 VAL   B C   
6451 O  O   . VAL   B 155 ? 0.1533 0.1440 0.2667 0.0030  -0.0106 -0.0370 155 VAL   B O   
6452 C  CB  . VAL   B 155 ? 0.1398 0.1400 0.2614 -0.0047 -0.0154 0.0018  155 VAL   B CB  
6453 C  CG1 . VAL   B 155 ? 0.1493 0.1352 0.2592 -0.0127 -0.0120 0.0028  155 VAL   B CG1 
6454 C  CG2 . VAL   B 155 ? 0.1367 0.1526 0.2791 -0.0064 -0.0093 0.0284  155 VAL   B CG2 
6464 N  N   . PHE   B 156 ? 0.1265 0.1356 0.2467 0.0015  -0.0051 -0.0235 156 PHE   B N   
6465 C  CA  . PHE   B 156 ? 0.1316 0.1424 0.2805 0.0028  -0.0051 -0.0150 156 PHE   B CA  
6466 C  C   . PHE   B 156 ? 0.1286 0.1523 0.3130 0.0103  -0.0043 -0.0346 156 PHE   B C   
6467 O  O   . PHE   B 156 ? 0.1550 0.1712 0.3393 0.0230  0.0065  -0.0396 156 PHE   B O   
6468 C  CB  . PHE   B 156 ? 0.1408 0.1387 0.2804 0.0016  -0.0099 -0.0088 156 PHE   B CB  
6469 C  CG  . PHE   B 156 ? 0.1404 0.1561 0.2845 -0.0031 -0.0113 0.0143  156 PHE   B CG  
6470 C  CD1 . PHE   B 156 ? 0.1432 0.1818 0.3152 0.0016  -0.0059 0.0412  156 PHE   B CD1 
6471 C  CD2 . PHE   B 156 ? 0.1462 0.1673 0.2811 0.0090  -0.0162 0.0176  156 PHE   B CD2 
6472 C  CE1 . PHE   B 156 ? 0.1429 0.1976 0.3266 0.0034  -0.0077 0.0395  156 PHE   B CE1 
6473 C  CE2 . PHE   B 156 ? 0.1538 0.1934 0.3004 0.0111  -0.0152 0.0174  156 PHE   B CE2 
6474 C  CZ  . PHE   B 156 ? 0.1403 0.2000 0.3221 0.0152  -0.0195 0.0278  156 PHE   B CZ  
6484 N  N   . ASP   B 157 ? 0.1338 0.1429 0.3330 0.0099  -0.0186 -0.0221 157 ASP   B N   
6485 C  CA  . ASP   B 157 ? 0.1454 0.1552 0.3539 0.0076  -0.0218 -0.0330 157 ASP   B CA  
6486 C  C   . ASP   B 157 ? 0.1491 0.1494 0.3559 0.0091  -0.0144 -0.0476 157 ASP   B C   
6487 O  O   . ASP   B 157 ? 0.1346 0.1458 0.3466 0.0057  -0.0120 -0.0360 157 ASP   B O   
6488 C  CB  . ASP   B 157 ? 0.1673 0.1739 0.3705 0.0044  -0.0445 -0.0152 157 ASP   B CB  
6489 C  CG  . ASP   B 157 ? 0.2033 0.1874 0.3979 0.0017  -0.0342 -0.0148 157 ASP   B CG  
6490 O  OD1 . ASP   B 157 ? 0.2139 0.1790 0.4130 0.0088  -0.0258 -0.0057 157 ASP   B OD1 
6491 O  OD2 . ASP   B 157 ? 0.2328 0.2091 0.4216 -0.0015 -0.0202 -0.0128 157 ASP   B OD2 
6496 N  N   A LYS   B 158 ? 0.1472 0.1741 0.3662 0.0087  -0.0051 -0.0731 158 LYS   B N   
6497 N  N   B LYS   B 158 ? 0.1629 0.1690 0.3394 0.0083  -0.0109 -0.0574 158 LYS   B N   
6498 C  CA  A LYS   B 158 ? 0.1634 0.1916 0.3712 0.0048  -0.0016 -0.0888 158 LYS   B CA  
6499 C  CA  B LYS   B 158 ? 0.1811 0.1839 0.3334 0.0072  -0.0102 -0.0642 158 LYS   B CA  
6500 C  C   A LYS   B 158 ? 0.1664 0.1773 0.3749 0.0026  -0.0086 -0.0783 158 LYS   B C   
6501 C  C   B LYS   B 158 ? 0.1776 0.1759 0.3433 0.0050  -0.0144 -0.0643 158 LYS   B C   
6502 O  O   A LYS   B 158 ? 0.1673 0.1724 0.3900 -0.0064 -0.0057 -0.0817 158 LYS   B O   
6503 O  O   B LYS   B 158 ? 0.1792 0.1755 0.3347 0.0024  -0.0132 -0.0646 158 LYS   B O   
6504 C  CB  A LYS   B 158 ? 0.1865 0.2336 0.3738 0.0082  0.0082  -0.1055 158 LYS   B CB  
6505 C  CB  B LYS   B 158 ? 0.2042 0.2092 0.3295 0.0094  -0.0051 -0.0673 158 LYS   B CB  
6506 C  CG  A LYS   B 158 ? 0.2209 0.2762 0.3776 0.0074  0.0119  -0.1143 158 LYS   B CG  
6507 C  CG  B LYS   B 158 ? 0.2283 0.2327 0.3357 0.0102  -0.0012 -0.0686 158 LYS   B CG  
6508 C  CD  A LYS   B 158 ? 0.2448 0.3193 0.3847 0.0056  0.0156  -0.1098 158 LYS   B CD  
6509 C  CD  B LYS   B 158 ? 0.2472 0.2559 0.3477 0.0103  0.0020  -0.0647 158 LYS   B CD  
6510 C  CE  A LYS   B 158 ? 0.2636 0.3497 0.3932 0.0058  0.0116  -0.1032 158 LYS   B CE  
6511 C  CE  B LYS   B 158 ? 0.2612 0.2718 0.3597 0.0114  0.0023  -0.0598 158 LYS   B CE  
6512 N  NZ  A LYS   B 158 ? 0.2652 0.3618 0.3913 0.0022  0.0060  -0.1006 158 LYS   B NZ  
6513 N  NZ  B LYS   B 158 ? 0.2661 0.2790 0.3652 0.0113  0.0020  -0.0572 158 LYS   B NZ  
6540 N  N   . ASN   B 159 ? 0.1723 0.1677 0.3784 0.0025  -0.0200 -0.0625 159 ASN   B N   
6541 C  CA  . ASN   B 159 ? 0.1855 0.1562 0.4106 0.0155  -0.0329 -0.0541 159 ASN   B CA  
6542 C  C   . ASN   B 159 ? 0.1660 0.1441 0.4108 0.0113  -0.0453 -0.0435 159 ASN   B C   
6543 O  O   . ASN   B 159 ? 0.1684 0.1400 0.4334 -0.0043 -0.0481 -0.0305 159 ASN   B O   
6544 C  CB  . ASN   B 159 ? 0.2066 0.1684 0.4360 0.0270  -0.0368 -0.0535 159 ASN   B CB  
6545 C  CG  . ASN   B 159 ? 0.2352 0.1935 0.4681 0.0284  -0.0451 -0.0618 159 ASN   B CG  
6546 O  OD1 . ASN   B 159 ? 0.2508 0.2060 0.4733 0.0328  -0.0473 -0.0663 159 ASN   B OD1 
6547 N  ND2 . ASN   B 159 ? 0.2364 0.2002 0.4850 0.0334  -0.0489 -0.0560 159 ASN   B ND2 
6555 N  N   . LEU   B 160 ? 0.1491 0.1415 0.3897 0.0079  -0.0472 -0.0370 160 LEU   B N   
6556 C  CA  . LEU   B 160 ? 0.1498 0.1469 0.3524 0.0091  -0.0380 -0.0224 160 LEU   B CA  
6557 C  C   . LEU   B 160 ? 0.1456 0.1354 0.3468 -0.0015 -0.0243 -0.0294 160 LEU   B C   
6558 O  O   . LEU   B 160 ? 0.1382 0.1375 0.3423 -0.0025 -0.0232 -0.0150 160 LEU   B O   
6559 C  CB  . LEU   B 160 ? 0.1482 0.1559 0.3263 0.0095  -0.0373 -0.0104 160 LEU   B CB  
6560 C  CG  . LEU   B 160 ? 0.1482 0.1700 0.3036 0.0068  -0.0367 -0.0026 160 LEU   B CG  
6561 C  CD1 . LEU   B 160 ? 0.1635 0.1845 0.3048 -0.0056 -0.0130 -0.0082 160 LEU   B CD1 
6562 C  CD2 . LEU   B 160 ? 0.1549 0.1747 0.2979 0.0204  -0.0341 -0.0099 160 LEU   B CD2 
6574 N  N   . TYR   B 161 ? 0.1413 0.1425 0.3515 -0.0092 -0.0025 -0.0393 161 TYR   B N   
6575 C  CA  . TYR   B 161 ? 0.1531 0.1401 0.3388 -0.0154 0.0166  -0.0437 161 TYR   B CA  
6576 C  C   . TYR   B 161 ? 0.1579 0.1417 0.3289 -0.0123 0.0168  -0.0369 161 TYR   B C   
6577 O  O   . TYR   B 161 ? 0.1612 0.1433 0.3255 -0.0199 0.0065  -0.0336 161 TYR   B O   
6578 C  CB  . TYR   B 161 ? 0.1694 0.1545 0.3310 -0.0278 0.0345  -0.0543 161 TYR   B CB  
6579 C  CG  . TYR   B 161 ? 0.1952 0.1627 0.3179 -0.0352 0.0407  -0.0648 161 TYR   B CG  
6580 C  CD1 . TYR   B 161 ? 0.2009 0.1614 0.3153 -0.0515 0.0408  -0.0619 161 TYR   B CD1 
6581 C  CD2 . TYR   B 161 ? 0.2178 0.1728 0.3054 -0.0330 0.0356  -0.0667 161 TYR   B CD2 
6582 C  CE1 . TYR   B 161 ? 0.2219 0.1810 0.3169 -0.0496 0.0415  -0.0611 161 TYR   B CE1 
6583 C  CE2 . TYR   B 161 ? 0.2370 0.1891 0.3092 -0.0391 0.0372  -0.0668 161 TYR   B CE2 
6584 C  CZ  . TYR   B 161 ? 0.2396 0.1920 0.3119 -0.0542 0.0338  -0.0561 161 TYR   B CZ  
6585 O  OH  . TYR   B 161 ? 0.2691 0.2121 0.3292 -0.0557 0.0383  -0.0481 161 TYR   B OH  
6595 N  N   . ASP   B 162 ? 0.1625 0.1379 0.3370 -0.0149 0.0046  -0.0521 162 ASP   B N   
6596 C  CA  . ASP   B 162 ? 0.1728 0.1481 0.3397 -0.0085 -0.0005 -0.0496 162 ASP   B CA  
6597 C  C   . ASP   B 162 ? 0.1703 0.1410 0.3275 -0.0126 -0.0071 -0.0415 162 ASP   B C   
6598 O  O   . ASP   B 162 ? 0.1707 0.1478 0.3406 -0.0196 -0.0225 -0.0320 162 ASP   B O   
6599 C  CB  . ASP   B 162 ? 0.1904 0.1629 0.3619 -0.0058 -0.0101 -0.0713 162 ASP   B CB  
6600 C  CG  . ASP   B 162 ? 0.1958 0.1895 0.3873 0.0055  -0.0097 -0.0850 162 ASP   B CG  
6601 O  OD1 . ASP   B 162 ? 0.1960 0.2092 0.3792 0.0027  0.0081  -0.0804 162 ASP   B OD1 
6602 O  OD2 . ASP   B 162 ? 0.2045 0.2129 0.4192 0.0214  -0.0083 -0.0833 162 ASP   B OD2 
6607 N  N   A LYS   B 163 ? 0.1681 0.1225 0.3216 -0.0124 -0.0257 -0.0290 163 LYS   B N   
6608 N  N   B LYS   B 163 ? 0.1786 0.1527 0.3200 -0.0122 -0.0147 -0.0279 163 LYS   B N   
6609 C  CA  A LYS   B 163 ? 0.1780 0.1323 0.3270 -0.0191 -0.0193 -0.0086 163 LYS   B CA  
6610 C  CA  B LYS   B 163 ? 0.1892 0.1710 0.3197 -0.0133 -0.0150 -0.0137 163 LYS   B CA  
6611 C  C   A LYS   B 163 ? 0.1471 0.1302 0.3174 -0.0208 -0.0212 -0.0060 163 LYS   B C   
6612 C  C   B LYS   B 163 ? 0.1611 0.1505 0.3033 -0.0148 -0.0194 -0.0079 163 LYS   B C   
6613 O  O   A LYS   B 163 ? 0.1387 0.1436 0.3390 -0.0190 -0.0187 -0.0065 163 LYS   B O   
6614 O  O   B LYS   B 163 ? 0.1591 0.1556 0.3046 -0.0142 -0.0191 -0.0055 163 LYS   B O   
6615 C  CB  A LYS   B 163 ? 0.2240 0.1595 0.3566 -0.0176 -0.0178 0.0038  163 LYS   B CB  
6616 C  CB  B LYS   B 163 ? 0.2268 0.2109 0.3456 -0.0122 -0.0142 -0.0074 163 LYS   B CB  
6617 C  CG  A LYS   B 163 ? 0.2918 0.2253 0.3974 -0.0207 -0.0058 0.0080  163 LYS   B CG  
6618 C  CG  B LYS   B 163 ? 0.2653 0.2520 0.3786 -0.0127 -0.0101 -0.0036 163 LYS   B CG  
6619 C  CD  A LYS   B 163 ? 0.3519 0.2788 0.4426 -0.0310 -0.0007 0.0025  163 LYS   B CD  
6620 C  CD  B LYS   B 163 ? 0.3003 0.2896 0.4159 -0.0154 -0.0073 -0.0027 163 LYS   B CD  
6621 C  CE  A LYS   B 163 ? 0.3915 0.3163 0.4712 -0.0376 0.0052  0.0017  163 LYS   B CE  
6622 C  CE  B LYS   B 163 ? 0.3274 0.3202 0.4441 -0.0176 -0.0041 -0.0017 163 LYS   B CE  
6623 N  NZ  A LYS   B 163 ? 0.4166 0.3354 0.4923 -0.0408 0.0077  -0.0028 163 LYS   B NZ  
6624 N  NZ  B LYS   B 163 ? 0.3355 0.3269 0.4624 -0.0186 -0.0028 -0.0025 163 LYS   B NZ  
6651 N  N   . LEU   B 164 ? 0.1375 0.1285 0.2960 -0.0151 -0.0230 -0.0062 164 LEU   B N   
6652 C  CA  . LEU   B 164 ? 0.1392 0.1252 0.2832 -0.0110 -0.0260 0.0015  164 LEU   B CA  
6653 C  C   . LEU   B 164 ? 0.1471 0.1257 0.2900 -0.0144 -0.0291 0.0057  164 LEU   B C   
6654 O  O   . LEU   B 164 ? 0.1462 0.1489 0.3088 -0.0164 -0.0281 0.0020  164 LEU   B O   
6655 C  CB  . LEU   B 164 ? 0.1358 0.1231 0.2672 -0.0087 -0.0211 -0.0008 164 LEU   B CB  
6656 C  CG  . LEU   B 164 ? 0.1460 0.1399 0.2766 -0.0089 -0.0095 0.0021  164 LEU   B CG  
6657 C  CD1 . LEU   B 164 ? 0.1496 0.1374 0.2702 -0.0158 -0.0206 -0.0072 164 LEU   B CD1 
6658 C  CD2 . LEU   B 164 ? 0.1588 0.1776 0.2974 -0.0078 0.0107  -0.0108 164 LEU   B CD2 
6671 N  N   . VAL   B 165 ? 0.1765 0.1345 0.3069 -0.0255 -0.0376 -0.0054 165 VAL   B N   
6672 C  CA  . VAL   B 165 ? 0.2152 0.1518 0.3089 -0.0326 -0.0542 -0.0066 165 VAL   B CA  
6673 C  C   . VAL   B 165 ? 0.2401 0.1572 0.3413 -0.0400 -0.0784 -0.0077 165 VAL   B C   
6674 O  O   . VAL   B 165 ? 0.2609 0.1737 0.3534 -0.0421 -0.0833 -0.0026 165 VAL   B O   
6675 C  CB  . VAL   B 165 ? 0.2385 0.1675 0.3021 -0.0171 -0.0255 -0.0150 165 VAL   B CB  
6676 C  CG1 . VAL   B 165 ? 0.2516 0.1774 0.3152 -0.0202 -0.0131 -0.0084 165 VAL   B CG1 
6677 C  CG2 . VAL   B 165 ? 0.2370 0.1742 0.2954 -0.0143 -0.0148 -0.0150 165 VAL   B CG2 
6687 N  N   . SER   B 166 ? 0.2478 0.1463 0.3771 -0.0377 -0.0859 -0.0275 166 SER   B N   
6688 C  CA  . SER   B 166 ? 0.2408 0.1460 0.4218 -0.0377 -0.0753 -0.0340 166 SER   B CA  
6689 C  C   . SER   B 166 ? 0.2255 0.1580 0.4331 -0.0392 -0.0749 -0.0082 166 SER   B C   
6690 O  O   . SER   B 166 ? 0.2308 0.1809 0.4583 -0.0522 -0.0866 -0.0279 166 SER   B O   
6691 C  CB  . SER   B 166 ? 0.2406 0.1572 0.4476 -0.0272 -0.0662 -0.0450 166 SER   B CB  
6692 O  OG  . SER   B 166 ? 0.2273 0.1581 0.4671 -0.0196 -0.0665 -0.0278 166 SER   B OG  
6698 N  N   . SER   B 167 ? 0.2039 0.1479 0.4038 -0.0412 -0.0761 0.0285  167 SER   B N   
6699 C  CA  . SER   B 167 ? 0.1957 0.1573 0.3852 -0.0375 -0.0527 0.0257  167 SER   B CA  
6700 C  C   . SER   B 167 ? 0.1924 0.1655 0.3650 -0.0481 -0.0433 0.0422  167 SER   B C   
6701 O  O   . SER   B 167 ? 0.1927 0.1813 0.3703 -0.0491 -0.0437 0.0399  167 SER   B O   
6702 C  CB  . SER   B 167 ? 0.1878 0.1668 0.3910 -0.0328 -0.0265 0.0241  167 SER   B CB  
6703 O  OG  . SER   B 167 ? 0.1803 0.1757 0.3887 -0.0182 -0.0106 0.0232  167 SER   B OG  
6709 N  N   . PHE   B 168 ? 0.1952 0.1654 0.3498 -0.0447 -0.0270 0.0494  168 PHE   B N   
6710 C  CA  . PHE   B 168 ? 0.2007 0.1633 0.3204 -0.0448 -0.0283 0.0316  168 PHE   B CA  
6711 C  C   . PHE   B 168 ? 0.1703 0.1525 0.2784 -0.0264 -0.0111 0.0158  168 PHE   B C   
6712 O  O   . PHE   B 168 ? 0.1992 0.1473 0.2890 0.0019  -0.0130 0.0022  168 PHE   B O   
6713 C  CB  . PHE   B 168 ? 0.2206 0.1672 0.3212 -0.0532 -0.0440 0.0437  168 PHE   B CB  
6714 C  CG  . PHE   B 168 ? 0.2465 0.1533 0.3063 -0.0562 -0.0484 0.0188  168 PHE   B CG  
6715 C  CD1 . PHE   B 168 ? 0.2726 0.1610 0.3127 -0.0493 -0.0511 0.0160  168 PHE   B CD1 
6716 C  CD2 . PHE   B 168 ? 0.2398 0.1489 0.3009 -0.0494 -0.0456 0.0228  168 PHE   B CD2 
6717 C  CE1 . PHE   B 168 ? 0.2824 0.1725 0.3063 -0.0367 -0.0453 0.0194  168 PHE   B CE1 
6718 C  CE2 . PHE   B 168 ? 0.2629 0.1596 0.3006 -0.0372 -0.0536 0.0148  168 PHE   B CE2 
6719 C  CZ  . PHE   B 168 ? 0.2734 0.1597 0.3026 -0.0281 -0.0558 0.0255  168 PHE   B CZ  
6729 N  N   . LEU   B 169 ? 0.1747 0.1666 0.2744 0.0008  0.0023  -0.0005 169 LEU   B N   
6730 C  CA  . LEU   B 169 ? 0.1932 0.2008 0.3010 -0.0041 0.0066  -0.0279 169 LEU   B CA  
6731 C  C   . LEU   B 169 ? 0.2208 0.2237 0.3513 0.0055  0.0009  -0.0576 169 LEU   B C   
6732 O  O   . LEU   B 169 ? 0.2428 0.2440 0.4032 0.0038  0.0011  -0.0757 169 LEU   B O   
6733 C  CB  . LEU   B 169 ? 0.2103 0.2425 0.3027 -0.0115 0.0060  -0.0054 169 LEU   B CB  
6734 C  CG  . LEU   B 169 ? 0.2508 0.2807 0.3305 -0.0019 0.0076  -0.0021 169 LEU   B CG  
6735 C  CD1 . LEU   B 169 ? 0.2642 0.2979 0.3328 -0.0019 0.0068  0.0118  169 LEU   B CD1 
6736 C  CD2 . LEU   B 169 ? 0.2466 0.2876 0.3320 0.0133  0.0239  -0.0195 169 LEU   B CD2 
6737 O  OXT . LEU   B 169 ? 0.2392 0.2385 0.3540 0.0260  0.0052  -0.0593 169 LEU   B OXT 
6749 C  C1  T TFA   C .   ? 0.0944 0.1522 0.1175 -0.0031 0.0198  0.0276  201 TFA   A C1  
6750 C  C2  T TFA   C .   ? 0.1245 0.1742 0.1425 -0.0133 0.0100  0.0170  201 TFA   A C2  
6751 O  O   T TFA   C .   ? 0.0711 0.1248 0.1166 -0.0083 0.0265  0.0330  201 TFA   A O   
6752 F  F1  T TFA   C .   ? 0.1354 0.1844 0.1546 -0.0065 0.0062  0.0134  201 TFA   A F1  
6753 F  F2  T TFA   C .   ? 0.1346 0.1774 0.1435 -0.0119 0.0047  0.0237  201 TFA   A F2  
6754 F  F3  T TFA   C .   ? 0.1308 0.1781 0.1563 -0.0284 0.0162  0.0058  201 TFA   A F3  
6755 O  OXT T TFA   C .   ? 0.0935 0.1588 0.1230 0.0118  0.0245  0.0245  201 TFA   A OXT 
6756 N  N2  B A1A8W D .   ? 0.1421 0.1676 0.1985 -0.0060 -0.0178 0.0137  202 A1A8W A N2  
6757 C  C3  B A1A8W D .   ? 0.1442 0.1721 0.1919 -0.0020 -0.0140 0.0167  202 A1A8W A C3  
6758 C  C6  B A1A8W D .   ? 0.1358 0.1581 0.1839 -0.0016 -0.0178 0.0323  202 A1A8W A C6  
6759 C  C9  B A1A8W D .   ? 0.1557 0.2122 0.2474 -0.0008 0.0080  0.0054  202 A1A8W A C9  
6760 C  C12 B A1A8W D .   ? 0.1631 0.2198 0.2606 -0.0024 0.0048  0.0014  202 A1A8W A C12 
6761 C  C1  B A1A8W D .   ? 0.1327 0.1926 0.2105 0.0065  0.0097  0.0053  202 A1A8W A C1  
6762 C  C10 B A1A8W D .   ? 0.1642 0.2215 0.2572 0.0000  0.0096  0.0051  202 A1A8W A C10 
6763 C  C11 B A1A8W D .   ? 0.1674 0.2236 0.2600 -0.0007 0.0118  0.0042  202 A1A8W A C11 
6764 C  C2  B A1A8W D .   ? 0.1410 0.1943 0.2184 -0.0007 0.0071  0.0072  202 A1A8W A C2  
6765 C  C4  B A1A8W D .   ? 0.1424 0.1611 0.1971 -0.0074 -0.0184 0.0204  202 A1A8W A C4  
6766 C  C5  B A1A8W D .   ? 0.1296 0.1479 0.1814 -0.0048 -0.0167 0.0370  202 A1A8W A C5  
6767 C  C7  B A1A8W D .   ? 0.1274 0.1557 0.1839 0.0058  -0.0145 0.0362  202 A1A8W A C7  
6768 C  C8  B A1A8W D .   ? 0.1128 0.1498 0.1835 0.0024  -0.0176 0.0392  202 A1A8W A C8  
6769 N  N1  B A1A8W D .   ? 0.1455 0.1860 0.2057 -0.0041 -0.0051 0.0012  202 A1A8W A N1  
6770 N  N3  B A1A8W D .   ? 0.1393 0.1532 0.1902 -0.0074 -0.0178 0.0324  202 A1A8W A N3  
6771 N  N4  B A1A8W D .   ? 0.1134 0.1395 0.1761 0.0053  -0.0188 0.0403  202 A1A8W A N4  
6772 O  O1  B A1A8W D .   ? 0.1218 0.1885 0.2022 0.0118  0.0170  0.0055  202 A1A8W A O1  
6789 CL CL  B CL    E .   ? 0.1400 0.1151 0.2147 -0.0171 -0.0130 0.0021  203 CL    A CL  
6790 O  O   . HOH   F .   ? 0.1420 0.4539 0.2658 -0.0170 0.0209  0.0633  301 HOH   A O   
6791 O  O   . HOH   F .   ? 0.4147 0.7736 0.4813 -0.1079 0.0579  0.0850  302 HOH   A O   
6792 O  O   B HOH   F .   ? 0.3990 0.4167 0.3332 0.1026  0.0121  0.0083  303 HOH   A O   
6793 O  O   . HOH   F .   ? 0.7028 0.6070 0.4247 -0.1476 -0.0495 0.2265  304 HOH   A O   
6794 O  O   . HOH   F .   ? 0.6748 0.5345 0.5221 -0.1182 0.0306  0.2143  305 HOH   A O   
6795 O  O   . HOH   F .   ? 0.5855 0.4391 0.3207 0.1565  -0.1380 0.0400  306 HOH   A O   
6796 O  O   A HOH   F .   ? 0.2593 0.2241 0.3580 -0.0247 -0.0364 0.0551  307 HOH   A O   
6797 O  O   . HOH   F .   ? 0.2954 0.5940 0.5544 -0.0399 -0.0763 0.1894  308 HOH   A O   
6798 O  O   . HOH   F .   ? 0.2633 0.6096 0.3902 -0.0108 -0.0643 0.1017  309 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2849 0.2639 0.4471 -0.0440 -0.1267 0.1201  310 HOH   A O   
6800 O  O   . HOH   F .   ? 0.4429 0.3573 0.4867 -0.0519 0.1160  -0.0480 311 HOH   A O   
6801 O  O   . HOH   F .   ? 0.3036 0.3260 0.1816 -0.0439 0.0514  0.0551  312 HOH   A O   
6802 O  O   . HOH   F .   ? 0.5714 0.3622 0.5212 -0.0668 0.1663  0.0909  313 HOH   A O   
6803 O  O   B HOH   F .   ? 0.3208 0.3614 0.2870 0.0584  0.0661  0.0367  314 HOH   A O   
6804 O  O   . HOH   F .   ? 0.4077 0.4258 0.3375 0.1593  -0.0688 -0.1441 315 HOH   A O   
6805 O  O   . HOH   F .   ? 0.4858 0.2742 0.2717 -0.1178 0.0237  0.0360  316 HOH   A O   
6806 O  O   . HOH   F .   ? 0.5405 0.4934 0.4908 -0.0616 0.1309  0.2013  317 HOH   A O   
6807 O  O   B HOH   F .   ? 0.2069 0.2608 0.1742 0.1235  0.0435  0.0831  318 HOH   A O   
6808 O  O   . HOH   F .   ? 0.3628 0.3252 0.2748 -0.1421 0.0055  0.0740  319 HOH   A O   
6809 O  O   . HOH   F .   ? 0.5569 0.6268 0.4629 -0.1258 -0.1086 -0.1009 320 HOH   A O   
6810 O  O   . HOH   F .   ? 0.1622 0.3448 0.3127 0.0409  -0.0206 -0.0094 321 HOH   A O   
6811 O  O   . HOH   F .   ? 0.1982 0.1862 0.3528 -0.0493 0.0159  -0.0279 322 HOH   A O   
6812 O  O   . HOH   F .   ? 0.4460 0.4066 0.5388 0.1193  0.1230  -0.1383 323 HOH   A O   
6813 O  O   . HOH   F .   ? 0.5293 0.3500 0.3215 -0.1029 -0.0851 0.0135  324 HOH   A O   
6814 O  O   B HOH   F .   ? 0.2291 0.2113 0.1739 0.0251  0.0096  -0.0066 325 HOH   A O   
6815 O  O   . HOH   F .   ? 0.6675 0.5587 0.3543 -0.0309 -0.0291 0.1391  326 HOH   A O   
6816 O  O   . HOH   F .   ? 0.5390 0.2005 0.4780 0.0759  -0.0159 -0.0080 327 HOH   A O   
6817 O  O   . HOH   F .   ? 0.1497 0.1437 0.2342 -0.0196 0.0020  0.0108  328 HOH   A O   
6818 O  O   . HOH   F .   ? 0.3176 0.4473 0.2496 -0.0196 0.0557  0.0230  329 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3956 0.3675 0.3785 -0.0734 0.1771  0.0348  330 HOH   A O   
6820 O  O   . HOH   F .   ? 0.1598 0.1697 0.2220 0.0170  -0.0278 0.0260  331 HOH   A O   
6821 O  O   . HOH   F .   ? 0.1957 0.1568 0.1657 -0.0099 0.0130  0.0221  332 HOH   A O   
6822 O  O   . HOH   F .   ? 0.2283 0.2185 0.2909 0.0385  0.0339  0.0472  333 HOH   A O   
6823 O  O   . HOH   F .   ? 0.2075 0.4248 0.4691 -0.0322 -0.0771 0.2139  334 HOH   A O   
6824 O  O   A HOH   F .   ? 0.1438 0.1796 0.2065 0.0351  0.0338  0.0463  335 HOH   A O   
6825 O  O   . HOH   F .   ? 0.4577 0.3985 0.4482 -0.1892 -0.0857 0.1956  336 HOH   A O   
6826 O  O   A HOH   F .   ? 0.2119 0.2434 0.2354 -0.0308 0.0504  0.0573  337 HOH   A O   
6827 O  O   . HOH   F .   ? 0.5277 0.5252 0.4098 0.0437  -0.0677 -0.1119 338 HOH   A O   
6828 O  O   . HOH   F .   ? 0.1901 0.3434 0.4077 -0.0321 0.0388  -0.1016 339 HOH   A O   
6829 O  O   . HOH   F .   ? 0.1427 0.1725 0.2580 0.0044  -0.0278 -0.0419 340 HOH   A O   
6830 O  O   . HOH   F .   ? 0.4519 0.5294 0.6645 0.1733  0.1231  -0.0461 341 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2630 0.3637 0.3664 -0.0873 -0.0511 -0.0288 342 HOH   A O   
6832 O  O   A HOH   F .   ? 0.6447 0.2894 0.4878 -0.0737 -0.1173 0.0427  343 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2255 0.3976 0.3536 0.0821  -0.0595 -0.0234 344 HOH   A O   
6834 O  O   . HOH   F .   ? 0.5909 0.5291 0.4678 0.0429  0.2173  -0.0696 345 HOH   A O   
6835 O  O   . HOH   F .   ? 0.3768 0.4787 0.5758 0.0709  -0.0435 0.1485  346 HOH   A O   
6836 O  O   . HOH   F .   ? 0.2451 0.4177 0.5113 -0.0102 0.0880  0.2211  347 HOH   A O   
6837 O  O   . HOH   F .   ? 0.4885 0.5343 0.2848 -0.1064 0.1400  0.0840  348 HOH   A O   
6838 O  O   . HOH   F .   ? 0.5110 0.1850 0.4910 0.0148  -0.1458 0.0702  349 HOH   A O   
6839 O  O   . HOH   F .   ? 0.3460 0.2865 0.3313 -0.0933 -0.0044 -0.0151 350 HOH   A O   
6840 O  O   A HOH   F .   ? 0.1928 0.3101 0.2112 0.0316  0.0234  0.0265  351 HOH   A O   
6841 O  O   . HOH   F .   ? 0.2002 0.1665 0.2371 0.0230  -0.0373 0.0036  352 HOH   A O   
6842 O  O   . HOH   F .   ? 0.5964 0.4025 0.3214 -0.0162 0.0313  0.1670  353 HOH   A O   
6843 O  O   . HOH   F .   ? 0.1357 0.2165 0.2191 0.0016  -0.0121 0.0567  354 HOH   A O   
6844 O  O   . HOH   F .   ? 0.2402 0.2047 0.2371 -0.0366 0.0100  -0.0084 355 HOH   A O   
6845 O  O   A HOH   F .   ? 0.1958 0.1425 0.2443 -0.0113 -0.0554 -0.0047 356 HOH   A O   
6846 O  O   . HOH   F .   ? 0.1917 0.2032 0.3893 0.0178  0.0988  -0.0056 357 HOH   A O   
6847 O  O   . HOH   F .   ? 0.3645 0.4166 0.3505 0.1722  0.0639  0.0441  358 HOH   A O   
6848 O  O   . HOH   F .   ? 0.2466 0.4117 0.3281 -0.0450 0.0575  -0.0098 359 HOH   A O   
6849 O  O   . HOH   F .   ? 0.1429 0.1860 0.2599 0.0090  -0.0069 0.0069  360 HOH   A O   
6850 O  O   . HOH   F .   ? 0.2734 0.5809 0.5906 0.0977  0.0751  0.0859  361 HOH   A O   
6851 O  O   . HOH   F .   ? 0.2973 0.3247 0.4745 -0.0695 -0.1004 -0.0779 362 HOH   A O   
6852 O  O   . HOH   F .   ? 0.1378 0.1467 0.1618 -0.0089 -0.0145 0.0019  363 HOH   A O   
6853 O  O   . HOH   F .   ? 0.1247 0.1240 0.1481 -0.0053 0.0091  0.0092  364 HOH   A O   
6854 O  O   A HOH   F .   ? 0.3530 0.1552 0.1968 0.0131  -0.0155 0.0030  365 HOH   A O   
6855 O  O   . HOH   F .   ? 0.3188 0.3499 0.2318 -0.1010 -0.0211 -0.0690 366 HOH   A O   
6856 O  O   . HOH   F .   ? 0.1867 0.1872 0.2489 -0.0382 0.0075  0.0329  367 HOH   A O   
6857 O  O   . HOH   F .   ? 0.1483 0.1277 0.2382 -0.0107 0.0214  -0.0032 368 HOH   A O   
6858 O  O   . HOH   F .   ? 0.1685 0.2151 0.1944 -0.0186 0.0006  0.0562  369 HOH   A O   
6859 O  O   . HOH   F .   ? 0.2661 0.4207 0.3004 0.0668  0.0746  0.1720  370 HOH   A O   
6860 O  O   . HOH   F .   ? 0.3836 0.2062 0.2625 0.1163  0.0603  0.0291  371 HOH   A O   
6861 O  O   . HOH   F .   ? 0.4857 0.2549 0.4224 -0.1525 0.1855  -0.0637 372 HOH   A O   
6862 O  O   . HOH   F .   ? 0.3744 0.2262 0.4505 -0.1071 0.0858  0.0400  373 HOH   A O   
6863 O  O   . HOH   F .   ? 0.1963 0.2336 0.2293 -0.0366 -0.0521 0.0493  374 HOH   A O   
6864 O  O   . HOH   F .   ? 0.6110 0.4582 0.6562 0.0101  -0.0578 -0.0180 375 HOH   A O   
6865 O  O   . HOH   F .   ? 0.5922 0.5456 0.3853 0.1993  -0.0204 -0.0068 376 HOH   A O   
6866 O  O   A HOH   F .   ? 0.3891 0.2107 0.2704 0.0957  0.0777  0.0592  377 HOH   A O   
6867 O  O   . HOH   F .   ? 0.1536 0.1558 0.1984 -0.0003 -0.0269 0.0069  378 HOH   A O   
6868 O  O   . HOH   F .   ? 0.2263 0.4104 0.3361 -0.0589 -0.0106 0.0890  379 HOH   A O   
6869 O  O   . HOH   F .   ? 0.3093 0.2268 0.5178 -0.0622 -0.0243 -0.0005 380 HOH   A O   
6870 O  O   . HOH   F .   ? 0.1922 0.2604 0.3588 0.0274  0.0868  -0.0607 381 HOH   A O   
6871 O  O   . HOH   F .   ? 0.3352 0.6410 0.3745 -0.0937 0.0046  0.1477  382 HOH   A O   
6872 O  O   . HOH   F .   ? 0.2579 0.2025 0.1824 -0.0698 0.0062  0.0385  383 HOH   A O   
6873 O  O   . HOH   F .   ? 0.1666 0.1643 0.2344 -0.0201 0.0107  0.0379  384 HOH   A O   
6874 O  O   . HOH   F .   ? 0.3677 0.6694 0.4896 -0.0602 -0.1442 0.0860  385 HOH   A O   
6875 O  O   . HOH   F .   ? 0.1836 0.1756 0.1766 0.0000  0.0086  0.0164  386 HOH   A O   
6876 O  O   . HOH   F .   ? 0.2950 0.6798 0.3727 0.1439  0.0528  -0.0706 387 HOH   A O   
6877 O  O   T HOH   F .   ? 0.0861 0.1122 0.1631 -0.0275 0.0103  0.0435  388 HOH   A O   
6878 O  O   . HOH   F .   ? 0.3628 0.3246 0.2427 -0.0658 -0.0393 0.0177  389 HOH   A O   
6879 O  O   . HOH   F .   ? 0.3005 0.2994 0.2102 0.0230  0.0660  -0.0101 390 HOH   A O   
6880 O  O   . HOH   F .   ? 0.3292 0.2469 0.3229 -0.0231 -0.0451 0.0826  391 HOH   A O   
6881 O  O   . HOH   F .   ? 0.1416 0.1593 0.1856 0.0127  -0.0273 -0.0254 392 HOH   A O   
6882 O  O   . HOH   F .   ? 0.2089 0.2131 0.3391 0.0074  -0.0630 0.0309  393 HOH   A O   
6883 O  O   . HOH   F .   ? 0.1702 0.1833 0.4017 0.0319  0.0963  0.1048  394 HOH   A O   
6884 O  O   . HOH   F .   ? 0.2380 0.1689 0.2639 -0.0061 0.0126  0.0296  395 HOH   A O   
6885 O  O   . HOH   F .   ? 0.2552 0.3924 0.3432 -0.0351 0.0975  -0.0764 396 HOH   A O   
6886 O  O   . HOH   F .   ? 0.5446 0.5353 0.6378 -0.0897 0.0181  0.1509  397 HOH   A O   
6887 O  O   . HOH   F .   ? 0.3079 0.2741 0.2289 -0.0857 -0.0930 0.0414  398 HOH   A O   
6888 O  O   . HOH   F .   ? 0.1951 0.2165 0.2727 -0.0181 -0.0234 0.0874  399 HOH   A O   
6889 O  O   . HOH   F .   ? 0.3023 0.3559 0.3456 -0.1357 0.0731  -0.0150 400 HOH   A O   
6890 O  O   . HOH   F .   ? 0.2492 0.2790 0.3229 -0.0076 -0.0100 -0.0636 401 HOH   A O   
6891 O  O   . HOH   F .   ? 0.2179 0.1663 0.3047 0.0043  -0.0375 0.0064  402 HOH   A O   
6892 O  O   . HOH   F .   ? 0.1306 0.1376 0.1862 0.0001  -0.0165 0.0086  403 HOH   A O   
6893 O  O   . HOH   F .   ? 0.2638 0.3599 0.3428 -0.0406 0.0737  -0.0578 404 HOH   A O   
6894 O  O   A HOH   F .   ? 0.2120 0.2085 0.2588 0.0046  -0.0049 0.0638  405 HOH   A O   
6895 O  O   . HOH   F .   ? 0.2850 0.3737 0.4397 -0.0370 0.1355  -0.0020 406 HOH   A O   
6896 O  O   . HOH   F .   ? 0.1868 0.2493 0.3863 -0.0157 -0.0284 0.0127  407 HOH   A O   
6897 O  O   . HOH   F .   ? 0.5961 0.2718 0.5026 0.0973  -0.0153 -0.0032 408 HOH   A O   
6898 O  O   . HOH   F .   ? 0.4816 0.5343 0.2076 -0.0037 0.0864  0.1123  409 HOH   A O   
6899 O  O   A HOH   F .   ? 0.2007 0.1855 0.3081 -0.0199 0.0308  -0.0025 410 HOH   A O   
6900 O  O   . HOH   F .   ? 0.3329 0.3984 0.2200 -0.0571 -0.0888 0.0386  411 HOH   A O   
6901 O  O   . HOH   F .   ? 0.1647 0.1328 0.1702 -0.0231 0.0130  0.0011  412 HOH   A O   
6902 O  O   . HOH   F .   ? 0.2472 0.2068 0.2549 -0.0530 0.0046  0.0528  413 HOH   A O   
6903 O  O   . HOH   F .   ? 0.5692 0.5545 0.5216 0.0233  0.0822  0.0026  414 HOH   A O   
6904 O  O   . HOH   F .   ? 0.1439 0.1557 0.3121 -0.0057 -0.0010 0.0183  415 HOH   A O   
6905 O  O   . HOH   F .   ? 0.2036 0.2915 0.2652 -0.0233 -0.0520 0.0615  416 HOH   A O   
6906 O  O   . HOH   F .   ? 0.3191 0.1282 0.2220 0.0049  -0.0597 0.0115  417 HOH   A O   
6907 O  O   A HOH   F .   ? 0.1921 0.2163 0.3529 0.0149  -0.0412 -0.0646 418 HOH   A O   
6908 O  O   . HOH   F .   ? 0.2921 0.3625 0.7001 -0.0193 0.0869  -0.0577 419 HOH   A O   
6909 O  O   . HOH   F .   ? 0.2643 0.6285 0.1798 -0.0386 0.0463  0.0091  420 HOH   A O   
6910 O  O   . HOH   F .   ? 0.4463 0.6720 0.5493 0.1983  0.1060  0.0825  421 HOH   A O   
6911 O  O   . HOH   F .   ? 0.4149 0.2240 0.5324 -0.0895 -0.2266 0.1069  422 HOH   A O   
6912 O  O   . HOH   F .   ? 0.2242 0.4159 0.2787 0.1541  -0.0013 0.0301  423 HOH   A O   
6913 O  O   . HOH   F .   ? 0.6501 0.4101 0.5003 0.1834  -0.0896 0.1403  424 HOH   A O   
6914 O  O   B HOH   F .   ? 0.1320 0.1012 0.2274 -0.0130 0.0080  -0.0097 425 HOH   A O   
6915 O  O   A HOH   F .   ? 0.1461 0.2496 0.3027 -0.0285 0.0662  0.0446  426 HOH   A O   
6916 O  O   . HOH   F .   ? 0.1531 0.2022 0.2726 -0.0179 0.0031  0.0446  427 HOH   A O   
6917 O  O   . HOH   F .   ? 0.6144 0.7013 0.7043 -0.1141 -0.0834 -0.0687 428 HOH   A O   
6918 O  O   . HOH   F .   ? 0.4670 0.6319 0.3196 -0.0842 0.0008  0.1659  429 HOH   A O   
6919 O  O   . HOH   F .   ? 0.3592 0.3549 0.4320 0.0879  0.0470  -0.0119 430 HOH   A O   
6920 O  O   . HOH   F .   ? 0.6526 0.6743 0.6070 -0.1041 0.0298  0.0379  431 HOH   A O   
6921 O  O   . HOH   F .   ? 0.1959 0.1909 0.2893 0.0218  -0.0600 0.0265  432 HOH   A O   
6922 O  O   . HOH   F .   ? 0.8770 0.9460 0.7505 -0.0311 0.0030  0.0035  433 HOH   A O   
6923 O  O   . HOH   F .   ? 0.1652 0.1456 0.1740 -0.0056 -0.0219 -0.0039 434 HOH   A O   
6924 O  O   . HOH   F .   ? 0.5812 0.6601 0.4242 0.0260  0.2531  -0.0793 435 HOH   A O   
6925 O  O   . HOH   F .   ? 0.3492 0.2769 0.1837 -0.0919 0.0178  0.0658  436 HOH   A O   
6926 O  O   . HOH   F .   ? 0.1821 0.2078 0.5143 -0.0308 -0.0901 0.0624  437 HOH   A O   
6927 O  O   . HOH   F .   ? 0.6021 0.5846 0.6248 -0.1481 -0.0007 -0.1259 438 HOH   A O   
6928 O  O   . HOH   F .   ? 0.6408 0.4237 0.5219 0.0519  0.0690  0.1967  439 HOH   A O   
6929 O  O   . HOH   F .   ? 0.5213 0.4864 0.3766 -0.0385 -0.1528 0.0422  440 HOH   A O   
6930 O  O   . HOH   F .   ? 0.6990 0.6559 0.6200 0.0891  -0.1045 0.0093  441 HOH   A O   
6931 O  O   A HOH   F .   ? 0.1908 0.1560 0.2114 -0.0239 -0.0143 0.0125  442 HOH   A O   
6932 O  O   . HOH   F .   ? 0.2529 0.1605 0.2910 0.0077  0.0063  0.0115  443 HOH   A O   
6933 O  O   . HOH   F .   ? 0.4087 0.3611 0.3218 0.2266  -0.0529 -0.0321 444 HOH   A O   
6934 O  O   . HOH   F .   ? 0.6333 0.7341 0.4369 0.1628  -0.0953 0.2168  445 HOH   A O   
6935 O  O   B HOH   F .   ? 0.2431 0.2888 0.3052 0.0727  0.0050  -0.0494 446 HOH   A O   
6936 O  O   . HOH   F .   ? 0.5576 0.5045 0.6403 0.0689  0.0102  -0.1351 447 HOH   A O   
6937 O  O   A HOH   F .   ? 0.4663 0.3908 0.3558 0.1290  0.1068  0.1952  448 HOH   A O   
6938 O  O   . HOH   F .   ? 0.4509 0.4700 0.4605 -0.1049 -0.0916 -0.1294 449 HOH   A O   
6939 O  O   . HOH   F .   ? 0.2154 0.1995 0.2964 0.0076  0.0242  0.0131  450 HOH   A O   
6940 O  O   . HOH   F .   ? 0.2055 0.2663 0.2620 0.0001  -0.0190 -0.0490 451 HOH   A O   
6941 O  O   . HOH   F .   ? 0.6563 0.5426 0.7409 0.0547  -0.1093 0.1957  452 HOH   A O   
6942 O  O   A HOH   F .   ? 0.2692 0.3201 0.5060 -0.0141 0.1049  -0.1386 453 HOH   A O   
6943 O  O   . HOH   F .   ? 0.4142 0.5110 0.4127 0.0786  -0.0119 0.1054  454 HOH   A O   
6944 O  O   . HOH   F .   ? 0.5343 0.3775 0.4141 0.0155  0.0431  0.0442  455 HOH   A O   
6945 O  O   . HOH   F .   ? 0.3025 0.3771 0.3654 0.1379  -0.0215 0.0781  456 HOH   A O   
6946 O  O   . HOH   F .   ? 0.3977 0.3642 0.4516 0.0131  0.1035  0.0684  457 HOH   A O   
6947 O  O   . HOH   F .   ? 0.6465 0.5803 0.4942 -0.0577 0.1138  0.1061  458 HOH   A O   
6948 O  O   . HOH   F .   ? 0.7289 0.7659 0.4959 0.0279  -0.1148 -0.0303 459 HOH   A O   
6949 O  O   . HOH   F .   ? 0.2558 0.2744 0.3802 -0.0532 0.0362  -0.0864 460 HOH   A O   
6950 O  O   . HOH   F .   ? 0.3286 0.4901 0.5495 -0.1451 0.1189  -0.1530 461 HOH   A O   
6951 O  O   . HOH   F .   ? 0.3776 0.4619 0.4846 0.0497  -0.0474 0.1314  462 HOH   A O   
6952 O  O   . HOH   F .   ? 0.3221 0.4645 0.3771 -0.0776 -0.0322 -0.0078 463 HOH   A O   
6953 O  O   . HOH   F .   ? 0.2656 0.2748 0.3316 -0.0899 0.0507  -0.0264 464 HOH   A O   
6954 O  O   . HOH   F .   ? 0.2611 0.1784 0.2546 0.0310  -0.0860 -0.0309 465 HOH   A O   
6955 O  O   . HOH   F .   ? 0.2652 0.4310 0.4684 0.0680  -0.0075 -0.1551 466 HOH   A O   
6956 O  O   . HOH   F .   ? 0.6841 0.3432 0.7139 0.0573  0.0057  0.2354  467 HOH   A O   
6957 O  O   A HOH   F .   ? 0.2863 0.2432 0.5625 0.0705  -0.1912 -0.0667 468 HOH   A O   
6958 O  O   . HOH   F .   ? 0.3780 0.6167 0.3785 -0.0746 -0.0545 0.2142  469 HOH   A O   
6959 O  O   . HOH   F .   ? 0.5613 0.4593 0.4439 0.0160  0.0904  0.0357  470 HOH   A O   
6960 O  O   . HOH   F .   ? 0.3231 0.2354 0.3510 0.0112  0.0752  -0.0128 471 HOH   A O   
6961 O  O   . HOH   F .   ? 0.3834 0.5145 0.3718 0.0340  -0.0512 -0.0645 472 HOH   A O   
6962 O  O   . HOH   F .   ? 0.4408 0.4509 0.3266 -0.0455 -0.0340 -0.0279 473 HOH   A O   
6963 O  O   . HOH   F .   ? 0.7053 0.6469 0.6497 0.0935  0.1858  0.2506  474 HOH   A O   
6964 O  O   . HOH   F .   ? 0.5187 0.5548 0.4623 0.1335  -0.0456 -0.0921 475 HOH   A O   
6965 O  O   B HOH   F .   ? 0.2462 0.1963 0.2847 0.0401  0.0634  -0.0414 476 HOH   A O   
6966 O  O   . HOH   F .   ? 0.4126 0.4295 0.2721 -0.0084 -0.0138 -0.0113 477 HOH   A O   
6967 O  O   . HOH   F .   ? 0.5337 0.5348 0.5981 -0.1762 -0.1361 0.0372  478 HOH   A O   
6968 O  O   . HOH   F .   ? 0.4271 0.4145 0.5214 -0.2014 -0.0301 -0.0305 479 HOH   A O   
6969 O  O   . HOH   F .   ? 0.2867 0.4746 0.3304 -0.0326 -0.0199 -0.0852 480 HOH   A O   
6970 O  O   . HOH   F .   ? 0.7136 0.5608 0.6260 -0.0964 0.0585  -0.0959 481 HOH   A O   
6971 O  O   . HOH   F .   ? 0.2438 0.2158 0.2597 0.0257  -0.0005 0.0036  482 HOH   A O   
6972 O  O   B HOH   F .   ? 0.2140 0.1785 0.2636 0.0550  -0.0177 0.0723  483 HOH   A O   
6973 O  O   . HOH   F .   ? 0.4843 0.2740 0.3314 -0.0569 -0.1180 0.0672  484 HOH   A O   
6974 O  O   . HOH   F .   ? 0.5576 0.3961 0.3885 0.0250  0.0066  -0.1203 485 HOH   A O   
6975 O  O   B HOH   F .   ? 0.2776 0.1635 0.2171 0.0314  0.0037  -0.0083 486 HOH   A O   
6976 O  O   . HOH   F .   ? 0.7596 0.3792 0.3295 -0.0452 -0.1251 0.0274  487 HOH   A O   
6977 O  O   . HOH   F .   ? 0.2963 0.4161 0.4769 0.0056  0.1187  0.1275  488 HOH   A O   
6978 O  O   . HOH   F .   ? 0.5557 0.3823 0.4435 -0.0277 0.1332  -0.0163 489 HOH   A O   
6979 O  O   . HOH   F .   ? 0.2637 0.5087 0.3469 0.1076  0.0874  0.2332  490 HOH   A O   
6980 O  O   . HOH   F .   ? 0.6187 0.6070 0.4475 -0.0537 0.1415  0.1117  491 HOH   A O   
6981 O  O   B HOH   F .   ? 0.2433 0.2339 0.2390 0.0248  0.0409  0.0241  492 HOH   A O   
6982 O  O   . HOH   F .   ? 0.2385 0.2429 0.6880 -0.0037 -0.1320 0.0360  493 HOH   A O   
6983 O  O   . HOH   F .   ? 0.6374 0.4899 0.4875 -0.0873 -0.1176 -0.0786 494 HOH   A O   
6984 O  O   . HOH   F .   ? 0.5406 0.5279 0.5131 0.0784  -0.1234 0.0589  495 HOH   A O   
6985 O  O   . HOH   F .   ? 0.5585 0.5415 0.6766 0.0910  0.1782  -0.1008 496 HOH   A O   
6986 O  O   . HOH   F .   ? 0.4379 0.3936 0.2593 -0.1212 0.1325  -0.0632 497 HOH   A O   
6987 O  O   . HOH   F .   ? 0.4266 0.3750 0.4296 -0.0954 0.0506  0.0997  498 HOH   A O   
6988 O  O   . HOH   F .   ? 0.6369 0.2473 0.4424 -0.0743 0.0887  0.0618  499 HOH   A O   
6989 O  O   . HOH   F .   ? 0.4512 0.3092 0.4710 -0.0255 0.2327  0.0371  500 HOH   A O   
6990 O  O   . HOH   F .   ? 0.2808 0.2086 0.6008 0.0107  0.0490  0.0945  501 HOH   A O   
6991 O  O   . HOH   F .   ? 0.2540 0.3154 0.4423 -0.0100 0.0921  -0.0332 502 HOH   A O   
6992 O  O   . HOH   F .   ? 0.3923 0.7891 0.5395 -0.1057 -0.0481 0.2410  503 HOH   A O   
6993 O  O   . HOH   F .   ? 0.7457 0.6232 0.4777 0.1064  -0.1448 0.0025  504 HOH   A O   
6994 O  O   . HOH   F .   ? 0.2428 0.3995 0.3380 0.0762  -0.0404 0.0741  505 HOH   A O   
6995 O  O   . HOH   F .   ? 0.4740 0.2977 0.4095 -0.1721 -0.0067 0.0355  506 HOH   A O   
6996 O  O   B HOH   F .   ? 0.3951 0.3909 0.3185 0.0653  0.0779  0.1459  507 HOH   A O   
6997 O  O   . HOH   F .   ? 0.2720 0.4365 0.4415 0.0337  -0.0599 0.0190  508 HOH   A O   
6998 O  O   . HOH   F .   ? 0.5316 0.7241 0.4791 0.0965  -0.0594 0.0932  509 HOH   A O   
6999 O  O   . HOH   F .   ? 0.6892 0.4636 0.5336 0.0552  -0.0669 0.0691  510 HOH   A O   
7000 O  O   B HOH   F .   ? 0.3387 0.3895 0.3200 0.1001  0.0602  -0.0353 511 HOH   A O   
7001 O  O   B HOH   F .   ? 0.2413 0.2056 0.2492 0.0187  -0.0349 0.0162  512 HOH   A O   
7002 O  O   . HOH   F .   ? 0.2892 0.2361 0.4503 0.0140  0.0462  0.0649  513 HOH   A O   
7003 O  O   . HOH   F .   ? 0.5072 0.6833 0.4725 0.3159  -0.0087 0.1273  514 HOH   A O   
7004 O  O   T HOH   F .   ? 0.0931 0.0775 0.1314 -0.0153 -0.0043 -0.0051 515 HOH   A O   
7005 O  O   A HOH   F .   ? 0.3667 0.8799 0.3819 0.1107  0.0989  -0.0091 516 HOH   A O   
7006 O  O   . HOH   F .   ? 0.5554 0.5747 0.4395 -0.0749 -0.0679 -0.1151 517 HOH   A O   
7007 O  O   B HOH   F .   ? 0.3691 0.4065 0.3623 0.1093  -0.0067 0.0008  518 HOH   A O   
7008 O  O   . HOH   F .   ? 0.2595 0.7215 0.3605 0.0659  0.0301  -0.0233 519 HOH   A O   
7009 O  O   . HOH   F .   ? 0.5086 0.4668 0.4415 0.1449  -0.0369 0.1497  520 HOH   A O   
7010 O  O   . HOH   F .   ? 0.4234 0.6545 0.5405 -0.0583 -0.0376 0.0470  521 HOH   A O   
7011 O  O   . HOH   F .   ? 0.3006 0.4507 0.5634 -0.0390 -0.1038 0.2813  522 HOH   A O   
7012 O  O   . HOH   G .   ? 0.2213 0.2162 0.3338 0.0234  0.0852  0.0426  201 HOH   B O   
7013 O  O   . HOH   G .   ? 0.4512 0.3345 0.4093 -0.0430 -0.0043 -0.1324 202 HOH   B O   
7014 O  O   . HOH   G .   ? 0.6492 0.5943 0.5897 0.2181  -0.0000 -0.0233 203 HOH   B O   
7015 O  O   . HOH   G .   ? 0.3721 0.3024 0.6851 -0.0596 0.0738  -0.0490 204 HOH   B O   
7016 O  O   . HOH   G .   ? 0.3131 0.6896 0.3552 0.0626  0.0188  0.2077  205 HOH   B O   
7017 O  O   . HOH   G .   ? 0.4618 0.4952 0.2483 0.0122  -0.0258 -0.1189 206 HOH   B O   
7018 O  O   . HOH   G .   ? 0.3460 0.4580 0.5104 -0.1079 0.0170  -0.1418 207 HOH   B O   
7019 O  O   . HOH   G .   ? 0.4900 0.5882 0.4232 0.2876  -0.1167 -0.0071 208 HOH   B O   
7020 O  O   . HOH   G .   ? 0.7227 0.3143 0.4511 0.0662  0.1212  -0.0029 209 HOH   B O   
7021 O  O   . HOH   G .   ? 0.2900 0.5657 0.5091 -0.0120 0.1554  -0.1802 210 HOH   B O   
7022 O  O   . HOH   G .   ? 0.1604 0.1817 0.2948 -0.0168 -0.0055 0.0025  211 HOH   B O   
7023 O  O   . HOH   G .   ? 0.4726 0.4018 0.6072 0.0293  -0.1006 0.2607  212 HOH   B O   
7024 O  O   . HOH   G .   ? 0.1914 0.2220 0.3132 -0.0055 0.0212  -0.0284 213 HOH   B O   
7025 O  O   . HOH   G .   ? 0.3295 0.5617 0.5061 0.2299  0.0558  -0.0305 214 HOH   B O   
7026 O  O   . HOH   G .   ? 0.4889 0.3553 0.3519 0.0210  -0.1205 0.0394  215 HOH   B O   
7027 O  O   . HOH   G .   ? 0.2842 0.2624 0.6413 0.0585  -0.1081 0.0422  216 HOH   B O   
7028 O  O   . HOH   G .   ? 0.2972 0.2022 0.5497 0.0142  0.1905  0.0810  217 HOH   B O   
7029 O  O   . HOH   G .   ? 0.4251 0.5290 0.3549 0.2443  -0.0314 -0.0000 218 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4060 0.4322 0.6340 -0.0050 -0.1623 -0.1042 219 HOH   B O   
7031 O  O   . HOH   G .   ? 0.3386 0.3923 0.5090 0.0740  -0.0364 0.0217  220 HOH   B O   
7032 O  O   . HOH   G .   ? 0.4353 0.4508 0.3893 0.0215  0.0910  -0.1398 221 HOH   B O   
7033 O  O   . HOH   G .   ? 0.3262 0.2187 0.5110 0.0037  0.1876  0.0348  222 HOH   B O   
7034 O  O   . HOH   G .   ? 0.5543 0.2863 0.4146 -0.1616 0.0320  0.0104  223 HOH   B O   
7035 O  O   . HOH   G .   ? 0.4794 0.1964 0.3104 -0.0048 -0.0883 0.0034  224 HOH   B O   
7036 O  O   . HOH   G .   ? 0.2058 0.2176 0.4168 -0.0401 0.0035  -0.0531 225 HOH   B O   
7037 O  O   . HOH   G .   ? 0.6483 0.3701 0.2678 -0.0422 0.0847  -0.0052 226 HOH   B O   
7038 O  O   . HOH   G .   ? 0.3516 0.1718 0.2189 0.0173  -0.0892 -0.0077 227 HOH   B O   
7039 O  O   . HOH   G .   ? 0.2489 0.1715 0.2784 -0.0331 0.1097  -0.0061 228 HOH   B O   
7040 O  O   . HOH   G .   ? 0.6051 0.5940 0.3506 0.0935  -0.0015 0.0501  229 HOH   B O   
7041 O  O   . HOH   G .   ? 0.1700 0.2018 0.3221 -0.0151 0.0045  0.0009  230 HOH   B O   
7042 O  O   . HOH   G .   ? 0.4213 0.6501 0.4053 0.2120  0.0205  -0.0199 231 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3920 0.3718 0.5339 -0.1529 0.0009  0.0864  232 HOH   B O   
7044 O  O   . HOH   G .   ? 0.7003 0.4353 0.4579 0.1766  -0.0441 -0.1281 233 HOH   B O   
7045 O  O   . HOH   G .   ? 0.3372 0.3440 0.5914 -0.0094 0.0638  -0.0228 234 HOH   B O   
7046 O  O   . HOH   G .   ? 0.1998 0.1284 0.3365 0.0093  -0.0557 -0.0158 235 HOH   B O   
7047 O  O   . HOH   G .   ? 0.2861 0.2446 0.3089 0.0375  0.0192  -0.0853 236 HOH   B O   
7048 O  O   . HOH   G .   ? 0.3794 0.2686 0.3859 0.0780  -0.0332 -0.0515 237 HOH   B O   
7049 O  O   . HOH   G .   ? 0.2754 0.3853 0.3274 -0.0980 0.0400  -0.0202 238 HOH   B O   
7050 O  O   . HOH   G .   ? 0.1440 0.1396 0.1661 -0.0135 -0.0040 -0.0003 239 HOH   B O   
7051 O  O   . HOH   G .   ? 0.3547 0.2557 0.4109 0.0451  -0.1003 -0.1318 240 HOH   B O   
7052 O  O   . HOH   G .   ? 0.2196 0.1820 0.2238 -0.0319 -0.0400 0.0126  241 HOH   B O   
7053 O  O   . HOH   G .   ? 0.2038 0.2482 0.3177 -0.0556 0.0169  -0.0386 242 HOH   B O   
7054 O  O   . HOH   G .   ? 0.3504 0.3076 0.2308 0.0327  0.0549  0.0579  243 HOH   B O   
7055 O  O   . HOH   G .   ? 0.5215 0.3046 0.4115 -0.2225 -0.0063 0.0133  244 HOH   B O   
7056 O  O   . HOH   G .   ? 0.2117 0.3887 0.2358 -0.0517 -0.0167 0.0549  245 HOH   B O   
7057 O  O   . HOH   G .   ? 0.1425 0.1219 0.1751 -0.0000 -0.0093 0.0130  246 HOH   B O   
7058 O  O   . HOH   G .   ? 0.2903 0.4427 0.2966 -0.1159 -0.0198 -0.0585 247 HOH   B O   
7059 O  O   . HOH   G .   ? 0.3030 0.1742 0.6147 -0.0223 -0.1208 -0.0274 248 HOH   B O   
7060 O  O   . HOH   G .   ? 0.2373 0.1986 0.2686 0.0646  -0.0788 -0.0585 249 HOH   B O   
7061 O  O   . HOH   G .   ? 0.1517 0.1443 0.2777 -0.0087 0.0082  -0.0084 250 HOH   B O   
7062 O  O   . HOH   G .   ? 0.3226 0.3960 0.2181 0.0228  0.0740  0.0227  251 HOH   B O   
7063 O  O   . HOH   G .   ? 0.3230 0.5054 0.3363 -0.0315 -0.1115 0.1058  252 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2221 0.3573 0.3128 -0.0560 -0.0542 -0.0458 253 HOH   B O   
7065 O  O   . HOH   G .   ? 0.2056 0.1417 0.2250 -0.0262 -0.0370 0.0254  254 HOH   B O   
7066 O  O   . HOH   G .   ? 0.3260 0.2544 0.3089 -0.0436 0.0216  -0.0541 255 HOH   B O   
7067 O  O   . HOH   G .   ? 0.2862 0.2249 0.3016 0.0840  0.0867  -0.0065 256 HOH   B O   
7068 O  O   . HOH   G .   ? 0.2443 0.2216 0.2063 0.0126  -0.0041 0.0059  257 HOH   B O   
7069 O  O   . HOH   G .   ? 0.2282 0.4802 0.5534 0.1247  -0.0627 -0.1350 258 HOH   B O   
7070 O  O   . HOH   G .   ? 0.2589 0.4650 0.5740 0.0363  -0.0037 -0.1404 259 HOH   B O   
7071 O  O   . HOH   G .   ? 0.4644 0.3556 0.2858 0.0324  -0.0096 -0.0836 260 HOH   B O   
7072 O  O   . HOH   G .   ? 0.1552 0.1594 0.3114 -0.0221 -0.0193 0.0119  261 HOH   B O   
7073 O  O   . HOH   G .   ? 0.1782 0.2793 0.2747 0.0425  0.0457  0.1057  262 HOH   B O   
7074 O  O   . HOH   G .   ? 0.1334 0.1630 0.2228 -0.0091 0.0046  0.0148  263 HOH   B O   
7075 O  O   . HOH   G .   ? 0.2229 0.3079 0.2148 -0.0588 0.0318  0.0327  264 HOH   B O   
7076 O  O   . HOH   G .   ? 0.2249 0.1874 0.3376 0.0038  -0.0660 -0.0342 265 HOH   B O   
7077 O  O   . HOH   G .   ? 0.3378 0.3323 0.5407 -0.0330 -0.0143 -0.0490 266 HOH   B O   
7078 O  O   . HOH   G .   ? 0.4196 0.3639 0.3652 -0.0835 0.0724  -0.1062 267 HOH   B O   
7079 O  O   . HOH   G .   ? 0.2236 0.2108 0.2134 0.0088  -0.0036 -0.0082 268 HOH   B O   
7080 O  O   . HOH   G .   ? 0.2147 0.4228 0.4751 -0.0403 -0.0351 -0.1446 269 HOH   B O   
7081 O  O   . HOH   G .   ? 0.2502 0.1994 0.2802 -0.0639 0.0170  -0.0103 270 HOH   B O   
7082 O  O   . HOH   G .   ? 0.4043 0.2738 0.4620 0.0019  -0.1273 -0.0634 271 HOH   B O   
7083 O  O   . HOH   G .   ? 0.3272 0.3748 0.4540 0.1029  -0.0718 -0.1139 272 HOH   B O   
7084 O  O   . HOH   G .   ? 0.2419 0.2702 0.2487 -0.0315 -0.0681 0.0211  273 HOH   B O   
7085 O  O   . HOH   G .   ? 0.1810 0.1762 0.1866 -0.0444 -0.0402 0.0056  274 HOH   B O   
7086 O  O   . HOH   G .   ? 0.2567 0.3726 0.3941 0.0419  0.1185  0.0339  275 HOH   B O   
7087 O  O   . HOH   G .   ? 0.2435 0.3917 0.2321 0.1419  -0.0371 -0.0449 276 HOH   B O   
7088 O  O   . HOH   G .   ? 0.1962 0.1454 0.2399 -0.0267 -0.0171 0.0191  277 HOH   B O   
7089 O  O   . HOH   G .   ? 0.2306 0.2582 0.2303 -0.0409 -0.0568 -0.0362 278 HOH   B O   
7090 O  O   . HOH   G .   ? 0.1673 0.1361 0.4497 -0.0088 -0.0342 -0.0034 279 HOH   B O   
7091 O  O   . HOH   G .   ? 0.1580 0.1554 0.3303 -0.0136 0.0052  -0.0013 280 HOH   B O   
7092 O  O   . HOH   G .   ? 0.2404 0.3538 0.3185 -0.0690 0.0562  -0.1214 281 HOH   B O   
7093 O  O   . HOH   G .   ? 0.2783 0.2021 0.4790 0.0136  0.0425  0.0381  282 HOH   B O   
7094 O  O   . HOH   G .   ? 0.4225 0.4972 0.4431 -0.0090 -0.1500 0.0310  283 HOH   B O   
7095 O  O   . HOH   G .   ? 0.2551 0.6854 0.2516 0.0900  -0.0279 -0.0469 284 HOH   B O   
7096 O  O   . HOH   G .   ? 0.3869 0.7049 0.3361 0.1694  -0.0519 0.1110  285 HOH   B O   
7097 O  O   . HOH   G .   ? 0.1649 0.1473 0.1912 0.0008  0.0090  0.0008  286 HOH   B O   
7098 O  O   . HOH   G .   ? 0.2718 0.4676 0.4827 -0.1097 -0.1213 0.0921  287 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2665 0.6251 0.7130 0.1278  -0.0592 -0.0936 288 HOH   B O   
7100 O  O   . HOH   G .   ? 0.3361 0.2887 0.2891 -0.0268 0.0087  -0.1248 289 HOH   B O   
7101 O  O   . HOH   G .   ? 0.4737 0.6459 0.2467 -0.0083 -0.0951 0.0850  290 HOH   B O   
7102 O  O   . HOH   G .   ? 0.1672 0.1895 0.3136 0.0200  -0.0027 0.0029  291 HOH   B O   
7103 O  O   . HOH   G .   ? 0.3830 0.2074 0.3965 -0.1025 -0.2002 0.0749  292 HOH   B O   
7104 O  O   . HOH   G .   ? 0.5638 0.3775 0.3171 0.2553  0.1228  0.0945  293 HOH   B O   
7105 O  O   . HOH   G .   ? 0.1715 0.3185 0.4580 0.0182  0.0082  -0.1174 294 HOH   B O   
7106 O  O   . HOH   G .   ? 0.2425 0.2683 0.2732 0.0159  -0.0718 0.0146  295 HOH   B O   
7107 O  O   . HOH   G .   ? 0.1569 0.1975 0.1640 -0.0154 -0.0185 0.0049  296 HOH   B O   
7108 O  O   . HOH   G .   ? 0.3402 0.2537 0.2109 0.0146  -0.0771 -0.0126 297 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5085 0.3851 0.2479 0.1417  -0.1014 0.0448  298 HOH   B O   
7110 O  O   . HOH   G .   ? 0.1736 0.1585 0.2469 0.0070  0.0057  0.0132  299 HOH   B O   
7111 O  O   . HOH   G .   ? 0.2113 0.1664 0.2603 -0.0293 -0.0283 -0.0008 300 HOH   B O   
7112 O  O   . HOH   G .   ? 0.3453 0.3663 0.4029 -0.1442 0.1252  -0.0489 301 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4520 0.4062 0.2364 0.1196  -0.0754 -0.0088 302 HOH   B O   
7114 O  O   . HOH   G .   ? 0.4550 0.4818 0.2618 0.0172  0.0917  0.0970  303 HOH   B O   
7115 O  O   . HOH   G .   ? 0.2022 0.2718 0.6169 0.0368  -0.0506 -0.1145 304 HOH   B O   
7116 O  O   . HOH   G .   ? 0.3023 0.2843 0.4918 -0.0297 -0.0810 0.1144  305 HOH   B O   
7117 O  O   . HOH   G .   ? 0.1554 0.1432 0.3234 0.0056  -0.0060 -0.0077 306 HOH   B O   
7118 O  O   . HOH   G .   ? 0.3492 0.1855 0.3172 0.0751  0.1141  0.0487  307 HOH   B O   
7119 O  O   . HOH   G .   ? 0.5930 0.6290 0.5379 0.3061  0.0108  -0.0062 308 HOH   B O   
7120 O  O   . HOH   G .   ? 0.2089 0.1525 0.3382 0.0382  -0.0950 -0.0055 309 HOH   B O   
7121 O  O   . HOH   G .   ? 0.2938 0.3029 0.3476 -0.0511 0.1199  -0.0861 310 HOH   B O   
7122 O  O   . HOH   G .   ? 0.4559 0.3741 0.4323 -0.0553 0.0252  0.1334  311 HOH   B O   
7123 O  O   . HOH   G .   ? 0.5110 0.2863 0.2406 -0.1708 0.0787  -0.0211 312 HOH   B O   
7124 O  O   . HOH   G .   ? 0.2448 0.1457 0.2514 -0.0186 -0.0206 0.0282  313 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4473 0.4065 0.5832 0.0648  0.0029  0.0784  314 HOH   B O   
7126 O  O   . HOH   G .   ? 0.4759 0.4287 0.2845 0.0467  -0.0692 -0.0838 315 HOH   B O   
7127 O  O   . HOH   G .   ? 0.2204 0.1925 0.1889 -0.0100 0.0127  0.0131  316 HOH   B O   
7128 O  O   . HOH   G .   ? 0.2100 0.3094 0.4707 -0.0125 -0.0356 -0.0203 317 HOH   B O   
7129 O  O   . HOH   G .   ? 0.1583 0.1809 0.3032 -0.0262 -0.0154 0.0234  318 HOH   B O   
7130 O  O   . HOH   G .   ? 0.5268 0.3533 0.4600 0.0394  0.1016  -0.1409 319 HOH   B O   
7131 O  O   . HOH   G .   ? 0.3941 0.2202 0.2756 0.1362  0.1052  0.0322  320 HOH   B O   
7132 O  O   . HOH   G .   ? 0.3442 0.4095 0.7181 -0.0207 -0.0935 0.2028  321 HOH   B O   
7133 O  O   . HOH   G .   ? 0.1585 0.2790 0.2416 -0.0158 -0.0150 0.0746  322 HOH   B O   
7134 O  O   . HOH   G .   ? 0.1535 0.1575 0.3126 -0.0175 -0.0157 -0.0145 323 HOH   B O   
7135 O  O   . HOH   G .   ? 0.4478 0.3112 0.5100 0.1220  0.2127  0.1711  324 HOH   B O   
7136 O  O   . HOH   G .   ? 0.6450 0.4460 0.5199 0.1307  0.1766  0.0120  325 HOH   B O   
7137 O  O   . HOH   G .   ? 0.2078 0.6289 0.4604 -0.0661 -0.0277 -0.0101 326 HOH   B O   
7138 O  O   . HOH   G .   ? 0.3078 0.2164 0.2507 0.0189  -0.0243 0.0330  327 HOH   B O   
7139 O  O   . HOH   G .   ? 0.6048 0.4988 0.6403 0.1183  -0.0923 0.2083  328 HOH   B O   
7140 O  O   . HOH   G .   ? 0.4752 0.2365 0.3045 0.0388  0.0484  0.0709  329 HOH   B O   
7141 O  O   . HOH   G .   ? 0.1853 0.1962 0.2971 0.0263  0.0416  0.0176  330 HOH   B O   
7142 O  O   . HOH   G .   ? 0.1729 0.2656 0.3236 0.0225  -0.0108 -0.0644 331 HOH   B O   
7143 O  O   . HOH   G .   ? 0.5608 0.5470 0.5367 -0.1106 -0.0526 0.1419  332 HOH   B O   
7144 O  O   . HOH   G .   ? 0.2756 0.1929 0.5602 -0.0053 0.0040  0.0503  333 HOH   B O   
7145 O  O   . HOH   G .   ? 0.5914 0.3551 0.3430 0.0056  0.1134  0.1102  334 HOH   B O   
7146 O  O   . HOH   G .   ? 0.8102 0.2077 0.3102 0.0227  -0.0892 -0.0076 335 HOH   B O   
7147 O  O   . HOH   G .   ? 0.2875 0.3241 0.5186 -0.0611 -0.1641 0.1567  336 HOH   B O   
7148 O  O   . HOH   G .   ? 0.2147 0.2379 0.5436 -0.0530 -0.0078 0.1390  337 HOH   B O   
7149 O  O   . HOH   G .   ? 0.1734 0.1446 0.2392 0.0074  -0.0203 0.0101  338 HOH   B O   
7150 O  O   . HOH   G .   ? 0.5700 0.3927 0.6022 -0.0744 -0.0840 -0.0959 339 HOH   B O   
7151 O  O   . HOH   G .   ? 0.4400 0.7190 0.3574 -0.0139 -0.0717 0.1867  340 HOH   B O   
7152 O  O   . HOH   G .   ? 0.5081 0.3521 0.2948 0.0497  -0.1230 -0.0827 341 HOH   B O   
7153 O  O   . HOH   G .   ? 0.4682 0.5140 0.3679 0.0062  -0.0978 0.0246  342 HOH   B O   
7154 O  O   . HOH   G .   ? 0.1958 0.5448 0.6457 -0.0165 -0.0858 0.0146  343 HOH   B O   
7155 O  O   . HOH   G .   ? 0.6821 0.6389 0.3030 0.0058  -0.0650 0.1105  344 HOH   B O   
7156 O  O   . HOH   G .   ? 0.4135 0.5944 0.3880 -0.0992 -0.0973 -0.0665 345 HOH   B O   
7157 O  O   . HOH   G .   ? 0.2008 0.1946 0.3297 -0.0130 0.0640  -0.0110 346 HOH   B O   
7158 O  O   . HOH   G .   ? 0.4448 0.5185 0.5273 0.0234  -0.0798 0.1035  347 HOH   B O   
7159 O  O   . HOH   G .   ? 0.2869 0.1811 0.3981 0.0336  -0.1144 -0.0559 348 HOH   B O   
7160 O  O   . HOH   G .   ? 0.3305 0.3978 0.4899 -0.1371 0.0191  -0.0586 349 HOH   B O   
7161 O  O   . HOH   G .   ? 0.2818 0.2205 0.4715 -0.0258 -0.0954 -0.0456 350 HOH   B O   
7162 O  O   . HOH   G .   ? 0.2484 0.6301 0.3367 0.1647  -0.0576 -0.1409 351 HOH   B O   
7163 O  O   . HOH   G .   ? 0.4310 0.5418 0.6399 0.0164  0.0239  -0.0811 352 HOH   B O   
7164 O  O   . HOH   G .   ? 0.2088 0.3948 0.5124 0.0214  0.0408  0.0219  353 HOH   B O   
7165 O  O   . HOH   G .   ? 0.4686 0.5362 0.4838 -0.1065 0.0511  0.0958  354 HOH   B O   
7166 O  O   . HOH   G .   ? 0.3881 0.2131 0.3481 -0.0699 0.0393  -0.0784 355 HOH   B O   
7167 O  O   . HOH   G .   ? 0.4749 0.3107 0.5501 -0.1111 0.1320  0.0699  356 HOH   B O   
7168 O  O   . HOH   G .   ? 0.3633 0.2752 0.3662 -0.1051 0.0060  -0.0715 357 HOH   B O   
7169 O  O   . HOH   G .   ? 0.5000 0.3704 0.4077 0.0531  0.1258  -0.0650 358 HOH   B O   
7170 O  O   . HOH   G .   ? 0.4550 0.5158 0.4680 0.1612  -0.1129 0.1387  359 HOH   B O   
7171 O  O   . HOH   G .   ? 0.4765 0.4879 0.5870 0.0036  0.0387  0.0712  360 HOH   B O   
7172 O  O   . HOH   G .   ? 0.5061 0.3573 0.4925 -0.0214 -0.1516 -0.0519 361 HOH   B O   
7173 O  O   . HOH   G .   ? 0.5036 0.4067 0.6128 0.0709  0.1431  0.1351  362 HOH   B O   
7174 O  O   . HOH   G .   ? 0.2252 0.3538 0.6892 -0.0750 -0.0646 -0.0629 363 HOH   B O   
7175 O  O   . HOH   G .   ? 0.4257 0.6303 0.3155 0.2162  -0.0128 0.0164  364 HOH   B O   
7176 O  O   . HOH   G .   ? 0.4800 0.3088 0.5463 -0.1378 -0.0421 0.0180  365 HOH   B O   
7177 O  O   . HOH   G .   ? 0.5752 0.4423 0.4318 0.1004  0.0597  0.0701  366 HOH   B O   
7178 O  O   . HOH   G .   ? 0.6333 0.2224 0.3608 -0.0148 0.0110  0.0671  367 HOH   B O   
7179 O  O   . HOH   G .   ? 0.4960 0.3610 0.5477 0.1217  -0.1366 0.0029  368 HOH   B O   
7180 O  O   . HOH   G .   ? 0.5502 0.5712 0.3604 0.1709  -0.1556 0.0891  369 HOH   B O   
7181 O  O   . HOH   G .   ? 0.4946 0.5894 0.4163 -0.0845 -0.0451 -0.1132 370 HOH   B O   
7182 O  O   . HOH   G .   ? 0.8358 0.7776 0.5294 0.2556  -0.1403 0.0408  371 HOH   B O   
7183 O  O   . HOH   G .   ? 0.4218 0.5450 0.4877 0.2348  0.1094  0.1337  372 HOH   B O   
7184 O  O   . HOH   G .   ? 0.6198 0.3783 0.2788 -0.1103 -0.0943 -0.0385 373 HOH   B O   
7185 O  O   . HOH   G .   ? 0.4086 0.3447 0.4154 0.0774  -0.1611 -0.0514 374 HOH   B O   
7186 O  O   . HOH   G .   ? 0.4498 0.4681 0.4711 -0.0692 -0.0459 0.0409  375 HOH   B O   
7187 O  O   . HOH   G .   ? 0.2327 0.4119 0.4610 0.0081  -0.0625 -0.0908 376 HOH   B O   
7188 O  O   . HOH   G .   ? 0.4454 0.7088 0.5756 0.1314  0.0444  0.2883  377 HOH   B O   
7189 O  O   . HOH   G .   ? 0.5197 0.7306 0.4077 -0.1405 0.0224  -0.1444 378 HOH   B O   
7190 O  O   . HOH   G .   ? 0.3190 0.4408 0.2329 0.0310  0.0338  -0.0084 379 HOH   B O   
7191 O  O   . HOH   G .   ? 0.3734 0.4475 0.5109 0.1061  -0.0052 0.0305  380 HOH   B O   
7192 O  O   . HOH   G .   ? 0.7410 0.3617 0.4893 -0.0903 -0.0777 -0.0073 381 HOH   B O   
7193 O  O   . HOH   G .   ? 0.5221 0.6465 0.6025 -0.0485 0.2105  0.1380  382 HOH   B O   
7194 O  O   . HOH   G .   ? 0.3239 0.2471 0.3188 0.0192  0.0418  0.0471  383 HOH   B O   
7195 O  O   . HOH   G .   ? 0.4817 0.7602 0.5572 0.0880  0.2192  0.0546  384 HOH   B O   
7196 O  O   . HOH   G .   ? 0.4915 0.4955 0.4172 -0.0218 -0.0596 -0.0354 385 HOH   B O   
7197 O  O   . HOH   G .   ? 0.7082 0.3701 0.3908 0.0797  0.1200  -0.0428 386 HOH   B O   
7198 O  O   . HOH   G .   ? 0.6083 0.4057 0.5093 -0.0809 0.0680  -0.0392 387 HOH   B O   
7199 O  O   . HOH   G .   ? 0.2458 0.4164 0.4059 -0.0651 -0.1080 -0.0289 388 HOH   B O   
7200 O  O   . HOH   G .   ? 0.7519 0.5546 0.4457 0.2251  -0.0309 0.0120  389 HOH   B O   
7201 O  O   . HOH   G .   ? 0.4907 0.3661 0.3452 0.0136  0.0759  -0.0065 390 HOH   B O   
7202 O  O   . HOH   G .   ? 0.4013 0.2193 0.3229 0.0765  -0.0321 0.0140  391 HOH   B O   
7203 O  O   . HOH   G .   ? 0.4942 0.4072 0.4158 0.0335  0.0556  0.0816  392 HOH   B O   
7204 O  O   . HOH   G .   ? 0.4185 0.2152 0.5203 -0.0430 0.0890  0.0476  393 HOH   B O   
7205 O  O   . HOH   G .   ? 0.2537 0.3956 0.6683 -0.1221 -0.0681 -0.0059 394 HOH   B O   
7206 O  O   . HOH   G .   ? 0.4409 0.6101 0.4097 0.1422  0.0140  -0.1102 395 HOH   B O   
7207 O  O   . HOH   G .   ? 0.3311 0.3615 0.3964 0.0221  0.0258  -0.0754 396 HOH   B O   
7208 O  O   . HOH   G .   ? 0.2072 0.2832 0.5953 -0.0679 -0.0985 0.0419  397 HOH   B O   
7209 O  O   . HOH   G .   ? 0.4469 0.4300 0.4341 0.0233  0.1080  0.0841  398 HOH   B O   
7210 O  O   . HOH   G .   ? 0.5789 0.4283 0.3063 -0.2263 -0.0260 0.1147  399 HOH   B O   
7211 O  O   . HOH   G .   ? 0.5595 0.6355 0.7099 0.1331  -0.1327 0.1841  400 HOH   B O   
7212 O  O   . HOH   G .   ? 0.5738 0.6018 0.3614 0.1378  -0.0267 -0.0357 401 HOH   B O   
# 
