data_7HFP
# 
_entry.id   7HFP 
# 
_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   7HFP         pdb_00007hfp 10.2210/pdb7hfp/pdb 
WWPDB D_1001407415 ?            ?                   
# 
_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                        7HFP 
_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 'DIMETHYL SULFOXIDE'                                                78.133    1   ?                      ? ? ? 
3 non-polymer syn '4-{[methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' 262.308   1   ?                      ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                      35.453    1   ?                      ? ? ? 
5 water       nat water                                                               18.015    421 ?                      ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                DMS   
3 '4-{[methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' A1BBQ 
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 
A1BBQ non-polymer         . '4-{[methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' ? 'C13 H18 N4 O2'  262.308 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                           ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                     ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                             ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                           ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                               ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                          ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                             ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                              ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                          ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                       ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                             ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                              ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                           ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                            ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                              ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301 301  DMS   DMS A . 
D 3 A1BBQ 1   302 201  A1BBQ LA1 A . 
E 4 CL    1   303 1    CL    CL  A . 
F 5 HOH   1   401 196  HOH   HOH A . 
F 5 HOH   2   402 36   HOH   HOH A . 
F 5 HOH   3   403 209  HOH   HOH A . 
F 5 HOH   4   404 1301 HOH   HOH A . 
F 5 HOH   5   405 292  HOH   HOH A . 
F 5 HOH   6   406 199  HOH   HOH A . 
F 5 HOH   7   407 9    HOH   HOH A . 
F 5 HOH   8   408 964  HOH   HOH A . 
F 5 HOH   9   409 393  HOH   HOH A . 
F 5 HOH   10  410 86   HOH   HOH A . 
F 5 HOH   11  411 109  HOH   HOH A . 
F 5 HOH   12  412 192  HOH   HOH A . 
F 5 HOH   13  413 1300 HOH   HOH A . 
F 5 HOH   14  414 14   HOH   HOH A . 
F 5 HOH   15  415 625  HOH   HOH A . 
F 5 HOH   16  416 409  HOH   HOH A . 
F 5 HOH   17  417 105  HOH   HOH A . 
F 5 HOH   18  418 136  HOH   HOH A . 
F 5 HOH   19  419 10   HOH   HOH A . 
F 5 HOH   20  420 13   HOH   HOH A . 
F 5 HOH   21  421 661  HOH   HOH A . 
F 5 HOH   22  422 2    HOH   HOH A . 
F 5 HOH   23  423 124  HOH   HOH A . 
F 5 HOH   24  424 229  HOH   HOH A . 
F 5 HOH   25  425 76   HOH   HOH A . 
F 5 HOH   26  426 15   HOH   HOH A . 
F 5 HOH   27  427 247  HOH   HOH A . 
F 5 HOH   28  428 1283 HOH   HOH A . 
F 5 HOH   29  429 1295 HOH   HOH A . 
F 5 HOH   30  430 1310 HOH   HOH A . 
F 5 HOH   31  431 26   HOH   HOH A . 
F 5 HOH   32  432 469  HOH   HOH A . 
F 5 HOH   33  433 164  HOH   HOH A . 
F 5 HOH   34  434 165  HOH   HOH A . 
F 5 HOH   35  435 132  HOH   HOH A . 
F 5 HOH   36  436 15   HOH   HOH A . 
F 5 HOH   37  437 140  HOH   HOH A . 
F 5 HOH   38  438 39   HOH   HOH A . 
F 5 HOH   39  439 630  HOH   HOH A . 
F 5 HOH   40  440 155  HOH   HOH A . 
F 5 HOH   41  441 5    HOH   HOH A . 
F 5 HOH   42  442 236  HOH   HOH A . 
F 5 HOH   43  443 281  HOH   HOH A . 
F 5 HOH   44  444 337  HOH   HOH A . 
F 5 HOH   45  445 396  HOH   HOH A . 
F 5 HOH   46  446 1290 HOH   HOH A . 
F 5 HOH   47  447 461  HOH   HOH A . 
F 5 HOH   48  448 662  HOH   HOH A . 
F 5 HOH   49  449 241  HOH   HOH A . 
F 5 HOH   50  450 42   HOH   HOH A . 
F 5 HOH   51  451 33   HOH   HOH A . 
F 5 HOH   52  452 218  HOH   HOH A . 
F 5 HOH   53  453 153  HOH   HOH A . 
F 5 HOH   54  454 225  HOH   HOH A . 
F 5 HOH   55  455 939  HOH   HOH A . 
F 5 HOH   56  456 93   HOH   HOH A . 
F 5 HOH   57  457 169  HOH   HOH A . 
F 5 HOH   58  458 92   HOH   HOH A . 
F 5 HOH   59  459 102  HOH   HOH A . 
F 5 HOH   60  460 381  HOH   HOH A . 
F 5 HOH   61  461 5    HOH   HOH A . 
F 5 HOH   62  462 11   HOH   HOH A . 
F 5 HOH   63  463 66   HOH   HOH A . 
F 5 HOH   64  464 56   HOH   HOH A . 
F 5 HOH   65  465 320  HOH   HOH A . 
F 5 HOH   66  466 151  HOH   HOH A . 
F 5 HOH   67  467 354  HOH   HOH A . 
F 5 HOH   68  468 19   HOH   HOH A . 
F 5 HOH   69  469 17   HOH   HOH A . 
F 5 HOH   70  470 162  HOH   HOH A . 
F 5 HOH   71  471 138  HOH   HOH A . 
F 5 HOH   72  472 2    HOH   HOH A . 
F 5 HOH   73  473 57   HOH   HOH A . 
F 5 HOH   74  474 78   HOH   HOH A . 
F 5 HOH   75  475 4    HOH   HOH A . 
F 5 HOH   76  476 18   HOH   HOH A . 
F 5 HOH   77  477 46   HOH   HOH A . 
F 5 HOH   78  478 24   HOH   HOH A . 
F 5 HOH   79  479 366  HOH   HOH A . 
F 5 HOH   80  480 8    HOH   HOH A . 
F 5 HOH   81  481 134  HOH   HOH A . 
F 5 HOH   82  482 45   HOH   HOH A . 
F 5 HOH   83  483 62   HOH   HOH A . 
F 5 HOH   84  484 8    HOH   HOH A . 
F 5 HOH   85  485 1    HOH   HOH A . 
F 5 HOH   86  486 159  HOH   HOH A . 
F 5 HOH   87  487 278  HOH   HOH A . 
F 5 HOH   88  488 85   HOH   HOH A . 
F 5 HOH   89  489 49   HOH   HOH A . 
F 5 HOH   90  490 3    HOH   HOH A . 
F 5 HOH   91  491 186  HOH   HOH A . 
F 5 HOH   92  492 35   HOH   HOH A . 
F 5 HOH   93  493 116  HOH   HOH A . 
F 5 HOH   94  494 303  HOH   HOH A . 
F 5 HOH   95  495 27   HOH   HOH A . 
F 5 HOH   96  496 1308 HOH   HOH A . 
F 5 HOH   97  497 351  HOH   HOH A . 
F 5 HOH   98  498 83   HOH   HOH A . 
F 5 HOH   99  499 148  HOH   HOH A . 
F 5 HOH   100 500 1309 HOH   HOH A . 
F 5 HOH   101 501 21   HOH   HOH A . 
F 5 HOH   102 502 154  HOH   HOH A . 
F 5 HOH   103 503 139  HOH   HOH A . 
F 5 HOH   104 504 405  HOH   HOH A . 
F 5 HOH   105 505 58   HOH   HOH A . 
F 5 HOH   106 506 1296 HOH   HOH A . 
F 5 HOH   107 507 195  HOH   HOH A . 
F 5 HOH   108 508 67   HOH   HOH A . 
F 5 HOH   109 509 7    HOH   HOH A . 
F 5 HOH   110 510 212  HOH   HOH A . 
F 5 HOH   111 511 96   HOH   HOH A . 
F 5 HOH   112 512 6    HOH   HOH A . 
F 5 HOH   113 513 1068 HOH   HOH A . 
F 5 HOH   114 514 12   HOH   HOH A . 
F 5 HOH   115 515 51   HOH   HOH A . 
F 5 HOH   116 516 7    HOH   HOH A . 
F 5 HOH   117 517 68   HOH   HOH A . 
F 5 HOH   118 518 1315 HOH   HOH A . 
F 5 HOH   119 519 34   HOH   HOH A . 
F 5 HOH   120 520 74   HOH   HOH A . 
F 5 HOH   121 521 121  HOH   HOH A . 
F 5 HOH   122 522 1313 HOH   HOH A . 
F 5 HOH   123 523 1289 HOH   HOH A . 
F 5 HOH   124 524 156  HOH   HOH A . 
F 5 HOH   125 525 25   HOH   HOH A . 
F 5 HOH   126 526 123  HOH   HOH A . 
F 5 HOH   127 527 296  HOH   HOH A . 
F 5 HOH   128 528 582  HOH   HOH A . 
F 5 HOH   129 529 53   HOH   HOH A . 
F 5 HOH   130 530 70   HOH   HOH A . 
F 5 HOH   131 531 122  HOH   HOH A . 
F 5 HOH   132 532 1222 HOH   HOH A . 
F 5 HOH   133 533 115  HOH   HOH A . 
F 5 HOH   134 534 125  HOH   HOH A . 
F 5 HOH   135 535 397  HOH   HOH A . 
F 5 HOH   136 536 333  HOH   HOH A . 
F 5 HOH   137 537 95   HOH   HOH A . 
F 5 HOH   138 538 1275 HOH   HOH A . 
F 5 HOH   139 539 493  HOH   HOH A . 
F 5 HOH   140 540 71   HOH   HOH A . 
F 5 HOH   141 541 40   HOH   HOH A . 
F 5 HOH   142 542 16   HOH   HOH A . 
F 5 HOH   143 543 73   HOH   HOH A . 
F 5 HOH   144 544 1279 HOH   HOH A . 
F 5 HOH   145 545 80   HOH   HOH A . 
F 5 HOH   146 546 1286 HOH   HOH A . 
F 5 HOH   147 547 94   HOH   HOH A . 
F 5 HOH   148 548 1189 HOH   HOH A . 
F 5 HOH   149 549 1134 HOH   HOH A . 
F 5 HOH   150 550 952  HOH   HOH A . 
F 5 HOH   151 551 4    HOH   HOH A . 
F 5 HOH   152 552 104  HOH   HOH A . 
F 5 HOH   153 553 1238 HOH   HOH A . 
F 5 HOH   154 554 97   HOH   HOH A . 
F 5 HOH   155 555 576  HOH   HOH A . 
F 5 HOH   156 556 944  HOH   HOH A . 
F 5 HOH   157 557 1094 HOH   HOH A . 
F 5 HOH   158 558 188  HOH   HOH A . 
F 5 HOH   159 559 79   HOH   HOH A . 
F 5 HOH   160 560 1119 HOH   HOH A . 
F 5 HOH   161 561 330  HOH   HOH A . 
F 5 HOH   162 562 509  HOH   HOH A . 
F 5 HOH   163 563 163  HOH   HOH A . 
F 5 HOH   164 564 726  HOH   HOH A . 
F 5 HOH   165 565 107  HOH   HOH A . 
F 5 HOH   166 566 408  HOH   HOH A . 
F 5 HOH   167 567 756  HOH   HOH A . 
F 5 HOH   168 568 319  HOH   HOH A . 
F 5 HOH   169 569 361  HOH   HOH A . 
F 5 HOH   170 570 126  HOH   HOH A . 
F 5 HOH   171 571 801  HOH   HOH A . 
F 5 HOH   172 572 1276 HOH   HOH A . 
F 5 HOH   173 573 556  HOH   HOH A . 
F 5 HOH   174 574 63   HOH   HOH A . 
F 5 HOH   175 575 250  HOH   HOH A . 
F 5 HOH   176 576 3    HOH   HOH A . 
F 5 HOH   177 577 370  HOH   HOH A . 
F 5 HOH   178 578 280  HOH   HOH A . 
F 5 HOH   179 579 1307 HOH   HOH A . 
F 5 HOH   180 580 342  HOH   HOH A . 
F 5 HOH   181 581 1306 HOH   HOH A . 
F 5 HOH   182 582 224  HOH   HOH A . 
F 5 HOH   183 583 267  HOH   HOH A . 
F 5 HOH   184 584 521  HOH   HOH A . 
F 5 HOH   185 585 1287 HOH   HOH A . 
F 5 HOH   186 586 674  HOH   HOH A . 
F 5 HOH   187 587 695  HOH   HOH A . 
F 5 HOH   188 588 135  HOH   HOH A . 
F 5 HOH   189 589 318  HOH   HOH A . 
F 5 HOH   190 590 202  HOH   HOH A . 
F 5 HOH   191 591 326  HOH   HOH A . 
F 5 HOH   192 592 919  HOH   HOH A . 
F 5 HOH   193 593 331  HOH   HOH A . 
F 5 HOH   194 594 711  HOH   HOH A . 
F 5 HOH   195 595 309  HOH   HOH A . 
F 5 HOH   196 596 1299 HOH   HOH A . 
F 5 HOH   197 597 805  HOH   HOH A . 
F 5 HOH   198 598 315  HOH   HOH A . 
F 5 HOH   199 599 1314 HOH   HOH A . 
F 5 HOH   200 600 981  HOH   HOH A . 
F 5 HOH   201 601 208  HOH   HOH A . 
F 5 HOH   202 602 941  HOH   HOH A . 
F 5 HOH   203 603 152  HOH   HOH A . 
F 5 HOH   204 604 356  HOH   HOH A . 
F 5 HOH   205 605 263  HOH   HOH A . 
F 5 HOH   206 606 12   HOH   HOH A . 
F 5 HOH   207 607 180  HOH   HOH A . 
F 5 HOH   208 608 1284 HOH   HOH A . 
F 5 HOH   209 609 363  HOH   HOH A . 
F 5 HOH   210 610 371  HOH   HOH A . 
F 5 HOH   211 611 1071 HOH   HOH A . 
F 5 HOH   212 612 313  HOH   HOH A . 
F 5 HOH   213 613 429  HOH   HOH A . 
F 5 HOH   214 614 185  HOH   HOH A . 
F 5 HOH   215 615 376  HOH   HOH A . 
F 5 HOH   216 616 772  HOH   HOH A . 
F 5 HOH   217 617 1074 HOH   HOH A . 
F 5 HOH   218 618 1292 HOH   HOH A . 
F 5 HOH   219 619 346  HOH   HOH A . 
F 5 HOH   220 620 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 240  HOH   HOH B . 
G 5 HOH   3   203 398  HOH   HOH B . 
G 5 HOH   4   204 1249 HOH   HOH B . 
G 5 HOH   5   205 549  HOH   HOH B . 
G 5 HOH   6   206 900  HOH   HOH B . 
G 5 HOH   7   207 353  HOH   HOH B . 
G 5 HOH   8   208 654  HOH   HOH B . 
G 5 HOH   9   209 758  HOH   HOH B . 
G 5 HOH   10  210 332  HOH   HOH B . 
G 5 HOH   11  211 166  HOH   HOH B . 
G 5 HOH   12  212 120  HOH   HOH B . 
G 5 HOH   13  213 364  HOH   HOH B . 
G 5 HOH   14  214 50   HOH   HOH B . 
G 5 HOH   15  215 232  HOH   HOH B . 
G 5 HOH   16  216 358  HOH   HOH B . 
G 5 HOH   17  217 452  HOH   HOH B . 
G 5 HOH   18  218 444  HOH   HOH B . 
G 5 HOH   19  219 75   HOH   HOH B . 
G 5 HOH   20  220 531  HOH   HOH B . 
G 5 HOH   21  221 743  HOH   HOH B . 
G 5 HOH   22  222 264  HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 129  HOH   HOH B . 
G 5 HOH   25  225 54   HOH   HOH B . 
G 5 HOH   26  226 343  HOH   HOH B . 
G 5 HOH   27  227 302  HOH   HOH B . 
G 5 HOH   28  228 82   HOH   HOH B . 
G 5 HOH   29  229 1140 HOH   HOH B . 
G 5 HOH   30  230 221  HOH   HOH B . 
G 5 HOH   31  231 41   HOH   HOH B . 
G 5 HOH   32  232 325  HOH   HOH B . 
G 5 HOH   33  233 143  HOH   HOH B . 
G 5 HOH   34  234 1278 HOH   HOH B . 
G 5 HOH   35  235 181  HOH   HOH B . 
G 5 HOH   36  236 172  HOH   HOH B . 
G 5 HOH   37  237 131  HOH   HOH B . 
G 5 HOH   38  238 231  HOH   HOH B . 
G 5 HOH   39  239 69   HOH   HOH B . 
G 5 HOH   40  240 276  HOH   HOH B . 
G 5 HOH   41  241 128  HOH   HOH B . 
G 5 HOH   42  242 60   HOH   HOH B . 
G 5 HOH   43  243 133  HOH   HOH B . 
G 5 HOH   44  244 110  HOH   HOH B . 
G 5 HOH   45  245 272  HOH   HOH B . 
G 5 HOH   46  246 127  HOH   HOH B . 
G 5 HOH   47  247 391  HOH   HOH B . 
G 5 HOH   48  248 300  HOH   HOH B . 
G 5 HOH   49  249 52   HOH   HOH B . 
G 5 HOH   50  250 1312 HOH   HOH B . 
G 5 HOH   51  251 1    HOH   HOH B . 
G 5 HOH   52  252 77   HOH   HOH B . 
G 5 HOH   53  253 150  HOH   HOH B . 
G 5 HOH   54  254 271  HOH   HOH B . 
G 5 HOH   55  255 30   HOH   HOH B . 
G 5 HOH   56  256 9    HOH   HOH B . 
G 5 HOH   57  257 287  HOH   HOH B . 
G 5 HOH   58  258 282  HOH   HOH B . 
G 5 HOH   59  259 144  HOH   HOH B . 
G 5 HOH   60  260 14   HOH   HOH B . 
G 5 HOH   61  261 72   HOH   HOH B . 
G 5 HOH   62  262 103  HOH   HOH B . 
G 5 HOH   63  263 20   HOH   HOH B . 
G 5 HOH   64  264 47   HOH   HOH B . 
G 5 HOH   65  265 81   HOH   HOH B . 
G 5 HOH   66  266 31   HOH   HOH B . 
G 5 HOH   67  267 242  HOH   HOH B . 
G 5 HOH   68  268 10   HOH   HOH B . 
G 5 HOH   69  269 347  HOH   HOH B . 
G 5 HOH   70  270 1106 HOH   HOH B . 
G 5 HOH   71  271 723  HOH   HOH B . 
G 5 HOH   72  272 243  HOH   HOH B . 
G 5 HOH   73  273 59   HOH   HOH B . 
G 5 HOH   74  274 117  HOH   HOH B . 
G 5 HOH   75  275 114  HOH   HOH B . 
G 5 HOH   76  276 84   HOH   HOH B . 
G 5 HOH   77  277 61   HOH   HOH B . 
G 5 HOH   78  278 11   HOH   HOH B . 
G 5 HOH   79  279 1277 HOH   HOH B . 
G 5 HOH   80  280 88   HOH   HOH B . 
G 5 HOH   81  281 175  HOH   HOH B . 
G 5 HOH   82  282 1066 HOH   HOH B . 
G 5 HOH   83  283 362  HOH   HOH B . 
G 5 HOH   84  284 416  HOH   HOH B . 
G 5 HOH   85  285 147  HOH   HOH B . 
G 5 HOH   86  286 43   HOH   HOH B . 
G 5 HOH   87  287 235  HOH   HOH B . 
G 5 HOH   88  288 13   HOH   HOH B . 
G 5 HOH   89  289 22   HOH   HOH B . 
G 5 HOH   90  290 106  HOH   HOH B . 
G 5 HOH   91  291 1305 HOH   HOH B . 
G 5 HOH   92  292 252  HOH   HOH B . 
G 5 HOH   93  293 89   HOH   HOH B . 
G 5 HOH   94  294 1285 HOH   HOH B . 
G 5 HOH   95  295 220  HOH   HOH B . 
G 5 HOH   96  296 160  HOH   HOH B . 
G 5 HOH   97  297 38   HOH   HOH B . 
G 5 HOH   98  298 32   HOH   HOH B . 
G 5 HOH   99  299 445  HOH   HOH B . 
G 5 HOH   100 300 99   HOH   HOH B . 
G 5 HOH   101 301 137  HOH   HOH B . 
G 5 HOH   102 302 311  HOH   HOH B . 
G 5 HOH   103 303 316  HOH   HOH B . 
G 5 HOH   104 304 112  HOH   HOH B . 
G 5 HOH   105 305 299  HOH   HOH B . 
G 5 HOH   106 306 216  HOH   HOH B . 
G 5 HOH   107 307 170  HOH   HOH B . 
G 5 HOH   108 308 101  HOH   HOH B . 
G 5 HOH   109 309 91   HOH   HOH B . 
G 5 HOH   110 310 177  HOH   HOH B . 
G 5 HOH   111 311 297  HOH   HOH B . 
G 5 HOH   112 312 23   HOH   HOH B . 
G 5 HOH   113 313 142  HOH   HOH B . 
G 5 HOH   114 314 215  HOH   HOH B . 
G 5 HOH   115 315 37   HOH   HOH B . 
G 5 HOH   116 316 1291 HOH   HOH B . 
G 5 HOH   117 317 118  HOH   HOH B . 
G 5 HOH   118 318 197  HOH   HOH B . 
G 5 HOH   119 319 341  HOH   HOH B . 
G 5 HOH   120 320 387  HOH   HOH B . 
G 5 HOH   121 321 48   HOH   HOH B . 
G 5 HOH   122 322 44   HOH   HOH B . 
G 5 HOH   123 323 100  HOH   HOH B . 
G 5 HOH   124 324 28   HOH   HOH B . 
G 5 HOH   125 325 704  HOH   HOH B . 
G 5 HOH   126 326 141  HOH   HOH B . 
G 5 HOH   127 327 717  HOH   HOH B . 
G 5 HOH   128 328 98   HOH   HOH B . 
G 5 HOH   129 329 29   HOH   HOH B . 
G 5 HOH   130 330 1294 HOH   HOH B . 
G 5 HOH   131 331 161  HOH   HOH B . 
G 5 HOH   132 332 207  HOH   HOH B . 
G 5 HOH   133 333 1126 HOH   HOH B . 
G 5 HOH   134 334 55   HOH   HOH B . 
G 5 HOH   135 335 635  HOH   HOH B . 
G 5 HOH   136 336 334  HOH   HOH B . 
G 5 HOH   137 337 65   HOH   HOH B . 
G 5 HOH   138 338 234  HOH   HOH B . 
G 5 HOH   139 339 1274 HOH   HOH B . 
G 5 HOH   140 340 87   HOH   HOH B . 
G 5 HOH   141 341 1293 HOH   HOH B . 
G 5 HOH   142 342 339  HOH   HOH B . 
G 5 HOH   143 343 182  HOH   HOH B . 
G 5 HOH   144 344 619  HOH   HOH B . 
G 5 HOH   145 345 960  HOH   HOH B . 
G 5 HOH   146 346 178  HOH   HOH B . 
G 5 HOH   147 347 90   HOH   HOH B . 
G 5 HOH   148 348 1280 HOH   HOH B . 
G 5 HOH   149 349 463  HOH   HOH B . 
G 5 HOH   150 350 1304 HOH   HOH B . 
G 5 HOH   151 351 1046 HOH   HOH B . 
G 5 HOH   152 352 191  HOH   HOH B . 
G 5 HOH   153 353 623  HOH   HOH B . 
G 5 HOH   154 354 304  HOH   HOH B . 
G 5 HOH   155 355 1077 HOH   HOH B . 
G 5 HOH   156 356 203  HOH   HOH B . 
G 5 HOH   157 357 335  HOH   HOH B . 
G 5 HOH   158 358 290  HOH   HOH B . 
G 5 HOH   159 359 541  HOH   HOH B . 
G 5 HOH   160 360 389  HOH   HOH B . 
G 5 HOH   161 361 718  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 283  HOH   HOH B . 
G 5 HOH   164 364 291  HOH   HOH B . 
G 5 HOH   165 365 479  HOH   HOH B . 
G 5 HOH   166 366 615  HOH   HOH B . 
G 5 HOH   167 367 373  HOH   HOH B . 
G 5 HOH   168 368 340  HOH   HOH B . 
G 5 HOH   169 369 898  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 190  HOH   HOH B . 
G 5 HOH   172 372 310  HOH   HOH B . 
G 5 HOH   173 373 1316 HOH   HOH B . 
G 5 HOH   174 374 418  HOH   HOH B . 
G 5 HOH   175 375 431  HOH   HOH B . 
G 5 HOH   176 376 1303 HOH   HOH B . 
G 5 HOH   177 377 149  HOH   HOH B . 
G 5 HOH   178 378 183  HOH   HOH B . 
G 5 HOH   179 379 1173 HOH   HOH B . 
G 5 HOH   180 380 1000 HOH   HOH B . 
G 5 HOH   181 381 1163 HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 176  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 470  HOH   HOH B . 
G 5 HOH   187 387 265  HOH   HOH B . 
G 5 HOH   188 388 350  HOH   HOH B . 
G 5 HOH   189 389 1298 HOH   HOH B . 
G 5 HOH   190 390 248  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   195 395 314  HOH   HOH B . 
G 5 HOH   196 396 274  HOH   HOH B . 
G 5 HOH   197 397 157  HOH   HOH B . 
G 5 HOH   198 398 566  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 321  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           7HFP 
_cell.length_a           88.750 
_cell.length_b           88.750 
_cell.length_c           39.454 
_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                         7HFP 
_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          7HFP 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.53 
_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   2023-10-07 
_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                     7HFP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            0.970 
_reflns.number_obs                   181049 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.054 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.300 
_reflns.B_iso_Wilson_estimate        11.560 
_reflns.pdbx_redundancy              6.100 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1109237 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.970 0.990  ? 26678 8511 ? 0.912 ? ? ? 3.100 ? 0.800  ? ? ? ? ? ? 94.900 1.092 0.579 0.609 
1 2 5.310 44.370 ? 8130  1197 ? 0.042 ? ? ? 6.800 ? 39.200 ? ? ? ? ? ? 99.900 0.046 0.018 0.998 
# 
_refine.entry_id                                 7HFP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9700 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6600 
_refine.ls_number_reflns_obs                     180956 
_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                          0.1441 
_refine.ls_R_factor_R_work                       0.1435 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1564 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  8713 
_refine.ls_number_reflns_R_work                  172243 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.7283 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                77.850 
_refine.B_iso_min                                8.530 
_refine.pdbx_overall_phase_error                 18.2900 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9700 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               3011 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           18.21 
_refine_hist.pdbx_B_iso_mean_solvent          30.89 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9700 0.9800  30 92.0000  5342 . 0.4317 0.4315 . 264 0.0000 5606 . 'X-RAY DIFFRACTION' 
0.9800 0.9900  30 99.0000  5622 . 0.3674 0.3769 . 299 0.0000 5921 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 100.0000 5742 . 0.3193 0.3262 . 275 0.0000 6017 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 100.0000 5750 . 0.2765 0.2866 . 284 0.0000 6034 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5750 . 0.2462 0.2474 . 249 0.0000 5999 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5730 . 0.2235 0.2269 . 316 0.0000 6046 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5670 . 0.2047 0.2102 . 326 0.0000 5996 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5719 . 0.1781 0.2105 . 292 0.0000 6011 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5741 . 0.1605 0.1929 . 286 0.0000 6027 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5716 . 0.1537 0.1821 . 284 0.0000 6000 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5802 . 0.1451 0.1526 . 281 0.0000 6083 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5685 . 0.1371 0.1566 . 276 0.0000 5961 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5752 . 0.1311 0.1480 . 299 0.0000 6051 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5788 . 0.1260 0.1631 . 292 0.0000 6080 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5662 . 0.1179 0.1419 . 303 0.0000 5965 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5740 . 0.1198 0.1312 . 284 0.0000 6024 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5761 . 0.1182 0.1280 . 273 0.0000 6034 . 'X-RAY DIFFRACTION' 
1.2800 1.3200  30 100.0000 5767 . 0.1189 0.1381 . 313 0.0000 6080 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5704 . 0.1222 0.1439 . 301 0.0000 6005 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5768 . 0.1207 0.1480 . 277 0.0000 6045 . 'X-RAY DIFFRACTION' 
1.4000 1.4500  30 100.0000 5789 . 0.1238 0.1419 . 279 0.0000 6068 . 'X-RAY DIFFRACTION' 
1.4500 1.5100  30 100.0000 5746 . 0.1191 0.1218 . 281 0.0000 6027 . 'X-RAY DIFFRACTION' 
1.5100 1.5800  30 100.0000 5759 . 0.1182 0.1296 . 304 0.0000 6063 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 5750 . 0.1199 0.1264 . 301 0.0000 6051 . 'X-RAY DIFFRACTION' 
1.6600 1.7600  30 100.0000 5823 . 0.1301 0.1302 . 257 0.0000 6080 . 'X-RAY DIFFRACTION' 
1.7600 1.9000  30 100.0000 5772 . 0.1333 0.1411 . 311 0.0000 6083 . 'X-RAY DIFFRACTION' 
1.9000 2.0900  30 100.0000 5801 . 0.1350 0.1403 . 294 0.0000 6095 . 'X-RAY DIFFRACTION' 
2.0900 2.3900  30 100.0000 5774 . 0.1366 0.1403 . 324 0.0000 6098 . 'X-RAY DIFFRACTION' 
2.3900 3.0100  30 100.0000 5840 . 0.1469 0.1626 . 294 0.0000 6134 . 'X-RAY DIFFRACTION' 
3.0100 44.3800 30 100.0000 5978 . 0.1487 0.1696 . 294 0.0000 6272 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFP 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004318' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFP 
_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 7HFP A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFP 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 7HFP SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFP MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFP SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFP 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 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.10   -131.95 
2 1 SER A 128 ? B 73.23   -5.45   
3 1 PHE A 156 ? B -92.26  57.03   
4 1 ASP A 157 ? B -170.06 106.90  
5 1 HIS B 86  ? ? 57.92   -127.95 
# 
_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 617 ? 5.83 . 
2 1 O ? A HOH 618 ? 5.97 . 
3 1 O ? A HOH 619 ? 5.98 . 
4 1 O ? A HOH 620 ? 7.57 . 
5 1 O ? B HOH 401 ? 6.64 . 
# 
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 
A1BBQ N2   N  Y N 1   
A1BBQ C3   C  N N 2   
A1BBQ C6   C  N N 3   
A1BBQ C9   C  Y N 4   
A1BBQ C12  C  Y N 5   
A1BBQ C1   C  N N 6   
A1BBQ C10  C  Y N 7   
A1BBQ C11  C  Y N 8   
A1BBQ C13  C  Y N 9   
A1BBQ C2   C  N N 10  
A1BBQ C4   C  N N 11  
A1BBQ C5   C  N N 12  
A1BBQ C7   C  N N 13  
A1BBQ C8   C  Y N 14  
A1BBQ N1   N  N N 15  
A1BBQ N3   N  Y N 16  
A1BBQ N4   N  Y N 17  
A1BBQ O1   O  N N 18  
A1BBQ O2   O  N N 19  
A1BBQ H12  H  N N 20  
A1BBQ H11  H  N N 21  
A1BBQ H15  H  N N 22  
A1BBQ H16  H  N N 23  
A1BBQ H1   H  N N 24  
A1BBQ H3   H  N N 25  
A1BBQ H2   H  N N 26  
A1BBQ H17  H  N N 27  
A1BBQ H4   H  N N 28  
A1BBQ H5   H  N N 29  
A1BBQ H7   H  N N 30  
A1BBQ H8   H  N N 31  
A1BBQ H9   H  N N 32  
A1BBQ H10  H  N N 33  
A1BBQ H13  H  N N 34  
A1BBQ H14  H  N N 35  
A1BBQ H18  H  N N 36  
A1BBQ H6   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TYR   N    N  N N 369 
TYR   CA   C  N S 370 
TYR   C    C  N N 371 
TYR   O    O  N N 372 
TYR   CB   C  N N 373 
TYR   CG   C  Y N 374 
TYR   CD1  C  Y N 375 
TYR   CD2  C  Y N 376 
TYR   CE1  C  Y N 377 
TYR   CE2  C  Y N 378 
TYR   CZ   C  Y N 379 
TYR   OH   O  N N 380 
TYR   OXT  O  N N 381 
TYR   H    H  N N 382 
TYR   H2   H  N N 383 
TYR   HA   H  N N 384 
TYR   HB2  H  N N 385 
TYR   HB3  H  N N 386 
TYR   HD1  H  N N 387 
TYR   HD2  H  N N 388 
TYR   HE1  H  N N 389 
TYR   HE2  H  N N 390 
TYR   HH   H  N N 391 
TYR   HXT  H  N N 392 
VAL   N    N  N N 393 
VAL   CA   C  N S 394 
VAL   C    C  N N 395 
VAL   O    O  N N 396 
VAL   CB   C  N N 397 
VAL   CG1  C  N N 398 
VAL   CG2  C  N N 399 
VAL   OXT  O  N N 400 
VAL   H    H  N N 401 
VAL   H2   H  N N 402 
VAL   HA   H  N N 403 
VAL   HB   H  N N 404 
VAL   HG11 H  N N 405 
VAL   HG12 H  N N 406 
VAL   HG13 H  N N 407 
VAL   HG21 H  N N 408 
VAL   HG22 H  N N 409 
VAL   HG23 H  N N 410 
VAL   HXT  H  N N 411 
# 
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 
A1BBQ O2  C6   sing N N 1   
A1BBQ O2  C5   sing N N 2   
A1BBQ C6  C7   sing N N 3   
A1BBQ C5  C4   sing N N 4   
A1BBQ C7  C3   sing N N 5   
A1BBQ C4  C3   sing N N 6   
A1BBQ C1  N1   sing N N 7   
A1BBQ C3  C2   sing N N 8   
A1BBQ C3  O1   sing N N 9   
A1BBQ C2  N1   sing N N 10  
A1BBQ N1  C8   sing N N 11  
A1BBQ C8  N2   doub Y N 12  
A1BBQ C8  C11  sing Y N 13  
A1BBQ C12 C11  sing Y N 14  
A1BBQ C12 C13  doub Y N 15  
A1BBQ N2  C9   sing Y N 16  
A1BBQ C11 C10  doub Y N 17  
A1BBQ C13 N4   sing Y N 18  
A1BBQ C9  N3   doub Y N 19  
A1BBQ C10 N4   sing Y N 20  
A1BBQ C10 N3   sing Y N 21  
A1BBQ C6  H12  sing N N 22  
A1BBQ C6  H11  sing N N 23  
A1BBQ C9  H15  sing N N 24  
A1BBQ C12 H16  sing N N 25  
A1BBQ C1  H1   sing N N 26  
A1BBQ C1  H3   sing N N 27  
A1BBQ C1  H2   sing N N 28  
A1BBQ C13 H17  sing N N 29  
A1BBQ C2  H4   sing N N 30  
A1BBQ C2  H5   sing N N 31  
A1BBQ C4  H7   sing N N 32  
A1BBQ C4  H8   sing N N 33  
A1BBQ C5  H9   sing N N 34  
A1BBQ C5  H10  sing N N 35  
A1BBQ C7  H13  sing N N 36  
A1BBQ C7  H14  sing N N 37  
A1BBQ N4  H18  sing N N 38  
A1BBQ O1  H6   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TYR   N   CA   sing N N 354 
TYR   N   H    sing N N 355 
TYR   N   H2   sing N N 356 
TYR   CA  C    sing N N 357 
TYR   CA  CB   sing N N 358 
TYR   CA  HA   sing N N 359 
TYR   C   O    doub N N 360 
TYR   C   OXT  sing N N 361 
TYR   CB  CG   sing N N 362 
TYR   CB  HB2  sing N N 363 
TYR   CB  HB3  sing N N 364 
TYR   CG  CD1  doub Y N 365 
TYR   CG  CD2  sing Y N 366 
TYR   CD1 CE1  sing Y N 367 
TYR   CD1 HD1  sing N N 368 
TYR   CD2 CE2  doub Y N 369 
TYR   CD2 HD2  sing N N 370 
TYR   CE1 CZ   doub Y N 371 
TYR   CE1 HE1  sing N N 372 
TYR   CE2 CZ   sing Y N 373 
TYR   CE2 HE2  sing N N 374 
TYR   CZ  OH   sing N N 375 
TYR   OH  HH   sing N N 376 
TYR   OXT HXT  sing N N 377 
VAL   N   CA   sing N N 378 
VAL   N   H    sing N N 379 
VAL   N   H2   sing N N 380 
VAL   CA  C    sing N N 381 
VAL   CA  CB   sing N N 382 
VAL   CA  HA   sing N N 383 
VAL   C   O    doub N N 384 
VAL   C   OXT  sing N N 385 
VAL   CB  CG1  sing N N 386 
VAL   CB  CG2  sing N N 387 
VAL   CB  HB   sing N N 388 
VAL   CG1 HG11 sing N N 389 
VAL   CG1 HG12 sing N N 390 
VAL   CG1 HG13 sing N N 391 
VAL   CG2 HG21 sing N N 392 
VAL   CG2 HG22 sing N N 393 
VAL   CG2 HG23 sing N N 394 
VAL   OXT HXT  sing N N 395 
# 
_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                    7HFP 
_atom_sites.fract_transf_matrix[1][1]   0.011268 
_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]   0.011268 
_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]   0.025346 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.644 -16.296 22.205  0.50 59.03 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.629 -16.023 22.299  0.50 59.08 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.664 -15.226 22.350  0.50 58.56 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.640 -14.965 22.464  0.50 58.56 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.312 -13.875 22.061  0.50 56.56 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.263 -13.609 22.150  0.50 56.49 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.418 -13.597 22.525  0.50 57.12 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.351 -13.292 22.632  0.50 57.07 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.012 -15.250 23.749  0.50 59.65 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.029 -14.986 23.881  0.50 59.63 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 16.984 -14.135 23.881  0.50 60.00 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 16.961 -13.910 24.017  0.50 59.97 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.369 -16.604 24.014  0.50 59.99 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.451 -16.360 24.192  0.50 59.97 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.961 -15.358 21.700  0.50 70.26 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.919 -15.111 21.836  0.50 70.25 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.696 -15.108 24.422  0.50 71.56 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.725 -14.801 24.531  0.50 71.54 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.466 -14.278 24.689  0.50 71.99 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.482 -14.045 24.850  0.50 71.96 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.444 -13.283 23.932  0.50 71.99 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.387 -13.039 24.019  0.50 71.96 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.400 -14.152 23.107  0.50 71.99 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.348 -13.978 23.269  0.50 71.96 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.908 -16.573 24.867  0.50 71.97 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.001 -16.325 25.051  0.50 71.95 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.736 -16.796 23.304  0.50 71.97 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.819 -16.601 23.497  0.50 71.95 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.059 -17.284 24.035  0.50 71.97 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.172 -17.008 24.224  0.50 71.95 ?  3   VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.622 -13.041 21.284  0.50 53.54 ?  4   ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.573 -12.814 21.333  0.50 53.38 ?  4   ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.067 -11.684 20.992  0.50 50.22 ?  4   ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.003 -11.462 20.998  0.50 49.95 ?  4   ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.917 -10.712 21.242  0.50 47.17 ?  4   ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 17.851 -10.491 21.246  0.50 46.78 ?  4   ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.797 -11.111 21.577  0.50 47.26 ?  4   ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.751 -10.886 21.644  0.50 46.89 ?  4   ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.631 -11.562 19.569  0.50 49.77 ?  4   ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.542 -11.374 19.563  0.50 49.51 ?  4   ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.639 -11.980 18.503  0.50 49.30 ?  4   ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.541 -11.844 18.529  0.50 49.03 ?  4   ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.480 -11.567 18.517  0.50 49.09 ?  4   ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.376 -11.446 18.546  0.50 48.83 ?  4   ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.095 -12.807 17.568  0.50 49.15 ?  4   ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.994 -12.699 17.619  0.50 48.89 ?  4   ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.876 -13.249 20.907  0.50 64.24 ?  4   ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.834 -13.046 20.956  0.50 64.04 ?  4   ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.781 -11.460 21.603  0.50 60.26 ?  4   ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.728 -11.219 21.589  0.50 59.93 ?  4   ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.875 -10.635 19.406  0.50 59.71 ?  4   ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.766 -10.449 19.367  0.50 59.39 ?  4   ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.414 -12.128 19.489  0.50 59.71 ?  4   ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.334 -11.928 19.488  0.50 59.39 ?  4   ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.575 -13.074 16.937  0.50 58.97 ?  4   ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.468 -12.996 17.007  0.50 58.65 ?  4   ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.912 -13.077 17.593  0.50 58.97 ?  4   ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.815 -12.957 17.642  0.50 58.65 ?  4   ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.200 -9.421  21.070  0.50 43.83 ?  5   SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.109 -9.206  21.001  0.50 43.32 ?  5   SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.279 -8.356  21.447  0.50 40.38 ?  5   SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.195 -8.137  21.383  0.50 39.75 ?  5   SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.429 -7.854  20.285  0.50 36.18 ?  5   SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.323 -7.645  20.232  0.50 35.33 ?  5   SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.753 -6.831  20.427  0.50 36.29 ?  5   SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.690 -6.592  20.360  0.50 35.40 ?  5   SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.044 -7.190  22.076  0.50 41.03 ?  5   SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 17.970 -6.963  21.987  0.50 40.46 ?  5   SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 19.056 -6.715  21.206  0.50 41.40 ?  5   SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 18.866 -6.402  21.044  0.50 40.87 ?  5   SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.932 -9.136  20.723  0.50 52.58 ?  5   SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 18.818 -8.930  20.601  0.50 51.97 ?  5   SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.678 -8.703  22.125  0.50 48.45 ?  5   SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.608 -8.475  22.076  0.50 47.68 ?  5   SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.420 -6.467  22.259  0.50 49.22 ?  5   SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.337 -6.282  22.269  0.50 48.54 ?  5   SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.452 -7.489  22.903  0.50 49.22 ?  5   SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.477 -7.278  22.750  0.50 48.54 ?  5   SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.465 -6.075  21.565  0.50 49.67 ?  5   SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.277 -5.754  21.389  0.50 49.03 ?  5   SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.452 -8.535  19.142  0.50 31.74 ?  6   PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.275 -8.368  19.117  0.50 30.66 ?  6   PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.544 -8.185  18.057  0.50 27.55 ?  6   PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.353 -8.011  18.047  0.50 26.27 ?  6   PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.120 -8.564  18.446  0.50 26.84 ?  6   PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 13.928 -8.385  18.447  0.50 25.56 ?  6   PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.872 -9.674  18.926  0.50 27.21 ?  6   PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 13.700 -9.406  19.100  0.50 26.14 ?  6   PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 15.950 -8.908  16.775  0.50 24.54 ?  6   PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.744 -8.724  16.754  0.50 23.19 ?  6   PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.220 -8.386  16.158  0.50 22.10 ?  6   PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.036 -8.232  16.154  0.50 20.91 ?  6   PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.224 -7.194  15.454  0.50 20.99 ?  6   PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.082 -7.030  15.469  0.50 19.97 ?  6   PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.405 -9.092  16.275  0.50 21.71 ?  6   PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.198 -8.976  16.268  0.50 20.62 ?  6   PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.388 -6.714  14.882  0.50 20.57 ?  6   PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.265 -6.575  14.915  0.50 19.59 ?  6   PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.571 -8.618  15.705  0.50 21.52 ?  6   PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.381 -8.530  15.713  0.50 20.55 ?  6   PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.562 -7.427  15.008  0.50 21.06 ?  6   PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.414 -7.327  15.036  0.50 20.15 ?  6   PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.979 -9.193  18.971  0.50 38.08 ?  6   PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 16.762 -9.061  18.957  0.50 36.78 ?  6   PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.577 -7.232  17.900  0.50 33.05 ?  6   PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.388 -7.057  17.896  0.50 31.51 ?  6   PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.082 -9.849  16.974  0.50 29.43 ?  6   PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 15.846 -9.672  16.935  0.50 27.82 ?  6   PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.241 -8.808  16.121  0.50 29.43 ?  6   PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.043 -8.589  16.097  0.50 27.82 ?  6   PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.436 -6.711  15.366  0.50 25.18 ?  6   PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.307 -6.520  15.384  0.50 23.95 ?  6   PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.415 -9.896  16.745  0.50 26.04 ?  6   PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.179 -9.788  16.725  0.50 24.73 ?  6   PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.381 -5.911  14.412  0.50 24.68 ?  6   PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.283 -5.764  14.457  0.50 23.49 ?  6   PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.361 -9.102  15.793  0.50 25.81 ?  6   PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.156 -9.037  15.799  0.50 24.65 ?  6   PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.346 -7.104  14.624  0.50 25.26 ?  6   PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.209 -7.022  14.664  0.50 24.17 ?  6   PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.181 -7.641  18.236  0.50 25.91 ?  7   SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 12.963 -7.550  18.055  0.50 24.31 ?  7   SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.815 -7.789  18.721  0.50 25.75 ?  7   SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 11.586 -7.696  18.511  0.50 24.16 ?  7   SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.823 -7.550  17.593  0.50 24.06 ?  7   SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.609 -7.464  17.366  0.50 22.39 ?  7   SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.023 -6.672  16.750  0.50 24.28 ?  7   SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 10.801 -6.567  16.543  0.50 22.23 ?  7   SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.540 -6.791  19.853  0.50 27.19 ?  7   SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.289 -6.698  19.640  0.50 25.87 ?  7   SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.186 -6.842  20.263  0.50 28.35 ?  7   SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 9.972  -6.858  20.136  0.50 27.21 ?  7   SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.318 -6.909  17.804  0.50 31.08 ?  7   SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.093 -6.884  17.524  0.50 29.16 ?  7   SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.686 -8.686  19.061  0.50 30.89 ?  7   SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.456 -8.592  18.851  0.50 28.98 ?  7   SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.105 -7.010  20.610  0.50 32.62 ?  7   SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 11.924 -6.843  20.362  0.50 31.03 ?  7   SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.744 -5.895  19.538  0.50 32.62 ?  7   SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 11.391 -5.795  19.295  0.50 31.03 ?  7   SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.051 -6.286  20.878  0.50 34.00 ?  7   SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 9.834  -6.304  20.753  0.50 32.64 ?  7   SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.751  -8.339  17.585  0.50 22.63 ?  8   GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.553  -8.275  17.326  0.50 21.14 ?  8   GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.658  -8.106  16.665  0.50 21.29 ?  8   GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.471  -8.054  16.386  0.50 20.08 ?  8   GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.862  -8.612  15.258  0.50 19.78 ?  8   GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.693  -8.572  14.983  0.50 18.54 ?  8   GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.118  -8.208  14.359  0.50 20.53 ?  8   GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 7.968  -8.168  14.067  0.50 19.14 ?  8   GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.641  -9.014  18.103  0.50 27.15 ?  8   GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.446  -8.954  17.839  0.50 25.36 ?  8   GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.861  -8.532  17.013  0.50 25.53 ?  8   GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.670  -8.472  16.737  0.50 24.09 ?  8   GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.490  -7.153  16.613  0.50 25.53 ?  8   GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.305  -7.100  16.324  0.50 24.09 ?  8   GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.843  -9.481  15.030  0.50 17.78 ?  9   TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.666  -9.455  14.778  0.50 16.59 ?  9   TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.096 -10.009 13.700  0.50 16.10 ?  9   TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 9.963  -9.982  13.454  0.50 15.07 ?  9   TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.239  -11.234 13.422  0.50 15.47 ?  9   TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.130  -11.225 13.153  0.50 14.48 ?  9   TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.965  -12.050 14.309  0.50 16.41 ?  9   TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 8.835  -12.034 14.038  0.50 15.59 ?  9   TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.569 -10.395 13.533  0.50 15.54 ?  9   TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.451 -10.331 13.344  0.50 14.85 ?  9   TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.480 -9.206  13.367  0.50 15.05 ?  9   TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.340 -9.122  13.162  0.50 14.96 ?  9   TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.800 -8.405  14.450  0.50 15.44 ?  9   TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.651 -8.297  14.233  0.50 15.40 ?  9   TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 13.006 -8.874  12.125  0.50 14.50 ?  9   TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 12.855 -8.797  11.915  0.50 14.44 ?  9   TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.619 -7.309  14.310  0.50 15.91 ?  9   TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.450 -7.181  14.069  0.50 15.87 ?  9   TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.828 -7.775  11.973  0.50 14.89 ?  9   TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.656 -7.685  11.739  0.50 14.50 ?  9   TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.125 -6.995  13.069  0.50 15.92 ?  9   TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 13.945 -6.879  12.817  0.50 15.13 ?  9   TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 14.943 -5.904  12.926  0.50 17.21 ?  9   TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.737 -5.772  12.638  0.50 15.72 ?  9   TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.371 -9.787  15.635  0.50 21.33 ?  9   TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.163 -9.773  15.402  0.50 19.90 ?  9   TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.888  -9.329  13.041  0.50 19.31 ?  9   TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.759  -9.309  12.787  0.50 18.07 ?  9   TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.862 -10.888 14.312  0.50 18.64 ?  9   TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.730 -10.785 14.153  0.50 17.80 ?  9   TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.654 -10.946 12.739  0.50 18.64 ?  9   TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.576 -10.908 12.577  0.50 17.80 ?  9   TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.446 -8.609  15.286  0.50 18.52 ?  9   TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.309 -8.495  15.078  0.50 18.47 ?  9   TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.804 -9.398  11.383  0.50 17.39 ?  9   TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.654 -9.334  11.184  0.50 17.31 ?  9   TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.819 -6.778  15.046  0.50 19.08 ?  9   TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.651 -6.638  14.798  0.50 19.03 ?  9   TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.182 -7.564  11.137  0.50 17.86 ?  9   TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 13.996 -7.480  10.897  0.50 17.39 ?  9   TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.048 -5.525  13.666  0.50 20.64 ?  9   TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 14.852 -5.379  13.370  0.50 18.85 ?  9   TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.835  -11.361 12.163  0.50 14.94 ?  10  LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.751  -11.365 11.883  0.50 14.28 ?  10  LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.251  -12.586 11.644  0.50 15.02 ?  10  LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.195  -12.612 11.374  0.50 13.90 ?  10  LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.388  -13.495 11.188  0.50 14.11 ?  10  LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.348  -13.539 11.025  0.50 13.56 ?  10  LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.366 -13.027 10.603  0.50 13.74 ?  10  LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.303 -13.124 10.363  0.50 13.26 ?  10  LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.348  -12.241 10.458  0.50 16.30 ?  10  LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.365  -12.340 10.117  0.50 14.50 ?  10  LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.567  -13.376 9.797   0.50 17.93 ?  10  LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.889  -13.545 9.294   0.50 15.30 ?  10  LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.458  -13.883 10.702  0.50 18.86 ?  10  LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.784  -14.271 10.025  0.50 15.67 ?  10  LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.014  -12.934 8.451   0.50 19.17 ?  10  LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 6.419  -13.121 7.923   0.50 16.07 ?  10  LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.903  -10.732 11.571  0.50 17.92 ?  10  LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.813  -10.748 11.285  0.50 17.12 ?  10  LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.725  -13.025 12.333  0.50 18.01 ?  10  LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.634  -13.032 12.044  0.50 16.67 ?  10  LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.700  -11.582 10.754  0.50 19.55 ?  10  LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.572  -11.850 10.382  0.50 17.39 ?  10  LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.908  -11.840 9.771   0.50 19.55 ?  10  LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.896  -11.788 9.523   0.50 17.39 ?  10  LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.177  -14.108 9.634   0.50 21.50 ?  10  LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.627  -14.169 9.177   0.50 18.35 ?  10  LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.030  -14.641 10.276  0.50 22.62 ?  10  LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 5.421  -14.953 9.442   0.50 18.79 ?  10  LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.843  -14.154 11.550  0.50 22.62 ?  10  LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 6.146  -14.679 10.830  0.50 18.79 ?  10  LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.814  -13.173 10.843  0.50 22.62 ?  10  LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 5.093  -13.635 10.260  0.50 18.79 ?  10  LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.524  -13.673 8.062   0.50 23.00 ?  10  LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 6.129  -13.908 7.438   0.50 19.28 ?  10  LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.428  -12.176 8.585   0.50 23.00 ?  10  LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.682  -12.502 8.029   0.50 19.28 ?  10  LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.754  -12.685 7.874   0.50 23.00 ?  10  LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 7.153  -12.693 7.462   0.50 19.28 ?  10  LEU   A HD23 1 
ATOM   237  N  N    . LYS   A 1 11  ? 9.265  -14.787 11.475  1.00 13.94 ?  11  LYS   A N    1 
ATOM   238  C  CA   . LYS   A 1 11  ? 10.284 -15.774 11.143  1.00 13.75 ?  11  LYS   A CA   1 
ATOM   239  C  C    . LYS   A 1 11  ? 9.943  -16.364 9.782   1.00 14.27 ?  11  LYS   A C    1 
ATOM   240  O  O    . LYS   A 1 11  ? 8.875  -16.953 9.615   1.00 16.27 ?  11  LYS   A O    1 
ATOM   241  C  CB   . LYS   A 1 11  ? 10.319 -16.853 12.227  1.00 14.24 ?  11  LYS   A CB   1 
ATOM   242  C  CG   . LYS   A 1 11  ? 11.389 -17.928 12.067  1.00 14.02 ?  11  LYS   A CG   1 
ATOM   243  C  CD   . LYS   A 1 11  ? 11.470 -18.776 13.340  1.00 14.70 ?  11  LYS   A CD   1 
ATOM   244  C  CE   . LYS   A 1 11  ? 12.489 -19.904 13.249  1.00 14.41 ?  11  LYS   A CE   1 
ATOM   245  N  NZ   . LYS   A 1 11  ? 13.845 -19.386 12.961  1.00 14.41 ?  11  LYS   A NZ   1 
ATOM   246  H  H    A LYS   A 1 11  ? 8.573  -15.124 11.868  0.50 16.71 ?  11  LYS   A H    1 
ATOM   247  H  H    B LYS   A 1 11  ? 8.626  -15.082 11.976  0.50 16.71 ?  11  LYS   A H    1 
ATOM   248  H  HA   . LYS   A 1 11  ? 11.150 -15.342 11.091  1.00 16.49 ?  11  LYS   A HA   1 
ATOM   249  H  HB2  . LYS   A 1 11  ? 10.471 -16.415 13.080  1.00 17.08 ?  11  LYS   A HB2  1 
ATOM   250  H  HB3  . LYS   A 1 11  ? 9.460  -17.296 12.239  1.00 17.08 ?  11  LYS   A HB3  1 
ATOM   251  H  HG2  . LYS   A 1 11  ? 11.163 -18.506 11.322  1.00 16.81 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  . LYS   A 1 11  ? 12.254 -17.508 11.920  1.00 16.81 ?  11  LYS   A HG3  1 
ATOM   253  H  HD2  . LYS   A 1 11  ? 11.721 -18.207 14.085  1.00 17.63 ?  11  LYS   A HD2  1 
ATOM   254  H  HD3  . LYS   A 1 11  ? 10.602 -19.176 13.507  1.00 17.63 ?  11  LYS   A HD3  1 
ATOM   255  H  HE2  . LYS   A 1 11  ? 12.526 -20.380 14.097  1.00 17.29 ?  11  LYS   A HE2  1 
ATOM   256  H  HE3  . LYS   A 1 11  ? 12.242 -20.512 12.537  1.00 17.29 ?  11  LYS   A HE3  1 
ATOM   257  H  HZ1  . LYS   A 1 11  ? 14.414 -20.062 12.853  1.00 17.28 ?  11  LYS   A HZ1  1 
ATOM   258  H  HZ2  . LYS   A 1 11  ? 13.831 -18.899 12.216  1.00 17.28 ?  11  LYS   A HZ2  1 
ATOM   259  H  HZ3  . LYS   A 1 11  ? 14.127 -18.877 13.634  1.00 17.28 ?  11  LYS   A HZ3  1 
ATOM   260  N  N    . LEU   A 1 12  ? 10.823 -16.194 8.801   1.00 13.23 ?  12  LEU   A N    1 
ATOM   261  C  CA   . LEU   A 1 12  ? 10.570 -16.775 7.485   1.00 13.70 ?  12  LEU   A CA   1 
ATOM   262  C  C    . LEU   A 1 12  ? 11.153 -18.175 7.350   1.00 13.24 ?  12  LEU   A C    1 
ATOM   263  O  O    . LEU   A 1 12  ? 10.525 -19.053 6.748   1.00 13.82 ?  12  LEU   A O    1 
ATOM   264  C  CB   . LEU   A 1 12  ? 11.143 -15.886 6.376   1.00 13.89 ?  12  LEU   A CB   1 
ATOM   265  C  CG   . LEU   A 1 12  ? 10.464 -14.534 6.156   1.00 15.23 ?  12  LEU   A CG   1 
ATOM   266  C  CD1  . LEU   A 1 12  ? 11.186 -13.767 5.057   1.00 16.06 ?  12  LEU   A CD1  1 
ATOM   267  C  CD2  . LEU   A 1 12  ? 8.985  -14.718 5.821   1.00 16.01 ?  12  LEU   A CD2  1 
ATOM   268  H  H    . LEU   A 1 12  ? 11.563 -15.752 8.865   1.00 15.86 ?  12  LEU   A H    1 
ATOM   269  H  HA   . LEU   A 1 12  ? 9.612  -16.838 7.352   1.00 16.42 ?  12  LEU   A HA   1 
ATOM   270  H  HB2  . LEU   A 1 12  ? 12.072 -15.706 6.583   1.00 16.66 ?  12  LEU   A HB2  1 
ATOM   271  H  HB3  . LEU   A 1 12  ? 11.087 -16.374 5.541   1.00 16.66 ?  12  LEU   A HB3  1 
ATOM   272  H  HG   . LEU   A 1 12  ? 10.522 -14.017 6.972   1.00 18.27 ?  12  LEU   A HG   1 
ATOM   273  H  HD11 . LEU   A 1 12  ? 10.735 -12.924 4.910   1.00 19.26 ?  12  LEU   A HD11 1 
ATOM   274  H  HD12 . LEU   A 1 12  ? 12.104 -13.609 5.336   1.00 19.26 ?  12  LEU   A HD12 1 
ATOM   275  H  HD13 . LEU   A 1 12  ? 11.178 -14.297 4.243   1.00 19.26 ?  12  LEU   A HD13 1 
ATOM   276  H  HD21 . LEU   A 1 12  ? 8.621  -13.874 5.517   1.00 19.20 ?  12  LEU   A HD21 1 
ATOM   277  H  HD22 . LEU   A 1 12  ? 8.899  -15.387 5.121   1.00 19.20 ?  12  LEU   A HD22 1 
ATOM   278  H  HD23 . LEU   A 1 12  ? 8.513  -15.015 6.617   1.00 19.20 ?  12  LEU   A HD23 1 
ATOM   279  N  N    . THR   A 1 13  ? 12.361 -18.379 7.872   1.00 13.28 ?  13  THR   A N    1 
ATOM   280  C  CA   . THR   A 1 13  ? 13.068 -19.650 7.798   1.00 13.16 ?  13  THR   A CA   1 
ATOM   281  C  C    . THR   A 1 13  ? 13.838 -19.854 9.098   1.00 13.13 ?  13  THR   A C    1 
ATOM   282  O  O    . THR   A 1 13  ? 13.739 -19.062 10.040  1.00 13.48 ?  13  THR   A O    1 
ATOM   283  C  CB   . THR   A 1 13  ? 14.041 -19.686 6.616   1.00 13.93 ?  13  THR   A CB   1 
ATOM   284  O  OG1  . THR   A 1 13  ? 15.089 -18.747 6.856   1.00 14.25 ?  13  THR   A OG1  1 
ATOM   285  C  CG2  . THR   A 1 13  ? 13.361 -19.359 5.296   1.00 14.94 ?  13  THR   A CG2  1 
ATOM   286  H  H    . THR   A 1 13  ? 12.809 -17.770 8.280   1.00 15.93 ?  13  THR   A H    1 
ATOM   287  H  HA   . THR   A 1 13  ? 12.428 -20.376 7.689   1.00 15.78 ?  13  THR   A HA   1 
ATOM   288  H  HB   . THR   A 1 13  ? 14.430 -20.570 6.545   1.00 16.71 ?  13  THR   A HB   1 
ATOM   289  H  HG1  . THR   A 1 13  ? 15.764 -19.136 7.168   1.00 17.08 ?  13  THR   A HG1  1 
ATOM   290  H  HG21 . THR   A 1 13  ? 13.995 -19.467 4.564   1.00 17.91 ?  13  THR   A HG21 1 
ATOM   291  H  HG22 . THR   A 1 13  ? 12.617 -19.962 5.154   1.00 17.91 ?  13  THR   A HG22 1 
ATOM   292  H  HG23 . THR   A 1 13  ? 13.040 -18.448 5.302   1.00 17.91 ?  13  THR   A HG23 1 
ATOM   293  N  N    . ASP   A 1 14  ? 14.640 -20.919 9.132   1.00 13.84 ?  14  ASP   A N    1 
ATOM   294  C  CA   . ASP   A 1 14  ? 15.485 -21.172 10.287  1.00 14.72 ?  14  ASP   A CA   1 
ATOM   295  C  C    . ASP   A 1 14  ? 16.313 -19.948 10.671  1.00 14.20 ?  14  ASP   A C    1 
ATOM   296  O  O    . ASP   A 1 14  ? 16.549 -19.712 11.860  1.00 15.11 ?  14  ASP   A O    1 
ATOM   297  C  CB   . ASP   A 1 14  ? 16.418 -22.341 9.989   1.00 18.26 ?  14  ASP   A CB   1 
ATOM   298  C  CG   . ASP   A 1 14  ? 17.347 -22.631 11.137  1.00 23.52 ?  14  ASP   A CG   1 
ATOM   299  O  OD1  . ASP   A 1 14  ? 16.849 -23.017 12.217  1.00 25.47 ?  14  ASP   A OD1  1 
ATOM   300  O  OD2  . ASP   A 1 14  ? 18.571 -22.458 10.964  1.00 27.35 -1 14  ASP   A OD2  1 
ATOM   301  H  H    . ASP   A 1 14  ? 14.720 -21.491 8.496   1.00 16.60 ?  14  ASP   A H    1 
ATOM   302  H  HA   . ASP   A 1 14  ? 14.932 -21.412 11.043  1.00 17.65 ?  14  ASP   A HA   1 
ATOM   303  H  HB2  . ASP   A 1 14  ? 15.882 -23.137 9.813   1.00 21.90 ?  14  ASP   A HB2  1 
ATOM   304  H  HB3  . ASP   A 1 14  ? 16.954 -22.133 9.204   1.00 21.90 ?  14  ASP   A HB3  1 
ATOM   305  N  N    . ASN   A 1 15  ? 16.752 -19.148 9.688   1.00 13.21 ?  15  ASN   A N    1 
ATOM   306  C  CA   . ASN   A 1 15  ? 17.734 -18.101 9.944   1.00 13.66 ?  15  ASN   A CA   1 
ATOM   307  C  C    . ASN   A 1 15  ? 17.358 -16.719 9.421   1.00 13.97 ?  15  ASN   A C    1 
ATOM   308  O  O    . ASN   A 1 15  ? 18.129 -15.779 9.645   1.00 15.14 ?  15  ASN   A O    1 
ATOM   309  C  CB   . ASN   A 1 15  ? 19.108 -18.493 9.373   1.00 13.41 ?  15  ASN   A CB   1 
ATOM   310  C  CG   . ASN   A 1 15  ? 19.100 -18.588 7.864   1.00 13.75 ?  15  ASN   A CG   1 
ATOM   311  O  OD1  . ASN   A 1 15  ? 18.404 -19.435 7.288   1.00 14.60 ?  15  ASN   A OD1  1 
ATOM   312  N  ND2  . ASN   A 1 15  ? 19.874 -17.717 7.208   1.00 14.03 ?  15  ASN   A ND2  1 
ATOM   313  H  H    . ASN   A 1 15  ? 16.486 -19.190 8.878   1.00 15.84 ?  15  ASN   A H    1 
ATOM   314  H  HA   . ASN   A 1 15  ? 17.845 -18.015 10.904  1.00 16.37 ?  15  ASN   A HA   1 
ATOM   315  H  HB2  . ASN   A 1 15  ? 19.763 -17.819 9.635   1.00 16.08 ?  15  ASN   A HB2  1 
ATOM   316  H  HB3  . ASN   A 1 15  ? 19.369 -19.357 9.727   1.00 16.08 ?  15  ASN   A HB3  1 
ATOM   317  H  HD21 . ASN   A 1 15  ? 19.898 -17.726 6.350   1.00 16.83 ?  15  ASN   A HD21 1 
ATOM   318  H  HD22 . ASN   A 1 15  ? 20.341 -17.134 7.643   1.00 16.83 ?  15  ASN   A HD22 1 
ATOM   319  N  N    . VAL   A 1 16  ? 16.226 -16.560 8.734   1.00 13.59 ?  16  VAL   A N    1 
ATOM   320  C  CA   . VAL   A 1 16  ? 15.827 -15.281 8.156   1.00 13.18 ?  16  VAL   A CA   1 
ATOM   321  C  C    . VAL   A 1 16  ? 14.554 -14.795 8.833   1.00 12.91 ?  16  VAL   A C    1 
ATOM   322  O  O    . VAL   A 1 16  ? 13.556 -15.525 8.914   1.00 13.44 ?  16  VAL   A O    1 
ATOM   323  C  CB   . VAL   A 1 16  ? 15.646 -15.365 6.630   1.00 13.72 ?  16  VAL   A CB   1 
ATOM   324  C  CG1  . VAL   A 1 16  ? 15.211 -14.012 6.063   1.00 14.34 ?  16  VAL   A CG1  1 
ATOM   325  C  CG2  . VAL   A 1 16  ? 16.929 -15.830 5.961   1.00 14.30 ?  16  VAL   A CG2  1 
ATOM   326  H  H    . VAL   A 1 16  ? 15.664 -17.197 8.594   1.00 16.29 ?  16  VAL   A H    1 
ATOM   327  H  HA   . VAL   A 1 16  ? 16.525 -14.632 8.334   1.00 15.81 ?  16  VAL   A HA   1 
ATOM   328  H  HB   . VAL   A 1 16  ? 14.959 -16.013 6.431   1.00 16.45 ?  16  VAL   A HB   1 
ATOM   329  H  HG11 . VAL   A 1 16  ? 15.291 -14.040 5.097   1.00 17.20 ?  16  VAL   A HG11 1 
ATOM   330  H  HG12 . VAL   A 1 16  ? 14.289 -13.850 6.313   1.00 17.20 ?  16  VAL   A HG12 1 
ATOM   331  H  HG13 . VAL   A 1 16  ? 15.783 -13.319 6.423   1.00 17.20 ?  16  VAL   A HG13 1 
ATOM   332  H  HG21 . VAL   A 1 16  ? 16.804 -15.826 5.000   1.00 17.14 ?  16  VAL   A HG21 1 
ATOM   333  H  HG22 . VAL   A 1 16  ? 17.652 -15.228 6.202   1.00 17.14 ?  16  VAL   A HG22 1 
ATOM   334  H  HG23 . VAL   A 1 16  ? 17.138 -16.729 6.263   1.00 17.14 ?  16  VAL   A HG23 1 
ATOM   335  N  N    . TYR   A 1 17  ? 14.590 -13.537 9.275   1.00 12.73 ?  17  TYR   A N    1 
ATOM   336  C  CA   . TYR   A 1 17  ? 13.502 -12.853 9.961   1.00 12.72 ?  17  TYR   A CA   1 
ATOM   337  C  C    . TYR   A 1 17  ? 13.223 -11.542 9.238   1.00 13.02 ?  17  TYR   A C    1 
ATOM   338  O  O    . TYR   A 1 17  ? 14.124 -10.971 8.624   1.00 12.91 ?  17  TYR   A O    1 
ATOM   339  C  CB   . TYR   A 1 17  ? 13.930 -12.563 11.400  1.00 13.02 ?  17  TYR   A CB   1 
ATOM   340  C  CG   . TYR   A 1 17  ? 14.154 -13.814 12.227  1.00 14.03 ?  17  TYR   A CG   1 
ATOM   341  C  CD1  . TYR   A 1 17  ? 15.347 -14.531 12.159  1.00 15.13 ?  17  TYR   A CD1  1 
ATOM   342  C  CD2  . TYR   A 1 17  ? 13.156 -14.295 13.066  1.00 14.65 ?  17  TYR   A CD2  1 
ATOM   343  C  CE1  . TYR   A 1 17  ? 15.533 -15.698 12.910  1.00 15.78 ?  17  TYR   A CE1  1 
ATOM   344  C  CE2  . TYR   A 1 17  ? 13.337 -15.453 13.820  1.00 15.29 ?  17  TYR   A CE2  1 
ATOM   345  C  CZ   . TYR   A 1 17  ? 14.522 -16.149 13.741  1.00 16.08 ?  17  TYR   A CZ   1 
ATOM   346  O  OH   . TYR   A 1 17  ? 14.685 -17.291 14.496  1.00 17.07 ?  17  TYR   A OH   1 
ATOM   347  H  H    . TYR   A 1 17  ? 15.285 -13.036 9.171   1.00 15.26 ?  17  TYR   A H    1 
ATOM   348  H  HA   . TYR   A 1 17  ? 12.706 -13.403 9.953   1.00 15.25 ?  17  TYR   A HA   1 
ATOM   349  H  HB2  . TYR   A 1 17  ? 14.759 -12.067 11.386  1.00 15.61 ?  17  TYR   A HB2  1 
ATOM   350  H  HB3  . TYR   A 1 17  ? 13.239 -12.050 11.829  1.00 15.61 ?  17  TYR   A HB3  1 
ATOM   351  H  HD1  . TYR   A 1 17  ? 16.031 -14.237 11.597  1.00 18.14 ?  17  TYR   A HD1  1 
ATOM   352  H  HD2  . TYR   A 1 17  ? 12.351 -13.843 13.124  1.00 17.57 ?  17  TYR   A HD2  1 
ATOM   353  H  HE1  . TYR   A 1 17  ? 16.344 -16.163 12.860  1.00 18.92 ?  17  TYR   A HE1  1 
ATOM   354  H  HE2  . TYR   A 1 17  ? 12.660 -15.756 14.379  1.00 18.34 ?  17  TYR   A HE2  1 
ATOM   355  H  HH   . TYR   A 1 17  ? 13.959 -17.497 14.862  1.00 20.48 ?  17  TYR   A HH   1 
ATOM   356  N  N    A ILE   A 1 18  ? 11.997 -11.028 9.370   0.50 13.05 ?  18  ILE   A N    1 
ATOM   357  N  N    B ILE   A 1 18  ? 11.976 -11.069 9.273   0.50 13.04 ?  18  ILE   A N    1 
ATOM   358  C  CA   A ILE   A 1 18  ? 11.592 -9.814  8.665   0.50 13.02 ?  18  ILE   A CA   1 
ATOM   359  C  CA   B ILE   A 1 18  ? 11.585 -9.914  8.462   0.50 13.08 ?  18  ILE   A CA   1 
ATOM   360  C  C    A ILE   A 1 18  ? 10.650 -8.980  9.526   0.50 13.01 ?  18  ILE   A C    1 
ATOM   361  C  C    B ILE   A 1 18  ? 10.571 -9.056  9.209   0.50 13.31 ?  18  ILE   A C    1 
ATOM   362  O  O    A ILE   A 1 18  ? 9.864  -9.509  10.319  0.50 13.27 ?  18  ILE   A O    1 
ATOM   363  O  O    B ILE   A 1 18  ? 9.715  -9.574  9.933   0.50 13.32 ?  18  ILE   A O    1 
ATOM   364  C  CB   A ILE   A 1 18  ? 10.963 -10.169 7.300   0.50 13.46 ?  18  ILE   A CB   1 
ATOM   365  C  CB   B ILE   A 1 18  ? 11.078 -10.357 7.070   0.50 12.85 ?  18  ILE   A CB   1 
ATOM   366  C  CG1  A ILE   A 1 18  ? 10.889 -8.940  6.394   0.50 14.38 ?  18  ILE   A CG1  1 
ATOM   367  C  CG1  B ILE   A 1 18  ? 10.949 -9.162  6.123   0.50 12.98 ?  18  ILE   A CG1  1 
ATOM   368  C  CG2  A ILE   A 1 18  ? 9.602  -10.838 7.486   0.50 13.86 ?  18  ILE   A CG2  1 
ATOM   369  C  CG2  B ILE   A 1 18  ? 9.768  -11.126 7.187   0.50 12.63 ?  18  ILE   A CG2  1 
ATOM   370  C  CD1  A ILE   A 1 18  ? 10.682 -9.298  4.941   0.50 16.09 ?  18  ILE   A CD1  1 
ATOM   371  C  CD1  B ILE   A 1 18  ? 10.730 -9.574  4.680   0.50 14.20 ?  18  ILE   A CD1  1 
ATOM   372  H  H    A ILE   A 1 18  ? 11.386 -11.377 9.860   0.50 15.64 ?  18  ILE   A H    1 
ATOM   373  H  H    B ILE   A 1 18  ? 11.348 -11.406 9.753   0.50 15.64 ?  18  ILE   A H    1 
ATOM   374  H  HA   A ILE   A 1 18  ? 12.388 -9.286  8.492   0.50 15.61 ?  18  ILE   A HA   1 
ATOM   375  H  HA   B ILE   A 1 18  ? 12.366 -9.371  8.321   0.50 15.68 ?  18  ILE   A HA   1 
ATOM   376  H  HB   A ILE   A 1 18  ? 11.543 -10.809 6.870   0.50 16.14 ?  18  ILE   A HB   1 
ATOM   377  H  HB   B ILE   A 1 18  ? 11.736 -10.962 6.690   0.50 15.41 ?  18  ILE   A HB   1 
ATOM   378  H  HG12 A ILE   A 1 18  ? 10.146 -8.383  6.673   0.50 17.24 ?  18  ILE   A HG12 1 
ATOM   379  H  HG12 B ILE   A 1 18  ? 10.192 -8.624  6.398   0.50 15.57 ?  18  ILE   A HG12 1 
ATOM   380  H  HG13 A ILE   A 1 18  ? 11.720 -8.445  6.465   0.50 17.24 ?  18  ILE   A HG13 1 
ATOM   381  H  HG13 B ILE   A 1 18  ? 11.763 -8.641  6.164   0.50 15.57 ?  18  ILE   A HG13 1 
ATOM   382  H  HG21 A ILE   A 1 18  ? 9.312  -11.196 6.632   0.50 16.62 ?  18  ILE   A HG21 1 
ATOM   383  H  HG21 B ILE   A 1 18  ? 9.557  -11.523 6.326   0.50 15.15 ?  18  ILE   A HG21 1 
ATOM   384  H  HG22 A ILE   A 1 18  ? 9.691  -11.554 8.133   0.50 16.62 ?  18  ILE   A HG22 1 
ATOM   385  H  HG22 B ILE   A 1 18  ? 9.870  -11.821 7.854   0.50 15.15 ?  18  ILE   A HG22 1 
ATOM   386  H  HG23 A ILE   A 1 18  ? 8.964  -10.180 7.803   0.50 16.62 ?  18  ILE   A HG23 1 
ATOM   387  H  HG23 B ILE   A 1 18  ? 9.065  -10.513 7.449   0.50 15.15 ?  18  ILE   A HG23 1 
ATOM   388  H  HD11 A ILE   A 1 18  ? 10.665 -8.485  4.413   0.50 19.30 ?  18  ILE   A HD11 1 
ATOM   389  H  HD11 B ILE   A 1 18  ? 10.732 -8.777  4.125   0.50 17.03 ?  18  ILE   A HD11 1 
ATOM   390  H  HD12 A ILE   A 1 18  ? 11.415 -9.865  4.648   0.50 19.30 ?  18  ILE   A HD12 1 
ATOM   391  H  HD12 B ILE   A 1 18  ? 11.446 -10.167 4.410   0.50 17.03 ?  18  ILE   A HD12 1 
ATOM   392  H  HD13 A ILE   A 1 18  ? 9.841  -9.772  4.847   0.50 19.30 ?  18  ILE   A HD13 1 
ATOM   393  H  HD13 B ILE   A 1 18  ? 9.876  -10.026 4.606   0.50 17.03 ?  18  ILE   A HD13 1 
ATOM   394  N  N    A LYS   A 1 19  ? 10.719 -7.659  9.342   0.50 13.35 ?  19  LYS   A N    1 
ATOM   395  N  N    B LYS   A 1 19  ? 10.667 -7.739  9.020   0.50 13.37 ?  19  LYS   A N    1 
ATOM   396  C  CA   A LYS   A 1 19  ? 9.928  -6.719  10.125  0.50 14.31 ?  19  LYS   A CA   1 
ATOM   397  C  CA   B LYS   A 1 19  ? 9.806  -6.788  9.710   0.50 13.63 ?  19  LYS   A CA   1 
ATOM   398  C  C    A LYS   A 1 19  ? 9.718  -5.452  9.310   0.50 14.41 ?  19  LYS   A C    1 
ATOM   399  C  C    B LYS   A 1 19  ? 9.617  -5.551  8.841   0.50 13.06 ?  19  LYS   A C    1 
ATOM   400  O  O    A LYS   A 1 19  ? 10.627 -5.006  8.608   0.50 14.15 ?  19  LYS   A O    1 
ATOM   401  O  O    B LYS   A 1 19  ? 10.523 -5.147  8.107   0.50 12.21 ?  19  LYS   A O    1 
ATOM   402  C  CB   A LYS   A 1 19  ? 10.664 -6.380  11.427  0.50 14.95 ?  19  LYS   A CB   1 
ATOM   403  C  CB   B LYS   A 1 19  ? 10.441 -6.374  11.043  0.50 14.04 ?  19  LYS   A CB   1 
ATOM   404  C  CG   A LYS   A 1 19  ? 9.953  -5.427  12.363  0.50 16.08 ?  19  LYS   A CG   1 
ATOM   405  C  CG   B LYS   A 1 19  ? 9.626  -5.419  11.912  0.50 14.83 ?  19  LYS   A CG   1 
ATOM   406  C  CD   A LYS   A 1 19  ? 10.868 -5.116  13.535  0.50 16.35 ?  19  LYS   A CD   1 
ATOM   407  C  CD   B LYS   A 1 19  ? 10.392 -5.123  13.201  0.50 15.56 ?  19  LYS   A CD   1 
ATOM   408  C  CE   A LYS   A 1 19  ? 10.198 -4.244  14.573  0.50 17.05 ?  19  LYS   A CE   1 
ATOM   409  C  CE   B LYS   A 1 19  ? 9.659  -4.165  14.122  0.50 16.01 ?  19  LYS   A CE   1 
ATOM   410  N  NZ   A LYS   A 1 19  ? 11.103 -4.035  15.736  0.50 17.36 ?  19  LYS   A NZ   1 
ATOM   411  N  NZ   B LYS   A 1 19  ? 10.521 -3.793  15.282  0.50 16.22 ?  19  LYS   A NZ   1 
ATOM   412  H  H    A LYS   A 1 19  ? 11.226 -7.278  8.756   0.50 16.01 ?  19  LYS   A H    1 
ATOM   413  H  H    B LYS   A 1 19  ? 11.240 -7.383  8.492   0.50 16.03 ?  19  LYS   A H    1 
ATOM   414  H  HA   A LYS   A 1 19  ? 9.067  -7.106  10.339  0.50 17.16 ?  19  LYS   A HA   1 
ATOM   415  H  HA   B LYS   A 1 19  ? 8.942  -7.206  9.882   0.50 16.34 ?  19  LYS   A HA   1 
ATOM   416  H  HB2  A LYS   A 1 19  ? 10.810 -7.205  11.917  0.50 17.93 ?  19  LYS   A HB2  1 
ATOM   417  H  HB2  B LYS   A 1 19  ? 10.597 -7.175  11.565  0.50 16.84 ?  19  LYS   A HB2  1 
ATOM   418  H  HB3  A LYS   A 1 19  ? 11.521 -5.984  11.202  0.50 17.93 ?  19  LYS   A HB3  1 
ATOM   419  H  HB3  B LYS   A 1 19  ? 11.285 -5.944  10.848  0.50 16.84 ?  19  LYS   A HB3  1 
ATOM   420  H  HG2  A LYS   A 1 19  ? 9.753  -4.599  11.899  0.50 19.28 ?  19  LYS   A HG2  1 
ATOM   421  H  HG2  B LYS   A 1 19  ? 9.489  -4.582  11.439  0.50 17.79 ?  19  LYS   A HG2  1 
ATOM   422  H  HG3  A LYS   A 1 19  ? 9.144  -5.840  12.699  0.50 19.28 ?  19  LYS   A HG3  1 
ATOM   423  H  HG3  B LYS   A 1 19  ? 8.778  -5.824  12.143  0.50 17.79 ?  19  LYS   A HG3  1 
ATOM   424  H  HD2  A LYS   A 1 19  ? 11.129 -5.948  13.962  0.50 19.61 ?  19  LYS   A HD2  1 
ATOM   425  H  HD2  B LYS   A 1 19  ? 10.529 -5.955  13.685  0.50 18.66 ?  19  LYS   A HD2  1 
ATOM   426  H  HD3  A LYS   A 1 19  ? 11.654 -4.650  13.209  0.50 19.61 ?  19  LYS   A HD3  1 
ATOM   427  H  HD3  B LYS   A 1 19  ? 11.249 -4.727  12.979  0.50 18.66 ?  19  LYS   A HD3  1 
ATOM   428  H  HE2  A LYS   A 1 19  ? 9.991  -3.380  14.184  0.50 20.45 ?  19  LYS   A HE2  1 
ATOM   429  H  HE2  B LYS   A 1 19  ? 9.435  -3.356  13.635  0.50 19.20 ?  19  LYS   A HE2  1 
ATOM   430  H  HE3  A LYS   A 1 19  ? 9.389  -4.677  14.886  0.50 20.45 ?  19  LYS   A HE3  1 
ATOM   431  H  HE3  B LYS   A 1 19  ? 8.856  -4.590  14.462  0.50 19.20 ?  19  LYS   A HE3  1 
ATOM   432  H  HZ1  A LYS   A 1 19  ? 10.689 -3.554  16.359  0.50 20.82 ?  19  LYS   A HZ1  1 
ATOM   433  H  HZ1  B LYS   A 1 19  ? 10.088 -3.231  15.818  0.50 19.46 ?  19  LYS   A HZ1  1 
ATOM   434  H  HZ2  A LYS   A 1 19  ? 11.337 -4.820  16.083  0.50 20.82 ?  19  LYS   A HZ2  1 
ATOM   435  H  HZ2  B LYS   A 1 19  ? 10.742 -4.522  15.744  0.50 19.46 ?  19  LYS   A HZ2  1 
ATOM   436  H  HZ3  A LYS   A 1 19  ? 11.836 -3.603  15.476  0.50 20.82 ?  19  LYS   A HZ3  1 
ATOM   437  H  HZ3  B LYS   A 1 19  ? 11.267 -3.400  14.993  0.50 19.46 ?  19  LYS   A HZ3  1 
ATOM   438  N  N    A ASN   A 1 20  ? 8.518  -4.879  9.392   0.50 15.36 ?  20  ASN   A N    1 
ATOM   439  N  N    B ASN   A 1 20  ? 8.428  -4.957  8.926   0.50 13.73 ?  20  ASN   A N    1 
ATOM   440  C  CA   A ASN   A 1 20  ? 8.272  -3.556  8.826   0.50 16.20 ?  20  ASN   A CA   1 
ATOM   441  C  CA   B ASN   A 1 20  ? 8.175  -3.648  8.325   0.50 14.78 ?  20  ASN   A CA   1 
ATOM   442  C  C    A ASN   A 1 20  ? 8.885  -2.541  9.782   0.50 16.05 ?  20  ASN   A C    1 
ATOM   443  C  C    B ASN   A 1 20  ? 8.762  -2.602  9.264   0.50 14.94 ?  20  ASN   A C    1 
ATOM   444  O  O    A ASN   A 1 20  ? 8.387  -2.350  10.896  0.50 16.72 ?  20  ASN   A O    1 
ATOM   445  O  O    B ASN   A 1 20  ? 8.182  -2.299  10.309  0.50 16.04 ?  20  ASN   A O    1 
ATOM   446  C  CB   A ASN   A 1 20  ? 6.773  -3.327  8.635   0.50 17.44 ?  20  ASN   A CB   1 
ATOM   447  C  CB   B ASN   A 1 20  ? 6.678  -3.434  8.122   0.50 15.81 ?  20  ASN   A CB   1 
ATOM   448  C  CG   A ASN   A 1 20  ? 6.435  -1.914  8.160   0.50 19.17 ?  20  ASN   A CG   1 
ATOM   449  C  CG   B ASN   A 1 20  ? 6.324  -1.980  7.858   0.50 17.46 ?  20  ASN   A CG   1 
ATOM   450  O  OD1  A ASN   A 1 20  ? 5.422  -1.336  8.572   0.50 21.33 ?  20  ASN   A OD1  1 
ATOM   451  O  OD1  B ASN   A 1 20  ? 5.453  -1.408  8.524   0.50 20.10 ?  20  ASN   A OD1  1 
ATOM   452  N  ND2  A ASN   A 1 20  ? 7.275  -1.357  7.288   0.50 19.58 ?  20  ASN   A ND2  1 
ATOM   453  N  ND2  B ASN   A 1 20  ? 6.993  -1.376  6.882   0.50 17.67 ?  20  ASN   A ND2  1 
ATOM   454  H  H    A ASN   A 1 20  ? 7.834  -5.234  9.770   0.50 18.42 ?  20  ASN   A H    1 
ATOM   455  H  H    B ASN   A 1 20  ? 7.743  -5.305  9.324   0.50 16.47 ?  20  ASN   A H    1 
ATOM   456  H  HA   A ASN   A 1 20  ? 8.716  -3.483  7.967   0.50 19.43 ?  20  ASN   A HA   1 
ATOM   457  H  HA   B ASN   A 1 20  ? 8.622  -3.595  7.466   0.50 17.73 ?  20  ASN   A HA   1 
ATOM   458  H  HB2  A ASN   A 1 20  ? 6.446  -3.948  7.970   0.50 20.91 ?  20  ASN   A HB2  1 
ATOM   459  H  HB2  B ASN   A 1 20  ? 6.385  -3.954  7.361   0.50 18.96 ?  20  ASN   A HB2  1 
ATOM   460  H  HB3  A ASN   A 1 20  ? 6.325  -3.474  9.479   0.50 20.91 ?  20  ASN   A HB3  1 
ATOM   461  H  HB3  B ASN   A 1 20  ? 6.210  -3.720  8.923   0.50 18.96 ?  20  ASN   A HB3  1 
ATOM   462  H  HD21 A ASN   A 1 20  ? 7.123  -0.564  6.996   0.50 23.49 ?  20  ASN   A HD21 1 
ATOM   463  H  HD21 B ASN   A 1 20  ? 6.837  -0.552  6.704   0.50 21.20 ?  20  ASN   A HD21 1 
ATOM   464  H  HD22 A ASN   A 1 20  ? 7.968  -1.788  7.015   0.50 23.49 ?  20  ASN   A HD22 1 
ATOM   465  H  HD22 B ASN   A 1 20  ? 7.586  -1.811  6.432   0.50 21.20 ?  20  ASN   A HD22 1 
ATOM   466  N  N    A ALA   A 1 21  ? 9.989  -1.916  9.373   0.50 15.58 ?  21  ALA   A N    1 
ATOM   467  N  N    B ALA   A 1 21  ? 9.926  -2.055  8.906   0.50 14.69 ?  21  ALA   A N    1 
ATOM   468  C  CA   A ALA   A 1 21  ? 10.684 -1.001  10.264  0.50 15.94 ?  21  ALA   A CA   1 
ATOM   469  C  CA   B ALA   A 1 21  ? 10.618 -1.132  9.797   0.50 14.70 ?  21  ALA   A CA   1 
ATOM   470  C  C    A ALA   A 1 21  ? 11.660 -0.145  9.475   0.50 15.59 ?  21  ALA   A C    1 
ATOM   471  C  C    B ALA   A 1 21  ? 11.631 -0.304  9.020   0.50 13.62 ?  21  ALA   A C    1 
ATOM   472  O  O    A ALA   A 1 21  ? 12.130 -0.538  8.404   0.50 15.72 ?  21  ALA   A O    1 
ATOM   473  O  O    B ALA   A 1 21  ? 12.077 -0.684  7.933   0.50 13.90 ?  21  ALA   A O    1 
ATOM   474  C  CB   A ALA   A 1 21  ? 11.436 -1.760  11.361  0.50 16.92 ?  21  ALA   A CB   1 
ATOM   475  C  CB   B ALA   A 1 21  ? 11.323 -1.877  10.937  0.50 15.78 ?  21  ALA   A CB   1 
ATOM   476  H  H    A ALA   A 1 21  ? 10.353 -2.006  8.595   0.50 18.68 ?  21  ALA   A H    1 
ATOM   477  H  H    B ALA   A 1 21  ? 10.325 -2.204  8.157   0.50 17.62 ?  21  ALA   A H    1 
ATOM   478  H  HA   A ALA   A 1 21  ? 10.039 -0.411  10.685  0.50 19.12 ?  21  ALA   A HA   1 
ATOM   479  H  HA   B ALA   A 1 21  ? 9.961  -0.534  10.188  0.50 17.63 ?  21  ALA   A HA   1 
ATOM   480  H  HB1  A ALA   A 1 21  ? 11.819 -1.117  11.972  0.50 20.30 ?  21  ALA   A HB1  1 
ATOM   481  H  HB1  B ALA   A 1 21  ? 11.762 -1.229  11.508  0.50 18.93 ?  21  ALA   A HB1  1 
ATOM   482  H  HB2  A ALA   A 1 21  ? 10.805 -2.331  11.829  0.50 20.30 ?  21  ALA   A HB2  1 
ATOM   483  H  HB2  B ALA   A 1 21  ? 10.660 -2.372  11.451  0.50 18.93 ?  21  ALA   A HB2  1 
ATOM   484  H  HB3  A ALA   A 1 21  ? 12.129 -2.297  10.951  0.50 20.30 ?  21  ALA   A HB3  1 
ATOM   485  H  HB3  B ALA   A 1 21  ? 11.972 -2.489  10.562  0.50 18.93 ?  21  ALA   A HB3  1 
ATOM   486  N  N    A ASP   A 1 22  ? 11.946 1.033   10.027  0.50 15.32 ?  22  ASP   A N    1 
ATOM   487  N  N    B ASP   A 1 22  ? 11.980 0.839   9.610   0.50 13.33 ?  22  ASP   A N    1 
ATOM   488  C  CA   A ASP   A 1 22  ? 12.999 1.908   9.531   0.50 14.77 ?  22  ASP   A CA   1 
ATOM   489  C  CA   B ASP   A 1 22  ? 13.094 1.665   9.159   0.50 13.11 ?  22  ASP   A CA   1 
ATOM   490  C  C    A ASP   A 1 22  ? 14.331 1.429   10.098  0.50 13.64 ?  22  ASP   A C    1 
ATOM   491  C  C    B ASP   A 1 22  ? 14.377 1.129   9.790   0.50 12.02 ?  22  ASP   A C    1 
ATOM   492  O  O    A ASP   A 1 22  ? 14.530 1.448   11.318  0.50 13.69 ?  22  ASP   A O    1 
ATOM   493  O  O    B ASP   A 1 22  ? 14.497 1.086   11.019  0.50 12.50 ?  22  ASP   A O    1 
ATOM   494  C  CB   A ASP   A 1 22  ? 12.705 3.331   10.003  0.50 15.58 ?  22  ASP   A CB   1 
ATOM   495  C  CB   B ASP   A 1 22  ? 12.848 3.103   9.612   0.50 14.41 ?  22  ASP   A CB   1 
ATOM   496  C  CG   A ASP   A 1 22  ? 13.731 4.343   9.520   0.50 16.20 ?  22  ASP   A CG   1 
ATOM   497  C  CG   B ASP   A 1 22  ? 13.873 4.089   9.065   0.50 15.56 ?  22  ASP   A CG   1 
ATOM   498  O  OD1  A ASP   A 1 22  ? 14.792 3.949   8.993   0.50 16.12 ?  22  ASP   A OD1  1 
ATOM   499  O  OD1  B ASP   A 1 22  ? 15.005 3.678   8.724   0.50 15.06 ?  22  ASP   A OD1  1 
ATOM   500  O  OD2  A ASP   A 1 22  ? 13.462 5.555   9.672   0.50 16.89 -1 22  ASP   A OD2  1 
ATOM   501  O  OD2  B ASP   A 1 22  ? 13.536 5.289   8.978   0.50 17.50 -1 22  ASP   A OD2  1 
ATOM   502  H  H    A ASP   A 1 22  ? 11.523 1.357   10.703  0.50 18.37 ?  22  ASP   A H    1 
ATOM   503  H  H    B ASP   A 1 22  ? 11.560 1.162   10.292  0.50 15.99 ?  22  ASP   A H    1 
ATOM   504  H  HA   A ASP   A 1 22  ? 13.029 1.887   8.559   0.50 17.72 ?  22  ASP   A HA   1 
ATOM   505  H  HA   B ASP   A 1 22  ? 13.160 1.628   8.192   0.50 15.73 ?  22  ASP   A HA   1 
ATOM   506  H  HB2  A ASP   A 1 22  ? 11.835 3.601   9.674   0.50 18.68 ?  22  ASP   A HB2  1 
ATOM   507  H  HB2  B ASP   A 1 22  ? 11.977 3.386   9.303   0.50 17.29 ?  22  ASP   A HB2  1 
ATOM   508  H  HB3  A ASP   A 1 22  ? 12.706 3.341   10.976  0.50 18.68 ?  22  ASP   A HB3  1 
ATOM   509  H  HB3  B ASP   A 1 22  ? 12.880 3.129   10.584  0.50 17.29 ?  22  ASP   A HB3  1 
ATOM   510  N  N    A ILE   A 1 23  ? 15.239 0.998   9.216   0.50 13.14 ?  23  ILE   A N    1 
ATOM   511  N  N    B ILE   A 1 23  ? 15.331 0.712   8.951   0.50 11.73 ?  23  ILE   A N    1 
ATOM   512  C  CA   A ILE   A 1 23  ? 16.500 0.408   9.664   0.50 12.74 ?  23  ILE   A CA   1 
ATOM   513  C  CA   B ILE   A 1 23  ? 16.578 0.137   9.450   0.50 11.74 ?  23  ILE   A CA   1 
ATOM   514  C  C    A ILE   A 1 23  ? 17.282 1.375   10.542  0.50 12.75 ?  23  ILE   A C    1 
ATOM   515  C  C    B ILE   A 1 23  ? 17.291 1.100   10.388  0.50 11.99 ?  23  ILE   A C    1 
ATOM   516  O  O    A ILE   A 1 23  ? 18.015 0.952   11.444  0.50 13.51 ?  23  ILE   A O    1 
ATOM   517  O  O    B ILE   A 1 23  ? 17.968 0.671   11.331  0.50 12.28 ?  23  ILE   A O    1 
ATOM   518  C  CB   A ILE   A 1 23  ? 17.321 -0.100  8.458   0.50 12.76 ?  23  ILE   A CB   1 
ATOM   519  C  CB   B ILE   A 1 23  ? 17.484 -0.336  8.290   0.50 11.72 ?  23  ILE   A CB   1 
ATOM   520  C  CG1  A ILE   A 1 23  ? 18.480 -0.986  8.928   0.50 13.02 ?  23  ILE   A CG1  1 
ATOM   521  C  CG1  B ILE   A 1 23  ? 18.523 -1.329  8.814   0.50 12.03 ?  23  ILE   A CG1  1 
ATOM   522  C  CG2  A ILE   A 1 23  ? 17.807 1.066   7.602   0.50 12.96 ?  23  ILE   A CG2  1 
ATOM   523  C  CG2  B ILE   A 1 23  ? 18.172 0.840   7.604   0.50 11.46 ?  23  ILE   A CG2  1 
ATOM   524  C  CD1  A ILE   A 1 23  ? 19.199 -1.707  7.799   0.50 13.48 ?  23  ILE   A CD1  1 
ATOM   525  C  CD1  B ILE   A 1 23  ? 19.405 -1.920  7.736   0.50 11.95 ?  23  ILE   A CD1  1 
ATOM   526  H  H    A ILE   A 1 23  ? 15.141 1.032   8.364   0.50 15.76 ?  23  ILE   A H    1 
ATOM   527  H  H    B ILE   A 1 23  ? 15.270 0.734   8.106   0.50 14.07 ?  23  ILE   A H    1 
ATOM   528  H  HA   A ILE   A 1 23  ? 16.295 -0.365  10.209  0.50 15.27 ?  23  ILE   A HA   1 
ATOM   529  H  HA   B ILE   A 1 23  ? 16.349 -0.654  9.962   0.50 14.08 ?  23  ILE   A HA   1 
ATOM   530  H  HB   A ILE   A 1 23  ? 16.739 -0.643  7.907   0.50 15.30 ?  23  ILE   A HB   1 
ATOM   531  H  HB   B ILE   A 1 23  ? 16.936 -0.796  7.630   0.50 14.06 ?  23  ILE   A HB   1 
ATOM   532  H  HG12 A ILE   A 1 23  ? 19.132 -0.438  9.389   0.50 15.61 ?  23  ILE   A HG12 1 
ATOM   533  H  HG12 B ILE   A 1 23  ? 19.098 -0.877  9.450   0.50 14.42 ?  23  ILE   A HG12 1 
ATOM   534  H  HG13 A ILE   A 1 23  ? 18.131 -1.662  9.532   0.50 15.61 ?  23  ILE   A HG13 1 
ATOM   535  H  HG13 B ILE   A 1 23  ? 18.063 -2.065  9.253   0.50 14.42 ?  23  ILE   A HG13 1 
ATOM   536  H  HG21 A ILE   A 1 23  ? 18.177 0.717   6.774   0.50 15.55 ?  23  ILE   A HG21 1 
ATOM   537  H  HG21 B ILE   A 1 23  ? 18.536 0.540   6.754   0.50 13.74 ?  23  ILE   A HG21 1 
ATOM   538  H  HG22 A ILE   A 1 23  ? 17.054 1.646   7.405   0.50 15.55 ?  23  ILE   A HG22 1 
ATOM   539  H  HG22 B ILE   A 1 23  ? 17.521 1.539   7.456   0.50 13.74 ?  23  ILE   A HG22 1 
ATOM   540  H  HG23 A ILE   A 1 23  ? 18.486 1.557   8.087   0.50 15.55 ?  23  ILE   A HG23 1 
ATOM   541  H  HG23 B ILE   A 1 23  ? 18.887 1.162   8.173   0.50 13.74 ?  23  ILE   A HG23 1 
ATOM   542  H  HD11 A ILE   A 1 23  ? 19.876 -2.291  8.176   0.50 16.17 ?  23  ILE   A HD11 1 
ATOM   543  H  HD11 B ILE   A 1 23  ? 19.951 -2.621  8.126   0.50 14.33 ?  23  ILE   A HD11 1 
ATOM   544  H  HD12 A ILE   A 1 23  ? 18.554 -2.231  7.297   0.50 16.17 ?  23  ILE   A HD12 1 
ATOM   545  H  HD12 B ILE   A 1 23  ? 18.841 -2.290  7.039   0.50 14.33 ?  23  ILE   A HD12 1 
ATOM   546  H  HD13 A ILE   A 1 23  ? 19.614 -1.051  7.218   0.50 16.17 ?  23  ILE   A HD13 1 
ATOM   547  H  HD13 B ILE   A 1 23  ? 19.969 -1.222  7.373   0.50 14.33 ?  23  ILE   A HD13 1 
ATOM   548  N  N    A VAL   A 1 24  ? 17.136 2.680   10.307  0.50 12.69 ?  24  VAL   A N    1 
ATOM   549  N  N    B VAL   A 1 24  ? 17.148 2.407   10.157  0.50 12.64 ?  24  VAL   A N    1 
ATOM   550  C  CA   A VAL   A 1 24  ? 17.804 3.663   11.156  0.50 13.30 ?  24  VAL   A CA   1 
ATOM   551  C  CA   B VAL   A 1 24  ? 17.788 3.390   11.025  0.50 13.93 ?  24  VAL   A CA   1 
ATOM   552  C  C    A VAL   A 1 24  ? 17.275 3.580   12.580  0.50 13.73 ?  24  VAL   A C    1 
ATOM   553  C  C    B VAL   A 1 24  ? 17.196 3.330   12.427  0.50 14.33 ?  24  VAL   A C    1 
ATOM   554  O  O    A VAL   A 1 24  ? 18.041 3.495   13.547  0.50 14.45 ?  24  VAL   A O    1 
ATOM   555  O  O    B VAL   A 1 24  ? 17.919 3.408   13.426  0.50 15.13 ?  24  VAL   A O    1 
ATOM   556  C  CB   A VAL   A 1 24  ? 17.640 5.077   10.573  0.50 13.81 ?  24  VAL   A CB   1 
ATOM   557  C  CB   B VAL   A 1 24  ? 17.678 4.797   10.409  0.50 15.09 ?  24  VAL   A CB   1 
ATOM   558  C  CG1  A VAL   A 1 24  ? 18.096 6.125   11.583  0.50 14.63 ?  24  VAL   A CG1  1 
ATOM   559  C  CG1  B VAL   A 1 24  ? 18.338 5.825   11.309  0.50 16.54 ?  24  VAL   A CG1  1 
ATOM   560  C  CG2  A VAL   A 1 24  ? 18.410 5.203   9.272   0.50 13.90 ?  24  VAL   A CG2  1 
ATOM   561  C  CG2  B VAL   A 1 24  ? 18.291 4.818   9.018   0.50 15.44 ?  24  VAL   A CG2  1 
ATOM   562  H  H    A VAL   A 1 24  ? 16.649 3.020   9.678   0.50 15.22 ?  24  VAL   A H    1 
ATOM   563  H  H    B VAL   A 1 24  ? 16.675 2.742   9.519   0.50 15.15 ?  24  VAL   A H    1 
ATOM   564  H  HA   A VAL   A 1 24  ? 18.748 3.463   11.178  0.50 15.95 ?  24  VAL   A HA   1 
ATOM   565  H  HA   B VAL   A 1 24  ? 18.725 3.168   11.094  0.50 16.71 ?  24  VAL   A HA   1 
ATOM   566  H  HB   A VAL   A 1 24  ? 16.701 5.238   10.378  0.50 16.57 ?  24  VAL   A HB   1 
ATOM   567  H  HB   B VAL   A 1 24  ? 16.740 5.029   10.322  0.50 18.10 ?  24  VAL   A HB   1 
ATOM   568  H  HG11 A VAL   A 1 24  ? 18.267 6.957   11.117  0.50 17.55 ?  24  VAL   A HG11 1 
ATOM   569  H  HG11 B VAL   A 1 24  ? 18.426 6.657   10.820  0.50 19.84 ?  24  VAL   A HG11 1 
ATOM   570  H  HG12 A VAL   A 1 24  ? 17.399 6.253   12.243  0.50 17.55 ?  24  VAL   A HG12 1 
ATOM   571  H  HG12 B VAL   A 1 24  ? 17.782 5.959   12.092  0.50 19.84 ?  24  VAL   A HG12 1 
ATOM   572  H  HG13 A VAL   A 1 24  ? 18.909 5.813   12.010  0.50 17.55 ?  24  VAL   A HG13 1 
ATOM   573  H  HG13 B VAL   A 1 24  ? 19.212 5.500   11.571  0.50 19.84 ?  24  VAL   A HG13 1 
ATOM   574  H  HG21 A VAL   A 1 24  ? 18.242 6.076   8.885   0.50 16.67 ?  24  VAL   A HG21 1 
ATOM   575  H  HG21 B VAL   A 1 24  ? 18.284 5.728   8.686   0.50 18.51 ?  24  VAL   A HG21 1 
ATOM   576  H  HG22 A VAL   A 1 24  ? 19.357 5.099   9.455   0.50 16.67 ?  24  VAL   A HG22 1 
ATOM   577  H  HG22 B VAL   A 1 24  ? 19.203 4.491   9.071   0.50 18.51 ?  24  VAL   A HG22 1 
ATOM   578  H  HG23 A VAL   A 1 24  ? 18.115 4.509   8.660   0.50 16.67 ?  24  VAL   A HG23 1 
ATOM   579  H  HG23 B VAL   A 1 24  ? 17.770 4.247   8.431   0.50 18.51 ?  24  VAL   A HG23 1 
ATOM   580  N  N    A GLU   A 1 25  ? 15.951 3.625   12.731  0.50 14.35 ?  25  GLU   A N    1 
ATOM   581  N  N    B GLU   A 1 25  ? 15.874 3.181   12.528  0.50 14.74 ?  25  GLU   A N    1 
ATOM   582  C  CA   A GLU   A 1 25  ? 15.372 3.563   14.067  0.50 15.66 ?  25  GLU   A CA   1 
ATOM   583  C  CA   B GLU   A 1 25  ? 15.246 3.091   13.842  0.50 15.71 ?  25  GLU   A CA   1 
ATOM   584  C  C    A GLU   A 1 25  ? 15.609 2.201   14.707  0.50 14.71 ?  25  GLU   A C    1 
ATOM   585  C  C    B GLU   A 1 25  ? 15.553 1.756   14.510  0.50 15.69 ?  25  GLU   A C    1 
ATOM   586  O  O    A GLU   A 1 25  ? 15.836 2.114   15.918  0.50 14.93 ?  25  GLU   A O    1 
ATOM   587  O  O    B GLU   A 1 25  ? 15.786 1.704   15.722  0.50 16.34 ?  25  GLU   A O    1 
ATOM   588  C  CB   A GLU   A 1 25  ? 13.885 3.923   14.018  0.50 18.25 ?  25  GLU   A CB   1 
ATOM   589  C  CB   B GLU   A 1 25  ? 13.739 3.335   13.735  0.50 17.20 ?  25  GLU   A CB   1 
ATOM   590  C  CG   A GLU   A 1 25  ? 13.635 5.384   13.659  0.50 21.30 ?  25  GLU   A CG   1 
ATOM   591  C  CG   B GLU   A 1 25  ? 13.380 4.740   13.264  0.50 19.85 ?  25  GLU   A CG   1 
ATOM   592  C  CD   A GLU   A 1 25  ? 14.488 6.354   14.465  0.50 23.83 ?  25  GLU   A CD   1 
ATOM   593  C  CD   B GLU   A 1 25  ? 14.005 5.820   14.124  0.50 22.63 ?  25  GLU   A CD   1 
ATOM   594  O  OE1  A GLU   A 1 25  ? 14.592 6.187   15.699  0.50 24.78 ?  25  GLU   A OE1  1 
ATOM   595  O  OE1  B GLU   A 1 25  ? 14.011 5.658   15.365  0.50 23.86 ?  25  GLU   A OE1  1 
ATOM   596  O  OE2  A GLU   A 1 25  ? 15.075 7.272   13.854  0.50 24.92 -1 25  GLU   A OE2  1 
ATOM   597  O  OE2  B GLU   A 1 25  ? 14.492 6.825   13.562  0.50 23.78 -1 25  GLU   A OE2  1 
ATOM   598  H  H    A GLU   A 1 25  ? 15.377 3.701   12.089  0.50 17.21 ?  25  GLU   A H    1 
ATOM   599  H  H    B GLU   A 1 25  ? 15.328 3.125   11.865  0.50 17.67 ?  25  GLU   A H    1 
ATOM   600  H  HA   A GLU   A 1 25  ? 15.817 4.213   14.628  0.50 18.78 ?  25  GLU   A HA   1 
ATOM   601  H  HA   B GLU   A 1 25  ? 15.620 3.779   14.409  0.50 18.84 ?  25  GLU   A HA   1 
ATOM   602  H  HB2  A GLU   A 1 25  ? 13.443 3.378   13.343  0.50 21.88 ?  25  GLU   A HB2  1 
ATOM   603  H  HB2  B GLU   A 1 25  ? 13.361 2.705   13.103  0.50 20.63 ?  25  GLU   A HB2  1 
ATOM   604  H  HB3  A GLU   A 1 25  ? 13.482 3.759   14.885  0.50 21.88 ?  25  GLU   A HB3  1 
ATOM   605  H  HB3  B GLU   A 1 25  ? 13.337 3.204   14.610  0.50 20.63 ?  25  GLU   A HB3  1 
ATOM   606  H  HG2  A GLU   A 1 25  ? 13.856 5.522   12.728  0.50 25.55 ?  25  GLU   A HG2  1 
ATOM   607  H  HG2  B GLU   A 1 25  ? 13.692 4.858   12.353  0.50 23.81 ?  25  GLU   A HG2  1 
ATOM   608  H  HG3  A GLU   A 1 25  ? 12.701 5.593   13.819  0.50 25.55 ?  25  GLU   A HG3  1 
ATOM   609  H  HG3  B GLU   A 1 25  ? 12.419 4.855   13.305  0.50 23.81 ?  25  GLU   A HG3  1 
ATOM   610  N  N    A GLU   A 1 26  ? 15.570 1.131   13.908  0.50 14.37 ?  26  GLU   A N    1 
ATOM   611  N  N    B GLU   A 1 26  ? 15.570 0.666   13.737  0.50 15.62 ?  26  GLU   A N    1 
ATOM   612  C  CA   A GLU   A 1 26  ? 15.876 -0.198  14.432  0.50 14.89 ?  26  GLU   A CA   1 
ATOM   613  C  CA   B GLU   A 1 26  ? 15.968 -0.621  14.301  0.50 15.67 ?  26  GLU   A CA   1 
ATOM   614  C  C    A GLU   A 1 26  ? 17.298 -0.248  14.984  0.50 14.07 ?  26  GLU   A C    1 
ATOM   615  C  C    B GLU   A 1 26  ? 17.385 -0.552  14.854  0.50 14.58 ?  26  GLU   A C    1 
ATOM   616  O  O    A GLU   A 1 26  ? 17.526 -0.674  16.122  0.50 14.16 ?  26  GLU   A O    1 
ATOM   617  O  O    B GLU   A 1 26  ? 17.684 -1.137  15.901  0.50 14.50 ?  26  GLU   A O    1 
ATOM   618  C  CB   A GLU   A 1 26  ? 15.711 -1.242  13.324  0.50 17.08 ?  26  GLU   A CB   1 
ATOM   619  C  CB   B GLU   A 1 26  ? 15.870 -1.720  13.238  0.50 16.97 ?  26  GLU   A CB   1 
ATOM   620  C  CG   A GLU   A 1 26  ? 14.325 -1.820  13.171  0.50 19.84 ?  26  GLU   A CG   1 
ATOM   621  C  CG   B GLU   A 1 26  ? 14.456 -2.090  12.847  0.50 18.13 ?  26  GLU   A CG   1 
ATOM   622  C  CD   A GLU   A 1 26  ? 13.909 -2.630  14.382  0.50 21.97 ?  26  GLU   A CD   1 
ATOM   623  C  CD   B GLU   A 1 26  ? 13.695 -2.766  13.973  0.50 19.04 ?  26  GLU   A CD   1 
ATOM   624  O  OE1  A GLU   A 1 26  ? 14.430 -3.750  14.576  0.50 22.77 ?  26  GLU   A OE1  1 
ATOM   625  O  OE1  B GLU   A 1 26  ? 14.133 -3.840  14.452  0.50 19.78 ?  26  GLU   A OE1  1 
ATOM   626  O  OE2  A GLU   A 1 26  ? 13.077 -2.126  15.155  0.50 22.92 -1 26  GLU   A OE2  1 
ATOM   627  O  OE2  B GLU   A 1 26  ? 12.652 -2.215  14.378  0.50 18.47 -1 26  GLU   A OE2  1 
ATOM   628  H  H    A GLU   A 1 26  ? 15.367 1.156   13.071  0.50 17.24 ?  26  GLU   A H    1 
ATOM   629  H  H    B GLU   A 1 26  ? 15.359 0.642   12.905  0.50 18.73 ?  26  GLU   A H    1 
ATOM   630  H  HA   A GLU   A 1 26  ? 15.254 -0.407  15.145  0.50 17.85 ?  26  GLU   A HA   1 
ATOM   631  H  HA   B GLU   A 1 26  ? 15.373 -0.857  15.027  0.50 18.80 ?  26  GLU   A HA   1 
ATOM   632  H  HB2  A GLU   A 1 26  ? 15.948 -0.834  12.476  0.50 20.48 ?  26  GLU   A HB2  1 
ATOM   633  H  HB2  B GLU   A 1 26  ? 16.327 -1.424  12.434  0.50 20.35 ?  26  GLU   A HB2  1 
ATOM   634  H  HB3  A GLU   A 1 26  ? 16.312 -1.977  13.509  0.50 20.48 ?  26  GLU   A HB3  1 
ATOM   635  H  HB3  B GLU   A 1 26  ? 16.298 -2.526  13.574  0.50 20.35 ?  26  GLU   A HB3  1 
ATOM   636  H  HG2  A GLU   A 1 26  ? 13.695 -1.092  13.056  0.50 23.80 ?  26  GLU   A HG2  1 
ATOM   637  H  HG2  B GLU   A 1 26  ? 13.974 -1.283  12.606  0.50 21.74 ?  26  GLU   A HG2  1 
ATOM   638  H  HG3  A GLU   A 1 26  ? 14.307 -2.397  12.387  0.50 23.80 ?  26  GLU   A HG3  1 
ATOM   639  H  HG3  B GLU   A 1 26  ? 14.479 -2.700  12.093  0.50 21.74 ?  26  GLU   A HG3  1 
ATOM   640  N  N    . ALA   A 1 27  ? 18.273 0.171   14.173  1.00 13.81 ?  27  ALA   A N    1 
ATOM   641  C  CA   . ALA   A 1 27  ? 19.659 0.200   14.620  1.00 13.90 ?  27  ALA   A CA   1 
ATOM   642  C  C    . ALA   A 1 27  ? 19.812 1.029   15.891  1.00 15.59 ?  27  ALA   A C    1 
ATOM   643  O  O    . ALA   A 1 27  ? 20.478 0.604   16.842  1.00 15.56 ?  27  ALA   A O    1 
ATOM   644  C  CB   . ALA   A 1 27  ? 20.566 0.719   13.502  1.00 13.43 ?  27  ALA   A CB   1 
ATOM   645  H  H    A ALA   A 1 27  ? 18.152 0.438   13.364  0.50 16.56 ?  27  ALA   A H    1 
ATOM   646  H  H    B ALA   A 1 27  ? 18.096 0.644   13.477  0.50 16.56 ?  27  ALA   A H    1 
ATOM   647  H  HA   . ALA   A 1 27  ? 19.935 -0.705  14.823  1.00 16.67 ?  27  ALA   A HA   1 
ATOM   648  H  HB1  . ALA   A 1 27  ? 21.482 0.728   13.816  1.00 16.10 ?  27  ALA   A HB1  1 
ATOM   649  H  HB2  . ALA   A 1 27  ? 20.489 0.128   12.732  1.00 16.10 ?  27  ALA   A HB2  1 
ATOM   650  H  HB3  . ALA   A 1 27  ? 20.289 1.614   13.255  1.00 16.10 ?  27  ALA   A HB3  1 
ATOM   651  N  N    A LYS   A 1 28  ? 19.189 2.207   15.949  0.50 17.68 ?  28  LYS   A N    1 
ATOM   652  N  N    B LYS   A 1 28  ? 19.186 2.212   15.922  0.50 17.01 ?  28  LYS   A N    1 
ATOM   653  C  CA   A LYS   A 1 28  ? 19.355 3.034   17.142  0.50 20.47 ?  28  LYS   A CA   1 
ATOM   654  C  CA   B LYS   A 1 28  ? 19.269 3.070   17.099  0.50 19.20 ?  28  LYS   A CA   1 
ATOM   655  C  C    A LYS   A 1 28  ? 18.786 2.365   18.389  0.50 21.79 ?  28  LYS   A C    1 
ATOM   656  C  C    B LYS   A 1 28  ? 18.726 2.359   18.328  0.50 20.26 ?  28  LYS   A C    1 
ATOM   657  O  O    A LYS   A 1 28  ? 19.232 2.658   19.504  0.50 22.63 ?  28  LYS   A O    1 
ATOM   658  O  O    B LYS   A 1 28  ? 19.304 2.454   19.417  0.50 21.23 ?  28  LYS   A O    1 
ATOM   659  C  CB   A LYS   A 1 28  ? 18.744 4.419   16.936  0.50 22.27 ?  28  LYS   A CB   1 
ATOM   660  C  CB   B LYS   A 1 28  ? 18.498 4.374   16.863  0.50 20.68 ?  28  LYS   A CB   1 
ATOM   661  C  CG   A LYS   A 1 28  ? 19.643 5.350   16.141  0.50 23.78 ?  28  LYS   A CG   1 
ATOM   662  C  CG   B LYS   A 1 28  ? 19.053 5.268   15.771  0.50 22.24 ?  28  LYS   A CG   1 
ATOM   663  C  CD   A LYS   A 1 28  ? 19.137 6.779   16.151  0.50 25.20 ?  28  LYS   A CD   1 
ATOM   664  C  CD   B LYS   A 1 28  ? 18.472 6.674   15.878  0.50 24.03 ?  28  LYS   A CD   1 
ATOM   665  C  CE   A LYS   A 1 28  ? 17.816 6.899   15.417  0.50 26.34 ?  28  LYS   A CE   1 
ATOM   666  C  CE   B LYS   A 1 28  ? 18.436 7.376   14.530  0.50 25.51 ?  28  LYS   A CE   1 
ATOM   667  N  NZ   A LYS   A 1 28  ? 17.366 8.313   15.332  0.50 26.97 ?  28  LYS   A NZ   1 
ATOM   668  N  NZ   B LYS   A 1 28  ? 18.323 8.858   14.656  0.50 26.38 ?  28  LYS   A NZ   1 
ATOM   669  H  H    A LYS   A 1 28  ? 18.691 2.542   15.334  0.50 21.21 ?  28  LYS   A H    1 
ATOM   670  H  H    B LYS   A 1 28  ? 18.702 2.526   15.287  0.50 20.40 ?  28  LYS   A H    1 
ATOM   671  H  HA   A LYS   A 1 28  ? 20.304 3.159   17.291  0.50 24.55 ?  28  LYS   A HA   1 
ATOM   672  H  HA   B LYS   A 1 28  ? 20.192 3.298   17.271  0.50 23.02 ?  28  LYS   A HA   1 
ATOM   673  H  HB2  A LYS   A 1 28  ? 17.908 4.325   16.459  0.50 26.72 ?  28  LYS   A HB2  1 
ATOM   674  H  HB2  B LYS   A 1 28  ? 17.586 4.161   16.618  0.50 24.81 ?  28  LYS   A HB2  1 
ATOM   675  H  HB3  A LYS   A 1 28  ? 18.587 4.825   17.805  0.50 26.72 ?  28  LYS   A HB3  1 
ATOM   676  H  HB3  B LYS   A 1 28  ? 18.503 4.895   17.681  0.50 24.81 ?  28  LYS   A HB3  1 
ATOM   677  H  HG2  A LYS   A 1 28  ? 20.534 5.342   16.527  0.50 28.52 ?  28  LYS   A HG2  1 
ATOM   678  H  HG2  B LYS   A 1 28  ? 20.016 5.329   15.861  0.50 26.67 ?  28  LYS   A HG2  1 
ATOM   679  H  HG3  A LYS   A 1 28  ? 19.677 5.048   15.220  0.50 28.52 ?  28  LYS   A HG3  1 
ATOM   680  H  HG3  B LYS   A 1 28  ? 18.818 4.910   14.902  0.50 26.67 ?  28  LYS   A HG3  1 
ATOM   681  H  HD2  A LYS   A 1 28  ? 19.004 7.065   17.069  0.50 30.23 ?  28  LYS   A HD2  1 
ATOM   682  H  HD2  B LYS   A 1 28  ? 17.563 6.620   16.216  0.50 28.82 ?  28  LYS   A HD2  1 
ATOM   683  H  HD3  A LYS   A 1 28  ? 19.785 7.352   15.711  0.50 30.23 ?  28  LYS   A HD3  1 
ATOM   684  H  HD3  B LYS   A 1 28  ? 19.021 7.202   16.479  0.50 28.82 ?  28  LYS   A HD3  1 
ATOM   685  H  HE2  A LYS   A 1 28  ? 17.921 6.555   14.516  0.50 31.59 ?  28  LYS   A HE2  1 
ATOM   686  H  HE2  B LYS   A 1 28  ? 19.249 7.175   14.046  0.50 30.60 ?  28  LYS   A HE2  1 
ATOM   687  H  HE3  A LYS   A 1 28  ? 17.139 6.393   15.893  0.50 31.59 ?  28  LYS   A HE3  1 
ATOM   688  H  HE3  B LYS   A 1 28  ? 17.664 7.061   14.034  0.50 30.60 ?  28  LYS   A HE3  1 
ATOM   689  H  HZ1  A LYS   A 1 28  ? 16.592 8.360   14.898  0.50 32.35 ?  28  LYS   A HZ1  1 
ATOM   690  H  HZ1  B LYS   A 1 28  ? 18.304 9.231   13.848  0.50 31.64 ?  28  LYS   A HZ1  1 
ATOM   691  H  HZ2  A LYS   A 1 28  ? 17.263 8.649   16.150  0.50 32.35 ?  28  LYS   A HZ2  1 
ATOM   692  H  HZ2  B LYS   A 1 28  ? 17.576 9.071   15.090  0.50 31.64 ?  28  LYS   A HZ2  1 
ATOM   693  H  HZ3  A LYS   A 1 28  ? 17.973 8.798   14.896  0.50 32.35 ?  28  LYS   A HZ3  1 
ATOM   694  H  HZ3  B LYS   A 1 28  ? 19.021 9.178   15.106  0.50 31.64 ?  28  LYS   A HZ3  1 
ATOM   695  N  N    A LYS   A 1 29  ? 17.808 1.470   18.228  0.50 22.39 ?  29  LYS   A N    1 
ATOM   696  N  N    B LYS   A 1 29  ? 17.622 1.629   18.169  0.50 20.57 ?  29  LYS   A N    1 
ATOM   697  C  CA   A LYS   A 1 29  ? 17.229 0.772   19.374  0.50 23.98 ?  29  LYS   A CA   1 
ATOM   698  C  CA   B LYS   A 1 29  ? 16.979 0.978   19.304  0.50 22.04 ?  29  LYS   A CA   1 
ATOM   699  C  C    A LYS   A 1 29  ? 18.055 -0.450  19.771  0.50 23.00 ?  29  LYS   A C    1 
ATOM   700  C  C    B LYS   A 1 29  ? 17.752 -0.260  19.741  0.50 20.79 ?  29  LYS   A C    1 
ATOM   701  O  O    A LYS   A 1 29  ? 18.369 -0.640  20.951  0.50 23.82 ?  29  LYS   A O    1 
ATOM   702  O  O    B LYS   A 1 29  ? 17.977 -0.470  20.939  0.50 21.40 ?  29  LYS   A O    1 
ATOM   703  C  CB   A LYS   A 1 29  ? 15.794 0.351   19.050  0.50 26.65 ?  29  LYS   A CB   1 
ATOM   704  C  CB   B LYS   A 1 29  ? 15.545 0.597   18.934  0.50 25.13 ?  29  LYS   A CB   1 
ATOM   705  C  CG   A LYS   A 1 29  ? 15.082 -0.379  20.180  0.50 29.47 ?  29  LYS   A CG   1 
ATOM   706  C  CG   B LYS   A 1 29  ? 14.791 -0.130  20.036  0.50 28.38 ?  29  LYS   A CG   1 
ATOM   707  C  CD   A LYS   A 1 29  ? 14.759 0.560   21.328  0.50 32.01 ?  29  LYS   A CD   1 
ATOM   708  C  CD   B LYS   A 1 29  ? 14.545 0.784   21.224  0.50 31.16 ?  29  LYS   A CD   1 
ATOM   709  C  CE   A LYS   A 1 29  ? 13.858 -0.109  22.352  0.50 33.78 ?  29  LYS   A CE   1 
ATOM   710  C  CE   B LYS   A 1 29  ? 13.706 0.096   22.287  0.50 33.12 ?  29  LYS   A CE   1 
ATOM   711  N  NZ   A LYS   A 1 29  ? 13.387 0.853   23.384  0.50 34.79 ?  29  LYS   A NZ   1 
ATOM   712  N  NZ   B LYS   A 1 29  ? 13.384 1.015   23.412  0.50 34.25 ?  29  LYS   A NZ   1 
ATOM   713  H  H    A LYS   A 1 29  ? 17.453 1.267   17.474  0.50 26.86 ?  29  LYS   A H    1 
ATOM   714  H  H    B LYS   A 1 29  ? 17.233 1.487   17.413  0.50 24.67 ?  29  LYS   A H    1 
ATOM   715  H  HA   A LYS   A 1 29  ? 17.201 1.375   20.132  0.50 28.77 ?  29  LYS   A HA   1 
ATOM   716  H  HA   B LYS   A 1 29  ? 16.946 1.593   20.050  0.50 26.44 ?  29  LYS   A HA   1 
ATOM   717  H  HB2  A LYS   A 1 29  ? 15.277 1.145   18.843  0.50 31.97 ?  29  LYS   A HB2  1 
ATOM   718  H  HB2  B LYS   A 1 29  ? 15.051 1.405   18.727  0.50 30.14 ?  29  LYS   A HB2  1 
ATOM   719  H  HB3  A LYS   A 1 29  ? 15.809 -0.239  18.282  0.50 31.97 ?  29  LYS   A HB3  1 
ATOM   720  H  HB3  B LYS   A 1 29  ? 15.565 0.016   18.159  0.50 30.14 ?  29  LYS   A HB3  1 
ATOM   721  H  HG2  A LYS   A 1 29  ? 14.249 -0.744  19.845  0.50 35.35 ?  29  LYS   A HG2  1 
ATOM   722  H  HG2  B LYS   A 1 29  ? 13.933 -0.420  19.693  0.50 34.04 ?  29  LYS   A HG2  1 
ATOM   723  H  HG3  A LYS   A 1 29  ? 15.645 -1.094  20.519  0.50 35.35 ?  29  LYS   A HG3  1 
ATOM   724  H  HG3  B LYS   A 1 29  ? 15.305 -0.897  20.338  0.50 34.04 ?  29  LYS   A HG3  1 
ATOM   725  H  HD2  A LYS   A 1 29  ? 15.582 0.822   21.771  0.50 38.40 ?  29  LYS   A HD2  1 
ATOM   726  H  HD2  B LYS   A 1 29  ? 15.395 1.032   21.621  0.50 37.38 ?  29  LYS   A HD2  1 
ATOM   727  H  HD3  A LYS   A 1 29  ? 14.301 1.342   20.983  0.50 38.40 ?  29  LYS   A HD3  1 
ATOM   728  H  HD3  B LYS   A 1 29  ? 14.070 1.575   20.925  0.50 37.38 ?  29  LYS   A HD3  1 
ATOM   729  H  HE2  A LYS   A 1 29  ? 13.081 -0.477  21.902  0.50 40.53 ?  29  LYS   A HE2  1 
ATOM   730  H  HE2  B LYS   A 1 29  ? 12.874 -0.205  21.891  0.50 39.74 ?  29  LYS   A HE2  1 
ATOM   731  H  HE3  A LYS   A 1 29  ? 14.351 -0.816  22.798  0.50 40.53 ?  29  LYS   A HE3  1 
ATOM   732  H  HE3  B LYS   A 1 29  ? 14.200 -0.660  22.643  0.50 39.74 ?  29  LYS   A HE3  1 
ATOM   733  H  HZ1  A LYS   A 1 29  ? 12.862 0.437   23.970  0.50 41.73 ?  29  LYS   A HZ1  1 
ATOM   734  H  HZ1  B LYS   A 1 29  ? 12.893 0.590   24.020  0.50 41.09 ?  29  LYS   A HZ1  1 
ATOM   735  H  HZ2  A LYS   A 1 29  ? 14.083 1.201   23.815  0.50 41.73 ?  29  LYS   A HZ2  1 
ATOM   736  H  HZ2  B LYS   A 1 29  ? 14.134 1.302   23.794  0.50 41.09 ?  29  LYS   A HZ2  1 
ATOM   737  H  HZ3  A LYS   A 1 29  ? 12.927 1.510   22.999  0.50 41.73 ?  29  LYS   A HZ3  1 
ATOM   738  H  HZ3  B LYS   A 1 29  ? 12.927 1.716   23.109  0.50 41.09 ?  29  LYS   A HZ3  1 
ATOM   739  N  N    A VAL   A 1 30  ? 18.400 -1.296  18.800  0.50 21.58 ?  30  VAL   A N    1 
ATOM   740  N  N    B VAL   A 1 30  ? 18.144 -1.099  18.782  0.50 19.70 ?  30  VAL   A N    1 
ATOM   741  C  CA   A VAL   A 1 30  ? 19.041 -2.572  19.105  0.50 20.55 ?  30  VAL   A CA   1 
ATOM   742  C  CA   B VAL   A 1 30  ? 18.804 -2.356  19.114  0.50 18.77 ?  30  VAL   A CA   1 
ATOM   743  C  C    A VAL   A 1 30  ? 20.543 -2.413  19.322  0.50 19.19 ?  30  VAL   A C    1 
ATOM   744  C  C    B VAL   A 1 30  ? 20.303 -2.168  19.330  0.50 17.99 ?  30  VAL   A C    1 
ATOM   745  O  O    A VAL   A 1 30  ? 21.135 -3.133  20.135  0.50 19.63 ?  30  VAL   A O    1 
ATOM   746  O  O    B VAL   A 1 30  ? 20.903 -2.861  20.160  0.50 18.36 ?  30  VAL   A O    1 
ATOM   747  C  CB   A VAL   A 1 30  ? 18.746 -3.583  17.982  0.50 21.36 ?  30  VAL   A CB   1 
ATOM   748  C  CB   B VAL   A 1 30  ? 18.515 -3.401  18.020  0.50 19.25 ?  30  VAL   A CB   1 
ATOM   749  C  CG1  A VAL   A 1 30  ? 19.549 -4.864  18.184  0.50 21.90 ?  30  VAL   A CG1  1 
ATOM   750  C  CG1  B VAL   A 1 30  ? 19.289 -4.685  18.283  0.50 19.83 ?  30  VAL   A CG1  1 
ATOM   751  C  CG2  A VAL   A 1 30  ? 17.259 -3.888  17.912  0.50 21.82 ?  30  VAL   A CG2  1 
ATOM   752  C  CG2  B VAL   A 1 30  ? 17.021 -3.684  17.930  0.50 19.71 ?  30  VAL   A CG2  1 
ATOM   753  H  H    A VAL   A 1 30  ? 18.272 -1.158  17.964  0.50 25.88 ?  30  VAL   A H    1 
ATOM   754  H  H    B VAL   A 1 30  ? 18.020 -0.972  17.939  0.50 23.63 ?  30  VAL   A H    1 
ATOM   755  H  HA   A VAL   A 1 30  ? 18.654 -2.924  19.922  0.50 24.65 ?  30  VAL   A HA   1 
ATOM   756  H  HA   B VAL   A 1 30  ? 18.425 -2.692  19.938  0.50 22.52 ?  30  VAL   A HA   1 
ATOM   757  H  HB   A VAL   A 1 30  ? 19.016 -3.198  17.133  0.50 25.62 ?  30  VAL   A HB   1 
ATOM   758  H  HB   B VAL   A 1 30  ? 18.808 -3.051  17.164  0.50 23.09 ?  30  VAL   A HB   1 
ATOM   759  H  HG11 A VAL   A 1 30  ? 19.176 -5.560  17.620  0.50 26.27 ?  30  VAL   A HG11 1 
ATOM   760  H  HG11 B VAL   A 1 30  ? 18.896 -5.404  17.762  0.50 23.79 ?  30  VAL   A HG11 1 
ATOM   761  H  HG12 A VAL   A 1 30  ? 20.474 -4.705  17.940  0.50 26.27 ?  30  VAL   A HG12 1 
ATOM   762  H  HG12 B VAL   A 1 30  ? 20.216 -4.560  18.023  0.50 23.79 ?  30  VAL   A HG12 1 
ATOM   763  H  HG13 A VAL   A 1 30  ? 19.491 -5.130  19.115  0.50 26.27 ?  30  VAL   A HG13 1 
ATOM   764  H  HG13 B VAL   A 1 30  ? 19.236 -4.897  19.227  0.50 23.79 ?  30  VAL   A HG13 1 
ATOM   765  H  HG21 A VAL   A 1 30  ? 17.105 -4.541  17.212  0.50 26.18 ?  30  VAL   A HG21 1 
ATOM   766  H  HG21 B VAL   A 1 30  ? 16.870 -4.373  17.263  0.50 23.64 ?  30  VAL   A HG21 1 
ATOM   767  H  HG22 A VAL   A 1 30  ? 16.971 -4.243  18.767  0.50 26.18 ?  30  VAL   A HG22 1 
ATOM   768  H  HG22 B VAL   A 1 30  ? 16.706 -3.989  18.795  0.50 23.64 ?  30  VAL   A HG22 1 
ATOM   769  H  HG23 A VAL   A 1 30  ? 16.781 -3.069  17.713  0.50 26.18 ?  30  VAL   A HG23 1 
ATOM   770  H  HG23 B VAL   A 1 30  ? 16.561 -2.871  17.676  0.50 23.64 ?  30  VAL   A HG23 1 
ATOM   771  N  N    A LYS   A 1 31  ? 21.179 -1.493  18.606  0.50 18.16 ?  31  LYS   A N    1 
ATOM   772  N  N    B LYS   A 1 31  ? 20.925 -1.240  18.610  0.50 17.60 ?  31  LYS   A N    1 
ATOM   773  C  CA   A LYS   A 1 31  ? 22.632 -1.382  18.564  0.50 18.80 ?  31  LYS   A CA   1 
ATOM   774  C  CA   B LYS   A 1 31  ? 22.377 -1.116  18.562  0.50 18.13 ?  31  LYS   A CA   1 
ATOM   775  C  C    A LYS   A 1 31  ? 23.262 -2.737  18.225  0.50 16.54 ?  31  LYS   A C    1 
ATOM   776  C  C    B LYS   A 1 31  ? 23.019 -2.481  18.301  0.50 16.64 ?  31  LYS   A C    1 
ATOM   777  O  O    A LYS   A 1 31  ? 24.052 -3.276  19.006  0.50 16.84 ?  31  LYS   A O    1 
ATOM   778  O  O    B LYS   A 1 31  ? 23.766 -2.995  19.141  0.50 17.58 ?  31  LYS   A O    1 
ATOM   779  C  CB   A LYS   A 1 31  ? 23.204 -0.823  19.859  0.50 22.71 ?  31  LYS   A CB   1 
ATOM   780  C  CB   B LYS   A 1 31  ? 22.938 -0.480  19.826  0.50 21.31 ?  31  LYS   A CB   1 
ATOM   781  C  CG   A LYS   A 1 31  ? 22.509 0.436   20.360  0.50 26.71 ?  31  LYS   A CG   1 
ATOM   782  C  CG   B LYS   A 1 31  ? 22.262 0.826   20.200  0.50 25.13 ?  31  LYS   A CG   1 
ATOM   783  C  CD   A LYS   A 1 31  ? 23.515 1.488   20.804  0.50 29.90 ?  31  LYS   A CD   1 
ATOM   784  C  CD   B LYS   A 1 31  ? 23.253 1.820   20.775  0.50 28.31 ?  31  LYS   A CD   1 
ATOM   785  C  CE   A LYS   A 1 31  ? 22.878 2.528   21.716  0.50 32.01 ?  31  LYS   A CE   1 
ATOM   786  C  CE   B LYS   A 1 31  ? 22.541 2.947   21.501  0.50 30.61 ?  31  LYS   A CE   1 
ATOM   787  N  NZ   A LYS   A 1 31  ? 21.699 3.193   21.097  0.50 33.03 ?  31  LYS   A NZ   1 
ATOM   788  N  NZ   B LYS   A 1 31  ? 21.470 3.565   20.674  0.50 31.89 ?  31  LYS   A NZ   1 
ATOM   789  H  H    A LYS   A 1 31  ? 20.776 -0.913  18.121  0.50 21.78 ?  31  LYS   A H    1 
ATOM   790  H  H    B LYS   A 1 31  ? 20.513 -0.650  18.137  0.50 21.11 ?  31  LYS   A H    1 
ATOM   791  H  HA   A LYS   A 1 31  ? 22.863 -0.766  17.857  0.50 22.55 ?  31  LYS   A HA   1 
ATOM   792  H  HA   B LYS   A 1 31  ? 22.604 -0.537  17.822  0.50 21.74 ?  31  LYS   A HA   1 
ATOM   793  H  HB2  A LYS   A 1 31  ? 23.131 -1.499  20.547  0.50 27.24 ?  31  LYS   A HB2  1 
ATOM   794  H  HB2  B LYS   A 1 31  ? 22.824 -1.095  20.565  0.50 25.56 ?  31  LYS   A HB2  1 
ATOM   795  H  HB3  A LYS   A 1 31  ? 24.140 -0.605  19.713  0.50 27.24 ?  31  LYS   A HB3  1 
ATOM   796  H  HB3  B LYS   A 1 31  ? 23.882 -0.297  19.690  0.50 25.56 ?  31  LYS   A HB3  1 
ATOM   797  H  HG2  A LYS   A 1 31  ? 21.971 0.813   19.647  0.50 32.04 ?  31  LYS   A HG2  1 
ATOM   798  H  HG2  B LYS   A 1 31  ? 21.862 1.218   19.408  0.50 30.14 ?  31  LYS   A HG2  1 
ATOM   799  H  HG3  A LYS   A 1 31  ? 21.950 0.212   21.121  0.50 32.04 ?  31  LYS   A HG3  1 
ATOM   800  H  HG3  B LYS   A 1 31  ? 21.582 0.652   20.870  0.50 30.14 ?  31  LYS   A HG3  1 
ATOM   801  H  HD2  A LYS   A 1 31  ? 24.235 1.058   21.292  0.50 35.87 ?  31  LYS   A HD2  1 
ATOM   802  H  HD2  B LYS   A 1 31  ? 23.834 1.365   21.407  0.50 33.96 ?  31  LYS   A HD2  1 
ATOM   803  H  HD3  A LYS   A 1 31  ? 23.867 1.945   20.023  0.50 35.87 ?  31  LYS   A HD3  1 
ATOM   804  H  HD3  B LYS   A 1 31  ? 23.778 2.203   20.053  0.50 33.96 ?  31  LYS   A HD3  1 
ATOM   805  H  HE2  A LYS   A 1 31  ? 22.583 2.094   22.532  0.50 38.40 ?  31  LYS   A HE2  1 
ATOM   806  H  HE2  B LYS   A 1 31  ? 22.136 2.594   22.307  0.50 36.72 ?  31  LYS   A HE2  1 
ATOM   807  H  HE3  A LYS   A 1 31  ? 23.534 3.212   21.923  0.50 38.40 ?  31  LYS   A HE3  1 
ATOM   808  H  HE3  B LYS   A 1 31  ? 23.185 3.634   21.725  0.50 36.72 ?  31  LYS   A HE3  1 
ATOM   809  H  HZ1  A LYS   A 1 31  ? 21.364 3.801   21.655  0.50 39.63 ?  31  LYS   A HZ1  1 
ATOM   810  H  HZ1  B LYS   A 1 31  ? 21.120 4.261   21.104  0.50 38.26 ?  31  LYS   A HZ1  1 
ATOM   811  H  HZ2  A LYS   A 1 31  ? 21.939 3.597   20.341  0.50 39.63 ?  31  LYS   A HZ2  1 
ATOM   812  H  HZ2  B LYS   A 1 31  ? 21.807 3.841   19.899  0.50 38.26 ?  31  LYS   A HZ2  1 
ATOM   813  H  HZ3  A LYS   A 1 31  ? 21.069 2.591   20.916  0.50 39.63 ?  31  LYS   A HZ3  1 
ATOM   814  H  HZ3  B LYS   A 1 31  ? 20.826 2.970   20.515  0.50 38.26 ?  31  LYS   A HZ3  1 
ATOM   815  N  N    A PRO   A 1 32  ? 22.943 -3.298  17.061  0.50 15.11 ?  32  PRO   A N    1 
ATOM   816  N  N    B PRO   A 1 32  ? 22.754 -3.082  17.144  0.50 14.84 ?  32  PRO   A N    1 
ATOM   817  C  CA   A PRO   A 1 32  ? 23.426 -4.639  16.728  0.50 15.09 ?  32  PRO   A CA   1 
ATOM   818  C  CA   B PRO   A 1 32  ? 23.246 -4.434  16.876  0.50 14.50 ?  32  PRO   A CA   1 
ATOM   819  C  C    A PRO   A 1 32  ? 24.927 -4.653  16.501  0.50 14.83 ?  32  PRO   A C    1 
ATOM   820  C  C    B PRO   A 1 32  ? 24.751 -4.439  16.667  0.50 14.43 ?  32  PRO   A C    1 
ATOM   821  O  O    A PRO   A 1 32  ? 25.558 -3.629  16.229  0.50 14.45 ?  32  PRO   A O    1 
ATOM   822  O  O    B PRO   A 1 32  ? 25.407 -3.401  16.556  0.50 14.78 ?  32  PRO   A O    1 
ATOM   823  C  CB   A PRO   A 1 32  ? 22.690 -4.957  15.422  0.50 15.67 ?  32  PRO   A CB   1 
ATOM   824  C  CB   B PRO   A 1 32  ? 22.514 -4.806  15.583  0.50 14.68 ?  32  PRO   A CB   1 
ATOM   825  C  CG   A PRO   A 1 32  ? 22.495 -3.621  14.790  0.50 15.36 ?  32  PRO   A CG   1 
ATOM   826  C  CG   B PRO   A 1 32  ? 22.351 -3.500  14.881  0.50 14.56 ?  32  PRO   A CG   1 
ATOM   827  C  CD   A PRO   A 1 32  ? 22.208 -2.690  15.940  0.50 14.84 ?  32  PRO   A CD   1 
ATOM   828  C  CD   B PRO   A 1 32  ? 22.054 -2.513  15.980  0.50 14.34 ?  32  PRO   A CD   1 
ATOM   829  H  HA   A PRO   A 1 32  ? 23.178 -5.281  17.416  0.50 18.10 ?  32  PRO   A HA   1 
ATOM   830  H  HA   B PRO   A 1 32  ? 22.994 -5.049  17.586  0.50 17.39 ?  32  PRO   A HA   1 
ATOM   831  H  HB2  A PRO   A 1 32  ? 23.244 -5.530  14.865  0.50 18.79 ?  32  PRO   A HB2  1 
ATOM   832  H  HB2  B PRO   A 1 32  ? 23.056 -5.417  15.058  0.50 17.61 ?  32  PRO   A HB2  1 
ATOM   833  H  HB3  A PRO   A 1 32  ? 21.840 -5.383  15.616  0.50 18.79 ?  32  PRO   A HB3  1 
ATOM   834  H  HB3  B PRO   A 1 32  ? 21.648 -5.201  15.785  0.50 17.61 ?  32  PRO   A HB3  1 
ATOM   835  H  HG2  A PRO   A 1 32  ? 23.304 -3.361  14.324  0.50 18.41 ?  32  PRO   A HG2  1 
ATOM   836  H  HG2  B PRO   A 1 32  ? 23.174 -3.272  14.423  0.50 17.46 ?  32  PRO   A HG2  1 
ATOM   837  H  HG3  A PRO   A 1 32  ? 21.743 -3.660  14.178  0.50 18.41 ?  32  PRO   A HG3  1 
ATOM   838  H  HG3  B PRO   A 1 32  ? 21.612 -3.556  14.253  0.50 17.46 ?  32  PRO   A HG3  1 
ATOM   839  H  HD2  A PRO   A 1 32  ? 22.555 -1.806  15.740  0.50 17.80 ?  32  PRO   A HD2  1 
ATOM   840  H  HD2  B PRO   A 1 32  ? 22.419 -1.644  15.752  0.50 17.20 ?  32  PRO   A HD2  1 
ATOM   841  H  HD3  A PRO   A 1 32  ? 21.258 -2.670  16.121  0.50 17.80 ?  32  PRO   A HD3  1 
ATOM   842  H  HD3  B PRO   A 1 32  ? 21.096 -2.466  16.135  0.50 17.20 ?  32  PRO   A HD3  1 
ATOM   843  N  N    A THR   A 1 33  ? 25.493 -5.856  16.589  0.50 15.08 ?  33  THR   A N    1 
ATOM   844  N  N    B THR   A 1 33  ? 25.297 -5.650  16.598  0.50 14.53 ?  33  THR   A N    1 
ATOM   845  C  CA   A THR   A 1 33  ? 26.902 -6.020  16.260  0.50 15.32 ?  33  THR   A CA   1 
ATOM   846  C  CA   B THR   A 1 33  ? 26.719 -5.805  16.310  0.50 14.50 ?  33  THR   A CA   1 
ATOM   847  C  C    A THR   A 1 33  ? 27.184 -5.562  14.834  0.50 14.11 ?  33  THR   A C    1 
ATOM   848  C  C    B THR   A 1 33  ? 27.044 -5.357  14.887  0.50 13.20 ?  33  THR   A C    1 
ATOM   849  O  O    A THR   A 1 33  ? 28.252 -4.997  14.560  0.50 13.78 ?  33  THR   A O    1 
ATOM   850  O  O    B THR   A 1 33  ? 28.027 -4.639  14.661  0.50 13.00 ?  33  THR   A O    1 
ATOM   851  C  CB   A THR   A 1 33  ? 27.315 -7.480  16.456  0.50 17.07 ?  33  THR   A CB   1 
ATOM   852  C  CB   B THR   A 1 33  ? 27.124 -7.262  16.528  0.50 16.13 ?  33  THR   A CB   1 
ATOM   853  O  OG1  A THR   A 1 33  ? 27.070 -7.877  17.812  0.50 18.30 ?  33  THR   A OG1  1 
ATOM   854  O  OG1  B THR   A 1 33  ? 26.771 -7.659  17.859  0.50 17.42 ?  33  THR   A OG1  1 
ATOM   855  C  CG2  A THR   A 1 33  ? 28.789 -7.678  16.152  0.50 17.46 ?  33  THR   A CG2  1 
ATOM   856  C  CG2  B THR   A 1 33  ? 28.624 -7.449  16.316  0.50 16.89 ?  33  THR   A CG2  1 
ATOM   857  H  H    A THR   A 1 33  ? 25.090 -6.579  16.819  0.50 18.09 ?  33  THR   A H    1 
ATOM   858  H  H    B THR   A 1 33  ? 24.870 -6.387  16.723  0.50 17.43 ?  33  THR   A H    1 
ATOM   859  H  HA   A THR   A 1 33  ? 27.434 -5.474  16.859  0.50 18.37 ?  33  THR   A HA   1 
ATOM   860  H  HA   B THR   A 1 33  ? 27.227 -5.257  16.929  0.50 17.39 ?  33  THR   A HA   1 
ATOM   861  H  HB   A THR   A 1 33  ? 26.796 -8.044  15.860  0.50 20.48 ?  33  THR   A HB   1 
ATOM   862  H  HB   B THR   A 1 33  ? 26.656 -7.830  15.895  0.50 19.34 ?  33  THR   A HB   1 
ATOM   863  H  HG1  A THR   A 1 33  ? 27.496 -7.379  18.339  0.50 21.95 ?  33  THR   A HG1  1 
ATOM   864  H  HG1  B THR   A 1 33  ? 27.188 -7.191  18.422  0.50 20.89 ?  33  THR   A HG1  1 
ATOM   865  H  HG21 A THR   A 1 33  ? 29.067 -8.561  16.441  0.50 20.94 ?  33  THR   A HG21 1 
ATOM   866  H  HG21 B THR   A 1 33  ? 28.895 -8.334  16.606  0.50 20.26 ?  33  THR   A HG21 1 
ATOM   867  H  HG22 A THR   A 1 33  ? 28.947 -7.593  15.201  0.50 20.94 ?  33  THR   A HG22 1 
ATOM   868  H  HG22 B THR   A 1 33  ? 28.841 -7.348  15.375  0.50 20.26 ?  33  THR   A HG22 1 
ATOM   869  H  HG23 A THR   A 1 33  ? 29.314 -7.013  16.625  0.50 20.94 ?  33  THR   A HG23 1 
ATOM   870  H  HG23 B THR   A 1 33  ? 29.115 -6.787  16.826  0.50 20.26 ?  33  THR   A HG23 1 
ATOM   871  N  N    . VAL   A 1 34  ? 26.240 -5.787  13.915  1.00 13.15 ?  34  VAL   A N    1 
ATOM   872  C  CA   . VAL   A 1 34  ? 26.436 -5.458  12.506  1.00 12.21 ?  34  VAL   A CA   1 
ATOM   873  C  C    . VAL   A 1 34  ? 25.138 -4.913  11.932  1.00 11.62 ?  34  VAL   A C    1 
ATOM   874  O  O    . VAL   A 1 34  ? 24.106 -5.595  11.963  1.00 12.26 ?  34  VAL   A O    1 
ATOM   875  C  CB   . VAL   A 1 34  ? 26.894 -6.670  11.672  1.00 12.65 ?  34  VAL   A CB   1 
ATOM   876  C  CG1  . VAL   A 1 34  ? 27.089 -6.259  10.216  1.00 13.20 ?  34  VAL   A CG1  1 
ATOM   877  C  CG2  . VAL   A 1 34  ? 28.168 -7.304  12.233  1.00 14.20 ?  34  VAL   A CG2  1 
ATOM   878  H  H    A VAL   A 1 34  ? 25.471 -6.136  14.089  0.50 15.77 ?  34  VAL   A H    1 
ATOM   879  H  H    B VAL   A 1 34  ? 25.552 -6.288  14.053  0.50 15.77 ?  34  VAL   A H    1 
ATOM   880  H  HA   . VAL   A 1 34  ? 27.115 -4.765  12.433  1.00 14.64 ?  34  VAL   A HA   1 
ATOM   881  H  HB   . VAL   A 1 34  ? 26.192 -7.338  11.698  1.00 15.17 ?  34  VAL   A HB   1 
ATOM   882  H  HG11 . VAL   A 1 34  ? 27.582 -6.958  9.758   1.00 15.83 ?  34  VAL   A HG11 1 
ATOM   883  H  HG12 . VAL   A 1 34  ? 26.225 -6.136  9.796   1.00 15.83 ?  34  VAL   A HG12 1 
ATOM   884  H  HG13 . VAL   A 1 34  ? 27.595 -5.430  10.185  1.00 15.83 ?  34  VAL   A HG13 1 
ATOM   885  H  HG21 . VAL   A 1 34  ? 28.445 -8.022  11.640  1.00 17.03 ?  34  VAL   A HG21 1 
ATOM   886  H  HG22 . VAL   A 1 34  ? 28.862 -6.629  12.279  1.00 17.03 ?  34  VAL   A HG22 1 
ATOM   887  H  HG23 . VAL   A 1 34  ? 27.985 -7.656  13.115  1.00 17.03 ?  34  VAL   A HG23 1 
ATOM   888  N  N    . VAL   A 1 35  ? 25.203 -3.706  11.371  1.00 10.99 ?  35  VAL   A N    1 
ATOM   889  C  CA   . VAL   A 1 35  ? 24.177 -3.197  10.470  1.00 10.81 ?  35  VAL   A CA   1 
ATOM   890  C  C    . VAL   A 1 35  ? 24.739 -3.205  9.055   1.00 10.03 ?  35  VAL   A C    1 
ATOM   891  O  O    . VAL   A 1 35  ? 25.890 -2.806  8.831   1.00 10.46 ?  35  VAL   A O    1 
ATOM   892  C  CB   . VAL   A 1 35  ? 23.638 -1.807  10.877  1.00 11.25 ?  35  VAL   A CB   1 
ATOM   893  C  CG1  . VAL   A 1 35  ? 24.688 -0.710  10.753  1.00 11.83 ?  35  VAL   A CG1  1 
ATOM   894  C  CG2  . VAL   A 1 35  ? 22.398 -1.455  10.045  1.00 11.95 ?  35  VAL   A CG2  1 
ATOM   895  H  H    . VAL   A 1 35  ? 25.850 -3.150  11.490  1.00 13.17 ?  35  VAL   A H    1 
ATOM   896  H  HA   . VAL   A 1 35  ? 23.424 -3.812  10.485  1.00 12.96 ?  35  VAL   A HA   1 
ATOM   897  H  HB   . VAL   A 1 35  ? 23.355 -1.842  11.802  1.00 13.49 ?  35  VAL   A HB   1 
ATOM   898  H  HG11 . VAL   A 1 35  ? 24.330 0.117   11.118  1.00 14.18 ?  35  VAL   A HG11 1 
ATOM   899  H  HG12 . VAL   A 1 35  ? 25.478 -0.974  11.248  1.00 14.18 ?  35  VAL   A HG12 1 
ATOM   900  H  HG13 . VAL   A 1 35  ? 24.912 -0.584  9.816   1.00 14.18 ?  35  VAL   A HG13 1 
ATOM   901  H  HG21 . VAL   A 1 35  ? 22.041 -0.607  10.349  1.00 14.33 ?  35  VAL   A HG21 1 
ATOM   902  H  HG22 . VAL   A 1 35  ? 22.654 -1.386  9.108   1.00 14.33 ?  35  VAL   A HG22 1 
ATOM   903  H  HG23 . VAL   A 1 35  ? 21.734 -2.153  10.152  1.00 14.33 ?  35  VAL   A HG23 1 
ATOM   904  N  N    . VAL   A 1 36  ? 23.928 -3.661  8.103   1.00 9.63  ?  36  VAL   A N    1 
ATOM   905  C  CA   . VAL   A 1 36  ? 24.308 -3.670  6.695   1.00 9.58  ?  36  VAL   A CA   1 
ATOM   906  C  C    . VAL   A 1 36  ? 23.845 -2.382  6.030   1.00 9.59  ?  36  VAL   A C    1 
ATOM   907  O  O    . VAL   A 1 36  ? 22.684 -1.975  6.168   1.00 10.11 ?  36  VAL   A O    1 
ATOM   908  C  CB   . VAL   A 1 36  ? 23.714 -4.888  5.977   1.00 9.68  ?  36  VAL   A CB   1 
ATOM   909  C  CG1  . VAL   A 1 36  ? 23.989 -4.816  4.491   1.00 10.27 ?  36  VAL   A CG1  1 
ATOM   910  C  CG2  . VAL   A 1 36  ? 24.257 -6.173  6.570   1.00 10.47 ?  36  VAL   A CG2  1 
ATOM   911  H  H    . VAL   A 1 36  ? 23.135 -3.968  8.250   1.00 11.55 ?  36  VAL   A H    1 
ATOM   912  H  HA   . VAL   A 1 36  ? 25.278 -3.726  6.632   1.00 11.48 ?  36  VAL   A HA   1 
ATOM   913  H  HB   . VAL   A 1 36  ? 22.749 -4.880  6.102   1.00 11.60 ?  36  VAL   A HB   1 
ATOM   914  H  HG11 . VAL   A 1 36  ? 23.860 -5.695  4.108   1.00 12.31 ?  36  VAL   A HG11 1 
ATOM   915  H  HG12 . VAL   A 1 36  ? 23.385 -4.180  4.083   1.00 12.31 ?  36  VAL   A HG12 1 
ATOM   916  H  HG13 . VAL   A 1 36  ? 24.911 -4.532  4.360   1.00 12.31 ?  36  VAL   A HG13 1 
ATOM   917  H  HG21 . VAL   A 1 36  ? 23.874 -6.928  6.090   1.00 12.55 ?  36  VAL   A HG21 1 
ATOM   918  H  HG22 . VAL   A 1 36  ? 25.219 -6.181  6.486   1.00 12.55 ?  36  VAL   A HG22 1 
ATOM   919  H  HG23 . VAL   A 1 36  ? 24.004 -6.224  7.508   1.00 12.55 ?  36  VAL   A HG23 1 
ATOM   920  N  N    . ASN   A 1 37  ? 24.766 -1.744  5.299   1.00 9.07  ?  37  ASN   A N    1 
ATOM   921  C  CA   . ASN   A 1 37  ? 24.440 -0.630  4.426   1.00 9.06  ?  37  ASN   A CA   1 
ATOM   922  C  C    . ASN   A 1 37  ? 24.318 -1.107  2.986   1.00 9.00  ?  37  ASN   A C    1 
ATOM   923  O  O    . ASN   A 1 37  ? 25.116 -1.930  2.514   1.00 9.38  ?  37  ASN   A O    1 
ATOM   924  C  CB   . ASN   A 1 37  ? 25.517 0.455   4.509   1.00 9.32  ?  37  ASN   A CB   1 
ATOM   925  C  CG   . ASN   A 1 37  ? 25.191 1.652   3.655   1.00 9.54  ?  37  ASN   A CG   1 
ATOM   926  O  OD1  . ASN   A 1 37  ? 24.012 1.977   3.462   1.00 10.07 ?  37  ASN   A OD1  1 
ATOM   927  N  ND2  . ASN   A 1 37  ? 26.221 2.316   3.136   1.00 9.86  ?  37  ASN   A ND2  1 
ATOM   928  H  H    . ASN   A 1 37  ? 25.606 -1.943  5.304   1.00 10.87 ?  37  ASN   A H    1 
ATOM   929  H  HA   . ASN   A 1 37  ? 23.600 -0.239  4.704   1.00 10.87 ?  37  ASN   A HA   1 
ATOM   930  H  HB2  . ASN   A 1 37  ? 25.597 0.758   5.431   1.00 11.17 ?  37  ASN   A HB2  1 
ATOM   931  H  HB3  . ASN   A 1 37  ? 26.365 0.090   4.209   1.00 11.17 ?  37  ASN   A HB3  1 
ATOM   932  H  HD21 . ASN   A 1 37  ? 26.077 3.001   2.634   1.00 11.82 ?  37  ASN   A HD21 1 
ATOM   933  H  HD22 . ASN   A 1 37  ? 27.019 2.058   3.284   1.00 11.82 ?  37  ASN   A HD22 1 
ATOM   934  N  N    A ALA   A 1 38  ? 23.298 -0.582  2.303   0.50 9.18  ?  38  ALA   A N    1 
ATOM   935  N  N    B ALA   A 1 38  ? 23.306 -0.590  2.284   0.50 9.33  ?  38  ALA   A N    1 
ATOM   936  C  CA   A ALA   A 1 38  ? 23.115 -0.722  0.861   0.50 9.29  ?  38  ALA   A CA   1 
ATOM   937  C  CA   B ALA   A 1 38  ? 23.145 -0.829  0.849   0.50 9.71  ?  38  ALA   A CA   1 
ATOM   938  C  C    A ALA   A 1 38  ? 24.035 0.286   0.179   0.50 8.99  ?  38  ALA   A C    1 
ATOM   939  C  C    B ALA   A 1 38  ? 23.981 0.196   0.085   0.50 9.52  ?  38  ALA   A C    1 
ATOM   940  O  O    A ALA   A 1 38  ? 23.648 1.409   -0.158  0.50 8.53  ?  38  ALA   A O    1 
ATOM   941  O  O    B ALA   A 1 38  ? 23.488 1.209   -0.426  0.50 9.56  ?  38  ALA   A O    1 
ATOM   942  C  CB   A ALA   A 1 38  ? 21.655 -0.483  0.494   0.50 10.20 ?  38  ALA   A CB   1 
ATOM   943  C  CB   B ALA   A 1 38  ? 21.677 -0.768  0.455   0.50 10.28 ?  38  ALA   A CB   1 
ATOM   944  H  H    A ALA   A 1 38  ? 22.681 -0.108  2.675   0.50 11.00 ?  38  ALA   A H    1 
ATOM   945  H  H    B ALA   A 1 38  ? 22.692 -0.090  2.629   0.50 11.19 ?  38  ALA   A H    1 
ATOM   946  H  HA   A ALA   A 1 38  ? 23.366 -1.613  0.584   0.50 11.14 ?  38  ALA   A HA   1 
ATOM   947  H  HA   B ALA   A 1 38  ? 23.480 -1.718  0.642   0.50 11.64 ?  38  ALA   A HA   1 
ATOM   948  H  HB1  A ALA   A 1 38  ? 21.552 -0.572  -0.466  0.50 12.23 ?  38  ALA   A HB1  1 
ATOM   949  H  HB1  B ALA   A 1 38  ? 21.607 -0.934  -0.499  0.50 12.32 ?  38  ALA   A HB1  1 
ATOM   950  H  HB2  A ALA   A 1 38  ? 21.104 -1.139  0.949   0.50 12.23 ?  38  ALA   A HB2  1 
ATOM   951  H  HB2  B ALA   A 1 38  ? 21.186 -1.445  0.946   0.50 12.32 ?  38  ALA   A HB2  1 
ATOM   952  H  HB3  A ALA   A 1 38  ? 21.400 0.412   0.771   0.50 12.23 ?  38  ALA   A HB3  1 
ATOM   953  H  HB3  B ALA   A 1 38  ? 21.333 0.112   0.664   0.50 12.32 ?  38  ALA   A HB3  1 
ATOM   954  N  N    A ALA   A 1 39  ? 25.289 -0.126  -0.005  0.50 9.42  ?  39  ALA   A N    1 
ATOM   955  N  N    B ALA   A 1 39  ? 25.279 -0.085  0.005   0.50 10.06 ?  39  ALA   A N    1 
ATOM   956  C  CA   A ALA   A 1 39  ? 26.364 0.741   -0.456  0.50 8.90  ?  39  ALA   A CA   1 
ATOM   957  C  CA   B ALA   A 1 39  ? 26.251 0.860   -0.511  0.50 10.08 ?  39  ALA   A CA   1 
ATOM   958  C  C    A ALA   A 1 39  ? 26.518 0.705   -1.974  0.50 9.43  ?  39  ALA   A C    1 
ATOM   959  C  C    B ALA   A 1 39  ? 26.393 0.744   -2.025  0.50 9.74  ?  39  ALA   A C    1 
ATOM   960  O  O    A ALA   A 1 39  ? 26.052 -0.211  -2.658  0.50 9.84  ?  39  ALA   A O    1 
ATOM   961  O  O    B ALA   A 1 39  ? 25.975 -0.237  -2.648  0.50 10.44 ?  39  ALA   A O    1 
ATOM   962  C  CB   A ALA   A 1 39  ? 27.680 0.309   0.201   0.50 8.92  ?  39  ALA   A CB   1 
ATOM   963  C  CB   B ALA   A 1 39  ? 27.607 0.615   0.149   0.50 11.12 ?  39  ALA   A CB   1 
ATOM   964  H  H    A ALA   A 1 39  ? 25.550 -0.936  0.134   0.50 11.29 ?  39  ALA   A H    1 
ATOM   965  H  H    B ALA   A 1 39  ? 25.623 -0.844  0.248   0.50 12.06 ?  39  ALA   A H    1 
ATOM   966  H  HA   A ALA   A 1 39  ? 26.179 1.654   -0.189  0.50 10.67 ?  39  ALA   A HA   1 
ATOM   967  H  HA   B ALA   A 1 39  ? 25.960 1.758   -0.290  0.50 12.08 ?  39  ALA   A HA   1 
ATOM   968  H  HB1  A ALA   A 1 39  ? 28.396 0.896   -0.101  0.50 10.69 ?  39  ALA   A HB1  1 
ATOM   969  H  HB1  B ALA   A 1 39  ? 28.245 1.255   -0.203  0.50 13.33 ?  39  ALA   A HB1  1 
ATOM   970  H  HB2  A ALA   A 1 39  ? 27.592 0.379   1.168   0.50 10.69 ?  39  ALA   A HB2  1 
ATOM   971  H  HB2  B ALA   A 1 39  ? 27.519 0.732   1.110   0.50 13.33 ?  39  ALA   A HB2  1 
ATOM   972  H  HB3  A ALA   A 1 39  ? 27.879 -0.605  -0.046  0.50 10.69 ?  39  ALA   A HB3  1 
ATOM   973  H  HB3  B ALA   A 1 39  ? 27.898 -0.288  -0.048  0.50 13.33 ?  39  ALA   A HB3  1 
ATOM   974  N  N    A ASN   A 1 40  ? 27.209 1.720   -2.494  0.50 9.81  ?  40  ASN   A N    1 
ATOM   975  N  N    B ASN   A 1 40  ? 27.001 1.773   -2.614  0.50 9.37  ?  40  ASN   A N    1 
ATOM   976  C  CA   A ASN   A 1 40  ? 27.769 1.690   -3.838  0.50 9.86  ?  40  ASN   A CA   1 
ATOM   977  C  CA   B ASN   A 1 40  ? 27.515 1.712   -3.974  0.50 9.50  ?  40  ASN   A CA   1 
ATOM   978  C  C    A ASN   A 1 40  ? 29.292 1.590   -3.754  0.50 9.24  ?  40  ASN   A C    1 
ATOM   979  C  C    B ASN   A 1 40  ? 29.039 1.593   -3.932  0.50 9.13  ?  40  ASN   A C    1 
ATOM   980  O  O    A ASN   A 1 40  ? 29.883 1.700   -2.676  0.50 9.37  ?  40  ASN   A O    1 
ATOM   981  O  O    B ASN   A 1 40  ? 29.661 1.704   -2.874  0.50 9.15  ?  40  ASN   A O    1 
ATOM   982  C  CB   A ASN   A 1 40  ? 27.292 2.875   -4.692  0.50 10.76 ?  40  ASN   A CB   1 
ATOM   983  C  CB   B ASN   A 1 40  ? 27.049 2.912   -4.810  0.50 9.98  ?  40  ASN   A CB   1 
ATOM   984  C  CG   A ASN   A 1 40  ? 27.630 4.222   -4.088  0.50 11.50 ?  40  ASN   A CG   1 
ATOM   985  C  CG   B ASN   A 1 40  ? 27.436 4.240   -4.202  0.50 10.29 ?  40  ASN   A CG   1 
ATOM   986  O  OD1  A ASN   A 1 40  ? 28.779 4.484   -3.729  0.50 11.79 ?  40  ASN   A OD1  1 
ATOM   987  O  OD1  B ASN   A 1 40  ? 28.618 4.556   -4.069  0.50 10.98 ?  40  ASN   A OD1  1 
ATOM   988  N  ND2  A ASN   A 1 40  ? 26.627 5.091   -3.980  0.50 12.48 ?  40  ASN   A ND2  1 
ATOM   989  N  ND2  B ASN   A 1 40  ? 26.436 5.040   -3.853  0.50 11.31 ?  40  ASN   A ND2  1 
ATOM   990  H  H    A ASN   A 1 40  ? 27.380 2.452   -2.073  0.50 11.76 ?  40  ASN   A H    1 
ATOM   991  H  H    B ASN   A 1 40  ? 27.127 2.532   -2.230  0.50 11.24 ?  40  ASN   A H    1 
ATOM   992  H  HA   A ASN   A 1 40  ? 27.461 0.885   -4.277  0.50 11.82 ?  40  ASN   A HA   1 
ATOM   993  H  HA   B ASN   A 1 40  ? 27.163 0.907   -4.395  0.50 11.39 ?  40  ASN   A HA   1 
ATOM   994  H  HB2  A ASN   A 1 40  ? 27.710 2.820   -5.571  0.50 12.91 ?  40  ASN   A HB2  1 
ATOM   995  H  HB2  B ASN   A 1 40  ? 27.450 2.851   -5.687  0.50 11.96 ?  40  ASN   A HB2  1 
ATOM   996  H  HB3  A ASN   A 1 40  ? 26.329 2.826   -4.787  0.50 12.91 ?  40  ASN   A HB3  1 
ATOM   997  H  HB3  B ASN   A 1 40  ? 26.079 2.883   -4.884  0.50 11.96 ?  40  ASN   A HB3  1 
ATOM   998  H  HD21 A ASN   A 1 40  ? 26.768 5.875   -3.653  0.50 14.96 ?  40  ASN   A HD21 1 
ATOM   999  H  HD21 B ASN   A 1 40  ? 26.607 5.807   -3.503  0.50 13.57 ?  40  ASN   A HD21 1 
ATOM   1000 H  HD22 A ASN   A 1 40  ? 25.836 4.865   -4.227  0.50 14.96 ?  40  ASN   A HD22 1 
ATOM   1001 H  HD22 B ASN   A 1 40  ? 25.622 4.792   -3.970  0.50 13.57 ?  40  ASN   A HD22 1 
ATOM   1002 N  N    A VAL   A 1 41  ? 29.925 1.356   -4.909  0.50 9.43  ?  41  VAL   A N    1 
ATOM   1003 N  N    B VAL   A 1 41  ? 29.642 1.346   -5.098  0.50 9.56  ?  41  VAL   A N    1 
ATOM   1004 C  CA   A VAL   A 1 41  ? 31.352 1.033   -4.912  0.50 9.77  ?  41  VAL   A CA   1 
ATOM   1005 C  CA   B VAL   A 1 41  ? 31.075 1.051   -5.142  0.50 10.12 ?  41  VAL   A CA   1 
ATOM   1006 C  C    A VAL   A 1 41  ? 32.194 2.191   -4.401  0.50 9.60  ?  41  VAL   A C    1 
ATOM   1007 C  C    B VAL   A 1 41  ? 31.939 2.207   -4.660  0.50 9.79  ?  41  VAL   A C    1 
ATOM   1008 O  O    A VAL   A 1 41  ? 33.300 1.978   -3.886  0.50 9.86  ?  41  VAL   A O    1 
ATOM   1009 O  O    B VAL   A 1 41  ? 33.112 1.997   -4.320  0.50 9.62  ?  41  VAL   A O    1 
ATOM   1010 C  CB   A VAL   A 1 41  ? 31.847 0.536   -6.292  0.50 10.02 ?  41  VAL   A CB   1 
ATOM   1011 C  CB   B VAL   A 1 41  ? 31.535 0.590   -6.545  0.50 11.58 ?  41  VAL   A CB   1 
ATOM   1012 C  CG1  A VAL   A 1 41  ? 31.161 -0.767  -6.682  0.50 10.43 ?  41  VAL   A CG1  1 
ATOM   1013 C  CG1  B VAL   A 1 41  ? 30.785 -0.662  -6.979  0.50 12.55 ?  41  VAL   A CG1  1 
ATOM   1014 C  CG2  A VAL   A 1 41  ? 31.674 1.595   -7.372  0.50 10.67 ?  41  VAL   A CG2  1 
ATOM   1015 C  CG2  B VAL   A 1 41  ? 31.382 1.703   -7.569  0.50 12.42 ?  41  VAL   A CG2  1 
ATOM   1016 H  H    A VAL   A 1 41  ? 29.563 1.371   -5.687  0.50 11.30 ?  41  VAL   A H    1 
ATOM   1017 H  H    B VAL   A 1 41  ? 29.241 1.324   -5.860  0.50 11.46 ?  41  VAL   A H    1 
ATOM   1018 H  HA   A VAL   A 1 41  ? 31.500 0.303   -4.295  0.50 11.71 ?  41  VAL   A HA   1 
ATOM   1019 H  HA   B VAL   A 1 41  ? 31.236 0.306   -4.542  0.50 12.13 ?  41  VAL   A HA   1 
ATOM   1020 H  HB   A VAL   A 1 41  ? 32.798 0.347   -6.232  0.50 12.01 ?  41  VAL   A HB   1 
ATOM   1021 H  HB   B VAL   A 1 41  ? 32.476 0.358   -6.495  0.50 13.89 ?  41  VAL   A HB   1 
ATOM   1022 H  HG11 A VAL   A 1 41  ? 31.506 -1.072  -7.536  0.50 12.50 ?  41  VAL   A HG11 1 
ATOM   1023 H  HG11 B VAL   A 1 41  ? 31.035 -0.879  -7.890  0.50 15.05 ?  41  VAL   A HG11 1 
ATOM   1024 H  HG12 A VAL   A 1 41  ? 31.333 -1.435  -5.999  0.50 12.50 ?  41  VAL   A HG12 1 
ATOM   1025 H  HG12 B VAL   A 1 41  ? 31.022 -1.394  -6.387  0.50 15.05 ?  41  VAL   A HG12 1 
ATOM   1026 H  HG13 A VAL   A 1 41  ? 30.203 -0.611  -6.753  0.50 12.50 ?  41  VAL   A HG13 1 
ATOM   1027 H  HG13 B VAL   A 1 41  ? 29.832 -0.497  -6.929  0.50 15.05 ?  41  VAL   A HG13 1 
ATOM   1028 H  HG21 A VAL   A 1 41  ? 31.938 1.221   -8.230  0.50 12.80 ?  41  VAL   A HG21 1 
ATOM   1029 H  HG21 B VAL   A 1 41  ? 31.577 1.344   -8.450  0.50 14.89 ?  41  VAL   A HG21 1 
ATOM   1030 H  HG22 A VAL   A 1 41  ? 30.743 1.863   -7.404  0.50 12.80 ?  41  VAL   A HG22 1 
ATOM   1031 H  HG22 B VAL   A 1 41  ? 30.476 2.037   -7.538  0.50 14.89 ?  41  VAL   A HG22 1 
ATOM   1032 H  HG23 A VAL   A 1 41  ? 32.232 2.358   -7.160  0.50 12.80 ?  41  VAL   A HG23 1 
ATOM   1033 H  HG23 B VAL   A 1 41  ? 32.009 2.412   -7.356  0.50 14.89 ?  41  VAL   A HG23 1 
ATOM   1034 N  N    A TYR   A 1 42  ? 31.708 3.422   -4.544  0.50 10.18 ?  42  TYR   A N    1 
ATOM   1035 N  N    B TYR   A 1 42  ? 31.409 3.431   -4.664  0.50 9.77  ?  42  TYR   A N    1 
ATOM   1036 C  CA   A TYR   A 1 42  ? 32.435 4.607   -4.105  0.50 10.06 ?  42  TYR   A CA   1 
ATOM   1037 C  CA   B TYR   A 1 42  ? 32.153 4.619   -4.256  0.50 9.93  ?  42  TYR   A CA   1 
ATOM   1038 C  C    A TYR   A 1 42  ? 32.120 4.973   -2.664  0.50 9.95  ?  42  TYR   A C    1 
ATOM   1039 C  C    B TYR   A 1 42  ? 31.927 4.995   -2.799  0.50 10.03 ?  42  TYR   A C    1 
ATOM   1040 O  O    A TYR   A 1 42  ? 32.688 5.942   -2.143  0.50 10.48 ?  42  TYR   A O    1 
ATOM   1041 O  O    B TYR   A 1 42  ? 32.477 6.004   -2.341  0.50 10.81 ?  42  TYR   A O    1 
ATOM   1042 C  CB   A TYR   A 1 42  ? 32.122 5.800   -5.026  0.50 10.78 ?  42  TYR   A CB   1 
ATOM   1043 C  CB   B TYR   A 1 42  ? 31.780 5.809   -5.152  0.50 10.40 ?  42  TYR   A CB   1 
ATOM   1044 C  CG   A TYR   A 1 42  ? 32.292 5.478   -6.497  0.50 10.86 ?  42  TYR   A CG   1 
ATOM   1045 C  CG   B TYR   A 1 42  ? 31.930 5.519   -6.626  0.50 10.89 ?  42  TYR   A CG   1 
ATOM   1046 C  CD1  A TYR   A 1 42  ? 33.553 5.288   -7.038  0.50 11.62 ?  42  TYR   A CD1  1 
ATOM   1047 C  CD1  B TYR   A 1 42  ? 33.180 5.319   -7.193  0.50 11.14 ?  42  TYR   A CD1  1 
ATOM   1048 C  CD2  A TYR   A 1 42  ? 31.194 5.335   -7.336  0.50 11.38 ?  42  TYR   A CD2  1 
ATOM   1049 C  CD2  B TYR   A 1 42  ? 30.816 5.427   -7.447  0.50 12.46 ?  42  TYR   A CD2  1 
ATOM   1050 C  CE1  A TYR   A 1 42  ? 33.721 4.975   -8.374  0.50 11.78 ?  42  TYR   A CE1  1 
ATOM   1051 C  CE1  B TYR   A 1 42  ? 33.316 5.045   -8.544  0.50 11.76 ?  42  TYR   A CE1  1 
ATOM   1052 C  CE2  A TYR   A 1 42  ? 31.355 5.022   -8.680  0.50 11.80 ?  42  TYR   A CE2  1 
ATOM   1053 C  CE2  B TYR   A 1 42  ? 30.941 5.159   -8.793  0.50 13.17 ?  42  TYR   A CE2  1 
ATOM   1054 C  CZ   A TYR   A 1 42  ? 32.626 4.848   -9.191  0.50 11.93 ?  42  TYR   A CZ   1 
ATOM   1055 C  CZ   B TYR   A 1 42  ? 32.188 4.966   -9.338  0.50 13.01 ?  42  TYR   A CZ   1 
ATOM   1056 O  OH   A TYR   A 1 42  ? 32.812 4.530   -10.516 0.50 13.06 ?  42  TYR   A OH   1 
ATOM   1057 O  OH   B TYR   A 1 42  ? 32.298 4.699   -10.684 0.50 14.05 ?  42  TYR   A OH   1 
ATOM   1058 H  H    A TYR   A 1 42  ? 30.946 3.599   -4.886  0.50 12.20 ?  42  TYR   A H    1 
ATOM   1059 H  H    B TYR   A 1 42  ? 30.604 3.603   -4.925  0.50 11.71 ?  42  TYR   A H    1 
ATOM   1060 H  HA   A TYR   A 1 42  ? 33.391 4.433   -4.162  0.50 12.06 ?  42  TYR   A HA   1 
ATOM   1061 H  HA   B TYR   A 1 42  ? 33.097 4.452   -4.375  0.50 11.90 ?  42  TYR   A HA   1 
ATOM   1062 H  HB2  A TYR   A 1 42  ? 31.205 6.076   -4.881  0.50 12.93 ?  42  TYR   A HB2  1 
ATOM   1063 H  HB2  B TYR   A 1 42  ? 30.854 6.052   -4.991  0.50 12.46 ?  42  TYR   A HB2  1 
ATOM   1064 H  HB3  A TYR   A 1 42  ? 32.725 6.533   -4.806  0.50 12.93 ?  42  TYR   A HB3  1 
ATOM   1065 H  HB3  B TYR   A 1 42  ? 32.358 6.559   -4.940  0.50 12.46 ?  42  TYR   A HB3  1 
ATOM   1066 H  HD1  A TYR   A 1 42  ? 34.304 5.374   -6.495  0.50 13.93 ?  42  TYR   A HD1  1 
ATOM   1067 H  HD1  B TYR   A 1 42  ? 33.938 5.371   -6.657  0.50 13.36 ?  42  TYR   A HD1  1 
ATOM   1068 H  HD2  A TYR   A 1 42  ? 30.338 5.458   -6.988  0.50 13.64 ?  42  TYR   A HD2  1 
ATOM   1069 H  HD2  B TYR   A 1 42  ? 29.967 5.560   -7.086  0.50 14.94 ?  42  TYR   A HD2  1 
ATOM   1070 H  HE1  A TYR   A 1 42  ? 34.575 4.858   -8.725  0.50 14.12 ?  42  TYR   A HE1  1 
ATOM   1071 H  HE1  B TYR   A 1 42  ? 34.161 4.915   -8.910  0.50 14.10 ?  42  TYR   A HE1  1 
ATOM   1072 H  HE2  A TYR   A 1 42  ? 30.607 4.939   -9.231  0.50 14.15 ?  42  TYR   A HE2  1 
ATOM   1073 H  HE2  B TYR   A 1 42  ? 30.184 5.106   -9.330  0.50 15.80 ?  42  TYR   A HE2  1 
ATOM   1074 H  HH   A TYR   A 1 42  ? 33.622 4.381   -10.663 0.50 15.66 ?  42  TYR   A HH   1 
ATOM   1075 H  HH   B TYR   A 1 42  ? 31.536 4.685   -11.033 0.50 16.85 ?  42  TYR   A HH   1 
ATOM   1076 N  N    A LEU   A 1 43  ? 31.228 4.227   -2.017  0.50 9.68  ?  43  LEU   A N    1 
ATOM   1077 N  N    B LEU   A 1 43  ? 31.119 4.226   -2.071  0.50 10.08 ?  43  LEU   A N    1 
ATOM   1078 C  CA   A LEU   A 1 43  ? 30.770 4.546   -0.668  0.50 9.44  ?  43  LEU   A CA   1 
ATOM   1079 C  CA   B LEU   A 1 43  ? 30.683 4.582   -0.720  0.50 9.78  ?  43  LEU   A CA   1 
ATOM   1080 C  C    A LEU   A 1 43  ? 30.291 5.994   -0.567  0.50 9.88  ?  43  LEU   A C    1 
ATOM   1081 C  C    B LEU   A 1 43  ? 30.185 6.025   -0.646  0.50 9.95  ?  43  LEU   A C    1 
ATOM   1082 O  O    A LEU   A 1 43  ? 30.551 6.690   0.417   0.50 10.76 ?  43  LEU   A O    1 
ATOM   1083 O  O    B LEU   A 1 43  ? 30.413 6.734   0.336   0.50 10.80 ?  43  LEU   A O    1 
ATOM   1084 C  CB   A LEU   A 1 43  ? 31.823 4.218   0.393   0.50 9.97  ?  43  LEU   A CB   1 
ATOM   1085 C  CB   B LEU   A 1 43  ? 31.745 4.292   0.342   0.50 10.18 ?  43  LEU   A CB   1 
ATOM   1086 C  CG   A LEU   A 1 43  ? 32.341 2.779   0.453   0.50 10.32 ?  43  LEU   A CG   1 
ATOM   1087 C  CG   B LEU   A 1 43  ? 32.218 2.842   0.478   0.50 10.46 ?  43  LEU   A CG   1 
ATOM   1088 C  CD1  A LEU   A 1 43  ? 33.401 2.668   1.534   0.50 10.97 ?  43  LEU   A CD1  1 
ATOM   1089 C  CD1  B LEU   A 1 43  ? 33.240 2.744   1.602   0.50 10.98 ?  43  LEU   A CD1  1 
ATOM   1090 C  CD2  A LEU   A 1 43  ? 31.223 1.782   0.699   0.50 10.45 ?  43  LEU   A CD2  1 
ATOM   1091 C  CD2  B LEU   A 1 43  ? 31.055 1.883   0.707   0.50 10.74 ?  43  LEU   A CD2  1 
ATOM   1092 H  H    A LEU   A 1 43  ? 30.862 3.519   -2.345  0.50 11.61 ?  43  LEU   A H    1 
ATOM   1093 H  H    B LEU   A 1 43  ? 30.796 3.477   -2.343  0.50 12.09 ?  43  LEU   A H    1 
ATOM   1094 H  HA   A LEU   A 1 43  ? 30.004 3.982   -0.480  0.50 11.31 ?  43  LEU   A HA   1 
ATOM   1095 H  HA   B LEU   A 1 43  ? 29.921 4.023   -0.505  0.50 11.72 ?  43  LEU   A HA   1 
ATOM   1096 H  HB2  A LEU   A 1 43  ? 32.590 4.787   0.246   0.50 11.95 ?  43  LEU   A HB2  1 
ATOM   1097 H  HB2  B LEU   A 1 43  ? 32.523 4.831   0.148   0.50 12.21 ?  43  LEU   A HB2  1 
ATOM   1098 H  HB3  A LEU   A 1 43  ? 31.440 4.411   1.263   0.50 11.95 ?  43  LEU   A HB3  1 
ATOM   1099 H  HB3  B LEU   A 1 43  ? 31.380 4.552   1.205   0.50 12.21 ?  43  LEU   A HB3  1 
ATOM   1100 H  HG   A LEU   A 1 43  ? 32.759 2.553   -0.393  0.50 12.38 ?  43  LEU   A HG   1 
ATOM   1101 H  HG   B LEU   A 1 43  ? 32.657 2.580   -0.343  0.50 12.55 ?  43  LEU   A HG   1 
ATOM   1102 H  HD11 A LEU   A 1 43  ? 33.726 1.754   1.566   0.50 13.16 ?  43  LEU   A HD11 1 
ATOM   1103 H  HD11 B LEU   A 1 43  ? 33.536 1.823   1.681   0.50 13.17 ?  43  LEU   A HD11 1 
ATOM   1104 H  HD12 A LEU   A 1 43  ? 34.130 3.271   1.321   0.50 13.16 ?  43  LEU   A HD12 1 
ATOM   1105 H  HD12 B LEU   A 1 43  ? 33.995 3.317   1.391   0.50 13.17 ?  43  LEU   A HD12 1 
ATOM   1106 H  HD13 A LEU   A 1 43  ? 33.007 2.910   2.386   0.50 13.16 ?  43  LEU   A HD13 1 
ATOM   1107 H  HD13 B LEU   A 1 43  ? 32.829 3.032   2.432   0.50 13.17 ?  43  LEU   A HD13 1 
ATOM   1108 H  HD21 A LEU   A 1 43  ? 31.604 0.895   0.802   0.50 12.52 ?  43  LEU   A HD21 1 
ATOM   1109 H  HD21 B LEU   A 1 43  ? 31.406 1.002   0.906   0.50 12.88 ?  43  LEU   A HD21 1 
ATOM   1110 H  HD22 A LEU   A 1 43  ? 30.750 2.033   1.508   0.50 12.52 ?  43  LEU   A HD22 1 
ATOM   1111 H  HD22 B LEU   A 1 43  ? 30.521 2.204   1.450   0.50 12.88 ?  43  LEU   A HD22 1 
ATOM   1112 H  HD23 A LEU   A 1 43  ? 30.617 1.796   -0.057  0.50 12.52 ?  43  LEU   A HD23 1 
ATOM   1113 H  HD23 B LEU   A 1 43  ? 30.513 1.848   -0.098  0.50 12.88 ?  43  LEU   A HD23 1 
ATOM   1114 N  N    A LYS   A 1 44  ? 29.576 6.448   -1.602  0.50 10.04 ?  44  LYS   A N    1 
ATOM   1115 N  N    B LYS   A 1 44  ? 29.468 6.452   -1.689  0.50 9.83  ?  44  LYS   A N    1 
ATOM   1116 C  CA   A LYS   A 1 44  ? 28.947 7.768   -1.605  0.50 10.34 ?  44  LYS   A CA   1 
ATOM   1117 C  CA   B LYS   A 1 44  ? 28.797 7.751   -1.709  0.50 10.44 ?  44  LYS   A CA   1 
ATOM   1118 C  C    A LYS   A 1 44  ? 27.506 7.591   -1.144  0.50 9.86  ?  44  LYS   A C    1 
ATOM   1119 C  C    B LYS   A 1 44  ? 27.392 7.544   -1.161  0.50 10.12 ?  44  LYS   A C    1 
ATOM   1120 O  O    A LYS   A 1 44  ? 26.655 7.093   -1.886  0.50 10.56 ?  44  LYS   A O    1 
ATOM   1121 O  O    B LYS   A 1 44  ? 26.512 7.016   -1.845  0.50 10.40 ?  44  LYS   A O    1 
ATOM   1122 C  CB   A LYS   A 1 44  ? 29.030 8.405   -2.987  0.50 11.99 ?  44  LYS   A CB   1 
ATOM   1123 C  CB   B LYS   A 1 44  ? 28.775 8.325   -3.122  0.50 12.53 ?  44  LYS   A CB   1 
ATOM   1124 C  CG   A LYS   A 1 44  ? 30.436 8.807   -3.398  0.50 14.59 ?  44  LYS   A CG   1 
ATOM   1125 C  CG   B LYS   A 1 44  ? 30.101 8.903   -3.580  0.50 15.32 ?  44  LYS   A CG   1 
ATOM   1126 C  CD   A LYS   A 1 44  ? 31.090 9.727   -2.375  0.50 19.37 ?  44  LYS   A CD   1 
ATOM   1127 C  CD   B LYS   A 1 44  ? 30.702 9.836   -2.531  0.50 19.48 ?  44  LYS   A CD   1 
ATOM   1128 C  CE   A LYS   A 1 44  ? 32.368 10.340  -2.915  0.50 22.47 ?  44  LYS   A CE   1 
ATOM   1129 C  CE   B LYS   A 1 44  ? 32.050 10.368  -2.963  0.50 21.70 ?  44  LYS   A CE   1 
ATOM   1130 N  NZ   A LYS   A 1 44  ? 33.092 11.109  -1.873  0.50 24.14 ?  44  LYS   A NZ   1 
ATOM   1131 N  NZ   B LYS   A 1 44  ? 32.971 10.546  -1.803  0.50 22.18 ?  44  LYS   A NZ   1 
ATOM   1132 H  H    A LYS   A 1 44  ? 29.454 5.999   -2.329  0.50 12.03 ?  44  LYS   A H    1 
ATOM   1133 H  H    B LYS   A 1 44  ? 29.356 5.997   -2.409  0.50 11.79 ?  44  LYS   A H    1 
ATOM   1134 H  HA   A LYS   A 1 44  ? 29.397 8.333   -0.961  0.50 12.40 ?  44  LYS   A HA   1 
ATOM   1135 H  HA   B LYS   A 1 44  ? 29.242 8.359   -1.102  0.50 12.52 ?  44  LYS   A HA   1 
ATOM   1136 H  HB2  A LYS   A 1 44  ? 28.695 7.774   -3.642  0.50 14.37 ?  44  LYS   A HB2  1 
ATOM   1137 H  HB2  B LYS   A 1 44  ? 28.532 7.618   -3.743  0.50 15.02 ?  44  LYS   A HB2  1 
ATOM   1138 H  HB3  A LYS   A 1 44  ? 28.480 9.204   -2.988  0.50 14.37 ?  44  LYS   A HB3  1 
ATOM   1139 H  HB3  B LYS   A 1 44  ? 28.114 9.035   -3.163  0.50 15.02 ?  44  LYS   A HB3  1 
ATOM   1140 H  HG2  A LYS   A 1 44  ? 30.986 8.010   -3.484  0.50 17.50 ?  44  LYS   A HG2  1 
ATOM   1141 H  HG2  B LYS   A 1 44  ? 30.727 8.181   -3.743  0.50 18.37 ?  44  LYS   A HG2  1 
ATOM   1142 H  HG3  A LYS   A 1 44  ? 30.400 9.278   -4.247  0.50 17.50 ?  44  LYS   A HG3  1 
ATOM   1143 H  HG3  B LYS   A 1 44  ? 29.963 9.416   -4.396  0.50 18.37 ?  44  LYS   A HG3  1 
ATOM   1144 H  HD2  A LYS   A 1 44  ? 30.468 10.438  -2.150  0.50 23.23 ?  44  LYS   A HD2  1 
ATOM   1145 H  HD2  B LYS   A 1 44  ? 30.095 10.578  -2.378  0.50 23.37 ?  44  LYS   A HD2  1 
ATOM   1146 H  HD3  A LYS   A 1 44  ? 31.308 9.210   -1.582  0.50 23.23 ?  44  LYS   A HD3  1 
ATOM   1147 H  HD3  B LYS   A 1 44  ? 30.853 9.348   -1.706  0.50 23.37 ?  44  LYS   A HD3  1 
ATOM   1148 H  HE2  A LYS   A 1 44  ? 32.946 9.629   -3.232  0.50 26.95 ?  44  LYS   A HE2  1 
ATOM   1149 H  HE2  B LYS   A 1 44  ? 32.459 9.738   -3.577  0.50 26.03 ?  44  LYS   A HE2  1 
ATOM   1150 H  HE3  A LYS   A 1 44  ? 32.143 10.940  -3.642  0.50 26.95 ?  44  LYS   A HE3  1 
ATOM   1151 H  HE3  B LYS   A 1 44  ? 31.929 11.226  -3.391  0.50 26.03 ?  44  LYS   A HE3  1 
ATOM   1152 H  HZ1  A LYS   A 1 44  ? 33.855 11.419  -2.205  0.50 28.96 ?  44  LYS   A HZ1  1 
ATOM   1153 H  HZ1  B LYS   A 1 44  ? 33.754 10.861  -2.083  0.50 26.60 ?  44  LYS   A HZ1  1 
ATOM   1154 H  HZ2  A LYS   A 1 44  ? 32.593 11.794  -1.600  0.50 28.96 ?  44  LYS   A HZ2  1 
ATOM   1155 H  HZ2  B LYS   A 1 44  ? 32.619 11.124  -1.222  0.50 26.60 ?  44  LYS   A HZ2  1 
ATOM   1156 H  HZ3  A LYS   A 1 44  ? 33.269 10.584  -1.176  0.50 28.96 ?  44  LYS   A HZ3  1 
ATOM   1157 H  HZ3  B LYS   A 1 44  ? 33.100 9.768   -1.392  0.50 26.60 ?  44  LYS   A HZ3  1 
ATOM   1158 N  N    A HIS   A 1 45  ? 27.240 7.969   0.101   0.50 9.66  ?  45  HIS   A N    1 
ATOM   1159 N  N    B HIS   A 1 45  ? 27.189 7.930   0.096   0.50 9.99  ?  45  HIS   A N    1 
ATOM   1160 C  CA   A HIS   A 1 45  ? 26.001 7.597   0.781   0.50 9.63  ?  45  HIS   A CA   1 
ATOM   1161 C  CA   B HIS   A 1 45  ? 25.956 7.612   0.815   0.50 10.11 ?  45  HIS   A CA   1 
ATOM   1162 C  C    A HIS   A 1 45  ? 24.960 8.708   0.646   0.50 9.89  ?  45  HIS   A C    1 
ATOM   1163 C  C    B HIS   A 1 45  ? 24.934 8.722   0.587   0.50 10.40 ?  45  HIS   A C    1 
ATOM   1164 O  O    A HIS   A 1 45  ? 24.588 9.379   1.609   0.50 10.72 ?  45  HIS   A O    1 
ATOM   1165 O  O    B HIS   A 1 45  ? 24.674 9.560   1.451   0.50 11.87 ?  45  HIS   A O    1 
ATOM   1166 C  CB   A HIS   A 1 45  ? 26.290 7.285   2.241   0.50 9.44  ?  45  HIS   A CB   1 
ATOM   1167 C  CB   B HIS   A 1 45  ? 26.249 7.435   2.296   0.50 9.98  ?  45  HIS   A CB   1 
ATOM   1168 C  CG   A HIS   A 1 45  ? 27.416 6.322   2.443   0.50 9.04  ?  45  HIS   A CG   1 
ATOM   1169 C  CG   B HIS   A 1 45  ? 27.354 6.473   2.576   0.50 9.79  ?  45  HIS   A CG   1 
ATOM   1170 N  ND1  A HIS   A 1 45  ? 27.420 5.049   1.911   0.50 9.46  ?  45  HIS   A ND1  1 
ATOM   1171 N  ND1  B HIS   A 1 45  ? 27.365 5.184   2.089   0.50 10.09 ?  45  HIS   A ND1  1 
ATOM   1172 C  CD2  A HIS   A 1 45  ? 28.583 6.458   3.116   0.50 9.66  ?  45  HIS   A CD2  1 
ATOM   1173 C  CD2  B HIS   A 1 45  ? 28.502 6.629   3.275   0.50 9.34  ?  45  HIS   A CD2  1 
ATOM   1174 C  CE1  A HIS   A 1 45  ? 28.543 4.442   2.258   0.50 9.71  ?  45  HIS   A CE1  1 
ATOM   1175 C  CE1  B HIS   A 1 45  ? 28.471 4.584   2.491   0.50 9.30  ?  45  HIS   A CE1  1 
ATOM   1176 N  NE2  A HIS   A 1 45  ? 29.266 5.276   2.986   0.50 9.89  ?  45  HIS   A NE2  1 
ATOM   1177 N  NE2  B HIS   A 1 45  ? 29.178 5.438   3.211   0.50 9.17  ?  45  HIS   A NE2  1 
ATOM   1178 H  H    A HIS   A 1 45  ? 27.769 8.449   0.581   0.50 11.58 ?  45  HIS   A H    1 
ATOM   1179 H  H    B HIS   A 1 45  ? 27.753 8.386   0.559   0.50 11.97 ?  45  HIS   A H    1 
ATOM   1180 H  HA   A HIS   A 1 45  ? 25.636 6.802   0.366   0.50 11.55 ?  45  HIS   A HA   1 
ATOM   1181 H  HA   B HIS   A 1 45  ? 25.591 6.781   0.472   0.50 12.13 ?  45  HIS   A HA   1 
ATOM   1182 H  HB2  A HIS   A 1 45  ? 26.515 8.105   2.702   0.50 11.32 ?  45  HIS   A HB2  1 
ATOM   1183 H  HB2  B HIS   A 1 45  ? 26.492 8.295   2.670   0.50 11.96 ?  45  HIS   A HB2  1 
ATOM   1184 H  HB3  A HIS   A 1 45  ? 25.494 6.891   2.638   0.50 11.32 ?  45  HIS   A HB3  1 
ATOM   1185 H  HB3  B HIS   A 1 45  ? 25.445 7.103   2.732   0.50 11.96 ?  45  HIS   A HB3  1 
ATOM   1186 H  HD2  A HIS   A 1 45  ? 28.872 7.212   3.578   0.50 11.58 ?  45  HIS   A HD2  1 
ATOM   1187 H  HD2  B HIS   A 1 45  ? 28.777 7.402   3.718   0.50 11.20 ?  45  HIS   A HD2  1 
ATOM   1188 H  HE1  A HIS   A 1 45  ? 28.788 3.567   2.035   0.50 11.64 ?  45  HIS   A HE1  1 
ATOM   1189 H  HE1  B HIS   A 1 45  ? 28.707 3.709   2.300   0.50 11.15 ?  45  HIS   A HE1  1 
ATOM   1190 H  HE2  A HIS   A 1 45  ? 30.042 5.101   3.328   0.50 11.86 ?  45  HIS   A HE2  1 
ATOM   1191 H  HE2  B HIS   A 1 45  ? 29.935 5.275   3.578   0.50 10.99 ?  45  HIS   A HE2  1 
ATOM   1192 N  N    A GLY   A 1 46  ? 24.473 8.881   -0.581  0.50 10.59 ?  46  GLY   A N    1 
ATOM   1193 N  N    B GLY   A 1 46  ? 24.343 8.724   -0.603  0.50 10.70 ?  46  GLY   A N    1 
ATOM   1194 C  CA   A GLY   A 1 46  ? 23.679 10.051  -0.911  0.50 11.15 ?  46  GLY   A CA   1 
ATOM   1195 C  CA   B GLY   A 1 46  ? 23.500 9.837   -0.992  0.50 11.28 ?  46  GLY   A CA   1 
ATOM   1196 C  C    A GLY   A 1 46  ? 22.181 9.913   -0.710  0.50 11.34 ?  46  GLY   A C    1 
ATOM   1197 C  C    B GLY   A 1 46  ? 22.039 9.724   -0.601  0.50 11.10 ?  46  GLY   A C    1 
ATOM   1198 O  O    A GLY   A 1 46  ? 21.491 10.910  -0.463  0.50 11.87 ?  46  GLY   A O    1 
ATOM   1199 O  O    B GLY   A 1 46  ? 21.423 10.720  -0.199  0.50 12.43 ?  46  GLY   A O    1 
ATOM   1200 H  H    A GLY   A 1 46  ? 24.584 8.331   -1.231  0.50 12.69 ?  46  GLY   A H    1 
ATOM   1201 H  H    B GLY   A 1 46  ? 24.414 8.099   -1.192  0.50 12.83 ?  46  GLY   A H    1 
ATOM   1202 H  HA2  A GLY   A 1 46  ? 23.993 10.799  -0.376  0.50 13.37 ?  46  GLY   A HA2  1 
ATOM   1203 H  HA2  B GLY   A 1 46  ? 23.841 10.643  -0.579  0.50 13.53 ?  46  GLY   A HA2  1 
ATOM   1204 H  HA3  A GLY   A 1 46  ? 23.827 10.272  -1.843  0.50 13.37 ?  46  GLY   A HA3  1 
ATOM   1205 H  HA3  B GLY   A 1 46  ? 23.548 9.944   -1.950  0.50 13.53 ?  46  GLY   A HA3  1 
ATOM   1206 N  N    A GLY   A 1 47  ? 21.659 8.697   -0.844  0.50 11.08 ?  47  GLY   A N    1 
ATOM   1207 N  N    B GLY   A 1 47  ? 21.467 8.528   -0.720  0.50 10.62 ?  47  GLY   A N    1 
ATOM   1208 C  CA   A GLY   A 1 47  ? 20.226 8.480   -0.819  0.50 10.95 ?  47  GLY   A CA   1 
ATOM   1209 C  CA   B GLY   A 1 47  ? 20.034 8.369   -0.561  0.50 10.63 ?  47  GLY   A CA   1 
ATOM   1210 C  C    A GLY   A 1 47  ? 19.913 7.054   -0.424  0.50 10.31 ?  47  GLY   A C    1 
ATOM   1211 C  C    B GLY   A 1 47  ? 19.683 6.953   -0.168  0.50 9.88  ?  47  GLY   A C    1 
ATOM   1212 O  O    A GLY   A 1 47  ? 20.808 6.249   -0.154  0.50 10.84 ?  47  GLY   A O    1 
ATOM   1213 O  O    B GLY   A 1 47  ? 20.552 6.090   -0.024  0.50 9.89  ?  47  GLY   A O    1 
ATOM   1214 H  H    A GLY   A 1 47  ? 22.120 7.986   -0.952  0.50 13.28 ?  47  GLY   A H    1 
ATOM   1215 H  H    B GLY   A 1 47  ? 21.887 7.795   -0.882  0.50 12.74 ?  47  GLY   A H    1 
ATOM   1216 H  HA2  A GLY   A 1 47  ? 19.810 9.090   -0.187  0.50 13.12 ?  47  GLY   A HA2  1 
ATOM   1217 H  HA2  B GLY   A 1 47  ? 19.705 8.967   0.125   0.50 12.74 ?  47  GLY   A HA2  1 
ATOM   1218 H  HA3  A GLY   A 1 47  ? 19.858 8.652   -1.703  0.50 13.12 ?  47  GLY   A HA3  1 
ATOM   1219 H  HA3  B GLY   A 1 47  ? 19.581 8.575   -1.396  0.50 12.74 ?  47  GLY   A HA3  1 
ATOM   1220 N  N    A GLY   A 1 48  ? 18.622 6.737   -0.407  0.50 9.82  ?  48  GLY   A N    1 
ATOM   1221 N  N    B GLY   A 1 48  ? 18.381 6.715   -0.011  0.50 9.98  ?  48  GLY   A N    1 
ATOM   1222 C  CA   A GLY   A 1 48  ? 18.210 5.399   -0.030  0.50 10.10 ?  48  GLY   A CA   1 
ATOM   1223 C  CA   B GLY   A 1 48  ? 17.934 5.399   0.408   0.50 9.63  ?  48  GLY   A CA   1 
ATOM   1224 C  C    A GLY   A 1 48  ? 18.619 5.065   1.391   0.50 9.43  ?  48  GLY   A C    1 
ATOM   1225 C  C    B GLY   A 1 48  ? 18.508 5.026   1.759   0.50 9.79  ?  48  GLY   A C    1 
ATOM   1226 O  O    A GLY   A 1 48  ? 18.760 5.945   2.251   0.50 9.88  ?  48  GLY   A O    1 
ATOM   1227 O  O    B GLY   A 1 48  ? 18.675 5.869   2.654   0.50 10.12 ?  48  GLY   A O    1 
ATOM   1228 H  H    A GLY   A 1 48  ? 17.980 7.271   -0.602  0.50 11.77 ?  48  GLY   A H    1 
ATOM   1229 H  H    B GLY   A 1 48  ? 17.738 7.286   -0.147  0.50 11.97 ?  48  GLY   A H    1 
ATOM   1230 H  HA2  A GLY   A 1 48  ? 17.251 5.319   -0.094  0.50 12.11 ?  48  GLY   A HA2  1 
ATOM   1231 H  HA2  B GLY   A 1 48  ? 16.965 5.377   0.458   0.50 11.55 ?  48  GLY   A HA2  1 
ATOM   1232 H  HA3  A GLY   A 1 48  ? 18.623 4.750   -0.618  0.50 12.11 ?  48  GLY   A HA3  1 
ATOM   1233 H  HA3  B GLY   A 1 48  ? 18.223 4.737   -0.241  0.50 11.55 ?  48  GLY   A HA3  1 
ATOM   1234 N  N    A VAL   A 1 49  ? 18.811 3.766   1.645   0.50 9.93  ?  49  VAL   A N    1 
ATOM   1235 N  N    B VAL   A 1 49  ? 18.802 3.734   1.912   0.50 9.91  ?  49  VAL   A N    1 
ATOM   1236 C  CA   A VAL   A 1 49  ? 19.284 3.323   2.954   0.50 10.29 ?  49  VAL   A CA   1 
ATOM   1237 C  CA   B VAL   A 1 49  ? 19.405 3.225   3.141   0.50 9.98  ?  49  VAL   A CA   1 
ATOM   1238 C  C    A VAL   A 1 49  ? 20.602 4.001   3.311   0.50 9.44  ?  49  VAL   A C    1 
ATOM   1239 C  C    B VAL   A 1 49  ? 20.665 4.009   3.485   0.50 9.65  ?  49  VAL   A C    1 
ATOM   1240 O  O    A VAL   A 1 49  ? 20.811 4.414   4.456   0.50 9.64  ?  49  VAL   A O    1 
ATOM   1241 O  O    B VAL   A 1 49  ? 20.852 4.453   4.623   0.50 10.03 ?  49  VAL   A O    1 
ATOM   1242 C  CB   A VAL   A 1 49  ? 19.403 1.784   2.993   0.50 11.63 ?  49  VAL   A CB   1 
ATOM   1243 C  CB   B VAL   A 1 49  ? 19.705 1.721   2.992   0.50 10.35 ?  49  VAL   A CB   1 
ATOM   1244 C  CG1  A VAL   A 1 49  ? 20.140 1.331   4.254   0.50 12.12 ?  49  VAL   A CG1  1 
ATOM   1245 C  CG1  B VAL   A 1 49  ? 20.546 1.229   4.157   0.50 10.17 ?  49  VAL   A CG1  1 
ATOM   1246 C  CG2  A VAL   A 1 49  ? 18.024 1.129   2.927   0.50 12.69 ?  49  VAL   A CG2  1 
ATOM   1247 C  CG2  B VAL   A 1 49  ? 18.408 0.920   2.868   0.50 10.99 ?  49  VAL   A CG2  1 
ATOM   1248 H  H    A VAL   A 1 49  ? 18.668 3.130   1.087   0.50 11.90 ?  49  VAL   A H    1 
ATOM   1249 H  H    B VAL   A 1 49  ? 18.651 3.135   1.318   0.50 11.88 ?  49  VAL   A H    1 
ATOM   1250 H  HA   A VAL   A 1 49  ? 18.633 3.571   3.628   0.50 12.34 ?  49  VAL   A HA   1 
ATOM   1251 H  HA   B VAL   A 1 49  ? 18.777 3.332   3.872   0.50 11.97 ?  49  VAL   A HA   1 
ATOM   1252 H  HB   A VAL   A 1 49  ? 19.915 1.479   2.228   0.50 13.95 ?  49  VAL   A HB   1 
ATOM   1253 H  HB   B VAL   A 1 49  ? 20.212 1.582   2.178   0.50 12.41 ?  49  VAL   A HB   1 
ATOM   1254 H  HG11 A VAL   A 1 49  ? 19.965 0.385   4.402   0.50 14.53 ?  49  VAL   A HG11 1 
ATOM   1255 H  HG11 B VAL   A 1 49  ? 20.479 0.259   4.205   0.50 12.19 ?  49  VAL   A HG11 1 
ATOM   1256 H  HG12 A VAL   A 1 49  ? 21.091 1.473   4.140   0.50 14.53 ?  49  VAL   A HG12 1 
ATOM   1257 H  HG12 B VAL   A 1 49  ? 21.469 1.486   4.015   0.50 12.19 ?  49  VAL   A HG12 1 
ATOM   1258 H  HG13 A VAL   A 1 49  ? 19.814 1.842   5.012   0.50 14.53 ?  49  VAL   A HG13 1 
ATOM   1259 H  HG13 B VAL   A 1 49  ? 20.210 1.620   4.978   0.50 12.19 ?  49  VAL   A HG13 1 
ATOM   1260 H  HG21 A VAL   A 1 49  ? 18.130 0.164   2.947   0.50 15.22 ?  49  VAL   A HG21 1 
ATOM   1261 H  HG21 B VAL   A 1 49  ? 18.625 -0.015  2.739   0.50 13.17 ?  49  VAL   A HG21 1 
ATOM   1262 H  HG22 A VAL   A 1 49  ? 17.502 1.420   3.690   0.50 15.22 ?  49  VAL   A HG22 1 
ATOM   1263 H  HG22 B VAL   A 1 49  ? 17.890 1.032   3.680   0.50 13.17 ?  49  VAL   A HG22 1 
ATOM   1264 H  HG23 A VAL   A 1 49  ? 17.591 1.398   2.104   0.50 15.22 ?  49  VAL   A HG23 1 
ATOM   1265 H  HG23 B VAL   A 1 49  ? 17.904 1.250   2.106   0.50 13.17 ?  49  VAL   A HG23 1 
ATOM   1266 N  N    A ALA   A 1 50  ? 21.527 4.085   2.354   0.50 8.95  ?  50  ALA   A N    1 
ATOM   1267 N  N    B ALA   A 1 50  ? 21.565 4.151   2.513   0.50 9.26  ?  50  ALA   A N    1 
ATOM   1268 C  CA   A ALA   A 1 50  ? 22.845 4.637   2.646   0.50 8.98  ?  50  ALA   A CA   1 
ATOM   1269 C  CA   B ALA   A 1 50  ? 22.872 4.730   2.797   0.50 9.22  ?  50  ALA   A CA   1 
ATOM   1270 C  C    A ALA   A 1 50  ? 22.754 6.095   3.073   0.50 9.12  ?  50  ALA   A C    1 
ATOM   1271 C  C    B ALA   A 1 50  ? 22.748 6.182   3.231   0.50 9.30  ?  50  ALA   A C    1 
ATOM   1272 O  O    A ALA   A 1 50  ? 23.399 6.512   4.040   0.50 9.17  ?  50  ALA   A O    1 
ATOM   1273 O  O    B ALA   A 1 50  ? 23.366 6.605   4.216   0.50 9.59  ?  50  ALA   A O    1 
ATOM   1274 C  CB   A ALA   A 1 50  ? 23.740 4.492   1.422   0.50 9.45  ?  50  ALA   A CB   1 
ATOM   1275 C  CB   B ALA   A 1 50  ? 23.760 4.605   1.564   0.50 9.57  ?  50  ALA   A CB   1 
ATOM   1276 H  H    A ALA   A 1 50  ? 21.416 3.824   1.546   0.50 10.73 ?  50  ALA   A H    1 
ATOM   1277 H  H    B ALA   A 1 50  ? 21.437 3.933   1.690   0.50 11.11 ?  50  ALA   A H    1 
ATOM   1278 H  HA   A ALA   A 1 50  ? 23.244 4.141   3.378   0.50 10.77 ?  50  ALA   A HA   1 
ATOM   1279 H  HA   B ALA   A 1 50  ? 23.283 4.239   3.521   0.50 11.05 ?  50  ALA   A HA   1 
ATOM   1280 H  HB1  A ALA   A 1 50  ? 24.609 4.867   1.626   0.50 11.33 ?  50  ALA   A HB1  1 
ATOM   1281 H  HB1  B ALA   A 1 50  ? 24.625 4.990   1.761   0.50 11.47 ?  50  ALA   A HB1  1 
ATOM   1282 H  HB2  A ALA   A 1 50  ? 23.822 3.554   1.203   0.50 11.33 ?  50  ALA   A HB2  1 
ATOM   1283 H  HB2  B ALA   A 1 50  ? 23.855 3.665   1.343   0.50 11.47 ?  50  ALA   A HB2  1 
ATOM   1284 H  HB3  A ALA   A 1 50  ? 23.335 4.974   0.683   0.50 11.33 ?  50  ALA   A HB3  1 
ATOM   1285 H  HB3  B ALA   A 1 50  ? 23.343 5.078   0.827   0.50 11.47 ?  50  ALA   A HB3  1 
ATOM   1286 N  N    A GLY   A 1 51  ? 21.974 6.896   2.348   0.50 9.19  ?  51  GLY   A N    1 
ATOM   1287 N  N    B GLY   A 1 51  ? 21.952 6.966   2.503   0.50 9.61  ?  51  GLY   A N    1 
ATOM   1288 C  CA   A GLY   A 1 51  ? 21.822 8.286   2.735   0.50 9.51  ?  51  GLY   A CA   1 
ATOM   1289 C  CA   B GLY   A 1 51  ? 21.770 8.356   2.882   0.50 10.04 ?  51  GLY   A CA   1 
ATOM   1290 C  C    A GLY   A 1 51  ? 21.199 8.433   4.108   0.50 9.16  ?  51  GLY   A C    1 
ATOM   1291 C  C    B GLY   A 1 51  ? 21.170 8.494   4.267   0.50 9.84  ?  51  GLY   A C    1 
ATOM   1292 O  O    A GLY   A 1 51  ? 21.552 9.339   4.867   0.50 9.69  ?  51  GLY   A O    1 
ATOM   1293 O  O    B GLY   A 1 51  ? 21.559 9.375   5.040   0.50 10.31 ?  51  GLY   A O    1 
ATOM   1294 H  H    A GLY   A 1 51  ? 21.538 6.664   1.646   0.50 11.01 ?  51  GLY   A H    1 
ATOM   1295 H  H    B GLY   A 1 51  ? 21.514 6.721   1.802   0.50 11.53 ?  51  GLY   A H    1 
ATOM   1296 H  HA2  A GLY   A 1 51  ? 22.689 8.718   2.746   0.50 11.40 ?  51  GLY   A HA2  1 
ATOM   1297 H  HA2  B GLY   A 1 51  ? 22.627 8.810   2.869   0.50 12.04 ?  51  GLY   A HA2  1 
ATOM   1298 H  HA3  A GLY   A 1 51  ? 21.256 8.743   2.094   0.50 11.40 ?  51  GLY   A HA3  1 
ATOM   1299 H  HA3  B GLY   A 1 51  ? 21.184 8.793   2.239   0.50 12.04 ?  51  GLY   A HA3  1 
ATOM   1300 N  N    A ALA   A 1 52  ? 20.250 7.551   4.439   0.50 9.45  ?  52  ALA   A N    1 
ATOM   1301 N  N    B ALA   A 1 52  ? 20.210 7.625   4.598   0.50 9.68  ?  52  ALA   A N    1 
ATOM   1302 C  CA   A ALA   A 1 52  ? 19.585 7.607   5.737   0.50 10.02 ?  52  ALA   A CA   1 
ATOM   1303 C  CA   B ALA   A 1 52  ? 19.557 7.706   5.900   0.50 10.10 ?  52  ALA   A CA   1 
ATOM   1304 C  C    A ALA   A 1 52  ? 20.534 7.209   6.863   0.50 10.16 ?  52  ALA   A C    1 
ATOM   1305 C  C    B ALA   A 1 52  ? 20.490 7.258   7.021   0.50 9.73  ?  52  ALA   A C    1 
ATOM   1306 O  O    A ALA   A 1 52  ? 20.613 7.891   7.890   0.50 10.46 ?  52  ALA   A O    1 
ATOM   1307 O  O    B ALA   A 1 52  ? 20.536 7.885   8.085   0.50 10.46 ?  52  ALA   A O    1 
ATOM   1308 C  CB   A ALA   A 1 52  ? 18.344 6.711   5.725   0.50 10.74 ?  52  ALA   A CB   1 
ATOM   1309 C  CB   B ALA   A 1 52  ? 18.265 6.889   5.890   0.50 11.13 ?  52  ALA   A CB   1 
ATOM   1310 H  H    A ALA   A 1 52  ? 19.985 6.909   3.937   0.50 11.33 ?  52  ALA   A H    1 
ATOM   1311 H  H    B ALA   A 1 52  ? 19.931 6.988   4.089   0.50 11.61 ?  52  ALA   A H    1 
ATOM   1312 H  HA   A ALA   A 1 52  ? 19.291 8.514   5.905   0.50 12.02 ?  52  ALA   A HA   1 
ATOM   1313 H  HA   B ALA   A 1 52  ? 19.316 8.629   6.062   0.50 12.11 ?  52  ALA   A HA   1 
ATOM   1314 H  HB1  A ALA   A 1 52  ? 17.905 6.757   6.592   0.50 12.88 ?  52  ALA   A HB1  1 
ATOM   1315 H  HB1  B ALA   A 1 52  ? 17.840 6.961   6.760   0.50 13.34 ?  52  ALA   A HB1  1 
ATOM   1316 H  HB2  A ALA   A 1 52  ? 17.734 7.022   5.035   0.50 12.88 ?  52  ALA   A HB2  1 
ATOM   1317 H  HB2  B ALA   A 1 52  ? 17.671 7.238   5.205   0.50 13.34 ?  52  ALA   A HB2  1 
ATOM   1318 H  HB3  A ALA   A 1 52  ? 18.610 5.796   5.541   0.50 12.88 ?  52  ALA   A HB3  1 
ATOM   1319 H  HB3  B ALA   A 1 52  ? 18.475 5.960   5.702   0.50 13.34 ?  52  ALA   A HB3  1 
ATOM   1320 N  N    A LEU   A 1 53  ? 21.263 6.102   6.694   0.50 10.30 ?  53  LEU   A N    1 
ATOM   1321 N  N    B LEU   A 1 53  ? 21.242 6.175   6.809   0.50 9.25  ?  53  LEU   A N    1 
ATOM   1322 C  CA   A LEU   A 1 53  ? 22.206 5.684   7.729   0.50 10.94 ?  53  LEU   A CA   1 
ATOM   1323 C  CA   B LEU   A 1 53  ? 22.226 5.770   7.810   0.50 9.36  ?  53  LEU   A CA   1 
ATOM   1324 C  C    A LEU   A 1 53  ? 23.266 6.750   7.949   0.50 10.75 ?  53  LEU   A C    1 
ATOM   1325 C  C    B LEU   A 1 53  ? 23.264 6.866   8.001   0.50 8.83  ?  53  LEU   A C    1 
ATOM   1326 O  O    A LEU   A 1 53  ? 23.631 7.051   9.089   0.50 11.32 ?  53  LEU   A O    1 
ATOM   1327 O  O    B LEU   A 1 53  ? 23.553 7.277   9.129   0.50 9.12  ?  53  LEU   A O    1 
ATOM   1328 C  CB   A LEU   A 1 53  ? 22.874 4.359   7.350   0.50 11.60 ?  53  LEU   A CB   1 
ATOM   1329 C  CB   B LEU   A 1 53  ? 22.910 4.460   7.409   0.50 9.43  ?  53  LEU   A CB   1 
ATOM   1330 C  CG   A LEU   A 1 53  ? 21.992 3.107   7.380   0.50 12.05 ?  53  LEU   A CG   1 
ATOM   1331 C  CG   B LEU   A 1 53  ? 22.118 3.147   7.491   0.50 9.92  ?  53  LEU   A CG   1 
ATOM   1332 C  CD1  A LEU   A 1 53  ? 22.736 1.922   6.795   0.50 12.64 ?  53  LEU   A CD1  1 
ATOM   1333 C  CD1  B LEU   A 1 53  ? 22.934 2.029   6.873   0.50 10.85 ?  53  LEU   A CD1  1 
ATOM   1334 C  CD2  A LEU   A 1 53  ? 21.517 2.789   8.792   0.50 12.90 ?  53  LEU   A CD2  1 
ATOM   1335 C  CD2  B LEU   A 1 53  ? 21.746 2.790   8.923   0.50 10.99 ?  53  LEU   A CD2  1 
ATOM   1336 H  H    A LEU   A 1 53  ? 21.229 5.588   6.009   0.50 12.35 ?  53  LEU   A H    1 
ATOM   1337 H  H    B LEU   A 1 53  ? 21.198 5.670   6.113   0.50 11.09 ?  53  LEU   A H    1 
ATOM   1338 H  HA   A LEU   A 1 53  ? 21.732 5.555   8.564   0.50 13.12 ?  53  LEU   A HA   1 
ATOM   1339 H  HA   B LEU   A 1 53  ? 21.775 5.634   8.654   0.50 11.23 ?  53  LEU   A HA   1 
ATOM   1340 H  HB2  A LEU   A 1 53  ? 23.221 4.441   6.447   0.50 13.91 ?  53  LEU   A HB2  1 
ATOM   1341 H  HB2  B LEU   A 1 53  ? 23.200 4.549   6.487   0.50 11.31 ?  53  LEU   A HB2  1 
ATOM   1342 H  HB3  A LEU   A 1 53  ? 23.610 4.203   7.962   0.50 13.91 ?  53  LEU   A HB3  1 
ATOM   1343 H  HB3  B LEU   A 1 53  ? 23.687 4.350   7.974   0.50 11.31 ?  53  LEU   A HB3  1 
ATOM   1344 H  HG   A LEU   A 1 53  ? 21.208 3.261   6.829   0.50 14.45 ?  53  LEU   A HG   1 
ATOM   1345 H  HG   B LEU   A 1 53  ? 21.300 3.235   6.978   0.50 11.89 ?  53  LEU   A HG   1 
ATOM   1346 H  HD11 A LEU   A 1 53  ? 22.162 1.143   6.824   0.50 15.16 ?  53  LEU   A HD11 1 
ATOM   1347 H  HD11 B LEU   A 1 53  ? 22.432 1.201   6.934   0.50 13.00 ?  53  LEU   A HD11 1 
ATOM   1348 H  HD12 A LEU   A 1 53  ? 22.977 2.125   5.877   0.50 15.16 ?  53  LEU   A HD12 1 
ATOM   1349 H  HD12 B LEU   A 1 53  ? 23.109 2.243   5.943   0.50 13.00 ?  53  LEU   A HD12 1 
ATOM   1350 H  HD13 A LEU   A 1 53  ? 23.537 1.766   7.320   0.50 15.16 ?  53  LEU   A HD13 1 
ATOM   1351 H  HD13 B LEU   A 1 53  ? 23.770 1.945   7.357   0.50 13.00 ?  53  LEU   A HD13 1 
ATOM   1352 H  HD21 A LEU   A 1 53  ? 21.007 1.964   8.776   0.50 15.47 ?  53  LEU   A HD21 1 
ATOM   1353 H  HD21 B LEU   A 1 53  ? 21.212 1.979   8.917   0.50 13.17 ?  53  LEU   A HD21 1 
ATOM   1354 H  HD22 A LEU   A 1 53  ? 22.289 2.689   9.369   0.50 15.47 ?  53  LEU   A HD22 1 
ATOM   1355 H  HD22 B LEU   A 1 53  ? 22.554 2.652   9.435   0.50 13.17 ?  53  LEU   A HD22 1 
ATOM   1356 H  HD23 A LEU   A 1 53  ? 20.958 3.516   9.108   0.50 15.47 ?  53  LEU   A HD23 1 
ATOM   1357 H  HD23 B LEU   A 1 53  ? 21.230 3.519   9.304   0.50 13.17 ?  53  LEU   A HD23 1 
ATOM   1358 N  N    A ASN   A 1 54  ? 23.762 7.343   6.868   0.50 10.21 ?  54  ASN   A N    1 
ATOM   1359 N  N    B ASN   A 1 54  ? 23.818 7.372   6.902   0.50 8.86  ?  54  ASN   A N    1 
ATOM   1360 C  CA   A ASN   A 1 54  ? 24.816 8.335   7.019   0.50 10.03 ?  54  ASN   A CA   1 
ATOM   1361 C  CA   B ASN   A 1 54  ? 24.858 8.381   7.032   0.50 9.19  ?  54  ASN   A CA   1 
ATOM   1362 C  C    A ASN   A 1 54  ? 24.307 9.577   7.753   0.50 10.27 ?  54  ASN   A C    1 
ATOM   1363 C  C    B ASN   A 1 54  ? 24.329 9.627   7.736   0.50 9.96  ?  54  ASN   A C    1 
ATOM   1364 O  O    A ASN   A 1 54  ? 24.986 10.105  8.643   0.50 10.56 ?  54  ASN   A O    1 
ATOM   1365 O  O    B ASN   A 1 54  ? 25.018 10.214  8.580   0.50 10.22 ?  54  ASN   A O    1 
ATOM   1366 C  CB   A ASN   A 1 54  ? 25.389 8.697   5.655   0.50 10.03 ?  54  ASN   A CB   1 
ATOM   1367 C  CB   B ASN   A 1 54  ? 25.431 8.750   5.671   0.50 9.25  ?  54  ASN   A CB   1 
ATOM   1368 C  CG   A ASN   A 1 54  ? 26.449 9.759   5.758   0.50 10.34 ?  54  ASN   A CG   1 
ATOM   1369 C  CG   B ASN   A 1 54  ? 26.398 9.896   5.775   0.50 9.19  ?  54  ASN   A CG   1 
ATOM   1370 O  OD1  A ASN   A 1 54  ? 27.442 9.582   6.465   0.50 10.77 ?  54  ASN   A OD1  1 
ATOM   1371 O  OD1  B ASN   A 1 54  ? 27.412 9.783   6.466   0.50 9.13  ?  54  ASN   A OD1  1 
ATOM   1372 N  ND2  A ASN   A 1 54  ? 26.246 10.877  5.081   0.50 10.78 ?  54  ASN   A ND2  1 
ATOM   1373 N  ND2  B ASN   A 1 54  ? 26.077 11.021  5.142   0.50 10.07 ?  54  ASN   A ND2  1 
ATOM   1374 H  H    A ASN   A 1 54  ? 23.508 7.191   6.059   0.50 12.24 ?  54  ASN   A H    1 
ATOM   1375 H  H    B ASN   A 1 54  ? 23.611 7.158   6.093   0.50 10.63 ?  54  ASN   A H    1 
ATOM   1376 H  HA   A ASN   A 1 54  ? 25.525 7.949   7.548   0.50 12.02 ?  54  ASN   A HA   1 
ATOM   1377 H  HA   B ASN   A 1 54  ? 25.572 8.021   7.571   0.50 11.02 ?  54  ASN   A HA   1 
ATOM   1378 H  HB2  A ASN   A 1 54  ? 25.787 7.901   5.260   0.50 12.02 ?  54  ASN   A HB2  1 
ATOM   1379 H  HB2  B ASN   A 1 54  ? 25.909 7.985   5.312   0.50 11.08 ?  54  ASN   A HB2  1 
ATOM   1380 H  HB3  A ASN   A 1 54  ? 24.678 9.029   5.087   0.50 12.02 ?  54  ASN   A HB3  1 
ATOM   1381 H  HB3  B ASN   A 1 54  ? 24.713 9.009   5.077   0.50 11.08 ?  54  ASN   A HB3  1 
ATOM   1382 H  HD21 A ASN   A 1 54  ? 26.828 11.506  5.118   0.50 12.93 ?  54  ASN   A HD21 1 
ATOM   1383 H  HD21 B ASN   A 1 54  ? 26.599 11.706  5.181   0.50 12.07 ?  54  ASN   A HD21 1 
ATOM   1384 H  HD22 A ASN   A 1 54  ? 25.537 10.966  4.605   0.50 12.93 ?  54  ASN   A HD22 1 
ATOM   1385 H  HD22 B ASN   A 1 54  ? 25.354 11.061  4.679   0.50 12.07 ?  54  ASN   A HD22 1 
ATOM   1386 N  N    . LYS   A 1 55  ? 23.111 10.055  7.393   1.00 10.16 ?  55  LYS   A N    1 
ATOM   1387 C  CA   . LYS   A 1 55  ? 22.525 11.212  8.064   1.00 11.09 ?  55  LYS   A CA   1 
ATOM   1388 C  C    . LYS   A 1 55  ? 22.426 10.973  9.563   1.00 11.14 ?  55  LYS   A C    1 
ATOM   1389 O  O    . LYS   A 1 55  ? 22.707 11.870  10.367  1.00 11.83 ?  55  LYS   A O    1 
ATOM   1390 C  CB   . LYS   A 1 55  ? 21.152 11.512  7.456   1.00 12.20 ?  55  LYS   A CB   1 
ATOM   1391 C  CG   . LYS   A 1 55  ? 20.416 12.691  8.076   1.00 13.85 ?  55  LYS   A CG   1 
ATOM   1392 C  CD   . LYS   A 1 55  ? 19.110 12.966  7.334   1.00 15.67 ?  55  LYS   A CD   1 
ATOM   1393 C  CE   . LYS   A 1 55  ? 18.329 14.109  7.957   1.00 17.88 ?  55  LYS   A CE   1 
ATOM   1394 N  NZ   . LYS   A 1 55  ? 16.994 14.276  7.320   1.00 19.08 ?  55  LYS   A NZ   1 
ATOM   1395 H  H    A LYS   A 1 55  ? 22.617 9.726   6.767   0.50 12.18 ?  55  LYS   A H    1 
ATOM   1396 H  H    B LYS   A 1 55  ? 22.607 9.696   6.792   0.50 12.18 ?  55  LYS   A H    1 
ATOM   1397 H  HA   . LYS   A 1 55  ? 23.095 11.985  7.919   1.00 13.30 ?  55  LYS   A HA   1 
ATOM   1398 H  HB2  . LYS   A 1 55  ? 21.267 11.704  6.513   1.00 14.63 ?  55  LYS   A HB2  1 
ATOM   1399 H  HB3  . LYS   A 1 55  ? 20.590 10.729  7.564   1.00 14.63 ?  55  LYS   A HB3  1 
ATOM   1400 H  HG2  . LYS   A 1 55  ? 20.206 12.489  9.002   1.00 16.61 ?  55  LYS   A HG2  1 
ATOM   1401 H  HG3  . LYS   A 1 55  ? 20.975 13.483  8.022   1.00 16.61 ?  55  LYS   A HG3  1 
ATOM   1402 H  HD2  . LYS   A 1 55  ? 19.319 13.197  6.413   1.00 18.79 ?  55  LYS   A HD2  1 
ATOM   1403 H  HD3  . LYS   A 1 55  ? 18.563 12.165  7.359   1.00 18.79 ?  55  LYS   A HD3  1 
ATOM   1404 H  HE2  . LYS   A 1 55  ? 18.199 13.926  8.898   1.00 21.44 ?  55  LYS   A HE2  1 
ATOM   1405 H  HE3  . LYS   A 1 55  ? 18.828 14.932  7.839   1.00 21.44 ?  55  LYS   A HE3  1 
ATOM   1406 H  HZ1  . LYS   A 1 55  ? 16.425 14.644  7.901   1.00 22.89 ?  55  LYS   A HZ1  1 
ATOM   1407 H  HZ2  . LYS   A 1 55  ? 17.056 14.809  6.608   1.00 22.89 ?  55  LYS   A HZ2  1 
ATOM   1408 H  HZ3  . LYS   A 1 55  ? 16.671 13.487  7.065   1.00 22.89 ?  55  LYS   A HZ3  1 
ATOM   1409 N  N    . ALA   A 1 56  ? 22.029 9.763   9.960   1.00 11.37 ?  56  ALA   A N    1 
ATOM   1410 C  CA   . ALA   A 1 56  ? 21.899 9.441   11.374  1.00 11.75 ?  56  ALA   A CA   1 
ATOM   1411 C  C    . ALA   A 1 56  ? 23.237 9.467   12.103  1.00 12.08 ?  56  ALA   A C    1 
ATOM   1412 O  O    . ALA   A 1 56  ? 23.252 9.649   13.323  1.00 13.46 ?  56  ALA   A O    1 
ATOM   1413 C  CB   . ALA   A 1 56  ? 21.196 8.089   11.551  1.00 12.97 ?  56  ALA   A CB   1 
ATOM   1414 H  H    . ALA   A 1 56  ? 21.829 9.122   9.429   1.00 13.63 ?  56  ALA   A H    1 
ATOM   1415 H  HA   . ALA   A 1 56  ? 21.345 10.108  11.794  1.00 14.08 ?  56  ALA   A HA   1 
ATOM   1416 H  HB1  . ALA   A 1 56  ? 21.125 7.889   12.499  1.00 15.55 ?  56  ALA   A HB1  1 
ATOM   1417 H  HB2  . ALA   A 1 56  ? 20.306 8.146   11.162  1.00 15.55 ?  56  ALA   A HB2  1 
ATOM   1418 H  HB3  . ALA   A 1 56  ? 21.707 7.398   11.104  1.00 15.55 ?  56  ALA   A HB3  1 
ATOM   1419 N  N    . THR   A 1 57  ? 24.355 9.290   11.389  1.00 10.98 ?  57  THR   A N    1 
ATOM   1420 C  CA   . THR   A 1 57  ? 25.691 9.421   11.974  1.00 11.46 ?  57  THR   A CA   1 
ATOM   1421 C  C    . THR   A 1 57  ? 26.242 10.841  11.899  1.00 11.55 ?  57  THR   A C    1 
ATOM   1422 O  O    . THR   A 1 57  ? 27.426 11.053  12.196  1.00 11.91 ?  57  THR   A O    1 
ATOM   1423 C  CB   . THR   A 1 57  ? 26.714 8.477   11.310  1.00 11.23 ?  57  THR   A CB   1 
ATOM   1424 O  OG1  . THR   A 1 57  ? 27.105 8.969   10.012  1.00 10.47 ?  57  THR   A OG1  1 
ATOM   1425 C  CG2  . THR   A 1 57  ? 26.201 7.035   11.223  1.00 11.36 ?  57  THR   A CG2  1 
ATOM   1426 H  H    . THR   A 1 57  ? 24.370 9.073   10.552  1.00 13.17 ?  57  THR   A H    1 
ATOM   1427 H  HA   . THR   A 1 57  ? 25.643 9.169   12.914  1.00 13.75 ?  57  THR   A HA   1 
ATOM   1428 H  HB   . THR   A 1 57  ? 27.511 8.454   11.872  1.00 13.47 ?  57  THR   A HB   1 
ATOM   1429 H  HG1  . THR   A 1 57  ? 26.424 9.030   9.522   1.00 12.56 ?  57  THR   A HG1  1 
ATOM   1430 H  HG21 . THR   A 1 57  ? 26.873 6.463   10.814  1.00 13.62 ?  57  THR   A HG21 1 
ATOM   1431 H  HG22 . THR   A 1 57  ? 26.003 6.693   12.111  1.00 13.62 ?  57  THR   A HG22 1 
ATOM   1432 H  HG23 . THR   A 1 57  ? 25.395 6.998   10.688  1.00 13.62 ?  57  THR   A HG23 1 
ATOM   1433 N  N    . ASN   A 1 58  ? 25.430 11.810  11.485  1.00 12.10 ?  58  ASN   A N    1 
ATOM   1434 C  CA   . ASN   A 1 58  ? 25.888 13.191  11.384  1.00 13.31 ?  58  ASN   A CA   1 
ATOM   1435 C  C    . ASN   A 1 58  ? 27.036 13.324  10.378  1.00 11.95 ?  58  ASN   A C    1 
ATOM   1436 O  O    . ASN   A 1 58  ? 27.927 14.163  10.539  1.00 12.66 ?  58  ASN   A O    1 
ATOM   1437 C  CB   . ASN   A 1 58  ? 26.263 13.738  12.773  1.00 15.93 ?  58  ASN   A CB   1 
ATOM   1438 C  CG   . ASN   A 1 58  ? 26.607 15.211  12.762  1.00 20.19 ?  58  ASN   A CG   1 
ATOM   1439 O  OD1  . ASN   A 1 58  ? 25.966 15.999  12.077  1.00 21.88 ?  58  ASN   A OD1  1 
ATOM   1440 N  ND2  . ASN   A 1 58  ? 27.620 15.595  13.535  1.00 21.84 ?  58  ASN   A ND2  1 
ATOM   1441 H  H    . ASN   A 1 58  ? 24.610 11.688  11.254  1.00 14.51 ?  58  ASN   A H    1 
ATOM   1442 H  HA   . ASN   A 1 58  ? 25.151 13.723  11.057  1.00 15.97 ?  58  ASN   A HA   1 
ATOM   1443 H  HB2  . ASN   A 1 58  ? 25.508 13.607  13.379  1.00 19.10 ?  58  ASN   A HB2  1 
ATOM   1444 H  HB3  . ASN   A 1 58  ? 27.035 13.265  13.110  1.00 19.10 ?  58  ASN   A HB3  1 
ATOM   1445 H  HD21 . ASN   A 1 58  ? 27.837 16.428  13.564  1.00 26.20 ?  58  ASN   A HD21 1 
ATOM   1446 H  HD22 . ASN   A 1 58  ? 28.037 15.019  14.006  1.00 26.20 ?  58  ASN   A HD22 1 
ATOM   1447 N  N    . ASN   A 1 59  ? 27.027 12.497  9.330   1.00 11.13 ?  59  ASN   A N    1 
ATOM   1448 C  CA   . ASN   A 1 59  ? 28.019 12.472  8.246   1.00 10.67 ?  59  ASN   A CA   1 
ATOM   1449 C  C    . ASN   A 1 59  ? 29.332 11.796  8.646   1.00 10.33 ?  59  ASN   A C    1 
ATOM   1450 O  O    . ASN   A 1 59  ? 30.257 11.754  7.825   1.00 10.56 ?  59  ASN   A O    1 
ATOM   1451 C  CB   . ASN   A 1 59  ? 28.311 13.860  7.645   1.00 11.04 ?  59  ASN   A CB   1 
ATOM   1452 C  CG   . ASN   A 1 59  ? 28.682 13.796  6.176   1.00 11.13 ?  59  ASN   A CG   1 
ATOM   1453 O  OD1  . ASN   A 1 59  ? 27.982 13.168  5.374   1.00 11.45 ?  59  ASN   A OD1  1 
ATOM   1454 N  ND2  . ASN   A 1 59  ? 29.774 14.460  5.806   1.00 11.93 ?  59  ASN   A ND2  1 
ATOM   1455 H  H    . ASN   A 1 59  ? 26.414 11.901  9.220   1.00 13.35 ?  59  ASN   A H    1 
ATOM   1456 H  HA   . ASN   A 1 59  ? 27.640 11.947  7.530   1.00 12.79 ?  59  ASN   A HA   1 
ATOM   1457 H  HB2  . ASN   A 1 59  ? 27.521 14.421  7.724   1.00 13.24 ?  59  ASN   A HB2  1 
ATOM   1458 H  HB3  . ASN   A 1 59  ? 29.052 14.268  8.120   1.00 13.24 ?  59  ASN   A HB3  1 
ATOM   1459 H  HD21 . ASN   A 1 59  ? 30.032 14.452  4.983   1.00 14.30 ?  59  ASN   A HD21 1 
ATOM   1460 H  HD22 . ASN   A 1 59  ? 30.243 14.888  6.392   1.00 14.30 ?  59  ASN   A HD22 1 
ATOM   1461 N  N    . ALA   A 1 60  ? 29.449 11.257  9.859   1.00 10.45 ?  60  ALA   A N    1 
ATOM   1462 C  CA   . ALA   A 1 60  ? 30.685 10.575  10.224  1.00 10.72 ?  60  ALA   A CA   1 
ATOM   1463 C  C    . ALA   A 1 60  ? 30.923 9.342   9.357   1.00 10.66 ?  60  ALA   A C    1 
ATOM   1464 O  O    . ALA   A 1 60  ? 32.075 9.025   9.029   1.00 10.84 ?  60  ALA   A O    1 
ATOM   1465 C  CB   . ALA   A 1 60  ? 30.676 10.222  11.708  1.00 11.56 ?  60  ALA   A CB   1 
ATOM   1466 H  H    . ALA   A 1 60  ? 28.842 11.273  10.473  1.00 12.53 ?  60  ALA   A H    1 
ATOM   1467 H  HA   . ALA   A 1 60  ? 31.425 11.185  10.072  1.00 12.86 ?  60  ALA   A HA   1 
ATOM   1468 H  HB1  . ALA   A 1 60  ? 31.505 9.773   11.931  1.00 13.86 ?  60  ALA   A HB1  1 
ATOM   1469 H  HB2  . ALA   A 1 60  ? 30.593 11.040  12.229  1.00 13.86 ?  60  ALA   A HB2  1 
ATOM   1470 H  HB3  . ALA   A 1 60  ? 29.922 9.640   11.891  1.00 13.86 ?  60  ALA   A HB3  1 
ATOM   1471 N  N    . MET   A 1 61  ? 29.855 8.639   8.970   1.00 10.05 ?  61  MET   A N    1 
ATOM   1472 C  CA   . MET   A 1 61  ? 30.001 7.500   8.070   1.00 10.02 ?  61  MET   A CA   1 
ATOM   1473 C  C    . MET   A 1 61  ? 30.634 7.929   6.747   1.00 9.83  ?  61  MET   A C    1 
ATOM   1474 O  O    . MET   A 1 61  ? 31.534 7.255   6.232   1.00 10.21 ?  61  MET   A O    1 
ATOM   1475 C  CB   . MET   A 1 61  ? 28.637 6.836   7.854   1.00 9.98  ?  61  MET   A CB   1 
ATOM   1476 C  CG   . MET   A 1 61  ? 28.654 5.680   6.874   1.00 10.48 ?  61  MET   A CG   1 
ATOM   1477 S  SD   . MET   A 1 61  ? 27.038 4.920   6.660   1.00 11.36 ?  61  MET   A SD   1 
ATOM   1478 C  CE   . MET   A 1 61  ? 26.912 4.029   8.214   1.00 12.63 ?  61  MET   A CE   1 
ATOM   1479 H  H    . MET   A 1 61  ? 29.042 8.799   9.212   1.00 12.05 ?  61  MET   A H    1 
ATOM   1480 H  HA   . MET   A 1 61  ? 30.582 6.844   8.494   1.00 12.02 ?  61  MET   A HA   1 
ATOM   1481 H  HB2  . MET   A 1 61  ? 28.322 6.490   8.703   1.00 11.97 ?  61  MET   A HB2  1 
ATOM   1482 H  HB3  . MET   A 1 61  ? 28.019 7.495   7.515   1.00 11.97 ?  61  MET   A HB3  1 
ATOM   1483 H  HG2  . MET   A 1 61  ? 28.943 5.994   6.002   1.00 12.56 ?  61  MET   A HG2  1 
ATOM   1484 H  HG3  . MET   A 1 61  ? 29.263 4.992   7.193   1.00 12.56 ?  61  MET   A HG3  1 
ATOM   1485 H  HE1  . MET   A 1 61  ? 26.079 3.534   8.229   1.00 15.15 ?  61  MET   A HE1  1 
ATOM   1486 H  HE2  . MET   A 1 61  ? 27.663 3.421   8.290   1.00 15.15 ?  61  MET   A HE2  1 
ATOM   1487 H  HE3  . MET   A 1 61  ? 26.929 4.666   8.950   1.00 15.15 ?  61  MET   A HE3  1 
ATOM   1488 N  N    . GLN   A 1 62  ? 30.189 9.057   6.190   1.00 9.88  ?  62  GLN   A N    1 
ATOM   1489 C  CA   . GLN   A 1 62  ? 30.758 9.524   4.928   1.00 10.04 ?  62  GLN   A CA   1 
ATOM   1490 C  C    . GLN   A 1 62  ? 32.225 9.906   5.080   1.00 10.04 ?  62  GLN   A C    1 
ATOM   1491 O  O    . GLN   A 1 62  ? 33.041 9.597   4.204   1.00 10.40 ?  62  GLN   A O    1 
ATOM   1492 C  CB   . GLN   A 1 62  ? 29.961 10.709  4.386   1.00 10.16 ?  62  GLN   A CB   1 
ATOM   1493 C  CG   . GLN   A 1 62  ? 30.335 11.068  2.960   1.00 10.19 ?  62  GLN   A CG   1 
ATOM   1494 C  CD   . GLN   A 1 62  ? 30.002 9.937   2.012   1.00 10.14 ?  62  GLN   A CD   1 
ATOM   1495 O  OE1  . GLN   A 1 62  ? 28.829 9.633   1.797   1.00 10.80 ?  62  GLN   A OE1  1 
ATOM   1496 N  NE2  . GLN   A 1 62  ? 31.022 9.255   1.499   1.00 10.76 ?  62  GLN   A NE2  1 
ATOM   1497 H  H    . GLN   A 1 62  ? 29.572 9.554   6.517   1.00 11.84 ?  62  GLN   A H    1 
ATOM   1498 H  HA   . GLN   A 1 62  ? 30.706 8.801   4.284   1.00 12.03 ?  62  GLN   A HA   1 
ATOM   1499 H  HB2  . GLN   A 1 62  ? 29.020 10.493  4.410   1.00 12.18 ?  62  GLN   A HB2  1 
ATOM   1500 H  HB3  . GLN   A 1 62  ? 30.140 11.485  4.945   1.00 12.18 ?  62  GLN   A HB3  1 
ATOM   1501 H  HG2  . GLN   A 1 62  ? 29.826 11.846  2.685   1.00 12.22 ?  62  GLN   A HG2  1 
ATOM   1502 H  HG3  . GLN   A 1 62  ? 31.284 11.245  2.905   1.00 12.22 ?  62  GLN   A HG3  1 
ATOM   1503 H  HE21 . GLN   A 1 62  ? 31.830 9.485   1.688   1.00 12.91 ?  62  GLN   A HE21 1 
ATOM   1504 H  HE22 . GLN   A 1 62  ? 30.878 8.597   0.964   1.00 12.91 ?  62  GLN   A HE22 1 
ATOM   1505 N  N    . VAL   A 1 63  ? 32.580 10.586  6.173   1.00 10.70 ?  63  VAL   A N    1 
ATOM   1506 C  CA   . VAL   A 1 63  ? 33.968 10.986  6.390   1.00 11.24 ?  63  VAL   A CA   1 
ATOM   1507 C  C    . VAL   A 1 63  ? 34.866 9.753   6.455   1.00 10.95 ?  63  VAL   A C    1 
ATOM   1508 O  O    . VAL   A 1 63  ? 35.923 9.686   5.810   1.00 11.38 ?  63  VAL   A O    1 
ATOM   1509 C  CB   . VAL   A 1 63  ? 34.069 11.855  7.657   1.00 12.71 ?  63  VAL   A CB   1 
ATOM   1510 C  CG1  . VAL   A 1 63  ? 35.513 12.084  8.045   1.00 14.49 ?  63  VAL   A CG1  1 
ATOM   1511 C  CG2  . VAL   A 1 63  ? 33.363 13.194  7.437   1.00 13.07 ?  63  VAL   A CG2  1 
ATOM   1512 H  H    . VAL   A 1 63  ? 32.038 10.820  6.797   1.00 12.83 ?  63  VAL   A H    1 
ATOM   1513 H  HA   . VAL   A 1 63  ? 34.257 11.521  5.640   1.00 13.48 ?  63  VAL   A HA   1 
ATOM   1514 H  HB   . VAL   A 1 63  ? 33.628 11.404  8.394   1.00 15.24 ?  63  VAL   A HB   1 
ATOM   1515 H  HG11 . VAL   A 1 63  ? 35.556 12.822  8.671   1.00 17.37 ?  63  VAL   A HG11 1 
ATOM   1516 H  HG12 . VAL   A 1 63  ? 35.862 11.279  8.453   1.00 17.37 ?  63  VAL   A HG12 1 
ATOM   1517 H  HG13 . VAL   A 1 63  ? 36.019 12.301  7.245   1.00 17.37 ?  63  VAL   A HG13 1 
ATOM   1518 H  HG21 . VAL   A 1 63  ? 33.439 13.729  8.247   1.00 15.68 ?  63  VAL   A HG21 1 
ATOM   1519 H  HG22 . VAL   A 1 63  ? 33.788 13.660  6.699   1.00 15.68 ?  63  VAL   A HG22 1 
ATOM   1520 H  HG23 . VAL   A 1 63  ? 32.430 13.034  7.236   1.00 15.68 ?  63  VAL   A HG23 1 
ATOM   1521 N  N    . GLU   A 1 64  ? 34.445 8.745   7.224   1.00 10.72 ?  64  GLU   A N    1 
ATOM   1522 C  CA   . GLU   A 1 64  ? 35.208 7.510   7.327   1.00 10.63 ?  64  GLU   A CA   1 
ATOM   1523 C  C    . GLU   A 1 64  ? 35.308 6.825   5.972   1.00 10.48 ?  64  GLU   A C    1 
ATOM   1524 O  O    . GLU   A 1 64  ? 36.362 6.287   5.602   1.00 10.85 ?  64  GLU   A O    1 
ATOM   1525 C  CB   . GLU   A 1 64  ? 34.515 6.594   8.336   1.00 11.56 ?  64  GLU   A CB   1 
ATOM   1526 C  CG   . GLU   A 1 64  ? 35.173 5.249   8.503   1.00 11.96 ?  64  GLU   A CG   1 
ATOM   1527 C  CD   . GLU   A 1 64  ? 34.301 4.250   9.228   1.00 12.73 ?  64  GLU   A CD   1 
ATOM   1528 O  OE1  . GLU   A 1 64  ? 33.061 4.351   9.100   1.00 13.48 ?  64  GLU   A OE1  1 
ATOM   1529 O  OE2  . GLU   A 1 64  ? 34.868 3.356   9.901   1.00 13.11 -1 64  GLU   A OE2  1 
ATOM   1530 H  H    . GLU   A 1 64  ? 33.715 8.749   7.681   1.00 12.86 ?  64  GLU   A H    1 
ATOM   1531 H  HA   . GLU   A 1 64  ? 36.101 7.703   7.649   1.00 12.75 ?  64  GLU   A HA   1 
ATOM   1532 H  HB2  . GLU   A 1 64  ? 34.514 7.032   9.207   1.00 13.86 ?  64  GLU   A HB2  1 
ATOM   1533 H  HB3  . GLU   A 1 64  ? 33.599 6.450   8.048   1.00 13.86 ?  64  GLU   A HB3  1 
ATOM   1534 H  HG2  . GLU   A 1 64  ? 35.378 4.876   7.629   1.00 14.34 ?  64  GLU   A HG2  1 
ATOM   1535 H  HG3  . GLU   A 1 64  ? 35.987 5.359   9.013   1.00 14.34 ?  64  GLU   A HG3  1 
ATOM   1536 N  N    . SER   A 1 65  ? 34.198 6.808   5.236   1.00 10.14 ?  65  SER   A N    1 
ATOM   1537 C  CA   . SER   A 1 65  ? 34.148 6.145   3.939   1.00 10.24 ?  65  SER   A CA   1 
ATOM   1538 C  C    . SER   A 1 65  ? 35.064 6.813   2.925   1.00 10.39 ?  65  SER   A C    1 
ATOM   1539 O  O    . SER   A 1 65  ? 35.708 6.133   2.118   1.00 11.17 ?  65  SER   A O    1 
ATOM   1540 C  CB   . SER   A 1 65  ? 32.714 6.156   3.410   1.00 10.10 ?  65  SER   A CB   1 
ATOM   1541 O  OG   . SER   A 1 65  ? 31.864 5.334   4.202   1.00 10.73 ?  65  SER   A OG   1 
ATOM   1542 H  H    . SER   A 1 65  ? 33.459 7.182   5.466   1.00 12.16 ?  65  SER   A H    1 
ATOM   1543 H  HA   . SER   A 1 65  ? 34.430 5.225   4.038   1.00 12.27 ?  65  SER   A HA   1 
ATOM   1544 H  HB2  . SER   A 1 65  ? 32.375 7.061   3.426   1.00 12.11 ?  65  SER   A HB2  1 
ATOM   1545 H  HB3  . SER   A 1 65  ? 32.715 5.818   2.499   1.00 12.11 ?  65  SER   A HB3  1 
ATOM   1546 H  HG   . SER   A 1 65  ? 31.857 5.611   4.999   1.00 12.87 ?  65  SER   A HG   1 
ATOM   1547 N  N    . ASP   A 1 66  ? 35.132 8.145   2.935   1.00 10.26 ?  66  ASP   A N    1 
ATOM   1548 C  CA   . ASP   A 1 66  ? 35.999 8.842   1.989   1.00 11.27 ?  66  ASP   A CA   1 
ATOM   1549 C  C    . ASP   A 1 66  ? 37.465 8.501   2.240   1.00 11.23 ?  66  ASP   A C    1 
ATOM   1550 O  O    . ASP   A 1 66  ? 38.245 8.336   1.295   1.00 12.21 ?  66  ASP   A O    1 
ATOM   1551 C  CB   . ASP   A 1 66  ? 35.770 10.347  2.082   1.00 12.21 ?  66  ASP   A CB   1 
ATOM   1552 C  CG   . ASP   A 1 66  ? 34.430 10.799  1.465   1.00 13.82 ?  66  ASP   A CG   1 
ATOM   1553 O  OD1  . ASP   A 1 66  ? 33.732 9.992   0.810   1.00 14.22 ?  66  ASP   A OD1  1 
ATOM   1554 O  OD2  . ASP   A 1 66  ? 34.105 11.998  1.618   1.00 16.51 -1 66  ASP   A OD2  1 
ATOM   1555 H  H    . ASP   A 1 66  ? 34.685 8.661   3.464   1.00 12.30 ?  66  ASP   A H    1 
ATOM   1556 H  HA   . ASP   A 1 66  ? 35.772 8.558   1.088   1.00 13.51 ?  66  ASP   A HA   1 
ATOM   1557 H  HB2  . ASP   A 1 66  ? 35.766 10.608  3.016   1.00 14.64 ?  66  ASP   A HB2  1 
ATOM   1558 H  HB3  . ASP   A 1 66  ? 36.485 10.803  1.613   1.00 14.64 ?  66  ASP   A HB3  1 
ATOM   1559 N  N    . ASP   A 1 67  ? 37.855 8.381   3.508   1.00 11.36 ?  67  ASP   A N    1 
ATOM   1560 C  CA   . ASP   A 1 67  ? 39.209 7.940   3.820   1.00 12.48 ?  67  ASP   A CA   1 
ATOM   1561 C  C    . ASP   A 1 67  ? 39.440 6.510   3.348   1.00 12.25 ?  67  ASP   A C    1 
ATOM   1562 O  O    . ASP   A 1 67  ? 40.506 6.195   2.804   1.00 13.13 ?  67  ASP   A O    1 
ATOM   1563 C  CB   . ASP   A 1 67  ? 39.471 8.079   5.320   1.00 13.65 ?  67  ASP   A CB   1 
ATOM   1564 C  CG   . ASP   A 1 67  ? 40.767 7.423   5.748   1.00 14.76 ?  67  ASP   A CG   1 
ATOM   1565 O  OD1  . ASP   A 1 67  ? 41.837 8.066   5.627   1.00 17.57 ?  67  ASP   A OD1  1 
ATOM   1566 O  OD2  . ASP   A 1 67  ? 40.717 6.259   6.203   1.00 14.52 -1 67  ASP   A OD2  1 
ATOM   1567 H  H    . ASP   A 1 67  ? 37.366 8.547   4.194   1.00 13.62 ?  67  ASP   A H    1 
ATOM   1568 H  HA   . ASP   A 1 67  ? 39.842 8.504   3.352   1.00 14.97 ?  67  ASP   A HA   1 
ATOM   1569 H  HB2  . ASP   A 1 67  ? 39.524 9.017   5.543   1.00 16.37 ?  67  ASP   A HB2  1 
ATOM   1570 H  HB3  . ASP   A 1 67  ? 38.746 7.656   5.808   1.00 16.37 ?  67  ASP   A HB3  1 
ATOM   1571 N  N    . TYR   A 1 68  ? 38.450 5.628   3.534   1.00 11.88 ?  68  TYR   A N    1 
ATOM   1572 C  CA   . TYR   A 1 68  ? 38.582 4.250   3.066   1.00 12.17 ?  68  TYR   A CA   1 
ATOM   1573 C  C    . TYR   A 1 68  ? 38.828 4.202   1.560   1.00 12.01 ?  68  TYR   A C    1 
ATOM   1574 O  O    . TYR   A 1 68  ? 39.709 3.470   1.088   1.00 12.54 ?  68  TYR   A O    1 
ATOM   1575 C  CB   . TYR   A 1 68  ? 37.333 3.418   3.439   1.00 12.53 ?  68  TYR   A CB   1 
ATOM   1576 C  CG   . TYR   A 1 68  ? 37.366 2.031   2.815   1.00 13.82 ?  68  TYR   A CG   1 
ATOM   1577 C  CD1  . TYR   A 1 68  ? 36.919 1.834   1.510   1.00 15.32 ?  68  TYR   A CD1  1 
ATOM   1578 C  CD2  . TYR   A 1 68  ? 37.912 0.954   3.488   1.00 15.71 ?  68  TYR   A CD2  1 
ATOM   1579 C  CE1  . TYR   A 1 68  ? 37.003 0.622   0.897   1.00 16.71 ?  68  TYR   A CE1  1 
ATOM   1580 C  CE2  . TYR   A 1 68  ? 37.978 -0.303  2.880   1.00 16.33 ?  68  TYR   A CE2  1 
ATOM   1581 C  CZ   . TYR   A 1 68  ? 37.534 -0.441  1.580   1.00 16.89 ?  68  TYR   A CZ   1 
ATOM   1582 O  OH   . TYR   A 1 68  ? 37.627 -1.656  0.950   1.00 18.38 ?  68  TYR   A OH   1 
ATOM   1583 H  H    . TYR   A 1 68  ? 37.698 5.800   3.925   1.00 14.25 ?  68  TYR   A H    1 
ATOM   1584 H  HA   . TYR   A 1 68  ? 39.340 3.839   3.504   1.00 14.59 ?  68  TYR   A HA   1 
ATOM   1585 H  HB2  . TYR   A 1 68  ? 37.288 3.316   4.403   1.00 15.03 ?  68  TYR   A HB2  1 
ATOM   1586 H  HB3  . TYR   A 1 68  ? 36.534 3.877   3.118   1.00 15.03 ?  68  TYR   A HB3  1 
ATOM   1587 H  HD1  . TYR   A 1 68  ? 36.574 2.558   1.037   1.00 18.37 ?  68  TYR   A HD1  1 
ATOM   1588 H  HD2  . TYR   A 1 68  ? 38.227 1.065   4.353   1.00 18.84 ?  68  TYR   A HD2  1 
ATOM   1589 H  HE1  . TYR   A 1 68  ? 36.694 0.515   0.026   1.00 20.04 ?  68  TYR   A HE1  1 
ATOM   1590 H  HE2  . TYR   A 1 68  ? 38.351 -1.027  3.327   1.00 19.58 ?  68  TYR   A HE2  1 
ATOM   1591 H  HH   . TYR   A 1 68  ? 37.957 -2.228  1.473   1.00 22.04 ?  68  TYR   A HH   1 
ATOM   1592 N  N    . ILE   A 1 69  ? 38.043 4.959   0.784   1.00 11.49 ?  69  ILE   A N    1 
ATOM   1593 C  CA   . ILE   A 1 69  ? 38.182 4.941   -0.672  1.00 11.59 ?  69  ILE   A CA   1 
ATOM   1594 C  C    . ILE   A 1 69  ? 39.506 5.562   -1.100  1.00 11.21 ?  69  ILE   A C    1 
ATOM   1595 O  O    . ILE   A 1 69  ? 40.153 5.083   -2.039  1.00 11.65 ?  69  ILE   A O    1 
ATOM   1596 C  CB   . ILE   A 1 69  ? 36.984 5.645   -1.339  1.00 12.51 ?  69  ILE   A CB   1 
ATOM   1597 C  CG1  . ILE   A 1 69  ? 35.673 4.907   -1.065  1.00 12.64 ?  69  ILE   A CG1  1 
ATOM   1598 C  CG2  . ILE   A 1 69  ? 37.213 5.821   -2.847  1.00 14.20 ?  69  ILE   A CG2  1 
ATOM   1599 C  CD1  . ILE   A 1 69  ? 35.507 3.618   -1.836  1.00 13.88 ?  69  ILE   A CD1  1 
ATOM   1600 H  H    . ILE   A 1 69  ? 37.428 5.486   1.077   1.00 13.77 ?  69  ILE   A H    1 
ATOM   1601 H  HA   . ILE   A 1 69  ? 38.182 4.020   -0.969  1.00 13.90 ?  69  ILE   A HA   1 
ATOM   1602 H  HB   . ILE   A 1 69  ? 36.905 6.528   -0.949  1.00 15.00 ?  69  ILE   A HB   1 
ATOM   1603 H  HG12 . ILE   A 1 69  ? 35.629 4.691   -0.115  1.00 15.16 ?  69  ILE   A HG12 1 
ATOM   1604 H  HG13 . ILE   A 1 69  ? 34.932 5.489   -1.295  1.00 15.16 ?  69  ILE   A HG13 1 
ATOM   1605 H  HG21 . ILE   A 1 69  ? 36.362 6.023   -3.274  1.00 17.02 ?  69  ILE   A HG21 1 
ATOM   1606 H  HG22 . ILE   A 1 69  ? 37.831 6.557   -2.991  1.00 17.02 ?  69  ILE   A HG22 1 
ATOM   1607 H  HG23 . ILE   A 1 69  ? 37.577 5.003   -3.213  1.00 17.02 ?  69  ILE   A HG23 1 
ATOM   1608 H  HD11 . ILE   A 1 69  ? 34.726 3.151   -1.503  1.00 16.64 ?  69  ILE   A HD11 1 
ATOM   1609 H  HD12 . ILE   A 1 69  ? 35.392 3.826   -2.776  1.00 16.64 ?  69  ILE   A HD12 1 
ATOM   1610 H  HD13 . ILE   A 1 69  ? 36.298 3.070   -1.710  1.00 16.64 ?  69  ILE   A HD13 1 
ATOM   1611 N  N    . ALA   A 1 70  ? 39.915 6.646   -0.444  1.00 11.72 ?  70  ALA   A N    1 
ATOM   1612 C  CA   . ALA   A 1 70  ? 41.186 7.267   -0.793  1.00 12.75 ?  70  ALA   A CA   1 
ATOM   1613 C  C    . ALA   A 1 70  ? 42.343 6.287   -0.624  1.00 13.10 ?  70  ALA   A C    1 
ATOM   1614 O  O    . ALA   A 1 70  ? 43.326 6.348   -1.369  1.00 15.25 ?  70  ALA   A O    1 
ATOM   1615 C  CB   . ALA   A 1 70  ? 41.402 8.520   0.055   1.00 13.32 ?  70  ALA   A CB   1 
ATOM   1616 H  H    . ALA   A 1 70  ? 39.479 7.037   0.185   1.00 14.06 ?  70  ALA   A H    1 
ATOM   1617 H  HA   . ALA   A 1 70  ? 41.158 7.544   -1.724  1.00 15.29 ?  70  ALA   A HA   1 
ATOM   1618 H  HB1  . ALA   A 1 70  ? 42.251 8.922   -0.186  1.00 15.97 ?  70  ALA   A HB1  1 
ATOM   1619 H  HB2  . ALA   A 1 70  ? 40.680 9.147   -0.115  1.00 15.97 ?  70  ALA   A HB2  1 
ATOM   1620 H  HB3  . ALA   A 1 70  ? 41.407 8.269   0.992   1.00 15.97 ?  70  ALA   A HB3  1 
ATOM   1621 N  N    . THR   A 1 71  ? 42.240 5.370   0.330   1.00 12.74 ?  71  THR   A N    1 
ATOM   1622 C  CA   . THR   A 1 71  ? 43.292 4.397   0.593   1.00 14.48 ?  71  THR   A CA   1 
ATOM   1623 C  C    . THR   A 1 71  ? 43.190 3.167   -0.294  1.00 14.52 ?  71  THR   A C    1 
ATOM   1624 O  O    . THR   A 1 71  ? 44.210 2.666   -0.784  1.00 16.78 ?  71  THR   A O    1 
ATOM   1625 C  CB   . THR   A 1 71  ? 43.216 3.962   2.057   1.00 16.88 ?  71  THR   A CB   1 
ATOM   1626 O  OG1  . THR   A 1 71  ? 43.469 5.092   2.895   1.00 18.46 ?  71  THR   A OG1  1 
ATOM   1627 C  CG2  . THR   A 1 71  ? 44.219 2.853   2.365   1.00 18.13 ?  71  THR   A CG2  1 
ATOM   1628 H  H    . THR   A 1 71  ? 41.543 5.267   0.827   1.00 15.28 ?  71  THR   A H    1 
ATOM   1629 H  HA   . THR   A 1 71  ? 44.151 4.808   0.434   1.00 17.37 ?  71  THR   A HA   1 
ATOM   1630 H  HB   . THR   A 1 71  ? 42.328 3.624   2.244   1.00 20.24 ?  71  THR   A HB   1 
ATOM   1631 H  HG1  . THR   A 1 71  ? 42.900 5.691   2.746   1.00 22.14 ?  71  THR   A HG1  1 
ATOM   1632 H  HG21 . THR   A 1 71  ? 44.351 2.787   3.324   1.00 21.74 ?  71  THR   A HG21 1 
ATOM   1633 H  HG22 . THR   A 1 71  ? 43.892 2.002   2.034   1.00 21.74 ?  71  THR   A HG22 1 
ATOM   1634 H  HG23 . THR   A 1 71  ? 45.072 3.050   1.945   1.00 21.74 ?  71  THR   A HG23 1 
ATOM   1635 N  N    . ASN   A 1 72  ? 41.971 2.661   -0.498  1.00 13.52 ?  72  ASN   A N    1 
ATOM   1636 C  CA   . ASN   A 1 72  ? 41.754 1.337   -1.061  1.00 13.53 ?  72  ASN   A CA   1 
ATOM   1637 C  C    . ASN   A 1 72  ? 41.140 1.330   -2.449  1.00 13.62 ?  72  ASN   A C    1 
ATOM   1638 O  O    . ASN   A 1 72  ? 41.136 0.274   -3.097  1.00 14.75 ?  72  ASN   A O    1 
ATOM   1639 C  CB   . ASN   A 1 72  ? 40.856 0.520   -0.124  1.00 14.29 ?  72  ASN   A CB   1 
ATOM   1640 C  CG   . ASN   A 1 72  ? 41.469 0.350   1.240   1.00 15.50 ?  72  ASN   A CG   1 
ATOM   1641 O  OD1  . ASN   A 1 72  ? 41.013 0.939   2.215   1.00 17.20 ?  72  ASN   A OD1  1 
ATOM   1642 N  ND2  . ASN   A 1 72  ? 42.531 -0.425  1.312   1.00 16.31 ?  72  ASN   A ND2  1 
ATOM   1643 H  H    . ASN   A 1 72  ? 41.235 3.083   -0.322  1.00 16.22 ?  72  ASN   A H    1 
ATOM   1644 H  HA   . ASN   A 1 72  ? 42.605 0.884   -1.123  1.00 16.22 ?  72  ASN   A HA   1 
ATOM   1645 H  HB2  . ASN   A 1 72  ? 40.006 0.971   -0.021  1.00 17.13 ?  72  ASN   A HB2  1 
ATOM   1646 H  HB3  . ASN   A 1 72  ? 40.724 -0.365  -0.500  1.00 17.13 ?  72  ASN   A HB3  1 
ATOM   1647 H  HD21 . ASN   A 1 72  ? 42.924 -0.545  2.069   1.00 19.56 ?  72  ASN   A HD21 1 
ATOM   1648 H  HD22 . ASN   A 1 72  ? 42.829 -0.809  0.606   1.00 19.56 ?  72  ASN   A HD22 1 
ATOM   1649 N  N    . GLY   A 1 73  ? 40.595 2.445   -2.910  1.00 12.95 ?  73  GLY   A N    1 
ATOM   1650 C  CA   . GLY   A 1 73  ? 39.857 2.461   -4.145  1.00 13.05 ?  73  GLY   A CA   1 
ATOM   1651 C  C    . GLY   A 1 73  ? 38.470 1.872   -3.978  1.00 12.14 ?  73  GLY   A C    1 
ATOM   1652 O  O    . GLY   A 1 73  ? 38.084 1.417   -2.893  1.00 12.75 ?  73  GLY   A O    1 
ATOM   1653 H  H    . GLY   A 1 73  ? 40.636 3.214   -2.516  1.00 15.53 ?  73  GLY   A H    1 
ATOM   1654 H  HA2  . GLY   A 1 73  ? 39.775 3.378   -4.459  1.00 15.65 ?  73  GLY   A HA2  1 
ATOM   1655 H  HA3  . GLY   A 1 73  ? 40.334 1.947   -4.814  1.00 15.65 ?  73  GLY   A HA3  1 
ATOM   1656 N  N    . PRO   A 1 74  ? 37.693 1.880   -5.060  1.00 12.59 ?  74  PRO   A N    1 
ATOM   1657 C  CA   . PRO   A 1 74  ? 36.300 1.438   -4.980  1.00 12.93 ?  74  PRO   A CA   1 
ATOM   1658 C  C    . PRO   A 1 74  ? 36.158 -0.044  -4.657  1.00 12.17 ?  74  PRO   A C    1 
ATOM   1659 O  O    . PRO   A 1 74  ? 37.031 -0.868  -4.948  1.00 13.11 ?  74  PRO   A O    1 
ATOM   1660 C  CB   . PRO   A 1 74  ? 35.756 1.732   -6.384  1.00 14.62 ?  74  PRO   A CB   1 
ATOM   1661 C  CG   . PRO   A 1 74  ? 36.684 2.750   -6.962  1.00 16.99 ?  74  PRO   A CG   1 
ATOM   1662 C  CD   . PRO   A 1 74  ? 38.025 2.401   -6.397  1.00 14.69 ?  74  PRO   A CD   1 
ATOM   1663 H  HA   . PRO   A 1 74  ? 35.818 1.962   -4.322  1.00 15.51 ?  74  PRO   A HA   1 
ATOM   1664 H  HB2  . PRO   A 1 74  ? 35.759 0.921   -6.912  1.00 17.53 ?  74  PRO   A HB2  1 
ATOM   1665 H  HB3  . PRO   A 1 74  ? 34.856 2.093   -6.312  1.00 17.53 ?  74  PRO   A HB3  1 
ATOM   1666 H  HG2  . PRO   A 1 74  ? 36.692 2.679   -7.926  1.00 20.37 ?  74  PRO   A HG2  1 
ATOM   1667 H  HG3  . PRO   A 1 74  ? 36.419 3.637   -6.679  1.00 20.37 ?  74  PRO   A HG3  1 
ATOM   1668 H  HD2  . PRO   A 1 74  ? 38.459 1.716   -6.938  1.00 17.62 ?  74  PRO   A HD2  1 
ATOM   1669 H  HD3  . PRO   A 1 74  ? 38.580 3.195   -6.329  1.00 17.62 ?  74  PRO   A HD3  1 
ATOM   1670 N  N    . LEU   A 1 75  ? 35.016 -0.372  -4.060  1.00 11.39 ?  75  LEU   A N    1 
ATOM   1671 C  CA   . LEU   A 1 75  ? 34.634 -1.764  -3.901  1.00 11.06 ?  75  LEU   A CA   1 
ATOM   1672 C  C    . LEU   A 1 75  ? 34.264 -2.359  -5.256  1.00 11.42 ?  75  LEU   A C    1 
ATOM   1673 O  O    . LEU   A 1 75  ? 34.086 -1.655  -6.252  1.00 12.86 ?  75  LEU   A O    1 
ATOM   1674 C  CB   . LEU   A 1 75  ? 33.444 -1.890  -2.952  1.00 11.26 ?  75  LEU   A CB   1 
ATOM   1675 C  CG   . LEU   A 1 75  ? 33.636 -1.480  -1.494  1.00 12.99 ?  75  LEU   A CG   1 
ATOM   1676 C  CD1  . LEU   A 1 75  ? 32.326 -1.650  -0.723  1.00 14.77 ?  75  LEU   A CD1  1 
ATOM   1677 C  CD2  . LEU   A 1 75  ? 34.739 -2.232  -0.811  1.00 16.32 ?  75  LEU   A CD2  1 
ATOM   1678 H  H    . LEU   A 1 75  ? 34.448 0.189   -3.741  1.00 13.65 ?  75  LEU   A H    1 
ATOM   1679 H  HA   . LEU   A 1 75  ? 35.381 -2.265  -3.533  1.00 13.25 ?  75  LEU   A HA   1 
ATOM   1680 H  HB2  . LEU   A 1 75  ? 32.723 -1.349  -3.306  1.00 13.50 ?  75  LEU   A HB2  1 
ATOM   1681 H  HB3  . LEU   A 1 75  ? 33.165 -2.822  -2.949  1.00 13.50 ?  75  LEU   A HB3  1 
ATOM   1682 H  HG   . LEU   A 1 75  ? 33.873 -0.540  -1.471  1.00 15.57 ?  75  LEU   A HG   1 
ATOM   1683 H  HD11 . LEU   A 1 75  ? 32.471 -1.380  0.199   1.00 17.72 ?  75  LEU   A HD11 1 
ATOM   1684 H  HD12 . LEU   A 1 75  ? 31.651 -1.086  -1.130  1.00 17.72 ?  75  LEU   A HD12 1 
ATOM   1685 H  HD13 . LEU   A 1 75  ? 32.058 -2.577  -0.761  1.00 17.72 ?  75  LEU   A HD13 1 
ATOM   1686 H  HD21 . LEU   A 1 75  ? 34.792 -1.946  0.115   1.00 19.57 ?  75  LEU   A HD21 1 
ATOM   1687 H  HD22 . LEU   A 1 75  ? 34.551 -3.183  -0.852  1.00 19.57 ?  75  LEU   A HD22 1 
ATOM   1688 H  HD23 . LEU   A 1 75  ? 35.581 -2.044  -1.260  1.00 19.57 ?  75  LEU   A HD23 1 
ATOM   1689 N  N    . LYS   A 1 76  ? 34.145 -3.683  -5.279  1.00 11.38 ?  76  LYS   A N    1 
ATOM   1690 C  CA   . LYS   A 1 76  ? 33.558 -4.408  -6.399  1.00 12.08 ?  76  LYS   A CA   1 
ATOM   1691 C  C    . LYS   A 1 76  ? 32.044 -4.484  -6.228  1.00 10.94 ?  76  LYS   A C    1 
ATOM   1692 O  O    . LYS   A 1 76  ? 31.541 -4.588  -5.111  1.00 10.92 ?  76  LYS   A O    1 
ATOM   1693 C  CB   . LYS   A 1 76  ? 34.098 -5.845  -6.428  1.00 13.12 ?  76  LYS   A CB   1 
ATOM   1694 C  CG   . LYS   A 1 76  ? 35.603 -5.942  -6.660  1.00 14.49 ?  76  LYS   A CG   1 
ATOM   1695 C  CD   . LYS   A 1 76  ? 36.135 -7.332  -6.415  1.00 15.84 ?  76  LYS   A CD   1 
ATOM   1696 C  CE   . LYS   A 1 76  ? 37.626 -7.395  -6.665  1.00 18.13 ?  76  LYS   A CE   1 
ATOM   1697 N  NZ   . LYS   A 1 76  ? 38.181 -8.746  -6.449  1.00 19.30 ?  76  LYS   A NZ   1 
ATOM   1698 H  H    . LYS   A 1 76  ? 34.403 -4.197  -4.637  1.00 13.64 ?  76  LYS   A H    1 
ATOM   1699 H  HA   . LYS   A 1 76  ? 33.770 -3.968  -7.237  1.00 14.48 ?  76  LYS   A HA   1 
ATOM   1700 H  HB2  . LYS   A 1 76  ? 33.906 -6.267  -5.576  1.00 15.73 ?  76  LYS   A HB2  1 
ATOM   1701 H  HB3  . LYS   A 1 76  ? 33.659 -6.329  -7.142  1.00 15.73 ?  76  LYS   A HB3  1 
ATOM   1702 H  HG2  . LYS   A 1 76  ? 35.798 -5.700  -7.580  1.00 17.37 ?  76  LYS   A HG2  1 
ATOM   1703 H  HG3  . LYS   A 1 76  ? 36.058 -5.333  -6.054  1.00 17.37 ?  76  LYS   A HG3  1 
ATOM   1704 H  HD2  . LYS   A 1 76  ? 35.965 -7.582  -5.493  1.00 18.99 ?  76  LYS   A HD2  1 
ATOM   1705 H  HD3  . LYS   A 1 76  ? 35.693 -7.953  -7.017  1.00 18.99 ?  76  LYS   A HD3  1 
ATOM   1706 H  HE2  . LYS   A 1 76  ? 37.802 -7.143  -7.584  1.00 21.75 ?  76  LYS   A HE2  1 
ATOM   1707 H  HE3  . LYS   A 1 76  ? 38.074 -6.791  -6.058  1.00 21.75 ?  76  LYS   A HE3  1 
ATOM   1708 H  HZ1  . LYS   A 1 76  ? 39.058 -8.751  -6.608  1.00 23.14 ?  76  LYS   A HZ1  1 
ATOM   1709 H  HZ2  . LYS   A 1 76  ? 38.039 -9.013  -5.611  1.00 23.14 ?  76  LYS   A HZ2  1 
ATOM   1710 H  HZ3  . LYS   A 1 76  ? 37.792 -9.335  -7.002  1.00 23.14 ?  76  LYS   A HZ3  1 
ATOM   1711 N  N    . VAL   A 1 77  ? 31.316 -4.478  -7.347  1.00 11.44 ?  77  VAL   A N    1 
ATOM   1712 C  CA   . VAL   A 1 77  ? 29.907 -4.858  -7.279  1.00 11.47 ?  77  VAL   A CA   1 
ATOM   1713 C  C    . VAL   A 1 77  ? 29.841 -6.309  -6.824  1.00 11.18 ?  77  VAL   A C    1 
ATOM   1714 O  O    . VAL   A 1 77  ? 30.508 -7.181  -7.395  1.00 11.80 ?  77  VAL   A O    1 
ATOM   1715 C  CB   . VAL   A 1 77  ? 29.208 -4.664  -8.634  1.00 12.48 ?  77  VAL   A CB   1 
ATOM   1716 C  CG1  . VAL   A 1 77  ? 27.738 -5.083  -8.548  1.00 13.39 ?  77  VAL   A CG1  1 
ATOM   1717 C  CG2  . VAL   A 1 77  ? 29.326 -3.222  -9.093  1.00 13.54 ?  77  VAL   A CG2  1 
ATOM   1718 H  H    . VAL   A 1 77  ? 31.606 -4.265  -8.128  1.00 13.72 ?  77  VAL   A H    1 
ATOM   1719 H  HA   . VAL   A 1 77  ? 29.458 -4.307  -6.620  1.00 13.75 ?  77  VAL   A HA   1 
ATOM   1720 H  HB   . VAL   A 1 77  ? 29.642 -5.225  -9.296  1.00 14.96 ?  77  VAL   A HB   1 
ATOM   1721 H  HG11 . VAL   A 1 77  ? 27.290 -4.818  -9.367  1.00 16.05 ?  77  VAL   A HG11 1 
ATOM   1722 H  HG12 . VAL   A 1 77  ? 27.684 -6.041  -8.435  1.00 16.05 ?  77  VAL   A HG12 1 
ATOM   1723 H  HG13 . VAL   A 1 77  ? 27.328 -4.632  -7.791  1.00 16.05 ?  77  VAL   A HG13 1 
ATOM   1724 H  HG21 . VAL   A 1 77  ? 28.821 -3.113  -9.913  1.00 16.24 ?  77  VAL   A HG21 1 
ATOM   1725 H  HG22 . VAL   A 1 77  ? 28.970 -2.643  -8.403  1.00 16.24 ?  77  VAL   A HG22 1 
ATOM   1726 H  HG23 . VAL   A 1 77  ? 30.261 -3.016  -9.250  1.00 16.24 ?  77  VAL   A HG23 1 
ATOM   1727 N  N    . GLY   A 1 78  ? 29.040 -6.576  -5.787  1.00 10.63 ?  78  GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 78  ? 29.011 -7.861  -5.119  1.00 11.03 ?  78  GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 78  ? 29.921 -7.948  -3.911  1.00 10.88 ?  78  GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 78  ? 29.856 -8.948  -3.179  1.00 11.55 ?  78  GLY   A O    1 
ATOM   1731 H  H    . GLY   A 1 78  ? 28.478 -6.005  -5.458  1.00 12.74 ?  78  GLY   A H    1 
ATOM   1732 H  HA2  . GLY   A 1 78  ? 28.105 -8.049  -4.837  1.00 13.23 ?  78  GLY   A HA2  1 
ATOM   1733 H  HA3  . GLY   A 1 78  ? 29.280 -8.546  -5.754  1.00 13.23 ?  78  GLY   A HA3  1 
ATOM   1734 N  N    . GLY   A 1 79  ? 30.772 -6.936  -3.692  1.00 10.86 ?  79  GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 79  ? 31.722 -6.930  -2.603  1.00 10.99 ?  79  GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 79  ? 31.247 -6.138  -1.393  1.00 10.48 ?  79  GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 79  ? 30.127 -5.628  -1.337  1.00 10.98 ?  79  GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 79  ? 30.822 -6.231  -4.190  1.00 13.02 ?  79  GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 79  ? 31.890 -7.848  -2.325  1.00 13.18 ?  79  GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 79  ? 32.560 -6.552  -2.908  1.00 13.18 ?  79  GLY   A HA3  1 
ATOM   1741 N  N    . SER   A 1 80  ? 32.141 -6.044  -0.408  1.00 11.28 ?  80  SER   A N    1 
ATOM   1742 C  CA   . SER   A 1 80  ? 31.807 -5.408  0.858   1.00 10.77 ?  80  SER   A CA   1 
ATOM   1743 C  C    . SER   A 1 80  ? 33.069 -4.943  1.565   1.00 10.54 ?  80  SER   A C    1 
ATOM   1744 O  O    . SER   A 1 80  ? 34.189 -5.373  1.256   1.00 11.89 ?  80  SER   A O    1 
ATOM   1745 C  CB   . SER   A 1 80  ? 31.049 -6.363  1.785   1.00 11.05 ?  80  SER   A CB   1 
ATOM   1746 O  OG   . SER   A 1 80  ? 31.876 -7.414  2.255   1.00 12.90 ?  80  SER   A OG   1 
ATOM   1747 H  H    . SER   A 1 80  ? 32.948 -6.333  -0.454  1.00 13.52 ?  80  SER   A H    1 
ATOM   1748 H  HA   . SER   A 1 80  ? 31.251 -4.635  0.676   1.00 12.92 ?  80  SER   A HA   1 
ATOM   1749 H  HB2  . SER   A 1 80  ? 30.722 -5.860  2.548   1.00 13.25 ?  80  SER   A HB2  1 
ATOM   1750 H  HB3  . SER   A 1 80  ? 30.304 -6.743  1.298   1.00 13.25 ?  80  SER   A HB3  1 
ATOM   1751 H  HG   . SER   A 1 80  ? 32.166 -7.862  1.606   1.00 15.47 ?  80  SER   A HG   1 
ATOM   1752 N  N    . CYS   A 1 81  ? 32.864 -4.093  2.570   1.00 10.40 ?  81  CYS   A N    1 
ATOM   1753 C  CA   . CYS   A 1 81  ? 33.910 -3.801  3.539   1.00 10.53 ?  81  CYS   A CA   1 
ATOM   1754 C  C    . CYS   A 1 81  ? 33.257 -3.575  4.895   1.00 10.18 ?  81  CYS   A C    1 
ATOM   1755 O  O    . CYS   A 1 81  ? 32.092 -3.170  4.977   1.00 11.45 ?  81  CYS   A O    1 
ATOM   1756 C  CB   . CYS   A 1 81  ? 34.778 -2.607  3.121   1.00 11.26 ?  81  CYS   A CB   1 
ATOM   1757 S  SG   . CYS   A 1 81  ? 33.866 -1.041  3.114   1.00 11.27 ?  81  CYS   A SG   1 
ATOM   1758 H  H    . CYS   A 1 81  ? 32.124 -3.677  2.716   1.00 12.47 ?  81  CYS   A H    1 
ATOM   1759 H  HA   . CYS   A 1 81  ? 34.491 -4.569  3.615   1.00 12.63 ?  81  CYS   A HA   1 
ATOM   1760 H  HB2  . CYS   A 1 81  ? 35.522 -2.523  3.741   1.00 13.50 ?  81  CYS   A HB2  1 
ATOM   1761 H  HB3  . CYS   A 1 81  ? 35.115 -2.760  2.223   1.00 13.50 ?  81  CYS   A HB3  1 
ATOM   1762 H  HG   . CYS   A 1 81  ? 34.606 -0.156  2.785   1.00 13.51 ?  81  CYS   A HG   1 
ATOM   1763 N  N    . VAL   A 1 82  ? 34.021 -3.847  5.952   1.00 10.59 ?  82  VAL   A N    1 
ATOM   1764 C  CA   . VAL   A 1 82  ? 33.592 -3.608  7.324   1.00 11.04 ?  82  VAL   A CA   1 
ATOM   1765 C  C    . VAL   A 1 82  ? 34.187 -2.293  7.800   1.00 11.27 ?  82  VAL   A C    1 
ATOM   1766 O  O    . VAL   A 1 82  ? 35.409 -2.118  7.799   1.00 11.99 ?  82  VAL   A O    1 
ATOM   1767 C  CB   . VAL   A 1 82  ? 34.010 -4.754  8.258   1.00 12.65 ?  82  VAL   A CB   1 
ATOM   1768 C  CG1  . VAL   A 1 82  ? 33.557 -4.467  9.683   1.00 14.06 ?  82  VAL   A CG1  1 
ATOM   1769 C  CG2  . VAL   A 1 82  ? 33.460 -6.077  7.771   1.00 13.53 ?  82  VAL   A CG2  1 
ATOM   1770 H  H    . VAL   A 1 82  ? 34.809 -4.201  5.896   1.00 12.70 ?  82  VAL   A H    1 
ATOM   1771 H  HA   . VAL   A 1 82  ? 32.625 -3.533  7.349   1.00 13.23 ?  82  VAL   A HA   1 
ATOM   1772 H  HB   . VAL   A 1 82  ? 34.977 -4.817  8.262   1.00 15.17 ?  82  VAL   A HB   1 
ATOM   1773 H  HG11 . VAL   A 1 82  ? 33.642 -5.275  10.211  1.00 16.86 ?  82  VAL   A HG11 1 
ATOM   1774 H  HG12 . VAL   A 1 82  ? 34.110 -3.765  10.061  1.00 16.86 ?  82  VAL   A HG12 1 
ATOM   1775 H  HG13 . VAL   A 1 82  ? 32.627 -4.181  9.668   1.00 16.86 ?  82  VAL   A HG13 1 
ATOM   1776 H  HG21 . VAL   A 1 82  ? 33.693 -6.771  8.406   1.00 16.22 ?  82  VAL   A HG21 1 
ATOM   1777 H  HG22 . VAL   A 1 82  ? 32.492 -6.010  7.698   1.00 16.22 ?  82  VAL   A HG22 1 
ATOM   1778 H  HG23 . VAL   A 1 82  ? 33.841 -6.281  6.902   1.00 16.22 ?  82  VAL   A HG23 1 
ATOM   1779 N  N    . LEU   A 1 83  ? 33.327 -1.368  8.205   1.00 10.88 ?  83  LEU   A N    1 
ATOM   1780 C  CA   . LEU   A 1 83  ? 33.728 -0.094  8.781   1.00 10.83 ?  83  LEU   A CA   1 
ATOM   1781 C  C    . LEU   A 1 83  ? 33.003 0.081   10.113  1.00 10.77 ?  83  LEU   A C    1 
ATOM   1782 O  O    . LEU   A 1 83  ? 32.277 -0.807  10.574  1.00 11.47 ?  83  LEU   A O    1 
ATOM   1783 C  CB   . LEU   A 1 83  ? 33.475 1.056   7.794   1.00 11.08 ?  83  LEU   A CB   1 
ATOM   1784 C  CG   . LEU   A 1 83  ? 34.376 1.049   6.552   1.00 12.19 ?  83  LEU   A CG   1 
ATOM   1785 C  CD1  . LEU   A 1 83  ? 33.943 2.114   5.562   1.00 12.72 ?  83  LEU   A CD1  1 
ATOM   1786 C  CD2  . LEU   A 1 83  ? 35.837 1.263   6.937   1.00 12.88 ?  83  LEU   A CD2  1 
ATOM   1787 H  H    . LEU   A 1 83  ? 32.475 -1.455  8.144   1.00 13.05 ?  83  LEU   A H    1 
ATOM   1788 H  HA   . LEU   A 1 83  ? 34.678 -0.110  8.965   1.00 12.99 ?  83  LEU   A HA   1 
ATOM   1789 H  HB2  . LEU   A 1 83  ? 32.552 1.005   7.483   1.00 13.28 ?  83  LEU   A HB2  1 
ATOM   1790 H  HB3  . LEU   A 1 83  ? 33.609 1.902   8.249   1.00 13.28 ?  83  LEU   A HB3  1 
ATOM   1791 H  HG   . LEU   A 1 83  ? 34.304 0.186   6.116   1.00 14.61 ?  83  LEU   A HG   1 
ATOM   1792 H  HD11 . LEU   A 1 83  ? 34.528 2.078   4.787   1.00 15.25 ?  83  LEU   A HD11 1 
ATOM   1793 H  HD12 . LEU   A 1 83  ? 33.029 1.942   5.293   1.00 15.25 ?  83  LEU   A HD12 1 
ATOM   1794 H  HD13 . LEU   A 1 83  ? 34.009 2.983   5.985   1.00 15.25 ?  83  LEU   A HD13 1 
ATOM   1795 H  HD21 . LEU   A 1 83  ? 36.356 1.423   6.132   1.00 15.45 ?  83  LEU   A HD21 1 
ATOM   1796 H  HD22 . LEU   A 1 83  ? 35.900 2.030   7.528   1.00 15.45 ?  83  LEU   A HD22 1 
ATOM   1797 H  HD23 . LEU   A 1 83  ? 36.167 0.470   7.389   1.00 15.45 ?  83  LEU   A HD23 1 
ATOM   1798 N  N    . SER   A 1 84  ? 33.202 1.233   10.743  1.00 11.58 ?  84  SER   A N    1 
ATOM   1799 C  CA   . SER   A 1 84  ? 32.553 1.485   12.017  1.00 11.89 ?  84  SER   A CA   1 
ATOM   1800 C  C    . SER   A 1 84  ? 31.035 1.560   11.853  1.00 11.72 ?  84  SER   A C    1 
ATOM   1801 O  O    . SER   A 1 84  ? 30.517 2.016   10.833  1.00 11.69 ?  84  SER   A O    1 
ATOM   1802 C  CB   . SER   A 1 84  ? 33.045 2.810   12.591  1.00 12.77 ?  84  SER   A CB   1 
ATOM   1803 O  OG   . SER   A 1 84  ? 32.409 3.103   13.816  1.00 13.67 ?  84  SER   A OG   1 
ATOM   1804 H  H    . SER   A 1 84  ? 33.692 1.882   10.454  1.00 13.88 ?  84  SER   A H    1 
ATOM   1805 H  HA   . SER   A 1 84  ? 32.771 0.769   12.636  1.00 14.26 ?  84  SER   A HA   1 
ATOM   1806 H  HB2  . SER   A 1 84  ? 34.007 2.757   12.721  1.00 15.32 ?  84  SER   A HB2  1 
ATOM   1807 H  HB3  . SER   A 1 84  ? 32.835 3.520   11.967  1.00 15.32 ?  84  SER   A HB3  1 
ATOM   1808 H  HG   . SER   A 1 84  ? 32.713 3.821   14.134  1.00 16.40 ?  84  SER   A HG   1 
ATOM   1809 N  N    . GLY   A 1 85  ? 30.318 1.144   12.896  1.00 12.50 ?  85  GLY   A N    1 
ATOM   1810 C  CA   . GLY   A 1 85  ? 28.893 1.391   12.968  1.00 13.05 ?  85  GLY   A CA   1 
ATOM   1811 C  C    . GLY   A 1 85  ? 28.516 2.701   13.619  1.00 12.56 ?  85  GLY   A C    1 
ATOM   1812 O  O    . GLY   A 1 85  ? 27.328 3.019   13.725  1.00 13.30 ?  85  GLY   A O    1 
ATOM   1813 H  H    . GLY   A 1 85  ? 30.641 0.710   13.574  1.00 14.99 ?  85  GLY   A H    1 
ATOM   1814 H  HA2  . GLY   A 1 85  ? 28.532 1.385   12.067  1.00 15.65 ?  85  GLY   A HA2  1 
ATOM   1815 H  HA3  . GLY   A 1 85  ? 28.473 0.678   13.465  1.00 15.65 ?  85  GLY   A HA3  1 
ATOM   1816 N  N    . HIS   A 1 86  ? 29.500 3.483   14.061  1.00 12.53 ?  86  HIS   A N    1 
ATOM   1817 C  CA   . HIS   A 1 86  ? 29.267 4.817   14.628  1.00 13.02 ?  86  HIS   A CA   1 
ATOM   1818 C  C    . HIS   A 1 86  ? 28.271 4.695   15.777  1.00 13.89 ?  86  HIS   A C    1 
ATOM   1819 O  O    . HIS   A 1 86  ? 28.457 3.828   16.642  1.00 15.13 ?  86  HIS   A O    1 
ATOM   1820 C  CB   . HIS   A 1 86  ? 28.900 5.796   13.522  1.00 13.16 ?  86  HIS   A CB   1 
ATOM   1821 C  CG   . HIS   A 1 86  ? 29.961 5.901   12.485  1.00 13.11 ?  86  HIS   A CG   1 
ATOM   1822 N  ND1  . HIS   A 1 86  ? 31.050 6.739   12.618  1.00 14.14 ?  86  HIS   A ND1  1 
ATOM   1823 C  CD2  . HIS   A 1 86  ? 30.150 5.206   11.340  1.00 12.93 ?  86  HIS   A CD2  1 
ATOM   1824 C  CE1  . HIS   A 1 86  ? 31.846 6.578   11.577  1.00 14.08 ?  86  HIS   A CE1  1 
ATOM   1825 N  NE2  . HIS   A 1 86  ? 31.329 5.647   10.794  1.00 13.19 ?  86  HIS   A NE2  1 
ATOM   1826 H  H    . HIS   A 1 86  ? 30.334 3.267   14.044  1.00 15.02 ?  86  HIS   A H    1 
ATOM   1827 H  HA   . HIS   A 1 86  ? 30.095 5.133   15.009  1.00 15.61 ?  86  HIS   A HA   1 
ATOM   1828 H  HB2  . HIS   A 1 86  ? 28.082 5.505   13.086  1.00 15.78 ?  86  HIS   A HB2  1 
ATOM   1829 H  HB3  . HIS   A 1 86  ? 28.771 6.682   13.903  1.00 15.78 ?  86  HIS   A HB3  1 
ATOM   1830 H  HD2  . HIS   A 1 86  ? 29.593 4.547   10.985  1.00 15.50 ?  86  HIS   A HD2  1 
ATOM   1831 H  HE1  . HIS   A 1 86  ? 32.639 7.038   11.416  1.00 16.89 ?  86  HIS   A HE1  1 
ATOM   1832 H  HE2  . HIS   A 1 86  ? 31.671 5.375   10.043  1.00 15.81 ?  86  HIS   A HE2  1 
ATOM   1833 N  N    . ASN   A 1 87  ? 27.241 5.531   15.826  1.00 14.64 ?  87  ASN   A N    1 
ATOM   1834 C  CA   . ASN   A 1 87  ? 26.246 5.527   16.882  1.00 15.64 ?  87  ASN   A CA   1 
ATOM   1835 C  C    . ASN   A 1 87  ? 25.112 4.544   16.624  1.00 16.53 ?  87  ASN   A C    1 
ATOM   1836 O  O    . ASN   A 1 87  ? 24.156 4.509   17.400  1.00 19.24 ?  87  ASN   A O    1 
ATOM   1837 C  CB   . ASN   A 1 87  ? 25.665 6.939   17.049  1.00 16.38 ?  87  ASN   A CB   1 
ATOM   1838 C  CG   . ASN   A 1 87  ? 25.140 7.524   15.739  1.00 16.98 ?  87  ASN   A CG   1 
ATOM   1839 O  OD1  . ASN   A 1 87  ? 25.760 7.394   14.689  1.00 17.43 ?  87  ASN   A OD1  1 
ATOM   1840 N  ND2  . ASN   A 1 87  ? 24.000 8.186   15.807  1.00 18.32 ?  87  ASN   A ND2  1 
ATOM   1841 H  H    . ASN   A 1 87  ? 27.086 6.127   15.231  1.00 17.55 ?  87  ASN   A H    1 
ATOM   1842 H  HA   . ASN   A 1 87  ? 26.668 5.272   17.720  1.00 18.76 ?  87  ASN   A HA   1 
ATOM   1843 H  HB2  . ASN   A 1 87  ? 24.926 6.902   17.681  1.00 19.65 ?  87  ASN   A HB2  1 
ATOM   1844 H  HB3  . ASN   A 1 87  ? 26.360 7.522   17.387  1.00 19.65 ?  87  ASN   A HB3  1 
ATOM   1845 H  HD21 . ASN   A 1 87  ? 23.666 8.532   15.096  1.00 21.98 ?  87  ASN   A HD21 1 
ATOM   1846 H  HD22 . ASN   A 1 87  ? 23.596 8.269   16.560  1.00 21.98 ?  87  ASN   A HD22 1 
ATOM   1847 N  N    A LEU   A 1 88  ? 25.202 3.743   15.564  0.50 15.34 ?  88  LEU   A N    1 
ATOM   1848 N  N    B LEU   A 1 88  ? 25.200 3.733   15.569  0.50 15.41 ?  88  LEU   A N    1 
ATOM   1849 C  CA   A LEU   A 1 88  ? 24.111 2.867   15.148  0.50 14.99 ?  88  LEU   A CA   1 
ATOM   1850 C  CA   B LEU   A 1 88  ? 24.099 2.869   15.165  0.50 15.00 ?  88  LEU   A CA   1 
ATOM   1851 C  C    A LEU   A 1 88  ? 24.341 1.401   15.486  0.50 14.67 ?  88  LEU   A C    1 
ATOM   1852 C  C    B LEU   A 1 88  ? 24.339 1.387   15.416  0.50 14.71 ?  88  LEU   A C    1 
ATOM   1853 O  O    A LEU   A 1 88  ? 23.371 0.673   15.727  0.50 15.38 ?  88  LEU   A O    1 
ATOM   1854 O  O    B LEU   A 1 88  ? 23.367 0.631   15.516  0.50 15.21 ?  88  LEU   A O    1 
ATOM   1855 C  CB   A LEU   A 1 88  ? 23.903 2.987   13.634  0.50 15.22 ?  88  LEU   A CB   1 
ATOM   1856 C  CB   B LEU   A 1 88  ? 23.808 3.066   13.672  0.50 15.21 ?  88  LEU   A CB   1 
ATOM   1857 C  CG   A LEU   A 1 88  ? 23.632 4.391   13.090  0.50 16.47 ?  88  LEU   A CG   1 
ATOM   1858 C  CG   B LEU   A 1 88  ? 23.482 4.506   13.269  0.50 16.09 ?  88  LEU   A CG   1 
ATOM   1859 C  CD1  A LEU   A 1 88  ? 23.520 4.349   11.576  0.50 16.63 ?  88  LEU   A CD1  1 
ATOM   1860 C  CD1  B LEU   A 1 88  ? 23.259 4.613   11.767  0.50 16.17 ?  88  LEU   A CD1  1 
ATOM   1861 C  CD2  A LEU   A 1 88  ? 22.373 4.988   13.709  0.50 17.93 ?  88  LEU   A CD2  1 
ATOM   1862 C  CD2  B LEU   A 1 88  ? 22.266 5.024   14.030  0.50 16.92 ?  88  LEU   A CD2  1 
ATOM   1863 H  H    A LEU   A 1 88  ? 25.902 3.681   15.068  0.50 18.39 ?  88  LEU   A H    1 
ATOM   1864 H  H    B LEU   A 1 88  ? 25.896 3.665   15.073  0.50 18.48 ?  88  LEU   A H    1 
ATOM   1865 H  HA   A LEU   A 1 88  ? 23.295 3.146   15.583  0.50 17.97 ?  88  LEU   A HA   1 
ATOM   1866 H  HA   B LEU   A 1 88  ? 23.302 3.121   15.655  0.50 17.98 ?  88  LEU   A HA   1 
ATOM   1867 H  HB2  A LEU   A 1 88  ? 24.696 2.658   13.187  0.50 18.25 ?  88  LEU   A HB2  1 
ATOM   1868 H  HB2  B LEU   A 1 88  ? 24.586 2.787   13.165  0.50 18.24 ?  88  LEU   A HB2  1 
ATOM   1869 H  HB3  A LEU   A 1 88  ? 23.143 2.437   13.387  0.50 18.25 ?  88  LEU   A HB3  1 
ATOM   1870 H  HB3  B LEU   A 1 88  ? 23.046 2.515   13.429  0.50 18.24 ?  88  LEU   A HB3  1 
ATOM   1871 H  HG   A LEU   A 1 88  ? 24.378 4.967   13.316  0.50 19.75 ?  88  LEU   A HG   1 
ATOM   1872 H  HG   B LEU   A 1 88  ? 24.238 5.072   13.492  0.50 19.30 ?  88  LEU   A HG   1 
ATOM   1873 H  HD11 A LEU   A 1 88  ? 23.372 5.249   11.244  0.50 19.95 ?  88  LEU   A HD11 1 
ATOM   1874 H  HD11 B LEU   A 1 88  ? 23.069 5.537   11.540  0.50 19.39 ?  88  LEU   A HD11 1 
ATOM   1875 H  HD12 A LEU   A 1 88  ? 24.342 3.991   11.208  0.50 19.95 ?  88  LEU   A HD12 1 
ATOM   1876 H  HD12 B LEU   A 1 88  ? 24.060 4.318   11.305  0.50 19.39 ?  88  LEU   A HD12 1 
ATOM   1877 H  HD13 A LEU   A 1 88  ? 22.772 3.780   11.331  0.50 19.95 ?  88  LEU   A HD13 1 
ATOM   1878 H  HD13 B LEU   A 1 88  ? 22.508 4.051   11.517  0.50 19.39 ?  88  LEU   A HD13 1 
ATOM   1879 H  HD21 A LEU   A 1 88  ? 22.185 5.839   13.284  0.50 21.50 ?  88  LEU   A HD21 1 
ATOM   1880 H  HD21 B LEU   A 1 88  ? 21.995 5.872   13.645  0.50 20.29 ?  88  LEU   A HD21 1 
ATOM   1881 H  HD22 A LEU   A 1 88  ? 21.633 4.377   13.569  0.50 21.50 ?  88  LEU   A HD22 1 
ATOM   1882 H  HD22 B LEU   A 1 88  ? 21.549 4.378   13.951  0.50 20.29 ?  88  LEU   A HD22 1 
ATOM   1883 H  HD23 A LEU   A 1 88  ? 22.520 5.117   14.659  0.50 21.50 ?  88  LEU   A HD23 1 
ATOM   1884 H  HD23 B LEU   A 1 88  ? 22.508 5.143   14.960  0.50 20.29 ?  88  LEU   A HD23 1 
ATOM   1885 N  N    . ALA   A 1 89  ? 25.591 0.956   15.501  1.00 14.18 ?  89  ALA   A N    1 
ATOM   1886 C  CA   . ALA   A 1 89  ? 25.932 -0.452  15.634  1.00 13.90 ?  89  ALA   A CA   1 
ATOM   1887 C  C    . ALA   A 1 89  ? 27.416 -0.497  15.951  1.00 14.20 ?  89  ALA   A C    1 
ATOM   1888 O  O    . ALA   A 1 89  ? 28.117 0.508   15.834  1.00 14.95 ?  89  ALA   A O    1 
ATOM   1889 C  CB   . ALA   A 1 89  ? 25.677 -1.187  14.318  1.00 13.61 ?  89  ALA   A CB   1 
ATOM   1890 H  H    A ALA   A 1 89  ? 26.278 1.467   15.432  0.50 17.01 ?  89  ALA   A H    1 
ATOM   1891 H  H    B ALA   A 1 89  ? 26.276 1.472   15.461  0.50 17.01 ?  89  ALA   A H    1 
ATOM   1892 H  HA   . ALA   A 1 89  ? 25.421 -0.865  16.351  1.00 16.67 ?  89  ALA   A HA   1 
ATOM   1893 H  HB1  . ALA   A 1 89  ? 25.936 -2.116  14.417  1.00 16.33 ?  89  ALA   A HB1  1 
ATOM   1894 H  HB2  . ALA   A 1 89  ? 24.733 -1.129  14.097  1.00 16.33 ?  89  ALA   A HB2  1 
ATOM   1895 H  HB3  . ALA   A 1 89  ? 26.205 -0.771  13.618  1.00 16.33 ?  89  ALA   A HB3  1 
ATOM   1896 N  N    A LYS   A 1 90  ? 27.903 -1.679  16.319  0.50 14.52 ?  90  LYS   A N    1 
ATOM   1897 N  N    B LYS   A 1 90  ? 27.895 -1.665  16.372  0.50 14.33 ?  90  LYS   A N    1 
ATOM   1898 C  CA   A LYS   A 1 90  ? 29.347 -1.829  16.467  0.50 15.29 ?  90  LYS   A CA   1 
ATOM   1899 C  CA   B LYS   A 1 90  ? 29.336 -1.808  16.540  0.50 14.89 ?  90  LYS   A CA   1 
ATOM   1900 C  C    A LYS   A 1 90  ? 30.048 -1.661  15.122  0.50 14.59 ?  90  LYS   A C    1 
ATOM   1901 C  C    B LYS   A 1 90  ? 30.049 -1.630  15.206  0.50 13.79 ?  90  LYS   A C    1 
ATOM   1902 O  O    A LYS   A 1 90  ? 30.961 -0.833  14.979  0.50 15.63 ?  90  LYS   A O    1 
ATOM   1903 O  O    B LYS   A 1 90  ? 31.027 -0.875  15.099  0.50 14.74 ?  90  LYS   A O    1 
ATOM   1904 C  CB   A LYS   A 1 90  ? 29.684 -3.177  17.109  0.50 17.53 ?  90  LYS   A CB   1 
ATOM   1905 C  CB   B LYS   A 1 90  ? 29.674 -3.164  17.159  0.50 17.23 ?  90  LYS   A CB   1 
ATOM   1906 C  CG   A LYS   A 1 90  ? 31.172 -3.367  17.392  0.50 21.17 ?  90  LYS   A CG   1 
ATOM   1907 C  CG   B LYS   A 1 90  ? 31.156 -3.332  17.466  0.50 20.97 ?  90  LYS   A CG   1 
ATOM   1908 C  CD   A LYS   A 1 90  ? 31.416 -4.574  18.288  0.50 24.45 ?  90  LYS   A CD   1 
ATOM   1909 C  CD   B LYS   A 1 90  ? 31.408 -4.566  18.316  0.50 24.31 ?  90  LYS   A CD   1 
ATOM   1910 C  CE   A LYS   A 1 90  ? 32.841 -4.605  18.832  0.50 26.99 ?  90  LYS   A CE   1 
ATOM   1911 C  CE   B LYS   A 1 90  ? 32.798 -4.548  18.935  0.50 26.88 ?  90  LYS   A CE   1 
ATOM   1912 N  NZ   A LYS   A 1 90  ? 33.839 -5.061  17.827  0.50 28.62 ?  90  LYS   A NZ   1 
ATOM   1913 N  NZ   B LYS   A 1 90  ? 33.878 -4.677  17.921  0.50 28.48 ?  90  LYS   A NZ   1 
ATOM   1914 H  H    A LYS   A 1 90  ? 27.436 -2.379  16.487  0.50 17.41 ?  90  LYS   A H    1 
ATOM   1915 H  H    B LYS   A 1 90  ? 27.422 -2.354  16.571  0.50 17.19 ?  90  LYS   A H    1 
ATOM   1916 H  HA   A LYS   A 1 90  ? 29.674 -1.134  17.056  0.50 18.34 ?  90  LYS   A HA   1 
ATOM   1917 H  HA   B LYS   A 1 90  ? 29.653 -1.116  17.138  0.50 17.85 ?  90  LYS   A HA   1 
ATOM   1918 H  HB2  A LYS   A 1 90  ? 29.208 -3.247  17.956  0.50 21.02 ?  90  LYS   A HB2  1 
ATOM   1919 H  HB2  B LYS   A 1 90  ? 29.182 -3.257  17.991  0.50 20.67 ?  90  LYS   A HB2  1 
ATOM   1920 H  HB3  A LYS   A 1 90  ? 29.398 -3.890  16.517  0.50 21.02 ?  90  LYS   A HB3  1 
ATOM   1921 H  HB3  B LYS   A 1 90  ? 29.412 -3.864  16.542  0.50 20.67 ?  90  LYS   A HB3  1 
ATOM   1922 H  HG2  A LYS   A 1 90  ? 31.641 -3.509  16.555  0.50 25.40 ?  90  LYS   A HG2  1 
ATOM   1923 H  HG2  B LYS   A 1 90  ? 31.648 -3.426  16.635  0.50 25.15 ?  90  LYS   A HG2  1 
ATOM   1924 H  HG3  A LYS   A 1 90  ? 31.516 -2.579  17.841  0.50 25.40 ?  90  LYS   A HG3  1 
ATOM   1925 H  HG3  B LYS   A 1 90  ? 31.471 -2.557  17.955  0.50 25.15 ?  90  LYS   A HG3  1 
ATOM   1926 H  HD2  A LYS   A 1 90  ? 30.806 -4.540  19.041  0.50 29.32 ?  90  LYS   A HD2  1 
ATOM   1927 H  HD2  B LYS   A 1 90  ? 30.756 -4.597  19.034  0.50 29.16 ?  90  LYS   A HD2  1 
ATOM   1928 H  HD3  A LYS   A 1 90  ? 31.270 -5.385  17.776  0.50 29.32 ?  90  LYS   A HD3  1 
ATOM   1929 H  HD3  B LYS   A 1 90  ? 31.332 -5.358  17.761  0.50 29.16 ?  90  LYS   A HD3  1 
ATOM   1930 H  HE2  A LYS   A 1 90  ? 33.090 -3.712  19.117  0.50 32.38 ?  90  LYS   A HE2  1 
ATOM   1931 H  HE2  B LYS   A 1 90  ? 32.925 -3.708  19.403  0.50 32.24 ?  90  LYS   A HE2  1 
ATOM   1932 H  HE3  A LYS   A 1 90  ? 32.877 -5.214  19.586  0.50 32.38 ?  90  LYS   A HE3  1 
ATOM   1933 H  HE3  B LYS   A 1 90  ? 32.878 -5.290  19.555  0.50 32.24 ?  90  LYS   A HE3  1 
ATOM   1934 H  HZ1  A LYS   A 1 90  ? 34.646 -5.114  18.202  0.50 34.34 ?  90  LYS   A HZ1  1 
ATOM   1935 H  HZ1  B LYS   A 1 90  ? 34.674 -4.665  18.321  0.50 34.16 ?  90  LYS   A HZ1  1 
ATOM   1936 H  HZ2  A LYS   A 1 90  ? 33.613 -5.863  17.515  0.50 34.34 ?  90  LYS   A HZ2  1 
ATOM   1937 H  HZ2  B LYS   A 1 90  ? 33.790 -5.445  17.479  0.50 34.16 ?  90  LYS   A HZ2  1 
ATOM   1938 H  HZ3  A LYS   A 1 90  ? 33.873 -4.485  17.149  0.50 34.34 ?  90  LYS   A HZ3  1 
ATOM   1939 H  HZ3  B LYS   A 1 90  ? 33.835 -4.004  17.342  0.50 34.16 ?  90  LYS   A HZ3  1 
ATOM   1940 N  N    A HIS   A 1 91  ? 29.610 -2.417  14.116  0.50 13.21 ?  91  HIS   A N    1 
ATOM   1941 N  N    B HIS   A 1 91  ? 29.552 -2.308  14.173  0.50 12.06 ?  91  HIS   A N    1 
ATOM   1942 C  CA   A HIS   A 1 91  ? 30.198 -2.400  12.788  0.50 12.91 ?  91  HIS   A CA   1 
ATOM   1943 C  CA   B HIS   A 1 91  ? 30.140 -2.290  12.848  0.50 11.63 ?  91  HIS   A CA   1 
ATOM   1944 C  C    A HIS   A 1 91  ? 29.114 -2.143  11.758  0.50 11.29 ?  91  HIS   A C    1 
ATOM   1945 C  C    B HIS   A 1 91  ? 29.063 -2.008  11.815  0.50 10.88 ?  91  HIS   A C    1 
ATOM   1946 O  O    A HIS   A 1 91  ? 27.965 -2.566  11.918  0.50 10.87 ?  91  HIS   A O    1 
ATOM   1947 O  O    B HIS   A 1 91  ? 27.878 -2.287  12.022  0.50 11.62 ?  91  HIS   A O    1 
ATOM   1948 C  CB   A HIS   A 1 91  ? 30.814 -3.758  12.428  0.50 15.26 ?  91  HIS   A CB   1 
ATOM   1949 C  CB   B HIS   A 1 91  ? 30.755 -3.652  12.498  0.50 13.78 ?  91  HIS   A CB   1 
ATOM   1950 C  CG   A HIS   A 1 91  ? 31.808 -4.263  13.424  0.50 18.50 ?  91  HIS   A CG   1 
ATOM   1951 C  CG   B HIS   A 1 91  ? 31.718 -4.163  13.519  0.50 17.02 ?  91  HIS   A CG   1 
ATOM   1952 N  ND1  A HIS   A 1 91  ? 33.077 -3.740  13.539  0.50 20.03 ?  91  HIS   A ND1  1 
ATOM   1953 N  ND1  B HIS   A 1 91  ? 32.998 -3.671  13.645  0.50 18.70 ?  91  HIS   A ND1  1 
ATOM   1954 C  CD2  A HIS   A 1 91  ? 31.729 -5.261  14.336  0.50 19.99 ?  91  HIS   A CD2  1 
ATOM   1955 C  CD2  B HIS   A 1 91  ? 31.592 -5.130  14.458  0.50 18.54 ?  91  HIS   A CD2  1 
ATOM   1956 C  CE1  A HIS   A 1 91  ? 33.733 -4.384  14.488  0.50 20.83 ?  91  HIS   A CE1  1 
ATOM   1957 C  CE1  B HIS   A 1 91  ? 33.620 -4.309  14.621  0.50 19.49 ?  91  HIS   A CE1  1 
ATOM   1958 N  NE2  A HIS   A 1 91  ? 32.937 -5.313  14.987  0.50 20.95 ?  91  HIS   A NE2  1 
ATOM   1959 N  NE2  B HIS   A 1 91  ? 32.787 -5.200  15.131  0.50 19.60 ?  91  HIS   A NE2  1 
ATOM   1960 H  H    A HIS   A 1 91  ? 28.945 -2.971  14.186  0.50 15.84 ?  91  HIS   A H    1 
ATOM   1961 H  H    B HIS   A 1 91  ? 28.846 -2.814  14.226  0.50 14.46 ?  91  HIS   A H    1 
ATOM   1962 H  HA   A HIS   A 1 91  ? 30.876 -1.714  12.723  0.50 15.48 ?  91  HIS   A HA   1 
ATOM   1963 H  HA   B HIS   A 1 91  ? 30.822 -1.608  12.800  0.50 13.95 ?  91  HIS   A HA   1 
ATOM   1964 H  HB2  A HIS   A 1 91  ? 30.105 -4.417  12.362  0.50 18.30 ?  91  HIS   A HB2  1 
ATOM   1965 H  HB2  B HIS   A 1 91  ? 30.042 -4.305  12.411  0.50 16.52 ?  91  HIS   A HB2  1 
ATOM   1966 H  HB3  A HIS   A 1 91  ? 31.267 -3.679  11.574  0.50 18.30 ?  91  HIS   A HB3  1 
ATOM   1967 H  HB3  B HIS   A 1 91  ? 31.228 -3.570  11.656  0.50 16.52 ?  91  HIS   A HB3  1 
ATOM   1968 H  HD1  A HIS   A 1 91  ? 33.391 -3.089  13.069  0.50 24.03 ?  91  HIS   A HD1  1 
ATOM   1969 H  HD1  B HIS   A 1 91  ? 33.339 -3.041  13.162  0.50 22.42 ?  91  HIS   A HD1  1 
ATOM   1970 H  HD2  A HIS   A 1 91  ? 30.993 -5.804  14.495  0.50 23.97 ?  91  HIS   A HD2  1 
ATOM   1971 H  HD2  B HIS   A 1 91  ? 30.843 -5.651  14.619  0.50 22.23 ?  91  HIS   A HD2  1 
ATOM   1972 H  HE1  A HIS   A 1 91  ? 34.607 -4.209  14.756  0.50 24.98 ?  91  HIS   A HE1  1 
ATOM   1973 H  HE1  B HIS   A 1 91  ? 34.497 -4.153  14.897  0.50 23.37 ?  91  HIS   A HE1  1 
ATOM   1974 N  N    . CYS   A 1 92  ? 29.497 -1.476  10.676  1.00 10.84 ?  92  CYS   A N    1 
ATOM   1975 C  CA   . CYS   A 1 92  ? 28.670 -1.391  9.481   1.00 10.87 ?  92  CYS   A CA   1 
ATOM   1976 C  C    . CYS   A 1 92  ? 29.328 -2.208  8.378   1.00 10.19 ?  92  CYS   A C    1 
ATOM   1977 O  O    . CYS   A 1 92  ? 30.489 -1.964  8.022   1.00 11.02 ?  92  CYS   A O    1 
ATOM   1978 C  CB   . CYS   A 1 92  ? 28.457 0.047   9.021   1.00 10.82 ?  92  CYS   A CB   1 
ATOM   1979 S  SG   . CYS   A 1 92  ? 27.452 0.143   7.498   1.00 10.66 ?  92  CYS   A SG   1 
ATOM   1980 H  H    A CYS   A 1 92  ? 30.241 -1.052  10.615  0.50 13.00 ?  92  CYS   A H    1 
ATOM   1981 H  H    B CYS   A 1 92  ? 30.290 -1.165  10.567  0.50 13.00 ?  92  CYS   A H    1 
ATOM   1982 H  HA   . CYS   A 1 92  ? 27.800 -1.779  9.667   1.00 13.03 ?  92  CYS   A HA   1 
ATOM   1983 H  HB2  . CYS   A 1 92  ? 27.989 0.539   9.713   1.00 12.98 ?  92  CYS   A HB2  1 
ATOM   1984 H  HB3  . CYS   A 1 92  ? 29.312 0.455   8.835   1.00 12.98 ?  92  CYS   A HB3  1 
ATOM   1985 H  HG   . CYS   A 1 92  ? 27.311 1.292   7.199   1.00 12.78 ?  92  CYS   A HG   1 
ATOM   1986 N  N    . LEU   A 1 93  ? 28.600 -3.199  7.873   1.00 9.86  ?  93  LEU   A N    1 
ATOM   1987 C  CA   . LEU   A 1 93  ? 29.020 -3.961  6.702   1.00 9.77  ?  93  LEU   A CA   1 
ATOM   1988 C  C    . LEU   A 1 93  ? 28.430 -3.275  5.470   1.00 9.45  ?  93  LEU   A C    1 
ATOM   1989 O  O    . LEU   A 1 93  ? 27.215 -3.341  5.231   1.00 9.44  ?  93  LEU   A O    1 
ATOM   1990 C  CB   . LEU   A 1 93  ? 28.542 -5.410  6.816   1.00 10.43 ?  93  LEU   A CB   1 
ATOM   1991 C  CG   . LEU   A 1 93  ? 28.944 -6.301  5.645   1.00 10.54 ?  93  LEU   A CG   1 
ATOM   1992 C  CD1  . LEU   A 1 93  ? 30.447 -6.556  5.644   1.00 11.25 ?  93  LEU   A CD1  1 
ATOM   1993 C  CD2  . LEU   A 1 93  ? 28.177 -7.636  5.685   1.00 11.55 ?  93  LEU   A CD2  1 
ATOM   1994 H  H    . LEU   A 1 93  ? 27.841 -3.452  8.204   1.00 11.83 ?  93  LEU   A H    1 
ATOM   1995 H  HA   . LEU   A 1 93  ? 29.983 -3.947  6.640   1.00 11.71 ?  93  LEU   A HA   1 
ATOM   1996 H  HB2  . LEU   A 1 93  ? 28.922 -5.794  7.625   1.00 12.51 ?  93  LEU   A HB2  1 
ATOM   1997 H  HB3  . LEU   A 1 93  ? 27.578 -5.414  6.876   1.00 12.51 ?  93  LEU   A HB3  1 
ATOM   1998 H  HG   . LEU   A 1 93  ? 28.721 -5.855  4.817   1.00 12.64 ?  93  LEU   A HG   1 
ATOM   1999 H  HD11 . LEU   A 1 93  ? 30.666 -7.166  4.924   1.00 13.49 ?  93  LEU   A HD11 1 
ATOM   2000 H  HD12 . LEU   A 1 93  ? 30.915 -5.715  5.519   1.00 13.49 ?  93  LEU   A HD12 1 
ATOM   2001 H  HD13 . LEU   A 1 93  ? 30.704 -6.950  6.497   1.00 13.49 ?  93  LEU   A HD13 1 
ATOM   2002 H  HD21 . LEU   A 1 93  ? 28.456 -8.181  4.932   1.00 13.85 ?  93  LEU   A HD21 1 
ATOM   2003 H  HD22 . LEU   A 1 93  ? 28.383 -8.094  6.517   1.00 13.85 ?  93  LEU   A HD22 1 
ATOM   2004 H  HD23 . LEU   A 1 93  ? 27.228 -7.456  5.633   1.00 13.85 ?  93  LEU   A HD23 1 
ATOM   2005 N  N    . HIS   A 1 94  ? 29.279 -2.576  4.716   1.00 9.31  ?  94  HIS   A N    1 
ATOM   2006 C  CA   . HIS   A 1 94  ? 28.859 -1.913  3.485   1.00 9.48  ?  94  HIS   A CA   1 
ATOM   2007 C  C    . HIS   A 1 94  ? 28.886 -2.948  2.374   1.00 9.31  ?  94  HIS   A C    1 
ATOM   2008 O  O    . HIS   A 1 94  ? 29.959 -3.458  2.045   1.00 10.86 ?  94  HIS   A O    1 
ATOM   2009 C  CB   . HIS   A 1 94  ? 29.809 -0.756  3.155   1.00 9.60  ?  94  HIS   A CB   1 
ATOM   2010 C  CG   . HIS   A 1 94  ? 29.789 0.333   4.171   1.00 9.54  ?  94  HIS   A CG   1 
ATOM   2011 N  ND1  . HIS   A 1 94  ? 28.915 1.397   4.102   1.00 9.61  ?  94  HIS   A ND1  1 
ATOM   2012 C  CD2  . HIS   A 1 94  ? 30.525 0.507   5.292   1.00 10.17 ?  94  HIS   A CD2  1 
ATOM   2013 C  CE1  . HIS   A 1 94  ? 29.117 2.177   5.147   1.00 9.98  ?  94  HIS   A CE1  1 
ATOM   2014 N  NE2  . HIS   A 1 94  ? 30.090 1.664   5.881   1.00 10.38 ?  94  HIS   A NE2  1 
ATOM   2015 H  H    . HIS   A 1 94  ? 30.108 -2.472  4.901   1.00 11.16 ?  94  HIS   A H    1 
ATOM   2016 H  HA   . HIS   A 1 94  ? 27.954 -1.566  3.578   1.00 11.37 ?  94  HIS   A HA   1 
ATOM   2017 H  HB2  . HIS   A 1 94  ? 30.708 -1.098  3.101   1.00 11.51 ?  94  HIS   A HB2  1 
ATOM   2018 H  HB3  . HIS   A 1 94  ? 29.543 -0.370  2.304   1.00 11.51 ?  94  HIS   A HB3  1 
ATOM   2019 H  HD2  . HIS   A 1 94  ? 31.198 -0.050  5.607   1.00 12.19 ?  94  HIS   A HD2  1 
ATOM   2020 H  HE1  . HIS   A 1 94  ? 28.655 2.969   5.326   1.00 11.96 ?  94  HIS   A HE1  1 
ATOM   2021 H  HE2  . HIS   A 1 94  ? 30.400 2.011   6.604   1.00 12.44 ?  94  HIS   A HE2  1 
ATOM   2022 N  N    . VAL   A 1 95  ? 27.723 -3.272  1.810   1.00 9.08  ?  95  VAL   A N    1 
ATOM   2023 C  CA   . VAL   A 1 95  ? 27.601 -4.311  0.796   1.00 9.12  ?  95  VAL   A CA   1 
ATOM   2024 C  C    . VAL   A 1 95  ? 27.051 -3.690  -0.475  1.00 9.14  ?  95  VAL   A C    1 
ATOM   2025 O  O    . VAL   A 1 95  ? 26.038 -2.974  -0.432  1.00 9.74  ?  95  VAL   A O    1 
ATOM   2026 C  CB   . VAL   A 1 95  ? 26.680 -5.459  1.248   1.00 9.71  ?  95  VAL   A CB   1 
ATOM   2027 C  CG1  . VAL   A 1 95  ? 26.604 -6.516  0.156   1.00 10.52 ?  95  VAL   A CG1  1 
ATOM   2028 C  CG2  . VAL   A 1 95  ? 27.157 -6.048  2.564   1.00 10.08 ?  95  VAL   A CG2  1 
ATOM   2029 H  H    . VAL   A 1 95  ? 26.973 -2.901  2.016   1.00 10.89 ?  95  VAL   A H    1 
ATOM   2030 H  HA   . VAL   A 1 95  ? 28.474 -4.678  0.606   1.00 10.93 ?  95  VAL   A HA   1 
ATOM   2031 H  HB   . VAL   A 1 95  ? 25.790 -5.110  1.390   1.00 11.64 ?  95  VAL   A HB   1 
ATOM   2032 H  HG11 . VAL   A 1 95  ? 26.221 -7.327  0.528   1.00 12.62 ?  95  VAL   A HG11 1 
ATOM   2033 H  HG12 . VAL   A 1 95  ? 26.041 -6.189  -0.564  1.00 12.62 ?  95  VAL   A HG12 1 
ATOM   2034 H  HG13 . VAL   A 1 95  ? 27.497 -6.696  -0.177  1.00 12.62 ?  95  VAL   A HG13 1 
ATOM   2035 H  HG21 . VAL   A 1 95  ? 26.601 -6.811  2.783   1.00 12.09 ?  95  VAL   A HG21 1 
ATOM   2036 H  HG22 . VAL   A 1 95  ? 28.080 -6.322  2.469   1.00 12.09 ?  95  VAL   A HG22 1 
ATOM   2037 H  HG23 . VAL   A 1 95  ? 27.079 -5.372  3.255   1.00 12.09 ?  95  VAL   A HG23 1 
ATOM   2038 N  N    . VAL   A 1 96  ? 27.698 -3.978  -1.605  1.00 9.41  ?  96  VAL   A N    1 
ATOM   2039 C  CA   . VAL   A 1 96  ? 27.293 -3.436  -2.897  1.00 9.56  ?  96  VAL   A CA   1 
ATOM   2040 C  C    . VAL   A 1 96  ? 26.515 -4.495  -3.671  1.00 10.02 ?  96  VAL   A C    1 
ATOM   2041 O  O    . VAL   A 1 96  ? 27.094 -5.440  -4.215  1.00 10.83 ?  96  VAL   A O    1 
ATOM   2042 C  CB   . VAL   A 1 96  ? 28.489 -2.950  -3.716  1.00 10.16 ?  96  VAL   A CB   1 
ATOM   2043 C  CG1  . VAL   A 1 96  ? 27.994 -2.331  -5.010  1.00 10.18 ?  96  VAL   A CG1  1 
ATOM   2044 C  CG2  . VAL   A 1 96  ? 29.335 -1.963  -2.921  1.00 10.59 ?  96  VAL   A CG2  1 
ATOM   2045 H  H    . VAL   A 1 96  ? 28.398 -4.484  -1.641  1.00 11.28 ?  96  VAL   A H    1 
ATOM   2046 H  HA   . VAL   A 1 96  ? 26.708 -2.679  -2.749  1.00 11.46 ?  96  VAL   A HA   1 
ATOM   2047 H  HB   . VAL   A 1 96  ? 29.051 -3.703  -3.942  1.00 12.19 ?  96  VAL   A HB   1 
ATOM   2048 H  HG11 . VAL   A 1 96  ? 28.723 -1.838  -5.424  1.00 12.21 ?  96  VAL   A HG11 1 
ATOM   2049 H  HG12 . VAL   A 1 96  ? 27.691 -3.030  -5.605  1.00 12.21 ?  96  VAL   A HG12 1 
ATOM   2050 H  HG13 . VAL   A 1 96  ? 27.263 -1.721  -4.812  1.00 12.21 ?  96  VAL   A HG13 1 
ATOM   2051 H  HG21 . VAL   A 1 96  ? 30.037 -1.615  -3.490  1.00 12.70 ?  96  VAL   A HG21 1 
ATOM   2052 H  HG22 . VAL   A 1 96  ? 28.766 -1.236  -2.614  1.00 12.70 ?  96  VAL   A HG22 1 
ATOM   2053 H  HG23 . VAL   A 1 96  ? 29.721 -2.422  -2.158  1.00 12.70 ?  96  VAL   A HG23 1 
ATOM   2054 N  N    A GLY   A 1 97  ? 25.193 -4.360  -3.681  0.50 10.10 ?  97  GLY   A N    1 
ATOM   2055 N  N    B GLY   A 1 97  ? 25.198 -4.335  -3.770  0.50 9.99  ?  97  GLY   A N    1 
ATOM   2056 C  CA   A GLY   A 1 97  ? 24.373 -5.117  -4.588  0.50 10.56 ?  97  GLY   A CA   1 
ATOM   2057 C  CA   B GLY   A 1 97  ? 24.426 -5.134  -4.693  0.50 10.32 ?  97  GLY   A CA   1 
ATOM   2058 C  C    A GLY   A 1 97  ? 24.363 -4.441  -5.942  0.50 10.38 ?  97  GLY   A C    1 
ATOM   2059 C  C    B GLY   A 1 97  ? 24.506 -4.560  -6.098  0.50 10.54 ?  97  GLY   A C    1 
ATOM   2060 O  O    A GLY   A 1 97  ? 24.621 -3.238  -6.057  0.50 10.53 ?  97  GLY   A O    1 
ATOM   2061 O  O    B GLY   A 1 97  ? 24.831 -3.382  -6.291  0.50 11.17 ?  97  GLY   A O    1 
ATOM   2062 H  H    A GLY   A 1 97  ? 24.752 -3.828  -3.166  0.50 12.11 ?  97  GLY   A H    1 
ATOM   2063 H  H    B GLY   A 1 97  ? 24.732 -3.774  -3.310  0.50 11.97 ?  97  GLY   A H    1 
ATOM   2064 H  HA2  A GLY   A 1 97  ? 24.730 -6.011  -4.680  0.50 12.66 ?  97  GLY   A HA2  1 
ATOM   2065 H  HA2  B GLY   A 1 97  ? 24.769 -6.045  -4.694  0.50 12.37 ?  97  GLY   A HA2  1 
ATOM   2066 H  HA3  A GLY   A 1 97  ? 23.464 -5.169  -4.250  0.50 12.66 ?  97  GLY   A HA3  1 
ATOM   2067 H  HA3  B GLY   A 1 97  ? 23.497 -5.157  -4.412  0.50 12.37 ?  97  GLY   A HA3  1 
ATOM   2068 N  N    A PRO   A 1 98  ? 24.060 -5.194  -6.996  0.50 10.46 ?  98  PRO   A N    1 
ATOM   2069 N  N    B PRO   A 1 98  ? 24.208 -5.376  -7.111  0.50 10.99 ?  98  PRO   A N    1 
ATOM   2070 C  CA   A PRO   A 1 98  ? 23.968 -4.584  -8.325  0.50 10.94 ?  98  PRO   A CA   1 
ATOM   2071 C  CA   B PRO   A 1 98  ? 24.183 -4.856  -8.484  0.50 11.39 ?  98  PRO   A CA   1 
ATOM   2072 C  C    A PRO   A 1 98  ? 22.853 -3.551  -8.374  0.50 11.02 ?  98  PRO   A C    1 
ATOM   2073 C  C    B PRO   A 1 98  ? 23.076 -3.829  -8.677  0.50 11.19 ?  98  PRO   A C    1 
ATOM   2074 O  O    A PRO   A 1 98  ? 21.785 -3.729  -7.781  0.50 10.93 ?  98  PRO   A O    1 
ATOM   2075 O  O    B PRO   A 1 98  ? 21.969 -3.958  -8.147  0.50 11.51 ?  98  PRO   A O    1 
ATOM   2076 C  CB   A PRO   A 1 98  ? 23.673 -5.778  -9.242  0.50 11.20 ?  98  PRO   A CB   1 
ATOM   2077 C  CB   B PRO   A 1 98  ? 23.936 -6.109  -9.336  0.50 11.69 ?  98  PRO   A CB   1 
ATOM   2078 C  CG   A PRO   A 1 98  ? 23.044 -6.804  -8.346  0.50 11.30 ?  98  PRO   A CG   1 
ATOM   2079 C  CG   B PRO   A 1 98  ? 23.275 -7.080  -8.408  0.50 12.18 ?  98  PRO   A CG   1 
ATOM   2080 C  CD   A PRO   A 1 98  ? 23.739 -6.632  -7.019  0.50 10.88 ?  98  PRO   A CD   1 
ATOM   2081 C  CD   B PRO   A 1 98  ? 23.928 -6.824  -7.071  0.50 11.40 ?  98  PRO   A CD   1 
ATOM   2082 H  HA   A PRO   A 1 98  ? 24.809 -4.176  -8.577  0.50 13.12 ?  98  PRO   A HA   1 
ATOM   2083 H  HA   B PRO   A 1 98  ? 25.047 -4.475  -8.718  0.50 13.65 ?  98  PRO   A HA   1 
ATOM   2084 H  HB2  A PRO   A 1 98  ? 23.055 -5.514  -9.939  0.50 13.43 ?  98  PRO   A HB2  1 
ATOM   2085 H  HB2  B PRO   A 1 98  ? 23.348 -5.889  -10.073 0.50 14.01 ?  98  PRO   A HB2  1 
ATOM   2086 H  HB3  A PRO   A 1 98  ? 24.500 -6.115  -9.620  0.50 13.43 ?  98  PRO   A HB3  1 
ATOM   2087 H  HB3  B PRO   A 1 98  ? 24.778 -6.468  -9.658  0.50 14.01 ?  98  PRO   A HB3  1 
ATOM   2088 H  HG2  A PRO   A 1 98  ? 22.095 -6.633  -8.257  0.50 13.55 ?  98  PRO   A HG2  1 
ATOM   2089 H  HG2  B PRO   A 1 98  ? 22.322 -6.897  -8.364  0.50 14.61 ?  98  PRO   A HG2  1 
ATOM   2090 H  HG3  A PRO   A 1 98  ? 23.204 -7.695  -8.698  0.50 13.55 ?  98  PRO   A HG3  1 
ATOM   2091 H  HG3  B PRO   A 1 98  ? 23.438 -7.988  -8.708  0.50 14.61 ?  98  PRO   A HG3  1 
ATOM   2092 H  HD2  A PRO   A 1 98  ? 23.142 -6.860  -6.286  0.50 13.04 ?  98  PRO   A HD2  1 
ATOM   2093 H  HD2  B PRO   A 1 98  ? 23.316 -7.038  -6.348  0.50 13.67 ?  98  PRO   A HD2  1 
ATOM   2094 H  HD3  A PRO   A 1 98  ? 24.556 -7.159  -6.984  0.50 13.04 ?  98  PRO   A HD3  1 
ATOM   2095 H  HD3  B PRO   A 1 98  ? 24.753 -7.341  -6.996  0.50 13.67 ?  98  PRO   A HD3  1 
ATOM   2096 N  N    A ASN   A 1 99  ? 23.119 -2.456  -9.082  0.50 11.79 ?  99  ASN   A N    1 
ATOM   2097 N  N    B ASN   A 1 99  ? 23.391 -2.797  -9.449  0.50 11.56 ?  99  ASN   A N    1 
ATOM   2098 C  CA   A ASN   A 1 99  ? 22.136 -1.403  -9.314  0.50 13.34 ?  99  ASN   A CA   1 
ATOM   2099 C  CA   B ASN   A 1 99  ? 22.445 -1.746  -9.805  0.50 12.30 ?  99  ASN   A CA   1 
ATOM   2100 C  C    A ASN   A 1 99  ? 21.563 -1.611  -10.710 0.50 14.70 ?  99  ASN   A C    1 
ATOM   2101 C  C    B ASN   A 1 99  ? 21.929 -2.069  -11.203 0.50 12.87 ?  99  ASN   A C    1 
ATOM   2102 O  O    A ASN   A 1 99  ? 22.255 -1.397  -11.711 0.50 15.71 ?  99  ASN   A O    1 
ATOM   2103 O  O    B ASN   A 1 99  ? 22.634 -1.883  -12.199 0.50 12.80 ?  99  ASN   A O    1 
ATOM   2104 C  CB   A ASN   A 1 99  ? 22.786 -0.025  -9.189  0.50 13.76 ?  99  ASN   A CB   1 
ATOM   2105 C  CB   B ASN   A 1 99  ? 23.142 -0.392  -9.770  0.50 13.12 ?  99  ASN   A CB   1 
ATOM   2106 C  CG   A ASN   A 1 99  ? 21.765 1.118   -9.154  0.50 14.70 ?  99  ASN   A CG   1 
ATOM   2107 C  CG   B ASN   A 1 99  ? 22.202 0.754   -10.052 0.50 14.09 ?  99  ASN   A CG   1 
ATOM   2108 O  OD1  A ASN   A 1 99  ? 20.748 1.086   -9.846  0.50 15.43 ?  99  ASN   A OD1  1 
ATOM   2109 O  OD1  B ASN   A 1 99  ? 21.205 0.596   -10.751 0.50 13.73 ?  99  ASN   A OD1  1 
ATOM   2110 N  ND2  A ASN   A 1 99  ? 22.044 2.131   -8.343  0.50 15.17 ?  99  ASN   A ND2  1 
ATOM   2111 N  ND2  B ASN   A 1 99  ? 22.518 1.923   -9.509  0.50 15.36 ?  99  ASN   A ND2  1 
ATOM   2112 H  H    A ASN   A 1 99  ? 23.884 -2.297  -9.435  0.50 14.13 ?  99  ASN   A H    1 
ATOM   2113 H  H    B ASN   A 1 99  ? 24.177 -2.680  -9.775  0.50 13.86 ?  99  ASN   A H    1 
ATOM   2114 H  HA   A ASN   A 1 99  ? 21.416 -1.475  -8.667  0.50 15.99 ?  99  ASN   A HA   1 
ATOM   2115 H  HA   B ASN   A 1 99  ? 21.702 -1.748  -9.179  0.50 14.75 ?  99  ASN   A HA   1 
ATOM   2116 H  HB2  A ASN   A 1 99  ? 23.303 0.004   -8.373  0.50 16.50 ?  99  ASN   A HB2  1 
ATOM   2117 H  HB2  B ASN   A 1 99  ? 23.533 -0.258  -8.892  0.50 15.74 ?  99  ASN   A HB2  1 
ATOM   2118 H  HB3  A ASN   A 1 99  ? 23.364 0.115   -9.957  0.50 16.50 ?  99  ASN   A HB3  1 
ATOM   2119 H  HB3  B ASN   A 1 99  ? 23.833 -0.378  -10.448 0.50 15.74 ?  99  ASN   A HB3  1 
ATOM   2120 H  HD21 A ASN   A 1 99  ? 21.504 2.795   -8.283  0.50 18.19 ?  99  ASN   A HD21 1 
ATOM   2121 H  HD21 B ASN   A 1 99  ? 22.015 2.609   -9.630  0.50 18.42 ?  99  ASN   A HD21 1 
ATOM   2122 H  HD22 A ASN   A 1 99  ? 22.768 2.119   -7.876  0.50 18.19 ?  99  ASN   A HD22 1 
ATOM   2123 H  HD22 B ASN   A 1 99  ? 23.234 1.995   -9.033  0.50 18.42 ?  99  ASN   A HD22 1 
ATOM   2124 N  N    A VAL   A 1 100 ? 20.300 -2.043  -10.773 0.50 16.01 ?  100 VAL   A N    1 
ATOM   2125 N  N    B VAL   A 1 100 ? 20.692 -2.564  -11.273 0.50 14.47 ?  100 VAL   A N    1 
ATOM   2126 C  CA   A VAL   A 1 100 ? 19.662 -2.296  -12.063 0.50 17.65 ?  100 VAL   A CA   1 
ATOM   2127 C  CA   B VAL   A 1 100 ? 20.120 -2.951  -12.555 0.50 16.99 ?  100 VAL   A CA   1 
ATOM   2128 C  C    A VAL   A 1 100 ? 19.587 -1.016  -12.885 0.50 19.00 ?  100 VAL   A C    1 
ATOM   2129 C  C    B VAL   A 1 100 ? 19.879 -1.745  -13.453 0.50 17.14 ?  100 VAL   A C    1 
ATOM   2130 O  O    A VAL   A 1 100 ? 19.716 -1.049  -14.115 0.50 19.24 ?  100 VAL   A O    1 
ATOM   2131 O  O    B VAL   A 1 100 ? 19.842 -1.894  -14.680 0.50 17.98 ?  100 VAL   A O    1 
ATOM   2132 C  CB   A VAL   A 1 100 ? 18.281 -2.962  -11.864 0.50 18.70 ?  100 VAL   A CB   1 
ATOM   2133 C  CB   B VAL   A 1 100 ? 18.861 -3.813  -12.331 0.50 19.87 ?  100 VAL   A CB   1 
ATOM   2134 C  CG1  A VAL   A 1 100 ? 17.546 -3.100  -13.190 0.50 19.51 ?  100 VAL   A CG1  1 
ATOM   2135 C  CG1  B VAL   A 1 100 ? 17.818 -3.583  -13.423 0.50 20.91 ?  100 VAL   A CG1  1 
ATOM   2136 C  CG2  A VAL   A 1 100 ? 18.445 -4.326  -11.205 0.50 18.85 ?  100 VAL   A CG2  1 
ATOM   2137 C  CG2  B VAL   A 1 100 ? 19.243 -5.283  -12.260 0.50 20.86 ?  100 VAL   A CG2  1 
ATOM   2138 H  H    A VAL   A 1 100 ? 19.792 -2.192  -10.092 0.50 19.20 ?  100 VAL   A H    1 
ATOM   2139 H  H    B VAL   A 1 100 ? 20.172 -2.679  -10.599 0.50 17.35 ?  100 VAL   A H    1 
ATOM   2140 H  HA   A VAL   A 1 100 ? 20.206 -2.925  -12.559 0.50 21.17 ?  100 VAL   A HA   1 
ATOM   2141 H  HA   B VAL   A 1 100 ? 20.764 -3.517  -13.011 0.50 20.38 ?  100 VAL   A HA   1 
ATOM   2142 H  HB   A VAL   A 1 100 ? 17.738 -2.412  -11.278 0.50 22.43 ?  100 VAL   A HB   1 
ATOM   2143 H  HB   B VAL   A 1 100 ? 18.458 -3.565  -11.485 0.50 23.83 ?  100 VAL   A HB   1 
ATOM   2144 H  HG11 A VAL   A 1 100 ? 16.793 -3.705  -13.073 0.50 23.40 ?  100 VAL   A HG11 1 
ATOM   2145 H  HG11 B VAL   A 1 100 ? 17.116 -4.249  -13.328 0.50 25.08 ?  100 VAL   A HG11 1 
ATOM   2146 H  HG12 A VAL   A 1 100 ? 17.225 -2.229  -13.469 0.50 23.40 ?  100 VAL   A HG12 1 
ATOM   2147 H  HG12 B VAL   A 1 100 ? 17.436 -2.695  -13.324 0.50 25.08 ?  100 VAL   A HG12 1 
ATOM   2148 H  HG13 A VAL   A 1 100 ? 18.155 -3.461  -13.853 0.50 23.40 ?  100 VAL   A HG13 1 
ATOM   2149 H  HG13 B VAL   A 1 100 ? 18.236 -3.673  -14.292 0.50 25.08 ?  100 VAL   A HG13 1 
ATOM   2150 H  HG21 A VAL   A 1 100 ? 17.572 -4.741  -11.113 0.50 22.61 ?  100 VAL   A HG21 1 
ATOM   2151 H  HG21 B VAL   A 1 100 ? 18.445 -5.808  -12.087 0.50 25.02 ?  100 VAL   A HG21 1 
ATOM   2152 H  HG22 A VAL   A 1 100 ? 19.016 -4.878  -11.761 0.50 22.61 ?  100 VAL   A HG22 1 
ATOM   2153 H  HG22 B VAL   A 1 100 ? 19.635 -5.549  -13.107 0.50 25.02 ?  100 VAL   A HG22 1 
ATOM   2154 H  HG23 A VAL   A 1 100 ? 18.848 -4.206  -10.331 0.50 22.61 ?  100 VAL   A HG23 1 
ATOM   2155 H  HG23 B VAL   A 1 100 ? 19.883 -5.406  -11.544 0.50 25.02 ?  100 VAL   A HG23 1 
ATOM   2156 N  N    A ASN   A 1 101 ? 19.396 0.129   -12.230 0.50 19.93 ?  101 ASN   A N    1 
ATOM   2157 N  N    B ASN   A 1 101 ? 19.712 -0.549  -12.880 0.50 16.83 ?  101 ASN   A N    1 
ATOM   2158 C  CA   A ASN   A 1 101 ? 19.332 1.398   -12.945 0.50 21.13 ?  101 ASN   A CA   1 
ATOM   2159 C  CA   B ASN   A 1 101 ? 19.619 0.660   -13.695 0.50 17.23 ?  101 ASN   A CA   1 
ATOM   2160 C  C    A ASN   A 1 101 ? 20.685 1.836   -13.495 0.50 22.69 ?  101 ASN   A C    1 
ATOM   2161 C  C    B ASN   A 1 101 ? 20.928 0.977   -14.409 0.50 18.06 ?  101 ASN   A C    1 
ATOM   2162 O  O    A ASN   A 1 101 ? 20.748 2.847   -14.205 0.50 23.34 ?  101 ASN   A O    1 
ATOM   2163 O  O    B ASN   A 1 101 ? 20.912 1.711   -15.403 0.50 18.47 ?  101 ASN   A O    1 
ATOM   2164 C  CB   A ASN   A 1 101 ? 18.737 2.476   -12.037 0.50 20.28 ?  101 ASN   A CB   1 
ATOM   2165 C  CB   B ASN   A 1 101 ? 19.187 1.855   -12.838 0.50 17.24 ?  101 ASN   A CB   1 
ATOM   2166 C  CG   A ASN   A 1 101 ? 17.400 2.065   -11.449 0.50 19.71 ?  101 ASN   A CG   1 
ATOM   2167 C  CG   B ASN   A 1 101 ? 17.865 1.619   -12.126 0.50 18.28 ?  101 ASN   A CG   1 
ATOM   2168 O  OD1  A ASN   A 1 101 ? 16.534 1.541   -12.150 0.50 19.35 ?  101 ASN   A OD1  1 
ATOM   2169 O  OD1  B ASN   A 1 101 ? 16.925 1.055   -12.693 0.50 19.73 ?  101 ASN   A OD1  1 
ATOM   2170 N  ND2  A ASN   A 1 101 ? 17.233 2.285   -10.150 0.50 20.06 ?  101 ASN   A ND2  1 
ATOM   2171 N  ND2  B ASN   A 1 101 ? 17.794 2.039   -10.870 0.50 18.60 ?  101 ASN   A ND2  1 
ATOM   2172 H  H    A ASN   A 1 101 ? 19.298 0.192   -11.380 0.50 23.91 ?  101 ASN   A H    1 
ATOM   2173 H  H    B ASN   A 1 101 ? 19.637 -0.418  -12.034 0.50 20.19 ?  101 ASN   A H    1 
ATOM   2174 H  HA   A ASN   A 1 101 ? 18.734 1.293   -13.700 0.50 25.34 ?  101 ASN   A HA   1 
ATOM   2175 H  HA   B ASN   A 1 101 ? 18.947 0.528   -14.375 0.50 20.66 ?  101 ASN   A HA   1 
ATOM   2176 H  HB2  A ASN   A 1 101 ? 19.347 2.647   -11.305 0.50 24.33 ?  101 ASN   A HB2  1 
ATOM   2177 H  HB2  B ASN   A 1 101 ? 19.867 2.030   -12.166 0.50 20.68 ?  101 ASN   A HB2  1 
ATOM   2178 H  HB3  A ASN   A 1 101 ? 18.600 3.284   -12.555 0.50 24.33 ?  101 ASN   A HB3  1 
ATOM   2179 H  HB3  B ASN   A 1 101 ? 19.083 2.633   -13.409 0.50 20.68 ?  101 ASN   A HB3  1 
ATOM   2180 H  HD21 A ASN   A 1 101 ? 16.492 2.067   -9.769  0.50 24.07 ?  101 ASN   A HD21 1 
ATOM   2181 H  HD21 B ASN   A 1 101 ? 17.072 1.923   -10.422 0.50 22.30 ?  101 ASN   A HD21 1 
ATOM   2182 H  HD22 A ASN   A 1 101 ? 17.861 2.650   -9.691  0.50 24.07 ?  101 ASN   A HD22 1 
ATOM   2183 H  HD22 B ASN   A 1 101 ? 18.472 2.424   -10.505 0.50 22.30 ?  101 ASN   A HD22 1 
ATOM   2184 N  N    A LYS   A 1 102 ? 21.759 1.108   -13.187 0.50 23.89 ?  102 LYS   A N    1 
ATOM   2185 N  N    B LYS   A 1 102 ? 22.051 0.437   -13.929 0.50 18.93 ?  102 LYS   A N    1 
ATOM   2186 C  CA   A LYS   A 1 102 ? 23.051 1.297   -13.834 0.50 25.19 ?  102 LYS   A CA   1 
ATOM   2187 C  CA   B LYS   A 1 102 ? 23.361 0.625   -14.542 0.50 20.12 ?  102 LYS   A CA   1 
ATOM   2188 C  C    A LYS   A 1 102 ? 23.358 0.200   -14.843 0.50 25.51 ?  102 LYS   A C    1 
ATOM   2189 C  C    B LYS   A 1 102 ? 23.772 -0.548  -15.428 0.50 19.88 ?  102 LYS   A C    1 
ATOM   2190 O  O    A LYS   A 1 102 ? 24.433 0.219   -15.451 0.50 25.96 ?  102 LYS   A O    1 
ATOM   2191 O  O    B LYS   A 1 102 ? 24.922 -0.604  -15.873 0.50 20.95 ?  102 LYS   A O    1 
ATOM   2192 C  CB   A LYS   A 1 102 ? 24.172 1.352   -12.790 0.50 26.29 ?  102 LYS   A CB   1 
ATOM   2193 C  CB   B LYS   A 1 102 ? 24.429 0.838   -13.462 0.50 21.67 ?  102 LYS   A CB   1 
ATOM   2194 C  CG   A LYS   A 1 102 ? 24.077 2.519   -11.825 0.50 27.17 ?  102 LYS   A CG   1 
ATOM   2195 C  CG   B LYS   A 1 102 ? 24.423 2.209   -12.808 0.50 23.56 ?  102 LYS   A CG   1 
ATOM   2196 C  CD   A LYS   A 1 102 ? 25.218 2.486   -10.819 0.50 28.19 ?  102 LYS   A CD   1 
ATOM   2197 C  CD   B LYS   A 1 102 ? 25.493 2.300   -11.727 0.50 25.50 ?  102 LYS   A CD   1 
ATOM   2198 C  CE   A LYS   A 1 102 ? 25.167 3.676   -9.876  0.50 28.89 ?  102 LYS   A CE   1 
ATOM   2199 C  CE   B LYS   A 1 102 ? 25.824 3.743   -11.383 0.50 27.07 ?  102 LYS   A CE   1 
ATOM   2200 N  NZ   A LYS   A 1 102 ? 26.198 3.575   -8.805  0.50 29.32 ?  102 LYS   A NZ   1 
ATOM   2201 N  NZ   B LYS   A 1 102 ? 24.617 4.525   -11.006 0.50 28.12 ?  102 LYS   A NZ   1 
ATOM   2202 H  H    A LYS   A 1 102 ? 21.762 0.483   -12.595 0.50 28.66 ?  102 LYS   A H    1 
ATOM   2203 H  H    B LYS   A 1 102 ? 22.079 -0.061  -13.222 0.50 22.70 ?  102 LYS   A H    1 
ATOM   2204 H  HA   A LYS   A 1 102 ? 23.047 2.141   -14.308 0.50 30.22 ?  102 LYS   A HA   1 
ATOM   2205 H  HA   B LYS   A 1 102 ? 23.338 1.427   -15.085 0.50 24.13 ?  102 LYS   A HA   1 
ATOM   2206 H  HB2  A LYS   A 1 102 ? 24.150 0.536   -12.266 0.50 31.53 ?  102 LYS   A HB2  1 
ATOM   2207 H  HB2  B LYS   A 1 102 ? 24.300 0.183   -12.759 0.50 25.99 ?  102 LYS   A HB2  1 
ATOM   2208 H  HB3  A LYS   A 1 102 ? 25.023 1.420   -13.251 0.50 31.53 ?  102 LYS   A HB3  1 
ATOM   2209 H  HB3  B LYS   A 1 102 ? 25.307 0.715   -13.860 0.50 25.99 ?  102 LYS   A HB3  1 
ATOM   2210 H  HG2  A LYS   A 1 102 ? 24.130 3.351   -12.322 0.50 32.60 ?  102 LYS   A HG2  1 
ATOM   2211 H  HG2  B LYS   A 1 102 ? 24.609 2.889   -13.475 0.50 28.26 ?  102 LYS   A HG2  1 
ATOM   2212 H  HG3  A LYS   A 1 102 ? 23.239 2.468   -11.340 0.50 32.60 ?  102 LYS   A HG3  1 
ATOM   2213 H  HG3  B LYS   A 1 102 ? 23.560 2.369   -12.395 0.50 28.26 ?  102 LYS   A HG3  1 
ATOM   2214 H  HD2  A LYS   A 1 102 ? 25.155 1.676   -10.290 0.50 33.82 ?  102 LYS   A HD2  1 
ATOM   2215 H  HD2  B LYS   A 1 102 ? 25.174 1.863   -10.921 0.50 30.59 ?  102 LYS   A HD2  1 
ATOM   2216 H  HD3  A LYS   A 1 102 ? 26.064 2.511   -11.295 0.50 33.82 ?  102 LYS   A HD3  1 
ATOM   2217 H  HD3  B LYS   A 1 102 ? 26.305 1.870   -12.041 0.50 30.59 ?  102 LYS   A HD3  1 
ATOM   2218 H  HE2  A LYS   A 1 102 ? 25.331 4.490   -10.380 0.50 34.66 ?  102 LYS   A HE2  1 
ATOM   2219 H  HE2  B LYS   A 1 102 ? 26.440 3.759   -10.633 0.50 32.48 ?  102 LYS   A HE2  1 
ATOM   2220 H  HE3  A LYS   A 1 102 ? 24.294 3.713   -9.456  0.50 34.66 ?  102 LYS   A HE3  1 
ATOM   2221 H  HE3  B LYS   A 1 102 ? 26.230 4.168   -12.155 0.50 32.48 ?  102 LYS   A HE3  1 
ATOM   2222 H  HZ1  A LYS   A 1 102 ? 26.148 4.282   -8.267  0.50 35.17 ?  102 LYS   A HZ1  1 
ATOM   2223 H  HZ1  B LYS   A 1 102 ? 24.851 5.348   -10.763 0.50 33.73 ?  102 LYS   A HZ1  1 
ATOM   2224 H  HZ2  A LYS   A 1 102 ? 26.066 2.837   -8.326  0.50 35.17 ?  102 LYS   A HZ2  1 
ATOM   2225 H  HZ2  B LYS   A 1 102 ? 24.059 4.574   -11.697 0.50 33.73 ?  102 LYS   A HZ2  1 
ATOM   2226 H  HZ3  A LYS   A 1 102 ? 27.011 3.544   -9.167  0.50 35.17 ?  102 LYS   A HZ3  1 
ATOM   2227 H  HZ3  B LYS   A 1 102 ? 24.201 4.130   -10.326 0.50 33.73 ?  102 LYS   A HZ3  1 
ATOM   2228 N  N    A GLY   A 1 103 ? 22.446 -0.752  -15.032 0.50 25.65 ?  103 GLY   A N    1 
ATOM   2229 N  N    B GLY   A 1 103 ? 22.870 -1.490  -15.686 0.50 19.04 ?  103 GLY   A N    1 
ATOM   2230 C  CA   A GLY   A 1 103 ? 22.668 -1.845  -15.955 0.50 25.68 ?  103 GLY   A CA   1 
ATOM   2231 C  CA   B GLY   A 1 103 ? 23.214 -2.651  -16.484 0.50 18.92 ?  103 GLY   A CA   1 
ATOM   2232 C  C    A GLY   A 1 103 ? 23.519 -2.968  -15.412 0.50 25.69 ?  103 GLY   A C    1 
ATOM   2233 C  C    B GLY   A 1 103 ? 24.009 -3.714  -15.758 0.50 18.10 ?  103 GLY   A C    1 
ATOM   2234 O  O    A GLY   A 1 103 ? 24.063 -3.752  -16.197 0.50 26.43 ?  103 GLY   A O    1 
ATOM   2235 O  O    B GLY   A 1 103 ? 24.563 -4.610  -16.404 0.50 18.80 ?  103 GLY   A O    1 
ATOM   2236 H  H    A GLY   A 1 103 ? 21.686 -0.783  -14.634 0.50 30.76 ?  103 GLY   A H    1 
ATOM   2237 H  H    B GLY   A 1 103 ? 22.056 -1.463  -15.417 0.50 22.84 ?  103 GLY   A H    1 
ATOM   2238 H  HA2  A GLY   A 1 103 ? 21.807 -2.205  -16.232 0.50 30.80 ?  103 GLY   A HA2  1 
ATOM   2239 H  HA2  B GLY   A 1 103 ? 22.395 -3.060  -16.795 0.50 22.69 ?  103 GLY   A HA2  1 
ATOM   2240 H  HA3  A GLY   A 1 103 ? 23.115 -1.504  -16.743 0.50 30.80 ?  103 GLY   A HA3  1 
ATOM   2241 H  HA3  B GLY   A 1 103 ? 23.713 -2.348  -17.265 0.50 22.69 ?  103 GLY   A HA3  1 
ATOM   2242 N  N    A GLU   A 1 104 ? 23.661 -3.070  -14.095 0.50 24.69 ?  104 GLU   A N    1 
ATOM   2243 N  N    B GLU   A 1 104 ? 24.065 -3.662  -14.432 0.50 16.23 ?  104 GLU   A N    1 
ATOM   2244 C  CA   A GLU   A 1 104 ? 24.533 -4.072  -13.502 0.50 23.73 ?  104 GLU   A CA   1 
ATOM   2245 C  CA   B GLU   A 1 104 ? 24.899 -4.585  -13.678 0.50 14.26 ?  104 GLU   A CA   1 
ATOM   2246 C  C    A GLU   A 1 104 ? 23.841 -5.429  -13.406 0.50 23.58 ?  104 GLU   A C    1 
ATOM   2247 C  C    B GLU   A 1 104 ? 24.188 -5.922  -13.493 0.50 14.48 ?  104 GLU   A C    1 
ATOM   2248 O  O    A GLU   A 1 104 ? 22.619 -5.526  -13.253 0.50 23.54 ?  104 GLU   A O    1 
ATOM   2249 O  O    B GLU   A 1 104 ? 22.961 -5.990  -13.362 0.50 15.36 ?  104 GLU   A O    1 
ATOM   2250 C  CB   A GLU   A 1 104 ? 25.032 -3.592  -12.136 0.50 22.97 ?  104 GLU   A CB   1 
ATOM   2251 C  CB   B GLU   A 1 104 ? 25.304 -3.964  -12.338 0.50 13.04 ?  104 GLU   A CB   1 
ATOM   2252 C  CG   A GLU   A 1 104 ? 25.995 -2.410  -12.275 0.50 22.69 ?  104 GLU   A CG   1 
ATOM   2253 C  CG   B GLU   A 1 104 ? 26.162 -2.711  -12.534 0.50 13.16 ?  104 GLU   A CG   1 
ATOM   2254 C  CD   A GLU   A 1 104 ? 26.303 -1.683  -10.974 0.50 22.39 ?  104 GLU   A CD   1 
ATOM   2255 C  CD   B GLU   A 1 104 ? 26.489 -1.929  -11.262 0.50 12.87 ?  104 GLU   A CD   1 
ATOM   2256 O  OE1  A GLU   A 1 104 ? 25.707 -2.012  -9.929  0.50 21.57 ?  104 GLU   A OE1  1 
ATOM   2257 O  OE1  B GLU   A 1 104 ? 25.966 -2.244  -10.172 0.50 12.87 ?  104 GLU   A OE1  1 
ATOM   2258 O  OE2  A GLU   A 1 104 ? 27.142 -0.756  -11.006 0.50 23.18 -1 104 GLU   A OE2  1 
ATOM   2259 O  OE2  B GLU   A 1 104 ? 27.282 -0.967  -11.372 0.50 13.51 -1 104 GLU   A OE2  1 
ATOM   2260 H  H    A GLU   A 1 104 ? 23.272 -2.558  -13.525 0.50 29.62 ?  104 GLU   A H    1 
ATOM   2261 H  H    B GLU   A 1 104 ? 23.617 -3.108  -13.953 0.50 19.46 ?  104 GLU   A H    1 
ATOM   2262 H  HA   A GLU   A 1 104 ? 25.305 -4.180  -14.074 0.50 28.46 ?  104 GLU   A HA   1 
ATOM   2263 H  HA   B GLU   A 1 104 ? 25.711 -4.748  -14.186 0.50 17.10 ?  104 GLU   A HA   1 
ATOM   2264 H  HB2  A GLU   A 1 104 ? 24.274 -3.309  -11.601 0.50 27.55 ?  104 GLU   A HB2  1 
ATOM   2265 H  HB2  B GLU   A 1 104 ? 24.508 -3.718  -11.851 0.50 15.63 ?  104 GLU   A HB2  1 
ATOM   2266 H  HB3  A GLU   A 1 104 ? 25.499 -4.321  -11.696 0.50 27.55 ?  104 GLU   A HB3  1 
ATOM   2267 H  HB3  B GLU   A 1 104 ? 25.824 -4.614  -11.839 0.50 15.63 ?  104 GLU   A HB3  1 
ATOM   2268 H  HG2  A GLU   A 1 104 ? 26.826 -2.737  -12.658 0.50 27.22 ?  104 GLU   A HG2  1 
ATOM   2269 H  HG2  B GLU   A 1 104 ? 27.000 -2.977  -12.946 0.50 15.78 ?  104 GLU   A HG2  1 
ATOM   2270 H  HG3  A GLU   A 1 104 ? 25.597 -1.757  -12.868 0.50 27.22 ?  104 GLU   A HG3  1 
ATOM   2271 H  HG3  B GLU   A 1 104 ? 25.686 -2.108  -13.130 0.50 15.78 ?  104 GLU   A HG3  1 
ATOM   2272 N  N    A ASP   A 1 105 ? 24.650 -6.484  -13.501 0.50 23.69 ?  105 ASP   A N    1 
ATOM   2273 N  N    B ASP   A 1 105 ? 24.987 -6.989  -13.499 0.50 14.56 ?  105 ASP   A N    1 
ATOM   2274 C  CA   A ASP   A 1 105 ? 24.149 -7.847  -13.632 0.50 24.16 ?  105 ASP   A CA   1 
ATOM   2275 C  CA   B ASP   A 1 105 ? 24.490 -8.359  -13.559 0.50 15.66 ?  105 ASP   A CA   1 
ATOM   2276 C  C    A ASP   A 1 105 ? 23.486 -8.294  -12.333 0.50 22.68 ?  105 ASP   A C    1 
ATOM   2277 C  C    B ASP   A 1 105 ? 23.725 -8.722  -12.288 0.50 14.24 ?  105 ASP   A C    1 
ATOM   2278 O  O    A ASP   A 1 105 ? 24.132 -8.343  -11.282 0.50 21.96 ?  105 ASP   A O    1 
ATOM   2279 O  O    B ASP   A 1 105 ? 24.296 -8.738  -11.196 0.50 12.78 ?  105 ASP   A O    1 
ATOM   2280 C  CB   A ASP   A 1 105 ? 25.315 -8.769  -13.982 0.50 26.16 ?  105 ASP   A CB   1 
ATOM   2281 C  CB   B ASP   A 1 105 ? 25.695 -9.281  -13.736 0.50 17.74 ?  105 ASP   A CB   1 
ATOM   2282 C  CG   A ASP   A 1 105 ? 24.875 -10.196 -14.223 0.50 27.94 ?  105 ASP   A CG   1 
ATOM   2283 C  CG   B ASP   A 1 105 ? 25.308 -10.725 -13.941 0.50 19.60 ?  105 ASP   A CG   1 
ATOM   2284 O  OD1  A ASP   A 1 105 ? 23.653 -10.430 -14.323 0.50 28.39 ?  105 ASP   A OD1  1 
ATOM   2285 O  OD1  B ASP   A 1 105 ? 24.099 -11.034 -13.966 0.50 19.59 ?  105 ASP   A OD1  1 
ATOM   2286 O  OD2  A ASP   A 1 105 ? 25.752 -11.081 -14.314 0.50 28.88 -1 105 ASP   A OD2  1 
ATOM   2287 O  OD2  B ASP   A 1 105 ? 26.230 -11.557 -14.077 0.50 21.03 -1 105 ASP   A OD2  1 
ATOM   2288 H  H    A ASP   A 1 105 ? 25.506 -6.434  -13.484 0.50 28.41 ?  105 ASP   A H    1 
ATOM   2289 H  H    B ASP   A 1 105 ? 25.847 -6.944  -13.470 0.50 17.46 ?  105 ASP   A H    1 
ATOM   2290 H  HA   A ASP   A 1 105 ? 23.496 -7.897  -14.347 0.50 28.98 ?  105 ASP   A HA   1 
ATOM   2291 H  HA   B ASP   A 1 105 ? 23.902 -8.472  -14.320 0.50 18.78 ?  105 ASP   A HA   1 
ATOM   2292 H  HB2  A ASP   A 1 105 ? 25.742 -8.449  -14.795 0.50 31.38 ?  105 ASP   A HB2  1 
ATOM   2293 H  HB2  B ASP   A 1 105 ? 26.213 -8.983  -14.507 0.50 21.27 ?  105 ASP   A HB2  1 
ATOM   2294 H  HB3  A ASP   A 1 105 ? 25.957 -8.763  -13.252 0.50 31.38 ?  105 ASP   A HB3  1 
ATOM   2295 H  HB3  B ASP   A 1 105 ? 26.249 -9.244  -12.940 0.50 21.27 ?  105 ASP   A HB3  1 
ATOM   2296 N  N    A ILE   A 1 106 ? 22.196 -8.630  -12.408 0.50 21.94 ?  106 ILE   A N    1 
ATOM   2297 N  N    B ILE   A 1 106 ? 22.439 -9.048  -12.434 0.50 14.99 ?  106 ILE   A N    1 
ATOM   2298 C  CA   A ILE   A 1 106 ? 21.451 -9.038  -11.223 0.50 20.96 ?  106 ILE   A CA   1 
ATOM   2299 C  CA   B ILE   A 1 106 ? 21.621 -9.427  -11.283 0.50 15.47 ?  106 ILE   A CA   1 
ATOM   2300 C  C    A ILE   A 1 106 ? 21.993 -10.327 -10.624 0.50 20.38 ?  106 ILE   A C    1 
ATOM   2301 C  C    B ILE   A 1 106 ? 22.193 -10.647 -10.577 0.50 15.09 ?  106 ILE   A C    1 
ATOM   2302 O  O    A ILE   A 1 106 ? 21.774 -10.595 -9.438  0.50 19.89 ?  106 ILE   A O    1 
ATOM   2303 O  O    B ILE   A 1 106 ? 21.961 -10.838 -9.376  0.50 14.97 ?  106 ILE   A O    1 
ATOM   2304 C  CB   A ILE   A 1 106 ? 19.942 -9.133  -11.547 0.50 21.13 ?  106 ILE   A CB   1 
ATOM   2305 C  CB   B ILE   A 1 106 ? 20.164 -9.655  -11.727 0.50 17.37 ?  106 ILE   A CB   1 
ATOM   2306 C  CG1  A ILE   A 1 106 ? 19.113 -9.199  -10.264 0.50 21.07 ?  106 ILE   A CG1  1 
ATOM   2307 C  CG1  B ILE   A 1 106 ? 19.232 -9.782  -10.519 0.50 18.45 ?  106 ILE   A CG1  1 
ATOM   2308 C  CG2  A ILE   A 1 106 ? 19.649 -10.348 -12.417 0.50 21.29 ?  106 ILE   A CG2  1 
ATOM   2309 C  CG2  B ILE   A 1 106 ? 20.060 -10.911 -12.567 0.50 17.87 ?  106 ILE   A CG2  1 
ATOM   2310 C  CD1  A ILE   A 1 106 ? 19.317 -8.015  -9.346  0.50 20.99 ?  106 ILE   A CD1  1 
ATOM   2311 C  CD1  B ILE   A 1 106 ? 19.052 -8.504  -9.747  0.50 18.95 ?  106 ILE   A CD1  1 
ATOM   2312 H  H    A ILE   A 1 106 ? 21.734 -8.617  -13.130 0.50 26.32 ?  106 ILE   A H    1 
ATOM   2313 H  H    B ILE   A 1 106 ? 22.028 -9.060  -13.181 0.50 17.98 ?  106 ILE   A H    1 
ATOM   2314 H  HA   A ILE   A 1 106 ? 21.565 -8.351  -10.555 0.50 25.14 ?  106 ILE   A HA   1 
ATOM   2315 H  HA   B ILE   A 1 106 ? 21.632 -8.708  -10.644 0.50 18.55 ?  106 ILE   A HA   1 
ATOM   2316 H  HB   A ILE   A 1 106 ? 19.682 -8.339  -12.039 0.50 25.35 ?  106 ILE   A HB   1 
ATOM   2317 H  HB   B ILE   A 1 106 ? 19.884 -8.899  -12.262 0.50 20.83 ?  106 ILE   A HB   1 
ATOM   2318 H  HG12 A ILE   A 1 106 ? 18.171 -9.228  -10.500 0.50 25.28 ?  106 ILE   A HG12 1 
ATOM   2319 H  HG12 B ILE   A 1 106 ? 18.359 -10.068 -10.835 0.50 22.13 ?  106 ILE   A HG12 1 
ATOM   2320 H  HG13 A ILE   A 1 106 ? 19.352 -9.999  -9.774  0.50 25.28 ?  106 ILE   A HG13 1 
ATOM   2321 H  HG13 B ILE   A 1 106 ? 19.590 -10.452 -9.914  0.50 22.13 ?  106 ILE   A HG13 1 
ATOM   2322 H  HG21 A ILE   A 1 106 ? 18.749 -10.271 -12.771 0.50 25.54 ?  106 ILE   A HG21 1 
ATOM   2323 H  HG21 B ILE   A 1 106 ? 19.187 -10.933 -12.983 0.50 21.44 ?  106 ILE   A HG21 1 
ATOM   2324 H  HG22 A ILE   A 1 106 ? 20.290 -10.373 -13.143 0.50 25.54 ?  106 ILE   A HG22 1 
ATOM   2325 H  HG22 B ILE   A 1 106 ? 20.754 -10.893 -13.245 0.50 21.44 ?  106 ILE   A HG22 1 
ATOM   2326 H  HG23 A ILE   A 1 106 ? 19.726 -11.149 -11.877 0.50 25.54 ?  106 ILE   A HG23 1 
ATOM   2327 H  HG23 B ILE   A 1 106 ? 20.175 -11.686 -11.995 0.50 21.44 ?  106 ILE   A HG23 1 
ATOM   2328 H  HD11 A ILE   A 1 106 ? 18.570 -7.961  -8.732  0.50 25.17 ?  106 ILE   A HD11 1 
ATOM   2329 H  HD11 B ILE   A 1 106 ? 18.344 -8.633  -9.097  0.50 22.73 ?  106 ILE   A HD11 1 
ATOM   2330 H  HD12 A ILE   A 1 106 ? 20.144 -8.136  -8.854  0.50 25.17 ?  106 ILE   A HD12 1 
ATOM   2331 H  HD12 B ILE   A 1 106 ? 19.881 -8.288  -9.299  0.50 22.73 ?  106 ILE   A HD12 1 
ATOM   2332 H  HD13 A ILE   A 1 106 ? 19.364 -7.207  -9.882  0.50 25.17 ?  106 ILE   A HD13 1 
ATOM   2333 H  HD13 B ILE   A 1 106 ? 18.810 -7.799  -10.367 0.50 22.73 ?  106 ILE   A HD13 1 
ATOM   2334 N  N    A GLN   A 1 107 ? 22.713 -11.130 -11.413 0.50 21.07 ?  107 GLN   A N    1 
ATOM   2335 N  N    B GLN   A 1 107 ? 22.939 -11.493 -11.299 0.50 15.67 ?  107 GLN   A N    1 
ATOM   2336 C  CA   A GLN   A 1 107 ? 23.306 -12.358 -10.894 0.50 22.37 ?  107 GLN   A CA   1 
ATOM   2337 C  CA   B GLN   A 1 107 ? 23.581 -12.645 -10.667 0.50 17.44 ?  107 GLN   A CA   1 
ATOM   2338 C  C    A GLN   A 1 107 ? 24.292 -12.084 -9.764  0.50 20.44 ?  107 GLN   A C    1 
ATOM   2339 C  C    B GLN   A 1 107 ? 24.512 -12.220 -9.540  0.50 15.62 ?  107 GLN   A C    1 
ATOM   2340 O  O    A GLN   A 1 107 ? 24.529 -12.966 -8.932  0.50 21.63 ?  107 GLN   A O    1 
ATOM   2341 O  O    B GLN   A 1 107 ? 24.765 -12.996 -8.608  0.50 16.09 ?  107 GLN   A O    1 
ATOM   2342 C  CB   A GLN   A 1 107 ? 23.991 -13.127 -12.033 0.50 26.00 ?  107 GLN   A CB   1 
ATOM   2343 C  CB   B GLN   A 1 107 ? 24.346 -13.463 -11.717 0.50 21.53 ?  107 GLN   A CB   1 
ATOM   2344 C  CG   A GLN   A 1 107 ? 23.108 -13.344 -13.260 0.50 29.74 ?  107 GLN   A CG   1 
ATOM   2345 C  CG   B GLN   A 1 107 ? 23.455 -14.068 -12.789 0.50 25.83 ?  107 GLN   A CG   1 
ATOM   2346 C  CD   A GLN   A 1 107 ? 21.832 -14.094 -12.939 0.50 32.80 ?  107 GLN   A CD   1 
ATOM   2347 C  CD   B GLN   A 1 107 ? 22.433 -15.026 -12.212 0.50 29.40 ?  107 GLN   A CD   1 
ATOM   2348 O  OE1  A GLN   A 1 107 ? 21.855 -15.127 -12.268 0.50 33.99 ?  107 GLN   A OE1  1 
ATOM   2349 O  OE1  B GLN   A 1 107 ? 22.726 -15.781 -11.284 0.50 30.74 ?  107 GLN   A OE1  1 
ATOM   2350 N  NE2  A GLN   A 1 107 ? 20.706 -13.575 -13.415 0.50 33.88 ?  107 GLN   A NE2  1 
ATOM   2351 N  NE2  B GLN   A 1 107 ? 21.221 -14.993 -12.752 0.50 30.73 ?  107 GLN   A NE2  1 
ATOM   2352 H  H    A GLN   A 1 107 ? 22.878 -10.979 -12.242 0.50 25.27 ?  107 GLN   A H    1 
ATOM   2353 H  H    B GLN   A 1 107 ? 23.088 -11.431 -12.148 0.50 18.79 ?  107 GLN   A H    1 
ATOM   2354 H  HA   A GLN   A 1 107 ? 22.605 -12.925 -10.542 0.50 26.83 ?  107 GLN   A HA   1 
ATOM   2355 H  HA   B GLN   A 1 107 ? 22.907 -13.220 -10.287 0.50 20.92 ?  107 GLN   A HA   1 
ATOM   2356 H  HB2  A GLN   A 1 107 ? 24.774 -12.633 -12.322 0.50 31.19 ?  107 GLN   A HB2  1 
ATOM   2357 H  HB2  B GLN   A 1 107 ? 24.993 -12.891 -12.163 0.50 25.83 ?  107 GLN   A HB2  1 
ATOM   2358 H  HB3  A GLN   A 1 107 ? 24.256 -14.002 -11.710 0.50 31.19 ?  107 GLN   A HB3  1 
ATOM   2359 H  HB3  B GLN   A 1 107 ? 24.811 -14.196 -11.277 0.50 25.83 ?  107 GLN   A HB3  1 
ATOM   2360 H  HG2  A GLN   A 1 107 ? 22.859 -12.484 -13.634 0.50 35.68 ?  107 GLN   A HG2  1 
ATOM   2361 H  HG2  B GLN   A 1 107 ? 22.979 -13.355 -13.242 0.50 30.98 ?  107 GLN   A HG2  1 
ATOM   2362 H  HG3  A GLN   A 1 107 ? 23.603 -13.857 -13.920 0.50 35.68 ?  107 GLN   A HG3  1 
ATOM   2363 H  HG3  B GLN   A 1 107 ? 24.003 -14.558 -13.423 0.50 30.98 ?  107 GLN   A HG3  1 
ATOM   2364 H  HE21 A GLN   A 1 107 ? 20.727 -12.850 -13.879 0.50 40.64 ?  107 GLN   A HE21 1 
ATOM   2365 H  HE21 B GLN   A 1 107 ? 21.053 -14.451 -13.397 0.50 36.86 ?  107 GLN   A HE21 1 
ATOM   2366 H  HE22 A GLN   A 1 107 ? 19.955 -13.965 -13.261 0.50 40.64 ?  107 GLN   A HE22 1 
ATOM   2367 H  HE22 B GLN   A 1 107 ? 20.607 -15.517 -12.457 0.50 36.86 ?  107 GLN   A HE22 1 
ATOM   2368 N  N    A LEU   A 1 108 ? 24.855 -10.873 -9.699  0.50 17.57 ?  108 LEU   A N    1 
ATOM   2369 N  N    B LEU   A 1 108 ? 25.029 -10.992 -9.602  0.50 14.26 ?  108 LEU   A N    1 
ATOM   2370 C  CA   A LEU   A 1 108 ? 25.804 -10.517 -8.649  0.50 15.51 ?  108 LEU   A CA   1 
ATOM   2371 C  CA   B LEU   A 1 108 ? 25.891 -10.487 -8.545  0.50 13.50 ?  108 LEU   A CA   1 
ATOM   2372 C  C    A LEU   A 1 108 ? 25.134 -10.325 -7.293  0.50 13.47 ?  108 LEU   A C    1 
ATOM   2373 C  C    B LEU   A 1 108 ? 25.137 -10.259 -7.242  0.50 12.46 ?  108 LEU   A C    1 
ATOM   2374 O  O    A LEU   A 1 108 ? 25.835 -10.197 -6.285  0.50 13.56 ?  108 LEU   A O    1 
ATOM   2375 O  O    B LEU   A 1 108 ? 25.781 -10.042 -6.210  0.50 12.99 ?  108 LEU   A O    1 
ATOM   2376 C  CB   A LEU   A 1 108 ? 26.572 -9.254  -9.051  0.50 15.46 ?  108 LEU   A CB   1 
ATOM   2377 C  CB   B LEU   A 1 108 ? 26.598 -9.206  -8.998  0.50 13.94 ?  108 LEU   A CB   1 
ATOM   2378 C  CG   A LEU   A 1 108 ? 27.534 -9.426  -10.230 0.50 16.33 ?  108 LEU   A CG   1 
ATOM   2379 C  CG   B LEU   A 1 108 ? 27.619 -9.400  -10.122 0.50 15.40 ?  108 LEU   A CG   1 
ATOM   2380 C  CD1  A LEU   A 1 108 ? 27.982 -8.081  -10.778 0.50 16.84 ?  108 LEU   A CD1  1 
ATOM   2381 C  CD1  B LEU   A 1 108 ? 28.056 -8.067  -10.707 0.50 16.06 ?  108 LEU   A CD1  1 
ATOM   2382 C  CD2  A LEU   A 1 108 ? 28.741 -10.250 -9.813  0.50 17.29 ?  108 LEU   A CD2  1 
ATOM   2383 C  CD2  B LEU   A 1 108 ? 28.828 -10.170 -9.617  0.50 16.58 ?  108 LEU   A CD2  1 
ATOM   2384 H  H    A LEU   A 1 108 ? 24.697 -10.244 -10.257 0.50 21.07 ?  108 LEU   A H    1 
ATOM   2385 H  H    B LEU   A 1 108 ? 24.897 -10.438 -10.246 0.50 17.11 ?  108 LEU   A H    1 
ATOM   2386 H  HA   A LEU   A 1 108 ? 26.448 -11.236 -8.557  0.50 18.60 ?  108 LEU   A HA   1 
ATOM   2387 H  HA   B LEU   A 1 108 ? 26.577 -11.148 -8.367  0.50 16.18 ?  108 LEU   A HA   1 
ATOM   2388 H  HB2  A LEU   A 1 108 ? 25.932 -8.569  -9.298  0.50 18.54 ?  108 LEU   A HB2  1 
ATOM   2389 H  HB2  B LEU   A 1 108 ? 25.932 -8.578  -9.315  0.50 16.72 ?  108 LEU   A HB2  1 
ATOM   2390 H  HB3  A LEU   A 1 108 ? 27.094 -8.957  -8.292  0.50 18.54 ?  108 LEU   A HB3  1 
ATOM   2391 H  HB3  B LEU   A 1 108 ? 27.069 -8.828  -8.240  0.50 16.72 ?  108 LEU   A HB3  1 
ATOM   2392 H  HG   A LEU   A 1 108 ? 27.080 -9.901  -10.943 0.50 19.59 ?  108 LEU   A HG   1 
ATOM   2393 H  HG   B LEU   A 1 108 ? 27.211 -9.916  -10.835 0.50 18.47 ?  108 LEU   A HG   1 
ATOM   2394 H  HD11 A LEU   A 1 108 ? 28.586 -8.228  -11.524 0.50 20.20 ?  108 LEU   A HD11 1 
ATOM   2395 H  HD11 B LEU   A 1 108 ? 28.675 -8.229  -11.437 0.50 19.26 ?  108 LEU   A HD11 1 
ATOM   2396 H  HD12 A LEU   A 1 108 ? 27.204 -7.585  -11.077 0.50 20.20 ?  108 LEU   A HD12 1 
ATOM   2397 H  HD12 B LEU   A 1 108 ? 27.276 -7.594  -11.036 0.50 19.26 ?  108 LEU   A HD12 1 
ATOM   2398 H  HD13 A LEU   A 1 108 ? 28.438 -7.589  -10.077 0.50 20.20 ?  108 LEU   A HD13 1 
ATOM   2399 H  HD13 B LEU   A 1 108 ? 28.492 -7.545  -10.015 0.50 19.26 ?  108 LEU   A HD13 1 
ATOM   2400 H  HD21 A LEU   A 1 108 ? 29.378 -10.268 -10.544 0.50 20.74 ?  108 LEU   A HD21 1 
ATOM   2401 H  HD21 B LEU   A 1 108 ? 29.514 -10.165 -10.303 0.50 19.88 ?  108 LEU   A HD21 1 
ATOM   2402 H  HD22 A LEU   A 1 108 ? 29.146 -9.841  -9.032  0.50 20.74 ?  108 LEU   A HD22 1 
ATOM   2403 H  HD22 B LEU   A 1 108 ? 29.159 -9.743  -8.813  0.50 19.88 ?  108 LEU   A HD22 1 
ATOM   2404 H  HD23 A LEU   A 1 108 ? 28.452 -11.150 -9.603  0.50 20.74 ?  108 LEU   A HD23 1 
ATOM   2405 H  HD23 B LEU   A 1 108 ? 28.561 -11.082 -9.423  0.50 19.88 ?  108 LEU   A HD23 1 
ATOM   2406 N  N    . LEU   A 1 109 ? 23.801 -10.324 -7.248  1.00 12.77 ?  109 LEU   A N    1 
ATOM   2407 C  CA   . LEU   A 1 109 ? 23.086 -10.197 -5.986  1.00 12.27 ?  109 LEU   A CA   1 
ATOM   2408 C  C    . LEU   A 1 109 ? 23.412 -11.359 -5.054  1.00 11.38 ?  109 LEU   A C    1 
ATOM   2409 O  O    . LEU   A 1 109 ? 23.528 -11.181 -3.838  1.00 11.55 ?  109 LEU   A O    1 
ATOM   2410 C  CB   . LEU   A 1 109 ? 21.586 -10.115 -6.259  1.00 13.02 ?  109 LEU   A CB   1 
ATOM   2411 C  CG   . LEU   A 1 109 ? 20.687 -9.837  -5.060  1.00 13.18 ?  109 LEU   A CG   1 
ATOM   2412 C  CD1  . LEU   A 1 109 ? 21.133 -8.604  -4.300  1.00 13.26 ?  109 LEU   A CD1  1 
ATOM   2413 C  CD2  . LEU   A 1 109 ? 19.245 -9.675  -5.525  1.00 14.32 ?  109 LEU   A CD2  1 
ATOM   2414 H  H    A LEU   A 1 109 ? 23.291 -10.403 -7.937  0.50 15.31 ?  109 LEU   A H    1 
ATOM   2415 H  H    B LEU   A 1 109 ? 23.309 -10.441 -7.944  0.50 15.31 ?  109 LEU   A H    1 
ATOM   2416 H  HA   . LEU   A 1 109 ? 23.365 -9.376  -5.555  1.00 14.72 ?  109 LEU   A HA   1 
ATOM   2417 H  HB2  . LEU   A 1 109 ? 21.431 -9.404  -6.899  1.00 15.62 ?  109 LEU   A HB2  1 
ATOM   2418 H  HB3  . LEU   A 1 109 ? 21.297 -10.958 -6.637  1.00 15.62 ?  109 LEU   A HB3  1 
ATOM   2419 H  HG   . LEU   A 1 109 ? 20.717 -10.588 -4.450  1.00 15.81 ?  109 LEU   A HG   1 
ATOM   2420 H  HD11 . LEU   A 1 109 ? 20.446 -8.348  -3.667  1.00 15.90 ?  109 LEU   A HD11 1 
ATOM   2421 H  HD12 . LEU   A 1 109 ? 21.959 -8.803  -3.831  1.00 15.90 ?  109 LEU   A HD12 1 
ATOM   2422 H  HD13 . LEU   A 1 109 ? 21.282 -7.880  -4.933  1.00 15.90 ?  109 LEU   A HD13 1 
ATOM   2423 H  HD21 . LEU   A 1 109 ? 18.689 -9.418  -4.767  1.00 17.18 ?  109 LEU   A HD21 1 
ATOM   2424 H  HD22 . LEU   A 1 109 ? 19.203 -8.984  -6.206  1.00 17.18 ?  109 LEU   A HD22 1 
ATOM   2425 H  HD23 . LEU   A 1 109 ? 18.930 -10.517 -5.890  1.00 17.18 ?  109 LEU   A HD23 1 
ATOM   2426 N  N    . LYS   A 1 110 ? 23.550 -12.570 -5.599  1.00 11.58 ?  110 LYS   A N    1 
ATOM   2427 C  CA   . LYS   A 1 110 ? 23.927 -13.695 -4.752  1.00 11.85 ?  110 LYS   A CA   1 
ATOM   2428 C  C    . LYS   A 1 110 ? 25.300 -13.462 -4.134  1.00 11.27 ?  110 LYS   A C    1 
ATOM   2429 O  O    . LYS   A 1 110 ? 25.494 -13.680 -2.935  1.00 11.33 ?  110 LYS   A O    1 
ATOM   2430 C  CB   . LYS   A 1 110 ? 23.884 -15.010 -5.536  1.00 12.78 ?  110 LYS   A CB   1 
ATOM   2431 C  CG   . LYS   A 1 110 ? 24.044 -16.229 -4.637  1.00 12.74 ?  110 LYS   A CG   1 
ATOM   2432 C  CD   . LYS   A 1 110 ? 23.795 -17.540 -5.364  1.00 13.42 ?  110 LYS   A CD   1 
ATOM   2433 C  CE   . LYS   A 1 110 ? 23.903 -18.728 -4.425  1.00 14.20 ?  110 LYS   A CE   1 
ATOM   2434 N  NZ   . LYS   A 1 110 ? 22.729 -18.869 -3.531  1.00 14.72 ?  110 LYS   A NZ   1 
ATOM   2435 H  H    . LYS   A 1 110 ? 23.437 -12.760 -6.428  1.00 13.88 ?  110 LYS   A H    1 
ATOM   2436 H  HA   . LYS   A 1 110 ? 23.281 -13.766 -4.028  1.00 14.21 ?  110 LYS   A HA   1 
ATOM   2437 H  HB2  . LYS   A 1 110 ? 23.031 -15.082 -5.990  1.00 15.33 ?  110 LYS   A HB2  1 
ATOM   2438 H  HB3  . LYS   A 1 110 ? 24.609 -15.017 -6.178  1.00 15.33 ?  110 LYS   A HB3  1 
ATOM   2439 H  HG2  . LYS   A 1 110 ? 24.945 -16.247 -4.283  1.00 15.28 ?  110 LYS   A HG2  1 
ATOM   2440 H  HG3  . LYS   A 1 110 ? 23.404 -16.165 -3.906  1.00 15.28 ?  110 LYS   A HG3  1 
ATOM   2441 H  HD2  . LYS   A 1 110 ? 22.901 -17.528 -5.737  1.00 16.10 ?  110 LYS   A HD2  1 
ATOM   2442 H  HD3  . LYS   A 1 110 ? 24.455 -17.639 -6.063  1.00 16.10 ?  110 LYS   A HD3  1 
ATOM   2443 H  HE2  . LYS   A 1 110 ? 23.983 -19.537 -4.950  1.00 17.03 ?  110 LYS   A HE2  1 
ATOM   2444 H  HE3  . LYS   A 1 110 ? 24.692 -18.618 -3.865  1.00 17.03 ?  110 LYS   A HE3  1 
ATOM   2445 H  HZ1  . LYS   A 1 110 ? 22.827 -19.576 -2.999  1.00 17.65 ?  110 LYS   A HZ1  1 
ATOM   2446 H  HZ2  . LYS   A 1 110 ? 22.634 -18.140 -3.027  1.00 17.65 ?  110 LYS   A HZ2  1 
ATOM   2447 H  HZ3  . LYS   A 1 110 ? 21.987 -18.978 -4.017  1.00 17.65 ?  110 LYS   A HZ3  1 
ATOM   2448 N  N    . SER   A 1 111 ? 26.260 -13.000 -4.937  1.00 11.40 ?  111 SER   A N    1 
ATOM   2449 C  CA   . SER   A 1 111 ? 27.586 -12.701 -4.409  1.00 11.27 ?  111 SER   A CA   1 
ATOM   2450 C  C    . SER   A 1 111 ? 27.509 -11.663 -3.298  1.00 10.88 ?  111 SER   A C    1 
ATOM   2451 O  O    . SER   A 1 111 ? 28.209 -11.771 -2.282  1.00 11.43 ?  111 SER   A O    1 
ATOM   2452 C  CB   . SER   A 1 111 ? 28.487 -12.218 -5.543  1.00 13.00 ?  111 SER   A CB   1 
ATOM   2453 O  OG   . SER   A 1 111 ? 28.529 -13.188 -6.575  1.00 14.73 ?  111 SER   A OG   1 
ATOM   2454 H  H    . SER   A 1 111 ? 26.161 -12.848 -5.775  1.00 13.66 ?  111 SER   A H    1 
ATOM   2455 H  HA   . SER   A 1 111 ? 27.969 -13.514 -4.042  1.00 13.51 ?  111 SER   A HA   1 
ATOM   2456 H  HB2  . SER   A 1 111 ? 28.125 -11.399 -5.912  1.00 15.59 ?  111 SER   A HB2  1 
ATOM   2457 H  HB3  . SER   A 1 111 ? 29.380 -12.068 -5.198  1.00 15.59 ?  111 SER   A HB3  1 
ATOM   2458 H  HG   . SER   A 1 111 ? 29.046 -12.932 -7.193  1.00 17.67 ?  111 SER   A HG   1 
ATOM   2459 N  N    . ALA   A 1 112 ? 26.674 -10.635 -3.486  1.00 10.72 ?  112 ALA   A N    1 
ATOM   2460 C  CA   . ALA   A 1 112 ? 26.509 -9.605  -2.465  1.00 10.62 ?  112 ALA   A CA   1 
ATOM   2461 C  C    . ALA   A 1 112 ? 26.027 -10.217 -1.152  1.00 10.43 ?  112 ALA   A C    1 
ATOM   2462 O  O    . ALA   A 1 112 ? 26.571 -9.938  -0.078  1.00 10.95 ?  112 ALA   A O    1 
ATOM   2463 C  CB   . ALA   A 1 112 ? 25.541 -8.527  -2.961  1.00 11.12 ?  112 ALA   A CB   1 
ATOM   2464 H  H    . ALA   A 1 112 ? 26.202 -10.509 -4.195  1.00 12.86 ?  112 ALA   A H    1 
ATOM   2465 H  HA   . ALA   A 1 112 ? 27.366 -9.180  -2.299  1.00 12.74 ?  112 ALA   A HA   1 
ATOM   2466 H  HB1  . ALA   A 1 112 ? 25.464 -7.833  -2.283  1.00 13.33 ?  112 ALA   A HB1  1 
ATOM   2467 H  HB2  . ALA   A 1 112 ? 25.888 -8.141  -3.782  1.00 13.33 ?  112 ALA   A HB2  1 
ATOM   2468 H  HB3  . ALA   A 1 112 ? 24.674 -8.926  -3.125  1.00 13.33 ?  112 ALA   A HB3  1 
ATOM   2469 N  N    . TYR   A 1 113 ? 24.992 -11.064 -1.217  1.00 10.39 ?  113 TYR   A N    1 
ATOM   2470 C  CA   . TYR   A 1 113 ? 24.469 -11.676 0.003   1.00 10.36 ?  113 TYR   A CA   1 
ATOM   2471 C  C    . TYR   A 1 113 ? 25.472 -12.621 0.657   1.00 10.15 ?  113 TYR   A C    1 
ATOM   2472 O  O    . TYR   A 1 113 ? 25.418 -12.817 1.873   1.00 10.73 ?  113 TYR   A O    1 
ATOM   2473 C  CB   . TYR   A 1 113 ? 23.157 -12.411 -0.281  1.00 10.70 ?  113 TYR   A CB   1 
ATOM   2474 C  CG   . TYR   A 1 113 ? 21.935 -11.520 -0.238  1.00 10.84 ?  113 TYR   A CG   1 
ATOM   2475 C  CD1  . TYR   A 1 113 ? 21.561 -10.883 0.939   1.00 11.45 ?  113 TYR   A CD1  1 
ATOM   2476 C  CD2  . TYR   A 1 113 ? 21.138 -11.348 -1.359  1.00 11.15 ?  113 TYR   A CD2  1 
ATOM   2477 C  CE1  . TYR   A 1 113 ? 20.431 -10.093 0.994   1.00 11.98 ?  113 TYR   A CE1  1 
ATOM   2478 C  CE2  . TYR   A 1 113 ? 19.990 -10.551 -1.315  1.00 11.42 ?  113 TYR   A CE2  1 
ATOM   2479 C  CZ   . TYR   A 1 113 ? 19.650 -9.927  -0.138  1.00 11.47 ?  113 TYR   A CZ   1 
ATOM   2480 O  OH   . TYR   A 1 113 ? 18.520 -9.140  -0.058  1.00 12.95 ?  113 TYR   A OH   1 
ATOM   2481 H  H    . TYR   A 1 113 ? 24.588 -11.294 -1.943  1.00 12.46 ?  113 TYR   A H    1 
ATOM   2482 H  HA   . TYR   A 1 113 ? 24.283 -10.972 0.641   1.00 12.43 ?  113 TYR   A HA   1 
ATOM   2483 H  HB2  . TYR   A 1 113 ? 23.208 -12.802 -1.167  1.00 12.83 ?  113 TYR   A HB2  1 
ATOM   2484 H  HB3  . TYR   A 1 113 ? 23.046 -13.109 0.382   1.00 12.83 ?  113 TYR   A HB3  1 
ATOM   2485 H  HD1  . TYR   A 1 113 ? 22.084 -11.002 1.704   1.00 13.73 ?  113 TYR   A HD1  1 
ATOM   2486 H  HD2  . TYR   A 1 113 ? 21.369 -11.775 -2.151  1.00 13.37 ?  113 TYR   A HD2  1 
ATOM   2487 H  HE1  . TYR   A 1 113 ? 20.199 -9.679  1.791   1.00 14.37 ?  113 TYR   A HE1  1 
ATOM   2488 H  HE2  . TYR   A 1 113 ? 19.462 -10.439 -2.070  1.00 13.69 ?  113 TYR   A HE2  1 
ATOM   2489 H  HH   . TYR   A 1 113 ? 18.133 -9.122  -0.805  1.00 15.53 ?  113 TYR   A HH   1 
ATOM   2490 N  N    . GLU   A 1 114 ? 26.381 -13.229 -0.120  1.00 10.50 ?  114 GLU   A N    1 
ATOM   2491 C  CA   . GLU   A 1 114 ? 27.366 -14.127 0.484   1.00 11.13 ?  114 GLU   A CA   1 
ATOM   2492 C  C    . GLU   A 1 114 ? 28.206 -13.410 1.536   1.00 10.83 ?  114 GLU   A C    1 
ATOM   2493 O  O    . GLU   A 1 114 ? 28.693 -14.042 2.481   1.00 11.06 ?  114 GLU   A O    1 
ATOM   2494 C  CB   . GLU   A 1 114 ? 28.253 -14.764 -0.595  1.00 11.16 ?  114 GLU   A CB   1 
ATOM   2495 C  CG   . GLU   A 1 114 ? 27.497 -15.808 -1.398  1.00 11.77 ?  114 GLU   A CG   1 
ATOM   2496 C  CD   . GLU   A 1 114 ? 28.216 -16.325 -2.644  1.00 12.10 ?  114 GLU   A CD   1 
ATOM   2497 O  OE1  . GLU   A 1 114 ? 29.170 -15.688 -3.138  1.00 12.40 ?  114 GLU   A OE1  1 
ATOM   2498 O  OE2  . GLU   A 1 114 ? 27.789 -17.394 -3.142  1.00 13.35 -1 114 GLU   A OE2  1 
ATOM   2499 H  H    . GLU   A 1 114 ? 26.439 -13.140 -0.978  1.00 12.59 ?  114 GLU   A H    1 
ATOM   2500 H  HA   . GLU   A 1 114 ? 26.888 -14.842 0.930   1.00 13.34 ?  114 GLU   A HA   1 
ATOM   2501 H  HB2  . GLU   A 1 114 ? 28.552 -14.073 -1.210  1.00 13.38 ?  114 GLU   A HB2  1 
ATOM   2502 H  HB3  . GLU   A 1 114 ? 29.008 -15.192 -0.174  1.00 13.38 ?  114 GLU   A HB3  1 
ATOM   2503 H  HG2  . GLU   A 1 114 ? 27.331 -16.572 -0.822  1.00 14.11 ?  114 GLU   A HG2  1 
ATOM   2504 H  HG3  . GLU   A 1 114 ? 26.652 -15.430 -1.683  1.00 14.11 ?  114 GLU   A HG3  1 
ATOM   2505 N  N    . ASN   A 1 115 ? 28.383 -12.092 1.399   1.00 10.65 ?  115 ASN   A N    1 
ATOM   2506 C  CA   . ASN   A 1 115 ? 29.141 -11.360 2.407   1.00 10.87 ?  115 ASN   A CA   1 
ATOM   2507 C  C    . ASN   A 1 115 ? 28.510 -11.484 3.788   1.00 10.73 ?  115 ASN   A C    1 
ATOM   2508 O  O    . ASN   A 1 115 ? 29.210 -11.405 4.805   1.00 11.00 ?  115 ASN   A O    1 
ATOM   2509 C  CB   . ASN   A 1 115 ? 29.250 -9.884  2.019   1.00 11.36 ?  115 ASN   A CB   1 
ATOM   2510 C  CG   . ASN   A 1 115 ? 30.067 -9.673  0.771   1.00 11.68 ?  115 ASN   A CG   1 
ATOM   2511 O  OD1  . ASN   A 1 115 ? 31.283 -9.790  0.797   1.00 15.01 ?  115 ASN   A OD1  1 
ATOM   2512 N  ND2  . ASN   A 1 115 ? 29.401 -9.365  -0.330  1.00 11.19 ?  115 ASN   A ND2  1 
ATOM   2513 H  H    . ASN   A 1 115 ? 28.073 -11.609 0.754   1.00 12.77 ?  115 ASN   A H    1 
ATOM   2514 H  HA   . ASN   A 1 115 ? 30.037 -11.728 2.451   1.00 13.03 ?  115 ASN   A HA   1 
ATOM   2515 H  HB2  . ASN   A 1 115 ? 28.355 -9.533  1.869   1.00 13.62 ?  115 ASN   A HB2  1 
ATOM   2516 H  HB3  . ASN   A 1 115 ? 29.672 -9.400  2.749   1.00 13.62 ?  115 ASN   A HB3  1 
ATOM   2517 H  HD21 . ASN   A 1 115 ? 29.828 -9.226  -1.063  1.00 13.41 ?  115 ASN   A HD21 1 
ATOM   2518 H  HD22 . ASN   A 1 115 ? 28.543 -9.301  -0.313  1.00 13.41 ?  115 ASN   A HD22 1 
ATOM   2519 N  N    . PHE   A 1 116 ? 27.185 -11.655 3.849   1.00 10.59 ?  116 PHE   A N    1 
ATOM   2520 C  CA   . PHE   A 1 116 ? 26.527 -11.753 5.146   1.00 10.70 ?  116 PHE   A CA   1 
ATOM   2521 C  C    . PHE   A 1 116 ? 27.003 -12.980 5.925   1.00 11.36 ?  116 PHE   A C    1 
ATOM   2522 O  O    . PHE   A 1 116 ? 26.922 -13.000 7.157   1.00 11.64 ?  116 PHE   A O    1 
ATOM   2523 C  CB   . PHE   A 1 116 ? 25.002 -11.884 5.000   1.00 10.99 ?  116 PHE   A CB   1 
ATOM   2524 C  CG   . PHE   A 1 116 ? 24.247 -10.643 4.520   1.00 10.48 ?  116 PHE   A CG   1 
ATOM   2525 C  CD1  . PHE   A 1 116 ? 24.819 -9.626  3.763   1.00 10.68 ?  116 PHE   A CD1  1 
ATOM   2526 C  CD2  . PHE   A 1 116 ? 22.893 -10.538 4.829   1.00 11.21 ?  116 PHE   A CD2  1 
ATOM   2527 C  CE1  . PHE   A 1 116 ? 24.056 -8.562  3.329   1.00 11.02 ?  116 PHE   A CE1  1 
ATOM   2528 C  CE2  . PHE   A 1 116 ? 22.133 -9.465  4.406   1.00 11.58 ?  116 PHE   A CE2  1 
ATOM   2529 C  CZ   . PHE   A 1 116 ? 22.712 -8.482  3.651   1.00 10.89 ?  116 PHE   A CZ   1 
ATOM   2530 H  H    . PHE   A 1 116 ? 26.660 -11.710 3.169   1.00 12.69 ?  116 PHE   A H    1 
ATOM   2531 H  HA   . PHE   A 1 116 ? 26.716 -10.966 5.671   1.00 12.82 ?  116 PHE   A HA   1 
ATOM   2532 H  HB2  . PHE   A 1 116 ? 24.815 -12.601 4.368   1.00 13.18 ?  116 PHE   A HB2  1 
ATOM   2533 H  HB3  . PHE   A 1 116 ? 24.634 -12.131 5.868   1.00 13.18 ?  116 PHE   A HB3  1 
ATOM   2534 H  HD1  . PHE   A 1 116 ? 25.714 -9.687  3.533   1.00 12.81 ?  116 PHE   A HD1  1 
ATOM   2535 H  HD2  . PHE   A 1 116 ? 22.483 -11.212 5.329   1.00 13.45 ?  116 PHE   A HD2  1 
ATOM   2536 H  HE1  . PHE   A 1 116 ? 24.453 -7.888  2.829   1.00 13.22 ?  116 PHE   A HE1  1 
ATOM   2537 H  HE2  . PHE   A 1 116 ? 21.229 -9.413  4.624   1.00 13.89 ?  116 PHE   A HE2  1 
ATOM   2538 H  HZ   . PHE   A 1 116 ? 22.212 -7.749  3.372   1.00 13.06 ?  116 PHE   A HZ   1 
ATOM   2539 N  N    . ASN   A 1 117 ? 27.451 -14.030 5.228   1.00 11.47 ?  117 ASN   A N    1 
ATOM   2540 C  CA   . ASN   A 1 117 ? 27.819 -15.275 5.899   1.00 11.59 ?  117 ASN   A CA   1 
ATOM   2541 C  C    . ASN   A 1 117 ? 29.073 -15.159 6.743   1.00 12.11 ?  117 ASN   A C    1 
ATOM   2542 O  O    . ASN   A 1 117 ? 29.368 -16.079 7.514   1.00 12.77 ?  117 ASN   A O    1 
ATOM   2543 C  CB   . ASN   A 1 117 ? 27.945 -16.394 4.877   1.00 11.59 ?  117 ASN   A CB   1 
ATOM   2544 C  CG   . ASN   A 1 117 ? 26.600 -16.777 4.321   1.00 11.76 ?  117 ASN   A CG   1 
ATOM   2545 O  OD1  . ASN   A 1 117 ? 25.609 -16.800 5.057   1.00 12.72 ?  117 ASN   A OD1  1 
ATOM   2546 N  ND2  . ASN   A 1 117 ? 26.535 -17.038 3.033   1.00 11.55 ?  117 ASN   A ND2  1 
ATOM   2547 H  H    . ASN   A 1 117 ? 27.546 -14.044 4.374   1.00 13.75 ?  117 ASN   A H    1 
ATOM   2548 H  HA   . ASN   A 1 117 ? 27.091 -15.509 6.499   1.00 13.90 ?  117 ASN   A HA   1 
ATOM   2549 H  HB2  . ASN   A 1 117 ? 28.502 -16.092 4.143   1.00 13.90 ?  117 ASN   A HB2  1 
ATOM   2550 H  HB3  . ASN   A 1 117 ? 28.336 -17.168 5.305   1.00 13.90 ?  117 ASN   A HB3  1 
ATOM   2551 H  HD21 . ASN   A 1 117 ? 25.786 -17.260 2.681   1.00 13.85 ?  117 ASN   A HD21 1 
ATOM   2552 H  HD22 . ASN   A 1 117 ? 27.247 -16.999 2.556   1.00 13.85 ?  117 ASN   A HD22 1 
ATOM   2553 N  N    . GLN   A 1 118 ? 29.803 -14.048 6.628   1.00 11.89 ?  118 GLN   A N    1 
ATOM   2554 C  CA   . GLN   A 1 118 ? 30.971 -13.808 7.462   1.00 12.66 ?  118 GLN   A CA   1 
ATOM   2555 C  C    . GLN   A 1 118 ? 30.615 -13.230 8.829   1.00 12.63 ?  118 GLN   A C    1 
ATOM   2556 O  O    . GLN   A 1 118 ? 31.527 -12.945 9.614   1.00 13.92 ?  118 GLN   A O    1 
ATOM   2557 C  CB   . GLN   A 1 118 ? 31.964 -12.897 6.730   1.00 12.79 ?  118 GLN   A CB   1 
ATOM   2558 C  CG   . GLN   A 1 118 ? 32.445 -13.479 5.404   1.00 12.77 ?  118 GLN   A CG   1 
ATOM   2559 C  CD   . GLN   A 1 118 ? 33.293 -14.731 5.587   1.00 13.09 ?  118 GLN   A CD   1 
ATOM   2560 O  OE1  . GLN   A 1 118 ? 34.155 -14.787 6.475   1.00 13.96 ?  118 GLN   A OE1  1 
ATOM   2561 N  NE2  . GLN   A 1 118 ? 33.057 -15.739 4.744   1.00 13.35 ?  118 GLN   A NE2  1 
ATOM   2562 H  H    . GLN   A 1 118 ? 29.629 -13.401 6.076   1.00 14.26 ?  118 GLN   A H    1 
ATOM   2563 H  HA   . GLN   A 1 118 ? 31.405 -14.659 7.612   1.00 15.18 ?  118 GLN   A HA   1 
ATOM   2564 H  HB2  . GLN   A 1 118 ? 31.535 -12.047 6.551   1.00 15.34 ?  118 GLN   A HB2  1 
ATOM   2565 H  HB3  . GLN   A 1 118 ? 32.738 -12.764 7.300   1.00 15.34 ?  118 GLN   A HB3  1 
ATOM   2566 H  HG2  . GLN   A 1 118 ? 31.677 -13.711 4.856   1.00 15.32 ?  118 GLN   A HG2  1 
ATOM   2567 H  HG3  . GLN   A 1 118 ? 32.987 -12.817 4.944   1.00 15.32 ?  118 GLN   A HG3  1 
ATOM   2568 H  HE21 . GLN   A 1 118 ? 32.443 -15.665 4.138   1.00 16.00 ?  118 GLN   A HE21 1 
ATOM   2569 H  HE22 . GLN   A 1 118 ? 33.505 -16.470 4.804   1.00 16.00 ?  118 GLN   A HE22 1 
ATOM   2570 N  N    . HIS   A 1 119 ? 29.324 -13.069 9.135   1.00 12.03 ?  119 HIS   A N    1 
ATOM   2571 C  CA   . HIS   A 1 119 ? 28.858 -12.458 10.377  1.00 12.58 ?  119 HIS   A CA   1 
ATOM   2572 C  C    . HIS   A 1 119 ? 27.719 -13.285 10.943  1.00 12.81 ?  119 HIS   A C    1 
ATOM   2573 O  O    . HIS   A 1 119 ? 26.779 -13.619 10.219  1.00 13.10 ?  119 HIS   A O    1 
ATOM   2574 C  CB   . HIS   A 1 119 ? 28.397 -11.028 10.100  1.00 12.76 ?  119 HIS   A CB   1 
ATOM   2575 C  CG   . HIS   A 1 119 ? 29.469 -10.223 9.462   1.00 14.12 ?  119 HIS   A CG   1 
ATOM   2576 N  ND1  . HIS   A 1 119 ? 30.451 -9.604  10.199  1.00 16.01 ?  119 HIS   A ND1  1 
ATOM   2577 C  CD2  . HIS   A 1 119 ? 29.801 -10.053 8.162   1.00 15.06 ?  119 HIS   A CD2  1 
ATOM   2578 C  CE1  . HIS   A 1 119 ? 31.312 -9.033  9.377   1.00 16.33 ?  119 HIS   A CE1  1 
ATOM   2579 N  NE2  . HIS   A 1 119 ? 30.952 -9.303  8.136   1.00 16.33 ?  119 HIS   A NE2  1 
ATOM   2580 H  H    . HIS   A 1 119 ? 28.674 -13.329 8.625   1.00 14.42 ?  119 HIS   A H    1 
ATOM   2581 H  HA   . HIS   A 1 119 ? 29.580 -12.441 11.023  1.00 15.08 ?  119 HIS   A HA   1 
ATOM   2582 H  HB2  . HIS   A 1 119 ? 27.634 -11.051 9.506   1.00 15.31 ?  119 HIS   A HB2  1 
ATOM   2583 H  HB3  . HIS   A 1 119 ? 28.159 -10.608 10.942  1.00 15.31 ?  119 HIS   A HB3  1 
ATOM   2584 H  HD1  . HIS   A 1 119 ? 30.487 -9.575  11.057  1.00 19.21 ?  119 HIS   A HD1  1 
ATOM   2585 H  HD2  . HIS   A 1 119 ? 29.336 -10.383 7.425   1.00 18.06 ?  119 HIS   A HD2  1 
ATOM   2586 H  HE1  . HIS   A 1 119 ? 32.051 -8.528  9.627   1.00 19.59 ?  119 HIS   A HE1  1 
ATOM   2587 N  N    A GLU   A 1 120 ? 27.795 -13.598 12.238  0.50 13.74 ?  120 GLU   A N    1 
ATOM   2588 N  N    B GLU   A 1 120 ? 27.799 -13.588 12.241  0.50 13.81 ?  120 GLU   A N    1 
ATOM   2589 C  CA   A GLU   A 1 120 ? 26.834 -14.534 12.818  0.50 15.10 ?  120 GLU   A CA   1 
ATOM   2590 C  CA   B GLU   A 1 120 ? 26.847 -14.516 12.848  0.50 15.24 ?  120 GLU   A CA   1 
ATOM   2591 C  C    A GLU   A 1 120 ? 25.420 -13.963 12.885  0.50 13.99 ?  120 GLU   A C    1 
ATOM   2592 C  C    B GLU   A 1 120 ? 25.427 -13.957 12.862  0.50 14.19 ?  120 GLU   A C    1 
ATOM   2593 O  O    A GLU   A 1 120 ? 24.449 -14.725 12.784  0.50 13.90 ?  120 GLU   A O    1 
ATOM   2594 O  O    B GLU   A 1 120 ? 24.460 -14.712 12.698  0.50 14.33 ?  120 GLU   A O    1 
ATOM   2595 C  CB   A GLU   A 1 120 ? 27.288 -14.978 14.207  0.50 18.61 ?  120 GLU   A CB   1 
ATOM   2596 C  CB   B GLU   A 1 120 ? 27.291 -14.872 14.266  0.50 18.70 ?  120 GLU   A CB   1 
ATOM   2597 C  CG   A GLU   A 1 120 ? 28.472 -15.929 14.190  0.50 23.14 ?  120 GLU   A CG   1 
ATOM   2598 C  CG   B GLU   A 1 120 ? 28.517 -15.764 14.320  0.50 23.32 ?  120 GLU   A CG   1 
ATOM   2599 C  CD   A GLU   A 1 120 ? 28.645 -16.664 15.502  0.50 27.06 ?  120 GLU   A CD   1 
ATOM   2600 C  CD   B GLU   A 1 120 ? 28.614 -16.532 15.620  0.50 27.23 ?  120 GLU   A CD   1 
ATOM   2601 O  OE1  A GLU   A 1 120 ? 28.382 -16.059 16.564  0.50 28.59 ?  120 GLU   A OE1  1 
ATOM   2602 O  OE1  B GLU   A 1 120 ? 28.174 -15.995 16.661  0.50 28.55 ?  120 GLU   A OE1  1 
ATOM   2603 O  OE2  A GLU   A 1 120 ? 29.032 -17.852 15.469  0.50 28.95 -1 120 GLU   A OE2  1 
ATOM   2604 O  OE2  B GLU   A 1 120 ? 29.118 -17.675 15.599  0.50 29.17 -1 120 GLU   A OE2  1 
ATOM   2605 H  H    A GLU   A 1 120 ? 28.385 -13.297 12.789  0.50 16.48 ?  120 GLU   A H    1 
ATOM   2606 H  H    B GLU   A 1 120 ? 28.393 -13.280 12.784  0.50 16.56 ?  120 GLU   A H    1 
ATOM   2607 H  HA   A GLU   A 1 120 ? 26.803 -15.324 12.260  0.50 18.11 ?  120 GLU   A HA   1 
ATOM   2608 H  HA   B GLU   A 1 120 ? 26.836 -15.334 12.331  0.50 18.28 ?  120 GLU   A HA   1 
ATOM   2609 H  HB2  A GLU   A 1 120 ? 27.542 -14.198 14.722  0.50 22.32 ?  120 GLU   A HB2  1 
ATOM   2610 H  HB2  B GLU   A 1 120 ? 27.501 -14.058 14.749  0.50 22.43 ?  120 GLU   A HB2  1 
ATOM   2611 H  HB3  A GLU   A 1 120 ? 26.551 -15.435 14.646  0.50 22.32 ?  120 GLU   A HB3  1 
ATOM   2612 H  HB3  B GLU   A 1 120 ? 26.569 -15.342 14.716  0.50 22.43 ?  120 GLU   A HB3  1 
ATOM   2613 H  HG2  A GLU   A 1 120 ? 28.341 -16.590 13.494  0.50 27.76 ?  120 GLU   A HG2  1 
ATOM   2614 H  HG2  B GLU   A 1 120 ? 28.481 -16.401 13.589  0.50 27.97 ?  120 GLU   A HG2  1 
ATOM   2615 H  HG3  A GLU   A 1 120 ? 29.282 -15.423 14.023  0.50 27.76 ?  120 GLU   A HG3  1 
ATOM   2616 H  HG3  B GLU   A 1 120 ? 29.314 -15.217 14.247  0.50 27.97 ?  120 GLU   A HG3  1 
ATOM   2617 N  N    . VAL   A 1 121 ? 25.281 -12.650 13.078  1.00 13.66 ?  121 VAL   A N    1 
ATOM   2618 C  CA   . VAL   A 1 121 ? 23.979 -11.992 13.184  1.00 13.87 ?  121 VAL   A CA   1 
ATOM   2619 C  C    . VAL   A 1 121 ? 24.088 -10.609 12.545  1.00 12.55 ?  121 VAL   A C    1 
ATOM   2620 O  O    . VAL   A 1 121 ? 25.049 -9.871  12.800  1.00 13.14 ?  121 VAL   A O    1 
ATOM   2621 C  CB   . VAL   A 1 121 ? 23.519 -11.841 14.656  1.00 16.97 ?  121 VAL   A CB   1 
ATOM   2622 C  CG1  . VAL   A 1 121 ? 22.137 -11.199 14.723  1.00 17.72 ?  121 VAL   A CG1  1 
ATOM   2623 C  CG2  . VAL   A 1 121 ? 23.504 -13.163 15.400  1.00 19.20 ?  121 VAL   A CG2  1 
ATOM   2624 H  H    A VAL   A 1 121 ? 25.944 -12.106 13.160  0.50 16.38 ?  121 VAL   A H    1 
ATOM   2625 H  H    B VAL   A 1 121 ? 25.943 -12.106 13.166  0.50 16.38 ?  121 VAL   A H    1 
ATOM   2626 H  HA   . VAL   A 1 121 ? 23.314 -12.510 12.706  1.00 16.63 ?  121 VAL   A HA   1 
ATOM   2627 H  HB   . VAL   A 1 121 ? 24.135 -11.252 15.115  1.00 20.36 ?  121 VAL   A HB   1 
ATOM   2628 H  HG11 . VAL   A 1 121 ? 21.802 -11.259 15.634  1.00 21.26 ?  121 VAL   A HG11 1 
ATOM   2629 H  HG12 . VAL   A 1 121 ? 22.201 -10.266 14.461  1.00 21.26 ?  121 VAL   A HG12 1 
ATOM   2630 H  HG13 . VAL   A 1 121 ? 21.536 -11.669 14.123  1.00 21.26 ?  121 VAL   A HG13 1 
ATOM   2631 H  HG21 . VAL   A 1 121 ? 23.157 -13.015 16.302  1.00 23.03 ?  121 VAL   A HG21 1 
ATOM   2632 H  HG22 . VAL   A 1 121 ? 22.923 -13.786 14.933  1.00 23.03 ?  121 VAL   A HG22 1 
ATOM   2633 H  HG23 . VAL   A 1 121 ? 24.400 -13.515 15.450  1.00 23.03 ?  121 VAL   A HG23 1 
ATOM   2634 N  N    . LEU   A 1 122 ? 23.087 -10.237 11.740  1.00 11.80 ?  122 LEU   A N    1 
ATOM   2635 C  CA   . LEU   A 1 122 ? 23.084 -8.941  11.066  1.00 11.58 ?  122 LEU   A CA   1 
ATOM   2636 C  C    . LEU   A 1 122 ? 21.682 -8.361  11.035  1.00 11.26 ?  122 LEU   A C    1 
ATOM   2637 O  O    . LEU   A 1 122 ? 20.701 -9.088  10.883  1.00 12.61 ?  122 LEU   A O    1 
ATOM   2638 C  CB   . LEU   A 1 122 ? 23.495 -9.044  9.592   1.00 13.15 ?  122 LEU   A CB   1 
ATOM   2639 C  CG   . LEU   A 1 122 ? 24.727 -9.870  9.252   1.00 12.79 ?  122 LEU   A CG   1 
ATOM   2640 C  CD1  . LEU   A 1 122 ? 24.342 -11.320 9.019   1.00 13.58 ?  122 LEU   A CD1  1 
ATOM   2641 C  CD2  . LEU   A 1 122 ? 25.431 -9.309  8.034   1.00 12.27 ?  122 LEU   A CD2  1 
ATOM   2642 H  H    . LEU   A 1 122 ? 22.386 -10.717 11.574  1.00 14.14 ?  122 LEU   A H    1 
ATOM   2643 H  HA   . LEU   A 1 122 ? 23.683 -8.325  11.515  1.00 13.88 ?  122 LEU   A HA   1 
ATOM   2644 H  HB2  . LEU   A 1 122 ? 22.759 -9.436  9.098   1.00 15.77 ?  122 LEU   A HB2  1 
ATOM   2645 H  HB3  . LEU   A 1 122 ? 23.664 -8.152  9.258   1.00 15.77 ?  122 LEU   A HB3  1 
ATOM   2646 H  HG   . LEU   A 1 122 ? 25.356 -9.848  9.991   1.00 15.34 ?  122 LEU   A HG   1 
ATOM   2647 H  HD11 . LEU   A 1 122 ? 25.129 -11.832 8.780   1.00 16.29 ?  122 LEU   A HD11 1 
ATOM   2648 H  HD12 . LEU   A 1 122 ? 23.951 -11.678 9.832   1.00 16.29 ?  122 LEU   A HD12 1 
ATOM   2649 H  HD13 . LEU   A 1 122 ? 23.691 -11.363 8.297   1.00 16.29 ?  122 LEU   A HD13 1 
ATOM   2650 H  HD21 . LEU   A 1 122 ? 26.198 -9.869  7.814   1.00 14.72 ?  122 LEU   A HD21 1 
ATOM   2651 H  HD22 . LEU   A 1 122 ? 24.814 -9.295  7.286   1.00 14.72 ?  122 LEU   A HD22 1 
ATOM   2652 H  HD23 . LEU   A 1 122 ? 25.734 -8.408  8.230   1.00 14.72 ?  122 LEU   A HD23 1 
ATOM   2653 N  N    . LEU   A 1 123 ? 21.613 -7.032  11.125  1.00 11.34 ?  123 LEU   A N    1 
ATOM   2654 C  CA   . LEU   A 1 123 ? 20.437 -6.247  10.759  1.00 10.98 ?  123 LEU   A CA   1 
ATOM   2655 C  C    . LEU   A 1 123 ? 20.679 -5.708  9.356   1.00 10.79 ?  123 LEU   A C    1 
ATOM   2656 O  O    . LEU   A 1 123 ? 21.730 -5.110  9.111   1.00 11.45 ?  123 LEU   A O    1 
ATOM   2657 C  CB   . LEU   A 1 123 ? 20.283 -5.079  11.736  1.00 11.55 ?  123 LEU   A CB   1 
ATOM   2658 C  CG   . LEU   A 1 123 ? 19.244 -4.020  11.385  1.00 12.15 ?  123 LEU   A CG   1 
ATOM   2659 C  CD1  . LEU   A 1 123 ? 17.832 -4.601  11.370  1.00 13.23 ?  123 LEU   A CD1  1 
ATOM   2660 C  CD2  . LEU   A 1 123 ? 19.335 -2.845  12.349  1.00 12.93 ?  123 LEU   A CD2  1 
ATOM   2661 H  H    . LEU   A 1 123 ? 22.269 -6.544  11.402  1.00 13.60 ?  123 LEU   A H    1 
ATOM   2662 H  HA   . LEU   A 1 123 ? 19.642 -6.800  10.770  1.00 13.16 ?  123 LEU   A HA   1 
ATOM   2663 H  HB2  . LEU   A 1 123 ? 20.038 -5.441  12.604  1.00 13.85 ?  123 LEU   A HB2  1 
ATOM   2664 H  HB3  . LEU   A 1 123 ? 21.136 -4.626  11.809  1.00 13.85 ?  123 LEU   A HB3  1 
ATOM   2665 H  HG   . LEU   A 1 123 ? 19.423 -3.678  10.495  1.00 14.57 ?  123 LEU   A HG   1 
ATOM   2666 H  HD11 . LEU   A 1 123 ? 17.201 -3.895  11.161  1.00 15.86 ?  123 LEU   A HD11 1 
ATOM   2667 H  HD12 . LEU   A 1 123 ? 17.784 -5.297  10.697  1.00 15.86 ?  123 LEU   A HD12 1 
ATOM   2668 H  HD13 . LEU   A 1 123 ? 17.636 -4.972  12.245  1.00 15.86 ?  123 LEU   A HD13 1 
ATOM   2669 H  HD21 . LEU   A 1 123 ? 18.667 -2.187  12.111  1.00 15.50 ?  123 LEU   A HD21 1 
ATOM   2670 H  HD22 . LEU   A 1 123 ? 19.177 -3.169  13.251  1.00 15.50 ?  123 LEU   A HD22 1 
ATOM   2671 H  HD23 . LEU   A 1 123 ? 20.222 -2.460  12.286  1.00 15.50 ?  123 LEU   A HD23 1 
ATOM   2672 N  N    . ALA   A 1 124 ? 19.728 -5.897  8.439   1.00 10.54 ?  124 ALA   A N    1 
ATOM   2673 C  CA   . ALA   A 1 124 ? 20.020 -5.609  7.043   1.00 10.25 ?  124 ALA   A CA   1 
ATOM   2674 C  C    . ALA   A 1 124 ? 18.776 -5.177  6.281   1.00 10.33 ?  124 ALA   A C    1 
ATOM   2675 O  O    . ALA   A 1 124 ? 17.648 -5.545  6.649   1.00 11.02 ?  124 ALA   A O    1 
ATOM   2676 C  CB   . ALA   A 1 124 ? 20.610 -6.833  6.338   1.00 11.29 ?  124 ALA   A CB   1 
ATOM   2677 H  H    . ALA   A 1 124 ? 18.928 -6.187  8.594   1.00 12.63 ?  124 ALA   A H    1 
ATOM   2678 H  HA   . ALA   A 1 124 ? 20.679 -4.896  7.019   1.00 12.29 ?  124 ALA   A HA   1 
ATOM   2679 H  HB1  . ALA   A 1 124 ? 20.804 -6.607  5.414   1.00 13.53 ?  124 ALA   A HB1  1 
ATOM   2680 H  HB2  . ALA   A 1 124 ? 21.437 -7.089  6.789   1.00 13.53 ?  124 ALA   A HB2  1 
ATOM   2681 H  HB3  . ALA   A 1 124 ? 19.976 -7.560  6.379   1.00 13.53 ?  124 ALA   A HB3  1 
ATOM   2682 N  N    A PRO   A 1 125 ? 18.956 -4.413  5.207   0.50 10.66 ?  125 PRO   A N    1 
ATOM   2683 N  N    B PRO   A 1 125 ? 18.953 -4.441  5.185   0.50 10.23 ?  125 PRO   A N    1 
ATOM   2684 C  CA   A PRO   A 1 125 ? 17.886 -4.175  4.241   0.50 11.06 ?  125 PRO   A CA   1 
ATOM   2685 C  CA   B PRO   A 1 125 ? 17.894 -4.282  4.191   0.50 10.24 ?  125 PRO   A CA   1 
ATOM   2686 C  C    A PRO   A 1 125 ? 17.961 -5.222  3.133   0.50 11.43 ?  125 PRO   A C    1 
ATOM   2687 C  C    B PRO   A 1 125 ? 18.012 -5.365  3.129   0.50 10.18 ?  125 PRO   A C    1 
ATOM   2688 O  O    A PRO   A 1 125 ? 18.914 -6.001  3.041   0.50 11.76 ?  125 PRO   A O    1 
ATOM   2689 O  O    B PRO   A 1 125 ? 19.051 -6.013  2.978   0.50 10.54 ?  125 PRO   A O    1 
ATOM   2690 C  CB   A PRO   A 1 125 ? 18.286 -2.807  3.677   0.50 11.23 ?  125 PRO   A CB   1 
ATOM   2691 C  CB   B PRO   A 1 125 ? 18.255 -2.926  3.569   0.50 10.66 ?  125 PRO   A CB   1 
ATOM   2692 C  CG   A PRO   A 1 125 ? 19.797 -2.928  3.582   0.50 11.46 ?  125 PRO   A CG   1 
ATOM   2693 C  CG   B PRO   A 1 125 ? 19.777 -2.973  3.525   0.50 10.76 ?  125 PRO   A CG   1 
ATOM   2694 C  CD   A PRO   A 1 125 ? 20.204 -3.734  4.805   0.50 11.19 ?  125 PRO   A CD   1 
ATOM   2695 C  CD   B PRO   A 1 125 ? 20.200 -3.777  4.752   0.50 10.53 ?  125 PRO   A CD   1 
ATOM   2696 H  HA   A PRO   A 1 125 ? 17.005 -4.146  4.657   0.50 13.26 ?  125 PRO   A HA   1 
ATOM   2697 H  HA   B PRO   A 1 125 ? 17.011 -4.271  4.588   0.50 12.27 ?  125 PRO   A HA   1 
ATOM   2698 H  HB2  A PRO   A 1 125 ? 17.881 -2.674  2.803   0.50 13.47 ?  125 PRO   A HB2  1 
ATOM   2699 H  HB2  B PRO   A 1 125 ? 17.876 -2.859  2.675   0.50 12.78 ?  125 PRO   A HB2  1 
ATOM   2700 H  HB3  A PRO   A 1 125 ? 18.023 -2.099  4.292   0.50 13.47 ?  125 PRO   A HB3  1 
ATOM   2701 H  HB3  B PRO   A 1 125 ? 17.936 -2.207  4.136   0.50 12.78 ?  125 PRO   A HB3  1 
ATOM   2702 H  HG2  A PRO   A 1 125 ? 20.036 -3.395  2.766   0.50 13.74 ?  125 PRO   A HG2  1 
ATOM   2703 H  HG2  B PRO   A 1 125 ? 20.066 -3.410  2.709   0.50 12.90 ?  125 PRO   A HG2  1 
ATOM   2704 H  HG3  A PRO   A 1 125 ? 20.197 -2.044  3.601   0.50 13.74 ?  125 PRO   A HG3  1 
ATOM   2705 H  HG3  B PRO   A 1 125 ? 20.128 -2.067  3.567   0.50 12.90 ?  125 PRO   A HG3  1 
ATOM   2706 H  HD2  A PRO   A 1 125 ? 20.884 -4.384  4.568   0.50 13.42 ?  125 PRO   A HD2  1 
ATOM   2707 H  HD2  B PRO   A 1 125 ? 20.874 -4.430  4.505   0.50 12.62 ?  125 PRO   A HD2  1 
ATOM   2708 H  HD3  A PRO   A 1 125 ? 20.512 -3.140  5.510   0.50 13.42 ?  125 PRO   A HD3  1 
ATOM   2709 H  HD3  B PRO   A 1 125 ? 20.524 -3.179  5.446   0.50 12.62 ?  125 PRO   A HD3  1 
ATOM   2710 N  N    A LEU   A 1 126 ? 16.945 -5.206  2.273   0.50 11.56 ?  126 LEU   A N    1 
ATOM   2711 N  N    B LEU   A 1 126 ? 16.929 -5.548  2.379   0.50 10.05 ?  126 LEU   A N    1 
ATOM   2712 C  CA   A LEU   A 1 126 ? 16.925 -6.070  1.096   0.50 11.50 ?  126 LEU   A CA   1 
ATOM   2713 C  CA   B LEU   A 1 126 ? 17.052 -6.264  1.119   0.50 10.32 ?  126 LEU   A CA   1 
ATOM   2714 C  C    A LEU   A 1 126 ? 17.856 -5.505  0.030   0.50 11.42 ?  126 LEU   A C    1 
ATOM   2715 C  C    B LEU   A 1 126 ? 17.966 -5.460  0.202   0.50 11.11 ?  126 LEU   A C    1 
ATOM   2716 O  O    A LEU   A 1 126 ? 17.547 -4.485  -0.599  0.50 11.60 ?  126 LEU   A O    1 
ATOM   2717 O  O    B LEU   A 1 126 ? 17.927 -4.227  0.190   0.50 12.82 ?  126 LEU   A O    1 
ATOM   2718 C  CB   A LEU   A 1 126 ? 15.507 -6.181  0.557   0.50 12.02 ?  126 LEU   A CB   1 
ATOM   2719 C  CB   B LEU   A 1 126 ? 15.677 -6.454  0.481   0.50 10.93 ?  126 LEU   A CB   1 
ATOM   2720 C  CG   A LEU   A 1 126 ? 14.585 -7.111  1.337   0.50 12.23 ?  126 LEU   A CG   1 
ATOM   2721 C  CG   B LEU   A 1 126 ? 14.759 -7.449  1.199   0.50 12.06 ?  126 LEU   A CG   1 
ATOM   2722 C  CD1  A LEU   A 1 126 ? 13.175 -6.953  0.821   0.50 13.26 ?  126 LEU   A CD1  1 
ATOM   2723 C  CD1  B LEU   A 1 126 ? 13.341 -7.371  0.653   0.50 13.26 ?  126 LEU   A CD1  1 
ATOM   2724 C  CD2  A LEU   A 1 126 ? 15.035 -8.561  1.220   0.50 12.13 ?  126 LEU   A CD2  1 
ATOM   2725 C  CD2  B LEU   A 1 126 ? 15.305 -8.869  1.073   0.50 12.06 ?  126 LEU   A CD2  1 
ATOM   2726 H  H    A LEU   A 1 126 ? 16.249 -4.704  2.355   0.50 13.86 ?  126 LEU   A H    1 
ATOM   2727 H  H    B LEU   A 1 126 ? 16.139 -5.269  2.562   0.50 12.05 ?  126 LEU   A H    1 
ATOM   2728 H  HA   A LEU   A 1 126 ? 17.244 -6.949  1.339   0.50 13.79 ?  126 LEU   A HA   1 
ATOM   2729 H  HA   B LEU   A 1 126 ? 17.452 -7.132  1.268   0.50 12.38 ?  126 LEU   A HA   1 
ATOM   2730 H  HB2  A LEU   A 1 126 ? 15.107 -5.295  0.568   0.50 14.41 ?  126 LEU   A HB2  1 
ATOM   2731 H  HB2  B LEU   A 1 126 ? 15.219 -5.600  0.469   0.50 13.10 ?  126 LEU   A HB2  1 
ATOM   2732 H  HB3  A LEU   A 1 126 ? 15.552 -6.505  -0.353  0.50 14.41 ?  126 LEU   A HB3  1 
ATOM   2733 H  HB3  B LEU   A 1 126 ? 15.795 -6.773  -0.427  0.50 13.10 ?  126 LEU   A HB3  1 
ATOM   2734 H  HG   A LEU   A 1 126 ? 14.599 -6.861  2.276   0.50 14.67 ?  126 LEU   A HG   1 
ATOM   2735 H  HG   B LEU   A 1 126 ? 14.729 -7.230  2.144   0.50 14.46 ?  126 LEU   A HG   1 
ATOM   2736 H  HD11 A LEU   A 1 126 ? 12.592 -7.552  1.312   0.50 15.90 ?  126 LEU   A HD11 1 
ATOM   2737 H  HD11 B LEU   A 1 126 ? 12.783 -8.012  1.125   0.50 15.90 ?  126 LEU   A HD11 1 
ATOM   2738 H  HD12 A LEU   A 1 126 ? 12.893 -6.034  0.948   0.50 15.90 ?  126 LEU   A HD12 1 
ATOM   2739 H  HD12 B LEU   A 1 126 ? 13.001 -6.474  0.791   0.50 15.90 ?  126 LEU   A HD12 1 
ATOM   2740 H  HD13 A LEU   A 1 126 ? 13.160 -7.176  -0.124  0.50 15.90 ?  126 LEU   A HD13 1 
ATOM   2741 H  HD13 B LEU   A 1 126 ? 13.355 -7.580  -0.293  0.50 15.90 ?  126 LEU   A HD13 1 
ATOM   2742 H  HD21 A LEU   A 1 126 ? 14.349 -9.134  1.590   0.50 14.55 ?  126 LEU   A HD21 1 
ATOM   2743 H  HD21 B LEU   A 1 126 ? 14.653 -9.494  1.425   0.50 14.46 ?  126 LEU   A HD21 1 
ATOM   2744 H  HD22 A LEU   A 1 126 ? 15.177 -8.772  0.284   0.50 14.55 ?  126 LEU   A HD22 1 
ATOM   2745 H  HD22 B LEU   A 1 126 ? 15.474 -9.060  0.137   0.50 14.46 ?  126 LEU   A HD22 1 
ATOM   2746 H  HD23 A LEU   A 1 126 ? 15.866 -8.677  1.712   0.50 14.55 ?  126 LEU   A HD23 1 
ATOM   2747 H  HD23 B LEU   A 1 126 ? 16.133 -8.937  1.577   0.50 14.46 ?  126 LEU   A HD23 1 
ATOM   2748 N  N    A LEU   A 1 127 ? 18.972 -6.194  -0.203  0.50 10.78 ?  127 LEU   A N    1 
ATOM   2749 N  N    B LEU   A 1 127 ? 18.817 -6.154  -0.545  0.50 10.62 ?  127 LEU   A N    1 
ATOM   2750 C  CA   A LEU   A 1 127 ? 19.964 -5.730  -1.161  0.50 10.66 ?  127 LEU   A CA   1 
ATOM   2751 C  CA   B LEU   A 1 127 ? 19.794 -5.506  -1.406  0.50 10.67 ?  127 LEU   A CA   1 
ATOM   2752 C  C    A LEU   A 1 127 ? 19.336 -5.524  -2.530  0.50 10.46 ?  127 LEU   A C    1 
ATOM   2753 C  C    B LEU   A 1 127 ? 19.324 -5.490  -2.859  0.50 10.78 ?  127 LEU   A C    1 
ATOM   2754 O  O    A LEU   A 1 127 ? 18.464 -6.285  -2.961  0.50 11.19 ?  127 LEU   A O    1 
ATOM   2755 O  O    B LEU   A 1 127 ? 18.548 -6.345  -3.302  0.50 10.73 ?  127 LEU   A O    1 
ATOM   2756 C  CB   A LEU   A 1 127 ? 21.107 -6.741  -1.264  0.50 10.74 ?  127 LEU   A CB   1 
ATOM   2757 C  CB   B LEU   A 1 127 ? 21.152 -6.208  -1.306  0.50 11.47 ?  127 LEU   A CB   1 
ATOM   2758 C  CG   A LEU   A 1 127 ? 21.944 -6.927  -0.000  0.50 11.06 ?  127 LEU   A CG   1 
ATOM   2759 C  CG   B LEU   A 1 127 ? 21.873 -6.142  0.050   0.50 12.58 ?  127 LEU   A CG   1 
ATOM   2760 C  CD1  A LEU   A 1 127 ? 23.057 -7.915  -0.273  0.50 10.82 ?  127 LEU   A CD1  1 
ATOM   2761 C  CD1  B LEU   A 1 127 ? 23.102 -7.045  0.065   0.50 13.62 ?  127 LEU   A CD1  1 
ATOM   2762 C  CD2  A LEU   A 1 127 ? 22.524 -5.610  0.481   0.50 12.16 ?  127 LEU   A CD2  1 
ATOM   2763 C  CD2  B LEU   A 1 127 ? 22.256 -4.706  0.408   0.50 13.34 ?  127 LEU   A CD2  1 
ATOM   2764 H  H    A LEU   A 1 127 ? 19.169 -6.941  0.169   0.50 12.92 ?  127 LEU   A H    1 
ATOM   2765 H  H    B LEU   A 1 127 ? 18.847 -7.013  -0.564  0.50 12.73 ?  127 LEU   A H    1 
ATOM   2766 H  HA   A LEU   A 1 127 ? 20.327 -4.883  -0.871  0.50 12.79 ?  127 LEU   A HA   1 
ATOM   2767 H  HA   B LEU   A 1 127 ? 19.907 -4.586  -1.107  0.50 12.80 ?  127 LEU   A HA   1 
ATOM   2768 H  HB2  A LEU   A 1 127 ? 20.734 -7.607  -1.490  0.50 12.88 ?  127 LEU   A HB2  1 
ATOM   2769 H  HB2  B LEU   A 1 127 ? 21.022 -7.144  -1.517  0.50 13.75 ?  127 LEU   A HB2  1 
ATOM   2770 H  HB3  A LEU   A 1 127 ? 21.710 -6.456  -1.969  0.50 12.88 ?  127 LEU   A HB3  1 
ATOM   2771 H  HB3  B LEU   A 1 127 ? 21.742 -5.808  -1.964  0.50 13.75 ?  127 LEU   A HB3  1 
ATOM   2772 H  HG   A LEU   A 1 127 ? 21.385 -7.286  0.706   0.50 13.26 ?  127 LEU   A HG   1 
ATOM   2773 H  HG   B LEU   A 1 127 ? 21.270 -6.466  0.735   0.50 15.09 ?  127 LEU   A HG   1 
ATOM   2774 H  HD11 A LEU   A 1 127 ? 23.560 -8.061  0.546   0.50 12.98 ?  127 LEU   A HD11 1 
ATOM   2775 H  HD11 B LEU   A 1 127 ? 23.533 -6.979  0.932   0.50 16.34 ?  127 LEU   A HD11 1 
ATOM   2776 H  HD12 A LEU   A 1 127 ? 22.672 -8.750  -0.577  0.50 12.98 ?  127 LEU   A HD12 1 
ATOM   2777 H  HD12 B LEU   A 1 127 ? 22.823 -7.963  -0.094  0.50 16.34 ?  127 LEU   A HD12 1 
ATOM   2778 H  HD13 A LEU   A 1 127 ? 23.641 -7.551  -0.957  0.50 12.98 ?  127 LEU   A HD13 1 
ATOM   2779 H  HD13 B LEU   A 1 127 ? 23.714 -6.762  -0.632  0.50 16.34 ?  127 LEU   A HD13 1 
ATOM   2780 H  HD21 A LEU   A 1 127 ? 23.181 -5.787  1.173   0.50 14.58 ?  127 LEU   A HD21 1 
ATOM   2781 H  HD21 B LEU   A 1 127 ? 22.777 -4.714  1.226   0.50 16.00 ?  127 LEU   A HD21 1 
ATOM   2782 H  HD22 A LEU   A 1 127 ? 22.950 -5.161  -0.269  0.50 14.58 ?  127 LEU   A HD22 1 
ATOM   2783 H  HD22 B LEU   A 1 127 ? 22.780 -4.329  -0.315  0.50 16.00 ?  127 LEU   A HD22 1 
ATOM   2784 H  HD23 A LEU   A 1 127 ? 21.811 -5.057  0.834   0.50 14.58 ?  127 LEU   A HD23 1 
ATOM   2785 H  HD23 B LEU   A 1 127 ? 21.446 -4.188  0.536   0.50 16.00 ?  127 LEU   A HD23 1 
ATOM   2786 N  N    A SER   A 1 128 ? 19.791 -4.474  -3.209  0.50 10.54 ?  128 SER   A N    1 
ATOM   2787 N  N    B SER   A 1 128 ? 19.817 -4.489  -3.590  0.50 10.83 ?  128 SER   A N    1 
ATOM   2788 C  CA   A SER   A 1 128 ? 19.408 -4.086  -4.560  0.50 10.26 ?  128 SER   A CA   1 
ATOM   2789 C  CA   B SER   A 1 128 ? 19.555 -4.261  -5.010  0.50 10.94 ?  128 SER   A CA   1 
ATOM   2790 C  C    A SER   A 1 128 ? 17.956 -3.642  -4.673  0.50 10.52 ?  128 SER   A C    1 
ATOM   2791 C  C    B SER   A 1 128 ? 18.155 -3.739  -5.322  0.50 11.23 ?  128 SER   A C    1 
ATOM   2792 O  O    A SER   A 1 128 ? 17.512 -3.330  -5.779  0.50 10.96 ?  128 SER   A O    1 
ATOM   2793 O  O    B SER   A 1 128 ? 17.877 -3.409  -6.477  0.50 11.90 ?  128 SER   A O    1 
ATOM   2794 C  CB   A SER   A 1 128 ? 19.759 -5.135  -5.625  0.50 10.27 ?  128 SER   A CB   1 
ATOM   2795 C  CB   B SER   A 1 128 ? 19.897 -5.487  -5.863  0.50 11.14 ?  128 SER   A CB   1 
ATOM   2796 O  OG   A SER   A 1 128 ? 21.168 -5.311  -5.687  0.50 10.38 ?  128 SER   A OG   1 
ATOM   2797 O  OG   B SER   A 1 128 ? 21.299 -5.673  -5.953  0.50 11.45 ?  128 SER   A OG   1 
ATOM   2798 H  H    A SER   A 1 128 ? 20.370 -3.928  -2.877  0.50 12.64 ?  128 SER   A H    1 
ATOM   2799 H  H    B SER   A 1 128 ? 20.361 -3.904  -3.263  0.50 12.99 ?  128 SER   A H    1 
ATOM   2800 H  HA   A SER   A 1 128 ? 19.931 -3.307  -4.781  0.50 12.30 ?  128 SER   A HA   1 
ATOM   2801 H  HA   B SER   A 1 128 ? 20.159 -3.566  -5.292  0.50 13.12 ?  128 SER   A HA   1 
ATOM   2802 H  HB2  A SER   A 1 128 ? 19.342 -5.978  -5.400  0.50 12.31 ?  128 SER   A HB2  1 
ATOM   2803 H  HB2  B SER   A 1 128 ? 19.499 -6.278  -5.475  0.50 13.36 ?  128 SER   A HB2  1 
ATOM   2804 H  HB3  A SER   A 1 128 ? 19.444 -4.826  -6.492  0.50 12.31 ?  128 SER   A HB3  1 
ATOM   2805 H  HB3  B SER   A 1 128 ? 19.559 -5.348  -6.761  0.50 13.36 ?  128 SER   A HB3  1 
ATOM   2806 H  HG   A SER   A 1 128 ? 21.541 -4.578  -5.872  0.50 12.44 ?  128 SER   A HG   1 
ATOM   2807 H  HG   B SER   A 1 128 ? 21.663 -4.985  -6.268  0.50 13.73 ?  128 SER   A HG   1 
ATOM   2808 N  N    A ALA   A 1 129 ? 17.211 -3.582  -3.572  0.50 10.92 ?  129 ALA   A N    1 
ATOM   2809 N  N    B ALA   A 1 129 ? 17.280 -3.646  -4.321  0.50 11.25 ?  129 ALA   A N    1 
ATOM   2810 C  CA   A ALA   A 1 129 ? 15.854 -3.052  -3.590  0.50 11.46 ?  129 ALA   A CA   1 
ATOM   2811 C  CA   B ALA   A 1 129 ? 15.938 -3.114  -4.529  0.50 12.14 ?  129 ALA   A CA   1 
ATOM   2812 C  C    A ALA   A 1 129 ? 15.910 -1.526  -3.514  0.50 11.45 ?  129 ALA   A C    1 
ATOM   2813 C  C    B ALA   A 1 129 ? 15.947 -1.589  -4.354  0.50 13.13 ?  129 ALA   A C    1 
ATOM   2814 O  O    A ALA   A 1 129 ? 16.976 -0.906  -3.579  0.50 11.84 ?  129 ALA   A O    1 
ATOM   2815 O  O    B ALA   A 1 129 ? 17.003 -0.949  -4.323  0.50 13.15 ?  129 ALA   A O    1 
ATOM   2816 C  CB   A ALA   A 1 129 ? 15.023 -3.665  -2.463  0.50 12.60 ?  129 ALA   A CB   1 
ATOM   2817 C  CB   B ALA   A 1 129 ? 14.937 -3.853  -3.638  0.50 13.03 ?  129 ALA   A CB   1 
ATOM   2818 H  H    A ALA   A 1 129 ? 17.469 -3.846  -2.794  0.50 13.09 ?  129 ALA   A H    1 
ATOM   2819 H  H    B ALA   A 1 129 ? 17.437 -3.894  -3.510  0.50 13.49 ?  129 ALA   A H    1 
ATOM   2820 H  HA   A ALA   A 1 129 ? 15.435 -3.290  -4.429  0.50 13.74 ?  129 ALA   A HA   1 
ATOM   2821 H  HA   B ALA   A 1 129 ? 15.682 -3.290  -5.446  0.50 14.56 ?  129 ALA   A HA   1 
ATOM   2822 H  HB1  A ALA   A 1 129 ? 14.122 -3.303  -2.502  0.50 15.11 ?  129 ALA   A HB1  1 
ATOM   2823 H  HB1  B ALA   A 1 129 ? 14.048 -3.494  -3.800  0.50 15.63 ?  129 ALA   A HB1  1 
ATOM   2824 H  HB2  A ALA   A 1 129 ? 14.999 -4.626  -2.573  0.50 15.11 ?  129 ALA   A HB2  1 
ATOM   2825 H  HB2  B ALA   A 1 129 ? 14.952 -4.799  -3.860  0.50 15.63 ?  129 ALA   A HB2  1 
ATOM   2826 H  HB3  A ALA   A 1 129 ? 15.430 -3.439  -1.610  0.50 15.11 ?  129 ALA   A HB3  1 
ATOM   2827 H  HB3  B ALA   A 1 129 ? 15.181 -3.728  -2.711  0.50 15.63 ?  129 ALA   A HB3  1 
ATOM   2828 N  N    A GLY   A 1 130 ? 14.749 -0.899  -3.377  0.50 12.22 ?  130 GLY   A N    1 
ATOM   2829 N  N    B GLY   A 1 130 ? 14.762 -0.988  -4.273  0.50 14.30 ?  130 GLY   A N    1 
ATOM   2830 C  CA   A GLY   A 1 130 ? 14.737 0.548   -3.294  0.50 13.80 ?  130 GLY   A CA   1 
ATOM   2831 C  CA   B GLY   A 1 130 ? 14.682 0.458   -4.128  0.50 14.82 ?  130 GLY   A CA   1 
ATOM   2832 C  C    A GLY   A 1 130 ? 15.272 1.164   -4.569  0.50 14.01 ?  130 GLY   A C    1 
ATOM   2833 C  C    B GLY   A 1 130 ? 15.406 1.158   -5.259  0.50 15.36 ?  130 GLY   A C    1 
ATOM   2834 O  O    A GLY   A 1 130 ? 14.975 0.711   -5.679  0.50 13.13 ?  130 GLY   A O    1 
ATOM   2835 O  O    B GLY   A 1 130 ? 15.257 0.799   -6.432  0.50 15.60 ?  130 GLY   A O    1 
ATOM   2836 H  H    A GLY   A 1 130 ? 13.975 -1.280  -3.343  0.50 14.66 ?  130 GLY   A H    1 
ATOM   2837 H  H    B GLY   A 1 130 ? 14.002 -1.388  -4.310  0.50 17.15 ?  130 GLY   A H    1 
ATOM   2838 H  HA2  A GLY   A 1 130 ? 13.829 0.858   -3.144  0.50 16.55 ?  130 GLY   A HA2  1 
ATOM   2839 H  HA2  B GLY   A 1 130 ? 13.751 0.734   -4.132  0.50 17.78 ?  130 GLY   A HA2  1 
ATOM   2840 H  HA3  A GLY   A 1 130 ? 15.292 0.835   -2.556  0.50 16.55 ?  130 GLY   A HA3  1 
ATOM   2841 H  HA3  B GLY   A 1 130 ? 15.084 0.726   -3.289  0.50 17.78 ?  130 GLY   A HA3  1 
ATOM   2842 N  N    A ILE   A 1 131 ? 16.092 2.203   -4.416  0.50 14.56 ?  131 ILE   A N    1 
ATOM   2843 N  N    B ILE   A 1 131 ? 16.217 2.164   -4.905  0.50 15.95 ?  131 ILE   A N    1 
ATOM   2844 C  CA   A ILE   A 1 131 ? 16.577 2.965   -5.564  0.50 13.69 ?  131 ILE   A CA   1 
ATOM   2845 C  CA   B ILE   A 1 131 ? 16.915 2.972   -5.899  0.50 15.39 ?  131 ILE   A CA   1 
ATOM   2846 C  C    A ILE   A 1 131 ? 17.599 2.188   -6.385  0.50 12.70 ?  131 ILE   A C    1 
ATOM   2847 C  C    B ILE   A 1 131 ? 17.897 2.170   -6.737  0.50 14.83 ?  131 ILE   A C    1 
ATOM   2848 O  O    A ILE   A 1 131 ? 18.055 2.681   -7.422  0.50 12.67 ?  131 ILE   A O    1 
ATOM   2849 O  O    B ILE   A 1 131 ? 18.338 2.661   -7.781  0.50 15.84 ?  131 ILE   A O    1 
ATOM   2850 C  CB   A ILE   A 1 131 ? 17.122 4.346   -5.153  0.50 14.41 ?  131 ILE   A CB   1 
ATOM   2851 C  CB   B ILE   A 1 131 ? 17.590 4.242   -5.307  0.50 15.76 ?  131 ILE   A CB   1 
ATOM   2852 C  CG1  A ILE   A 1 131 ? 18.385 4.212   -4.295  0.50 14.71 ?  131 ILE   A CG1  1 
ATOM   2853 C  CG1  B ILE   A 1 131 ? 18.753 3.898   -4.360  0.50 15.78 ?  131 ILE   A CG1  1 
ATOM   2854 C  CG2  A ILE   A 1 131 ? 16.040 5.134   -4.432  0.50 15.02 ?  131 ILE   A CG2  1 
ATOM   2855 C  CG2  B ILE   A 1 131 ? 16.562 5.131   -4.619  0.50 16.43 ?  131 ILE   A CG2  1 
ATOM   2856 C  CD1  A ILE   A 1 131 ? 19.053 5.541   -3.970  0.50 14.97 ?  131 ILE   A CD1  1 
ATOM   2857 C  CD1  B ILE   A 1 131 ? 19.448 5.135   -3.753  0.50 15.92 ?  131 ILE   A CD1  1 
ATOM   2858 H  H    A ILE   A 1 131 ? 16.367 2.490   -3.658  0.50 17.45 ?  131 ILE   A H    1 
ATOM   2859 H  H    B ILE   A 1 131 ? 16.375 2.392   -4.091  0.50 19.13 ?  131 ILE   A H    1 
ATOM   2860 H  HA   A ILE   A 1 131 ? 15.819 3.120   -6.152  0.50 16.42 ?  131 ILE   A HA   1 
ATOM   2861 H  HA   B ILE   A 1 131 ? 16.257 3.293   -6.522  0.50 18.46 ?  131 ILE   A HA   1 
ATOM   2862 H  HB   A ILE   A 1 131 ? 17.351 4.824   -5.962  0.50 17.28 ?  131 ILE   A HB   1 
ATOM   2863 H  HB   B ILE   A 1 131 ? 17.961 4.748   -6.046  0.50 18.90 ?  131 ILE   A HB   1 
ATOM   2864 H  HG12 A ILE   A 1 131 ? 18.147 3.781   -3.459  0.50 17.64 ?  131 ILE   A HG12 1 
ATOM   2865 H  HG12 B ILE   A 1 131 ? 18.417 3.364   -3.626  0.50 18.93 ?  131 ILE   A HG12 1 
ATOM   2866 H  HG13 A ILE   A 1 131 ? 19.031 3.666   -4.772  0.50 17.64 ?  131 ILE   A HG13 1 
ATOM   2867 H  HG13 B ILE   A 1 131 ? 19.427 3.402   -4.850  0.50 18.93 ?  131 ILE   A HG13 1 
ATOM   2868 H  HG21 A ILE   A 1 131 ? 16.372 6.023   -4.244  0.50 18.01 ?  131 ILE   A HG21 1 
ATOM   2869 H  HG21 B ILE   A 1 131 ? 16.791 6.061   -4.781  0.50 19.70 ?  131 ILE   A HG21 1 
ATOM   2870 H  HG22 A ILE   A 1 131 ? 15.258 5.187   -5.004  0.50 18.01 ?  131 ILE   A HG22 1 
ATOM   2871 H  HG22 B ILE   A 1 131 ? 15.686 4.938   -4.984  0.50 19.70 ?  131 ILE   A HG22 1 
ATOM   2872 H  HG23 A ILE   A 1 131 ? 15.815 4.680   -3.605  0.50 18.01 ?  131 ILE   A HG23 1 
ATOM   2873 H  HG23 B ILE   A 1 131 ? 16.573 4.951   -3.667  0.50 19.70 ?  131 ILE   A HG23 1 
ATOM   2874 H  HD11 A ILE   A 1 131 ? 19.903 5.366   -3.537  0.50 17.95 ?  131 ILE   A HD11 1 
ATOM   2875 H  HD11 B ILE   A 1 131 ? 20.234 4.850   -3.259  0.50 19.10 ?  131 ILE   A HD11 1 
ATOM   2876 H  HD12 A ILE   A 1 131 ? 19.196 6.032   -4.794  0.50 17.95 ?  131 ILE   A HD12 1 
ATOM   2877 H  HD12 B ILE   A 1 131 ? 19.709 5.737   -4.468  0.50 19.10 ?  131 ILE   A HD12 1 
ATOM   2878 H  HD13 A ILE   A 1 131 ? 18.477 6.047   -3.377  0.50 17.95 ?  131 ILE   A HD13 1 
ATOM   2879 H  HD13 B ILE   A 1 131 ? 18.831 5.586   -3.153  0.50 19.10 ?  131 ILE   A HD13 1 
ATOM   2880 N  N    A PHE   A 1 132 ? 17.964 0.979   -5.941  0.50 12.31 ?  132 PHE   A N    1 
ATOM   2881 N  N    B PHE   A 1 132 ? 18.250 0.950   -6.316  0.50 13.06 ?  132 PHE   A N    1 
ATOM   2882 C  CA   A PHE   A 1 132 ? 18.832 0.114   -6.734  0.50 12.37 ?  132 PHE   A CA   1 
ATOM   2883 C  CA   B PHE   A 1 132 ? 19.142 0.114   -7.113  0.50 12.62 ?  132 PHE   A CA   1 
ATOM   2884 C  C    A PHE   A 1 132 ? 18.075 -0.648  -7.823  0.50 12.62 ?  132 PHE   A C    1 
ATOM   2885 C  C    B PHE   A 1 132 ? 18.420 -0.637  -8.234  0.50 13.16 ?  132 PHE   A C    1 
ATOM   2886 O  O    A PHE   A 1 132 ? 18.708 -1.274  -8.679  0.50 13.52 ?  132 PHE   A O    1 
ATOM   2887 O  O    B PHE   A 1 132 ? 19.088 -1.235  -9.086  0.50 14.09 ?  132 PHE   A O    1 
ATOM   2888 C  CB   A PHE   A 1 132 ? 19.591 -0.859  -5.827  0.50 12.34 ?  132 PHE   A CB   1 
ATOM   2889 C  CB   B PHE   A 1 132 ? 19.932 -0.860  -6.223  0.50 11.51 ?  132 PHE   A CB   1 
ATOM   2890 C  CG   A PHE   A 1 132 ? 20.802 -0.260  -5.152  0.50 11.97 ?  132 PHE   A CG   1 
ATOM   2891 C  CG   B PHE   A 1 132 ? 21.130 -0.237  -5.526  0.50 11.56 ?  132 PHE   A CG   1 
ATOM   2892 C  CD1  A PHE   A 1 132 ? 20.669 0.766   -4.229  0.50 12.55 ?  132 PHE   A CD1  1 
ATOM   2893 C  CD1  B PHE   A 1 132 ? 20.974 0.793   -4.611  0.50 12.29 ?  132 PHE   A CD1  1 
ATOM   2894 C  CD2  A PHE   A 1 132 ? 22.072 -0.756  -5.416  0.50 12.12 ?  132 PHE   A CD2  1 
ATOM   2895 C  CD2  B PHE   A 1 132 ? 22.413 -0.715  -5.766  0.50 12.33 ?  132 PHE   A CD2  1 
ATOM   2896 C  CE1  A PHE   A 1 132 ? 21.781 1.308   -3.604  0.50 12.36 ?  132 PHE   A CE1  1 
ATOM   2897 C  CE1  B PHE   A 1 132 ? 22.075 1.352   -3.969  0.50 12.80 ?  132 PHE   A CE1  1 
ATOM   2898 C  CE2  A PHE   A 1 132 ? 23.186 -0.225  -4.787  0.50 12.26 ?  132 PHE   A CE2  1 
ATOM   2899 C  CE2  B PHE   A 1 132 ? 23.512 -0.161  -5.126  0.50 13.30 ?  132 PHE   A CE2  1 
ATOM   2900 C  CZ   A PHE   A 1 132 ? 23.040 0.809   -3.879  0.50 12.09 ?  132 PHE   A CZ   1 
ATOM   2901 C  CZ   B PHE   A 1 132 ? 23.341 0.868   -4.224  0.50 13.30 ?  132 PHE   A CZ   1 
ATOM   2902 H  H    A PHE   A 1 132 ? 17.723 0.634   -5.185  0.50 14.76 ?  132 PHE   A H    1 
ATOM   2903 H  H    B PHE   A 1 132 ? 17.996 0.588   -5.573  0.50 15.66 ?  132 PHE   A H    1 
ATOM   2904 H  HA   A PHE   A 1 132 ? 19.491 0.664   -7.176  0.50 14.84 ?  132 PHE   A HA   1 
ATOM   2905 H  HA   B PHE   A 1 132 ? 19.795 0.687   -7.534  0.50 15.13 ?  132 PHE   A HA   1 
ATOM   2906 H  HB2  A PHE   A 1 132 ? 18.992 -1.168  -5.127  0.50 14.79 ?  132 PHE   A HB2  1 
ATOM   2907 H  HB2  B PHE   A 1 132 ? 19.347 -1.210  -5.533  0.50 13.80 ?  132 PHE   A HB2  1 
ATOM   2908 H  HB3  A PHE   A 1 132 ? 19.892 -1.615  -6.356  0.50 14.79 ?  132 PHE   A HB3  1 
ATOM   2909 H  HB3  B PHE   A 1 132 ? 20.264 -1.594  -6.769  0.50 13.80 ?  132 PHE   A HB3  1 
ATOM   2910 H  HD1  A PHE   A 1 132 ? 19.826 1.105   -4.038  0.50 15.05 ?  132 PHE   A HD1  1 
ATOM   2911 H  HD1  B PHE   A 1 132 ? 20.125 1.120   -4.430  0.50 14.74 ?  132 PHE   A HD1  1 
ATOM   2912 H  HD2  A PHE   A 1 132 ? 22.175 -1.451  -6.028  0.50 14.53 ?  132 PHE   A HD2  1 
ATOM   2913 H  HD2  B PHE   A 1 132 ? 22.543 -1.410  -6.369  0.50 14.79 ?  132 PHE   A HD2  1 
ATOM   2914 H  HE1  A PHE   A 1 132 ? 21.681 2.000   -2.992  0.50 14.82 ?  132 PHE   A HE1  1 
ATOM   2915 H  HE1  B PHE   A 1 132 ? 21.956 2.046   -3.359  0.50 15.34 ?  132 PHE   A HE1  1 
ATOM   2916 H  HE2  A PHE   A 1 132 ? 24.035 -0.559  -4.983  0.50 14.70 ?  132 PHE   A HE2  1 
ATOM   2917 H  HE2  B PHE   A 1 132 ? 24.370 -0.487  -5.301  0.50 15.95 ?  132 PHE   A HE2  1 
ATOM   2918 H  HZ   A PHE   A 1 132 ? 23.790 1.170   -3.463  0.50 14.50 ?  132 PHE   A HZ   1 
ATOM   2919 H  HZ   B PHE   A 1 132 ? 24.081 1.243   -3.795  0.50 15.95 ?  132 PHE   A HZ   1 
ATOM   2920 N  N    A GLY   A 1 133 ? 16.743 -0.622  -7.811  0.50 12.72 ?  133 GLY   A N    1 
ATOM   2921 N  N    B GLY   A 1 133 ? 17.087 -0.630  -8.258  0.50 13.25 ?  133 GLY   A N    1 
ATOM   2922 C  CA   A GLY   A 1 133 ? 15.960 -1.010  -8.966  0.50 13.48 ?  133 GLY   A CA   1 
ATOM   2923 C  CA   B GLY   A 1 133 ? 16.350 -0.992  -9.449  0.50 13.98 ?  133 GLY   A CA   1 
ATOM   2924 C  C    A GLY   A 1 133 ? 15.610 -2.480  -9.119  0.50 14.33 ?  133 GLY   A C    1 
ATOM   2925 C  C    B GLY   A 1 133 ? 15.738 -2.379  -9.498  0.50 14.61 ?  133 GLY   A C    1 
ATOM   2926 O  O    A GLY   A 1 133 ? 14.854 -2.812  -10.038 0.50 15.64 ?  133 GLY   A O    1 
ATOM   2927 O  O    B GLY   A 1 133 ? 14.970 -2.640  -10.429 0.50 15.54 ?  133 GLY   A O    1 
ATOM   2928 H  H    A GLY   A 1 133 ? 16.269 -0.381  -7.138  0.50 15.25 ?  133 GLY   A H    1 
ATOM   2929 H  H    B GLY   A 1 133 ? 16.594 -0.414  -7.591  0.50 15.89 ?  133 GLY   A H    1 
ATOM   2930 H  HA2  A GLY   A 1 133 ? 15.119 -0.540  -8.940  0.50 16.16 ?  133 GLY   A HA2  1 
ATOM   2931 H  HA2  B GLY   A 1 133 ? 15.634 -0.358  -9.573  0.50 16.76 ?  133 GLY   A HA2  1 
ATOM   2932 H  HA3  A GLY   A 1 133 ? 16.434 -0.732  -9.765  0.50 16.16 ?  133 GLY   A HA3  1 
ATOM   2933 H  HA3  B GLY   A 1 133 ? 16.942 -0.927  -10.214 0.50 16.76 ?  133 GLY   A HA3  1 
ATOM   2934 N  N    A ALA   A 1 134 ? 16.115 -3.374  -8.270  0.50 13.93 ?  134 ALA   A N    1 
ATOM   2935 N  N    B ALA   A 1 134 ? 16.046 -3.276  -8.561  0.50 14.58 ?  134 ALA   A N    1 
ATOM   2936 C  CA   A ALA   A 1 134 ? 15.801 -4.786  -8.443  0.50 14.08 ?  134 ALA   A CA   1 
ATOM   2937 C  CA   B ALA   A 1 134 ? 15.560 -4.648  -8.646  0.50 14.87 ?  134 ALA   A CA   1 
ATOM   2938 C  C    A ALA   A 1 134 ? 14.420 -5.101  -7.869  0.50 14.26 ?  134 ALA   A C    1 
ATOM   2939 C  C    B ALA   A 1 134 ? 14.284 -4.858  -7.828  0.50 14.84 ?  134 ALA   A C    1 
ATOM   2940 O  O    A ALA   A 1 134 ? 13.829 -4.315  -7.124  0.50 14.77 ?  134 ALA   A O    1 
ATOM   2941 O  O    B ALA   A 1 134 ? 13.921 -4.053  -6.968  0.50 15.56 ?  134 ALA   A O    1 
ATOM   2942 C  CB   A ALA   A 1 134 ? 16.864 -5.664  -7.782  0.50 14.23 ?  134 ALA   A CB   1 
ATOM   2943 C  CB   B ALA   A 1 134 ? 16.640 -5.641  -8.207  0.50 15.30 ?  134 ALA   A CB   1 
ATOM   2944 H  H    A ALA   A 1 134 ? 16.622 -3.191  -7.598  0.50 16.71 ?  134 ALA   A H    1 
ATOM   2945 H  H    B ALA   A 1 134 ? 16.550 -3.115  -7.873  0.50 17.48 ?  134 ALA   A H    1 
ATOM   2946 H  HA   A ALA   A 1 134 ? 15.794 -4.998  -9.392  0.50 16.88 ?  134 ALA   A HA   1 
ATOM   2947 H  HA   B ALA   A 1 134 ? 15.355 -4.835  -9.573  0.50 17.84 ?  134 ALA   A HA   1 
ATOM   2948 H  HB1  A ALA   A 1 134 ? 16.640 -6.597  -7.931  0.50 17.07 ?  134 ALA   A HB1  1 
ATOM   2949 H  HB1  B ALA   A 1 134 ? 16.294 -6.540  -8.310  0.50 18.35 ?  134 ALA   A HB1  1 
ATOM   2950 H  HB2  A ALA   A 1 134 ? 17.732 -5.469  -8.176  0.50 17.07 ?  134 ALA   A HB2  1 
ATOM   2951 H  HB2  B ALA   A 1 134 ? 17.422 -5.521  -8.770  0.50 18.35 ?  134 ALA   A HB2  1 
ATOM   2952 H  HB3  A ALA   A 1 134 ? 16.884 -5.477  -6.832  0.50 17.07 ?  134 ALA   A HB3  1 
ATOM   2953 H  HB3  B ALA   A 1 134 ? 16.867 -5.473  -7.282  0.50 18.35 ?  134 ALA   A HB3  1 
ATOM   2954 N  N    A ASP   A 1 135 ? 13.907 -6.271  -8.229  0.50 14.53 ?  135 ASP   A N    1 
ATOM   2955 N  N    B ASP   A 1 135 ? 13.609 -5.970  -8.115  0.50 15.28 ?  135 ASP   A N    1 
ATOM   2956 C  CA   A ASP   A 1 135 ? 12.637 -6.740  -7.685  0.50 14.79 ?  135 ASP   A CA   1 
ATOM   2957 C  CA   B ASP   A 1 135 ? 12.351 -6.319  -7.458  0.50 15.68 ?  135 ASP   A CA   1 
ATOM   2958 C  C    A ASP   A 1 135 ? 12.852 -7.192  -6.246  0.50 14.44 ?  135 ASP   A C    1 
ATOM   2959 C  C    B ASP   A 1 135 ? 12.641 -6.879  -6.070  0.50 14.79 ?  135 ASP   A C    1 
ATOM   2960 O  O    A ASP   A 1 135 ? 13.631 -8.125  -6.011  0.50 14.04 ?  135 ASP   A O    1 
ATOM   2961 O  O    B ASP   A 1 135 ? 13.384 -7.863  -5.955  0.50 14.52 ?  135 ASP   A O    1 
ATOM   2962 C  CB   A ASP   A 1 135 ? 12.124 -7.902  -8.535  0.50 15.99 ?  135 ASP   A CB   1 
ATOM   2963 C  CB   B ASP   A 1 135 ? 11.634 -7.370  -8.302  0.50 17.43 ?  135 ASP   A CB   1 
ATOM   2964 C  CG   A ASP   A 1 135 ? 10.836 -8.525  -8.001  0.50 17.50 ?  135 ASP   A CG   1 
ATOM   2965 C  CG   B ASP   A 1 135 ? 10.292 -7.802  -7.718  0.50 19.12 ?  135 ASP   A CG   1 
ATOM   2966 O  OD1  A ASP   A 1 135 ? 10.236 -8.008  -7.036  0.50 17.69 ?  135 ASP   A OD1  1 
ATOM   2967 O  OD1  B ASP   A 1 135 ? 9.936  -7.372  -6.600  0.50 19.46 ?  135 ASP   A OD1  1 
ATOM   2968 O  OD2  A ASP   A 1 135 ? 10.420 -9.555  -8.568  0.50 19.56 -1 135 ASP   A OD2  1 
ATOM   2969 O  OD2  B ASP   A 1 135 ? 9.592  -8.588  -8.391  0.50 20.38 -1 135 ASP   A OD2  1 
ATOM   2970 H  H    A ASP   A 1 135 ? 14.277 -6.811  -8.789  0.50 17.42 ?  135 ASP   A H    1 
ATOM   2971 H  H    B ASP   A 1 135 ? 13.862 -6.544  -8.695  0.50 18.33 ?  135 ASP   A H    1 
ATOM   2972 H  HA   A ASP   A 1 135 ? 11.996 -6.019  -7.715  0.50 17.74 ?  135 ASP   A HA   1 
ATOM   2973 H  HA   B ASP   A 1 135 ? 11.783 -5.529  -7.394  0.50 18.80 ?  135 ASP   A HA   1 
ATOM   2974 H  HB2  A ASP   A 1 135 ? 11.951 -7.579  -9.431  0.50 19.18 ?  135 ASP   A HB2  1 
ATOM   2975 H  HB2  B ASP   A 1 135 ? 11.482 -7.008  -9.191  0.50 20.91 ?  135 ASP   A HB2  1 
ATOM   2976 H  HB3  A ASP   A 1 135 ? 12.795 -8.598  -8.552  0.50 19.18 ?  135 ASP   A HB3  1 
ATOM   2977 H  HB3  B ASP   A 1 135 ? 12.191 -8.158  -8.357  0.50 20.91 ?  135 ASP   A HB3  1 
ATOM   2978 N  N    A PRO   A 1 136 ? 12.197 -6.577  -5.261  0.50 14.49 ?  136 PRO   A N    1 
ATOM   2979 N  N    B PRO   A 1 136 ? 12.091 -6.297  -4.999  0.50 14.58 ?  136 PRO   A N    1 
ATOM   2980 C  CA   A PRO   A 1 136 ? 12.421 -6.992  -3.865  0.50 14.55 ?  136 PRO   A CA   1 
ATOM   2981 C  CA   B PRO   A 1 136 ? 12.373 -6.829  -3.654  0.50 14.83 ?  136 PRO   A CA   1 
ATOM   2982 C  C    A PRO   A 1 136 ? 11.988 -8.416  -3.565  0.50 14.30 ?  136 PRO   A C    1 
ATOM   2983 C  C    B PRO   A 1 136 ? 11.937 -8.272  -3.453  0.50 14.67 ?  136 PRO   A C    1 
ATOM   2984 O  O    A PRO   A 1 136 ? 12.606 -9.066  -2.714  0.50 14.15 ?  136 PRO   A O    1 
ATOM   2985 O  O    B PRO   A 1 136 ? 12.492 -8.958  -2.585  0.50 14.09 ?  136 PRO   A O    1 
ATOM   2986 C  CB   A PRO   A 1 136 ? 11.615 -5.965  -3.059  0.50 15.27 ?  136 PRO   A CB   1 
ATOM   2987 C  CB   B PRO   A 1 136 ? 11.625 -5.861  -2.724  0.50 15.73 ?  136 PRO   A CB   1 
ATOM   2988 C  CG   A PRO   A 1 136 ? 10.585 -5.459  -4.015  0.50 15.80 ?  136 PRO   A CG   1 
ATOM   2989 C  CG   B PRO   A 1 136 ? 10.609 -5.189  -3.592  0.50 16.34 ?  136 PRO   A CG   1 
ATOM   2990 C  CD   A PRO   A 1 136 ? 11.226 -5.476  -5.365  0.50 15.06 ?  136 PRO   A CD   1 
ATOM   2991 C  CD   B PRO   A 1 136 ? 11.239 -5.095  -4.945  0.50 14.91 ?  136 PRO   A CD   1 
ATOM   2992 H  HA   A PRO   A 1 136 ? 13.363 -6.905  -3.636  0.50 17.45 ?  136 PRO   A HA   1 
ATOM   2993 H  HA   B PRO   A 1 136 ? 13.324 -6.760  -3.468  0.50 17.78 ?  136 PRO   A HA   1 
ATOM   2994 H  HB2  A PRO   A 1 136 ? 11.202 -6.403  -2.298  0.50 18.31 ?  136 PRO   A HB2  1 
ATOM   2995 H  HB2  B PRO   A 1 136 ? 11.196 -6.357  -2.011  0.50 18.86 ?  136 PRO   A HB2  1 
ATOM   2996 H  HB3  A PRO   A 1 136 ? 12.205 -5.251  -2.767  0.50 18.31 ?  136 PRO   A HB3  1 
ATOM   2997 H  HB3  B PRO   A 1 136 ? 12.248 -5.210  -2.360  0.50 18.86 ?  136 PRO   A HB3  1 
ATOM   2998 H  HG2  A PRO   A 1 136 ? 9.814  -6.044  -3.997  0.50 18.95 ?  136 PRO   A HG2  1 
ATOM   2999 H  HG2  B PRO   A 1 136 ? 9.804  -5.729  -3.629  0.50 19.60 ?  136 PRO   A HG2  1 
ATOM   3000 H  HG3  A PRO   A 1 136 ? 10.339 -4.555  -3.771  0.50 18.95 ?  136 PRO   A HG3  1 
ATOM   3001 H  HG3  B PRO   A 1 136 ? 10.414 -4.305  -3.246  0.50 19.60 ?  136 PRO   A HG3  1 
ATOM   3002 H  HD2  A PRO   A 1 136 ? 10.570 -5.682  -6.050  0.50 18.06 ?  136 PRO   A HD2  1 
ATOM   3003 H  HD2  B PRO   A 1 136 ? 10.557 -5.130  -5.636  0.50 17.88 ?  136 PRO   A HD2  1 
ATOM   3004 H  HD3  A PRO   A 1 136 ? 11.681 -4.640  -5.546  0.50 18.06 ?  136 PRO   A HD3  1 
ATOM   3005 H  HD3  B PRO   A 1 136 ? 11.775 -4.288  -5.018  0.50 17.88 ?  136 PRO   A HD3  1 
ATOM   3006 N  N    A ILE   A 1 137 ? 10.934 -8.921  -4.212  0.50 14.83 ?  137 ILE   A N    1 
ATOM   3007 N  N    B ILE   A 1 137 ? 10.943 -8.749  -4.206  0.50 15.42 ?  137 ILE   A N    1 
ATOM   3008 C  CA   A ILE   A 1 137 ? 10.569 -10.323 -4.021  0.50 15.06 ?  137 ILE   A CA   1 
ATOM   3009 C  CA   B ILE   A 1 137 ? 10.534 -10.150 -4.102  0.50 15.94 ?  137 ILE   A CA   1 
ATOM   3010 C  C    A ILE   A 1 137 ? 11.728 -11.224 -4.424  0.50 14.37 ?  137 ILE   A C    1 
ATOM   3011 C  C    B ILE   A 1 137 ? 11.691 -11.066 -4.490  0.50 15.82 ?  137 ILE   A C    1 
ATOM   3012 O  O    A ILE   A 1 137 ? 12.058 -12.195 -3.728  0.50 14.22 ?  137 ILE   A O    1 
ATOM   3013 O  O    B ILE   A 1 137 ? 11.982 -12.060 -3.810  0.50 16.24 ?  137 ILE   A O    1 
ATOM   3014 C  CB   A ILE   A 1 137 ? 9.276  -10.658 -4.790  0.50 16.29 ?  137 ILE   A CB   1 
ATOM   3015 C  CB   B ILE   A 1 137 ? 9.280  -10.407 -4.960  0.50 16.94 ?  137 ILE   A CB   1 
ATOM   3016 C  CG1  A ILE   A 1 137 ? 8.102  -9.842  -4.238  0.50 17.85 ?  137 ILE   A CG1  1 
ATOM   3017 C  CG1  B ILE   A 1 137 ? 8.129  -9.485  -4.524  0.50 18.10 ?  137 ILE   A CG1  1 
ATOM   3018 C  CG2  A ILE   A 1 137 ? 8.972  -12.150 -4.698  0.50 16.69 ?  137 ILE   A CG2  1 
ATOM   3019 C  CG2  B ILE   A 1 137 ? 8.864  -11.867 -4.866  0.50 17.46 ?  137 ILE   A CG2  1 
ATOM   3020 C  CD1  A ILE   A 1 137 ? 6.801  -10.047 -4.977  0.50 18.83 ?  137 ILE   A CD1  1 
ATOM   3021 C  CD1  B ILE   A 1 137 ? 6.874  -9.608  -5.370  0.50 18.90 ?  137 ILE   A CD1  1 
ATOM   3022 H  H    A ILE   A 1 137 ? 10.428 -8.486  -4.752  0.50 17.78 ?  137 ILE   A H    1 
ATOM   3023 H  H    B ILE   A 1 137 ? 10.488 -8.282  -4.766  0.50 18.49 ?  137 ILE   A H    1 
ATOM   3024 H  HA   A ILE   A 1 137 ? 10.396 -10.477 -3.082  0.50 18.06 ?  137 ILE   A HA   1 
ATOM   3025 H  HA   B ILE   A 1 137 ? 10.307 -10.341 -3.181  0.50 19.12 ?  137 ILE   A HA   1 
ATOM   3026 H  HB   A ILE   A 1 137 ? 9.396  -10.426 -5.721  0.50 19.54 ?  137 ILE   A HB   1 
ATOM   3027 H  HB   B ILE   A 1 137 ? 9.493  -10.209 -5.883  0.50 20.32 ?  137 ILE   A HB   1 
ATOM   3028 H  HG12 A ILE   A 1 137 ? 7.958  -10.085 -3.310  0.50 21.41 ?  137 ILE   A HG12 1 
ATOM   3029 H  HG12 B ILE   A 1 137 ? 7.891  -9.698  -3.608  0.50 21.71 ?  137 ILE   A HG12 1 
ATOM   3030 H  HG13 A ILE   A 1 137 ? 8.327  -8.896  -4.294  0.50 21.41 ?  137 ILE   A HG13 1 
ATOM   3031 H  HG13 B ILE   A 1 137 ? 8.427  -8.564  -4.579  0.50 21.71 ?  137 ILE   A HG13 1 
ATOM   3032 H  HG21 A ILE   A 1 137 ? 8.196  -12.353 -5.243  0.50 20.02 ?  137 ILE   A HG21 1 
ATOM   3033 H  HG21 B ILE   A 1 137 ? 8.044  -11.999 -5.368  0.50 20.94 ?  137 ILE   A HG21 1 
ATOM   3034 H  HG22 A ILE   A 1 137 ? 9.725  -12.656 -5.024  0.50 20.02 ?  137 ILE   A HG22 1 
ATOM   3035 H  HG22 B ILE   A 1 137 ? 9.564  -12.422 -5.239  0.50 20.94 ?  137 ILE   A HG22 1 
ATOM   3036 H  HG23 A ILE   A 1 137 ? 8.792  -12.375 -3.772  0.50 20.02 ?  137 ILE   A HG23 1 
ATOM   3037 H  HG23 B ILE   A 1 137 ? 8.720  -12.094 -3.934  0.50 20.94 ?  137 ILE   A HG23 1 
ATOM   3038 H  HD11 A ILE   A 1 137 ? 6.094  -9.671  -4.438  0.50 22.59 ?  137 ILE   A HD11 1 
ATOM   3039 H  HD11 B ILE   A 1 137 ? 6.282  -8.867  -5.167  0.50 22.66 ?  137 ILE   A HD11 1 
ATOM   3040 H  HD12 A ILE   A 1 137 ? 6.848  -9.594  -5.835  0.50 22.59 ?  137 ILE   A HD12 1 
ATOM   3041 H  HD12 B ILE   A 1 137 ? 7.121  -9.587  -6.308  0.50 22.66 ?  137 ILE   A HD12 1 
ATOM   3042 H  HD13 A ILE   A 1 137 ? 6.636  -10.991 -5.108  0.50 22.59 ?  137 ILE   A HD13 1 
ATOM   3043 H  HD13 B ILE   A 1 137 ? 6.433  -10.448 -5.163  0.50 22.66 ?  137 ILE   A HD13 1 
ATOM   3044 N  N    A HIS   A 1 138 ? 12.364 -10.919 -5.556  0.50 14.42 ?  138 HIS   A N    1 
ATOM   3045 N  N    B HIS   A 1 138 ? 12.366 -10.744 -5.594  0.50 15.78 ?  138 HIS   A N    1 
ATOM   3046 C  CA   A HIS   A 1 138 ? 13.552 -11.667 -5.949  0.50 14.38 ?  138 HIS   A CA   1 
ATOM   3047 C  CA   B HIS   A 1 138 ? 13.518 -11.533 -6.017  0.50 15.53 ?  138 HIS   A CA   1 
ATOM   3048 C  C    A HIS   A 1 138 ? 14.677 -11.489 -4.937  0.50 13.63 ?  138 HIS   A C    1 
ATOM   3049 C  C    B HIS   A 1 138 ? 14.650 -11.454 -4.996  0.50 14.49 ?  138 HIS   A C    1 
ATOM   3050 O  O    A HIS   A 1 138 ? 15.351 -12.461 -4.573  0.50 13.74 ?  138 HIS   A O    1 
ATOM   3051 O  O    B HIS   A 1 138 ? 15.288 -12.465 -4.677  0.50 14.87 ?  138 HIS   A O    1 
ATOM   3052 C  CB   A HIS   A 1 138 ? 14.007 -11.248 -7.345  0.50 15.18 ?  138 HIS   A CB   1 
ATOM   3053 C  CB   B HIS   A 1 138 ? 13.980 -11.042 -7.388  0.50 16.34 ?  138 HIS   A CB   1 
ATOM   3054 C  CG   A HIS   A 1 138 ? 15.263 -11.929 -7.791  0.50 15.85 ?  138 HIS   A CG   1 
ATOM   3055 C  CG   B HIS   A 1 138 ? 15.259 -11.659 -7.850  0.50 17.30 ?  138 HIS   A CG   1 
ATOM   3056 N  ND1  A HIS   A 1 138 ? 15.339 -13.291 -7.993  0.50 16.53 ?  138 HIS   A ND1  1 
ATOM   3057 N  ND1  B HIS   A 1 138 ? 15.368 -12.993 -8.176  0.50 18.12 ?  138 HIS   A ND1  1 
ATOM   3058 C  CD2  A HIS   A 1 138 ? 16.496 -11.439 -8.059  0.50 15.98 ?  138 HIS   A CD2  1 
ATOM   3059 C  CD2  B HIS   A 1 138 ? 16.488 -11.123 -8.037  0.50 17.58 ?  138 HIS   A CD2  1 
ATOM   3060 C  CE1  A HIS   A 1 138 ? 16.564 -13.608 -8.374  0.50 16.62 ?  138 HIS   A CE1  1 
ATOM   3061 C  CE1  B HIS   A 1 138 ? 16.610 -13.253 -8.543  0.50 18.13 ?  138 HIS   A CE1  1 
ATOM   3062 N  NE2  A HIS   A 1 138 ? 17.286 -12.503 -8.420  0.50 16.35 ?  138 HIS   A NE2  1 
ATOM   3063 N  NE2  B HIS   A 1 138 ? 17.310 -12.135 -8.468  0.50 18.03 ?  138 HIS   A NE2  1 
ATOM   3064 H  H    A HIS   A 1 138 ? 12.128 -10.297 -6.104  0.50 17.29 ?  138 HIS   A H    1 
ATOM   3065 H  H    B HIS   A 1 138 ? 12.178 -10.081 -6.112  0.50 18.93 ?  138 HIS   A H    1 
ATOM   3066 H  HA   A HIS   A 1 138 ? 13.328 -12.608 -5.985  0.50 17.24 ?  138 HIS   A HA   1 
ATOM   3067 H  HA   B HIS   A 1 138 ? 13.252 -12.460 -6.104  0.50 18.62 ?  138 HIS   A HA   1 
ATOM   3068 H  HB2  A HIS   A 1 138 ? 13.308 -11.469 -7.984  0.50 18.21 ?  138 HIS   A HB2  1 
ATOM   3069 H  HB2  B HIS   A 1 138 ? 13.294 -11.255 -8.044  0.50 19.60 ?  138 HIS   A HB2  1 
ATOM   3070 H  HB3  A HIS   A 1 138 ? 14.168 -10.293 -7.352  0.50 18.21 ?  138 HIS   A HB3  1 
ATOM   3071 H  HB3  B HIS   A 1 138 ? 14.109 -10.082 -7.352  0.50 19.60 ?  138 HIS   A HB3  1 
ATOM   3072 H  HD1  A HIS   A 1 138 ? 14.692 -13.847 -7.892  0.50 19.82 ?  138 HIS   A HD1  1 
ATOM   3073 H  HD2  A HIS   A 1 138 ? 16.757 -10.547 -8.009  0.50 19.17 ?  138 HIS   A HD2  1 
ATOM   3074 H  HD2  B HIS   A 1 138 ? 16.728 -10.236 -7.899  0.50 21.09 ?  138 HIS   A HD2  1 
ATOM   3075 H  HE1  A HIS   A 1 138 ? 16.868 -14.463 -8.575  0.50 19.93 ?  138 HIS   A HE1  1 
ATOM   3076 H  HE1  B HIS   A 1 138 ? 16.935 -14.082 -8.811  0.50 21.75 ?  138 HIS   A HE1  1 
ATOM   3077 H  HE2  B HIS   A 1 138 ? 18.143 -12.054 -8.659  0.50 21.63 ?  138 HIS   A HE2  1 
ATOM   3078 N  N    . SER   A 1 139 ? 14.903 -10.257 -4.466  1.00 13.22 ?  139 SER   A N    1 
ATOM   3079 C  CA   . SER   A 1 139 ? 15.974 -10.068 -3.498  1.00 12.92 ?  139 SER   A CA   1 
ATOM   3080 C  C    . SER   A 1 139 ? 15.746 -10.911 -2.249  1.00 12.48 ?  139 SER   A C    1 
ATOM   3081 O  O    . SER   A 1 139 ? 16.690 -11.495 -1.705  1.00 12.59 ?  139 SER   A O    1 
ATOM   3082 C  CB   . SER   A 1 139 ? 16.094 -8.588  -3.139  1.00 12.97 ?  139 SER   A CB   1 
ATOM   3083 O  OG   . SER   A 1 139 ? 17.173 -8.400  -2.243  1.00 13.04 ?  139 SER   A OG   1 
ATOM   3084 H  H    A SER   A 1 139 ? 14.469 -9.549  -4.680  0.50 15.85 ?  139 SER   A H    1 
ATOM   3085 H  H    B SER   A 1 139 ? 14.464 -9.543  -4.646  0.50 15.85 ?  139 SER   A H    1 
ATOM   3086 H  HA   . SER   A 1 139 ? 16.815 -10.347 -3.892  1.00 15.49 ?  139 SER   A HA   1 
ATOM   3087 H  HB2  . SER   A 1 139 ? 16.257 -8.072  -3.944  1.00 15.55 ?  139 SER   A HB2  1 
ATOM   3088 H  HB3  . SER   A 1 139 ? 15.274 -8.291  -2.711  1.00 15.55 ?  139 SER   A HB3  1 
ATOM   3089 H  HG   . SER   A 1 139 ? 17.247 -7.581  -2.039  1.00 15.64 ?  139 SER   A HG   1 
ATOM   3090 N  N    A LEU   A 1 140 ? 14.509 -10.952 -1.752  0.50 12.56 ?  140 LEU   A N    1 
ATOM   3091 N  N    B LEU   A 1 140 ? 14.495 -11.023 -1.806  0.50 12.76 ?  140 LEU   A N    1 
ATOM   3092 C  CA   A LEU   A 1 140 ? 14.229 -11.772 -0.577  0.50 12.13 ?  140 LEU   A CA   1 
ATOM   3093 C  CA   B LEU   A 1 140 ? 14.216 -11.836 -0.629  0.50 12.44 ?  140 LEU   A CA   1 
ATOM   3094 C  C    A LEU   A 1 140 ? 14.477 -13.246 -0.873  0.50 12.29 ?  140 LEU   A C    1 
ATOM   3095 C  C    B LEU   A 1 140 ? 14.521 -13.306 -0.889  0.50 12.45 ?  140 LEU   A C    1 
ATOM   3096 O  O    A LEU   A 1 140 ? 15.014 -13.977 -0.031  0.50 12.69 ?  140 LEU   A O    1 
ATOM   3097 O  O    B LEU   A 1 140 ? 15.100 -13.987 -0.033  0.50 12.76 ?  140 LEU   A O    1 
ATOM   3098 C  CB   A LEU   A 1 140 ? 12.790 -11.537 -0.106  0.50 12.32 ?  140 LEU   A CB   1 
ATOM   3099 C  CB   B LEU   A 1 140 ? 12.761 -11.656 -0.196  0.50 12.77 ?  140 LEU   A CB   1 
ATOM   3100 C  CG   A LEU   A 1 140 ? 12.284 -12.418 1.039   0.50 12.76 ?  140 LEU   A CG   1 
ATOM   3101 C  CG   B LEU   A 1 140 ? 12.350 -12.529 0.990   0.50 13.13 ?  140 LEU   A CG   1 
ATOM   3102 C  CD1  A LEU   A 1 140 ? 13.216 -12.351 2.240   0.50 13.34 ?  140 LEU   A CD1  1 
ATOM   3103 C  CD1  B LEU   A 1 140 ? 13.143 -12.150 2.231   0.50 13.39 ?  140 LEU   A CD1  1 
ATOM   3104 C  CD2  A LEU   A 1 140 ? 10.853 -12.019 1.432   0.50 12.97 ?  140 LEU   A CD2  1 
ATOM   3105 C  CD2  B LEU   A 1 140 ? 10.855 -12.404 1.243   0.50 13.81 ?  140 LEU   A CD2  1 
ATOM   3106 H  H    A LEU   A 1 140 ? 13.829 -10.521 -2.067  0.50 15.06 ?  140 LEU   A H    1 
ATOM   3107 H  H    B LEU   A 1 140 ? 13.805 -10.650 -2.164  0.50 15.30 ?  140 LEU   A H    1 
ATOM   3108 H  HA   A LEU   A 1 140 ? 14.818 -11.505 0.141   0.50 14.55 ?  140 LEU   A HA   1 
ATOM   3109 H  HA   B LEU   A 1 140 ? 14.779 -11.543 0.096   0.50 14.92 ?  140 LEU   A HA   1 
ATOM   3110 H  HB2  A LEU   A 1 140 ? 12.710 -10.617 0.192   0.50 14.78 ?  140 LEU   A HB2  1 
ATOM   3111 H  HB2  B LEU   A 1 140 ? 12.625 -10.730 0.062   0.50 15.32 ?  140 LEU   A HB2  1 
ATOM   3112 H  HB3  A LEU   A 1 140 ? 12.193 -11.679 -0.858  0.50 14.78 ?  140 LEU   A HB3  1 
ATOM   3113 H  HB3  B LEU   A 1 140 ? 12.179 -11.876 -0.941  0.50 15.32 ?  140 LEU   A HB3  1 
ATOM   3114 H  HG   A LEU   A 1 140 ? 12.249 -13.340 0.735   0.50 15.30 ?  140 LEU   A HG   1 
ATOM   3115 H  HG   B LEU   A 1 140 ? 12.532 -13.461 0.784   0.50 15.74 ?  140 LEU   A HG   1 
ATOM   3116 H  HD11 A LEU   A 1 140 ? 12.818 -12.849 2.974   0.50 15.99 ?  140 LEU   A HD11 1 
ATOM   3117 H  HD11 B LEU   A 1 140 ? 12.779 -12.632 2.990   0.50 16.05 ?  140 LEU   A HD11 1 
ATOM   3118 H  HD12 A LEU   A 1 140 ? 14.065 -12.745 1.997   0.50 15.99 ?  140 LEU   A HD12 1 
ATOM   3119 H  HD12 B LEU   A 1 140 ? 14.070 -12.393 2.098   0.50 16.05 ?  140 LEU   A HD12 1 
ATOM   3120 H  HD13 A LEU   A 1 140 ? 13.333 -11.425 2.494   0.50 15.99 ?  140 LEU   A HD13 1 
ATOM   3121 H  HD13 B LEU   A 1 140 ? 13.061 -11.196 2.374   0.50 16.05 ?  140 LEU   A HD13 1 
ATOM   3122 H  HD21 A LEU   A 1 140 ? 10.549 -12.592 2.157   0.50 15.55 ?  140 LEU   A HD21 1 
ATOM   3123 H  HD21 B LEU   A 1 140 ? 10.616 -12.972 1.992   0.50 16.56 ?  140 LEU   A HD21 1 
ATOM   3124 H  HD22 A LEU   A 1 140 ? 10.848 -11.094 1.721   0.50 15.55 ?  140 LEU   A HD22 1 
ATOM   3125 H  HD22 B LEU   A 1 140 ? 10.648 -11.480 1.446   0.50 16.56 ?  140 LEU   A HD22 1 
ATOM   3126 H  HD23 A LEU   A 1 140 ? 10.267 -12.128 0.664   0.50 15.55 ?  140 LEU   A HD23 1 
ATOM   3127 H  HD23 B LEU   A 1 140 ? 10.375 -12.685 0.448   0.50 16.56 ?  140 LEU   A HD23 1 
ATOM   3128 N  N    A ARG   A 1 141 ? 14.099 -13.698 -2.071  0.50 12.86 ?  141 ARG   A N    1 
ATOM   3129 N  N    B ARG   A 1 141 ? 14.135 -13.818 -2.060  0.50 12.78 ?  141 ARG   A N    1 
ATOM   3130 C  CA   A ARG   A 1 141 ? 14.355 -15.081 -2.461  0.50 13.65 ?  141 ARG   A CA   1 
ATOM   3131 C  CA   B ARG   A 1 141 ? 14.398 -15.222 -2.353  0.50 13.56 ?  141 ARG   A CA   1 
ATOM   3132 C  C    A ARG   A 1 141 ? 15.848 -15.396 -2.407  0.50 12.96 ?  141 ARG   A C    1 
ATOM   3133 C  C    B ARG   A 1 141 ? 15.895 -15.492 -2.444  0.50 13.34 ?  141 ARG   A C    1 
ATOM   3134 O  O    A ARG   A 1 141 ? 16.267 -16.381 -1.786  0.50 12.66 ?  141 ARG   A O    1 
ATOM   3135 O  O    B ARG   A 1 141 ? 16.371 -16.539 -1.989  0.50 13.12 ?  141 ARG   A O    1 
ATOM   3136 C  CB   A ARG   A 1 141 ? 13.793 -15.321 -3.865  0.50 14.78 ?  141 ARG   A CB   1 
ATOM   3137 C  CB   B ARG   A 1 141 ? 13.688 -15.643 -3.639  0.50 14.16 ?  141 ARG   A CB   1 
ATOM   3138 C  CG   A ARG   A 1 141 ? 13.813 -16.771 -4.325  0.50 16.83 ?  141 ARG   A CG   1 
ATOM   3139 C  CG   B ARG   A 1 141 ? 13.799 -17.138 -3.937  0.50 14.97 ?  141 ARG   A CG   1 
ATOM   3140 C  CD   A ARG   A 1 141 ? 12.792 -17.600 -3.573  0.50 18.10 ?  141 ARG   A CD   1 
ATOM   3141 C  CD   B ARG   A 1 141 ? 13.191 -17.983 -2.828  0.50 15.16 ?  141 ARG   A CD   1 
ATOM   3142 N  NE   A ARG   A 1 141 ? 13.399 -18.392 -2.511  0.50 18.55 ?  141 ARG   A NE   1 
ATOM   3143 N  NE   B ARG   A 1 141 ? 11.778 -17.675 -2.635  0.50 15.69 ?  141 ARG   A NE   1 
ATOM   3144 C  CZ   A ARG   A 1 141 ? 12.713 -18.964 -1.530  0.50 19.07 ?  141 ARG   A CZ   1 
ATOM   3145 C  CZ   B ARG   A 1 141 ? 11.020 -18.183 -1.673  0.50 16.11 ?  141 ARG   A CZ   1 
ATOM   3146 N  NH1  A ARG   A 1 141 ? 11.408 -18.791 -1.406  0.50 19.73 ?  141 ARG   A NH1  1 
ATOM   3147 N  NH1  B ARG   A 1 141 ? 11.506 -19.033 -0.781  0.50 16.52 ?  141 ARG   A NH1  1 
ATOM   3148 N  NH2  A ARG   A 1 141 ? 13.355 -19.719 -0.643  0.50 19.49 ?  141 ARG   A NH2  1 
ATOM   3149 N  NH2  B ARG   A 1 141 ? 9.737  -17.831 -1.606  0.50 16.24 ?  141 ARG   A NH2  1 
ATOM   3150 H  H    A ARG   A 1 141 ? 13.695 -13.226 -2.667  0.50 15.42 ?  141 ARG   A H    1 
ATOM   3151 H  H    B ARG   A 1 141 ? 13.736 -13.388 -2.688  0.50 15.33 ?  141 ARG   A H    1 
ATOM   3152 H  HA   A ARG   A 1 141 ? 13.897 -15.674 -1.845  0.50 16.37 ?  141 ARG   A HA   1 
ATOM   3153 H  HA   B ARG   A 1 141 ? 14.049 -15.757 -1.627  0.50 16.25 ?  141 ARG   A HA   1 
ATOM   3154 H  HB2  A ARG   A 1 141 ? 12.871 -15.021 -3.886  0.50 17.73 ?  141 ARG   A HB2  1 
ATOM   3155 H  HB2  B ARG   A 1 141 ? 12.745 -15.428 -3.563  0.50 16.98 ?  141 ARG   A HB2  1 
ATOM   3156 H  HB3  A ARG   A 1 141 ? 14.317 -14.812 -4.498  0.50 17.73 ?  141 ARG   A HB3  1 
ATOM   3157 H  HB3  B ARG   A 1 141 ? 14.076 -15.162 -4.387  0.50 16.98 ?  141 ARG   A HB3  1 
ATOM   3158 H  HG2  A ARG   A 1 141 ? 13.598 -16.816 -5.269  0.50 20.19 ?  141 ARG   A HG2  1 
ATOM   3159 H  HG2  B ARG   A 1 141 ? 13.328 -17.333 -4.764  0.50 17.96 ?  141 ARG   A HG2  1 
ATOM   3160 H  HG3  A ARG   A 1 141 ? 14.690 -17.156 -4.162  0.50 20.19 ?  141 ARG   A HG3  1 
ATOM   3161 H  HG3  B ARG   A 1 141 ? 14.737 -17.378 -4.027  0.50 17.96 ?  141 ARG   A HG3  1 
ATOM   3162 H  HD2  A ARG   A 1 141 ? 12.140 -17.010 -3.163  0.50 21.71 ?  141 ARG   A HD2  1 
ATOM   3163 H  HD2  B ARG   A 1 141 ? 13.259 -18.914 -3.070  0.50 18.18 ?  141 ARG   A HD2  1 
ATOM   3164 H  HD3  A ARG   A 1 141 ? 12.349 -18.204 -4.191  0.50 21.71 ?  141 ARG   A HD3  1 
ATOM   3165 H  HD3  B ARG   A 1 141 ? 13.659 -17.818 -1.995  0.50 18.18 ?  141 ARG   A HD3  1 
ATOM   3166 H  HE   A ARG   A 1 141 ? 14.234 -18.587 -2.582  0.50 22.25 ?  141 ARG   A HE   1 
ATOM   3167 H  HE   B ARG   A 1 141 ? 11.405 -17.132 -3.193  0.50 18.82 ?  141 ARG   A HE   1 
ATOM   3168 H  HH11 A ARG   A 1 141 ? 10.979 -18.313 -1.975  0.50 23.66 ?  141 ARG   A HH11 1 
ATOM   3169 H  HH11 B ARG   A 1 141 ? 12.331 -19.268 -0.817  0.50 19.81 ?  141 ARG   A HH11 1 
ATOM   3170 H  HH12 A ARG   A 1 141 ? 10.986 -19.169 -0.758  0.50 23.66 ?  141 ARG   A HH12 1 
ATOM   3171 H  HH12 B ARG   A 1 141 ? 10.992 -19.353 -0.171  0.50 19.81 ?  141 ARG   A HH12 1 
ATOM   3172 H  HH21 A ARG   A 1 141 ? 14.206 -19.836 -0.711  0.50 23.37 ?  141 ARG   A HH21 1 
ATOM   3173 H  HH21 B ARG   A 1 141 ? 9.410  -17.280 -2.181  0.50 19.48 ?  141 ARG   A HH21 1 
ATOM   3174 H  HH22 A ARG   A 1 141 ? 12.924 -20.086 0.005   0.50 23.37 ?  141 ARG   A HH22 1 
ATOM   3175 H  HH22 B ARG   A 1 141 ? 9.232  -18.156 -0.991  0.50 19.48 ?  141 ARG   A HH22 1 
ATOM   3176 N  N    A VAL   A 1 142 ? 16.671 -14.565 -3.053  0.50 12.45 ?  142 VAL   A N    1 
ATOM   3177 N  N    B VAL   A 1 142 ? 16.655 -14.565 -3.028  0.50 12.99 ?  142 VAL   A N    1 
ATOM   3178 C  CA   A VAL   A 1 142 ? 18.115 -14.802 -3.049  0.50 12.31 ?  142 VAL   A CA   1 
ATOM   3179 C  CA   B VAL   A 1 142 ? 18.105 -14.733 -3.067  0.50 13.04 ?  142 VAL   A CA   1 
ATOM   3180 C  C    A VAL   A 1 142 ? 18.664 -14.757 -1.628  0.50 11.96 ?  142 VAL   A C    1 
ATOM   3181 C  C    B VAL   A 1 142 ? 18.674 -14.725 -1.655  0.50 12.48 ?  142 VAL   A C    1 
ATOM   3182 O  O    A VAL   A 1 142 ? 19.525 -15.563 -1.254  0.50 12.18 ?  142 VAL   A O    1 
ATOM   3183 O  O    B VAL   A 1 142 ? 19.551 -15.528 -1.314  0.50 12.95 ?  142 VAL   A O    1 
ATOM   3184 C  CB   A VAL   A 1 142 ? 18.839 -13.816 -3.987  0.50 12.04 ?  142 VAL   A CB   1 
ATOM   3185 C  CB   B VAL   A 1 142 ? 18.755 -13.656 -3.956  0.50 13.29 ?  142 VAL   A CB   1 
ATOM   3186 C  CG1  A VAL   A 1 142 ? 20.352 -14.034 -3.936  0.50 11.38 ?  142 VAL   A CG1  1 
ATOM   3187 C  CG1  B VAL   A 1 142 ? 20.265 -13.813 -3.948  0.50 12.88 ?  142 VAL   A CG1  1 
ATOM   3188 C  CG2  A VAL   A 1 142 ? 18.335 -13.964 -5.416  0.50 13.26 ?  142 VAL   A CG2  1 
ATOM   3189 C  CG2  B VAL   A 1 142 ? 18.226 -13.742 -5.379  0.50 14.24 ?  142 VAL   A CG2  1 
ATOM   3190 H  H    A VAL   A 1 142 ? 16.423 -13.876 -3.500  0.50 14.93 ?  142 VAL   A H    1 
ATOM   3191 H  H    B VAL   A 1 142 ? 16.362 -13.846 -3.399  0.50 15.58 ?  142 VAL   A H    1 
ATOM   3192 H  HA   A VAL   A 1 142 ? 18.280 -15.692 -3.392  0.50 14.76 ?  142 VAL   A HA   1 
ATOM   3193 H  HA   B VAL   A 1 142 ? 18.307 -15.591 -3.464  0.50 15.64 ?  142 VAL   A HA   1 
ATOM   3194 H  HB   A VAL   A 1 142 ? 18.659 -12.908 -3.698  0.50 14.44 ?  142 VAL   A HB   1 
ATOM   3195 H  HB   B VAL   A 1 142 ? 18.539 -12.774 -3.608  0.50 15.94 ?  142 VAL   A HB   1 
ATOM   3196 H  HG11 A VAL   A 1 142 ? 20.767 -13.550 -4.668  0.50 13.64 ?  142 VAL   A HG11 1 
ATOM   3197 H  HG11 B VAL   A 1 142 ? 20.642 -13.253 -4.646  0.50 15.45 ?  142 VAL   A HG11 1 
ATOM   3198 H  HG12 A VAL   A 1 142 ? 20.694 -13.704 -3.090  0.50 13.64 ?  142 VAL   A HG12 1 
ATOM   3199 H  HG12 B VAL   A 1 142 ? 20.608 -13.537 -3.084  0.50 15.45 ?  142 VAL   A HG12 1 
ATOM   3200 H  HG13 A VAL   A 1 142 ? 20.539 -14.982 -4.022  0.50 13.64 ?  142 VAL   A HG13 1 
ATOM   3201 H  HG13 B VAL   A 1 142 ? 20.483 -14.741 -4.114  0.50 15.45 ?  142 VAL   A HG13 1 
ATOM   3202 H  HG21 A VAL   A 1 142 ? 18.836 -13.366 -5.992  0.50 15.90 ?  142 VAL   A HG21 1 
ATOM   3203 H  HG21 B VAL   A 1 142 ? 18.626 -13.034 -5.907  0.50 17.07 ?  142 VAL   A HG21 1 
ATOM   3204 H  HG22 A VAL   A 1 142 ? 18.460 -14.881 -5.700  0.50 15.90 ?  142 VAL   A HG22 1 
ATOM   3205 H  HG22 B VAL   A 1 142 ? 18.466 -14.606 -5.748  0.50 17.07 ?  142 VAL   A HG22 1 
ATOM   3206 H  HG23 A VAL   A 1 142 ? 17.392 -13.734 -5.441  0.50 15.90 ?  142 VAL   A HG23 1 
ATOM   3207 H  HG23 B VAL   A 1 142 ? 17.263 -13.643 -5.367  0.50 17.07 ?  142 VAL   A HG23 1 
ATOM   3208 N  N    . CYS   A 1 143 ? 18.188 -13.812 -0.814  1.00 12.03 ?  143 CYS   A N    1 
ATOM   3209 C  CA   . CYS   A 1 143 ? 18.640 -13.749 0.570   1.00 12.35 ?  143 CYS   A CA   1 
ATOM   3210 C  C    . CYS   A 1 143 ? 18.413 -15.083 1.273   1.00 12.23 ?  143 CYS   A C    1 
ATOM   3211 O  O    . CYS   A 1 143 ? 19.330 -15.661 1.863   1.00 12.16 ?  143 CYS   A O    1 
ATOM   3212 C  CB   . CYS   A 1 143 ? 17.892 -12.634 1.294   1.00 12.81 ?  143 CYS   A CB   1 
ATOM   3213 S  SG   . CYS   A 1 143 ? 18.360 -12.444 3.027   1.00 13.05 ?  143 CYS   A SG   1 
ATOM   3214 H  H    A CYS   A 1 143 ? 17.612 -13.214 -1.032  0.50 14.42 ?  143 CYS   A H    1 
ATOM   3215 H  H    B CYS   A 1 143 ? 17.599 -13.222 -1.019  0.50 14.42 ?  143 CYS   A H    1 
ATOM   3216 H  HA   . CYS   A 1 143 ? 19.587 -13.557 0.596   1.00 14.81 ?  143 CYS   A HA   1 
ATOM   3217 H  HB2  . CYS   A 1 143 ? 18.073 -11.795 0.844   1.00 15.36 ?  143 CYS   A HB2  1 
ATOM   3218 H  HB3  . CYS   A 1 143 ? 16.944 -12.823 1.262   1.00 15.36 ?  143 CYS   A HB3  1 
ATOM   3219 H  HG   . CYS   A 1 143 ? 17.758 -11.511 3.490   1.00 15.65 ?  143 CYS   A HG   1 
ATOM   3220 N  N    . VAL   A 1 144 ? 17.185 -15.593 1.213   1.00 12.64 ?  144 VAL   A N    1 
ATOM   3221 C  CA   . VAL   A 1 144 ? 16.843 -16.830 1.909   1.00 13.94 ?  144 VAL   A CA   1 
ATOM   3222 C  C    . VAL   A 1 144 ? 17.670 -18.000 1.394   1.00 13.42 ?  144 VAL   A C    1 
ATOM   3223 O  O    . VAL   A 1 144 ? 18.032 -18.907 2.157   1.00 14.59 ?  144 VAL   A O    1 
ATOM   3224 C  CB   . VAL   A 1 144 ? 15.330 -17.080 1.762   1.00 16.12 ?  144 VAL   A CB   1 
ATOM   3225 C  CG1  . VAL   A 1 144 ? 14.972 -18.526 2.062   1.00 17.79 ?  144 VAL   A CG1  1 
ATOM   3226 C  CG2  . VAL   A 1 144 ? 14.560 -16.102 2.648   1.00 16.02 ?  144 VAL   A CG2  1 
ATOM   3227 H  H    . VAL   A 1 144 ? 16.530 -15.243 0.777   1.00 15.16 ?  144 VAL   A H    1 
ATOM   3228 H  HA   . VAL   A 1 144 ? 17.027 -16.727 2.851   1.00 16.72 ?  144 VAL   A HA   1 
ATOM   3229 H  HB   . VAL   A 1 144 ? 15.068 -16.903 0.841   1.00 19.33 ?  144 VAL   A HB   1 
ATOM   3230 H  HG11 . VAL   A 1 144 ? 14.015 -18.587 2.224   1.00 21.34 ?  144 VAL   A HG11 1 
ATOM   3231 H  HG12 . VAL   A 1 144 ? 15.208 -19.078 1.300   1.00 21.34 ?  144 VAL   A HG12 1 
ATOM   3232 H  HG13 . VAL   A 1 144 ? 15.456 -18.813 2.849   1.00 21.34 ?  144 VAL   A HG13 1 
ATOM   3233 H  HG21 . VAL   A 1 144 ? 13.606 -16.269 2.558   1.00 19.22 ?  144 VAL   A HG21 1 
ATOM   3234 H  HG22 . VAL   A 1 144 ? 14.829 -16.232 3.571   1.00 19.22 ?  144 VAL   A HG22 1 
ATOM   3235 H  HG23 . VAL   A 1 144 ? 14.762 -15.195 2.369   1.00 19.22 ?  144 VAL   A HG23 1 
ATOM   3236 N  N    . ASP   A 1 145 ? 17.953 -18.020 0.094   1.00 13.42 ?  145 ASP   A N    1 
ATOM   3237 C  CA   . ASP   A 1 145 ? 18.675 -19.121 -0.533  1.00 13.88 ?  145 ASP   A CA   1 
ATOM   3238 C  C    . ASP   A 1 145 ? 20.196 -18.971 -0.468  1.00 14.05 ?  145 ASP   A C    1 
ATOM   3239 O  O    . ASP   A 1 145 ? 20.911 -19.857 -0.954  1.00 15.87 ?  145 ASP   A O    1 
ATOM   3240 C  CB   . ASP   A 1 145 ? 18.244 -19.253 -1.995  1.00 15.16 ?  145 ASP   A CB   1 
ATOM   3241 C  CG   . ASP   A 1 145 ? 16.820 -19.760 -2.145  1.00 16.93 ?  145 ASP   A CG   1 
ATOM   3242 O  OD1  . ASP   A 1 145 ? 16.256 -20.308 -1.168  1.00 18.09 ?  145 ASP   A OD1  1 
ATOM   3243 O  OD2  . ASP   A 1 145 ? 16.273 -19.610 -3.254  1.00 18.83 -1 145 ASP   A OD2  1 
ATOM   3244 H  H    . ASP   A 1 145 ? 17.717 -17.401 -0.459  1.00 16.09 ?  145 ASP   A H    1 
ATOM   3245 H  HA   . ASP   A 1 145 ? 18.435 -19.946 -0.083  1.00 16.64 ?  145 ASP   A HA   1 
ATOM   3246 H  HB2  . ASP   A 1 145 ? 18.295 -18.380 -2.420  1.00 18.18 ?  145 ASP   A HB2  1 
ATOM   3247 H  HB3  . ASP   A 1 145 ? 18.838 -19.873 -2.445  1.00 18.18 ?  145 ASP   A HB3  1 
ATOM   3248 N  N    . THR   A 1 146 ? 20.705 -17.876 0.102   1.00 12.56 ?  146 THR   A N    1 
ATOM   3249 C  CA   . THR   A 1 146 ? 22.141 -17.606 0.133   1.00 11.98 ?  146 THR   A CA   1 
ATOM   3250 C  C    . THR   A 1 146 ? 22.682 -17.416 1.539   1.00 12.38 ?  146 THR   A C    1 
ATOM   3251 O  O    . THR   A 1 146 ? 23.764 -17.935 1.862   1.00 13.09 ?  146 THR   A O    1 
ATOM   3252 C  CB   . THR   A 1 146 ? 22.454 -16.352 -0.704  1.00 12.36 ?  146 THR   A CB   1 
ATOM   3253 O  OG1  . THR   A 1 146 ? 21.944 -16.529 -2.028  1.00 12.62 ?  146 THR   A OG1  1 
ATOM   3254 C  CG2  . THR   A 1 146 ? 23.954 -16.096 -0.771  1.00 12.80 ?  146 THR   A CG2  1 
ATOM   3255 H  H    . THR   A 1 146 ? 20.227 -17.262 0.480   1.00 15.06 ?  146 THR   A H    1 
ATOM   3256 H  HA   . THR   A 1 146 ? 22.609 -18.350 -0.264  1.00 14.36 ?  146 THR   A HA   1 
ATOM   3257 H  HB   . THR   A 1 146 ? 22.034 -15.577 -0.300  1.00 14.82 ?  146 THR   A HB   1 
ATOM   3258 H  HG1  . THR   A 1 146 ? 21.108 -16.617 -2.003  1.00 15.14 ?  146 THR   A HG1  1 
ATOM   3259 H  HG21 . THR   A 1 146 ? 24.144 -15.427 -1.449  1.00 15.35 ?  146 THR   A HG21 1 
ATOM   3260 H  HG22 . THR   A 1 146 ? 24.275 -15.771 0.085   1.00 15.35 ?  146 THR   A HG22 1 
ATOM   3261 H  HG23 . THR   A 1 146 ? 24.420 -16.914 -0.997  1.00 15.35 ?  146 THR   A HG23 1 
ATOM   3262 N  N    . VAL   A 1 147 ? 21.994 -16.630 2.362   1.00 12.16 ?  147 VAL   A N    1 
ATOM   3263 C  CA   . VAL   A 1 147 ? 22.467 -16.331 3.705   1.00 12.03 ?  147 VAL   A CA   1 
ATOM   3264 C  C    . VAL   A 1 147 ? 22.151 -17.507 4.616   1.00 12.48 ?  147 VAL   A C    1 
ATOM   3265 O  O    . VAL   A 1 147 ? 21.014 -17.995 4.647   1.00 13.15 ?  147 VAL   A O    1 
ATOM   3266 C  CB   . VAL   A 1 147 ? 21.820 -15.034 4.214   1.00 12.21 ?  147 VAL   A CB   1 
ATOM   3267 C  CG1  . VAL   A 1 147 ? 22.316 -14.704 5.597   1.00 12.92 ?  147 VAL   A CG1  1 
ATOM   3268 C  CG2  . VAL   A 1 147 ? 22.086 -13.883 3.237   1.00 12.13 ?  147 VAL   A CG2  1 
ATOM   3269 H  H    . VAL   A 1 147 ? 21.236 -16.266 2.172   1.00 14.58 ?  147 VAL   A H    1 
ATOM   3270 H  HA   . VAL   A 1 147 ? 23.429 -16.203 3.684   1.00 14.43 ?  147 VAL   A HA   1 
ATOM   3271 H  HB   . VAL   A 1 147 ? 20.862 -15.160 4.267   1.00 14.64 ?  147 VAL   A HB   1 
ATOM   3272 H  HG11 . VAL   A 1 147 ? 22.038 -13.801 5.821   1.00 15.50 ?  147 VAL   A HG11 1 
ATOM   3273 H  HG12 . VAL   A 1 147 ? 21.928 -15.332 6.226   1.00 15.50 ?  147 VAL   A HG12 1 
ATOM   3274 H  HG13 . VAL   A 1 147 ? 23.280 -14.768 5.609   1.00 15.50 ?  147 VAL   A HG13 1 
ATOM   3275 H  HG21 . VAL   A 1 147 ? 21.750 -13.059 3.623   1.00 14.55 ?  147 VAL   A HG21 1 
ATOM   3276 H  HG22 . VAL   A 1 147 ? 23.037 -13.816 3.080   1.00 14.55 ?  147 VAL   A HG22 1 
ATOM   3277 H  HG23 . VAL   A 1 147 ? 21.622 -14.069 2.403   1.00 14.55 ?  147 VAL   A HG23 1 
ATOM   3278 N  N    . ARG   A 1 148 ? 23.167 -17.950 5.364   1.00 12.54 ?  148 ARG   A N    1 
ATOM   3279 C  CA   . ARG   A 1 148 ? 23.038 -19.025 6.333   1.00 13.21 ?  148 ARG   A CA   1 
ATOM   3280 C  C    . ARG   A 1 148 ? 23.148 -18.551 7.770   1.00 13.21 ?  148 ARG   A C    1 
ATOM   3281 O  O    . ARG   A 1 148 ? 22.733 -19.281 8.679   1.00 14.79 ?  148 ARG   A O    1 
ATOM   3282 C  CB   . ARG   A 1 148 ? 24.086 -20.117 6.069   1.00 13.72 ?  148 ARG   A CB   1 
ATOM   3283 C  CG   . ARG   A 1 148 ? 23.951 -20.764 4.703   1.00 14.96 ?  148 ARG   A CG   1 
ATOM   3284 C  CD   . ARG   A 1 148 ? 25.049 -21.793 4.452   1.00 15.80 ?  148 ARG   A CD   1 
ATOM   3285 N  NE   . ARG   A 1 148 ? 26.382 -21.198 4.489   1.00 15.83 ?  148 ARG   A NE   1 
ATOM   3286 C  CZ   . ARG   A 1 148 ? 26.900 -20.475 3.505   1.00 15.04 ?  148 ARG   A CZ   1 
ATOM   3287 N  NH1  . ARG   A 1 148 ? 26.232 -20.258 2.385   1.00 15.26 ?  148 ARG   A NH1  1 
ATOM   3288 N  NH2  . ARG   A 1 148 ? 28.121 -19.955 3.648   1.00 15.39 ?  148 ARG   A NH2  1 
ATOM   3289 H  H    . ARG   A 1 148 ? 23.969 -17.623 5.318   1.00 15.03 ?  148 ARG   A H    1 
ATOM   3290 H  HA   . ARG   A 1 148 ? 22.164 -19.421 6.232   1.00 15.84 ?  148 ARG   A HA   1 
ATOM   3291 H  HB2  . ARG   A 1 148 ? 24.968 -19.733 6.136   1.00 16.45 ?  148 ARG   A HB2  1 
ATOM   3292 H  HB3  . ARG   A 1 148 ? 23.974 -20.817 6.736   1.00 16.45 ?  148 ARG   A HB3  1 
ATOM   3293 H  HG2  . ARG   A 1 148 ? 23.089 -21.203 4.645   1.00 17.94 ?  148 ARG   A HG2  1 
ATOM   3294 H  HG3  . ARG   A 1 148 ? 24.016 -20.068 4.025   1.00 17.94 ?  148 ARG   A HG3  1 
ATOM   3295 H  HD2  . ARG   A 1 148 ? 25.003 -22.471 5.142   1.00 18.95 ?  148 ARG   A HD2  1 
ATOM   3296 H  HD3  . ARG   A 1 148 ? 24.913 -22.189 3.580   1.00 18.95 ?  148 ARG   A HD3  1 
ATOM   3297 H  HE   . ARG   A 1 148 ? 26.862 -21.330 5.186   1.00 18.99 ?  148 ARG   A HE   1 
ATOM   3298 H  HH11 . ARG   A 1 148 ? 25.444 -20.577 2.282   1.00 18.30 ?  148 ARG   A HH11 1 
ATOM   3299 H  HH12 . ARG   A 1 148 ? 26.587 -19.778 1.761   1.00 18.30 ?  148 ARG   A HH12 1 
ATOM   3300 H  HH21 . ARG   A 1 148 ? 28.564 -20.092 4.370   1.00 18.46 ?  148 ARG   A HH21 1 
ATOM   3301 H  HH22 . ARG   A 1 148 ? 28.467 -19.484 3.014   1.00 18.46 ?  148 ARG   A HH22 1 
ATOM   3302 N  N    . THR   A 1 149 ? 23.695 -17.360 7.990   1.00 13.13 ?  149 THR   A N    1 
ATOM   3303 C  CA   . THR   A 1 149 ? 23.757 -16.764 9.309   1.00 13.20 ?  149 THR   A CA   1 
ATOM   3304 C  C    . THR   A 1 149 ? 22.429 -16.067 9.598   1.00 12.50 ?  149 THR   A C    1 
ATOM   3305 O  O    . THR   A 1 149 ? 21.503 -16.064 8.775   1.00 13.18 ?  149 THR   A O    1 
ATOM   3306 C  CB   . THR   A 1 149 ? 24.951 -15.821 9.374   1.00 13.45 ?  149 THR   A CB   1 
ATOM   3307 O  OG1  . THR   A 1 149 ? 24.836 -14.900 8.286   1.00 13.27 ?  149 THR   A OG1  1 
ATOM   3308 C  CG2  . THR   A 1 149 ? 26.268 -16.604 9.269   1.00 13.96 ?  149 THR   A CG2  1 
ATOM   3309 H  H    . THR   A 1 149 ? 24.055 -16.869 7.380   1.00 15.74 ?  149 THR   A H    1 
ATOM   3310 H  HA   . THR   A 1 149 ? 23.888 -17.465 9.972   1.00 15.83 ?  149 THR   A HA   1 
ATOM   3311 H  HB   . THR   A 1 149 ? 24.935 -15.340 10.216  1.00 16.13 ?  149 THR   A HB   1 
ATOM   3312 H  HG1  . THR   A 1 149 ? 25.475 -14.362 8.295   1.00 15.92 ?  149 THR   A HG1  1 
ATOM   3313 H  HG21 . THR   A 1 149 ? 27.021 -15.995 9.328   1.00 16.74 ?  149 THR   A HG21 1 
ATOM   3314 H  HG22 . THR   A 1 149 ? 26.332 -17.252 9.990   1.00 16.74 ?  149 THR   A HG22 1 
ATOM   3315 H  HG23 . THR   A 1 149 ? 26.311 -17.075 8.421   1.00 16.74 ?  149 THR   A HG23 1 
ATOM   3316 N  N    . ASN   A 1 150 ? 22.295 -15.525 10.803  1.00 12.93 ?  150 ASN   A N    1 
ATOM   3317 C  CA   . ASN   A 1 150 ? 21.004 -15.021 11.256  1.00 13.38 ?  150 ASN   A CA   1 
ATOM   3318 C  C    . ASN   A 1 150 ? 20.825 -13.584 10.788  1.00 12.67 ?  150 ASN   A C    1 
ATOM   3319 O  O    . ASN   A 1 150 ? 21.582 -12.693 11.194  1.00 14.16 ?  150 ASN   A O    1 
ATOM   3320 C  CB   . ASN   A 1 150 ? 20.899 -15.126 12.771  1.00 15.43 ?  150 ASN   A CB   1 
ATOM   3321 C  CG   . ASN   A 1 150 ? 20.794 -16.563 13.233  1.00 19.07 ?  150 ASN   A CG   1 
ATOM   3322 O  OD1  . ASN   A 1 150 ? 20.255 -17.410 12.521  1.00 20.44 ?  150 ASN   A OD1  1 
ATOM   3323 N  ND2  . ASN   A 1 150 ? 21.327 -16.852 14.417  1.00 21.10 ?  150 ASN   A ND2  1 
ATOM   3324 H  H    . ASN   A 1 150 ? 22.937 -15.435 11.374  1.00 15.50 ?  150 ASN   A H    1 
ATOM   3325 H  HA   . ASN   A 1 150 ? 20.300 -15.559 10.866  1.00 16.04 ?  150 ASN   A HA   1 
ATOM   3326 H  HB2  . ASN   A 1 150 ? 21.686 -14.739 13.179  1.00 18.50 ?  150 ASN   A HB2  1 
ATOM   3327 H  HB3  . ASN   A 1 150 ? 20.101 -14.666 13.071  1.00 18.50 ?  150 ASN   A HB3  1 
ATOM   3328 H  HD21 . ASN   A 1 150 ? 21.302 -17.660 14.724  1.00 25.31 ?  150 ASN   A HD21 1 
ATOM   3329 H  HD22 . ASN   A 1 150 ? 21.697 -16.233 14.887  1.00 25.31 ?  150 ASN   A HD22 1 
ATOM   3330 N  N    . VAL   A 1 151 ? 19.836 -13.361 9.926   1.00 12.57 ?  151 VAL   A N    1 
ATOM   3331 C  CA   . VAL   A 1 151 ? 19.625 -12.057 9.323   1.00 12.41 ?  151 VAL   A CA   1 
ATOM   3332 C  C    . VAL   A 1 151 ? 18.229 -11.551 9.664   1.00 12.26 ?  151 VAL   A C    1 
ATOM   3333 O  O    . VAL   A 1 151 ? 17.228 -12.268 9.507   1.00 13.40 ?  151 VAL   A O    1 
ATOM   3334 C  CB   . VAL   A 1 151 ? 19.942 -12.042 7.812   1.00 13.62 ?  151 VAL   A CB   1 
ATOM   3335 C  CG1  . VAL   A 1 151 ? 19.126 -13.062 7.040   1.00 14.50 ?  151 VAL   A CG1  1 
ATOM   3336 C  CG2  . VAL   A 1 151 ? 19.759 -10.633 7.240   1.00 13.84 ?  151 VAL   A CG2  1 
ATOM   3337 H  H    . VAL   A 1 151 ? 19.273 -13.959 9.671   1.00 15.07 ?  151 VAL   A H    1 
ATOM   3338 H  HA   . VAL   A 1 151 ? 20.257 -11.439 9.732   1.00 14.88 ?  151 VAL   A HA   1 
ATOM   3339 H  HB   . VAL   A 1 151 ? 20.880 -12.275 7.693   1.00 16.33 ?  151 VAL   A HB   1 
ATOM   3340 H  HG11 . VAL   A 1 151 ? 19.355 -13.010 6.096   1.00 17.39 ?  151 VAL   A HG11 1 
ATOM   3341 H  HG12 . VAL   A 1 151 ? 19.334 -13.954 7.373   1.00 17.39 ?  151 VAL   A HG12 1 
ATOM   3342 H  HG13 . VAL   A 1 151 ? 18.184 -12.878 7.161   1.00 17.39 ?  151 VAL   A HG13 1 
ATOM   3343 H  HG21 . VAL   A 1 151 ? 20.096 -10.618 6.328   1.00 16.60 ?  151 VAL   A HG21 1 
ATOM   3344 H  HG22 . VAL   A 1 151 ? 18.819 -10.407 7.247   1.00 16.60 ?  151 VAL   A HG22 1 
ATOM   3345 H  HG23 . VAL   A 1 151 ? 20.260 -10.004 7.783   1.00 16.60 ?  151 VAL   A HG23 1 
ATOM   3346 N  N    . TYR   A 1 152 ? 18.197 -10.304 10.142  1.00 12.12 ?  152 TYR   A N    1 
ATOM   3347 C  CA   . TYR   A 1 152 ? 16.993 -9.581  10.524  1.00 11.95 ?  152 TYR   A CA   1 
ATOM   3348 C  C    . TYR   A 1 152 ? 16.793 -8.478  9.495   1.00 11.60 ?  152 TYR   A C    1 
ATOM   3349 O  O    . TYR   A 1 152 ? 17.563 -7.506  9.454   1.00 12.01 ?  152 TYR   A O    1 
ATOM   3350 C  CB   . TYR   A 1 152 ? 17.171 -9.035  11.936  1.00 12.98 ?  152 TYR   A CB   1 
ATOM   3351 C  CG   . TYR   A 1 152 ? 17.119 -10.150 12.948  1.00 13.81 ?  152 TYR   A CG   1 
ATOM   3352 C  CD1  . TYR   A 1 152 ? 18.242 -10.914 13.239  1.00 15.26 ?  152 TYR   A CD1  1 
ATOM   3353 C  CD2  . TYR   A 1 152 ? 15.931 -10.477 13.577  1.00 14.10 ?  152 TYR   A CD2  1 
ATOM   3354 C  CE1  . TYR   A 1 152 ? 18.188 -11.959 14.142  1.00 16.62 ?  152 TYR   A CE1  1 
ATOM   3355 C  CE2  . TYR   A 1 152 ? 15.864 -11.530 14.484  1.00 15.63 ?  152 TYR   A CE2  1 
ATOM   3356 C  CZ   . TYR   A 1 152 ? 16.999 -12.265 14.763  1.00 16.68 ?  152 TYR   A CZ   1 
ATOM   3357 O  OH   . TYR   A 1 152 ? 16.958 -13.310 15.659  1.00 19.12 ?  152 TYR   A OH   1 
ATOM   3358 H  H    . TYR   A 1 152 ? 18.913 -9.822  10.236  1.00 14.53 ?  152 TYR   A H    1 
ATOM   3359 H  HA   . TYR   A 1 152 ? 16.234 -10.179 10.504  1.00 14.33 ?  152 TYR   A HA   1 
ATOM   3360 H  HB2  . TYR   A 1 152 ? 18.040 -8.606  12.004  1.00 15.56 ?  152 TYR   A HB2  1 
ATOM   3361 H  HB3  . TYR   A 1 152 ? 16.467 -8.407  12.130  1.00 15.56 ?  152 TYR   A HB3  1 
ATOM   3362 H  HD1  . TYR   A 1 152 ? 19.049 -10.713 12.817  1.00 18.30 ?  152 TYR   A HD1  1 
ATOM   3363 H  HD2  . TYR   A 1 152 ? 15.163 -9.986  13.383  1.00 16.91 ?  152 TYR   A HD2  1 
ATOM   3364 H  HE1  . TYR   A 1 152 ? 18.954 -12.451 14.329  1.00 19.93 ?  152 TYR   A HE1  1 
ATOM   3365 H  HE2  . TYR   A 1 152 ? 15.059 -11.728 14.902  1.00 18.74 ?  152 TYR   A HE2  1 
ATOM   3366 H  HH   . TYR   A 1 152 ? 16.182 -13.380 15.971  1.00 22.93 ?  152 TYR   A HH   1 
ATOM   3367 N  N    . LEU   A 1 153 ? 15.787 -8.653  8.641   1.00 11.86 ?  153 LEU   A N    1 
ATOM   3368 C  CA   . LEU   A 1 153 ? 15.528 -7.763  7.519   1.00 12.00 ?  153 LEU   A CA   1 
ATOM   3369 C  C    . LEU   A 1 153 ? 14.521 -6.693  7.910   1.00 12.38 ?  153 LEU   A C    1 
ATOM   3370 O  O    . LEU   A 1 153 ? 13.423 -7.006  8.388   1.00 13.68 ?  153 LEU   A O    1 
ATOM   3371 C  CB   . LEU   A 1 153 ? 14.977 -8.544  6.325   1.00 12.20 ?  153 LEU   A CB   1 
ATOM   3372 C  CG   . LEU   A 1 153 ? 15.932 -9.551  5.684   1.00 12.43 ?  153 LEU   A CG   1 
ATOM   3373 C  CD1  . LEU   A 1 153 ? 15.156 -10.452 4.731   1.00 12.63 ?  153 LEU   A CD1  1 
ATOM   3374 C  CD2  . LEU   A 1 153 ? 17.061 -8.828  4.960   1.00 12.62 ?  153 LEU   A CD2  1 
ATOM   3375 H  H    . LEU   A 1 153 ? 15.214 -9.301  8.703   1.00 14.23 ?  153 LEU   A H    1 
ATOM   3376 H  HA   . LEU   A 1 153 ? 16.356 -7.336  7.263   1.00 14.39 ?  153 LEU   A HA   1 
ATOM   3377 H  HB2  . LEU   A 1 153 ? 14.194 -9.029  6.617   1.00 14.62 ?  153 LEU   A HB2  1 
ATOM   3378 H  HB3  . LEU   A 1 153 ? 14.729 -7.903  5.641   1.00 14.62 ?  153 LEU   A HB3  1 
ATOM   3379 H  HG   . LEU   A 1 153 ? 16.328 -10.107 6.376   1.00 14.90 ?  153 LEU   A HG   1 
ATOM   3380 H  HD11 . LEU   A 1 153 ? 15.748 -11.143 4.396   1.00 15.15 ?  153 LEU   A HD11 1 
ATOM   3381 H  HD12 . LEU   A 1 153 ? 14.415 -10.851 5.207   1.00 15.15 ?  153 LEU   A HD12 1 
ATOM   3382 H  HD13 . LEU   A 1 153 ? 14.826 -9.914  3.992   1.00 15.15 ?  153 LEU   A HD13 1 
ATOM   3383 H  HD21 . LEU   A 1 153 ? 17.625 -9.486  4.531   1.00 15.14 ?  153 LEU   A HD21 1 
ATOM   3384 H  HD22 . LEU   A 1 153 ? 16.671 -8.238  4.297   1.00 15.14 ?  153 LEU   A HD22 1 
ATOM   3385 H  HD23 . LEU   A 1 153 ? 17.569 -8.318  5.605   1.00 15.14 ?  153 LEU   A HD23 1 
ATOM   3386 N  N    A ALA   A 1 154 ? 14.920 -5.433  7.748   0.50 12.04 ?  154 ALA   A N    1 
ATOM   3387 N  N    B ALA   A 1 154 ? 14.864 -5.439  7.634   0.50 11.98 ?  154 ALA   A N    1 
ATOM   3388 C  CA   A ALA   A 1 154 ? 14.070 -4.280  8.011   0.50 12.39 ?  154 ALA   A CA   1 
ATOM   3389 C  CA   B ALA   A 1 154 ? 13.973 -4.301  7.831   0.50 12.15 ?  154 ALA   A CA   1 
ATOM   3390 C  C    A ALA   A 1 154 ? 13.555 -3.751  6.681   0.50 12.43 ?  154 ALA   A C    1 
ATOM   3391 C  C    B ALA   A 1 154 ? 13.529 -3.793  6.462   0.50 12.29 ?  154 ALA   A C    1 
ATOM   3392 O  O    A ALA   A 1 154 ? 14.345 -3.335  5.826   0.50 12.60 ?  154 ALA   A O    1 
ATOM   3393 O  O    B ALA   A 1 154 ? 14.358 -3.339  5.666   0.50 13.05 ?  154 ALA   A O    1 
ATOM   3394 C  CB   A ALA   A 1 154 ? 14.853 -3.182  8.727   0.50 12.82 ?  154 ALA   A CB   1 
ATOM   3395 C  CB   B ALA   A 1 154 ? 14.689 -3.195  8.606   0.50 12.51 ?  154 ALA   A CB   1 
ATOM   3396 H  H    A ALA   A 1 154 ? 15.708 -5.216  7.476   0.50 14.43 ?  154 ALA   A H    1 
ATOM   3397 H  H    B ALA   A 1 154 ? 15.629 -5.216  7.309   0.50 14.37 ?  154 ALA   A H    1 
ATOM   3398 H  HA   A ALA   A 1 154 ? 13.313 -4.540  8.557   0.50 14.86 ?  154 ALA   A HA   1 
ATOM   3399 H  HA   B ALA   A 1 154 ? 13.190 -4.579  8.339   0.50 14.57 ?  154 ALA   A HA   1 
ATOM   3400 H  HB1  A ALA   A 1 154 ? 14.263 -2.427  8.885   0.50 15.37 ?  154 ALA   A HB1  1 
ATOM   3401 H  HB1  B ALA   A 1 154 ? 14.081 -2.451  8.732   0.50 15.00 ?  154 ALA   A HB1  1 
ATOM   3402 H  HB2  A ALA   A 1 154 ? 15.181 -3.528  9.570   0.50 15.37 ?  154 ALA   A HB2  1 
ATOM   3403 H  HB2  B ALA   A 1 154 ? 14.968 -3.543  9.471   0.50 15.00 ?  154 ALA   A HB2  1 
ATOM   3404 H  HB3  A ALA   A 1 154 ? 15.596 -2.908  8.167   0.50 15.37 ?  154 ALA   A HB3  1 
ATOM   3405 H  HB3  B ALA   A 1 154 ? 15.466 -2.909  8.102   0.50 15.00 ?  154 ALA   A HB3  1 
ATOM   3406 N  N    A VAL   A 1 155 ? 12.236 -3.755  6.519   0.50 12.87 ?  155 VAL   A N    1 
ATOM   3407 N  N    B VAL   A 1 155 ? 12.227 -3.885  6.191   0.50 12.30 ?  155 VAL   A N    1 
ATOM   3408 C  CA   A VAL   A 1 155 ? 11.576 -3.293  5.306   0.50 13.31 ?  155 VAL   A CA   1 
ATOM   3409 C  CA   B VAL   A 1 155 ? 11.624 -3.458  4.930   0.50 12.27 ?  155 VAL   A CA   1 
ATOM   3410 C  C    A VAL   A 1 155 ? 10.857 -2.000  5.645   0.50 14.35 ?  155 VAL   A C    1 
ATOM   3411 C  C    B VAL   A 1 155 ? 10.838 -2.182  5.208   0.50 12.40 ?  155 VAL   A C    1 
ATOM   3412 O  O    A VAL   A 1 155 ? 9.959  -1.984  6.497   0.50 14.46 ?  155 VAL   A O    1 
ATOM   3413 O  O    B VAL   A 1 155 ? 9.830  -2.212  5.922   0.50 12.45 ?  155 VAL   A O    1 
ATOM   3414 C  CB   A VAL   A 1 155 ? 10.603 -4.344  4.753   0.50 13.15 ?  155 VAL   A CB   1 
ATOM   3415 C  CB   B VAL   A 1 155 ? 10.722 -4.555  4.342   0.50 12.03 ?  155 VAL   A CB   1 
ATOM   3416 C  CG1  A VAL   A 1 155 ? 9.866  -3.798  3.540   0.50 13.37 ?  155 VAL   A CG1  1 
ATOM   3417 C  CG1  B VAL   A 1 155 ? 10.037 -4.079  3.067   0.50 12.27 ?  155 VAL   A CG1  1 
ATOM   3418 C  CG2  A VAL   A 1 155 ? 11.355 -5.612  4.388   0.50 13.61 ?  155 VAL   A CG2  1 
ATOM   3419 C  CG2  B VAL   A 1 155 ? 11.532 -5.823  4.068   0.50 12.86 ?  155 VAL   A CG2  1 
ATOM   3420 H  H    A VAL   A 1 155 ? 11.688 -4.020  7.123   0.50 15.43 ?  155 VAL   A H    1 
ATOM   3421 H  H    B VAL   A 1 155 ? 11.654 -4.231  6.737   0.50 14.75 ?  155 VAL   A H    1 
ATOM   3422 H  HA   A VAL   A 1 155 ? 12.238 -3.103  4.626   0.50 15.96 ?  155 VAL   A HA   1 
ATOM   3423 H  HA   B VAL   A 1 155 ? 12.319 -3.263  4.286   0.50 14.71 ?  155 VAL   A HA   1 
ATOM   3424 H  HB   A VAL   A 1 155 ? 9.945  -4.561  5.433   0.50 15.76 ?  155 VAL   A HB   1 
ATOM   3425 H  HB   B VAL   A 1 155 ? 10.030 -4.783  4.984   0.50 14.42 ?  155 VAL   A HB   1 
ATOM   3426 H  HG11 A VAL   A 1 155 ? 9.409  -4.528  3.095   0.50 16.03 ?  155 VAL   A HG11 1 
ATOM   3427 H  HG11 B VAL   A 1 155 ? 9.621  -4.840  2.626   0.50 14.71 ?  155 VAL   A HG11 1 
ATOM   3428 H  HG12 A VAL   A 1 155 ? 9.220  -3.133  3.830   0.50 16.03 ?  155 VAL   A HG12 1 
ATOM   3429 H  HG12 B VAL   A 1 155 ? 9.357  -3.426  3.297   0.50 14.71 ?  155 VAL   A HG12 1 
ATOM   3430 H  HG13 A VAL   A 1 155 ? 10.508 -3.394  2.936   0.50 16.03 ?  155 VAL   A HG13 1 
ATOM   3431 H  HG13 B VAL   A 1 155 ? 10.698 -3.682  2.482   0.50 14.71 ?  155 VAL   A HG13 1 
ATOM   3432 H  HG21 A VAL   A 1 155 ? 10.739 -6.238  3.976   0.50 16.32 ?  155 VAL   A HG21 1 
ATOM   3433 H  HG21 B VAL   A 1 155 ? 10.957 -6.487  3.653   0.50 15.42 ?  155 VAL   A HG21 1 
ATOM   3434 H  HG22 A VAL   A 1 155 ? 12.065 -5.389  3.764   0.50 16.32 ?  155 VAL   A HG22 1 
ATOM   3435 H  HG22 B VAL   A 1 155 ? 12.267 -5.606  3.474   0.50 15.42 ?  155 VAL   A HG22 1 
ATOM   3436 H  HG23 A VAL   A 1 155 ? 11.733 -5.998  5.193   0.50 16.32 ?  155 VAL   A HG23 1 
ATOM   3437 H  HG23 B VAL   A 1 155 ? 11.876 -6.166  4.908   0.50 15.42 ?  155 VAL   A HG23 1 
ATOM   3438 N  N    A PHE   A 1 156 ? 11.249 -0.917  4.975   0.50 15.26 ?  156 PHE   A N    1 
ATOM   3439 N  N    B PHE   A 1 156 ? 11.277 -1.062  4.637   0.50 13.46 ?  156 PHE   A N    1 
ATOM   3440 C  CA   A PHE   A 1 156 ? 10.738 0.402   5.329   0.50 16.63 ?  156 PHE   A CA   1 
ATOM   3441 C  CA   B PHE   A 1 156 ? 10.707 0.251   4.959   0.50 15.69 ?  156 PHE   A CA   1 
ATOM   3442 C  C    A PHE   A 1 156 ? 9.271  0.562   4.945   0.50 16.94 ?  156 PHE   A C    1 
ATOM   3443 C  C    B PHE   A 1 156 ? 9.570  0.618   4.001   0.50 17.41 ?  156 PHE   A C    1 
ATOM   3444 O  O    A PHE   A 1 156 ? 8.487  1.143   5.704   0.50 17.95 ?  156 PHE   A O    1 
ATOM   3445 O  O    B PHE   A 1 156 ? 9.580  1.660   3.338   0.50 18.59 ?  156 PHE   A O    1 
ATOM   3446 C  CB   A PHE   A 1 156 ? 11.595 1.472   4.656   0.50 17.45 ?  156 PHE   A CB   1 
ATOM   3447 C  CB   B PHE   A 1 156 ? 11.802 1.311   4.938   0.50 17.26 ?  156 PHE   A CB   1 
ATOM   3448 C  CG   A PHE   A 1 156 ? 11.184 2.877   4.990   0.50 18.58 ?  156 PHE   A CG   1 
ATOM   3449 C  CG   B PHE   A 1 156 ? 11.420 2.615   5.598   0.50 18.78 ?  156 PHE   A CG   1 
ATOM   3450 C  CD1  A PHE   A 1 156 ? 11.186 3.313   6.307   0.50 19.56 ?  156 PHE   A CD1  1 
ATOM   3451 C  CD1  B PHE   A 1 156 ? 10.400 2.678   6.533   0.50 19.90 ?  156 PHE   A CD1  1 
ATOM   3452 C  CD2  A PHE   A 1 156 ? 10.798 3.761   3.995   0.50 19.12 ?  156 PHE   A CD2  1 
ATOM   3453 C  CD2  B PHE   A 1 156 ? 12.095 3.779   5.280   0.50 19.12 ?  156 PHE   A CD2  1 
ATOM   3454 C  CE1  A PHE   A 1 156 ? 10.806 4.602   6.626   0.50 20.42 ?  156 PHE   A CE1  1 
ATOM   3455 C  CE1  B PHE   A 1 156 ? 10.063 3.876   7.136   0.50 20.46 ?  156 PHE   A CE1  1 
ATOM   3456 C  CE2  A PHE   A 1 156 ? 10.421 5.056   4.306   0.50 19.86 ?  156 PHE   A CE2  1 
ATOM   3457 C  CE2  B PHE   A 1 156 ? 11.760 4.981   5.879   0.50 19.41 ?  156 PHE   A CE2  1 
ATOM   3458 C  CZ   A PHE   A 1 156 ? 10.427 5.479   5.624   0.50 20.30 ?  156 PHE   A CZ   1 
ATOM   3459 C  CZ   B PHE   A 1 156 ? 10.741 5.029   6.807   0.50 20.39 ?  156 PHE   A CZ   1 
ATOM   3460 H  H    A PHE   A 1 156 ? 11.809 -0.919  4.322   0.50 18.30 ?  156 PHE   A H    1 
ATOM   3461 H  H    B PHE   A 1 156 ? 11.916 -1.038  4.069   0.50 16.14 ?  156 PHE   A H    1 
ATOM   3462 H  HA   A PHE   A 1 156 ? 10.815 0.525   6.291   0.50 19.94 ?  156 PHE   A HA   1 
ATOM   3463 H  HA   B PHE   A 1 156 ? 10.342 0.195   5.857   0.50 18.81 ?  156 PHE   A HA   1 
ATOM   3464 H  HB2  A PHE   A 1 156 ? 12.519 1.360   4.937   0.50 20.93 ?  156 PHE   A HB2  1 
ATOM   3465 H  HB2  B PHE   A 1 156 ? 12.571 0.966   5.411   0.50 20.70 ?  156 PHE   A HB2  1 
ATOM   3466 H  HB3  A PHE   A 1 156 ? 11.530 1.368   3.695   0.50 20.93 ?  156 PHE   A HB3  1 
ATOM   3467 H  HB3  B PHE   A 1 156 ? 12.040 1.500   4.014   0.50 20.70 ?  156 PHE   A HB3  1 
ATOM   3468 H  HD1  A PHE   A 1 156 ? 11.441 2.726   6.986   0.50 23.47 ?  156 PHE   A HD1  1 
ATOM   3469 H  HD1  B PHE   A 1 156 ? 9.938  1.901   6.760   0.50 23.87 ?  156 PHE   A HD1  1 
ATOM   3470 H  HD2  A PHE   A 1 156 ? 10.797 3.479   3.110   0.50 22.94 ?  156 PHE   A HD2  1 
ATOM   3471 H  HD2  B PHE   A 1 156 ? 12.786 3.755   4.653   0.50 22.93 ?  156 PHE   A HD2  1 
ATOM   3472 H  HE1  A PHE   A 1 156 ? 10.810 4.884   7.514   0.50 24.49 ?  156 PHE   A HE1  1 
ATOM   3473 H  HE1  B PHE   A 1 156 ? 9.376  3.898   7.760   0.50 24.54 ?  156 PHE   A HE1  1 
ATOM   3474 H  HE2  A PHE   A 1 156 ? 10.165 5.639   3.632   0.50 23.83 ?  156 PHE   A HE2  1 
ATOM   3475 H  HE2  B PHE   A 1 156 ? 12.224 5.757   5.654   0.50 23.28 ?  156 PHE   A HE2  1 
ATOM   3476 H  HZ   A PHE   A 1 156 ? 10.171 6.347   5.838   0.50 24.35 ?  156 PHE   A HZ   1 
ATOM   3477 H  HZ   B PHE   A 1 156 ? 10.516 5.833   7.211   0.50 24.46 ?  156 PHE   A HZ   1 
ATOM   3478 N  N    A ASP   A 1 157 ? 8.884  0.067   3.773   0.50 16.75 ?  157 ASP   A N    1 
ATOM   3479 N  N    B ASP   A 1 157 ? 8.568  -0.257  3.953   0.50 17.92 ?  157 ASP   A N    1 
ATOM   3480 C  CA   A ASP   A 1 157 ? 7.557  0.298   3.213   0.50 17.98 ?  157 ASP   A CA   1 
ATOM   3481 C  CA   B ASP   A 1 157 ? 7.450  -0.111  3.031   0.50 18.11 ?  157 ASP   A CA   1 
ATOM   3482 C  C    A ASP   A 1 157 ? 6.585  -0.754  3.739   0.50 18.04 ?  157 ASP   A C    1 
ATOM   3483 C  C    B ASP   A 1 157 ? 6.386  -1.126  3.409   0.50 16.83 ?  157 ASP   A C    1 
ATOM   3484 O  O    A ASP   A 1 157 ? 6.786  -1.956  3.523   0.50 17.09 ?  157 ASP   A O    1 
ATOM   3485 O  O    B ASP   A 1 157 ? 6.567  -2.319  3.161   0.50 16.14 ?  157 ASP   A O    1 
ATOM   3486 C  CB   A ASP   A 1 157 ? 7.645  0.218   1.691   0.50 18.76 ?  157 ASP   A CB   1 
ATOM   3487 C  CB   B ASP   A 1 157 ? 7.930  -0.372  1.602   0.50 19.41 ?  157 ASP   A CB   1 
ATOM   3488 C  CG   A ASP   A 1 157 ? 6.376  0.695   1.003   0.50 20.30 ?  157 ASP   A CG   1 
ATOM   3489 C  CG   B ASP   A 1 157 ? 6.853  -0.148  0.562   0.50 20.93 ?  157 ASP   A CG   1 
ATOM   3490 O  OD1  A ASP   A 1 157 ? 6.043  1.895   1.110   0.50 21.50 ?  157 ASP   A OD1  1 
ATOM   3491 O  OD1  B ASP   A 1 157 ? 5.656  -0.182  0.911   0.50 21.46 ?  157 ASP   A OD1  1 
ATOM   3492 O  OD2  A ASP   A 1 157 ? 5.712  -0.145  0.354   0.50 20.66 -1 157 ASP   A OD2  1 
ATOM   3493 O  OD2  B ASP   A 1 157 ? 7.212  0.031   -0.621  0.50 22.07 -1 157 ASP   A OD2  1 
ATOM   3494 H  H    A ASP   A 1 157 ? 9.392  -0.417  3.276   0.50 20.09 ?  157 ASP   A H    1 
ATOM   3495 H  H    B ASP   A 1 157 ? 8.517  -0.965  4.450   0.50 21.50 ?  157 ASP   A H    1 
ATOM   3496 H  HA   A ASP   A 1 157 ? 7.245  1.182   3.469   0.50 21.56 ?  157 ASP   A HA   1 
ATOM   3497 H  HA   B ASP   A 1 157 ? 7.075  0.776   3.094   0.50 21.72 ?  157 ASP   A HA   1 
ATOM   3498 H  HB2  A ASP   A 1 157 ? 8.425  0.729   1.400   0.50 22.50 ?  157 ASP   A HB2  1 
ATOM   3499 H  HB2  B ASP   A 1 157 ? 8.679  0.208   1.413   0.50 23.28 ?  157 ASP   A HB2  1 
ATOM   3500 H  HB3  A ASP   A 1 157 ? 7.756  -0.709  1.437   0.50 22.50 ?  157 ASP   A HB3  1 
ATOM   3501 H  HB3  B ASP   A 1 157 ? 8.201  -1.299  1.522   0.50 23.28 ?  157 ASP   A HB3  1 
ATOM   3502 N  N    A LYS   A 1 158 ? 5.530  -0.304  4.426   0.50 19.63 ?  158 LYS   A N    1 
ATOM   3503 N  N    B LYS   A 1 158 ? 5.280  -0.668  4.001   0.50 17.19 ?  158 LYS   A N    1 
ATOM   3504 C  CA   A LYS   A 1 158 ? 4.569  -1.244  4.995   0.50 20.82 ?  158 LYS   A CA   1 
ATOM   3505 C  CA   B LYS   A 1 158 ? 4.280  -1.589  4.537   0.50 17.84 ?  158 LYS   A CA   1 
ATOM   3506 C  C    A LYS   A 1 158 ? 3.832  -2.011  3.904   0.50 20.58 ?  158 LYS   A C    1 
ATOM   3507 C  C    B LYS   A 1 158 ? 3.661  -2.444  3.435   0.50 16.53 ?  158 LYS   A C    1 
ATOM   3508 O  O    A LYS   A 1 158 ? 3.614  -3.222  4.028   0.50 20.64 ?  158 LYS   A O    1 
ATOM   3509 O  O    B LYS   A 1 158 ? 3.548  -3.668  3.572   0.50 15.83 ?  158 LYS   A O    1 
ATOM   3510 C  CB   A LYS   A 1 158 ? 3.588  -0.507  5.910   0.50 22.46 ?  158 LYS   A CB   1 
ATOM   3511 C  CB   B LYS   A 1 158 ? 3.208  -0.799  5.295   0.50 20.23 ?  158 LYS   A CB   1 
ATOM   3512 C  CG   A LYS   A 1 158 ? 2.389  -1.336  6.369   0.50 24.36 ?  158 LYS   A CG   1 
ATOM   3513 C  CG   B LYS   A 1 158 ? 1.989  -1.610  5.731   0.50 22.53 ?  158 LYS   A CG   1 
ATOM   3514 C  CD   A LYS   A 1 158 ? 2.799  -2.576  7.156   0.50 25.83 ?  158 LYS   A CD   1 
ATOM   3515 C  CD   B LYS   A 1 158 ? 2.359  -2.727  6.691   0.50 24.37 ?  158 LYS   A CD   1 
ATOM   3516 C  CE   A LYS   A 1 158 ? 1.578  -3.268  7.751   0.50 26.78 ?  158 LYS   A CE   1 
ATOM   3517 C  CE   B LYS   A 1 158 ? 1.122  -3.274  7.386   0.50 25.66 ?  158 LYS   A CE   1 
ATOM   3518 N  NZ   A LYS   A 1 158 ? 1.872  -4.643  8.242   0.50 27.36 ?  158 LYS   A NZ   1 
ATOM   3519 N  NZ   B LYS   A 1 158 ? 1.415  -4.477  8.209   0.50 26.47 ?  158 LYS   A NZ   1 
ATOM   3520 H  H    A LYS   A 1 158 ? 5.356  0.527   4.570   0.50 23.55 ?  158 LYS   A H    1 
ATOM   3521 H  H    B LYS   A 1 158 ? 5.087  0.159   4.101   0.50 20.61 ?  158 LYS   A H    1 
ATOM   3522 H  HA   A LYS   A 1 158 ? 5.047  -1.888  5.536   0.50 24.97 ?  158 LYS   A HA   1 
ATOM   3523 H  HA   B LYS   A 1 158 ? 4.701  -2.186  5.174   0.50 21.40 ?  158 LYS   A HA   1 
ATOM   3524 H  HB2  A LYS   A 1 158 ? 4.064  -0.218  6.707   0.50 26.95 ?  158 LYS   A HB2  1 
ATOM   3525 H  HB2  B LYS   A 1 158 ? 3.605  -0.425  6.100   0.50 24.26 ?  158 LYS   A HB2  1 
ATOM   3526 H  HB3  A LYS   A 1 158 ? 3.246  0.270   5.440   0.50 26.95 ?  158 LYS   A HB3  1 
ATOM   3527 H  HB3  B LYS   A 1 158 ? 2.888  -0.080  4.729   0.50 24.26 ?  158 LYS   A HB3  1 
ATOM   3528 H  HG2  A LYS   A 1 158 ? 1.833  -0.788  6.944   0.50 29.22 ?  158 LYS   A HG2  1 
ATOM   3529 H  HG2  B LYS   A 1 158 ? 1.365  -1.021  6.186   0.50 27.03 ?  158 LYS   A HG2  1 
ATOM   3530 H  HG3  A LYS   A 1 158 ? 1.876  -1.621  5.595   0.50 29.22 ?  158 LYS   A HG3  1 
ATOM   3531 H  HG3  B LYS   A 1 158 ? 1.561  -2.002  4.954   0.50 27.03 ?  158 LYS   A HG3  1 
ATOM   3532 H  HD2  A LYS   A 1 158 ? 3.246  -3.200  6.565   0.50 30.99 ?  158 LYS   A HD2  1 
ATOM   3533 H  HD2  B LYS   A 1 158 ? 2.778  -3.449  6.198   0.50 29.23 ?  158 LYS   A HD2  1 
ATOM   3534 H  HD3  A LYS   A 1 158 ? 3.386  -2.315  7.882   0.50 30.99 ?  158 LYS   A HD3  1 
ATOM   3535 H  HD3  B LYS   A 1 158 ? 2.965  -2.383  7.367   0.50 29.23 ?  158 LYS   A HD3  1 
ATOM   3536 H  HE2  A LYS   A 1 158 ? 1.243  -2.744  8.496   0.50 32.12 ?  158 LYS   A HE2  1 
ATOM   3537 H  HE2  B LYS   A 1 158 ? 0.761  -2.588  7.972   0.50 30.78 ?  158 LYS   A HE2  1 
ATOM   3538 H  HE3  A LYS   A 1 158 ? 0.894  -3.333  7.070   0.50 32.12 ?  158 LYS   A HE3  1 
ATOM   3539 H  HE3  B LYS   A 1 158 ? 0.465  -3.516  6.716   0.50 30.78 ?  158 LYS   A HE3  1 
ATOM   3540 H  HZ1  A LYS   A 1 158 ? 1.134  -5.007  8.582   0.50 32.82 ?  158 LYS   A HZ1  1 
ATOM   3541 H  HZ1  B LYS   A 1 158 ? 0.670  -4.767  8.599   0.50 31.75 ?  158 LYS   A HZ1  1 
ATOM   3542 H  HZ2  A LYS   A 1 158 ? 2.160  -5.147  7.569   0.50 32.82 ?  158 LYS   A HZ2  1 
ATOM   3543 H  HZ2  B LYS   A 1 158 ? 1.743  -5.124  7.694   0.50 31.75 ?  158 LYS   A HZ2  1 
ATOM   3544 H  HZ3  A LYS   A 1 158 ? 2.498  -4.614  8.873   0.50 32.82 ?  158 LYS   A HZ3  1 
ATOM   3545 H  HZ3  B LYS   A 1 158 ? 2.012  -4.278  8.838   0.50 31.75 ?  158 LYS   A HZ3  1 
ATOM   3546 N  N    A ASN   A 1 159 ? 3.440  -1.328  2.826   0.50 20.67 ?  159 ASN   A N    1 
ATOM   3547 N  N    B ASN   A 1 159 ? 3.244  -1.818  2.333   0.50 16.70 ?  159 ASN   A N    1 
ATOM   3548 C  CA   A ASN   A 1 159 ? 2.774  -2.018  1.727   0.50 21.08 ?  159 ASN   A CA   1 
ATOM   3549 C  CA   B ASN   A 1 159 ? 2.630  -2.583  1.251   0.50 17.07 ?  159 ASN   A CA   1 
ATOM   3550 C  C    A ASN   A 1 159 ? 3.671  -3.099  1.136   0.50 19.62 ?  159 ASN   A C    1 
ATOM   3551 C  C    B ASN   A 1 159 ? 3.589  -3.641  0.711   0.50 16.08 ?  159 ASN   A C    1 
ATOM   3552 O  O    A ASN   A 1 159 ? 3.210  -4.208  0.845   0.50 19.96 ?  159 ASN   A O    1 
ATOM   3553 O  O    B ASN   A 1 159 ? 3.196  -4.790  0.474   0.50 16.43 ?  159 ASN   A O    1 
ATOM   3554 C  CB   A ASN   A 1 159 ? 2.335  -1.011  0.661   0.50 23.38 ?  159 ASN   A CB   1 
ATOM   3555 C  CB   B ASN   A 1 159 ? 2.173  -1.639  0.137   0.50 19.53 ?  159 ASN   A CB   1 
ATOM   3556 C  CG   A ASN   A 1 159 ? 1.149  -0.171  1.106   0.50 25.69 ?  159 ASN   A CG   1 
ATOM   3557 C  CG   B ASN   A 1 159 ? 0.959  -0.815  0.529   0.50 22.15 ?  159 ASN   A CG   1 
ATOM   3558 O  OD1  A ASN   A 1 159 ? 0.252  -0.661  1.796   0.50 26.54 ?  159 ASN   A OD1  1 
ATOM   3559 O  OD1  B ASN   A 1 159 ? 0.736  -0.530  1.707   0.50 23.54 ?  159 ASN   A OD1  1 
ATOM   3560 N  ND2  A ASN   A 1 159 ? 1.134  1.097   0.709   0.50 26.47 ?  159 ASN   A ND2  1 
ATOM   3561 N  ND2  B ASN   A 1 159 ? 0.167  -0.425  -0.462  0.50 23.00 ?  159 ASN   A ND2  1 
ATOM   3562 H  H    A ASN   A 1 159 ? 3.552  -0.485  2.708   0.50 24.80 ?  159 ASN   A H    1 
ATOM   3563 H  H    B ASN   A 1 159 ? 3.306  -0.975  2.195   0.50 20.03 ?  159 ASN   A H    1 
ATOM   3564 H  HA   A ASN   A 1 159 ? 1.977  -2.453  2.065   0.50 25.28 ?  159 ASN   A HA   1 
ATOM   3565 H  HA   B ASN   A 1 159 ? 1.836  -3.032  1.592   0.50 20.48 ?  159 ASN   A HA   1 
ATOM   3566 H  HB2  A ASN   A 1 159 ? 3.070  -0.409  0.467   0.50 28.04 ?  159 ASN   A HB2  1 
ATOM   3567 H  HB2  B ASN   A 1 159 ? 2.896  -1.025  -0.074  0.50 23.42 ?  159 ASN   A HB2  1 
ATOM   3568 H  HB3  A ASN   A 1 159 ? 2.074  -1.489  -0.143  0.50 28.04 ?  159 ASN   A HB3  1 
ATOM   3569 H  HB3  B ASN   A 1 159 ? 1.937  -2.157  -0.645  0.50 23.42 ?  159 ASN   A HB3  1 
ATOM   3570 H  HD21 A ASN   A 1 159 ? 0.487  1.611   0.938   0.50 31.76 ?  159 ASN   A HD21 1 
ATOM   3571 H  HD21 B ASN   A 1 159 ? -0.534 0.049   -0.294  0.50 27.58 ?  159 ASN   A HD21 1 
ATOM   3572 H  HD22 A ASN   A 1 159 ? 1.774  1.405   0.228   0.50 31.76 ?  159 ASN   A HD22 1 
ATOM   3573 H  HD22 B ASN   A 1 159 ? 0.352  -0.643  -1.272  0.50 27.58 ?  159 ASN   A HD22 1 
ATOM   3574 N  N    A LEU   A 1 160 ? 4.962  -2.805  0.971   0.50 18.38 ?  160 LEU   A N    1 
ATOM   3575 N  N    B LEU   A 1 160 ? 4.860  -3.277  0.528   0.50 15.83 ?  160 LEU   A N    1 
ATOM   3576 C  CA   A LEU   A 1 160 ? 5.867  -3.819  0.439   0.50 17.55 ?  160 LEU   A CA   1 
ATOM   3577 C  CA   B LEU   A 1 160 ? 5.837  -4.236  0.026   0.50 16.49 ?  160 LEU   A CA   1 
ATOM   3578 C  C    A LEU   A 1 160 ? 6.086  -4.944  1.443   0.50 16.79 ?  160 LEU   A C    1 
ATOM   3579 C  C    B LEU   A 1 160 ? 6.060  -5.366  1.018   0.50 15.13 ?  160 LEU   A C    1 
ATOM   3580 O  O    A LEU   A 1 160 ? 6.134  -6.120  1.064   0.50 17.42 ?  160 LEU   A O    1 
ATOM   3581 O  O    B LEU   A 1 160 ? 6.112  -6.538  0.630   0.50 15.49 ?  160 LEU   A O    1 
ATOM   3582 C  CB   A LEU   A 1 160 ? 7.197  -3.190  0.032   0.50 17.03 ?  160 LEU   A CB   1 
ATOM   3583 C  CB   B LEU   A 1 160 ? 7.158  -3.531  -0.259  0.50 18.96 ?  160 LEU   A CB   1 
ATOM   3584 C  CG   A LEU   A 1 160 ? 8.239  -4.215  -0.426  0.50 16.73 ?  160 LEU   A CG   1 
ATOM   3585 C  CG   B LEU   A 1 160 ? 7.329  -2.902  -1.639  0.50 22.03 ?  160 LEU   A CG   1 
ATOM   3586 C  CD1  A LEU   A 1 160 ? 7.775  -4.952  -1.668  0.50 17.47 ?  160 LEU   A CD1  1 
ATOM   3587 C  CD1  B LEU   A 1 160 ? 8.754  -2.408  -1.811  0.50 23.01 ?  160 LEU   A CD1  1 
ATOM   3588 C  CD2  A LEU   A 1 160 ? 9.556  -3.524  -0.681  0.50 16.14 ?  160 LEU   A CD2  1 
ATOM   3589 C  CD2  B LEU   A 1 160 ? 6.964  -3.903  -2.721  0.50 23.16 ?  160 LEU   A CD2  1 
ATOM   3590 H  H    A LEU   A 1 160 ? 5.325  -2.045  1.158   0.50 22.04 ?  160 LEU   A H    1 
ATOM   3591 H  H    B LEU   A 1 160 ? 5.169  -2.498  0.694   0.50 18.98 ?  160 LEU   A H    1 
ATOM   3592 H  HA   A LEU   A 1 160 ? 5.467  -4.197  -0.357  0.50 21.05 ?  160 LEU   A HA   1 
ATOM   3593 H  HA   B LEU   A 1 160 ? 5.496  -4.625  -0.793  0.50 19.78 ?  160 LEU   A HA   1 
ATOM   3594 H  HB2  A LEU   A 1 160 ? 7.046  -2.564  -0.700  0.50 20.43 ?  160 LEU   A HB2  1 
ATOM   3595 H  HB2  B LEU   A 1 160 ? 7.258  -2.824  0.396   0.50 22.74 ?  160 LEU   A HB2  1 
ATOM   3596 H  HB3  A LEU   A 1 160 ? 7.565  -2.717  0.794   0.50 20.43 ?  160 LEU   A HB3  1 
ATOM   3597 H  HB3  B LEU   A 1 160 ? 7.871  -4.176  -0.143  0.50 22.74 ?  160 LEU   A HB3  1 
ATOM   3598 H  HG   A LEU   A 1 160 ? 8.382  -4.864  0.279   0.50 20.06 ?  160 LEU   A HG   1 
ATOM   3599 H  HG   B LEU   A 1 160 ? 6.739  -2.138  -1.712  0.50 26.43 ?  160 LEU   A HG   1 
ATOM   3600 H  HD11 A LEU   A 1 160 ? 8.501  -5.502  -1.994  0.50 20.95 ?  160 LEU   A HD11 1 
ATOM   3601 H  HD11 B LEU   A 1 160 ? 8.873  -2.100  -2.722  0.50 27.60 ?  160 LEU   A HD11 1 
ATOM   3602 H  HD12 A LEU   A 1 160 ? 7.013  -5.509  -1.438  0.50 20.95 ?  160 LEU   A HD12 1 
ATOM   3603 H  HD12 B LEU   A 1 160 ? 8.913  -1.680  -1.191  0.50 27.60 ?  160 LEU   A HD12 1 
ATOM   3604 H  HD13 A LEU   A 1 160 ? 7.519  -4.303  -2.342  0.50 20.95 ?  160 LEU   A HD13 1 
ATOM   3605 H  HD13 B LEU   A 1 160 ? 9.365  -3.139  -1.625  0.50 27.60 ?  160 LEU   A HD13 1 
ATOM   3606 H  HD21 A LEU   A 1 160 ? 10.208 -4.184  -0.964  0.50 19.35 ?  160 LEU   A HD21 1 
ATOM   3607 H  HD21 B LEU   A 1 160 ? 7.400  -3.649  -3.544  0.50 27.78 ?  160 LEU   A HD21 1 
ATOM   3608 H  HD22 A LEU   A 1 160 ? 9.435  -2.857  -1.375  0.50 19.35 ?  160 LEU   A HD22 1 
ATOM   3609 H  HD22 B LEU   A 1 160 ? 7.261  -4.786  -2.443  0.50 27.78 ?  160 LEU   A HD22 1 
ATOM   3610 H  HD23 A LEU   A 1 160 ? 9.855  -3.096  0.139   0.50 19.35 ?  160 LEU   A HD23 1 
ATOM   3611 H  HD23 B LEU   A 1 160 ? 6.001  -3.903  -2.837  0.50 27.78 ?  160 LEU   A HD23 1 
ATOM   3612 N  N    A TYR   A 1 161 ? 6.223  -4.603  2.726   0.50 16.48 ?  161 TYR   A N    1 
ATOM   3613 N  N    B TYR   A 1 161 ? 6.201  -5.032  2.300   0.50 14.38 ?  161 TYR   A N    1 
ATOM   3614 C  CA   A TYR   A 1 161 ? 6.368  -5.632  3.749   0.50 16.23 ?  161 TYR   A CA   1 
ATOM   3615 C  CA   B TYR   A 1 161 ? 6.344  -6.053  3.329   0.50 14.13 ?  161 TYR   A CA   1 
ATOM   3616 C  C    A TYR   A 1 161 ? 5.224  -6.635  3.692   0.50 16.99 ?  161 TYR   A C    1 
ATOM   3617 C  C    B TYR   A 1 161 ? 5.212  -7.063  3.251   0.50 14.43 ?  161 TYR   A C    1 
ATOM   3618 O  O    A TYR   A 1 161 ? 5.446  -7.848  3.773   0.50 16.58 ?  161 TYR   A O    1 
ATOM   3619 O  O    B TYR   A 1 161 ? 5.448  -8.272  3.194   0.50 14.35 ?  161 TYR   A O    1 
ATOM   3620 C  CB   A TYR   A 1 161 ? 6.455  -4.992  5.135   0.50 15.83 ?  161 TYR   A CB   1 
ATOM   3621 C  CB   B TYR   A 1 161 ? 6.368  -5.407  4.713   0.50 14.24 ?  161 TYR   A CB   1 
ATOM   3622 C  CG   A TYR   A 1 161 ? 6.328  -5.995  6.259   0.50 15.44 ?  161 TYR   A CG   1 
ATOM   3623 C  CG   B TYR   A 1 161 ? 6.358  -6.431  5.820   0.50 14.72 ?  161 TYR   A CG   1 
ATOM   3624 C  CD1  A TYR   A 1 161 ? 7.433  -6.694  6.724   0.50 15.14 ?  161 TYR   A CD1  1 
ATOM   3625 C  CD1  B TYR   A 1 161 ? 7.531  -7.038  6.228   0.50 14.66 ?  161 TYR   A CD1  1 
ATOM   3626 C  CD2  A TYR   A 1 161 ? 5.097  -6.241  6.853   0.50 15.91 ?  161 TYR   A CD2  1 
ATOM   3627 C  CD2  B TYR   A 1 161 ? 5.172  -6.817  6.437   0.50 15.39 ?  161 TYR   A CD2  1 
ATOM   3628 C  CE1  A TYR   A 1 161 ? 7.314  -7.619  7.748   0.50 15.65 ?  161 TYR   A CE1  1 
ATOM   3629 C  CE1  B TYR   A 1 161 ? 7.533  -7.991  7.226   0.50 14.35 ?  161 TYR   A CE1  1 
ATOM   3630 C  CE2  A TYR   A 1 161 ? 4.968  -7.159  7.874   0.50 16.23 ?  161 TYR   A CE2  1 
ATOM   3631 C  CE2  B TYR   A 1 161 ? 5.164  -7.770  7.439   0.50 15.57 ?  161 TYR   A CE2  1 
ATOM   3632 C  CZ   A TYR   A 1 161 ? 6.077  -7.844  8.321   0.50 16.74 ?  161 TYR   A CZ   1 
ATOM   3633 C  CZ   B TYR   A 1 161 ? 6.351  -8.353  7.827   0.50 15.03 ?  161 TYR   A CZ   1 
ATOM   3634 O  OH   A TYR   A 1 161 ? 5.939  -8.755  9.343   0.50 17.86 ?  161 TYR   A OH   1 
ATOM   3635 O  OH   B TYR   A 1 161 ? 6.358  -9.302  8.822   0.50 15.35 ?  161 TYR   A OH   1 
ATOM   3636 H  H    A TYR   A 1 161 ? 6.231  -3.796  3.023   0.50 19.76 ?  161 TYR   A H    1 
ATOM   3637 H  H    B TYR   A 1 161 ? 6.209  -4.236  2.596   0.50 17.24 ?  161 TYR   A H    1 
ATOM   3638 H  HA   A TYR   A 1 161 ? 7.187  -6.116  3.590   0.50 19.46 ?  161 TYR   A HA   1 
ATOM   3639 H  HA   B TYR   A 1 161 ? 7.175  -6.535  3.201   0.50 16.94 ?  161 TYR   A HA   1 
ATOM   3640 H  HB2  A TYR   A 1 161 ? 7.312  -4.550  5.221   0.50 18.98 ?  161 TYR   A HB2  1 
ATOM   3641 H  HB2  B TYR   A 1 161 ? 7.175  -4.881  4.800   0.50 17.08 ?  161 TYR   A HB2  1 
ATOM   3642 H  HB3  A TYR   A 1 161 ? 5.737  -4.344  5.229   0.50 18.98 ?  161 TYR   A HB3  1 
ATOM   3643 H  HB3  B TYR   A 1 161 ? 5.585  -4.846  4.818   0.50 17.08 ?  161 TYR   A HB3  1 
ATOM   3644 H  HD1  A TYR   A 1 161 ? 8.267  -6.539  6.338   0.50 18.16 ?  161 TYR   A HD1  1 
ATOM   3645 H  HD1  B TYR   A 1 161 ? 8.332  -6.805  5.821   0.50 17.58 ?  161 TYR   A HD1  1 
ATOM   3646 H  HD2  A TYR   A 1 161 ? 4.343  -5.785  6.554   0.50 19.09 ?  161 TYR   A HD2  1 
ATOM   3647 H  HD2  B TYR   A 1 161 ? 4.371  -6.425  6.177   0.50 18.46 ?  161 TYR   A HD2  1 
ATOM   3648 H  HE1  A TYR   A 1 161 ? 8.065  -8.075  8.049   0.50 18.77 ?  161 TYR   A HE1  1 
ATOM   3649 H  HE1  B TYR   A 1 161 ? 8.331  -8.391  7.488   0.50 17.21 ?  161 TYR   A HE1  1 
ATOM   3650 H  HE2  A TYR   A 1 161 ? 4.135  -7.315  8.259   0.50 19.47 ?  161 TYR   A HE2  1 
ATOM   3651 H  HE2  B TYR   A 1 161 ? 4.363  -8.014  7.848   0.50 18.67 ?  161 TYR   A HE2  1 
ATOM   3652 H  HH   A TYR   A 1 161 ? 5.138  -8.772  9.600   0.50 21.43 ?  161 TYR   A HH   1 
ATOM   3653 H  HH   B TYR   A 1 161 ? 5.573  -9.428  9.102   0.50 18.41 ?  161 TYR   A HH   1 
ATOM   3654 N  N    A ASP   A 1 162 ? 3.988  -6.151  3.551   0.50 18.26 ?  162 ASP   A N    1 
ATOM   3655 N  N    B ASP   A 1 162 ? 3.967  -6.582  3.251   0.50 15.38 ?  162 ASP   A N    1 
ATOM   3656 C  CA   A ASP   A 1 162 ? 2.854  -7.068  3.481   0.50 19.69 ?  162 ASP   A CA   1 
ATOM   3657 C  CA   B ASP   A 1 162 ? 2.829  -7.493  3.179   0.50 16.38 ?  162 ASP   A CA   1 
ATOM   3658 C  C    A ASP   A 1 162 ? 2.921  -7.939  2.231   0.50 20.67 ?  162 ASP   A C    1 
ATOM   3659 C  C    B ASP   A 1 162 ? 2.889  -8.337  1.913   0.50 17.28 ?  162 ASP   A C    1 
ATOM   3660 O  O    A ASP   A 1 162 ? 2.550  -9.118  2.268   0.50 21.37 ?  162 ASP   A O    1 
ATOM   3661 O  O    B ASP   A 1 162 ? 2.588  -9.536  1.937   0.50 18.03 ?  162 ASP   A O    1 
ATOM   3662 C  CB   A ASP   A 1 162 ? 1.528  -6.301  3.529   0.50 20.54 ?  162 ASP   A CB   1 
ATOM   3663 C  CB   B ASP   A 1 162 ? 1.510  -6.713  3.252   0.50 17.27 ?  162 ASP   A CB   1 
ATOM   3664 C  CG   A ASP   A 1 162 ? 1.276  -5.620  4.869   0.50 21.32 ?  162 ASP   A CG   1 
ATOM   3665 C  CG   B ASP   A 1 162 ? 1.197  -6.191  4.648   0.50 18.13 ?  162 ASP   A CG   1 
ATOM   3666 O  OD1  A ASP   A 1 162 ? 1.870  -6.021  5.889   0.50 21.61 ?  162 ASP   A OD1  1 
ATOM   3667 O  OD1  B ASP   A 1 162 ? 1.877  -6.591  5.616   0.50 19.32 ?  162 ASP   A OD1  1 
ATOM   3668 O  OD2  A ASP   A 1 162 ? 0.453  -4.681  4.901   0.50 22.12 -1 162 ASP   A OD2  1 
ATOM   3669 O  OD2  B ASP   A 1 162 ? 0.238  -5.390  4.775   0.50 18.40 -1 162 ASP   A OD2  1 
ATOM   3670 H  H    A ASP   A 1 162 ? 3.778  -5.317  3.498   0.50 21.90 ?  162 ASP   A H    1 
ATOM   3671 H  H    B ASP   A 1 162 ? 3.755  -5.757  3.288   0.50 18.44 ?  162 ASP   A H    1 
ATOM   3672 H  HA   A ASP   A 1 162 ? 2.876  -7.658  4.248   0.50 23.62 ?  162 ASP   A HA   1 
ATOM   3673 H  HA   B ASP   A 1 162 ? 2.849  -8.106  3.928   0.50 19.64 ?  162 ASP   A HA   1 
ATOM   3674 H  HB2  A ASP   A 1 162 ? 1.532  -5.609  2.855   0.50 24.64 ?  162 ASP   A HB2  1 
ATOM   3675 H  HB2  B ASP   A 1 162 ? 1.549  -5.955  2.654   0.50 20.72 ?  162 ASP   A HB2  1 
ATOM   3676 H  HB3  A ASP   A 1 162 ? 0.794  -6.920  3.368   0.50 24.64 ?  162 ASP   A HB3  1 
ATOM   3677 H  HB3  B ASP   A 1 162 ? 0.771  -7.292  3.011   0.50 20.72 ?  162 ASP   A HB3  1 
ATOM   3678 N  N    A LYS   A 1 163 ? 3.396  -7.381  1.112   0.50 21.60 ?  163 LYS   A N    1 
ATOM   3679 N  N    B LYS   A 1 163 ? 3.297  -7.732  0.799   0.50 18.44 ?  163 LYS   A N    1 
ATOM   3680 C  CA   A LYS   A 1 163 ? 3.497  -8.160  -0.121  0.50 22.63 ?  163 LYS   A CA   1 
ATOM   3681 C  CA   B LYS   A 1 163 ? 3.426  -8.483  -0.443  0.50 19.91 ?  163 LYS   A CA   1 
ATOM   3682 C  C    A LYS   A 1 163 ? 4.590  -9.224  -0.035  0.50 21.67 ?  163 LYS   A C    1 
ATOM   3683 C  C    B LYS   A 1 163 ? 4.513  -9.551  -0.335  0.50 18.75 ?  163 LYS   A C    1 
ATOM   3684 O  O    A LYS   A 1 163 ? 4.447  -10.306 -0.614  0.50 22.37 ?  163 LYS   A O    1 
ATOM   3685 O  O    B LYS   A 1 163 ? 4.302  -10.718 -0.692  0.50 19.90 ?  163 LYS   A O    1 
ATOM   3686 C  CB   A LYS   A 1 163 ? 3.748  -7.228  -1.309  0.50 24.95 ?  163 LYS   A CB   1 
ATOM   3687 C  CB   B LYS   A 1 163 ? 3.746  -7.520  -1.573  0.50 22.81 ?  163 LYS   A CB   1 
ATOM   3688 C  CG   A LYS   A 1 163 ? 3.792  -7.926  -2.663  0.50 27.04 ?  163 LYS   A CG   1 
ATOM   3689 C  CG   B LYS   A 1 163 ? 2.534  -6.863  -2.235  0.50 25.53 ?  163 LYS   A CG   1 
ATOM   3690 C  CD   A LYS   A 1 163 ? 4.212  -6.965  -3.767  0.50 29.30 ?  163 LYS   A CD   1 
ATOM   3691 C  CD   B LYS   A 1 163 ? 2.924  -6.279  -3.585  0.50 27.96 ?  163 LYS   A CD   1 
ATOM   3692 C  CE   A LYS   A 1 163 ? 4.131  -7.619  -5.138  0.50 31.04 ?  163 LYS   A CE   1 
ATOM   3693 C  CE   B LYS   A 1 163 ? 3.660  -7.313  -4.448  0.50 29.82 ?  163 LYS   A CE   1 
ATOM   3694 N  NZ   A LYS   A 1 163 ? 4.813  -6.810  -6.186  0.50 31.88 ?  163 LYS   A NZ   1 
ATOM   3695 N  NZ   B LYS   A 1 163 ? 4.462  -6.698  -5.507  0.50 30.63 ?  163 LYS   A NZ   1 
ATOM   3696 H  H    A LYS   A 1 163 ? 3.661  -6.567  1.043   0.50 25.91 ?  163 LYS   A H    1 
ATOM   3697 H  H    B LYS   A 1 163 ? 3.502  -6.897  0.736   0.50 22.12 ?  163 LYS   A H    1 
ATOM   3698 H  HA   A LYS   A 1 163 ? 2.654  -8.611  -0.277  0.50 27.15 ?  163 LYS   A HA   1 
ATOM   3699 H  HA   B LYS   A 1 163 ? 2.588  -8.912  -0.659  0.50 23.88 ?  163 LYS   A HA   1 
ATOM   3700 H  HB2  A LYS   A 1 163 ? 3.037  -6.568  -1.343  0.50 29.93 ?  163 LYS   A HB2  1 
ATOM   3701 H  HB2  B LYS   A 1 163 ? 4.298  -6.796  -1.254  0.50 27.36 ?  163 LYS   A HB2  1 
ATOM   3702 H  HB3  A LYS   A 1 163 ? 4.600  -6.782  -1.182  0.50 29.93 ?  163 LYS   A HB3  1 
ATOM   3703 H  HB3  B LYS   A 1 163 ? 4.253  -8.048  -2.195  0.50 27.36 ?  163 LYS   A HB3  1 
ATOM   3704 H  HG2  A LYS   A 1 163 ? 4.436  -8.650  -2.636  0.50 32.43 ?  163 LYS   A HG2  1 
ATOM   3705 H  HG2  B LYS   A 1 163 ? 1.832  -7.516  -2.372  0.50 30.62 ?  163 LYS   A HG2  1 
ATOM   3706 H  HG3  A LYS   A 1 163 ? 2.910  -8.267  -2.877  0.50 32.43 ?  163 LYS   A HG3  1 
ATOM   3707 H  HG3  B LYS   A 1 163 ? 2.209  -6.135  -1.668  0.50 30.62 ?  163 LYS   A HG3  1 
ATOM   3708 H  HD2  A LYS   A 1 163 ? 3.619  -6.196  -3.764  0.50 35.15 ?  163 LYS   A HD2  1 
ATOM   3709 H  HD2  B LYS   A 1 163 ? 2.116  -6.007  -4.063  0.50 33.54 ?  163 LYS   A HD2  1 
ATOM   3710 H  HD3  A LYS   A 1 163 ? 5.127  -6.683  -3.616  0.50 35.15 ?  163 LYS   A HD3  1 
ATOM   3711 H  HD3  B LYS   A 1 163 ? 3.502  -5.513  -3.450  0.50 33.54 ?  163 LYS   A HD3  1 
ATOM   3712 H  HE2  A LYS   A 1 163 ? 4.546  -8.494  -5.107  0.50 37.24 ?  163 LYS   A HE2  1 
ATOM   3713 H  HE2  B LYS   A 1 163 ? 4.290  -7.854  -3.948  0.50 35.77 ?  163 LYS   A HE2  1 
ATOM   3714 H  HE3  A LYS   A 1 163 ? 3.200  -7.708  -5.389  0.50 37.24 ?  163 LYS   A HE3  1 
ATOM   3715 H  HE3  B LYS   A 1 163 ? 2.994  -7.890  -4.832  0.50 35.77 ?  163 LYS   A HE3  1 
ATOM   3716 H  HZ1  A LYS   A 1 163 ? 4.751  -7.219  -6.974  0.50 38.25 ?  163 LYS   A HZ1  1 
ATOM   3717 H  HZ1  B LYS   A 1 163 ? 4.878  -7.337  -5.963  0.50 36.75 ?  163 LYS   A HZ1  1 
ATOM   3718 H  HZ2  A LYS   A 1 163 ? 4.431  -6.008  -6.245  0.50 38.25 ?  163 LYS   A HZ2  1 
ATOM   3719 H  HZ2  B LYS   A 1 163 ? 3.936  -6.240  -6.046  0.50 36.75 ?  163 LYS   A HZ2  1 
ATOM   3720 H  HZ3  A LYS   A 1 163 ? 5.673  -6.707  -5.981  0.50 38.25 ?  163 LYS   A HZ3  1 
ATOM   3721 H  HZ3  B LYS   A 1 163 ? 5.071  -6.153  -5.151  0.50 36.75 ?  163 LYS   A HZ3  1 
ATOM   3722 N  N    A LEU   A 1 164 ? 5.686  -8.936  0.669   0.50 20.09 ?  164 LEU   A N    1 
ATOM   3723 N  N    B LEU   A 1 164 ? 5.701  -9.155  0.128   0.50 17.25 ?  164 LEU   A N    1 
ATOM   3724 C  CA   A LEU   A 1 164 ? 6.781  -9.898  0.777   0.50 19.16 ?  164 LEU   A CA   1 
ATOM   3725 C  CA   B LEU   A 1 164 ? 6.785  -10.113 0.320   0.50 16.42 ?  164 LEU   A CA   1 
ATOM   3726 C  C    A LEU   A 1 164 ? 6.381  -11.104 1.618   0.50 19.56 ?  164 LEU   A C    1 
ATOM   3727 C  C    B LEU   A 1 164 ? 6.335  -11.287 1.177   0.50 16.66 ?  164 LEU   A C    1 
ATOM   3728 O  O    A LEU   A 1 164 ? 6.757  -12.239 1.305   0.50 20.18 ?  164 LEU   A O    1 
ATOM   3729 O  O    B LEU   A 1 164 ? 6.633  -12.447 0.867   0.50 17.56 ?  164 LEU   A O    1 
ATOM   3730 C  CB   A LEU   A 1 164 ? 8.003  -9.217  1.389   0.50 18.05 ?  164 LEU   A CB   1 
ATOM   3731 C  CB   B LEU   A 1 164 ? 7.967  -9.413  0.990   0.50 16.00 ?  164 LEU   A CB   1 
ATOM   3732 C  CG   A LEU   A 1 164 ? 8.674  -8.151  0.522   0.50 17.40 ?  164 LEU   A CG   1 
ATOM   3733 C  CG   B LEU   A 1 164 ? 8.784  -8.448  0.136   0.50 15.57 ?  164 LEU   A CG   1 
ATOM   3734 C  CD1  A LEU   A 1 164 ? 9.621  -7.294  1.355   0.50 16.89 ?  164 LEU   A CD1  1 
ATOM   3735 C  CD1  B LEU   A 1 164 ? 9.551  -7.459  1.001   0.50 15.08 ?  164 LEU   A CD1  1 
ATOM   3736 C  CD2  A LEU   A 1 164 ? 9.419  -8.805  -0.638  0.50 17.36 ?  164 LEU   A CD2  1 
ATOM   3737 C  CD2  B LEU   A 1 164 ? 9.745  -9.248  -0.700  0.50 16.16 ?  164 LEU   A CD2  1 
ATOM   3738 H  H    A LEU   A 1 164 ? 5.819  -8.201  1.086   0.50 24.10 ?  164 LEU   A H    1 
ATOM   3739 H  H    B LEU   A 1 164 ? 5.901  -8.349  0.337   0.50 20.69 ?  164 LEU   A H    1 
ATOM   3740 H  HA   A LEU   A 1 164 ? 7.018  -10.218 -0.107  0.50 22.98 ?  164 LEU   A HA   1 
ATOM   3741 H  HA   B LEU   A 1 164 ? 7.070  -10.462 -0.537  0.50 19.70 ?  164 LEU   A HA   1 
ATOM   3742 H  HB2  A LEU   A 1 164 ? 7.733  -8.793  2.216   0.50 21.65 ?  164 LEU   A HB2  1 
ATOM   3743 H  HB2  B LEU   A 1 164 ? 7.628  -8.915  1.746   0.50 19.19 ?  164 LEU   A HB2  1 
ATOM   3744 H  HB3  A LEU   A 1 164 ? 8.669  -9.899  1.578   0.50 21.65 ?  164 LEU   A HB3  1 
ATOM   3745 H  HB3  B LEU   A 1 164 ? 8.576  -10.100 1.307   0.50 19.19 ?  164 LEU   A HB3  1 
ATOM   3746 H  HG   A LEU   A 1 164 ? 7.992  -7.571  0.151   0.50 20.87 ?  164 LEU   A HG   1 
ATOM   3747 H  HG   B LEU   A 1 164 ? 8.194  -7.954  -0.455  0.50 18.68 ?  164 LEU   A HG   1 
ATOM   3748 H  HD11 A LEU   A 1 164 ? 10.041 -6.637  0.780   0.50 20.25 ?  164 LEU   A HD11 1 
ATOM   3749 H  HD11 B LEU   A 1 164 ? 10.061 -6.867  0.427   0.50 18.08 ?  164 LEU   A HD11 1 
ATOM   3750 H  HD12 A LEU   A 1 164 ? 9.111  -6.848  2.051   0.50 20.25 ?  164 LEU   A HD12 1 
ATOM   3751 H  HD12 B LEU   A 1 164 ? 8.920  -6.944  1.529   0.50 18.08 ?  164 LEU   A HD12 1 
ATOM   3752 H  HD13 A LEU   A 1 164 ? 10.295 -7.865  1.755   0.50 20.25 ?  164 LEU   A HD13 1 
ATOM   3753 H  HD13 B LEU   A 1 164 ? 10.149 -7.948  1.587   0.50 18.08 ?  164 LEU   A HD13 1 
ATOM   3754 H  HD21 A LEU   A 1 164 ? 9.881  -8.117  -1.145  0.50 20.82 ?  164 LEU   A HD21 1 
ATOM   3755 H  HD21 B LEU   A 1 164 ? 10.216 -8.651  -1.298  0.50 19.38 ?  164 LEU   A HD21 1 
ATOM   3756 H  HD22 A LEU   A 1 164 ? 10.061 -9.440  -0.284  0.50 20.82 ?  164 LEU   A HD22 1 
ATOM   3757 H  HD22 B LEU   A 1 164 ? 10.378 -9.694  -0.111  0.50 19.38 ?  164 LEU   A HD22 1 
ATOM   3758 H  HD23 A LEU   A 1 164 ? 8.781  -9.262  -1.208  0.50 20.82 ?  164 LEU   A HD23 1 
ATOM   3759 H  HD23 B LEU   A 1 164 ? 9.248  -9.908  -1.207  0.50 19.38 ?  164 LEU   A HD23 1 
ATOM   3760 N  N    A VAL   A 1 165 ? 5.648  -10.872 2.705   0.50 19.82 ?  165 VAL   A N    1 
ATOM   3761 N  N    B VAL   A 1 165 ? 5.614  -11.000 2.261   0.50 16.98 ?  165 VAL   A N    1 
ATOM   3762 C  CA   A VAL   A 1 165 ? 5.165  -11.971 3.536   0.50 20.31 ?  165 VAL   A CA   1 
ATOM   3763 C  CA   B VAL   A 1 165 ? 5.230  -12.037 3.214   0.50 18.05 ?  165 VAL   A CA   1 
ATOM   3764 C  C    A VAL   A 1 165 ? 4.131  -12.793 2.778   0.50 21.19 ?  165 VAL   A C    1 
ATOM   3765 C  C    B VAL   A 1 165 ? 4.161  -12.941 2.616   0.50 18.30 ?  165 VAL   A C    1 
ATOM   3766 O  O    A VAL   A 1 165 ? 4.263  -14.014 2.632   0.50 21.62 ?  165 VAL   A O    1 
ATOM   3767 O  O    B VAL   A 1 165 ? 4.232  -14.173 2.712   0.50 19.02 ?  165 VAL   A O    1 
ATOM   3768 C  CB   A VAL   A 1 165 ? 4.591  -11.412 4.851   0.50 20.13 ?  165 VAL   A CB   1 
ATOM   3769 C  CB   B VAL   A 1 165 ? 4.765  -11.383 4.529   0.50 19.20 ?  165 VAL   A CB   1 
ATOM   3770 C  CG1  A VAL   A 1 165 ? 3.900  -12.507 5.649   0.50 20.50 ?  165 VAL   A CG1  1 
ATOM   3771 C  CG1  B VAL   A 1 165 ? 4.027  -12.381 5.403   0.50 19.90 ?  165 VAL   A CG1  1 
ATOM   3772 C  CG2  A VAL   A 1 165 ? 5.690  -10.734 5.664   0.50 19.71 ?  165 VAL   A CG2  1 
ATOM   3773 C  CG2  B VAL   A 1 165 ? 5.955  -10.788 5.267   0.50 19.26 ?  165 VAL   A CG2  1 
ATOM   3774 H  H    A VAL   A 1 165 ? 5.423  -10.095 2.985   0.50 23.77 ?  165 VAL   A H    1 
ATOM   3775 H  H    B VAL   A 1 165 ? 5.327  -10.212 2.467   0.50 20.36 ?  165 VAL   A H    1 
ATOM   3776 H  HA   A VAL   A 1 165 ? 5.904  -12.556 3.757   0.50 24.36 ?  165 VAL   A HA   1 
ATOM   3777 H  HA   B VAL   A 1 165 ? 5.997  -12.584 3.413   0.50 21.65 ?  165 VAL   A HA   1 
ATOM   3778 H  HB   A VAL   A 1 165 ? 3.928  -10.738 4.641   0.50 24.15 ?  165 VAL   A HB   1 
ATOM   3779 H  HB   B VAL   A 1 165 ? 4.156  -10.654 4.329   0.50 23.03 ?  165 VAL   A HB   1 
ATOM   3780 H  HG11 A VAL   A 1 165 ? 3.756  -12.190 6.553   0.50 24.59 ?  165 VAL   A HG11 1 
ATOM   3781 H  HG11 B VAL   A 1 165 ? 4.008  -12.045 6.313   0.50 23.87 ?  165 VAL   A HG11 1 
ATOM   3782 H  HG12 A VAL   A 1 165 ? 3.048  -12.710 5.232   0.50 24.59 ?  165 VAL   A HG12 1 
ATOM   3783 H  HG12 B VAL   A 1 165 ? 3.122  -12.480 5.070   0.50 23.87 ?  165 VAL   A HG12 1 
ATOM   3784 H  HG13 A VAL   A 1 165 ? 4.465  -13.292 5.659   0.50 24.59 ?  165 VAL   A HG13 1 
ATOM   3785 H  HG13 B VAL   A 1 165 ? 4.494  -13.227 5.373   0.50 23.87 ?  165 VAL   A HG13 1 
ATOM   3786 H  HG21 A VAL   A 1 165 ? 5.317  -10.413 6.500   0.50 23.64 ?  165 VAL   A HG21 1 
ATOM   3787 H  HG21 B VAL   A 1 165 ? 5.654  -10.412 6.108   0.50 23.10 ?  165 VAL   A HG21 1 
ATOM   3788 H  HG22 A VAL   A 1 165 ? 6.397  -11.374 5.841   0.50 23.64 ?  165 VAL   A HG22 1 
ATOM   3789 H  HG22 B VAL   A 1 165 ? 6.607  -11.487 5.432   0.50 23.10 ?  165 VAL   A HG22 1 
ATOM   3790 H  HG23 A VAL   A 1 165 ? 6.045  -9.985  5.154   0.50 23.64 ?  165 VAL   A HG23 1 
ATOM   3791 H  HG23 B VAL   A 1 165 ? 6.353  -10.091 4.718   0.50 23.10 ?  165 VAL   A HG23 1 
ATOM   3792 N  N    A SER   A 1 166 ? 3.084  -12.130 2.283   0.50 21.86 ?  166 SER   A N    1 
ATOM   3793 N  N    B SER   A 1 166 ? 3.152  -12.336 1.985   0.50 18.55 ?  166 SER   A N    1 
ATOM   3794 C  CA   A SER   A 1 166 ? 1.966  -12.828 1.657   0.50 22.54 ?  166 SER   A CA   1 
ATOM   3795 C  CA   B SER   A 1 166 ? 2.020  -13.103 1.480   0.50 19.47 ?  166 SER   A CA   1 
ATOM   3796 C  C    A SER   A 1 166 ? 2.362  -13.570 0.390   0.50 21.64 ?  166 SER   A C    1 
ATOM   3797 C  C    B SER   A 1 166 ? 2.474  -14.191 0.525   0.50 19.40 ?  166 SER   A C    1 
ATOM   3798 O  O    A SER   A 1 166 ? 1.651  -14.499 -0.015  0.50 21.81 ?  166 SER   A O    1 
ATOM   3799 O  O    B SER   A 1 166 ? 1.941  -15.306 0.543   0.50 19.67 ?  166 SER   A O    1 
ATOM   3800 C  CB   A SER   A 1 166 ? 0.856  -11.828 1.328   0.50 24.08 ?  166 SER   A CB   1 
ATOM   3801 C  CB   B SER   A 1 166 ? 1.035  -12.174 0.769   0.50 20.77 ?  166 SER   A CB   1 
ATOM   3802 O  OG   A SER   A 1 166 ? 0.418  -11.151 2.497   0.50 25.68 ?  166 SER   A OG   1 
ATOM   3803 O  OG   B SER   A 1 166 ? 0.379  -11.329 1.695   0.50 22.67 ?  166 SER   A OG   1 
ATOM   3804 H  H    A SER   A 1 166 ? 2.985  -11.280 2.316   0.50 26.22 ?  166 SER   A H    1 
ATOM   3805 H  H    B SER   A 1 166 ? 3.093  -11.496 1.841   0.50 22.25 ?  166 SER   A H    1 
ATOM   3806 H  HA   A SER   A 1 166 ? 1.597  -13.474 2.283   0.50 27.04 ?  166 SER   A HA   1 
ATOM   3807 H  HA   B SER   A 1 166 ? 1.547  -13.517 2.219   0.50 23.35 ?  166 SER   A HA   1 
ATOM   3808 H  HB2  A SER   A 1 166 ? 1.193  -11.180 0.688   0.50 28.88 ?  166 SER   A HB2  1 
ATOM   3809 H  HB2  B SER   A 1 166 ? 1.523  -11.639 0.119   0.50 24.92 ?  166 SER   A HB2  1 
ATOM   3810 H  HB3  A SER   A 1 166 ? 0.100  -12.304 0.944   0.50 28.88 ?  166 SER   A HB3  1 
ATOM   3811 H  HB3  B SER   A 1 166 ? 0.364  -12.707 0.309   0.50 24.92 ?  166 SER   A HB3  1 
ATOM   3812 H  HG   A SER   A 1 166 ? 1.055  -10.712 2.830   0.50 30.80 ?  166 SER   A HG   1 
ATOM   3813 H  HG   B SER   A 1 166 ? 0.942  -10.825 2.071   0.50 27.20 ?  166 SER   A HG   1 
ATOM   3814 N  N    A SER   A 1 167 ? 3.463  -13.182 -0.253  0.50 21.10 ?  167 SER   A N    1 
ATOM   3815 N  N    B SER   A 1 167 ? 3.458  -13.886 -0.313  0.50 19.31 ?  167 SER   A N    1 
ATOM   3816 C  CA   A SER   A 1 167 ? 3.929  -13.857 -1.456  0.50 20.63 ?  167 SER   A CA   1 
ATOM   3817 C  CA   B SER   A 1 167 ? 3.879  -14.771 -1.384  0.50 19.10 ?  167 SER   A CA   1 
ATOM   3818 C  C    A SER   A 1 167 ? 5.124  -14.765 -1.204  0.50 20.63 ?  167 SER   A C    1 
ATOM   3819 C  C    B SER   A 1 167 ? 5.044  -15.662 -0.990  0.50 18.29 ?  167 SER   A C    1 
ATOM   3820 O  O    A SER   A 1 167 ? 5.675  -15.317 -2.161  0.50 20.61 ?  167 SER   A O    1 
ATOM   3821 O  O    B SER   A 1 167 ? 5.667  -16.259 -1.872  0.50 18.44 ?  167 SER   A O    1 
ATOM   3822 C  CB   A SER   A 1 167 ? 4.275  -12.842 -2.550  0.50 20.96 ?  167 SER   A CB   1 
ATOM   3823 C  CB   B SER   A 1 167 ? 4.252  -13.947 -2.619  0.50 19.55 ?  167 SER   A CB   1 
ATOM   3824 O  OG   A SER   A 1 167 ? 5.415  -12.074 -2.197  0.50 21.56 ?  167 SER   A OG   1 
ATOM   3825 O  OG   B SER   A 1 167 ? 5.279  -13.010 -2.318  0.50 20.36 ?  167 SER   A OG   1 
ATOM   3826 H  H    A SER   A 1 167 ? 3.950  -12.516 -0.013  0.50 25.31 ?  167 SER   A H    1 
ATOM   3827 H  H    B SER   A 1 167 ? 3.899  -13.153 -0.279  0.50 23.17 ?  167 SER   A H    1 
ATOM   3828 H  HA   A SER   A 1 167 ? 3.210  -14.415 -1.790  0.50 24.75 ?  167 SER   A HA   1 
ATOM   3829 H  HA   B SER   A 1 167 ? 3.133  -15.348 -1.621  0.50 22.91 ?  167 SER   A HA   1 
ATOM   3830 H  HB2  A SER   A 1 167 ? 4.457  -13.324 -3.373  0.50 25.14 ?  167 SER   A HB2  1 
ATOM   3831 H  HB2  B SER   A 1 167 ? 4.560  -14.550 -3.313  0.50 23.45 ?  167 SER   A HB2  1 
ATOM   3832 H  HB3  A SER   A 1 167 ? 3.515  -12.250 -2.677  0.50 25.14 ?  167 SER   A HB3  1 
ATOM   3833 H  HB3  B SER   A 1 167 ? 3.458  -13.474 -2.924  0.50 23.45 ?  167 SER   A HB3  1 
ATOM   3834 H  HG   A SER   A 1 167 ? 5.259  -11.657 -1.484  0.50 25.86 ?  167 SER   A HG   1 
ATOM   3835 H  HG   B SER   A 1 167 ? 4.993  -12.460 -1.750  0.50 24.42 ?  167 SER   A HG   1 
ATOM   3836 N  N    A PHE   A 1 168 ? 5.538  -14.940 0.050   0.50 20.57 ?  168 PHE   A N    1 
ATOM   3837 N  N    B PHE   A 1 168 ? 5.337  -15.799 0.306   0.50 17.39 ?  168 PHE   A N    1 
ATOM   3838 C  CA   A PHE   A 1 168 ? 6.732  -15.726 0.330   0.50 21.15 ?  168 PHE   A CA   1 
ATOM   3839 C  CA   B PHE   A 1 168 ? 6.589  -16.451 0.682   0.50 16.94 ?  168 PHE   A CA   1 
ATOM   3840 C  C    A PHE   A 1 168 ? 6.422  -17.212 0.239   0.50 23.65 ?  168 PHE   A C    1 
ATOM   3841 C  C    B PHE   A 1 168 ? 6.539  -17.971 0.543   0.50 17.80 ?  168 PHE   A C    1 
ATOM   3842 O  O    A PHE   A 1 168 ? 5.431  -17.688 0.802   0.50 24.35 ?  168 PHE   A O    1 
ATOM   3843 O  O    B PHE   A 1 168 ? 7.448  -18.563 -0.051  0.50 17.95 ?  168 PHE   A O    1 
ATOM   3844 C  CB   A PHE   A 1 168 ? 7.308  -15.409 1.708   0.50 19.44 ?  168 PHE   A CB   1 
ATOM   3845 C  CB   B PHE   A 1 168 ? 7.050  -16.056 2.085   0.50 17.22 ?  168 PHE   A CB   1 
ATOM   3846 C  CG   A PHE   A 1 168 ? 8.558  -16.192 2.022   0.50 17.99 ?  168 PHE   A CG   1 
ATOM   3847 C  CG   B PHE   A 1 168 ? 8.419  -16.581 2.420   0.50 17.12 ?  168 PHE   A CG   1 
ATOM   3848 C  CD1  A PHE   A 1 168 ? 9.759  -15.868 1.417   0.50 17.49 ?  168 PHE   A CD1  1 
ATOM   3849 C  CD1  B PHE   A 1 168 ? 9.537  -16.061 1.791   0.50 17.41 ?  168 PHE   A CD1  1 
ATOM   3850 C  CD2  A PHE   A 1 168 ? 8.528  -17.261 2.903   0.50 17.05 ?  168 PHE   A CD2  1 
ATOM   3851 C  CD2  B PHE   A 1 168 ? 8.589  -17.608 3.333   0.50 16.88 ?  168 PHE   A CD2  1 
ATOM   3852 C  CE1  A PHE   A 1 168 ? 10.908 -16.585 1.689   0.50 16.72 ?  168 PHE   A CE1  1 
ATOM   3853 C  CE1  B PHE   A 1 168 ? 10.798 -16.543 2.075   0.50 17.66 ?  168 PHE   A CE1  1 
ATOM   3854 C  CE2  A PHE   A 1 168 ? 9.681  -17.982 3.181   0.50 16.41 ?  168 PHE   A CE2  1 
ATOM   3855 C  CE2  B PHE   A 1 168 ? 9.855  -18.095 3.621   0.50 17.02 ?  168 PHE   A CE2  1 
ATOM   3856 C  CZ   A PHE   A 1 168 ? 10.870 -17.640 2.572   0.50 16.43 ?  168 PHE   A CZ   1 
ATOM   3857 C  CZ   B PHE   A 1 168 ? 10.959 -17.559 2.992   0.50 17.57 ?  168 PHE   A CZ   1 
ATOM   3858 H  H    A PHE   A 1 168 ? 5.150  -14.621 0.751   0.50 24.67 ?  168 PHE   A H    1 
ATOM   3859 H  H    B PHE   A 1 168 ? 4.850  -15.538 0.965   0.50 20.86 ?  168 PHE   A H    1 
ATOM   3860 H  HA   A PHE   A 1 168 ? 7.408  -15.522 -0.331  0.50 25.37 ?  168 PHE   A HA   1 
ATOM   3861 H  HA   B PHE   A 1 168 ? 7.274  -16.148 0.070   0.50 20.32 ?  168 PHE   A HA   1 
ATOM   3862 H  HB2  A PHE   A 1 168 ? 7.532  -14.466 1.747   0.50 23.32 ?  168 PHE   A HB2  1 
ATOM   3863 H  HB2  B PHE   A 1 168 ? 7.078  -15.090 2.146   0.50 20.65 ?  168 PHE   A HB2  1 
ATOM   3864 H  HB3  A PHE   A 1 168 ? 6.646  -15.618 2.386   0.50 23.32 ?  168 PHE   A HB3  1 
ATOM   3865 H  HB3  B PHE   A 1 168 ? 6.428  -16.414 2.737   0.50 20.65 ?  168 PHE   A HB3  1 
ATOM   3866 H  HD1  A PHE   A 1 168 ? 9.798  -15.153 0.824   0.50 20.98 ?  168 PHE   A HD1  1 
ATOM   3867 H  HD1  B PHE   A 1 168 ? 9.439  -15.375 1.172   0.50 20.89 ?  168 PHE   A HD1  1 
ATOM   3868 H  HD2  A PHE   A 1 168 ? 7.728  -17.495 3.317   0.50 20.45 ?  168 PHE   A HD2  1 
ATOM   3869 H  HD2  B PHE   A 1 168 ? 7.846  -17.974 3.759   0.50 20.24 ?  168 PHE   A HD2  1 
ATOM   3870 H  HE1  A PHE   A 1 168 ? 11.713 -16.351 1.281   0.50 20.05 ?  168 PHE   A HE1  1 
ATOM   3871 H  HE1  B PHE   A 1 168 ? 11.544 -16.180 1.651   0.50 21.18 ?  168 PHE   A HE1  1 
ATOM   3872 H  HE2  A PHE   A 1 168 ? 9.652  -18.698 3.777   0.50 19.68 ?  168 PHE   A HE2  1 
ATOM   3873 H  HE2  B PHE   A 1 168 ? 9.960  -18.784 4.240   0.50 20.41 ?  168 PHE   A HE2  1 
ATOM   3874 H  HZ   A PHE   A 1 168 ? 11.647 -18.123 2.757   0.50 19.71 ?  168 PHE   A HZ   1 
ATOM   3875 H  HZ   B PHE   A 1 168 ? 11.810 -17.884 3.185   0.50 21.07 ?  168 PHE   A HZ   1 
ATOM   3876 N  N    A LEU   A 1 169 ? 7.284  -17.942 -0.455  0.50 25.16 ?  169 LEU   A N    1 
ATOM   3877 N  N    B LEU   A 1 169 ? 5.534  -18.627 1.123   0.50 19.32 ?  169 LEU   A N    1 
ATOM   3878 C  CA   A LEU   A 1 169 ? 7.128  -19.378 -0.593  0.50 26.64 ?  169 LEU   A CA   1 
ATOM   3879 C  CA   B LEU   A 1 169 ? 5.503  -20.099 1.109   0.50 21.54 ?  169 LEU   A CA   1 
ATOM   3880 C  C    A LEU   A 1 169 ? 8.016  -20.085 0.423   0.50 27.18 ?  169 LEU   A C    1 
ATOM   3881 C  C    B LEU   A 1 169 ? 4.867  -20.636 -0.169  0.50 22.70 ?  169 LEU   A C    1 
ATOM   3882 O  O    A LEU   A 1 169 ? 7.531  -20.520 1.469   0.50 27.60 ?  169 LEU   A O    1 
ATOM   3883 O  O    B LEU   A 1 169 ? 3.895  -20.079 -0.674  0.50 22.94 ?  169 LEU   A O    1 
ATOM   3884 C  CB   A LEU   A 1 169 ? 7.478  -19.810 -2.018  0.50 27.41 ?  169 LEU   A CB   1 
ATOM   3885 C  CB   B LEU   A 1 169 ? 4.765  -20.657 2.335   0.50 22.63 ?  169 LEU   A CB   1 
ATOM   3886 C  CG   A LEU   A 1 169 ? 7.110  -21.241 -2.407  0.50 28.05 ?  169 LEU   A CG   1 
ATOM   3887 C  CG   B LEU   A 1 169 ? 5.140  -22.063 2.843   0.50 23.61 ?  169 LEU   A CG   1 
ATOM   3888 C  CD1  A LEU   A 1 169 ? 5.669  -21.540 -2.036  0.50 28.28 ?  169 LEU   A CD1  1 
ATOM   3889 C  CD1  B LEU   A 1 169 ? 4.434  -22.365 4.160   0.50 24.02 ?  169 LEU   A CD1  1 
ATOM   3890 C  CD2  A LEU   A 1 169 ? 7.332  -21.453 -3.896  0.50 28.21 ?  169 LEU   A CD2  1 
ATOM   3891 C  CD2  B LEU   A 1 169 ? 4.840  -23.171 1.841   0.50 24.45 ?  169 LEU   A CD2  1 
ATOM   3892 O  OXT  A LEU   A 1 169 ? 9.229  -20.222 0.242   0.50 27.03 -1 169 LEU   A OXT  1 
ATOM   3893 O  OXT  B LEU   A 1 169 ? 5.307  -21.646 -0.722  0.50 23.68 -1 169 LEU   A OXT  1 
ATOM   3894 H  H    A LEU   A 1 169 ? 7.974  -17.627 -0.856  0.50 30.18 ?  169 LEU   A H    1 
ATOM   3895 H  H    B LEU   A 1 169 ? 4.874  -18.255 1.534   0.50 23.17 ?  169 LEU   A H    1 
ATOM   3896 H  HA   A LEU   A 1 169 ? 6.208  -19.615 -0.408  0.50 31.96 ?  169 LEU   A HA   1 
ATOM   3897 H  HA   B LEU   A 1 169 ? 6.413  -20.421 1.140   0.50 25.83 ?  169 LEU   A HA   1 
ATOM   3898 H  HB2  A LEU   A 1 169 ? 7.019  -19.219 -2.634  0.50 32.88 ?  169 LEU   A HB2  1 
ATOM   3899 H  HB2  B LEU   A 1 169 ? 4.913  -20.049 3.072   0.50 27.15 ?  169 LEU   A HB2  1 
ATOM   3900 H  HB3  A LEU   A 1 169 ? 8.436  -19.717 -2.138  0.50 32.88 ?  169 LEU   A HB3  1 
ATOM   3901 H  HB3  B LEU   A 1 169 ? 3.820  -20.681 2.125   0.50 27.15 ?  169 LEU   A HB3  1 
ATOM   3902 H  HG   A LEU   A 1 169 ? 7.682  -21.860 -1.926  0.50 33.65 ?  169 LEU   A HG   1 
ATOM   3903 H  HG   B LEU   A 1 169 ? 6.092  -22.082 3.018   0.50 28.31 ?  169 LEU   A HG   1 
ATOM   3904 H  HD11 A LEU   A 1 169 ? 5.382  -22.338 -2.504  0.50 33.93 ?  169 LEU   A HD11 1 
ATOM   3905 H  HD11 B LEU   A 1 169 ? 4.556  -23.303 4.375   0.50 28.82 ?  169 LEU   A HD11 1 
ATOM   3906 H  HD12 A LEU   A 1 169 ? 5.612  -21.681 -1.077  0.50 33.93 ?  169 LEU   A HD12 1 
ATOM   3907 H  HD12 B LEU   A 1 169 ? 4.821  -21.815 4.859   0.50 28.82 ?  169 LEU   A HD12 1 
ATOM   3908 H  HD13 A LEU   A 1 169 ? 5.114  -20.787 -2.295  0.50 33.93 ?  169 LEU   A HD13 1 
ATOM   3909 H  HD13 B LEU   A 1 169 ? 3.490  -22.168 4.065   0.50 28.82 ?  169 LEU   A HD13 1 
ATOM   3910 H  HD21 A LEU   A 1 169 ? 7.103  -22.368 -4.122  0.50 33.84 ?  169 LEU   A HD21 1 
ATOM   3911 H  HD21 B LEU   A 1 169 ? 5.119  -24.021 2.221   0.50 29.33 ?  169 LEU   A HD21 1 
ATOM   3912 H  HD22 A LEU   A 1 169 ? 6.766  -20.838 -4.389  0.50 33.84 ?  169 LEU   A HD22 1 
ATOM   3913 H  HD22 B LEU   A 1 169 ? 3.888  -23.191 1.667   0.50 29.33 ?  169 LEU   A HD22 1 
ATOM   3914 H  HD23 A LEU   A 1 169 ? 8.264  -21.284 -4.103  0.50 33.84 ?  169 LEU   A HD23 1 
ATOM   3915 H  HD23 B LEU   A 1 169 ? 5.328  -23.003 1.023   0.50 29.33 ?  169 LEU   A HD23 1 
ATOM   3916 N  N    A SER   B 1 1   ? 50.867 -9.180  -23.674 0.50 28.51 ?  1   SER   B N    1 
ATOM   3917 N  N    B SER   B 1 1   ? 50.801 -9.301  -23.724 0.50 26.47 ?  1   SER   B N    1 
ATOM   3918 C  CA   A SER   B 1 1   ? 51.393 -10.261 -22.815 0.50 28.36 ?  1   SER   B CA   1 
ATOM   3919 C  CA   B SER   B 1 1   ? 51.313 -10.305 -22.769 0.50 26.28 ?  1   SER   B CA   1 
ATOM   3920 C  C    A SER   B 1 1   ? 50.326 -11.316 -22.560 0.50 27.31 ?  1   SER   B C    1 
ATOM   3921 C  C    B SER   B 1 1   ? 50.267 -11.379 -22.511 0.50 25.32 ?  1   SER   B C    1 
ATOM   3922 O  O    A SER   B 1 1   ? 49.138 -11.115 -22.840 0.50 26.99 ?  1   SER   B O    1 
ATOM   3923 O  O    B SER   B 1 1   ? 49.065 -11.179 -22.731 0.50 24.93 ?  1   SER   B O    1 
ATOM   3924 C  CB   A SER   B 1 1   ? 51.898 -9.698  -21.489 0.50 29.10 ?  1   SER   B CB   1 
ATOM   3925 C  CB   B SER   B 1 1   ? 51.709 -9.646  -21.451 0.50 26.89 ?  1   SER   B CB   1 
ATOM   3926 O  OG   A SER   B 1 1   ? 50.821 -9.361  -20.636 0.50 30.24 ?  1   SER   B OG   1 
ATOM   3927 O  OG   B SER   B 1 1   ? 50.579 -9.469  -20.616 0.50 27.95 ?  1   SER   B OG   1 
ATOM   3928 H  H1   A SER   B 1 1   ? 50.729 -9.502  -24.490 0.50 34.21 ?  1   SER   B H1   1 
ATOM   3929 H  H1   B SER   B 1 1   ? 50.702 -9.683  -24.520 0.50 31.75 ?  1   SER   B H1   1 
ATOM   3930 H  H2   A SER   B 1 1   ? 50.105 -8.884  -23.332 0.50 34.21 ?  1   SER   B H2   1 
ATOM   3931 H  H2   B SER   B 1 1   ? 50.021 -8.997  -23.435 0.50 31.75 ?  1   SER   B H2   1 
ATOM   3932 H  H3   A SER   B 1 1   ? 51.463 -8.523  -23.705 0.50 34.21 ?  1   SER   B H3   1 
ATOM   3933 H  H3   B SER   B 1 1   ? 51.385 -8.635  -23.780 0.50 31.75 ?  1   SER   B H3   1 
ATOM   3934 H  HA   A SER   B 1 1   ? 52.135 -10.677 -23.274 0.50 34.02 ?  1   SER   B HA   1 
ATOM   3935 H  HA   B SER   B 1 1   ? 52.096 -10.720 -23.155 0.50 31.53 ?  1   SER   B HA   1 
ATOM   3936 H  HB2  A SER   B 1 1   ? 52.448 -10.370 -21.060 0.50 34.91 ?  1   SER   B HB2  1 
ATOM   3937 H  HB2  B SER   B 1 1   ? 52.352 -10.216 -21.004 0.50 32.26 ?  1   SER   B HB2  1 
ATOM   3938 H  HB3  A SER   B 1 1   ? 52.421 -8.900  -21.664 0.50 34.91 ?  1   SER   B HB3  1 
ATOM   3939 H  HB3  B SER   B 1 1   ? 52.103 -8.780  -21.637 0.50 32.26 ?  1   SER   B HB3  1 
ATOM   3940 H  HG   A SER   B 1 1   ? 51.113 -8.977  -19.949 0.50 36.28 ?  1   SER   B HG   1 
ATOM   3941 H  HG   B SER   B 1 1   ? 50.808 -9.060  -19.917 0.50 33.53 ?  1   SER   B HG   1 
ATOM   3942 N  N    A MET   B 1 2   ? 50.768 -12.439 -22.009 0.50 26.64 ?  2   MET   B N    1 
ATOM   3943 N  N    B MET   B 1 2   ? 50.743 -12.521 -22.031 0.50 24.82 ?  2   MET   B N    1 
ATOM   3944 C  CA   A MET   B 1 2   ? 49.944 -13.627 -21.841 0.50 26.43 ?  2   MET   B CA   1 
ATOM   3945 C  CA   B MET   B 1 2   ? 49.925 -13.711 -21.846 0.50 24.78 ?  2   MET   B CA   1 
ATOM   3946 C  C    A MET   B 1 2   ? 49.702 -13.829 -20.351 0.50 23.87 ?  2   MET   B C    1 
ATOM   3947 C  C    B MET   B 1 2   ? 49.685 -13.902 -20.358 0.50 23.17 ?  2   MET   B C    1 
ATOM   3948 O  O    A MET   B 1 2   ? 50.643 -14.076 -19.591 0.50 23.87 ?  2   MET   B O    1 
ATOM   3949 O  O    B MET   B 1 2   ? 50.613 -14.221 -19.609 0.50 23.42 ?  2   MET   B O    1 
ATOM   3950 C  CB   A MET   B 1 2   ? 50.661 -14.825 -22.455 0.50 29.54 ?  2   MET   B CB   1 
ATOM   3951 C  CB   B MET   B 1 2   ? 50.652 -14.909 -22.430 0.50 27.16 ?  2   MET   B CB   1 
ATOM   3952 C  CG   A MET   B 1 2   ? 49.819 -16.082 -22.581 0.50 32.45 ?  2   MET   B CG   1 
ATOM   3953 C  CG   B MET   B 1 2   ? 49.763 -16.095 -22.785 0.50 29.07 ?  2   MET   B CG   1 
ATOM   3954 S  SD   A MET   B 1 2   ? 50.664 -17.338 -23.564 0.50 35.11 ?  2   MET   B SD   1 
ATOM   3955 S  SD   B MET   B 1 2   ? 50.608 -17.213 -23.907 0.50 30.67 ?  2   MET   B SD   1 
ATOM   3956 C  CE   A MET   B 1 2   ? 51.184 -16.338 -24.954 0.50 35.48 ?  2   MET   B CE   1 
ATOM   3957 C  CE   B MET   B 1 2   ? 51.546 -16.029 -24.852 0.50 31.28 ?  2   MET   B CE   1 
ATOM   3958 H  H    A MET   B 1 2   ? 51.571 -12.541 -21.714 0.50 31.95 ?  2   MET   B H    1 
ATOM   3959 H  H    B MET   B 1 2   ? 51.566 -12.641 -21.804 0.50 29.77 ?  2   MET   B H    1 
ATOM   3960 H  HA   A MET   B 1 2   ? 49.100 -13.513 -22.302 0.50 31.70 ?  2   MET   B HA   1 
ATOM   3961 H  HA   B MET   B 1 2   ? 49.083 -13.616 -22.317 0.50 29.72 ?  2   MET   B HA   1 
ATOM   3962 H  HB2  A MET   B 1 2   ? 50.952 -14.553 -23.338 0.50 35.44 ?  2   MET   B HB2  1 
ATOM   3963 H  HB2  B MET   B 1 2   ? 51.087 -14.549 -23.208 0.50 32.58 ?  2   MET   B HB2  1 
ATOM   3964 H  HB3  A MET   B 1 2   ? 51.432 -15.053 -21.917 0.50 35.44 ?  2   MET   B HB3  1 
ATOM   3965 H  HB3  B MET   B 1 2   ? 51.316 -15.242 -21.815 0.50 32.58 ?  2   MET   B HB3  1 
ATOM   3966 H  HG2  A MET   B 1 2   ? 49.651 -16.447 -21.695 0.50 38.93 ?  2   MET   B HG2  1 
ATOM   3967 H  HG2  B MET   B 1 2   ? 49.539 -16.591 -21.976 0.50 34.87 ?  2   MET   B HG2  1 
ATOM   3968 H  HG3  A MET   B 1 2   ? 48.981 -15.870 -23.021 0.50 38.93 ?  2   MET   B HG3  1 
ATOM   3969 H  HG3  B MET   B 1 2   ? 48.956 -15.790 -23.222 0.50 34.87 ?  2   MET   B HG3  1 
ATOM   3970 H  HE1  A MET   B 1 2   ? 51.340 -16.914 -25.708 0.50 42.56 ?  2   MET   B HE1  1 
ATOM   3971 H  HE1  B MET   B 1 2   ? 51.785 -16.473 -25.646 0.50 37.52 ?  2   MET   B HE1  1 
ATOM   3972 H  HE2  A MET   B 1 2   ? 50.481 -15.698 -25.160 0.50 42.56 ?  2   MET   B HE2  1 
ATOM   3973 H  HE2  B MET   B 1 2   ? 50.989 -15.255 -25.070 0.50 37.52 ?  2   MET   B HE2  1 
ATOM   3974 H  HE3  A MET   B 1 2   ? 52.001 -15.862 -24.720 0.50 42.56 ?  2   MET   B HE3  1 
ATOM   3975 H  HE3  B MET   B 1 2   ? 52.346 -15.747 -24.357 0.50 37.52 ?  2   MET   B HE3  1 
ATOM   3976 N  N    . VAL   B 1 3   ? 48.443 -13.704 -19.937 1.00 21.53 ?  3   VAL   B N    1 
ATOM   3977 C  CA   . VAL   B 1 3   ? 48.033 -13.945 -18.562 1.00 20.24 ?  3   VAL   B CA   1 
ATOM   3978 C  C    . VAL   B 1 3   ? 46.798 -14.830 -18.585 1.00 18.63 ?  3   VAL   B C    1 
ATOM   3979 O  O    . VAL   B 1 3   ? 46.075 -14.904 -19.580 1.00 19.11 ?  3   VAL   B O    1 
ATOM   3980 C  CB   . VAL   B 1 3   ? 47.746 -12.636 -17.794 1.00 21.96 ?  3   VAL   B CB   1 
ATOM   3981 C  CG1  . VAL   B 1 3   ? 49.009 -11.781 -17.689 1.00 22.50 ?  3   VAL   B CG1  1 
ATOM   3982 C  CG2  . VAL   B 1 3   ? 46.611 -11.870 -18.464 1.00 22.49 ?  3   VAL   B CG2  1 
ATOM   3983 H  H    A VAL   B 1 3   ? 47.795 -13.477 -20.455 0.50 25.83 ?  3   VAL   B H    1 
ATOM   3984 H  H    B VAL   B 1 3   ? 47.807 -13.428 -20.445 0.50 25.83 ?  3   VAL   B H    1 
ATOM   3985 H  HA   . VAL   B 1 3   ? 48.737 -14.424 -18.096 1.00 24.28 ?  3   VAL   B HA   1 
ATOM   3986 H  HB   . VAL   B 1 3   ? 47.464 -12.865 -16.894 1.00 26.34 ?  3   VAL   B HB   1 
ATOM   3987 H  HG11 . VAL   B 1 3   ? 48.799 -10.976 -17.194 1.00 26.99 ?  3   VAL   B HG11 1 
ATOM   3988 H  HG12 . VAL   B 1 3   ? 49.694 -12.289 -17.224 1.00 26.99 ?  3   VAL   B HG12 1 
ATOM   3989 H  HG13 . VAL   B 1 3   ? 49.311 -11.557 -18.581 1.00 26.99 ?  3   VAL   B HG13 1 
ATOM   3990 H  HG21 . VAL   B 1 3   ? 46.550 -10.994 -18.061 1.00 26.98 ?  3   VAL   B HG21 1 
ATOM   3991 H  HG22 . VAL   B 1 3   ? 46.800 -11.793 -19.410 1.00 26.98 ?  3   VAL   B HG22 1 
ATOM   3992 H  HG23 . VAL   B 1 3   ? 45.781 -12.357 -18.330 1.00 26.98 ?  3   VAL   B HG23 1 
ATOM   3993 N  N    . ASN   B 1 4   ? 46.566 -15.515 -17.467 1.00 16.66 ?  4   ASN   B N    1 
ATOM   3994 C  CA   . ASN   B 1 4   ? 45.427 -16.422 -17.339 1.00 15.55 ?  4   ASN   B CA   1 
ATOM   3995 C  C    . ASN   B 1 4   ? 45.358 -17.390 -18.519 1.00 15.70 ?  4   ASN   B C    1 
ATOM   3996 O  O    . ASN   B 1 4   ? 44.292 -17.637 -19.080 1.00 16.53 ?  4   ASN   B O    1 
ATOM   3997 C  CB   . ASN   B 1 4   ? 44.113 -15.651 -17.185 1.00 14.99 ?  4   ASN   B CB   1 
ATOM   3998 C  CG   . ASN   B 1 4   ? 44.055 -14.850 -15.895 1.00 14.50 ?  4   ASN   B CG   1 
ATOM   3999 O  OD1  . ASN   B 1 4   ? 44.343 -15.365 -14.817 1.00 14.21 ?  4   ASN   B OD1  1 
ATOM   4000 N  ND2  . ASN   B 1 4   ? 43.686 -13.579 -16.004 1.00 15.20 ?  4   ASN   B ND2  1 
ATOM   4001 H  H    . ASN   B 1 4   ? 47.064 -15.484 -16.769 1.00 19.98 ?  4   ASN   B H    1 
ATOM   4002 H  HA   . ASN   B 1 4   ? 45.548 -16.950 -16.531 1.00 18.65 ?  4   ASN   B HA   1 
ATOM   4003 H  HB2  . ASN   B 1 4   ? 44.021 -15.035 -17.929 1.00 17.97 ?  4   ASN   B HB2  1 
ATOM   4004 H  HB3  . ASN   B 1 4   ? 43.374 -16.282 -17.186 1.00 17.97 ?  4   ASN   B HB3  1 
ATOM   4005 H  HD21 . ASN   B 1 4   ? 43.633 -13.083 -15.302 1.00 18.23 ?  4   ASN   B HD21 1 
ATOM   4006 H  HD22 . ASN   B 1 4   ? 43.492 -13.249 -16.776 1.00 18.23 ?  4   ASN   B HD22 1 
ATOM   4007 N  N    . SER   B 1 5   ? 46.510 -17.944 -18.902 1.00 16.76 ?  5   SER   B N    1 
ATOM   4008 C  CA   . SER   B 1 5   ? 46.592 -18.864 -20.036 1.00 18.94 ?  5   SER   B CA   1 
ATOM   4009 C  C    . SER   B 1 5   ? 46.571 -20.292 -19.503 1.00 20.53 ?  5   SER   B C    1 
ATOM   4010 O  O    . SER   B 1 5   ? 47.580 -20.987 -19.439 1.00 22.71 ?  5   SER   B O    1 
ATOM   4011 C  CB   . SER   B 1 5   ? 47.848 -18.585 -20.862 1.00 20.68 ?  5   SER   B CB   1 
ATOM   4012 O  OG   . SER   B 1 5   ? 49.028 -18.794 -20.101 1.00 23.45 ?  5   SER   B OG   1 
ATOM   4013 H  H    . SER   B 1 5   ? 47.262 -17.814 -18.509 1.00 20.10 ?  5   SER   B H    1 
ATOM   4014 H  HA   . SER   B 1 5   ? 45.816 -18.745 -20.606 1.00 22.72 ?  5   SER   B HA   1 
ATOM   4015 H  HB2  . SER   B 1 5   ? 47.851 -19.182 -21.631 1.00 24.81 ?  5   SER   B HB2  1 
ATOM   4016 H  HB3  . SER   B 1 5   ? 47.814 -17.665 -21.162 1.00 24.81 ?  5   SER   B HB3  1 
ATOM   4017 H  HG   . SER   B 1 5   ? 49.064 -19.599 -19.862 1.00 28.12 ?  5   SER   B HG   1 
ATOM   4018 N  N    . PHE   B 1 6   ? 45.381 -20.702 -19.077 1.00 21.30 ?  6   PHE   B N    1 
ATOM   4019 C  CA   . PHE   B 1 6   ? 45.180 -22.046 -18.560 1.00 20.91 ?  6   PHE   B CA   1 
ATOM   4020 C  C    . PHE   B 1 6   ? 45.076 -23.012 -19.729 1.00 24.60 ?  6   PHE   B C    1 
ATOM   4021 O  O    . PHE   B 1 6   ? 44.394 -22.726 -20.718 1.00 26.55 ?  6   PHE   B O    1 
ATOM   4022 C  CB   . PHE   B 1 6   ? 43.903 -22.098 -17.725 1.00 19.14 ?  6   PHE   B CB   1 
ATOM   4023 C  CG   . PHE   B 1 6   ? 43.943 -21.228 -16.500 1.00 17.63 ?  6   PHE   B CG   1 
ATOM   4024 C  CD1  . PHE   B 1 6   ? 44.443 -21.718 -15.310 1.00 16.49 ?  6   PHE   B CD1  1 
ATOM   4025 C  CD2  . PHE   B 1 6   ? 43.468 -19.925 -16.540 1.00 16.98 ?  6   PHE   B CD2  1 
ATOM   4026 C  CE1  . PHE   B 1 6   ? 44.472 -20.922 -14.177 1.00 15.65 ?  6   PHE   B CE1  1 
ATOM   4027 C  CE2  . PHE   B 1 6   ? 43.499 -19.124 -15.419 1.00 16.99 ?  6   PHE   B CE2  1 
ATOM   4028 C  CZ   . PHE   B 1 6   ? 44.003 -19.617 -14.236 1.00 15.89 ?  6   PHE   B CZ   1 
ATOM   4029 H  H    . PHE   B 1 6   ? 44.663 -20.227 -19.086 1.00 25.55 ?  6   PHE   B H    1 
ATOM   4030 H  HA   . PHE   B 1 6   ? 45.927 -22.310 -18.004 1.00 25.08 ?  6   PHE   B HA   1 
ATOM   4031 H  HB2  . PHE   B 1 6   ? 43.156 -21.807 -18.271 1.00 22.96 ?  6   PHE   B HB2  1 
ATOM   4032 H  HB3  . PHE   B 1 6   ? 43.752 -23.015 -17.432 1.00 22.96 ?  6   PHE   B HB3  1 
ATOM   4033 H  HD1  . PHE   B 1 6   ? 44.767 -22.593 -15.266 1.00 19.78 ?  6   PHE   B HD1  1 
ATOM   4034 H  HD2  . PHE   B 1 6   ? 43.125 -19.594 -17.337 1.00 20.37 ?  6   PHE   B HD2  1 
ATOM   4035 H  HE1  . PHE   B 1 6   ? 44.823 -21.254 -13.378 1.00 18.77 ?  6   PHE   B HE1  1 
ATOM   4036 H  HE2  . PHE   B 1 6   ? 43.177 -18.255 -15.462 1.00 20.37 ?  6   PHE   B HE2  1 
ATOM   4037 H  HZ   . PHE   B 1 6   ? 44.026 -19.081 -13.477 1.00 19.06 ?  6   PHE   B HZ   1 
ATOM   4038 N  N    . SER   B 1 7   ? 45.771 -24.143 -19.623 1.00 26.30 ?  7   SER   B N    1 
ATOM   4039 C  CA   . SER   B 1 7   ? 45.840 -25.115 -20.703 1.00 29.30 ?  7   SER   B CA   1 
ATOM   4040 C  C    . SER   B 1 7   ? 45.791 -26.525 -20.134 1.00 28.09 ?  7   SER   B C    1 
ATOM   4041 O  O    . SER   B 1 7   ? 46.417 -26.817 -19.111 1.00 28.85 ?  7   SER   B O    1 
ATOM   4042 C  CB   . SER   B 1 7   ? 47.126 -24.928 -21.523 1.00 32.43 ?  7   SER   B CB   1 
ATOM   4043 O  OG   . SER   B 1 7   ? 47.157 -25.801 -22.639 1.00 34.35 ?  7   SER   B OG   1 
ATOM   4044 H  H    . SER   B 1 7   ? 46.227 -24.369 -18.926 1.00 31.54 ?  7   SER   B H    1 
ATOM   4045 H  HA   . SER   B 1 7   ? 45.084 -25.000 -21.295 1.00 35.14 ?  7   SER   B HA   1 
ATOM   4046 H  HB2  . SER   B 1 7   ? 47.170 -24.008 -21.838 1.00 38.91 ?  7   SER   B HB2  1 
ATOM   4047 H  HB3  . SER   B 1 7   ? 47.894 -25.116 -20.960 1.00 38.91 ?  7   SER   B HB3  1 
ATOM   4048 H  HG   . SER   B 1 7   ? 47.864 -25.678 -23.081 1.00 41.21 ?  7   SER   B HG   1 
ATOM   4049 N  N    A GLY   B 1 8   ? 45.039 -27.395 -20.802 0.50 27.53 ?  8   GLY   B N    1 
ATOM   4050 N  N    B GLY   B 1 8   ? 45.042 -27.397 -20.803 0.50 27.49 ?  8   GLY   B N    1 
ATOM   4051 C  CA   A GLY   B 1 8   ? 44.990 -28.788 -20.416 0.50 26.73 ?  8   GLY   B CA   1 
ATOM   4052 C  CA   B GLY   B 1 8   ? 44.990 -28.791 -20.419 0.50 26.66 ?  8   GLY   B CA   1 
ATOM   4053 C  C    A GLY   B 1 8   ? 44.059 -29.102 -19.273 0.50 25.67 ?  8   GLY   B C    1 
ATOM   4054 C  C    B GLY   B 1 8   ? 44.043 -29.115 -19.290 0.50 25.58 ?  8   GLY   B C    1 
ATOM   4055 O  O    A GLY   B 1 8   ? 44.223 -30.144 -18.628 0.50 26.64 ?  8   GLY   B O    1 
ATOM   4056 O  O    B GLY   B 1 8   ? 44.178 -30.179 -18.675 0.50 26.43 ?  8   GLY   B O    1 
ATOM   4057 H  H    A GLY   B 1 8   ? 44.552 -27.195 -21.480 0.50 33.02 ?  8   GLY   B H    1 
ATOM   4058 H  H    B GLY   B 1 8   ? 44.561 -27.199 -21.485 0.50 32.98 ?  8   GLY   B H    1 
ATOM   4059 H  HA2  A GLY   B 1 8   ? 44.710 -29.314 -21.179 0.50 32.07 ?  8   GLY   B HA2  1 
ATOM   4060 H  HA2  B GLY   B 1 8   ? 44.724 -29.317 -21.188 0.50 31.98 ?  8   GLY   B HA2  1 
ATOM   4061 H  HA3  A GLY   B 1 8   ? 45.878 -29.076 -20.159 0.50 32.07 ?  8   GLY   B HA3  1 
ATOM   4062 H  HA3  B GLY   B 1 8   ? 45.875 -29.078 -20.149 0.50 31.98 ?  8   GLY   B HA3  1 
ATOM   4063 N  N    . TYR   B 1 9   ? 43.073 -28.249 -19.008 1.00 24.13 ?  9   TYR   B N    1 
ATOM   4064 C  CA   . TYR   B 1 9   ? 42.123 -28.503 -17.938 1.00 21.61 ?  9   TYR   B CA   1 
ATOM   4065 C  C    . TYR   B 1 9   ? 40.931 -29.294 -18.445 1.00 20.63 ?  9   TYR   B C    1 
ATOM   4066 O  O    . TYR   B 1 9   ? 40.501 -29.153 -19.594 1.00 22.15 ?  9   TYR   B O    1 
ATOM   4067 C  CB   . TYR   B 1 9   ? 41.630 -27.212 -17.290 1.00 20.80 ?  9   TYR   B CB   1 
ATOM   4068 C  CG   . TYR   B 1 9   ? 42.661 -26.599 -16.378 1.00 19.95 ?  9   TYR   B CG   1 
ATOM   4069 C  CD1  . TYR   B 1 9   ? 43.747 -25.923 -16.902 1.00 19.98 ?  9   TYR   B CD1  1 
ATOM   4070 C  CD2  . TYR   B 1 9   ? 42.566 -26.716 -15.000 1.00 19.30 ?  9   TYR   B CD2  1 
ATOM   4071 C  CE1  . TYR   B 1 9   ? 44.709 -25.367 -16.080 1.00 20.17 ?  9   TYR   B CE1  1 
ATOM   4072 C  CE2  . TYR   B 1 9   ? 43.525 -26.166 -14.166 1.00 19.52 ?  9   TYR   B CE2  1 
ATOM   4073 C  CZ   . TYR   B 1 9   ? 44.596 -25.486 -14.714 1.00 19.80 ?  9   TYR   B CZ   1 
ATOM   4074 O  OH   . TYR   B 1 9   ? 45.555 -24.944 -13.894 1.00 20.29 ?  9   TYR   B OH   1 
ATOM   4075 H  H    A TYR   B 1 9   ? 42.920 -27.525 -19.446 0.50 28.94 ?  9   TYR   B H    1 
ATOM   4076 H  H    B TYR   B 1 9   ? 42.931 -27.515 -19.433 0.50 28.94 ?  9   TYR   B H    1 
ATOM   4077 H  HA   . TYR   B 1 9   ? 42.545 -29.034 -17.254 1.00 25.92 ?  9   TYR   B HA   1 
ATOM   4078 H  HB2  . TYR   B 1 9   ? 41.404 -26.564 -17.978 1.00 24.95 ?  9   TYR   B HB2  1 
ATOM   4079 H  HB3  . TYR   B 1 9   ? 40.847 -27.419 -16.759 1.00 24.95 ?  9   TYR   B HB3  1 
ATOM   4080 H  HD1  . TYR   B 1 9   ? 43.827 -25.837 -17.826 1.00 23.96 ?  9   TYR   B HD1  1 
ATOM   4081 H  HD2  . TYR   B 1 9   ? 41.835 -27.178 -14.632 1.00 23.14 ?  9   TYR   B HD2  1 
ATOM   4082 H  HE1  . TYR   B 1 9   ? 45.425 -24.913 -16.449 1.00 24.19 ?  9   TYR   B HE1  1 
ATOM   4083 H  HE2  . TYR   B 1 9   ? 43.432 -26.256 -13.245 1.00 23.41 ?  9   TYR   B HE2  1 
ATOM   4084 H  HH   . TYR   B 1 9   ? 46.128 -24.563 -14.362 1.00 24.33 ?  9   TYR   B HH   1 
ATOM   4085 N  N    . LEU   B 1 10  ? 40.414 -30.146 -17.565 1.00 19.10 ?  10  LEU   B N    1 
ATOM   4086 C  CA   . LEU   B 1 10  ? 39.209 -30.914 -17.819 1.00 18.87 ?  10  LEU   B CA   1 
ATOM   4087 C  C    . LEU   B 1 10  ? 38.022 -30.144 -17.260 1.00 18.81 ?  10  LEU   B C    1 
ATOM   4088 O  O    . LEU   B 1 10  ? 38.038 -29.724 -16.099 1.00 18.22 ?  10  LEU   B O    1 
ATOM   4089 C  CB   . LEU   B 1 10  ? 39.312 -32.275 -17.131 1.00 19.64 ?  10  LEU   B CB   1 
ATOM   4090 C  CG   . LEU   B 1 10  ? 38.198 -33.260 -17.472 1.00 20.84 ?  10  LEU   B CG   1 
ATOM   4091 C  CD1  . LEU   B 1 10  ? 38.414 -33.829 -18.867 1.00 21.88 ?  10  LEU   B CD1  1 
ATOM   4092 C  CD2  . LEU   B 1 10  ? 38.097 -34.365 -16.436 1.00 21.59 ?  10  LEU   B CD2  1 
ATOM   4093 H  H    . LEU   B 1 10  ? 40.742 -30.290 -16.782 1.00 22.90 ?  10  LEU   B H    1 
ATOM   4094 H  HA   . LEU   B 1 10  ? 39.077 -31.043 -18.769 1.00 22.63 ?  10  LEU   B HA   1 
ATOM   4095 H  HB2  . LEU   B 1 10  ? 40.153 -32.681 -17.386 1.00 23.55 ?  10  LEU   B HB2  1 
ATOM   4096 H  HB3  . LEU   B 1 10  ? 39.296 -32.138 -16.168 1.00 23.55 ?  10  LEU   B HB3  1 
ATOM   4097 H  HG   . LEU   B 1 10  ? 37.352 -32.784 -17.477 1.00 25.00 ?  10  LEU   B HG   1 
ATOM   4098 H  HD11 . LEU   B 1 10  ? 37.715 -34.472 -19.055 1.00 26.25 ?  10  LEU   B HD11 1 
ATOM   4099 H  HD12 . LEU   B 1 10  ? 38.379 -33.104 -19.511 1.00 26.25 ?  10  LEU   B HD12 1 
ATOM   4100 H  HD13 . LEU   B 1 10  ? 39.281 -34.260 -18.899 1.00 26.25 ?  10  LEU   B HD13 1 
ATOM   4101 H  HD21 . LEU   B 1 10  ? 37.384 -34.967 -16.692 1.00 25.89 ?  10  LEU   B HD21 1 
ATOM   4102 H  HD22 . LEU   B 1 10  ? 38.940 -34.835 -16.399 1.00 25.89 ?  10  LEU   B HD22 1 
ATOM   4103 H  HD23 . LEU   B 1 10  ? 37.900 -33.963 -15.574 1.00 25.89 ?  10  LEU   B HD23 1 
ATOM   4104 N  N    A LYS   B 1 11  ? 37.002 -29.961 -18.091 0.50 19.95 ?  11  LYS   B N    1 
ATOM   4105 N  N    B LYS   B 1 11  ? 36.998 -29.965 -18.088 0.50 19.99 ?  11  LYS   B N    1 
ATOM   4106 C  CA   A LYS   B 1 11  ? 35.796 -29.253 -17.691 0.50 21.91 ?  11  LYS   B CA   1 
ATOM   4107 C  CA   B LYS   B 1 11  ? 35.798 -29.245 -17.688 0.50 21.99 ?  11  LYS   B CA   1 
ATOM   4108 C  C    A LYS   B 1 11  ? 34.951 -30.176 -16.820 0.50 20.69 ?  11  LYS   B C    1 
ATOM   4109 C  C    B LYS   B 1 11  ? 34.931 -30.161 -16.831 0.50 20.82 ?  11  LYS   B C    1 
ATOM   4110 O  O    A LYS   B 1 11  ? 34.629 -31.296 -17.227 0.50 21.39 ?  11  LYS   B O    1 
ATOM   4111 O  O    B LYS   B 1 11  ? 34.565 -31.259 -17.263 0.50 21.63 ?  11  LYS   B O    1 
ATOM   4112 C  CB   A LYS   B 1 11  ? 35.029 -28.838 -18.947 0.50 25.68 ?  11  LYS   B CB   1 
ATOM   4113 C  CB   B LYS   B 1 11  ? 35.043 -28.805 -18.942 0.50 25.74 ?  11  LYS   B CB   1 
ATOM   4114 C  CG   A LYS   B 1 11  ? 33.965 -27.777 -18.740 0.50 28.96 ?  11  LYS   B CG   1 
ATOM   4115 C  CG   B LYS   B 1 11  ? 33.917 -27.816 -18.706 0.50 29.01 ?  11  LYS   B CG   1 
ATOM   4116 C  CD   A LYS   B 1 11  ? 33.281 -27.445 -20.062 0.50 31.57 ?  11  LYS   B CD   1 
ATOM   4117 C  CD   B LYS   B 1 11  ? 33.203 -27.494 -20.014 0.50 31.61 ?  11  LYS   B CD   1 
ATOM   4118 C  CE   A LYS   B 1 11  ? 32.247 -26.346 -19.901 0.50 33.44 ?  11  LYS   B CE   1 
ATOM   4119 C  CE   B LYS   B 1 11  ? 32.151 -26.412 -19.831 0.50 33.47 ?  11  LYS   B CE   1 
ATOM   4120 N  NZ   A LYS   B 1 11  ? 32.873 -25.042 -19.560 0.50 34.46 ?  11  LYS   B NZ   1 
ATOM   4121 N  NZ   B LYS   B 1 11  ? 32.760 -25.079 -19.569 0.50 34.49 ?  11  LYS   B NZ   1 
ATOM   4122 H  H    A LYS   B 1 11  ? 36.973 -30.250 -18.903 0.50 23.93 ?  11  LYS   B H    1 
ATOM   4123 H  H    B LYS   B 1 11  ? 36.965 -30.261 -18.897 0.50 23.98 ?  11  LYS   B H    1 
ATOM   4124 H  HA   A LYS   B 1 11  ? 36.020 -28.461 -17.185 0.50 26.28 ?  11  LYS   B HA   1 
ATOM   4125 H  HA   B LYS   B 1 11  ? 36.030 -28.462 -17.172 0.50 26.37 ?  11  LYS   B HA   1 
ATOM   4126 H  HB2  A LYS   B 1 11  ? 35.663 -28.484 -19.593 0.50 30.80 ?  11  LYS   B HB2  1 
ATOM   4127 H  HB2  B LYS   B 1 11  ? 35.673 -28.382 -19.549 0.50 30.88 ?  11  LYS   B HB2  1 
ATOM   4128 H  HB3  A LYS   B 1 11  ? 34.589 -29.617 -19.321 0.50 30.80 ?  11  LYS   B HB3  1 
ATOM   4129 H  HB3  B LYS   B 1 11  ? 34.656 -29.585 -19.369 0.50 30.88 ?  11  LYS   B HB3  1 
ATOM   4130 H  HG2  A LYS   B 1 11  ? 33.294 -28.107 -18.124 0.50 34.74 ?  11  LYS   B HG2  1 
ATOM   4131 H  HG2  B LYS   B 1 11  ? 33.273 -28.202 -18.093 0.50 34.80 ?  11  LYS   B HG2  1 
ATOM   4132 H  HG3  A LYS   B 1 11  ? 34.375 -26.968 -18.397 0.50 34.74 ?  11  LYS   B HG3  1 
ATOM   4133 H  HG3  B LYS   B 1 11  ? 34.280 -26.993 -18.346 0.50 34.80 ?  11  LYS   B HG3  1 
ATOM   4134 H  HD2  A LYS   B 1 11  ? 33.948 -27.144 -20.700 0.50 37.87 ?  11  LYS   B HD2  1 
ATOM   4135 H  HD2  B LYS   B 1 11  ? 33.852 -27.179 -20.664 0.50 37.92 ?  11  LYS   B HD2  1 
ATOM   4136 H  HD3  A LYS   B 1 11  ? 32.834 -28.238 -20.398 0.50 37.87 ?  11  LYS   B HD3  1 
ATOM   4137 H  HD3  B LYS   B 1 11  ? 32.762 -28.293 -20.343 0.50 37.92 ?  11  LYS   B HD3  1 
ATOM   4138 H  HE2  A LYS   B 1 11  ? 31.761 -26.241 -20.735 0.50 40.11 ?  11  LYS   B HE2  1 
ATOM   4139 H  HE2  B LYS   B 1 11  ? 31.617 -26.347 -20.638 0.50 40.16 ?  11  LYS   B HE2  1 
ATOM   4140 H  HE3  A LYS   B 1 11  ? 31.636 -26.587 -19.187 0.50 40.11 ?  11  LYS   B HE3  1 
ATOM   4141 H  HE3  B LYS   B 1 11  ? 31.588 -26.642 -19.076 0.50 40.16 ?  11  LYS   B HE3  1 
ATOM   4142 H  HZ1  A LYS   B 1 11  ? 32.247 -24.414 -19.486 0.50 41.34 ?  11  LYS   B HZ1  1 
ATOM   4143 H  HZ1  B LYS   B 1 11  ? 32.123 -24.461 -19.504 0.50 41.37 ?  11  LYS   B HZ1  1 
ATOM   4144 H  HZ2  A LYS   B 1 11  ? 33.311 -25.108 -18.789 0.50 41.34 ?  11  LYS   B HZ2  1 
ATOM   4145 H  HZ2  B LYS   B 1 11  ? 33.222 -25.100 -18.808 0.50 41.37 ?  11  LYS   B HZ2  1 
ATOM   4146 H  HZ3  A LYS   B 1 11  ? 33.446 -24.804 -20.199 0.50 41.34 ?  11  LYS   B HZ3  1 
ATOM   4147 H  HZ3  B LYS   B 1 11  ? 33.308 -24.859 -20.235 0.50 41.37 ?  11  LYS   B HZ3  1 
ATOM   4148 N  N    . LEU   B 1 12  ? 34.609 -29.719 -15.615 1.00 19.29 ?  12  LEU   B N    1 
ATOM   4149 C  CA   . LEU   B 1 12  ? 33.672 -30.430 -14.749 1.00 17.99 ?  12  LEU   B CA   1 
ATOM   4150 C  C    . LEU   B 1 12  ? 32.281 -29.822 -14.821 1.00 17.48 ?  12  LEU   B C    1 
ATOM   4151 O  O    . LEU   B 1 12  ? 31.297 -30.537 -14.991 1.00 18.09 ?  12  LEU   B O    1 
ATOM   4152 C  CB   . LEU   B 1 12  ? 34.154 -30.439 -13.292 1.00 17.29 ?  12  LEU   B CB   1 
ATOM   4153 C  CG   . LEU   B 1 12  ? 35.480 -31.139 -13.009 1.00 16.90 ?  12  LEU   B CG   1 
ATOM   4154 C  CD1  . LEU   B 1 12  ? 35.817 -31.076 -11.527 1.00 17.08 ?  12  LEU   B CD1  1 
ATOM   4155 C  CD2  . LEU   B 1 12  ? 35.450 -32.577 -13.489 1.00 17.33 ?  12  LEU   B CD2  1 
ATOM   4156 H  H    A LEU   B 1 12  ? 34.906 -28.990 -15.275 0.50 23.13 ?  12  LEU   B H    1 
ATOM   4157 H  H    B LEU   B 1 12  ? 34.917 -28.998 -15.269 0.50 23.13 ?  12  LEU   B H    1 
ATOM   4158 H  HA   . LEU   B 1 12  ? 33.596 -31.347 -15.045 1.00 21.58 ?  12  LEU   B HA   1 
ATOM   4159 H  HB2  . LEU   B 1 12  ? 34.242 -29.521 -12.999 1.00 20.74 ?  12  LEU   B HB2  1 
ATOM   4160 H  HB3  . LEU   B 1 12  ? 33.475 -30.882 -12.756 1.00 20.74 ?  12  LEU   B HB3  1 
ATOM   4161 H  HG   . LEU   B 1 12  ? 36.182 -30.677 -13.493 1.00 20.27 ?  12  LEU   B HG   1 
ATOM   4162 H  HD11 . LEU   B 1 12  ? 36.665 -31.525 -11.377 1.00 20.49 ?  12  LEU   B HD11 1 
ATOM   4163 H  HD12 . LEU   B 1 12  ? 35.881 -30.148 -11.254 1.00 20.49 ?  12  LEU   B HD12 1 
ATOM   4164 H  HD13 . LEU   B 1 12  ? 35.116 -31.521 -11.023 1.00 20.49 ?  12  LEU   B HD13 1 
ATOM   4165 H  HD21 . LEU   B 1 12  ? 36.246 -33.032 -13.178 1.00 20.79 ?  12  LEU   B HD21 1 
ATOM   4166 H  HD22 . LEU   B 1 12  ? 34.658 -33.013 -13.133 1.00 20.79 ?  12  LEU   B HD22 1 
ATOM   4167 H  HD23 . LEU   B 1 12  ? 35.420 -32.587 -14.460 1.00 20.79 ?  12  LEU   B HD23 1 
ATOM   4168 N  N    . THR   B 1 13  ? 32.196 -28.505 -14.694 1.00 17.52 ?  13  THR   B N    1 
ATOM   4169 C  CA   . THR   B 1 13  ? 30.979 -27.747 -14.905 1.00 17.46 ?  13  THR   B CA   1 
ATOM   4170 C  C    . THR   B 1 13  ? 31.329 -26.560 -15.794 1.00 19.25 ?  13  THR   B C    1 
ATOM   4171 O  O    . THR   B 1 13  ? 32.483 -26.375 -16.201 1.00 20.52 ?  13  THR   B O    1 
ATOM   4172 C  CB   . THR   B 1 13  ? 30.386 -27.260 -13.579 1.00 17.26 ?  13  THR   B CB   1 
ATOM   4173 O  OG1  . THR   B 1 13  ? 31.248 -26.254 -13.033 1.00 16.83 ?  13  THR   B OG1  1 
ATOM   4174 C  CG2  . THR   B 1 13  ? 30.250 -28.403 -12.586 1.00 18.08 ?  13  THR   B CG2  1 
ATOM   4175 H  H    . THR   B 1 13  ? 32.860 -28.011 -14.473 1.00 21.01 ?  13  THR   B H    1 
ATOM   4176 H  HA   . THR   B 1 13  ? 30.314 -28.304 -15.350 1.00 20.94 ?  13  THR   B HA   1 
ATOM   4177 H  HB   . THR   B 1 13  ? 29.502 -26.880 -13.734 1.00 20.70 ?  13  THR   B HB   1 
ATOM   4178 H  HG1  . THR   B 1 13  ? 31.040 -25.498 -13.344 1.00 20.19 ?  13  THR   B HG1  1 
ATOM   4179 H  HG21 . THR   B 1 13  ? 29.744 -28.110 -11.811 1.00 21.68 ?  13  THR   B HG21 1 
ATOM   4180 H  HG22 . THR   B 1 13  ? 29.784 -29.145 -13.002 1.00 21.68 ?  13  THR   B HG22 1 
ATOM   4181 H  HG23 . THR   B 1 13  ? 31.126 -28.698 -12.301 1.00 21.68 ?  13  THR   B HG23 1 
ATOM   4182 N  N    . ASP   B 1 14  ? 30.329 -25.730 -16.081 1.00 20.53 ?  14  ASP   B N    1 
ATOM   4183 C  CA   . ASP   B 1 14  ? 30.573 -24.584 -16.947 1.00 22.23 ?  14  ASP   B CA   1 
ATOM   4184 C  C    . ASP   B 1 14  ? 31.668 -23.676 -16.399 1.00 20.31 ?  14  ASP   B C    1 
ATOM   4185 O  O    . ASP   B 1 14  ? 32.326 -22.973 -17.177 1.00 21.98 ?  14  ASP   B O    1 
ATOM   4186 C  CB   . ASP   B 1 14  ? 29.286 -23.791 -17.161 1.00 26.11 ?  14  ASP   B CB   1 
ATOM   4187 C  CG   . ASP   B 1 14  ? 28.308 -24.496 -18.079 1.00 30.03 ?  14  ASP   B CG   1 
ATOM   4188 O  OD1  . ASP   B 1 14  ? 28.737 -25.345 -18.894 1.00 31.41 ?  14  ASP   B OD1  1 
ATOM   4189 O  OD2  . ASP   B 1 14  ? 27.098 -24.209 -17.977 1.00 31.82 -1 14  ASP   B OD2  1 
ATOM   4190 H  H    . ASP   B 1 14  ? 29.523 -25.797 -15.789 1.00 24.62 ?  14  ASP   B H    1 
ATOM   4191 H  HA   . ASP   B 1 14  ? 30.873 -24.902 -17.808 1.00 26.66 ?  14  ASP   B HA   1 
ATOM   4192 H  HB2  . ASP   B 1 14  ? 28.834 -23.682 -16.314 1.00 31.32 ?  14  ASP   B HB2  1 
ATOM   4193 H  HB3  . ASP   B 1 14  ? 29.509 -22.922 -17.535 1.00 31.32 ?  14  ASP   B HB3  1 
ATOM   4194 N  N    . ASN   B 1 15  ? 31.881 -23.666 -15.077 1.00 17.32 ?  15  ASN   B N    1 
ATOM   4195 C  CA   . ASN   B 1 15  ? 32.844 -22.748 -14.472 1.00 15.62 ?  15  ASN   B CA   1 
ATOM   4196 C  C    . ASN   B 1 15  ? 33.932 -23.410 -13.635 1.00 14.42 ?  15  ASN   B C    1 
ATOM   4197 O  O    . ASN   B 1 15  ? 34.804 -22.693 -13.126 1.00 14.46 ?  15  ASN   B O    1 
ATOM   4198 C  CB   . ASN   B 1 15  ? 32.138 -21.692 -13.607 1.00 15.37 ?  15  ASN   B CB   1 
ATOM   4199 C  CG   . ASN   B 1 15  ? 31.508 -22.293 -12.365 1.00 15.47 ?  15  ASN   B CG   1 
ATOM   4200 O  OD1  . ASN   B 1 15  ? 30.559 -23.079 -12.455 1.00 17.32 ?  15  ASN   B OD1  1 
ATOM   4201 N  ND2  . ASN   B 1 15  ? 32.043 -21.957 -11.204 1.00 14.43 ?  15  ASN   B ND2  1 
ATOM   4202 H  H    . ASN   B 1 15  ? 31.455 -24.156 -14.508 1.00 20.78 ?  15  ASN   B H    1 
ATOM   4203 H  HA   . ASN   B 1 15  ? 33.286 -22.265 -15.181 1.00 18.73 ?  15  ASN   B HA   1 
ATOM   4204 H  HB2  . ASN   B 1 15  ? 32.786 -21.022 -13.324 1.00 18.43 ?  15  ASN   B HB2  1 
ATOM   4205 H  HB3  . ASN   B 1 15  ? 31.434 -21.263 -14.125 1.00 18.43 ?  15  ASN   B HB3  1 
ATOM   4206 H  HD21 . ASN   B 1 15  ? 31.716 -22.265 -10.470 1.00 17.30 ?  15  ASN   B HD21 1 
ATOM   4207 H  HD22 . ASN   B 1 15  ? 32.710 -21.406 -11.173 1.00 17.30 ?  15  ASN   B HD22 1 
ATOM   4208 N  N    . VAL   B 1 16  ? 33.912 -24.729 -13.458 1.00 14.48 ?  16  VAL   B N    1 
ATOM   4209 C  CA   . VAL   B 1 16  ? 34.912 -25.423 -12.651 1.00 13.89 ?  16  VAL   B CA   1 
ATOM   4210 C  C    . VAL   B 1 16  ? 35.700 -26.362 -13.547 1.00 13.93 ?  16  VAL   B C    1 
ATOM   4211 O  O    . VAL   B 1 16  ? 35.120 -27.240 -14.204 1.00 15.04 ?  16  VAL   B O    1 
ATOM   4212 C  CB   . VAL   B 1 16  ? 34.291 -26.180 -11.468 1.00 14.14 ?  16  VAL   B CB   1 
ATOM   4213 C  CG1  . VAL   B 1 16  ? 35.382 -26.902 -10.679 1.00 14.26 ?  16  VAL   B CG1  1 
ATOM   4214 C  CG2  . VAL   B 1 16  ? 33.506 -25.223 -10.574 1.00 14.67 ?  16  VAL   B CG2  1 
ATOM   4215 H  H    . VAL   B 1 16  ? 33.303 -25.250 -13.787 1.00 17.37 ?  16  VAL   B H    1 
ATOM   4216 H  HA   . VAL   B 1 16  ? 35.524 -24.764 -12.285 1.00 16.66 ?  16  VAL   B HA   1 
ATOM   4217 H  HB   . VAL   B 1 16  ? 33.670 -26.847 -11.803 1.00 16.95 ?  16  VAL   B HB   1 
ATOM   4218 H  HG11 . VAL   B 1 16  ? 35.015 -27.189 -9.826  1.00 17.10 ?  16  VAL   B HG11 1 
ATOM   4219 H  HG12 . VAL   B 1 16  ? 35.685 -27.666 -11.183 1.00 17.10 ?  16  VAL   B HG12 1 
ATOM   4220 H  HG13 . VAL   B 1 16  ? 36.116 -26.284 -10.526 1.00 17.10 ?  16  VAL   B HG13 1 
ATOM   4221 H  HG21 . VAL   B 1 16  ? 33.176 -25.709 -9.799  1.00 17.59 ?  16  VAL   B HG21 1 
ATOM   4222 H  HG22 . VAL   B 1 16  ? 34.089 -24.505 -10.287 1.00 17.59 ?  16  VAL   B HG22 1 
ATOM   4223 H  HG23 . VAL   B 1 16  ? 32.757 -24.861 -11.076 1.00 17.59 ?  16  VAL   B HG23 1 
ATOM   4224 N  N    . TYR   B 1 17  ? 37.022 -26.190 -13.537 1.00 14.20 ?  17  TYR   B N    1 
ATOM   4225 C  CA   . TYR   B 1 17  ? 37.964 -26.935 -14.353 1.00 14.77 ?  17  TYR   B CA   1 
ATOM   4226 C  C    . TYR   B 1 17  ? 39.017 -27.555 -13.443 1.00 13.95 ?  17  TYR   B C    1 
ATOM   4227 O  O    . TYR   B 1 17  ? 39.311 -27.024 -12.368 1.00 14.33 ?  17  TYR   B O    1 
ATOM   4228 C  CB   . TYR   B 1 17  ? 38.674 -26.004 -15.346 1.00 18.50 ?  17  TYR   B CB   1 
ATOM   4229 C  CG   . TYR   B 1 17  ? 37.757 -25.228 -16.263 1.00 22.55 ?  17  TYR   B CG   1 
ATOM   4230 C  CD1  . TYR   B 1 17  ? 37.213 -24.009 -15.874 1.00 24.59 ?  17  TYR   B CD1  1 
ATOM   4231 C  CD2  . TYR   B 1 17  ? 37.443 -25.708 -17.527 1.00 24.98 ?  17  TYR   B CD2  1 
ATOM   4232 C  CE1  . TYR   B 1 17  ? 36.376 -23.293 -16.717 1.00 26.60 ?  17  TYR   B CE1  1 
ATOM   4233 C  CE2  . TYR   B 1 17  ? 36.611 -24.999 -18.378 1.00 26.87 ?  17  TYR   B CE2  1 
ATOM   4234 C  CZ   . TYR   B 1 17  ? 36.080 -23.796 -17.965 1.00 27.66 ?  17  TYR   B CZ   1 
ATOM   4235 O  OH   . TYR   B 1 17  ? 35.252 -23.091 -18.807 1.00 28.77 ?  17  TYR   B OH   1 
ATOM   4236 H  H    . TYR   B 1 17  ? 37.412 -25.598 -13.039 1.00 17.03 ?  17  TYR   B H    1 
ATOM   4237 H  HA   . TYR   B 1 17  ? 37.497 -27.634 -14.840 1.00 17.71 ?  17  TYR   B HA   1 
ATOM   4238 H  HB2  . TYR   B 1 17  ? 39.208 -25.366 -14.853 1.00 22.18 ?  17  TYR   B HB2  1 
ATOM   4239 H  HB3  . TYR   B 1 17  ? 39.241 -26.544 -15.909 1.00 22.18 ?  17  TYR   B HB3  1 
ATOM   4240 H  HD1  . TYR   B 1 17  ? 37.410 -23.665 -15.034 1.00 29.50 ?  17  TYR   B HD1  1 
ATOM   4241 H  HD2  . TYR   B 1 17  ? 37.796 -26.518 -17.812 1.00 29.97 ?  17  TYR   B HD2  1 
ATOM   4242 H  HE1  . TYR   B 1 17  ? 36.017 -22.479 -16.443 1.00 31.91 ?  17  TYR   B HE1  1 
ATOM   4243 H  HE2  . TYR   B 1 17  ? 36.404 -25.335 -19.222 1.00 32.23 ?  17  TYR   B HE2  1 
ATOM   4244 H  HH   . TYR   B 1 17  ? 35.151 -23.506 -19.531 1.00 34.51 ?  17  TYR   B HH   1 
ATOM   4245 N  N    . ILE   B 1 18  ? 39.616 -28.665 -13.876 1.00 13.86 ?  18  ILE   B N    1 
ATOM   4246 C  CA   . ILE   B 1 18  ? 40.546 -29.395 -13.021 1.00 13.88 ?  18  ILE   B CA   1 
ATOM   4247 C  C    . ILE   B 1 18  ? 41.701 -29.956 -13.844 1.00 14.57 ?  18  ILE   B C    1 
ATOM   4248 O  O    . ILE   B 1 18  ? 41.536 -30.356 -15.002 1.00 15.62 ?  18  ILE   B O    1 
ATOM   4249 C  CB   . ILE   B 1 18  ? 39.799 -30.494 -12.225 1.00 14.28 ?  18  ILE   B CB   1 
ATOM   4250 C  CG1  . ILE   B 1 18  ? 40.664 -31.043 -11.089 1.00 14.78 ?  18  ILE   B CG1  1 
ATOM   4251 C  CG2  . ILE   B 1 18  ? 39.288 -31.604 -13.161 1.00 15.09 ?  18  ILE   B CG2  1 
ATOM   4252 C  CD1  . ILE   B 1 18  ? 39.877 -31.883 -10.099 1.00 16.25 ?  18  ILE   B CD1  1 
ATOM   4253 H  H    . ILE   B 1 18  ? 39.504 -29.006 -14.654 1.00 16.62 ?  18  ILE   B H    1 
ATOM   4254 H  HA   . ILE   B 1 18  ? 40.909 -28.783 -12.363 1.00 16.65 ?  18  ILE   B HA   1 
ATOM   4255 H  HB   . ILE   B 1 18  ? 39.015 -30.092 -11.818 1.00 17.13 ?  18  ILE   B HB   1 
ATOM   4256 H  HG12 . ILE   B 1 18  ? 41.360 -31.600 -11.460 1.00 17.73 ?  18  ILE   B HG12 1 
ATOM   4257 H  HG13 . ILE   B 1 18  ? 41.047 -30.300 -10.602 1.00 17.73 ?  18  ILE   B HG13 1 
ATOM   4258 H  HG21 . ILE   B 1 18  ? 38.692 -32.188 -12.665 1.00 18.09 ?  18  ILE   B HG21 1 
ATOM   4259 H  HG22 . ILE   B 1 18  ? 38.807 -31.192 -13.897 1.00 18.09 ?  18  ILE   B HG22 1 
ATOM   4260 H  HG23 . ILE   B 1 18  ? 40.043 -32.106 -13.498 1.00 18.09 ?  18  ILE   B HG23 1 
ATOM   4261 H  HD11 . ILE   B 1 18  ? 40.464 -32.162 -9.378  1.00 19.48 ?  18  ILE   B HD11 1 
ATOM   4262 H  HD12 . ILE   B 1 18  ? 39.143 -31.357 -9.741  1.00 19.48 ?  18  ILE   B HD12 1 
ATOM   4263 H  HD13 . ILE   B 1 18  ? 39.523 -32.667 -10.554 1.00 19.48 ?  18  ILE   B HD13 1 
ATOM   4264 N  N    . LYS   B 1 19  ? 42.885 -29.986 -13.233 1.00 15.05 ?  19  LYS   B N    1 
ATOM   4265 C  CA   . LYS   B 1 19  ? 44.080 -30.477 -13.902 1.00 16.14 ?  19  LYS   B CA   1 
ATOM   4266 C  C    . LYS   B 1 19  ? 44.988 -31.147 -12.882 1.00 16.02 ?  19  LYS   B C    1 
ATOM   4267 O  O    . LYS   B 1 19  ? 45.077 -30.712 -11.732 1.00 15.57 ?  19  LYS   B O    1 
ATOM   4268 C  CB   . LYS   B 1 19  ? 44.838 -29.324 -14.570 1.00 18.19 ?  19  LYS   B CB   1 
ATOM   4269 C  CG   . LYS   B 1 19  ? 46.059 -29.747 -15.371 1.00 20.33 ?  19  LYS   B CG   1 
ATOM   4270 C  CD   . LYS   B 1 19  ? 46.800 -28.530 -15.913 1.00 22.46 ?  19  LYS   B CD   1 
ATOM   4271 C  CE   . LYS   B 1 19  ? 48.016 -28.925 -16.734 1.00 24.52 ?  19  LYS   B CE   1 
ATOM   4272 N  NZ   . LYS   B 1 19  ? 48.738 -27.737 -17.267 1.00 25.44 ?  19  LYS   B NZ   1 
ATOM   4273 H  H    . LYS   B 1 19  ? 43.014 -29.724 -12.422 1.00 18.04 ?  19  LYS   B H    1 
ATOM   4274 H  HA   . LYS   B 1 19  ? 43.825 -31.126 -14.580 1.00 19.36 ?  19  LYS   B HA   1 
ATOM   4275 H  HB2  . LYS   B 1 19  ? 44.229 -28.868 -15.172 1.00 21.81 ?  19  LYS   B HB2  1 
ATOM   4276 H  HB3  . LYS   B 1 19  ? 45.129 -28.711 -13.875 1.00 21.81 ?  19  LYS   B HB3  1 
ATOM   4277 H  HG2  . LYS   B 1 19  ? 46.659 -30.248 -14.799 1.00 24.38 ?  19  LYS   B HG2  1 
ATOM   4278 H  HG3  . LYS   B 1 19  ? 45.770 -30.296 -16.119 1.00 24.38 ?  19  LYS   B HG3  1 
ATOM   4279 H  HD2  . LYS   B 1 19  ? 46.200 -28.020 -16.481 1.00 26.94 ?  19  LYS   B HD2  1 
ATOM   4280 H  HD3  . LYS   B 1 19  ? 47.099 -27.984 -15.168 1.00 26.94 ?  19  LYS   B HD3  1 
ATOM   4281 H  HE2  . LYS   B 1 19  ? 48.627 -29.429 -16.173 1.00 29.41 ?  19  LYS   B HE2  1 
ATOM   4282 H  HE3  . LYS   B 1 19  ? 47.728 -29.470 -17.484 1.00 29.41 ?  19  LYS   B HE3  1 
ATOM   4283 H  HZ1  . LYS   B 1 19  ? 49.407 -27.998 -17.793 1.00 30.51 ?  19  LYS   B HZ1  1 
ATOM   4284 H  HZ2  . LYS   B 1 19  ? 48.180 -27.229 -17.739 1.00 30.51 ?  19  LYS   B HZ2  1 
ATOM   4285 H  HZ3  . LYS   B 1 19  ? 49.069 -27.256 -16.596 1.00 30.51 ?  19  LYS   B HZ3  1 
ATOM   4286 N  N    . ASN   B 1 20  ? 45.669 -32.204 -13.315 1.00 16.94 ?  20  ASN   B N    1 
ATOM   4287 C  CA   . ASN   B 1 20  ? 46.709 -32.831 -12.505 1.00 17.75 ?  20  ASN   B CA   1 
ATOM   4288 C  C    . ASN   B 1 20  ? 47.984 -32.013 -12.687 1.00 18.22 ?  20  ASN   B C    1 
ATOM   4289 O  O    . ASN   B 1 20  ? 48.620 -32.071 -13.745 1.00 20.05 ?  20  ASN   B O    1 
ATOM   4290 C  CB   . ASN   B 1 20  ? 46.893 -34.285 -12.940 1.00 19.57 ?  20  ASN   B CB   1 
ATOM   4291 C  CG   . ASN   B 1 20  ? 48.064 -34.980 -12.255 1.00 21.03 ?  20  ASN   B CG   1 
ATOM   4292 O  OD1  . ASN   B 1 20  ? 48.751 -35.802 -12.873 1.00 23.09 ?  20  ASN   B OD1  1 
ATOM   4293 N  ND2  . ASN   B 1 20  ? 48.286 -34.677 -10.980 1.00 20.71 ?  20  ASN   B ND2  1 
ATOM   4294 H  H    . ASN   B 1 20  ? 45.541 -32.580 -14.078 1.00 20.32 ?  20  ASN   B H    1 
ATOM   4295 H  HA   . ASN   B 1 20  ? 46.439 -32.817 -11.571 1.00 21.28 ?  20  ASN   B HA   1 
ATOM   4296 H  HB2  . ASN   B 1 20  ? 46.085 -34.786 -12.728 1.00 23.47 ?  20  ASN   B HB2  1 
ATOM   4297 H  HB3  . ASN   B 1 20  ? 47.050 -34.309 -13.895 1.00 23.47 ?  20  ASN   B HB3  1 
ATOM   4298 H  HD21 . ASN   B 1 20  ? 48.937 -35.036 -10.552 1.00 24.85 ?  20  ASN   B HD21 1 
ATOM   4299 H  HD22 . ASN   B 1 20  ? 47.782 -34.099 -10.576 1.00 24.85 ?  20  ASN   B HD22 1 
ATOM   4300 N  N    . ALA   B 1 21  ? 48.349 -31.233 -11.670 1.00 17.77 ?  21  ALA   B N    1 
ATOM   4301 C  CA   . ALA   B 1 21  ? 49.470 -30.318 -11.822 1.00 18.33 ?  21  ALA   B CA   1 
ATOM   4302 C  C    . ALA   B 1 21  ? 49.924 -29.812 -10.461 1.00 17.14 ?  21  ALA   B C    1 
ATOM   4303 O  O    . ALA   B 1 21  ? 49.172 -29.827 -9.481  1.00 16.91 ?  21  ALA   B O    1 
ATOM   4304 C  CB   . ALA   B 1 21  ? 49.097 -29.156 -12.738 1.00 20.04 ?  21  ALA   B CB   1 
ATOM   4305 H  H    . ALA   B 1 21  ? 47.969 -31.222 -10.895 1.00 21.31 ?  21  ALA   B H    1 
ATOM   4306 H  HA   . ALA   B 1 21  ? 50.209 -30.802 -12.225 1.00 21.98 ?  21  ALA   B HA   1 
ATOM   4307 H  HB1  . ALA   B 1 21  ? 49.891 -28.632 -12.896 1.00 24.04 ?  21  ALA   B HB1  1 
ATOM   4308 H  HB2  . ALA   B 1 21  ? 48.765 -29.520 -13.575 1.00 24.04 ?  21  ALA   B HB2  1 
ATOM   4309 H  HB3  . ALA   B 1 21  ? 48.412 -28.629 -12.309 1.00 24.04 ?  21  ALA   B HB3  1 
ATOM   4310 N  N    . ASP   B 1 22  ? 51.184 -29.371 -10.434 1.00 16.41 ?  22  ASP   B N    1 
ATOM   4311 C  CA   . ASP   B 1 22  ? 51.809 -28.681 -9.311  1.00 15.58 ?  22  ASP   B CA   1 
ATOM   4312 C  C    . ASP   B 1 22  ? 51.407 -27.209 -9.384  1.00 14.08 ?  22  ASP   B C    1 
ATOM   4313 O  O    . ASP   B 1 22  ? 51.714 -26.529 -10.369 1.00 14.46 ?  22  ASP   B O    1 
ATOM   4314 C  CB   . ASP   B 1 22  ? 53.326 -28.859 -9.476  1.00 17.15 ?  22  ASP   B CB   1 
ATOM   4315 C  CG   . ASP   B 1 22  ? 54.155 -28.118 -8.433  1.00 19.00 ?  22  ASP   B CG   1 
ATOM   4316 O  OD1  . ASP   B 1 22  ? 53.789 -27.003 -8.029  1.00 18.79 ?  22  ASP   B OD1  1 
ATOM   4317 O  OD2  . ASP   B 1 22  ? 55.217 -28.651 -8.039  1.00 21.49 -1 22  ASP   B OD2  1 
ATOM   4318 H  H    . ASP   B 1 22  ? 51.728 -29.470 -11.098 1.00 19.68 ?  22  ASP   B H    1 
ATOM   4319 H  HA   . ASP   B 1 22  ? 51.528 -29.067 -8.466  1.00 18.68 ?  22  ASP   B HA   1 
ATOM   4320 H  HB2  . ASP   B 1 22  ? 53.548 -29.797 -9.415  1.00 20.56 ?  22  ASP   B HB2  1 
ATOM   4321 H  HB3  . ASP   B 1 22  ? 53.588 -28.515 -10.348 1.00 20.56 ?  22  ASP   B HB3  1 
ATOM   4322 N  N    . ILE   B 1 23  ? 50.697 -26.722 -8.360  1.00 13.44 ?  23  ILE   B N    1 
ATOM   4323 C  CA   . ILE   B 1 23  ? 50.112 -25.378 -8.423  1.00 12.82 ?  23  ILE   B CA   1 
ATOM   4324 C  C    . ILE   B 1 23  ? 51.173 -24.292 -8.559  1.00 12.47 ?  23  ILE   B C    1 
ATOM   4325 O  O    . ILE   B 1 23  ? 50.907 -23.244 -9.151  1.00 12.00 ?  23  ILE   B O    1 
ATOM   4326 C  CB   . ILE   B 1 23  ? 49.175 -25.130 -7.222  1.00 12.89 ?  23  ILE   B CB   1 
ATOM   4327 C  CG1  . ILE   B 1 23  ? 48.340 -23.861 -7.418  1.00 13.31 ?  23  ILE   B CG1  1 
ATOM   4328 C  CG2  . ILE   B 1 23  ? 49.946 -25.113 -5.914  1.00 14.04 ?  23  ILE   B CG2  1 
ATOM   4329 C  CD1  . ILE   B 1 23  ? 47.239 -23.696 -6.371  1.00 14.26 ?  23  ILE   B CD1  1 
ATOM   4330 H  H    . ILE   B 1 23  ? 50.527 -27.151 -7.634  1.00 16.11 ?  23  ILE   B H    1 
ATOM   4331 H  HA   . ILE   B 1 23  ? 49.561 -25.328 -9.219  1.00 15.37 ?  23  ILE   B HA   1 
ATOM   4332 H  HB   . ILE   B 1 23  ? 48.553 -25.878 -7.185  1.00 15.46 ?  23  ILE   B HB   1 
ATOM   4333 H  HG12 . ILE   B 1 23  ? 48.926 -23.089 -7.361  1.00 15.96 ?  23  ILE   B HG12 1 
ATOM   4334 H  HG13 . ILE   B 1 23  ? 47.920 -23.890 -8.293  1.00 15.96 ?  23  ILE   B HG13 1 
ATOM   4335 H  HG21 . ILE   B 1 23  ? 49.315 -25.118 -5.178  1.00 16.84 ?  23  ILE   B HG21 1 
ATOM   4336 H  HG22 . ILE   B 1 23  ? 50.504 -25.908 -5.872  1.00 16.84 ?  23  ILE   B HG22 1 
ATOM   4337 H  HG23 . ILE   B 1 23  ? 50.495 -24.320 -5.882  1.00 16.84 ?  23  ILE   B HG23 1 
ATOM   4338 H  HD11 . ILE   B 1 23  ? 46.699 -22.924 -6.601  1.00 17.10 ?  23  ILE   B HD11 1 
ATOM   4339 H  HD12 . ILE   B 1 23  ? 46.690 -24.495 -6.365  1.00 17.10 ?  23  ILE   B HD12 1 
ATOM   4340 H  HD13 . ILE   B 1 23  ? 47.648 -23.567 -5.502  1.00 17.10 ?  23  ILE   B HD13 1 
ATOM   4341 N  N    . VAL   B 1 24  ? 52.372 -24.504 -8.008  1.00 12.69 ?  24  VAL   B N    1 
ATOM   4342 C  CA   . VAL   B 1 24  ? 53.449 -23.522 -8.167  1.00 13.35 ?  24  VAL   B CA   1 
ATOM   4343 C  C    . VAL   B 1 24  ? 53.908 -23.471 -9.617  1.00 13.29 ?  24  VAL   B C    1 
ATOM   4344 O  O    . VAL   B 1 24  ? 54.037 -22.394 -10.212 1.00 13.70 ?  24  VAL   B O    1 
ATOM   4345 C  CB   . VAL   B 1 24  ? 54.622 -23.839 -7.219  1.00 14.03 ?  24  VAL   B CB   1 
ATOM   4346 C  CG1  . VAL   B 1 24  ? 55.834 -22.961 -7.547  1.00 14.71 ?  24  VAL   B CG1  1 
ATOM   4347 C  CG2  . VAL   B 1 24  ? 54.193 -23.653 -5.784  1.00 15.21 ?  24  VAL   B CG2  1 
ATOM   4348 H  H    . VAL   B 1 24  ? 52.584 -25.195 -7.545  1.00 15.22 ?  24  VAL   B H    1 
ATOM   4349 H  HA   . VAL   B 1 24  ? 53.107 -22.644 -7.932  1.00 16.00 ?  24  VAL   B HA   1 
ATOM   4350 H  HB   . VAL   B 1 24  ? 54.881 -24.764 -7.335  1.00 16.83 ?  24  VAL   B HB   1 
ATOM   4351 H  HG11 . VAL   B 1 24  ? 56.427 -22.944 -6.778  1.00 17.64 ?  24  VAL   B HG11 1 
ATOM   4352 H  HG12 . VAL   B 1 24  ? 56.297 -23.335 -8.311  1.00 17.64 ?  24  VAL   B HG12 1 
ATOM   4353 H  HG13 . VAL   B 1 24  ? 55.530 -22.061 -7.746  1.00 17.64 ?  24  VAL   B HG13 1 
ATOM   4354 H  HG21 . VAL   B 1 24  ? 54.920 -23.915 -5.200  1.00 18.24 ?  24  VAL   B HG21 1 
ATOM   4355 H  HG22 . VAL   B 1 24  ? 53.971 -22.720 -5.638  1.00 18.24 ?  24  VAL   B HG22 1 
ATOM   4356 H  HG23 . VAL   B 1 24  ? 53.414 -24.208 -5.612  1.00 18.24 ?  24  VAL   B HG23 1 
ATOM   4357 N  N    . GLU   B 1 25  ? 54.173 -24.641 -10.204 1.00 14.30 ?  25  GLU   B N    1 
ATOM   4358 C  CA   . GLU   B 1 25  ? 54.560 -24.683 -11.607 1.00 16.19 ?  25  GLU   B CA   1 
ATOM   4359 C  C    . GLU   B 1 25  ? 53.453 -24.133 -12.492 1.00 14.97 ?  25  GLU   B C    1 
ATOM   4360 O  O    . GLU   B 1 25  ? 53.723 -23.423 -13.469 1.00 15.86 ?  25  GLU   B O    1 
ATOM   4361 C  CB   . GLU   B 1 25  ? 54.943 -26.109 -12.001 1.00 20.83 ?  25  GLU   B CB   1 
ATOM   4362 C  CG   . GLU   B 1 25  ? 56.237 -26.577 -11.349 1.00 26.61 ?  25  GLU   B CG   1 
ATOM   4363 C  CD   . GLU   B 1 25  ? 57.360 -25.554 -11.435 1.00 31.73 ?  25  GLU   B CD   1 
ATOM   4364 O  OE1  . GLU   B 1 25  ? 57.713 -25.138 -12.559 1.00 33.35 ?  25  GLU   B OE1  1 
ATOM   4365 O  OE2  . GLU   B 1 25  ? 57.881 -25.152 -10.370 1.00 33.24 -1 25  GLU   B OE2  1 
ATOM   4366 H  H    . GLU   B 1 25  ? 54.132 -25.408 -9.815  1.00 17.15 ?  25  GLU   B H    1 
ATOM   4367 H  HA   . GLU   B 1 25  ? 55.321 -24.107 -11.735 1.00 19.42 ?  25  GLU   B HA   1 
ATOM   4368 H  HB2  . GLU   B 1 25  ? 54.235 -26.717 -11.723 1.00 24.98 ?  25  GLU   B HB2  1 
ATOM   4369 H  HB3  . GLU   B 1 25  ? 55.054 -26.154 -12.963 1.00 24.98 ?  25  GLU   B HB3  1 
ATOM   4370 H  HG2  . GLU   B 1 25  ? 56.080 -26.737 -10.411 1.00 31.93 ?  25  GLU   B HG2  1 
ATOM   4371 H  HG3  . GLU   B 1 25  ? 56.538 -27.385 -11.789 1.00 31.93 ?  25  GLU   B HG3  1 
ATOM   4372 N  N    A GLU   B 1 26  ? 52.198 -24.444 -12.162 0.50 14.36 ?  26  GLU   B N    1 
ATOM   4373 N  N    B GLU   B 1 26  ? 52.197 -24.440 -12.159 0.50 14.44 ?  26  GLU   B N    1 
ATOM   4374 C  CA   A GLU   B 1 26  ? 51.077 -23.914 -12.929 0.50 14.74 ?  26  GLU   B CA   1 
ATOM   4375 C  CA   B GLU   B 1 26  ? 51.074 -23.917 -12.931 0.50 14.96 ?  26  GLU   B CA   1 
ATOM   4376 C  C    A GLU   B 1 26  ? 51.031 -22.397 -12.850 0.50 13.99 ?  26  GLU   B C    1 
ATOM   4377 C  C    B GLU   B 1 26  ? 51.011 -22.399 -12.847 0.50 14.02 ?  26  GLU   B C    1 
ATOM   4378 O  O    A GLU   B 1 26  ? 50.856 -21.716 -13.865 0.50 14.92 ?  26  GLU   B O    1 
ATOM   4379 O  O    B GLU   B 1 26  ? 50.795 -21.720 -13.856 0.50 14.86 ?  26  GLU   B O    1 
ATOM   4380 C  CB   A GLU   B 1 26  ? 49.763 -24.498 -12.411 0.50 16.20 ?  26  GLU   B CB   1 
ATOM   4381 C  CB   B GLU   B 1 26  ? 49.761 -24.518 -12.425 0.50 16.82 ?  26  GLU   B CB   1 
ATOM   4382 C  CG   A GLU   B 1 26  ? 49.412 -25.845 -12.999 0.50 18.33 ?  26  GLU   B CG   1 
ATOM   4383 C  CG   B GLU   B 1 26  ? 49.320 -25.764 -13.161 0.50 19.39 ?  26  GLU   B CG   1 
ATOM   4384 C  CD   A GLU   B 1 26  ? 49.219 -25.819 -14.506 0.50 19.20 ?  26  GLU   B CD   1 
ATOM   4385 C  CD   B GLU   B 1 26  ? 48.964 -25.475 -14.617 0.50 20.51 ?  26  GLU   B CD   1 
ATOM   4386 O  OE1  A GLU   B 1 26  ? 48.397 -25.022 -15.005 0.50 18.90 ?  26  GLU   B OE1  1 
ATOM   4387 O  OE1  B GLU   B 1 26  ? 47.877 -24.907 -14.881 0.50 21.34 ?  26  GLU   B OE1  1 
ATOM   4388 O  OE2  A GLU   B 1 26  ? 49.898 -26.605 -15.191 0.50 19.93 -1 26  GLU   B OE2  1 
ATOM   4389 O  OE2  B GLU   B 1 26  ? 49.777 -25.810 -15.496 0.50 20.50 -1 26  GLU   B OE2  1 
ATOM   4390 H  H    A GLU   B 1 26  ? 51.970 -24.953 -11.503 0.50 17.22 ?  26  GLU   B H    1 
ATOM   4391 H  H    B GLU   B 1 26  ? 51.968 -24.945 -11.497 0.50 17.32 ?  26  GLU   B H    1 
ATOM   4392 H  HA   A GLU   B 1 26  ? 51.178 -24.164 -13.858 0.50 17.67 ?  26  GLU   B HA   1 
ATOM   4393 H  HA   B GLU   B 1 26  ? 51.187 -24.163 -13.861 0.50 17.94 ?  26  GLU   B HA   1 
ATOM   4394 H  HB2  A GLU   B 1 26  ? 49.827 -24.606 -11.445 0.50 19.43 ?  26  GLU   B HB2  1 
ATOM   4395 H  HB2  B GLU   B 1 26  ? 49.860 -24.743 -11.489 0.50 20.17 ?  26  GLU   B HB2  1 
ATOM   4396 H  HB3  A GLU   B 1 26  ? 49.041 -23.882 -12.619 0.50 19.43 ?  26  GLU   B HB3  1 
ATOM   4397 H  HB3  B GLU   B 1 26  ? 49.057 -23.855 -12.531 0.50 20.17 ?  26  GLU   B HB3  1 
ATOM   4398 H  HG2  A GLU   B 1 26  ? 50.137 -26.450 -12.819 0.50 21.98 ?  26  GLU   B HG2  1 
ATOM   4399 H  HG2  B GLU   B 1 26  ? 50.035 -26.424 -13.099 0.50 23.26 ?  26  GLU   B HG2  1 
ATOM   4400 H  HG3  A GLU   B 1 26  ? 48.592 -26.154 -12.592 0.50 21.98 ?  26  GLU   B HG3  1 
ATOM   4401 H  HG3  B GLU   B 1 26  ? 48.517 -26.108 -12.747 0.50 23.26 ?  26  GLU   B HG3  1 
ATOM   4402 N  N    . ALA   B 1 27  ? 51.170 -21.848 -11.642 1.00 12.98 ?  27  ALA   B N    1 
ATOM   4403 C  CA   . ALA   B 1 27  ? 51.136 -20.401 -11.491 1.00 13.36 ?  27  ALA   B CA   1 
ATOM   4404 C  C    . ALA   B 1 27  ? 52.207 -19.745 -12.351 1.00 14.29 ?  27  ALA   B C    1 
ATOM   4405 O  O    . ALA   B 1 27  ? 51.947 -18.752 -13.044 1.00 14.83 ?  27  ALA   B O    1 
ATOM   4406 C  CB   . ALA   B 1 27  ? 51.300 -20.028 -10.015 1.00 12.97 ?  27  ALA   B CB   1 
ATOM   4407 H  H    A ALA   B 1 27  ? 51.280 -22.286 -10.909 0.50 15.57 ?  27  ALA   B H    1 
ATOM   4408 H  H    B ALA   B 1 27  ? 51.287 -22.285 -10.910 0.50 15.57 ?  27  ALA   B H    1 
ATOM   4409 H  HA   . ALA   B 1 27  ? 50.280 -20.067 -11.783 1.00 16.02 ?  27  ALA   B HA   1 
ATOM   4410 H  HB1  . ALA   B 1 27  ? 51.271 -19.061 -9.923  1.00 15.56 ?  27  ALA   B HB1  1 
ATOM   4411 H  HB2  . ALA   B 1 27  ? 50.571 -20.424 -9.505  1.00 15.56 ?  27  ALA   B HB2  1 
ATOM   4412 H  HB3  . ALA   B 1 27  ? 52.148 -20.364 -9.688  1.00 15.56 ?  27  ALA   B HB3  1 
ATOM   4413 N  N    . LYS   B 1 28  ? 53.421 -20.296 -12.338 1.00 15.51 ?  28  LYS   B N    1 
ATOM   4414 C  CA   . LYS   B 1 28  ? 54.499 -19.688 -13.109 1.00 17.88 ?  28  LYS   B CA   1 
ATOM   4415 C  C    . LYS   B 1 28  ? 54.243 -19.771 -14.608 1.00 18.31 ?  28  LYS   B C    1 
ATOM   4416 O  O    . LYS   B 1 28  ? 54.652 -18.872 -15.350 1.00 19.37 ?  28  LYS   B O    1 
ATOM   4417 C  CB   . LYS   B 1 28  ? 55.854 -20.282 -12.709 1.00 21.65 ?  28  LYS   B CB   1 
ATOM   4418 C  CG   . LYS   B 1 28  ? 56.245 -19.940 -11.272 1.00 25.98 ?  28  LYS   B CG   1 
ATOM   4419 C  CD   . LYS   B 1 28  ? 57.666 -20.364 -10.923 1.00 30.95 ?  28  LYS   B CD   1 
ATOM   4420 C  CE   . LYS   B 1 28  ? 57.757 -21.852 -10.676 1.00 34.77 ?  28  LYS   B CE   1 
ATOM   4421 N  NZ   . LYS   B 1 28  ? 59.110 -22.247 -10.194 1.00 37.71 ?  28  LYS   B NZ   1 
ATOM   4422 H  H    . LYS   B 1 28  ? 53.645 -21.003 -11.894 1.00 18.60 ?  28  LYS   B H    1 
ATOM   4423 H  HA   . LYS   B 1 28  ? 54.535 -18.751 -12.890 1.00 21.44 ?  28  LYS   B HA   1 
ATOM   4424 H  HB2  . LYS   B 1 28  ? 55.823 -21.247 -12.785 1.00 25.97 ?  28  LYS   B HB2  1 
ATOM   4425 H  HB3  . LYS   B 1 28  ? 56.545 -19.926 -13.295 1.00 25.97 ?  28  LYS   B HB3  1 
ATOM   4426 H  HG2  . LYS   B 1 28  ? 56.180 -18.979 -11.149 1.00 31.17 ?  28  LYS   B HG2  1 
ATOM   4427 H  HG3  . LYS   B 1 28  ? 55.640 -20.393 -10.667 1.00 31.17 ?  28  LYS   B HG3  1 
ATOM   4428 H  HD2  . LYS   B 1 28  ? 58.256 -20.138 -11.659 1.00 37.13 ?  28  LYS   B HD2  1 
ATOM   4429 H  HD3  . LYS   B 1 28  ? 57.946 -19.902 -10.116 1.00 37.13 ?  28  LYS   B HD3  1 
ATOM   4430 H  HE2  . LYS   B 1 28  ? 57.107 -22.104 -10.001 1.00 41.71 ?  28  LYS   B HE2  1 
ATOM   4431 H  HE3  . LYS   B 1 28  ? 57.579 -22.325 -11.504 1.00 41.71 ?  28  LYS   B HE3  1 
ATOM   4432 H  HZ1  . LYS   B 1 28  ? 59.140 -23.125 -10.056 1.00 45.24 ?  28  LYS   B HZ1  1 
ATOM   4433 H  HZ2  . LYS   B 1 28  ? 59.724 -22.027 -10.800 1.00 45.24 ?  28  LYS   B HZ2  1 
ATOM   4434 H  HZ3  . LYS   B 1 28  ? 59.295 -21.827 -9.431  1.00 45.24 ?  28  LYS   B HZ3  1 
ATOM   4435 N  N    . LYS   B 1 29  ? 53.538 -20.807 -15.068 1.00 19.15 ?  29  LYS   B N    1 
ATOM   4436 C  CA   . LYS   B 1 29  ? 53.268 -20.959 -16.494 1.00 21.94 ?  29  LYS   B CA   1 
ATOM   4437 C  C    . LYS   B 1 29  ? 52.026 -20.198 -16.944 1.00 20.93 ?  29  LYS   B C    1 
ATOM   4438 O  O    . LYS   B 1 29  ? 52.038 -19.569 -18.008 1.00 22.12 ?  29  LYS   B O    1 
ATOM   4439 C  CB   . LYS   B 1 29  ? 53.121 -22.442 -16.849 1.00 26.54 ?  29  LYS   B CB   1 
ATOM   4440 C  CG   . LYS   B 1 29  ? 52.832 -22.692 -18.322 1.00 30.83 ?  29  LYS   B CG   1 
ATOM   4441 C  CD   . LYS   B 1 29  ? 53.048 -24.152 -18.700 1.00 34.43 ?  29  LYS   B CD   1 
ATOM   4442 C  CE   . LYS   B 1 29  ? 51.946 -25.050 -18.163 1.00 36.93 ?  29  LYS   B CE   1 
ATOM   4443 N  NZ   . LYS   B 1 29  ? 52.182 -26.481 -18.518 1.00 38.31 ?  29  LYS   B NZ   1 
ATOM   4444 H  H    . LYS   B 1 29  ? 53.195 -21.431 -14.572 1.00 22.97 ?  29  LYS   B H    1 
ATOM   4445 H  HA   . LYS   B 1 29  ? 54.022 -20.613 -16.989 1.00 26.31 ?  29  LYS   B HA   1 
ATOM   4446 H  HB2  . LYS   B 1 29  ? 53.950 -22.899 -16.630 1.00 31.84 ?  29  LYS   B HB2  1 
ATOM   4447 H  HB3  . LYS   B 1 29  ? 52.392 -22.820 -16.336 1.00 31.84 ?  29  LYS   B HB3  1 
ATOM   4448 H  HG2  . LYS   B 1 29  ? 51.908 -22.464 -18.508 1.00 36.98 ?  29  LYS   B HG2  1 
ATOM   4449 H  HG3  . LYS   B 1 29  ? 53.427 -22.147 -18.862 1.00 36.98 ?  29  LYS   B HG3  1 
ATOM   4450 H  HD2  . LYS   B 1 29  ? 53.060 -24.234 -19.666 1.00 41.30 ?  29  LYS   B HD2  1 
ATOM   4451 H  HD3  . LYS   B 1 29  ? 53.892 -24.457 -18.329 1.00 41.30 ?  29  LYS   B HD3  1 
ATOM   4452 H  HE2  . LYS   B 1 29  ? 51.915 -24.979 -17.196 1.00 44.31 ?  29  LYS   B HE2  1 
ATOM   4453 H  HE3  . LYS   B 1 29  ? 51.096 -24.779 -18.546 1.00 44.31 ?  29  LYS   B HE3  1 
ATOM   4454 H  HZ1  . LYS   B 1 29  ? 51.525 -26.987 -18.195 1.00 45.96 ?  29  LYS   B HZ1  1 
ATOM   4455 H  HZ2  . LYS   B 1 29  ? 52.210 -26.574 -19.403 1.00 45.96 ?  29  LYS   B HZ2  1 
ATOM   4456 H  HZ3  . LYS   B 1 29  ? 52.955 -26.756 -18.174 1.00 45.96 ?  29  LYS   B HZ3  1 
ATOM   4457 N  N    . VAL   B 1 30  ? 50.954 -20.254 -16.152 1.00 19.54 ?  30  VAL   B N    1 
ATOM   4458 C  CA   . VAL   B 1 30  ? 49.667 -19.674 -16.536 1.00 19.64 ?  30  VAL   B CA   1 
ATOM   4459 C  C    . VAL   B 1 30  ? 49.664 -18.164 -16.375 1.00 18.04 ?  30  VAL   B C    1 
ATOM   4460 O  O    . VAL   B 1 30  ? 48.916 -17.456 -17.069 1.00 18.59 ?  30  VAL   B O    1 
ATOM   4461 C  CB   . VAL   B 1 30  ? 48.563 -20.297 -15.660 1.00 21.33 ?  30  VAL   B CB   1 
ATOM   4462 C  CG1  . VAL   B 1 30  ? 47.275 -19.478 -15.718 1.00 21.99 ?  30  VAL   B CG1  1 
ATOM   4463 C  CG2  . VAL   B 1 30  ? 48.320 -21.748 -16.055 1.00 22.12 ?  30  VAL   B CG2  1 
ATOM   4464 H  H    . VAL   B 1 30  ? 50.940 -20.648 -15.378 1.00 23.44 ?  30  VAL   B H    1 
ATOM   4465 H  HA   . VAL   B 1 30  ? 49.475 -19.901 -17.460 1.00 23.55 ?  30  VAL   B HA   1 
ATOM   4466 H  HB   . VAL   B 1 30  ? 48.861 -20.300 -14.737 1.00 25.59 ?  30  VAL   B HB   1 
ATOM   4467 H  HG11 . VAL   B 1 30  ? 46.534 -20.056 -15.478 1.00 26.37 ?  30  VAL   B HG11 1 
ATOM   4468 H  HG12 . VAL   B 1 30  ? 47.334 -18.745 -15.087 1.00 26.37 ?  30  VAL   B HG12 1 
ATOM   4469 H  HG13 . VAL   B 1 30  ? 47.148 -19.148 -16.616 1.00 26.37 ?  30  VAL   B HG13 1 
ATOM   4470 H  HG21 . VAL   B 1 30  ? 47.626 -22.124 -15.485 1.00 26.53 ?  30  VAL   B HG21 1 
ATOM   4471 H  HG22 . VAL   B 1 30  ? 48.031 -21.780 -16.983 1.00 26.53 ?  30  VAL   B HG22 1 
ATOM   4472 H  HG23 . VAL   B 1 30  ? 49.141 -22.249 -15.947 1.00 26.53 ?  30  VAL   B HG23 1 
ATOM   4473 N  N    A LYS   B 1 31  ? 50.476 -17.650 -15.459 0.50 17.58 ?  31  LYS   B N    1 
ATOM   4474 N  N    B LYS   B 1 31  ? 50.472 -17.654 -15.453 0.50 17.59 ?  31  LYS   B N    1 
ATOM   4475 C  CA   A LYS   B 1 31  ? 50.481 -16.238 -15.097 0.50 17.85 ?  31  LYS   B CA   1 
ATOM   4476 C  CA   B LYS   B 1 31  ? 50.483 -16.242 -15.094 0.50 17.85 ?  31  LYS   B CA   1 
ATOM   4477 C  C    A LYS   B 1 31  ? 49.084 -15.743 -14.705 0.50 15.88 ?  31  LYS   B C    1 
ATOM   4478 C  C    B LYS   B 1 31  ? 49.082 -15.752 -14.711 0.50 15.86 ?  31  LYS   B C    1 
ATOM   4479 O  O    A LYS   B 1 31  ? 48.542 -14.829 -15.333 0.50 16.21 ?  31  LYS   B O    1 
ATOM   4480 O  O    B LYS   B 1 31  ? 48.532 -14.855 -15.358 0.50 16.11 ?  31  LYS   B O    1 
ATOM   4481 C  CB   A LYS   B 1 31  ? 51.087 -15.386 -16.204 0.50 20.35 ?  31  LYS   B CB   1 
ATOM   4482 C  CB   B LYS   B 1 31  ? 51.089 -15.402 -16.211 0.50 20.33 ?  31  LYS   B CB   1 
ATOM   4483 C  CG   A LYS   B 1 31  ? 52.535 -15.758 -16.499 0.50 23.13 ?  31  LYS   B CG   1 
ATOM   4484 C  CG   B LYS   B 1 31  ? 52.496 -15.860 -16.574 0.50 23.04 ?  31  LYS   B CG   1 
ATOM   4485 C  CD   A LYS   B 1 31  ? 53.108 -14.957 -17.649 0.50 25.59 ?  31  LYS   B CD   1 
ATOM   4486 C  CD   B LYS   B 1 31  ? 53.061 -15.097 -17.750 0.50 25.45 ?  31  LYS   B CD   1 
ATOM   4487 C  CE   A LYS   B 1 31  ? 54.590 -15.228 -17.814 0.50 27.49 ?  31  LYS   B CE   1 
ATOM   4488 C  CE   B LYS   B 1 31  ? 54.555 -15.311 -17.863 0.50 27.27 ?  31  LYS   B CE   1 
ATOM   4489 N  NZ   A LYS   B 1 31  ? 55.357 -14.847 -16.594 0.50 28.73 ?  31  LYS   B NZ   1 
ATOM   4490 N  NZ   B LYS   B 1 31  ? 55.259 -14.851 -16.631 0.50 28.44 ?  31  LYS   B NZ   1 
ATOM   4491 H  H    A LYS   B 1 31  ? 51.055 -18.123 -15.032 0.50 21.08 ?  31  LYS   B H    1 
ATOM   4492 H  H    B LYS   B 1 31  ? 51.046 -18.128 -15.019 0.50 21.10 ?  31  LYS   B H    1 
ATOM   4493 H  HA   A LYS   B 1 31  ? 51.042 -16.147 -14.323 0.50 21.41 ?  31  LYS   B HA   1 
ATOM   4494 H  HA   B LYS   B 1 31  ? 51.042 -16.144 -14.318 0.50 21.41 ?  31  LYS   B HA   1 
ATOM   4495 H  HB2  A LYS   B 1 31  ? 50.573 -15.508 -17.018 0.50 24.41 ?  31  LYS   B HB2  1 
ATOM   4496 H  HB2  B LYS   B 1 31  ? 50.539 -15.474 -17.005 0.50 24.38 ?  31  LYS   B HB2  1 
ATOM   4497 H  HB3  A LYS   B 1 31  ? 51.063 -14.460 -15.927 0.50 24.41 ?  31  LYS   B HB3  1 
ATOM   4498 H  HB3  B LYS   B 1 31  ? 51.141 -14.483 -15.916 0.50 24.38 ?  31  LYS   B HB3  1 
ATOM   4499 H  HG2  A LYS   B 1 31  ? 53.068 -15.588 -15.707 0.50 27.75 ?  31  LYS   B HG2  1 
ATOM   4500 H  HG2  B LYS   B 1 31  ? 53.075 -15.724 -15.808 0.50 27.64 ?  31  LYS   B HG2  1 
ATOM   4501 H  HG3  A LYS   B 1 31  ? 52.580 -16.701 -16.732 0.50 27.75 ?  31  LYS   B HG3  1 
ATOM   4502 H  HG3  B LYS   B 1 31  ? 52.475 -16.802 -16.809 0.50 27.64 ?  31  LYS   B HG3  1 
ATOM   4503 H  HD2  A LYS   B 1 31  ? 52.655 -15.210 -18.468 0.50 30.69 ?  31  LYS   B HD2  1 
ATOM   4504 H  HD2  B LYS   B 1 31  ? 52.642 -15.414 -18.565 0.50 30.53 ?  31  LYS   B HD2  1 
ATOM   4505 H  HD3  A LYS   B 1 31  ? 52.984 -14.014 -17.470 0.50 30.69 ?  31  LYS   B HD3  1 
ATOM   4506 H  HD3  B LYS   B 1 31  ? 52.893 -14.152 -17.626 0.50 30.53 ?  31  LYS   B HD3  1 
ATOM   4507 H  HE2  A LYS   B 1 31  ? 54.728 -16.176 -17.976 0.50 32.97 ?  31  LYS   B HE2  1 
ATOM   4508 H  HE2  B LYS   B 1 31  ? 54.737 -16.258 -17.982 0.50 32.72 ?  31  LYS   B HE2  1 
ATOM   4509 H  HE3  A LYS   B 1 31  ? 54.927 -14.708 -18.560 0.50 32.97 ?  31  LYS   B HE3  1 
ATOM   4510 H  HE3  B LYS   B 1 31  ? 54.895 -14.806 -18.617 0.50 32.72 ?  31  LYS   B HE3  1 
ATOM   4511 H  HZ1  A LYS   B 1 31  ? 56.230 -14.914 -16.749 0.50 34.47 ?  31  LYS   B HZ1  1 
ATOM   4512 H  HZ1  B LYS   B 1 31  ? 56.134 -14.805 -16.779 0.50 34.11 ?  31  LYS   B HZ1  1 
ATOM   4513 H  HZ2  A LYS   B 1 31  ? 55.167 -14.008 -16.366 0.50 34.47 ?  31  LYS   B HZ2  1 
ATOM   4514 H  HZ2  B LYS   B 1 31  ? 54.962 -14.045 -16.396 0.50 34.11 ?  31  LYS   B HZ2  1 
ATOM   4515 H  HZ3  A LYS   B 1 31  ? 55.141 -15.385 -15.917 0.50 34.47 ?  31  LYS   B HZ3  1 
ATOM   4516 H  HZ3  B LYS   B 1 31  ? 55.108 -15.419 -15.962 0.50 34.11 ?  31  LYS   B HZ3  1 
ATOM   4517 N  N    . PRO   B 1 32  ? 48.484 -16.325 -13.663 1.00 14.48 ?  32  PRO   B N    1 
ATOM   4518 C  CA   . PRO   B 1 32  ? 47.111 -15.957 -13.293 1.00 13.67 ?  32  PRO   B CA   1 
ATOM   4519 C  C    . PRO   B 1 32  ? 47.039 -14.617 -12.577 1.00 13.71 ?  32  PRO   B C    1 
ATOM   4520 O  O    . PRO   B 1 32  ? 47.973 -14.198 -11.883 1.00 14.73 ?  32  PRO   B O    1 
ATOM   4521 C  CB   . PRO   B 1 32  ? 46.713 -17.077 -12.322 1.00 13.86 ?  32  PRO   B CB   1 
ATOM   4522 C  CG   . PRO   B 1 32  ? 48.011 -17.408 -11.644 1.00 14.24 ?  32  PRO   B CG   1 
ATOM   4523 C  CD   . PRO   B 1 32  ? 49.062 -17.303 -12.719 1.00 14.44 ?  32  PRO   B CD   1 
ATOM   4524 H  HA   . PRO   B 1 32  ? 46.521 -15.972 -14.076 1.00 16.39 ?  32  PRO   B HA   1 
ATOM   4525 H  HB2  . PRO   B 1 32  ? 46.059 -16.748 -11.686 1.00 16.62 ?  32  PRO   B HB2  1 
ATOM   4526 H  HB3  . PRO   B 1 32  ? 46.369 -17.846 -12.809 1.00 16.62 ?  32  PRO   B HB3  1 
ATOM   4527 H  HG2  . PRO   B 1 32  ? 48.180 -16.766 -10.936 1.00 17.07 ?  32  PRO   B HG2  1 
ATOM   4528 H  HG3  . PRO   B 1 32  ? 47.973 -18.309 -11.286 1.00 17.07 ?  32  PRO   B HG3  1 
ATOM   4529 H  HD2  . PRO   B 1 32  ? 49.887 -16.963 -12.348 1.00 17.32 ?  32  PRO   B HD2  1 
ATOM   4530 H  HD3  . PRO   B 1 32  ? 49.186 -18.165 -13.147 1.00 17.32 ?  32  PRO   B HD3  1 
ATOM   4531 N  N    . THR   B 1 33  ? 45.884 -13.960 -12.729 1.00 13.00 ?  33  THR   B N    1 
ATOM   4532 C  CA   . THR   B 1 33  ? 45.611 -12.781 -11.917 1.00 13.05 ?  33  THR   B CA   1 
ATOM   4533 C  C    . THR   B 1 33  ? 45.563 -13.135 -10.437 1.00 12.76 ?  33  THR   B C    1 
ATOM   4534 O  O    . THR   B 1 33  ? 46.034 -12.356 -9.595  1.00 13.64 ?  33  THR   B O    1 
ATOM   4535 C  CB   . THR   B 1 33  ? 44.294 -12.136 -12.357 1.00 13.81 ?  33  THR   B CB   1 
ATOM   4536 O  OG1  . THR   B 1 33  ? 44.316 -11.903 -13.767 1.00 14.20 ?  33  THR   B OG1  1 
ATOM   4537 C  CG2  . THR   B 1 33  ? 44.070 -10.830 -11.631 1.00 15.33 ?  33  THR   B CG2  1 
ATOM   4538 H  H    . THR   B 1 33  ? 45.254 -14.183 -13.283 1.00 15.59 ?  33  THR   B H    1 
ATOM   4539 H  HA   . THR   B 1 33  ? 46.322 -12.142 -12.060 1.00 15.65 ?  33  THR   B HA   1 
ATOM   4540 H  HB   . THR   B 1 33  ? 43.559 -12.737 -12.151 1.00 16.57 ?  33  THR   B HB   1 
ATOM   4541 H  HG1  . THR   B 1 33  ? 43.600 -11.533 -14.015 1.00 17.03 ?  33  THR   B HG1  1 
ATOM   4542 H  HG21 . THR   B 1 33  ? 43.312 -10.366 -12.010 1.00 18.39 ?  33  THR   B HG21 1 
ATOM   4543 H  HG22 . THR   B 1 33  ? 43.901 -11.000 -10.690 1.00 18.39 ?  33  THR   B HG22 1 
ATOM   4544 H  HG23 . THR   B 1 33  ? 44.859 -10.269 -11.712 1.00 18.39 ?  33  THR   B HG23 1 
ATOM   4545 N  N    . VAL   B 1 34  ? 44.995 -14.298 -10.097 1.00 12.07 ?  34  VAL   B N    1 
ATOM   4546 C  CA   . VAL   B 1 34  ? 44.794 -14.697 -8.706  1.00 11.57 ?  34  VAL   B CA   1 
ATOM   4547 C  C    . VAL   B 1 34  ? 45.208 -16.147 -8.537  1.00 10.90 ?  34  VAL   B C    1 
ATOM   4548 O  O    . VAL   B 1 34  ? 44.681 -17.033 -9.220  1.00 11.50 ?  34  VAL   B O    1 
ATOM   4549 C  CB   . VAL   B 1 34  ? 43.325 -14.546 -8.264  1.00 12.51 ?  34  VAL   B CB   1 
ATOM   4550 C  CG1  . VAL   B 1 34  ? 43.157 -14.997 -6.813  1.00 12.96 ?  34  VAL   B CG1  1 
ATOM   4551 C  CG2  . VAL   B 1 34  ? 42.833 -13.122 -8.460  1.00 13.68 ?  34  VAL   B CG2  1 
ATOM   4552 H  H    . VAL   B 1 34  ? 44.735 -14.891 -10.668 1.00 14.48 ?  34  VAL   B H    1 
ATOM   4553 H  HA   . VAL   B 1 34  ? 45.342 -14.144 -8.129  1.00 13.87 ?  34  VAL   B HA   1 
ATOM   4554 H  HB   . VAL   B 1 34  ? 42.771 -15.118 -8.823  1.00 15.01 ?  34  VAL   B HB   1 
ATOM   4555 H  HG11 . VAL   B 1 34  ? 42.307 -14.666 -6.475  1.00 15.54 ?  34  VAL   B HG11 1 
ATOM   4556 H  HG12 . VAL   B 1 34  ? 43.169 -15.965 -6.777  1.00 15.54 ?  34  VAL   B HG12 1 
ATOM   4557 H  HG13 . VAL   B 1 34  ? 43.883 -14.633 -6.284  1.00 15.54 ?  34  VAL   B HG13 1 
ATOM   4558 H  HG21 . VAL   B 1 34  ? 41.912 -13.057 -8.156  1.00 16.40 ?  34  VAL   B HG21 1 
ATOM   4559 H  HG22 . VAL   B 1 34  ? 43.393 -12.519 -7.950  1.00 16.40 ?  34  VAL   B HG22 1 
ATOM   4560 H  HG23 . VAL   B 1 34  ? 42.879 -12.893 -9.406  1.00 16.40 ?  34  VAL   B HG23 1 
ATOM   4561 N  N    . VAL   B 1 35  ? 46.111 -16.396 -7.591  1.00 10.32 ?  35  VAL   B N    1 
ATOM   4562 C  CA   . VAL   B 1 35  ? 46.347 -17.738 -7.071  1.00 10.12 ?  35  VAL   B CA   1 
ATOM   4563 C  C    . VAL   B 1 35  ? 45.802 -17.790 -5.654  1.00 9.65  ?  35  VAL   B C    1 
ATOM   4564 O  O    . VAL   B 1 35  ? 46.023 -16.867 -4.862  1.00 9.97  ?  35  VAL   B O    1 
ATOM   4565 C  CB   . VAL   B 1 35  ? 47.825 -18.172 -7.154  1.00 10.74 ?  35  VAL   B CB   1 
ATOM   4566 C  CG1  . VAL   B 1 35  ? 48.724 -17.353 -6.238  1.00 11.37 ?  35  VAL   B CG1  1 
ATOM   4567 C  CG2  . VAL   B 1 35  ? 47.962 -19.670 -6.848  1.00 11.42 ?  35  VAL   B CG2  1 
ATOM   4568 H  H    . VAL   B 1 35  ? 46.600 -15.792 -7.219  1.00 12.38 ?  35  VAL   B H    1 
ATOM   4569 H  HA   . VAL   B 1 35  ? 45.827 -18.363 -7.598  1.00 12.13 ?  35  VAL   B HA   1 
ATOM   4570 H  HB   . VAL   B 1 35  ? 48.134 -18.046 -8.065  1.00 12.87 ?  35  VAL   B HB   1 
ATOM   4571 H  HG11 . VAL   B 1 35  ? 49.646 -17.588 -6.424  1.00 13.63 ?  35  VAL   B HG11 1 
ATOM   4572 H  HG12 . VAL   B 1 35  ? 48.567 -16.422 -6.410  1.00 13.63 ?  35  VAL   B HG12 1 
ATOM   4573 H  HG13 . VAL   B 1 35  ? 48.506 -17.574 -5.317  1.00 13.63 ?  35  VAL   B HG13 1 
ATOM   4574 H  HG21 . VAL   B 1 35  ? 48.887 -19.940 -6.947  1.00 13.69 ?  35  VAL   B HG21 1 
ATOM   4575 H  HG22 . VAL   B 1 35  ? 47.667 -19.840 -5.934  1.00 13.69 ?  35  VAL   B HG22 1 
ATOM   4576 H  HG23 . VAL   B 1 35  ? 47.404 -20.180 -7.463  1.00 13.69 ?  35  VAL   B HG23 1 
ATOM   4577 N  N    . VAL   B 1 36  ? 45.081 -18.864 -5.340  1.00 9.89  ?  36  VAL   B N    1 
ATOM   4578 C  CA   . VAL   B 1 36  ? 44.532 -19.075 -4.008  1.00 9.71  ?  36  VAL   B CA   1 
ATOM   4579 C  C    . VAL   B 1 36  ? 45.536 -19.839 -3.155  1.00 9.44  ?  36  VAL   B C    1 
ATOM   4580 O  O    . VAL   B 1 36  ? 46.075 -20.874 -3.571  1.00 10.08 ?  36  VAL   B O    1 
ATOM   4581 C  CB   . VAL   B 1 36  ? 43.191 -19.825 -4.083  1.00 9.79  ?  36  VAL   B CB   1 
ATOM   4582 C  CG1  . VAL   B 1 36  ? 42.684 -20.190 -2.686  1.00 10.47 ?  36  VAL   B CG1  1 
ATOM   4583 C  CG2  . VAL   B 1 36  ? 42.166 -18.999 -4.837  1.00 10.58 ?  36  VAL   B CG2  1 
ATOM   4584 H  H    . VAL   B 1 36  ? 44.908 -19.506 -5.890  1.00 11.86 ?  36  VAL   B H    1 
ATOM   4585 H  HA   . VAL   B 1 36  ? 44.371 -18.221 -3.590  1.00 11.64 ?  36  VAL   B HA   1 
ATOM   4586 H  HB   . VAL   B 1 36  ? 43.320 -20.654 -4.576  1.00 11.74 ?  36  VAL   B HB   1 
ATOM   4587 H  HG11 . VAL   B 1 36  ? 41.746 -20.423 -2.744  1.00 12.56 ?  36  VAL   B HG11 1 
ATOM   4588 H  HG12 . VAL   B 1 36  ? 43.194 -20.940 -2.350  1.00 12.56 ?  36  VAL   B HG12 1 
ATOM   4589 H  HG13 . VAL   B 1 36  ? 42.798 -19.420 -2.105  1.00 12.56 ?  36  VAL   B HG13 1 
ATOM   4590 H  HG21 . VAL   B 1 36  ? 41.324 -19.481 -4.856  1.00 12.68 ?  36  VAL   B HG21 1 
ATOM   4591 H  HG22 . VAL   B 1 36  ? 42.055 -18.150 -4.388  1.00 12.68 ?  36  VAL   B HG22 1 
ATOM   4592 H  HG23 . VAL   B 1 36  ? 42.483 -18.856 -5.746  1.00 12.68 ?  36  VAL   B HG23 1 
ATOM   4593 N  N    . ASN   B 1 37  ? 45.762 -19.337 -1.942  1.00 9.39  ?  37  ASN   B N    1 
ATOM   4594 C  CA   . ASN   B 1 37  ? 46.505 -20.059 -0.924  1.00 9.85  ?  37  ASN   B CA   1 
ATOM   4595 C  C    . ASN   B 1 37  ? 45.544 -20.730 0.052   1.00 10.05 ?  37  ASN   B C    1 
ATOM   4596 O  O    . ASN   B 1 37  ? 44.535 -20.145 0.467   1.00 10.47 ?  37  ASN   B O    1 
ATOM   4597 C  CB   . ASN   B 1 37  ? 47.423 -19.116 -0.152  1.00 9.96  ?  37  ASN   B CB   1 
ATOM   4598 C  CG   . ASN   B 1 37  ? 48.273 -19.835 0.858   1.00 10.07 ?  37  ASN   B CG   1 
ATOM   4599 O  OD1  . ASN   B 1 37  ? 48.603 -21.009 0.685   1.00 10.67 ?  37  ASN   B OD1  1 
ATOM   4600 N  ND2  . ASN   B 1 37  ? 48.632 -19.137 1.929   1.00 10.38 ?  37  ASN   B ND2  1 
ATOM   4601 H  H    . ASN   B 1 37  ? 45.491 -18.565 -1.683  1.00 11.26 ?  37  ASN   B H    1 
ATOM   4602 H  HA   . ASN   B 1 37  ? 47.045 -20.751 -1.337  1.00 11.81 ?  37  ASN   B HA   1 
ATOM   4603 H  HB2  . ASN   B 1 37  ? 48.017 -18.681 -0.777  1.00 11.94 ?  37  ASN   B HB2  1 
ATOM   4604 H  HB3  . ASN   B 1 37  ? 46.885 -18.463 0.317   1.00 11.94 ?  37  ASN   B HB3  1 
ATOM   4605 H  HD21 . ASN   B 1 37  ? 49.130 -19.498 2.529   1.00 12.45 ?  37  ASN   B HD21 1 
ATOM   4606 H  HD22 . ASN   B 1 37  ? 48.393 -18.321 2.010   1.00 12.45 ?  37  ASN   B HD22 1 
ATOM   4607 N  N    . ALA   B 1 38  ? 45.888 -21.967 0.426   1.00 10.25 ?  38  ALA   B N    1 
ATOM   4608 C  CA   . ALA   B 1 38  ? 45.235 -22.709 1.507   1.00 10.73 ?  38  ALA   B CA   1 
ATOM   4609 C  C    . ALA   B 1 38  ? 45.824 -22.219 2.832   1.00 10.52 ?  38  ALA   B C    1 
ATOM   4610 O  O    . ALA   B 1 38  ? 46.720 -22.834 3.425   1.00 11.13 ?  38  ALA   B O    1 
ATOM   4611 C  CB   . ALA   B 1 38  ? 45.450 -24.206 1.319   1.00 11.94 ?  38  ALA   B CB   1 
ATOM   4612 H  H    . ALA   B 1 38  ? 46.533 -22.409 0.066   1.00 12.29 ?  38  ALA   B H    1 
ATOM   4613 H  HA   . ALA   B 1 38  ? 44.286 -22.526 1.503   1.00 12.87 ?  38  ALA   B HA   1 
ATOM   4614 H  HB1  . ALA   B 1 38  ? 45.006 -24.682 2.046   1.00 14.31 ?  38  ALA   B HB1  1 
ATOM   4615 H  HB2  . ALA   B 1 38  ? 45.062 -24.475 0.472   1.00 14.31 ?  38  ALA   B HB2  1 
ATOM   4616 H  HB3  . ALA   B 1 38  ? 46.396 -24.399 1.331   1.00 14.31 ?  38  ALA   B HB3  1 
ATOM   4617 N  N    . ALA   B 1 39  ? 45.305 -21.080 3.293   1.00 10.16 ?  39  ALA   B N    1 
ATOM   4618 C  CA   . ALA   B 1 39  ? 45.855 -20.347 4.423   1.00 10.50 ?  39  ALA   B CA   1 
ATOM   4619 C  C    . ALA   B 1 39  ? 45.241 -20.797 5.749   1.00 10.48 ?  39  ALA   B C    1 
ATOM   4620 O  O    . ALA   B 1 39  ? 44.206 -21.465 5.801   1.00 11.42 ?  39  ALA   B O    1 
ATOM   4621 C  CB   . ALA   B 1 39  ? 45.630 -18.845 4.231   1.00 10.95 ?  39  ALA   B CB   1 
ATOM   4622 H  H    . ALA   B 1 39  ? 44.609 -20.706 2.949   1.00 12.19 ?  39  ALA   B H    1 
ATOM   4623 H  HA   . ALA   B 1 39  ? 46.810 -20.506 4.464   1.00 12.59 ?  39  ALA   B HA   1 
ATOM   4624 H  HB1  . ALA   B 1 39  ? 46.006 -18.371 4.988   1.00 13.13 ?  39  ALA   B HB1  1 
ATOM   4625 H  HB2  . ALA   B 1 39  ? 46.073 -18.561 3.412   1.00 13.13 ?  39  ALA   B HB2  1 
ATOM   4626 H  HB3  . ALA   B 1 39  ? 44.679 -18.671 4.167   1.00 13.13 ?  39  ALA   B HB3  1 
ATOM   4627 N  N    . ASN   B 1 40  ? 45.887 -20.378 6.835   1.00 11.30 ?  40  ASN   B N    1 
ATOM   4628 C  CA   . ASN   B 1 40  ? 45.331 -20.421 8.178   1.00 12.07 ?  40  ASN   B CA   1 
ATOM   4629 C  C    . ASN   B 1 40  ? 45.145 -18.990 8.695   1.00 11.53 ?  40  ASN   B C    1 
ATOM   4630 O  O    . ASN   B 1 40  ? 45.553 -18.013 8.058   1.00 11.32 ?  40  ASN   B O    1 
ATOM   4631 C  CB   . ASN   B 1 40  ? 46.186 -21.298 9.107   1.00 12.73 ?  40  ASN   B CB   1 
ATOM   4632 C  CG   . ASN   B 1 40  ? 47.636 -20.887 9.129   1.00 13.71 ?  40  ASN   B CG   1 
ATOM   4633 O  OD1  . ASN   B 1 40  ? 47.943 -19.704 9.186   1.00 15.85 ?  40  ASN   B OD1  1 
ATOM   4634 N  ND2  . ASN   B 1 40  ? 48.537 -21.855 9.074   1.00 13.92 ?  40  ASN   B ND2  1 
ATOM   4635 H  H    . ASN   B 1 40  ? 46.682 -20.046 6.811   1.00 13.55 ?  40  ASN   B H    1 
ATOM   4636 H  HA   . ASN   B 1 40  ? 44.452 -20.824 8.133   1.00 14.47 ?  40  ASN   B HA   1 
ATOM   4637 H  HB2  . ASN   B 1 40  ? 45.843 -21.227 10.011  1.00 15.26 ?  40  ASN   B HB2  1 
ATOM   4638 H  HB3  . ASN   B 1 40  ? 46.141 -22.216 8.804   1.00 15.26 ?  40  ASN   B HB3  1 
ATOM   4639 H  HD21 . ASN   B 1 40  ? 49.379 -21.669 9.087   1.00 16.70 ?  40  ASN   B HD21 1 
ATOM   4640 H  HD22 . ASN   B 1 40  ? 48.283 -22.675 9.031   1.00 16.70 ?  40  ASN   B HD22 1 
ATOM   4641 N  N    . VAL   B 1 41  ? 44.478 -18.860 9.846   1.00 12.02 ?  41  VAL   B N    1 
ATOM   4642 C  CA   . VAL   B 1 41  ? 44.029 -17.537 10.292  1.00 12.57 ?  41  VAL   B CA   1 
ATOM   4643 C  C    . VAL   B 1 41  ? 45.182 -16.582 10.582  1.00 12.10 ?  41  VAL   B C    1 
ATOM   4644 O  O    . VAL   B 1 41  ? 45.004 -15.360 10.505  1.00 12.58 ?  41  VAL   B O    1 
ATOM   4645 C  CB   . VAL   B 1 41  ? 43.061 -17.615 11.491  1.00 14.31 ?  41  VAL   B CB   1 
ATOM   4646 C  CG1  . VAL   B 1 41  ? 41.749 -18.274 11.091  1.00 14.61 ?  41  VAL   B CG1  1 
ATOM   4647 C  CG2  . VAL   B 1 41  ? 43.712 -18.326 12.667  1.00 15.21 ?  41  VAL   B CG2  1 
ATOM   4648 H  H    . VAL   B 1 41  ? 44.274 -19.506 10.368  1.00 14.41 ?  41  VAL   B H    1 
ATOM   4649 H  HA   . VAL   B 1 41  ? 43.521 -17.144 9.567   1.00 15.07 ?  41  VAL   B HA   1 
ATOM   4650 H  HB   . VAL   B 1 41  ? 42.853 -16.714 11.780  1.00 17.16 ?  41  VAL   B HB   1 
ATOM   4651 H  HG11 . VAL   B 1 41  ? 41.149 -18.282 11.855  1.00 17.53 ?  41  VAL   B HG11 1 
ATOM   4652 H  HG12 . VAL   B 1 41  ? 41.351 -17.773 10.363  1.00 17.53 ?  41  VAL   B HG12 1 
ATOM   4653 H  HG13 . VAL   B 1 41  ? 41.927 -19.186 10.805  1.00 17.53 ?  41  VAL   B HG13 1 
ATOM   4654 H  HG21 . VAL   B 1 41  ? 43.096 -18.336 13.414  1.00 18.24 ?  41  VAL   B HG21 1 
ATOM   4655 H  HG22 . VAL   B 1 41  ? 43.924 -19.241 12.406  1.00 18.24 ?  41  VAL   B HG22 1 
ATOM   4656 H  HG23 . VAL   B 1 41  ? 44.524 -17.860 12.911  1.00 18.24 ?  41  VAL   B HG23 1 
ATOM   4657 N  N    . TYR   B 1 42  ? 46.352 -17.099 10.966  1.00 12.46 ?  42  TYR   B N    1 
ATOM   4658 C  CA   . TYR   B 1 42  ? 47.510 -16.252 11.235  1.00 12.71 ?  42  TYR   B CA   1 
ATOM   4659 C  C    . TYR   B 1 42  ? 48.472 -16.177 10.054  1.00 12.09 ?  42  TYR   B C    1 
ATOM   4660 O  O    . TYR   B 1 42  ? 49.559 -15.599 10.185  1.00 13.29 ?  42  TYR   B O    1 
ATOM   4661 C  CB   . TYR   B 1 42  ? 48.214 -16.655 12.538  1.00 14.34 ?  42  TYR   B CB   1 
ATOM   4662 C  CG   . TYR   B 1 42  ? 47.623 -15.963 13.763  1.00 14.86 ?  42  TYR   B CG   1 
ATOM   4663 C  CD1  . TYR   B 1 42  ? 47.837 -14.603 13.983  1.00 14.04 ?  42  TYR   B CD1  1 
ATOM   4664 C  CD2  . TYR   B 1 42  ? 46.841 -16.651 14.680  1.00 16.85 ?  42  TYR   B CD2  1 
ATOM   4665 C  CE1  . TYR   B 1 42  ? 47.304 -13.955 15.078  1.00 15.39 ?  42  TYR   B CE1  1 
ATOM   4666 C  CE2  . TYR   B 1 42  ? 46.304 -16.008 15.789  1.00 17.02 ?  42  TYR   B CE2  1 
ATOM   4667 C  CZ   . TYR   B 1 42  ? 46.539 -14.655 15.980  1.00 17.16 ?  42  TYR   B CZ   1 
ATOM   4668 O  OH   . TYR   B 1 42  ? 46.022 -14.000 17.080  1.00 19.55 ?  42  TYR   B OH   1 
ATOM   4669 H  H    . TYR   B 1 42  ? 46.497 -17.943 11.071  1.00 14.94 ?  42  TYR   B H    1 
ATOM   4670 H  HA   . TYR   B 1 42  ? 47.179 -15.352 11.371  1.00 15.24 ?  42  TYR   B HA   1 
ATOM   4671 H  HB2  . TYR   B 1 42  ? 48.126 -17.611 12.663  1.00 17.20 ?  42  TYR   B HB2  1 
ATOM   4672 H  HB3  . TYR   B 1 42  ? 49.151 -16.410 12.476  1.00 17.20 ?  42  TYR   B HB3  1 
ATOM   4673 H  HD1  . TYR   B 1 42  ? 48.361 -14.121 13.373  1.00 16.83 ?  42  TYR   B HD1  1 
ATOM   4674 H  HD2  . TYR   B 1 42  ? 46.678 -17.558 14.550  1.00 20.20 ?  42  TYR   B HD2  1 
ATOM   4675 H  HE1  . TYR   B 1 42  ? 47.470 -13.049 15.206  1.00 18.46 ?  42  TYR   B HE1  1 
ATOM   4676 H  HE2  . TYR   B 1 42  ? 45.783 -16.484 16.391  1.00 20.41 ?  42  TYR   B HE2  1 
ATOM   4677 H  HH   . TYR   B 1 42  ? 46.243 -13.197 17.057  1.00 23.45 ?  42  TYR   B HH   1 
ATOM   4678 N  N    . LEU   B 1 43  ? 48.070 -16.695 8.895   1.00 11.24 ?  43  LEU   B N    1 
ATOM   4679 C  CA   . LEU   B 1 43  ? 48.884 -16.633 7.685   1.00 11.11 ?  43  LEU   B CA   1 
ATOM   4680 C  C    . LEU   B 1 43  ? 50.297 -17.143 7.946   1.00 11.54 ?  43  LEU   B C    1 
ATOM   4681 O  O    . LEU   B 1 43  ? 51.280 -16.545 7.505   1.00 12.31 ?  43  LEU   B O    1 
ATOM   4682 C  CB   . LEU   B 1 43  ? 48.908 -15.229 7.072   1.00 11.07 ?  43  LEU   B CB   1 
ATOM   4683 C  CG   . LEU   B 1 43  ? 47.550 -14.616 6.715   1.00 11.63 ?  43  LEU   B CG   1 
ATOM   4684 C  CD1  . LEU   B 1 43  ? 47.761 -13.224 6.135   1.00 12.76 ?  43  LEU   B CD1  1 
ATOM   4685 C  CD2  . LEU   B 1 43  ? 46.774 -15.500 5.755   1.00 11.76 ?  43  LEU   B CD2  1 
ATOM   4686 H  H    . LEU   B 1 43  ? 47.320 -17.104 8.786   1.00 13.47 ?  43  LEU   B H    1 
ATOM   4687 H  HA   . LEU   B 1 43  ? 48.481 -17.226 7.026   1.00 13.32 ?  43  LEU   B HA   1 
ATOM   4688 H  HB2  . LEU   B 1 43  ? 49.337 -14.635 7.700   1.00 13.28 ?  43  LEU   B HB2  1 
ATOM   4689 H  HB3  . LEU   B 1 43  ? 49.427 -15.271 6.254   1.00 13.28 ?  43  LEU   B HB3  1 
ATOM   4690 H  HG   . LEU   B 1 43  ? 47.023 -14.526 7.522   1.00 13.95 ?  43  LEU   B HG   1 
ATOM   4691 H  HD11 . LEU   B 1 43  ? 46.895 -12.839 5.912   1.00 15.30 ?  43  LEU   B HD11 1 
ATOM   4692 H  HD12 . LEU   B 1 43  ? 48.203 -12.670 6.797   1.00 15.30 ?  43  LEU   B HD12 1 
ATOM   4693 H  HD13 . LEU   B 1 43  ? 48.306 -13.289 5.338   1.00 15.30 ?  43  LEU   B HD13 1 
ATOM   4694 H  HD21 . LEU   B 1 43  ? 45.976 -15.035 5.467   1.00 14.10 ?  43  LEU   B HD21 1 
ATOM   4695 H  HD22 . LEU   B 1 43  ? 47.334 -15.706 4.990   1.00 14.10 ?  43  LEU   B HD22 1 
ATOM   4696 H  HD23 . LEU   B 1 43  ? 46.529 -16.324 6.213   1.00 14.10 ?  43  LEU   B HD23 1 
ATOM   4697 N  N    . LYS   B 1 44  ? 50.397 -18.265 8.666   1.00 11.57 ?  44  LYS   B N    1 
ATOM   4698 C  CA   . LYS   B 1 44  ? 51.664 -18.941 8.909   1.00 12.14 ?  44  LYS   B CA   1 
ATOM   4699 C  C    . LYS   B 1 44  ? 51.781 -20.057 7.880   1.00 11.87 ?  44  LYS   B C    1 
ATOM   4700 O  O    . LYS   B 1 44  ? 51.081 -21.072 7.963   1.00 12.90 ?  44  LYS   B O    1 
ATOM   4701 C  CB   . LYS   B 1 44  ? 51.718 -19.460 10.344  1.00 14.04 ?  44  LYS   B CB   1 
ATOM   4702 C  CG   . LYS   B 1 44  ? 51.935 -18.352 11.373  1.00 17.03 ?  44  LYS   B CG   1 
ATOM   4703 C  CD   . LYS   B 1 44  ? 53.100 -17.457 10.943  1.00 20.46 ?  44  LYS   B CD   1 
ATOM   4704 C  CE   . LYS   B 1 44  ? 53.739 -16.707 12.086  1.00 23.57 ?  44  LYS   B CE   1 
ATOM   4705 N  NZ   . LYS   B 1 44  ? 54.788 -15.769 11.635  1.00 24.97 ?  44  LYS   B NZ   1 
ATOM   4706 H  H    . LYS   B 1 44  ? 49.721 -18.645 9.047   1.00 13.87 ?  44  LYS   B H    1 
ATOM   4707 H  HA   . LYS   B 1 44  ? 52.390 -18.326 8.747   1.00 14.56 ?  44  LYS   B HA   1 
ATOM   4708 H  HB2  . LYS   B 1 44  ? 50.874 -19.900 10.552  1.00 16.84 ?  44  LYS   B HB2  1 
ATOM   4709 H  HB3  . LYS   B 1 44  ? 52.445 -20.095 10.422  1.00 16.84 ?  44  LYS   B HB3  1 
ATOM   4710 H  HG2  . LYS   B 1 44  ? 51.136 -17.814 11.446  1.00 20.43 ?  44  LYS   B HG2  1 
ATOM   4711 H  HG3  . LYS   B 1 44  ? 52.158 -18.753 12.232  1.00 20.43 ?  44  LYS   B HG3  1 
ATOM   4712 H  HD2  . LYS   B 1 44  ? 53.777 -18.013 10.517  1.00 24.54 ?  44  LYS   B HD2  1 
ATOM   4713 H  HD3  . LYS   B 1 44  ? 52.764 -16.805 10.304  1.00 24.54 ?  44  LYS   B HD3  1 
ATOM   4714 H  HE2  . LYS   B 1 44  ? 53.068 -16.157 12.486  1.00 28.27 ?  44  LYS   B HE2  1 
ATOM   4715 H  HE3  . LYS   B 1 44  ? 54.112 -17.337 12.732  1.00 28.27 ?  44  LYS   B HE3  1 
ATOM   4716 H  HZ1  . LYS   B 1 44  ? 55.136 -15.346 12.336  1.00 29.95 ?  44  LYS   B HZ1  1 
ATOM   4717 H  HZ2  . LYS   B 1 44  ? 55.429 -16.205 11.207  1.00 29.95 ?  44  LYS   B HZ2  1 
ATOM   4718 H  HZ3  . LYS   B 1 44  ? 54.430 -15.163 11.084  1.00 29.95 ?  44  LYS   B HZ3  1 
ATOM   4719 N  N    . HIS   B 1 45  ? 52.635 -19.843 6.880   1.00 11.48 ?  45  HIS   B N    1 
ATOM   4720 C  CA   . HIS   B 1 45  ? 52.655 -20.676 5.677   1.00 11.94 ?  45  HIS   B CA   1 
ATOM   4721 C  C    . HIS   B 1 45  ? 53.667 -21.804 5.836   1.00 14.08 ?  45  HIS   B C    1 
ATOM   4722 O  O    . HIS   B 1 45  ? 54.734 -21.816 5.234   1.00 16.54 ?  45  HIS   B O    1 
ATOM   4723 C  CB   . HIS   B 1 45  ? 52.973 -19.821 4.461   1.00 11.62 ?  45  HIS   B CB   1 
ATOM   4724 C  CG   . HIS   B 1 45  ? 52.105 -18.618 4.350   1.00 11.42 ?  45  HIS   B CG   1 
ATOM   4725 N  ND1  . HIS   B 1 45  ? 50.728 -18.694 4.331   1.00 11.58 ?  45  HIS   B ND1  1 
ATOM   4726 C  CD2  . HIS   B 1 45  ? 52.425 -17.307 4.262   1.00 12.08 ?  45  HIS   B CD2  1 
ATOM   4727 C  CE1  . HIS   B 1 45  ? 50.244 -17.469 4.228   1.00 11.44 ?  45  HIS   B CE1  1 
ATOM   4728 N  NE2  . HIS   B 1 45  ? 51.248 -16.611 4.180   1.00 11.98 ?  45  HIS   B NE2  1 
ATOM   4729 H  H    . HIS   B 1 45  ? 53.203 -19.198 6.865   1.00 13.77 ?  45  HIS   B H    1 
ATOM   4730 H  HA   . HIS   B 1 45  ? 51.778 -21.072 5.544   1.00 14.32 ?  45  HIS   B HA   1 
ATOM   4731 H  HB2  . HIS   B 1 45  ? 53.895 -19.529 4.509   1.00 13.93 ?  45  HIS   B HB2  1 
ATOM   4732 H  HB3  . HIS   B 1 45  ? 52.845 -20.360 3.655   1.00 13.93 ?  45  HIS   B HB3  1 
ATOM   4733 H  HD2  . HIS   B 1 45  ? 53.285 -16.944 4.251   1.00 14.49 ?  45  HIS   B HD2  1 
ATOM   4734 H  HE1  . HIS   B 1 45  ? 49.341 -17.250 4.189   1.00 13.71 ?  45  HIS   B HE1  1 
ATOM   4735 H  HE2  . HIS   B 1 45  ? 51.173 -15.758 4.121   1.00 14.37 ?  45  HIS   B HE2  1 
ATOM   4736 N  N    A GLY   B 1 46  ? 53.285 -22.788 6.645   0.50 14.90 ?  46  GLY   B N    1 
ATOM   4737 N  N    B GLY   B 1 46  ? 53.294 -22.776 6.660   0.50 14.84 ?  46  GLY   B N    1 
ATOM   4738 C  CA   A GLY   B 1 46  ? 54.206 -23.840 7.034   0.50 16.56 ?  46  GLY   B CA   1 
ATOM   4739 C  CA   B GLY   B 1 46  ? 54.212 -23.841 7.013   0.50 16.37 ?  46  GLY   B CA   1 
ATOM   4740 C  C    A GLY   B 1 46  ? 54.242 -25.071 6.146   0.50 17.91 ?  46  GLY   B C    1 
ATOM   4741 C  C    B GLY   B 1 46  ? 54.230 -25.012 6.051   0.50 17.71 ?  46  GLY   B C    1 
ATOM   4742 O  O    A GLY   B 1 46  ? 55.320 -25.515 5.737   0.50 19.95 ?  46  GLY   B O    1 
ATOM   4743 O  O    B GLY   B 1 46  ? 55.274 -25.339 5.475   0.50 19.48 ?  46  GLY   B O    1 
ATOM   4744 H  H    A GLY   B 1 46  ? 52.499 -22.858 6.991   0.50 17.87 ?  46  GLY   B H    1 
ATOM   4745 H  H    B GLY   B 1 46  ? 52.519 -22.832 7.033   0.50 17.79 ?  46  GLY   B H    1 
ATOM   4746 H  HA2  A GLY   B 1 46  ? 55.101 -23.470 7.066   0.50 19.86 ?  46  GLY   B HA2  1 
ATOM   4747 H  HA2  B GLY   B 1 46  ? 55.110 -23.478 7.060   0.50 19.64 ?  46  GLY   B HA2  1 
ATOM   4748 H  HA3  A GLY   B 1 46  ? 53.975 -24.136 7.929   0.50 19.86 ?  46  GLY   B HA3  1 
ATOM   4749 H  HA3  B GLY   B 1 46  ? 53.979 -24.175 7.895   0.50 19.64 ?  46  GLY   B HA3  1 
ATOM   4750 N  N    . GLY   B 1 47  ? 53.079 -25.655 5.858   1.00 17.79 ?  47  GLY   B N    1 
ATOM   4751 C  CA   . GLY   B 1 47  ? 53.012 -26.925 5.165   1.00 15.91 ?  47  GLY   B CA   1 
ATOM   4752 C  C    . GLY   B 1 47  ? 52.120 -26.892 3.938   1.00 13.79 ?  47  GLY   B C    1 
ATOM   4753 O  O    . GLY   B 1 47  ? 51.489 -25.880 3.633   1.00 14.19 ?  47  GLY   B O    1 
ATOM   4754 H  H    A GLY   B 1 47  ? 52.308 -25.336 6.077   0.50 21.34 ?  47  GLY   B H    1 
ATOM   4755 H  H    B GLY   B 1 47  ? 52.313 -25.368 6.133   0.50 21.34 ?  47  GLY   B H    1 
ATOM   4756 H  HA2  . GLY   B 1 47  ? 53.896 -27.191 4.878   1.00 19.09 ?  47  GLY   B HA2  1 
ATOM   4757 H  HA3  . GLY   B 1 47  ? 52.672 -27.602 5.772   1.00 19.09 ?  47  GLY   B HA3  1 
ATOM   4758 N  N    . GLY   B 1 48  ? 52.066 -28.032 3.251   1.00 12.93 ?  48  GLY   B N    1 
ATOM   4759 C  CA   . GLY   B 1 48  ? 51.154 -28.173 2.130   1.00 12.54 ?  48  GLY   B CA   1 
ATOM   4760 C  C    . GLY   B 1 48  ? 51.294 -27.056 1.121   1.00 11.97 ?  48  GLY   B C    1 
ATOM   4761 O  O    . GLY   B 1 48  ? 52.401 -26.591 0.812   1.00 12.40 ?  48  GLY   B O    1 
ATOM   4762 H  H    . GLY   B 1 48  ? 52.545 -28.718 3.410   1.00 15.51 ?  48  GLY   B H    1 
ATOM   4763 H  HA2  . GLY   B 1 48  ? 51.328 -29.017 1.679   1.00 15.04 ?  48  GLY   B HA2  1 
ATOM   4764 H  HA3  . GLY   B 1 48  ? 50.239 -28.179 2.447   1.00 15.04 ?  48  GLY   B HA3  1 
ATOM   4765 N  N    . VAL   B 1 49  ? 50.151 -26.615 0.593   1.00 11.68 ?  49  VAL   B N    1 
ATOM   4766 C  CA   . VAL   B 1 49  ? 50.152 -25.587 -0.445  1.00 12.03 ?  49  VAL   B CA   1 
ATOM   4767 C  C    . VAL   B 1 49  ? 50.809 -24.301 0.050   1.00 11.06 ?  49  VAL   B C    1 
ATOM   4768 O  O    . VAL   B 1 49  ? 51.602 -23.678 -0.668  1.00 11.80 ?  49  VAL   B O    1 
ATOM   4769 C  CB   . VAL   B 1 49  ? 48.713 -25.332 -0.944  1.00 13.19 ?  49  VAL   B CB   1 
ATOM   4770 C  CG1  . VAL   B 1 49  ? 48.657 -24.087 -1.823  1.00 13.32 ?  49  VAL   B CG1  1 
ATOM   4771 C  CG2  . VAL   B 1 49  ? 48.182 -26.554 -1.688  1.00 14.53 ?  49  VAL   B CG2  1 
ATOM   4772 H  H    . VAL   B 1 49  ? 49.366 -26.882 0.821   1.00 14.00 ?  49  VAL   B H    1 
ATOM   4773 H  HA   . VAL   B 1 49  ? 50.668 -25.905 -1.201  1.00 14.42 ?  49  VAL   B HA   1 
ATOM   4774 H  HB   . VAL   B 1 49  ? 48.139 -25.180 -0.182  1.00 15.82 ?  49  VAL   B HB   1 
ATOM   4775 H  HG11 . VAL   B 1 49  ? 47.833 -24.104 -2.338  1.00 15.97 ?  49  VAL   B HG11 1 
ATOM   4776 H  HG12 . VAL   B 1 49  ? 48.674 -23.299 -1.259  1.00 15.97 ?  49  VAL   B HG12 1 
ATOM   4777 H  HG13 . VAL   B 1 49  ? 49.418 -24.086 -2.423  1.00 15.97 ?  49  VAL   B HG13 1 
ATOM   4778 H  HG21 . VAL   B 1 49  ? 47.280 -26.371 -1.995  1.00 17.42 ?  49  VAL   B HG21 1 
ATOM   4779 H  HG22 . VAL   B 1 49  ? 48.757 -26.737 -2.449  1.00 17.42 ?  49  VAL   B HG22 1 
ATOM   4780 H  HG23 . VAL   B 1 49  ? 48.180 -27.313 -1.086  1.00 17.42 ?  49  VAL   B HG23 1 
ATOM   4781 N  N    . ALA   B 1 50  ? 50.472 -23.865 1.266   1.00 10.88 ?  50  ALA   B N    1 
ATOM   4782 C  CA   . ALA   B 1 50  ? 50.993 -22.590 1.752   1.00 10.72 ?  50  ALA   B CA   1 
ATOM   4783 C  C    . ALA   B 1 50  ? 52.510 -22.620 1.854   1.00 10.83 ?  50  ALA   B C    1 
ATOM   4784 O  O    . ALA   B 1 50  ? 53.192 -21.648 1.492   1.00 10.85 ?  50  ALA   B O    1 
ATOM   4785 C  CB   . ALA   B 1 50  ? 50.366 -22.246 3.102   1.00 11.15 ?  50  ALA   B CB   1 
ATOM   4786 H  H    . ALA   B 1 50  ? 49.952 -24.278 1.813   1.00 13.04 ?  50  ALA   B H    1 
ATOM   4787 H  HA   . ALA   B 1 50  ? 50.764 -21.893 1.130   1.00 12.86 ?  50  ALA   B HA   1 
ATOM   4788 H  HB1  . ALA   B 1 50  ? 50.720 -21.401 3.414   1.00 13.36 ?  50  ALA   B HB1  1 
ATOM   4789 H  HB2  . ALA   B 1 50  ? 49.400 -22.177 2.990   1.00 13.36 ?  50  ALA   B HB2  1 
ATOM   4790 H  HB3  . ALA   B 1 50  ? 50.569 -22.949 3.741   1.00 13.36 ?  50  ALA   B HB3  1 
ATOM   4791 N  N    . GLY   B 1 51  ? 53.059 -23.721 2.359   1.00 11.55 ?  51  GLY   B N    1 
ATOM   4792 C  CA   . GLY   B 1 51  ? 54.504 -23.825 2.438   1.00 12.47 ?  51  GLY   B CA   1 
ATOM   4793 C  C    . GLY   B 1 51  ? 55.151 -23.776 1.070   1.00 12.23 ?  51  GLY   B C    1 
ATOM   4794 O  O    . GLY   B 1 51  ? 56.199 -23.151 0.891   1.00 12.83 ?  51  GLY   B O    1 
ATOM   4795 H  H    . GLY   B 1 51  ? 52.634 -24.417 2.646   1.00 13.85 ?  51  GLY   B H    1 
ATOM   4796 H  HA2  . GLY   B 1 51  ? 54.855 -23.092 2.969   1.00 14.95 ?  51  GLY   B HA2  1 
ATOM   4797 H  HA3  . GLY   B 1 51  ? 54.754 -24.661 2.869   1.00 14.95 ?  51  GLY   B HA3  1 
ATOM   4798 N  N    . ALA   B 1 52  ? 54.541 -24.433 0.086   1.00 11.82 ?  52  ALA   B N    1 
ATOM   4799 C  CA   . ALA   B 1 52  ? 55.104 -24.444 -1.257  1.00 11.97 ?  52  ALA   B CA   1 
ATOM   4800 C  C    . ALA   B 1 52  ? 55.036 -23.066 -1.906  1.00 11.51 ?  52  ALA   B C    1 
ATOM   4801 O  O    . ALA   B 1 52  ? 56.007 -22.625 -2.536  1.00 12.22 ?  52  ALA   B O    1 
ATOM   4802 C  CB   . ALA   B 1 52  ? 54.378 -25.473 -2.114  1.00 12.64 ?  52  ALA   B CB   1 
ATOM   4803 H  H    . ALA   B 1 52  ? 53.796 -24.861 0.168   1.00 14.17 ?  52  ALA   B H    1 
ATOM   4804 H  HA   . ALA   B 1 52  ? 56.035 -24.701 -1.201  1.00 14.35 ?  52  ALA   B HA   1 
ATOM   4805 H  HB1  . ALA   B 1 52  ? 54.770 -25.471 -3.003  1.00 15.15 ?  52  ALA   B HB1  1 
ATOM   4806 H  HB2  . ALA   B 1 52  ? 54.488 -26.349 -1.709  1.00 15.15 ?  52  ALA   B HB2  1 
ATOM   4807 H  HB3  . ALA   B 1 52  ? 53.441 -25.243 -2.162  1.00 15.15 ?  52  ALA   B HB3  1 
ATOM   4808 N  N    . LEU   B 1 53  ? 53.893 -22.383 -1.788  1.00 11.27 ?  53  LEU   B N    1 
ATOM   4809 C  CA   . LEU   B 1 53  ? 53.791 -21.043 -2.354  1.00 11.26 ?  53  LEU   B CA   1 
ATOM   4810 C  C    . LEU   B 1 53  ? 54.803 -20.111 -1.701  1.00 11.40 ?  53  LEU   B C    1 
ATOM   4811 O  O    . LEU   B 1 53  ? 55.508 -19.358 -2.384  1.00 12.00 ?  53  LEU   B O    1 
ATOM   4812 C  CB   . LEU   B 1 53  ? 52.370 -20.495 -2.184  1.00 11.47 ?  53  LEU   B CB   1 
ATOM   4813 C  CG   . LEU   B 1 53  ? 51.231 -21.213 -2.919  1.00 12.21 ?  53  LEU   B CG   1 
ATOM   4814 C  CD1  . LEU   B 1 53  ? 49.899 -20.582 -2.565  1.00 13.25 ?  53  LEU   B CD1  1 
ATOM   4815 C  CD2  . LEU   B 1 53  ? 51.437 -21.192 -4.430  1.00 13.98 ?  53  LEU   B CD2  1 
ATOM   4816 H  H    . LEU   B 1 53  ? 53.188 -22.663 -1.391  1.00 13.52 ?  53  LEU   B H    1 
ATOM   4817 H  HA   . LEU   B 1 53  ? 53.992 -21.085 -3.306  1.00 13.50 ?  53  LEU   B HA   1 
ATOM   4818 H  HB2  . LEU   B 1 53  ? 52.156 -20.521 -1.241  1.00 13.75 ?  53  LEU   B HB2  1 
ATOM   4819 H  HB3  . LEU   B 1 53  ? 52.366 -19.579 -2.490  1.00 13.75 ?  53  LEU   B HB3  1 
ATOM   4820 H  HG   . LEU   B 1 53  ? 51.200 -22.140 -2.633  1.00 14.64 ?  53  LEU   B HG   1 
ATOM   4821 H  HD11 . LEU   B 1 53  ? 49.188 -21.049 -3.036  1.00 15.89 ?  53  LEU   B HD11 1 
ATOM   4822 H  HD12 . LEU   B 1 53  ? 49.756 -20.654 -1.606  1.00 15.89 ?  53  LEU   B HD12 1 
ATOM   4823 H  HD13 . LEU   B 1 53  ? 49.908 -19.649 -2.826  1.00 15.89 ?  53  LEU   B HD13 1 
ATOM   4824 H  HD21 . LEU   B 1 53  ? 50.738 -21.709 -4.854  1.00 16.77 ?  53  LEU   B HD21 1 
ATOM   4825 H  HD22 . LEU   B 1 53  ? 51.400 -20.272 -4.740  1.00 16.77 ?  53  LEU   B HD22 1 
ATOM   4826 H  HD23 . LEU   B 1 53  ? 52.304 -21.576 -4.638  1.00 16.77 ?  53  LEU   B HD23 1 
ATOM   4827 N  N    . ASN   B 1 54  ? 54.885 -20.136 -0.375  1.00 11.00 ?  54  ASN   B N    1 
ATOM   4828 C  CA   . ASN   B 1 54  ? 55.802 -19.227 0.296   1.00 11.54 ?  54  ASN   B CA   1 
ATOM   4829 C  C    . ASN   B 1 54  ? 57.248 -19.514 -0.098  1.00 12.14 ?  54  ASN   B C    1 
ATOM   4830 O  O    . ASN   B 1 54  ? 58.028 -18.583 -0.334  1.00 12.25 ?  54  ASN   B O    1 
ATOM   4831 C  CB   . ASN   B 1 54  ? 55.636 -19.300 1.808   1.00 12.37 ?  54  ASN   B CB   1 
ATOM   4832 C  CG   . ASN   B 1 54  ? 56.608 -18.383 2.520   1.00 12.29 ?  54  ASN   B CG   1 
ATOM   4833 O  OD1  . ASN   B 1 54  ? 56.625 -17.180 2.273   1.00 12.37 ?  54  ASN   B OD1  1 
ATOM   4834 N  ND2  . ASN   B 1 54  ? 57.442 -18.950 3.387   1.00 14.07 ?  54  ASN   B ND2  1 
ATOM   4835 H  H    . ASN   B 1 54  ? 54.441 -20.654 0.139   1.00 13.19 ?  54  ASN   B H    1 
ATOM   4836 H  HA   . ASN   B 1 54  ? 55.600 -18.320 0.017   1.00 13.84 ?  54  ASN   B HA   1 
ATOM   4837 H  HB2  . ASN   B 1 54  ? 54.733 -19.022 2.040   1.00 14.83 ?  54  ASN   B HB2  1 
ATOM   4838 H  HB3  . ASN   B 1 54  ? 55.796 -20.204 2.106   1.00 14.83 ?  54  ASN   B HB3  1 
ATOM   4839 H  HD21 . ASN   B 1 54  ? 58.017 -18.467 3.811   1.00 16.87 ?  54  ASN   B HD21 1 
ATOM   4840 H  HD22 . ASN   B 1 54  ? 57.410 -19.797 3.528   1.00 16.87 ?  54  ASN   B HD22 1 
ATOM   4841 N  N    . LYS   B 1 55  ? 57.628 -20.795 -0.163  1.00 12.44 ?  55  LYS   B N    1 
ATOM   4842 C  CA   . LYS   B 1 55  ? 58.983 -21.144 -0.580  1.00 13.57 ?  55  LYS   B CA   1 
ATOM   4843 C  C    . LYS   B 1 55  ? 59.283 -20.600 -1.971  1.00 13.60 ?  55  LYS   B C    1 
ATOM   4844 O  O    . LYS   B 1 55  ? 60.385 -20.099 -2.224  1.00 14.07 ?  55  LYS   B O    1 
ATOM   4845 C  CB   . LYS   B 1 55  ? 59.163 -22.663 -0.537  1.00 15.35 ?  55  LYS   B CB   1 
ATOM   4846 C  CG   . LYS   B 1 55  ? 60.536 -23.129 -0.972  1.00 19.65 ?  55  LYS   B CG   1 
ATOM   4847 C  CD   . LYS   B 1 55  ? 60.701 -24.630 -0.805  1.00 23.08 ?  55  LYS   B CD   1 
ATOM   4848 C  CE   . LYS   B 1 55  ? 60.712 -25.041 0.665   1.00 25.82 ?  55  LYS   B CE   1 
ATOM   4849 N  NZ   . LYS   B 1 55  ? 61.100 -26.459 0.848   1.00 27.55 ?  55  LYS   B NZ   1 
ATOM   4850 H  H    . LYS   B 1 55  ? 57.125 -21.464 0.030   1.00 14.92 ?  55  LYS   B H    1 
ATOM   4851 H  HA   . LYS   B 1 55  ? 59.616 -20.747 0.037   1.00 16.27 ?  55  LYS   B HA   1 
ATOM   4852 H  HB2  . LYS   B 1 55  ? 59.015 -22.959 0.376   1.00 18.41 ?  55  LYS   B HB2  1 
ATOM   4853 H  HB3  . LYS   B 1 55  ? 58.507 -23.070 -1.124  1.00 18.41 ?  55  LYS   B HB3  1 
ATOM   4854 H  HG2  . LYS   B 1 55  ? 60.662 -22.909 -1.909  1.00 23.57 ?  55  LYS   B HG2  1 
ATOM   4855 H  HG3  . LYS   B 1 55  ? 61.206 -22.681 -0.431  1.00 23.57 ?  55  LYS   B HG3  1 
ATOM   4856 H  HD2  . LYS   B 1 55  ? 59.961 -25.083 -1.241  1.00 27.68 ?  55  LYS   B HD2  1 
ATOM   4857 H  HD3  . LYS   B 1 55  ? 61.542 -24.903 -1.202  1.00 27.68 ?  55  LYS   B HD3  1 
ATOM   4858 H  HE2  . LYS   B 1 55  ? 61.347 -24.480 1.143   1.00 30.97 ?  55  LYS   B HE2  1 
ATOM   4859 H  HE3  . LYS   B 1 55  ? 59.821 -24.917 1.034   1.00 30.97 ?  55  LYS   B HE3  1 
ATOM   4860 H  HZ1  . LYS   B 1 55  ? 61.092 -26.664 1.714   1.00 33.04 ?  55  LYS   B HZ1  1 
ATOM   4861 H  HZ2  . LYS   B 1 55  ? 60.529 -26.987 0.419   1.00 33.04 ?  55  LYS   B HZ2  1 
ATOM   4862 H  HZ3  . LYS   B 1 55  ? 61.918 -26.592 0.527   1.00 33.04 ?  55  LYS   B HZ3  1 
ATOM   4863 N  N    . ALA   B 1 56  ? 58.310 -20.678 -2.886  1.00 13.23 ?  56  ALA   B N    1 
ATOM   4864 C  CA   . ALA   B 1 56  ? 58.536 -20.181 -4.239  1.00 13.85 ?  56  ALA   B CA   1 
ATOM   4865 C  C    . ALA   B 1 56  ? 58.818 -18.686 -4.239  1.00 13.31 ?  56  ALA   B C    1 
ATOM   4866 O  O    . ALA   B 1 56  ? 59.547 -18.186 -5.108  1.00 14.52 ?  56  ALA   B O    1 
ATOM   4867 C  CB   . ALA   B 1 56  ? 57.337 -20.510 -5.130  1.00 14.72 ?  56  ALA   B CB   1 
ATOM   4868 H  H    . ALA   B 1 56  ? 57.519 -21.001 -2.745  1.00 15.87 ?  56  ALA   B H    1 
ATOM   4869 H  HA   . ALA   B 1 56  ? 59.309 -20.625 -4.606  1.00 16.60 ?  56  ALA   B HA   1 
ATOM   4870 H  HB1  . ALA   B 1 56  ? 57.510 -20.177 -6.026  1.00 17.65 ?  56  ALA   B HB1  1 
ATOM   4871 H  HB2  . ALA   B 1 56  ? 57.217 -21.473 -5.155  1.00 17.65 ?  56  ALA   B HB2  1 
ATOM   4872 H  HB3  . ALA   B 1 56  ? 56.542 -20.088 -4.768  1.00 17.65 ?  56  ALA   B HB3  1 
ATOM   4873 N  N    . THR   B 1 57  ? 58.245 -17.954 -3.280  1.00 13.15 ?  57  THR   B N    1 
ATOM   4874 C  CA   . THR   B 1 57  ? 58.488 -16.519 -3.152  1.00 13.17 ?  57  THR   B CA   1 
ATOM   4875 C  C    . THR   B 1 57  ? 59.741 -16.195 -2.346  1.00 13.54 ?  57  THR   B C    1 
ATOM   4876 O  O    . THR   B 1 57  ? 59.979 -15.019 -2.051  1.00 14.05 ?  57  THR   B O    1 
ATOM   4877 C  CB   . THR   B 1 57  ? 57.292 -15.783 -2.519  1.00 12.45 ?  57  THR   B CB   1 
ATOM   4878 O  OG1  . THR   B 1 57  ? 57.262 -15.997 -1.100  1.00 12.17 ?  57  THR   B OG1  1 
ATOM   4879 C  CG2  . THR   B 1 57  ? 55.966 -16.201 -3.158  1.00 12.64 ?  57  THR   B CG2  1 
ATOM   4880 H  H    . THR   B 1 57  ? 57.692 -18.263 -2.691  1.00 15.77 ?  57  THR   B H    1 
ATOM   4881 H  HA   . THR   B 1 57  ? 58.611 -16.149 -4.042  1.00 15.80 ?  57  THR   B HA   1 
ATOM   4882 H  HB   . THR   B 1 57  ? 57.401 -14.830 -2.682  1.00 14.93 ?  57  THR   B HB   1 
ATOM   4883 H  HG1  . THR   B 1 57  ? 57.182 -16.819 -0.939  1.00 14.59 ?  57  THR   B HG1  1 
ATOM   4884 H  HG21 . THR   B 1 57  ? 55.244 -15.655 -2.817  1.00 15.16 ?  57  THR   B HG21 1 
ATOM   4885 H  HG22 . THR   B 1 57  ? 56.013 -16.094 -4.124  1.00 15.16 ?  57  THR   B HG22 1 
ATOM   4886 H  HG23 . THR   B 1 57  ? 55.780 -17.131 -2.959  1.00 15.16 ?  57  THR   B HG23 1 
ATOM   4887 N  N    . ASN   B 1 58  ? 60.535 -17.200 -1.981  1.00 14.64 ?  58  ASN   B N    1 
ATOM   4888 C  CA   . ASN   B 1 58  ? 61.732 -16.987 -1.170  1.00 17.37 ?  58  ASN   B CA   1 
ATOM   4889 C  C    . ASN   B 1 58  ? 61.396 -16.272 0.139   1.00 14.87 ?  58  ASN   B C    1 
ATOM   4890 O  O    . ASN   B 1 58  ? 62.135 -15.397 0.606   1.00 15.39 ?  58  ASN   B O    1 
ATOM   4891 C  CB   . ASN   B 1 58  ? 62.820 -16.239 -1.946  1.00 23.96 ?  58  ASN   B CB   1 
ATOM   4892 C  CG   . ASN   B 1 58  ? 64.190 -16.385 -1.313  1.00 31.35 ?  58  ASN   B CG   1 
ATOM   4893 O  OD1  . ASN   B 1 58  ? 64.525 -17.438 -0.770  1.00 34.55 ?  58  ASN   B OD1  1 
ATOM   4894 N  ND2  . ASN   B 1 58  ? 64.988 -15.325 -1.375  1.00 35.78 ?  58  ASN   B ND2  1 
ATOM   4895 H  H    . ASN   B 1 58  ? 60.398 -18.027 -2.187  1.00 17.56 ?  58  ASN   B H    1 
ATOM   4896 H  HA   . ASN   B 1 58  ? 62.098 -17.862 -0.949  1.00 20.83 ?  58  ASN   B HA   1 
ATOM   4897 H  HB2  . ASN   B 1 58  ? 62.869 -16.592 -2.851  1.00 28.74 ?  58  ASN   B HB2  1 
ATOM   4898 H  HB3  . ASN   B 1 58  ? 62.601 -15.297 -1.970  1.00 28.74 ?  58  ASN   B HB3  1 
ATOM   4899 H  HD21 . ASN   B 1 58  ? 65.776 -15.359 -1.030  1.00 42.93 ?  58  ASN   B HD21 1 
ATOM   4900 H  HD22 . ASN   B 1 58  ? 64.719 -14.605 -1.760  1.00 42.93 ?  58  ASN   B HD22 1 
ATOM   4901 N  N    . ASN   B 1 59  ? 60.268 -16.655 0.737   1.00 13.79 ?  59  ASN   B N    1 
ATOM   4902 C  CA   . ASN   B 1 59  ? 59.792 -16.186 2.036   1.00 13.68 ?  59  ASN   B CA   1 
ATOM   4903 C  C    . ASN   B 1 59  ? 59.196 -14.779 1.976   1.00 12.87 ?  59  ASN   B C    1 
ATOM   4904 O  O    . ASN   B 1 59  ? 58.772 -14.268 3.017   1.00 12.98 ?  59  ASN   B O    1 
ATOM   4905 C  CB   . ASN   B 1 59  ? 60.868 -16.254 3.136   1.00 14.77 ?  59  ASN   B CB   1 
ATOM   4906 C  CG   . ASN   B 1 59  ? 60.281 -16.402 4.518   1.00 15.22 ?  59  ASN   B CG   1 
ATOM   4907 O  OD1  . ASN   B 1 59  ? 59.440 -17.268 4.756   1.00 15.62 ?  59  ASN   B OD1  1 
ATOM   4908 N  ND2  . ASN   B 1 59  ? 60.714 -15.551 5.440   1.00 15.81 ?  59  ASN   B ND2  1 
ATOM   4909 H  H    . ASN   B 1 59  ? 59.727 -17.230 0.385   1.00 16.54 ?  59  ASN   B H    1 
ATOM   4910 H  HA   . ASN   B 1 59  ? 59.082 -16.787 2.319   1.00 16.40 ?  59  ASN   B HA   1 
ATOM   4911 H  HB2  . ASN   B 1 59  ? 61.442 -17.023 2.985   1.00 17.71 ?  59  ASN   B HB2  1 
ATOM   4912 H  HB3  . ASN   B 1 59  ? 61.391 -15.441 3.126   1.00 17.71 ?  59  ASN   B HB3  1 
ATOM   4913 H  HD21 . ASN   B 1 59  ? 60.409 -15.592 6.246   1.00 18.96 ?  59  ASN   B HD21 1 
ATOM   4914 H  HD22 . ASN   B 1 59  ? 61.303 -14.958 5.237   1.00 18.96 ?  59  ASN   B HD22 1 
ATOM   4915 N  N    . ALA   B 1 60  ? 59.132 -14.143 0.803   1.00 12.69 ?  60  ALA   B N    1 
ATOM   4916 C  CA   . ALA   B 1 60  ? 58.544 -12.808 0.729   1.00 12.96 ?  60  ALA   B CA   1 
ATOM   4917 C  C    . ALA   B 1 60  ? 57.073 -12.824 1.127   1.00 12.31 ?  60  ALA   B C    1 
ATOM   4918 O  O    . ALA   B 1 60  ? 56.571 -11.866 1.731   1.00 13.00 ?  60  ALA   B O    1 
ATOM   4919 C  CB   . ALA   B 1 60  ? 58.712 -12.231 -0.677  1.00 14.20 ?  60  ALA   B CB   1 
ATOM   4920 H  H    . ALA   B 1 60  ? 59.425 -14.464 0.057   1.00 15.22 ?  60  ALA   B H    1 
ATOM   4921 H  HA   . ALA   B 1 60  ? 59.017 -12.233 1.347   1.00 15.54 ?  60  ALA   B HA   1 
ATOM   4922 H  HB1  . ALA   B 1 60  ? 58.315 -11.350 -0.699  1.00 17.03 ?  60  ALA   B HB1  1 
ATOM   4923 H  HB2  . ALA   B 1 60  ? 59.657 -12.179 -0.887  1.00 17.03 ?  60  ALA   B HB2  1 
ATOM   4924 H  HB3  . ALA   B 1 60  ? 58.265 -12.816 -1.311  1.00 17.03 ?  60  ALA   B HB3  1 
ATOM   4925 N  N    . MET   B 1 61  ? 56.360 -13.898 0.776   1.00 11.91 ?  61  MET   B N    1 
ATOM   4926 C  CA   . MET   B 1 61  ? 54.965 -14.024 1.173   1.00 11.32 ?  61  MET   B CA   1 
ATOM   4927 C  C    . MET   B 1 61  ? 54.827 -14.024 2.693   1.00 11.33 ?  61  MET   B C    1 
ATOM   4928 O  O    . MET   B 1 61  ? 53.932 -13.364 3.239   1.00 11.17 ?  61  MET   B O    1 
ATOM   4929 C  CB   . MET   B 1 61  ? 54.380 -15.290 0.548   1.00 11.23 ?  61  MET   B CB   1 
ATOM   4930 C  CG   . MET   B 1 61  ? 52.944 -15.582 0.961   1.00 11.33 ?  61  MET   B CG   1 
ATOM   4931 S  SD   . MET   B 1 61  ? 52.295 -17.071 0.195   1.00 11.99 ?  61  MET   B SD   1 
ATOM   4932 C  CE   . MET   B 1 61  ? 52.046 -16.478 -1.477  1.00 13.13 ?  61  MET   B CE   1 
ATOM   4933 H  H    . MET   B 1 61  ? 56.661 -14.561 0.304   1.00 14.28 ?  61  MET   B H    1 
ATOM   4934 H  HA   . MET   B 1 61  ? 54.473 -13.271 0.807   1.00 13.57 ?  61  MET   B HA   1 
ATOM   4935 H  HB2  . MET   B 1 61  ? 54.391 -15.204 -0.420  1.00 13.47 ?  61  MET   B HB2  1 
ATOM   4936 H  HB3  . MET   B 1 61  ? 54.923 -16.052 0.810   1.00 13.47 ?  61  MET   B HB3  1 
ATOM   4937 H  HG2  . MET   B 1 61  ? 52.912 -15.710 1.924   1.00 13.58 ?  61  MET   B HG2  1 
ATOM   4938 H  HG3  . MET   B 1 61  ? 52.383 -14.841 0.702   1.00 13.58 ?  61  MET   B HG3  1 
ATOM   4939 H  HE1  . MET   B 1 61  ? 51.648 -17.185 -2.004  1.00 15.75 ?  61  MET   B HE1  1 
ATOM   4940 H  HE2  . MET   B 1 61  ? 51.461 -15.707 -1.452  1.00 15.75 ?  61  MET   B HE2  1 
ATOM   4941 H  HE3  . MET   B 1 61  ? 52.907 -16.229 -1.852  1.00 15.75 ?  61  MET   B HE3  1 
ATOM   4942 N  N    . GLN   B 1 62  ? 55.704 -14.743 3.397   1.00 11.30 ?  62  GLN   B N    1 
ATOM   4943 C  CA   . GLN   B 1 62  ? 55.593 -14.790 4.850   1.00 11.54 ?  62  GLN   B CA   1 
ATOM   4944 C  C    . GLN   B 1 62  ? 55.877 -13.431 5.475   1.00 11.80 ?  62  GLN   B C    1 
ATOM   4945 O  O    . GLN   B 1 62  ? 55.199 -13.027 6.425   1.00 12.17 ?  62  GLN   B O    1 
ATOM   4946 C  CB   . GLN   B 1 62  ? 56.545 -15.832 5.427   1.00 12.33 ?  62  GLN   B CB   1 
ATOM   4947 C  CG   . GLN   B 1 62  ? 56.307 -16.099 6.899   1.00 12.50 ?  62  GLN   B CG   1 
ATOM   4948 C  CD   . GLN   B 1 62  ? 54.931 -16.690 7.133   1.00 12.00 ?  62  GLN   B CD   1 
ATOM   4949 O  OE1  . GLN   B 1 62  ? 54.677 -17.837 6.769   1.00 12.46 ?  62  GLN   B OE1  1 
ATOM   4950 N  NE2  . GLN   B 1 62  ? 54.019 -15.897 7.694   1.00 12.32 ?  62  GLN   B NE2  1 
ATOM   4951 H  H    . GLN   B 1 62  ? 56.348 -15.194 3.063   1.00 13.55 ?  62  GLN   B H    1 
ATOM   4952 H  HA   . GLN   B 1 62  ? 54.687 -15.038 5.087   1.00 13.84 ?  62  GLN   B HA   1 
ATOM   4953 H  HB2  . GLN   B 1 62  ? 56.425 -16.667 4.943   1.00 14.78 ?  62  GLN   B HB2  1 
ATOM   4954 H  HB3  . GLN   B 1 62  ? 57.457 -15.519 5.321   1.00 14.78 ?  62  GLN   B HB3  1 
ATOM   4955 H  HG2  . GLN   B 1 62  ? 56.966 -16.740 7.216   1.00 14.99 ?  62  GLN   B HG2  1 
ATOM   4956 H  HG3  . GLN   B 1 62  ? 56.373 -15.274 7.395   1.00 14.99 ?  62  GLN   B HG3  1 
ATOM   4957 H  HE21 . GLN   B 1 62  ? 54.230 -15.096 7.925   1.00 14.77 ?  62  GLN   B HE21 1 
ATOM   4958 H  HE22 . GLN   B 1 62  ? 53.225 -16.192 7.844   1.00 14.77 ?  62  GLN   B HE22 1 
ATOM   4959 N  N    . VAL   B 1 63  ? 56.892 -12.718 4.980   1.00 12.32 ?  63  VAL   B N    1 
ATOM   4960 C  CA   . VAL   B 1 63  ? 57.199 -11.401 5.534   1.00 13.34 ?  63  VAL   B CA   1 
ATOM   4961 C  C    . VAL   B 1 63  ? 56.008 -10.466 5.351   1.00 12.50 ?  63  VAL   B C    1 
ATOM   4962 O  O    . VAL   B 1 63  ? 55.596 -9.757  6.278   1.00 12.77 ?  63  VAL   B O    1 
ATOM   4963 C  CB   . VAL   B 1 63  ? 58.486 -10.845 4.905   1.00 14.22 ?  63  VAL   B CB   1 
ATOM   4964 C  CG1  . VAL   B 1 63  ? 58.715 -9.406  5.345   1.00 15.01 ?  63  VAL   B CG1  1 
ATOM   4965 C  CG2  . VAL   B 1 63  ? 59.675 -11.722 5.286   1.00 15.13 ?  63  VAL   B CG2  1 
ATOM   4966 H  H    . VAL   B 1 63  ? 57.406 -12.971 4.333   1.00 14.77 ?  63  VAL   B H    1 
ATOM   4967 H  HA   . VAL   B 1 63  ? 57.358 -11.494 6.481   1.00 16.00 ?  63  VAL   B HA   1 
ATOM   4968 H  HB   . VAL   B 1 63  ? 58.411 -10.856 3.938   1.00 17.05 ?  63  VAL   B HB   1 
ATOM   4969 H  HG11 . VAL   B 1 63  ? 59.632 -9.160  5.159   1.00 18.00 ?  63  VAL   B HG11 1 
ATOM   4970 H  HG12 . VAL   B 1 63  ? 58.110 -8.828  4.854   1.00 18.00 ?  63  VAL   B HG12 1 
ATOM   4971 H  HG13 . VAL   B 1 63  ? 58.540 -9.340  6.297   1.00 18.00 ?  63  VAL   B HG13 1 
ATOM   4972 H  HG21 . VAL   B 1 63  ? 60.487 -11.347 4.908   1.00 18.15 ?  63  VAL   B HG21 1 
ATOM   4973 H  HG22 . VAL   B 1 63  ? 59.750 -11.750 6.256   1.00 18.15 ?  63  VAL   B HG22 1 
ATOM   4974 H  HG23 . VAL   B 1 63  ? 59.535 -12.618 4.943   1.00 18.15 ?  63  VAL   B HG23 1 
ATOM   4975 N  N    . GLU   B 1 64  ? 55.442 -10.453 4.146   1.00 11.76 ?  64  GLU   B N    1 
ATOM   4976 C  CA   . GLU   B 1 64  ? 54.271 -9.626  3.868   1.00 11.59 ?  64  GLU   B CA   1 
ATOM   4977 C  C    . GLU   B 1 64  ? 53.091 -10.019 4.749   1.00 11.40 ?  64  GLU   B C    1 
ATOM   4978 O  O    . GLU   B 1 64  ? 52.352 -9.153  5.245   1.00 11.80 ?  64  GLU   B O    1 
ATOM   4979 C  CB   . GLU   B 1 64  ? 53.910 -9.773  2.392   1.00 11.90 ?  64  GLU   B CB   1 
ATOM   4980 C  CG   . GLU   B 1 64  ? 52.639 -9.045  1.974   1.00 12.34 ?  64  GLU   B CG   1 
ATOM   4981 C  CD   . GLU   B 1 64  ? 52.115 -9.526  0.634   1.00 13.09 ?  64  GLU   B CD   1 
ATOM   4982 O  OE1  . GLU   B 1 64  ? 52.300 -10.730 0.321   1.00 13.57 ?  64  GLU   B OE1  1 
ATOM   4983 O  OE2  . GLU   B 1 64  ? 51.494 -8.703  -0.081  1.00 13.91 -1 64  GLU   B OE2  1 
ATOM   4984 H  H    . GLU   B 1 64  ? 55.709 -10.923 3.473   1.00 14.10 ?  64  GLU   B H    1 
ATOM   4985 H  HA   . GLU   B 1 64  ? 54.484 -8.698  4.036   1.00 13.90 ?  64  GLU   B HA   1 
ATOM   4986 H  HB2  . GLU   B 1 64  ? 54.634 -9.409  1.852   1.00 14.26 ?  64  GLU   B HB2  1 
ATOM   4987 H  HB3  . GLU   B 1 64  ? 53.793 -10.711 2.186   1.00 14.26 ?  64  GLU   B HB3  1 
ATOM   4988 H  HG2  . GLU   B 1 64  ? 51.935 -9.203  2.630   1.00 14.80 ?  64  GLU   B HG2  1 
ATOM   4989 H  HG3  . GLU   B 1 64  ? 52.816 -8.097  1.908   1.00 14.80 ?  64  GLU   B HG3  1 
ATOM   4990 N  N    . SER   B 1 65  ? 52.899 -11.324 4.940   1.00 11.38 ?  65  SER   B N    1 
ATOM   4991 C  CA   . SER   B 1 65  ? 51.788 -11.827 5.736   1.00 11.24 ?  65  SER   B CA   1 
ATOM   4992 C  C    . SER   B 1 65  ? 51.919 -11.420 7.197   1.00 11.56 ?  65  SER   B C    1 
ATOM   4993 O  O    . SER   B 1 65  ? 50.922 -11.049 7.829   1.00 11.87 ?  65  SER   B O    1 
ATOM   4994 C  CB   . SER   B 1 65  ? 51.713 -13.352 5.608   1.00 11.69 ?  65  SER   B CB   1 
ATOM   4995 O  OG   . SER   B 1 65  ? 51.370 -13.748 4.283   1.00 11.64 ?  65  SER   B OG   1 
ATOM   4996 H  H    . SER   B 1 65  ? 53.408 -11.944 4.620   1.00 13.65 ?  65  SER   B H    1 
ATOM   4997 H  HA   . SER   B 1 65  ? 50.959 -11.459 5.395   1.00 13.47 ?  65  SER   B HA   1 
ATOM   4998 H  HB2  . SER   B 1 65  ? 52.573 -13.732 5.840   1.00 14.02 ?  65  SER   B HB2  1 
ATOM   4999 H  HB3  . SER   B 1 65  ? 51.031 -13.684 6.217   1.00 14.02 ?  65  SER   B HB3  1 
ATOM   5000 H  HG   . SER   B 1 65  ? 51.956 -13.464 3.744   1.00 13.95 ?  65  SER   B HG   1 
ATOM   5001 N  N    . ASP   B 1 66  ? 53.127 -11.526 7.764   1.00 11.96 ?  66  ASP   B N    1 
ATOM   5002 C  CA   . ASP   B 1 66  ? 53.312 -11.130 9.158   1.00 12.38 ?  66  ASP   B CA   1 
ATOM   5003 C  C    . ASP   B 1 66  ? 52.992 -9.653  9.347   1.00 12.23 ?  66  ASP   B C    1 
ATOM   5004 O  O    . ASP   B 1 66  ? 52.412 -9.258  10.365  1.00 12.81 ?  66  ASP   B O    1 
ATOM   5005 C  CB   . ASP   B 1 66  ? 54.742 -11.432 9.613   1.00 13.31 ?  66  ASP   B CB   1 
ATOM   5006 C  CG   . ASP   B 1 66  ? 55.016 -12.924 9.775   1.00 15.00 ?  66  ASP   B CG   1 
ATOM   5007 O  OD1  . ASP   B 1 66  ? 54.065 -13.735 9.691   1.00 15.73 ?  66  ASP   B OD1  1 
ATOM   5008 O  OD2  . ASP   B 1 66  ? 56.198 -13.277 9.998   1.00 17.62 -1 66  ASP   B OD2  1 
ATOM   5009 H  H    . ASP   B 1 66  ? 53.828 -11.837 7.382   1.00 14.35 ?  66  ASP   B H    1 
ATOM   5010 H  HA   . ASP   B 1 66  ? 52.708 -11.638 9.724   1.00 14.84 ?  66  ASP   B HA   1 
ATOM   5011 H  HB2  . ASP   B 1 66  ? 55.362 -11.078 8.957   1.00 15.96 ?  66  ASP   B HB2  1 
ATOM   5012 H  HB3  . ASP   B 1 66  ? 54.896 -11.002 10.474  1.00 15.96 ?  66  ASP   B HB3  1 
ATOM   5013 N  N    . ASP   B 1 67  ? 53.371 -8.814  8.382   1.00 11.92 ?  67  ASP   B N    1 
ATOM   5014 C  CA   . ASP   B 1 67  ? 53.024 -7.402  8.461   1.00 12.30 ?  67  ASP   B CA   1 
ATOM   5015 C  C    . ASP   B 1 67  ? 51.514 -7.196  8.376   1.00 12.56 ?  67  ASP   B C    1 
ATOM   5016 O  O    . ASP   B 1 67  ? 50.950 -6.384  9.123   1.00 13.44 ?  67  ASP   B O    1 
ATOM   5017 C  CB   . ASP   B 1 67  ? 53.753 -6.637  7.362   1.00 13.72 ?  67  ASP   B CB   1 
ATOM   5018 C  CG   . ASP   B 1 67  ? 53.326 -5.198  7.298   1.00 15.19 ?  67  ASP   B CG   1 
ATOM   5019 O  OD1  . ASP   B 1 67  ? 53.837 -4.372  8.086   1.00 16.56 ?  67  ASP   B OD1  1 
ATOM   5020 O  OD2  . ASP   B 1 67  ? 52.436 -4.906  6.481   1.00 16.31 -1 67  ASP   B OD2  1 
ATOM   5021 H  H    . ASP   B 1 67  ? 53.830 -9.035  7.691   1.00 14.29 ?  67  ASP   B H    1 
ATOM   5022 H  HA   . ASP   B 1 67  ? 53.323 -7.048  9.312   1.00 14.75 ?  67  ASP   B HA   1 
ATOM   5023 H  HB2  . ASP   B 1 67  ? 54.708 -6.662  7.533   1.00 16.46 ?  67  ASP   B HB2  1 
ATOM   5024 H  HB3  . ASP   B 1 67  ? 53.560 -7.050  6.503   1.00 16.46 ?  67  ASP   B HB3  1 
ATOM   5025 N  N    . TYR   B 1 68  ? 50.837 -7.931  7.484   1.00 12.36 ?  68  TYR   B N    1 
ATOM   5026 C  CA   . TYR   B 1 68  ? 49.379 -7.852  7.410   1.00 12.75 ?  68  TYR   B CA   1 
ATOM   5027 C  C    . TYR   B 1 68  ? 48.741 -8.199  8.752   1.00 12.75 ?  68  TYR   B C    1 
ATOM   5028 O  O    . TYR   B 1 68  ? 47.805 -7.522  9.199   1.00 13.37 ?  68  TYR   B O    1 
ATOM   5029 C  CB   . TYR   B 1 68  ? 48.849 -8.787  6.313   1.00 13.79 ?  68  TYR   B CB   1 
ATOM   5030 C  CG   . TYR   B 1 68  ? 47.340 -8.941  6.369   1.00 15.07 ?  68  TYR   B CG   1 
ATOM   5031 C  CD1  . TYR   B 1 68  ? 46.754 -9.886  7.204   1.00 15.89 ?  68  TYR   B CD1  1 
ATOM   5032 C  CD2  . TYR   B 1 68  ? 46.507 -8.107  5.640   1.00 15.99 ?  68  TYR   B CD2  1 
ATOM   5033 C  CE1  . TYR   B 1 68  ? 45.388 -10.008 7.298   1.00 17.02 ?  68  TYR   B CE1  1 
ATOM   5034 C  CE2  . TYR   B 1 68  ? 45.124 -8.237  5.718   1.00 16.32 ?  68  TYR   B CE2  1 
ATOM   5035 C  CZ   . TYR   B 1 68  ? 44.587 -9.186  6.555   1.00 16.73 ?  68  TYR   B CZ   1 
ATOM   5036 O  OH   . TYR   B 1 68  ? 43.219 -9.300  6.656   1.00 17.80 ?  68  TYR   B OH   1 
ATOM   5037 H  H    . TYR   B 1 68  ? 51.196 -8.481  6.924   1.00 14.82 ?  68  TYR   B H    1 
ATOM   5038 H  HA   . TYR   B 1 68  ? 49.126 -6.947  7.183   1.00 15.29 ?  68  TYR   B HA   1 
ATOM   5039 H  HB2  . TYR   B 1 68  ? 49.078 -8.421  5.446   1.00 16.54 ?  68  TYR   B HB2  1 
ATOM   5040 H  HB3  . TYR   B 1 68  ? 49.245 -9.665  6.422   1.00 16.54 ?  68  TYR   B HB3  1 
ATOM   5041 H  HD1  . TYR   B 1 68  ? 47.295 -10.451 7.710   1.00 19.06 ?  68  TYR   B HD1  1 
ATOM   5042 H  HD2  . TYR   B 1 68  ? 46.876 -7.461  5.089   1.00 19.18 ?  68  TYR   B HD2  1 
ATOM   5043 H  HE1  . TYR   B 1 68  ? 45.009 -10.661 7.848   1.00 20.42 ?  68  TYR   B HE1  1 
ATOM   5044 H  HE2  . TYR   B 1 68  ? 44.566 -7.674  5.227   1.00 19.58 ?  68  TYR   B HE2  1 
ATOM   5045 H  HH   . TYR   B 1 68  ? 42.833 -8.751  6.139   1.00 21.34 ?  68  TYR   B HH   1 
ATOM   5046 N  N    . ILE   B 1 69  ? 49.223 -9.266  9.397   1.00 12.48 ?  69  ILE   B N    1 
ATOM   5047 C  CA   . ILE   B 1 69  ? 48.671 -9.687  10.684  1.00 12.63 ?  69  ILE   B CA   1 
ATOM   5048 C  C    . ILE   B 1 69  ? 48.923 -8.635  11.757  1.00 12.69 ?  69  ILE   B C    1 
ATOM   5049 O  O    . ILE   B 1 69  ? 48.052 -8.359  12.589  1.00 13.28 ?  69  ILE   B O    1 
ATOM   5050 C  CB   . ILE   B 1 69  ? 49.248 -11.056 11.085  1.00 13.41 ?  69  ILE   B CB   1 
ATOM   5051 C  CG1  . ILE   B 1 69  ? 48.716 -12.162 10.163  1.00 14.13 ?  69  ILE   B CG1  1 
ATOM   5052 C  CG2  . ILE   B 1 69  ? 48.958 -11.363 12.550  1.00 14.52 ?  69  ILE   B CG2  1 
ATOM   5053 C  CD1  . ILE   B 1 69  ? 47.243 -12.471 10.330  1.00 14.60 ?  69  ILE   B CD1  1 
ATOM   5054 H  H    . ILE   B 1 69  ? 49.874 -9.754  9.115   1.00 14.96 ?  69  ILE   B H    1 
ATOM   5055 H  HA   . ILE   B 1 69  ? 47.719 -9.782  10.593  1.00 15.15 ?  69  ILE   B HA   1 
ATOM   5056 H  HB   . ILE   B 1 69  ? 50.216 -11.019 10.976  1.00 16.08 ?  69  ILE   B HB   1 
ATOM   5057 H  HG12 . ILE   B 1 69  ? 48.859 -11.887 9.242   1.00 16.94 ?  69  ILE   B HG12 1 
ATOM   5058 H  HG13 . ILE   B 1 69  ? 49.214 -12.975 10.340  1.00 16.94 ?  69  ILE   B HG13 1 
ATOM   5059 H  HG21 . ILE   B 1 69  ? 49.098 -12.313 12.702  1.00 17.42 ?  69  ILE   B HG21 1 
ATOM   5060 H  HG22 . ILE   B 1 69  ? 49.560 -10.852 13.112  1.00 17.42 ?  69  ILE   B HG22 1 
ATOM   5061 H  HG23 . ILE   B 1 69  ? 48.038 -11.132 12.744  1.00 17.42 ?  69  ILE   B HG23 1 
ATOM   5062 H  HD11 . ILE   B 1 69  ? 47.005 -13.181 9.716   1.00 17.50 ?  69  ILE   B HD11 1 
ATOM   5063 H  HD12 . ILE   B 1 69  ? 47.082 -12.757 11.243  1.00 17.50 ?  69  ILE   B HD12 1 
ATOM   5064 H  HD13 . ILE   B 1 69  ? 46.726 -11.677 10.134  1.00 17.50 ?  69  ILE   B HD13 1 
ATOM   5065 N  N    . ALA   B 1 70  ? 50.119 -8.046  11.779  1.00 12.54 ?  70  ALA   B N    1 
ATOM   5066 C  CA   . ALA   B 1 70  ? 50.390 -7.004  12.766  1.00 12.48 ?  70  ALA   B CA   1 
ATOM   5067 C  C    . ALA   B 1 70  ? 49.386 -5.868  12.650  1.00 13.11 ?  70  ALA   B C    1 
ATOM   5068 O  O    . ALA   B 1 70  ? 48.936 -5.322  13.660  1.00 13.43 ?  70  ALA   B O    1 
ATOM   5069 C  CB   . ALA   B 1 70  ? 51.814 -6.476  12.598  1.00 13.11 ?  70  ALA   B CB   1 
ATOM   5070 H  H    . ALA   B 1 70  ? 50.772 -8.222  11.253  1.00 15.04 ?  70  ALA   B H    1 
ATOM   5071 H  HA   . ALA   B 1 70  ? 50.319 -7.380  13.659  1.00 14.96 ?  70  ALA   B HA   1 
ATOM   5072 H  HB1  . ALA   B 1 70  ? 51.999 -5.827  13.298  1.00 15.72 ?  70  ALA   B HB1  1 
ATOM   5073 H  HB2  . ALA   B 1 70  ? 52.439 -7.216  12.667  1.00 15.72 ?  70  ALA   B HB2  1 
ATOM   5074 H  HB3  . ALA   B 1 70  ? 51.898 -6.056  11.727  1.00 15.72 ?  70  ALA   B HB3  1 
ATOM   5075 N  N    A THR   B 1 71  ? 49.021 -5.497  11.424  0.50 13.37 ?  71  THR   B N    1 
ATOM   5076 N  N    B THR   B 1 71  ? 49.014 -5.514  11.420  0.50 13.46 ?  71  THR   B N    1 
ATOM   5077 C  CA   A THR   B 1 71  ? 48.111 -4.372  11.230  0.50 14.22 ?  71  THR   B CA   1 
ATOM   5078 C  CA   B THR   B 1 71  ? 48.130 -4.380  11.181  0.50 14.36 ?  71  THR   B CA   1 
ATOM   5079 C  C    A THR   B 1 71  ? 46.652 -4.759  11.454  0.50 14.65 ?  71  THR   B C    1 
ATOM   5080 C  C    B THR   B 1 71  ? 46.656 -4.730  11.364  0.50 14.78 ?  71  THR   B C    1 
ATOM   5081 O  O    A THR   B 1 71  ? 45.883 -3.979  12.034  0.50 15.66 ?  71  THR   B O    1 
ATOM   5082 O  O    B THR   B 1 71  ? 45.876 -3.881  11.820  0.50 15.78 ?  71  THR   B O    1 
ATOM   5083 C  CB   A THR   B 1 71  ? 48.305 -3.789  9.828   0.50 15.64 ?  71  THR   B CB   1 
ATOM   5084 C  CB   B THR   B 1 71  ? 48.365 -3.855  9.763   0.50 15.90 ?  71  THR   B CB   1 
ATOM   5085 O  OG1  A THR   B 1 71  ? 49.594 -3.170  9.745   0.50 16.97 ?  71  THR   B OG1  1 
ATOM   5086 O  OG1  B THR   B 1 71  ? 49.717 -3.399  9.638   0.50 17.09 ?  71  THR   B OG1  1 
ATOM   5087 C  CG2  A THR   B 1 71  ? 47.248 -2.745  9.519   0.50 16.09 ?  71  THR   B CG2  1 
ATOM   5088 C  CG2  B THR   B 1 71  ? 47.397 -2.724  9.426   0.50 16.47 ?  71  THR   B CG2  1 
ATOM   5089 H  H    A THR   B 1 71  ? 49.283 -5.879  10.700  0.50 16.03 ?  71  THR   B H    1 
ATOM   5090 H  H    B THR   B 1 71  ? 49.265 -5.922  10.707  0.50 16.14 ?  71  THR   B H    1 
ATOM   5091 H  HA   A THR   B 1 71  ? 48.333 -3.680  11.869  0.50 17.06 ?  71  THR   B HA   1 
ATOM   5092 H  HA   B THR   B 1 71  ? 48.350 -3.673  11.804  0.50 17.22 ?  71  THR   B HA   1 
ATOM   5093 H  HB   A THR   B 1 71  ? 48.236 -4.505  9.171   0.50 18.75 ?  71  THR   B HB   1 
ATOM   5094 H  HB   B THR   B 1 71  ? 48.229 -4.569  9.125   0.50 19.07 ?  71  THR   B HB   1 
ATOM   5095 H  HG1  A THR   B 1 71  ? 49.722 -2.873  8.968   0.50 20.35 ?  71  THR   B HG1  1 
ATOM   5096 H  HG1  B THR   B 1 71  ? 49.842 -3.074  8.871   0.50 20.49 ?  71  THR   B HG1  1 
ATOM   5097 H  HG21 A THR   B 1 71  ? 47.541 -2.195  8.774   0.50 19.30 ?  71  THR   B HG21 1 
ATOM   5098 H  HG21 B THR   B 1 71  ? 47.706 -2.248  8.638   0.50 19.75 ?  71  THR   B HG21 1 
ATOM   5099 H  HG22 A THR   B 1 71  ? 46.413 -3.171  9.286   0.50 19.30 ?  71  THR   B HG22 1 
ATOM   5100 H  HG22 B THR   B 1 71  ? 46.514 -3.083  9.247   0.50 19.75 ?  71  THR   B HG22 1 
ATOM   5101 H  HG23 A THR   B 1 71  ? 47.115 -2.175  10.293  0.50 19.30 ?  71  THR   B HG23 1 
ATOM   5102 H  HG23 B THR   B 1 71  ? 47.342 -2.101  10.167  0.50 19.75 ?  71  THR   B HG23 1 
ATOM   5103 N  N    . ASN   B 1 72  ? 46.255 -5.957  11.013  1.00 14.12 ?  72  ASN   B N    1 
ATOM   5104 C  CA   . ASN   B 1 72  ? 44.846 -6.321  10.912  1.00 14.71 ?  72  ASN   B CA   1 
ATOM   5105 C  C    . ASN   B 1 72  ? 44.379 -7.414  11.864  1.00 15.12 ?  72  ASN   B C    1 
ATOM   5106 O  O    . ASN   B 1 72  ? 43.164 -7.568  12.045  1.00 16.40 ?  72  ASN   B O    1 
ATOM   5107 C  CB   . ASN   B 1 72  ? 44.520 -6.753  9.473   1.00 15.79 ?  72  ASN   B CB   1 
ATOM   5108 C  CG   . ASN   B 1 72  ? 44.810 -5.661  8.465   1.00 17.03 ?  72  ASN   B CG   1 
ATOM   5109 O  OD1  . ASN   B 1 72  ? 45.835 -5.677  7.786   1.00 18.26 ?  72  ASN   B OD1  1 
ATOM   5110 N  ND2  . ASN   B 1 72  ? 43.929 -4.685  8.392   1.00 18.55 ?  72  ASN   B ND2  1 
ATOM   5111 H  H    A ASN   B 1 72  ? 46.795 -6.586  10.763  0.50 16.93 ?  72  ASN   B H    1 
ATOM   5112 H  H    B ASN   B 1 72  ? 46.794 -6.604  10.813  0.50 16.93 ?  72  ASN   B H    1 
ATOM   5113 H  HA   . ASN   B 1 72  ? 44.316 -5.536  11.101  1.00 17.64 ?  72  ASN   B HA   1 
ATOM   5114 H  HB2  . ASN   B 1 72  ? 45.057 -7.527  9.241   1.00 18.93 ?  72  ASN   B HB2  1 
ATOM   5115 H  HB3  . ASN   B 1 72  ? 43.578 -6.970  9.413   1.00 18.93 ?  72  ASN   B HB3  1 
ATOM   5116 H  HD21 . ASN   B 1 72  ? 44.044 -4.039  7.831   1.00 22.25 ?  72  ASN   B HD21 1 
ATOM   5117 H  HD22 . ASN   B 1 72  ? 43.221 -4.704  8.879   1.00 22.25 ?  72  ASN   B HD22 1 
ATOM   5118 N  N    . GLY   B 1 73  ? 45.287 -8.165  12.476  1.00 14.78 ?  73  GLY   B N    1 
ATOM   5119 C  CA   . GLY   B 1 73  ? 44.901 -9.298  13.279  1.00 14.35 ?  73  GLY   B CA   1 
ATOM   5120 C  C    . GLY   B 1 73  ? 44.540 -10.488 12.416  1.00 13.25 ?  73  GLY   B C    1 
ATOM   5121 O  O    . GLY   B 1 73  ? 44.530 -10.414 11.185  1.00 13.18 ?  73  GLY   B O    1 
ATOM   5122 H  H    . GLY   B 1 73  ? 46.139 -8.032  12.443  1.00 17.72 ?  73  GLY   B H    1 
ATOM   5123 H  HA2  . GLY   B 1 73  ? 45.633 -9.546  13.867  1.00 17.21 ?  73  GLY   B HA2  1 
ATOM   5124 H  HA3  . GLY   B 1 73  ? 44.133 -9.064  13.825  1.00 17.21 ?  73  GLY   B HA3  1 
ATOM   5125 N  N    . PRO   B 1 74  ? 44.244 -11.616 13.059  1.00 13.61 ?  74  PRO   B N    1 
ATOM   5126 C  CA   . PRO   B 1 74  ? 43.982 -12.847 12.313  1.00 12.87 ?  74  PRO   B CA   1 
ATOM   5127 C  C    . PRO   B 1 74  ? 42.686 -12.784 11.523  1.00 12.43 ?  74  PRO   B C    1 
ATOM   5128 O  O    . PRO   B 1 74  ? 41.744 -12.052 11.853  1.00 13.71 ?  74  PRO   B O    1 
ATOM   5129 C  CB   . PRO   B 1 74  ? 43.897 -13.909 13.416  1.00 14.20 ?  74  PRO   B CB   1 
ATOM   5130 C  CG   . PRO   B 1 74  ? 43.466 -13.150 14.627  1.00 15.72 ?  74  PRO   B CG   1 
ATOM   5131 C  CD   . PRO   B 1 74  ? 44.144 -11.820 14.513  1.00 15.06 ?  74  PRO   B CD   1 
ATOM   5132 H  HA   . PRO   B 1 74  ? 44.720 -13.050 11.717  1.00 15.44 ?  74  PRO   B HA   1 
ATOM   5133 H  HB2  . PRO   B 1 74  ? 43.238 -14.580 13.173  1.00 17.03 ?  74  PRO   B HB2  1 
ATOM   5134 H  HB3  . PRO   B 1 74  ? 44.768 -14.312 13.550  1.00 17.03 ?  74  PRO   B HB3  1 
ATOM   5135 H  HG2  . PRO   B 1 74  ? 42.501 -13.046 14.618  1.00 18.85 ?  74  PRO   B HG2  1 
ATOM   5136 H  HG3  . PRO   B 1 74  ? 43.755 -13.617 15.423  1.00 18.85 ?  74  PRO   B HG3  1 
ATOM   5137 H  HD2  . PRO   B 1 74  ? 43.596 -11.128 14.918  1.00 18.06 ?  74  PRO   B HD2  1 
ATOM   5138 H  HD3  . PRO   B 1 74  ? 45.026 -11.856 14.911  1.00 18.06 ?  74  PRO   B HD3  1 
ATOM   5139 N  N    . LEU   B 1 75  ? 42.651 -13.590 10.469  1.00 11.78 ?  75  LEU   B N    1 
ATOM   5140 C  CA   . LEU   B 1 75  ? 41.438 -13.798 9.702   1.00 11.99 ?  75  LEU   B CA   1 
ATOM   5141 C  C    . LEU   B 1 75  ? 40.452 -14.646 10.501  1.00 12.70 ?  75  LEU   B C    1 
ATOM   5142 O  O    . LEU   B 1 75  ? 40.796 -15.255 11.516  1.00 13.70 ?  75  LEU   B O    1 
ATOM   5143 C  CB   . LEU   B 1 75  ? 41.764 -14.518 8.394   1.00 11.80 ?  75  LEU   B CB   1 
ATOM   5144 C  CG   . LEU   B 1 75  ? 42.588 -13.759 7.351   1.00 13.70 ?  75  LEU   B CG   1 
ATOM   5145 C  CD1  . LEU   B 1 75  ? 42.818 -14.621 6.115   1.00 15.43 ?  75  LEU   B CD1  1 
ATOM   5146 C  CD2  . LEU   B 1 75  ? 41.932 -12.460 6.972   1.00 17.20 ?  75  LEU   B CD2  1 
ATOM   5147 H  H    . LEU   B 1 75  ? 43.327 -14.039 10.180  1.00 14.13 ?  75  LEU   B H    1 
ATOM   5148 H  HA   . LEU   B 1 75  ? 41.024 -12.948 9.496   1.00 14.38 ?  75  LEU   B HA   1 
ATOM   5149 H  HB2  . LEU   B 1 75  ? 42.260 -15.329 8.609   1.00 14.15 ?  75  LEU   B HB2  1 
ATOM   5150 H  HB3  . LEU   B 1 75  ? 40.929 -14.768 7.966   1.00 14.15 ?  75  LEU   B HB3  1 
ATOM   5151 H  HG   . LEU   B 1 75  ? 43.456 -13.556 7.733   1.00 16.43 ?  75  LEU   B HG   1 
ATOM   5152 H  HD11 . LEU   B 1 75  ? 43.349 -14.115 5.475   1.00 18.51 ?  75  LEU   B HD11 1 
ATOM   5153 H  HD12 . LEU   B 1 75  ? 43.298 -15.425 6.373   1.00 18.51 ?  75  LEU   B HD12 1 
ATOM   5154 H  HD13 . LEU   B 1 75  ? 41.964 -14.853 5.726   1.00 18.51 ?  75  LEU   B HD13 1 
ATOM   5155 H  HD21 . LEU   B 1 75  ? 42.419 -12.065 6.234   1.00 20.62 ?  75  LEU   B HD21 1 
ATOM   5156 H  HD22 . LEU   B 1 75  ? 41.015 -12.634 6.711   1.00 20.62 ?  75  LEU   B HD22 1 
ATOM   5157 H  HD23 . LEU   B 1 75  ? 41.950 -11.863 7.738   1.00 20.62 ?  75  LEU   B HD23 1 
ATOM   5158 N  N    . LYS   B 1 76  ? 39.208 -14.686 10.019  1.00 13.58 ?  76  LYS   B N    1 
ATOM   5159 C  CA   . LYS   B 1 76  ? 38.220 -15.661 10.466  1.00 14.86 ?  76  LYS   B CA   1 
ATOM   5160 C  C    . LYS   B 1 76  ? 38.348 -16.944 9.645   1.00 13.96 ?  76  LYS   B C    1 
ATOM   5161 O  O    . LYS   B 1 76  ? 38.631 -16.902 8.450   1.00 13.47 ?  76  LYS   B O    1 
ATOM   5162 C  CB   . LYS   B 1 76  ? 36.800 -15.114 10.246  1.00 16.70 ?  76  LYS   B CB   1 
ATOM   5163 C  CG   . LYS   B 1 76  ? 36.501 -13.744 10.869  1.00 18.28 ?  76  LYS   B CG   1 
ATOM   5164 C  CD   . LYS   B 1 76  ? 35.120 -13.201 10.458  1.00 19.35 ?  76  LYS   B CD   1 
ATOM   5165 C  CE   . LYS   B 1 76  ? 34.820 -11.861 11.113  1.00 20.83 ?  76  LYS   B CE   1 
ATOM   5166 N  NZ   . LYS   B 1 76  ? 33.560 -11.248 10.604  1.00 21.41 ?  76  LYS   B NZ   1 
ATOM   5167 H  H    . LYS   B 1 76  ? 38.910 -14.154 9.409   1.00 16.28 ?  76  LYS   B H    1 
ATOM   5168 H  HA   . LYS   B 1 76  ? 38.347 -15.867 11.405  1.00 17.82 ?  76  LYS   B HA   1 
ATOM   5169 H  HB2  . LYS   B 1 76  ? 36.648 -15.034 9.292   1.00 20.03 ?  76  LYS   B HB2  1 
ATOM   5170 H  HB3  . LYS   B 1 76  ? 36.167 -15.744 10.623  1.00 20.03 ?  76  LYS   B HB3  1 
ATOM   5171 H  HG2  . LYS   B 1 76  ? 36.518 -13.821 11.837  1.00 21.93 ?  76  LYS   B HG2  1 
ATOM   5172 H  HG3  . LYS   B 1 76  ? 37.173 -13.105 10.577  1.00 21.93 ?  76  LYS   B HG3  1 
ATOM   5173 H  HD2  . LYS   B 1 76  ? 35.097 -13.078 9.495   1.00 23.21 ?  76  LYS   B HD2  1 
ATOM   5174 H  HD3  . LYS   B 1 76  ? 34.434 -13.831 10.730  1.00 23.21 ?  76  LYS   B HD3  1 
ATOM   5175 H  HE2  . LYS   B 1 76  ? 34.726 -11.990 12.070  1.00 24.99 ?  76  LYS   B HE2  1 
ATOM   5176 H  HE3  . LYS   B 1 76  ? 35.549 -11.248 10.929  1.00 24.99 ?  76  LYS   B HE3  1 
ATOM   5177 H  HZ1  . LYS   B 1 76  ? 33.417 -10.467 11.007  1.00 25.69 ?  76  LYS   B HZ1  1 
ATOM   5178 H  HZ2  . LYS   B 1 76  ? 33.621 -11.111 9.726   1.00 25.69 ?  76  LYS   B HZ2  1 
ATOM   5179 H  HZ3  . LYS   B 1 76  ? 32.871 -11.787 10.765  1.00 25.69 ?  76  LYS   B HZ3  1 
ATOM   5180 N  N    . VAL   B 1 77  ? 38.107 -18.094 10.286  1.00 14.28 ?  77  VAL   B N    1 
ATOM   5181 C  CA   . VAL   B 1 77  ? 37.905 -19.317 9.513   1.00 14.42 ?  77  VAL   B CA   1 
ATOM   5182 C  C    . VAL   B 1 77  ? 36.712 -19.096 8.592   1.00 13.27 ?  77  VAL   B C    1 
ATOM   5183 O  O    . VAL   B 1 77  ? 35.646 -18.646 9.031   1.00 13.57 ?  77  VAL   B O    1 
ATOM   5184 C  CB   . VAL   B 1 77  ? 37.707 -20.530 10.435  1.00 16.16 ?  77  VAL   B CB   1 
ATOM   5185 C  CG1  . VAL   B 1 77  ? 37.422 -21.776 9.600   1.00 16.72 ?  77  VAL   B CG1  1 
ATOM   5186 C  CG2  . VAL   B 1 77  ? 38.935 -20.737 11.319  1.00 17.02 ?  77  VAL   B CG2  1 
ATOM   5187 H  H    . VAL   B 1 77  ? 38.066 -18.189 11.133  1.00 17.13 ?  77  VAL   B H    1 
ATOM   5188 H  HA   . VAL   B 1 77  ? 38.684 -19.478 8.957   1.00 17.30 ?  77  VAL   B HA   1 
ATOM   5189 H  HB   . VAL   B 1 77  ? 36.938 -20.366 11.006  1.00 19.38 ?  77  VAL   B HB   1 
ATOM   5190 H  HG11 . VAL   B 1 77  ? 37.459 -22.552 10.181  1.00 20.05 ?  77  VAL   B HG11 1 
ATOM   5191 H  HG12 . VAL   B 1 77  ? 36.541 -21.704 9.202   1.00 20.05 ?  77  VAL   B HG12 1 
ATOM   5192 H  HG13 . VAL   B 1 77  ? 38.096 -21.851 8.907   1.00 20.05 ?  77  VAL   B HG13 1 
ATOM   5193 H  HG21 . VAL   B 1 77  ? 38.800 -21.532 11.855  1.00 20.41 ?  77  VAL   B HG21 1 
ATOM   5194 H  HG22 . VAL   B 1 77  ? 39.712 -20.842 10.752  1.00 20.41 ?  77  VAL   B HG22 1 
ATOM   5195 H  HG23 . VAL   B 1 77  ? 39.041 -19.962 11.892  1.00 20.41 ?  77  VAL   B HG23 1 
ATOM   5196 N  N    . GLY   B 1 78  ? 36.894 -19.383 7.303   1.00 12.78 ?  78  GLY   B N    1 
ATOM   5197 C  CA   . GLY   B 1 78  ? 35.918 -19.063 6.285   1.00 12.72 ?  78  GLY   B CA   1 
ATOM   5198 C  C    . GLY   B 1 78  ? 36.151 -17.743 5.586   1.00 12.23 ?  78  GLY   B C    1 
ATOM   5199 O  O    . GLY   B 1 78  ? 35.459 -17.458 4.601   1.00 12.59 ?  78  GLY   B O    1 
ATOM   5200 H  H    . GLY   B 1 78  ? 37.591 -19.781 6.991   1.00 15.33 ?  78  GLY   B H    1 
ATOM   5201 H  HA2  . GLY   B 1 78  ? 35.918 -19.758 5.612   1.00 15.25 ?  78  GLY   B HA2  1 
ATOM   5202 H  HA3  . GLY   B 1 78  ? 35.037 -19.029 6.687   1.00 15.25 ?  78  GLY   B HA3  1 
ATOM   5203 N  N    . GLY   B 1 79  ? 37.101 -16.932 6.066   1.00 11.91 ?  79  GLY   B N    1 
ATOM   5204 C  CA   . GLY   B 1 79  ? 37.402 -15.641 5.484   1.00 11.80 ?  79  GLY   B CA   1 
ATOM   5205 C  C    . GLY   B 1 79  ? 38.639 -15.669 4.599   1.00 11.46 ?  79  GLY   B C    1 
ATOM   5206 O  O    . GLY   B 1 79  ? 39.254 -16.709 4.367   1.00 11.72 ?  79  GLY   B O    1 
ATOM   5207 H  H    . GLY   B 1 79  ? 37.602 -17.118 6.740   1.00 14.28 ?  79  GLY   B H    1 
ATOM   5208 H  HA2  . GLY   B 1 79  ? 36.651 -15.341 4.944   1.00 14.15 ?  79  GLY   B HA2  1 
ATOM   5209 H  HA3  . GLY   B 1 79  ? 37.547 -14.989 6.189   1.00 14.15 ?  79  GLY   B HA3  1 
ATOM   5210 N  N    . SER   B 1 80  ? 39.010 -14.476 4.123   1.00 11.40 ?  80  SER   B N    1 
ATOM   5211 C  CA   . SER   B 1 80  ? 40.119 -14.349 3.186   1.00 11.19 ?  80  SER   B CA   1 
ATOM   5212 C  C    . SER   B 1 80  ? 40.705 -12.942 3.238   1.00 10.70 ?  80  SER   B C    1 
ATOM   5213 O  O    . SER   B 1 80  ? 40.091 -11.999 3.749   1.00 11.91 ?  80  SER   B O    1 
ATOM   5214 C  CB   . SER   B 1 80  ? 39.679 -14.654 1.751   1.00 11.54 ?  80  SER   B CB   1 
ATOM   5215 O  OG   . SER   B 1 80  ? 38.840 -13.636 1.235   1.00 12.47 ?  80  SER   B OG   1 
ATOM   5216 H  H    . SER   B 1 80  ? 38.647 -13.730 4.337   1.00 13.66 ?  80  SER   B H    1 
ATOM   5217 H  HA   . SER   B 1 80  ? 40.811 -14.979 3.434   1.00 13.41 ?  80  SER   B HA   1 
ATOM   5218 H  HB2  . SER   B 1 80  ? 40.459 -14.725 1.183   1.00 13.84 ?  80  SER   B HB2  1 
ATOM   5219 H  HB3  . SER   B 1 80  ? 39.185 -15.492 1.741   1.00 13.84 ?  80  SER   B HB3  1 
ATOM   5220 H  HG   . SER   B 1 80  ? 38.146 -13.558 1.711   1.00 14.95 ?  80  SER   B HG   1 
ATOM   5221 N  N    . CYS   B 1 81  ? 41.899 -12.805 2.658   1.00 10.88 ?  81  CYS   B N    1 
ATOM   5222 C  CA   . CYS   B 1 81  ? 42.446 -11.492 2.344   1.00 11.06 ?  81  CYS   B CA   1 
ATOM   5223 C  C    . CYS   B 1 81  ? 43.219 -11.582 1.038   1.00 10.07 ?  81  CYS   B C    1 
ATOM   5224 O  O    . CYS   B 1 81  ? 43.716 -12.648 0.659   1.00 11.15 ?  81  CYS   B O    1 
ATOM   5225 C  CB   . CYS   B 1 81  ? 43.335 -10.947 3.462   1.00 11.77 ?  81  CYS   B CB   1 
ATOM   5226 S  SG   . CYS   B 1 81  ? 44.854 -11.897 3.702   1.00 11.85 ?  81  CYS   B SG   1 
ATOM   5227 H  H    . CYS   B 1 81  ? 42.404 -13.460 2.424   1.00 13.04 ?  81  CYS   B H    1 
ATOM   5228 H  HA   . CYS   B 1 81  ? 41.714 -10.870 2.210   1.00 13.26 ?  81  CYS   B HA   1 
ATOM   5229 H  HB2  . CYS   B 1 81  ? 43.582 -10.036 3.252   1.00 14.11 ?  81  CYS   B HB2  1 
ATOM   5230 H  HB3  . CYS   B 1 81  ? 42.831 -10.967 4.295   1.00 14.11 ?  81  CYS   B HB3  1 
ATOM   5231 H  HG   . CYS   B 1 81  ? 45.488 -11.410 4.603   1.00 14.21 ?  81  CYS   B HG   1 
ATOM   5232 N  N    . VAL   B 1 82  ? 43.330 -10.441 0.364   1.00 10.91 ?  82  VAL   B N    1 
ATOM   5233 C  CA   . VAL   B 1 82  ? 44.084 -10.317 -0.880  1.00 10.90 ?  82  VAL   B CA   1 
ATOM   5234 C  C    . VAL   B 1 82  ? 45.426 -9.672  -0.569  1.00 11.02 ?  82  VAL   B C    1 
ATOM   5235 O  O    . VAL   B 1 82  ? 45.485 -8.552  -0.042  1.00 12.30 ?  82  VAL   B O    1 
ATOM   5236 C  CB   . VAL   B 1 82  ? 43.329 -9.479  -1.924  1.00 12.06 ?  82  VAL   B CB   1 
ATOM   5237 C  CG1  . VAL   B 1 82  ? 44.163 -9.354  -3.192  1.00 13.30 ?  82  VAL   B CG1  1 
ATOM   5238 C  CG2  . VAL   B 1 82  ? 41.964 -10.065 -2.226  1.00 12.67 ?  82  VAL   B CG2  1 
ATOM   5239 H  H    . VAL   B 1 82  ? 42.959 -9.699  0.610   1.00 13.08 ?  82  VAL   B H    1 
ATOM   5240 H  HA   . VAL   B 1 82  ? 44.243 -11.195 -1.249  1.00 13.07 ?  82  VAL   B HA   1 
ATOM   5241 H  HB   . VAL   B 1 82  ? 43.196 -8.586  -1.575  1.00 14.46 ?  82  VAL   B HB   1 
ATOM   5242 H  HG11 . VAL   B 1 82  ? 43.600 -9.028  -3.912  1.00 15.95 ?  82  VAL   B HG11 1 
ATOM   5243 H  HG12 . VAL   B 1 82  ? 44.890 -8.726  -3.037  1.00 15.95 ?  82  VAL   B HG12 1 
ATOM   5244 H  HG13 . VAL   B 1 82  ? 44.523 -10.224 -3.424  1.00 15.95 ?  82  VAL   B HG13 1 
ATOM   5245 H  HG21 . VAL   B 1 82  ? 41.534 -9.533  -2.916  1.00 15.19 ?  82  VAL   B HG21 1 
ATOM   5246 H  HG22 . VAL   B 1 82  ? 42.072 -10.979 -2.540  1.00 15.19 ?  82  VAL   B HG22 1 
ATOM   5247 H  HG23 . VAL   B 1 82  ? 41.428 -10.055 -1.419  1.00 15.19 ?  82  VAL   B HG23 1 
ATOM   5248 N  N    . LEU   B 1 83  ? 46.500 -10.366 -0.927  1.00 10.66 ?  83  LEU   B N    1 
ATOM   5249 C  CA   . LEU   B 1 83  ? 47.859 -9.853  -0.806  1.00 10.60 ?  83  LEU   B CA   1 
ATOM   5250 C  C    . LEU   B 1 83  ? 48.560 -9.997  -2.155  1.00 10.56 ?  83  LEU   B C    1 
ATOM   5251 O  O    . LEU   B 1 83  ? 47.952 -10.416 -3.145  1.00 10.83 ?  83  LEU   B O    1 
ATOM   5252 C  CB   . LEU   B 1 83  ? 48.603 -10.540 0.347   1.00 10.94 ?  83  LEU   B CB   1 
ATOM   5253 C  CG   . LEU   B 1 83  ? 48.105 -10.171 1.751   1.00 12.32 ?  83  LEU   B CG   1 
ATOM   5254 C  CD1  . LEU   B 1 83  ? 48.740 -11.027 2.830   1.00 13.11 ?  83  LEU   B CD1  1 
ATOM   5255 C  CD2  . LEU   B 1 83  ? 48.327 -8.684  2.042   1.00 13.94 ?  83  LEU   B CD2  1 
ATOM   5256 H  H    . LEU   B 1 83  ? 46.458 -11.162 -1.258  1.00 12.78 ?  83  LEU   B H    1 
ATOM   5257 H  HA   . LEU   B 1 83  ? 47.811 -8.910  -0.609  1.00 12.71 ?  83  LEU   B HA   1 
ATOM   5258 H  HB2  . LEU   B 1 83  ? 48.507 -11.500 0.252   1.00 13.12 ?  83  LEU   B HB2  1 
ATOM   5259 H  HB3  . LEU   B 1 83  ? 49.538 -10.298 0.296   1.00 13.12 ?  83  LEU   B HB3  1 
ATOM   5260 H  HG   . LEU   B 1 83  ? 47.150 -10.323 1.785   1.00 14.77 ?  83  LEU   B HG   1 
ATOM   5261 H  HD11 . LEU   B 1 83  ? 48.387 -10.757 3.697   1.00 15.72 ?  83  LEU   B HD11 1 
ATOM   5262 H  HD12 . LEU   B 1 83  ? 48.520 -11.957 2.664   1.00 15.72 ?  83  LEU   B HD12 1 
ATOM   5263 H  HD13 . LEU   B 1 83  ? 49.700 -10.903 2.814   1.00 15.72 ?  83  LEU   B HD13 1 
ATOM   5264 H  HD21 . LEU   B 1 83  ? 48.165 -8.517  2.984   1.00 16.72 ?  83  LEU   B HD21 1 
ATOM   5265 H  HD22 . LEU   B 1 83  ? 49.243 -8.450  1.819   1.00 16.72 ?  83  LEU   B HD22 1 
ATOM   5266 H  HD23 . LEU   B 1 83  ? 47.714 -8.159  1.504   1.00 16.72 ?  83  LEU   B HD23 1 
ATOM   5267 N  N    . SER   B 1 84  ? 49.841 -9.637  -2.212  1.00 11.52 ?  84  SER   B N    1 
ATOM   5268 C  CA   . SER   B 1 84  ? 50.569 -9.757  -3.467  1.00 11.86 ?  84  SER   B CA   1 
ATOM   5269 C  C    . SER   B 1 84  ? 50.735 -11.218 -3.867  1.00 11.28 ?  84  SER   B C    1 
ATOM   5270 O  O    . SER   B 1 84  ? 50.856 -12.106 -3.026  1.00 11.17 ?  84  SER   B O    1 
ATOM   5271 C  CB   . SER   B 1 84  ? 51.961 -9.139  -3.334  1.00 13.60 ?  84  SER   B CB   1 
ATOM   5272 O  OG   . SER   B 1 84  ? 52.712 -9.373  -4.514  1.00 14.66 ?  84  SER   B OG   1 
ATOM   5273 H  H    . SER   B 1 84  ? 50.296 -9.318  -1.550  1.00 13.81 ?  84  SER   B H    1 
ATOM   5274 H  HA   . SER   B 1 84  ? 50.087 -9.296  -4.168  1.00 14.22 ?  84  SER   B HA   1 
ATOM   5275 H  HB2  . SER   B 1 84  ? 51.871 -8.178  -3.198  1.00 16.30 ?  84  SER   B HB2  1 
ATOM   5276 H  HB3  . SER   B 1 84  ? 52.421 -9.536  -2.581  1.00 16.30 ?  84  SER   B HB3  1 
ATOM   5277 H  HG   . SER   B 1 84  ? 53.479 -9.022  -4.440  1.00 17.59 ?  84  SER   B HG   1 
ATOM   5278 N  N    . GLY   B 1 85  ? 50.801 -11.453 -5.173  1.00 12.06 ?  85  GLY   B N    1 
ATOM   5279 C  CA   . GLY   B 1 85  ? 51.152 -12.749 -5.698  1.00 13.05 ?  85  GLY   B CA   1 
ATOM   5280 C  C    . GLY   B 1 85  ? 52.622 -12.939 -6.004  1.00 12.06 ?  85  GLY   B C    1 
ATOM   5281 O  O    . GLY   B 1 85  ? 53.007 -14.020 -6.455  1.00 12.45 ?  85  GLY   B O    1 
ATOM   5282 H  H    . GLY   B 1 85  ? 50.648 -10.868 -5.777  1.00 14.46 ?  85  GLY   B H    1 
ATOM   5283 H  HA2  . GLY   B 1 85  ? 50.889 -13.434 -5.062  1.00 15.65 ?  85  GLY   B HA2  1 
ATOM   5284 H  HA3  . GLY   B 1 85  ? 50.665 -12.902 -6.519  1.00 15.65 ?  85  GLY   B HA3  1 
ATOM   5285 N  N    . HIS   B 1 86  ? 53.465 -11.932 -5.787  1.00 11.87 ?  86  HIS   B N    1 
ATOM   5286 C  CA   . HIS   B 1 86  ? 54.928 -12.095 -5.868  1.00 12.00 ?  86  HIS   B CA   1 
ATOM   5287 C  C    . HIS   B 1 86  ? 55.306 -12.606 -7.256  1.00 12.28 ?  86  HIS   B C    1 
ATOM   5288 O  O    . HIS   B 1 86  ? 54.920 -11.994 -8.265  1.00 13.04 ?  86  HIS   B O    1 
ATOM   5289 C  CB   . HIS   B 1 86  ? 55.432 -12.930 -4.689  1.00 12.51 ?  86  HIS   B CB   1 
ATOM   5290 C  CG   . HIS   B 1 86  ? 55.116 -12.317 -3.366  1.00 12.59 ?  86  HIS   B CG   1 
ATOM   5291 N  ND1  . HIS   B 1 86  ? 55.932 -11.382 -2.767  1.00 13.96 ?  86  HIS   B ND1  1 
ATOM   5292 C  CD2  . HIS   B 1 86  ? 54.047 -12.470 -2.550  1.00 12.87 ?  86  HIS   B CD2  1 
ATOM   5293 C  CE1  . HIS   B 1 86  ? 55.374 -10.986 -1.636  1.00 13.56 ?  86  HIS   B CE1  1 
ATOM   5294 N  NE2  . HIS   B 1 86  ? 54.229 -11.628 -1.483  1.00 12.91 ?  86  HIS   B NE2  1 
ATOM   5295 H  H    . HIS   B 1 86  ? 53.224 -11.134 -5.599  1.00 14.24 ?  86  HIS   B H    1 
ATOM   5296 H  HA   . HIS   B 1 86  ? 55.337 -11.223 -5.774  1.00 14.39 ?  86  HIS   B HA   1 
ATOM   5297 H  HB2  . HIS   B 1 86  ? 55.020 -13.809 -4.724  1.00 15.00 ?  86  HIS   B HB2  1 
ATOM   5298 H  HB3  . HIS   B 1 86  ? 56.400 -13.022 -4.755  1.00 15.00 ?  86  HIS   B HB3  1 
ATOM   5299 H  HD2  . HIS   B 1 86  ? 53.320 -13.035 -2.696  1.00 15.44 ?  86  HIS   B HD2  1 
ATOM   5300 H  HE1  . HIS   B 1 86  ? 55.738 -10.373 -1.043  1.00 16.26 ?  86  HIS   B HE1  1 
ATOM   5301 H  HE2  . HIS   B 1 86  ? 53.699 -11.552 -0.813  1.00 15.48 ?  86  HIS   B HE2  1 
ATOM   5302 N  N    . ASN   B 1 87  ? 56.077 -13.687 -7.361  1.00 12.80 ?  87  ASN   B N    1 
ATOM   5303 C  CA   . ASN   B 1 87  ? 56.478 -14.265 -8.635  1.00 13.68 ?  87  ASN   B CA   1 
ATOM   5304 C  C    . ASN   B 1 87  ? 55.495 -15.304 -9.142  1.00 13.42 ?  87  ASN   B C    1 
ATOM   5305 O  O    . ASN   B 1 87  ? 55.807 -16.005 -10.108 1.00 14.94 ?  87  ASN   B O    1 
ATOM   5306 C  CB   . ASN   B 1 87  ? 57.870 -14.901 -8.521  1.00 15.55 ?  87  ASN   B CB   1 
ATOM   5307 C  CG   . ASN   B 1 87  ? 57.940 -15.987 -7.454  1.00 16.34 ?  87  ASN   B CG   1 
ATOM   5308 O  OD1  . ASN   B 1 87  ? 57.290 -15.894 -6.409  1.00 15.36 ?  87  ASN   B OD1  1 
ATOM   5309 N  ND2  . ASN   B 1 87  ? 58.720 -17.039 -7.725  1.00 18.37 ?  87  ASN   B ND2  1 
ATOM   5310 H  H    . ASN   B 1 87  ? 56.386 -14.123 -6.686  1.00 15.34 ?  87  ASN   B H    1 
ATOM   5311 H  HA   . ASN   B 1 87  ? 56.529 -13.565 -9.296  1.00 16.40 ?  87  ASN   B HA   1 
ATOM   5312 H  HB2  . ASN   B 1 87  ? 58.109 -15.305 -9.376  1.00 18.65 ?  87  ASN   B HB2  1 
ATOM   5313 H  HB3  . ASN   B 1 87  ? 58.514 -14.214 -8.294  1.00 18.65 ?  87  ASN   B HB3  1 
ATOM   5314 H  HD21 . ASN   B 1 87  ? 58.801 -17.675 -7.153  1.00 22.04 ?  87  ASN   B HD21 1 
ATOM   5315 H  HD22 . ASN   B 1 87  ? 59.156 -17.077 -8.470  1.00 22.04 ?  87  ASN   B HD22 1 
ATOM   5316 N  N    . LEU   B 1 88  ? 54.319 -15.412 -8.524  1.00 12.12 ?  88  LEU   B N    1 
ATOM   5317 C  CA   . LEU   B 1 88  ? 53.339 -16.442 -8.851  1.00 12.58 ?  88  LEU   B CA   1 
ATOM   5318 C  C    . LEU   B 1 88  ? 52.101 -15.923 -9.565  1.00 12.20 ?  88  LEU   B C    1 
ATOM   5319 O  O    . LEU   B 1 88  ? 51.501 -16.664 -10.354 1.00 13.87 ?  88  LEU   B O    1 
ATOM   5320 C  CB   . LEU   B 1 88  ? 52.875 -17.129 -7.564  1.00 13.50 ?  88  LEU   B CB   1 
ATOM   5321 C  CG   . LEU   B 1 88  ? 54.005 -17.775 -6.769  1.00 15.87 ?  88  LEU   B CG   1 
ATOM   5322 C  CD1  . LEU   B 1 88  ? 53.527 -18.156 -5.375  1.00 17.18 ?  88  LEU   B CD1  1 
ATOM   5323 C  CD2  . LEU   B 1 88  ? 54.536 -18.985 -7.512  1.00 19.30 ?  88  LEU   B CD2  1 
ATOM   5324 H  H    . LEU   B 1 88  ? 54.058 -14.888 -7.889  1.00 14.53 ?  88  LEU   B H    1 
ATOM   5325 H  HA   . LEU   B 1 88  ? 53.755 -17.109 -9.415  1.00 15.09 ?  88  LEU   B HA   1 
ATOM   5326 H  HB2  . LEU   B 1 88  ? 52.449 -16.471 -6.991  1.00 16.19 ?  88  LEU   B HB2  1 
ATOM   5327 H  HB3  . LEU   B 1 88  ? 52.236 -17.825 -7.792  1.00 16.19 ?  88  LEU   B HB3  1 
ATOM   5328 H  HG   . LEU   B 1 88  ? 54.728 -17.139 -6.674  1.00 19.03 ?  88  LEU   B HG   1 
ATOM   5329 H  HD11 . LEU   B 1 88  ? 54.218 -18.679 -4.940  1.00 20.61 ?  88  LEU   B HD11 1 
ATOM   5330 H  HD12 . LEU   B 1 88  ? 53.356 -17.346 -4.869  1.00 20.61 ?  88  LEU   B HD12 1 
ATOM   5331 H  HD13 . LEU   B 1 88  ? 52.715 -18.676 -5.454  1.00 20.61 ?  88  LEU   B HD13 1 
ATOM   5332 H  HD21 . LEU   B 1 88  ? 55.182 -19.441 -6.948  1.00 23.14 ?  88  LEU   B HD21 1 
ATOM   5333 H  HD22 . LEU   B 1 88  ? 53.798 -19.581 -7.715  1.00 23.14 ?  88  LEU   B HD22 1 
ATOM   5334 H  HD23 . LEU   B 1 88  ? 54.962 -18.693 -8.332  1.00 23.14 ?  88  LEU   B HD23 1 
ATOM   5335 N  N    . ALA   B 1 89  ? 51.696 -14.689 -9.295  1.00 11.60 ?  89  ALA   B N    1 
ATOM   5336 C  CA   . ALA   B 1 89  ? 50.401 -14.195 -9.735  1.00 11.31 ?  89  ALA   B CA   1 
ATOM   5337 C  C    . ALA   B 1 89  ? 50.385 -12.707 -9.450  1.00 11.68 ?  89  ALA   B C    1 
ATOM   5338 O  O    . ALA   B 1 89  ? 51.218 -12.202 -8.698  1.00 12.02 ?  89  ALA   B O    1 
ATOM   5339 C  CB   . ALA   B 1 89  ? 49.275 -14.871 -8.962  1.00 11.15 ?  89  ALA   B CB   1 
ATOM   5340 H  H    . ALA   B 1 89  ? 52.158 -14.109 -8.861  1.00 13.90 ?  89  ALA   B H    1 
ATOM   5341 H  HA   . ALA   B 1 89  ? 50.278 -14.348 -10.689 1.00 13.56 ?  89  ALA   B HA   1 
ATOM   5342 H  HB1  . ALA   B 1 89  ? 48.426 -14.531 -9.276  1.00 13.37 ?  89  ALA   B HB1  1 
ATOM   5343 H  HB2  . ALA   B 1 89  ? 49.323 -15.832 -9.109  1.00 13.37 ?  89  ALA   B HB2  1 
ATOM   5344 H  HB3  . ALA   B 1 89  ? 49.385 -14.679 -8.018  1.00 13.37 ?  89  ALA   B HB3  1 
ATOM   5345 N  N    . LYS   B 1 90  ? 49.419 -12.002 -10.031 1.00 12.59 ?  90  LYS   B N    1 
ATOM   5346 C  CA   . LYS   B 1 90  ? 49.236 -10.615 -9.624  1.00 12.84 ?  90  LYS   B CA   1 
ATOM   5347 C  C    . LYS   B 1 90  ? 48.906 -10.539 -8.136  1.00 12.17 ?  90  LYS   B C    1 
ATOM   5348 O  O    . LYS   B 1 90  ? 49.541 -9.788  -7.379  1.00 12.83 ?  90  LYS   B O    1 
ATOM   5349 C  CB   . LYS   B 1 90  ? 48.168 -9.948  -10.489 1.00 13.74 ?  90  LYS   B CB   1 
ATOM   5350 C  CG   . LYS   B 1 90  ? 47.854 -8.519  -10.088 1.00 13.99 ?  90  LYS   B CG   1 
ATOM   5351 C  CD   . LYS   B 1 90  ? 49.049 -7.606  -10.156 1.00 16.09 ?  90  LYS   B CD   1 
ATOM   5352 C  CE   . LYS   B 1 90  ? 48.564 -6.204  -9.887  1.00 18.05 ?  90  LYS   B CE   1 
ATOM   5353 N  NZ   . LYS   B 1 90  ? 49.665 -5.217  -9.803  1.00 17.63 ?  90  LYS   B NZ   1 
ATOM   5354 H  H    . LYS   B 1 90  ? 48.883 -12.294 -10.635 1.00 15.09 ?  90  LYS   B H    1 
ATOM   5355 H  HA   . LYS   B 1 90  ? 50.066 -10.142 -9.762  1.00 15.40 ?  90  LYS   B HA   1 
ATOM   5356 H  HB2  . LYS   B 1 90  ? 48.480 -9.932  -11.411 1.00 16.47 ?  90  LYS   B HB2  1 
ATOM   5357 H  HB3  . LYS   B 1 90  ? 47.349 -10.463 -10.434 1.00 16.47 ?  90  LYS   B HB3  1 
ATOM   5358 H  HG2  . LYS   B 1 90  ? 47.174 -8.167  -10.685 1.00 16.78 ?  90  LYS   B HG2  1 
ATOM   5359 H  HG3  . LYS   B 1 90  ? 47.517 -8.510  -9.174  1.00 16.78 ?  90  LYS   B HG3  1 
ATOM   5360 H  HD2  . LYS   B 1 90  ? 49.698 -7.847  -9.474  1.00 19.30 ?  90  LYS   B HD2  1 
ATOM   5361 H  HD3  . LYS   B 1 90  ? 49.447 -7.638  -11.040 1.00 19.30 ?  90  LYS   B HD3  1 
ATOM   5362 H  HE2  . LYS   B 1 90  ? 47.976 -5.923  -10.608 1.00 21.65 ?  90  LYS   B HE2  1 
ATOM   5363 H  HE3  . LYS   B 1 90  ? 48.087 -6.181  -9.044  1.00 21.65 ?  90  LYS   B HE3  1 
ATOM   5364 H  HZ1  . LYS   B 1 90  ? 49.340 -4.400  -9.646  1.00 21.15 ?  90  LYS   B HZ1  1 
ATOM   5365 H  HZ2  . LYS   B 1 90  ? 50.223 -5.433  -9.144  1.00 21.15 ?  90  LYS   B HZ2  1 
ATOM   5366 H  HZ3  . LYS   B 1 90  ? 50.121 -5.197  -10.570 1.00 21.15 ?  90  LYS   B HZ3  1 
ATOM   5367 N  N    . HIS   B 1 91  ? 47.932 -11.348 -7.697  1.00 10.71 ?  91  HIS   B N    1 
ATOM   5368 C  CA   . HIS   B 1 91  ? 47.453 -11.373 -6.327  1.00 10.84 ?  91  HIS   B CA   1 
ATOM   5369 C  C    . HIS   B 1 91  ? 47.439 -12.799 -5.805  1.00 10.30 ?  91  HIS   B C    1 
ATOM   5370 O  O    . HIS   B 1 91  ? 47.218 -13.754 -6.560  1.00 10.90 ?  91  HIS   B O    1 
ATOM   5371 C  CB   . HIS   B 1 91  ? 46.002 -10.875 -6.221  1.00 12.61 ?  91  HIS   B CB   1 
ATOM   5372 C  CG   . HIS   B 1 91  ? 45.808 -9.461  -6.640  1.00 15.50 ?  91  HIS   B CG   1 
ATOM   5373 N  ND1  . HIS   B 1 91  ? 46.441 -8.402  -6.025  1.00 17.72 ?  91  HIS   B ND1  1 
ATOM   5374 C  CD2  . HIS   B 1 91  ? 45.019 -8.923  -7.596  1.00 17.60 ?  91  HIS   B CD2  1 
ATOM   5375 C  CE1  . HIS   B 1 91  ? 46.069 -7.271  -6.600  1.00 18.71 ?  91  HIS   B CE1  1 
ATOM   5376 N  NE2  . HIS   B 1 91  ? 45.203 -7.561  -7.554  1.00 18.68 ?  91  HIS   B NE2  1 
ATOM   5377 H  H    . HIS   B 1 91  ? 47.517 -11.909 -8.204  1.00 12.85 ?  91  HIS   B H    1 
ATOM   5378 H  HA   . HIS   B 1 91  ? 48.023 -10.820 -5.761  1.00 12.99 ?  91  HIS   B HA   1 
ATOM   5379 H  HB2  . HIS   B 1 91  ? 45.437 -11.424 -6.786  1.00 15.12 ?  91  HIS   B HB2  1 
ATOM   5380 H  HB3  . HIS   B 1 91  ? 45.708 -10.946 -5.297  1.00 15.12 ?  91  HIS   B HB3  1 
ATOM   5381 H  HD1  . HIS   B 1 91  ? 46.999 -8.463  -5.373  1.00 21.26 ?  91  HIS   B HD1  1 
ATOM   5382 H  HD2  . HIS   B 1 91  ? 44.466 -9.373  -8.185  1.00 21.11 ?  91  HIS   B HD2  1 
ATOM   5383 H  HE1  . HIS   B 1 91  ? 46.364 -6.413  -6.365  1.00 22.44 ?  91  HIS   B HE1  1 
ATOM   5384 N  N    . CYS   B 1 92  ? 47.624 -12.929 -4.498  1.00 10.09 ?  92  CYS   B N    1 
ATOM   5385 C  CA   . CYS   B 1 92  ? 47.330 -14.165 -3.787  1.00 10.16 ?  92  CYS   B CA   1 
ATOM   5386 C  C    . CYS   B 1 92  ? 46.107 -13.926 -2.910  1.00 9.63  ?  92  CYS   B C    1 
ATOM   5387 O  O    . CYS   B 1 92  ? 46.107 -13.017 -2.070  1.00 10.42 ?  92  CYS   B O    1 
ATOM   5388 C  CB   . CYS   B 1 92  ? 48.511 -14.628 -2.936  1.00 10.51 ?  92  CYS   B CB   1 
ATOM   5389 S  SG   . CYS   B 1 92  ? 48.140 -16.166 -2.035  1.00 10.57 ?  92  CYS   B SG   1 
ATOM   5390 H  H    . CYS   B 1 92  ? 47.940 -12.302 -3.992  1.00 12.10 ?  92  CYS   B H    1 
ATOM   5391 H  HA   . CYS   B 1 92  ? 47.128 -14.858 -4.432  1.00 12.19 ?  92  CYS   B HA   1 
ATOM   5392 H  HB2  . CYS   B 1 92  ? 49.274 -14.789 -3.509  1.00 12.60 ?  92  CYS   B HB2  1 
ATOM   5393 H  HB3  . CYS   B 1 92  ? 48.719 -13.938 -2.286  1.00 12.60 ?  92  CYS   B HB3  1 
ATOM   5394 H  HG   . CYS   B 1 92  ? 49.107 -16.486 -1.401  1.00 12.67 ?  92  CYS   B HG   1 
ATOM   5395 N  N    . LEU   B 1 93  ? 45.069 -14.738 -3.117  1.00 9.55  ?  93  LEU   B N    1 
ATOM   5396 C  CA   . LEU   B 1 93  ? 43.890 -14.742 -2.262  1.00 9.91  ?  93  LEU   B CA   1 
ATOM   5397 C  C    . LEU   B 1 93  ? 44.116 -15.807 -1.196  1.00 9.43  ?  93  LEU   B C    1 
ATOM   5398 O  O    . LEU   B 1 93  ? 44.071 -17.008 -1.490  1.00 9.90  ?  93  LEU   B O    1 
ATOM   5399 C  CB   . LEU   B 1 93  ? 42.628 -15.033 -3.071  1.00 10.37 ?  93  LEU   B CB   1 
ATOM   5400 C  CG   . LEU   B 1 93  ? 41.328 -15.051 -2.263  1.00 10.88 ?  93  LEU   B CG   1 
ATOM   5401 C  CD1  . LEU   B 1 93  ? 40.966 -13.673 -1.760  1.00 11.53 ?  93  LEU   B CD1  1 
ATOM   5402 C  CD2  . LEU   B 1 93  ? 40.198 -15.640 -3.094  1.00 11.41 ?  93  LEU   B CD2  1 
ATOM   5403 H  H    . LEU   B 1 93  ? 45.036 -15.317 -3.763  1.00 11.45 ?  93  LEU   B H    1 
ATOM   5404 H  HA   . LEU   B 1 93  ? 43.800 -13.884 -1.834  1.00 11.88 ?  93  LEU   B HA   1 
ATOM   5405 H  HB2  . LEU   B 1 93  ? 42.540 -14.347 -3.754  1.00 12.43 ?  93  LEU   B HB2  1 
ATOM   5406 H  HB3  . LEU   B 1 93  ? 42.723 -15.899 -3.494  1.00 12.43 ?  93  LEU   B HB3  1 
ATOM   5407 H  HG   . LEU   B 1 93  ? 41.451 -15.619 -1.488  1.00 13.04 ?  93  LEU   B HG   1 
ATOM   5408 H  HD11 . LEU   B 1 93  ? 40.115 -13.719 -1.294  1.00 13.82 ?  93  LEU   B HD11 1 
ATOM   5409 H  HD12 . LEU   B 1 93  ? 41.657 -13.362 -1.154  1.00 13.82 ?  93  LEU   B HD12 1 
ATOM   5410 H  HD13 . LEU   B 1 93  ? 40.894 -13.067 -2.517  1.00 13.82 ?  93  LEU   B HD13 1 
ATOM   5411 H  HD21 . LEU   B 1 93  ? 39.379 -15.627 -2.573  1.00 13.68 ?  93  LEU   B HD21 1 
ATOM   5412 H  HD22 . LEU   B 1 93  ? 40.085 -15.114 -3.900  1.00 13.68 ?  93  LEU   B HD22 1 
ATOM   5413 H  HD23 . LEU   B 1 93  ? 40.422 -16.557 -3.328  1.00 13.68 ?  93  LEU   B HD23 1 
ATOM   5414 N  N    . HIS   B 1 94  ? 44.388 -15.369 0.030   1.00 9.59  ?  94  HIS   B N    1 
ATOM   5415 C  CA   . HIS   B 1 94  ? 44.603 -16.277 1.150   1.00 9.65  ?  94  HIS   B CA   1 
ATOM   5416 C  C    . HIS   B 1 94  ? 43.240 -16.626 1.727   1.00 9.81  ?  94  HIS   B C    1 
ATOM   5417 O  O    . HIS   B 1 94  ? 42.563 -15.748 2.267   1.00 11.09 ?  94  HIS   B O    1 
ATOM   5418 C  CB   . HIS   B 1 94  ? 45.473 -15.604 2.207   1.00 10.20 ?  94  HIS   B CB   1 
ATOM   5419 C  CG   . HIS   B 1 94  ? 46.853 -15.305 1.736   1.00 9.76  ?  94  HIS   B CG   1 
ATOM   5420 N  ND1  . HIS   B 1 94  ? 47.880 -16.221 1.823   1.00 10.06 ?  94  HIS   B ND1  1 
ATOM   5421 C  CD2  . HIS   B 1 94  ? 47.362 -14.198 1.142   1.00 10.20 ?  94  HIS   B CD2  1 
ATOM   5422 C  CE1  . HIS   B 1 94  ? 48.971 -15.671 1.319   1.00 10.07 ?  94  HIS   B CE1  1 
ATOM   5423 N  NE2  . HIS   B 1 94  ? 48.685 -14.447 0.896   1.00 10.49 ?  94  HIS   B NE2  1 
ATOM   5424 H  H    . HIS   B 1 94  ? 44.452 -14.535 0.236   1.00 11.50 ?  94  HIS   B H    1 
ATOM   5425 H  HA   . HIS   B 1 94  ? 45.040 -17.085 0.840   1.00 11.57 ?  94  HIS   B HA   1 
ATOM   5426 H  HB2  . HIS   B 1 94  ? 45.058 -14.766 2.464   1.00 12.23 ?  94  HIS   B HB2  1 
ATOM   5427 H  HB3  . HIS   B 1 94  ? 45.539 -16.192 2.973   1.00 12.23 ?  94  HIS   B HB3  1 
ATOM   5428 H  HD2  . HIS   B 1 94  ? 46.908 -13.417 0.945   1.00 12.23 ?  94  HIS   B HD2  1 
ATOM   5429 H  HE1  . HIS   B 1 94  ? 49.804 -16.091 1.264   1.00 12.07 ?  94  HIS   B HE1  1 
ATOM   5430 H  HE2  . HIS   B 1 94  ? 49.246 -13.912 0.529   1.00 12.57 ?  94  HIS   B HE2  1 
ATOM   5431 N  N    . VAL   B 1 95  ? 42.812 -17.882 1.583   1.00 9.77  ?  95  VAL   B N    1 
ATOM   5432 C  CA   . VAL   B 1 95  ? 41.479 -18.313 2.004   1.00 10.05 ?  95  VAL   B CA   1 
ATOM   5433 C  C    . VAL   B 1 95  ? 41.635 -19.348 3.099   1.00 10.30 ?  95  VAL   B C    1 
ATOM   5434 O  O    . VAL   B 1 95  ? 42.407 -20.303 2.945   1.00 10.71 ?  95  VAL   B O    1 
ATOM   5435 C  CB   . VAL   B 1 95  ? 40.664 -18.918 0.846   1.00 10.47 ?  95  VAL   B CB   1 
ATOM   5436 C  CG1  . VAL   B 1 95  ? 39.296 -19.357 1.344   1.00 11.54 ?  95  VAL   B CG1  1 
ATOM   5437 C  CG2  . VAL   B 1 95  ? 40.530 -17.930 -0.286  1.00 10.48 ?  95  VAL   B CG2  1 
ATOM   5438 H  H    . VAL   B 1 95  ? 43.280 -18.513 1.223   1.00 11.71 ?  95  VAL   B H    1 
ATOM   5439 H  HA   . VAL   B 1 95  ? 40.989 -17.555 2.356   1.00 12.05 ?  95  VAL   B HA   1 
ATOM   5440 H  HB   . VAL   B 1 95  ? 41.121 -19.698 0.503   1.00 12.55 ?  95  VAL   B HB   1 
ATOM   5441 H  HG11 . VAL   B 1 95  ? 38.712 -19.516 0.581   1.00 13.83 ?  95  VAL   B HG11 1 
ATOM   5442 H  HG12 . VAL   B 1 95  ? 39.387 -20.173 1.859   1.00 13.83 ?  95  VAL   B HG12 1 
ATOM   5443 H  HG13 . VAL   B 1 95  ? 38.916 -18.655 1.900   1.00 13.83 ?  95  VAL   B HG13 1 
ATOM   5444 H  HG21 . VAL   B 1 95  ? 39.953 -18.313 -0.968  1.00 12.56 ?  95  VAL   B HG21 1 
ATOM   5445 H  HG22 . VAL   B 1 95  ? 40.133 -17.114 0.058   1.00 12.56 ?  95  VAL   B HG22 1 
ATOM   5446 H  HG23 . VAL   B 1 95  ? 41.405 -17.752 -0.650  1.00 12.56 ?  95  VAL   B HG23 1 
ATOM   5447 N  N    . VAL   B 1 96  ? 40.907 -19.167 4.196   1.00 10.72 ?  96  VAL   B N    1 
ATOM   5448 C  CA   . VAL   B 1 96  ? 40.989 -20.078 5.336   1.00 11.19 ?  96  VAL   B CA   1 
ATOM   5449 C  C    . VAL   B 1 96  ? 39.797 -21.033 5.293   1.00 11.62 ?  96  VAL   B C    1 
ATOM   5450 O  O    . VAL   B 1 96  ? 38.684 -20.675 5.686   1.00 12.29 ?  96  VAL   B O    1 
ATOM   5451 C  CB   . VAL   B 1 96  ? 41.048 -19.326 6.669   1.00 11.80 ?  96  VAL   B CB   1 
ATOM   5452 C  CG1  . VAL   B 1 96  ? 41.198 -20.315 7.815   1.00 12.59 ?  96  VAL   B CG1  1 
ATOM   5453 C  CG2  . VAL   B 1 96  ? 42.173 -18.292 6.675   1.00 12.01 ?  96  VAL   B CG2  1 
ATOM   5454 H  H    . VAL   B 1 96  ? 40.346 -18.520 4.307   1.00 12.86 ?  96  VAL   B H    1 
ATOM   5455 H  HA   . VAL   B 1 96  ? 41.798 -20.604 5.259   1.00 13.41 ?  96  VAL   B HA   1 
ATOM   5456 H  HB   . VAL   B 1 96  ? 40.211 -18.852 6.797   1.00 14.15 ?  96  VAL   B HB   1 
ATOM   5457 H  HG11 . VAL   B 1 96  ? 41.402 -19.827 8.630   1.00 15.10 ?  96  VAL   B HG11 1 
ATOM   5458 H  HG12 . VAL   B 1 96  ? 40.367 -20.805 7.928   1.00 15.10 ?  96  VAL   B HG12 1 
ATOM   5459 H  HG13 . VAL   B 1 96  ? 41.920 -20.930 7.612   1.00 15.10 ?  96  VAL   B HG13 1 
ATOM   5460 H  HG21 . VAL   B 1 96  ? 42.219 -17.878 7.552   1.00 14.41 ?  96  VAL   B HG21 1 
ATOM   5461 H  HG22 . VAL   B 1 96  ? 43.009 -18.731 6.469   1.00 14.41 ?  96  VAL   B HG22 1 
ATOM   5462 H  HG23 . VAL   B 1 96  ? 41.981 -17.613 6.004   1.00 14.41 ?  96  VAL   B HG23 1 
ATOM   5463 N  N    . GLY   B 1 97  ? 40.027 -22.265 4.844   1.00 11.94 ?  97  GLY   B N    1 
ATOM   5464 C  CA   . GLY   B 1 97  ? 39.055 -23.321 5.011   1.00 12.36 ?  97  GLY   B CA   1 
ATOM   5465 C  C    . GLY   B 1 97  ? 39.187 -23.939 6.384   1.00 13.54 ?  97  GLY   B C    1 
ATOM   5466 O  O    . GLY   B 1 97  ? 40.230 -23.814 7.037   1.00 13.89 ?  97  GLY   B O    1 
ATOM   5467 H  H    . GLY   B 1 97  ? 40.754 -22.505 4.439   1.00 14.31 ?  97  GLY   B H    1 
ATOM   5468 H  HA2  . GLY   B 1 97  ? 38.164 -22.954 4.903   1.00 14.82 ?  97  GLY   B HA2  1 
ATOM   5469 H  HA3  . GLY   B 1 97  ? 39.197 -24.005 4.336   1.00 14.82 ?  97  GLY   B HA3  1 
ATOM   5470 N  N    . PRO   B 1 98  ? 38.138 -24.613 6.856   1.00 14.56 ?  98  PRO   B N    1 
ATOM   5471 C  CA   . PRO   B 1 98  ? 38.231 -25.300 8.148   1.00 15.48 ?  98  PRO   B CA   1 
ATOM   5472 C  C    . PRO   B 1 98  ? 39.255 -26.423 8.109   1.00 15.12 ?  98  PRO   B C    1 
ATOM   5473 O  O    . PRO   B 1 98  ? 39.360 -27.162 7.131   1.00 15.44 ?  98  PRO   B O    1 
ATOM   5474 C  CB   . PRO   B 1 98  ? 36.813 -25.842 8.360   1.00 16.14 ?  98  PRO   B CB   1 
ATOM   5475 C  CG   . PRO   B 1 98  ? 36.247 -25.972 6.999   1.00 15.76 ?  98  PRO   B CG   1 
ATOM   5476 C  CD   . PRO   B 1 98  ? 36.819 -24.811 6.225   1.00 14.88 ?  98  PRO   B CD   1 
ATOM   5477 H  HA   . PRO   B 1 98  ? 38.455 -24.673 8.850   1.00 18.57 ?  98  PRO   B HA   1 
ATOM   5478 H  HB2  . PRO   B 1 98  ? 36.856 -26.707 8.796   1.00 19.36 ?  98  PRO   B HB2  1 
ATOM   5479 H  HB3  . PRO   B 1 98  ? 36.297 -25.213 8.885   1.00 19.36 ?  98  PRO   B HB3  1 
ATOM   5480 H  HG2  . PRO   B 1 98  ? 36.526 -26.817 6.608   1.00 18.90 ?  98  PRO   B HG2  1 
ATOM   5481 H  HG3  . PRO   B 1 98  ? 35.281 -25.917 7.039   1.00 18.90 ?  98  PRO   B HG3  1 
ATOM   5482 H  HD2  . PRO   B 1 98  ? 36.915 -25.045 5.284   1.00 17.85 ?  98  PRO   B HD2  1 
ATOM   5483 H  HD3  . PRO   B 1 98  ? 36.269 -24.022 6.338   1.00 17.85 ?  98  PRO   B HD3  1 
ATOM   5484 N  N    . ASN   B 1 99  ? 40.011 -26.544 9.193   1.00 16.42 ?  99  ASN   B N    1 
ATOM   5485 C  CA   . ASN   B 1 99  ? 40.991 -27.615 9.357   1.00 17.83 ?  99  ASN   B CA   1 
ATOM   5486 C  C    . ASN   B 1 99  ? 40.364 -28.694 10.236  1.00 20.80 ?  99  ASN   B C    1 
ATOM   5487 O  O    . ASN   B 1 99  ? 40.298 -28.550 11.459  1.00 21.05 ?  99  ASN   B O    1 
ATOM   5488 C  CB   . ASN   B 1 99  ? 42.271 -27.061 9.972   1.00 18.04 ?  99  ASN   B CB   1 
ATOM   5489 C  CG   . ASN   B 1 99  ? 43.404 -28.067 9.967   1.00 18.91 ?  99  ASN   B CG   1 
ATOM   5490 O  OD1  . ASN   B 1 99  ? 43.188 -29.258 10.155  1.00 19.78 ?  99  ASN   B OD1  1 
ATOM   5491 N  ND2  . ASN   B 1 99  ? 44.618 -27.591 9.749   1.00 19.22 ?  99  ASN   B ND2  1 
ATOM   5492 H  H    . ASN   B 1 99  ? 39.972 -26.006 9.859   1.00 19.69 ?  99  ASN   B H    1 
ATOM   5493 H  HA   . ASN   B 1 99  ? 41.198 -28.006 8.495   1.00 21.39 ?  99  ASN   B HA   1 
ATOM   5494 H  HB2  . ASN   B 1 99  ? 42.549 -26.289 9.473   1.00 21.63 ?  99  ASN   B HB2  1 
ATOM   5495 H  HB3  . ASN   B 1 99  ? 42.089 -26.821 10.898  1.00 21.63 ?  99  ASN   B HB3  1 
ATOM   5496 H  HD21 . ASN   B 1 99  ? 45.292 -28.121 9.735   1.00 23.05 ?  99  ASN   B HD21 1 
ATOM   5497 H  HD22 . ASN   B 1 99  ? 44.724 -26.748 9.627   1.00 23.05 ?  99  ASN   B HD22 1 
ATOM   5498 N  N    A VAL   B 1 100 ? 39.897 -29.775 9.605   0.50 23.04 ?  100 VAL   B N    1 
ATOM   5499 N  N    B VAL   B 1 100 ? 39.902 -29.775 9.600   0.50 23.05 ?  100 VAL   B N    1 
ATOM   5500 C  CA   A VAL   B 1 100 ? 39.276 -30.864 10.355  0.50 25.64 ?  100 VAL   B CA   1 
ATOM   5501 C  CA   B VAL   B 1 100 ? 39.277 -30.875 10.332  0.50 25.63 ?  100 VAL   B CA   1 
ATOM   5502 C  C    A VAL   B 1 100 ? 40.284 -31.520 11.289  0.50 26.18 ?  100 VAL   B C    1 
ATOM   5503 C  C    B VAL   B 1 100 ? 40.276 -31.547 11.266  0.50 26.11 ?  100 VAL   B C    1 
ATOM   5504 O  O    A VAL   B 1 100 ? 39.924 -31.979 12.381  0.50 26.89 ?  100 VAL   B O    1 
ATOM   5505 O  O    B VAL   B 1 100 ? 39.900 -32.048 12.334  0.50 26.69 ?  100 VAL   B O    1 
ATOM   5506 C  CB   A VAL   B 1 100 ? 38.627 -31.878 9.391   0.50 27.48 ?  100 VAL   B CB   1 
ATOM   5507 C  CB   B VAL   B 1 100 ? 38.640 -31.869 9.339   0.50 27.49 ?  100 VAL   B CB   1 
ATOM   5508 C  CG1  A VAL   B 1 100 ? 38.151 -33.110 10.145  0.50 28.24 ?  100 VAL   B CG1  1 
ATOM   5509 C  CG1  B VAL   B 1 100 ? 38.141 -33.110 10.059  0.50 28.24 ?  100 VAL   B CG1  1 
ATOM   5510 C  CG2  A VAL   B 1 100 ? 37.468 -31.227 8.651   0.50 28.02 ?  100 VAL   B CG2  1 
ATOM   5511 C  CG2  B VAL   B 1 100 ? 37.501 -31.198 8.583   0.50 28.03 ?  100 VAL   B CG2  1 
ATOM   5512 H  H    A VAL   B 1 100 ? 39.930 -29.900 8.753   0.50 27.63 ?  100 VAL   B H    1 
ATOM   5513 H  H    B VAL   B 1 100 ? 39.934 -29.891 8.746   0.50 27.64 ?  100 VAL   B H    1 
ATOM   5514 H  HA   A VAL   B 1 100 ? 38.564 -30.494 10.900  0.50 30.75 ?  100 VAL   B HA   1 
ATOM   5515 H  HA   B VAL   B 1 100 ? 38.560 -30.515 10.875  0.50 30.74 ?  100 VAL   B HA   1 
ATOM   5516 H  HB   A VAL   B 1 100 ? 39.284 -32.161 8.735   0.50 32.97 ?  100 VAL   B HB   1 
ATOM   5517 H  HB   B VAL   B 1 100 ? 39.307 -32.145 8.690   0.50 32.97 ?  100 VAL   B HB   1 
ATOM   5518 H  HG11 A VAL   B 1 100 ? 37.551 -33.616 9.574   0.50 33.87 ?  100 VAL   B HG11 1 
ATOM   5519 H  HG11 B VAL   B 1 100 ? 37.558 -33.607 9.463   0.50 33.88 ?  100 VAL   B HG11 1 
ATOM   5520 H  HG12 A VAL   B 1 100 ? 38.918 -33.656 10.381  0.50 33.87 ?  100 VAL   B HG12 1 
ATOM   5521 H  HG12 B VAL   B 1 100 ? 38.900 -33.660 10.308  0.50 33.88 ?  100 VAL   B HG12 1 
ATOM   5522 H  HG13 A VAL   B 1 100 ? 37.683 -32.829 10.947  0.50 33.87 ?  100 VAL   B HG13 1 
ATOM   5523 H  HG13 B VAL   B 1 100 ? 37.650 -32.840 10.850  0.50 33.88 ?  100 VAL   B HG13 1 
ATOM   5524 H  HG21 A VAL   B 1 100 ? 37.065 -31.880 8.059   0.50 33.62 ?  100 VAL   B HG21 1 
ATOM   5525 H  HG21 B VAL   B 1 100 ? 37.096 -31.843 7.983   0.50 33.62 ?  100 VAL   B HG21 1 
ATOM   5526 H  HG22 A VAL   B 1 100 ? 36.814 -30.920 9.299   0.50 33.62 ?  100 VAL   B HG22 1 
ATOM   5527 H  HG22 B VAL   B 1 100 ? 36.843 -30.882 9.222   0.50 33.62 ?  100 VAL   B HG22 1 
ATOM   5528 H  HG23 A VAL   B 1 100 ? 37.804 -30.476 8.138   0.50 33.62 ?  100 VAL   B HG23 1 
ATOM   5529 H  HG23 B VAL   B 1 100 ? 37.855 -30.451 8.076   0.50 33.62 ?  100 VAL   B HG23 1 
ATOM   5530 N  N    . ASN   B 1 101 ? 41.555 -31.580 10.884  1.00 26.55 ?  101 ASN   B N    1 
ATOM   5531 C  CA   . ASN   B 1 101 ? 42.588 -32.121 11.764  1.00 28.64 ?  101 ASN   B CA   1 
ATOM   5532 C  C    . ASN   B 1 101 ? 42.760 -31.284 13.027  1.00 32.22 ?  101 ASN   B C    1 
ATOM   5533 O  O    . ASN   B 1 101 ? 43.368 -31.759 13.994  1.00 32.92 ?  101 ASN   B O    1 
ATOM   5534 C  CB   . ASN   B 1 101 ? 43.914 -32.254 11.011  1.00 27.90 ?  101 ASN   B CB   1 
ATOM   5535 C  CG   . ASN   B 1 101 ? 43.910 -33.412 10.028  1.00 27.11 ?  101 ASN   B CG   1 
ATOM   5536 O  OD1  . ASN   B 1 101 ? 43.213 -34.404 10.230  1.00 27.59 ?  101 ASN   B OD1  1 
ATOM   5537 N  ND2  . ASN   B 1 101 ? 44.682 -33.287 8.956   1.00 26.68 ?  101 ASN   B ND2  1 
ATOM   5538 H  H    A ASN   B 1 101 ? 41.833 -31.326 10.110  0.50 31.85 ?  101 ASN   B H    1 
ATOM   5539 H  H    B ASN   B 1 101 ? 41.841 -31.305 10.120  0.50 31.85 ?  101 ASN   B H    1 
ATOM   5540 H  HA   . ASN   B 1 101 ? 42.320 -33.006 12.040  1.00 34.36 ?  101 ASN   B HA   1 
ATOM   5541 H  HB2  . ASN   B 1 101 ? 44.087 -31.442 10.512  1.00 33.47 ?  101 ASN   B HB2  1 
ATOM   5542 H  HB3  . ASN   B 1 101 ? 44.627 -32.407 11.651  1.00 33.47 ?  101 ASN   B HB3  1 
ATOM   5543 H  HD21 . ASN   B 1 101 ? 44.713 -33.920 8.373   1.00 32.00 ?  101 ASN   B HD21 1 
ATOM   5544 H  HD22 . ASN   B 1 101 ? 45.154 -32.578 8.847   1.00 32.00 ?  101 ASN   B HD22 1 
ATOM   5545 N  N    A LYS   B 1 102 ? 42.243 -30.054 13.036  0.50 34.15 ?  102 LYS   B N    1 
ATOM   5546 N  N    B LYS   B 1 102 ? 42.244 -30.055 13.039  0.50 34.13 ?  102 LYS   B N    1 
ATOM   5547 C  CA   A LYS   B 1 102 ? 42.203 -29.213 14.225  0.50 36.26 ?  102 LYS   B CA   1 
ATOM   5548 C  CA   B LYS   B 1 102 ? 42.207 -29.226 14.235  0.50 36.23 ?  102 LYS   B CA   1 
ATOM   5549 C  C    A LYS   B 1 102 ? 40.824 -29.189 14.873  0.50 35.82 ?  102 LYS   B C    1 
ATOM   5550 C  C    B LYS   B 1 102 ? 40.816 -29.169 14.855  0.50 35.77 ?  102 LYS   B C    1 
ATOM   5551 O  O    A LYS   B 1 102 ? 40.601 -28.406 15.801  0.50 35.89 ?  102 LYS   B O    1 
ATOM   5552 O  O    B LYS   B 1 102 ? 40.577 -28.346 15.744  0.50 35.76 ?  102 LYS   B O    1 
ATOM   5553 C  CB   A LYS   B 1 102 ? 42.618 -27.781 13.881  0.50 38.75 ?  102 LYS   B CB   1 
ATOM   5554 C  CB   B LYS   B 1 102 ? 42.684 -27.807 13.919  0.50 38.76 ?  102 LYS   B CB   1 
ATOM   5555 C  CG   A LYS   B 1 102 ? 44.075 -27.596 13.500  0.50 41.06 ?  102 LYS   B CG   1 
ATOM   5556 C  CG   B LYS   B 1 102 ? 44.149 -27.701 13.533  0.50 41.15 ?  102 LYS   B CG   1 
ATOM   5557 C  CD   A LYS   B 1 102 ? 44.332 -26.140 13.140  0.50 43.02 ?  102 LYS   B CD   1 
ATOM   5558 C  CD   B LYS   B 1 102 ? 44.486 -26.281 13.111  0.50 43.21 ?  102 LYS   B CD   1 
ATOM   5559 C  CE   A LYS   B 1 102 ? 45.793 -25.870 12.835  0.50 44.42 ?  102 LYS   B CE   1 
ATOM   5560 C  CE   B LYS   B 1 102 ? 45.973 -26.100 12.863  0.50 44.71 ?  102 LYS   B CE   1 
ATOM   5561 N  NZ   A LYS   B 1 102 ? 46.010 -24.444 12.456  0.50 45.17 ?  102 LYS   B NZ   1 
ATOM   5562 N  NZ   B LYS   B 1 102 ? 46.283 -24.709 12.424  0.50 45.54 ?  102 LYS   B NZ   1 
ATOM   5563 H  H    A LYS   B 1 102 ? 41.897 -29.677 12.345  0.50 40.97 ?  102 LYS   B H    1 
ATOM   5564 H  H    B LYS   B 1 102 ? 41.899 -29.673 12.350  0.50 40.94 ?  102 LYS   B H    1 
ATOM   5565 H  HA   A LYS   B 1 102 ? 42.834 -29.557 14.875  0.50 43.50 ?  102 LYS   B HA   1 
ATOM   5566 H  HA   B LYS   B 1 102 ? 42.814 -29.599 14.893  0.50 43.46 ?  102 LYS   B HA   1 
ATOM   5567 H  HB2  A LYS   B 1 102 ? 42.082 -27.476 13.134  0.50 46.48 ?  102 LYS   B HB2  1 
ATOM   5568 H  HB2  B LYS   B 1 102 ? 42.161 -27.461 13.181  0.50 46.50 ?  102 LYS   B HB2  1 
ATOM   5569 H  HB3  A LYS   B 1 102 ? 42.448 -27.218 14.653  0.50 46.48 ?  102 LYS   B HB3  1 
ATOM   5570 H  HB3  B LYS   B 1 102 ? 42.548 -27.252 14.704  0.50 46.50 ?  102 LYS   B HB3  1 
ATOM   5571 H  HG2  A LYS   B 1 102 ? 44.642 -27.833 14.251  0.50 49.26 ?  102 LYS   B HG2  1 
ATOM   5572 H  HG2  B LYS   B 1 102 ? 44.704 -27.934 14.295  0.50 49.37 ?  102 LYS   B HG2  1 
ATOM   5573 H  HG3  A LYS   B 1 102 ? 44.283 -28.147 12.729  0.50 49.26 ?  102 LYS   B HG3  1 
ATOM   5574 H  HG3  B LYS   B 1 102 ? 44.331 -28.294 12.787  0.50 49.37 ?  102 LYS   B HG3  1 
ATOM   5575 H  HD2  A LYS   B 1 102 ? 43.812 -25.912 12.353  0.50 51.61 ?  102 LYS   B HD2  1 
ATOM   5576 H  HD2  B LYS   B 1 102 ? 44.014 -26.073 12.289  0.50 51.84 ?  102 LYS   B HD2  1 
ATOM   5577 H  HD3  A LYS   B 1 102 ? 44.070 -25.578 13.886  0.50 51.61 ?  102 LYS   B HD3  1 
ATOM   5578 H  HD3  B LYS   B 1 102 ? 44.218 -25.668 13.814  0.50 51.84 ?  102 LYS   B HD3  1 
ATOM   5579 H  HE2  A LYS   B 1 102 ? 46.326 -26.061 13.623  0.50 53.30 ?  102 LYS   B HE2  1 
ATOM   5580 H  HE2  B LYS   B 1 102 ? 46.458 -26.275 13.685  0.50 53.64 ?  102 LYS   B HE2  1 
ATOM   5581 H  HE3  A LYS   B 1 102 ? 46.075 -26.429 12.094  0.50 53.30 ?  102 LYS   B HE3  1 
ATOM   5582 H  HE3  B LYS   B 1 102 ? 46.259 -26.711 12.167  0.50 53.64 ?  102 LYS   B HE3  1 
ATOM   5583 H  HZ1  A LYS   B 1 102 ? 46.870 -24.302 12.281  0.50 54.20 ?  102 LYS   B HZ1  1 
ATOM   5584 H  HZ1  B LYS   B 1 102 ? 47.157 -24.622 12.284  0.50 54.64 ?  102 LYS   B HZ1  1 
ATOM   5585 H  HZ2  A LYS   B 1 102 ? 45.530 -24.245 11.732  0.50 54.20 ?  102 LYS   B HZ2  1 
ATOM   5586 H  HZ2  B LYS   B 1 102 ? 45.849 -24.526 11.669  0.50 54.64 ?  102 LYS   B HZ2  1 
ATOM   5587 H  HZ3  A LYS   B 1 102 ? 45.759 -23.910 13.123  0.50 54.20 ?  102 LYS   B HZ3  1 
ATOM   5588 H  HZ3  B LYS   B 1 102 ? 46.030 -24.129 13.050  0.50 54.64 ?  102 LYS   B HZ3  1 
ATOM   5589 N  N    . GLY   B 1 103 ? 39.892 -30.011 14.396  1.00 35.41 ?  103 GLY   B N    1 
ATOM   5590 C  CA   . GLY   B 1 103 ? 38.557 -30.054 14.957  1.00 35.16 ?  103 GLY   B CA   1 
ATOM   5591 C  C    . GLY   B 1 103 ? 37.619 -28.966 14.486  1.00 34.49 ?  103 GLY   B C    1 
ATOM   5592 O  O    . GLY   B 1 103 ? 36.521 -28.837 15.040  1.00 34.73 ?  103 GLY   B O    1 
ATOM   5593 H  H    A GLY   B 1 103 ? 40.013 -30.556 13.743  0.50 42.48 ?  103 GLY   B H    1 
ATOM   5594 H  H    B GLY   B 1 103 ? 40.017 -30.565 13.751  0.50 42.48 ?  103 GLY   B H    1 
ATOM   5595 H  HA2  . GLY   B 1 103 ? 38.157 -30.913 14.746  1.00 42.18 ?  103 GLY   B HA2  1 
ATOM   5596 H  HA3  . GLY   B 1 103 ? 38.618 -29.983 15.921  1.00 42.18 ?  103 GLY   B HA3  1 
ATOM   5597 N  N    . GLU   B 1 104 ? 38.009 -28.177 13.488  1.00 33.16 ?  104 GLU   B N    1 
ATOM   5598 C  CA   . GLU   B 1 104 ? 37.159 -27.093 13.017  1.00 31.93 ?  104 GLU   B CA   1 
ATOM   5599 C  C    . GLU   B 1 104 ? 35.970 -27.636 12.227  1.00 32.62 ?  104 GLU   B C    1 
ATOM   5600 O  O    . GLU   B 1 104 ? 36.018 -28.729 11.654  1.00 33.08 ?  104 GLU   B O    1 
ATOM   5601 C  CB   . GLU   B 1 104 ? 37.984 -26.100 12.196  1.00 30.66 ?  104 GLU   B CB   1 
ATOM   5602 C  CG   . GLU   B 1 104 ? 39.080 -25.449 13.036  1.00 29.38 ?  104 GLU   B CG   1 
ATOM   5603 C  CD   . GLU   B 1 104 ? 40.025 -24.563 12.251  1.00 28.04 ?  104 GLU   B CD   1 
ATOM   5604 O  OE1  . GLU   B 1 104 ? 40.026 -24.617 11.005  1.00 26.33 ?  104 GLU   B OE1  1 
ATOM   5605 O  OE2  . GLU   B 1 104 ? 40.778 -23.805 12.896  1.00 27.84 -1 104 GLU   B OE2  1 
ATOM   5606 H  H    . GLU   B 1 104 ? 38.763 -28.240 13.079  1.00 39.78 ?  104 GLU   B H    1 
ATOM   5607 H  HA   . GLU   B 1 104 ? 36.808 -26.619 13.784  1.00 38.31 ?  104 GLU   B HA   1 
ATOM   5608 H  HB2  . GLU   B 1 104 ? 38.403 -26.565 11.456  1.00 36.77 ?  104 GLU   B HB2  1 
ATOM   5609 H  HB3  . GLU   B 1 104 ? 37.400 -25.399 11.863  1.00 36.77 ?  104 GLU   B HB3  1 
ATOM   5610 H  HG2  . GLU   B 1 104 ? 38.666 -24.902 13.721  1.00 35.24 ?  104 GLU   B HG2  1 
ATOM   5611 H  HG3  . GLU   B 1 104 ? 39.614 -26.144 13.448  1.00 35.24 ?  104 GLU   B HG3  1 
ATOM   5612 N  N    A ASP   B 1 105 ? 34.896 -26.850 12.200  0.50 32.79 ?  105 ASP   B N    1 
ATOM   5613 N  N    B ASP   B 1 105 ? 34.888 -26.860 12.212  0.50 32.62 ?  105 ASP   B N    1 
ATOM   5614 C  CA   A ASP   B 1 105 ? 33.631 -27.298 11.630  0.50 33.18 ?  105 ASP   B CA   1 
ATOM   5615 C  CA   B ASP   B 1 105 ? 33.629 -27.326 11.641  0.50 32.85 ?  105 ASP   B CA   1 
ATOM   5616 C  C    A ASP   B 1 105 ? 33.722 -27.341 10.110  0.50 31.21 ?  105 ASP   B C    1 
ATOM   5617 C  C    B ASP   B 1 105 ? 33.714 -27.346 10.120  0.50 30.99 ?  105 ASP   B C    1 
ATOM   5618 O  O    A ASP   B 1 105 ? 33.924 -26.307 9.464   0.50 30.47 ?  105 ASP   B O    1 
ATOM   5619 O  O    B ASP   B 1 105 ? 33.904 -26.302 9.487   0.50 30.11 ?  105 ASP   B O    1 
ATOM   5620 C  CB   A ASP   B 1 105 ? 32.513 -26.352 12.063  0.50 35.58 ?  105 ASP   B CB   1 
ATOM   5621 C  CB   B ASP   B 1 105 ? 32.482 -26.426 12.095  0.50 35.00 ?  105 ASP   B CB   1 
ATOM   5622 C  CG   A ASP   B 1 105 ? 31.143 -26.824 11.617  0.50 37.58 ?  105 ASP   B CG   1 
ATOM   5623 C  CG   B ASP   B 1 105 ? 31.121 -26.982 11.718  0.50 36.76 ?  105 ASP   B CG   1 
ATOM   5624 O  OD1  A ASP   B 1 105 ? 31.047 -27.938 11.059  0.50 37.96 ?  105 ASP   B OD1  1 
ATOM   5625 O  OD1  B ASP   B 1 105 ? 31.070 -28.009 11.009  0.50 37.17 ?  105 ASP   B OD1  1 
ATOM   5626 O  OD2  A ASP   B 1 105 ? 30.162 -26.078 11.820  0.50 38.64 -1 105 ASP   B OD2  1 
ATOM   5627 O  OD2  B ASP   B 1 105 ? 30.100 -26.398 12.138  0.50 37.49 -1 105 ASP   B OD2  1 
ATOM   5628 H  H    A ASP   B 1 105 ? 34.876 -26.047 12.506  0.50 39.34 ?  105 ASP   B H    1 
ATOM   5629 H  H    B ASP   B 1 105 ? 34.857 -26.061 12.525  0.50 39.13 ?  105 ASP   B H    1 
ATOM   5630 H  HA   A ASP   B 1 105 ? 33.424 -28.188 11.952  0.50 39.80 ?  105 ASP   B HA   1 
ATOM   5631 H  HA   B ASP   B 1 105 ? 33.449 -28.227 11.947  0.50 39.41 ?  105 ASP   B HA   1 
ATOM   5632 H  HB2  A ASP   B 1 105 ? 32.519 -26.278 13.031  0.50 42.68 ?  105 ASP   B HB2  1 
ATOM   5633 H  HB2  B ASP   B 1 105 ? 32.510 -26.338 13.060  0.50 41.99 ?  105 ASP   B HB2  1 
ATOM   5634 H  HB3  A ASP   B 1 105 ? 32.662 -25.480 11.665  0.50 42.68 ?  105 ASP   B HB3  1 
ATOM   5635 H  HB3  B ASP   B 1 105 ? 32.578 -25.554 11.679  0.50 41.99 ?  105 ASP   B HB3  1 
ATOM   5636 N  N    . ILE   B 1 106 ? 33.549 -28.536 9.538   1.00 30.19 ?  106 ILE   B N    1 
ATOM   5637 C  CA   . ILE   B 1 106 ? 33.563 -28.692 8.089   1.00 28.37 ?  106 ILE   B CA   1 
ATOM   5638 C  C    . ILE   B 1 106 ? 32.476 -27.858 7.419   1.00 26.62 ?  106 ILE   B C    1 
ATOM   5639 O  O    . ILE   B 1 106 ? 32.581 -27.543 6.230   1.00 25.46 ?  106 ILE   B O    1 
ATOM   5640 C  CB   . ILE   B 1 106 ? 33.452 -30.196 7.736   1.00 28.81 ?  106 ILE   B CB   1 
ATOM   5641 C  CG1  . ILE   B 1 106 ? 33.747 -30.438 6.255   1.00 29.03 ?  106 ILE   B CG1  1 
ATOM   5642 C  CG2  . ILE   B 1 106 ? 32.070 -30.733 8.096   1.00 29.49 ?  106 ILE   B CG2  1 
ATOM   5643 C  CD1  . ILE   B 1 106 ? 35.118 -29.972 5.831   1.00 29.01 ?  106 ILE   B CD1  1 
ATOM   5644 H  H    A ILE   B 1 106 ? 33.423 -29.268 9.970   0.50 36.22 ?  106 ILE   B H    1 
ATOM   5645 H  H    B ILE   B 1 106 ? 33.425 -29.270 9.967   0.50 36.22 ?  106 ILE   B H    1 
ATOM   5646 H  HA   . ILE   B 1 106 ? 34.413 -28.371 7.759   1.00 34.03 ?  106 ILE   B HA   1 
ATOM   5647 H  HB   . ILE   B 1 106 ? 34.109 -30.682 8.259   1.00 34.56 ?  106 ILE   B HB   1 
ATOM   5648 H  HG12 . ILE   B 1 106 ? 33.692 -31.393 6.077   1.00 34.82 ?  106 ILE   B HG12 1 
ATOM   5649 H  HG13 . ILE   B 1 106 ? 33.092 -29.967 5.720   1.00 34.82 ?  106 ILE   B HG13 1 
ATOM   5650 H  HG21 . ILE   B 1 106 ? 32.083 -31.701 8.030   1.00 35.38 ?  106 ILE   B HG21 1 
ATOM   5651 H  HG22 . ILE   B 1 106 ? 31.856 -30.466 9.002   1.00 35.38 ?  106 ILE   B HG22 1 
ATOM   5652 H  HG23 . ILE   B 1 106 ? 31.419 -30.368 7.478   1.00 35.38 ?  106 ILE   B HG23 1 
ATOM   5653 H  HD11 . ILE   B 1 106 ? 35.344 -30.388 4.986   1.00 34.81 ?  106 ILE   B HD11 1 
ATOM   5654 H  HD12 . ILE   B 1 106 ? 35.107 -29.007 5.732   1.00 34.81 ?  106 ILE   B HD12 1 
ATOM   5655 H  HD13 . ILE   B 1 106 ? 35.763 -30.230 6.509   1.00 34.81 ?  106 ILE   B HD13 1 
ATOM   5656 N  N    A GLN   B 1 107 ? 31.432 -27.480 8.160   0.50 26.79 ?  107 GLN   B N    1 
ATOM   5657 N  N    B GLN   B 1 107 ? 31.433 -27.482 8.162   0.50 26.73 ?  107 GLN   B N    1 
ATOM   5658 C  CA   A GLN   B 1 107 ? 30.355 -26.686 7.580   0.50 27.01 ?  107 GLN   B CA   1 
ATOM   5659 C  CA   B GLN   B 1 107 ? 30.351 -26.687 7.592   0.50 26.90 ?  107 GLN   B CA   1 
ATOM   5660 C  C    A GLN   B 1 107 ? 30.844 -25.328 7.094   0.50 24.68 ?  107 GLN   B C    1 
ATOM   5661 C  C    B GLN   B 1 107 ? 30.827 -25.318 7.119   0.50 24.56 ?  107 GLN   B C    1 
ATOM   5662 O  O    A GLN   B 1 107 ? 30.213 -24.737 6.212   0.50 24.95 ?  107 GLN   B O    1 
ATOM   5663 O  O    B GLN   B 1 107 ? 30.171 -24.711 6.268   0.50 24.83 ?  107 GLN   B O    1 
ATOM   5664 C  CB   A GLN   B 1 107 ? 29.234 -26.502 8.605   0.50 30.12 ?  107 GLN   B CB   1 
ATOM   5665 C  CB   B GLN   B 1 107 ? 29.229 -26.532 8.622   0.50 30.00 ?  107 GLN   B CB   1 
ATOM   5666 C  CG   A GLN   B 1 107 ? 27.906 -26.026 8.022   0.50 32.96 ?  107 GLN   B CG   1 
ATOM   5667 C  CG   B GLN   B 1 107 ? 27.880 -26.128 8.039   0.50 32.86 ?  107 GLN   B CG   1 
ATOM   5668 C  CD   A GLN   B 1 107 ? 27.821 -24.516 7.894   0.50 35.17 ?  107 GLN   B CD   1 
ATOM   5669 C  CD   B GLN   B 1 107 ? 27.720 -24.626 7.909   0.50 35.10 ?  107 GLN   B CD   1 
ATOM   5670 O  OE1  A GLN   B 1 107 ? 28.636 -23.785 8.458   0.50 35.99 ?  107 GLN   B OE1  1 
ATOM   5671 O  OE1  B GLN   B 1 107 ? 28.456 -23.854 8.524   0.50 35.91 ?  107 GLN   B OE1  1 
ATOM   5672 N  NE2  A GLN   B 1 107 ? 26.825 -24.041 7.151   0.50 35.98 ?  107 GLN   B NE2  1 
ATOM   5673 N  NE2  B GLN   B 1 107 ? 26.749 -24.202 7.108   0.50 35.91 ?  107 GLN   B NE2  1 
ATOM   5674 H  H    A GLN   B 1 107 ? 31.332 -27.660 8.991   0.50 32.14 ?  107 GLN   B H    1 
ATOM   5675 H  H    B GLN   B 1 107 ? 31.332 -27.672 8.990   0.50 32.06 ?  107 GLN   B H    1 
ATOM   5676 H  HA   A GLN   B 1 107 ? 29.986 -27.165 6.819   0.50 32.40 ?  107 GLN   B HA   1 
ATOM   5677 H  HA   B GLN   B 1 107 ? 29.987 -27.158 6.825   0.50 32.26 ?  107 GLN   B HA   1 
ATOM   5678 H  HB2  A GLN   B 1 107 ? 29.074 -27.351 9.038   0.50 36.14 ?  107 GLN   B HB2  1 
ATOM   5679 H  HB2  B GLN   B 1 107 ? 29.109 -27.379 9.074   0.50 35.99 ?  107 GLN   B HB2  1 
ATOM   5680 H  HB3  A GLN   B 1 107 ? 29.521 -25.848 9.261   0.50 36.14 ?  107 GLN   B HB3  1 
ATOM   5681 H  HB3  B GLN   B 1 107 ? 29.490 -25.854 9.264   0.50 35.99 ?  107 GLN   B HB3  1 
ATOM   5682 H  HG2  A GLN   B 1 107 ? 27.792 -26.405 7.138   0.50 39.54 ?  107 GLN   B HG2  1 
ATOM   5683 H  HG2  B GLN   B 1 107 ? 27.787 -26.515 7.154   0.50 39.42 ?  107 GLN   B HG2  1 
ATOM   5684 H  HG3  A GLN   B 1 107 ? 27.185 -26.320 8.603   0.50 39.54 ?  107 GLN   B HG3  1 
ATOM   5685 H  HG3  B GLN   B 1 107 ? 27.174 -26.459 8.619   0.50 39.42 ?  107 GLN   B HG3  1 
ATOM   5686 H  HE21 A GLN   B 1 107 ? 26.274 -24.583 6.771   0.50 43.16 ?  107 GLN   B HE21 1 
ATOM   5687 H  HE21 B GLN   B 1 107 ? 26.254 -24.770 6.693   0.50 43.08 ?  107 GLN   B HE21 1 
ATOM   5688 H  HE22 A GLN   B 1 107 ? 26.730 -23.192 7.050   0.50 43.16 ?  107 GLN   B HE22 1 
ATOM   5689 H  HE22 B GLN   B 1 107 ? 26.615 -23.359 7.003   0.50 43.08 ?  107 GLN   B HE22 1 
ATOM   5690 N  N    . LEU   B 1 108 ? 31.958 -24.827 7.636   1.00 22.34 ?  108 LEU   B N    1 
ATOM   5691 C  CA   . LEU   B 1 108 ? 32.503 -23.529 7.230   1.00 19.27 ?  108 LEU   B CA   1 
ATOM   5692 C  C    . LEU   B 1 108 ? 33.159 -23.556 5.860   1.00 16.66 ?  108 LEU   B C    1 
ATOM   5693 O  O    . LEU   B 1 108 ? 33.592 -22.500 5.375   1.00 15.77 ?  108 LEU   B O    1 
ATOM   5694 C  CB   . LEU   B 1 108 ? 33.501 -23.029 8.275   1.00 19.67 ?  108 LEU   B CB   1 
ATOM   5695 C  CG   . LEU   B 1 108 ? 32.891 -22.444 9.549   1.00 21.17 ?  108 LEU   B CG   1 
ATOM   5696 C  CD1  . LEU   B 1 108 ? 33.882 -22.504 10.693  1.00 21.79 ?  108 LEU   B CD1  1 
ATOM   5697 C  CD2  . LEU   B 1 108 ? 32.444 -21.004 9.314   1.00 21.84 ?  108 LEU   B CD2  1 
ATOM   5698 H  H    A LEU   B 1 108 ? 32.407 -25.219 8.252   0.50 26.80 ?  108 LEU   B H    1 
ATOM   5699 H  H    B LEU   B 1 108 ? 32.424 -25.230 8.233   0.50 26.80 ?  108 LEU   B H    1 
ATOM   5700 H  HA   . LEU   B 1 108 ? 31.775 -22.893 7.192   1.00 23.11 ?  108 LEU   B HA   1 
ATOM   5701 H  HB2  . LEU   B 1 108 ? 34.062 -23.771 8.544   1.00 23.59 ?  108 LEU   B HB2  1 
ATOM   5702 H  HB3  . LEU   B 1 108 ? 34.044 -22.338 7.873   1.00 23.59 ?  108 LEU   B HB3  1 
ATOM   5703 H  HG   . LEU   B 1 108 ? 32.108 -22.959 9.800   1.00 25.40 ?  108 LEU   B HG   1 
ATOM   5704 H  HD11 . LEU   B 1 108 ? 33.464 -22.150 11.495  1.00 26.14 ?  108 LEU   B HD11 1 
ATOM   5705 H  HD12 . LEU   B 1 108 ? 34.142 -23.427 10.836  1.00 26.14 ?  108 LEU   B HD12 1 
ATOM   5706 H  HD13 . LEU   B 1 108 ? 34.660 -21.971 10.465  1.00 26.14 ?  108 LEU   B HD13 1 
ATOM   5707 H  HD21 . LEU   B 1 108 ? 32.058 -20.653 10.132  1.00 26.19 ?  108 LEU   B HD21 1 
ATOM   5708 H  HD22 . LEU   B 1 108 ? 33.217 -20.472 9.060   1.00 26.19 ?  108 LEU   B HD22 1 
ATOM   5709 H  HD23 . LEU   B 1 108 ? 31.785 -20.988 8.603   1.00 26.19 ?  108 LEU   B HD23 1 
ATOM   5710 N  N    . LEU   B 1 109 ? 33.220 -24.725 5.228   1.00 15.27 ?  109 LEU   B N    1 
ATOM   5711 C  CA   . LEU   B 1 109 ? 33.853 -24.837 3.923   1.00 14.15 ?  109 LEU   B CA   1 
ATOM   5712 C  C    . LEU   B 1 109 ? 33.083 -24.066 2.857   1.00 13.42 ?  109 LEU   B C    1 
ATOM   5713 O  O    . LEU   B 1 109 ? 33.693 -23.486 1.953   1.00 13.09 ?  109 LEU   B O    1 
ATOM   5714 C  CB   . LEU   B 1 109 ? 33.972 -26.316 3.557   1.00 14.25 ?  109 LEU   B CB   1 
ATOM   5715 C  CG   . LEU   B 1 109 ? 34.751 -26.663 2.296   1.00 13.71 ?  109 LEU   B CG   1 
ATOM   5716 C  CD1  . LEU   B 1 109 ? 36.131 -26.008 2.311   1.00 13.73 ?  109 LEU   B CD1  1 
ATOM   5717 C  CD2  . LEU   B 1 109 ? 34.873 -28.181 2.147   1.00 14.95 ?  109 LEU   B CD2  1 
ATOM   5718 H  H    . LEU   B 1 109 ? 32.914 -25.464 5.531   1.00 18.31 ?  109 LEU   B H    1 
ATOM   5719 H  HA   . LEU   B 1 109 ? 34.751 -24.463 3.971   1.00 16.97 ?  109 LEU   B HA   1 
ATOM   5720 H  HB2  . LEU   B 1 109 ? 34.409 -26.775 4.290   1.00 17.09 ?  109 LEU   B HB2  1 
ATOM   5721 H  HB3  . LEU   B 1 109 ? 33.079 -26.672 3.442   1.00 17.09 ?  109 LEU   B HB3  1 
ATOM   5722 H  HG   . LEU   B 1 109 ? 34.271 -26.337 1.519   1.00 16.44 ?  109 LEU   B HG   1 
ATOM   5723 H  HD11 . LEU   B 1 109 ? 36.672 -26.381 1.595   1.00 16.47 ?  109 LEU   B HD11 1 
ATOM   5724 H  HD12 . LEU   B 1 109 ? 36.027 -25.053 2.180   1.00 16.47 ?  109 LEU   B HD12 1 
ATOM   5725 H  HD13 . LEU   B 1 109 ? 36.555 -26.182 3.166   1.00 16.47 ?  109 LEU   B HD13 1 
ATOM   5726 H  HD21 . LEU   B 1 109 ? 35.441 -28.385 1.382   1.00 17.93 ?  109 LEU   B HD21 1 
ATOM   5727 H  HD22 . LEU   B 1 109 ? 35.269 -28.551 2.952   1.00 17.93 ?  109 LEU   B HD22 1 
ATOM   5728 H  HD23 . LEU   B 1 109 ? 33.991 -28.563 2.009   1.00 17.93 ?  109 LEU   B HD23 1 
ATOM   5729 N  N    . LYS   B 1 110 ? 31.749 -24.029 2.940   1.00 13.31 ?  110 LYS   B N    1 
ATOM   5730 C  CA   . LYS   B 1 110 ? 30.999 -23.275 1.941   1.00 13.28 ?  110 LYS   B CA   1 
ATOM   5731 C  C    . LYS   B 1 110 ? 31.331 -21.788 2.029   1.00 12.90 ?  110 LYS   B C    1 
ATOM   5732 O  O    . LYS   B 1 110 ? 31.581 -21.137 1.009   1.00 12.74 ?  110 LYS   B O    1 
ATOM   5733 C  CB   . LYS   B 1 110 ? 29.492 -23.525 2.083   1.00 13.84 ?  110 LYS   B CB   1 
ATOM   5734 C  CG   . LYS   B 1 110 ? 28.684 -22.917 0.923   1.00 13.97 ?  110 LYS   B CG   1 
ATOM   5735 C  CD   . LYS   B 1 110 ? 27.213 -23.342 0.961   1.00 14.72 ?  110 LYS   B CD   1 
ATOM   5736 C  CE   . LYS   B 1 110 ? 26.440 -22.800 -0.238  1.00 15.37 ?  110 LYS   B CE   1 
ATOM   5737 N  NZ   . LYS   B 1 110 ? 26.782 -23.509 -1.500  1.00 15.59 ?  110 LYS   B NZ   1 
ATOM   5738 H  H    . LYS   B 1 110 ? 31.280 -24.427 3.537   1.00 15.96 ?  110 LYS   B H    1 
ATOM   5739 H  HA   . LYS   B 1 110 ? 31.265 -23.581 1.061   1.00 15.93 ?  110 LYS   B HA   1 
ATOM   5740 H  HB2  . LYS   B 1 110 ? 29.331 -24.479 2.098   1.00 16.60 ?  110 LYS   B HB2  1 
ATOM   5741 H  HB3  . LYS   B 1 110 ? 29.183 -23.120 2.908   1.00 16.60 ?  110 LYS   B HB3  1 
ATOM   5742 H  HG2  . LYS   B 1 110 ? 28.711 -21.951 0.976   1.00 16.76 ?  110 LYS   B HG2  1 
ATOM   5743 H  HG3  . LYS   B 1 110 ? 29.053 -23.218 0.078   1.00 16.76 ?  110 LYS   B HG3  1 
ATOM   5744 H  HD2  . LYS   B 1 110 ? 27.153 -24.311 0.941   1.00 17.66 ?  110 LYS   B HD2  1 
ATOM   5745 H  HD3  . LYS   B 1 110 ? 26.797 -22.999 1.768   1.00 17.66 ?  110 LYS   B HD3  1 
ATOM   5746 H  HE2  . LYS   B 1 110 ? 25.488 -22.900 -0.083  1.00 18.43 ?  110 LYS   B HE2  1 
ATOM   5747 H  HE3  . LYS   B 1 110 ? 26.657 -21.857 -0.356  1.00 18.43 ?  110 LYS   B HE3  1 
ATOM   5748 H  HZ1  . LYS   B 1 110 ? 26.320 -23.169 -2.178  1.00 18.70 ?  110 LYS   B HZ1  1 
ATOM   5749 H  HZ2  . LYS   B 1 110 ? 27.652 -23.424 -1.668  1.00 18.70 ?  110 LYS   B HZ2  1 
ATOM   5750 H  HZ3  . LYS   B 1 110 ? 26.587 -24.375 -1.419  1.00 18.70 ?  110 LYS   B HZ3  1 
ATOM   5751 N  N    . SER   B 1 111 ? 31.351 -21.237 3.247   1.00 13.19 ?  111 SER   B N    1 
ATOM   5752 C  CA   . SER   B 1 111 ? 31.748 -19.841 3.422   1.00 13.02 ?  111 SER   B CA   1 
ATOM   5753 C  C    . SER   B 1 111 ? 33.126 -19.584 2.827   1.00 12.49 ?  111 SER   B C    1 
ATOM   5754 O  O    . SER   B 1 111 ? 33.349 -18.555 2.171   1.00 12.73 ?  111 SER   B O    1 
ATOM   5755 C  CB   . SER   B 1 111 ? 31.750 -19.484 4.908   1.00 14.04 ?  111 SER   B CB   1 
ATOM   5756 O  OG   . SER   B 1 111 ? 30.445 -19.498 5.449   1.00 15.72 ?  111 SER   B OG   1 
ATOM   5757 H  H    . SER   B 1 111 ? 31.153 -21.650 3.975   1.00 15.81 ?  111 SER   B H    1 
ATOM   5758 H  HA   . SER   B 1 111 ? 31.112 -19.270 2.971   1.00 15.62 ?  111 SER   B HA   1 
ATOM   5759 H  HB2  . SER   B 1 111 ? 32.287 -20.133 5.389   1.00 16.84 ?  111 SER   B HB2  1 
ATOM   5760 H  HB3  . SER   B 1 111 ? 32.124 -18.598 5.019   1.00 16.84 ?  111 SER   B HB3  1 
ATOM   5761 H  HG   . SER   B 1 111 ? 30.467 -19.292 6.271   1.00 18.85 ?  111 SER   B HG   1 
ATOM   5762 N  N    . ALA   B 1 112 ? 34.065 -20.504 3.046   1.00 12.55 ?  112 ALA   B N    1 
ATOM   5763 C  CA   . ALA   B 1 112 ? 35.407 -20.332 2.504   1.00 12.30 ?  112 ALA   B CA   1 
ATOM   5764 C  C    . ALA   B 1 112 ? 35.380 -20.238 0.981   1.00 11.92 ?  112 ALA   B C    1 
ATOM   5765 O  O    . ALA   B 1 112 ? 36.001 -19.348 0.389   1.00 12.14 ?  112 ALA   B O    1 
ATOM   5766 C  CB   . ALA   B 1 112 ? 36.313 -21.469 2.982   1.00 12.47 ?  112 ALA   B CB   1 
ATOM   5767 H  H    . ALA   B 1 112 ? 33.951 -21.232 3.497   1.00 15.05 ?  112 ALA   B H    1 
ATOM   5768 H  HA   . ALA   B 1 112 ? 35.774 -19.504 2.845   1.00 14.75 ?  112 ALA   B HA   1 
ATOM   5769 H  HB1  . ALA   B 1 112 ? 37.205 -21.337 2.618   1.00 14.96 ?  112 ALA   B HB1  1 
ATOM   5770 H  HB2  . ALA   B 1 112 ? 36.353 -21.456 3.953   1.00 14.96 ?  112 ALA   B HB2  1 
ATOM   5771 H  HB3  . ALA   B 1 112 ? 35.955 -22.315 2.678   1.00 14.96 ?  112 ALA   B HB3  1 
ATOM   5772 N  N    . TYR   B 1 113 ? 34.649 -21.141 0.324   1.00 11.52 ?  113 TYR   B N    1 
ATOM   5773 C  CA   . TYR   B 1 113 ? 34.572 -21.097 -1.132  1.00 11.54 ?  113 TYR   B CA   1 
ATOM   5774 C  C    . TYR   B 1 113 ? 33.865 -19.848 -1.649  1.00 11.28 ?  113 TYR   B C    1 
ATOM   5775 O  O    . TYR   B 1 113 ? 34.142 -19.414 -2.772  1.00 11.26 ?  113 TYR   B O    1 
ATOM   5776 C  CB   . TYR   B 1 113 ? 33.905 -22.358 -1.681  1.00 11.41 ?  113 TYR   B CB   1 
ATOM   5777 C  CG   . TYR   B 1 113 ? 34.862 -23.509 -1.924  1.00 11.86 ?  113 TYR   B CG   1 
ATOM   5778 C  CD1  . TYR   B 1 113 ? 35.863 -23.415 -2.878  1.00 12.56 ?  113 TYR   B CD1  1 
ATOM   5779 C  CD2  . TYR   B 1 113 ? 34.754 -24.696 -1.213  1.00 12.14 ?  113 TYR   B CD2  1 
ATOM   5780 C  CE1  . TYR   B 1 113 ? 36.740 -24.452 -3.116  1.00 12.56 ?  113 TYR   B CE1  1 
ATOM   5781 C  CE2  . TYR   B 1 113 ? 35.626 -25.755 -1.446  1.00 12.43 ?  113 TYR   B CE2  1 
ATOM   5782 C  CZ   . TYR   B 1 113 ? 36.607 -25.622 -2.405  1.00 12.81 ?  113 TYR   B CZ   1 
ATOM   5783 O  OH   . TYR   B 1 113 ? 37.493 -26.629 -2.682  1.00 13.66 ?  113 TYR   B OH   1 
ATOM   5784 H  H    . TYR   B 1 113 ? 34.192 -21.769 0.696   1.00 13.81 ?  113 TYR   B H    1 
ATOM   5785 H  HA   . TYR   B 1 113 ? 35.473 -21.080 -1.474  1.00 13.83 ?  113 TYR   B HA   1 
ATOM   5786 H  HB2  . TYR   B 1 113 ? 33.231 -22.665 -1.047  1.00 13.68 ?  113 TYR   B HB2  1 
ATOM   5787 H  HB3  . TYR   B 1 113 ? 33.476 -22.145 -2.526  1.00 13.68 ?  113 TYR   B HB3  1 
ATOM   5788 H  HD1  . TYR   B 1 113 ? 35.953 -22.628 -3.365  1.00 15.06 ?  113 TYR   B HD1  1 
ATOM   5789 H  HD2  . TYR   B 1 113 ? 34.081 -24.787 -0.577  1.00 14.56 ?  113 TYR   B HD2  1 
ATOM   5790 H  HE1  . TYR   B 1 113 ? 37.403 -24.362 -3.761  1.00 15.07 ?  113 TYR   B HE1  1 
ATOM   5791 H  HE2  . TYR   B 1 113 ? 35.541 -26.547 -0.969  1.00 14.90 ?  113 TYR   B HE2  1 
ATOM   5792 H  HH   . TYR   B 1 113 ? 37.329 -27.294 -2.198  1.00 16.38 ?  113 TYR   B HH   1 
ATOM   5793 N  N    . GLU   B 1 114 ? 32.941 -19.273 -0.875  1.00 11.28 ?  114 GLU   B N    1 
ATOM   5794 C  CA   . GLU   B 1 114 ? 32.259 -18.063 -1.329  1.00 11.23 ?  114 GLU   B CA   1 
ATOM   5795 C  C    . GLU   B 1 114 ? 33.246 -16.943 -1.624  1.00 11.22 ?  114 GLU   B C    1 
ATOM   5796 O  O    . GLU   B 1 114 ? 32.964 -16.070 -2.447  1.00 11.43 ?  114 GLU   B O    1 
ATOM   5797 C  CB   . GLU   B 1 114 ? 31.195 -17.634 -0.309  1.00 11.61 ?  114 GLU   B CB   1 
ATOM   5798 C  CG   . GLU   B 1 114 ? 29.983 -18.560 -0.375  1.00 12.16 ?  114 GLU   B CG   1 
ATOM   5799 C  CD   . GLU   B 1 114 ? 28.956 -18.380 0.734   1.00 12.36 ?  114 GLU   B CD   1 
ATOM   5800 O  OE1  . GLU   B 1 114 ? 29.247 -17.767 1.780   1.00 12.51 ?  114 GLU   B OE1  1 
ATOM   5801 O  OE2  . GLU   B 1 114 ? 27.832 -18.916 0.566   1.00 13.31 -1 114 GLU   B OE2  1 
ATOM   5802 H  H    . GLU   B 1 114 ? 32.687 -19.566 -0.105  1.00 13.52 ?  114 GLU   B H    1 
ATOM   5803 H  HA   . GLU   B 1 114 ? 31.794 -18.264 -2.155  1.00 13.47 ?  114 GLU   B HA   1 
ATOM   5804 H  HB2  . GLU   B 1 114 ? 31.567 -17.686 0.589   1.00 13.92 ?  114 GLU   B HB2  1 
ATOM   5805 H  HB3  . GLU   B 1 114 ? 30.902 -16.733 -0.501  1.00 13.92 ?  114 GLU   B HB3  1 
ATOM   5806 H  HG2  . GLU   B 1 114 ? 29.526 -18.402 -1.213  1.00 14.58 ?  114 GLU   B HG2  1 
ATOM   5807 H  HG3  . GLU   B 1 114 ? 30.295 -19.476 -0.339  1.00 14.58 ?  114 GLU   B HG3  1 
ATOM   5808 N  N    . ASN   B 1 115 ? 34.411 -16.944 -0.973  1.00 11.16 ?  115 ASN   B N    1 
ATOM   5809 C  CA   . ASN   B 1 115 ? 35.407 -15.914 -1.265  1.00 11.01 ?  115 ASN   B CA   1 
ATOM   5810 C  C    . ASN   B 1 115 ? 35.823 -15.935 -2.728  1.00 10.92 ?  115 ASN   B C    1 
ATOM   5811 O  O    . ASN   B 1 115 ? 36.205 -14.892 -3.282  1.00 11.25 ?  115 ASN   B O    1 
ATOM   5812 C  CB   . ASN   B 1 115 ? 36.647 -16.081 -0.376  1.00 11.66 ?  115 ASN   B CB   1 
ATOM   5813 C  CG   . ASN   B 1 115 ? 36.371 -15.803 1.085   1.00 11.85 ?  115 ASN   B CG   1 
ATOM   5814 O  OD1  . ASN   B 1 115 ? 36.380 -14.655 1.518   1.00 13.50 ?  115 ASN   B OD1  1 
ATOM   5815 N  ND2  . ASN   B 1 115 ? 36.171 -16.860 1.868   1.00 11.95 ?  115 ASN   B ND2  1 
ATOM   5816 H  H    . ASN   B 1 115 ? 34.637 -17.507 -0.361  1.00 13.38 ?  115 ASN   B H    1 
ATOM   5817 H  HA   . ASN   B 1 115 ? 35.023 -15.044 -1.077  1.00 13.20 ?  115 ASN   B HA   1 
ATOM   5818 H  HB2  . ASN   B 1 115 ? 36.972 -16.991 -0.451  1.00 13.98 ?  115 ASN   B HB2  1 
ATOM   5819 H  HB3  . ASN   B 1 115 ? 37.331 -15.458 -0.669  1.00 13.98 ?  115 ASN   B HB3  1 
ATOM   5820 H  HD21 . ASN   B 1 115 ? 36.022 -16.749 2.712   1.00 14.33 ?  115 ASN   B HD21 1 
ATOM   5821 H  HD22 . ASN   B 1 115 ? 36.185 -17.652 1.538   1.00 14.33 ?  115 ASN   B HD22 1 
ATOM   5822 N  N    . PHE   B 1 116 ? 35.798 -17.111 -3.363  1.00 10.75 ?  116 PHE   B N    1 
ATOM   5823 C  CA   . PHE   B 1 116 ? 36.222 -17.202 -4.753  1.00 10.82 ?  116 PHE   B CA   1 
ATOM   5824 C  C    . PHE   B 1 116 ? 35.321 -16.373 -5.665  1.00 10.86 ?  116 PHE   B C    1 
ATOM   5825 O  O    . PHE   B 1 116 ? 35.757 -15.947 -6.741  1.00 11.28 ?  116 PHE   B O    1 
ATOM   5826 C  CB   . PHE   B 1 116 ? 36.186 -18.647 -5.276  1.00 10.70 ?  116 PHE   B CB   1 
ATOM   5827 C  CG   . PHE   B 1 116 ? 37.251 -19.603 -4.722  1.00 10.56 ?  116 PHE   B CG   1 
ATOM   5828 C  CD1  . PHE   B 1 116 ? 37.908 -19.412 -3.514  1.00 11.46 ?  116 PHE   B CD1  1 
ATOM   5829 C  CD2  . PHE   B 1 116 ? 37.548 -20.742 -5.453  1.00 11.02 ?  116 PHE   B CD2  1 
ATOM   5830 C  CE1  . PHE   B 1 116 ? 38.832 -20.358 -3.058  1.00 11.62 ?  116 PHE   B CE1  1 
ATOM   5831 C  CE2  . PHE   B 1 116 ? 38.468 -21.674 -5.005  1.00 11.00 ?  116 PHE   B CE2  1 
ATOM   5832 C  CZ   . PHE   B 1 116 ? 39.102 -21.482 -3.812  1.00 10.99 ?  116 PHE   B CZ   1 
ATOM   5833 H  H    . PHE   B 1 116 ? 35.545 -17.861 -3.016  1.00 12.89 ?  116 PHE   B H    1 
ATOM   5834 H  HA   . PHE   B 1 116 ? 37.127 -16.870 -4.837  1.00 12.98 ?  116 PHE   B HA   1 
ATOM   5835 H  HB2  . PHE   B 1 116 ? 35.316 -19.024 -5.061  1.00 12.82 ?  116 PHE   B HB2  1 
ATOM   5836 H  HB3  . PHE   B 1 116 ? 36.293 -18.623 -6.240  1.00 12.82 ?  116 PHE   B HB3  1 
ATOM   5837 H  HD1  . PHE   B 1 116 ? 37.716 -18.661 -2.994  1.00 13.74 ?  116 PHE   B HD1  1 
ATOM   5838 H  HD2  . PHE   B 1 116 ? 37.105 -20.892 -6.259  1.00 13.21 ?  116 PHE   B HD2  1 
ATOM   5839 H  HE1  . PHE   B 1 116 ? 39.272 -20.218 -2.251  1.00 13.93 ?  116 PHE   B HE1  1 
ATOM   5840 H  HE2  . PHE   B 1 116 ? 38.648 -22.426 -5.515  1.00 13.19 ?  116 PHE   B HE2  1 
ATOM   5841 H  HZ   . PHE   B 1 116 ? 39.730 -22.092 -3.514  1.00 13.17 ?  116 PHE   B HZ   1 
ATOM   5842 N  N    . ASN   B 1 117 ? 34.053 -16.166 -5.280  1.00 11.20 ?  117 ASN   B N    1 
ATOM   5843 C  CA   . ASN   B 1 117 ? 33.106 -15.463 -6.144  1.00 11.31 ?  117 ASN   B CA   1 
ATOM   5844 C  C    . ASN   B 1 117 ? 33.418 -13.985 -6.289  1.00 11.68 ?  117 ASN   B C    1 
ATOM   5845 O  O    . ASN   B 1 117 ? 32.815 -13.328 -7.139  1.00 12.88 ?  117 ASN   B O    1 
ATOM   5846 C  CB   . ASN   B 1 117 ? 31.681 -15.681 -5.652  1.00 11.66 ?  117 ASN   B CB   1 
ATOM   5847 C  CG   . ASN   B 1 117 ? 31.231 -17.094 -5.903  1.00 12.08 ?  117 ASN   B CG   1 
ATOM   5848 O  OD1  . ASN   B 1 117 ? 31.598 -17.683 -6.920  1.00 12.75 ?  117 ASN   B OD1  1 
ATOM   5849 N  ND2  . ASN   B 1 117 ? 30.492 -17.673 -4.967  1.00 12.09 ?  117 ASN   B ND2  1 
ATOM   5850 H  H    . ASN   B 1 117 ? 33.727 -16.412 -4.520  1.00 13.43 ?  117 ASN   B H    1 
ATOM   5851 H  HA   . ASN   B 1 117 ? 33.165 -15.853 -7.022  1.00 13.56 ?  117 ASN   B HA   1 
ATOM   5852 H  HB2  . ASN   B 1 117 ? 31.638 -15.510 -4.692  1.00 13.98 ?  117 ASN   B HB2  1 
ATOM   5853 H  HB3  . ASN   B 1 117 ? 31.082 -15.075 -6.120  1.00 13.98 ?  117 ASN   B HB3  1 
ATOM   5854 H  HD21 . ASN   B 1 117 ? 30.219 -18.479 -5.068  1.00 14.49 ?  117 ASN   B HD21 1 
ATOM   5855 H  HD22 . ASN   B 1 117 ? 30.266 -17.228 -4.260  1.00 14.49 ?  117 ASN   B HD22 1 
ATOM   5856 N  N    . GLN   B 1 118 ? 34.348 -13.462 -5.506  1.00 11.20 ?  118 GLN   B N    1 
ATOM   5857 C  CA   . GLN   B 1 118 ? 34.780 -12.076 -5.637  1.00 11.84 ?  118 GLN   B CA   1 
ATOM   5858 C  C    . GLN   B 1 118 ? 35.854 -11.882 -6.706  1.00 12.12 ?  118 GLN   B C    1 
ATOM   5859 O  O    . GLN   B 1 118 ? 36.330 -10.754 -6.883  1.00 13.57 ?  118 GLN   B O    1 
ATOM   5860 C  CB   . GLN   B 1 118 ? 35.258 -11.553 -4.278  1.00 12.28 ?  118 GLN   B CB   1 
ATOM   5861 C  CG   . GLN   B 1 118 ? 34.166 -11.583 -3.214  1.00 12.63 ?  118 GLN   B CG   1 
ATOM   5862 C  CD   . GLN   B 1 118 ? 33.001 -10.679 -3.560  1.00 12.97 ?  118 GLN   B CD   1 
ATOM   5863 O  OE1  . GLN   B 1 118 ? 33.198 -9.540  -3.995  1.00 13.46 ?  118 GLN   B OE1  1 
ATOM   5864 N  NE2  . GLN   B 1 118 ? 31.790 -11.176 -3.381  1.00 13.23 ?  118 GLN   B NE2  1 
ATOM   5865 H  H    . GLN   B 1 118 ? 34.759 -13.891 -4.884  1.00 13.42 ?  118 GLN   B H    1 
ATOM   5866 H  HA   . GLN   B 1 118 ? 34.016 -11.543 -5.904  1.00 14.20 ?  118 GLN   B HA   1 
ATOM   5867 H  HB2  . GLN   B 1 118 ? 35.995 -12.095 -3.967  1.00 14.72 ?  118 GLN   B HB2  1 
ATOM   5868 H  HB3  . GLN   B 1 118 ? 35.543 -10.628 -4.377  1.00 14.72 ?  118 GLN   B HB3  1 
ATOM   5869 H  HG2  . GLN   B 1 118 ? 33.830 -12.493 -3.131  1.00 15.14 ?  118 GLN   B HG2  1 
ATOM   5870 H  HG3  . GLN   B 1 118 ? 34.538 -11.292 -2.366  1.00 15.14 ?  118 GLN   B HG3  1 
ATOM   5871 H  HE21 . GLN   B 1 118 ? 31.692 -11.975 -3.077  1.00 15.87 ?  118 GLN   B HE21 1 
ATOM   5872 H  HE22 . GLN   B 1 118 ? 31.104 -10.699 -3.571  1.00 15.87 ?  118 GLN   B HE22 1 
ATOM   5873 N  N    . HIS   B 1 119 ? 36.210 -12.938 -7.443  1.00 11.74 ?  119 HIS   B N    1 
ATOM   5874 C  CA   . HIS   B 1 119 ? 37.258 -12.889 -8.458  1.00 11.75 ?  119 HIS   B CA   1 
ATOM   5875 C  C    . HIS   B 1 119 ? 36.777 -13.614 -9.703  1.00 12.06 ?  119 HIS   B C    1 
ATOM   5876 O  O    . HIS   B 1 119 ? 36.274 -14.735 -9.609  1.00 12.49 ?  119 HIS   B O    1 
ATOM   5877 C  CB   . HIS   B 1 119 ? 38.534 -13.533 -7.910  1.00 12.15 ?  119 HIS   B CB   1 
ATOM   5878 C  CG   . HIS   B 1 119 ? 39.013 -12.852 -6.678  1.00 13.50 ?  119 HIS   B CG   1 
ATOM   5879 N  ND1  . HIS   B 1 119 ? 39.806 -11.727 -6.721  1.00 15.21 ?  119 HIS   B ND1  1 
ATOM   5880 C  CD2  . HIS   B 1 119 ? 38.727 -13.065 -5.374  1.00 14.70 ?  119 HIS   B CD2  1 
ATOM   5881 C  CE1  . HIS   B 1 119 ? 40.014 -11.295 -5.490  1.00 16.05 ?  119 HIS   B CE1  1 
ATOM   5882 N  NE2  . HIS   B 1 119 ? 39.365 -12.085 -4.655  1.00 16.26 ?  119 HIS   B NE2  1 
ATOM   5883 H  H    . HIS   B 1 119 ? 35.843 -13.719 -7.371  1.00 14.08 ?  119 HIS   B H    1 
ATOM   5884 H  HA   . HIS   B 1 119 ? 37.444 -11.962 -8.682  1.00 14.09 ?  119 HIS   B HA   1 
ATOM   5885 H  HB2  . HIS   B 1 119 ? 38.360 -14.460 -7.696  1.00 14.57 ?  119 HIS   B HB2  1 
ATOM   5886 H  HB3  . HIS   B 1 119 ? 39.234 -13.468 -8.582  1.00 14.57 ?  119 HIS   B HB3  1 
ATOM   5887 H  HD2  . HIS   B 1 119 ? 38.202 -13.747 -5.027  1.00 17.63 ?  119 HIS   B HD2  1 
ATOM   5888 H  HE1  . HIS   B 1 119 ? 40.549 -10.569 -5.245  1.00 19.25 ?  119 HIS   B HE1  1 
ATOM   5889 H  HE2  . HIS   B 1 119 ? 39.376 -12.021 -3.793  1.00 19.50 ?  119 HIS   B HE2  1 
ATOM   5890 N  N    . GLU   B 1 120 ? 36.935 -12.984 -10.872 1.00 12.79 ?  120 GLU   B N    1 
ATOM   5891 C  CA   . GLU   B 1 120 ? 36.343 -13.564 -12.075 1.00 14.43 ?  120 GLU   B CA   1 
ATOM   5892 C  C    . GLU   B 1 120 ? 37.016 -14.866 -12.494 1.00 12.89 ?  120 GLU   B C    1 
ATOM   5893 O  O    . GLU   B 1 120 ? 36.354 -15.738 -13.077 1.00 13.12 ?  120 GLU   B O    1 
ATOM   5894 C  CB   . GLU   B 1 120 ? 36.362 -12.552 -13.219 1.00 19.49 ?  120 GLU   B CB   1 
ATOM   5895 C  CG   . GLU   B 1 120 ? 35.394 -11.398 -13.019 1.00 25.66 ?  120 GLU   B CG   1 
ATOM   5896 C  CD   . GLU   B 1 120 ? 35.176 -10.586 -14.276 1.00 31.08 ?  120 GLU   B CD   1 
ATOM   5897 O  OE1  . GLU   B 1 120 ? 36.142 -10.413 -15.050 1.00 33.47 ?  120 GLU   B OE1  1 
ATOM   5898 O  OE2  . GLU   B 1 120 ? 34.036 -10.122 -14.488 1.00 33.90 -1 120 GLU   B OE2  1 
ATOM   5899 H  H    . GLU   B 1 120 ? 37.363 -12.240 -10.988 1.00 15.34 ?  120 GLU   B H    1 
ATOM   5900 H  HA   . GLU   B 1 120 ? 35.418 -13.764 -11.884 1.00 17.31 ?  120 GLU   B HA   1 
ATOM   5901 H  HB2  . GLU   B 1 120 ? 37.251 -12.179 -13.302 1.00 23.37 ?  120 GLU   B HB2  1 
ATOM   5902 H  HB3  . GLU   B 1 120 ? 36.113 -13.006 -14.041 1.00 23.37 ?  120 GLU   B HB3  1 
ATOM   5903 H  HG2  . GLU   B 1 120 ? 34.530 -11.747 -12.748 1.00 30.79 ?  120 GLU   B HG2  1 
ATOM   5904 H  HG3  . GLU   B 1 120 ? 35.741 -10.802 -12.340 1.00 30.79 ?  120 GLU   B HG3  1 
ATOM   5905 N  N    . VAL   B 1 121 ? 38.313 -15.016 -12.225 1.00 12.43 ?  121 VAL   B N    1 
ATOM   5906 C  CA   . VAL   B 1 121 ? 39.054 -16.226 -12.577 1.00 12.31 ?  121 VAL   B CA   1 
ATOM   5907 C  C    . VAL   B 1 121 ? 40.170 -16.441 -11.559 1.00 11.85 ?  121 VAL   B C    1 
ATOM   5908 O  O    . VAL   B 1 121 ? 40.863 -15.492 -11.172 1.00 12.64 ?  121 VAL   B O    1 
ATOM   5909 C  CB   . VAL   B 1 121 ? 39.571 -16.174 -14.033 1.00 14.31 ?  121 VAL   B CB   1 
ATOM   5910 C  CG1  . VAL   B 1 121 ? 40.418 -14.931 -14.280 1.00 15.64 ?  121 VAL   B CG1  1 
ATOM   5911 C  CG2  . VAL   B 1 121 ? 40.330 -17.448 -14.387 1.00 15.96 ?  121 VAL   B CG2  1 
ATOM   5912 H  H    . VAL   B 1 121 ? 38.796 -14.418 -11.832 1.00 14.91 ?  121 VAL   B H    1 
ATOM   5913 H  HA   . VAL   B 1 121 ? 38.445 -16.976 -12.513 1.00 14.76 ?  121 VAL   B HA   1 
ATOM   5914 H  HB   . VAL   B 1 121 ? 38.801 -16.121 -14.626 1.00 17.16 ?  121 VAL   B HB   1 
ATOM   5915 H  HG11 . VAL   B 1 121 ? 40.739 -14.944 -15.194 1.00 18.75 ?  121 VAL   B HG11 1 
ATOM   5916 H  HG12 . VAL   B 1 121 ? 39.872 -14.140 -14.133 1.00 18.75 ?  121 VAL   B HG12 1 
ATOM   5917 H  HG13 . VAL   B 1 121 ? 41.167 -14.932 -13.665 1.00 18.75 ?  121 VAL   B HG13 1 
ATOM   5918 H  HG21 . VAL   B 1 121 ? 40.522 -17.444 -15.339 1.00 19.15 ?  121 VAL   B HG21 1 
ATOM   5919 H  HG22 . VAL   B 1 121 ? 41.160 -17.471 -13.885 1.00 19.15 ?  121 VAL   B HG22 1 
ATOM   5920 H  HG23 . VAL   B 1 121 ? 39.784 -18.216 -14.164 1.00 19.15 ?  121 VAL   B HG23 1 
ATOM   5921 N  N    . LEU   B 1 122 ? 40.348 -17.697 -11.136 1.00 11.37 ?  122 LEU   B N    1 
ATOM   5922 C  CA   . LEU   B 1 122 ? 41.320 -18.057 -10.108 1.00 10.91 ?  122 LEU   B CA   1 
ATOM   5923 C  C    . LEU   B 1 122 ? 41.976 -19.386 -10.441 1.00 10.91 ?  122 LEU   B C    1 
ATOM   5924 O  O    . LEU   B 1 122 ? 41.312 -20.309 -10.931 1.00 12.05 ?  122 LEU   B O    1 
ATOM   5925 C  CB   . LEU   B 1 122 ? 40.656 -18.300 -8.740  1.00 12.56 ?  122 LEU   B CB   1 
ATOM   5926 C  CG   . LEU   B 1 122 ? 39.638 -17.267 -8.248  1.00 12.66 ?  122 LEU   B CG   1 
ATOM   5927 C  CD1  . LEU   B 1 122 ? 38.247 -17.622 -8.739  1.00 13.39 ?  122 LEU   B CD1  1 
ATOM   5928 C  CD2  . LEU   B 1 122 ? 39.666 -17.174 -6.735  1.00 12.33 ?  122 LEU   B CD2  1 
ATOM   5929 H  H    . LEU   B 1 122 ? 39.912 -18.375 -11.440 1.00 13.64 ?  122 LEU   B H    1 
ATOM   5930 H  HA   . LEU   B 1 122 ? 41.998 -17.365 -10.021 1.00 13.09 ?  122 LEU   B HA   1 
ATOM   5931 H  HB2  . LEU   B 1 122 ? 40.201 -19.151 -8.777  1.00 15.06 ?  122 LEU   B HB2  1 
ATOM   5932 H  HB3  . LEU   B 1 122 ? 41.360 -18.342 -8.072  1.00 15.06 ?  122 LEU   B HB3  1 
ATOM   5933 H  HG   . LEU   B 1 122 ? 39.873 -16.395 -8.603  1.00 15.18 ?  122 LEU   B HG   1 
ATOM   5934 H  HD11 . LEU   B 1 122 ? 37.617 -16.978 -8.385  1.00 16.06 ?  122 LEU   B HD11 1 
ATOM   5935 H  HD12 . LEU   B 1 122 ? 38.240 -17.593 -9.709  1.00 16.06 ?  122 LEU   B HD12 1 
ATOM   5936 H  HD13 . LEU   B 1 122 ? 38.023 -18.512 -8.431  1.00 16.06 ?  122 LEU   B HD13 1 
ATOM   5937 H  HD21 . LEU   B 1 122 ? 38.996 -16.534 -6.441  1.00 14.79 ?  122 LEU   B HD21 1 
ATOM   5938 H  HD22 . LEU   B 1 122 ? 39.474 -18.047 -6.357  1.00 14.79 ?  122 LEU   B HD22 1 
ATOM   5939 H  HD23 . LEU   B 1 122 ? 40.547 -16.879 -6.447  1.00 14.79 ?  122 LEU   B HD23 1 
ATOM   5940 N  N    . LEU   B 1 123 ? 43.264 -19.496 -10.091 1.00 10.49 ?  123 LEU   B N    1 
ATOM   5941 C  CA   . LEU   B 1 123 ? 43.974 -20.769 -9.965  1.00 10.63 ?  123 LEU   B CA   1 
ATOM   5942 C  C    . LEU   B 1 123 ? 43.939 -21.158 -8.491  1.00 10.39 ?  123 LEU   B C    1 
ATOM   5943 O  O    . LEU   B 1 123 ? 44.297 -20.335 -7.639  1.00 10.81 ?  123 LEU   B O    1 
ATOM   5944 C  CB   . LEU   B 1 123 ? 45.427 -20.603 -10.420 1.00 11.19 ?  123 LEU   B CB   1 
ATOM   5945 C  CG   . LEU   B 1 123 ? 46.358 -21.793 -10.178 1.00 11.57 ?  123 LEU   B CG   1 
ATOM   5946 C  CD1  . LEU   B 1 123 ? 45.925 -23.033 -10.953 1.00 12.19 ?  123 LEU   B CD1  1 
ATOM   5947 C  CD2  . LEU   B 1 123 ? 47.780 -21.403 -10.550 1.00 12.41 ?  123 LEU   B CD2  1 
ATOM   5948 H  H    . LEU   B 1 123 ? 43.761 -18.818 -9.891  1.00 12.57 ?  123 LEU   B H    1 
ATOM   5949 H  HA   . LEU   B 1 123 ? 43.534 -21.455 -10.487 1.00 12.74 ?  123 LEU   B HA   1 
ATOM   5950 H  HB2  . LEU   B 1 123 ? 45.422 -20.431 -11.372 1.00 13.42 ?  123 LEU   B HB2  1 
ATOM   5951 H  HB3  . LEU   B 1 123 ? 45.805 -19.845 -9.953  1.00 13.42 ?  123 LEU   B HB3  1 
ATOM   5952 H  HG   . LEU   B 1 123 ? 46.352 -22.021 -9.234  1.00 13.87 ?  123 LEU   B HG   1 
ATOM   5953 H  HD11 . LEU   B 1 123 ? 46.553 -23.749 -10.779 1.00 14.62 ?  123 LEU   B HD11 1 
ATOM   5954 H  HD12 . LEU   B 1 123 ? 45.036 -23.293 -10.657 1.00 14.62 ?  123 LEU   B HD12 1 
ATOM   5955 H  HD13 . LEU   B 1 123 ? 45.910 -22.822 -11.898 1.00 14.62 ?  123 LEU   B HD13 1 
ATOM   5956 H  HD21 . LEU   B 1 123 ? 48.365 -22.160 -10.400 1.00 14.88 ?  123 LEU   B HD21 1 
ATOM   5957 H  HD22 . LEU   B 1 123 ? 47.799 -21.148 -11.487 1.00 14.88 ?  123 LEU   B HD22 1 
ATOM   5958 H  HD23 . LEU   B 1 123 ? 48.053 -20.655 -9.998  1.00 14.88 ?  123 LEU   B HD23 1 
ATOM   5959 N  N    . ALA   B 1 124 ? 43.499 -22.384 -8.180  1.00 10.26 ?  124 ALA   B N    1 
ATOM   5960 C  CA   . ALA   B 1 124 ? 43.246 -22.713 -6.783  1.00 10.36 ?  124 ALA   B CA   1 
ATOM   5961 C  C    . ALA   B 1 124 ? 43.518 -24.174 -6.460  1.00 10.42 ?  124 ALA   B C    1 
ATOM   5962 O  O    . ALA   B 1 124 ? 43.373 -25.049 -7.327  1.00 10.74 ?  124 ALA   B O    1 
ATOM   5963 C  CB   . ALA   B 1 124 ? 41.790 -22.411 -6.407  1.00 11.09 ?  124 ALA   B CB   1 
ATOM   5964 H  H    . ALA   B 1 124 ? 43.347 -23.023 -8.740  1.00 12.30 ?  124 ALA   B H    1 
ATOM   5965 H  HA   . ALA   B 1 124 ? 43.821 -22.163 -6.230  1.00 12.42 ?  124 ALA   B HA   1 
ATOM   5966 H  HB1  . ALA   B 1 124 ? 41.645 -22.633 -5.475  1.00 13.30 ?  124 ALA   B HB1  1 
ATOM   5967 H  HB2  . ALA   B 1 124 ? 41.620 -21.462 -6.548  1.00 13.30 ?  124 ALA   B HB2  1 
ATOM   5968 H  HB3  . ALA   B 1 124 ? 41.201 -22.935 -6.970  1.00 13.30 ?  124 ALA   B HB3  1 
ATOM   5969 N  N    . PRO   B 1 125 ? 43.820 -24.470 -5.199  1.00 10.58 ?  125 PRO   B N    1 
ATOM   5970 C  CA   . PRO   B 1 125 ? 43.747 -25.838 -4.684  1.00 11.19 ?  125 PRO   B CA   1 
ATOM   5971 C  C    . PRO   B 1 125 ? 42.344 -26.102 -4.133  1.00 11.31 ?  125 PRO   B C    1 
ATOM   5972 O  O    . PRO   B 1 125 ? 41.550 -25.182 -3.925  1.00 11.61 ?  125 PRO   B O    1 
ATOM   5973 C  CB   . PRO   B 1 125 ? 44.741 -25.782 -3.521  1.00 12.33 ?  125 PRO   B CB   1 
ATOM   5974 C  CG   . PRO   B 1 125 ? 44.505 -24.390 -2.939  1.00 11.99 ?  125 PRO   B CG   1 
ATOM   5975 C  CD   . PRO   B 1 125 ? 44.152 -23.512 -4.131  1.00 11.01 ?  125 PRO   B CD   1 
ATOM   5976 H  HA   . PRO   B 1 125 ? 44.010 -26.505 -5.341  1.00 13.42 ?  125 PRO   B HA   1 
ATOM   5977 H  HB2  . PRO   B 1 125 ? 44.532 -26.474 -2.868  1.00 14.79 ?  125 PRO   B HB2  1 
ATOM   5978 H  HB3  . PRO   B 1 125 ? 45.649 -25.880 -3.848  1.00 14.79 ?  125 PRO   B HB3  1 
ATOM   5979 H  HG2  . PRO   B 1 125 ? 43.769 -24.412 -2.307  1.00 14.38 ?  125 PRO   B HG2  1 
ATOM   5980 H  HG3  . PRO   B 1 125 ? 45.315 -24.070 -2.505  1.00 14.38 ?  125 PRO   B HG3  1 
ATOM   5981 H  HD2  . PRO   B 1 125 ? 43.390 -22.956 -3.930  1.00 13.20 ?  125 PRO   B HD2  1 
ATOM   5982 H  HD3  . PRO   B 1 125 ? 44.925 -22.975 -4.389  1.00 13.20 ?  125 PRO   B HD3  1 
ATOM   5983 N  N    . LEU   B 1 126 ? 42.074 -27.379 -3.840  1.00 11.90 ?  126 LEU   B N    1 
ATOM   5984 C  CA   . LEU   B 1 126 ? 40.858 -27.743 -3.121  1.00 12.46 ?  126 LEU   B CA   1 
ATOM   5985 C  C    . LEU   B 1 126 ? 40.982 -27.340 -1.659  1.00 12.61 ?  126 LEU   B C    1 
ATOM   5986 O  O    . LEU   B 1 126 ? 41.877 -27.802 -0.945  1.00 15.08 ?  126 LEU   B O    1 
ATOM   5987 C  CB   . LEU   B 1 126 ? 40.599 -29.239 -3.231  1.00 13.55 ?  126 LEU   B CB   1 
ATOM   5988 C  CG   . LEU   B 1 126 ? 40.076 -29.724 -4.584  1.00 15.07 ?  126 LEU   B CG   1 
ATOM   5989 C  CD1  . LEU   B 1 126 ? 40.106 -31.243 -4.628  1.00 16.54 ?  126 LEU   B CD1  1 
ATOM   5990 C  CD2  . LEU   B 1 126 ? 38.667 -29.210 -4.867  1.00 15.09 ?  126 LEU   B CD2  1 
ATOM   5991 H  H    . LEU   B 1 126 ? 42.584 -28.046 -4.036  1.00 14.27 ?  126 LEU   B H    1 
ATOM   5992 H  HA   . LEU   B 1 126 ? 40.105 -27.263 -3.509  1.00 14.94 ?  126 LEU   B HA   1 
ATOM   5993 H  HB2  . LEU   B 1 126 ? 41.431 -29.700 -3.058  1.00 16.25 ?  126 LEU   B HB2  1 
ATOM   5994 H  HB3  . LEU   B 1 126 ? 39.943 -29.480 -2.564  1.00 16.25 ?  126 LEU   B HB3  1 
ATOM   5995 H  HG   . LEU   B 1 126 ? 40.662 -29.394 -5.286  1.00 18.07 ?  126 LEU   B HG   1 
ATOM   5996 H  HD11 . LEU   B 1 126 ? 39.767 -31.541 -5.488  1.00 19.83 ?  126 LEU   B HD11 1 
ATOM   5997 H  HD12 . LEU   B 1 126 ? 41.015 -31.549 -4.504  1.00 19.83 ?  126 LEU   B HD12 1 
ATOM   5998 H  HD13 . LEU   B 1 126 ? 39.539 -31.588 -3.916  1.00 19.83 ?  126 LEU   B HD13 1 
ATOM   5999 H  HD21 . LEU   B 1 126 ? 38.335 -29.627 -5.676  1.00 18.10 ?  126 LEU   B HD21 1 
ATOM   6000 H  HD22 . LEU   B 1 126 ? 38.095 -29.432 -4.118  1.00 18.10 ?  126 LEU   B HD22 1 
ATOM   6001 H  HD23 . LEU   B 1 126 ? 38.699 -28.245 -4.982  1.00 18.10 ?  126 LEU   B HD23 1 
ATOM   6002 N  N    . LEU   B 1 127 ? 40.048 -26.518 -1.196  1.00 12.61 ?  127 LEU   B N    1 
ATOM   6003 C  CA   . LEU   B 1 127 ? 40.102 -26.029 0.170   1.00 13.32 ?  127 LEU   B CA   1 
ATOM   6004 C  C    . LEU   B 1 127 ? 39.814 -27.144 1.164   1.00 12.99 ?  127 LEU   B C    1 
ATOM   6005 O  O    . LEU   B 1 127 ? 38.993 -28.036 0.932   1.00 13.25 ?  127 LEU   B O    1 
ATOM   6006 C  CB   . LEU   B 1 127 ? 39.092 -24.905 0.380   1.00 13.37 ?  127 LEU   B CB   1 
ATOM   6007 C  CG   . LEU   B 1 127 ? 39.290 -23.645 -0.462  1.00 13.91 ?  127 LEU   B CG   1 
ATOM   6008 C  CD1  . LEU   B 1 127 ? 38.172 -22.658 -0.154  1.00 14.17 ?  127 LEU   B CD1  1 
ATOM   6009 C  CD2  . LEU   B 1 127 ? 40.657 -23.013 -0.221  1.00 14.65 ?  127 LEU   B CD2  1 
ATOM   6010 H  H    . LEU   B 1 127 ? 39.373 -26.224 -1.653  1.00 15.12 ?  127 LEU   B H    1 
ATOM   6011 H  HA   . LEU   B 1 127 ? 40.989 -25.677 0.347   1.00 15.98 ?  127 LEU   B HA   1 
ATOM   6012 H  HB2  . LEU   B 1 127 ? 38.206 -25.249 0.178   1.00 16.03 ?  127 LEU   B HB2  1 
ATOM   6013 H  HB3  . LEU   B 1 127 ? 39.124 -24.636 1.312   1.00 16.03 ?  127 LEU   B HB3  1 
ATOM   6014 H  HG   . LEU   B 1 127 ? 39.224 -23.877 -1.399  1.00 16.68 ?  127 LEU   B HG   1 
ATOM   6015 H  HD11 . LEU   B 1 127 ? 38.309 -21.854 -0.682  1.00 17.00 ?  127 LEU   B HD11 1 
ATOM   6016 H  HD12 . LEU   B 1 127 ? 37.321 -23.060 -0.376  1.00 17.00 ?  127 LEU   B HD12 1 
ATOM   6017 H  HD13 . LEU   B 1 127 ? 38.199 -22.436 0.792   1.00 17.00 ?  127 LEU   B HD13 1 
ATOM   6018 H  HD21 . LEU   B 1 127 ? 40.700 -22.162 -0.680  1.00 17.57 ?  127 LEU   B HD21 1 
ATOM   6019 H  HD22 . LEU   B 1 127 ? 40.781 -22.881 0.734   1.00 17.57 ?  127 LEU   B HD22 1 
ATOM   6020 H  HD23 . LEU   B 1 127 ? 41.343 -23.610 -0.561  1.00 17.57 ?  127 LEU   B HD23 1 
ATOM   6021 N  N    . SER   B 1 128 ? 40.491 -27.062 2.300   1.00 13.01 ?  128 SER   B N    1 
ATOM   6022 C  CA   . SER   B 1 128 ? 40.365 -27.966 3.429   1.00 13.76 ?  128 SER   B CA   1 
ATOM   6023 C  C    . SER   B 1 128 ? 40.850 -29.381 3.115   1.00 14.75 ?  128 SER   B C    1 
ATOM   6024 O  O    . SER   B 1 128 ? 40.747 -30.248 3.982   1.00 16.29 ?  128 SER   B O    1 
ATOM   6025 C  CB   . SER   B 1 128 ? 38.959 -27.958 4.056   1.00 13.63 ?  128 SER   B CB   1 
ATOM   6026 O  OG   . SER   B 1 128 ? 38.668 -26.675 4.605   1.00 14.30 ?  128 SER   B OG   1 
ATOM   6027 H  H    . SER   B 1 128 ? 41.062 -26.434 2.448   1.00 15.60 ?  128 SER   B H    1 
ATOM   6028 H  HA   . SER   B 1 128 ? 40.956 -27.637 4.109   1.00 16.50 ?  128 SER   B HA   1 
ATOM   6029 H  HB2  . SER   B 1 128 ? 38.300 -28.183 3.378   1.00 16.35 ?  128 SER   B HB2  1 
ATOM   6030 H  HB3  . SER   B 1 128 ? 38.930 -28.620 4.772   1.00 16.35 ?  128 SER   B HB3  1 
ATOM   6031 H  HG   . SER   B 1 128 ? 39.244 -26.473 5.175   1.00 17.15 ?  128 SER   B HG   1 
ATOM   6032 N  N    . ALA   B 1 129 ? 41.413 -29.625 1.927   1.00 15.82 ?  129 ALA   B N    1 
ATOM   6033 C  CA   . ALA   B 1 129 ? 41.959 -30.922 1.565   1.00 16.81 ?  129 ALA   B CA   1 
ATOM   6034 C  C    . ALA   B 1 129 ? 43.356 -31.097 2.154   1.00 15.68 ?  129 ALA   B C    1 
ATOM   6035 O  O    . ALA   B 1 129 ? 43.915 -30.200 2.801   1.00 15.35 ?  129 ALA   B O    1 
ATOM   6036 C  CB   . ALA   B 1 129 ? 42.003 -31.073 0.044   1.00 18.88 ?  129 ALA   B CB   1 
ATOM   6037 H  H    . ALA   B 1 129 ? 41.485 -29.036 1.293   1.00 18.98 ?  129 ALA   B H    1 
ATOM   6038 H  HA   . ALA   B 1 129 ? 41.384 -31.616 1.915   1.00 20.16 ?  129 ALA   B HA   1 
ATOM   6039 H  HB1  . ALA   B 1 129 ? 42.360 -31.947 -0.179  1.00 22.65 ?  129 ALA   B HB1  1 
ATOM   6040 H  HB2  . ALA   B 1 129 ? 41.105 -30.983 -0.312  1.00 22.65 ?  129 ALA   B HB2  1 
ATOM   6041 H  HB3  . ALA   B 1 129 ? 42.575 -30.380 -0.328  1.00 22.65 ?  129 ALA   B HB3  1 
ATOM   6042 N  N    . GLY   B 1 130 ? 43.924 -32.276 1.916   1.00 15.76 ?  130 GLY   B N    1 
ATOM   6043 C  CA   . GLY   B 1 130 ? 45.316 -32.505 2.256   1.00 16.07 ?  130 GLY   B CA   1 
ATOM   6044 C  C    . GLY   B 1 130 ? 45.541 -32.404 3.745   1.00 15.98 ?  130 GLY   B C    1 
ATOM   6045 O  O    . GLY   B 1 130 ? 44.843 -33.044 4.544   1.00 17.01 ?  130 GLY   B O    1 
ATOM   6046 H  H    . GLY   B 1 130 ? 43.532 -32.949 1.548   1.00 18.90 ?  130 GLY   B H    1 
ATOM   6047 H  HA2  . GLY   B 1 130 ? 45.582 -33.393 1.961   1.00 19.27 ?  130 GLY   B HA2  1 
ATOM   6048 H  HA3  . GLY   B 1 130 ? 45.876 -31.853 1.810   1.00 19.27 ?  130 GLY   B HA3  1 
ATOM   6049 N  N    . ILE   B 1 131 ? 46.520 -31.578 4.129   1.00 16.45 ?  131 ILE   B N    1 
ATOM   6050 C  CA   . ILE   B 1 131 ? 46.897 -31.450 5.528   1.00 17.51 ?  131 ILE   B CA   1 
ATOM   6051 C  C    . ILE   B 1 131 ? 45.786 -30.859 6.378   1.00 16.76 ?  131 ILE   B C    1 
ATOM   6052 O  O    . ILE   B 1 131 ? 45.866 -30.924 7.605   1.00 18.05 ?  131 ILE   B O    1 
ATOM   6053 C  CB   . ILE   B 1 131 ? 48.220 -30.664 5.722   1.00 19.24 ?  131 ILE   B CB   1 
ATOM   6054 C  CG1  . ILE   B 1 131 ? 48.049 -29.185 5.350   1.00 20.28 ?  131 ILE   B CG1  1 
ATOM   6055 C  CG2  . ILE   B 1 131 ? 49.349 -31.292 4.911   1.00 20.05 ?  131 ILE   B CG2  1 
ATOM   6056 C  CD1  . ILE   B 1 131 ? 49.268 -28.334 5.643   1.00 21.41 ?  131 ILE   B CD1  1 
ATOM   6057 H  H    . ILE   B 1 131 ? 46.972 -31.076 3.591   1.00 19.73 ?  131 ILE   B H    1 
ATOM   6058 H  HA   . ILE   B 1 131 ? 47.055 -32.340 5.868   1.00 21.01 ?  131 ILE   B HA   1 
ATOM   6059 H  HB   . ILE   B 1 131 ? 48.457 -30.710 6.662   1.00 23.07 ?  131 ILE   B HB   1 
ATOM   6060 H  HG12 . ILE   B 1 131 ? 47.858 -29.123 4.401   1.00 24.32 ?  131 ILE   B HG12 1 
ATOM   6061 H  HG13 . ILE   B 1 131 ? 47.304 -28.811 5.854   1.00 24.32 ?  131 ILE   B HG13 1 
ATOM   6062 H  HG21 . ILE   B 1 131 ? 50.187 -30.886 5.178   1.00 24.05 ?  131 ILE   B HG21 1 
ATOM   6063 H  HG22 . ILE   B 1 131 ? 49.366 -32.242 5.087   1.00 24.05 ?  131 ILE   B HG22 1 
ATOM   6064 H  HG23 . ILE   B 1 131 ? 49.182 -31.128 3.970   1.00 24.05 ?  131 ILE   B HG23 1 
ATOM   6065 H  HD11 . ILE   B 1 131 ? 49.039 -27.402 5.500   1.00 25.68 ?  131 ILE   B HD11 1 
ATOM   6066 H  HD12 . ILE   B 1 131 ? 49.531 -28.474 6.565   1.00 25.68 ?  131 ILE   B HD12 1 
ATOM   6067 H  HD13 . ILE   B 1 131 ? 49.983 -28.597 5.047   1.00 25.68 ?  131 ILE   B HD13 1 
ATOM   6068 N  N    . PHE   B 1 132 ? 44.747 -30.289 5.758   1.00 15.51 ?  132 PHE   B N    1 
ATOM   6069 C  CA   . PHE   B 1 132 ? 43.602 -29.768 6.499   1.00 16.04 ?  132 PHE   B CA   1 
ATOM   6070 C  C    . PHE   B 1 132 ? 42.575 -30.850 6.835   1.00 17.53 ?  132 PHE   B C    1 
ATOM   6071 O  O    . PHE   B 1 132 ? 41.674 -30.594 7.643   1.00 19.17 ?  132 PHE   B O    1 
ATOM   6072 C  CB   . PHE   B 1 132 ? 42.917 -28.641 5.717   1.00 15.04 ?  132 PHE   B CB   1 
ATOM   6073 C  CG   . PHE   B 1 132 ? 43.614 -27.298 5.810   1.00 14.48 ?  132 PHE   B CG   1 
ATOM   6074 C  CD1  . PHE   B 1 132 ? 44.907 -27.122 5.341   1.00 15.89 ?  132 PHE   B CD1  1 
ATOM   6075 C  CD2  . PHE   B 1 132 ? 42.935 -26.200 6.312   1.00 14.13 ?  132 PHE   B CD2  1 
ATOM   6076 C  CE1  . PHE   B 1 132 ? 45.518 -25.883 5.415   1.00 16.25 ?  132 PHE   B CE1  1 
ATOM   6077 C  CE2  . PHE   B 1 132 ? 43.537 -24.958 6.381   1.00 14.58 ?  132 PHE   B CE2  1 
ATOM   6078 C  CZ   . PHE   B 1 132 ? 44.828 -24.805 5.932   1.00 15.52 ?  132 PHE   B CZ   1 
ATOM   6079 H  H    . PHE   B 1 132 ? 44.685 -30.194 4.907   1.00 18.60 ?  132 PHE   B H    1 
ATOM   6080 H  HA   . PHE   B 1 132 ? 43.922 -29.399 7.334   1.00 19.24 ?  132 PHE   B HA   1 
ATOM   6081 H  HB2  . PHE   B 1 132 ? 42.888 -28.897 4.785   1.00 18.04 ?  132 PHE   B HB2  1 
ATOM   6082 H  HB3  . PHE   B 1 132 ? 42.016 -28.539 6.061   1.00 18.04 ?  132 PHE   B HB3  1 
ATOM   6083 H  HD1  . PHE   B 1 132 ? 45.374 -27.855 4.998   1.00 19.06 ?  132 PHE   B HD1  1 
ATOM   6084 H  HD2  . PHE   B 1 132 ? 42.060 -26.308 6.619   1.00 16.94 ?  132 PHE   B HD2  1 
ATOM   6085 H  HE1  . PHE   B 1 132 ? 46.389 -25.781 5.112   1.00 19.48 ?  132 PHE   B HE1  1 
ATOM   6086 H  HE2  . PHE   B 1 132 ? 43.070 -24.235 6.734   1.00 17.48 ?  132 PHE   B HE2  1 
ATOM   6087 H  HZ   . PHE   B 1 132 ? 45.238 -23.972 5.982   1.00 18.61 ?  132 PHE   B HZ   1 
ATOM   6088 N  N    . GLY   B 1 133 ? 42.668 -32.040 6.227   1.00 16.99 ?  133 GLY   B N    1 
ATOM   6089 C  CA   . GLY   B 1 133 ? 41.965 -33.208 6.723   1.00 17.95 ?  133 GLY   B CA   1 
ATOM   6090 C  C    . GLY   B 1 133 ? 40.570 -33.474 6.189   1.00 18.58 ?  133 GLY   B C    1 
ATOM   6091 O  O    . GLY   B 1 133 ? 39.983 -34.497 6.559   1.00 20.54 ?  133 GLY   B O    1 
ATOM   6092 H  H    . GLY   B 1 133 ? 43.133 -32.182 5.516   1.00 20.38 ?  133 GLY   B H    1 
ATOM   6093 H  HA2  . GLY   B 1 133 ? 42.505 -33.990 6.528   1.00 21.53 ?  133 GLY   B HA2  1 
ATOM   6094 H  HA3  . GLY   B 1 133 ? 41.897 -33.133 7.687   1.00 21.53 ?  133 GLY   B HA3  1 
ATOM   6095 N  N    . ALA   B 1 134 ? 40.010 -32.611 5.347   1.00 17.84 ?  134 ALA   B N    1 
ATOM   6096 C  CA   . ALA   B 1 134 ? 38.684 -32.892 4.815   1.00 17.74 ?  134 ALA   B CA   1 
ATOM   6097 C  C    . ALA   B 1 134 ? 38.772 -33.872 3.649   1.00 17.57 ?  134 ALA   B C    1 
ATOM   6098 O  O    . ALA   B 1 134 ? 39.825 -34.048 3.028   1.00 18.49 ?  134 ALA   B O    1 
ATOM   6099 C  CB   . ALA   B 1 134 ? 37.989 -31.606 4.365   1.00 18.12 ?  134 ALA   B CB   1 
ATOM   6100 H  H    . ALA   B 1 134 ? 40.366 -31.874 5.079   1.00 21.39 ?  134 ALA   B H    1 
ATOM   6101 H  HA   . ALA   B 1 134 ? 38.144 -33.300 5.509   1.00 21.27 ?  134 ALA   B HA   1 
ATOM   6102 H  HB1  . ALA   B 1 134 ? 37.101 -31.829 4.041   1.00 21.73 ?  134 ALA   B HB1  1 
ATOM   6103 H  HB2  . ALA   B 1 134 ? 37.923 -31.005 5.122   1.00 21.73 ?  134 ALA   B HB2  1 
ATOM   6104 H  HB3  . ALA   B 1 134 ? 38.508 -31.198 3.658   1.00 21.73 ?  134 ALA   B HB3  1 
ATOM   6105 N  N    . ASP   B 1 135 ? 37.643 -34.507 3.353   1.00 18.07 ?  135 ASP   B N    1 
ATOM   6106 C  CA   . ASP   B 1 135 ? 37.551 -35.392 2.201   1.00 18.80 ?  135 ASP   B CA   1 
ATOM   6107 C  C    . ASP   B 1 135 ? 37.645 -34.546 0.938   1.00 17.34 ?  135 ASP   B C    1 
ATOM   6108 O  O    . ASP   B 1 135 ? 36.784 -33.679 0.720   1.00 17.16 ?  135 ASP   B O    1 
ATOM   6109 C  CB   . ASP   B 1 135 ? 36.216 -36.131 2.245   1.00 20.62 ?  135 ASP   B CB   1 
ATOM   6110 C  CG   . ASP   B 1 135 ? 36.053 -37.125 1.110   1.00 22.32 ?  135 ASP   B CG   1 
ATOM   6111 O  OD1  . ASP   B 1 135 ? 36.933 -37.183 0.225   1.00 22.37 ?  135 ASP   B OD1  1 
ATOM   6112 O  OD2  . ASP   B 1 135 ? 35.040 -37.862 1.114   1.00 25.22 -1 135 ASP   B OD2  1 
ATOM   6113 H  H    . ASP   B 1 135 ? 36.910 -34.431 3.797   1.00 21.67 ?  135 ASP   B H    1 
ATOM   6114 H  HA   . ASP   B 1 135 ? 38.271 -36.041 2.226   1.00 22.55 ?  135 ASP   B HA   1 
ATOM   6115 H  HB2  . ASP   B 1 135 ? 36.154 -36.614 3.083   1.00 24.73 ?  135 ASP   B HB2  1 
ATOM   6116 H  HB3  . ASP   B 1 135 ? 35.498 -35.489 2.173   1.00 24.73 ?  135 ASP   B HB3  1 
ATOM   6117 N  N    . PRO   B 1 136 ? 38.654 -34.748 0.086   1.00 17.31 ?  136 PRO   B N    1 
ATOM   6118 C  CA   . PRO   B 1 136 ? 38.740 -33.928 -1.132  1.00 16.54 ?  136 PRO   B CA   1 
ATOM   6119 C  C    . PRO   B 1 136 ? 37.546 -34.087 -2.051  1.00 15.61 ?  136 PRO   B C    1 
ATOM   6120 O  O    . PRO   B 1 136 ? 37.212 -33.145 -2.775  1.00 14.76 ?  136 PRO   B O    1 
ATOM   6121 C  CB   . PRO   B 1 136 ? 40.049 -34.397 -1.786  1.00 17.60 ?  136 PRO   B CB   1 
ATOM   6122 C  CG   . PRO   B 1 136 ? 40.282 -35.763 -1.225  1.00 18.50 ?  136 PRO   B CG   1 
ATOM   6123 C  CD   . PRO   B 1 136 ? 39.766 -35.707 0.178   1.00 18.22 ?  136 PRO   B CD   1 
ATOM   6124 H  HA   . PRO   B 1 136 ? 38.827 -32.992 -0.899  1.00 19.84 ?  136 PRO   B HA   1 
ATOM   6125 H  HB2  . PRO   B 1 136 ? 39.945 -34.435 -2.751  1.00 21.10 ?  136 PRO   B HB2  1 
ATOM   6126 H  HB3  . PRO   B 1 136 ? 40.770 -33.798 -1.542  1.00 21.10 ?  136 PRO   B HB3  1 
ATOM   6127 H  HG2  . PRO   B 1 136 ? 39.789 -36.421 -1.743  1.00 22.19 ?  136 PRO   B HG2  1 
ATOM   6128 H  HG3  . PRO   B 1 136 ? 41.230 -35.965 -1.231  1.00 22.19 ?  136 PRO   B HG3  1 
ATOM   6129 H  HD2  . PRO   B 1 136 ? 39.442 -36.579 0.456   1.00 21.86 ?  136 PRO   B HD2  1 
ATOM   6130 H  HD3  . PRO   B 1 136 ? 40.446 -35.369 0.782   1.00 21.86 ?  136 PRO   B HD3  1 
ATOM   6131 N  N    . ILE   B 1 137 ? 36.895 -35.252 -2.055  1.00 16.07 ?  137 ILE   B N    1 
ATOM   6132 C  CA   . ILE   B 1 137 ? 35.673 -35.419 -2.836  1.00 16.83 ?  137 ILE   B CA   1 
ATOM   6133 C  C    . ILE   B 1 137 ? 34.602 -34.446 -2.355  1.00 16.45 ?  137 ILE   B C    1 
ATOM   6134 O  O    . ILE   B 1 137 ? 33.877 -33.840 -3.156  1.00 16.04 ?  137 ILE   B O    1 
ATOM   6135 C  CB   . ILE   B 1 137 ? 35.197 -36.885 -2.769  1.00 19.04 ?  137 ILE   B CB   1 
ATOM   6136 C  CG1  . ILE   B 1 137 ? 36.189 -37.795 -3.494  1.00 21.20 ?  137 ILE   B CG1  1 
ATOM   6137 C  CG2  . ILE   B 1 137 ? 33.814 -37.031 -3.377  1.00 19.52 ?  137 ILE   B CG2  1 
ATOM   6138 C  CD1  . ILE   B 1 137 ? 35.857 -39.274 -3.383  1.00 23.17 ?  137 ILE   B CD1  1 
ATOM   6139 H  H    . ILE   B 1 137 ? 37.145 -35.953 -1.632  1.00 19.28 ?  137 ILE   B H    1 
ATOM   6140 H  HA   . ILE   B 1 137 ? 35.860 -35.215 -3.770  1.00 20.19 ?  137 ILE   B HA   1 
ATOM   6141 H  HB   . ILE   B 1 137 ? 35.155 -37.154 -1.842  1.00 22.84 ?  137 ILE   B HB   1 
ATOM   6142 H  HG12 . ILE   B 1 137 ? 36.198 -37.572 -4.438  1.00 25.43 ?  137 ILE   B HG12 1 
ATOM   6143 H  HG13 . ILE   B 1 137 ? 37.072 -37.668 -3.117  1.00 25.43 ?  137 ILE   B HG13 1 
ATOM   6144 H  HG21 . ILE   B 1 137 ? 33.538 -37.959 -3.336  1.00 23.42 ?  137 ILE   B HG21 1 
ATOM   6145 H  HG22 . ILE   B 1 137 ? 33.184 -36.495 -2.879  1.00 23.42 ?  137 ILE   B HG22 1 
ATOM   6146 H  HG23 . ILE   B 1 137 ? 33.844 -36.738 -4.302  1.00 23.42 ?  137 ILE   B HG23 1 
ATOM   6147 H  HD11 . ILE   B 1 137 ? 36.487 -39.766 -3.925  1.00 27.79 ?  137 ILE   B HD11 1 
ATOM   6148 H  HD12 . ILE   B 1 137 ? 35.927 -39.547 -2.454  1.00 27.79 ?  137 ILE   B HD12 1 
ATOM   6149 H  HD13 . ILE   B 1 137 ? 34.959 -39.438 -3.710  1.00 27.79 ?  137 ILE   B HD13 1 
ATOM   6150 N  N    . HIS   B 1 138 ? 34.470 -34.303 -1.038  1.00 16.35 ?  138 HIS   B N    1 
ATOM   6151 C  CA   . HIS   B 1 138 ? 33.523 -33.334 -0.499  1.00 16.72 ?  138 HIS   B CA   1 
ATOM   6152 C  C    . HIS   B 1 138 ? 33.936 -31.905 -0.824  1.00 15.68 ?  138 HIS   B C    1 
ATOM   6153 O  O    . HIS   B 1 138 ? 33.088 -31.061 -1.128  1.00 15.98 ?  138 HIS   B O    1 
ATOM   6154 C  CB   . HIS   B 1 138 ? 33.410 -33.512 1.007   1.00 17.94 ?  138 HIS   B CB   1 
ATOM   6155 C  CG   . HIS   B 1 138 ? 32.493 -32.525 1.649   1.00 19.24 ?  138 HIS   B CG   1 
ATOM   6156 N  ND1  . HIS   B 1 138 ? 31.150 -32.455 1.347   1.00 20.67 ?  138 HIS   B ND1  1 
ATOM   6157 C  CD2  . HIS   B 1 138 ? 32.726 -31.548 2.557   1.00 19.65 ?  138 HIS   B CD2  1 
ATOM   6158 C  CE1  . HIS   B 1 138 ? 30.593 -31.485 2.049   1.00 20.78 ?  138 HIS   B CE1  1 
ATOM   6159 N  NE2  . HIS   B 1 138 ? 31.527 -30.922 2.796   1.00 20.33 ?  138 HIS   B NE2  1 
ATOM   6160 H  H    . HIS   B 1 138 ? 34.913 -34.748 -0.449  1.00 19.60 ?  138 HIS   B H    1 
ATOM   6161 H  HA   . HIS   B 1 138 ? 32.652 -33.496 -0.891  1.00 20.06 ?  138 HIS   B HA   1 
ATOM   6162 H  HB2  . HIS   B 1 138 ? 33.064 -34.403 1.193   1.00 21.52 ?  138 HIS   B HB2  1 
ATOM   6163 H  HB3  . HIS   B 1 138 ? 34.285 -33.410 1.406   1.00 21.52 ?  138 HIS   B HB3  1 
ATOM   6164 H  HD1  . HIS   B 1 138 ? 30.736 -32.969 0.791   1.00 24.79 ?  138 HIS   B HD1  1 
ATOM   6165 H  HD2  . HIS   B 1 138 ? 33.538 -31.348 2.957   1.00 23.57 ?  138 HIS   B HD2  1 
ATOM   6166 H  HE1  . HIS   B 1 138 ? 29.690 -31.250 2.032   1.00 24.92 ?  138 HIS   B HE1  1 
ATOM   6167 N  N    . SER   B 1 139 ? 35.230 -31.608 -0.753  1.00 15.26 ?  139 SER   B N    1 
ATOM   6168 C  CA   . SER   B 1 139 ? 35.669 -30.261 -1.067  1.00 14.44 ?  139 SER   B CA   1 
ATOM   6169 C  C    . SER   B 1 139 ? 35.340 -29.904 -2.507  1.00 13.50 ?  139 SER   B C    1 
ATOM   6170 O  O    . SER   B 1 139 ? 34.892 -28.786 -2.786  1.00 13.75 ?  139 SER   B O    1 
ATOM   6171 C  CB   . SER   B 1 139 ? 37.161 -30.125 -0.799  1.00 14.45 ?  139 SER   B CB   1 
ATOM   6172 O  OG   . SER   B 1 139 ? 37.584 -28.800 -1.064  1.00 14.83 ?  139 SER   B OG   1 
ATOM   6173 H  H    . SER   B 1 139 ? 35.857 -32.152 -0.540  1.00 18.29 ?  139 SER   B H    1 
ATOM   6174 H  HA   . SER   B 1 139 ? 35.197 -29.632 -0.500  1.00 17.31 ?  139 SER   B HA   1 
ATOM   6175 H  HB2  . SER   B 1 139 ? 37.336 -30.334 0.129   1.00 17.33 ?  139 SER   B HB2  1 
ATOM   6176 H  HB3  . SER   B 1 139 ? 37.648 -30.725 -1.380  1.00 17.33 ?  139 SER   B HB3  1 
ATOM   6177 H  HG   . SER   B 1 139 ? 38.412 -28.720 -0.905  1.00 17.79 ?  139 SER   B HG   1 
ATOM   6178 N  N    . LEU   B 1 140 ? 35.526 -30.850 -3.432  1.00 13.65 ?  140 LEU   B N    1 
ATOM   6179 C  CA   . LEU   B 1 140 ? 35.162 -30.602 -4.821  1.00 13.61 ?  140 LEU   B CA   1 
ATOM   6180 C  C    . LEU   B 1 140 ? 33.661 -30.369 -4.956  1.00 13.90 ?  140 LEU   B C    1 
ATOM   6181 O  O    . LEU   B 1 140 ? 33.229 -29.479 -5.694  1.00 13.74 ?  140 LEU   B O    1 
ATOM   6182 C  CB   . LEU   B 1 140 ? 35.622 -31.766 -5.699  1.00 13.60 ?  140 LEU   B CB   1 
ATOM   6183 C  CG   . LEU   B 1 140 ? 35.273 -31.656 -7.175  1.00 14.11 ?  140 LEU   B CG   1 
ATOM   6184 C  CD1  . LEU   B 1 140 ? 35.856 -30.392 -7.772  1.00 14.91 ?  140 LEU   B CD1  1 
ATOM   6185 C  CD2  . LEU   B 1 140 ? 35.745 -32.893 -7.916  1.00 15.06 ?  140 LEU   B CD2  1 
ATOM   6186 H  H    . LEU   B 1 140 ? 35.847 -31.631 -3.284  1.00 16.36 ?  140 LEU   B H    1 
ATOM   6187 H  HA   . LEU   B 1 140 ? 35.619 -29.804 -5.130  1.00 16.32 ?  140 LEU   B HA   1 
ATOM   6188 H  HB2  . LEU   B 1 140 ? 36.587 -31.841 -5.633  1.00 16.31 ?  140 LEU   B HB2  1 
ATOM   6189 H  HB3  . LEU   B 1 140 ? 35.211 -32.582 -5.370  1.00 16.31 ?  140 LEU   B HB3  1 
ATOM   6190 H  HG   . LEU   B 1 140 ? 34.312 -31.598 -7.266  1.00 16.93 ?  140 LEU   B HG   1 
ATOM   6191 H  HD11 . LEU   B 1 140 ? 35.743 -30.422 -8.734  1.00 17.88 ?  140 LEU   B HD11 1 
ATOM   6192 H  HD12 . LEU   B 1 140 ? 35.390 -29.624 -7.407  1.00 17.88 ?  140 LEU   B HD12 1 
ATOM   6193 H  HD13 . LEU   B 1 140 ? 36.799 -30.346 -7.550  1.00 17.88 ?  140 LEU   B HD13 1 
ATOM   6194 H  HD21 . LEU   B 1 140 ? 35.511 -32.801 -8.854  1.00 18.07 ?  140 LEU   B HD21 1 
ATOM   6195 H  HD22 . LEU   B 1 140 ? 36.701 -32.976 -7.816  1.00 18.07 ?  140 LEU   B HD22 1 
ATOM   6196 H  HD23 . LEU   B 1 140 ? 35.297 -33.666 -7.540  1.00 18.07 ?  140 LEU   B HD23 1 
ATOM   6197 N  N    . ARG   B 1 141 ? 32.854 -31.162 -4.246  1.00 14.17 ?  141 ARG   B N    1 
ATOM   6198 C  CA   . ARG   B 1 141 ? 31.404 -30.979 -4.234  1.00 15.03 ?  141 ARG   B CA   1 
ATOM   6199 C  C    . ARG   B 1 141 ? 31.025 -29.569 -3.799  1.00 14.49 ?  141 ARG   B C    1 
ATOM   6200 O  O    . ARG   B 1 141 ? 30.234 -28.888 -4.466  1.00 14.75 ?  141 ARG   B O    1 
ATOM   6201 C  CB   . ARG   B 1 141 ? 30.802 -32.015 -3.276  1.00 16.67 ?  141 ARG   B CB   1 
ATOM   6202 C  CG   . ARG   B 1 141 ? 29.338 -31.888 -2.961  1.00 18.84 ?  141 ARG   B CG   1 
ATOM   6203 C  CD   . ARG   B 1 141 ? 28.544 -32.526 -4.032  1.00 20.67 ?  141 ARG   B CD   1 
ATOM   6204 N  NE   . ARG   B 1 141 ? 28.276 -31.606 -5.126  1.00 20.91 ?  141 ARG   B NE   1 
ATOM   6205 C  CZ   . ARG   B 1 141 ? 28.233 -31.949 -6.406  1.00 20.53 ?  141 ARG   B CZ   1 
ATOM   6206 N  NH1  . ARG   B 1 141 ? 28.623 -33.143 -6.818  1.00 20.48 ?  141 ARG   B NH1  1 
ATOM   6207 N  NH2  . ARG   B 1 141 ? 27.788 -31.068 -7.297  1.00 21.51 ?  141 ARG   B NH2  1 
ATOM   6208 H  H    . ARG   B 1 141 ? 33.128 -31.814 -3.763  1.00 16.99 ?  141 ARG   B H    1 
ATOM   6209 H  HA   . ARG   B 1 141 ? 31.047 -31.131 -5.119  1.00 18.03 ?  141 ARG   B HA   1 
ATOM   6210 H  HB2  . ARG   B 1 141 ? 30.950 -32.897 -3.657  1.00 20.00 ?  141 ARG   B HB2  1 
ATOM   6211 H  HB3  . ARG   B 1 141 ? 31.279 -31.956 -2.436  1.00 20.00 ?  141 ARG   B HB3  1 
ATOM   6212 H  HG2  . ARG   B 1 141 ? 29.155 -32.333 -2.123  1.00 22.60 ?  141 ARG   B HG2  1 
ATOM   6213 H  HG3  . ARG   B 1 141 ? 29.087 -30.947 -2.903  1.00 22.60 ?  141 ARG   B HG3  1 
ATOM   6214 H  HD2  . ARG   B 1 141 ? 29.033 -33.293 -4.379  1.00 24.80 ?  141 ARG   B HD2  1 
ATOM   6215 H  HD3  . ARG   B 1 141 ? 27.703 -32.818 -3.662  1.00 24.80 ?  141 ARG   B HD3  1 
ATOM   6216 H  HE   . ARG   B 1 141 ? 28.119 -30.785 -4.925  1.00 25.08 ?  141 ARG   B HE   1 
ATOM   6217 H  HH11 . ARG   B 1 141 ? 28.895 -33.733 -6.255  1.00 24.57 ?  141 ARG   B HH11 1 
ATOM   6218 H  HH12 . ARG   B 1 141 ? 28.584 -33.340 -7.653  1.00 24.57 ?  141 ARG   B HH12 1 
ATOM   6219 H  HH21 . ARG   B 1 141 ? 27.541 -30.283 -7.042  1.00 25.80 ?  141 ARG   B HH21 1 
ATOM   6220 H  HH22 . ARG   B 1 141 ? 27.771 -31.270 -8.133  1.00 25.80 ?  141 ARG   B HH22 1 
ATOM   6221 N  N    . VAL   B 1 142 ? 31.570 -29.123 -2.666  1.00 14.26 ?  142 VAL   B N    1 
ATOM   6222 C  CA   . VAL   B 1 142 ? 31.245 -27.789 -2.179  1.00 13.89 ?  142 VAL   B CA   1 
ATOM   6223 C  C    . VAL   B 1 142 ? 31.723 -26.735 -3.172  1.00 13.74 ?  142 VAL   B C    1 
ATOM   6224 O  O    . VAL   B 1 142 ? 31.026 -25.749 -3.435  1.00 14.08 ?  142 VAL   B O    1 
ATOM   6225 C  CB   . VAL   B 1 142 ? 31.798 -27.561 -0.757  1.00 14.44 ?  142 VAL   B CB   1 
ATOM   6226 C  CG1  . VAL   B 1 142 ? 31.486 -26.148 -0.280  1.00 14.56 ?  142 VAL   B CG1  1 
ATOM   6227 C  CG2  . VAL   B 1 142 ? 31.224 -28.578 0.209   1.00 15.24 ?  142 VAL   B CG2  1 
ATOM   6228 H  H    . VAL   B 1 142 ? 32.114 -29.565 -2.167  1.00 17.10 ?  142 VAL   B H    1 
ATOM   6229 H  HA   . VAL   B 1 142 ? 30.287 -27.707 -2.117  1.00 16.65 ?  142 VAL   B HA   1 
ATOM   6230 H  HB   . VAL   B 1 142 ? 32.766 -27.671 -0.762  1.00 17.32 ?  142 VAL   B HB   1 
ATOM   6231 H  HG11 . VAL   B 1 142 ? 31.680 -26.085 0.668   1.00 17.46 ?  142 VAL   B HG11 1 
ATOM   6232 H  HG12 . VAL   B 1 142 ? 32.045 -25.521 -0.770  1.00 17.46 ?  142 VAL   B HG12 1 
ATOM   6233 H  HG13 . VAL   B 1 142 ? 30.553 -25.962 -0.444  1.00 17.46 ?  142 VAL   B HG13 1 
ATOM   6234 H  HG21 . VAL   B 1 142 ? 31.557 -28.391 1.101   1.00 18.28 ?  142 VAL   B HG21 1 
ATOM   6235 H  HG22 . VAL   B 1 142 ? 30.257 -28.507 0.196   1.00 18.28 ?  142 VAL   B HG22 1 
ATOM   6236 H  HG23 . VAL   B 1 142 ? 31.496 -29.465 -0.067  1.00 18.28 ?  142 VAL   B HG23 1 
ATOM   6237 N  N    . CYS   B 1 143 ? 32.904 -26.938 -3.757  1.00 13.26 ?  143 CYS   B N    1 
ATOM   6238 C  CA   . CYS   B 1 143 ? 33.401 -26.002 -4.759  1.00 13.19 ?  143 CYS   B CA   1 
ATOM   6239 C  C    . CYS   B 1 143 ? 32.400 -25.858 -5.899  1.00 13.46 ?  143 CYS   B C    1 
ATOM   6240 O  O    . CYS   B 1 143 ? 32.001 -24.744 -6.260  1.00 13.56 ?  143 CYS   B O    1 
ATOM   6241 C  CB   . CYS   B 1 143 ? 34.758 -26.486 -5.282  1.00 13.20 ?  143 CYS   B CB   1 
ATOM   6242 S  SG   . CYS   B 1 143 ? 35.511 -25.394 -6.508  1.00 13.50 ?  143 CYS   B SG   1 
ATOM   6243 H  H    . CYS   B 1 143 ? 33.432 -27.592 -3.587  1.00 15.90 ?  143 CYS   B H    1 
ATOM   6244 H  HA   . CYS   B 1 143 ? 33.526 -25.124 -4.352  1.00 15.82 ?  143 CYS   B HA   1 
ATOM   6245 H  HB2  . CYS   B 1 143 ? 35.378 -26.553 -4.538  1.00 15.83 ?  143 CYS   B HB2  1 
ATOM   6246 H  HB3  . CYS   B 1 143 ? 34.642 -27.348 -5.691  1.00 15.83 ?  143 CYS   B HB3  1 
ATOM   6247 H  HG   . CYS   B 1 143 ? 36.579 -25.832 -6.826  1.00 16.19 ?  143 CYS   B HG   1 
ATOM   6248 N  N    . VAL   B 1 144 ? 31.995 -26.980 -6.490  1.00 14.03 ?  144 VAL   B N    1 
ATOM   6249 C  CA   . VAL   B 1 144 ? 31.094 -26.917 -7.634  1.00 14.86 ?  144 VAL   B CA   1 
ATOM   6250 C  C    . VAL   B 1 144 ? 29.751 -26.303 -7.264  1.00 15.12 ?  144 VAL   B C    1 
ATOM   6251 O  O    . VAL   B 1 144 ? 29.132 -25.609 -8.081  1.00 16.44 ?  144 VAL   B O    1 
ATOM   6252 C  CB   . VAL   B 1 144 ? 30.941 -28.326 -8.215  1.00 17.17 ?  144 VAL   B CB   1 
ATOM   6253 C  CG1  . VAL   B 1 144 ? 29.658 -28.461 -9.029  1.00 19.50 ?  144 VAL   B CG1  1 
ATOM   6254 C  CG2  . VAL   B 1 144 ? 32.183 -28.706 -9.027  1.00 17.66 ?  144 VAL   B CG2  1 
ATOM   6255 H  H    . VAL   B 1 144 ? 32.227 -27.772 -6.255  1.00 16.82 ?  144 VAL   B H    1 
ATOM   6256 H  HA   . VAL   B 1 144 ? 31.489 -26.357 -8.319  1.00 17.82 ?  144 VAL   B HA   1 
ATOM   6257 H  HB   . VAL   B 1 144 ? 30.881 -28.955 -7.480  1.00 20.59 ?  144 VAL   B HB   1 
ATOM   6258 H  HG11 . VAL   B 1 144 ? 29.728 -29.255 -9.591  1.00 23.39 ?  144 VAL   B HG11 1 
ATOM   6259 H  HG12 . VAL   B 1 144 ? 28.906 -28.561 -8.425  1.00 23.39 ?  144 VAL   B HG12 1 
ATOM   6260 H  HG13 . VAL   B 1 144 ? 29.546 -27.679 -9.584  1.00 23.39 ?  144 VAL   B HG13 1 
ATOM   6261 H  HG21 . VAL   B 1 144 ? 32.067 -29.602 -9.381  1.00 21.18 ?  144 VAL   B HG21 1 
ATOM   6262 H  HG22 . VAL   B 1 144 ? 32.284 -28.074 -9.760  1.00 21.18 ?  144 VAL   B HG22 1 
ATOM   6263 H  HG23 . VAL   B 1 144 ? 32.959 -28.672 -8.451  1.00 21.18 ?  144 VAL   B HG23 1 
ATOM   6264 N  N    . ASP   B 1 145 ? 29.285 -26.536 -6.040  1.00 14.91 ?  145 ASP   B N    1 
ATOM   6265 C  CA   . ASP   B 1 145 ? 27.976 -26.071 -5.608  1.00 15.81 ?  145 ASP   B CA   1 
ATOM   6266 C  C    . ASP   B 1 145 ? 28.002 -24.646 -5.072  1.00 15.38 ?  145 ASP   B C    1 
ATOM   6267 O  O    . ASP   B 1 145 ? 26.941 -24.108 -4.739  1.00 17.27 ?  145 ASP   B O    1 
ATOM   6268 C  CB   . ASP   B 1 145 ? 27.403 -26.995 -4.522  1.00 17.67 ?  145 ASP   B CB   1 
ATOM   6269 C  CG   . ASP   B 1 145 ? 27.018 -28.364 -5.041  1.00 19.48 ?  145 ASP   B CG   1 
ATOM   6270 O  OD1  . ASP   B 1 145 ? 26.897 -28.536 -6.269  1.00 19.83 ?  145 ASP   B OD1  1 
ATOM   6271 O  OD2  . ASP   B 1 145 ? 26.829 -29.261 -4.197  1.00 21.56 -1 145 ASP   B OD2  1 
ATOM   6272 H  H    . ASP   B 1 145 ? 29.726 -26.950 -5.431  1.00 17.88 ?  145 ASP   B H    1 
ATOM   6273 H  HA   . ASP   B 1 145 ? 27.376 -26.072 -6.365  1.00 18.97 ?  145 ASP   B HA   1 
ATOM   6274 H  HB2  . ASP   B 1 145 ? 28.068 -27.120 -3.835  1.00 21.19 ?  145 ASP   B HB2  1 
ATOM   6275 H  HB3  . ASP   B 1 145 ? 26.609 -26.579 -4.151  1.00 21.19 ?  145 ASP   B HB3  1 
ATOM   6276 N  N    . THR   B 1 146 ? 29.181 -24.033 -4.965  1.00 13.79 ?  146 THR   B N    1 
ATOM   6277 C  CA   . THR   B 1 146 ? 29.322 -22.714 -4.360  1.00 13.40 ?  146 THR   B CA   1 
ATOM   6278 C  C    . THR   B 1 146 ? 29.958 -21.689 -5.282  1.00 12.76 ?  146 THR   B C    1 
ATOM   6279 O  O    . THR   B 1 146 ? 29.501 -20.533 -5.337  1.00 13.26 ?  146 THR   B O    1 
ATOM   6280 C  CB   . THR   B 1 146 ? 30.154 -22.823 -3.079  1.00 13.57 ?  146 THR   B CB   1 
ATOM   6281 O  OG1  . THR   B 1 146 ? 29.569 -23.807 -2.220  1.00 13.99 ?  146 THR   B OG1  1 
ATOM   6282 C  CG2  . THR   B 1 146 ? 30.224 -21.485 -2.361  1.00 14.23 ?  146 THR   B CG2  1 
ATOM   6283 H  H    . THR   B 1 146 ? 29.929 -24.367 -5.240  1.00 16.54 ?  146 THR   B H    1 
ATOM   6284 H  HA   . THR   B 1 146 ? 28.451 -22.388 -4.111  1.00 16.06 ?  146 THR   B HA   1 
ATOM   6285 H  HB   . THR   B 1 146 ? 31.066 -23.086 -3.300  1.00 16.28 ?  146 THR   B HB   1 
ATOM   6286 H  HG1  . THR   B 1 146 ? 29.605 -24.566 -2.591  1.00 16.77 ?  146 THR   B HG1  1 
ATOM   6287 H  HG21 . THR   B 1 146 ? 30.570 -21.602 -1.464  1.00 17.06 ?  146 THR   B HG21 1 
ATOM   6288 H  HG22 . THR   B 1 146 ? 30.813 -20.877 -2.843  1.00 17.06 ?  146 THR   B HG22 1 
ATOM   6289 H  HG23 . THR   B 1 146 ? 29.341 -21.090 -2.311  1.00 17.06 ?  146 THR   B HG23 1 
ATOM   6290 N  N    . VAL   B 1 147 ? 31.023 -22.066 -5.981  1.00 12.60 ?  147 VAL   B N    1 
ATOM   6291 C  CA   . VAL   B 1 147 ? 31.741 -21.125 -6.825  1.00 12.58 ?  147 VAL   B CA   1 
ATOM   6292 C  C    . VAL   B 1 147 ? 31.011 -20.991 -8.150  1.00 12.95 ?  147 VAL   B C    1 
ATOM   6293 O  O    . VAL   B 1 147 ? 30.637 -21.991 -8.779  1.00 13.79 ?  147 VAL   B O    1 
ATOM   6294 C  CB   . VAL   B 1 147 ? 33.197 -21.575 -7.021  1.00 12.18 ?  147 VAL   B CB   1 
ATOM   6295 C  CG1  . VAL   B 1 147 ? 33.954 -20.540 -7.838  1.00 12.14 ?  147 VAL   B CG1  1 
ATOM   6296 C  CG2  . VAL   B 1 147 ? 33.867 -21.788 -5.675  1.00 12.64 ?  147 VAL   B CG2  1 
ATOM   6297 H  H    . VAL   B 1 147 ? 31.346 -22.866 -5.986  1.00 15.10 ?  147 VAL   B H    1 
ATOM   6298 H  HA   . VAL   B 1 147 ? 31.751 -20.258 -6.389  1.00 15.09 ?  147 VAL   B HA   1 
ATOM   6299 H  HB   . VAL   B 1 147 ? 33.213 -22.414 -7.505  1.00 14.60 ?  147 VAL   B HB   1 
ATOM   6300 H  HG11 . VAL   B 1 147 ? 34.897 -20.756 -7.826  1.00 14.56 ?  147 VAL   B HG11 1 
ATOM   6301 H  HG12 . VAL   B 1 147 ? 33.622 -20.550 -8.749  1.00 14.56 ?  147 VAL   B HG12 1 
ATOM   6302 H  HG13 . VAL   B 1 147 ? 33.810 -19.663 -7.444  1.00 14.56 ?  147 VAL   B HG13 1 
ATOM   6303 H  HG21 . VAL   B 1 147 ? 34.809 -21.962 -5.815  1.00 15.15 ?  147 VAL   B HG21 1 
ATOM   6304 H  HG22 . VAL   B 1 147 ? 33.751 -20.991 -5.136  1.00 15.15 ?  147 VAL   B HG22 1 
ATOM   6305 H  HG23 . VAL   B 1 147 ? 33.452 -22.548 -5.234  1.00 15.15 ?  147 VAL   B HG23 1 
ATOM   6306 N  N    . ARG   B 1 148 ? 30.815 -19.742 -8.575  1.00 12.75 ?  148 ARG   B N    1 
ATOM   6307 C  CA   . ARG   B 1 148 ? 30.183 -19.413 -9.842  1.00 12.91 ?  148 ARG   B CA   1 
ATOM   6308 C  C    . ARG   B 1 148 ? 31.138 -18.728 -10.808 1.00 13.01 ?  148 ARG   B C    1 
ATOM   6309 O  O    . ARG   B 1 148 ? 30.860 -18.710 -12.011 1.00 14.53 ?  148 ARG   B O    1 
ATOM   6310 C  CB   . ARG   B 1 148 ? 28.942 -18.533 -9.611  1.00 13.57 ?  148 ARG   B CB   1 
ATOM   6311 C  CG   . ARG   B 1 148 ? 27.870 -19.255 -8.806  1.00 14.00 ?  148 ARG   B CG   1 
ATOM   6312 C  CD   . ARG   B 1 148 ? 26.657 -18.378 -8.502  1.00 15.13 ?  148 ARG   B CD   1 
ATOM   6313 N  NE   . ARG   B 1 148 ? 27.017 -17.172 -7.764  1.00 15.15 ?  148 ARG   B NE   1 
ATOM   6314 C  CZ   . ARG   B 1 148 ? 27.335 -17.144 -6.476  1.00 14.31 ?  148 ARG   B CZ   1 
ATOM   6315 N  NH1  . ARG   B 1 148 ? 27.297 -18.236 -5.725  1.00 14.44 ?  148 ARG   B NH1  1 
ATOM   6316 N  NH2  . ARG   B 1 148 ? 27.720 -15.993 -5.930  1.00 14.32 ?  148 ARG   B NH2  1 
ATOM   6317 H  H    . ARG   B 1 148 ? 31.057 -19.043 -8.123  1.00 15.28 ?  148 ARG   B H    1 
ATOM   6318 H  HA   . ARG   B 1 148 ? 29.891 -20.235 -10.257 1.00 15.48 ?  148 ARG   B HA   1 
ATOM   6319 H  HB2  . ARG   B 1 148 ? 29.201 -17.739 -9.123  1.00 16.28 ?  148 ARG   B HB2  1 
ATOM   6320 H  HB3  . ARG   B 1 148 ? 28.564 -18.295 -10.470 1.00 16.28 ?  148 ARG   B HB3  1 
ATOM   6321 H  HG2  . ARG   B 1 148 ? 27.565 -20.029 -9.311  1.00 16.79 ?  148 ARG   B HG2  1 
ATOM   6322 H  HG3  . ARG   B 1 148 ? 28.250 -19.546 -7.962  1.00 16.79 ?  148 ARG   B HG3  1 
ATOM   6323 H  HD2  . ARG   B 1 148 ? 26.245 -18.110 -9.339  1.00 18.15 ?  148 ARG   B HD2  1 
ATOM   6324 H  HD3  . ARG   B 1 148 ? 26.026 -18.885 -7.967  1.00 18.15 ?  148 ARG   B HD3  1 
ATOM   6325 H  HE   . ARG   B 1 148 ? 27.049 -16.433 -8.198  1.00 18.17 ?  148 ARG   B HE   1 
ATOM   6326 H  HH11 . ARG   B 1 148 ? 27.052 -18.988 -6.065  1.00 17.31 ?  148 ARG   B HH11 1 
ATOM   6327 H  HH12 . ARG   B 1 148 ? 27.500 -18.192 -4.889  1.00 17.31 ?  148 ARG   B HH12 1 
ATOM   6328 H  HH21 . ARG   B 1 148 ? 27.753 -15.282 -6.409  1.00 17.18 ?  148 ARG   B HH21 1 
ATOM   6329 H  HH22 . ARG   B 1 148 ? 27.923 -15.960 -5.095  1.00 17.18 ?  148 ARG   B HH22 1 
ATOM   6330 N  N    . THR   B 1 149 ? 32.246 -18.177 -10.317 1.00 12.87 ?  149 THR   B N    1 
ATOM   6331 C  CA   . THR   B 1 149 ? 33.288 -17.619 -11.165 1.00 12.75 ?  149 THR   B CA   1 
ATOM   6332 C  C    . THR   B 1 149 ? 34.171 -18.756 -11.678 1.00 12.53 ?  149 THR   B C    1 
ATOM   6333 O  O    . THR   B 1 149 ? 33.973 -19.926 -11.343 1.00 13.12 ?  149 THR   B O    1 
ATOM   6334 C  CB   . THR   B 1 149 ? 34.062 -16.573 -10.376 1.00 12.99 ?  149 THR   B CB   1 
ATOM   6335 O  OG1  . THR   B 1 149 ? 34.518 -17.185 -9.166  1.00 12.92 ?  149 THR   B OG1  1 
ATOM   6336 C  CG2  . THR   B 1 149 ? 33.177 -15.366 -10.065 1.00 13.65 ?  149 THR   B CG2  1 
ATOM   6337 H  H    . THR   B 1 149 ? 32.408 -18.102 -9.473  1.00 15.44 ?  149 THR   B H    1 
ATOM   6338 H  HA   . THR   B 1 149 ? 32.873 -17.178 -11.927 1.00 15.28 ?  149 THR   B HA   1 
ATOM   6339 H  HB   . THR   B 1 149 ? 34.822 -16.280 -10.893 1.00 15.57 ?  149 THR   B HB   1 
ATOM   6340 H  HG1  . THR   B 1 149 ? 34.948 -16.627 -8.704  1.00 15.49 ?  149 THR   B HG1  1 
ATOM   6341 H  HG21 . THR   B 1 149 ? 33.689 -14.700 -9.575  1.00 16.37 ?  149 THR   B HG21 1 
ATOM   6342 H  HG22 . THR   B 1 149 ? 32.856 -14.969 -10.888 1.00 16.37 ?  149 THR   B HG22 1 
ATOM   6343 H  HG23 . THR   B 1 149 ? 32.418 -15.635 -9.525  1.00 16.37 ?  149 THR   B HG23 1 
ATOM   6344 N  N    . ASN   B 1 150 ? 35.134 -18.433 -12.529 1.00 12.35 ?  150 ASN   B N    1 
ATOM   6345 C  CA   . ASN   B 1 150 ? 35.897 -19.460 -13.230 1.00 12.82 ?  150 ASN   B CA   1 
ATOM   6346 C  C    . ASN   B 1 150 ? 37.060 -19.914 -12.363 1.00 12.51 ?  150 ASN   B C    1 
ATOM   6347 O  O    . ASN   B 1 150 ? 38.001 -19.154 -12.126 1.00 12.99 ?  150 ASN   B O    1 
ATOM   6348 C  CB   . ASN   B 1 150 ? 36.375 -18.930 -14.574 1.00 14.87 ?  150 ASN   B CB   1 
ATOM   6349 C  CG   . ASN   B 1 150 ? 35.237 -18.718 -15.531 1.00 17.55 ?  150 ASN   B CG   1 
ATOM   6350 O  OD1  . ASN   B 1 150 ? 34.330 -19.542 -15.610 1.00 18.69 ?  150 ASN   B OD1  1 
ATOM   6351 N  ND2  . ASN   B 1 150 ? 35.251 -17.601 -16.238 1.00 19.50 ?  150 ASN   B ND2  1 
ATOM   6352 H  H    . ASN   B 1 150 ? 35.372 -17.626 -12.707 1.00 14.81 ?  150 ASN   B H    1 
ATOM   6353 H  HA   . ASN   B 1 150 ? 35.316 -20.225 -13.390 1.00 15.37 ?  150 ASN   B HA   1 
ATOM   6354 H  HB2  . ASN   B 1 150 ? 36.816 -18.077 -14.435 1.00 17.84 ?  150 ASN   B HB2  1 
ATOM   6355 H  HB3  . ASN   B 1 150 ? 36.989 -19.568 -14.961 1.00 17.84 ?  150 ASN   B HB3  1 
ATOM   6356 H  HD21 . ASN   B 1 150 ? 34.623 -17.435 -16.803 1.00 23.39 ?  150 ASN   B HD21 1 
ATOM   6357 H  HD22 . ASN   B 1 150 ? 35.899 -17.039 -16.145 1.00 23.39 ?  150 ASN   B HD22 1 
ATOM   6358 N  N    . VAL   B 1 151 ? 37.008 -21.155 -11.899 1.00 12.31 ?  151 VAL   B N    1 
ATOM   6359 C  CA   . VAL   B 1 151 ? 38.023 -21.686 -11.005 1.00 12.22 ?  151 VAL   B CA   1 
ATOM   6360 C  C    . VAL   B 1 151 ? 38.721 -22.858 -11.682 1.00 12.23 ?  151 VAL   B C    1 
ATOM   6361 O  O    . VAL   B 1 151 ? 38.075 -23.790 -12.184 1.00 13.17 ?  151 VAL   B O    1 
ATOM   6362 C  CB   . VAL   B 1 151 ? 37.465 -22.031 -9.610  1.00 13.20 ?  151 VAL   B CB   1 
ATOM   6363 C  CG1  . VAL   B 1 151 ? 36.307 -23.023 -9.694  1.00 14.02 ?  151 VAL   B CG1  1 
ATOM   6364 C  CG2  . VAL   B 1 151 ? 38.575 -22.542 -8.698  1.00 13.73 ?  151 VAL   B CG2  1 
ATOM   6365 H  H    . VAL   B 1 151 ? 36.382 -21.718 -12.082 1.00 14.76 ?  151 VAL   B H    1 
ATOM   6366 H  HA   . VAL   B 1 151 ? 38.694 -20.995 -10.863 1.00 14.65 ?  151 VAL   B HA   1 
ATOM   6367 H  HB   . VAL   B 1 151 ? 37.119 -21.221 -9.203  1.00 15.83 ?  151 VAL   B HB   1 
ATOM   6368 H  HG11 . VAL   B 1 151 ? 35.984 -23.217 -8.799  1.00 16.81 ?  151 VAL   B HG11 1 
ATOM   6369 H  HG12 . VAL   B 1 151 ? 35.595 -22.635 -10.225 1.00 16.81 ?  151 VAL   B HG12 1 
ATOM   6370 H  HG13 . VAL   B 1 151 ? 36.621 -23.843 -10.113 1.00 16.81 ?  151 VAL   B HG13 1 
ATOM   6371 H  HG21 . VAL   B 1 151 ? 38.231 -22.616 -7.791  1.00 16.47 ?  151 VAL   B HG21 1 
ATOM   6372 H  HG22 . VAL   B 1 151 ? 38.866 -23.415 -9.007  1.00 16.47 ?  151 VAL   B HG22 1 
ATOM   6373 H  HG23 . VAL   B 1 151 ? 39.315 -21.918 -8.718  1.00 16.47 ?  151 VAL   B HG23 1 
ATOM   6374 N  N    . TYR   B 1 152 ? 40.049 -22.779 -11.705 1.00 11.56 ?  152 TYR   B N    1 
ATOM   6375 C  CA   . TYR   B 1 152 ? 40.944 -23.768 -12.287 1.00 11.97 ?  152 TYR   B CA   1 
ATOM   6376 C  C    . TYR   B 1 152 ? 41.667 -24.447 -11.127 1.00 11.15 ?  152 TYR   B C    1 
ATOM   6377 O  O    . TYR   B 1 152 ? 42.530 -23.836 -10.483 1.00 11.62 ?  152 TYR   B O    1 
ATOM   6378 C  CB   . TYR   B 1 152 ? 41.921 -23.076 -13.243 1.00 12.74 ?  152 TYR   B CB   1 
ATOM   6379 C  CG   . TYR   B 1 152 ? 41.244 -22.603 -14.511 1.00 13.31 ?  152 TYR   B CG   1 
ATOM   6380 C  CD1  . TYR   B 1 152 ? 40.611 -21.364 -14.575 1.00 13.90 ?  152 TYR   B CD1  1 
ATOM   6381 C  CD2  . TYR   B 1 152 ? 41.228 -23.403 -15.638 1.00 14.51 ?  152 TYR   B CD2  1 
ATOM   6382 C  CE1  . TYR   B 1 152 ? 39.977 -20.946 -15.731 1.00 15.36 ?  152 TYR   B CE1  1 
ATOM   6383 C  CE2  . TYR   B 1 152 ? 40.596 -23.000 -16.793 1.00 15.41 ?  152 TYR   B CE2  1 
ATOM   6384 C  CZ   . TYR   B 1 152 ? 39.978 -21.768 -16.836 1.00 15.98 ?  152 TYR   B CZ   1 
ATOM   6385 O  OH   . TYR   B 1 152 ? 39.353 -21.376 -17.995 1.00 18.46 ?  152 TYR   B OH   1 
ATOM   6386 H  H    . TYR   B 1 152 ? 40.488 -22.110 -11.362 1.00 13.86 ?  152 TYR   B H    1 
ATOM   6387 H  HA   . TYR   B 1 152 ? 40.430 -24.431 -12.770 1.00 14.35 ?  152 TYR   B HA   1 
ATOM   6388 H  HB2  . TYR   B 1 152 ? 42.304 -22.308 -12.797 1.00 15.28 ?  152 TYR   B HB2  1 
ATOM   6389 H  HB3  . TYR   B 1 152 ? 42.618 -23.704 -13.486 1.00 15.28 ?  152 TYR   B HB3  1 
ATOM   6390 H  HD1  . TYR   B 1 152 ? 40.604 -20.811 -13.825 1.00 16.67 ?  152 TYR   B HD1  1 
ATOM   6391 H  HD2  . TYR   B 1 152 ? 41.635 -24.243 -15.610 1.00 17.40 ?  152 TYR   B HD2  1 
ATOM   6392 H  HE1  . TYR   B 1 152 ? 39.557 -20.117 -15.768 1.00 18.42 ?  152 TYR   B HE1  1 
ATOM   6393 H  HE2  . TYR   B 1 152 ? 40.595 -23.555 -17.544 1.00 18.48 ?  152 TYR   B HE2  1 
ATOM   6394 H  HH   . TYR   B 1 152 ? 39.019 -20.608 -17.896 1.00 22.14 ?  152 TYR   B HH   1 
ATOM   6395 N  N    . LEU   B 1 153 ? 41.300 -25.701 -10.858 1.00 11.41 ?  153 LEU   B N    1 
ATOM   6396 C  CA   . LEU   B 1 153 ? 41.807 -26.457 -9.721  1.00 11.28 ?  153 LEU   B CA   1 
ATOM   6397 C  C    . LEU   B 1 153 ? 43.037 -27.260 -10.118 1.00 11.82 ?  153 LEU   B C    1 
ATOM   6398 O  O    . LEU   B 1 153 ? 43.014 -27.995 -11.109 1.00 12.90 ?  153 LEU   B O    1 
ATOM   6399 C  CB   . LEU   B 1 153 ? 40.729 -27.418 -9.212  1.00 11.67 ?  153 LEU   B CB   1 
ATOM   6400 C  CG   . LEU   B 1 153 ? 39.477 -26.763 -8.638  1.00 12.49 ?  153 LEU   B CG   1 
ATOM   6401 C  CD1  . LEU   B 1 153 ? 38.379 -27.802 -8.473  1.00 13.19 ?  153 LEU   B CD1  1 
ATOM   6402 C  CD2  . LEU   B 1 153 ? 39.768 -26.080 -7.309  1.00 12.81 ?  153 LEU   B CD2  1 
ATOM   6403 H  H    . LEU   B 1 153 ? 40.732 -26.147 -11.332 1.00 13.68 ?  153 LEU   B H    1 
ATOM   6404 H  HA   . LEU   B 1 153 ? 42.037 -25.849 -9.004  1.00 13.52 ?  153 LEU   B HA   1 
ATOM   6405 H  HB2  . LEU   B 1 153 ? 40.450 -27.986 -9.946  1.00 13.99 ?  153 LEU   B HB2  1 
ATOM   6406 H  HB3  . LEU   B 1 153 ? 41.113 -27.967 -8.508  1.00 13.99 ?  153 LEU   B HB3  1 
ATOM   6407 H  HG   . LEU   B 1 153 ? 39.153 -26.090 -9.259  1.00 14.98 ?  153 LEU   B HG   1 
ATOM   6408 H  HD11 . LEU   B 1 153 ? 37.576 -27.364 -8.149  1.00 15.82 ?  153 LEU   B HD11 1 
ATOM   6409 H  HD12 . LEU   B 1 153 ? 38.208 -28.216 -9.331  1.00 15.82 ?  153 LEU   B HD12 1 
ATOM   6410 H  HD13 . LEU   B 1 153 ? 38.674 -28.468 -7.834  1.00 15.82 ?  153 LEU   B HD13 1 
ATOM   6411 H  HD21 . LEU   B 1 153 ? 38.945 -25.717 -6.949  1.00 15.37 ?  153 LEU   B HD21 1 
ATOM   6412 H  HD22 . LEU   B 1 153 ? 40.141 -26.731 -6.696  1.00 15.37 ?  153 LEU   B HD22 1 
ATOM   6413 H  HD23 . LEU   B 1 153 ? 40.407 -25.364 -7.460  1.00 15.37 ?  153 LEU   B HD23 1 
ATOM   6414 N  N    . ALA   B 1 154 ? 44.088 -27.153 -9.314  1.00 12.06 ?  154 ALA   B N    1 
ATOM   6415 C  CA   . ALA   B 1 154 ? 45.318 -27.909 -9.505  1.00 12.63 ?  154 ALA   B CA   1 
ATOM   6416 C  C    . ALA   B 1 154 ? 45.386 -28.988 -8.433  1.00 13.30 ?  154 ALA   B C    1 
ATOM   6417 O  O    . ALA   B 1 154 ? 45.337 -28.689 -7.231  1.00 14.66 ?  154 ALA   B O    1 
ATOM   6418 C  CB   . ALA   B 1 154 ? 46.539 -26.998 -9.432  1.00 13.81 ?  154 ALA   B CB   1 
ATOM   6419 H  H    . ALA   B 1 154 ? 44.112 -26.629 -8.627  1.00 14.46 ?  154 ALA   B H    1 
ATOM   6420 H  HA   . ALA   B 1 154 ? 45.301 -28.338 -10.374 1.00 15.15 ?  154 ALA   B HA   1 
ATOM   6421 H  HB1  . ALA   B 1 154 ? 47.337 -27.530 -9.563  1.00 16.57 ?  154 ALA   B HB1  1 
ATOM   6422 H  HB2  . ALA   B 1 154 ? 46.470 -26.324 -10.126 1.00 16.57 ?  154 ALA   B HB2  1 
ATOM   6423 H  HB3  . ALA   B 1 154 ? 46.562 -26.572 -8.559  1.00 16.57 ?  154 ALA   B HB3  1 
ATOM   6424 N  N    . VAL   B 1 155 ? 45.481 -30.237 -8.868  1.00 12.70 ?  155 VAL   B N    1 
ATOM   6425 C  CA   . VAL   B 1 155 ? 45.580 -31.385 -7.979  1.00 13.51 ?  155 VAL   B CA   1 
ATOM   6426 C  C    . VAL   B 1 155 ? 46.912 -32.066 -8.260  1.00 13.47 ?  155 VAL   B C    1 
ATOM   6427 O  O    . VAL   B 1 155 ? 47.145 -32.554 -9.373  1.00 15.22 ?  155 VAL   B O    1 
ATOM   6428 C  CB   . VAL   B 1 155 ? 44.412 -32.365 -8.174  1.00 14.75 ?  155 VAL   B CB   1 
ATOM   6429 C  CG1  . VAL   B 1 155 ? 44.598 -33.574 -7.265  1.00 14.63 ?  155 VAL   B CG1  1 
ATOM   6430 C  CG2  . VAL   B 1 155 ? 43.081 -31.667 -7.908  1.00 15.63 ?  155 VAL   B CG2  1 
ATOM   6431 H  H    . VAL   B 1 155 ? 45.500 -30.452 -9.702  1.00 15.22 ?  155 VAL   B H    1 
ATOM   6432 H  HA   . VAL   B 1 155 ? 45.575 -31.089 -7.057  1.00 16.20 ?  155 VAL   B HA   1 
ATOM   6433 H  HB   . VAL   B 1 155 ? 44.409 -32.678 -9.093  1.00 17.68 ?  155 VAL   B HB   1 
ATOM   6434 H  HG11 . VAL   B 1 155 ? 43.761 -34.067 -7.220  1.00 17.54 ?  155 VAL   B HG11 1 
ATOM   6435 H  HG12 . VAL   B 1 155 ? 45.294 -34.145 -7.628  1.00 17.54 ?  155 VAL   B HG12 1 
ATOM   6436 H  HG13 . VAL   B 1 155 ? 44.846 -33.269 -6.378  1.00 17.54 ?  155 VAL   B HG13 1 
ATOM   6437 H  HG21 . VAL   B 1 155 ? 42.362 -32.311 -7.990  1.00 18.74 ?  155 VAL   B HG21 1 
ATOM   6438 H  HG22 . VAL   B 1 155 ? 43.093 -31.296 -7.011  1.00 18.74 ?  155 VAL   B HG22 1 
ATOM   6439 H  HG23 . VAL   B 1 155 ? 42.963 -30.954 -8.557  1.00 18.74 ?  155 VAL   B HG23 1 
ATOM   6440 N  N    . PHE   B 1 156 ? 47.778 -32.108 -7.248  1.00 13.93 ?  156 PHE   B N    1 
ATOM   6441 C  CA   . PHE   B 1 156 ? 49.156 -32.561 -7.455  1.00 14.87 ?  156 PHE   B CA   1 
ATOM   6442 C  C    . PHE   B 1 156 ? 49.250 -34.059 -7.746  1.00 15.99 ?  156 PHE   B C    1 
ATOM   6443 O  O    . PHE   B 1 156 ? 49.985 -34.486 -8.649  1.00 17.93 ?  156 PHE   B O    1 
ATOM   6444 C  CB   . PHE   B 1 156 ? 49.981 -32.205 -6.222  1.00 14.53 ?  156 PHE   B CB   1 
ATOM   6445 C  CG   . PHE   B 1 156 ? 51.405 -32.667 -6.285  1.00 15.05 ?  156 PHE   B CG   1 
ATOM   6446 C  CD1  . PHE   B 1 156 ? 52.284 -32.128 -7.207  1.00 16.92 ?  156 PHE   B CD1  1 
ATOM   6447 C  CD2  . PHE   B 1 156 ? 51.872 -33.623 -5.402  1.00 15.74 ?  156 PHE   B CD2  1 
ATOM   6448 C  CE1  . PHE   B 1 156 ? 53.600 -32.547 -7.257  1.00 17.78 ?  156 PHE   B CE1  1 
ATOM   6449 C  CE2  . PHE   B 1 156 ? 53.186 -34.041 -5.448  1.00 17.22 ?  156 PHE   B CE2  1 
ATOM   6450 C  CZ   . PHE   B 1 156 ? 54.046 -33.501 -6.378  1.00 17.33 ?  156 PHE   B CZ   1 
ATOM   6451 H  H    . PHE   B 1 156 ? 47.590 -31.892 -6.435  1.00 16.71 ?  156 PHE   B H    1 
ATOM   6452 H  HA   . PHE   B 1 156 ? 49.524 -32.082 -8.207  1.00 17.84 ?  156 PHE   B HA   1 
ATOM   6453 H  HB2  . PHE   B 1 156 ? 49.985 -31.237 -6.124  1.00 17.43 ?  156 PHE   B HB2  1 
ATOM   6454 H  HB3  . PHE   B 1 156 ? 49.570 -32.608 -5.440  1.00 17.43 ?  156 PHE   B HB3  1 
ATOM   6455 H  HD1  . PHE   B 1 156 ? 51.983 -31.476 -7.805  1.00 20.29 ?  156 PHE   B HD1  1 
ATOM   6456 H  HD2  . PHE   B 1 156 ? 51.287 -33.992 -4.777  1.00 18.87 ?  156 PHE   B HD2  1 
ATOM   6457 H  HE1  . PHE   B 1 156 ? 54.183 -32.179 -7.883  1.00 21.33 ?  156 PHE   B HE1  1 
ATOM   6458 H  HE2  . PHE   B 1 156 ? 53.481 -34.693 -4.855  1.00 20.65 ?  156 PHE   B HE2  1 
ATOM   6459 H  HZ   . PHE   B 1 156 ? 54.931 -33.786 -6.410  1.00 20.79 ?  156 PHE   B HZ   1 
ATOM   6460 N  N    . ASP   B 1 157 ? 48.577 -34.877 -6.951  1.00 16.55 ?  157 ASP   B N    1 
ATOM   6461 C  CA   . ASP   B 1 157 ? 48.725 -36.325 -7.047  1.00 17.74 ?  157 ASP   B CA   1 
ATOM   6462 C  C    . ASP   B 1 157 ? 47.808 -36.870 -8.137  1.00 17.91 ?  157 ASP   B C    1 
ATOM   6463 O  O    . ASP   B 1 157 ? 46.584 -36.735 -8.043  1.00 17.26 ?  157 ASP   B O    1 
ATOM   6464 C  CB   . ASP   B 1 157 ? 48.364 -36.938 -5.700  1.00 19.21 ?  157 ASP   B CB   1 
ATOM   6465 C  CG   . ASP   B 1 157 ? 48.497 -38.448 -5.683  1.00 21.21 ?  157 ASP   B CG   1 
ATOM   6466 O  OD1  . ASP   B 1 157 ? 48.852 -39.056 -6.721  1.00 21.55 ?  157 ASP   B OD1  1 
ATOM   6467 O  OD2  . ASP   B 1 157 ? 48.246 -39.037 -4.612  1.00 23.36 -1 157 ASP   B OD2  1 
ATOM   6468 H  H    . ASP   B 1 157 ? 48.032 -34.623 -6.346  1.00 19.84 ?  157 ASP   B H    1 
ATOM   6469 H  HA   . ASP   B 1 157 ? 49.642 -36.556 -7.265  1.00 21.28 ?  157 ASP   B HA   1 
ATOM   6470 H  HB2  . ASP   B 1 157 ? 48.945 -36.565 -5.022  1.00 23.04 ?  157 ASP   B HB2  1 
ATOM   6471 H  HB3  . ASP   B 1 157 ? 47.439 -36.715 -5.495  1.00 23.04 ?  157 ASP   B HB3  1 
ATOM   6472 N  N    A LYS   B 1 158 ? 48.401 -37.517 -9.148  0.50 18.51 ?  158 LYS   B N    1 
ATOM   6473 N  N    B LYS   B 1 158 ? 48.402 -37.478 -9.172  0.50 18.71 ?  158 LYS   B N    1 
ATOM   6474 C  CA   A LYS   B 1 158 ? 47.624 -38.135 -10.223 0.50 19.03 ?  158 LYS   B CA   1 
ATOM   6475 C  CA   B LYS   B 1 158 ? 47.622 -38.039 -10.276 0.50 19.57 ?  158 LYS   B CA   1 
ATOM   6476 C  C    A LYS   B 1 158 ? 46.562 -39.090 -9.683  0.50 18.72 ?  158 LYS   B C    1 
ATOM   6477 C  C    B LYS   B 1 158 ? 46.559 -39.013 -9.774  0.50 19.42 ?  158 LYS   B C    1 
ATOM   6478 O  O    A LYS   B 1 158 ? 45.452 -39.170 -10.223 0.50 18.50 ?  158 LYS   B O    1 
ATOM   6479 O  O    B LYS   B 1 158 ? 45.463 -39.098 -10.341 0.50 19.47 ?  158 LYS   B O    1 
ATOM   6480 C  CB   A LYS   B 1 158 ? 48.575 -38.870 -11.175 0.50 20.62 ?  158 LYS   B CB   1 
ATOM   6481 C  CB   B LYS   B 1 158 ? 48.565 -38.731 -11.269 0.50 21.22 ?  158 LYS   B CB   1 
ATOM   6482 C  CG   A LYS   B 1 158 ? 47.899 -39.772 -12.196 0.50 22.51 ?  158 LYS   B CG   1 
ATOM   6483 C  CG   B LYS   B 1 158 ? 47.882 -39.620 -12.303 0.50 23.07 ?  158 LYS   B CG   1 
ATOM   6484 C  CD   A LYS   B 1 158 ? 47.044 -38.986 -13.165 0.50 24.11 ?  158 LYS   B CD   1 
ATOM   6485 C  CD   B LYS   B 1 158 ? 46.995 -38.827 -13.242 0.50 24.73 ?  158 LYS   B CD   1 
ATOM   6486 C  CE   A LYS   B 1 158 ? 46.454 -39.896 -14.224 0.50 25.34 ?  158 LYS   B CE   1 
ATOM   6487 C  CE   B LYS   B 1 158 ? 46.433 -39.713 -14.341 0.50 25.98 ?  158 LYS   B CE   1 
ATOM   6488 N  NZ   A LYS   B 1 158 ? 45.405 -39.206 -15.023 0.50 25.70 ?  158 LYS   B NZ   1 
ATOM   6489 N  NZ   B LYS   B 1 158 ? 45.347 -39.037 -15.105 0.50 26.47 ?  158 LYS   B NZ   1 
ATOM   6490 H  H    A LYS   B 1 158 ? 49.254 -37.614 -9.230  0.50 22.20 ?  158 LYS   B H    1 
ATOM   6491 H  H    B LYS   B 1 158 ? 49.254 -37.583 -9.252  0.50 22.44 ?  158 LYS   B H    1 
ATOM   6492 H  HA   A LYS   B 1 158 ? 47.176 -37.442 -10.729 0.50 22.82 ?  158 LYS   B HA   1 
ATOM   6493 H  HA   B LYS   B 1 158 ? 47.178 -37.318 -10.749 0.50 23.48 ?  158 LYS   B HA   1 
ATOM   6494 H  HB2  A LYS   B 1 158 ? 49.091 -38.211 -11.671 0.50 24.73 ?  158 LYS   B HB2  1 
ATOM   6495 H  HB2  B LYS   B 1 158 ? 49.059 -38.050 -11.758 0.50 25.45 ?  158 LYS   B HB2  1 
ATOM   6496 H  HB3  A LYS   B 1 158 ? 49.178 -39.423 -10.652 0.50 24.73 ?  158 LYS   B HB3  1 
ATOM   6497 H  HB3  B LYS   B 1 158 ? 49.187 -39.285 -10.774 0.50 25.45 ?  158 LYS   B HB3  1 
ATOM   6498 H  HG2  A LYS   B 1 158 ? 48.582 -40.232 -12.708 0.50 27.00 ?  158 LYS   B HG2  1 
ATOM   6499 H  HG2  B LYS   B 1 158 ? 48.565 -40.056 -12.837 0.50 27.67 ?  158 LYS   B HG2  1 
ATOM   6500 H  HG3  A LYS   B 1 158 ? 47.337 -40.422 -11.745 0.50 27.00 ?  158 LYS   B HG3  1 
ATOM   6501 H  HG3  B LYS   B 1 158 ? 47.341 -40.291 -11.858 0.50 27.67 ?  158 LYS   B HG3  1 
ATOM   6502 H  HD2  A LYS   B 1 158 ? 46.316 -38.561 -12.684 0.50 28.92 ?  158 LYS   B HD2  1 
ATOM   6503 H  HD2  B LYS   B 1 158 ? 46.254 -38.450 -12.743 0.50 29.67 ?  158 LYS   B HD2  1 
ATOM   6504 H  HD3  A LYS   B 1 158 ? 47.591 -38.316 -13.607 0.50 28.92 ?  158 LYS   B HD3  1 
ATOM   6505 H  HD3  B LYS   B 1 158 ? 47.517 -38.121 -13.656 0.50 29.67 ?  158 LYS   B HD3  1 
ATOM   6506 H  HE2  A LYS   B 1 158 ? 47.156 -40.181 -14.828 0.50 30.40 ?  158 LYS   B HE2  1 
ATOM   6507 H  HE2  B LYS   B 1 158 ? 47.143 -39.941 -14.962 0.50 31.17 ?  158 LYS   B HE2  1 
ATOM   6508 H  HE3  A LYS   B 1 158 ? 46.050 -40.666 -13.793 0.50 30.40 ?  158 LYS   B HE3  1 
ATOM   6509 H  HE3  B LYS   B 1 158 ? 46.067 -40.519 -13.944 0.50 31.17 ?  158 LYS   B HE3  1 
ATOM   6510 H  HZ1  A LYS   B 1 158 ? 45.075 -39.760 -15.634 0.50 30.83 ?  158 LYS   B HZ1  1 
ATOM   6511 H  HZ1  B LYS   B 1 158 ? 45.038 -39.579 -15.739 0.50 31.75 ?  158 LYS   B HZ1  1 
ATOM   6512 H  HZ2  A LYS   B 1 158 ? 44.745 -38.936 -14.489 0.50 30.83 ?  158 LYS   B HZ2  1 
ATOM   6513 H  HZ2  B LYS   B 1 158 ? 44.679 -38.822 -14.556 0.50 31.75 ?  158 LYS   B HZ2  1 
ATOM   6514 H  HZ3  A LYS   B 1 158 ? 45.753 -38.496 -15.432 0.50 30.83 ?  158 LYS   B HZ3  1 
ATOM   6515 H  HZ3  B LYS   B 1 158 ? 45.659 -38.295 -15.484 0.50 31.75 ?  158 LYS   B HZ3  1 
ATOM   6516 N  N    A ASN   B 1 159 ? 46.888 -39.843 -8.630  0.50 19.07 ?  159 ASN   B N    1 
ATOM   6517 N  N    B ASN   B 1 159 ? 46.871 -39.772 -8.722  0.50 19.64 ?  159 ASN   B N    1 
ATOM   6518 C  CA   A ASN   B 1 159 ? 45.933 -40.818 -8.112  0.50 19.45 ?  159 ASN   B CA   1 
ATOM   6519 C  CA   B ASN   B 1 159 ? 45.913 -40.754 -8.221  0.50 19.74 ?  159 ASN   B CA   1 
ATOM   6520 C  C    A ASN   B 1 159 ? 44.740 -40.143 -7.445  0.50 18.59 ?  159 ASN   B C    1 
ATOM   6521 C  C    B ASN   B 1 159 ? 44.721 -40.083 -7.543  0.50 18.80 ?  159 ASN   B C    1 
ATOM   6522 O  O    A ASN   B 1 159 ? 43.616 -40.657 -7.518  0.50 18.65 ?  159 ASN   B O    1 
ATOM   6523 O  O    B ASN   B 1 159 ? 43.579 -40.538 -7.693  0.50 18.82 ?  159 ASN   B O    1 
ATOM   6524 C  CB   A ASN   B 1 159 ? 46.635 -41.773 -7.150  0.50 20.92 ?  159 ASN   B CB   1 
ATOM   6525 C  CB   B ASN   B 1 159 ? 46.613 -41.738 -7.285  0.50 20.97 ?  159 ASN   B CB   1 
ATOM   6526 C  CG   A ASN   B 1 159 ? 47.669 -42.637 -7.844  0.50 22.64 ?  159 ASN   B CG   1 
ATOM   6527 C  CG   B ASN   B 1 159 ? 47.619 -42.608 -8.010  0.50 22.45 ?  159 ASN   B CG   1 
ATOM   6528 O  OD1  A ASN   B 1 159 ? 47.435 -43.147 -8.943  0.50 23.74 ?  159 ASN   B OD1  1 
ATOM   6529 O  OD1  B ASN   B 1 159 ? 47.373 -43.051 -9.135  0.50 23.26 ?  159 ASN   B OD1  1 
ATOM   6530 N  ND2  A ASN   B 1 159 ? 48.823 -42.805 -7.208  0.50 23.22 ?  159 ASN   B ND2  1 
ATOM   6531 N  ND2  B ASN   B 1 159 ? 48.762 -42.857 -7.371  0.50 23.15 ?  159 ASN   B ND2  1 
ATOM   6532 H  H    A ASN   B 1 159 ? 47.634 -39.802 -8.207  0.50 22.87 ?  159 ASN   B H    1 
ATOM   6533 H  H    B ASN   B 1 159 ? 47.618 -39.736 -8.298  0.50 23.55 ?  159 ASN   B H    1 
ATOM   6534 H  HA   A ASN   B 1 159 ? 45.601 -41.345 -8.856  0.50 23.32 ?  159 ASN   B HA   1 
ATOM   6535 H  HA   B ASN   B 1 159 ? 45.579 -41.263 -8.976  0.50 23.68 ?  159 ASN   B HA   1 
ATOM   6536 H  HB2  A ASN   B 1 159 ? 47.083 -41.260 -6.460  0.50 25.09 ?  159 ASN   B HB2  1 
ATOM   6537 H  HB2  B ASN   B 1 159 ? 47.084 -41.246 -6.597  0.50 25.15 ?  159 ASN   B HB2  1 
ATOM   6538 H  HB3  A ASN   B 1 159 ? 45.973 -42.360 -6.753  0.50 25.09 ?  159 ASN   B HB3  1 
ATOM   6539 H  HB3  B ASN   B 1 159 ? 45.948 -42.320 -6.886  0.50 25.15 ?  159 ASN   B HB3  1 
ATOM   6540 H  HD21 A ASN   B 1 159 ? 49.441 -43.292 -7.561  0.50 27.85 ?  159 ASN   B HD21 1 
ATOM   6541 H  HD21 B ASN   B 1 159 ? 49.369 -43.351 -7.737  0.50 27.77 ?  159 ASN   B HD21 1 
ATOM   6542 H  HD22 A ASN   B 1 159 ? 48.950 -42.444 -6.439  0.50 27.85 ?  159 ASN   B HD22 1 
ATOM   6543 H  HD22 B ASN   B 1 159 ? 48.896 -42.535 -6.584  0.50 27.77 ?  159 ASN   B HD22 1 
ATOM   6544 N  N    . LEU   B 1 160 ? 44.954 -38.994 -6.801  1.00 18.01 ?  160 LEU   B N    1 
ATOM   6545 C  CA   . LEU   B 1 160 ? 43.831 -38.251 -6.241  1.00 17.05 ?  160 LEU   B CA   1 
ATOM   6546 C  C    . LEU   B 1 160 ? 43.034 -37.589 -7.351  1.00 16.61 ?  160 LEU   B C    1 
ATOM   6547 O  O    . LEU   B 1 160 ? 41.796 -37.585 -7.316  1.00 16.21 ?  160 LEU   B O    1 
ATOM   6548 C  CB   . LEU   B 1 160 ? 44.303 -37.211 -5.229  1.00 17.05 ?  160 LEU   B CB   1 
ATOM   6549 C  CG   . LEU   B 1 160 ? 43.167 -36.322 -4.699  1.00 17.03 ?  160 LEU   B CG   1 
ATOM   6550 C  CD1  . LEU   B 1 160 ? 42.047 -37.155 -4.079  1.00 18.01 ?  160 LEU   B CD1  1 
ATOM   6551 C  CD2  . LEU   B 1 160 ? 43.698 -35.300 -3.702  1.00 17.16 ?  160 LEU   B CD2  1 
ATOM   6552 H  H    A LEU   B 1 160 ? 45.727 -38.635 -6.682  0.50 21.60 ?  160 LEU   B H    1 
ATOM   6553 H  H    B LEU   B 1 160 ? 45.733 -38.675 -6.622  0.50 21.60 ?  160 LEU   B H    1 
ATOM   6554 H  HA   . LEU   B 1 160 ? 43.248 -38.873 -5.787  1.00 20.45 ?  160 LEU   B HA   1 
ATOM   6555 H  HB2  . LEU   B 1 160 ? 44.707 -37.671 -4.475  1.00 20.45 ?  160 LEU   B HB2  1 
ATOM   6556 H  HB3  . LEU   B 1 160 ? 44.964 -36.636 -5.653  1.00 20.45 ?  160 LEU   B HB3  1 
ATOM   6557 H  HG   . LEU   B 1 160 ? 42.786 -35.831 -5.441  1.00 20.42 ?  160 LEU   B HG   1 
ATOM   6558 H  HD11 . LEU   B 1 160 ? 41.425 -36.564 -3.633  1.00 21.61 ?  160 LEU   B HD11 1 
ATOM   6559 H  HD12 . LEU   B 1 160 ? 41.589 -37.651 -4.779  1.00 21.61 ?  160 LEU   B HD12 1 
ATOM   6560 H  HD13 . LEU   B 1 160 ? 42.432 -37.777 -3.437  1.00 21.61 ?  160 LEU   B HD13 1 
ATOM   6561 H  HD21 . LEU   B 1 160 ? 42.962 -34.742 -3.408  1.00 20.58 ?  160 LEU   B HD21 1 
ATOM   6562 H  HD22 . LEU   B 1 160 ? 44.083 -35.769 -2.947  1.00 20.58 ?  160 LEU   B HD22 1 
ATOM   6563 H  HD23 . LEU   B 1 160 ? 44.373 -34.759 -4.139  1.00 20.58 ?  160 LEU   B HD23 1 
ATOM   6564 N  N    A TYR   B 1 161 ? 43.727 -37.032 -8.345  0.50 16.60 ?  161 TYR   B N    1 
ATOM   6565 N  N    B TYR   B 1 161 ? 43.722 -37.028 -8.351  0.50 16.71 ?  161 TYR   B N    1 
ATOM   6566 C  CA   A TYR   B 1 161 ? 43.057 -36.461 -9.507  0.50 16.27 ?  161 TYR   B CA   1 
ATOM   6567 C  CA   B TYR   B 1 161 ? 43.033 -36.456 -9.505  0.50 16.49 ?  161 TYR   B CA   1 
ATOM   6568 C  C    A TYR   B 1 161 ? 42.102 -37.473 -10.129 0.50 16.43 ?  161 TYR   B C    1 
ATOM   6569 C  C    B TYR   B 1 161 ? 42.089 -37.479 -10.124 0.50 16.53 ?  161 TYR   B C    1 
ATOM   6570 O  O    A TYR   B 1 161 ? 40.931 -37.170 -10.384 0.50 16.17 ?  161 TYR   B O    1 
ATOM   6571 O  O    B TYR   B 1 161 ? 40.915 -37.188 -10.376 0.50 16.30 ?  161 TYR   B O    1 
ATOM   6572 C  CB   A TYR   B 1 161 ? 44.115 -36.008 -10.517 0.50 16.72 ?  161 TYR   B CB   1 
ATOM   6573 C  CB   B TYR   B 1 161 ? 44.055 -35.962 -10.539 0.50 17.10 ?  161 TYR   B CB   1 
ATOM   6574 C  CG   A TYR   B 1 161 ? 43.557 -35.523 -11.831 0.50 17.05 ?  161 TYR   B CG   1 
ATOM   6575 C  CG   B TYR   B 1 161 ? 43.448 -35.478 -11.843 0.50 17.61 ?  161 TYR   B CG   1 
ATOM   6576 C  CD1  A TYR   B 1 161 ? 43.175 -34.200 -11.995 0.50 17.02 ?  161 TYR   B CD1  1 
ATOM   6577 C  CD1  B TYR   B 1 161 ? 43.076 -34.150 -12.008 0.50 17.55 ?  161 TYR   B CD1  1 
ATOM   6578 C  CD2  A TYR   B 1 161 ? 43.405 -36.390 -12.905 0.50 17.64 ?  161 TYR   B CD2  1 
ATOM   6579 C  CD2  B TYR   B 1 161 ? 43.242 -36.351 -12.907 0.50 18.13 ?  161 TYR   B CD2  1 
ATOM   6580 C  CE1  A TYR   B 1 161 ? 42.663 -33.754 -13.190 0.50 17.91 ?  161 TYR   B CE1  1 
ATOM   6581 C  CE1  B TYR   B 1 161 ? 42.520 -33.705 -13.192 0.50 18.39 ?  161 TYR   B CE1  1 
ATOM   6582 C  CE2  A TYR   B 1 161 ? 42.891 -35.954 -14.103 0.50 18.40 ?  161 TYR   B CE2  1 
ATOM   6583 C  CE2  B TYR   B 1 161 ? 42.682 -35.915 -14.094 0.50 18.78 ?  161 TYR   B CE2  1 
ATOM   6584 C  CZ   A TYR   B 1 161 ? 42.523 -34.634 -14.243 0.50 18.67 ?  161 TYR   B CZ   1 
ATOM   6585 C  CZ   B TYR   B 1 161 ? 42.327 -34.590 -14.232 0.50 19.00 ?  161 TYR   B CZ   1 
ATOM   6586 O  OH   A TYR   B 1 161 ? 42.012 -34.195 -15.438 0.50 20.14 ?  161 TYR   B OH   1 
ATOM   6587 O  OH   B TYR   B 1 161 ? 41.767 -34.154 -15.410 0.50 20.20 ?  161 TYR   B OH   1 
ATOM   6588 H  H    A TYR   B 1 161 ? 44.583 -36.978 -8.374  0.50 19.90 ?  161 TYR   B H    1 
ATOM   6589 H  H    B TYR   B 1 161 ? 44.576 -36.971 -8.388  0.50 20.04 ?  161 TYR   B H    1 
ATOM   6590 H  HA   A TYR   B 1 161 ? 42.542 -35.687 -9.239  0.50 19.52 ?  161 TYR   B HA   1 
ATOM   6591 H  HA   B TYR   B 1 161 ? 42.504 -35.696 -9.221  0.50 19.77 ?  161 TYR   B HA   1 
ATOM   6592 H  HB2  A TYR   B 1 161 ? 44.623 -35.279 -10.128 0.50 20.05 ?  161 TYR   B HB2  1 
ATOM   6593 H  HB2  B TYR   B 1 161 ? 44.551 -35.222 -10.157 0.50 20.50 ?  161 TYR   B HB2  1 
ATOM   6594 H  HB3  A TYR   B 1 161 ? 44.706 -36.753 -10.707 0.50 20.05 ?  161 TYR   B HB3  1 
ATOM   6595 H  HB3  B TYR   B 1 161 ? 44.660 -36.688 -10.752 0.50 20.50 ?  161 TYR   B HB3  1 
ATOM   6596 H  HD1  A TYR   B 1 161 ? 43.273 -33.603 -11.286 0.50 20.41 ?  161 TYR   B HD1  1 
ATOM   6597 H  HD1  B TYR   B 1 161 ? 43.206 -33.546 -11.312 0.50 21.05 ?  161 TYR   B HD1  1 
ATOM   6598 H  HD2  A TYR   B 1 161 ? 43.650 -37.283 -12.813 0.50 21.15 ?  161 TYR   B HD2  1 
ATOM   6599 H  HD2  B TYR   B 1 161 ? 43.479 -37.245 -12.821 0.50 21.75 ?  161 TYR   B HD2  1 
ATOM   6600 H  HE1  A TYR   B 1 161 ? 42.415 -32.860 -13.285 0.50 21.48 ?  161 TYR   B HE1  1 
ATOM   6601 H  HE1  B TYR   B 1 161 ? 42.281 -32.808 -13.288 0.50 22.06 ?  161 TYR   B HE1  1 
ATOM   6602 H  HE2  A TYR   B 1 161 ? 42.792 -36.544 -14.815 0.50 22.07 ?  161 TYR   B HE2  1 
ATOM   6603 H  HE2  B TYR   B 1 161 ? 42.553 -36.509 -14.799 0.50 22.53 ?  161 TYR   B HE2  1 
ATOM   6604 H  HH   A TYR   B 1 161 ? 41.981 -34.828 -15.986 0.50 24.15 ?  161 TYR   B HH   1 
ATOM   6605 H  HH   B TYR   B 1 161 ? 41.715 -34.790 -15.956 0.50 24.23 ?  161 TYR   B HH   1 
ATOM   6606 N  N    . ASP   B 1 162 ? 42.587 -38.695 -10.360 1.00 16.96 ?  162 ASP   B N    1 
ATOM   6607 C  CA   . ASP   B 1 162 ? 41.746 -39.727 -10.958 1.00 17.99 ?  162 ASP   B CA   1 
ATOM   6608 C  C    . ASP   B 1 162 ? 40.545 -40.051 -10.075 1.00 17.49 ?  162 ASP   B C    1 
ATOM   6609 O  O    . ASP   B 1 162 ? 39.435 -40.259 -10.577 1.00 17.68 ?  162 ASP   B O    1 
ATOM   6610 C  CB   . ASP   B 1 162 ? 42.568 -40.996 -11.208 1.00 19.41 ?  162 ASP   B CB   1 
ATOM   6611 C  CG   . ASP   B 1 162 ? 43.579 -40.846 -12.333 1.00 20.90 ?  162 ASP   B CG   1 
ATOM   6612 O  OD1  . ASP   B 1 162 ? 43.459 -39.906 -13.145 1.00 21.29 ?  162 ASP   B OD1  1 
ATOM   6613 O  OD2  . ASP   B 1 162 ? 44.483 -41.708 -12.418 1.00 22.48 -1 162 ASP   B OD2  1 
ATOM   6614 H  H    A ASP   B 1 162 ? 43.388 -38.949 -10.180 0.50 20.34 ?  162 ASP   B H    1 
ATOM   6615 H  H    B ASP   B 1 162 ? 43.391 -38.943 -10.186 0.50 20.34 ?  162 ASP   B H    1 
ATOM   6616 H  HA   . ASP   B 1 162 ? 41.412 -39.414 -11.811 1.00 21.58 ?  162 ASP   B HA   1 
ATOM   6617 H  HB2  . ASP   B 1 162 ? 43.057 -41.220 -10.404 1.00 23.28 ?  162 ASP   B HB2  1 
ATOM   6618 H  HB3  . ASP   B 1 162 ? 41.965 -41.720 -11.445 1.00 23.28 ?  162 ASP   B HB3  1 
ATOM   6619 N  N    . LYS   B 1 163 ? 40.751 -40.129 -8.759  1.00 16.60 ?  163 LYS   B N    1 
ATOM   6620 C  CA   . LYS   B 1 163 ? 39.636 -40.401 -7.857  1.00 17.03 ?  163 LYS   B CA   1 
ATOM   6621 C  C    . LYS   B 1 163 ? 38.598 -39.288 -7.913  1.00 15.68 ?  163 LYS   B C    1 
ATOM   6622 O  O    . LYS   B 1 163 ? 37.386 -39.551 -7.912  1.00 16.52 ?  163 LYS   B O    1 
ATOM   6623 C  CB   . LYS   B 1 163 ? 40.145 -40.571 -6.427  1.00 20.10 ?  163 LYS   B CB   1 
ATOM   6624 C  CG   . LYS   B 1 163 ? 39.067 -41.033 -5.471  1.00 25.53 ?  163 LYS   B CG   1 
ATOM   6625 C  CD   . LYS   B 1 163 ? 39.584 -41.243 -4.060  1.00 30.79 ?  163 LYS   B CD   1 
ATOM   6626 C  CE   . LYS   B 1 163 ? 38.487 -41.826 -3.180  1.00 34.33 ?  163 LYS   B CE   1 
ATOM   6627 N  NZ   . LYS   B 1 163 ? 38.752 -41.639 -1.728  1.00 37.32 ?  163 LYS   B NZ   1 
ATOM   6628 H  H    . LYS   B 1 163 ? 41.516 -40.033 -8.376  1.00 19.91 ?  163 LYS   B H    1 
ATOM   6629 H  HA   . LYS   B 1 163 ? 39.208 -41.225 -8.123  1.00 20.43 ?  163 LYS   B HA   1 
ATOM   6630 H  HB2  . LYS   B 1 163 ? 40.855 -41.234 -6.421  1.00 24.11 ?  163 LYS   B HB2  1 
ATOM   6631 H  HB3  . LYS   B 1 163 ? 40.484 -39.721 -6.107  1.00 24.11 ?  163 LYS   B HB3  1 
ATOM   6632 H  HG2  . LYS   B 1 163 ? 38.365 -40.366 -5.435  1.00 30.62 ?  163 LYS   B HG2  1 
ATOM   6633 H  HG3  . LYS   B 1 163 ? 38.706 -41.878 -5.786  1.00 30.62 ?  163 LYS   B HG3  1 
ATOM   6634 H  HD2  . LYS   B 1 163 ? 40.328 -41.866 -4.076  1.00 36.94 ?  163 LYS   B HD2  1 
ATOM   6635 H  HD3  . LYS   B 1 163 ? 39.860 -40.393 -3.686  1.00 36.94 ?  163 LYS   B HD3  1 
ATOM   6636 H  HE2  . LYS   B 1 163 ? 37.643 -41.400 -3.393  1.00 41.18 ?  163 LYS   B HE2  1 
ATOM   6637 H  HE3  . LYS   B 1 163 ? 38.422 -42.778 -3.351  1.00 41.18 ?  163 LYS   B HE3  1 
ATOM   6638 H  HZ1  . LYS   B 1 163 ? 38.088 -41.991 -1.251  1.00 44.77 ?  163 LYS   B HZ1  1 
ATOM   6639 H  HZ2  . LYS   B 1 163 ? 39.513 -42.040 -1.506  1.00 44.77 ?  163 LYS   B HZ2  1 
ATOM   6640 H  HZ3  . LYS   B 1 163 ? 38.815 -40.772 -1.540  1.00 44.77 ?  163 LYS   B HZ3  1 
ATOM   6641 N  N    . LEU   B 1 164 ? 39.060 -38.037 -7.963  1.00 14.56 ?  164 LEU   B N    1 
ATOM   6642 C  CA   . LEU   B 1 164 ? 38.153 -36.896 -8.019  1.00 14.35 ?  164 LEU   B CA   1 
ATOM   6643 C  C    . LEU   B 1 164 ? 37.359 -36.874 -9.320  1.00 14.78 ?  164 LEU   B C    1 
ATOM   6644 O  O    . LEU   B 1 164 ? 36.137 -36.665 -9.309  1.00 15.97 ?  164 LEU   B O    1 
ATOM   6645 C  CB   . LEU   B 1 164 ? 38.947 -35.596 -7.867  1.00 14.12 ?  164 LEU   B CB   1 
ATOM   6646 C  CG   . LEU   B 1 164 ? 39.498 -35.326 -6.470  1.00 14.90 ?  164 LEU   B CG   1 
ATOM   6647 C  CD1  . LEU   B 1 164 ? 40.573 -34.262 -6.535  1.00 15.19 ?  164 LEU   B CD1  1 
ATOM   6648 C  CD2  . LEU   B 1 164 ? 38.399 -34.908 -5.510  1.00 16.64 ?  164 LEU   B CD2  1 
ATOM   6649 H  H    . LEU   B 1 164 ? 39.897 -37.820 -7.967  1.00 17.46 ?  164 LEU   B H    1 
ATOM   6650 H  HA   . LEU   B 1 164 ? 37.525 -36.952 -7.291  1.00 17.21 ?  164 LEU   B HA   1 
ATOM   6651 H  HB2  . LEU   B 1 164 ? 39.706 -35.626 -8.474  1.00 16.93 ?  164 LEU   B HB2  1 
ATOM   6652 H  HB3  . LEU   B 1 164 ? 38.373 -34.854 -8.105  1.00 16.93 ?  164 LEU   B HB3  1 
ATOM   6653 H  HG   . LEU   B 1 164 ? 39.900 -36.134 -6.126  1.00 17.87 ?  164 LEU   B HG   1 
ATOM   6654 H  HD11 . LEU   B 1 164 ? 40.904 -34.089 -5.637  1.00 18.21 ?  164 LEU   B HD11 1 
ATOM   6655 H  HD12 . LEU   B 1 164 ? 41.301 -34.580 -7.095  1.00 18.21 ?  164 LEU   B HD12 1 
ATOM   6656 H  HD13 . LEU   B 1 164 ? 40.200 -33.449 -6.909  1.00 18.21 ?  164 LEU   B HD13 1 
ATOM   6657 H  HD21 . LEU   B 1 164 ? 38.793 -34.688 -4.652  1.00 19.96 ?  164 LEU   B HD21 1 
ATOM   6658 H  HD22 . LEU   B 1 164 ? 37.939 -34.132 -5.870  1.00 19.96 ?  164 LEU   B HD22 1 
ATOM   6659 H  HD23 . LEU   B 1 164 ? 37.773 -35.643 -5.407  1.00 19.96 ?  164 LEU   B HD23 1 
ATOM   6660 N  N    . VAL   B 1 165 ? 38.042 -37.046 -10.455 1.00 16.27 ?  165 VAL   B N    1 
ATOM   6661 C  CA   . VAL   B 1 165 ? 37.378 -36.977 -11.753 1.00 18.20 ?  165 VAL   B CA   1 
ATOM   6662 C  C    . VAL   B 1 165 ? 36.463 -38.179 -11.942 1.00 20.12 ?  165 VAL   B C    1 
ATOM   6663 O  O    . VAL   B 1 165 ? 35.296 -38.042 -12.335 1.00 21.59 ?  165 VAL   B O    1 
ATOM   6664 C  CB   . VAL   B 1 165 ? 38.419 -36.885 -12.884 1.00 19.22 ?  165 VAL   B CB   1 
ATOM   6665 C  CG1  . VAL   B 1 165 ? 37.750 -37.003 -14.237 1.00 20.39 ?  165 VAL   B CG1  1 
ATOM   6666 C  CG2  . VAL   B 1 165 ? 39.209 -35.594 -12.783 1.00 19.15 ?  165 VAL   B CG2  1 
ATOM   6667 H  H    . VAL   B 1 165 ? 38.890 -37.197 -10.501 1.00 19.51 ?  165 VAL   B H    1 
ATOM   6668 H  HA   . VAL   B 1 165 ? 36.831 -36.180 -11.790 1.00 21.83 ?  165 VAL   B HA   1 
ATOM   6669 H  HB   . VAL   B 1 165 ? 39.051 -37.616 -12.795 1.00 23.05 ?  165 VAL   B HB   1 
ATOM   6670 H  HG11 . VAL   B 1 165 ? 38.355 -36.677 -14.919 1.00 24.46 ?  165 VAL   B HG11 1 
ATOM   6671 H  HG12 . VAL   B 1 165 ? 37.546 -37.938 -14.402 1.00 24.46 ?  165 VAL   B HG12 1 
ATOM   6672 H  HG13 . VAL   B 1 165 ? 36.936 -36.481 -14.234 1.00 24.46 ?  165 VAL   B HG13 1 
ATOM   6673 H  HG21 . VAL   B 1 165 ? 39.821 -35.535 -13.534 1.00 22.97 ?  165 VAL   B HG21 1 
ATOM   6674 H  HG22 . VAL   B 1 165 ? 38.594 -34.843 -12.802 1.00 22.97 ?  165 VAL   B HG22 1 
ATOM   6675 H  HG23 . VAL   B 1 165 ? 39.709 -35.588 -11.950 1.00 22.97 ?  165 VAL   B HG23 1 
ATOM   6676 N  N    . SER   B 1 166 ? 36.987 -39.381 -11.664 1.00 21.35 ?  166 SER   B N    1 
ATOM   6677 C  CA   . SER   B 1 166 ? 36.238 -40.597 -11.948 1.00 22.38 ?  166 SER   B CA   1 
ATOM   6678 C  C    . SER   B 1 166 ? 34.975 -40.684 -11.106 1.00 22.79 ?  166 SER   B C    1 
ATOM   6679 O  O    . SER   B 1 166 ? 34.002 -41.305 -11.532 1.00 24.04 ?  166 SER   B O    1 
ATOM   6680 C  CB   . SER   B 1 166 ? 37.116 -41.848 -11.770 1.00 23.31 ?  166 SER   B CB   1 
ATOM   6681 O  OG   . SER   B 1 166 ? 37.460 -42.067 -10.411 1.00 23.62 ?  166 SER   B OG   1 
ATOM   6682 H  H    . SER   B 1 166 ? 37.773 -39.512 -11.320 1.00 25.61 ?  166 SER   B H    1 
ATOM   6683 H  HA   . SER   B 1 166 ? 35.971 -40.578 -12.877 1.00 26.84 ?  166 SER   B HA   1 
ATOM   6684 H  HB2  . SER   B 1 166 ? 36.634 -42.621 -12.097 1.00 27.96 ?  166 SER   B HB2  1 
ATOM   6685 H  HB3  . SER   B 1 166 ? 37.936 -41.735 -12.289 1.00 27.96 ?  166 SER   B HB3  1 
ATOM   6686 H  HG   . SER   B 1 166 ? 37.898 -41.405 -10.121 1.00 28.33 ?  166 SER   B HG   1 
ATOM   6687 N  N    . SER   B 1 167 ? 34.955 -40.065 -9.926  1.00 20.88 ?  167 SER   B N    1 
ATOM   6688 C  CA   . SER   B 1 167 ? 33.800 -40.123 -9.038  1.00 20.15 ?  167 SER   B CA   1 
ATOM   6689 C  C    . SER   B 1 167 ? 32.889 -38.898 -9.131  1.00 19.71 ?  167 SER   B C    1 
ATOM   6690 O  O    . SER   B 1 167 ? 31.814 -38.891 -8.521  1.00 20.07 ?  167 SER   B O    1 
ATOM   6691 C  CB   . SER   B 1 167 ? 34.247 -40.307 -7.581  1.00 20.24 ?  167 SER   B CB   1 
ATOM   6692 O  OG   . SER   B 1 167 ? 34.907 -39.142 -7.100  1.00 20.44 ?  167 SER   B OG   1 
ATOM   6693 H  H    . SER   B 1 167 ? 35.605 -39.602 -9.618  1.00 25.05 ?  167 SER   B H    1 
ATOM   6694 H  HA   . SER   B 1 167 ? 33.267 -40.900 -9.281  1.00 24.17 ?  167 SER   B HA   1 
ATOM   6695 H  HB2  . SER   B 1 167 ? 33.461 -40.484 -7.034  1.00 24.27 ?  167 SER   B HB2  1 
ATOM   6696 H  HB3  . SER   B 1 167 ? 34.847 -41.076 -7.535  1.00 24.27 ?  167 SER   B HB3  1 
ATOM   6697 H  HG   . SER   B 1 167 ? 35.595 -39.012 -7.555  1.00 24.51 ?  167 SER   B HG   1 
ATOM   6698 N  N    . PHE   B 1 168 ? 33.278 -37.858 -9.866  1.00 19.52 ?  168 PHE   B N    1 
ATOM   6699 C  CA   . PHE   B 1 168 ? 32.447 -36.654 -9.916  1.00 18.89 ?  168 PHE   B CA   1 
ATOM   6700 C  C    . PHE   B 1 168 ? 31.136 -36.908 -10.655 1.00 16.49 ?  168 PHE   B C    1 
ATOM   6701 O  O    . PHE   B 1 168 ? 30.094 -36.310 -10.318 1.00 16.73 ?  168 PHE   B O    1 
ATOM   6702 C  CB   . PHE   B 1 168 ? 33.213 -35.507 -10.571 1.00 19.39 ?  168 PHE   B CB   1 
ATOM   6703 C  CG   . PHE   B 1 168 ? 32.395 -34.263 -10.737 1.00 19.56 ?  168 PHE   B CG   1 
ATOM   6704 C  CD1  . PHE   B 1 168 ? 32.027 -33.514 -9.629  1.00 20.41 ?  168 PHE   B CD1  1 
ATOM   6705 C  CD2  . PHE   B 1 168 ? 31.973 -33.852 -11.987 1.00 18.99 ?  168 PHE   B CD2  1 
ATOM   6706 C  CE1  . PHE   B 1 168 ? 31.257 -32.375 -9.762  1.00 20.82 ?  168 PHE   B CE1  1 
ATOM   6707 C  CE2  . PHE   B 1 168 ? 31.215 -32.695 -12.135 1.00 19.95 ?  168 PHE   B CE2  1 
ATOM   6708 C  CZ   . PHE   B 1 168 ? 30.851 -31.956 -11.019 1.00 20.18 ?  168 PHE   B CZ   1 
ATOM   6709 H  H    . PHE   B 1 168 ? 34.005 -37.819 -10.326 1.00 23.42 ?  168 PHE   B H    1 
ATOM   6710 H  HA   . PHE   B 1 168 ? 32.225 -36.391 -9.013  1.00 22.65 ?  168 PHE   B HA   1 
ATOM   6711 H  HB2  . PHE   B 1 168 ? 33.976 -35.285 -10.018 1.00 23.26 ?  168 PHE   B HB2  1 
ATOM   6712 H  HB3  . PHE   B 1 168 ? 33.507 -35.782 -11.451 1.00 23.26 ?  168 PHE   B HB3  1 
ATOM   6713 H  HD1  . PHE   B 1 168 ? 32.289 -33.793 -8.783  1.00 24.48 ?  168 PHE   B HD1  1 
ATOM   6714 H  HD2  . PHE   B 1 168 ? 32.213 -34.337 -12.739 1.00 22.78 ?  168 PHE   B HD2  1 
ATOM   6715 H  HE1  . PHE   B 1 168 ? 31.012 -31.886 -9.011  1.00 24.97 ?  168 PHE   B HE1  1 
ATOM   6716 H  HE2  . PHE   B 1 168 ? 30.934 -32.426 -12.982 1.00 23.93 ?  168 PHE   B HE2  1 
ATOM   6717 H  HZ   . PHE   B 1 168 ? 30.329 -31.192 -11.116 1.00 24.20 ?  168 PHE   B HZ   1 
ATOM   6718 N  N    A LEU   B 1 169 ? 31.167 -37.783 -11.655 0.50 17.42 ?  169 LEU   B N    1 
ATOM   6719 N  N    B LEU   B 1 169 ? 31.161 -37.784 -11.656 0.50 16.86 ?  169 LEU   B N    1 
ATOM   6720 C  CA   A LEU   B 1 169 ? 29.989 -38.111 -12.442 0.50 19.83 ?  169 LEU   B CA   1 
ATOM   6721 C  CA   B LEU   B 1 169 ? 29.972 -38.074 -12.449 0.50 18.86 ?  169 LEU   B CA   1 
ATOM   6722 C  C    A LEU   B 1 169 ? 30.043 -39.569 -12.870 0.50 21.77 ?  169 LEU   B C    1 
ATOM   6723 C  C    B LEU   B 1 169 ? 29.917 -39.509 -12.957 0.50 20.38 ?  169 LEU   B C    1 
ATOM   6724 O  O    A LEU   B 1 169 ? 29.071 -40.132 -13.378 0.50 23.12 ?  169 LEU   B O    1 
ATOM   6725 O  O    B LEU   B 1 169 ? 29.045 -39.839 -13.763 0.50 21.55 ?  169 LEU   B O    1 
ATOM   6726 C  CB   A LEU   B 1 169 ? 29.920 -37.222 -13.680 0.50 21.27 ?  169 LEU   B CB   1 
ATOM   6727 C  CB   B LEU   B 1 169 ? 29.899 -37.130 -13.648 0.50 20.41 ?  169 LEU   B CB   1 
ATOM   6728 C  CG   A LEU   B 1 169 ? 28.717 -36.288 -13.787 0.50 23.10 ?  169 LEU   B CG   1 
ATOM   6729 C  CG   B LEU   B 1 169 ? 28.649 -36.258 -13.750 0.50 22.43 ?  169 LEU   B CG   1 
ATOM   6730 C  CD1  A LEU   B 1 169 ? 28.700 -35.627 -15.150 0.50 23.57 ?  169 LEU   B CD1  1 
ATOM   6731 C  CD1  B LEU   B 1 169 ? 28.563 -35.644 -15.132 0.50 22.97 ?  169 LEU   B CD1  1 
ATOM   6732 C  CD2  A LEU   B 1 169 ? 27.422 -37.040 -13.535 0.50 23.35 ?  169 LEU   B CD2  1 
ATOM   6733 C  CD2  B LEU   B 1 169 ? 27.396 -37.057 -13.435 0.50 22.60 ?  169 LEU   B CD2  1 
ATOM   6734 O  OXT  A LEU   B 1 169 ? 31.081 -40.211 -12.720 0.50 22.38 -1 169 LEU   B OXT  1 
ATOM   6735 O  OXT  B LEU   B 1 169 ? 30.723 -40.361 -12.594 0.50 21.24 -1 169 LEU   B OXT  1 
ATOM   6736 H  H    A LEU   B 1 169 ? 31.871 -38.209 -11.906 0.50 20.89 ?  169 LEU   B H    1 
ATOM   6737 H  H    B LEU   B 1 169 ? 31.857 -38.223 -11.906 0.50 20.22 ?  169 LEU   B H    1 
ATOM   6738 H  HA   A LEU   B 1 169 ? 29.195 -37.972 -11.905 0.50 23.79 ?  169 LEU   B HA   1 
ATOM   6739 H  HA   B LEU   B 1 169 ? 29.196 -37.931 -11.889 0.50 22.63 ?  169 LEU   B HA   1 
ATOM   6740 H  HB2  A LEU   B 1 169 ? 30.715 -36.667 -13.700 0.50 25.51 ?  169 LEU   B HB2  1 
ATOM   6741 H  HB2  B LEU   B 1 169 ? 30.663 -36.534 -13.617 0.50 24.48 ?  169 LEU   B HB2  1 
ATOM   6742 H  HB3  A LEU   B 1 169 ? 29.906 -37.790 -14.466 0.50 25.51 ?  169 LEU   B HB3  1 
ATOM   6743 H  HB3  B LEU   B 1 169 ? 29.942 -37.662 -14.460 0.50 24.48 ?  169 LEU   B HB3  1 
ATOM   6744 H  HG   A LEU   B 1 169 ? 28.795 -35.590 -13.117 0.50 27.70 ?  169 LEU   B HG   1 
ATOM   6745 H  HG   B LEU   B 1 169 ? 28.715 -35.535 -13.106 0.50 26.91 ?  169 LEU   B HG   1 
ATOM   6746 H  HD11 A LEU   B 1 169 ? 27.944 -35.022 -15.198 0.50 28.27 ?  169 LEU   B HD11 1 
ATOM   6747 H  HD11 B LEU   B 1 169 ? 27.782 -35.071 -15.174 0.50 27.55 ?  169 LEU   B HD11 1 
ATOM   6748 H  HD12 A LEU   B 1 169 ? 29.527 -35.137 -15.271 0.50 28.27 ?  169 LEU   B HD12 1 
ATOM   6749 H  HD12 B LEU   B 1 169 ? 29.365 -35.125 -15.296 0.50 27.55 ?  169 LEU   B HD12 1 
ATOM   6750 H  HD13 A LEU   B 1 169 ? 28.619 -36.314 -15.830 0.50 28.27 ?  169 LEU   B HD13 1 
ATOM   6751 H  HD13 B LEU   B 1 169 ? 28.489 -36.356 -15.787 0.50 27.55 ?  169 LEU   B HD13 1 
ATOM   6752 H  HD21 A LEU   B 1 169 ? 26.692 -36.564 -13.957 0.50 28.01 ?  169 LEU   B HD21 1 
ATOM   6753 H  HD21 B LEU   B 1 169 ? 26.638 -36.642 -13.870 0.50 27.11 ?  169 LEU   B HD21 1 
ATOM   6754 H  HD22 A LEU   B 1 169 ? 27.500 -37.931 -13.913 0.50 28.01 ?  169 LEU   B HD22 1 
ATOM   6755 H  HD22 B LEU   B 1 169 ? 27.511 -37.965 -13.762 0.50 27.11 ?  169 LEU   B HD22 1 
ATOM   6756 H  HD23 A LEU   B 1 169 ? 27.273 -37.099 -12.579 0.50 28.01 ?  169 LEU   B HD23 1 
ATOM   6757 H  HD23 B LEU   B 1 169 ? 27.264 -37.067 -12.474 0.50 27.11 ?  169 LEU   B HD23 1 
HETATM 6758 S  S    B DMS   C 2 .   ? 10.395 3.329   0.559   0.50 32.43 ?  301 DMS   A S    1 
HETATM 6759 O  O    B DMS   C 2 .   ? 10.717 4.128   -0.681  0.50 32.62 ?  301 DMS   A O    1 
HETATM 6760 C  C1   B DMS   C 2 .   ? 8.606  3.500   0.823   0.50 32.79 ?  301 DMS   A C1   1 
HETATM 6761 C  C2   B DMS   C 2 .   ? 11.039 4.285   1.962   0.50 32.78 ?  301 DMS   A C2   1 
HETATM 6762 H  H11  B DMS   C 2 .   ? 8.130  3.238   -0.066  0.50 39.33 ?  301 DMS   A H11  1 
HETATM 6763 H  H12  B DMS   C 2 .   ? 8.476  4.490   1.075   0.50 39.33 ?  301 DMS   A H12  1 
HETATM 6764 H  H13  B DMS   C 2 .   ? 8.389  2.844   1.597   0.50 39.33 ?  301 DMS   A H13  1 
HETATM 6765 H  H21  B DMS   C 2 .   ? 12.062 4.411   1.815   0.50 39.32 ?  301 DMS   A H21  1 
HETATM 6766 H  H22  B DMS   C 2 .   ? 10.518 5.179   1.925   0.50 39.32 ?  301 DMS   A H22  1 
HETATM 6767 H  H23  B DMS   C 2 .   ? 10.818 3.713   2.790   0.50 39.32 ?  301 DMS   A H23  1 
HETATM 6768 N  N2   B A1BBQ D 3 .   ? 14.974 0.047   4.018   0.50 10.39 ?  302 A1BBQ A N2   1 
HETATM 6769 C  C3   B A1BBQ D 3 .   ? 13.943 -1.060  1.148   0.50 12.24 ?  302 A1BBQ A C3   1 
HETATM 6770 C  C6   B A1BBQ D 3 .   ? 13.050 -3.002  -0.262  0.50 15.37 ?  302 A1BBQ A C6   1 
HETATM 6771 C  C9   B A1BBQ D 3 .   ? 14.992 0.033   5.385   0.50 10.31 ?  302 A1BBQ A C9   1 
HETATM 6772 C  C12  B A1BBQ D 3 .   ? 15.466 3.865   3.917   0.50 10.38 ?  302 A1BBQ A C12  1 
HETATM 6773 C  C1   B A1BBQ D 3 .   ? 14.955 2.348   1.086   0.50 11.63 ?  302 A1BBQ A C1   1 
HETATM 6774 C  C10  B A1BBQ D 3 .   ? 15.258 2.252   5.502   0.50 10.31 ?  302 A1BBQ A C10  1 
HETATM 6775 C  C11  B A1BBQ D 3 .   ? 15.266 2.429   4.086   0.50 10.30 ?  302 A1BBQ A C11  1 
HETATM 6776 C  C13  B A1BBQ D 3 .   ? 15.546 4.447   5.175   0.50 9.92  ?  302 A1BBQ A C13  1 
HETATM 6777 C  C2   B A1BBQ D 3 .   ? 15.206 -0.134  1.224   0.50 11.30 ?  302 A1BBQ A C2   1 
HETATM 6778 C  C4   B A1BBQ D 3 .   ? 12.719 -0.257  0.615   0.50 13.81 ?  302 A1BBQ A C4   1 
HETATM 6779 C  C5   B A1BBQ D 3 .   ? 11.601 -1.129  0.041   0.50 15.30 ?  302 A1BBQ A C5   1 
HETATM 6780 C  C7   B A1BBQ D 3 .   ? 14.275 -2.261  0.257   0.50 13.80 ?  302 A1BBQ A C7   1 
HETATM 6781 C  C8   B A1BBQ D 3 .   ? 15.096 1.211   3.342   0.50 10.43 ?  302 A1BBQ A C8   1 
HETATM 6782 N  N1   B A1BBQ D 3 .   ? 15.078 1.137   1.928   0.50 10.77 ?  302 A1BBQ A N1   1 
HETATM 6783 N  N3   B A1BBQ D 3 .   ? 15.116 1.083   6.163   0.50 10.54 ?  302 A1BBQ A N3   1 
HETATM 6784 N  N4   B A1BBQ D 3 .   ? 15.420 3.455   6.108   0.50 10.24 ?  302 A1BBQ A N4   1 
HETATM 6785 O  O1   B A1BBQ D 3 .   ? 13.605 -1.516  2.430   0.50 10.84 ?  302 A1BBQ A O1   1 
HETATM 6786 O  O2   B A1BBQ D 3 .   ? 12.078 -2.149  -0.804  0.50 15.95 ?  302 A1BBQ A O2   1 
HETATM 6787 H  H12  B A1BBQ D 3 .   ? 13.320 -3.731  -1.071  0.50 18.44 ?  302 A1BBQ A H12  1 
HETATM 6788 H  H11  B A1BBQ D 3 .   ? 12.595 -3.654  0.518   0.50 18.44 ?  302 A1BBQ A H11  1 
HETATM 6789 H  H15  B A1BBQ D 3 .   ? 14.857 -0.932  5.950   0.50 12.36 ?  302 A1BBQ A H15  1 
HETATM 6790 H  H16  B A1BBQ D 3 .   ? 15.520 4.450   3.028   0.50 12.45 ?  302 A1BBQ A H16  1 
HETATM 6791 H  H1   B A1BBQ D 3 .   ? 14.833 2.113   0.010   0.50 13.94 ?  302 A1BBQ A H1   1 
HETATM 6792 H  H3   B A1BBQ D 3 .   ? 15.875 2.988   1.119   0.50 13.94 ?  302 A1BBQ A H3   1 
HETATM 6793 H  H2   B A1BBQ D 3 .   ? 14.142 3.065   1.318   0.50 13.94 ?  302 A1BBQ A H2   1 
HETATM 6794 H  H17  B A1BBQ D 3 .   ? 15.671 5.438   5.581   0.50 11.89 ?  302 A1BBQ A H17  1 
HETATM 6795 H  H4   B A1BBQ D 3 .   ? 15.585 0.060   0.191   0.50 13.55 ?  302 A1BBQ A H4   1 
HETATM 6796 H  H5   B A1BBQ D 3 .   ? 16.043 -0.721  1.681   0.50 13.55 ?  302 A1BBQ A H5   1 
HETATM 6797 H  H7   B A1BBQ D 3 .   ? 12.301 0.397   1.417   0.50 16.56 ?  302 A1BBQ A H7   1 
HETATM 6798 H  H8   B A1BBQ D 3 .   ? 13.029 0.458   -0.163  0.50 16.56 ?  302 A1BBQ A H8   1 
HETATM 6799 H  H9   B A1BBQ D 3 .   ? 10.993 -1.614  0.848   0.50 18.35 ?  302 A1BBQ A H9   1 
HETATM 6800 H  H10  B A1BBQ D 3 .   ? 10.816 -0.522  -0.499  0.50 18.35 ?  302 A1BBQ A H10  1 
HETATM 6801 H  H13  B A1BBQ D 3 .   ? 14.932 -1.943  -0.587  0.50 16.55 ?  302 A1BBQ A H13  1 
HETATM 6802 H  H14  B A1BBQ D 3 .   ? 14.901 -2.987  0.802   0.50 16.55 ?  302 A1BBQ A H14  1 
HETATM 6803 H  H18  B A1BBQ D 3 .   ? 15.452 3.607   7.129   0.50 12.27 ?  302 A1BBQ A H18  1 
HETATM 6804 H  H6   B A1BBQ D 3 .   ? 14.220 -2.193  2.724   0.50 13.00 ?  302 A1BBQ A H6   1 
HETATM 6805 CL CL   B CL    E 4 .   ? 18.227 1.998   -0.891  0.50 12.92 ?  303 CL    A CL   1 
HETATM 6806 O  O    . HOH   F 5 .   ? 4.925  3.734   0.350   1.00 34.15 ?  401 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 17.663 -1.894  0.345   1.00 21.88 ?  402 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 15.149 -12.290 18.600  1.00 45.91 ?  403 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? 11.761 -10.822 -10.086 1.00 50.40 ?  404 HOH   A O    1 
HETATM 6810 O  O    A HOH   F 5 .   ? 14.743 -4.664  20.357  0.50 31.90 ?  405 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 23.985 -15.800 -9.227  1.00 38.11 ?  406 HOH   A O    1 
HETATM 6812 O  O    B HOH   F 5 .   ? 17.323 -2.714  -1.665  0.50 27.31 ?  407 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 28.429 -0.244  -13.455 1.00 35.25 ?  408 HOH   A O    1 
HETATM 6814 O  O    A HOH   F 5 .   ? 3.595  -9.539  9.629   0.50 37.92 ?  409 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 6.894  -8.372  11.609  1.00 22.60 ?  410 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 28.958 0.402   -9.753  1.00 21.04 ?  411 HOH   A O    1 
HETATM 6817 O  O    . HOH   F 5 .   ? 14.223 -4.512  -11.901 1.00 40.59 ?  412 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 22.266 5.268   18.997  1.00 47.04 ?  413 HOH   A O    1 
HETATM 6819 O  O    B HOH   F 5 .   ? 14.548 -4.106  3.269   0.50 12.34 ?  414 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 34.396 -1.816  12.554  1.00 38.23 ?  415 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? -0.434 -3.166  3.072   1.00 40.38 ?  416 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 7.999  -13.016 -1.204  1.00 25.21 ?  417 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 14.705 -13.901 16.699  1.00 29.85 ?  418 HOH   A O    1 
HETATM 6824 O  O    B HOH   F 5 .   ? 18.873 -0.441  -2.663  0.50 21.47 ?  419 HOH   A O    1 
HETATM 6825 O  O    B HOH   F 5 .   ? 14.853 7.004   7.604   0.50 19.67 ?  420 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 9.052  -10.266 19.145  1.00 41.33 ?  421 HOH   A O    1 
HETATM 6827 O  O    B HOH   F 5 .   ? 12.157 -1.621  -3.329  0.50 17.10 ?  422 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 30.331 -13.322 -8.438  1.00 24.56 ?  423 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 11.930 0.265   14.648  1.00 35.10 ?  424 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 42.311 10.562  5.078   1.00 19.87 ?  425 HOH   A O    1 
HETATM 6831 O  O    B HOH   F 5 .   ? 14.912 -0.905  -12.393 0.50 27.28 ?  426 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 0.617  -4.900  -0.001  1.00 35.84 ?  427 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 14.881 3.894   17.619  1.00 40.06 ?  428 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 28.231 -6.266  19.563  1.00 40.99 ?  429 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 28.698 -10.616 -14.136 1.00 39.27 ?  430 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 25.785 -0.947  -7.512  1.00 16.97 ?  431 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 38.134 10.244  7.151   1.00 47.95 ?  432 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 37.441 2.835   10.276  1.00 23.70 ?  433 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 44.210 7.198   6.455   1.00 26.94 ?  434 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 10.881 1.467   12.430  1.00 22.59 ?  435 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 26.591 -19.341 -1.764  1.00 14.34 ?  436 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 31.057 -18.131 7.806   1.00 18.59 ?  437 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 13.480 -1.419  -6.834  1.00 22.07 ?  438 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 18.707 -19.358 13.508  1.00 31.07 ?  439 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 13.628 -15.317 -7.622  1.00 29.32 ?  440 HOH   A O    1 
HETATM 6846 O  O    B HOH   F 5 .   ? 15.684 3.096   -2.451  0.50 19.64 ?  441 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 36.199 -5.072  -0.492  1.00 30.76 ?  442 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 30.785 6.269   -12.244 1.00 26.41 ?  443 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 18.935 -22.026 6.847   1.00 33.23 ?  444 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 22.192 -19.335 11.317  1.00 33.54 ?  445 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? -0.754 -8.767  2.042   1.00 44.57 ?  446 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 22.601 -11.990 21.912  1.00 57.06 ?  447 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 8.336  -21.564 3.829   1.00 59.47 ?  448 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 27.302 13.759  2.824   1.00 31.58 ?  449 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 38.475 4.996   7.037   1.00 15.15 ?  450 HOH   A O    1 
HETATM 6856 O  O    A HOH   F 5 .   ? 14.263 0.517   6.738   0.50 25.58 ?  451 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 43.304 7.787   2.696   1.00 34.59 ?  452 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 17.253 -18.052 14.906  1.00 30.41 ?  453 HOH   A O    1 
HETATM 6859 O  O    . HOH   F 5 .   ? 34.020 -1.139  -8.912  1.00 25.28 ?  454 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 37.147 -2.811  9.760   1.00 51.87 ?  455 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 26.739 11.359  1.666   1.00 15.24 ?  456 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 14.437 -21.287 -4.368  1.00 26.03 ?  457 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 39.746 -1.018  -5.149  1.00 20.83 ?  458 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 31.581 8.189   14.866  1.00 24.48 ?  459 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 5.095  2.333   4.993   1.00 31.97 ?  460 HOH   A O    1 
HETATM 6866 O  O    . HOH   F 5 .   ? 30.725 3.077   8.320   1.00 11.82 ?  461 HOH   A O    1 
HETATM 6867 O  O    B HOH   F 5 .   ? 21.174 -2.262  -2.749  0.50 12.92 ?  462 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 35.821 -12.643 6.864   1.00 15.27 ?  463 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 18.428 9.436   8.908   1.00 21.33 ?  464 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 20.674 -19.801 -5.095  1.00 29.10 ?  465 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 20.053 -12.718 -8.762  1.00 25.64 ?  466 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 42.454 4.285   5.400   1.00 33.36 ?  467 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 31.178 -13.948 -2.430  1.00 13.57 ?  468 HOH   A O    1 
HETATM 6874 O  O    A HOH   F 5 .   ? 21.266 -2.436  -2.093  0.50 9.97  ?  469 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 37.186 11.989  4.972   1.00 28.42 ?  470 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 21.906 -21.900 8.424   1.00 29.36 ?  471 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 24.050 -2.165  -2.170  1.00 10.64 ?  472 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 9.936  -21.516 5.646   1.00 17.61 ?  473 HOH   A O    1 
HETATM 6879 O  O    A HOH   F 5 .   ? 20.124 4.505   -7.587  0.50 20.82 ?  474 HOH   A O    1 
HETATM 6880 O  O    A HOH   F 5 .   ? 18.974 -0.712  -1.674  0.50 10.90 ?  475 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 22.714 12.458  1.527   1.00 14.65 ?  476 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 27.390 -10.582 14.097  1.00 16.79 ?  477 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 6.337  -5.838  10.810  1.00 19.83 ?  478 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 21.080 10.179  14.965  1.00 33.95 ?  479 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 27.911 0.779   -7.191  1.00 14.01 ?  480 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 32.004 -7.277  -9.733  1.00 20.92 ?  481 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 33.670 -7.141  4.359   1.00 15.70 ?  482 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 33.614 -16.951 8.139   1.00 19.04 ?  483 HOH   A O    1 
HETATM 6889 O  O    B HOH   F 5 .   ? 22.672 5.825   -1.811  0.50 14.48 ?  484 HOH   A O    1 
HETATM 6890 O  O    B HOH   F 5 .   ? 7.632  -6.112  -5.656  0.50 30.12 ?  485 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 43.926 8.537   -2.997  1.00 26.33 ?  486 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 16.236 16.661  8.564   1.00 40.73 ?  487 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 24.615 1.916   -7.205  1.00 23.33 ?  488 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 17.093 -19.341 4.815   1.00 14.78 ?  489 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 26.913 4.125   -0.685  1.00 11.79 ?  490 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 16.663 -22.120 0.935   1.00 30.12 ?  491 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 24.178 -7.760  14.432  1.00 15.84 ?  492 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 37.502 -2.080  5.927   1.00 28.19 ?  493 HOH   A O    1 
HETATM 6899 O  O    A HOH   F 5 .   ? 15.795 -0.998  5.212   0.50 28.79 ?  494 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 24.377 3.528   -1.869  1.00 13.39 ?  495 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 27.668 -6.290  -14.026 1.00 33.08 ?  496 HOH   A O    1 
HETATM 6902 O  O    . HOH   F 5 .   ? 6.545  -3.634  12.607  1.00 29.88 ?  497 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 30.530 1.915   16.765  1.00 20.13 ?  498 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 13.791 -4.960  17.274  1.00 28.97 ?  499 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 10.428 -22.183 -1.413  1.00 57.32 ?  500 HOH   A O    1 
HETATM 6906 O  O    A HOH   F 5 .   ? 14.642 -3.708  3.034   0.50 15.32 ?  501 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 24.673 -17.551 12.703  1.00 23.39 ?  502 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 17.297 -17.787 -5.176  1.00 27.81 ?  503 HOH   A O    1 
HETATM 6909 O  O    . HOH   F 5 .   ? 8.811  -12.038 17.146  1.00 35.55 ?  504 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 32.767 -9.293  5.945   1.00 20.07 ?  505 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 19.089 -11.169 24.051  1.00 77.85 ?  506 HOH   A O    1 
HETATM 6912 O  O    A HOH   F 5 .   ? 14.529 -0.488  -12.100 0.50 24.94 ?  507 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 20.621 -20.047 2.702   1.00 18.72 ?  508 HOH   A O    1 
HETATM 6914 O  O    B HOH   F 5 .   ? 21.193 2.892   -0.025  0.50 12.02 ?  509 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 26.859 -3.164  19.529  1.00 37.72 ?  510 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 15.214 -8.103  -9.997  1.00 25.29 ?  511 HOH   A O    1 
HETATM 6917 O  O    A HOH   F 5 .   ? 21.354 3.115   -0.387  0.50 9.72  ?  512 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 40.994 -8.290  -6.800  1.00 34.12 ?  513 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 23.411 11.368  4.041   1.00 11.83 ?  514 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 10.514 -13.894 -1.989  1.00 17.55 ?  515 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 16.019 6.975   2.812   1.00 13.15 ?  516 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 38.052 -1.288  -1.900  1.00 17.98 ?  517 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 27.137 2.386   18.768  1.00 32.02 ?  518 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 14.173 -23.148 7.347   1.00 18.78 ?  519 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 15.303 -21.550 14.223  1.00 18.50 ?  520 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 30.032 -10.054 13.034  1.00 24.12 ?  521 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 15.790 2.048   24.665  1.00 51.29 ?  522 HOH   A O    1 
HETATM 6928 O  O    A HOH   F 5 .   ? 18.637 -2.498  -16.388 0.50 31.08 ?  523 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 32.568 -10.655 3.253   1.00 29.96 ?  524 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 24.026 -20.293 -1.356  1.00 17.83 ?  525 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 30.291 -12.891 13.569  1.00 19.14 ?  526 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 15.428 11.871  7.800   1.00 42.28 ?  527 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 16.226 -14.276 20.158  1.00 57.72 ?  528 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 35.239 -5.233  -3.057  1.00 17.59 ?  529 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 11.679 -10.857 16.839  1.00 27.78 ?  530 HOH   A O    1 
HETATM 6936 O  O    A HOH   F 5 .   ? 24.110 3.926   -4.945  0.50 16.92 ?  531 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 22.551 8.203   18.364  1.00 45.37 ?  532 HOH   A O    1 
HETATM 6938 O  O    A HOH   F 5 .   ? 11.071 -0.439  1.861   0.50 29.39 ?  533 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 32.835 -4.382  -9.873  1.00 25.85 ?  534 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 41.636 1.422   5.057   1.00 39.54 ?  535 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 21.839 -13.971 -8.258  1.00 50.37 ?  536 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 36.720 -4.925  5.442   1.00 24.93 ?  537 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 14.432 -24.612 11.537  1.00 35.31 ?  538 HOH   A O    1 
HETATM 6944 O  O    A HOH   F 5 .   ? 7.754  -6.389  -6.597  0.50 31.52 ?  539 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 23.457 -8.014  17.040  1.00 20.43 ?  540 HOH   A O    1 
HETATM 6946 O  O    A HOH   F 5 .   ? 16.267 2.900   -1.495  0.50 16.87 ?  541 HOH   A O    1 
HETATM 6947 O  O    A HOH   F 5 .   ? 18.872 1.989   -0.798  0.50 13.68 ?  542 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 37.827 -8.841  -3.429  1.00 22.69 ?  543 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 45.041 -0.503  3.040   1.00 40.40 ?  544 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 23.458 -20.952 1.322   1.00 19.15 ?  545 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 21.232 -9.086  21.236  1.00 51.07 ?  546 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 34.383 -8.134  -0.421  1.00 28.45 ?  547 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 20.505 -17.695 24.812  1.00 59.72 ?  548 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 29.811 -2.030  -12.803 1.00 53.54 ?  549 HOH   A O    1 
HETATM 6955 O  O    A HOH   F 5 .   ? 9.430  -16.385 -2.071  0.50 35.16 ?  550 HOH   A O    1 
HETATM 6956 O  O    B HOH   F 5 .   ? 13.184 2.621   -1.825  0.50 19.54 ?  551 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 31.400 -12.833 0.049   1.00 20.19 ?  552 HOH   A O    1 
HETATM 6958 O  O    . HOH   F 5 .   ? 18.529 4.918   -15.046 1.00 56.91 ?  553 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 30.530 14.742  2.756   1.00 20.19 ?  554 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 21.515 -14.829 17.792  1.00 54.04 ?  555 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 18.351 -16.108 16.311  1.00 39.22 ?  556 HOH   A O    1 
HETATM 6962 O  O    . HOH   F 5 .   ? -1.693 -4.569  7.458   1.00 62.30 ?  557 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 23.271 7.728   -3.451  1.00 22.98 ?  558 HOH   A O    1 
HETATM 6964 O  O    A HOH   F 5 .   ? 14.027 -0.393  3.399   0.50 30.97 ?  559 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 27.619 6.963   -6.481  1.00 32.23 ?  560 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 29.884 -16.128 10.770  1.00 34.72 ?  561 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 32.372 -15.959 10.932  1.00 29.36 ?  562 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 20.017 -17.451 -5.090  1.00 27.16 ?  563 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 24.664 5.542   20.657  1.00 51.19 ?  564 HOH   A O    1 
HETATM 6970 O  O    . HOH   F 5 .   ? 25.441 8.339   -4.934  1.00 20.76 ?  565 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 23.282 -22.382 -3.263  1.00 37.29 ?  566 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 24.572 14.564  7.739   1.00 36.74 ?  567 HOH   A O    1 
HETATM 6973 O  O    . HOH   F 5 .   ? 18.755 10.923  11.164  1.00 31.53 ?  568 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 26.943 11.577  -1.236  1.00 29.69 ?  569 HOH   A O    1 
HETATM 6975 O  O    . HOH   F 5 .   ? 15.872 -21.613 3.633   1.00 21.78 ?  570 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 27.459 -11.411 16.539  1.00 39.48 ?  571 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 11.905 -13.420 16.247  1.00 54.41 ?  572 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 39.785 -7.051  -3.472  1.00 42.25 ?  573 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 23.355 13.652  5.530   1.00 18.77 ?  574 HOH   A O    1 
HETATM 6980 O  O    . HOH   F 5 .   ? 25.953 10.805  -3.648  1.00 22.55 ?  575 HOH   A O    1 
HETATM 6981 O  O    B HOH   F 5 .   ? 11.509 1.145   -3.086  0.50 24.86 ?  576 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 18.186 -16.284 -8.960  1.00 46.38 ?  577 HOH   A O    1 
HETATM 6983 O  O    A HOH   F 5 .   ? 21.984 5.231   -5.871  0.50 32.86 ?  578 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 12.086 1.488   17.198  1.00 36.13 ?  579 HOH   A O    1 
HETATM 6985 O  O    . HOH   F 5 .   ? 11.068 -15.208 -6.220  1.00 35.42 ?  580 HOH   A O    1 
HETATM 6986 O  O    . HOH   F 5 .   ? 35.062 7.499   12.223  1.00 52.86 ?  581 HOH   A O    1 
HETATM 6987 O  O    . HOH   F 5 .   ? 15.765 -17.280 -7.096  1.00 32.20 ?  582 HOH   A O    1 
HETATM 6988 O  O    . HOH   F 5 .   ? 14.174 -10.325 -11.067 1.00 36.07 ?  583 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 28.723 -4.748  -12.290 1.00 37.46 ?  584 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 28.687 9.029   17.559  1.00 36.41 ?  585 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 41.015 -3.946  -0.322  1.00 37.10 ?  586 HOH   A O    1 
HETATM 6992 O  O    . HOH   F 5 .   ? 17.414 -18.755 19.678  1.00 52.42 ?  587 HOH   A O    1 
HETATM 6993 O  O    . HOH   F 5 .   ? 23.314 11.955  -4.089  1.00 21.45 ?  588 HOH   A O    1 
HETATM 6994 O  O    . HOH   F 5 .   ? 44.382 10.436  -1.656  1.00 36.33 ?  589 HOH   A O    1 
HETATM 6995 O  O    . HOH   F 5 .   ? 16.947 -20.504 16.095  1.00 33.34 ?  590 HOH   A O    1 
HETATM 6996 O  O    . HOH   F 5 .   ? 20.656 -15.996 -7.525  1.00 29.69 ?  591 HOH   A O    1 
HETATM 6997 O  O    . HOH   F 5 .   ? 30.880 0.671   19.140  1.00 39.78 ?  592 HOH   A O    1 
HETATM 6998 O  O    . HOH   F 5 .   ? 39.165 2.433   7.450   1.00 31.59 ?  593 HOH   A O    1 
HETATM 6999 O  O    . HOH   F 5 .   ? 16.113 -6.873  -11.896 1.00 47.80 ?  594 HOH   A O    1 
HETATM 7000 O  O    . HOH   F 5 .   ? 41.686 9.485   -3.859  1.00 30.68 ?  595 HOH   A O    1 
HETATM 7001 O  O    . HOH   F 5 .   ? 23.128 -12.940 19.153  1.00 49.75 ?  596 HOH   A O    1 
HETATM 7002 O  O    . HOH   F 5 .   ? 18.518 -23.222 1.890   1.00 47.25 ?  597 HOH   A O    1 
HETATM 7003 O  O    . HOH   F 5 .   ? 31.572 -0.606  -10.529 1.00 24.77 ?  598 HOH   A O    1 
HETATM 7004 O  O    . HOH   F 5 .   ? 28.867 -8.038  -15.290 1.00 52.53 ?  599 HOH   A O    1 
HETATM 7005 O  O    . HOH   F 5 .   ? 25.779 -18.922 -11.880 1.00 40.65 ?  600 HOH   A O    1 
HETATM 7006 O  O    . HOH   F 5 .   ? 16.221 -23.404 5.745   1.00 31.81 ?  601 HOH   A O    1 
HETATM 7007 O  O    . HOH   F 5 .   ? 13.917 -25.334 8.739   1.00 39.01 ?  602 HOH   A O    1 
HETATM 7008 O  O    . HOH   F 5 .   ? 20.165 -22.376 4.129   1.00 29.77 ?  603 HOH   A O    1 
HETATM 7009 O  O    . HOH   F 5 .   ? 30.737 5.779   -14.762 1.00 35.82 ?  604 HOH   A O    1 
HETATM 7010 O  O    . HOH   F 5 .   ? 40.589 -0.253  -7.763  1.00 31.07 ?  605 HOH   A O    1 
HETATM 7011 O  O    B HOH   F 5 .   ? 14.792 7.979   5.030   0.50 14.59 ?  606 HOH   A O    1 
HETATM 7012 O  O    . HOH   F 5 .   ? 37.423 -6.613  7.665   1.00 25.40 ?  607 HOH   A O    1 
HETATM 7013 O  O    . HOH   F 5 .   ? 8.119  -3.089  -5.782  1.00 56.20 ?  608 HOH   A O    1 
HETATM 7014 O  O    . HOH   F 5 .   ? 39.510 -0.055  6.629   1.00 31.83 ?  609 HOH   A O    1 
HETATM 7015 O  O    . HOH   F 5 .   ? 28.936 14.419  0.901   1.00 47.89 ?  610 HOH   A O    1 
HETATM 7016 O  O    . HOH   F 5 .   ? 30.820 -5.801  -11.936 1.00 53.05 ?  611 HOH   A O    1 
HETATM 7017 O  O    . HOH   F 5 .   ? 37.892 14.013  6.728   1.00 36.57 ?  612 HOH   A O    1 
HETATM 7018 O  O    . HOH   F 5 .   ? 36.527 -6.455  10.238  1.00 46.21 ?  613 HOH   A O    1 
HETATM 7019 O  O    . HOH   F 5 .   ? 22.127 -24.039 4.497   1.00 27.60 ?  614 HOH   A O    1 
HETATM 7020 O  O    A HOH   F 5 .   ? 14.830 8.596   4.834   0.50 27.51 ?  615 HOH   A O    1 
HETATM 7021 O  O    . HOH   F 5 .   ? 17.168 -6.757  -14.278 1.00 48.38 ?  616 HOH   A O    1 
HETATM 7022 O  O    . HOH   F 5 .   ? 24.200 9.272   -7.243  1.00 35.33 ?  617 HOH   A O    1 
HETATM 7023 O  O    . HOH   F 5 .   ? 15.823 -12.365 27.354  1.00 45.20 ?  618 HOH   A O    1 
HETATM 7024 O  O    . HOH   F 5 .   ? 16.227 -21.209 18.741  1.00 43.97 ?  619 HOH   A O    1 
HETATM 7025 O  O    . HOH   F 5 .   ? 14.638 -22.685 19.812  1.00 36.03 ?  620 HOH   A O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 29.936 -22.433 5.532   1.00 19.48 ?  201 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 27.682 -29.118 -1.939  1.00 35.07 ?  202 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 27.909 -41.619 -15.158 1.00 36.75 ?  203 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 38.028 -39.461 -0.221  1.00 40.13 ?  204 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 41.762 -36.066 -17.182 1.00 33.27 ?  205 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 49.434 -22.790 -19.730 1.00 49.61 ?  206 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 50.197 -3.482  7.081   1.00 31.89 ?  207 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 47.472 -7.394  -3.838  1.00 42.15 ?  208 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 41.349 -7.877  5.479   1.00 40.15 ?  209 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 56.736 -30.788 -7.793  1.00 30.50 ?  210 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 44.945 -43.558 -10.599 1.00 27.00 ?  211 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 54.606 -9.402  -8.661  1.00 18.79 ?  212 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 59.182 -18.765 6.917   1.00 33.57 ?  213 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 30.247 -40.968 -8.056  1.00 16.60 ?  214 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 30.074 -26.318 4.095   1.00 27.71 ?  215 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 48.100 -6.965  15.562  1.00 30.50 ?  216 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 57.742 -24.486 5.023   1.00 38.25 ?  217 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 44.557 -7.112  1.990   1.00 37.36 ?  218 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 34.616 -36.396 -7.144  1.00 18.70 ?  219 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 53.101 -13.386 -20.340 1.00 34.62 ?  220 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 56.467 -19.768 7.156   1.00 29.13 ?  221 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 58.316 -12.974 8.398   1.00 27.00 ?  222 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 31.010 -28.739 4.413   1.00 28.94 ?  223 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 43.091 -43.226 -8.156  1.00 28.62 ?  224 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 57.463 -16.280 -12.224 1.00 18.03 ?  225 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 55.471 -16.519 -14.302 1.00 32.73 ?  226 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 49.816 -0.519  10.234  1.00 28.77 ?  227 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 41.520 -39.182 -14.889 1.00 21.53 ?  228 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 57.192 -26.843 -7.636  1.00 39.45 ?  229 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 30.566 -42.218 -10.628 1.00 31.23 ?  230 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 38.583 -11.038 -2.281  1.00 19.53 ?  231 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 46.434 -1.615  13.245  1.00 26.86 ?  232 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 43.217 -32.390 -17.068 1.00 23.58 ?  233 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 37.249 -19.665 -18.120 1.00 44.85 ?  234 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 28.587 -19.662 -13.158 1.00 25.77 ?  235 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 34.992 -24.648 13.794  1.00 39.21 ?  236 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 50.796 -6.091  0.232   1.00 26.26 ?  237 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 51.653 -13.872 10.956  1.00 26.40 ?  238 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 32.786 -43.740 -11.331 1.00 22.21 ?  239 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 29.828 -34.125 -0.361  1.00 35.11 ?  240 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 40.627 -16.100 14.108  1.00 23.33 ?  241 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 51.735 -6.529  4.397   1.00 19.91 ?  242 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 44.596 -27.773 -0.645  1.00 21.52 ?  243 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 35.202 -8.011  -2.930  1.00 17.59 ?  244 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 39.377 -10.833 6.124   1.00 22.99 ?  245 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 41.475 -9.624  13.102  1.00 21.97 ?  246 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 50.992 -39.965 -8.179  1.00 30.98 ?  247 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 25.475 -25.913 -1.289  1.00 32.19 ?  248 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 57.712 -24.404 -3.746  1.00 21.25 ?  249 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 48.637 -36.523 -15.522 1.00 40.75 ?  250 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 50.852 -12.997 -0.424  1.00 11.43 ?  251 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 28.301 -34.295 -9.295  1.00 21.55 ?  252 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 58.277 -10.618 -4.000  1.00 20.20 ?  253 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 31.878 -17.876 -14.437 1.00 27.12 ?  254 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 39.640 -11.143 0.360   1.00 16.05 ?  255 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 42.723 -22.870 3.911   1.00 11.43 ?  256 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 46.981 -29.540 9.720   1.00 31.54 ?  257 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 36.103 -43.400 -8.402  1.00 39.69 ?  258 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 34.398 -18.408 11.489  1.00 25.73 ?  259 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 42.647 -25.377 2.712   1.00 14.97 ?  260 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 41.971 -23.536 9.351   1.00 18.19 ?  261 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 27.156 -31.766 -9.908  1.00 23.30 ?  262 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 49.372 -28.753 -6.926  1.00 15.45 ?  263 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 29.792 -25.179 -10.746 1.00 17.12 ?  264 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 32.165 -9.307  -6.565  1.00 23.44 ?  265 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 40.459 -12.754 -11.485 1.00 15.17 ?  266 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 56.249 -23.554 -14.653 1.00 26.72 ?  267 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 30.941 -15.745 2.705   1.00 13.51 ?  268 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 38.994 -11.923 12.379  1.00 39.17 ?  269 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 57.146 -12.107 12.363  1.00 35.15 ?  270 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 45.148 -35.011 6.791   1.00 37.62 ?  271 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 28.515 -30.883 -14.798 1.00 32.14 ?  272 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 48.104 -22.786 5.872   1.00 16.65 ?  273 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 42.462 -9.961  9.316   1.00 19.74 ?  274 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 46.637 -31.296 -4.792  1.00 18.78 ?  275 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 57.013 -8.628  8.449   1.00 19.29 ?  276 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 57.562 -9.226  1.431   1.00 19.65 ?  277 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 43.516 -15.837 -12.142 1.00 14.25 ?  278 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 35.010 -33.314 -19.193 1.00 28.47 ?  279 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 52.585 -10.404 12.964  1.00 20.89 ?  280 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 34.553 -12.795 2.659   1.00 23.38 ?  281 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 36.930 -12.797 -1.491  1.00 25.63 ?  282 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 28.896 -42.796 -12.378 1.00 38.61 ?  283 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 42.945 -20.264 -20.689 1.00 39.33 ?  284 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 42.490 -34.688 3.842   1.00 26.46 ?  285 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 28.039 -22.863 -7.963  1.00 17.65 ?  286 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 27.680 -26.698 -15.600 1.00 34.12 ?  287 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 48.802 -20.042 5.962   1.00 13.81 ?  288 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 48.487 -25.066 3.127   1.00 13.23 ?  289 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 33.642 -15.283 -13.876 1.00 21.17 ?  290 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 41.154 -5.587  11.530  1.00 44.35 ?  291 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 47.975 -24.554 -17.805 1.00 31.81 ?  292 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 47.125 -34.015 -4.620  1.00 17.66 ?  293 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 51.723 -5.952  -7.926  1.00 42.32 ?  294 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 50.055 -24.686 5.845   1.00 34.10 ?  295 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 42.862 -12.194 -18.417 1.00 26.84 ?  296 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 26.047 -21.491 -3.452  1.00 17.13 ?  297 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 40.383 -10.859 -9.430  1.00 17.40 ?  298 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 45.765 -36.320 -16.037 1.00 36.64 ?  299 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 45.394 -33.388 -15.951 1.00 23.66 ?  300 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 51.259 -37.628 -9.665  1.00 27.28 ?  301 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 37.519 -17.911 13.127  1.00 31.72 ?  302 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 52.649 -35.650 -8.759  1.00 30.15 ?  303 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 44.693 -27.491 2.040   1.00 15.52 ?  304 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 45.901 -40.365 -3.477  1.00 29.15 ?  305 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 59.866 -15.353 8.236   1.00 28.72 ?  306 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 62.812 -13.600 4.793   1.00 26.31 ?  307 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 53.436 -30.255 4.598   1.00 18.51 ?  308 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 41.897 -8.083  1.374   1.00 22.55 ?  309 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 37.143 -30.528 -20.973 1.00 30.57 ?  310 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 35.163 -33.584 4.642   1.00 31.51 ?  311 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 43.308 -21.422 10.714  1.00 15.93 ?  312 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 44.084 -29.383 -4.634  1.00 21.86 ?  313 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 53.134 -15.991 -12.716 1.00 24.66 ?  314 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 37.970 -10.229 -10.676 1.00 17.91 ?  315 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 48.197 -32.689 -16.601 1.00 45.93 ?  316 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 52.573 -29.238 -13.038 1.00 26.36 ?  317 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 53.710 -12.545 -22.280 1.00 34.89 ?  318 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 43.639 -15.380 18.188  1.00 25.89 ?  319 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 42.531 -9.766  -14.819 1.00 38.60 ?  320 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 32.870 -34.610 -5.851  1.00 16.54 ?  321 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 38.382 -12.676 7.982   1.00 16.95 ?  322 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 44.726 -24.613 9.620   1.00 20.75 ?  323 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 26.436 -21.057 -6.207  1.00 16.39 ?  324 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 62.976 -20.283 -0.729  1.00 38.69 ?  325 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 57.584 -21.947 3.436   1.00 31.76 ?  326 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 33.672 -31.113 11.099  1.00 35.51 ?  327 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 47.289 -24.465 8.216   1.00 25.20 ?  328 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 36.799 -12.420 4.284   1.00 17.09 ?  329 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 44.138 -1.742  7.720   1.00 48.18 ?  330 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 60.060 -17.269 -10.435 1.00 37.14 ?  331 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 48.697 -12.045 -14.134 1.00 26.62 ?  332 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 41.328 -24.505 15.801  1.00 42.78 ?  333 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 43.197 -34.597 0.087   1.00 21.34 ?  334 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 37.248 -35.661 7.254   1.00 34.30 ?  335 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 27.776 -14.734 -9.452  1.00 37.60 ?  336 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 47.541 -27.449 2.040   1.00 14.78 ?  337 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 42.967 -43.536 -14.415 1.00 45.45 ?  338 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 51.522 -33.041 -10.929 1.00 45.08 ?  339 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 34.459 -10.373 7.737   1.00 21.02 ?  340 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 37.129 -15.094 -16.543 1.00 40.06 ?  341 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 39.659 -23.467 -20.334 1.00 37.58 ?  342 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 38.523 -9.386  -13.257 1.00 29.82 ?  343 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 46.858 -19.955 12.258  1.00 30.79 ?  344 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 38.542 -12.147 -16.222 1.00 46.81 ?  345 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 37.091 -45.196 -9.680  1.00 36.52 ?  346 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 33.088 -14.705 1.099   1.00 19.65 ?  347 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 44.210 -37.409 -17.766 1.00 35.30 ?  348 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 39.905 -44.235 -11.229 1.00 44.40 ?  349 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 38.588 -22.464 15.101  1.00 45.87 ?  350 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 62.594 -20.040 -4.793  1.00 49.15 ?  351 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 40.385 -43.479 -9.122  1.00 26.75 ?  352 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 33.805 -9.558  -8.812  1.00 29.27 ?  353 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 55.764 -8.269  10.772  1.00 26.62 ?  354 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 33.935 -7.966  11.520  1.00 38.73 ?  355 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 23.360 -23.696 6.789   1.00 35.63 ?  356 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 27.871 -26.629 -0.519  1.00 30.83 ?  357 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 56.714 -7.294  3.033   1.00 27.05 ?  358 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 36.246 -8.491  -9.742  1.00 33.13 ?  359 HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 61.609 -19.887 1.788   1.00 39.28 ?  360 HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 56.989 -21.527 -16.411 1.00 40.89 ?  361 HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 27.239 -25.924 -11.306 1.00 33.70 ?  362 HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 40.315 -8.830  9.888   1.00 36.22 ?  363 HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 40.512 -11.332 -13.869 1.00 32.36 ?  364 HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 43.248 -12.693 -21.180 1.00 39.96 ?  365 HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 48.359 -26.440 8.847   1.00 41.76 ?  366 HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 59.077 -10.531 9.191   1.00 43.95 ?  367 HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 36.192 -8.599  8.995   1.00 32.67 ?  368 HOH   B O    1 
HETATM 7194 O  O    . HOH   G 5 .   ? 32.565 -23.610 14.006  1.00 43.44 ?  369 HOH   B O    1 
HETATM 7195 O  O    . HOH   G 5 .   ? 39.912 -7.154  7.847   1.00 41.58 ?  370 HOH   B O    1 
HETATM 7196 O  O    . HOH   G 5 .   ? 56.120 -7.889  -0.576  1.00 36.77 ?  371 HOH   B O    1 
HETATM 7197 O  O    . HOH   G 5 .   ? 52.142 -12.955 13.309  1.00 29.50 ?  372 HOH   B O    1 
HETATM 7198 O  O    . HOH   G 5 .   ? 54.413 -5.826  2.919   1.00 37.48 ?  373 HOH   B O    1 
HETATM 7199 O  O    . HOH   G 5 .   ? 40.225 -7.828  3.105   1.00 42.08 ?  374 HOH   B O    1 
HETATM 7200 O  O    . HOH   G 5 .   ? 63.133 -12.406 6.996   1.00 34.80 ?  375 HOH   B O    1 
HETATM 7201 O  O    . HOH   G 5 .   ? 41.871 -9.957  -17.377 1.00 61.74 ?  376 HOH   B O    1 
HETATM 7202 O  O    . HOH   G 5 .   ? 38.115 -10.521 10.005  1.00 27.34 ?  377 HOH   B O    1 
HETATM 7203 O  O    . HOH   G 5 .   ? 36.552 -22.834 13.298  1.00 33.43 ?  378 HOH   B O    1 
HETATM 7204 O  O    . HOH   G 5 .   ? 41.855 -6.860  -4.852  1.00 46.83 ?  379 HOH   B O    1 
HETATM 7205 O  O    . HOH   G 5 .   ? 42.763 -17.104 -23.142 1.00 43.55 ?  380 HOH   B O    1 
HETATM 7206 O  O    . HOH   G 5 .   ? 44.148 -5.597  -3.390  1.00 41.50 ?  381 HOH   B O    1 
HETATM 7207 O  O    . HOH   G 5 .   ? 39.664 -14.032 15.679  1.00 52.27 ?  382 HOH   B O    1 
HETATM 7208 O  O    . HOH   G 5 .   ? 60.483 -22.247 2.981   1.00 51.35 ?  383 HOH   B O    1 
HETATM 7209 O  O    . HOH   G 5 .   ? 52.929 -29.936 7.258   1.00 22.25 ?  384 HOH   B O    1 
HETATM 7210 O  O    . HOH   G 5 .   ? 46.782 -5.361  2.937   1.00 41.32 ?  385 HOH   B O    1 
HETATM 7211 O  O    . HOH   G 5 .   ? 35.507 -33.771 7.399   1.00 43.97 ?  386 HOH   B O    1 
HETATM 7212 O  O    . HOH   G 5 .   ? 35.200 -20.383 13.306  1.00 35.52 ?  387 HOH   B O    1 
HETATM 7213 O  O    . HOH   G 5 .   ? 23.304 -23.801 1.552   1.00 33.60 ?  388 HOH   B O    1 
HETATM 7214 O  O    . HOH   G 5 .   ? 40.914 -9.754  15.814  1.00 43.75 ?  389 HOH   B O    1 
HETATM 7215 O  O    . HOH   G 5 .   ? 24.016 -20.921 -7.697  1.00 28.15 ?  390 HOH   B O    1 
HETATM 7216 O  O    . HOH   G 5 .   ? 40.787 -6.626  -0.804  1.00 25.71 ?  391 HOH   B O    1 
HETATM 7217 O  O    . HOH   G 5 .   ? 44.244 -31.747 -3.766  1.00 42.19 ?  392 HOH   B O    1 
HETATM 7218 O  O    . HOH   G 5 .   ? 28.078 -27.035 2.310   1.00 30.16 ?  393 HOH   B O    1 
HETATM 7219 O  O    . HOH   G 5 .   ? 26.738 -27.932 -13.428 1.00 37.67 ?  394 HOH   B O    1 
HETATM 7220 O  O    . HOH   G 5 .   ? 50.683 -30.964 8.772   1.00 30.73 ?  395 HOH   B O    1 
HETATM 7221 O  O    . HOH   G 5 .   ? 24.766 -20.649 -10.515 1.00 39.74 ?  396 HOH   B O    1 
HETATM 7222 O  O    . HOH   G 5 .   ? 26.877 -30.577 -12.618 1.00 29.50 ?  397 HOH   B O    1 
HETATM 7223 O  O    . HOH   G 5 .   ? 34.446 -33.492 9.610   1.00 33.82 ?  398 HOH   B O    1 
HETATM 7224 O  O    . HOH   G 5 .   ? 45.758 -20.103 15.242  1.00 47.94 ?  399 HOH   B O    1 
HETATM 7225 O  O    . HOH   G 5 .   ? 57.814 -6.580  -2.376  1.00 31.87 ?  400 HOH   B O    1 
HETATM 7226 O  O    . HOH   G 5 .   ? 40.866 -11.818 -22.316 1.00 40.47 ?  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   ? 0.7114 0.7052 0.8265 0.0121  -0.0130 0.0582  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7152 0.7021 0.8275 0.0117  -0.0127 0.0568  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7079 0.7021 0.8150 0.0109  -0.0125 0.0579  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7117 0.6988 0.8144 0.0105  -0.0123 0.0566  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6906 0.6866 0.7717 0.0048  -0.0136 0.0589  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6937 0.6826 0.7700 0.0041  -0.0133 0.0571  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6945 0.6897 0.7859 0.0061  -0.0151 0.0603  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6979 0.6860 0.7843 0.0053  -0.0148 0.0582  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7185 0.7116 0.8361 0.0146  -0.0101 0.0568  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7226 0.7087 0.8344 0.0144  -0.0100 0.0561  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7221 0.7148 0.8429 0.0158  -0.0092 0.0565  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7263 0.7119 0.8405 0.0157  -0.0091 0.0560  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7219 0.7146 0.8427 0.0159  -0.0090 0.0568  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7260 0.7117 0.8407 0.0159  -0.0090 0.0563  3   VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.6663 0.6653 0.7027 -0.0038 -0.0118 0.0581  4   ASN   A N   
32   N  N   B ASN   A 4   ? 0.6684 0.6600 0.6996 -0.0046 -0.0114 0.0565  4   ASN   A N   
33   C  CA  A ASN   A 4   ? 0.6398 0.6421 0.6264 -0.0136 -0.0089 0.0558  4   ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.6408 0.6355 0.6218 -0.0146 -0.0082 0.0543  4   ASN   A CA  
35   C  C   A ASN   A 4   ? 0.6001 0.6114 0.5806 -0.0302 0.0048  0.0450  4   ASN   A C   
36   C  C   B ASN   A 4   ? 0.5998 0.6033 0.5744 -0.0315 0.0078  0.0434  4   ASN   A C   
37   O  O   A ASN   A 4   ? 0.6030 0.6134 0.5794 -0.0305 0.0040  0.0456  4   ASN   A O   
38   O  O   B ASN   A 4   ? 0.6027 0.6057 0.5731 -0.0317 0.0069  0.0446  4   ASN   A O   
39   C  CB  A ASN   A 4   ? 0.6505 0.6474 0.5931 -0.0081 -0.0179 0.0634  4   ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.6517 0.6410 0.5883 -0.0091 -0.0194 0.0624  4   ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.6591 0.6511 0.5628 -0.0040 -0.0251 0.0702  4   ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.6604 0.6448 0.5578 -0.0050 -0.0284 0.0693  4   ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.6624 0.6523 0.5506 -0.0027 -0.0281 0.0723  4   ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.6638 0.6459 0.5454 -0.0038 -0.0321 0.0716  4   ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.6616 0.6523 0.5534 -0.0024 -0.0274 0.0731  4   ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.6628 0.6461 0.5485 -0.0034 -0.0314 0.0724  4   ASN   A ND2 
59   N  N   A SER   A 5   ? 0.5550 0.5760 0.5342 -0.0472 0.0191  0.0339  5   SER   A N   
60   N  N   B SER   A 5   ? 0.5531 0.5660 0.5268 -0.0491 0.0249  0.0314  5   SER   A N   
61   C  CA  A SER   A 5   ? 0.5080 0.5380 0.4884 -0.0635 0.0344  0.0239  5   SER   A CA  
62   C  CA  B SER   A 5   ? 0.5042 0.5261 0.4798 -0.0665 0.0432  0.0204  5   SER   A CA  
63   C  C   A SER   A 5   ? 0.4561 0.4924 0.4263 -0.0758 0.0521  0.0190  5   SER   A C   
64   C  C   B SER   A 5   ? 0.4498 0.4778 0.4146 -0.0816 0.0646  0.0166  5   SER   A C   
65   O  O   A SER   A 5   ? 0.4592 0.4955 0.4239 -0.0753 0.0536  0.0151  5   SER   A O   
66   O  O   B SER   A 5   ? 0.4535 0.4815 0.4100 -0.0803 0.0656  0.0114  5   SER   A O   
67   C  CB  A SER   A 5   ? 0.5119 0.5434 0.5035 -0.0662 0.0332  0.0207  5   SER   A CB  
68   C  CB  B SER   A 5   ? 0.5086 0.5322 0.4965 -0.0681 0.0416  0.0157  5   SER   A CB  
69   O  OG  A SER   A 5   ? 0.5141 0.5463 0.5125 -0.0674 0.0331  0.0186  5   SER   A OG  
70   O  OG  B SER   A 5   ? 0.5111 0.5354 0.5065 -0.0688 0.0416  0.0127  5   SER   A OG  
81   N  N   A PHE   A 6   ? 0.3997 0.4422 0.3642 -0.0876 0.0692  0.0214  6   PHE   A N   
82   N  N   B PHE   A 6   ? 0.3897 0.4242 0.3511 -0.0979 0.0862  0.0221  6   PHE   A N   
83   C  CA  A PHE   A 6   ? 0.3452 0.3930 0.3086 -0.0961 0.0802  0.0269  6   PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3318 0.3714 0.2949 -0.1103 0.0996  0.0319  6   PHE   A CA  
85   C  C   A PHE   A 6   ? 0.3303 0.3830 0.3065 -0.1012 0.0973  0.0230  6   PHE   A C   
86   C  C   B PHE   A 6   ? 0.3139 0.3601 0.2970 -0.1141 0.1149  0.0283  6   PHE   A C   
87   O  O   A PHE   A 6   ? 0.3309 0.3842 0.3188 -0.1061 0.1016  0.0286  6   PHE   A O   
88   O  O   B PHE   A 6   ? 0.3141 0.3617 0.3174 -0.1150 0.1191  0.0313  6   PHE   A O   
89   C  CB  A PHE   A 6   ? 0.3112 0.3580 0.2631 -0.0911 0.0633  0.0284  6   PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.2983 0.3353 0.2478 -0.1092 0.0841  0.0369  6   PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2808 0.3290 0.2297 -0.0828 0.0467  0.0291  6   PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2704 0.3085 0.2156 -0.1014 0.0668  0.0383  6   PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.2662 0.3157 0.2157 -0.0778 0.0348  0.0290  6   PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2579 0.2963 0.2046 -0.0970 0.0546  0.0371  6   PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2742 0.3187 0.2318 -0.0732 0.0401  0.0262  6   PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2647 0.2999 0.2188 -0.0917 0.0552  0.0331  6   PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.2590 0.3081 0.2146 -0.0740 0.0292  0.0291  6   PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2512 0.2900 0.2031 -0.0928 0.0461  0.0349  6   PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2682 0.3117 0.2377 -0.0683 0.0324  0.0226  6   PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2592 0.2947 0.2268 -0.0857 0.0435  0.0247  6   PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2637 0.3074 0.2290 -0.0680 0.0274  0.0240  6   PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2560 0.2899 0.2197 -0.0860 0.0400  0.0268  6   PHE   A CZ  
121  N  N   A SER   A 7   ? 0.3147 0.3726 0.2971 -0.0967 0.1072  0.0124  7   SER   A N   
122  N  N   B SER   A 7   ? 0.2938 0.3480 0.2818 -0.1126 0.1266  0.0222  7   SER   A N   
123  C  CA  A SER   A 7   ? 0.3043 0.3666 0.3075 -0.0829 0.1051  -0.0083 7   SER   A CA  
124  C  CA  B SER   A 7   ? 0.2820 0.3425 0.2936 -0.0968 0.1154  0.0033  7   SER   A CA  
125  C  C   A SER   A 7   ? 0.2780 0.3419 0.2944 -0.0787 0.1106  -0.0103 7   SER   A C   
126  C  C   B SER   A 7   ? 0.2569 0.3154 0.2784 -0.0926 0.1126  0.0086  7   SER   A C   
127  O  O   A SER   A 7   ? 0.2816 0.3406 0.3002 -0.0796 0.1073  -0.0100 7   SER   A O   
128  O  O   B SER   A 7   ? 0.2547 0.3077 0.2824 -0.1037 0.1104  0.0202  7   SER   A O   
129  C  CB  A SER   A 7   ? 0.3179 0.3804 0.3349 -0.0747 0.0910  -0.0183 7   SER   A CB  
130  C  CB  B SER   A 7   ? 0.2968 0.3599 0.3262 -0.0847 0.0975  -0.0099 7   SER   A CB  
131  O  OG  A SER   A 7   ? 0.3289 0.3898 0.3583 -0.0684 0.0806  -0.0226 7   SER   A OG  
132  O  OG  B SER   A 7   ? 0.3104 0.3716 0.3518 -0.0760 0.0848  -0.0176 7   SER   A OG  
143  N  N   A GLY   A 8   ? 0.2546 0.3203 0.2850 -0.0704 0.1054  -0.0132 8   GLY   A N   
144  N  N   B GLY   A 8   ? 0.2380 0.2968 0.2686 -0.0753 0.0938  0.0000  8   GLY   A N   
145  C  CA  A GLY   A 8   ? 0.2313 0.2988 0.2787 -0.0580 0.0995  -0.0108 8   GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2202 0.2794 0.2636 -0.0540 0.0755  0.0005  8   GLY   A CA  
147  C  C   A GLY   A 8   ? 0.2068 0.2763 0.2684 -0.0471 0.0880  -0.0080 8   GLY   A C   
148  C  C   B GLY   A 8   ? 0.1964 0.2591 0.2490 -0.0370 0.0568  0.0028  8   GLY   A C   
149  O  O   A GLY   A 8   ? 0.2076 0.2816 0.2907 -0.0356 0.0899  -0.0183 8   GLY   A O   
150  O  O   B GLY   A 8   ? 0.1951 0.2649 0.2674 -0.0204 0.0571  -0.0050 8   GLY   A O   
157  N  N   A TYR   A 9   ? 0.1838 0.2476 0.2443 -0.0436 0.0733  0.0041  9   TYR   A N   
158  N  N   B TYR   A 9   ? 0.1780 0.2317 0.2208 -0.0327 0.0462  0.0094  9   TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1657 0.2217 0.2243 -0.0388 0.0583  0.0205  9   TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1585 0.2088 0.2052 -0.0266 0.0367  0.0208  9   TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1639 0.2064 0.2176 -0.0323 0.0555  0.0403  9   TYR   A C   
162  C  C   B TYR   A 9   ? 0.1562 0.1923 0.2018 -0.0142 0.0301  0.0305  9   TYR   A C   
163  O  O   A TYR   A 9   ? 0.1822 0.2162 0.2253 -0.0345 0.0425  0.0374  9   TYR   A O   
164  O  O   B TYR   A 9   ? 0.1765 0.2047 0.2111 -0.0166 0.0219  0.0161  9   TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1584 0.2197 0.2125 -0.0274 0.0454  0.0165  9   TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1558 0.2110 0.1973 -0.0242 0.0296  0.0206  9   TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1516 0.2184 0.2019 -0.0150 0.0395  0.0080  9   TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1536 0.2155 0.1992 -0.0206 0.0307  0.0129  9   TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1555 0.2223 0.2088 -0.0140 0.0421  -0.0018 9   TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1583 0.2211 0.2058 -0.0271 0.0370  0.0067  9   TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1445 0.2100 0.1964 -0.0121 0.0303  0.0087  9   TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1451 0.2072 0.1962 -0.0168 0.0246  0.0159  9   TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1594 0.2244 0.2207 -0.0108 0.0376  -0.0068 9   TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1616 0.2230 0.2184 -0.0255 0.0358  0.0060  9   TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1483 0.2100 0.2075 -0.0138 0.0300  0.0021  9   TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1429 0.2051 0.2030 -0.0169 0.0284  0.0129  9   TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1573 0.2186 0.2291 -0.0190 0.0418  -0.0037 9   TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1454 0.2110 0.2184 -0.0279 0.0399  0.0120  9   TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1730 0.2244 0.2565 -0.0272 0.0402  -0.0091 9   TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1491 0.2127 0.2354 -0.0350 0.0392  0.0117  9   TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1588 0.1907 0.2183 -0.0307 0.0465  0.0547  10  LEU   A N   
200  N  N   B LEU   A 10  ? 0.1513 0.1790 0.2123 -0.0132 0.0177  0.0410  10  LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1535 0.1843 0.2329 -0.0414 0.0306  0.0589  10  LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1453 0.1722 0.2106 -0.0265 0.0017  0.0481  10  LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1458 0.1707 0.2194 -0.0371 0.0270  0.0566  10  LEU   A C   
204  C  C   B LEU   A 10  ? 0.1416 0.1639 0.2098 -0.0280 0.0083  0.0499  10  LEU   A C   
205  O  O   A LEU   A 10  ? 0.1481 0.1627 0.2114 -0.0329 0.0408  0.0516  10  LEU   A O   
206  O  O   B LEU   A 10  ? 0.1433 0.1566 0.2040 -0.0224 0.0114  0.0419  10  LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1598 0.1942 0.2653 -0.0468 0.0178  0.0666  10  LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1492 0.1785 0.2234 -0.0280 -0.0108 0.0513  10  LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1756 0.2049 0.3007 -0.0426 -0.0098 0.0698  10  LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1623 0.1855 0.2335 -0.0290 -0.0292 0.0543  10  LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1878 0.2105 0.3183 -0.0438 -0.0090 0.0692  10  LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1664 0.1916 0.2373 -0.0245 -0.0186 0.0480  10  LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1919 0.2202 0.3164 -0.0369 -0.0054 0.0607  10  LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1729 0.1951 0.2427 -0.0278 -0.0137 0.0453  10  LEU   A CD2 
237  N  N   . LYS   A 11  ? 0.1470 0.1662 0.2163 -0.0334 0.0173  0.0599  11  LYS   A N   
238  C  CA  . LYS   A 11  ? 0.1464 0.1603 0.2157 -0.0325 0.0198  0.0591  11  LYS   A CA  
239  C  C   . LYS   A 11  ? 0.1449 0.1717 0.2256 -0.0394 0.0153  0.0406  11  LYS   A C   
240  O  O   . LYS   A 11  ? 0.1524 0.2088 0.2572 -0.0645 0.0273  0.0250  11  LYS   A O   
241  C  CB  . LYS   A 11  ? 0.1619 0.1650 0.2142 -0.0298 0.0193  0.0508  11  LYS   A CB  
242  C  CG  . LYS   A 11  ? 0.1703 0.1568 0.2055 -0.0361 0.0171  0.0537  11  LYS   A CG  
243  C  CD  . LYS   A 11  ? 0.1897 0.1658 0.2031 -0.0322 0.0083  0.0443  11  LYS   A CD  
244  C  CE  . LYS   A 11  ? 0.1962 0.1619 0.1895 -0.0223 0.0081  0.0454  11  LYS   A CE  
245  N  NZ  . LYS   A 11  ? 0.1895 0.1607 0.1974 -0.0191 0.0074  0.0461  11  LYS   A NZ  
260  N  N   . LEU   A 12  ? 0.1395 0.1580 0.2051 -0.0315 0.0093  0.0368  12  LEU   A N   
261  C  CA  . LEU   A 12  ? 0.1465 0.1707 0.2032 -0.0345 0.0043  0.0416  12  LEU   A CA  
262  C  C   . LEU   A 12  ? 0.1453 0.1608 0.1972 -0.0350 0.0121  0.0426  12  LEU   A C   
263  O  O   . LEU   A 12  ? 0.1496 0.1652 0.2104 -0.0312 0.0082  0.0419  12  LEU   A O   
264  C  CB  . LEU   A 12  ? 0.1500 0.1674 0.2103 -0.0286 0.0024  0.0530  12  LEU   A CB  
265  C  CG  . LEU   A 12  ? 0.1622 0.1774 0.2392 -0.0242 0.0091  0.0529  12  LEU   A CG  
266  C  CD1 . LEU   A 12  ? 0.1784 0.1841 0.2475 -0.0188 0.0163  0.0642  12  LEU   A CD1 
267  C  CD2 . LEU   A 12  ? 0.1614 0.1833 0.2638 -0.0134 0.0037  0.0467  12  LEU   A CD2 
279  N  N   . THR   A 13  ? 0.1367 0.1602 0.2079 -0.0294 0.0068  0.0345  13  THR   A N   
280  C  CA  . THR   A 13  ? 0.1451 0.1530 0.2018 -0.0322 0.0118  0.0335  13  THR   A CA  
281  C  C   . THR   A 13  ? 0.1417 0.1481 0.2092 -0.0347 0.0094  0.0354  13  THR   A C   
282  O  O   . THR   A 13  ? 0.1497 0.1526 0.2097 -0.0226 0.0106  0.0338  13  THR   A O   
283  C  CB  . THR   A 13  ? 0.1545 0.1639 0.2109 -0.0238 0.0164  0.0422  13  THR   A CB  
284  O  OG1 . THR   A 13  ? 0.1551 0.1644 0.2218 -0.0240 0.0136  0.0423  13  THR   A OG1 
285  C  CG2 . THR   A 13  ? 0.1659 0.1852 0.2164 -0.0214 0.0281  0.0195  13  THR   A CG2 
293  N  N   . ASP   A 14  ? 0.1541 0.1497 0.2222 -0.0280 0.0112  0.0485  14  ASP   A N   
294  C  CA  . ASP   A 14  ? 0.1618 0.1621 0.2353 -0.0273 0.0072  0.0635  14  ASP   A CA  
295  C  C   . ASP   A 14  ? 0.1561 0.1667 0.2166 -0.0244 -0.0018 0.0570  14  ASP   A C   
296  O  O   . ASP   A 14  ? 0.1724 0.1765 0.2253 -0.0366 -0.0119 0.0612  14  ASP   A O   
297  C  CB  . ASP   A 14  ? 0.2075 0.1951 0.2913 -0.0336 0.0061  0.1055  14  ASP   A CB  
298  C  CG  . ASP   A 14  ? 0.2488 0.2584 0.3865 -0.0317 -0.0063 0.1056  14  ASP   A CG  
299  O  OD1 . ASP   A 14  ? 0.2669 0.2821 0.4187 -0.0133 -0.0303 0.1047  14  ASP   A OD1 
300  O  OD2 . ASP   A 14  ? 0.2975 0.2975 0.4440 -0.0282 -0.0059 0.0882  14  ASP   A OD2 
305  N  N   . ASN   A 15  ? 0.1379 0.1531 0.2109 -0.0252 0.0061  0.0554  15  ASN   A N   
306  C  CA  . ASN   A 15  ? 0.1419 0.1493 0.2276 -0.0226 0.0025  0.0443  15  ASN   A CA  
307  C  C   . ASN   A 15  ? 0.1408 0.1424 0.2477 -0.0232 -0.0012 0.0452  15  ASN   A C   
308  O  O   . ASN   A 15  ? 0.1471 0.1510 0.2771 -0.0262 -0.0221 0.0512  15  ASN   A O   
309  C  CB  . ASN   A 15  ? 0.1392 0.1474 0.2228 -0.0138 0.0028  0.0424  15  ASN   A CB  
310  C  CG  . ASN   A 15  ? 0.1364 0.1534 0.2325 -0.0143 0.0116  0.0314  15  ASN   A CG  
311  O  OD1 . ASN   A 15  ? 0.1515 0.1593 0.2441 -0.0246 0.0087  0.0290  15  ASN   A OD1 
312  N  ND2 . ASN   A 15  ? 0.1415 0.1690 0.2226 -0.0213 0.0173  0.0272  15  ASN   A ND2 
319  N  N   . VAL   A 16  ? 0.1407 0.1383 0.2373 -0.0161 0.0047  0.0497  16  VAL   A N   
320  C  CA  . VAL   A 16  ? 0.1313 0.1438 0.2259 -0.0199 0.0185  0.0502  16  VAL   A CA  
321  C  C   . VAL   A 16  ? 0.1279 0.1419 0.2206 -0.0198 0.0077  0.0480  16  VAL   A C   
322  O  O   . VAL   A 16  ? 0.1283 0.1481 0.2342 -0.0193 0.0180  0.0413  16  VAL   A O   
323  C  CB  . VAL   A 16  ? 0.1480 0.1539 0.2193 0.0007  0.0242  0.0517  16  VAL   A CB  
324  C  CG1 . VAL   A 16  ? 0.1599 0.1651 0.2200 0.0040  0.0227  0.0441  16  VAL   A CG1 
325  C  CG2 . VAL   A 16  ? 0.1583 0.1662 0.2187 -0.0026 0.0267  0.0524  16  VAL   A CG2 
335  N  N   . TYR   A 17  ? 0.1252 0.1435 0.2150 -0.0173 0.0134  0.0508  17  TYR   A N   
336  C  CA  . TYR   A 17  ? 0.1311 0.1505 0.2016 -0.0229 0.0083  0.0423  17  TYR   A CA  
337  C  C   . TYR   A 17  ? 0.1298 0.1454 0.2193 -0.0203 0.0174  0.0452  17  TYR   A C   
338  O  O   . TYR   A 17  ? 0.1298 0.1513 0.2095 -0.0164 0.0164  0.0486  17  TYR   A O   
339  C  CB  . TYR   A 17  ? 0.1449 0.1514 0.1982 -0.0262 0.0060  0.0381  17  TYR   A CB  
340  C  CG  . TYR   A 17  ? 0.1668 0.1659 0.2003 -0.0321 -0.0011 0.0392  17  TYR   A CG  
341  C  CD1 . TYR   A 17  ? 0.1826 0.1762 0.2160 -0.0171 -0.0083 0.0403  17  TYR   A CD1 
342  C  CD2 . TYR   A 17  ? 0.1825 0.1703 0.2038 -0.0403 -0.0005 0.0420  17  TYR   A CD2 
343  C  CE1 . TYR   A 17  ? 0.2035 0.1756 0.2205 -0.0212 -0.0153 0.0423  17  TYR   A CE1 
344  C  CE2 . TYR   A 17  ? 0.2024 0.1738 0.2048 -0.0480 -0.0049 0.0325  17  TYR   A CE2 
345  C  CZ  . TYR   A 17  ? 0.2169 0.1772 0.2170 -0.0350 -0.0228 0.0455  17  TYR   A CZ  
346  O  OH  . TYR   A 17  ? 0.2357 0.1807 0.2323 -0.0367 -0.0188 0.0518  17  TYR   A OH  
356  N  N   A ILE   A 18  ? 0.1286 0.1451 0.2220 -0.0224 0.0255  0.0471  18  ILE   A N   
357  N  N   B ILE   A 18  ? 0.1356 0.1389 0.2209 -0.0177 0.0193  0.0455  18  ILE   A N   
358  C  CA  A ILE   A 18  ? 0.1287 0.1502 0.2157 -0.0144 0.0280  0.0338  18  ILE   A CA  
359  C  CA  B ILE   A 18  ? 0.1421 0.1357 0.2190 -0.0159 0.0157  0.0334  18  ILE   A CA  
360  C  C   A ILE   A 18  ? 0.1207 0.1615 0.2119 -0.0158 0.0250  0.0319  18  ILE   A C   
361  C  C   B ILE   A 18  ? 0.1407 0.1422 0.2227 -0.0222 0.0234  0.0261  18  ILE   A C   
362  O  O   A ILE   A 18  ? 0.1194 0.1716 0.2131 -0.0272 0.0287  0.0340  18  ILE   A O   
363  O  O   B ILE   A 18  ? 0.1382 0.1495 0.2183 -0.0313 0.0192  0.0238  18  ILE   A O   
364  C  CB  A ILE   A 18  ? 0.1478 0.1516 0.2119 -0.0071 0.0300  0.0405  18  ILE   A CB  
365  C  CB  B ILE   A 18  ? 0.1539 0.1301 0.2043 -0.0087 0.0081  0.0372  18  ILE   A CB  
366  C  CG1 A ILE   A 18  ? 0.1631 0.1636 0.2196 -0.0076 0.0298  0.0425  18  ILE   A CG1 
367  C  CG1 B ILE   A 18  ? 0.1631 0.1342 0.1960 -0.0014 0.0012  0.0317  18  ILE   A CG1 
368  C  CG2 A ILE   A 18  ? 0.1546 0.1530 0.2189 -0.0135 0.0278  0.0331  18  ILE   A CG2 
369  C  CG2 B ILE   A 18  ? 0.1475 0.1235 0.2090 -0.0010 0.0044  0.0334  18  ILE   A CG2 
370  C  CD1 A ILE   A 18  ? 0.1911 0.1795 0.2408 -0.0056 0.0206  0.0445  18  ILE   A CD1 
371  C  CD1 B ILE   A 18  ? 0.1888 0.1412 0.2095 -0.0007 0.0001  0.0358  18  ILE   A CD1 
394  N  N   A LYS   A 19  ? 0.1228 0.1672 0.2174 -0.0111 0.0349  0.0277  19  LYS   A N   
395  N  N   B LYS   A 19  ? 0.1395 0.1453 0.2230 -0.0212 0.0300  0.0285  19  LYS   A N   
396  C  CA  A LYS   A 19  ? 0.1322 0.1816 0.2298 -0.0035 0.0295  0.0200  19  LYS   A CA  
397  C  CA  B LYS   A 19  ? 0.1425 0.1581 0.2172 -0.0166 0.0202  0.0284  19  LYS   A CA  
398  C  C   A LYS   A 19  ? 0.1334 0.1789 0.2353 0.0085  0.0288  0.0156  19  LYS   A C   
399  C  C   B LYS   A 19  ? 0.1329 0.1499 0.2133 -0.0135 0.0220  0.0279  19  LYS   A C   
400  O  O   A LYS   A 19  ? 0.1289 0.1755 0.2333 0.0077  0.0284  0.0277  19  LYS   A O   
401  O  O   B LYS   A 19  ? 0.1254 0.1391 0.1995 -0.0125 0.0186  0.0319  19  LYS   A O   
402  C  CB  A LYS   A 19  ? 0.1359 0.1942 0.2379 -0.0032 0.0320  0.0198  19  LYS   A CB  
403  C  CB  B LYS   A 19  ? 0.1436 0.1756 0.2143 -0.0144 0.0245  0.0281  19  LYS   A CB  
404  C  CG  A LYS   A 19  ? 0.1626 0.2084 0.2399 -0.0033 0.0270  0.0192  19  LYS   A CG  
405  C  CG  B LYS   A 19  ? 0.1503 0.1942 0.2192 -0.0193 0.0053  0.0189  19  LYS   A CG  
406  C  CD  A LYS   A 19  ? 0.1740 0.2174 0.2298 -0.0079 0.0367  0.0250  19  LYS   A CD  
407  C  CD  B LYS   A 19  ? 0.1670 0.2118 0.2123 -0.0218 -0.0046 0.0065  19  LYS   A CD  
408  C  CE  A LYS   A 19  ? 0.1873 0.2246 0.2359 -0.0079 0.0272  0.0237  19  LYS   A CE  
409  C  CE  B LYS   A 19  ? 0.1789 0.2201 0.2093 -0.0280 0.0005  0.0075  19  LYS   A CE  
410  N  NZ  A LYS   A 19  ? 0.1953 0.2296 0.2348 -0.0120 0.0280  0.0254  19  LYS   A NZ  
411  N  NZ  B LYS   A 19  ? 0.1850 0.2282 0.2032 -0.0263 0.0076  -0.0023 19  LYS   A NZ  
438  N  N   A ASN   A 20  ? 0.1459 0.1860 0.2518 0.0135  0.0264  0.0130  20  ASN   A N   
439  N  N   B ASN   A 20  ? 0.1360 0.1568 0.2291 -0.0174 0.0224  0.0324  20  ASN   A N   
440  C  CA  A ASN   A 20  ? 0.1539 0.2023 0.2592 0.0303  0.0310  0.0082  20  ASN   A CA  
441  C  CA  B ASN   A 20  ? 0.1434 0.1735 0.2447 -0.0005 0.0241  0.0260  20  ASN   A CA  
442  C  C   A ASN   A 20  ? 0.1680 0.1965 0.2453 0.0254  0.0361  0.0003  20  ASN   A C   
443  C  C   B ASN   A 20  ? 0.1594 0.1790 0.2291 -0.0117 0.0418  0.0204  20  ASN   A C   
444  O  O   A ASN   A 20  ? 0.1870 0.2056 0.2427 0.0191  0.0353  0.0140  20  ASN   A O   
445  O  O   B ASN   A 20  ? 0.1773 0.1966 0.2354 -0.0145 0.0420  0.0283  20  ASN   A O   
446  C  CB  A ASN   A 20  ? 0.1570 0.2207 0.2849 0.0406  0.0333  0.0199  20  ASN   A CB  
447  C  CB  B ASN   A 20  ? 0.1408 0.1862 0.2737 0.0129  0.0252  0.0402  20  ASN   A CB  
448  C  CG  A ASN   A 20  ? 0.1686 0.2361 0.3239 0.0486  0.0327  0.0304  20  ASN   A CG  
449  C  CG  B ASN   A 20  ? 0.1474 0.1995 0.3166 0.0335  0.0209  0.0524  20  ASN   A CG  
450  O  OD1 A ASN   A 20  ? 0.1924 0.2507 0.3672 0.0546  0.0425  0.0236  20  ASN   A OD1 
451  O  OD1 B ASN   A 20  ? 0.1823 0.2160 0.3653 0.0406  0.0348  0.0372  20  ASN   A OD1 
452  N  ND2 A ASN   A 20  ? 0.1785 0.2375 0.3281 0.0442  0.0261  0.0386  20  ASN   A ND2 
453  N  ND2 B ASN   A 20  ? 0.1563 0.1989 0.3163 0.0356  0.0129  0.0654  20  ASN   A ND2 
466  N  N   A ALA   A 21  ? 0.1651 0.1903 0.2364 0.0235  0.0235  -0.0101 21  ALA   A N   
467  N  N   B ALA   A 21  ? 0.1606 0.1740 0.2235 -0.0212 0.0422  0.0125  21  ALA   A N   
468  C  CA  A ALA   A 21  ? 0.1763 0.1938 0.2356 0.0142  0.0127  -0.0034 21  ALA   A CA  
469  C  CA  B ALA   A 21  ? 0.1680 0.1719 0.2186 -0.0224 0.0423  0.0090  21  ALA   A CA  
470  C  C   A ALA   A 21  ? 0.1737 0.1948 0.2237 0.0168  0.0113  0.0064  21  ALA   A C   
471  C  C   B ALA   A 21  ? 0.1516 0.1620 0.2038 -0.0238 0.0393  0.0007  21  ALA   A C   
472  O  O   A ALA   A 21  ? 0.1759 0.2059 0.2157 0.0106  0.0145  0.0099  21  ALA   A O   
473  O  O   B ALA   A 21  ? 0.1457 0.1681 0.2143 -0.0268 0.0290  -0.0125 21  ALA   A O   
474  C  CB  A ALA   A 21  ? 0.1938 0.2010 0.2481 0.0024  -0.0022 0.0034  21  ALA   A CB  
475  C  CB  B ALA   A 21  ? 0.1909 0.1863 0.2226 -0.0253 0.0406  0.0117  21  ALA   A CB  
486  N  N   A ASP   A 22  ? 0.1740 0.1891 0.2190 0.0218  0.0080  0.0162  22  ASP   A N   
487  N  N   B ASP   A 22  ? 0.1509 0.1562 0.1995 -0.0192 0.0420  -0.0024 22  ASP   A N   
488  C  CA  A ASP   A 22  ? 0.1734 0.1862 0.2018 0.0207  0.0017  0.0238  22  ASP   A CA  
489  C  CA  B ASP   A 22  ? 0.1524 0.1546 0.1912 -0.0161 0.0360  -0.0036 22  ASP   A CA  
490  C  C   A ASP   A 22  ? 0.1612 0.1903 0.1668 0.0136  0.0159  0.0342  22  ASP   A C   
491  C  C   B ASP   A 22  ? 0.1435 0.1553 0.1577 -0.0246 0.0364  -0.0017 22  ASP   A C   
492  O  O   A ASP   A 22  ? 0.1575 0.2007 0.1618 0.0067  0.0304  0.0318  22  ASP   A O   
493  O  O   B ASP   A 22  ? 0.1524 0.1621 0.1605 -0.0279 0.0318  -0.0127 22  ASP   A O   
494  C  CB  A ASP   A 22  ? 0.1895 0.1821 0.2203 0.0276  -0.0075 0.0112  22  ASP   A CB  
495  C  CB  B ASP   A 22  ? 0.1683 0.1588 0.2205 -0.0087 0.0401  -0.0116 22  ASP   A CB  
496  C  CG  A ASP   A 22  ? 0.2088 0.1770 0.2298 0.0240  -0.0148 0.0048  22  ASP   A CG  
497  C  CG  B ASP   A 22  ? 0.1842 0.1583 0.2486 -0.0015 0.0503  -0.0036 22  ASP   A CG  
498  O  OD1 A ASP   A 22  ? 0.2078 0.1742 0.2306 0.0043  -0.0306 0.0243  22  ASP   A OD1 
499  O  OD1 B ASP   A 22  ? 0.1806 0.1546 0.2370 -0.0082 0.0488  0.0118  22  ASP   A OD1 
500  O  OD2 A ASP   A 22  ? 0.2267 0.1807 0.2345 0.0306  -0.0030 -0.0166 22  ASP   A OD2 
501  O  OD2 B ASP   A 22  ? 0.2047 0.1727 0.2875 -0.0063 0.0507  0.0031  22  ASP   A OD2 
510  N  N   A ILE   A 23  ? 0.1622 0.1859 0.1513 0.0107  0.0217  0.0347  23  ILE   A N   
511  N  N   B ILE   A 23  ? 0.1455 0.1462 0.1540 -0.0171 0.0292  0.0084  23  ILE   A N   
512  C  CA  A ILE   A 23  ? 0.1603 0.1761 0.1475 0.0090  0.0207  0.0263  23  ILE   A CA  
513  C  CA  B ILE   A 23  ? 0.1456 0.1511 0.1494 -0.0137 0.0194  0.0207  23  ILE   A CA  
514  C  C   A ILE   A 23  ? 0.1548 0.1836 0.1461 0.0090  0.0242  0.0253  23  ILE   A C   
515  C  C   B ILE   A 23  ? 0.1481 0.1622 0.1453 -0.0166 0.0188  0.0159  23  ILE   A C   
516  O  O   A ILE   A 23  ? 0.1582 0.1972 0.1578 0.0053  0.0243  0.0315  23  ILE   A O   
517  O  O   B ILE   A 23  ? 0.1492 0.1667 0.1508 -0.0125 0.0165  0.0130  23  ILE   A O   
518  C  CB  A ILE   A 23  ? 0.1703 0.1720 0.1425 0.0119  0.0217  0.0220  23  ILE   A CB  
519  C  CB  B ILE   A 23  ? 0.1483 0.1497 0.1475 -0.0034 0.0151  0.0260  23  ILE   A CB  
520  C  CG1 A ILE   A 23  ? 0.1724 0.1687 0.1536 0.0174  0.0232  0.0110  23  ILE   A CG1 
521  C  CG1 B ILE   A 23  ? 0.1508 0.1516 0.1547 -0.0047 0.0119  0.0186  23  ILE   A CG1 
522  C  CG2 A ILE   A 23  ? 0.1731 0.1743 0.1451 0.0136  0.0298  0.0269  23  ILE   A CG2 
523  C  CG2 B ILE   A 23  ? 0.1440 0.1458 0.1456 0.0022  0.0119  0.0340  23  ILE   A CG2 
524  C  CD1 A ILE   A 23  ? 0.1723 0.1672 0.1728 0.0183  0.0169  0.0058  23  ILE   A CD1 
525  C  CD1 B ILE   A 23  ? 0.1458 0.1495 0.1587 -0.0096 0.0071  0.0139  23  ILE   A CD1 
548  N  N   A VAL   A 24  ? 0.1557 0.1820 0.1446 0.0030  0.0156  0.0170  24  VAL   A N   
549  N  N   B VAL   A 24  ? 0.1597 0.1692 0.1512 -0.0239 0.0155  0.0146  24  VAL   A N   
550  C  CA  A VAL   A 24  ? 0.1605 0.1901 0.1548 -0.0046 0.0149  0.0091  24  VAL   A CA  
551  C  CA  B VAL   A 24  ? 0.1737 0.1798 0.1759 -0.0329 0.0171  0.0051  24  VAL   A CA  
552  C  C   A VAL   A 24  ? 0.1648 0.2041 0.1528 -0.0077 0.0161  0.0108  24  VAL   A C   
553  C  C   B VAL   A 24  ? 0.1820 0.1962 0.1664 -0.0356 0.0200  -0.0068 24  VAL   A C   
554  O  O   A VAL   A 24  ? 0.1789 0.2118 0.1581 -0.0057 0.0155  0.0085  24  VAL   A O   
555  O  O   B VAL   A 24  ? 0.1929 0.2060 0.1762 -0.0329 0.0231  -0.0074 24  VAL   A O   
556  C  CB  A VAL   A 24  ? 0.1640 0.1863 0.1745 -0.0080 0.0195  0.0152  24  VAL   A CB  
557  C  CB  B VAL   A 24  ? 0.1828 0.1782 0.2124 -0.0420 0.0140  0.0144  24  VAL   A CB  
558  C  CG1 A VAL   A 24  ? 0.1761 0.1937 0.1863 -0.0014 0.0253  0.0021  24  VAL   A CG1 
559  C  CG1 B VAL   A 24  ? 0.2006 0.1858 0.2421 -0.0371 0.0048  0.0103  24  VAL   A CG1 
560  C  CG2 A VAL   A 24  ? 0.1723 0.1843 0.1715 -0.0109 0.0254  0.0205  24  VAL   A CG2 
561  C  CG2 B VAL   A 24  ? 0.1916 0.1766 0.2184 -0.0478 0.0147  0.0186  24  VAL   A CG2 
580  N  N   A GLU   A 25  ? 0.1643 0.2185 0.1626 -0.0128 0.0258  0.0089  25  GLU   A N   
581  N  N   B GLU   A 25  ? 0.1841 0.2120 0.1639 -0.0343 0.0357  -0.0114 25  GLU   A N   
582  C  CA  A GLU   A 25  ? 0.1790 0.2347 0.1815 -0.0035 0.0331  0.0125  25  GLU   A CA  
583  C  CA  B GLU   A 25  ? 0.1955 0.2334 0.1680 -0.0404 0.0407  -0.0141 25  GLU   A CA  
584  C  C   A GLU   A 25  ? 0.1690 0.2318 0.1581 -0.0050 0.0392  0.0142  25  GLU   A C   
585  C  C   B GLU   A 25  ? 0.1958 0.2436 0.1566 -0.0402 0.0360  -0.0086 25  GLU   A C   
586  O  O   A GLU   A 25  ? 0.1676 0.2357 0.1638 -0.0057 0.0339  0.0131  25  GLU   A O   
587  O  O   B GLU   A 25  ? 0.2041 0.2533 0.1635 -0.0373 0.0296  -0.0166 25  GLU   A O   
588  C  CB  A GLU   A 25  ? 0.2048 0.2575 0.2310 -0.0024 0.0286  0.0156  25  GLU   A CB  
589  C  CB  B GLU   A 25  ? 0.2097 0.2447 0.1993 -0.0471 0.0487  -0.0112 25  GLU   A CB  
590  C  CG  A GLU   A 25  ? 0.2344 0.2782 0.2966 -0.0111 0.0159  0.0106  25  GLU   A CG  
591  C  CG  B GLU   A 25  ? 0.2349 0.2613 0.2579 -0.0513 0.0455  -0.0118 25  GLU   A CG  
592  C  CD  A GLU   A 25  ? 0.2580 0.2944 0.3529 -0.0229 0.0052  0.0069  25  GLU   A CD  
593  C  CD  B GLU   A 25  ? 0.2582 0.2801 0.3215 -0.0536 0.0406  -0.0108 25  GLU   A CD  
594  O  OE1 A GLU   A 25  ? 0.2687 0.3011 0.3716 -0.0246 -0.0047 -0.0008 25  GLU   A OE1 
595  O  OE1 B GLU   A 25  ? 0.2686 0.2876 0.3504 -0.0518 0.0386  -0.0119 25  GLU   A OE1 
596  O  OE2 A GLU   A 25  ? 0.2651 0.3011 0.3808 -0.0303 0.0015  -0.0011 25  GLU   A OE2 
597  O  OE2 B GLU   A 25  ? 0.2663 0.2874 0.3500 -0.0549 0.0405  -0.0102 25  GLU   A OE2 
610  N  N   A GLU   A 26  ? 0.1635 0.2262 0.1564 -0.0175 0.0401  0.0159  26  GLU   A N   
611  N  N   B GLU   A 26  ? 0.1890 0.2409 0.1635 -0.0442 0.0433  -0.0017 26  GLU   A N   
612  C  CA  A GLU   A 26  ? 0.1793 0.2304 0.1558 -0.0311 0.0339  0.0135  26  GLU   A CA  
613  C  CA  B GLU   A 26  ? 0.1929 0.2371 0.1656 -0.0478 0.0450  0.0050  26  GLU   A CA  
614  C  C   A GLU   A 26  ? 0.1745 0.2200 0.1403 -0.0283 0.0270  0.0122  26  GLU   A C   
615  C  C   B GLU   A 26  ? 0.1812 0.2262 0.1467 -0.0387 0.0352  0.0062  26  GLU   A C   
616  O  O   A GLU   A 26  ? 0.1844 0.2161 0.1375 -0.0290 0.0263  0.0107  26  GLU   A O   
617  O  O   B GLU   A 26  ? 0.1887 0.2225 0.1399 -0.0360 0.0377  0.0037  26  GLU   A O   
618  C  CB  A GLU   A 26  ? 0.2027 0.2462 0.2001 -0.0459 0.0285  0.0174  26  GLU   A CB  
619  C  CB  B GLU   A 26  ? 0.2059 0.2409 0.1980 -0.0567 0.0352  -0.0023 26  GLU   A CB  
620  C  CG  A GLU   A 26  ? 0.2219 0.2677 0.2644 -0.0531 0.0371  0.0156  26  GLU   A CG  
621  C  CG  B GLU   A 26  ? 0.2120 0.2483 0.2285 -0.0627 0.0485  -0.0174 26  GLU   A CG  
622  C  CD  A GLU   A 26  ? 0.2365 0.2865 0.3117 -0.0598 0.0571  0.0161  26  GLU   A CD  
623  C  CD  B GLU   A 26  ? 0.2169 0.2554 0.2512 -0.0693 0.0667  -0.0304 26  GLU   A CD  
624  O  OE1 A GLU   A 26  ? 0.2325 0.3077 0.3250 -0.0500 0.0790  0.0051  26  GLU   A OE1 
625  O  OE1 B GLU   A 26  ? 0.2200 0.2690 0.2626 -0.0665 0.0922  -0.0404 26  GLU   A OE1 
626  O  OE2 A GLU   A 26  ? 0.2556 0.2909 0.3244 -0.0641 0.0625  0.0244  26  GLU   A OE2 
627  O  OE2 B GLU   A 26  ? 0.2203 0.2572 0.2242 -0.0687 0.0682  -0.0364 26  GLU   A OE2 
640  N  N   . ALA   A 27  ? 0.1623 0.2173 0.1451 -0.0287 0.0320  0.0133  27  ALA   A N   
641  C  CA  . ALA   A 27  ? 0.1654 0.2209 0.1419 -0.0311 0.0238  0.0105  27  ALA   A CA  
642  C  C   . ALA   A 27  ? 0.1973 0.2469 0.1480 -0.0366 0.0229  -0.0087 27  ALA   A C   
643  O  O   . ALA   A 27  ? 0.2006 0.2431 0.1474 -0.0387 0.0154  -0.0006 27  ALA   A O   
644  C  CB  . ALA   A 27  ? 0.1510 0.2084 0.1508 -0.0280 0.0213  0.0158  27  ALA   A CB  
651  N  N   A LYS   A 28  ? 0.2266 0.2720 0.1734 -0.0309 0.0261  -0.0247 28  LYS   A N   
652  N  N   B LYS   A 28  ? 0.2218 0.2648 0.1596 -0.0296 0.0226  -0.0301 28  LYS   A N   
653  C  CA  A LYS   A 28  ? 0.2621 0.3052 0.2104 -0.0199 0.0253  -0.0313 28  LYS   A CA  
654  C  CA  B LYS   A 28  ? 0.2527 0.2924 0.1843 -0.0167 0.0186  -0.0391 28  LYS   A CA  
655  C  C   A LYS   A 28  ? 0.2828 0.3316 0.2133 -0.0269 0.0292  -0.0258 28  LYS   A C   
656  C  C   B LYS   A 28  ? 0.2725 0.3155 0.1818 -0.0174 0.0221  -0.0313 28  LYS   A C   
657  O  O   A LYS   A 28  ? 0.2939 0.3379 0.2279 -0.0240 0.0157  -0.0333 28  LYS   A O   
658  O  O   B LYS   A 28  ? 0.2847 0.3244 0.1975 -0.0161 0.0081  -0.0370 28  LYS   A O   
659  C  CB  A LYS   A 28  ? 0.2792 0.3154 0.2517 -0.0047 0.0214  -0.0354 28  LYS   A CB  
660  C  CB  B LYS   A 28  ? 0.2663 0.3012 0.2183 -0.0059 0.0130  -0.0470 28  LYS   A CB  
661  C  CG  A LYS   A 28  ? 0.2916 0.3253 0.2865 0.0050  0.0254  -0.0319 28  LYS   A CG  
662  C  CG  B LYS   A 28  ? 0.2777 0.3123 0.2550 0.0008  0.0152  -0.0464 28  LYS   A CG  
663  C  CD  A LYS   A 28  ? 0.3008 0.3358 0.3209 0.0105  0.0281  -0.0279 28  LYS   A CD  
664  C  CD  B LYS   A 28  ? 0.2913 0.3243 0.2973 0.0066  0.0166  -0.0462 28  LYS   A CD  
665  C  CE  A LYS   A 28  ? 0.3091 0.3439 0.3475 0.0131  0.0288  -0.0258 28  LYS   A CE  
666  C  CE  B LYS   A 28  ? 0.3027 0.3326 0.3341 0.0071  0.0172  -0.0456 28  LYS   A CE  
667  N  NZ  A LYS   A 28  ? 0.3149 0.3474 0.3624 0.0150  0.0312  -0.0245 28  LYS   A NZ  
668  N  NZ  B LYS   A 28  ? 0.3095 0.3374 0.3553 0.0084  0.0161  -0.0451 28  LYS   A NZ  
695  N  N   A LYS   A 29  ? 0.2895 0.3518 0.2094 -0.0385 0.0551  -0.0076 29  LYS   A N   
696  N  N   B LYS   A 29  ? 0.2768 0.3308 0.1738 -0.0198 0.0496  -0.0108 29  LYS   A N   
697  C  CA  A LYS   A 29  ? 0.3054 0.3718 0.2341 -0.0463 0.0675  0.0069  29  LYS   A CA  
698  C  CA  B LYS   A 29  ? 0.2899 0.3478 0.1997 -0.0209 0.0627  0.0062  29  LYS   A CA  
699  C  C   A LYS   A 29  ? 0.3011 0.3634 0.2092 -0.0603 0.0556  0.0185  29  LYS   A C   
700  C  C   B LYS   A 29  ? 0.2817 0.3354 0.1729 -0.0241 0.0547  0.0156  29  LYS   A C   
701  O  O   A LYS   A 29  ? 0.3104 0.3724 0.2222 -0.0553 0.0471  0.0122  29  LYS   A O   
702  O  O   B LYS   A 29  ? 0.2854 0.3442 0.1833 -0.0206 0.0490  0.0100  29  LYS   A O   
703  C  CB  A LYS   A 29  ? 0.3246 0.3965 0.2916 -0.0362 0.0831  0.0085  29  LYS   A CB  
704  C  CB  B LYS   A 29  ? 0.3135 0.3755 0.2658 -0.0151 0.0770  0.0076  29  LYS   A CB  
705  C  CG  A LYS   A 29  ? 0.3466 0.4181 0.3551 -0.0253 0.0870  0.0094  29  LYS   A CG  
706  C  CG  B LYS   A 29  ? 0.3399 0.4007 0.3377 -0.0085 0.0818  0.0066  29  LYS   A CG  
707  C  CD  A LYS   A 29  ? 0.3649 0.4356 0.4156 -0.0170 0.0870  0.0089  29  LYS   A CD  
708  C  CD  B LYS   A 29  ? 0.3611 0.4206 0.4022 -0.0039 0.0826  0.0061  29  LYS   A CD  
709  C  CE  A LYS   A 29  ? 0.3782 0.4476 0.4579 -0.0108 0.0870  0.0094  29  LYS   A CE  
710  C  CE  B LYS   A 29  ? 0.3764 0.4346 0.4475 -0.0007 0.0827  0.0059  29  LYS   A CE  
711  N  NZ  A LYS   A 29  ? 0.3847 0.4541 0.4830 -0.0065 0.0858  0.0087  29  LYS   A NZ  
712  N  NZ  B LYS   A 29  ? 0.3844 0.4422 0.4747 0.0018  0.0810  0.0055  29  LYS   A NZ  
739  N  N   A VAL   A 30  ? 0.2871 0.3447 0.1881 -0.0761 0.0508  0.0290  30  VAL   A N   
740  N  N   B VAL   A 30  ? 0.2694 0.3151 0.1640 -0.0299 0.0513  0.0233  30  VAL   A N   
741  C  CA  A VAL   A 30  ? 0.2823 0.3284 0.1703 -0.0861 0.0322  0.0421  30  VAL   A CA  
742  C  CA  B VAL   A 30  ? 0.2609 0.2987 0.1538 -0.0354 0.0313  0.0338  30  VAL   A CA  
743  C  C   A VAL   A 30  ? 0.2802 0.3116 0.1374 -0.0838 0.0245  0.0526  30  VAL   A C   
744  C  C   B VAL   A 30  ? 0.2596 0.2868 0.1371 -0.0266 0.0148  0.0318  30  VAL   A C   
745  O  O   A VAL   A 30  ? 0.2835 0.3129 0.1496 -0.0833 0.0182  0.0536  30  VAL   A O   
746  O  O   B VAL   A 30  ? 0.2648 0.2858 0.1470 -0.0245 0.0046  0.0326  30  VAL   A O   
747  C  CB  A VAL   A 30  ? 0.2825 0.3295 0.1995 -0.0931 0.0171  0.0385  30  VAL   A CB  
748  C  CB  B VAL   A 30  ? 0.2588 0.2936 0.1791 -0.0462 0.0223  0.0375  30  VAL   A CB  
749  C  CG1 A VAL   A 30  ? 0.2884 0.3306 0.2133 -0.0912 0.0097  0.0345  30  VAL   A CG1 
750  C  CG1 B VAL   A 30  ? 0.2638 0.2922 0.1976 -0.0469 0.0148  0.0325  30  VAL   A CG1 
751  C  CG2 A VAL   A 30  ? 0.2808 0.3305 0.2180 -0.0985 0.0171  0.0367  30  VAL   A CG2 
752  C  CG2 B VAL   A 30  ? 0.2578 0.2941 0.1970 -0.0524 0.0237  0.0389  30  VAL   A CG2 
771  N  N   A LYS   A 31  ? 0.2750 0.2932 0.1217 -0.0771 0.0158  0.0495  31  LYS   A N   
772  N  N   B LYS   A 31  ? 0.2567 0.2765 0.1355 -0.0200 0.0003  0.0252  31  LYS   A N   
773  C  CA  A LYS   A 31  ? 0.2819 0.2869 0.1456 -0.0589 -0.0087 0.0440  31  LYS   A CA  
774  C  CA  B LYS   A 31  ? 0.2594 0.2726 0.1568 -0.0112 -0.0182 0.0189  31  LYS   A CA  
775  C  C   A LYS   A 31  ? 0.2615 0.2591 0.1079 -0.0483 -0.0165 0.0675  31  LYS   A C   
776  C  C   B LYS   A 31  ? 0.2371 0.2576 0.1376 -0.0052 -0.0089 0.0312  31  LYS   A C   
777  O  O   A LYS   A 31  ? 0.2635 0.2617 0.1145 -0.0423 -0.0230 0.0736  31  LYS   A O   
778  O  O   B LYS   A 31  ? 0.2471 0.2628 0.1582 -0.0009 -0.0095 0.0254  31  LYS   A O   
779  C  CB  A LYS   A 31  ? 0.3129 0.3107 0.2394 -0.0477 -0.0196 0.0203  31  LYS   A CB  
780  C  CB  B LYS   A 31  ? 0.2895 0.2887 0.2315 -0.0068 -0.0344 -0.0005 31  LYS   A CB  
781  C  CG  A LYS   A 31  ? 0.3443 0.3331 0.3374 -0.0322 -0.0286 0.0041  31  LYS   A CG  
782  C  CG  B LYS   A 31  ? 0.3209 0.3100 0.3239 -0.0024 -0.0475 -0.0147 31  LYS   A CG  
783  C  CD  A LYS   A 31  ? 0.3698 0.3504 0.4159 -0.0202 -0.0377 -0.0071 31  LYS   A CD  
784  C  CD  B LYS   A 31  ? 0.3455 0.3285 0.4016 0.0008  -0.0608 -0.0261 31  LYS   A CD  
785  C  CE  A LYS   A 31  ? 0.3863 0.3607 0.4691 -0.0113 -0.0453 -0.0147 31  LYS   A CE  
786  C  CE  B LYS   A 31  ? 0.3631 0.3427 0.4574 -0.0000 -0.0699 -0.0353 31  LYS   A CE  
787  N  NZ  A LYS   A 31  ? 0.3944 0.3655 0.4952 -0.0052 -0.0496 -0.0182 31  LYS   A NZ  
788  N  NZ  B LYS   A 31  ? 0.3745 0.3511 0.4861 -0.0010 -0.0730 -0.0409 31  LYS   A NZ  
815  N  N   A PRO   A 32  ? 0.2360 0.2345 0.1034 -0.0466 -0.0164 0.0585  32  PRO   A N   
816  N  N   B PRO   A 32  ? 0.2078 0.2417 0.1144 -0.0066 0.0090  0.0325  32  PRO   A N   
817  C  CA  A PRO   A 32  ? 0.2283 0.2215 0.1237 -0.0433 -0.0237 0.0594  32  PRO   A CA  
818  C  CA  B PRO   A 32  ? 0.1993 0.2327 0.1190 -0.0066 0.0068  0.0406  32  PRO   A CA  
819  C  C   A PRO   A 32  ? 0.2208 0.2151 0.1276 -0.0369 -0.0245 0.0564  32  PRO   A C   
820  C  C   B PRO   A 32  ? 0.1971 0.2288 0.1223 -0.0039 0.0020  0.0451  32  PRO   A C   
821  O  O   A PRO   A 32  ? 0.2169 0.2057 0.1264 -0.0471 -0.0230 0.0461  32  PRO   A O   
822  O  O   B PRO   A 32  ? 0.1950 0.2274 0.1392 -0.0039 -0.0075 0.0383  32  PRO   A O   
823  C  CB  A PRO   A 32  ? 0.2257 0.2269 0.1428 -0.0450 -0.0263 0.0446  32  PRO   A CB  
824  C  CB  B PRO   A 32  ? 0.1881 0.2351 0.1348 -0.0077 0.0060  0.0237  32  PRO   A CB  
825  C  CG  A PRO   A 32  ? 0.2263 0.2334 0.1237 -0.0397 -0.0314 0.0405  32  PRO   A CG  
826  C  CG  B PRO   A 32  ? 0.1898 0.2418 0.1214 -0.0044 0.0013  0.0164  32  PRO   A CG  
827  C  CD  A PRO   A 32  ? 0.2276 0.2309 0.1055 -0.0408 -0.0268 0.0517  32  PRO   A CD  
828  C  CD  B PRO   A 32  ? 0.1941 0.2415 0.1094 -0.0046 0.0113  0.0222  32  PRO   A CD  
843  N  N   A THR   A 33  ? 0.2199 0.2153 0.1379 -0.0264 -0.0291 0.0574  33  THR   A N   
844  N  N   B THR   A 33  ? 0.1991 0.2235 0.1297 -0.0035 0.0026  0.0473  33  THR   A N   
845  C  CA  A THR   A 33  ? 0.2153 0.2164 0.1504 -0.0155 -0.0377 0.0506  33  THR   A CA  
846  C  CA  B THR   A 33  ? 0.2001 0.2155 0.1353 0.0038  -0.0101 0.0501  33  THR   A CA  
847  C  C   A THR   A 33  ? 0.1868 0.2049 0.1443 -0.0205 -0.0357 0.0405  33  THR   A C   
848  C  C   B THR   A 33  ? 0.1779 0.1953 0.1282 -0.0062 -0.0081 0.0447  33  THR   A C   
849  O  O   A THR   A 33  ? 0.1770 0.2016 0.1452 -0.0187 -0.0529 0.0388  33  THR   A O   
850  O  O   B THR   A 33  ? 0.1718 0.1835 0.1387 -0.0027 -0.0036 0.0361  33  THR   A O   
851  C  CB  A THR   A 33  ? 0.2392 0.2311 0.1784 -0.0016 -0.0374 0.0586  33  THR   A CB  
852  C  CB  B THR   A 33  ? 0.2244 0.2316 0.1568 0.0173  -0.0144 0.0631  33  THR   A CB  
853  O  OG1 A THR   A 33  ? 0.2558 0.2384 0.2010 0.0089  -0.0310 0.0676  33  THR   A OG1 
854  O  OG1 B THR   A 33  ? 0.2392 0.2464 0.1760 0.0262  -0.0121 0.0724  33  THR   A OG1 
855  C  CG2 A THR   A 33  ? 0.2439 0.2352 0.1842 0.0059  -0.0430 0.0603  33  THR   A CG2 
856  C  CG2 B THR   A 33  ? 0.2312 0.2377 0.1729 0.0206  -0.0153 0.0559  33  THR   A CG2 
871  N  N   . VAL   A 34  ? 0.1698 0.1946 0.1352 -0.0201 -0.0153 0.0432  34  VAL   A N   
872  C  CA  . VAL   A 34  ? 0.1616 0.1762 0.1263 -0.0188 -0.0144 0.0382  34  VAL   A CA  
873  C  C   . VAL   A 34  ? 0.1509 0.1698 0.1207 -0.0181 -0.0065 0.0316  34  VAL   A C   
874  O  O   . VAL   A 34  ? 0.1505 0.1731 0.1423 -0.0306 -0.0137 0.0413  34  VAL   A O   
875  C  CB  . VAL   A 34  ? 0.1676 0.1698 0.1433 -0.0220 -0.0032 0.0351  34  VAL   A CB  
876  C  CG1 . VAL   A 34  ? 0.1838 0.1743 0.1434 -0.0117 -0.0001 0.0171  34  VAL   A CG1 
877  C  CG2 . VAL   A 34  ? 0.1737 0.1856 0.1804 -0.0246 -0.0037 0.0301  34  VAL   A CG2 
888  N  N   . VAL   A 35  ? 0.1374 0.1610 0.1192 -0.0244 -0.0066 0.0311  35  VAL   A N   
889  C  CA  . VAL   A 35  ? 0.1359 0.1564 0.1183 -0.0168 -0.0008 0.0271  35  VAL   A CA  
890  C  C   . VAL   A 35  ? 0.1287 0.1455 0.1070 -0.0139 -0.0000 0.0199  35  VAL   A C   
891  O  O   . VAL   A 35  ? 0.1206 0.1550 0.1218 -0.0182 0.0044  0.0111  35  VAL   A O   
892  C  CB  . VAL   A 35  ? 0.1430 0.1592 0.1253 -0.0109 0.0072  0.0207  35  VAL   A CB  
893  C  CG1 . VAL   A 35  ? 0.1514 0.1651 0.1328 -0.0070 -0.0027 0.0090  35  VAL   A CG1 
894  C  CG2 . VAL   A 35  ? 0.1417 0.1566 0.1558 -0.0082 0.0146  0.0103  35  VAL   A CG2 
904  N  N   . VAL   A 36  ? 0.1196 0.1377 0.1087 -0.0165 0.0076  0.0252  36  VAL   A N   
905  C  CA  . VAL   A 36  ? 0.1154 0.1277 0.1209 -0.0138 0.0010  0.0216  36  VAL   A CA  
906  C  C   . VAL   A 36  ? 0.1105 0.1332 0.1208 -0.0162 0.0041  0.0157  36  VAL   A C   
907  O  O   . VAL   A 36  ? 0.1162 0.1337 0.1342 -0.0118 0.0102  0.0194  36  VAL   A O   
908  C  CB  . VAL   A 36  ? 0.1137 0.1231 0.1307 -0.0133 0.0022  0.0169  36  VAL   A CB  
909  C  CG1 . VAL   A 36  ? 0.1189 0.1331 0.1381 -0.0111 0.0070  0.0071  36  VAL   A CG1 
910  C  CG2 . VAL   A 36  ? 0.1274 0.1271 0.1432 -0.0134 -0.0052 0.0278  36  VAL   A CG2 
920  N  N   . ASN   A 37  ? 0.1090 0.1206 0.1150 -0.0064 -0.0020 0.0141  37  ASN   A N   
921  C  CA  . ASN   A 37  ? 0.1066 0.1176 0.1202 -0.0005 0.0048  0.0175  37  ASN   A CA  
922  C  C   . ASN   A 37  ? 0.1071 0.1164 0.1183 -0.0052 0.0081  0.0210  37  ASN   A C   
923  O  O   . ASN   A 37  ? 0.1212 0.1216 0.1137 0.0033  0.0047  0.0136  37  ASN   A O   
924  C  CB  . ASN   A 37  ? 0.1131 0.1140 0.1269 -0.0037 0.0047  0.0095  37  ASN   A CB  
925  C  CG  . ASN   A 37  ? 0.1147 0.1186 0.1292 0.0050  0.0043  0.0141  37  ASN   A CG  
926  O  OD1 . ASN   A 37  ? 0.1174 0.1189 0.1465 -0.0040 0.0023  0.0169  37  ASN   A OD1 
927  N  ND2 . ASN   A 37  ? 0.1143 0.1205 0.1398 0.0004  0.0004  0.0278  37  ASN   A ND2 
934  N  N   A ALA   A 38  ? 0.1081 0.1197 0.1208 0.0000  0.0086  0.0089  38  ALA   A N   
935  N  N   B ALA   A 38  ? 0.1086 0.1200 0.1260 -0.0053 -0.0000 0.0184  38  ALA   A N   
936  C  CA  A ALA   A 38  ? 0.1147 0.1200 0.1183 0.0038  0.0007  0.0010  38  ALA   A CA  
937  C  CA  B ALA   A 38  ? 0.1164 0.1239 0.1286 -0.0077 -0.0144 0.0209  38  ALA   A CA  
938  C  C   A ALA   A 38  ? 0.1140 0.1168 0.1109 0.0093  -0.0037 -0.0012 38  ALA   A C   
939  C  C   B ALA   A 38  ? 0.1153 0.1223 0.1240 -0.0082 -0.0114 0.0137  38  ALA   A C   
940  O  O   A ALA   A 38  ? 0.1152 0.1117 0.0971 0.0014  -0.0149 -0.0030 38  ALA   A O   
941  O  O   B ALA   A 38  ? 0.1150 0.1173 0.1310 -0.0076 -0.0151 0.0070  38  ALA   A O   
942  C  CB  A ALA   A 38  ? 0.1203 0.1356 0.1318 -0.0104 -0.0008 -0.0006 38  ALA   A CB  
943  C  CB  B ALA   A 38  ? 0.1245 0.1285 0.1375 -0.0143 -0.0240 0.0202  38  ALA   A CB  
954  N  N   A ALA   A 39  ? 0.1148 0.1179 0.1251 0.0107  0.0040  0.0059  39  ALA   A N   
955  N  N   B ALA   A 39  ? 0.1196 0.1306 0.1319 -0.0101 0.0028  0.0279  39  ALA   A N   
956  C  CA  A ALA   A 39  ? 0.1080 0.1053 0.1249 0.0078  0.0108  0.0028  39  ALA   A CA  
957  C  CA  B ALA   A 39  ? 0.1189 0.1304 0.1336 -0.0155 0.0090  0.0230  39  ALA   A CA  
958  C  C   A ALA   A 39  ? 0.1142 0.1152 0.1290 0.0058  0.0036  0.0102  39  ALA   A C   
959  C  C   B ALA   A 39  ? 0.1142 0.1246 0.1311 -0.0116 0.0040  0.0203  39  ALA   A C   
960  O  O   A ALA   A 39  ? 0.1261 0.1184 0.1295 -0.0004 0.0068  0.0135  39  ALA   A O   
961  O  O   B ALA   A 39  ? 0.1339 0.1245 0.1382 -0.0158 -0.0003 0.0132  39  ALA   A O   
962  C  CB  A ALA   A 39  ? 0.1022 0.1072 0.1294 0.0047  -0.0095 0.0011  39  ALA   A CB  
963  C  CB  B ALA   A 39  ? 0.1348 0.1416 0.1461 -0.0129 0.0001  0.0181  39  ALA   A CB  
974  N  N   A ASN   A 40  ? 0.1167 0.1272 0.1288 -0.0005 0.0125  0.0055  40  ASN   A N   
975  N  N   B ASN   A 40  ? 0.1184 0.1228 0.1149 -0.0061 0.0113  0.0184  40  ASN   A N   
976  C  CA  A ASN   A 40  ? 0.1241 0.1201 0.1303 -0.0099 0.0018  0.0065  40  ASN   A CA  
977  C  CA  B ASN   A 40  ? 0.1253 0.1178 0.1179 0.0002  0.0024  0.0199  40  ASN   A CA  
978  C  C   A ASN   A 40  ? 0.1214 0.1104 0.1192 -0.0052 0.0065  0.0072  40  ASN   A C   
979  C  C   B ASN   A 40  ? 0.1215 0.1169 0.1083 -0.0015 0.0121  0.0196  40  ASN   A C   
980  O  O   A ASN   A 40  ? 0.1228 0.1094 0.1237 -0.0038 0.0004  0.0118  40  ASN   A O   
981  O  O   B ASN   A 40  ? 0.1138 0.1220 0.1118 -0.0078 0.0135  0.0205  40  ASN   A O   
982  C  CB  A ASN   A 40  ? 0.1315 0.1309 0.1465 -0.0028 -0.0026 0.0039  40  ASN   A CB  
983  C  CB  B ASN   A 40  ? 0.1316 0.1245 0.1231 -0.0009 -0.0004 0.0157  40  ASN   A CB  
984  C  CG  A ASN   A 40  ? 0.1470 0.1337 0.1564 0.0069  -0.0039 0.0095  40  ASN   A CG  
985  C  CG  B ASN   A 40  ? 0.1364 0.1254 0.1292 -0.0032 -0.0071 0.0153  40  ASN   A CG  
986  O  OD1 A ASN   A 40  ? 0.1588 0.1335 0.1557 0.0095  -0.0077 0.0093  40  ASN   A OD1 
987  O  OD1 B ASN   A 40  ? 0.1435 0.1283 0.1455 -0.0143 0.0076  0.0079  40  ASN   A OD1 
988  N  ND2 A ASN   A 40  ? 0.1510 0.1454 0.1778 0.0134  -0.0011 -0.0040 40  ASN   A ND2 
989  N  ND2 B ASN   A 40  ? 0.1397 0.1357 0.1545 -0.0020 -0.0048 -0.0042 40  ASN   A ND2 
1002 N  N   A VAL   A 41  ? 0.1259 0.1142 0.1182 -0.0026 0.0090  0.0102  41  VAL   A N   
1003 N  N   B VAL   A 41  ? 0.1255 0.1220 0.1158 -0.0032 0.0120  0.0214  41  VAL   A N   
1004 C  CA  A VAL   A 41  ? 0.1272 0.1173 0.1265 -0.0012 0.0136  0.0125  41  VAL   A CA  
1005 C  CA  B VAL   A 41  ? 0.1296 0.1300 0.1249 -0.0053 0.0196  0.0171  41  VAL   A CA  
1006 C  C   A VAL   A 41  ? 0.1242 0.1148 0.1257 -0.0023 0.0103  0.0108  41  VAL   A C   
1007 C  C   B VAL   A 41  ? 0.1280 0.1254 0.1184 -0.0063 0.0241  0.0173  41  VAL   A C   
1008 O  O   A VAL   A 41  ? 0.1343 0.1097 0.1305 0.0039  0.0032  0.0097  41  VAL   A O   
1009 O  O   B VAL   A 41  ? 0.1388 0.1213 0.1053 -0.0016 0.0163  0.0115  41  VAL   A O   
1010 C  CB  A VAL   A 41  ? 0.1374 0.1176 0.1255 -0.0044 0.0202  0.0061  41  VAL   A CB  
1011 C  CB  B VAL   A 41  ? 0.1509 0.1482 0.1410 -0.0094 0.0273  0.0144  41  VAL   A CB  
1012 C  CG1 A VAL   A 41  ? 0.1372 0.1202 0.1388 0.0016  0.0081  -0.0025 41  VAL   A CG1 
1013 C  CG1 B VAL   A 41  ? 0.1656 0.1561 0.1551 -0.0060 0.0268  -0.0002 41  VAL   A CG1 
1014 C  CG2 A VAL   A 41  ? 0.1541 0.1269 0.1246 0.0019  0.0200  0.0024  41  VAL   A CG2 
1015 C  CG2 B VAL   A 41  ? 0.1672 0.1595 0.1453 -0.0138 0.0279  0.0185  41  VAL   A CG2 
1034 N  N   A TYR   A 42  ? 0.1169 0.1163 0.1536 0.0001  0.0146  0.0179  42  TYR   A N   
1035 N  N   B TYR   A 42  ? 0.1173 0.1143 0.1394 -0.0025 0.0273  0.0241  42  TYR   A N   
1036 C  CA  A TYR   A 42  ? 0.1162 0.1145 0.1516 -0.0054 0.0151  0.0195  42  TYR   A CA  
1037 C  CA  B TYR   A 42  ? 0.1175 0.1128 0.1469 -0.0013 0.0337  0.0202  42  TYR   A CA  
1038 C  C   A TYR   A 42  ? 0.1140 0.1123 0.1518 -0.0034 0.0153  0.0151  42  TYR   A C   
1039 C  C   B TYR   A 42  ? 0.1194 0.1180 0.1436 -0.0010 0.0244  0.0223  42  TYR   A C   
1040 O  O   A TYR   A 42  ? 0.1194 0.1139 0.1650 -0.0144 0.0124  0.0052  42  TYR   A O   
1041 O  O   B TYR   A 42  ? 0.1239 0.1239 0.1628 -0.0070 0.0186  0.0168  42  TYR   A O   
1042 C  CB  A TYR   A 42  ? 0.1309 0.1272 0.1516 -0.0037 0.0206  0.0225  42  TYR   A CB  
1043 C  CB  B TYR   A 42  ? 0.1253 0.1139 0.1558 -0.0004 0.0257  0.0261  42  TYR   A CB  
1044 C  CG  A TYR   A 42  ? 0.1363 0.1376 0.1389 -0.0031 0.0190  0.0296  42  TYR   A CG  
1045 C  CG  B TYR   A 42  ? 0.1346 0.1259 0.1531 0.0047  0.0116  0.0319  42  TYR   A CG  
1046 C  CD1 A TYR   A 42  ? 0.1420 0.1557 0.1438 -0.0026 0.0119  0.0266  42  TYR   A CD1 
1047 C  CD1 B TYR   A 42  ? 0.1357 0.1365 0.1512 0.0011  0.0159  0.0342  42  TYR   A CD1 
1048 C  CD2 A TYR   A 42  ? 0.1384 0.1562 0.1377 0.0029  0.0115  0.0301  42  TYR   A CD2 
1049 C  CD2 B TYR   A 42  ? 0.1527 0.1503 0.1704 0.0102  0.0050  0.0206  42  TYR   A CD2 
1050 C  CE1 A TYR   A 42  ? 0.1419 0.1662 0.1394 -0.0038 0.0140  0.0229  42  TYR   A CE1 
1051 C  CE1 B TYR   A 42  ? 0.1469 0.1489 0.1511 0.0016  0.0202  0.0363  42  TYR   A CE1 
1052 C  CE2 A TYR   A 42  ? 0.1398 0.1647 0.1441 -0.0004 0.0063  0.0322  42  TYR   A CE2 
1053 C  CE2 B TYR   A 42  ? 0.1621 0.1664 0.1722 0.0058  0.0074  0.0237  42  TYR   A CE2 
1054 C  CZ  A TYR   A 42  ? 0.1466 0.1719 0.1350 -0.0034 0.0044  0.0288  42  TYR   A CZ  
1055 C  CZ  B TYR   A 42  ? 0.1650 0.1623 0.1670 0.0053  0.0191  0.0234  42  TYR   A CZ  
1056 O  OH  A TYR   A 42  ? 0.1574 0.1874 0.1514 -0.0066 0.0076  0.0109  42  TYR   A OH  
1057 O  OH  B TYR   A 42  ? 0.1724 0.1763 0.1850 0.0007  0.0157  0.0138  42  TYR   A OH  
1076 N  N   A LEU   A 43  ? 0.1156 0.1131 0.1392 -0.0037 0.0159  0.0036  43  LEU   A N   
1077 N  N   B LEU   A 43  ? 0.1193 0.1206 0.1432 -0.0028 0.0173  0.0146  43  LEU   A N   
1078 C  CA  A LEU   A 43  ? 0.1097 0.1116 0.1373 -0.0052 0.0136  0.0034  43  LEU   A CA  
1079 C  CA  B LEU   A 43  ? 0.1169 0.1186 0.1360 -0.0075 0.0110  0.0206  43  LEU   A CA  
1080 C  C   A LEU   A 43  ? 0.1184 0.1164 0.1408 0.0024  0.0137  -0.0021 43  LEU   A C   
1081 C  C   B LEU   A 43  ? 0.1216 0.1266 0.1297 -0.0074 0.0028  0.0161  43  LEU   A C   
1082 O  O   A LEU   A 43  ? 0.1362 0.1158 0.1567 0.0139  0.0021  -0.0115 43  LEU   A O   
1083 O  O   B LEU   A 43  ? 0.1368 0.1330 0.1408 -0.0094 -0.0051 0.0148  43  LEU   A O   
1084 C  CB  A LEU   A 43  ? 0.1163 0.1160 0.1465 -0.0043 0.0058  0.0030  43  LEU   A CB  
1085 C  CB  B LEU   A 43  ? 0.1218 0.1111 0.1541 -0.0085 0.0127  0.0166  43  LEU   A CB  
1086 C  CG  A LEU   A 43  ? 0.1239 0.1203 0.1480 0.0007  -0.0008 0.0028  43  LEU   A CG  
1087 C  CG  B LEU   A 43  ? 0.1266 0.1106 0.1603 -0.0059 0.0114  0.0143  43  LEU   A CG  
1088 C  CD1 A LEU   A 43  ? 0.1264 0.1302 0.1604 0.0012  -0.0156 0.0073  43  LEU   A CD1 
1089 C  CD1 B LEU   A 43  ? 0.1230 0.1156 0.1788 -0.0050 0.0118  0.0187  43  LEU   A CD1 
1090 C  CD2 A LEU   A 43  ? 0.1263 0.1259 0.1447 -0.0040 0.0012  0.0096  43  LEU   A CD2 
1091 C  CD2 B LEU   A 43  ? 0.1371 0.1117 0.1595 -0.0084 0.0073  0.0242  43  LEU   A CD2 
1114 N  N   A LYS   A 44  ? 0.1251 0.1143 0.1419 0.0051  0.0182  0.0053  44  LYS   A N   
1115 N  N   B LYS   A 44  ? 0.1221 0.1241 0.1274 -0.0032 -0.0030 0.0155  44  LYS   A N   
1116 C  CA  A LYS   A 44  ? 0.1314 0.1158 0.1459 0.0013  0.0185  0.0228  44  LYS   A CA  
1117 C  CA  B LYS   A 44  ? 0.1311 0.1290 0.1368 -0.0072 -0.0019 0.0158  44  LYS   A CA  
1118 C  C   A LYS   A 44  ? 0.1247 0.1144 0.1356 0.0061  0.0050  0.0172  44  LYS   A C   
1119 C  C   B LYS   A 44  ? 0.1228 0.1274 0.1343 -0.0097 -0.0008 0.0129  44  LYS   A C   
1120 O  O   A LYS   A 44  ? 0.1272 0.1305 0.1436 0.0035  0.0011  0.0059  44  LYS   A O   
1121 O  O   B LYS   A 44  ? 0.1233 0.1338 0.1381 -0.0118 0.0053  -0.0040 44  LYS   A O   
1122 C  CB  A LYS   A 44  ? 0.1515 0.1270 0.1770 -0.0055 0.0285  0.0473  44  LYS   A CB  
1123 C  CB  B LYS   A 44  ? 0.1511 0.1503 0.1746 0.0025  0.0172  0.0259  44  LYS   A CB  
1124 C  CG  A LYS   A 44  ? 0.1822 0.1512 0.2210 -0.0134 0.0473  0.0594  44  LYS   A CG  
1125 C  CG  B LYS   A 44  ? 0.1689 0.1831 0.2299 0.0099  0.0325  0.0273  44  LYS   A CG  
1126 C  CD  A LYS   A 44  ? 0.2197 0.1982 0.3181 -0.0196 0.0405  0.0378  44  LYS   A CD  
1127 C  CD  B LYS   A 44  ? 0.1943 0.2327 0.3132 0.0056  0.0201  0.0170  44  LYS   A CD  
1128 C  CE  A LYS   A 44  ? 0.2426 0.2272 0.3839 -0.0225 0.0413  0.0233  44  LYS   A CE  
1129 C  CE  B LYS   A 44  ? 0.2069 0.2514 0.3663 -0.0026 0.0146  0.0131  44  LYS   A CE  
1130 N  NZ  A LYS   A 44  ? 0.2548 0.2455 0.4169 -0.0258 0.0428  0.0168  44  LYS   A NZ  
1131 N  NZ  B LYS   A 44  ? 0.2118 0.2438 0.3871 -0.0144 0.0102  0.0102  44  LYS   A NZ  
1158 N  N   A HIS   A 45  ? 0.1190 0.1096 0.1384 0.0027  0.0066  0.0158  45  HIS   A N   
1159 N  N   B HIS   A 45  ? 0.1183 0.1234 0.1377 -0.0149 -0.0057 0.0113  45  HIS   A N   
1160 C  CA  A HIS   A 45  ? 0.1208 0.1160 0.1291 0.0060  0.0010  0.0095  45  HIS   A CA  
1161 C  CA  B HIS   A 45  ? 0.1186 0.1298 0.1359 -0.0101 -0.0098 0.0105  45  HIS   A CA  
1162 C  C   A HIS   A 45  ? 0.1235 0.1231 0.1293 0.0069  0.0033  0.0054  45  HIS   A C   
1163 C  C   B HIS   A 45  ? 0.1244 0.1382 0.1325 -0.0094 -0.0063 0.0119  45  HIS   A C   
1164 O  O   A HIS   A 45  ? 0.1351 0.1213 0.1507 0.0152  0.0032  0.0043  45  HIS   A O   
1165 O  O   B HIS   A 45  ? 0.1393 0.1494 0.1623 0.0056  -0.0017 0.0168  45  HIS   A O   
1166 C  CB  A HIS   A 45  ? 0.1272 0.1126 0.1189 0.0035  0.0023  0.0096  45  HIS   A CB  
1167 C  CB  B HIS   A 45  ? 0.1157 0.1238 0.1396 -0.0096 -0.0116 0.0055  45  HIS   A CB  
1168 C  CG  A HIS   A 45  ? 0.1266 0.1055 0.1112 -0.0032 0.0019  0.0117  45  HIS   A CG  
1169 C  CG  B HIS   A 45  ? 0.1128 0.1224 0.1369 -0.0093 -0.0008 0.0072  45  HIS   A CG  
1170 N  ND1 A HIS   A 45  ? 0.1221 0.1138 0.1235 -0.0033 0.0022  0.0081  45  HIS   A ND1 
1171 N  ND1 B HIS   A 45  ? 0.1058 0.1274 0.1503 -0.0012 -0.0117 0.0140  45  HIS   A ND1 
1172 C  CD2 A HIS   A 45  ? 0.1341 0.1175 0.1154 -0.0063 -0.0033 0.0178  45  HIS   A CD2 
1173 C  CD2 B HIS   A 45  ? 0.1082 0.1166 0.1301 -0.0078 0.0023  0.0051  45  HIS   A CD2 
1174 C  CE1 A HIS   A 45  ? 0.1284 0.1224 0.1181 -0.0072 0.0038  0.0185  45  HIS   A CE1 
1175 C  CE1 B HIS   A 45  ? 0.1085 0.1168 0.1283 -0.0096 -0.0038 0.0054  45  HIS   A CE1 
1176 N  NE2 A HIS   A 45  ? 0.1349 0.1245 0.1164 -0.0004 0.0022  0.0240  45  HIS   A NE2 
1177 N  NE2 B HIS   A 45  ? 0.1076 0.1179 0.1228 -0.0038 0.0047  0.0037  45  HIS   A NE2 
1192 N  N   A GLY   A 46  ? 0.1250 0.1321 0.1452 0.0122  -0.0089 0.0169  46  GLY   A N   
1193 N  N   B GLY   A 46  ? 0.1289 0.1383 0.1393 -0.0105 -0.0155 0.0172  46  GLY   A N   
1194 C  CA  A GLY   A 46  ? 0.1273 0.1319 0.1645 0.0080  -0.0195 0.0243  46  GLY   A CA  
1195 C  CA  B GLY   A 46  ? 0.1341 0.1399 0.1547 -0.0083 -0.0159 0.0196  46  GLY   A CA  
1196 C  C   A GLY   A 46  ? 0.1354 0.1271 0.1683 0.0135  -0.0180 0.0287  46  GLY   A C   
1197 C  C   B GLY   A 46  ? 0.1390 0.1382 0.1446 -0.0026 -0.0057 0.0267  46  GLY   A C   
1198 O  O   A GLY   A 46  ? 0.1378 0.1232 0.1898 0.0179  -0.0315 0.0391  46  GLY   A O   
1199 O  O   B GLY   A 46  ? 0.1464 0.1431 0.1828 -0.0032 -0.0117 0.0190  46  GLY   A O   
1206 N  N   A GLY   A 47  ? 0.1335 0.1295 0.1580 0.0123  -0.0091 0.0279  47  GLY   A N   
1207 N  N   B GLY   A 47  ? 0.1374 0.1387 0.1276 -0.0002 -0.0052 0.0185  47  GLY   A N   
1208 C  CA  A GLY   A 47  ? 0.1325 0.1345 0.1490 0.0134  -0.0170 0.0169  47  GLY   A CA  
1209 C  CA  B GLY   A 47  ? 0.1318 0.1386 0.1333 0.0005  -0.0092 0.0188  47  GLY   A CA  
1210 C  C   A GLY   A 47  ? 0.1270 0.1306 0.1342 0.0141  -0.0170 0.0101  47  GLY   A C   
1211 C  C   B GLY   A 47  ? 0.1211 0.1313 0.1230 0.0070  -0.0062 0.0147  47  GLY   A C   
1212 O  O   A GLY   A 47  ? 0.1323 0.1262 0.1533 0.0198  -0.0169 0.0066  47  GLY   A O   
1213 O  O   B GLY   A 47  ? 0.1196 0.1280 0.1283 0.0087  -0.0141 0.0147  47  GLY   A O   
1220 N  N   A GLY   A 48  ? 0.1237 0.1316 0.1178 0.0197  -0.0097 0.0033  48  GLY   A N   
1221 N  N   B GLY   A 48  ? 0.1216 0.1340 0.1237 0.0108  -0.0030 0.0149  48  GLY   A N   
1222 C  CA  A GLY   A 48  ? 0.1239 0.1300 0.1298 0.0086  -0.0001 -0.0024 48  GLY   A CA  
1223 C  CA  B GLY   A 48  ? 0.1221 0.1266 0.1172 0.0047  0.0029  0.0040  48  GLY   A CA  
1224 C  C   A GLY   A 48  ? 0.1213 0.1225 0.1146 -0.0012 0.0004  0.0030  48  GLY   A C   
1225 C  C   B GLY   A 48  ? 0.1240 0.1241 0.1238 -0.0020 0.0042  0.0040  48  GLY   A C   
1226 O  O   A GLY   A 48  ? 0.1252 0.1231 0.1273 -0.0004 -0.0019 0.0058  48  GLY   A O   
1227 O  O   B GLY   A 48  ? 0.1349 0.1209 0.1285 0.0038  0.0058  -0.0047 48  GLY   A O   
1234 N  N   A VAL   A 49  ? 0.1263 0.1235 0.1274 -0.0064 -0.0036 0.0070  49  VAL   A N   
1235 N  N   B VAL   A 49  ? 0.1148 0.1247 0.1371 -0.0033 0.0021  0.0019  49  VAL   A N   
1236 C  CA  A VAL   A 49  ? 0.1377 0.1209 0.1324 -0.0118 0.0033  0.0091  49  VAL   A CA  
1237 C  CA  B VAL   A 49  ? 0.1094 0.1302 0.1396 -0.0024 0.0029  0.0117  49  VAL   A CA  
1238 C  C   A VAL   A 49  ? 0.1305 0.1087 0.1194 -0.0027 -0.0030 0.0119  49  VAL   A C   
1239 C  C   B VAL   A 49  ? 0.1103 0.1272 0.1292 0.0053  0.0047  -0.0031 49  VAL   A C   
1240 O  O   A VAL   A 49  ? 0.1391 0.1100 0.1171 -0.0079 0.0076  0.0043  49  VAL   A O   
1241 O  O   B VAL   A 49  ? 0.1207 0.1326 0.1277 0.0033  0.0144  -0.0005 49  VAL   A O   
1242 C  CB  A VAL   A 49  ? 0.1564 0.1267 0.1589 -0.0177 -0.0035 -0.0009 49  VAL   A CB  
1243 C  CB  B VAL   A 49  ? 0.1035 0.1284 0.1615 0.0039  -0.0052 0.0212  49  VAL   A CB  
1244 C  CG1 A VAL   A 49  ? 0.1588 0.1258 0.1757 -0.0073 -0.0017 -0.0030 49  VAL   A CG1 
1245 C  CG1 B VAL   A 49  ? 0.1022 0.1154 0.1687 0.0100  -0.0088 0.0313  49  VAL   A CG1 
1246 C  CG2 A VAL   A 49  ? 0.1620 0.1266 0.1936 -0.0298 0.0019  -0.0037 49  VAL   A CG2 
1247 C  CG2 B VAL   A 49  ? 0.1001 0.1353 0.1821 0.0081  -0.0064 0.0188  49  VAL   A CG2 
1266 N  N   A ALA   A 50  ? 0.1237 0.1028 0.1137 -0.0031 -0.0091 0.0219  50  ALA   A N   
1267 N  N   B ALA   A 50  ? 0.1070 0.1285 0.1165 0.0043  0.0045  -0.0031 50  ALA   A N   
1268 C  CA  A ALA   A 50  ? 0.1196 0.1016 0.1202 -0.0118 -0.0151 0.0195  50  ALA   A CA  
1269 C  CA  B ALA   A 50  ? 0.1052 0.1313 0.1140 -0.0017 0.0088  -0.0102 50  ALA   A CA  
1270 C  C   A ALA   A 50  ? 0.1176 0.1044 0.1244 -0.0020 -0.0153 0.0155  50  ALA   A C   
1271 C  C   B ALA   A 50  ? 0.1032 0.1328 0.1173 -0.0028 0.0062  -0.0086 50  ALA   A C   
1272 O  O   A ALA   A 50  ? 0.1274 0.1038 0.1171 0.0039  -0.0191 0.0177  50  ALA   A O   
1273 O  O   B ALA   A 50  ? 0.1086 0.1362 0.1196 -0.0043 0.0124  -0.0099 50  ALA   A O   
1274 C  CB  A ALA   A 50  ? 0.1151 0.1086 0.1352 -0.0211 -0.0116 0.0168  50  ALA   A CB  
1275 C  CB  B ALA   A 50  ? 0.1071 0.1349 0.1216 0.0028  0.0127  -0.0197 50  ALA   A CB  
1286 N  N   A GLY   A 51  ? 0.1185 0.1009 0.1297 0.0028  -0.0116 0.0127  51  GLY   A N   
1287 N  N   B GLY   A 51  ? 0.1144 0.1255 0.1253 -0.0019 -0.0034 -0.0103 51  GLY   A N   
1288 C  CA  A GLY   A 51  ? 0.1249 0.0999 0.1365 0.0047  -0.0122 0.0158  51  GLY   A CA  
1289 C  CA  B GLY   A 51  ? 0.1292 0.1231 0.1292 -0.0048 -0.0084 -0.0074 51  GLY   A CA  
1290 C  C   A GLY   A 51  ? 0.1076 0.1071 0.1333 0.0114  -0.0034 0.0064  51  GLY   A C   
1291 C  C   B GLY   A 51  ? 0.1223 0.1254 0.1261 -0.0040 -0.0041 -0.0119 51  GLY   A C   
1292 O  O   A GLY   A 51  ? 0.1073 0.1212 0.1397 0.0070  -0.0108 0.0050  51  GLY   A O   
1293 O  O   B GLY   A 51  ? 0.1283 0.1330 0.1303 -0.0079 -0.0068 -0.0131 51  GLY   A O   
1300 N  N   A ALA   A 52  ? 0.1029 0.1208 0.1352 0.0055  -0.0006 0.0010  52  ALA   A N   
1301 N  N   B ALA   A 52  ? 0.1165 0.1298 0.1216 -0.0042 -0.0037 -0.0199 52  ALA   A N   
1302 C  CA  A ALA   A 52  ? 0.1106 0.1361 0.1342 -0.0001 0.0040  -0.0002 52  ALA   A CA  
1303 C  CA  B ALA   A 52  ? 0.1206 0.1404 0.1226 -0.0013 -0.0012 -0.0152 52  ALA   A CA  
1304 C  C   A ALA   A 52  ? 0.1181 0.1395 0.1285 -0.0095 0.0057  0.0046  52  ALA   A C   
1305 C  C   B ALA   A 52  ? 0.1222 0.1355 0.1119 -0.0037 0.0041  -0.0159 52  ALA   A C   
1306 O  O   A ALA   A 52  ? 0.1238 0.1467 0.1270 -0.0071 0.0023  0.0039  52  ALA   A O   
1307 O  O   B ALA   A 52  ? 0.1276 0.1425 0.1273 0.0001  0.0057  -0.0168 52  ALA   A O   
1308 C  CB  A ALA   A 52  ? 0.1148 0.1594 0.1338 -0.0060 0.0079  0.0055  52  ALA   A CB  
1309 C  CB  B ALA   A 52  ? 0.1329 0.1595 0.1305 0.0002  -0.0047 -0.0104 52  ALA   A CB  
1320 N  N   A LEU   A 53  ? 0.1204 0.1382 0.1329 -0.0120 0.0033  0.0086  53  LEU   A N   
1321 N  N   B LEU   A 53  ? 0.1186 0.1279 0.1049 -0.0076 -0.0018 -0.0104 53  LEU   A N   
1322 C  CA  A LEU   A 53  ? 0.1277 0.1454 0.1426 -0.0092 0.0065  0.0061  53  LEU   A CA  
1323 C  CA  B LEU   A 53  ? 0.1200 0.1350 0.1007 -0.0045 -0.0086 0.0015  53  LEU   A CA  
1324 C  C   A LEU   A 53  ? 0.1282 0.1472 0.1332 -0.0024 0.0078  -0.0001 53  LEU   A C   
1325 C  C   B LEU   A 53  ? 0.1212 0.1343 0.0801 0.0039  -0.0116 0.0090  53  LEU   A C   
1326 O  O   A LEU   A 53  ? 0.1378 0.1479 0.1445 -0.0096 0.0053  -0.0109 53  LEU   A O   
1327 O  O   B LEU   A 53  ? 0.1311 0.1311 0.0842 0.0016  -0.0092 0.0017  53  LEU   A O   
1328 C  CB  A LEU   A 53  ? 0.1401 0.1447 0.1559 -0.0042 0.0103  0.0092  53  LEU   A CB  
1329 C  CB  B LEU   A 53  ? 0.1216 0.1322 0.1046 -0.0046 -0.0144 0.0129  53  LEU   A CB  
1330 C  CG  A LEU   A 53  ? 0.1554 0.1480 0.1547 -0.0084 0.0129  0.0080  53  LEU   A CG  
1331 C  CG  B LEU   A 53  ? 0.1323 0.1373 0.1072 -0.0077 -0.0171 0.0127  53  LEU   A CG  
1332 C  CD1 A LEU   A 53  ? 0.1655 0.1548 0.1601 -0.0022 0.0032  0.0070  53  LEU   A CD1 
1333 C  CD1 B LEU   A 53  ? 0.1521 0.1399 0.1201 -0.0051 -0.0197 0.0087  53  LEU   A CD1 
1334 C  CD2 A LEU   A 53  ? 0.1710 0.1564 0.1628 -0.0149 0.0190  0.0092  53  LEU   A CD2 
1335 C  CD2 B LEU   A 53  ? 0.1455 0.1480 0.1241 -0.0182 -0.0119 0.0114  53  LEU   A CD2 
1358 N  N   A ASN   A 54  ? 0.1179 0.1354 0.1347 -0.0016 0.0018  0.0021  54  ASN   A N   
1359 N  N   B ASN   A 54  ? 0.1147 0.1317 0.0904 0.0062  -0.0035 0.0028  54  ASN   A N   
1360 C  CA  A ASN   A 54  ? 0.1145 0.1295 0.1370 -0.0015 -0.0097 0.0007  54  ASN   A CA  
1361 C  CA  B ASN   A 54  ? 0.1096 0.1302 0.1094 0.0014  -0.0059 -0.0046 54  ASN   A CA  
1362 C  C   A ASN   A 54  ? 0.1207 0.1337 0.1360 -0.0042 -0.0020 0.0003  54  ASN   A C   
1363 C  C   B ASN   A 54  ? 0.1179 0.1344 0.1261 -0.0055 -0.0011 -0.0056 54  ASN   A C   
1364 O  O   A ASN   A 54  ? 0.1234 0.1441 0.1338 -0.0010 -0.0037 -0.0057 54  ASN   A O   
1365 O  O   B ASN   A 54  ? 0.1183 0.1411 0.1287 -0.0070 -0.0065 -0.0165 54  ASN   A O   
1366 C  CB  A ASN   A 54  ? 0.1124 0.1255 0.1431 -0.0091 -0.0177 0.0033  54  ASN   A CB  
1367 C  CB  B ASN   A 54  ? 0.1087 0.1297 0.1129 0.0021  -0.0023 0.0013  54  ASN   A CB  
1368 C  CG  A ASN   A 54  ? 0.1148 0.1256 0.1527 -0.0043 -0.0155 0.0032  54  ASN   A CG  
1369 C  CG  B ASN   A 54  ? 0.1088 0.1273 0.1131 0.0094  0.0053  -0.0054 54  ASN   A CG  
1370 O  OD1 A ASN   A 54  ? 0.1165 0.1200 0.1727 -0.0036 -0.0133 0.0168  54  ASN   A OD1 
1371 O  OD1 B ASN   A 54  ? 0.1103 0.1294 0.1074 0.0057  -0.0061 -0.0049 54  ASN   A OD1 
1372 N  ND2 A ASN   A 54  ? 0.1184 0.1282 0.1632 -0.0128 -0.0264 0.0109  54  ASN   A ND2 
1373 N  ND2 B ASN   A 54  ? 0.1173 0.1270 0.1384 0.0019  0.0076  0.0051  54  ASN   A ND2 
1386 N  N   . LYS   A 55  ? 0.1191 0.1374 0.1294 -0.0001 -0.0046 -0.0050 55  LYS   A N   
1387 C  CA  . LYS   A 55  ? 0.1305 0.1429 0.1480 0.0068  -0.0061 -0.0169 55  LYS   A CA  
1388 C  C   . LYS   A 55  ? 0.1263 0.1528 0.1441 0.0038  -0.0017 -0.0174 55  LYS   A C   
1389 O  O   . LYS   A 55  ? 0.1436 0.1638 0.1420 0.0092  -0.0071 -0.0309 55  LYS   A O   
1390 C  CB  . LYS   A 55  ? 0.1413 0.1582 0.1641 0.0203  -0.0130 -0.0198 55  LYS   A CB  
1391 C  CG  . LYS   A 55  ? 0.1555 0.1878 0.1829 0.0369  -0.0186 -0.0338 55  LYS   A CG  
1392 C  CD  . LYS   A 55  ? 0.1695 0.2190 0.2067 0.0510  -0.0216 -0.0302 55  LYS   A CD  
1393 C  CE  . LYS   A 55  ? 0.1928 0.2482 0.2383 0.0608  -0.0290 -0.0347 55  LYS   A CE  
1394 N  NZ  . LYS   A 55  ? 0.2103 0.2627 0.2521 0.0639  -0.0314 -0.0279 55  LYS   A NZ  
1409 N  N   . ALA   A 56  ? 0.1259 0.1592 0.1467 -0.0076 0.0007  -0.0144 56  ALA   A N   
1410 C  CA  . ALA   A 56  ? 0.1378 0.1732 0.1353 -0.0066 0.0132  -0.0143 56  ALA   A CA  
1411 C  C   . ALA   A 56  ? 0.1424 0.1884 0.1281 -0.0092 0.0060  -0.0241 56  ALA   A C   
1412 O  O   . ALA   A 56  ? 0.1468 0.2263 0.1384 -0.0006 0.0062  -0.0146 56  ALA   A O   
1413 C  CB  . ALA   A 56  ? 0.1482 0.1934 0.1511 -0.0120 0.0157  -0.0004 56  ALA   A CB  
1419 N  N   . THR   A 57  ? 0.1280 0.1675 0.1218 -0.0042 0.0013  -0.0165 57  THR   A N   
1420 C  CA  . THR   A 57  ? 0.1393 0.1643 0.1320 -0.0025 0.0015  -0.0150 57  THR   A CA  
1421 C  C   . THR   A 57  ? 0.1388 0.1675 0.1326 -0.0005 0.0012  -0.0275 57  THR   A C   
1422 O  O   . THR   A 57  ? 0.1424 0.1712 0.1388 -0.0092 -0.0118 -0.0344 57  THR   A O   
1423 C  CB  . THR   A 57  ? 0.1332 0.1644 0.1292 -0.0065 -0.0015 -0.0069 57  THR   A CB  
1424 O  OG1 . THR   A 57  ? 0.1200 0.1563 0.1217 -0.0074 -0.0025 -0.0119 57  THR   A OG1 
1425 C  CG2 . THR   A 57  ? 0.1365 0.1589 0.1362 -0.0039 -0.0036 -0.0015 57  THR   A CG2 
1433 N  N   . ASN   A 58  ? 0.1405 0.1632 0.1560 -0.0026 0.0029  -0.0311 58  ASN   A N   
1434 C  CA  . ASN   A 58  ? 0.1658 0.1617 0.1784 -0.0073 0.0081  -0.0410 58  ASN   A CA  
1435 C  C   . ASN   A 58  ? 0.1423 0.1468 0.1650 0.0012  -0.0027 -0.0231 58  ASN   A C   
1436 O  O   . ASN   A 58  ? 0.1474 0.1570 0.1765 -0.0124 -0.0042 -0.0263 58  ASN   A O   
1437 C  CB  . ASN   A 58  ? 0.2127 0.1767 0.2158 -0.0187 0.0379  -0.0574 58  ASN   A CB  
1438 C  CG  . ASN   A 58  ? 0.2691 0.2012 0.2969 -0.0185 0.0462  -0.0486 58  ASN   A CG  
1439 O  OD1 . ASN   A 58  ? 0.2955 0.1957 0.3400 0.0202  0.0834  -0.0372 58  ASN   A OD1 
1440 N  ND2 . ASN   A 58  ? 0.2882 0.2180 0.3238 -0.0290 0.0328  -0.0538 58  ASN   A ND2 
1447 N  N   . ASN   A 59  ? 0.1283 0.1392 0.1554 -0.0023 -0.0127 -0.0152 59  ASN   A N   
1448 C  CA  . ASN   A 59  ? 0.1281 0.1316 0.1457 -0.0001 -0.0151 -0.0109 59  ASN   A CA  
1449 C  C   . ASN   A 59  ? 0.1257 0.1286 0.1382 -0.0064 -0.0096 -0.0012 59  ASN   A C   
1450 O  O   . ASN   A 59  ? 0.1211 0.1364 0.1436 -0.0032 -0.0047 0.0010  59  ASN   A O   
1451 C  CB  . ASN   A 59  ? 0.1299 0.1254 0.1642 0.0019  -0.0174 -0.0173 59  ASN   A CB  
1452 C  CG  . ASN   A 59  ? 0.1316 0.1270 0.1641 0.0008  -0.0252 -0.0035 59  ASN   A CG  
1453 O  OD1 . ASN   A 59  ? 0.1438 0.1378 0.1533 -0.0124 -0.0230 0.0011  59  ASN   A OD1 
1454 N  ND2 . ASN   A 59  ? 0.1430 0.1370 0.1733 -0.0134 -0.0198 0.0000  59  ASN   A ND2 
1461 N  N   . ALA   A 60  ? 0.1227 0.1329 0.1417 -0.0004 -0.0117 -0.0080 60  ALA   A N   
1462 C  CA  . ALA   A 60  ? 0.1263 0.1372 0.1439 -0.0002 -0.0182 -0.0093 60  ALA   A CA  
1463 C  C   . ALA   A 60  ? 0.1205 0.1344 0.1500 -0.0013 -0.0038 -0.0017 60  ALA   A C   
1464 O  O   . ALA   A 60  ? 0.1167 0.1349 0.1603 -0.0033 -0.0101 -0.0070 60  ALA   A O   
1465 C  CB  . ALA   A 60  ? 0.1353 0.1461 0.1578 -0.0033 -0.0225 -0.0134 60  ALA   A CB  
1471 N  N   . MET   A 61  ? 0.1161 0.1276 0.1382 -0.0030 -0.0036 -0.0070 61  MET   A N   
1472 C  CA  . MET   A 61  ? 0.1153 0.1237 0.1419 -0.0048 -0.0057 -0.0028 61  MET   A CA  
1473 C  C   . MET   A 61  ? 0.1135 0.1192 0.1409 -0.0075 -0.0047 -0.0069 61  MET   A C   
1474 O  O   . MET   A 61  ? 0.1141 0.1244 0.1495 -0.0052 0.0074  0.0010  61  MET   A O   
1475 C  CB  . MET   A 61  ? 0.1192 0.1276 0.1325 -0.0057 0.0025  0.0021  61  MET   A CB  
1476 C  CG  . MET   A 61  ? 0.1187 0.1288 0.1505 -0.0007 -0.0041 -0.0046 61  MET   A CG  
1477 S  SD  . MET   A 61  ? 0.1262 0.1323 0.1730 -0.0124 -0.0042 -0.0142 61  MET   A SD  
1478 C  CE  . MET   A 61  ? 0.1369 0.1472 0.1958 -0.0089 0.0101  -0.0080 61  MET   A CE  
1488 N  N   . GLN   A 62  ? 0.1121 0.1173 0.1459 -0.0053 -0.0039 -0.0037 62  GLN   A N   
1489 C  CA  . GLN   A 62  ? 0.1210 0.1166 0.1438 -0.0043 0.0045  0.0027  62  GLN   A CA  
1490 C  C   . GLN   A 62  ? 0.1210 0.1117 0.1489 -0.0022 -0.0006 0.0008  62  GLN   A C   
1491 O  O   . GLN   A 62  ? 0.1212 0.1269 0.1470 -0.0012 0.0056  0.0002  62  GLN   A O   
1492 C  CB  . GLN   A 62  ? 0.1219 0.1193 0.1447 0.0000  0.0063  0.0066  62  GLN   A CB  
1493 C  CG  . GLN   A 62  ? 0.1251 0.1157 0.1465 -0.0026 -0.0058 0.0123  62  GLN   A CG  
1494 C  CD  . GLN   A 62  ? 0.1265 0.1170 0.1416 -0.0032 0.0061  0.0061  62  GLN   A CD  
1495 O  OE1 . GLN   A 62  ? 0.1268 0.1335 0.1499 -0.0069 -0.0038 0.0004  62  GLN   A OE1 
1496 N  NE2 . GLN   A 62  ? 0.1312 0.1210 0.1568 0.0002  0.0030  -0.0069 62  GLN   A NE2 
1505 N  N   . VAL   A 63  ? 0.1163 0.1223 0.1679 -0.0064 0.0011  -0.0173 63  VAL   A N   
1506 C  CA  . VAL   A 63  ? 0.1191 0.1294 0.1788 -0.0122 -0.0032 -0.0119 63  VAL   A CA  
1507 C  C   . VAL   A 63  ? 0.1077 0.1282 0.1801 -0.0123 -0.0097 -0.0175 63  VAL   A C   
1508 O  O   . VAL   A 63  ? 0.1138 0.1289 0.1895 -0.0120 -0.0069 -0.0072 63  VAL   A O   
1509 C  CB  . VAL   A 63  ? 0.1297 0.1501 0.2032 -0.0107 -0.0059 -0.0384 63  VAL   A CB  
1510 C  CG1 . VAL   A 63  ? 0.1435 0.1711 0.2358 -0.0137 -0.0120 -0.0618 63  VAL   A CG1 
1511 C  CG2 . VAL   A 63  ? 0.1383 0.1381 0.2203 -0.0143 0.0029  -0.0399 63  VAL   A CG2 
1521 N  N   . GLU   A 64  ? 0.1133 0.1325 0.1616 -0.0051 -0.0071 -0.0139 64  GLU   A N   
1522 C  CA  . GLU   A 64  ? 0.1163 0.1280 0.1596 -0.0051 -0.0105 -0.0040 64  GLU   A CA  
1523 C  C   . GLU   A 64  ? 0.1094 0.1293 0.1594 -0.0055 -0.0015 0.0035  64  GLU   A C   
1524 O  O   . GLU   A 64  ? 0.1169 0.1346 0.1608 -0.0004 0.0028  -0.0024 64  GLU   A O   
1525 C  CB  . GLU   A 64  ? 0.1305 0.1452 0.1635 -0.0057 -0.0046 -0.0048 64  GLU   A CB  
1526 C  CG  . GLU   A 64  ? 0.1296 0.1476 0.1774 -0.0161 -0.0078 -0.0102 64  GLU   A CG  
1527 C  CD  . GLU   A 64  ? 0.1418 0.1542 0.1878 -0.0163 -0.0007 -0.0106 64  GLU   A CD  
1528 O  OE1 . GLU   A 64  ? 0.1450 0.1653 0.2020 -0.0243 0.0012  -0.0073 64  GLU   A OE1 
1529 O  OE2 . GLU   A 64  ? 0.1604 0.1492 0.1887 -0.0163 -0.0007 0.0065  64  GLU   A OE2 
1536 N  N   . SER   A 65  ? 0.1067 0.1274 0.1511 0.0030  0.0027  0.0020  65  SER   A N   
1537 C  CA  . SER   A 65  ? 0.1141 0.1211 0.1538 0.0021  -0.0019 -0.0054 65  SER   A CA  
1538 C  C   . SER   A 65  ? 0.1195 0.1299 0.1453 -0.0028 -0.0059 -0.0021 65  SER   A C   
1539 O  O   . SER   A 65  ? 0.1228 0.1373 0.1644 -0.0023 0.0097  -0.0038 65  SER   A O   
1540 C  CB  . SER   A 65  ? 0.1145 0.1223 0.1471 -0.0055 0.0047  0.0072  65  SER   A CB  
1541 O  OG  . SER   A 65  ? 0.1198 0.1320 0.1559 -0.0061 -0.0092 0.0073  65  SER   A OG  
1547 N  N   . ASP   A 66  ? 0.1185 0.1256 0.1457 -0.0059 0.0087  0.0033  66  ASP   A N   
1548 C  CA  . ASP   A 66  ? 0.1299 0.1363 0.1620 -0.0033 0.0047  0.0120  66  ASP   A CA  
1549 C  C   . ASP   A 66  ? 0.1254 0.1319 0.1695 -0.0082 0.0037  0.0153  66  ASP   A C   
1550 O  O   . ASP   A 66  ? 0.1281 0.1440 0.1917 -0.0042 0.0202  0.0235  66  ASP   A O   
1551 C  CB  . ASP   A 66  ? 0.1394 0.1426 0.1820 0.0044  0.0087  0.0204  66  ASP   A CB  
1552 C  CG  . ASP   A 66  ? 0.1656 0.1553 0.2044 0.0029  -0.0026 0.0405  66  ASP   A CG  
1553 O  OD1 . ASP   A 66  ? 0.1680 0.1871 0.1851 -0.0079 -0.0041 0.0388  66  ASP   A OD1 
1554 O  OD2 . ASP   A 66  ? 0.1797 0.1661 0.2815 0.0180  -0.0144 0.0278  66  ASP   A OD2 
1559 N  N   . ASP   A 67  ? 0.1152 0.1341 0.1823 -0.0042 0.0020  0.0153  67  ASP   A N   
1560 C  CA  . ASP   A 67  ? 0.1182 0.1505 0.2055 -0.0031 -0.0002 0.0266  67  ASP   A CA  
1561 C  C   . ASP   A 67  ? 0.1195 0.1542 0.1917 0.0052  0.0117  0.0298  67  ASP   A C   
1562 O  O   . ASP   A 67  ? 0.1187 0.1668 0.2132 0.0019  0.0241  0.0332  67  ASP   A O   
1563 C  CB  . ASP   A 67  ? 0.1276 0.1629 0.2282 -0.0057 -0.0157 0.0343  67  ASP   A CB  
1564 C  CG  . ASP   A 67  ? 0.1294 0.1792 0.2524 -0.0121 -0.0327 0.0425  67  ASP   A CG  
1565 O  OD1 . ASP   A 67  ? 0.1372 0.2013 0.3291 -0.0164 -0.0385 0.0610  67  ASP   A OD1 
1566 O  OD2 . ASP   A 67  ? 0.1302 0.1814 0.2400 -0.0032 -0.0201 0.0372  67  ASP   A OD2 
1571 N  N   . TYR   A 68  ? 0.1255 0.1406 0.1853 0.0060  0.0213  0.0257  68  TYR   A N   
1572 C  CA  . TYR   A 68  ? 0.1342 0.1358 0.1924 0.0061  0.0252  0.0298  68  TYR   A CA  
1573 C  C   . TYR   A 68  ? 0.1278 0.1343 0.1941 0.0021  0.0340  0.0261  68  TYR   A C   
1574 O  O   . TYR   A 68  ? 0.1322 0.1447 0.1997 0.0122  0.0360  0.0268  68  TYR   A O   
1575 C  CB  . TYR   A 68  ? 0.1447 0.1314 0.2001 0.0117  0.0435  0.0331  68  TYR   A CB  
1576 C  CG  . TYR   A 68  ? 0.1491 0.1509 0.2252 0.0075  0.0619  0.0258  68  TYR   A CG  
1577 C  CD1 . TYR   A 68  ? 0.1575 0.1620 0.2625 -0.0175 0.0492  -0.0136 68  TYR   A CD1 
1578 C  CD2 . TYR   A 68  ? 0.1709 0.1578 0.2681 0.0189  0.0640  0.0462  68  TYR   A CD2 
1579 C  CE1 . TYR   A 68  ? 0.1679 0.1718 0.2953 -0.0140 0.0495  -0.0107 68  TYR   A CE1 
1580 C  CE2 . TYR   A 68  ? 0.1669 0.1648 0.2888 0.0083  0.0724  0.0237  68  TYR   A CE2 
1581 C  CZ  . TYR   A 68  ? 0.1659 0.1667 0.3092 -0.0128 0.0614  -0.0097 68  TYR   A CZ  
1582 O  OH  . TYR   A 68  ? 0.1924 0.1669 0.3390 -0.0134 0.0405  -0.0376 68  TYR   A OH  
1592 N  N   . ILE   A 69  ? 0.1215 0.1282 0.1867 0.0015  0.0216  0.0150  69  ILE   A N   
1593 C  CA  . ILE   A 69  ? 0.1301 0.1340 0.1765 0.0065  0.0197  -0.0025 69  ILE   A CA  
1594 C  C   . ILE   A 69  ? 0.1269 0.1364 0.1625 0.0027  0.0166  0.0172  69  ILE   A C   
1595 O  O   . ILE   A 69  ? 0.1313 0.1474 0.1638 -0.0011 0.0237  0.0155  69  ILE   A O   
1596 C  CB  . ILE   A 69  ? 0.1392 0.1594 0.1768 0.0062  0.0217  -0.0117 69  ILE   A CB  
1597 C  CG1 . ILE   A 69  ? 0.1381 0.1621 0.1801 0.0031  0.0185  -0.0218 69  ILE   A CG1 
1598 C  CG2 . ILE   A 69  ? 0.1576 0.1829 0.1988 0.0105  0.0078  -0.0205 69  ILE   A CG2 
1599 C  CD1 . ILE   A 69  ? 0.1425 0.1755 0.2094 -0.0031 0.0225  -0.0262 69  ILE   A CD1 
1611 N  N   . ALA   A 70  ? 0.1338 0.1360 0.1756 -0.0077 0.0207  0.0190  70  ALA   A N   
1612 C  CA  . ALA   A 70  ? 0.1416 0.1503 0.1926 -0.0126 0.0253  0.0176  70  ALA   A CA  
1613 C  C   . ALA   A 70  ? 0.1373 0.1697 0.1906 -0.0110 0.0225  0.0236  70  ALA   A C   
1614 O  O   . ALA   A 70  ? 0.1520 0.2068 0.2206 0.0083  0.0401  0.0412  70  ALA   A O   
1615 C  CB  . ALA   A 70  ? 0.1438 0.1443 0.2180 -0.0199 0.0195  0.0105  70  ALA   A CB  
1621 N  N   . THR   A 71  ? 0.1307 0.1662 0.1871 -0.0051 0.0172  0.0232  71  THR   A N   
1622 C  CA  . THR   A 71  ? 0.1463 0.1815 0.2224 0.0085  0.0179  0.0344  71  THR   A CA  
1623 C  C   . THR   A 71  ? 0.1336 0.1742 0.2440 0.0202  0.0340  0.0235  71  THR   A C   
1624 O  O   . THR   A 71  ? 0.1420 0.1976 0.2978 0.0169  0.0483  0.0042  71  THR   A O   
1625 C  CB  . THR   A 71  ? 0.1774 0.2103 0.2537 0.0174  -0.0163 0.0363  71  THR   A CB  
1626 O  OG1 . THR   A 71  ? 0.2097 0.2289 0.2627 0.0072  -0.0399 0.0317  71  THR   A OG1 
1627 C  CG2 . THR   A 71  ? 0.1831 0.2265 0.2792 0.0263  -0.0170 0.0455  71  THR   A CG2 
1635 N  N   . ASN   A 72  ? 0.1348 0.1619 0.2171 0.0204  0.0290  0.0311  72  ASN   A N   
1636 C  CA  . ASN   A 72  ? 0.1435 0.1518 0.2186 0.0203  0.0369  0.0217  72  ASN   A CA  
1637 C  C   . ASN   A 72  ? 0.1565 0.1491 0.2120 0.0129  0.0516  0.0123  72  ASN   A C   
1638 O  O   . ASN   A 72  ? 0.1720 0.1524 0.2359 0.0131  0.0524  -0.0014 72  ASN   A O   
1639 C  CB  . ASN   A 72  ? 0.1651 0.1588 0.2189 0.0164  0.0418  0.0242  72  ASN   A CB  
1640 C  CG  . ASN   A 72  ? 0.1851 0.1730 0.2307 0.0283  0.0314  0.0311  72  ASN   A CG  
1641 O  OD1 . ASN   A 72  ? 0.2052 0.2014 0.2469 0.0283  0.0392  0.0344  72  ASN   A OD1 
1642 N  ND2 . ASN   A 72  ? 0.1970 0.1769 0.2457 0.0515  0.0163  0.0213  72  ASN   A ND2 
1649 N  N   . GLY   A 73  ? 0.1571 0.1434 0.1917 0.0013  0.0529  0.0082  73  GLY   A N   
1650 C  CA  . GLY   A 73  ? 0.1686 0.1466 0.1807 -0.0048 0.0430  0.0081  73  GLY   A CA  
1651 C  C   . GLY   A 73  ? 0.1566 0.1351 0.1695 0.0002  0.0528  0.0205  73  GLY   A C   
1652 O  O   . GLY   A 73  ? 0.1547 0.1469 0.1826 0.0094  0.0399  0.0221  73  GLY   A O   
1656 N  N   . PRO   A 74  ? 0.1639 0.1373 0.1773 -0.0113 0.0512  0.0093  74  PRO   A N   
1657 C  CA  . PRO   A 74  ? 0.1634 0.1363 0.1916 -0.0009 0.0437  0.0088  74  PRO   A CA  
1658 C  C   . PRO   A 74  ? 0.1543 0.1287 0.1793 0.0012  0.0305  0.0099  74  PRO   A C   
1659 O  O   . PRO   A 74  ? 0.1631 0.1360 0.1988 0.0070  0.0372  0.0013  74  PRO   A O   
1660 C  CB  . PRO   A 74  ? 0.1771 0.1625 0.2157 0.0027  0.0522  0.0263  74  PRO   A CB  
1661 C  CG  . PRO   A 74  ? 0.2027 0.1965 0.2463 -0.0129 0.0418  0.0187  74  PRO   A CG  
1662 C  CD  . PRO   A 74  ? 0.1851 0.1749 0.1982 -0.0222 0.0392  0.0032  74  PRO   A CD  
1670 N  N   . LEU   A 75  ? 0.1514 0.1198 0.1614 -0.0000 0.0239  0.0064  75  LEU   A N   
1671 C  CA  . LEU   A 75  ? 0.1532 0.1194 0.1475 -0.0019 0.0103  0.0099  75  LEU   A CA  
1672 C  C   . LEU   A 75  ? 0.1666 0.1255 0.1420 0.0054  0.0070  0.0146  75  LEU   A C   
1673 O  O   . LEU   A 75  ? 0.2041 0.1384 0.1463 0.0088  0.0064  0.0142  75  LEU   A O   
1674 C  CB  . LEU   A 75  ? 0.1550 0.1265 0.1463 -0.0037 0.0020  0.0196  75  LEU   A CB  
1675 C  CG  . LEU   A 75  ? 0.1761 0.1579 0.1594 -0.0320 0.0043  0.0124  75  LEU   A CG  
1676 C  CD1 . LEU   A 75  ? 0.1908 0.2061 0.1645 -0.0297 0.0070  0.0045  75  LEU   A CD1 
1677 C  CD2 . LEU   A 75  ? 0.2051 0.2044 0.2104 -0.0077 0.0022  0.0167  75  LEU   A CD2 
1689 N  N   . LYS   A 76  ? 0.1544 0.1231 0.1548 0.0022  0.0020  0.0114  76  LYS   A N   
1690 C  CA  . LYS   A 76  ? 0.1531 0.1458 0.1599 -0.0043 -0.0026 -0.0011 76  LYS   A CA  
1691 C  C   . LYS   A 76  ? 0.1530 0.1358 0.1267 0.0005  0.0048  0.0082  76  LYS   A C   
1692 O  O   . LYS   A 76  ? 0.1626 0.1272 0.1252 -0.0020 0.0114  0.0127  76  LYS   A O   
1693 C  CB  . LYS   A 76  ? 0.1581 0.1522 0.1882 0.0033  0.0045  -0.0188 76  LYS   A CB  
1694 C  CG  . LYS   A 76  ? 0.1676 0.1483 0.2345 0.0070  0.0016  -0.0167 76  LYS   A CG  
1695 C  CD  . LYS   A 76  ? 0.1728 0.1491 0.2798 0.0140  -0.0140 -0.0156 76  LYS   A CD  
1696 C  CE  . LYS   A 76  ? 0.1832 0.1675 0.3382 0.0076  -0.0112 -0.0250 76  LYS   A CE  
1697 N  NZ  . LYS   A 76  ? 0.1831 0.1645 0.3855 0.0005  -0.0143 -0.0347 76  LYS   A NZ  
1711 N  N   . VAL   A 77  ? 0.1656 0.1351 0.1342 -0.0021 0.0081  0.0148  77  VAL   A N   
1712 C  CA  . VAL   A 77  ? 0.1579 0.1396 0.1383 0.0021  0.0002  0.0111  77  VAL   A CA  
1713 C  C   . VAL   A 77  ? 0.1523 0.1323 0.1402 0.0029  0.0095  0.0055  77  VAL   A C   
1714 O  O   . VAL   A 77  ? 0.1683 0.1351 0.1450 0.0104  0.0257  0.0030  77  VAL   A O   
1715 C  CB  . VAL   A 77  ? 0.1696 0.1533 0.1511 0.0034  -0.0062 0.0132  77  VAL   A CB  
1716 C  CG1 . VAL   A 77  ? 0.1684 0.1627 0.1777 0.0055  -0.0049 0.0095  77  VAL   A CG1 
1717 C  CG2 . VAL   A 77  ? 0.1804 0.1616 0.1726 0.0030  -0.0138 0.0195  77  VAL   A CG2 
1727 N  N   . GLY   A 78  ? 0.1449 0.1296 0.1293 0.0020  0.0119  0.0091  78  GLY   A N   
1728 C  CA  . GLY   A 78  ? 0.1480 0.1262 0.1450 -0.0037 0.0249  0.0107  78  GLY   A CA  
1729 C  C   . GLY   A 78  ? 0.1375 0.1212 0.1546 0.0033  0.0165  0.0060  78  GLY   A C   
1730 O  O   . GLY   A 78  ? 0.1379 0.1282 0.1728 0.0028  0.0136  0.0249  78  GLY   A O   
1734 N  N   . GLY   A 79  ? 0.1443 0.1245 0.1438 0.0046  0.0070  0.0068  79  GLY   A N   
1735 C  CA  . GLY   A 79  ? 0.1408 0.1257 0.1513 -0.0048 0.0136  0.0093  79  GLY   A CA  
1736 C  C   . GLY   A 79  ? 0.1282 0.1178 0.1523 -0.0036 0.0143  0.0065  79  GLY   A C   
1737 O  O   . GLY   A 79  ? 0.1314 0.1324 0.1534 0.0118  0.0090  0.0070  79  GLY   A O   
1741 N  N   . SER   A 80  ? 0.1228 0.1364 0.1692 -0.0010 0.0094  -0.0005 80  SER   A N   
1742 C  CA  . SER   A 80  ? 0.1194 0.1304 0.1596 0.0035  0.0071  0.0025  80  SER   A CA  
1743 C  C   . SER   A 80  ? 0.1186 0.1266 0.1553 -0.0015 0.0134  0.0149  80  SER   A C   
1744 O  O   . SER   A 80  ? 0.1226 0.1496 0.1798 0.0067  0.0061  -0.0021 80  SER   A O   
1745 C  CB  . SER   A 80  ? 0.1369 0.1223 0.1607 -0.0106 0.0037  0.0104  80  SER   A CB  
1746 O  OG  . SER   A 80  ? 0.1571 0.1287 0.2043 0.0024  -0.0051 0.0221  80  SER   A OG  
1752 N  N   . CYS   A 81  ? 0.1169 0.1263 0.1520 -0.0013 0.0015  0.0159  81  CYS   A N   
1753 C  CA  . CYS   A 81  ? 0.1127 0.1320 0.1554 -0.0053 -0.0085 0.0210  81  CYS   A CA  
1754 C  C   . CYS   A 81  ? 0.1103 0.1310 0.1454 -0.0108 -0.0014 0.0206  81  CYS   A C   
1755 O  O   . CYS   A 81  ? 0.1148 0.1625 0.1577 0.0024  -0.0002 0.0268  81  CYS   A O   
1756 C  CB  . CYS   A 81  ? 0.1218 0.1415 0.1645 -0.0126 -0.0063 0.0281  81  CYS   A CB  
1757 S  SG  . CYS   A 81  ? 0.1362 0.1303 0.1616 -0.0155 -0.0015 0.0146  81  CYS   A SG  
1763 N  N   . VAL   A 82  ? 0.1169 0.1369 0.1486 -0.0004 -0.0122 0.0207  82  VAL   A N   
1764 C  CA  . VAL   A 82  ? 0.1295 0.1411 0.1486 0.0026  -0.0116 0.0259  82  VAL   A CA  
1765 C  C   . VAL   A 82  ? 0.1262 0.1450 0.1568 -0.0024 -0.0122 0.0189  82  VAL   A C   
1766 O  O   . VAL   A 82  ? 0.1183 0.1562 0.1810 -0.0030 -0.0032 0.0033  82  VAL   A O   
1767 C  CB  . VAL   A 82  ? 0.1547 0.1592 0.1666 0.0060  -0.0052 0.0314  82  VAL   A CB  
1768 C  CG1 . VAL   A 82  ? 0.1793 0.1751 0.1797 0.0044  0.0054  0.0232  82  VAL   A CG1 
1769 C  CG2 . VAL   A 82  ? 0.1633 0.1541 0.1967 -0.0061 -0.0064 0.0371  82  VAL   A CG2 
1779 N  N   . LEU   A 83  ? 0.1206 0.1420 0.1509 -0.0058 -0.0152 0.0126  83  LEU   A N   
1780 C  CA  . LEU   A 83  ? 0.1201 0.1480 0.1435 -0.0102 -0.0172 0.0064  83  LEU   A CA  
1781 C  C   . LEU   A 83  ? 0.1297 0.1440 0.1356 -0.0070 -0.0162 0.0155  83  LEU   A C   
1782 O  O   . LEU   A 83  ? 0.1399 0.1492 0.1467 -0.0170 -0.0096 0.0242  83  LEU   A O   
1783 C  CB  . LEU   A 83  ? 0.1244 0.1440 0.1526 -0.0087 -0.0199 0.0176  83  LEU   A CB  
1784 C  CG  . LEU   A 83  ? 0.1420 0.1549 0.1662 -0.0109 0.0009  0.0079  83  LEU   A CG  
1785 C  CD1 . LEU   A 83  ? 0.1604 0.1574 0.1656 -0.0188 -0.0051 0.0238  83  LEU   A CD1 
1786 C  CD2 . LEU   A 83  ? 0.1451 0.1715 0.1729 -0.0133 0.0134  0.0218  83  LEU   A CD2 
1798 N  N   . SER   A 84  ? 0.1438 0.1535 0.1426 -0.0160 -0.0109 0.0196  84  SER   A N   
1799 C  CA  . SER   A 84  ? 0.1560 0.1616 0.1344 -0.0143 -0.0078 0.0157  84  SER   A CA  
1800 C  C   . SER   A 84  ? 0.1599 0.1586 0.1267 -0.0185 -0.0011 0.0133  84  SER   A C   
1801 O  O   . SER   A 84  ? 0.1477 0.1712 0.1255 -0.0107 -0.0064 0.0168  84  SER   A O   
1802 C  CB  . SER   A 84  ? 0.1586 0.1850 0.1417 -0.0112 -0.0139 0.0048  84  SER   A CB  
1803 O  OG  . SER   A 84  ? 0.1654 0.2092 0.1449 -0.0095 -0.0283 -0.0053 84  SER   A OG  
1809 N  N   . GLY   A 85  ? 0.1681 0.1746 0.1322 -0.0238 0.0024  0.0101  85  GLY   A N   
1810 C  CA  . GLY   A 85  ? 0.1649 0.1803 0.1508 -0.0311 0.0108  0.0047  85  GLY   A CA  
1811 C  C   . GLY   A 85  ? 0.1620 0.1893 0.1261 -0.0190 -0.0066 0.0036  85  GLY   A C   
1812 O  O   . GLY   A 85  ? 0.1653 0.2032 0.1368 -0.0273 -0.0012 -0.0098 85  GLY   A O   
1816 N  N   . HIS   A 86  ? 0.1672 0.1802 0.1286 -0.0101 -0.0136 0.0075  86  HIS   A N   
1817 C  CA  . HIS   A 86  ? 0.1882 0.1866 0.1198 -0.0124 -0.0089 0.0119  86  HIS   A CA  
1818 C  C   . HIS   A 86  ? 0.2115 0.2058 0.1106 -0.0168 -0.0129 0.0099  86  HIS   A C   
1819 O  O   . HIS   A 86  ? 0.2224 0.2310 0.1213 -0.0131 -0.0070 0.0101  86  HIS   A O   
1820 C  CB  . HIS   A 86  ? 0.1893 0.1795 0.1312 -0.0100 -0.0060 0.0143  86  HIS   A CB  
1821 C  CG  . HIS   A 86  ? 0.1829 0.1750 0.1401 -0.0019 -0.0014 0.0117  86  HIS   A CG  
1822 N  ND1 . HIS   A 86  ? 0.1930 0.1728 0.1713 -0.0135 -0.0010 0.0125  86  HIS   A ND1 
1823 C  CD2 . HIS   A 86  ? 0.1821 0.1703 0.1389 0.0079  -0.0004 0.0129  86  HIS   A CD2 
1824 C  CE1 . HIS   A 86  ? 0.1883 0.1688 0.1781 -0.0081 0.0136  0.0175  86  HIS   A CE1 
1825 N  NE2 . HIS   A 86  ? 0.1827 0.1643 0.1541 0.0073  0.0105  0.0277  86  HIS   A NE2 
1833 N  N   . ASN   A 87  ? 0.2242 0.2119 0.1201 -0.0032 0.0048  -0.0053 87  ASN   A N   
1834 C  CA  . ASN   A 87  ? 0.2413 0.2268 0.1263 -0.0042 0.0219  -0.0063 87  ASN   A CA  
1835 C  C   . ASN   A 87  ? 0.2331 0.2394 0.1556 -0.0139 0.0447  0.0055  87  ASN   A C   
1836 O  O   . ASN   A 87  ? 0.2669 0.2671 0.1971 -0.0309 0.0822  0.0026  87  ASN   A O   
1837 C  CB  . ASN   A 87  ? 0.2602 0.2303 0.1319 0.0064  0.0220  -0.0115 87  ASN   A CB  
1838 C  CG  . ASN   A 87  ? 0.2768 0.2365 0.1318 0.0168  0.0307  -0.0067 87  ASN   A CG  
1839 O  OD1 . ASN   A 87  ? 0.2904 0.2319 0.1400 0.0352  0.0301  -0.0044 87  ASN   A OD1 
1840 N  ND2 . ASN   A 87  ? 0.2819 0.2623 0.1521 0.0167  0.0276  0.0003  87  ASN   A ND2 
1847 N  N   A LEU   A 88  ? 0.2085 0.2281 0.1461 -0.0143 0.0224  0.0179  88  LEU   A N   
1848 N  N   B LEU   A 88  ? 0.2077 0.2322 0.1455 -0.0146 0.0321  0.0106  88  LEU   A N   
1849 C  CA  A LEU   A 88  ? 0.1895 0.2245 0.1554 -0.0178 0.0213  0.0329  88  LEU   A CA  
1850 C  CA  B LEU   A 88  ? 0.1871 0.2318 0.1508 -0.0184 0.0395  0.0204  88  LEU   A CA  
1851 C  C   A LEU   A 88  ? 0.1799 0.2266 0.1510 -0.0165 0.0211  0.0381  88  LEU   A C   
1852 C  C   B LEU   A 88  ? 0.1793 0.2308 0.1490 -0.0159 0.0309  0.0351  88  LEU   A C   
1853 O  O   A LEU   A 88  ? 0.1784 0.2311 0.1751 -0.0170 0.0249  0.0465  88  LEU   A O   
1854 O  O   B LEU   A 88  ? 0.1780 0.2360 0.1638 -0.0140 0.0357  0.0521  88  LEU   A O   
1855 C  CB  A LEU   A 88  ? 0.1912 0.2219 0.1652 -0.0237 -0.0041 0.0463  88  LEU   A CB  
1856 C  CB  B LEU   A 88  ? 0.1863 0.2356 0.1561 -0.0258 0.0312  0.0188  88  LEU   A CB  
1857 C  CG  A LEU   A 88  ? 0.2090 0.2256 0.1912 -0.0194 -0.0209 0.0538  88  LEU   A CG  
1858 C  CG  B LEU   A 88  ? 0.1981 0.2432 0.1700 -0.0206 0.0249  0.0120  88  LEU   A CG  
1859 C  CD1 A LEU   A 88  ? 0.2169 0.2265 0.1887 -0.0225 -0.0284 0.0551  88  LEU   A CD1 
1860 C  CD1 B LEU   A 88  ? 0.2015 0.2468 0.1662 -0.0195 0.0244  0.0037  88  LEU   A CD1 
1861 C  CD2 A LEU   A 88  ? 0.2222 0.2362 0.2227 -0.0140 -0.0176 0.0419  88  LEU   A CD2 
1862 C  CD2 B LEU   A 88  ? 0.2095 0.2506 0.1827 -0.0134 0.0288  0.0007  88  LEU   A CD2 
1885 N  N   . ALA   A 89  ? 0.1790 0.2206 0.1392 -0.0125 0.0123  0.0268  89  ALA   A N   
1886 C  CA  . ALA   A 89  ? 0.1832 0.2185 0.1265 -0.0108 -0.0027 0.0285  89  ALA   A CA  
1887 C  C   . ALA   A 89  ? 0.1867 0.2233 0.1295 -0.0080 -0.0108 0.0246  89  ALA   A C   
1888 O  O   . ALA   A 89  ? 0.1802 0.2198 0.1680 -0.0203 -0.0123 -0.0023 89  ALA   A O   
1889 C  CB  . ALA   A 89  ? 0.1780 0.2169 0.1223 -0.0097 0.0009  0.0261  89  ALA   A CB  
1896 N  N   A LYS   A 90  ? 0.1917 0.2320 0.1280 -0.0110 -0.0173 0.0302  90  LYS   A N   
1897 N  N   B LYS   A 90  ? 0.1849 0.2313 0.1284 -0.0116 -0.0194 0.0240  90  LYS   A N   
1898 C  CA  A LYS   A 90  ? 0.1989 0.2414 0.1406 -0.0112 -0.0276 0.0377  90  LYS   A CA  
1899 C  CA  B LYS   A 90  ? 0.1853 0.2394 0.1408 -0.0129 -0.0313 0.0220  90  LYS   A CA  
1900 C  C   A LYS   A 90  ? 0.1883 0.2281 0.1379 -0.0117 -0.0236 0.0294  90  LYS   A C   
1901 C  C   B LYS   A 90  ? 0.1664 0.2237 0.1338 -0.0172 -0.0257 0.0059  90  LYS   A C   
1902 O  O   A LYS   A 90  ? 0.1955 0.2373 0.1612 -0.0133 -0.0270 0.0297  90  LYS   A O   
1903 O  O   B LYS   A 90  ? 0.1660 0.2381 0.1560 -0.0265 -0.0356 -0.0080 90  LYS   A O   
1904 C  CB  A LYS   A 90  ? 0.2202 0.2675 0.1783 -0.0104 -0.0360 0.0539  90  LYS   A CB  
1905 C  CB  B LYS   A 90  ? 0.2085 0.2665 0.1797 -0.0103 -0.0437 0.0370  90  LYS   A CB  
1906 C  CG  A LYS   A 90  ? 0.2455 0.2933 0.2658 -0.0112 -0.0351 0.0571  90  LYS   A CG  
1907 C  CG  B LYS   A 90  ? 0.2367 0.2922 0.2678 -0.0096 -0.0444 0.0404  90  LYS   A CG  
1908 C  CD  A LYS   A 90  ? 0.2689 0.3148 0.3452 -0.0134 -0.0261 0.0589  90  LYS   A CD  
1909 C  CD  B LYS   A 90  ? 0.2628 0.3139 0.3468 -0.0101 -0.0355 0.0411  90  LYS   A CD  
1910 C  CE  A LYS   A 90  ? 0.2868 0.3311 0.4076 -0.0165 -0.0192 0.0568  90  LYS   A CE  
1911 C  CE  B LYS   A 90  ? 0.2831 0.3303 0.4078 -0.0117 -0.0289 0.0372  90  LYS   A CE  
1912 N  NZ  A LYS   A 90  ? 0.2993 0.3417 0.4466 -0.0201 -0.0126 0.0544  90  LYS   A NZ  
1913 N  NZ  B LYS   A 90  ? 0.2967 0.3405 0.4447 -0.0138 -0.0221 0.0327  90  LYS   A NZ  
1940 N  N   A HIS   A 91  ? 0.1784 0.2032 0.1204 -0.0120 -0.0308 0.0322  91  HIS   A N   
1941 N  N   B HIS   A 91  ? 0.1569 0.1914 0.1098 -0.0144 -0.0266 0.0141  91  HIS   A N   
1942 C  CA  A HIS   A 91  ? 0.1679 0.1891 0.1336 -0.0087 -0.0320 0.0265  91  HIS   A CA  
1943 C  CA  B HIS   A 91  ? 0.1457 0.1760 0.1202 -0.0070 -0.0253 0.0078  91  HIS   A CA  
1944 C  C   A HIS   A 91  ? 0.1477 0.1676 0.1136 -0.0085 -0.0204 0.0231  91  HIS   A C   
1945 C  C   B HIS   A 91  ? 0.1372 0.1625 0.1138 -0.0108 -0.0143 0.0080  91  HIS   A C   
1946 O  O   A HIS   A 91  ? 0.1393 0.1599 0.1138 -0.0074 -0.0182 0.0230  91  HIS   A O   
1947 O  O   B HIS   A 91  ? 0.1338 0.1645 0.1432 -0.0192 -0.0067 0.0107  91  HIS   A O   
1948 C  CB  A HIS   A 91  ? 0.1921 0.2151 0.1726 0.0047  -0.0441 0.0257  91  HIS   A CB  
1949 C  CB  B HIS   A 91  ? 0.1655 0.2016 0.1562 0.0144  -0.0353 0.0134  91  HIS   A CB  
1950 C  CG  A HIS   A 91  ? 0.2226 0.2544 0.2260 0.0116  -0.0601 0.0134  91  HIS   A CG  
1951 C  CG  B HIS   A 91  ? 0.1935 0.2430 0.2101 0.0257  -0.0520 0.0055  91  HIS   A CG  
1952 N  ND1 A HIS   A 91  ? 0.2326 0.2756 0.2530 0.0119  -0.0684 -0.0001 91  HIS   A ND1 
1953 N  ND1 B HIS   A 91  ? 0.2027 0.2672 0.2405 0.0237  -0.0577 -0.0078 91  HIS   A ND1 
1954 C  CD2 A HIS   A 91  ? 0.2436 0.2704 0.2453 0.0158  -0.0647 0.0172  91  HIS   A CD2 
1955 C  CD2 B HIS   A 91  ? 0.2160 0.2588 0.2295 0.0304  -0.0569 0.0104  91  HIS   A CD2 
1956 C  CE1 A HIS   A 91  ? 0.2431 0.2830 0.2653 0.0168  -0.0702 0.0053  91  HIS   A CE1 
1957 C  CE1 B HIS   A 91  ? 0.2149 0.2736 0.2520 0.0274  -0.0568 -0.0025 91  HIS   A CE1 
1958 N  NE2 A HIS   A 91  ? 0.2530 0.2811 0.2618 0.0208  -0.0680 0.0142  91  HIS   A NE2 
1959 N  NE2 B HIS   A 91  ? 0.2258 0.2714 0.2477 0.0323  -0.0570 0.0053  91  HIS   A NE2 
1974 N  N   . CYS   A 92  ? 0.1394 0.1595 0.1131 -0.0145 -0.0120 0.0198  92  CYS   A N   
1975 C  CA  . CYS   A 92  ? 0.1338 0.1519 0.1274 -0.0151 -0.0003 0.0173  92  CYS   A CA  
1976 C  C   . CYS   A 92  ? 0.1246 0.1414 0.1212 -0.0136 -0.0027 0.0223  92  CYS   A C   
1977 O  O   . CYS   A 92  ? 0.1248 0.1494 0.1446 -0.0188 -0.0021 0.0146  92  CYS   A O   
1978 C  CB  . CYS   A 92  ? 0.1258 0.1487 0.1368 -0.0060 -0.0161 0.0132  92  CYS   A CB  
1979 S  SG  . CYS   A 92  ? 0.1310 0.1370 0.1371 -0.0087 -0.0081 0.0141  92  CYS   A SG  
1986 N  N   . LEU   A 93  ? 0.1194 0.1280 0.1274 -0.0101 0.0011  0.0117  93  LEU   A N   
1987 C  CA  . LEU   A 93  ? 0.1186 0.1254 0.1271 -0.0041 -0.0041 0.0222  93  LEU   A CA  
1988 C  C   . LEU   A 93  ? 0.1116 0.1162 0.1313 -0.0029 0.0047  0.0129  93  LEU   A C   
1989 O  O   . LEU   A 93  ? 0.1104 0.1270 0.1214 -0.0021 0.0004  0.0134  93  LEU   A O   
1990 C  CB  . LEU   A 93  ? 0.1249 0.1273 0.1442 -0.0021 -0.0066 0.0237  93  LEU   A CB  
1991 C  CG  . LEU   A 93  ? 0.1296 0.1303 0.1407 -0.0026 -0.0001 0.0206  93  LEU   A CG  
1992 C  CD1 . LEU   A 93  ? 0.1381 0.1282 0.1612 -0.0048 0.0116  0.0154  93  LEU   A CD1 
1993 C  CD2 . LEU   A 93  ? 0.1444 0.1296 0.1650 -0.0095 -0.0048 0.0137  93  LEU   A CD2 
2005 N  N   . HIS   A 94  ? 0.1117 0.1133 0.1288 -0.0066 0.0039  0.0204  94  HIS   A N   
2006 C  CA  . HIS   A 94  ? 0.1090 0.1158 0.1355 -0.0036 -0.0031 0.0221  94  HIS   A CA  
2007 C  C   . HIS   A 94  ? 0.1048 0.1116 0.1374 -0.0052 -0.0030 0.0144  94  HIS   A C   
2008 O  O   . HIS   A 94  ? 0.1129 0.1357 0.1641 -0.0013 -0.0033 -0.0093 94  HIS   A O   
2009 C  CB  . HIS   A 94  ? 0.1090 0.1109 0.1448 -0.0021 -0.0046 0.0216  94  HIS   A CB  
2010 C  CG  . HIS   A 94  ? 0.1123 0.1121 0.1380 -0.0089 -0.0076 0.0267  94  HIS   A CG  
2011 N  ND1 . HIS   A 94  ? 0.1129 0.1093 0.1428 -0.0074 -0.0001 0.0200  94  HIS   A ND1 
2012 C  CD2 . HIS   A 94  ? 0.1213 0.1266 0.1386 -0.0100 -0.0127 0.0168  94  HIS   A CD2 
2013 C  CE1 . HIS   A 94  ? 0.1205 0.1189 0.1397 -0.0041 -0.0115 0.0061  94  HIS   A CE1 
2014 N  NE2 . HIS   A 94  ? 0.1295 0.1214 0.1435 -0.0104 -0.0139 0.0033  94  HIS   A NE2 
2022 N  N   . VAL   A 95  ? 0.1141 0.1083 0.1228 -0.0003 0.0073  0.0120  95  VAL   A N   
2023 C  CA  . VAL   A 95  ? 0.1171 0.1118 0.1174 -0.0031 0.0038  0.0085  95  VAL   A CA  
2024 C  C   . VAL   A 95  ? 0.1144 0.1118 0.1211 -0.0079 0.0047  0.0041  95  VAL   A C   
2025 O  O   . VAL   A 95  ? 0.1200 0.1194 0.1306 0.0047  0.0007  0.0084  95  VAL   A O   
2026 C  CB  . VAL   A 95  ? 0.1209 0.1188 0.1292 -0.0119 0.0020  0.0087  95  VAL   A CB  
2027 C  CG1 . VAL   A 95  ? 0.1392 0.1144 0.1463 -0.0173 -0.0040 0.0010  95  VAL   A CG1 
2028 C  CG2 . VAL   A 95  ? 0.1188 0.1272 0.1371 -0.0141 0.0071  0.0264  95  VAL   A CG2 
2038 N  N   . VAL   A 96  ? 0.1198 0.1160 0.1216 -0.0060 -0.0003 0.0167  96  VAL   A N   
2039 C  CA  . VAL   A 96  ? 0.1224 0.1156 0.1252 -0.0002 0.0015  0.0221  96  VAL   A CA  
2040 C  C   . VAL   A 96  ? 0.1265 0.1201 0.1343 -0.0016 0.0046  0.0235  96  VAL   A C   
2041 O  O   . VAL   A 96  ? 0.1376 0.1246 0.1491 -0.0035 0.0072  0.0015  96  VAL   A O   
2042 C  CB  . VAL   A 96  ? 0.1322 0.1223 0.1317 -0.0026 0.0117  0.0126  96  VAL   A CB  
2043 C  CG1 . VAL   A 96  ? 0.1395 0.1248 0.1226 -0.0025 0.0031  0.0101  96  VAL   A CG1 
2044 C  CG2 . VAL   A 96  ? 0.1265 0.1316 0.1443 -0.0134 0.0131  0.0098  96  VAL   A CG2 
2054 N  N   A GLY   A 97  ? 0.1256 0.1263 0.1319 -0.0062 0.0016  0.0165  97  GLY   A N   
2055 N  N   B GLY   A 97  ? 0.1286 0.1245 0.1264 -0.0063 -0.0015 0.0113  97  GLY   A N   
2056 C  CA  A GLY   A 97  ? 0.1303 0.1385 0.1323 -0.0059 -0.0045 0.0144  97  GLY   A CA  
2057 C  CA  B GLY   A 97  ? 0.1320 0.1316 0.1285 -0.0069 -0.0023 0.0136  97  GLY   A CA  
2058 C  C   A GLY   A 97  ? 0.1394 0.1474 0.1077 -0.0019 -0.0082 0.0100  97  GLY   A C   
2059 C  C   B GLY   A 97  ? 0.1372 0.1361 0.1272 -0.0022 0.0011  0.0159  97  GLY   A C   
2060 O  O   A GLY   A 97  ? 0.1403 0.1464 0.1133 -0.0001 -0.0031 0.0064  97  GLY   A O   
2061 O  O   B GLY   A 97  ? 0.1398 0.1339 0.1506 -0.0065 0.0074  0.0163  97  GLY   A O   
2068 N  N   A PRO   A 98  ? 0.1497 0.1481 0.0996 0.0002  -0.0161 0.0152  98  PRO   A N   
2069 N  N   B PRO   A 98  ? 0.1469 0.1365 0.1341 0.0003  0.0029  0.0179  98  PRO   A N   
2070 C  CA  A PRO   A 98  ? 0.1518 0.1641 0.0999 -0.0033 -0.0117 0.0132  98  PRO   A CA  
2071 C  CA  B PRO   A 98  ? 0.1478 0.1389 0.1460 0.0055  0.0059  0.0087  98  PRO   A CA  
2072 C  C   A PRO   A 98  ? 0.1505 0.1782 0.0900 -0.0064 -0.0111 0.0187  98  PRO   A C   
2073 C  C   B PRO   A 98  ? 0.1531 0.1321 0.1401 0.0068  0.0041  0.0093  98  PRO   A C   
2074 O  O   A PRO   A 98  ? 0.1435 0.1661 0.1059 -0.0060 -0.0051 0.0140  98  PRO   A O   
2075 O  O   B PRO   A 98  ? 0.1514 0.1288 0.1573 0.0072  0.0007  0.0097  98  PRO   A O   
2076 C  CB  A PRO   A 98  ? 0.1603 0.1636 0.1016 0.0056  -0.0145 -0.0031 98  PRO   A CB  
2077 C  CB  B PRO   A 98  ? 0.1537 0.1395 0.1508 0.0142  0.0029  0.0119  98  PRO   A CB  
2078 C  CG  A PRO   A 98  ? 0.1589 0.1591 0.1115 0.0049  -0.0243 -0.0059 98  PRO   A CG  
2079 C  CG  B PRO   A 98  ? 0.1575 0.1425 0.1628 0.0080  -0.0022 0.0082  98  PRO   A CG  
2080 C  CD  A PRO   A 98  ? 0.1537 0.1488 0.1108 0.0013  -0.0185 0.0098  98  PRO   A CD  
2081 C  CD  B PRO   A 98  ? 0.1474 0.1373 0.1483 0.0059  -0.0013 0.0154  98  PRO   A CD  
2096 N  N   A ASN   A 99  ? 0.1543 0.1983 0.0954 -0.0025 -0.0003 0.0224  99  ASN   A N   
2097 N  N   B ASN   A 99  ? 0.1687 0.1327 0.1378 0.0106  0.0020  0.0211  99  ASN   A N   
2098 C  CA  A ASN   A 99  ? 0.1747 0.2165 0.1155 -0.0067 -0.0134 0.0286  99  ASN   A CA  
2099 C  CA  B ASN   A 99  ? 0.1898 0.1357 0.1421 0.0169  0.0012  0.0307  99  ASN   A CA  
2100 C  C   A ASN   A 99  ? 0.2030 0.2408 0.1149 -0.0108 -0.0062 0.0269  99  ASN   A C   
2101 C  C   B ASN   A 99  ? 0.1996 0.1446 0.1449 0.0134  -0.0114 0.0400  99  ASN   A C   
2102 O  O   A ASN   A 99  ? 0.2145 0.2552 0.1273 0.0014  -0.0044 0.0246  99  ASN   A O   
2103 O  O   B ASN   A 99  ? 0.2029 0.1493 0.1343 0.0224  -0.0188 0.0314  99  ASN   A O   
2104 C  CB  A ASN   A 99  ? 0.1714 0.2160 0.1353 -0.0084 -0.0218 0.0366  99  ASN   A CB  
2105 C  CB  B ASN   A 99  ? 0.2076 0.1360 0.1550 0.0236  -0.0084 0.0315  99  ASN   A CB  
2106 C  CG  A ASN   A 99  ? 0.1753 0.2192 0.1642 -0.0068 -0.0192 0.0367  99  ASN   A CG  
2107 C  CG  B ASN   A 99  ? 0.2275 0.1441 0.1636 0.0236  -0.0100 0.0316  99  ASN   A CG  
2108 O  OD1 A ASN   A 99  ? 0.1856 0.2256 0.1752 -0.0030 -0.0248 0.0212  99  ASN   A OD1 
2109 O  OD1 B ASN   A 99  ? 0.2198 0.1439 0.1580 0.0333  -0.0114 0.0368  99  ASN   A OD1 
2110 N  ND2 A ASN   A 99  ? 0.1789 0.2166 0.1807 -0.0049 -0.0141 0.0605  99  ASN   A ND2 
2111 N  ND2 B ASN   A 99  ? 0.2424 0.1460 0.1953 0.0261  -0.0163 0.0219  99  ASN   A ND2 
2124 N  N   A VAL   A 100 ? 0.2195 0.2519 0.1368 -0.0178 -0.0200 0.0148  100 VAL   A N   
2125 N  N   B VAL   A 100 ? 0.2149 0.1630 0.1718 0.0087  -0.0346 0.0467  100 VAL   A N   
2126 C  CA  A VAL   A 100 ? 0.2387 0.2666 0.1655 -0.0149 -0.0238 0.0116  100 VAL   A CA  
2127 C  CA  B VAL   A 100 ? 0.2478 0.1831 0.2148 -0.0013 -0.0501 0.0458  100 VAL   A CA  
2128 C  C   A VAL   A 100 ? 0.2560 0.2811 0.1848 -0.0152 -0.0219 0.0300  100 VAL   A C   
2129 C  C   B VAL   A 100 ? 0.2604 0.1845 0.2063 0.0043  -0.0650 0.0402  100 VAL   A C   
2130 O  O   A VAL   A 100 ? 0.2605 0.2833 0.1872 -0.0139 -0.0130 0.0316  100 VAL   A O   
2131 O  O   B VAL   A 100 ? 0.2731 0.1927 0.2173 -0.0010 -0.0676 0.0332  100 VAL   A O   
2132 C  CB  A VAL   A 100 ? 0.2477 0.2690 0.1937 -0.0116 -0.0221 -0.0056 100 VAL   A CB  
2133 C  CB  B VAL   A 100 ? 0.2664 0.2068 0.2818 -0.0155 -0.0345 0.0457  100 VAL   A CB  
2134 C  CG1 A VAL   A 100 ? 0.2527 0.2728 0.2157 -0.0121 -0.0152 -0.0185 100 VAL   A CG1 
2135 C  CG1 B VAL   A 100 ? 0.2708 0.2125 0.3111 -0.0136 -0.0337 0.0420  100 VAL   A CG1 
2136 C  CG2 A VAL   A 100 ? 0.2534 0.2699 0.1931 -0.0164 -0.0240 -0.0092 100 VAL   A CG2 
2137 C  CG2 B VAL   A 100 ? 0.2726 0.2139 0.3060 -0.0189 -0.0197 0.0544  100 VAL   A CG2 
2156 N  N   A ASN   A 101 ? 0.2680 0.2923 0.1970 -0.0170 -0.0242 0.0461  101 ASN   A N   
2157 N  N   B ASN   A 101 ? 0.2616 0.1835 0.1944 0.0086  -0.0730 0.0415  101 ASN   A N   
2158 C  CA  A ASN   A 101 ? 0.2857 0.3017 0.2153 -0.0163 -0.0207 0.0588  101 ASN   A CA  
2159 C  CA  B ASN   A 101 ? 0.2674 0.1945 0.1928 0.0173  -0.0641 0.0456  101 ASN   A CA  
2160 C  C   A ASN   A 101 ? 0.3034 0.3205 0.2382 -0.0113 -0.0130 0.0808  101 ASN   A C   
2161 C  C   B ASN   A 101 ? 0.2941 0.2093 0.1829 0.0250  -0.0496 0.0516  101 ASN   A C   
2162 O  O   A ASN   A 101 ? 0.3105 0.3228 0.2534 -0.0092 -0.0163 0.0814  101 ASN   A O   
2163 O  O   B ASN   A 101 ? 0.3055 0.2175 0.1786 0.0254  -0.0461 0.0513  101 ASN   A O   
2164 C  CB  A ASN   A 101 ? 0.2858 0.2902 0.1946 -0.0200 -0.0277 0.0464  101 ASN   A CB  
2165 C  CB  B ASN   A 101 ? 0.2472 0.1931 0.2147 0.0104  -0.0577 0.0535  101 ASN   A CB  
2166 C  CG  A ASN   A 101 ? 0.2864 0.2805 0.1819 -0.0214 -0.0304 0.0163  101 ASN   A CG  
2167 C  CG  B ASN   A 101 ? 0.2364 0.2051 0.2531 0.0003  -0.0491 0.0441  101 ASN   A CG  
2168 O  OD1 A ASN   A 101 ? 0.2853 0.2795 0.1706 -0.0151 -0.0301 -0.0111 101 ASN   A OD1 
2169 O  OD1 B ASN   A 101 ? 0.2444 0.2203 0.2851 -0.0035 -0.0505 0.0381  101 ASN   A OD1 
2170 N  ND2 A ASN   A 101 ? 0.2931 0.2778 0.1914 -0.0248 -0.0282 0.0071  101 ASN   A ND2 
2171 N  ND2 B ASN   A 101 ? 0.2292 0.2018 0.2755 0.0011  -0.0269 0.0331  101 ASN   A ND2 
2184 N  N   A LYS   A 102 ? 0.3113 0.3392 0.2574 -0.0112 -0.0011 0.0915  102 LYS   A N   
2185 N  N   B LYS   A 102 ? 0.3065 0.2162 0.1964 0.0318  -0.0349 0.0517  102 LYS   A N   
2186 C  CA  A LYS   A 102 ? 0.3229 0.3560 0.2784 -0.0088 -0.0037 0.0901  102 LYS   A CA  
2187 C  CA  B LYS   A 102 ? 0.3214 0.2354 0.2075 0.0293  -0.0138 0.0533  102 LYS   A CA  
2188 C  C   A LYS   A 102 ? 0.3310 0.3671 0.2713 0.0011  -0.0052 0.0813  102 LYS   A C   
2189 C  C   B LYS   A 102 ? 0.3224 0.2415 0.1916 0.0354  -0.0218 0.0694  102 LYS   A C   
2190 O  O   A LYS   A 102 ? 0.3346 0.3732 0.2784 0.0061  -0.0061 0.0811  102 LYS   A O   
2191 O  O   B LYS   A 102 ? 0.3328 0.2476 0.2157 0.0378  -0.0111 0.0729  102 LYS   A O   
2192 C  CB  A LYS   A 102 ? 0.3265 0.3613 0.3111 -0.0156 -0.0070 0.0891  102 LYS   A CB  
2193 C  CB  B LYS   A 102 ? 0.3319 0.2464 0.2449 0.0263  -0.0022 0.0373  102 LYS   A CB  
2194 C  CG  A LYS   A 102 ? 0.3299 0.3634 0.3392 -0.0215 -0.0117 0.0853  102 LYS   A CG  
2195 C  CG  B LYS   A 102 ? 0.3427 0.2601 0.2922 0.0224  0.0059  0.0198  102 LYS   A CG  
2196 C  CD  A LYS   A 102 ? 0.3345 0.3673 0.3693 -0.0252 -0.0188 0.0762  102 LYS   A CD  
2197 C  CD  B LYS   A 102 ? 0.3522 0.2765 0.3403 0.0175  0.0132  0.0108  102 LYS   A CD  
2198 C  CE  A LYS   A 102 ? 0.3382 0.3687 0.3909 -0.0271 -0.0266 0.0720  102 LYS   A CE  
2199 C  CE  B LYS   A 102 ? 0.3601 0.2894 0.3792 0.0144  0.0156  0.0080  102 LYS   A CE  
2200 N  NZ  A LYS   A 102 ? 0.3406 0.3705 0.4027 -0.0292 -0.0275 0.0678  102 LYS   A NZ  
2201 N  NZ  B LYS   A 102 ? 0.3649 0.2978 0.4057 0.0132  0.0145  0.0059  102 LYS   A NZ  
2228 N  N   A GLY   A 103 ? 0.3341 0.3705 0.2699 0.0078  -0.0084 0.0664  103 GLY   A N   
2229 N  N   B GLY   A 103 ? 0.3117 0.2487 0.1632 0.0391  -0.0359 0.0537  103 GLY   A N   
2230 C  CA  A GLY   A 103 ? 0.3372 0.3722 0.2662 0.0115  -0.0108 0.0535  103 GLY   A CA  
2231 C  CA  B GLY   A 103 ? 0.2998 0.2500 0.1691 0.0413  -0.0389 0.0490  103 GLY   A CA  
2232 C  C   A GLY   A 103 ? 0.3370 0.3736 0.2653 0.0117  -0.0109 0.0415  103 GLY   A C   
2233 C  C   B GLY   A 103 ? 0.2826 0.2453 0.1597 0.0417  -0.0440 0.0395  103 GLY   A C   
2234 O  O   A GLY   A 103 ? 0.3413 0.3783 0.2845 0.0154  -0.0140 0.0327  103 GLY   A O   
2235 O  O   B GLY   A 103 ? 0.2973 0.2554 0.1616 0.0458  -0.0426 0.0402  103 GLY   A O   
2242 N  N   A GLU   A 104 ? 0.3300 0.3676 0.2406 0.0051  -0.0044 0.0353  104 GLU   A N   
2243 N  N   B GLU   A 104 ? 0.2458 0.2242 0.1466 0.0368  -0.0434 0.0365  104 GLU   A N   
2244 C  CA  A GLU   A 104 ? 0.3212 0.3585 0.2219 -0.0043 0.0022  0.0280  104 GLU   A CA  
2245 C  CA  B GLU   A 104 ? 0.2133 0.2009 0.1274 0.0246  -0.0334 0.0331  104 GLU   A CA  
2246 C  C   A GLU   A 104 ? 0.3201 0.3571 0.2186 -0.0023 -0.0047 0.0146  104 GLU   A C   
2247 C  C   B GLU   A 104 ? 0.2058 0.1986 0.1459 0.0261  -0.0232 0.0156  104 GLU   A C   
2248 O  O   A GLU   A 104 ? 0.3207 0.3551 0.2186 -0.0022 -0.0101 0.0117  104 GLU   A O   
2249 O  O   B GLU   A 104 ? 0.2000 0.1975 0.1860 0.0278  -0.0259 0.0137  104 GLU   A O   
2250 C  CB  A GLU   A 104 ? 0.3120 0.3507 0.2101 -0.0146 0.0159  0.0372  104 GLU   A CB  
2251 C  CB  B GLU   A 104 ? 0.1966 0.1842 0.1145 0.0079  -0.0209 0.0412  104 GLU   A CB  
2252 C  CG  A GLU   A 104 ? 0.3047 0.3453 0.2121 -0.0222 0.0274  0.0417  104 GLU   A CG  
2253 C  CG  B GLU   A 104 ? 0.1867 0.1856 0.1278 -0.0072 -0.0205 0.0390  104 GLU   A CG  
2254 C  CD  A GLU   A 104 ? 0.2980 0.3415 0.2111 -0.0282 0.0396  0.0474  104 GLU   A CD  
2255 C  CD  B GLU   A 104 ? 0.1796 0.1887 0.1209 -0.0176 -0.0193 0.0449  104 GLU   A CD  
2256 O  OE1 A GLU   A 104 ? 0.2902 0.3403 0.1890 -0.0309 0.0526  0.0546  104 GLU   A OE1 
2257 O  OE1 B GLU   A 104 ? 0.1676 0.1916 0.1299 -0.0144 -0.0262 0.0430  104 GLU   A OE1 
2258 O  OE2 A GLU   A 104 ? 0.3036 0.3419 0.2354 -0.0295 0.0351  0.0445  104 GLU   A OE2 
2259 O  OE2 B GLU   A 104 ? 0.1922 0.1936 0.1274 -0.0262 -0.0023 0.0452  104 GLU   A OE2 
2272 N  N   A ASP   A 105 ? 0.3176 0.3585 0.2238 0.0017  -0.0056 0.0029  105 ASP   A N   
2273 N  N   B ASP   A 105 ? 0.2142 0.1971 0.1420 0.0235  -0.0151 0.0106  105 ASP   A N   
2274 C  CA  A ASP   A 105 ? 0.3135 0.3594 0.2451 0.0060  -0.0068 -0.0181 105 ASP   A CA  
2275 C  CA  B ASP   A 105 ? 0.2281 0.1913 0.1756 0.0278  -0.0100 -0.0022 105 ASP   A CA  
2276 C  C   A ASP   A 105 ? 0.2914 0.3469 0.2233 -0.0070 -0.0166 -0.0295 105 ASP   A C   
2277 C  C   B ASP   A 105 ? 0.2237 0.1664 0.1511 0.0204  -0.0085 -0.0069 105 ASP   A C   
2278 O  O   A ASP   A 105 ? 0.2877 0.3496 0.1970 -0.0082 -0.0203 -0.0253 105 ASP   A O   
2279 O  O   B ASP   A 105 ? 0.2155 0.1531 0.1170 0.0157  -0.0093 -0.0054 105 ASP   A O   
2280 C  CB  A ASP   A 105 ? 0.3283 0.3705 0.2951 0.0195  -0.0014 -0.0256 105 ASP   A CB  
2281 C  CB  B ASP   A 105 ? 0.2398 0.2078 0.2262 0.0387  -0.0047 -0.0183 105 ASP   A CB  
2282 C  CG  A ASP   A 105 ? 0.3403 0.3792 0.3419 0.0300  -0.0008 -0.0314 105 ASP   A CG  
2283 C  CG  B ASP   A 105 ? 0.2515 0.2199 0.2732 0.0492  0.0025  -0.0455 105 ASP   A CG  
2284 O  OD1 A ASP   A 105 ? 0.3455 0.3824 0.3506 0.0325  -0.0023 -0.0395 105 ASP   A OD1 
2285 O  OD1 B ASP   A 105 ? 0.2575 0.2218 0.2652 0.0438  -0.0094 -0.0576 105 ASP   A OD1 
2286 O  OD2 A ASP   A 105 ? 0.3457 0.3827 0.3690 0.0353  -0.0002 -0.0268 105 ASP   A OD2 
2287 O  OD2 B ASP   A 105 ? 0.2571 0.2260 0.3161 0.0574  0.0156  -0.0479 105 ASP   A OD2 
2296 N  N   A ILE   A 106 ? 0.2726 0.3304 0.2306 -0.0187 -0.0281 -0.0480 106 ILE   A N   
2297 N  N   B ILE   A 106 ? 0.2263 0.1770 0.1663 0.0209  -0.0226 -0.0055 106 ILE   A N   
2298 C  CA  A ILE   A 106 ? 0.2495 0.3120 0.2350 -0.0329 -0.0437 -0.0675 106 ILE   A CA  
2299 C  CA  B ILE   A 106 ? 0.2209 0.1797 0.1870 0.0101  -0.0353 -0.0128 106 ILE   A CA  
2300 C  C   A ILE   A 106 ? 0.2320 0.3025 0.2400 -0.0493 -0.0420 -0.0778 106 ILE   A C   
2301 C  C   B ILE   A 106 ? 0.2202 0.1732 0.1801 0.0030  -0.0258 0.0073  106 ILE   A C   
2302 O  O   A ILE   A 106 ? 0.2143 0.2999 0.2414 -0.0589 -0.0355 -0.0789 106 ILE   A O   
2303 O  O   B ILE   A 106 ? 0.2074 0.1744 0.1870 -0.0076 -0.0123 0.0127  106 ILE   A O   
2304 C  CB  A ILE   A 106 ? 0.2477 0.3033 0.2519 -0.0272 -0.0570 -0.0659 106 ILE   A CB  
2305 C  CB  B ILE   A 106 ? 0.2274 0.2049 0.2277 0.0064  -0.0507 -0.0254 106 ILE   A CB  
2306 C  CG1 A ILE   A 106 ? 0.2421 0.2958 0.2628 -0.0200 -0.0602 -0.0613 106 ILE   A CG1 
2307 C  CG1 B ILE   A 106 ? 0.2296 0.2190 0.2524 0.0070  -0.0499 -0.0304 106 ILE   A CG1 
2308 C  CG2 A ILE   A 106 ? 0.2495 0.3032 0.2564 -0.0264 -0.0614 -0.0685 106 ILE   A CG2 
2309 C  CG2 B ILE   A 106 ? 0.2313 0.2116 0.2363 0.0050  -0.0563 -0.0328 106 ILE   A CG2 
2310 C  CD1 A ILE   A 106 ? 0.2355 0.2933 0.2686 -0.0146 -0.0667 -0.0532 106 ILE   A CD1 
2311 C  CD1 B ILE   A 106 ? 0.2291 0.2227 0.2683 0.0066  -0.0485 -0.0387 106 ILE   A CD1 
2334 N  N   A GLN   A 107 ? 0.2447 0.2955 0.2603 -0.0463 -0.0309 -0.0886 107 GLN   A N   
2335 N  N   B GLN   A 107 ? 0.2380 0.1643 0.1928 0.0123  -0.0234 0.0097  107 GLN   A N   
2336 C  CA  A GLN   A 107 ? 0.2563 0.2897 0.3039 -0.0365 -0.0139 -0.0887 107 GLN   A CA  
2337 C  CA  B GLN   A 107 ? 0.2563 0.1706 0.2358 0.0137  -0.0222 0.0072  107 GLN   A CA  
2338 C  C   A GLN   A 107 ? 0.2324 0.2615 0.2829 -0.0331 0.0062  -0.0696 107 GLN   A C   
2339 C  C   B GLN   A 107 ? 0.2338 0.1498 0.2097 0.0171  -0.0177 0.0203  107 GLN   A C   
2340 O  O   A GLN   A 107 ? 0.2409 0.2663 0.3146 -0.0324 0.0147  -0.0627 107 GLN   A O   
2341 O  O   B GLN   A 107 ? 0.2393 0.1490 0.2230 0.0132  -0.0257 0.0177  107 GLN   A O   
2342 C  CB  A GLN   A 107 ? 0.2925 0.3169 0.3785 -0.0336 -0.0166 -0.0944 107 GLN   A CB  
2343 C  CB  B GLN   A 107 ? 0.2941 0.2164 0.3077 0.0015  -0.0341 -0.0003 107 GLN   A CB  
2344 C  CG  A GLN   A 107 ? 0.3255 0.3441 0.4604 -0.0283 -0.0169 -0.0882 107 GLN   A CG  
2345 C  CG  B GLN   A 107 ? 0.3282 0.2691 0.3840 -0.0106 -0.0452 0.0077  107 GLN   A CG  
2346 C  CD  A GLN   A 107 ? 0.3512 0.3636 0.5315 -0.0258 -0.0176 -0.0800 107 GLN   A CD  
2347 C  CD  B GLN   A 107 ? 0.3546 0.3102 0.4524 -0.0188 -0.0528 0.0171  107 GLN   A CD  
2348 O  OE1 A GLN   A 107 ? 0.3607 0.3715 0.5593 -0.0241 -0.0183 -0.0759 107 GLN   A OE1 
2349 O  OE1 B GLN   A 107 ? 0.3653 0.3292 0.4737 -0.0215 -0.0550 0.0222  107 GLN   A OE1 
2350 N  NE2 A GLN   A 107 ? 0.3597 0.3713 0.5561 -0.0275 -0.0200 -0.0790 107 GLN   A NE2 
2351 N  NE2 B GLN   A 107 ? 0.3635 0.3245 0.4794 -0.0227 -0.0561 0.0183  107 GLN   A NE2 
2368 N  N   A LEU   A 108 ? 0.2046 0.2307 0.2322 -0.0309 0.0164  -0.0573 108 LEU   A N   
2369 N  N   B LEU   A 108 ? 0.2122 0.1464 0.1833 0.0081  -0.0019 0.0147  108 LEU   A N   
2370 C  CA  A LEU   A 108 ? 0.1875 0.2046 0.1973 -0.0144 0.0212  -0.0252 108 LEU   A CA  
2371 C  CA  B LEU   A 108 ? 0.1933 0.1483 0.1712 0.0057  0.0114  0.0158  108 LEU   A CA  
2372 C  C   A LEU   A 108 ? 0.1702 0.1702 0.1714 -0.0048 0.0167  -0.0005 108 LEU   A C   
2373 C  C   B LEU   A 108 ? 0.1719 0.1428 0.1589 0.0079  0.0139  0.0241  108 LEU   A C   
2374 O  O   A LEU   A 108 ? 0.1670 0.1665 0.1819 -0.0069 0.0148  -0.0013 108 LEU   A O   
2375 O  O   B LEU   A 108 ? 0.1660 0.1455 0.1822 0.0135  0.0166  0.0294  108 LEU   A O   
2376 C  CB  A LEU   A 108 ? 0.1886 0.2135 0.1853 -0.0128 0.0272  -0.0212 108 LEU   A CB  
2377 C  CB  B LEU   A 108 ? 0.1992 0.1623 0.1681 -0.0048 0.0202  0.0066  108 LEU   A CB  
2378 C  CG  A LEU   A 108 ? 0.1964 0.2273 0.1968 -0.0081 0.0325  -0.0142 108 LEU   A CG  
2379 C  CG  B LEU   A 108 ? 0.2117 0.1861 0.1873 -0.0038 0.0259  0.0004  108 LEU   A CG  
2380 C  CD1 A LEU   A 108 ? 0.2043 0.2306 0.2049 -0.0119 0.0341  -0.0083 108 LEU   A CD1 
2381 C  CD1 B LEU   A 108 ? 0.2197 0.1928 0.1978 -0.0072 0.0315  0.0052  108 LEU   A CD1 
2382 C  CD2 A LEU   A 108 ? 0.1999 0.2411 0.2160 -0.0022 0.0370  -0.0088 108 LEU   A CD2 
2383 C  CD2 B LEU   A 108 ? 0.2158 0.2047 0.2094 -0.0019 0.0270  -0.0007 108 LEU   A CD2 
2406 N  N   . LEU   A 109 ? 0.1616 0.1488 0.1748 0.0068  0.0128  0.0159  109 LEU   A N   
2407 C  CA  . LEU   A 109 ? 0.1524 0.1401 0.1739 0.0031  0.0058  0.0125  109 LEU   A CA  
2408 C  C   . LEU   A 109 ? 0.1341 0.1277 0.1708 -0.0038 0.0040  0.0023  109 LEU   A C   
2409 O  O   . LEU   A 109 ? 0.1342 0.1242 0.1806 -0.0030 0.0006  -0.0012 109 LEU   A O   
2410 C  CB  . LEU   A 109 ? 0.1622 0.1481 0.1845 0.0095  -0.0012 0.0251  109 LEU   A CB  
2411 C  CG  . LEU   A 109 ? 0.1494 0.1517 0.1999 0.0065  0.0089  0.0259  109 LEU   A CG  
2412 C  CD1 . LEU   A 109 ? 0.1541 0.1405 0.2092 0.0008  0.0122  0.0118  109 LEU   A CD1 
2413 C  CD2 . LEU   A 109 ? 0.1533 0.1677 0.2232 0.0028  0.0042  0.0300  109 LEU   A CD2 
2426 N  N   . LYS   A 110 ? 0.1414 0.1261 0.1724 -0.0060 -0.0080 0.0018  110 LYS   A N   
2427 C  CA  . LYS   A 110 ? 0.1349 0.1223 0.1932 -0.0072 -0.0064 0.0141  110 LYS   A CA  
2428 C  C   . LYS   A 110 ? 0.1364 0.1117 0.1801 -0.0067 0.0017  0.0081  110 LYS   A C   
2429 O  O   . LYS   A 110 ? 0.1358 0.1200 0.1749 -0.0044 0.0031  0.0044  110 LYS   A O   
2430 C  CB  . LYS   A 110 ? 0.1455 0.1310 0.2092 -0.0091 -0.0135 -0.0024 110 LYS   A CB  
2431 C  CG  . LYS   A 110 ? 0.1395 0.1295 0.2152 -0.0020 -0.0043 -0.0049 110 LYS   A CG  
2432 C  CD  . LYS   A 110 ? 0.1513 0.1286 0.2302 -0.0083 -0.0049 -0.0108 110 LYS   A CD  
2433 C  CE  . LYS   A 110 ? 0.1621 0.1319 0.2456 -0.0084 0.0145  -0.0074 110 LYS   A CE  
2434 N  NZ  . LYS   A 110 ? 0.1610 0.1388 0.2595 -0.0162 0.0097  -0.0106 110 LYS   A NZ  
2448 N  N   . SER   A 111 ? 0.1381 0.1182 0.1767 -0.0033 -0.0030 0.0029  111 SER   A N   
2449 C  CA  . SER   A 111 ? 0.1342 0.1256 0.1684 -0.0031 0.0091  0.0018  111 SER   A CA  
2450 C  C   . SER   A 111 ? 0.1271 0.1186 0.1677 -0.0069 -0.0001 0.0119  111 SER   A C   
2451 O  O   . SER   A 111 ? 0.1368 0.1208 0.1768 -0.0046 0.0024  0.0113  111 SER   A O   
2452 C  CB  . SER   A 111 ? 0.1515 0.1538 0.1887 -0.0011 0.0114  -0.0157 111 SER   A CB  
2453 O  OG  . SER   A 111 ? 0.1912 0.1693 0.1993 0.0047  0.0211  -0.0212 111 SER   A OG  
2459 N  N   . ALA   A 112 ? 0.1332 0.1135 0.1608 -0.0030 0.0097  0.0074  112 ALA   A N   
2460 C  CA  . ALA   A 112 ? 0.1311 0.1138 0.1587 -0.0085 0.0131  0.0036  112 ALA   A CA  
2461 C  C   . ALA   A 112 ? 0.1227 0.1091 0.1644 -0.0051 0.0047  0.0072  112 ALA   A C   
2462 O  O   . ALA   A 112 ? 0.1269 0.1152 0.1740 -0.0125 0.0059  0.0105  112 ALA   A O   
2463 C  CB  . ALA   A 112 ? 0.1422 0.1175 0.1628 -0.0026 0.0072  0.0120  112 ALA   A CB  
2469 N  N   . TYR   A 113 ? 0.1214 0.1160 0.1573 -0.0034 0.0048  0.0096  113 TYR   A N   
2470 C  CA  . TYR   A 113 ? 0.1177 0.1166 0.1595 -0.0055 0.0039  0.0190  113 TYR   A CA  
2471 C  C   . TYR   A 113 ? 0.1127 0.1126 0.1604 -0.0143 0.0061  0.0117  113 TYR   A C   
2472 O  O   . TYR   A 113 ? 0.1194 0.1201 0.1681 -0.0047 0.0143  0.0103  113 TYR   A O   
2473 C  CB  . TYR   A 113 ? 0.1182 0.1216 0.1668 -0.0047 -0.0025 0.0168  113 TYR   A CB  
2474 C  CG  . TYR   A 113 ? 0.1223 0.1237 0.1660 -0.0075 0.0088  0.0122  113 TYR   A CG  
2475 C  CD1 . TYR   A 113 ? 0.1267 0.1381 0.1703 -0.0027 0.0088  0.0169  113 TYR   A CD1 
2476 C  CD2 . TYR   A 113 ? 0.1290 0.1311 0.1635 -0.0126 -0.0004 0.0122  113 TYR   A CD2 
2477 C  CE1 . TYR   A 113 ? 0.1294 0.1507 0.1751 0.0022  0.0045  0.0082  113 TYR   A CE1 
2478 C  CE2 . TYR   A 113 ? 0.1280 0.1364 0.1695 -0.0103 0.0024  0.0244  113 TYR   A CE2 
2479 C  CZ  . TYR   A 113 ? 0.1217 0.1340 0.1803 -0.0012 0.0027  0.0199  113 TYR   A CZ  
2480 O  OH  . TYR   A 113 ? 0.1244 0.1445 0.2232 0.0071  -0.0022 0.0098  113 TYR   A OH  
2490 N  N   . GLU   A 114 ? 0.1151 0.1127 0.1713 -0.0076 0.0090  0.0135  114 GLU   A N   
2491 C  CA  . GLU   A 114 ? 0.1201 0.1143 0.1885 -0.0003 0.0066  0.0127  114 GLU   A CA  
2492 C  C   . GLU   A 114 ? 0.1185 0.1166 0.1765 -0.0060 0.0131  0.0134  114 GLU   A C   
2493 O  O   . GLU   A 114 ? 0.1281 0.1198 0.1722 0.0005  0.0072  0.0185  114 GLU   A O   
2494 C  CB  . GLU   A 114 ? 0.1225 0.1108 0.1908 -0.0007 0.0072  0.0099  114 GLU   A CB  
2495 C  CG  . GLU   A 114 ? 0.1279 0.1214 0.1978 0.0005  0.0074  0.0058  114 GLU   A CG  
2496 C  CD  . GLU   A 114 ? 0.1375 0.1211 0.2010 -0.0029 0.0033  0.0018  114 GLU   A CD  
2497 O  OE1 . GLU   A 114 ? 0.1362 0.1263 0.2087 -0.0110 0.0127  -0.0034 114 GLU   A OE1 
2498 O  OE2 . GLU   A 114 ? 0.1625 0.1300 0.2148 -0.0138 0.0038  -0.0076 114 GLU   A OE2 
2505 N  N   . ASN   A 115 ? 0.1191 0.1184 0.1673 -0.0085 0.0081  0.0038  115 ASN   A N   
2506 C  CA  . ASN   A 115 ? 0.1221 0.1225 0.1683 -0.0061 0.0123  0.0143  115 ASN   A CA  
2507 C  C   . ASN   A 115 ? 0.1206 0.1232 0.1639 -0.0094 0.0082  0.0114  115 ASN   A C   
2508 O  O   . ASN   A 115 ? 0.1254 0.1284 0.1643 -0.0088 0.0122  0.0169  115 ASN   A O   
2509 C  CB  . ASN   A 115 ? 0.1365 0.1319 0.1633 -0.0082 0.0072  0.0107  115 ASN   A CB  
2510 C  CG  . ASN   A 115 ? 0.1271 0.1469 0.1697 -0.0181 0.0141  0.0141  115 ASN   A CG  
2511 O  OD1 . ASN   A 115 ? 0.1327 0.2409 0.1966 -0.0162 0.0240  0.0246  115 ASN   A OD1 
2512 N  ND2 . ASN   A 115 ? 0.1335 0.1258 0.1658 -0.0119 0.0187  0.0129  115 ASN   A ND2 
2519 N  N   . PHE   A 116 ? 0.1177 0.1232 0.1613 -0.0020 0.0104  0.0156  116 PHE   A N   
2520 C  CA  . PHE   A 116 ? 0.1210 0.1248 0.1606 -0.0046 0.0162  0.0190  116 PHE   A CA  
2521 C  C   . PHE   A 116 ? 0.1222 0.1340 0.1755 -0.0080 0.0120  0.0291  116 PHE   A C   
2522 O  O   . PHE   A 116 ? 0.1218 0.1424 0.1781 -0.0009 0.0066  0.0344  116 PHE   A O   
2523 C  CB  . PHE   A 116 ? 0.1254 0.1202 0.1719 -0.0078 0.0174  0.0184  116 PHE   A CB  
2524 C  CG  . PHE   A 116 ? 0.1231 0.1177 0.1575 -0.0083 0.0030  0.0168  116 PHE   A CG  
2525 C  CD1 . PHE   A 116 ? 0.1231 0.1198 0.1630 -0.0047 0.0077  0.0167  116 PHE   A CD1 
2526 C  CD2 . PHE   A 116 ? 0.1275 0.1238 0.1749 -0.0095 0.0149  0.0260  116 PHE   A CD2 
2527 C  CE1 . PHE   A 116 ? 0.1282 0.1224 0.1682 -0.0145 0.0067  0.0068  116 PHE   A CE1 
2528 C  CE2 . PHE   A 116 ? 0.1267 0.1234 0.1898 -0.0056 0.0099  0.0154  116 PHE   A CE2 
2529 C  CZ  . PHE   A 116 ? 0.1316 0.1171 0.1652 -0.0023 0.0044  0.0133  116 PHE   A CZ  
2539 N  N   . ASN   A 117 ? 0.1253 0.1281 0.1823 -0.0086 0.0098  0.0236  117 ASN   A N   
2540 C  CA  . ASN   A 117 ? 0.1259 0.1236 0.1910 -0.0061 0.0179  0.0321  117 ASN   A CA  
2541 C  C   . ASN   A 117 ? 0.1282 0.1378 0.1942 -0.0022 0.0168  0.0278  117 ASN   A C   
2542 O  O   . ASN   A 117 ? 0.1360 0.1443 0.2049 -0.0015 0.0002  0.0402  117 ASN   A O   
2543 C  CB  . ASN   A 117 ? 0.1202 0.1274 0.1930 -0.0052 0.0123  0.0270  117 ASN   A CB  
2544 C  CG  . ASN   A 117 ? 0.1239 0.1283 0.1947 -0.0021 0.0153  0.0328  117 ASN   A CG  
2545 O  OD1 . ASN   A 117 ? 0.1292 0.1487 0.2056 -0.0099 0.0173  0.0221  117 ASN   A OD1 
2546 N  ND2 . ASN   A 117 ? 0.1198 0.1275 0.1916 -0.0053 0.0078  0.0296  117 ASN   A ND2 
2553 N  N   . GLN   A 118 ? 0.1195 0.1382 0.1941 -0.0073 0.0042  0.0335  118 GLN   A N   
2554 C  CA  . GLN   A 118 ? 0.1283 0.1476 0.2051 -0.0097 0.0056  0.0259  118 GLN   A CA  
2555 C  C   . GLN   A 118 ? 0.1303 0.1552 0.1946 -0.0080 0.0044  0.0312  118 GLN   A C   
2556 O  O   . GLN   A 118 ? 0.1286 0.1856 0.2147 0.0023  -0.0107 0.0175  118 GLN   A O   
2557 C  CB  . GLN   A 118 ? 0.1262 0.1447 0.2150 -0.0031 0.0109  0.0242  118 GLN   A CB  
2558 C  CG  . GLN   A 118 ? 0.1303 0.1458 0.2092 -0.0003 0.0096  0.0294  118 GLN   A CG  
2559 C  CD  . GLN   A 118 ? 0.1251 0.1500 0.2223 -0.0002 0.0105  0.0224  118 GLN   A CD  
2560 O  OE1 . GLN   A 118 ? 0.1300 0.1671 0.2332 0.0069  -0.0040 0.0203  118 GLN   A OE1 
2561 N  NE2 . GLN   A 118 ? 0.1312 0.1509 0.2250 0.0015  0.0081  0.0287  118 GLN   A NE2 
2570 N  N   . HIS   A 119 ? 0.1315 0.1464 0.1791 -0.0052 -0.0043 0.0339  119 HIS   A N   
2571 C  CA  . HIS   A 119 ? 0.1405 0.1600 0.1773 0.0007  -0.0032 0.0363  119 HIS   A CA  
2572 C  C   . HIS   A 119 ? 0.1495 0.1650 0.1721 -0.0081 0.0051  0.0492  119 HIS   A C   
2573 O  O   . HIS   A 119 ? 0.1520 0.1699 0.1760 -0.0237 0.0028  0.0378  119 HIS   A O   
2574 C  CB  . HIS   A 119 ? 0.1411 0.1535 0.1904 0.0005  0.0165  0.0333  119 HIS   A CB  
2575 C  CG  . HIS   A 119 ? 0.1500 0.1574 0.2291 0.0028  0.0182  0.0445  119 HIS   A CG  
2576 N  ND1 . HIS   A 119 ? 0.1616 0.1678 0.2790 -0.0066 0.0088  0.0306  119 HIS   A ND1 
2577 C  CD2 . HIS   A 119 ? 0.1613 0.1632 0.2478 0.0140  0.0390  0.0607  119 HIS   A CD2 
2578 C  CE1 . HIS   A 119 ? 0.1574 0.1673 0.2959 -0.0083 0.0265  0.0483  119 HIS   A CE1 
2579 N  NE2 . HIS   A 119 ? 0.1664 0.1710 0.2830 0.0060  0.0472  0.0607  119 HIS   A NE2 
2587 N  N   A GLU   A 120 ? 0.1591 0.1834 0.1796 -0.0070 0.0006  0.0597  120 GLU   A N   
2588 N  N   B GLU   A 120 ? 0.1597 0.1841 0.1810 -0.0060 0.0053  0.0605  120 GLU   A N   
2589 C  CA  A GLU   A 120 ? 0.1728 0.2055 0.1956 0.0002  -0.0037 0.0867  120 GLU   A CA  
2590 C  CA  B GLU   A 120 ? 0.1744 0.2070 0.1978 0.0024  0.0058  0.0880  120 GLU   A CA  
2591 C  C   A GLU   A 120 ? 0.1602 0.1940 0.1774 -0.0075 0.0002  0.0838  120 GLU   A C   
2592 C  C   B GLU   A 120 ? 0.1619 0.1978 0.1794 -0.0042 0.0048  0.0808  120 GLU   A C   
2593 O  O   A GLU   A 120 ? 0.1572 0.1865 0.1844 -0.0090 0.0028  0.0876  120 GLU   A O   
2594 O  O   B GLU   A 120 ? 0.1597 0.1959 0.1890 -0.0024 0.0060  0.0764  120 GLU   A O   
2595 C  CB  A GLU   A 120 ? 0.2095 0.2438 0.2536 0.0119  -0.0089 0.1078  120 GLU   A CB  
2596 C  CB  B GLU   A 120 ? 0.2120 0.2438 0.2548 0.0147  0.0078  0.1149  120 GLU   A CB  
2597 C  CG  A GLU   A 120 ? 0.2549 0.2791 0.3454 0.0261  -0.0098 0.1048  120 GLU   A CG  
2598 C  CG  B GLU   A 120 ? 0.2582 0.2795 0.3482 0.0294  0.0105  0.1133  120 GLU   A CG  
2599 C  CD  A GLU   A 120 ? 0.2905 0.3085 0.4293 0.0390  -0.0041 0.0953  120 GLU   A CD  
2600 C  CD  B GLU   A 120 ? 0.2949 0.3089 0.4309 0.0434  0.0182  0.1060  120 GLU   A CD  
2601 O  OE1 A GLU   A 120 ? 0.3066 0.3242 0.4554 0.0392  -0.0017 0.0909  120 GLU   A OE1 
2602 O  OE1 B GLU   A 120 ? 0.3099 0.3232 0.4517 0.0454  0.0238  0.1032  120 GLU   A OE1 
2603 O  OE2 A GLU   A 120 ? 0.3118 0.3217 0.4667 0.0386  -0.0017 0.0914  120 GLU   A OE2 
2604 O  OE2 B GLU   A 120 ? 0.3165 0.3220 0.4698 0.0446  0.0191  0.1043  120 GLU   A OE2 
2617 N  N   . VAL   A 121 ? 0.1567 0.1986 0.1637 -0.0044 0.0074  0.0753  121 VAL   A N   
2618 C  CA  . VAL   A 121 ? 0.1619 0.2084 0.1566 -0.0051 0.0204  0.0779  121 VAL   A CA  
2619 C  C   . VAL   A 121 ? 0.1464 0.1887 0.1417 -0.0131 0.0141  0.0553  121 VAL   A C   
2620 O  O   . VAL   A 121 ? 0.1498 0.1909 0.1585 -0.0205 -0.0056 0.0454  121 VAL   A O   
2621 C  CB  . VAL   A 121 ? 0.1987 0.2488 0.1974 0.0076  0.0323  0.0848  121 VAL   A CB  
2622 C  CG1 . VAL   A 121 ? 0.2024 0.2699 0.2012 0.0151  0.0476  0.0834  121 VAL   A CG1 
2623 C  CG2 . VAL   A 121 ? 0.2261 0.2657 0.2378 0.0016  0.0269  0.0729  121 VAL   A CG2 
2634 N  N   . LEU   A 122 ? 0.1341 0.1617 0.1524 -0.0129 0.0072  0.0449  122 LEU   A N   
2635 C  CA  . LEU   A 122 ? 0.1398 0.1502 0.1498 -0.0166 0.0175  0.0457  122 LEU   A CA  
2636 C  C   . LEU   A 122 ? 0.1369 0.1477 0.1431 -0.0187 0.0092  0.0372  122 LEU   A C   
2637 O  O   . LEU   A 122 ? 0.1391 0.1554 0.1848 -0.0248 0.0079  0.0399  122 LEU   A O   
2638 C  CB  . LEU   A 122 ? 0.1570 0.1566 0.1861 -0.0034 0.0048  0.0417  122 LEU   A CB  
2639 C  CG  . LEU   A 122 ? 0.1614 0.1598 0.1649 -0.0092 0.0126  0.0375  122 LEU   A CG  
2640 C  CD1 . LEU   A 122 ? 0.1754 0.1600 0.1807 -0.0172 0.0219  0.0374  122 LEU   A CD1 
2641 C  CD2 . LEU   A 122 ? 0.1679 0.1465 0.1519 -0.0048 0.0240  0.0311  122 LEU   A CD2 
2653 N  N   . LEU   A 123 ? 0.1327 0.1478 0.1504 -0.0197 0.0063  0.0352  123 LEU   A N   
2654 C  CA  . LEU   A 123 ? 0.1297 0.1435 0.1439 -0.0120 0.0044  0.0341  123 LEU   A CA  
2655 C  C   . LEU   A 123 ? 0.1185 0.1436 0.1480 -0.0172 0.0030  0.0347  123 LEU   A C   
2656 O  O   . LEU   A 123 ? 0.1268 0.1546 0.1538 -0.0262 -0.0005 0.0347  123 LEU   A O   
2657 C  CB  . LEU   A 123 ? 0.1377 0.1551 0.1460 -0.0147 0.0087  0.0362  123 LEU   A CB  
2658 C  CG  . LEU   A 123 ? 0.1401 0.1681 0.1535 -0.0106 0.0092  0.0249  123 LEU   A CG  
2659 C  CD1 . LEU   A 123 ? 0.1480 0.1841 0.1706 0.0003  0.0056  0.0181  123 LEU   A CD1 
2660 C  CD2 . LEU   A 123 ? 0.1481 0.1761 0.1669 -0.0054 0.0029  0.0212  123 LEU   A CD2 
2672 N  N   . ALA   A 124 ? 0.1231 0.1371 0.1401 -0.0180 0.0071  0.0344  124 ALA   A N   
2673 C  CA  . ALA   A 124 ? 0.1191 0.1295 0.1409 -0.0108 0.0095  0.0280  124 ALA   A CA  
2674 C  C   . ALA   A 124 ? 0.1199 0.1291 0.1433 -0.0115 0.0044  0.0296  124 ALA   A C   
2675 O  O   . ALA   A 124 ? 0.1190 0.1412 0.1586 -0.0116 0.0095  0.0343  124 ALA   A O   
2676 C  CB  . ALA   A 124 ? 0.1287 0.1337 0.1665 -0.0092 0.0008  0.0299  124 ALA   A CB  
2682 N  N   A PRO   A 125 ? 0.1213 0.1351 0.1488 -0.0085 0.0052  0.0361  125 PRO   A N   
2683 N  N   B PRO   A 125 ? 0.1159 0.1233 0.1495 -0.0069 0.0025  0.0304  125 PRO   A N   
2684 C  CA  A PRO   A 125 ? 0.1258 0.1388 0.1555 -0.0072 -0.0002 0.0321  125 PRO   A CA  
2685 C  CA  B PRO   A 125 ? 0.1154 0.1176 0.1560 -0.0026 -0.0018 0.0252  125 PRO   A CA  
2686 C  C   A PRO   A 125 ? 0.1274 0.1463 0.1608 -0.0084 -0.0039 0.0332  125 PRO   A C   
2687 C  C   B PRO   A 125 ? 0.1093 0.1167 0.1609 -0.0078 0.0045  0.0213  125 PRO   A C   
2688 O  O   A PRO   A 125 ? 0.1300 0.1488 0.1679 -0.0070 -0.0021 0.0323  125 PRO   A O   
2689 O  O   B PRO   A 125 ? 0.1080 0.1195 0.1730 -0.0048 0.0039  0.0164  125 PRO   A O   
2690 C  CB  A PRO   A 125 ? 0.1371 0.1383 0.1515 -0.0125 0.0024  0.0277  125 PRO   A CB  
2691 C  CB  B PRO   A 125 ? 0.1319 0.1196 0.1536 -0.0092 -0.0065 0.0207  125 PRO   A CB  
2692 C  CG  A PRO   A 125 ? 0.1385 0.1409 0.1561 -0.0159 0.0059  0.0290  125 PRO   A CG  
2693 C  CG  B PRO   A 125 ? 0.1339 0.1215 0.1534 -0.0170 0.0004  0.0199  125 PRO   A CG  
2694 C  CD  A PRO   A 125 ? 0.1270 0.1433 0.1548 -0.0147 0.0115  0.0393  125 PRO   A CD  
2695 C  CD  B PRO   A 125 ? 0.1211 0.1273 0.1516 -0.0153 0.0064  0.0292  125 PRO   A CD  
2710 N  N   A LEU   A 126 ? 0.1280 0.1485 0.1629 -0.0056 -0.0062 0.0286  126 LEU   A N   
2711 N  N   B LEU   A 126 ? 0.1072 0.1143 0.1605 -0.0044 0.0088  0.0170  126 LEU   A N   
2712 C  CA  A LEU   A 126 ? 0.1250 0.1536 0.1584 -0.0112 0.0024  0.0226  126 LEU   A CA  
2713 C  CA  B LEU   A 126 ? 0.1160 0.1149 0.1615 0.0025  0.0089  0.0184  126 LEU   A CA  
2714 C  C   A LEU   A 126 ? 0.1271 0.1518 0.1550 -0.0053 0.0027  0.0189  126 LEU   A C   
2715 C  C   B LEU   A 126 ? 0.1298 0.1235 0.1687 0.0025  0.0043  0.0230  126 LEU   A C   
2716 O  O   A LEU   A 126 ? 0.1266 0.1515 0.1625 -0.0055 0.0020  0.0215  126 LEU   A O   
2717 O  O   B LEU   A 126 ? 0.1452 0.1283 0.2137 -0.0019 0.0163  0.0236  126 LEU   A O   
2718 C  CB  A LEU   A 126 ? 0.1271 0.1594 0.1702 -0.0194 0.0026  0.0100  126 LEU   A CB  
2719 C  CB  B LEU   A 126 ? 0.1232 0.1170 0.1750 0.0043  0.0018  0.0135  126 LEU   A CB  
2720 C  CG  A LEU   A 126 ? 0.1201 0.1631 0.1816 -0.0190 0.0120  -0.0040 126 LEU   A CG  
2721 C  CG  B LEU   A 126 ? 0.1308 0.1309 0.1965 0.0036  -0.0006 0.0127  126 LEU   A CG  
2722 C  CD1 A LEU   A 126 ? 0.1248 0.1693 0.2097 -0.0133 0.0072  -0.0143 126 LEU   A CD1 
2723 C  CD1 B LEU   A 126 ? 0.1386 0.1377 0.2276 0.0118  -0.0008 0.0029  126 LEU   A CD1 
2724 C  CD2 A LEU   A 126 ? 0.1193 0.1638 0.1779 -0.0206 0.0127  0.0042  126 LEU   A CD2 
2725 C  CD2 B LEU   A 126 ? 0.1434 0.1332 0.1817 -0.0016 0.0030  0.0199  126 LEU   A CD2 
2748 N  N   A LEU   A 127 ? 0.1223 0.1521 0.1351 -0.0046 0.0038  0.0114  127 LEU   A N   
2749 N  N   B LEU   A 127 ? 0.1316 0.1353 0.1366 -0.0085 0.0011  0.0176  127 LEU   A N   
2750 C  CA  A LEU   A 127 ? 0.1262 0.1486 0.1304 -0.0060 0.0015  0.0137  127 LEU   A CA  
2751 C  CA  B LEU   A 127 ? 0.1323 0.1425 0.1308 -0.0143 0.0041  0.0212  127 LEU   A CA  
2752 C  C   A LEU   A 127 ? 0.1316 0.1447 0.1210 -0.0030 0.0115  0.0153  127 LEU   A C   
2753 C  C   B LEU   A 127 ? 0.1298 0.1339 0.1459 -0.0164 -0.0022 0.0105  127 LEU   A C   
2754 O  O   A LEU   A 127 ? 0.1402 0.1576 0.1275 -0.0096 0.0140  0.0154  127 LEU   A O   
2755 O  O   B LEU   A 127 ? 0.1330 0.1355 0.1391 -0.0343 -0.0033 0.0066  127 LEU   A O   
2756 C  CB  A LEU   A 127 ? 0.1239 0.1451 0.1391 -0.0006 0.0057  0.0163  127 LEU   A CB  
2757 C  CB  B LEU   A 127 ? 0.1384 0.1637 0.1337 -0.0156 0.0126  0.0247  127 LEU   A CB  
2758 C  CG  A LEU   A 127 ? 0.1292 0.1470 0.1442 -0.0011 -0.0048 0.0227  127 LEU   A CG  
2759 C  CG  B LEU   A 127 ? 0.1471 0.1835 0.1475 -0.0127 0.0089  0.0283  127 LEU   A CG  
2760 C  CD1 A LEU   A 127 ? 0.1267 0.1354 0.1491 -0.0125 -0.0035 0.0167  127 LEU   A CD1 
2761 C  CD1 B LEU   A 127 ? 0.1513 0.1941 0.1723 -0.0106 0.0095  0.0231  127 LEU   A CD1 
2762 C  CD2 A LEU   A 127 ? 0.1397 0.1506 0.1717 0.0074  -0.0151 0.0238  127 LEU   A CD2 
2763 C  CD2 B LEU   A 127 ? 0.1638 0.1888 0.1544 -0.0093 -0.0058 0.0242  127 LEU   A CD2 
2786 N  N   A SER   A 128 ? 0.1380 0.1395 0.1230 -0.0038 0.0046  0.0195  128 SER   A N   
2787 N  N   B SER   A 128 ? 0.1312 0.1295 0.1508 -0.0171 -0.0069 0.0059  128 SER   A N   
2788 C  CA  A SER   A 128 ? 0.1404 0.1368 0.1127 -0.0085 0.0062  0.0174  128 SER   A CA  
2789 C  CA  B SER   A 128 ? 0.1379 0.1325 0.1454 -0.0049 -0.0004 0.0003  128 SER   A CA  
2790 C  C   A SER   A 128 ? 0.1447 0.1450 0.1099 -0.0074 0.0014  0.0139  128 SER   A C   
2791 C  C   B SER   A 128 ? 0.1384 0.1412 0.1470 -0.0025 -0.0013 0.0064  128 SER   A C   
2792 O  O   A SER   A 128 ? 0.1559 0.1530 0.1077 -0.0106 0.0004  0.0089  128 SER   A O   
2793 O  O   B SER   A 128 ? 0.1417 0.1557 0.1548 0.0040  -0.0003 0.0260  128 SER   A O   
2794 C  CB  A SER   A 128 ? 0.1407 0.1329 0.1164 -0.0149 -0.0080 0.0228  128 SER   A CB  
2795 C  CB  B SER   A 128 ? 0.1445 0.1341 0.1446 0.0037  -0.0029 0.0032  128 SER   A CB  
2796 O  OG  A SER   A 128 ? 0.1344 0.1352 0.1247 -0.0087 -0.0048 0.0149  128 SER   A OG  
2797 O  OG  B SER   A 128 ? 0.1421 0.1418 0.1510 0.0100  -0.0006 0.0055  128 SER   A OG  
2808 N  N   A ALA   A 129 ? 0.1400 0.1508 0.1240 -0.0050 -0.0021 0.0186  129 ALA   A N   
2809 N  N   B ALA   A 129 ? 0.1357 0.1449 0.1469 0.0000  -0.0054 -0.0038 129 ALA   A N   
2810 C  CA  A ALA   A 129 ? 0.1453 0.1480 0.1422 -0.0148 0.0012  0.0179  129 ALA   A CA  
2811 C  CA  B ALA   A 129 ? 0.1394 0.1508 0.1711 -0.0055 0.0033  -0.0147 129 ALA   A CA  
2812 C  C   A ALA   A 129 ? 0.1645 0.1433 0.1272 -0.0248 0.0047  -0.0030 129 ALA   A C   
2813 C  C   B ALA   A 129 ? 0.1557 0.1603 0.1831 -0.0014 0.0028  -0.0051 129 ALA   A C   
2814 O  O   A ALA   A 129 ? 0.1784 0.1595 0.1121 -0.0338 -0.0002 0.0119  129 ALA   A O   
2815 O  O   B ALA   A 129 ? 0.1607 0.1639 0.1751 -0.0086 0.0077  0.0006  129 ALA   A O   
2816 C  CB  A ALA   A 129 ? 0.1510 0.1573 0.1705 -0.0033 -0.0000 0.0381  129 ALA   A CB  
2817 C  CB  B ALA   A 129 ? 0.1414 0.1584 0.1954 -0.0061 0.0141  -0.0180 129 ALA   A CB  
2828 N  N   A GLY   A 130 ? 0.1783 0.1315 0.1545 -0.0207 0.0370  -0.0236 130 GLY   A N   
2829 N  N   B GLY   A 130 ? 0.1746 0.1686 0.2000 0.0113  -0.0032 -0.0100 130 GLY   A N   
2830 C  CA  A GLY   A 130 ? 0.2003 0.1348 0.1892 -0.0160 0.0429  -0.0148 130 GLY   A CA  
2831 C  CA  B GLY   A 130 ? 0.1812 0.1701 0.2119 0.0149  -0.0144 -0.0162 130 GLY   A CA  
2832 C  C   A GLY   A 130 ? 0.1978 0.1270 0.2074 -0.0090 0.0411  0.0017  130 GLY   A C   
2833 C  C   B GLY   A 130 ? 0.1853 0.1680 0.2302 0.0153  -0.0076 -0.0074 130 GLY   A C   
2834 O  O   A GLY   A 130 ? 0.1756 0.1192 0.2039 -0.0113 0.0258  0.0085  130 GLY   A O   
2835 O  O   B GLY   A 130 ? 0.1749 0.1712 0.2465 0.0156  -0.0096 -0.0008 130 GLY   A O   
2842 N  N   A ILE   A 131 ? 0.2084 0.1262 0.2185 -0.0166 0.0411  -0.0027 131 ILE   A N   
2843 N  N   B ILE   A 131 ? 0.1911 0.1660 0.2490 0.0071  -0.0009 -0.0037 131 ILE   A N   
2844 C  CA  A ILE   A 131 ? 0.1984 0.1248 0.1970 -0.0174 0.0204  0.0034  131 ILE   A CA  
2845 C  CA  B ILE   A 131 ? 0.1833 0.1568 0.2447 0.0112  -0.0064 0.0060  131 ILE   A CA  
2846 C  C   A ILE   A 131 ? 0.1803 0.1346 0.1676 -0.0172 0.0067  0.0007  131 ILE   A C   
2847 C  C   B ILE   A 131 ? 0.1753 0.1617 0.2264 0.0120  -0.0133 0.0159  131 ILE   A C   
2848 O  O   A ILE   A 131 ? 0.1817 0.1440 0.1557 -0.0159 0.0027  0.0023  131 ILE   A O   
2849 O  O   B ILE   A 131 ? 0.1885 0.1787 0.2348 0.0153  -0.0157 0.0204  131 ILE   A O   
2850 C  CB  A ILE   A 131 ? 0.2076 0.1246 0.2154 -0.0156 0.0106  -0.0005 131 ILE   A CB  
2851 C  CB  B ILE   A 131 ? 0.1904 0.1564 0.2520 0.0144  -0.0060 0.0017  131 ILE   A CB  
2852 C  CG1 A ILE   A 131 ? 0.2167 0.1358 0.2063 -0.0100 -0.0057 -0.0038 131 ILE   A CG1 
2853 C  CG1 B ILE   A 131 ? 0.2010 0.1602 0.2383 0.0162  -0.0059 0.0057  131 ILE   A CG1 
2854 C  CG2 A ILE   A 131 ? 0.2112 0.1197 0.2397 -0.0210 0.0139  -0.0108 131 ILE   A CG2 
2855 C  CG2 B ILE   A 131 ? 0.1939 0.1573 0.2731 0.0145  0.0024  -0.0097 131 ILE   A CG2 
2856 C  CD1 A ILE   A 131 ? 0.2196 0.1382 0.2109 -0.0085 -0.0174 -0.0118 131 ILE   A CD1 
2857 C  CD1 B ILE   A 131 ? 0.2083 0.1607 0.2360 0.0136  -0.0095 0.0003  131 ILE   A CD1 
2880 N  N   A PHE   A 132 ? 0.1720 0.1351 0.1605 -0.0133 0.0020  0.0074  132 PHE   A N   
2881 N  N   B PHE   A 132 ? 0.1557 0.1465 0.1941 0.0130  -0.0097 0.0186  132 PHE   A N   
2882 C  CA  A PHE   A 132 ? 0.1722 0.1462 0.1518 -0.0117 0.0012  -0.0039 132 PHE   A CA  
2883 C  CA  B PHE   A 132 ? 0.1430 0.1496 0.1868 0.0084  -0.0088 0.0122  132 PHE   A CA  
2884 C  C   A PHE   A 132 ? 0.1705 0.1577 0.1515 -0.0150 -0.0057 0.0037  132 PHE   A C   
2885 C  C   B PHE   A 132 ? 0.1469 0.1600 0.1933 0.0201  -0.0163 0.0101  132 PHE   A C   
2886 O  O   A PHE   A 132 ? 0.1771 0.1740 0.1627 -0.0177 -0.0026 -0.0022 132 PHE   A O   
2887 O  O   B PHE   A 132 ? 0.1587 0.1822 0.1946 0.0208  -0.0125 0.0052  132 PHE   A O   
2888 C  CB  A PHE   A 132 ? 0.1773 0.1461 0.1453 -0.0101 -0.0023 -0.0078 132 PHE   A CB  
2889 C  CB  B PHE   A 132 ? 0.1356 0.1477 0.1539 0.0039  -0.0022 0.0213  132 PHE   A CB  
2890 C  CG  A PHE   A 132 ? 0.1786 0.1473 0.1288 -0.0027 0.0020  -0.0007 132 PHE   A CG  
2891 C  CG  B PHE   A 132 ? 0.1427 0.1492 0.1472 0.0143  -0.0092 0.0254  132 PHE   A CG  
2892 C  CD1 A PHE   A 132 ? 0.1860 0.1549 0.1359 0.0012  0.0030  -0.0034 132 PHE   A CD1 
2893 C  CD1 B PHE   A 132 ? 0.1450 0.1606 0.1614 0.0169  -0.0050 0.0218  132 PHE   A CD1 
2894 C  CD2 A PHE   A 132 ? 0.1741 0.1585 0.1278 -0.0033 0.0047  0.0032  132 PHE   A CD2 
2895 C  CD2 B PHE   A 132 ? 0.1455 0.1687 0.1543 0.0210  -0.0143 0.0205  132 PHE   A CD2 
2896 C  CE1 A PHE   A 132 ? 0.1838 0.1600 0.1259 0.0028  0.0029  -0.0047 132 PHE   A CE1 
2897 C  CE1 B PHE   A 132 ? 0.1472 0.1689 0.1701 0.0120  -0.0138 0.0196  132 PHE   A CE1 
2898 C  CE2 A PHE   A 132 ? 0.1682 0.1662 0.1313 0.0056  0.0035  0.0028  132 PHE   A CE2 
2899 C  CE2 B PHE   A 132 ? 0.1451 0.1860 0.1743 0.0212  -0.0217 0.0159  132 PHE   A CE2 
2900 C  CZ  A PHE   A 132 ? 0.1764 0.1625 0.1205 0.0015  0.0019  -0.0001 132 PHE   A CZ  
2901 C  CZ  B PHE   A 132 ? 0.1454 0.1808 0.1792 0.0113  -0.0268 0.0159  132 PHE   A CZ  
2920 N  N   A GLY   A 133 ? 0.1687 0.1620 0.1526 -0.0130 -0.0205 0.0082  133 GLY   A N   
2921 N  N   B GLY   A 133 ? 0.1511 0.1588 0.1934 0.0136  -0.0191 0.0116  133 GLY   A N   
2922 C  CA  A GLY   A 133 ? 0.1766 0.1728 0.1628 -0.0149 -0.0290 0.0103  133 GLY   A CA  
2923 C  CA  B GLY   A 133 ? 0.1618 0.1683 0.2010 0.0132  -0.0221 0.0010  133 GLY   A CA  
2924 C  C   A GLY   A 133 ? 0.1844 0.1821 0.1779 -0.0116 -0.0495 0.0046  133 GLY   A C   
2925 C  C   B GLY   A 133 ? 0.1702 0.1769 0.2080 0.0014  -0.0337 -0.0034 133 GLY   A C   
2926 O  O   A GLY   A 133 ? 0.2060 0.2009 0.1875 -0.0155 -0.0603 -0.0098 133 GLY   A O   
2927 O  O   B GLY   A 133 ? 0.1895 0.1913 0.2096 -0.0136 -0.0361 -0.0094 133 GLY   A O   
2934 N  N   A ALA   A 134 ? 0.1767 0.1711 0.1816 -0.0109 -0.0410 0.0103  134 ALA   A N   
2935 N  N   B ALA   A 134 ? 0.1669 0.1648 0.2223 -0.0083 -0.0355 -0.0082 134 ALA   A N   
2936 C  CA  A ALA   A 134 ? 0.1704 0.1729 0.1915 -0.0077 -0.0452 0.0078  134 ALA   A CA  
2937 C  CA  B ALA   A 134 ? 0.1637 0.1594 0.2419 -0.0051 -0.0458 -0.0103 134 ALA   A CA  
2938 C  C   A ALA   A 134 ? 0.1679 0.1725 0.2014 -0.0107 -0.0358 0.0065  134 ALA   A C   
2939 C  C   B ALA   A 134 ? 0.1686 0.1553 0.2401 -0.0078 -0.0389 -0.0027 134 ALA   A C   
2940 O  O   A ALA   A 134 ? 0.1746 0.1732 0.2132 -0.0216 -0.0207 0.0038  134 ALA   A O   
2941 O  O   B ALA   A 134 ? 0.1743 0.1540 0.2628 -0.0134 -0.0132 -0.0112 134 ALA   A O   
2942 C  CB  A ALA   A 134 ? 0.1727 0.1742 0.1938 -0.0042 -0.0546 0.0073  134 ALA   A CB  
2943 C  CB  B ALA   A 134 ? 0.1634 0.1591 0.2589 -0.0028 -0.0538 -0.0160 134 ALA   A CB  
2954 N  N   A ASP   A 135 ? 0.1651 0.1733 0.2136 -0.0036 -0.0332 0.0077  135 ASP   A N   
2955 N  N   B ASP   A 135 ? 0.1794 0.1643 0.2370 -0.0159 -0.0452 0.0096  135 ASP   A N   
2956 C  CA  A ASP   A 135 ? 0.1664 0.1725 0.2230 -0.0091 -0.0417 0.0105  135 ASP   A CA  
2957 C  CA  B ASP   A 135 ? 0.1823 0.1681 0.2453 -0.0245 -0.0458 0.0123  135 ASP   A CA  
2958 C  C   A ASP   A 135 ? 0.1604 0.1662 0.2222 -0.0027 -0.0398 0.0186  135 ASP   A C   
2959 C  C   B ASP   A 135 ? 0.1680 0.1603 0.2335 -0.0180 -0.0363 0.0196  135 ASP   A C   
2960 O  O   A ASP   A 135 ? 0.1512 0.1604 0.2219 0.0026  -0.0396 0.0214  135 ASP   A O   
2961 O  O   B ASP   A 135 ? 0.1613 0.1584 0.2319 -0.0186 -0.0271 0.0265  135 ASP   A O   
2962 C  CB  A ASP   A 135 ? 0.1775 0.1871 0.2429 -0.0218 -0.0534 -0.0038 135 ASP   A CB  
2963 C  CB  B ASP   A 135 ? 0.1983 0.1927 0.2714 -0.0305 -0.0506 0.0014  135 ASP   A CB  
2964 C  CG  A ASP   A 135 ? 0.1972 0.2042 0.2636 -0.0340 -0.0537 -0.0148 135 ASP   A CG  
2965 C  CG  B ASP   A 135 ? 0.2117 0.2157 0.2993 -0.0299 -0.0500 -0.0054 135 ASP   A CG  
2966 O  OD1 A ASP   A 135 ? 0.1937 0.2094 0.2689 -0.0414 -0.0603 -0.0021 135 ASP   A OD1 
2967 O  OD1 B ASP   A 135 ? 0.2175 0.2159 0.3059 -0.0280 -0.0393 -0.0137 135 ASP   A OD1 
2968 O  OD2 A ASP   A 135 ? 0.2245 0.2198 0.2990 -0.0336 -0.0274 -0.0222 135 ASP   A OD2 
2969 O  OD2 B ASP   A 135 ? 0.2201 0.2327 0.3217 -0.0293 -0.0527 0.0002  135 ASP   A OD2 
2978 N  N   A PRO   A 136 ? 0.1586 0.1633 0.2287 -0.0029 -0.0286 0.0231  136 PRO   A N   
2979 N  N   B PRO   A 136 ? 0.1588 0.1593 0.2360 -0.0075 -0.0285 0.0296  136 PRO   A N   
2980 C  CA  A PRO   A 136 ? 0.1580 0.1604 0.2344 -0.0039 -0.0258 0.0209  136 PRO   A CA  
2981 C  CA  B PRO   A 136 ? 0.1526 0.1664 0.2444 -0.0012 -0.0185 0.0284  136 PRO   A CA  
2982 C  C   A PRO   A 136 ? 0.1411 0.1559 0.2464 -0.0104 -0.0217 0.0226  136 PRO   A C   
2983 C  C   B PRO   A 136 ? 0.1344 0.1745 0.2486 -0.0024 -0.0032 0.0294  136 PRO   A C   
2984 O  O   A PRO   A 136 ? 0.1375 0.1545 0.2455 -0.0129 -0.0170 0.0314  136 PRO   A O   
2985 O  O   B PRO   A 136 ? 0.1205 0.1740 0.2409 0.0019  0.0162  0.0348  136 PRO   A O   
2986 C  CB  A PRO   A 136 ? 0.1770 0.1652 0.2379 -0.0004 -0.0178 0.0125  136 PRO   A CB  
2987 C  CB  B PRO   A 136 ? 0.1722 0.1682 0.2572 0.0004  -0.0167 0.0212  136 PRO   A CB  
2988 C  CG  A PRO   A 136 ? 0.1821 0.1728 0.2454 0.0044  -0.0151 0.0039  136 PRO   A CG  
2989 C  CG  B PRO   A 136 ? 0.1813 0.1731 0.2665 0.0034  -0.0174 0.0229  136 PRO   A CG  
2990 C  CD  A PRO   A 136 ? 0.1697 0.1678 0.2348 0.0023  -0.0193 0.0212  136 PRO   A CD  
2991 C  CD  B PRO   A 136 ? 0.1641 0.1585 0.2440 -0.0022 -0.0209 0.0361  136 PRO   A CD  
3006 N  N   A ILE   A 137 ? 0.1399 0.1601 0.2634 -0.0107 -0.0298 0.0275  137 ILE   A N   
3007 N  N   B ILE   A 137 ? 0.1401 0.1828 0.2629 -0.0039 -0.0138 0.0310  137 ILE   A N   
3008 C  CA  A ILE   A 137 ? 0.1373 0.1672 0.2678 -0.0215 -0.0307 0.0361  137 ILE   A CA  
3009 C  CA  B ILE   A 137 ? 0.1461 0.1958 0.2637 -0.0122 -0.0205 0.0349  137 ILE   A CA  
3010 C  C   A ILE   A 137 ? 0.1374 0.1607 0.2478 -0.0231 -0.0379 0.0312  137 ILE   A C   
3011 C  C   B ILE   A 137 ? 0.1502 0.1939 0.2571 -0.0150 -0.0256 0.0207  137 ILE   A C   
3012 O  O   A ILE   A 137 ? 0.1356 0.1491 0.2556 -0.0234 -0.0291 0.0290  137 ILE   A O   
3013 O  O   B ILE   A 137 ? 0.1537 0.1947 0.2687 -0.0155 -0.0209 0.0204  137 ILE   A O   
3014 C  CB  A ILE   A 137 ? 0.1420 0.1877 0.2892 -0.0273 -0.0490 0.0423  137 ILE   A CB  
3015 C  CB  B ILE   A 137 ? 0.1553 0.2105 0.2779 -0.0176 -0.0395 0.0459  137 ILE   A CB  
3016 C  CG1 A ILE   A 137 ? 0.1584 0.2099 0.3102 -0.0233 -0.0405 0.0525  137 ILE   A CG1 
3017 C  CG1 B ILE   A 137 ? 0.1688 0.2269 0.2920 -0.0058 -0.0400 0.0600  137 ILE   A CG1 
3018 C  CG2 A ILE   A 137 ? 0.1454 0.1926 0.2963 -0.0318 -0.0662 0.0321  137 ILE   A CG2 
3019 C  CG2 B ILE   A 137 ? 0.1652 0.2119 0.2863 -0.0215 -0.0489 0.0412  137 ILE   A CG2 
3020 C  CD1 A ILE   A 137 ? 0.1710 0.2207 0.3238 -0.0178 -0.0315 0.0587  137 ILE   A CD1 
3021 C  CD1 B ILE   A 137 ? 0.1800 0.2324 0.3056 -0.0007 -0.0333 0.0667  137 ILE   A CD1 
3044 N  N   A HIS   A 138 ? 0.1437 0.1769 0.2272 -0.0154 -0.0350 0.0238  138 HIS   A N   
3045 N  N   B HIS   A 138 ? 0.1552 0.2008 0.2437 -0.0135 -0.0207 0.0054  138 HIS   A N   
3046 C  CA  A HIS   A 138 ? 0.1498 0.1836 0.2129 -0.0129 -0.0272 0.0252  138 HIS   A CA  
3047 C  CA  B HIS   A 138 ? 0.1569 0.1991 0.2339 -0.0153 -0.0164 0.0039  138 HIS   A CA  
3048 C  C   A HIS   A 138 ? 0.1438 0.1720 0.2022 -0.0094 -0.0240 0.0307  138 HIS   A C   
3049 C  C   B HIS   A 138 ? 0.1502 0.1816 0.2189 -0.0136 -0.0126 0.0147  138 HIS   A C   
3050 O  O   A HIS   A 138 ? 0.1531 0.1712 0.1979 -0.0077 -0.0275 0.0259  138 HIS   A O   
3051 O  O   B HIS   A 138 ? 0.1613 0.1834 0.2201 -0.0160 -0.0087 0.0067  138 HIS   A O   
3052 C  CB  A HIS   A 138 ? 0.1681 0.1985 0.2103 -0.0169 -0.0338 0.0263  138 HIS   A CB  
3053 C  CB  B HIS   A 138 ? 0.1678 0.2141 0.2391 -0.0198 -0.0283 -0.0085 138 HIS   A CB  
3054 C  CG  A HIS   A 138 ? 0.1883 0.2039 0.2099 -0.0189 -0.0263 0.0268  138 HIS   A CG  
3055 C  CG  B HIS   A 138 ? 0.1828 0.2256 0.2489 -0.0221 -0.0266 -0.0230 138 HIS   A CG  
3056 N  ND1 A HIS   A 138 ? 0.1982 0.2087 0.2210 -0.0202 -0.0191 0.0187  138 HIS   A ND1 
3057 N  ND1 B HIS   A 138 ? 0.1919 0.2322 0.2643 -0.0202 -0.0195 -0.0303 138 HIS   A ND1 
3058 C  CD2 A HIS   A 138 ? 0.1945 0.2075 0.2052 -0.0159 -0.0267 0.0307  138 HIS   A CD2 
3059 C  CD2 B HIS   A 138 ? 0.1866 0.2307 0.2508 -0.0201 -0.0313 -0.0239 138 HIS   A CD2 
3060 C  CE1 A HIS   A 138 ? 0.2026 0.2127 0.2161 -0.0153 -0.0176 0.0229  138 HIS   A CE1 
3061 C  CE1 B HIS   A 138 ? 0.1941 0.2343 0.2605 -0.0177 -0.0198 -0.0294 138 HIS   A CE1 
3062 N  NE2 A HIS   A 138 ? 0.2012 0.2116 0.2086 -0.0141 -0.0194 0.0290  138 HIS   A NE2 
3063 N  NE2 B HIS   A 138 ? 0.1924 0.2357 0.2570 -0.0184 -0.0260 -0.0270 138 HIS   A NE2 
3078 N  N   . SER   A 139 ? 0.1342 0.1645 0.2036 -0.0066 -0.0101 0.0260  139 SER   A N   
3079 C  CA  . SER   A 139 ? 0.1302 0.1626 0.1979 -0.0063 -0.0057 0.0272  139 SER   A CA  
3080 C  C   . SER   A 139 ? 0.1227 0.1465 0.2050 -0.0159 -0.0023 0.0216  139 SER   A C   
3081 O  O   . SER   A 139 ? 0.1223 0.1456 0.2103 -0.0132 -0.0043 0.0184  139 SER   A O   
3082 C  CB  . SER   A 139 ? 0.1262 0.1638 0.2026 -0.0046 -0.0073 0.0299  139 SER   A CB  
3083 O  OG  . SER   A 139 ? 0.1258 0.1539 0.2159 -0.0163 -0.0124 0.0350  139 SER   A OG  
3090 N  N   A LEU   A 140 ? 0.1216 0.1469 0.2085 -0.0162 -0.0024 0.0320  140 LEU   A N   
3091 N  N   B LEU   A 140 ? 0.1228 0.1530 0.2088 -0.0103 -0.0035 0.0245  140 LEU   A N   
3092 C  CA  A LEU   A 140 ? 0.1161 0.1407 0.2042 -0.0167 -0.0016 0.0320  140 LEU   A CA  
3093 C  CA  B LEU   A 140 ? 0.1200 0.1532 0.1996 -0.0087 -0.0020 0.0231  140 LEU   A CA  
3094 C  C   A LEU   A 140 ? 0.1171 0.1452 0.2046 -0.0213 -0.0020 0.0258  140 LEU   A C   
3095 C  C   B LEU   A 140 ? 0.1199 0.1553 0.1978 -0.0116 -0.0003 0.0253  140 LEU   A C   
3096 O  O   A LEU   A 140 ? 0.1176 0.1477 0.2171 -0.0162 -0.0053 0.0230  140 LEU   A O   
3097 O  O   B LEU   A 140 ? 0.1197 0.1554 0.2098 -0.0085 0.0015  0.0262  140 LEU   A O   
3098 C  CB  A LEU   A 140 ? 0.1140 0.1434 0.2109 -0.0165 -0.0018 0.0284  140 LEU   A CB  
3099 C  CB  B LEU   A 140 ? 0.1216 0.1611 0.2027 -0.0120 -0.0010 0.0162  140 LEU   A CB  
3100 C  CG  A LEU   A 140 ? 0.1169 0.1506 0.2173 -0.0202 0.0060  0.0321  140 LEU   A CG  
3101 C  CG  B LEU   A 140 ? 0.1249 0.1675 0.2064 -0.0186 0.0082  0.0170  140 LEU   A CG  
3102 C  CD1 A LEU   A 140 ? 0.1262 0.1549 0.2255 -0.0092 0.0016  0.0276  140 LEU   A CD1 
3103 C  CD1 B LEU   A 140 ? 0.1332 0.1671 0.2082 -0.0195 0.0189  0.0309  140 LEU   A CD1 
3104 C  CD2 A LEU   A 140 ? 0.1216 0.1510 0.2202 -0.0235 0.0159  0.0352  140 LEU   A CD2 
3105 C  CD2 B LEU   A 140 ? 0.1391 0.1720 0.2135 -0.0192 0.0029  0.0004  140 LEU   A CD2 
3128 N  N   A ARG   A 141 ? 0.1239 0.1551 0.2095 -0.0230 -0.0130 0.0132  141 ARG   A N   
3129 N  N   B ARG   A 141 ? 0.1268 0.1635 0.1953 -0.0091 -0.0085 0.0174  141 ARG   A N   
3130 C  CA  A ARG   A 141 ? 0.1395 0.1605 0.2189 -0.0272 -0.0135 0.0039  141 ARG   A CA  
3131 C  CA  B ARG   A 141 ? 0.1396 0.1674 0.2081 -0.0113 -0.0038 0.0080  141 ARG   A CA  
3132 C  C   A ARG   A 141 ? 0.1375 0.1489 0.2060 -0.0199 -0.0006 0.0055  141 ARG   A C   
3133 C  C   B ARG   A 141 ? 0.1410 0.1560 0.2097 -0.0075 -0.0026 0.0043  141 ARG   A C   
3134 O  O   A ARG   A 141 ? 0.1319 0.1400 0.2091 -0.0180 0.0116  0.0034  141 ARG   A O   
3135 O  O   B ARG   A 141 ? 0.1351 0.1434 0.2200 -0.0051 -0.0010 -0.0038 141 ARG   A O   
3136 C  CB  A ARG   A 141 ? 0.1536 0.1742 0.2339 -0.0344 -0.0288 -0.0112 141 ARG   A CB  
3137 C  CB  B ARG   A 141 ? 0.1436 0.1832 0.2111 -0.0167 0.0018  0.0025  141 ARG   A CB  
3138 C  CG  A ARG   A 141 ? 0.1861 0.1961 0.2574 -0.0368 -0.0411 -0.0218 141 ARG   A CG  
3139 C  CG  B ARG   A 141 ? 0.1645 0.1918 0.2126 -0.0163 0.0100  0.0083  141 ARG   A CG  
3140 C  CD  A ARG   A 141 ? 0.2019 0.2177 0.2681 -0.0431 -0.0443 -0.0169 141 ARG   A CD  
3141 C  CD  B ARG   A 141 ? 0.1742 0.1898 0.2120 -0.0214 -0.0004 0.0164  141 ARG   A CD  
3142 N  NE  A ARG   A 141 ? 0.2035 0.2319 0.2695 -0.0481 -0.0374 -0.0164 141 ARG   A NE  
3143 N  NE  B ARG   A 141 ? 0.1798 0.2031 0.2134 -0.0185 0.0024  0.0134  141 ARG   A NE  
3144 C  CZ  A ARG   A 141 ? 0.1998 0.2542 0.2707 -0.0574 -0.0299 -0.0138 141 ARG   A CZ  
3145 C  CZ  B ARG   A 141 ? 0.1849 0.2101 0.2170 -0.0239 0.0109  0.0200  141 ARG   A CZ  
3146 N  NH1 A ARG   A 141 ? 0.2020 0.2661 0.2816 -0.0529 -0.0334 -0.0140 141 ARG   A NH1 
3147 N  NH1 B ARG   A 141 ? 0.1899 0.2196 0.2181 -0.0273 0.0223  0.0117  141 ARG   A NH1 
3148 N  NH2 A ARG   A 141 ? 0.2036 0.2650 0.2719 -0.0534 -0.0234 -0.0146 141 ARG   A NH2 
3149 N  NH2 B ARG   A 141 ? 0.1861 0.2160 0.2150 -0.0204 0.0102  0.0237  141 ARG   A NH2 
3176 N  N   A VAL   A 142 ? 0.1244 0.1488 0.2001 -0.0182 -0.0015 0.0039  142 VAL   A N   
3177 N  N   B VAL   A 142 ? 0.1332 0.1537 0.2067 -0.0080 -0.0054 0.0060  142 VAL   A N   
3178 C  CA  A VAL   A 142 ? 0.1226 0.1461 0.1989 -0.0151 0.0152  0.0046  142 VAL   A CA  
3179 C  CA  B VAL   A 142 ? 0.1374 0.1489 0.2093 -0.0070 0.0056  0.0070  142 VAL   A CA  
3180 C  C   A VAL   A 142 ? 0.1152 0.1445 0.1949 -0.0140 0.0106  0.0088  142 VAL   A C   
3181 C  C   B VAL   A 142 ? 0.1239 0.1449 0.2053 -0.0089 0.0023  0.0092  142 VAL   A C   
3182 O  O   A VAL   A 142 ? 0.1228 0.1454 0.1946 -0.0086 0.0097  0.0116  142 VAL   A O   
3183 O  O   B VAL   A 142 ? 0.1310 0.1452 0.2158 -0.0021 -0.0041 0.0089  142 VAL   A O   
3184 C  CB  A VAL   A 142 ? 0.1240 0.1454 0.1881 -0.0086 0.0132  0.0015  142 VAL   A CB  
3185 C  CB  B VAL   A 142 ? 0.1510 0.1518 0.2022 -0.0015 -0.0012 0.0135  142 VAL   A CB  
3186 C  CG1 A VAL   A 142 ? 0.1214 0.1300 0.1808 -0.0119 0.0198  0.0064  142 VAL   A CG1 
3187 C  CG1 B VAL   A 142 ? 0.1521 0.1441 0.1933 -0.0058 0.0007  0.0145  142 VAL   A CG1 
3188 C  CG2 A VAL   A 142 ? 0.1352 0.1606 0.2080 -0.0060 0.0090  -0.0093 142 VAL   A CG2 
3189 C  CG2 B VAL   A 142 ? 0.1650 0.1614 0.2146 0.0052  -0.0085 0.0173  142 VAL   A CG2 
3208 N  N   . CYS   A 143 ? 0.1221 0.1431 0.1919 -0.0139 -0.0033 0.0145  143 CYS   A N   
3209 C  CA  . CYS   A 143 ? 0.1234 0.1432 0.2027 -0.0127 0.0024  0.0189  143 CYS   A CA  
3210 C  C   . CYS   A 143 ? 0.1195 0.1435 0.2015 -0.0134 0.0062  0.0176  143 CYS   A C   
3211 O  O   . CYS   A 143 ? 0.1183 0.1409 0.2029 -0.0100 -0.0010 0.0182  143 CYS   A O   
3212 C  CB  . CYS   A 143 ? 0.1310 0.1465 0.2094 -0.0100 0.0062  0.0188  143 CYS   A CB  
3213 S  SG  . CYS   A 143 ? 0.1431 0.1551 0.1976 -0.0026 0.0067  0.0090  143 CYS   A SG  
3220 N  N   . VAL   A 144 ? 0.1234 0.1398 0.2173 -0.0121 0.0090  0.0194  144 VAL   A N   
3221 C  CA  . VAL   A 144 ? 0.1286 0.1525 0.2486 -0.0184 0.0135  0.0259  144 VAL   A CA  
3222 C  C   . VAL   A 144 ? 0.1282 0.1374 0.2442 -0.0196 -0.0005 0.0233  144 VAL   A C   
3223 O  O   . VAL   A 144 ? 0.1521 0.1488 0.2536 -0.0074 -0.0037 0.0281  144 VAL   A O   
3224 C  CB  . VAL   A 144 ? 0.1497 0.1695 0.2933 -0.0083 0.0201  0.0305  144 VAL   A CB  
3225 C  CG1 . VAL   A 144 ? 0.1652 0.1872 0.3235 -0.0244 0.0004  0.0236  144 VAL   A CG1 
3226 C  CG2 . VAL   A 144 ? 0.1317 0.1741 0.3030 -0.0102 0.0222  0.0392  144 VAL   A CG2 
3236 N  N   . ASP   A 145 ? 0.1346 0.1331 0.2421 -0.0192 -0.0005 0.0085  145 ASP   A N   
3237 C  CA  . ASP   A 145 ? 0.1463 0.1408 0.2402 -0.0191 -0.0012 -0.0013 145 ASP   A CA  
3238 C  C   . ASP   A 145 ? 0.1466 0.1397 0.2474 -0.0083 -0.0041 0.0017  145 ASP   A C   
3239 O  O   . ASP   A 145 ? 0.1542 0.1506 0.2982 -0.0134 -0.0032 -0.0330 145 ASP   A O   
3240 C  CB  . ASP   A 145 ? 0.1566 0.1718 0.2476 -0.0190 -0.0016 -0.0120 145 ASP   A CB  
3241 C  CG  . ASP   A 145 ? 0.1685 0.2008 0.2740 -0.0297 -0.0051 -0.0194 145 ASP   A CG  
3242 O  OD1 . ASP   A 145 ? 0.1711 0.2098 0.3064 -0.0420 0.0000  -0.0125 145 ASP   A OD1 
3243 O  OD2 . ASP   A 145 ? 0.1905 0.2267 0.2983 -0.0283 -0.0174 -0.0152 145 ASP   A OD2 
3248 N  N   . THR   A 146 ? 0.1318 0.1314 0.2139 -0.0102 0.0023  0.0062  146 THR   A N   
3249 C  CA  . THR   A 146 ? 0.1243 0.1283 0.2025 -0.0078 0.0001  0.0082  146 THR   A CA  
3250 C  C   . THR   A 146 ? 0.1275 0.1325 0.2105 -0.0044 0.0069  0.0120  146 THR   A C   
3251 O  O   . THR   A 146 ? 0.1337 0.1437 0.2201 0.0035  -0.0003 0.0157  146 THR   A O   
3252 C  CB  . THR   A 146 ? 0.1265 0.1365 0.2068 -0.0045 0.0032  0.0114  146 THR   A CB  
3253 O  OG1 . THR   A 146 ? 0.1250 0.1482 0.2065 -0.0019 -0.0008 0.0038  146 THR   A OG1 
3254 C  CG2 . THR   A 146 ? 0.1291 0.1394 0.2181 -0.0056 0.0079  0.0146  146 THR   A CG2 
3262 N  N   . VAL   A 147 ? 0.1258 0.1384 0.1976 -0.0090 0.0111  0.0235  147 VAL   A N   
3263 C  CA  . VAL   A 147 ? 0.1212 0.1383 0.1976 -0.0125 0.0282  0.0262  147 VAL   A CA  
3264 C  C   . VAL   A 147 ? 0.1266 0.1350 0.2125 -0.0152 0.0172  0.0273  147 VAL   A C   
3265 O  O   . VAL   A 147 ? 0.1296 0.1393 0.2306 -0.0157 0.0051  0.0286  147 VAL   A O   
3266 C  CB  . VAL   A 147 ? 0.1380 0.1388 0.1870 -0.0142 0.0167  0.0266  147 VAL   A CB  
3267 C  CG1 . VAL   A 147 ? 0.1622 0.1434 0.1853 -0.0121 0.0148  0.0374  147 VAL   A CG1 
3268 C  CG2 . VAL   A 147 ? 0.1325 0.1364 0.1921 -0.0096 0.0053  0.0241  147 VAL   A CG2 
3278 N  N   . ARG   A 148 ? 0.1258 0.1371 0.2134 -0.0161 0.0167  0.0462  148 ARG   A N   
3279 C  CA  . ARG   A 148 ? 0.1380 0.1423 0.2215 -0.0110 0.0095  0.0456  148 ARG   A CA  
3280 C  C   . ARG   A 148 ? 0.1467 0.1402 0.2149 -0.0149 0.0119  0.0573  148 ARG   A C   
3281 O  O   . ARG   A 148 ? 0.1805 0.1526 0.2287 -0.0172 0.0214  0.0539  148 ARG   A O   
3282 C  CB  . ARG   A 148 ? 0.1440 0.1349 0.2424 -0.0049 0.0192  0.0386  148 ARG   A CB  
3283 C  CG  . ARG   A 148 ? 0.1611 0.1432 0.2639 -0.0041 0.0367  0.0352  148 ARG   A CG  
3284 C  CD  . ARG   A 148 ? 0.1781 0.1399 0.2825 -0.0081 0.0449  0.0473  148 ARG   A CD  
3285 N  NE  . ARG   A 148 ? 0.1735 0.1477 0.2804 0.0084  0.0417  0.0565  148 ARG   A NE  
3286 C  CZ  . ARG   A 148 ? 0.1724 0.1395 0.2596 0.0044  0.0414  0.0476  148 ARG   A CZ  
3287 N  NH1 . ARG   A 148 ? 0.1853 0.1425 0.2521 -0.0115 0.0413  0.0179  148 ARG   A NH1 
3288 N  NH2 . ARG   A 148 ? 0.1586 0.1587 0.2675 0.0143  0.0455  0.0491  148 ARG   A NH2 
3302 N  N   . THR   A 149 ? 0.1443 0.1464 0.2081 -0.0147 0.0049  0.0465  149 THR   A N   
3303 C  CA  . THR   A 149 ? 0.1436 0.1549 0.2031 -0.0112 0.0008  0.0431  149 THR   A CA  
3304 C  C   . THR   A 149 ? 0.1364 0.1479 0.1906 -0.0205 0.0058  0.0473  149 THR   A C   
3305 O  O   . THR   A 149 ? 0.1385 0.1575 0.2050 -0.0216 0.0104  0.0459  149 THR   A O   
3306 C  CB  . THR   A 149 ? 0.1449 0.1616 0.2046 -0.0144 0.0078  0.0449  149 THR   A CB  
3307 O  OG1 . THR   A 149 ? 0.1483 0.1467 0.2093 -0.0174 0.0034  0.0395  149 THR   A OG1 
3308 C  CG2 . THR   A 149 ? 0.1424 0.1735 0.2146 -0.0073 0.0026  0.0379  149 THR   A CG2 
3316 N  N   . ASN   A 150 ? 0.1438 0.1519 0.1954 -0.0157 -0.0012 0.0584  150 ASN   A N   
3317 C  CA  . ASN   A 150 ? 0.1533 0.1634 0.1916 -0.0132 0.0088  0.0533  150 ASN   A CA  
3318 C  C   . ASN   A 150 ? 0.1362 0.1587 0.1864 -0.0165 0.0035  0.0483  150 ASN   A C   
3319 O  O   . ASN   A 150 ? 0.1513 0.1640 0.2227 -0.0132 -0.0140 0.0474  150 ASN   A O   
3320 C  CB  . ASN   A 150 ? 0.1900 0.1820 0.2143 -0.0230 0.0184  0.0738  150 ASN   A CB  
3321 C  CG  . ASN   A 150 ? 0.2458 0.2164 0.2625 -0.0248 0.0087  0.0755  150 ASN   A CG  
3322 O  OD1 . ASN   A 150 ? 0.2783 0.2264 0.2721 -0.0328 0.0048  0.0899  150 ASN   A OD1 
3323 N  ND2 . ASN   A 150 ? 0.2747 0.2343 0.2928 -0.0178 -0.0037 0.0775  150 ASN   A ND2 
3330 N  N   . VAL   A 151 ? 0.1336 0.1439 0.2000 -0.0170 0.0082  0.0466  151 VAL   A N   
3331 C  CA  . VAL   A 151 ? 0.1383 0.1434 0.1896 -0.0176 0.0101  0.0456  151 VAL   A CA  
3332 C  C   . VAL   A 151 ? 0.1347 0.1420 0.1893 -0.0252 0.0116  0.0515  151 VAL   A C   
3333 O  O   . VAL   A 151 ? 0.1370 0.1465 0.2256 -0.0257 0.0120  0.0386  151 VAL   A O   
3334 C  CB  . VAL   A 151 ? 0.1608 0.1615 0.1952 -0.0060 0.0123  0.0401  151 VAL   A CB  
3335 C  CG1 . VAL   A 151 ? 0.1550 0.1777 0.2181 -0.0088 0.0116  0.0381  151 VAL   A CG1 
3336 C  CG2 . VAL   A 151 ? 0.1740 0.1604 0.1916 -0.0064 0.0293  0.0456  151 VAL   A CG2 
3346 N  N   . TYR   A 152 ? 0.1279 0.1427 0.1899 -0.0205 0.0103  0.0397  152 TYR   A N   
3347 C  CA  . TYR   A 152 ? 0.1276 0.1532 0.1732 -0.0177 0.0150  0.0339  152 TYR   A CA  
3348 C  C   . TYR   A 152 ? 0.1231 0.1468 0.1709 -0.0170 0.0170  0.0463  152 TYR   A C   
3349 O  O   . TYR   A 152 ? 0.1362 0.1444 0.1758 -0.0259 0.0060  0.0355  152 TYR   A O   
3350 C  CB  . TYR   A 152 ? 0.1503 0.1646 0.1783 -0.0154 0.0192  0.0413  152 TYR   A CB  
3351 C  CG  . TYR   A 152 ? 0.1633 0.1855 0.1758 -0.0167 0.0217  0.0448  152 TYR   A CG  
3352 C  CD1 . TYR   A 152 ? 0.1826 0.2059 0.1912 -0.0079 0.0271  0.0567  152 TYR   A CD1 
3353 C  CD2 . TYR   A 152 ? 0.1677 0.1933 0.1748 -0.0292 0.0238  0.0429  152 TYR   A CD2 
3354 C  CE1 . TYR   A 152 ? 0.2126 0.2186 0.2003 -0.0058 0.0181  0.0666  152 TYR   A CE1 
3355 C  CE2 . TYR   A 152 ? 0.1946 0.2095 0.1896 -0.0366 0.0286  0.0530  152 TYR   A CE2 
3356 C  CZ  . TYR   A 152 ? 0.2279 0.2139 0.1918 -0.0213 0.0193  0.0773  152 TYR   A CZ  
3357 O  OH  . TYR   A 152 ? 0.2668 0.2365 0.2232 -0.0165 0.0182  0.0932  152 TYR   A OH  
3367 N  N   . LEU   A 153 ? 0.1235 0.1388 0.1885 -0.0213 0.0179  0.0447  153 LEU   A N   
3368 C  CA  . LEU   A 153 ? 0.1181 0.1393 0.1986 -0.0087 0.0146  0.0430  153 LEU   A CA  
3369 C  C   . LEU   A 153 ? 0.1225 0.1459 0.2019 -0.0114 0.0195  0.0396  153 LEU   A C   
3370 O  O   . LEU   A 153 ? 0.1274 0.1554 0.2368 -0.0119 0.0357  0.0324  153 LEU   A O   
3371 C  CB  . LEU   A 153 ? 0.1209 0.1393 0.2031 -0.0104 0.0051  0.0336  153 LEU   A CB  
3372 C  CG  . LEU   A 153 ? 0.1282 0.1462 0.1977 -0.0117 0.0082  0.0333  153 LEU   A CG  
3373 C  CD1 . LEU   A 153 ? 0.1384 0.1510 0.1906 -0.0190 0.0004  0.0274  153 LEU   A CD1 
3374 C  CD2 . LEU   A 153 ? 0.1345 0.1476 0.1975 -0.0148 0.0221  0.0220  153 LEU   A CD2 
3386 N  N   A ALA   A 154 ? 0.1242 0.1475 0.1857 -0.0047 0.0164  0.0459  154 ALA   A N   
3387 N  N   B ALA   A 154 ? 0.1202 0.1374 0.1977 -0.0143 0.0142  0.0408  154 ALA   A N   
3388 C  CA  A ALA   A 154 ? 0.1354 0.1552 0.1803 0.0012  0.0160  0.0413  154 ALA   A CA  
3389 C  CA  B ALA   A 154 ? 0.1275 0.1355 0.1986 -0.0129 0.0145  0.0345  154 ALA   A CA  
3390 C  C   A ALA   A 154 ? 0.1382 0.1614 0.1726 0.0112  0.0174  0.0382  154 ALA   A C   
3391 C  C   B ALA   A 154 ? 0.1281 0.1344 0.2045 -0.0056 0.0156  0.0375  154 ALA   A C   
3392 O  O   A ALA   A 154 ? 0.1410 0.1715 0.1664 0.0116  0.0185  0.0386  154 ALA   A O   
3393 O  O   B ALA   A 154 ? 0.1320 0.1471 0.2167 -0.0009 0.0123  0.0417  154 ALA   A O   
3394 C  CB  A ALA   A 154 ? 0.1429 0.1614 0.1827 0.0062  0.0197  0.0313  154 ALA   A CB  
3395 C  CB  B ALA   A 154 ? 0.1354 0.1408 0.1992 -0.0080 0.0169  0.0231  154 ALA   A CB  
3406 N  N   A VAL   A 155 ? 0.1436 0.1648 0.1804 0.0183  0.0117  0.0346  155 VAL   A N   
3407 N  N   B VAL   A 155 ? 0.1294 0.1351 0.2030 -0.0074 0.0148  0.0377  155 VAL   A N   
3408 C  CA  A VAL   A 155 ? 0.1513 0.1669 0.1874 0.0220  0.0003  0.0288  155 VAL   A CA  
3409 C  CA  B VAL   A 155 ? 0.1293 0.1302 0.2065 -0.0118 0.0156  0.0329  155 VAL   A CA  
3410 C  C   A VAL   A 155 ? 0.1643 0.1752 0.2055 0.0316  -0.0166 0.0271  155 VAL   A C   
3411 C  C   B VAL   A 155 ? 0.1304 0.1309 0.2097 -0.0123 0.0186  0.0256  155 VAL   A C   
3412 O  O   A VAL   A 155 ? 0.1634 0.1809 0.2052 0.0323  -0.0220 0.0040  155 VAL   A O   
3413 O  O   B VAL   A 155 ? 0.1308 0.1326 0.2098 -0.0016 0.0298  0.0204  155 VAL   A O   
3414 C  CB  A VAL   A 155 ? 0.1484 0.1692 0.1819 0.0219  -0.0003 0.0102  155 VAL   A CB  
3415 C  CB  B VAL   A 155 ? 0.1285 0.1278 0.2006 -0.0133 0.0107  0.0244  155 VAL   A CB  
3416 C  CG1 A VAL   A 155 ? 0.1561 0.1758 0.1762 0.0203  -0.0098 -0.0003 155 VAL   A CG1 
3417 C  CG1 B VAL   A 155 ? 0.1296 0.1327 0.2040 -0.0016 0.0096  0.0131  155 VAL   A CG1 
3418 C  CG2 A VAL   A 155 ? 0.1576 0.1733 0.1863 0.0285  0.0085  0.0162  155 VAL   A CG2 
3419 C  CG2 B VAL   A 155 ? 0.1462 0.1313 0.2112 0.0012  0.0035  0.0310  155 VAL   A CG2 
3438 N  N   A PHE   A 156 ? 0.1773 0.1740 0.2285 0.0425  -0.0127 0.0437  156 PHE   A N   
3439 N  N   B PHE   A 156 ? 0.1380 0.1366 0.2369 -0.0100 0.0180  0.0172  156 PHE   A N   
3440 C  CA  A PHE   A 156 ? 0.1975 0.1766 0.2577 0.0446  -0.0150 0.0536  156 PHE   A CA  
3441 C  CA  B PHE   A 156 ? 0.1553 0.1601 0.2807 -0.0107 -0.0022 0.0123  156 PHE   A CA  
3442 C  C   A PHE   A 156 ? 0.1925 0.1743 0.2766 0.0510  -0.0134 0.0626  156 PHE   A C   
3443 C  C   B PHE   A 156 ? 0.1733 0.1758 0.3125 -0.0041 -0.0179 0.0173  156 PHE   A C   
3444 O  O   A PHE   A 156 ? 0.1884 0.1895 0.3041 0.0508  -0.0075 0.0413  156 PHE   A O   
3445 O  O   B PHE   A 156 ? 0.1883 0.1912 0.3270 -0.0047 -0.0180 0.0249  156 PHE   A O   
3446 C  CB  A PHE   A 156 ? 0.2270 0.1743 0.2617 0.0421  -0.0234 0.0652  156 PHE   A CB  
3447 C  CB  B PHE   A 156 ? 0.1714 0.1751 0.3094 -0.0025 -0.0074 0.0048  156 PHE   A CB  
3448 C  CG  A PHE   A 156 ? 0.2573 0.1806 0.2680 0.0417  -0.0334 0.0674  156 PHE   A CG  
3449 C  CG  B PHE   A 156 ? 0.1848 0.2022 0.3266 0.0048  -0.0139 -0.0169 156 PHE   A CG  
3450 C  CD1 A PHE   A 156 ? 0.2748 0.1911 0.2775 0.0396  -0.0426 0.0538  156 PHE   A CD1 
3451 C  CD1 B PHE   A 156 ? 0.2023 0.2189 0.3347 0.0031  -0.0140 -0.0204 156 PHE   A CD1 
3452 C  CD2 A PHE   A 156 ? 0.2725 0.1842 0.2698 0.0455  -0.0324 0.0807  156 PHE   A CD2 
3453 C  CD2 B PHE   A 156 ? 0.1870 0.2144 0.3250 0.0058  -0.0169 -0.0254 156 PHE   A CD2 
3454 C  CE1 A PHE   A 156 ? 0.2862 0.1980 0.2915 0.0398  -0.0388 0.0488  156 PHE   A CE1 
3455 C  CE1 B PHE   A 156 ? 0.2086 0.2299 0.3388 0.0043  -0.0178 -0.0204 156 PHE   A CE1 
3456 C  CE2 A PHE   A 156 ? 0.2837 0.1923 0.2788 0.0460  -0.0383 0.0728  156 PHE   A CE2 
3457 C  CE2 B PHE   A 156 ? 0.1910 0.2238 0.3228 0.0057  -0.0150 -0.0249 156 PHE   A CE2 
3458 C  CZ  A PHE   A 156 ? 0.2872 0.1958 0.2883 0.0464  -0.0398 0.0531  156 PHE   A CZ  
3459 C  CZ  B PHE   A 156 ? 0.2077 0.2323 0.3346 0.0087  -0.0156 -0.0221 156 PHE   A CZ  
3478 N  N   A ASP   A 157 ? 0.1936 0.1722 0.2708 0.0477  -0.0153 0.0859  157 ASP   A N   
3479 N  N   B ASP   A 157 ? 0.1734 0.1812 0.3264 -0.0137 -0.0269 0.0276  157 ASP   A N   
3480 C  CA  A ASP   A 157 ? 0.1963 0.1956 0.2912 0.0426  -0.0280 0.0689  157 ASP   A CA  
3481 C  CA  B ASP   A 157 ? 0.1712 0.1858 0.3310 -0.0233 -0.0296 0.0280  157 ASP   A CA  
3482 C  C   A ASP   A 157 ? 0.1774 0.2114 0.2968 0.0453  -0.0209 0.0685  157 ASP   A C   
3483 C  C   B ASP   A 157 ? 0.1552 0.1719 0.3124 -0.0155 -0.0285 0.0109  157 ASP   A C   
3484 O  O   A ASP   A 157 ? 0.1652 0.1994 0.2848 0.0360  -0.0143 0.0770  157 ASP   A O   
3485 O  O   B ASP   A 157 ? 0.1547 0.1554 0.3033 -0.0113 -0.0202 0.0110  157 ASP   A O   
3486 C  CB  A ASP   A 157 ? 0.2125 0.1972 0.3031 0.0412  -0.0501 0.0621  157 ASP   A CB  
3487 C  CB  B ASP   A 157 ? 0.1822 0.2043 0.3512 -0.0323 -0.0310 0.0579  157 ASP   A CB  
3488 C  CG  A ASP   A 157 ? 0.2357 0.2083 0.3273 0.0390  -0.0567 0.0423  157 ASP   A CG  
3489 C  CG  B ASP   A 157 ? 0.1956 0.2212 0.3784 -0.0327 -0.0384 0.0832  157 ASP   A CG  
3490 O  OD1 A ASP   A 157 ? 0.2590 0.2141 0.3436 0.0325  -0.0608 0.0323  157 ASP   A OD1 
3491 O  OD1 B ASP   A 157 ? 0.1982 0.2312 0.3861 -0.0242 -0.0438 0.0945  157 ASP   A OD1 
3492 O  OD2 A ASP   A 157 ? 0.2315 0.2190 0.3346 0.0386  -0.0605 0.0398  157 ASP   A OD2 
3493 O  OD2 B ASP   A 157 ? 0.2058 0.2333 0.3993 -0.0389 -0.0418 0.0806  157 ASP   A OD2 
3502 N  N   A LYS   A 158 ? 0.1865 0.2420 0.3174 0.0480  -0.0077 0.0558  158 LYS   A N   
3503 N  N   B LYS   A 158 ? 0.1585 0.1822 0.3123 -0.0126 -0.0208 -0.0046 158 LYS   A N   
3504 C  CA  A LYS   A 158 ? 0.1862 0.2720 0.3330 0.0570  0.0053  0.0497  158 LYS   A CA  
3505 C  CA  B LYS   A 158 ? 0.1665 0.2015 0.3098 -0.0098 -0.0056 -0.0084 158 LYS   A CA  
3506 C  C   A LYS   A 158 ? 0.1836 0.2751 0.3231 0.0587  0.0005  0.0563  158 LYS   A C   
3507 C  C   B LYS   A 158 ? 0.1522 0.1855 0.2904 -0.0123 -0.0133 -0.0031 158 LYS   A C   
3508 O  O   A LYS   A 158 ? 0.1862 0.2794 0.3188 0.0534  0.0096  0.0565  158 LYS   A O   
3509 O  O   B LYS   A 158 ? 0.1433 0.1725 0.2856 -0.0168 -0.0033 0.0018  158 LYS   A O   
3510 C  CB  A LYS   A 158 ? 0.1964 0.2969 0.3602 0.0547  0.0233  0.0458  158 LYS   A CB  
3511 C  CB  B LYS   A 158 ? 0.1898 0.2411 0.3376 -0.0108 0.0133  -0.0052 158 LYS   A CB  
3512 C  CG  A LYS   A 158 ? 0.2124 0.3192 0.3940 0.0480  0.0350  0.0482  158 LYS   A CG  
3513 C  CG  B LYS   A 158 ? 0.2137 0.2737 0.3688 -0.0168 0.0334  0.0063  158 LYS   A CG  
3514 C  CD  A LYS   A 158 ? 0.2215 0.3358 0.4241 0.0430  0.0517  0.0539  158 LYS   A CD  
3515 C  CD  B LYS   A 158 ? 0.2296 0.2992 0.3971 -0.0253 0.0563  0.0208  158 LYS   A CD  
3516 C  CE  A LYS   A 158 ? 0.2277 0.3444 0.4452 0.0405  0.0645  0.0621  158 LYS   A CE  
3517 C  CE  B LYS   A 158 ? 0.2404 0.3137 0.4209 -0.0238 0.0669  0.0329  158 LYS   A CE  
3518 N  NZ  A LYS   A 158 ? 0.2322 0.3502 0.4570 0.0374  0.0743  0.0686  158 LYS   A NZ  
3519 N  NZ  B LYS   A 158 ? 0.2459 0.3227 0.4371 -0.0231 0.0713  0.0378  158 LYS   A NZ  
3546 N  N   A ASN   A 159 ? 0.1812 0.2767 0.3276 0.0591  -0.0138 0.0645  159 ASN   A N   
3547 N  N   B ASN   A 159 ? 0.1543 0.1905 0.2897 -0.0061 -0.0297 -0.0046 159 ASN   A N   
3548 C  CA  A ASN   A 159 ? 0.1872 0.2801 0.3335 0.0520  -0.0193 0.0726  159 ASN   A CA  
3549 C  CA  B ASN   A 159 ? 0.1590 0.1984 0.2914 -0.0027 -0.0406 0.0058  159 ASN   A CA  
3550 C  C   A ASN   A 159 ? 0.1739 0.2716 0.3001 0.0437  -0.0145 0.0699  159 ASN   A C   
3551 C  C   B ASN   A 159 ? 0.1452 0.1856 0.2801 -0.0107 -0.0400 0.0064  159 ASN   A C   
3552 O  O   A ASN   A 159 ? 0.1761 0.2766 0.3057 0.0404  -0.0062 0.0579  159 ASN   A O   
3553 O  O   B ASN   A 159 ? 0.1464 0.1852 0.2926 -0.0147 -0.0359 0.0096  159 ASN   A O   
3554 C  CB  A ASN   A 159 ? 0.2071 0.2939 0.3872 0.0465  -0.0189 0.0753  159 ASN   A CB  
3555 C  CB  B ASN   A 159 ? 0.1912 0.2303 0.3205 0.0069  -0.0442 0.0141  159 ASN   A CB  
3556 C  CG  A ASN   A 159 ? 0.2254 0.3085 0.4422 0.0359  -0.0074 0.0724  159 ASN   A CG  
3557 C  CG  B ASN   A 159 ? 0.2219 0.2653 0.3544 0.0137  -0.0349 0.0145  159 ASN   A CG  
3558 O  OD1 A ASN   A 159 ? 0.2260 0.3185 0.4639 0.0313  -0.0021 0.0656  159 ASN   A OD1 
3559 O  OD1 B ASN   A 159 ? 0.2318 0.2844 0.3784 0.0179  -0.0195 0.0159  159 ASN   A OD1 
3560 N  ND2 A ASN   A 159 ? 0.2314 0.3133 0.4612 0.0329  -0.0067 0.0734  159 ASN   A ND2 
3561 N  ND2 B ASN   A 159 ? 0.2330 0.2744 0.3663 0.0152  -0.0367 0.0188  159 ASN   A ND2 
3574 N  N   A LEU   A 160 ? 0.1648 0.2613 0.2723 0.0316  -0.0219 0.0733  160 LEU   A N   
3575 N  N   B LEU   A 160 ? 0.1492 0.1802 0.2720 -0.0166 -0.0406 0.0082  160 LEU   A N   
3576 C  CA  A LEU   A 160 ? 0.1608 0.2530 0.2529 0.0186  -0.0049 0.0696  160 LEU   A CA  
3577 C  CA  B LEU   A 160 ? 0.1637 0.1836 0.2793 -0.0227 -0.0231 -0.0069 160 LEU   A CA  
3578 C  C   A LEU   A 160 ? 0.1511 0.2465 0.2405 0.0148  0.0102  0.0571  160 LEU   A C   
3579 C  C   B LEU   A 160 ? 0.1534 0.1669 0.2546 -0.0074 -0.0181 -0.0041 160 LEU   A C   
3580 O  O   A LEU   A 160 ? 0.1550 0.2531 0.2539 0.0126  0.0125  0.0395  160 LEU   A O   
3581 O  O   B LEU   A 160 ? 0.1619 0.1640 0.2625 -0.0052 -0.0204 -0.0252 160 LEU   A O   
3582 C  CB  A LEU   A 160 ? 0.1585 0.2531 0.2357 0.0111  0.0063  0.0757  160 LEU   A CB  
3583 C  CB  B LEU   A 160 ? 0.1917 0.2121 0.3167 -0.0325 -0.0033 -0.0210 160 LEU   A CB  
3584 C  CG  A LEU   A 160 ? 0.1529 0.2569 0.2257 -0.0021 0.0187  0.0709  160 LEU   A CG  
3585 C  CG  B LEU   A 160 ? 0.2204 0.2501 0.3666 -0.0320 0.0158  -0.0346 160 LEU   A CG  
3586 C  CD1 A LEU   A 160 ? 0.1655 0.2626 0.2354 -0.0073 0.0215  0.0730  160 LEU   A CD1 
3587 C  CD1 B LEU   A 160 ? 0.2293 0.2619 0.3831 -0.0330 0.0204  -0.0421 160 LEU   A CD1 
3588 C  CD2 A LEU   A 160 ? 0.1460 0.2519 0.2152 -0.0001 0.0271  0.0668  160 LEU   A CD2 
3589 C  CD2 B LEU   A 160 ? 0.2321 0.2633 0.3847 -0.0322 0.0230  -0.0377 160 LEU   A CD2 
3612 N  N   A TYR   A 161 ? 0.1457 0.2377 0.2427 0.0146  0.0201  0.0558  161 TYR   A N   
3613 N  N   B TYR   A 161 ? 0.1441 0.1582 0.2439 -0.0059 -0.0038 0.0062  161 TYR   A N   
3614 C  CA  A TYR   A 161 ? 0.1390 0.2296 0.2479 0.0181  0.0198  0.0519  161 TYR   A CA  
3615 C  CA  B TYR   A 161 ? 0.1400 0.1584 0.2382 -0.0077 0.0022  0.0081  161 TYR   A CA  
3616 C  C   A TYR   A 161 ? 0.1331 0.2447 0.2678 0.0166  0.0190  0.0482  161 TYR   A C   
3617 C  C   B TYR   A 161 ? 0.1388 0.1572 0.2523 -0.0084 0.0026  0.0026  161 TYR   A C   
3618 O  O   A TYR   A 161 ? 0.1232 0.2450 0.2616 0.0164  0.0143  0.0378  161 TYR   A O   
3619 O  O   B TYR   A 161 ? 0.1425 0.1546 0.2479 -0.0042 -0.0011 -0.0031 161 TYR   A O   
3620 C  CB  A TYR   A 161 ? 0.1456 0.2063 0.2495 0.0197  0.0219  0.0475  161 TYR   A CB  
3621 C  CB  B TYR   A 161 ? 0.1391 0.1730 0.2291 -0.0020 0.0114  0.0080  161 TYR   A CB  
3622 C  CG  A TYR   A 161 ? 0.1513 0.1859 0.2495 0.0265  0.0213  0.0442  161 TYR   A CG  
3623 C  CG  B TYR   A 161 ? 0.1443 0.1826 0.2323 -0.0018 0.0133  0.0093  161 TYR   A CG  
3624 C  CD1 A TYR   A 161 ? 0.1482 0.1761 0.2509 0.0284  0.0193  0.0332  161 TYR   A CD1 
3625 C  CD1 B TYR   A 161 ? 0.1382 0.1870 0.2318 -0.0049 0.0114  0.0081  161 TYR   A CD1 
3626 C  CD2 A TYR   A 161 ? 0.1596 0.1883 0.2568 0.0293  0.0221  0.0337  161 TYR   A CD2 
3627 C  CD2 B TYR   A 161 ? 0.1466 0.1968 0.2414 0.0004  0.0168  0.0071  161 TYR   A CD2 
3628 C  CE1 A TYR   A 161 ? 0.1578 0.1821 0.2548 0.0261  0.0156  0.0367  161 TYR   A CE1 
3629 C  CE1 B TYR   A 161 ? 0.1379 0.1809 0.2264 -0.0090 0.0171  0.0181  161 TYR   A CE1 
3630 C  CE2 A TYR   A 161 ? 0.1674 0.1873 0.2620 0.0298  0.0206  0.0301  161 TYR   A CE2 
3631 C  CE2 B TYR   A 161 ? 0.1461 0.2034 0.2421 -0.0020 0.0228  0.0166  161 TYR   A CE2 
3632 C  CZ  A TYR   A 161 ? 0.1761 0.1893 0.2706 0.0260  0.0190  0.0359  161 TYR   A CZ  
3633 C  CZ  B TYR   A 161 ? 0.1465 0.1922 0.2325 -0.0037 0.0195  0.0221  161 TYR   A CZ  
3634 O  OH  A TYR   A 161 ? 0.1919 0.1917 0.2952 0.0304  0.0235  0.0337  161 TYR   A OH  
3635 O  OH  B TYR   A 161 ? 0.1520 0.1977 0.2334 -0.0054 0.0209  0.0343  161 TYR   A OH  
3654 N  N   A ASP   A 162 ? 0.1387 0.2594 0.2956 0.0132  0.0242  0.0580  162 ASP   A N   
3655 N  N   B ASP   A 162 ? 0.1361 0.1632 0.2850 -0.0130 0.0038  0.0106  162 ASP   A N   
3656 C  CA  A ASP   A 162 ? 0.1468 0.2820 0.3193 0.0065  0.0270  0.0573  162 ASP   A CA  
3657 C  CA  B ASP   A 162 ? 0.1298 0.1846 0.3079 -0.0171 0.0049  0.0073  162 ASP   A CA  
3658 C  C   A ASP   A 162 ? 0.1471 0.3072 0.3310 0.0053  0.0263  0.0503  162 ASP   A C   
3659 C  C   B ASP   A 162 ? 0.1258 0.1956 0.3351 -0.0192 -0.0083 -0.0127 162 ASP   A C   
3660 O  O   A ASP   A 162 ? 0.1528 0.3090 0.3501 0.0058  0.0379  0.0473  162 ASP   A O   
3661 O  O   B ASP   A 162 ? 0.1329 0.1850 0.3671 -0.0257 0.0049  -0.0160 162 ASP   A O   
3662 C  CB  A ASP   A 162 ? 0.1580 0.2842 0.3383 0.0037  0.0261  0.0521  162 ASP   A CB  
3663 C  CB  B ASP   A 162 ? 0.1380 0.2055 0.3127 -0.0121 0.0056  0.0220  162 ASP   A CB  
3664 C  CG  A ASP   A 162 ? 0.1685 0.2837 0.3578 0.0020  0.0266  0.0468  162 ASP   A CG  
3665 C  CG  B ASP   A 162 ? 0.1445 0.2279 0.3165 -0.0044 0.0089  0.0320  162 ASP   A CG  
3666 O  OD1 A ASP   A 162 ? 0.1738 0.2848 0.3625 -0.0007 0.0266  0.0438  162 ASP   A OD1 
3667 O  OD1 B ASP   A 162 ? 0.1626 0.2449 0.3267 -0.0001 0.0114  0.0340  162 ASP   A OD1 
3668 O  OD2 A ASP   A 162 ? 0.1827 0.2826 0.3751 0.0062  0.0273  0.0432  162 ASP   A OD2 
3669 O  OD2 B ASP   A 162 ? 0.1498 0.2335 0.3157 -0.0036 0.0121  0.0317  162 ASP   A OD2 
3678 N  N   A LYS   A 163 ? 0.1563 0.3293 0.3352 0.0019  0.0097  0.0405  163 LYS   A N   
3679 N  N   B LYS   A 163 ? 0.1338 0.2261 0.3408 -0.0179 -0.0278 -0.0224 163 LYS   A N   
3680 C  CA  A LYS   A 163 ? 0.1705 0.3470 0.3425 -0.0040 0.0046  0.0296  163 LYS   A CA  
3681 C  CA  B LYS   A 163 ? 0.1546 0.2516 0.3502 -0.0262 -0.0234 -0.0260 163 LYS   A CA  
3682 C  C   A LYS   A 163 ? 0.1526 0.3371 0.3336 -0.0154 0.0126  0.0199  163 LYS   A C   
3683 C  C   B LYS   A 163 ? 0.1461 0.2311 0.3352 -0.0344 -0.0107 -0.0409 163 LYS   A C   
3684 O  O   A LYS   A 163 ? 0.1450 0.3469 0.3580 -0.0267 0.0086  0.0187  163 LYS   A O   
3685 O  O   B LYS   A 163 ? 0.1537 0.2382 0.3640 -0.0402 -0.0071 -0.0495 163 LYS   A O   
3686 C  CB  A LYS   A 163 ? 0.2088 0.3719 0.3672 0.0042  -0.0046 0.0297  163 LYS   A CB  
3687 C  CB  B LYS   A 163 ? 0.1947 0.2930 0.3789 -0.0247 -0.0228 -0.0128 163 LYS   A CB  
3688 C  CG  A LYS   A 163 ? 0.2393 0.3921 0.3959 0.0095  -0.0074 0.0321  163 LYS   A CG  
3689 C  CG  B LYS   A 163 ? 0.2307 0.3271 0.4122 -0.0217 -0.0086 0.0038  163 LYS   A CG  
3690 C  CD  A LYS   A 163 ? 0.2730 0.4085 0.4319 0.0134  -0.0111 0.0326  163 LYS   A CD  
3691 C  CD  B LYS   A 163 ? 0.2629 0.3534 0.4459 -0.0193 0.0017  0.0160  163 LYS   A CD  
3692 C  CE  A LYS   A 163 ? 0.2953 0.4196 0.4644 0.0165  -0.0101 0.0349  163 LYS   A CE  
3693 C  CE  B LYS   A 163 ? 0.2836 0.3728 0.4766 -0.0177 0.0085  0.0231  163 LYS   A CE  
3694 N  NZ  A LYS   A 163 ? 0.3026 0.4258 0.4829 0.0181  -0.0107 0.0363  163 LYS   A NZ  
3695 N  NZ  B LYS   A 163 ? 0.2913 0.3813 0.4913 -0.0184 0.0132  0.0301  163 LYS   A NZ  
3722 N  N   A LEU   A 164 ? 0.1419 0.3155 0.3060 -0.0227 0.0166  0.0135  164 LEU   A N   
3723 N  N   B LEU   A 164 ? 0.1357 0.2139 0.3058 -0.0351 -0.0001 -0.0294 164 LEU   A N   
3724 C  CA  A LEU   A 164 ? 0.1440 0.2911 0.2929 -0.0279 0.0314  0.0138  164 LEU   A CA  
3725 C  CA  B LEU   A 164 ? 0.1351 0.1932 0.2957 -0.0327 0.0169  -0.0179 164 LEU   A CA  
3726 C  C   A LEU   A 164 ? 0.1502 0.2861 0.3070 -0.0362 0.0398  0.0136  164 LEU   A C   
3727 C  C   B LEU   A 164 ? 0.1403 0.1834 0.3092 -0.0300 0.0245  -0.0175 164 LEU   A C   
3728 O  O   A LEU   A 164 ? 0.1605 0.2893 0.3171 -0.0412 0.0468  0.0047  164 LEU   A O   
3729 O  O   B LEU   A 164 ? 0.1609 0.1829 0.3233 -0.0244 0.0265  -0.0293 164 LEU   A O   
3730 C  CB  A LEU   A 164 ? 0.1396 0.2751 0.2712 -0.0250 0.0336  0.0201  164 LEU   A CB  
3731 C  CB  B LEU   A 164 ? 0.1397 0.1884 0.2798 -0.0279 0.0167  -0.0065 164 LEU   A CB  
3732 C  CG  A LEU   A 164 ? 0.1415 0.2651 0.2547 -0.0171 0.0359  0.0248  164 LEU   A CG  
3733 C  CG  B LEU   A 164 ? 0.1396 0.1872 0.2649 -0.0218 0.0201  -0.0078 164 LEU   A CG  
3734 C  CD1 A LEU   A 164 ? 0.1367 0.2631 0.2419 -0.0096 0.0198  0.0263  164 LEU   A CD1 
3735 C  CD1 B LEU   A 164 ? 0.1353 0.1860 0.2515 -0.0207 0.0094  0.0048  164 LEU   A CD1 
3736 C  CD2 A LEU   A 164 ? 0.1467 0.2594 0.2535 -0.0109 0.0448  0.0200  164 LEU   A CD2 
3737 C  CD2 B LEU   A 164 ? 0.1474 0.1907 0.2760 -0.0077 0.0227  -0.0162 164 LEU   A CD2 
3760 N  N   A VAL   A 165 ? 0.1531 0.2824 0.3175 -0.0354 0.0400  0.0236  165 VAL   A N   
3761 N  N   B VAL   A 165 ? 0.1405 0.1873 0.3174 -0.0230 0.0235  -0.0015 165 VAL   A N   
3762 C  CA  A VAL   A 165 ? 0.1634 0.2763 0.3320 -0.0405 0.0468  0.0320  165 VAL   A CA  
3763 C  CA  B VAL   A 165 ? 0.1493 0.1989 0.3377 -0.0223 0.0216  0.0056  165 VAL   A CA  
3764 C  C   A VAL   A 165 ? 0.1646 0.2820 0.3587 -0.0322 0.0348  0.0361  165 VAL   A C   
3765 C  C   B VAL   A 165 ? 0.1360 0.1949 0.3646 -0.0283 0.0145  -0.0041 165 VAL   A C   
3766 O  O   A VAL   A 165 ? 0.1687 0.2859 0.3670 -0.0309 0.0373  0.0505  165 VAL   A O   
3767 O  O   B VAL   A 165 ? 0.1431 0.1965 0.3829 -0.0314 0.0200  0.0057  165 VAL   A O   
3768 C  CB  A VAL   A 165 ? 0.1687 0.2665 0.3298 -0.0519 0.0653  0.0363  165 VAL   A CB  
3769 C  CB  B VAL   A 165 ? 0.1731 0.2148 0.3418 -0.0117 0.0262  0.0152  165 VAL   A CB  
3770 C  CG1 A VAL   A 165 ? 0.1751 0.2664 0.3375 -0.0592 0.0638  0.0375  165 VAL   A CG1 
3771 C  CG1 B VAL   A 165 ? 0.1817 0.2253 0.3493 -0.0122 0.0224  0.0183  165 VAL   A CG1 
3772 C  CG2 A VAL   A 165 ? 0.1687 0.2587 0.3216 -0.0542 0.0735  0.0476  165 VAL   A CG2 
3773 C  CG2 B VAL   A 165 ? 0.1805 0.2169 0.3343 -0.0076 0.0256  0.0214  165 VAL   A CG2 
3792 N  N   A SER   A 166 ? 0.1668 0.2860 0.3776 -0.0219 0.0251  0.0305  166 SER   A N   
3793 N  N   B SER   A 166 ? 0.1296 0.2031 0.3723 -0.0246 0.0061  -0.0120 166 SER   A N   
3794 C  CA  A SER   A 166 ? 0.1740 0.2900 0.3925 -0.0142 0.0088  0.0306  166 SER   A CA  
3795 C  CA  B SER   A 166 ? 0.1436 0.2178 0.3784 -0.0178 -0.0049 -0.0156 166 SER   A CA  
3796 C  C   A SER   A 166 ? 0.1654 0.2841 0.3728 -0.0194 -0.0224 0.0413  166 SER   A C   
3797 C  C   B SER   A 166 ? 0.1506 0.2149 0.3715 -0.0200 -0.0056 -0.0115 166 SER   A C   
3798 O  O   A SER   A 166 ? 0.1669 0.2799 0.3817 -0.0232 -0.0190 0.0483  166 SER   A O   
3799 O  O   B SER   A 166 ? 0.1533 0.2118 0.3824 -0.0256 0.0008  -0.0088 166 SER   A O   
3800 C  CB  A SER   A 166 ? 0.1958 0.3005 0.4185 0.0019  0.0143  0.0168  166 SER   A CB  
3801 C  CB  B SER   A 166 ? 0.1653 0.2398 0.3843 -0.0132 -0.0277 -0.0171 166 SER   A CB  
3802 O  OG  A SER   A 166 ? 0.2267 0.3132 0.4358 0.0028  0.0173  0.0197  166 SER   A OG  
3803 O  OG  B SER   A 166 ? 0.2097 0.2578 0.3940 -0.0066 -0.0410 -0.0100 166 SER   A OG  
3814 N  N   A SER   A 167 ? 0.1709 0.2830 0.3479 -0.0125 -0.0426 0.0382  167 SER   A N   
3815 N  N   B SER   A 167 ? 0.1627 0.2167 0.3544 -0.0116 0.0045  0.0018  167 SER   A N   
3816 C  CA  A SER   A 167 ? 0.1880 0.2776 0.3184 -0.0089 -0.0574 0.0377  167 SER   A CA  
3817 C  CA  B SER   A 167 ? 0.1778 0.2211 0.3269 -0.0102 0.0122  0.0098  167 SER   A CA  
3818 C  C   A SER   A 167 ? 0.2050 0.2690 0.3098 -0.0083 -0.0473 0.0408  167 SER   A C   
3819 C  C   B SER   A 167 ? 0.1746 0.2202 0.3001 -0.0038 0.0204  0.0138  167 SER   A C   
3820 O  O   A SER   A 167 ? 0.2143 0.2625 0.3062 -0.0077 -0.0502 0.0410  167 SER   A O   
3821 O  O   B SER   A 167 ? 0.1868 0.2238 0.2901 0.0005  0.0203  0.0164  167 SER   A O   
3822 C  CB  A SER   A 167 ? 0.1912 0.2816 0.3236 -0.0036 -0.0613 0.0371  167 SER   A CB  
3823 C  CB  B SER   A 167 ? 0.1857 0.2284 0.3288 -0.0128 0.0161  0.0085  167 SER   A CB  
3824 O  OG  A SER   A 167 ? 0.2000 0.2839 0.3352 -0.0079 -0.0537 0.0321  167 SER   A OG  
3825 O  OG  B SER   A 167 ? 0.1992 0.2314 0.3428 -0.0138 0.0268  0.0088  167 SER   A OG  
3836 N  N   A PHE   A 168 ? 0.2074 0.2653 0.3088 -0.0083 -0.0440 0.0446  168 PHE   A N   
3837 N  N   B PHE   A 168 ? 0.1622 0.2177 0.2809 -0.0004 0.0283  -0.0014 168 PHE   A N   
3838 C  CA  A PHE   A 168 ? 0.2183 0.2640 0.3214 -0.0110 -0.0335 0.0349  168 PHE   A CA  
3839 C  CA  B PHE   A 168 ? 0.1581 0.2206 0.2649 0.0003  0.0503  -0.0049 168 PHE   A CA  
3840 C  C   A PHE   A 168 ? 0.2517 0.2783 0.3687 -0.0159 -0.0205 0.0186  168 PHE   A C   
3841 C  C   B PHE   A 168 ? 0.1688 0.2315 0.2762 -0.0066 0.0674  0.0000  168 PHE   A C   
3842 O  O   A PHE   A 168 ? 0.2560 0.2808 0.3883 -0.0166 -0.0207 0.0162  168 PHE   A O   
3843 O  O   B PHE   A 168 ? 0.1670 0.2310 0.2841 -0.0046 0.0748  0.0035  168 PHE   A O   
3844 C  CB  A PHE   A 168 ? 0.1988 0.2503 0.2896 -0.0186 -0.0369 0.0352  168 PHE   A CB  
3845 C  CB  B PHE   A 168 ? 0.1629 0.2238 0.2675 -0.0013 0.0355  -0.0043 168 PHE   A CB  
3846 C  CG  A PHE   A 168 ? 0.1841 0.2408 0.2588 -0.0230 -0.0401 0.0260  168 PHE   A CG  
3847 C  CG  B PHE   A 168 ? 0.1613 0.2259 0.2632 -0.0066 0.0290  0.0077  168 PHE   A CG  
3848 C  CD1 A PHE   A 168 ? 0.1791 0.2399 0.2456 -0.0263 -0.0386 0.0278  168 PHE   A CD1 
3849 C  CD1 B PHE   A 168 ? 0.1616 0.2332 0.2668 -0.0082 0.0276  0.0168  168 PHE   A CD1 
3850 C  CD2 A PHE   A 168 ? 0.1780 0.2328 0.2371 -0.0251 -0.0331 0.0166  168 PHE   A CD2 
3851 C  CD2 B PHE   A 168 ? 0.1612 0.2249 0.2552 -0.0063 0.0278  0.0072  168 PHE   A CD2 
3852 C  CE1 A PHE   A 168 ? 0.1716 0.2387 0.2249 -0.0265 -0.0457 0.0215  168 PHE   A CE1 
3853 C  CE1 B PHE   A 168 ? 0.1590 0.2398 0.2720 -0.0074 0.0196  0.0191  168 PHE   A CE1 
3854 C  CE2 A PHE   A 168 ? 0.1744 0.2264 0.2227 -0.0289 -0.0301 0.0136  168 PHE   A CE2 
3855 C  CE2 B PHE   A 168 ? 0.1609 0.2277 0.2579 -0.0091 0.0217  0.0124  168 PHE   A CE2 
3856 C  CZ  A PHE   A 168 ? 0.1719 0.2336 0.2189 -0.0264 -0.0384 0.0143  168 PHE   A CZ  
3857 C  CZ  B PHE   A 168 ? 0.1609 0.2364 0.2703 -0.0072 0.0216  0.0157  168 PHE   A CZ  
3876 N  N   A LEU   A 169 ? 0.2795 0.2840 0.3924 -0.0209 -0.0055 0.0005  169 LEU   A N   
3877 N  N   B LEU   A 169 ? 0.1977 0.2533 0.2829 -0.0067 0.0636  -0.0057 169 LEU   A N   
3878 C  CA  A LEU   A 169 ? 0.3060 0.2939 0.4125 -0.0203 0.0081  -0.0159 169 LEU   A CA  
3879 C  CA  B LEU   A 169 ? 0.2375 0.2820 0.2988 -0.0066 0.0432  -0.0170 169 LEU   A CA  
3880 C  C   A LEU   A 169 ? 0.3111 0.2922 0.4294 -0.0211 0.0210  -0.0148 169 LEU   A C   
3881 C  C   B LEU   A 169 ? 0.2577 0.2987 0.3061 -0.0071 0.0378  -0.0276 169 LEU   A C   
3882 O  O   A LEU   A 169 ? 0.3163 0.2945 0.4378 -0.0219 0.0217  -0.0107 169 LEU   A O   
3883 O  O   B LEU   A 169 ? 0.2550 0.3077 0.3088 -0.0107 0.0267  -0.0304 169 LEU   A O   
3884 C  CB  A LEU   A 169 ? 0.3244 0.3076 0.4094 -0.0166 0.0121  -0.0267 169 LEU   A CB  
3885 C  CB  B LEU   A 169 ? 0.2601 0.2937 0.3062 -0.0034 0.0325  -0.0183 169 LEU   A CB  
3886 C  CG  A LEU   A 169 ? 0.3402 0.3182 0.4073 -0.0136 0.0158  -0.0392 169 LEU   A CG  
3887 C  CG  B LEU   A 169 ? 0.2765 0.3044 0.3160 0.0008  0.0221  -0.0128 169 LEU   A CG  
3888 C  CD1 A LEU   A 169 ? 0.3452 0.3210 0.4085 -0.0121 0.0179  -0.0437 169 LEU   A CD1 
3889 C  CD1 B LEU   A 169 ? 0.2881 0.3108 0.3140 0.0049  0.0172  -0.0096 169 LEU   A CD1 
3890 C  CD2 A LEU   A 169 ? 0.3453 0.3216 0.4050 -0.0129 0.0166  -0.0432 169 LEU   A CD2 
3891 C  CD2 B LEU   A 169 ? 0.2869 0.3127 0.3296 0.0032  0.0137  -0.0132 169 LEU   A CD2 
3892 O  OXT A LEU   A 169 ? 0.3079 0.2900 0.4293 -0.0210 0.0348  -0.0233 169 LEU   A OXT 
3893 O  OXT B LEU   A 169 ? 0.2743 0.3076 0.3177 -0.0090 0.0336  -0.0294 169 LEU   A OXT 
3916 N  N   A SER   B 1   ? 0.3509 0.3591 0.3734 -0.0865 -0.0796 0.0465  1   SER   B N   
3917 N  N   B SER   B 1   ? 0.3277 0.3213 0.3568 -0.0990 -0.0658 0.0196  1   SER   B N   
3918 C  CA  A SER   B 1   ? 0.3452 0.3582 0.3741 -0.0895 -0.0824 0.0468  1   SER   B CA  
3919 C  CA  B SER   B 1   ? 0.3197 0.3235 0.3555 -0.1034 -0.0712 0.0184  1   SER   B CA  
3920 C  C   A SER   B 1   ? 0.3264 0.3523 0.3588 -0.0916 -0.0828 0.0650  1   SER   B C   
3921 C  C   B SER   B 1   ? 0.2990 0.3254 0.3375 -0.1030 -0.0764 0.0413  1   SER   B C   
3922 O  O   A SER   B 1   ? 0.3349 0.3511 0.3397 -0.0868 -0.0820 0.0668  1   SER   B O   
3923 O  O   B SER   B 1   ? 0.3065 0.3244 0.3161 -0.0997 -0.0704 0.0412  1   SER   B O   
3924 C  CB  A SER   B 1   ? 0.3551 0.3607 0.3900 -0.0884 -0.0802 0.0330  1   SER   B CB  
3925 C  CB  B SER   B 1   ? 0.3290 0.3198 0.3728 -0.1059 -0.0674 -0.0035 1   SER   B CB  
3926 O  OG  A SER   B 1   ? 0.3659 0.3667 0.4164 -0.0867 -0.0705 0.0257  1   SER   B OG  
3927 O  OG  B SER   B 1   ? 0.3390 0.3230 0.4000 -0.1065 -0.0610 -0.0162 1   SER   B OG  
3942 N  N   A MET   B 2   ? 0.3031 0.3470 0.3620 -0.0944 -0.0778 0.0909  2   MET   B N   
3943 N  N   B MET   B 2   ? 0.2782 0.3279 0.3368 -0.0986 -0.0805 0.0760  2   MET   B N   
3944 C  CA  A MET   B 2   ? 0.2854 0.3455 0.3732 -0.0848 -0.0736 0.1066  2   MET   B CA  
3945 C  CA  B MET   B 2   ? 0.2652 0.3338 0.3426 -0.0807 -0.0839 0.1034  2   MET   B CA  
3946 C  C   A MET   B 2   ? 0.2501 0.3248 0.3322 -0.0794 -0.0873 0.1325  2   MET   B C   
3947 C  C   B MET   B 2   ? 0.2401 0.3209 0.3192 -0.0760 -0.0910 0.1318  2   MET   B C   
3948 O  O   A MET   B 2   ? 0.2446 0.3314 0.3311 -0.0725 -0.0964 0.1343  2   MET   B O   
3949 O  O   B MET   B 2   ? 0.2349 0.3311 0.3239 -0.0668 -0.0995 0.1309  2   MET   B O   
3950 C  CB  A MET   B 2   ? 0.3089 0.3692 0.4445 -0.0692 -0.0494 0.0860  2   MET   B CB  
3951 C  CB  B MET   B 2   ? 0.2848 0.3568 0.3904 -0.0557 -0.0710 0.0942  2   MET   B CB  
3952 C  CG  A MET   B 2   ? 0.3307 0.3890 0.5132 -0.0540 -0.0253 0.0726  2   MET   B CG  
3953 C  CG  B MET   B 2   ? 0.3024 0.3748 0.4273 -0.0329 -0.0594 0.0959  2   MET   B CG  
3954 S  SD  A MET   B 2   ? 0.3513 0.4064 0.5763 -0.0405 -0.0086 0.0609  2   MET   B SD  
3955 S  SD  B MET   B 2   ? 0.3184 0.3915 0.4554 -0.0122 -0.0590 0.0988  2   MET   B SD  
3956 C  CE  A MET   B 2   ? 0.3520 0.4088 0.5872 -0.0410 -0.0004 0.0581  2   MET   B CE  
3957 C  CE  B MET   B 2   ? 0.3195 0.3953 0.4737 -0.0124 -0.0482 0.0914  2   MET   B CE  
3976 N  N   . VAL   B 3   ? 0.2203 0.2949 0.3029 -0.0888 -0.0852 0.1502  3   VAL   B N   
3977 C  CA  . VAL   B 3   ? 0.2112 0.2583 0.2995 -0.0812 -0.0738 0.1340  3   VAL   B CA  
3978 C  C   . VAL   B 3   ? 0.1973 0.2528 0.2579 -0.0747 -0.0749 0.1165  3   VAL   B C   
3979 O  O   . VAL   B 3   ? 0.1933 0.2753 0.2574 -0.0755 -0.0788 0.1202  3   VAL   B O   
3980 C  CB  . VAL   B 3   ? 0.2270 0.2514 0.3559 -0.0723 -0.0611 0.1121  3   VAL   B CB  
3981 C  CG1 . VAL   B 3   ? 0.2361 0.2438 0.3751 -0.0706 -0.0627 0.1090  3   VAL   B CG1 
3982 C  CG2 . VAL   B 3   ? 0.2325 0.2527 0.3694 -0.0609 -0.0469 0.1256  3   VAL   B CG2 
3993 N  N   . ASN   B 4   ? 0.1897 0.2255 0.2178 -0.0716 -0.0659 0.0924  4   ASN   B N   
3994 C  CA  . ASN   B 4   ? 0.1872 0.2237 0.1800 -0.0673 -0.0548 0.0605  4   ASN   B CA  
3995 C  C   . ASN   B 4   ? 0.1905 0.2358 0.1703 -0.0642 -0.0458 0.0455  4   ASN   B C   
3996 O  O   . ASN   B 4   ? 0.1933 0.2430 0.1918 -0.0577 -0.0416 0.0200  4   ASN   B O   
3997 C  CB  . ASN   B 4   ? 0.1894 0.2111 0.1690 -0.0607 -0.0522 0.0489  4   ASN   B CB  
3998 C  CG  . ASN   B 4   ? 0.1878 0.1940 0.1693 -0.0549 -0.0513 0.0366  4   ASN   B CG  
3999 O  OD1 . ASN   B 4   ? 0.1871 0.1766 0.1762 -0.0488 -0.0567 0.0361  4   ASN   B OD1 
4000 N  ND2 . ASN   B 4   ? 0.2084 0.1994 0.1698 -0.0331 -0.0402 0.0274  4   ASN   B ND2 
4007 N  N   . SER   B 5   ? 0.1969 0.2497 0.1902 -0.0694 -0.0379 0.0396  5   SER   B N   
4008 C  CA  . SER   B 5   ? 0.2189 0.2899 0.2110 -0.0585 -0.0145 0.0397  5   SER   B CA  
4009 C  C   . SER   B 5   ? 0.2436 0.2998 0.2367 -0.0806 0.0161  0.0297  5   SER   B C   
4010 O  O   . SER   B 5   ? 0.2648 0.2969 0.3011 -0.0724 0.0519  0.0288  5   SER   B O   
4011 C  CB  . SER   B 5   ? 0.2256 0.3099 0.2502 -0.0445 -0.0009 0.0520  5   SER   B CB  
4012 O  OG  . SER   B 5   ? 0.2497 0.3323 0.3088 -0.0275 -0.0015 0.0547  5   SER   B OG  
4018 N  N   . PHE   B 6   ? 0.2689 0.3231 0.2173 -0.0867 0.0342  0.0314  6   PHE   B N   
4019 C  CA  . PHE   B 6   ? 0.2835 0.3256 0.1854 -0.1079 0.0374  0.0169  6   PHE   B CA  
4020 C  C   . PHE   B 6   ? 0.3403 0.3566 0.2379 -0.1099 0.0619  -0.0071 6   PHE   B C   
4021 O  O   . PHE   B 6   ? 0.3554 0.3807 0.2728 -0.1018 0.0450  -0.0186 6   PHE   B O   
4022 C  CB  . PHE   B 6   ? 0.2546 0.3020 0.1707 -0.1049 0.0078  0.0152  6   PHE   B CB  
4023 C  CG  . PHE   B 6   ? 0.2276 0.2718 0.1707 -0.0956 -0.0066 0.0191  6   PHE   B CG  
4024 C  CD1 . PHE   B 6   ? 0.2262 0.2429 0.1575 -0.0851 -0.0184 0.0168  6   PHE   B CD1 
4025 C  CD2 . PHE   B 6   ? 0.2078 0.2693 0.1681 -0.0796 -0.0115 0.0401  6   PHE   B CD2 
4026 C  CE1 . PHE   B 6   ? 0.2207 0.2138 0.1602 -0.0735 -0.0230 0.0227  6   PHE   B CE1 
4027 C  CE2 . PHE   B 6   ? 0.2069 0.2454 0.1931 -0.0650 -0.0053 0.0420  6   PHE   B CE2 
4028 C  CZ  . PHE   B 6   ? 0.2094 0.2187 0.1758 -0.0686 -0.0151 0.0282  6   PHE   B CZ  
4038 N  N   . SER   B 7   ? 0.3795 0.3504 0.2692 -0.1275 0.1013  -0.0262 7   SER   B N   
4039 C  CA  . SER   B 7   ? 0.4159 0.3659 0.3312 -0.1276 0.1282  -0.0370 7   SER   B CA  
4040 C  C   . SER   B 7   ? 0.4147 0.3369 0.3156 -0.1360 0.1432  -0.0553 7   SER   B C   
4041 O  O   . SER   B 7   ? 0.4250 0.3333 0.3377 -0.1461 0.1427  -0.0542 7   SER   B O   
4042 C  CB  . SER   B 7   ? 0.4387 0.3909 0.4027 -0.1242 0.1451  -0.0294 7   SER   B CB  
4043 O  OG  . SER   B 7   ? 0.4522 0.3972 0.4557 -0.1220 0.1508  -0.0239 7   SER   B OG  
4049 N  N   A GLY   B 8   ? 0.4122 0.3253 0.3085 -0.1273 0.1443  -0.0637 8   GLY   B N   
4050 N  N   B GLY   B 8   ? 0.4121 0.3247 0.3078 -0.1276 0.1446  -0.0640 8   GLY   B N   
4051 C  CA  A GLY   B 8   ? 0.4025 0.3107 0.3026 -0.1219 0.1456  -0.0691 8   GLY   B CA  
4052 C  CA  B GLY   B 8   ? 0.4023 0.3094 0.3014 -0.1225 0.1463  -0.0696 8   GLY   B CA  
4053 C  C   A GLY   B 8   ? 0.3908 0.2911 0.2936 -0.1177 0.1444  -0.0695 8   GLY   B C   
4054 C  C   B GLY   B 8   ? 0.3905 0.2892 0.2921 -0.1186 0.1455  -0.0701 8   GLY   B C   
4055 O  O   A GLY   B 8   ? 0.3994 0.2995 0.3135 -0.1096 0.1440  -0.0727 8   GLY   B O   
4056 O  O   B GLY   B 8   ? 0.3984 0.2947 0.3111 -0.1127 0.1460  -0.0740 8   GLY   B O   
4063 N  N   . TYR   B 9   ? 0.3755 0.2693 0.2720 -0.1120 0.1294  -0.0761 9   TYR   B N   
4064 C  CA  . TYR   B 9   ? 0.3486 0.2323 0.2401 -0.0942 0.0971  -0.0623 9   TYR   B CA  
4065 C  C   . TYR   B 9   ? 0.3387 0.2229 0.2223 -0.0908 0.0635  -0.0491 9   TYR   B C   
4066 O  O   . TYR   B 9   ? 0.3470 0.2390 0.2555 -0.0916 0.0701  -0.0324 9   TYR   B O   
4067 C  CB  . TYR   B 9   ? 0.3387 0.2108 0.2409 -0.0813 0.0899  -0.0564 9   TYR   B CB  
4068 C  CG  . TYR   B 9   ? 0.3235 0.1919 0.2426 -0.0854 0.0791  -0.0514 9   TYR   B CG  
4069 C  CD1 . TYR   B 9   ? 0.3201 0.1863 0.2527 -0.0994 0.0770  -0.0459 9   TYR   B CD1 
4070 C  CD2 . TYR   B 9   ? 0.3086 0.1868 0.2378 -0.0803 0.0693  -0.0562 9   TYR   B CD2 
4071 C  CE1 . TYR   B 9   ? 0.3112 0.1980 0.2572 -0.1016 0.0755  -0.0539 9   TYR   B CE1 
4072 C  CE2 . TYR   B 9   ? 0.3044 0.1907 0.2466 -0.0802 0.0700  -0.0490 9   TYR   B CE2 
4073 C  CZ  . TYR   B 9   ? 0.3027 0.1999 0.2497 -0.0928 0.0725  -0.0609 9   TYR   B CZ  
4074 O  OH  . TYR   B 9   ? 0.2994 0.2142 0.2572 -0.0954 0.0661  -0.0779 9   TYR   B OH  
4085 N  N   . LEU   B 10  ? 0.3199 0.1987 0.2070 -0.0922 0.0316  -0.0476 10  LEU   B N   
4086 C  CA  . LEU   B 10  ? 0.3164 0.2002 0.2002 -0.0956 -0.0053 -0.0344 10  LEU   B CA  
4087 C  C   . LEU   B 10  ? 0.3071 0.2054 0.2022 -0.0888 -0.0238 -0.0301 10  LEU   B C   
4088 O  O   . LEU   B 10  ? 0.2896 0.2030 0.1995 -0.0809 -0.0176 -0.0224 10  LEU   B O   
4089 C  CB  . LEU   B 10  ? 0.3288 0.1992 0.2181 -0.0956 -0.0231 -0.0200 10  LEU   B CB  
4090 C  CG  . LEU   B 10  ? 0.3413 0.2045 0.2461 -0.0937 -0.0510 -0.0041 10  LEU   B CG  
4091 C  CD1 . LEU   B 10  ? 0.3496 0.2146 0.2673 -0.0864 -0.0483 0.0022  10  LEU   B CD1 
4092 C  CD2 . LEU   B 10  ? 0.3455 0.2111 0.2635 -0.0957 -0.0465 0.0195  10  LEU   B CD2 
4104 N  N   A LYS   B 11  ? 0.3162 0.2246 0.2173 -0.0849 -0.0321 -0.0279 11  LYS   B N   
4105 N  N   B LYS   B 11  ? 0.3157 0.2259 0.2181 -0.0833 -0.0316 -0.0278 11  LYS   B N   
4106 C  CA  A LYS   B 11  ? 0.3279 0.2475 0.2571 -0.0765 -0.0379 -0.0333 11  LYS   B CA  
4107 C  CA  B LYS   B 11  ? 0.3268 0.2499 0.2586 -0.0734 -0.0368 -0.0327 11  LYS   B CA  
4108 C  C   A LYS   B 11  ? 0.3072 0.2306 0.2485 -0.0915 -0.0377 -0.0389 11  LYS   B C   
4109 C  C   B LYS   B 11  ? 0.3070 0.2340 0.2501 -0.0872 -0.0353 -0.0368 11  LYS   B C   
4110 O  O   A LYS   B 11  ? 0.3159 0.2385 0.2582 -0.1065 -0.0439 -0.0603 11  LYS   B O   
4111 O  O   B LYS   B 11  ? 0.3159 0.2456 0.2604 -0.0974 -0.0385 -0.0542 11  LYS   B O   
4112 C  CB  A LYS   B 11  ? 0.3600 0.2870 0.3288 -0.0550 -0.0410 -0.0354 11  LYS   B CB  
4113 C  CB  B LYS   B 11  ? 0.3576 0.2894 0.3310 -0.0514 -0.0401 -0.0351 11  LYS   B CB  
4114 C  CG  A LYS   B 11  ? 0.3856 0.3152 0.3996 -0.0401 -0.0411 -0.0376 11  LYS   B CG  
4115 C  CG  B LYS   B 11  ? 0.3820 0.3174 0.4028 -0.0362 -0.0405 -0.0377 11  LYS   B CG  
4116 C  CD  A LYS   B 11  ? 0.4060 0.3356 0.4578 -0.0280 -0.0405 -0.0384 11  LYS   B CD  
4117 C  CD  B LYS   B 11  ? 0.4012 0.3374 0.4624 -0.0245 -0.0401 -0.0392 11  LYS   B CD  
4118 C  CE  A LYS   B 11  ? 0.4194 0.3499 0.5011 -0.0203 -0.0405 -0.0396 11  LYS   B CE  
4119 C  CE  B LYS   B 11  ? 0.4139 0.3512 0.5068 -0.0169 -0.0399 -0.0401 11  LYS   B CE  
4120 N  NZ  A LYS   B 11  ? 0.4268 0.3585 0.5241 -0.0161 -0.0407 -0.0390 11  LYS   B NZ  
4121 N  NZ  B LYS   B 11  ? 0.4208 0.3592 0.5304 -0.0133 -0.0399 -0.0395 11  LYS   B NZ  
4148 N  N   . LEU   B 12  ? 0.2772 0.2119 0.2437 -0.0860 -0.0417 -0.0366 12  LEU   B N   
4149 C  CA  . LEU   B 12  ? 0.2443 0.1882 0.2511 -0.0682 -0.0259 -0.0285 12  LEU   B CA  
4150 C  C   . LEU   B 12  ? 0.2220 0.1853 0.2568 -0.0675 -0.0428 -0.0212 12  LEU   B C   
4151 O  O   . LEU   B 12  ? 0.2185 0.1903 0.2785 -0.0721 -0.0634 -0.0172 12  LEU   B O   
4152 C  CB  . LEU   B 12  ? 0.2442 0.1667 0.2462 -0.0467 -0.0127 -0.0264 12  LEU   B CB  
4153 C  CG  . LEU   B 12  ? 0.2427 0.1579 0.2417 -0.0458 -0.0053 -0.0257 12  LEU   B CG  
4154 C  CD1 . LEU   B 12  ? 0.2487 0.1587 0.2416 -0.0268 -0.0033 -0.0100 12  LEU   B CD1 
4155 C  CD2 . LEU   B 12  ? 0.2486 0.1609 0.2490 -0.0471 -0.0010 -0.0318 12  LEU   B CD2 
4168 N  N   . THR   B 13  ? 0.2206 0.1920 0.2530 -0.0640 -0.0453 -0.0297 13  THR   B N   
4169 C  CA  . THR   B 13  ? 0.2193 0.1958 0.2484 -0.0687 -0.0706 -0.0173 13  THR   B CA  
4170 C  C   . THR   B 13  ? 0.2599 0.2113 0.2601 -0.0768 -0.0894 -0.0100 13  THR   B C   
4171 O  O   . THR   B 13  ? 0.2806 0.2128 0.2863 -0.0722 -0.0586 -0.0146 13  THR   B O   
4172 C  CB  . THR   B 13  ? 0.2014 0.1958 0.2586 -0.0604 -0.0580 -0.0138 13  THR   B CB  
4173 O  OG1 . THR   B 13  ? 0.1901 0.1920 0.2574 -0.0553 -0.0415 -0.0127 13  THR   B OG1 
4174 C  CG2 . THR   B 13  ? 0.2141 0.2019 0.2710 -0.0525 -0.0442 -0.0102 13  THR   B CG2 
4182 N  N   . ASP   B 14  ? 0.2823 0.2257 0.2720 -0.0830 -0.1164 0.0095  14  ASP   B N   
4183 C  CA  . ASP   B 14  ? 0.2996 0.2458 0.2992 -0.0818 -0.1269 0.0231  14  ASP   B CA  
4184 C  C   . ASP   B 14  ? 0.2814 0.2276 0.2625 -0.0841 -0.1074 0.0253  14  ASP   B C   
4185 O  O   . ASP   B 14  ? 0.3090 0.2524 0.2739 -0.0925 -0.0968 0.0291  14  ASP   B O   
4186 C  CB  . ASP   B 14  ? 0.3270 0.2884 0.3766 -0.0740 -0.1343 0.0319  14  ASP   B CB  
4187 C  CG  . ASP   B 14  ? 0.3549 0.3271 0.4592 -0.0644 -0.1297 0.0199  14  ASP   B CG  
4188 O  OD1 . ASP   B 14  ? 0.3713 0.3411 0.4811 -0.0633 -0.1302 0.0084  14  ASP   B OD1 
4189 O  OD2 . ASP   B 14  ? 0.3608 0.3461 0.5021 -0.0645 -0.1238 0.0211  14  ASP   B OD2 
4194 N  N   . ASN   B 15  ? 0.2385 0.1908 0.2289 -0.0580 -0.1013 0.0259  15  ASN   B N   
4195 C  CA  . ASN   B 15  ? 0.1997 0.1693 0.2244 -0.0367 -0.0684 0.0110  15  ASN   B CA  
4196 C  C   . ASN   B 15  ? 0.1793 0.1514 0.2172 -0.0265 -0.0517 0.0014  15  ASN   B C   
4197 O  O   . ASN   B 15  ? 0.1731 0.1413 0.2350 -0.0313 -0.0534 -0.0049 15  ASN   B O   
4198 C  CB  . ASN   B 15  ? 0.1834 0.1601 0.2404 -0.0172 -0.0696 0.0142  15  ASN   B CB  
4199 C  CG  . ASN   B 15  ? 0.1693 0.1636 0.2548 -0.0245 -0.0427 0.0165  15  ASN   B CG  
4200 O  OD1 . ASN   B 15  ? 0.1743 0.1953 0.2883 -0.0448 -0.0439 0.0216  15  ASN   B OD1 
4201 N  ND2 . ASN   B 15  ? 0.1688 0.1451 0.2342 -0.0179 -0.0106 -0.0055 15  ASN   B ND2 
4208 N  N   . VAL   B 16  ? 0.1809 0.1472 0.2222 -0.0336 -0.0597 -0.0008 16  VAL   B N   
4209 C  CA  . VAL   B 16  ? 0.1760 0.1463 0.2056 -0.0319 -0.0497 -0.0150 16  VAL   B CA  
4210 C  C   . VAL   B 16  ? 0.1750 0.1611 0.1931 -0.0397 -0.0518 -0.0065 16  VAL   B C   
4211 O  O   . VAL   B 16  ? 0.1819 0.1710 0.2185 -0.0332 -0.0474 -0.0218 16  VAL   B O   
4212 C  CB  . VAL   B 16  ? 0.1751 0.1431 0.2189 -0.0156 -0.0329 -0.0172 16  VAL   B CB  
4213 C  CG1 . VAL   B 16  ? 0.1796 0.1486 0.2135 -0.0074 -0.0229 -0.0109 16  VAL   B CG1 
4214 C  CG2 . VAL   B 16  ? 0.1766 0.1433 0.2375 -0.0055 -0.0290 -0.0194 16  VAL   B CG2 
4224 N  N   . TYR   B 17  ? 0.1812 0.1671 0.1911 -0.0364 -0.0409 -0.0133 17  TYR   B N   
4225 C  CA  . TYR   B 17  ? 0.1901 0.1889 0.1821 -0.0527 -0.0433 0.0069  17  TYR   B CA  
4226 C  C   . TYR   B 17  ? 0.1830 0.1560 0.1909 -0.0487 -0.0224 -0.0067 17  TYR   B C   
4227 O  O   . TYR   B 17  ? 0.1803 0.1652 0.1988 -0.0399 -0.0309 -0.0341 17  TYR   B O   
4228 C  CB  . TYR   B 17  ? 0.2279 0.2494 0.2254 -0.0426 -0.0494 0.0405  17  TYR   B CB  
4229 C  CG  . TYR   B 17  ? 0.2654 0.3070 0.2843 -0.0347 -0.0752 0.0578  17  TYR   B CG  
4230 C  CD1 . TYR   B 17  ? 0.2884 0.3300 0.3159 -0.0294 -0.0855 0.0727  17  TYR   B CD1 
4231 C  CD2 . TYR   B 17  ? 0.2899 0.3396 0.3197 -0.0254 -0.0869 0.0635  17  TYR   B CD2 
4232 C  CE1 . TYR   B 17  ? 0.3096 0.3583 0.3430 -0.0200 -0.0947 0.0781  17  TYR   B CE1 
4233 C  CE2 . TYR   B 17  ? 0.3105 0.3626 0.3476 -0.0131 -0.0975 0.0752  17  TYR   B CE2 
4234 C  CZ  . TYR   B 17  ? 0.3224 0.3714 0.3570 -0.0119 -0.1025 0.0813  17  TYR   B CZ  
4235 O  OH  . TYR   B 17  ? 0.3376 0.3854 0.3700 -0.0082 -0.1090 0.0819  17  TYR   B OH  
4245 N  N   . ILE   B 18  ? 0.1895 0.1581 0.1792 -0.0402 -0.0186 -0.0151 18  ILE   B N   
4246 C  CA  . ILE   B 18  ? 0.1901 0.1560 0.1814 -0.0455 -0.0007 -0.0254 18  ILE   B CA  
4247 C  C   . ILE   B 18  ? 0.2062 0.1601 0.1871 -0.0553 0.0007  -0.0403 18  ILE   B C   
4248 O  O   . ILE   B 18  ? 0.2293 0.1756 0.1887 -0.0508 0.0105  -0.0384 18  ILE   B O   
4249 C  CB  . ILE   B 18  ? 0.1947 0.1565 0.1914 -0.0544 -0.0042 -0.0163 18  ILE   B CB  
4250 C  CG1 . ILE   B 18  ? 0.1996 0.1654 0.1967 -0.0526 -0.0021 -0.0118 18  ILE   B CG1 
4251 C  CG2 . ILE   B 18  ? 0.2064 0.1704 0.1964 -0.0542 -0.0141 -0.0178 18  ILE   B CG2 
4252 C  CD1 . ILE   B 18  ? 0.2094 0.1912 0.2166 -0.0485 -0.0207 0.0109  18  ILE   B CD1 
4264 N  N   . LYS   B 19  ? 0.2095 0.1598 0.2024 -0.0379 0.0379  -0.0421 19  LYS   B N   
4265 C  CA  . LYS   B 19  ? 0.2191 0.1675 0.2266 -0.0409 0.0339  -0.0533 19  LYS   B CA  
4266 C  C   . LYS   B 19  ? 0.2039 0.1659 0.2387 -0.0321 0.0400  -0.0638 19  LYS   B C   
4267 O  O   . LYS   B 19  ? 0.1995 0.1697 0.2224 -0.0266 0.0310  -0.0599 19  LYS   B O   
4268 C  CB  . LYS   B 19  ? 0.2495 0.1963 0.2451 -0.0497 0.0485  -0.0483 19  LYS   B CB  
4269 C  CG  . LYS   B 19  ? 0.2822 0.2206 0.2696 -0.0594 0.0730  -0.0502 19  LYS   B CG  
4270 C  CD  . LYS   B 19  ? 0.3143 0.2499 0.2892 -0.0653 0.0937  -0.0444 19  LYS   B CD  
4271 C  CE  . LYS   B 19  ? 0.3411 0.2729 0.3174 -0.0678 0.0901  -0.0475 19  LYS   B CE  
4272 N  NZ  . LYS   B 19  ? 0.3569 0.2844 0.3251 -0.0686 0.0886  -0.0500 19  LYS   B NZ  
4286 N  N   . ASN   B 20  ? 0.1998 0.1786 0.2652 -0.0259 0.0468  -0.0745 20  ASN   B N   
4287 C  CA  . ASN   B 20  ? 0.2009 0.1853 0.2881 -0.0162 0.0487  -0.0939 20  ASN   B CA  
4288 C  C   . ASN   B 20  ? 0.1996 0.2088 0.2840 -0.0201 0.0603  -0.1024 20  ASN   B C   
4289 O  O   . ASN   B 20  ? 0.2189 0.2421 0.3010 -0.0252 0.0508  -0.0922 20  ASN   B O   
4290 C  CB  . ASN   B 20  ? 0.2235 0.1930 0.3269 0.0026  0.0320  -0.0948 20  ASN   B CB  
4291 C  CG  . ASN   B 20  ? 0.2494 0.1992 0.3504 0.0280  0.0297  -0.1097 20  ASN   B CG  
4292 O  OD1 . ASN   B 20  ? 0.2758 0.2305 0.3711 0.0379  0.0276  -0.1111 20  ASN   B OD1 
4293 N  ND2 . ASN   B 20  ? 0.2421 0.1995 0.3454 0.0233  0.0201  -0.1093 20  ASN   B ND2 
4300 N  N   . ALA   B 21  ? 0.1950 0.2025 0.2777 -0.0311 0.0622  -0.0929 21  ALA   B N   
4301 C  CA  . ALA   B 21  ? 0.2030 0.2080 0.2854 -0.0347 0.0541  -0.0723 21  ALA   B CA  
4302 C  C   . ALA   B 21  ? 0.1990 0.1829 0.2695 -0.0280 0.0519  -0.0518 21  ALA   B C   
4303 O  O   . ALA   B 21  ? 0.2077 0.1741 0.2609 -0.0339 0.0464  -0.0397 21  ALA   B O   
4304 C  CB  . ALA   B 21  ? 0.2178 0.2387 0.3050 -0.0459 0.0446  -0.0520 21  ALA   B CB  
4310 N  N   . ASP   B 22  ? 0.1941 0.1716 0.2579 -0.0290 0.0432  -0.0434 22  ASP   B N   
4311 C  CA  . ASP   B 22  ? 0.1875 0.1581 0.2463 -0.0195 0.0309  -0.0326 22  ASP   B CA  
4312 C  C   . ASP   B 22  ? 0.1818 0.1515 0.2015 -0.0220 0.0216  -0.0143 22  ASP   B C   
4313 O  O   . ASP   B 22  ? 0.1880 0.1585 0.2030 -0.0183 0.0105  -0.0104 22  ASP   B O   
4314 C  CB  . ASP   B 22  ? 0.1949 0.1623 0.2943 -0.0054 0.0279  -0.0236 22  ASP   B CB  
4315 C  CG  . ASP   B 22  ? 0.1980 0.1814 0.3424 0.0046  -0.0015 -0.0220 22  ASP   B CG  
4316 O  OD1 . ASP   B 22  ? 0.2076 0.1742 0.3322 0.0073  -0.0207 -0.0187 22  ASP   B OD1 
4317 O  OD2 . ASP   B 22  ? 0.2048 0.2099 0.4019 0.0192  -0.0279 -0.0298 22  ASP   B OD2 
4322 N  N   . ILE   B 23  ? 0.1824 0.1440 0.1841 -0.0139 0.0120  0.0117  23  ILE   B N   
4323 C  CA  . ILE   B 23  ? 0.1715 0.1429 0.1725 -0.0123 0.0036  0.0076  23  ILE   B CA  
4324 C  C   . ILE   B 23  ? 0.1662 0.1412 0.1665 -0.0097 -0.0110 0.0011  23  ILE   B C   
4325 O  O   . ILE   B 23  ? 0.1525 0.1465 0.1567 -0.0090 -0.0078 0.0043  23  ILE   B O   
4326 C  CB  . ILE   B 23  ? 0.1668 0.1459 0.1771 -0.0185 0.0001  0.0163  23  ILE   B CB  
4327 C  CG1 . ILE   B 23  ? 0.1626 0.1591 0.1841 -0.0110 0.0045  0.0234  23  ILE   B CG1 
4328 C  CG2 . ILE   B 23  ? 0.1767 0.1630 0.1938 -0.0134 -0.0002 0.0127  23  ILE   B CG2 
4329 C  CD1 . ILE   B 23  ? 0.1763 0.1723 0.1933 -0.0122 0.0055  0.0205  23  ILE   B CD1 
4341 N  N   . VAL   B 24  ? 0.1653 0.1435 0.1735 -0.0127 -0.0058 0.0051  24  VAL   B N   
4342 C  CA  . VAL   B 24  ? 0.1622 0.1509 0.1939 -0.0075 -0.0123 0.0008  24  VAL   B CA  
4343 C  C   . VAL   B 24  ? 0.1607 0.1522 0.1921 -0.0118 -0.0050 0.0007  24  VAL   B C   
4344 O  O   . VAL   B 24  ? 0.1580 0.1588 0.2035 -0.0186 -0.0015 0.0093  24  VAL   B O   
4345 C  CB  . VAL   B 24  ? 0.1669 0.1667 0.1995 -0.0012 -0.0187 0.0002  24  VAL   B CB  
4346 C  CG1 . VAL   B 24  ? 0.1675 0.1712 0.2203 -0.0093 -0.0219 -0.0011 24  VAL   B CG1 
4347 C  CG2 . VAL   B 24  ? 0.1812 0.1955 0.2011 0.0060  -0.0136 -0.0078 24  VAL   B CG2 
4357 N  N   . GLU   B 25  ? 0.1811 0.1653 0.1970 -0.0079 0.0084  0.0021  25  GLU   B N   
4358 C  CA  . GLU   B 25  ? 0.1964 0.1974 0.2214 0.0024  0.0167  -0.0142 25  GLU   B CA  
4359 C  C   . GLU   B 25  ? 0.1884 0.1955 0.1849 -0.0131 0.0154  -0.0047 25  GLU   B C   
4360 O  O   . GLU   B 25  ? 0.1945 0.2087 0.1993 -0.0185 0.0249  -0.0021 25  GLU   B O   
4361 C  CB  . GLU   B 25  ? 0.2335 0.2497 0.3082 0.0277  0.0290  -0.0224 25  GLU   B CB  
4362 C  CG  . GLU   B 25  ? 0.2700 0.3180 0.4232 0.0365  0.0290  -0.0246 25  GLU   B CG  
4363 C  CD  . GLU   B 25  ? 0.3208 0.3702 0.5147 0.0331  0.0270  -0.0240 25  GLU   B CD  
4364 O  OE1 . GLU   B 25  ? 0.3295 0.3919 0.5457 0.0364  0.0303  -0.0222 25  GLU   B OE1 
4365 O  OE2 . GLU   B 25  ? 0.3242 0.3918 0.5468 0.0313  0.0224  -0.0266 25  GLU   B OE2 
4372 N  N   A GLU   B 26  ? 0.1889 0.1873 0.1695 -0.0267 0.0159  -0.0052 26  GLU   B N   
4373 N  N   B GLU   B 26  ? 0.1829 0.1882 0.1775 -0.0247 0.0145  0.0036  26  GLU   B N   
4374 C  CA  A GLU   B 26  ? 0.1938 0.1955 0.1707 -0.0371 0.0012  -0.0029 26  GLU   B CA  
4375 C  CA  B GLU   B 26  ? 0.1816 0.1972 0.1895 -0.0327 -0.0004 0.0139  26  GLU   B CA  
4376 C  C   A GLU   B 26  ? 0.1793 0.1879 0.1644 -0.0340 0.0017  0.0068  26  GLU   B C   
4377 C  C   B GLU   B 26  ? 0.1718 0.1888 0.1720 -0.0312 0.0037  0.0163  26  GLU   B C   
4378 O  O   A GLU   B 26  ? 0.1903 0.2025 0.1739 -0.0314 -0.0062 0.0128  26  GLU   B O   
4379 O  O   B GLU   B 26  ? 0.1812 0.2033 0.1801 -0.0280 0.0002  0.0235  26  GLU   B O   
4380 C  CB  A GLU   B 26  ? 0.2244 0.2106 0.1806 -0.0422 0.0092  0.0019  26  GLU   B CB  
4381 C  CB  B GLU   B 26  ? 0.2028 0.2138 0.2225 -0.0349 0.0026  0.0320  26  GLU   B CB  
4382 C  CG  A GLU   B 26  ? 0.2556 0.2273 0.2133 -0.0477 0.0247  -0.0063 26  GLU   B CG  
4383 C  CG  B GLU   B 26  ? 0.2253 0.2337 0.2777 -0.0390 0.0124  0.0315  26  GLU   B CG  
4384 C  CD  A GLU   B 26  ? 0.2769 0.2341 0.2186 -0.0603 0.0477  -0.0170 26  GLU   B CD  
4385 C  CD  B GLU   B 26  ? 0.2348 0.2399 0.3047 -0.0533 0.0228  0.0259  26  GLU   B CD  
4386 O  OE1 A GLU   B 26  ? 0.2860 0.2274 0.2047 -0.0622 0.0807  -0.0195 26  GLU   B OE1 
4387 O  OE1 B GLU   B 26  ? 0.2383 0.2425 0.3298 -0.0668 0.0385  0.0062  26  GLU   B OE1 
4388 O  OE2 A GLU   B 26  ? 0.2831 0.2429 0.2313 -0.0633 0.0557  0.0050  26  GLU   B OE2 
4389 O  OE2 B GLU   B 26  ? 0.2353 0.2388 0.3048 -0.0527 0.0236  0.0338  26  GLU   B OE2 
4402 N  N   . ALA   B 27  ? 0.1585 0.1697 0.1651 -0.0332 0.0061  0.0110  27  ALA   B N   
4403 C  CA  . ALA   B 27  ? 0.1614 0.1649 0.1812 -0.0218 -0.0016 0.0223  27  ALA   B CA  
4404 C  C   . ALA   B 27  ? 0.1568 0.1851 0.2010 -0.0203 0.0091  0.0389  27  ALA   B C   
4405 O  O   . ALA   B 27  ? 0.1658 0.1860 0.2115 -0.0115 0.0071  0.0500  27  ALA   B O   
4406 C  CB  . ALA   B 27  ? 0.1721 0.1504 0.1705 -0.0192 0.0018  0.0180  27  ALA   B CB  
4413 N  N   . LYS   B 28  ? 0.1489 0.2082 0.2322 -0.0228 0.0162  0.0639  28  LYS   B N   
4414 C  CA  . LYS   B 28  ? 0.1706 0.2511 0.2576 -0.0130 0.0541  0.0875  28  LYS   B CA  
4415 C  C   . LYS   B 28  ? 0.1899 0.2663 0.2396 -0.0082 0.0593  0.0764  28  LYS   B C   
4416 O  O   . LYS   B 28  ? 0.2119 0.2768 0.2474 -0.0069 0.0676  0.0645  28  LYS   B O   
4417 C  CB  . LYS   B 28  ? 0.2057 0.2917 0.3253 -0.0017 0.0810  0.1188  28  LYS   B CB  
4418 C  CG  . LYS   B 28  ? 0.2506 0.3484 0.3882 0.0028  0.1074  0.1358  28  LYS   B CG  
4419 C  CD  . LYS   B 28  ? 0.3152 0.4021 0.4586 0.0057  0.1221  0.1469  28  LYS   B CD  
4420 C  CE  . LYS   B 28  ? 0.3654 0.4398 0.5158 0.0098  0.1233  0.1554  28  LYS   B CE  
4421 N  NZ  . LYS   B 28  ? 0.4284 0.4569 0.5475 0.0129  0.1203  0.1594  28  LYS   B NZ  
4435 N  N   . LYS   B 29  ? 0.2065 0.2849 0.2363 0.0032  0.0494  0.0648  29  LYS   B N   
4436 C  CA  . LYS   B 29  ? 0.2482 0.3183 0.2670 0.0020  0.0460  0.0614  29  LYS   B CA  
4437 C  C   . LYS   B 29  ? 0.2422 0.3142 0.2390 -0.0014 0.0275  0.0679  29  LYS   B C   
4438 O  O   . LYS   B 29  ? 0.2616 0.3324 0.2464 0.0090  0.0255  0.0654  29  LYS   B O   
4439 C  CB  . LYS   B 29  ? 0.3023 0.3571 0.3491 0.0023  0.0473  0.0537  29  LYS   B CB  
4440 C  CG  . LYS   B 29  ? 0.3445 0.3884 0.4384 0.0029  0.0496  0.0464  29  LYS   B CG  
4441 C  CD  . LYS   B 29  ? 0.3813 0.4121 0.5146 0.0023  0.0583  0.0396  29  LYS   B CD  
4442 C  CE  . LYS   B 29  ? 0.4062 0.4277 0.5695 0.0018  0.0664  0.0367  29  LYS   B CE  
4443 N  NZ  . LYS   B 29  ? 0.4177 0.4371 0.6007 0.0017  0.0703  0.0345  29  LYS   B NZ  
4457 N  N   . VAL   B 30  ? 0.2142 0.2915 0.2368 -0.0211 0.0134  0.0724  30  VAL   B N   
4458 C  CA  . VAL   B 30  ? 0.2045 0.2743 0.2674 -0.0326 -0.0191 0.0787  30  VAL   B CA  
4459 C  C   . VAL   B 30  ? 0.1797 0.2588 0.2471 -0.0361 -0.0210 0.0898  30  VAL   B C   
4460 O  O   . VAL   B 30  ? 0.1943 0.2753 0.2365 -0.0307 -0.0112 0.1004  30  VAL   B O   
4461 C  CB  . VAL   B 30  ? 0.2169 0.2713 0.3224 -0.0446 -0.0373 0.0763  30  VAL   B CB  
4462 C  CG1 . VAL   B 30  ? 0.2231 0.2815 0.3308 -0.0408 -0.0290 0.0711  30  VAL   B CG1 
4463 C  CG2 . VAL   B 30  ? 0.2300 0.2701 0.3402 -0.0486 -0.0453 0.0627  30  VAL   B CG2 
4473 N  N   A LYS   B 31  ? 0.1744 0.2321 0.2613 -0.0435 -0.0187 0.0968  31  LYS   B N   
4474 N  N   B LYS   B 31  ? 0.1762 0.2334 0.2589 -0.0427 -0.0209 0.0913  31  LYS   B N   
4475 C  CA  A LYS   B 31  ? 0.1652 0.2276 0.2855 -0.0445 -0.0163 0.0966  31  LYS   B CA  
4476 C  CA  B LYS   B 31  ? 0.1693 0.2292 0.2797 -0.0433 -0.0207 0.0872  31  LYS   B CA  
4477 C  C   A LYS   B 31  ? 0.1602 0.1966 0.2466 -0.0443 -0.0328 0.0852  31  LYS   B C   
4478 C  C   B LYS   B 31  ? 0.1633 0.1973 0.2419 -0.0439 -0.0361 0.0774  31  LYS   B C   
4479 O  O   A LYS   B 31  ? 0.1593 0.2041 0.2524 -0.0326 -0.0264 0.0944  31  LYS   B O   
4480 O  O   B LYS   B 31  ? 0.1638 0.2045 0.2439 -0.0329 -0.0324 0.0814  31  LYS   B O   
4481 C  CB  A LYS   B 31  ? 0.1736 0.2610 0.3386 -0.0414 0.0116  0.1037  31  LYS   B CB  
4482 C  CB  B LYS   B 31  ? 0.1805 0.2633 0.3287 -0.0392 0.0023  0.0880  31  LYS   B CB  
4483 C  CG  A LYS   B 31  ? 0.1950 0.2939 0.3899 -0.0371 0.0282  0.0972  31  LYS   B CG  
4484 C  CG  B LYS   B 31  ? 0.2033 0.2958 0.3765 -0.0350 0.0155  0.0772  31  LYS   B CG  
4485 C  CD  A LYS   B 31  ? 0.2149 0.3251 0.4322 -0.0320 0.0355  0.0866  31  LYS   B CD  
4486 C  CD  B LYS   B 31  ? 0.2231 0.3253 0.4187 -0.0322 0.0206  0.0660  31  LYS   B CD  
4487 C  CE  A LYS   B 31  ? 0.2311 0.3451 0.4683 -0.0278 0.0348  0.0762  31  LYS   B CE  
4488 C  CE  B LYS   B 31  ? 0.2373 0.3436 0.4553 -0.0306 0.0211  0.0571  31  LYS   B CE  
4489 N  NZ  A LYS   B 31  ? 0.2463 0.3580 0.4874 -0.0195 0.0283  0.0655  31  LYS   B NZ  
4490 N  NZ  B LYS   B 31  ? 0.2506 0.3558 0.4740 -0.0233 0.0139  0.0473  31  LYS   B NZ  
4517 N  N   . PRO   B 32  ? 0.1742 0.1693 0.2065 -0.0437 -0.0475 0.0575  32  PRO   B N   
4518 C  CA  . PRO   B 32  ? 0.1876 0.1604 0.1713 -0.0402 -0.0533 0.0373  32  PRO   B CA  
4519 C  C   . PRO   B 32  ? 0.1943 0.1502 0.1763 -0.0431 -0.0609 0.0392  32  PRO   B C   
4520 O  O   . PRO   B 32  ? 0.2088 0.1478 0.2030 -0.0450 -0.0811 0.0358  32  PRO   B O   
4521 C  CB  . PRO   B 32  ? 0.2089 0.1542 0.1635 -0.0458 -0.0398 0.0232  32  PRO   B CB  
4522 C  CG  . PRO   B 32  ? 0.2220 0.1438 0.1751 -0.0365 -0.0577 0.0312  32  PRO   B CG  
4523 C  CD  . PRO   B 32  ? 0.2027 0.1487 0.1972 -0.0304 -0.0631 0.0363  32  PRO   B CD  
4531 N  N   . THR   B 33  ? 0.1974 0.1372 0.1593 -0.0421 -0.0504 0.0280  33  THR   B N   
4532 C  CA  . THR   B 33  ? 0.2070 0.1382 0.1505 -0.0440 -0.0542 0.0359  33  THR   B CA  
4533 C  C   . THR   B 33  ? 0.2077 0.1340 0.1433 -0.0408 -0.0580 0.0201  33  THR   B C   
4534 O  O   . THR   B 33  ? 0.2250 0.1378 0.1553 -0.0504 -0.0607 0.0231  33  THR   B O   
4535 C  CB  . THR   B 33  ? 0.2198 0.1531 0.1520 -0.0313 -0.0594 0.0348  33  THR   B CB  
4536 O  OG1 . THR   B 33  ? 0.2073 0.1644 0.1680 -0.0308 -0.0593 0.0406  33  THR   B OG1 
4537 C  CG2 . THR   B 33  ? 0.2482 0.1615 0.1729 -0.0165 -0.0487 0.0209  33  THR   B CG2 
4545 N  N   . VAL   B 34  ? 0.1899 0.1292 0.1397 -0.0353 -0.0546 0.0175  34  VAL   B N   
4546 C  CA  . VAL   B 34  ? 0.1732 0.1316 0.1347 -0.0320 -0.0426 0.0152  34  VAL   B CA  
4547 C  C   . VAL   B 34  ? 0.1598 0.1243 0.1300 -0.0315 -0.0265 0.0075  34  VAL   B C   
4548 O  O   . VAL   B 34  ? 0.1772 0.1297 0.1299 -0.0320 -0.0358 0.0061  34  VAL   B O   
4549 C  CB  . VAL   B 34  ? 0.1815 0.1372 0.1568 -0.0171 -0.0349 0.0087  34  VAL   B CB  
4550 C  CG1 . VAL   B 34  ? 0.1785 0.1548 0.1591 -0.0156 -0.0178 -0.0012 34  VAL   B CG1 
4551 C  CG2 . VAL   B 34  ? 0.1902 0.1474 0.1821 -0.0163 -0.0378 0.0133  34  VAL   B CG2 
4561 N  N   . VAL   B 35  ? 0.1493 0.1213 0.1216 -0.0288 -0.0140 0.0076  35  VAL   B N   
4562 C  CA  . VAL   B 35  ? 0.1385 0.1222 0.1239 -0.0222 -0.0105 0.0098  35  VAL   B CA  
4563 C  C   . VAL   B 35  ? 0.1260 0.1190 0.1215 -0.0189 -0.0090 0.0101  35  VAL   B C   
4564 O  O   . VAL   B 35  ? 0.1379 0.1207 0.1201 -0.0218 -0.0037 -0.0028 35  VAL   B O   
4565 C  CB  . VAL   B 35  ? 0.1401 0.1408 0.1270 -0.0209 -0.0046 0.0093  35  VAL   B CB  
4566 C  CG1 . VAL   B 35  ? 0.1410 0.1468 0.1442 -0.0225 -0.0046 0.0114  35  VAL   B CG1 
4567 C  CG2 . VAL   B 35  ? 0.1462 0.1399 0.1478 -0.0125 -0.0063 0.0112  35  VAL   B CG2 
4577 N  N   . VAL   B 36  ? 0.1322 0.1213 0.1222 -0.0198 -0.0139 0.0057  36  VAL   B N   
4578 C  CA  . VAL   B 36  ? 0.1300 0.1172 0.1216 -0.0185 -0.0094 0.0069  36  VAL   B CA  
4579 C  C   . VAL   B 36  ? 0.1248 0.1159 0.1181 -0.0107 -0.0016 0.0052  36  VAL   B C   
4580 O  O   . VAL   B 36  ? 0.1348 0.1227 0.1253 -0.0077 -0.0021 -0.0030 36  VAL   B O   
4581 C  CB  . VAL   B 36  ? 0.1288 0.1195 0.1237 -0.0123 -0.0053 -0.0010 36  VAL   B CB  
4582 C  CG1 . VAL   B 36  ? 0.1319 0.1324 0.1337 -0.0168 -0.0012 0.0091  36  VAL   B CG1 
4583 C  CG2 . VAL   B 36  ? 0.1348 0.1240 0.1432 -0.0199 -0.0195 0.0033  36  VAL   B CG2 
4593 N  N   . ASN   B 37  ? 0.1272 0.1158 0.1137 -0.0016 -0.0077 0.0052  37  ASN   B N   
4594 C  CA  . ASN   B 37  ? 0.1287 0.1203 0.1254 0.0018  -0.0138 0.0035  37  ASN   B CA  
4595 C  C   . ASN   B 37  ? 0.1310 0.1281 0.1227 0.0042  -0.0076 0.0041  37  ASN   B C   
4596 O  O   . ASN   B 37  ? 0.1383 0.1347 0.1247 -0.0006 0.0032  0.0146  37  ASN   B O   
4597 C  CB  . ASN   B 37  ? 0.1238 0.1248 0.1299 0.0010  -0.0123 -0.0005 37  ASN   B CB  
4598 C  CG  . ASN   B 37  ? 0.1286 0.1228 0.1312 0.0016  -0.0113 0.0095  37  ASN   B CG  
4599 O  OD1 . ASN   B 37  ? 0.1387 0.1293 0.1376 0.0071  -0.0152 0.0023  37  ASN   B OD1 
4600 N  ND2 . ASN   B 37  ? 0.1416 0.1217 0.1311 0.0055  -0.0214 0.0089  37  ASN   B ND2 
4607 N  N   . ALA   B 38  ? 0.1447 0.1200 0.1247 0.0057  0.0036  0.0052  38  ALA   B N   
4608 C  CA  . ALA   B 38  ? 0.1456 0.1265 0.1357 -0.0005 0.0092  0.0071  38  ALA   B CA  
4609 C  C   . ALA   B 38  ? 0.1411 0.1224 0.1361 -0.0007 0.0051  0.0094  38  ALA   B C   
4610 O  O   . ALA   B 38  ? 0.1534 0.1321 0.1372 0.0105  0.0019  0.0105  38  ALA   B O   
4611 C  CB  . ALA   B 38  ? 0.1709 0.1320 0.1506 -0.0108 0.0074  0.0050  38  ALA   B CB  
4617 N  N   . ALA   B 39  ? 0.1418 0.1229 0.1215 0.0044  -0.0043 0.0073  39  ALA   B N   
4618 C  CA  . ALA   B 39  ? 0.1419 0.1336 0.1234 0.0062  -0.0066 0.0021  39  ALA   B CA  
4619 C  C   . ALA   B 39  ? 0.1499 0.1363 0.1120 0.0101  -0.0087 0.0029  39  ALA   B C   
4620 O  O   . ALA   B 39  ? 0.1565 0.1427 0.1346 0.0005  0.0004  0.0064  39  ALA   B O   
4621 C  CB  . ALA   B 39  ? 0.1427 0.1276 0.1459 -0.0028 -0.0072 -0.0002 39  ALA   B CB  
4627 N  N   . ASN   B 40  ? 0.1543 0.1553 0.1198 0.0023  0.0084  -0.0023 40  ASN   B N   
4628 C  CA  . ASN   B 40  ? 0.1638 0.1583 0.1364 0.0052  0.0005  0.0022  40  ASN   B CA  
4629 C  C   . ASN   B 40  ? 0.1649 0.1580 0.1153 0.0063  -0.0003 0.0047  40  ASN   B C   
4630 O  O   . ASN   B 40  ? 0.1611 0.1558 0.1132 0.0106  -0.0089 0.0013  40  ASN   B O   
4631 C  CB  . ASN   B 40  ? 0.1752 0.1590 0.1493 0.0118  -0.0061 0.0104  40  ASN   B CB  
4632 C  CG  . ASN   B 40  ? 0.1796 0.1638 0.1775 0.0099  -0.0165 0.0164  40  ASN   B CG  
4633 O  OD1 . ASN   B 40  ? 0.1743 0.1677 0.2602 -0.0003 -0.0304 0.0206  40  ASN   B OD1 
4634 N  ND2 . ASN   B 40  ? 0.1817 0.1645 0.1828 0.0085  -0.0184 0.0104  40  ASN   B ND2 
4641 N  N   . VAL   B 41  ? 0.1790 0.1635 0.1142 0.0136  0.0092  0.0102  41  VAL   B N   
4642 C  CA  . VAL   B 41  ? 0.1826 0.1746 0.1204 0.0109  0.0064  -0.0083 41  VAL   B CA  
4643 C  C   . VAL   B 41  ? 0.1763 0.1718 0.1116 0.0193  -0.0018 -0.0054 41  VAL   B C   
4644 O  O   . VAL   B 41  ? 0.1758 0.1753 0.1268 0.0205  -0.0078 -0.0120 41  VAL   B O   
4645 C  CB  . VAL   B 41  ? 0.1973 0.1905 0.1558 -0.0005 0.0248  -0.0200 41  VAL   B CB  
4646 C  CG1 . VAL   B 41  ? 0.2007 0.1910 0.1635 -0.0057 0.0281  -0.0257 41  VAL   B CG1 
4647 C  CG2 . VAL   B 41  ? 0.2067 0.2095 0.1617 -0.0063 0.0287  -0.0104 41  VAL   B CG2 
4657 N  N   . TYR   B 42  ? 0.1851 0.1780 0.1103 0.0183  -0.0129 -0.0044 42  TYR   B N   
4658 C  CA  . TYR   B 42  ? 0.1896 0.1792 0.1140 0.0215  -0.0264 -0.0120 42  TYR   B CA  
4659 C  C   . TYR   B 42  ? 0.1717 0.1656 0.1223 0.0224  -0.0183 -0.0126 42  TYR   B C   
4660 O  O   . TYR   B 42  ? 0.1737 0.1739 0.1572 0.0195  -0.0300 -0.0139 42  TYR   B O   
4661 C  CB  . TYR   B 42  ? 0.2085 0.2081 0.1282 0.0147  -0.0304 0.0017  42  TYR   B CB  
4662 C  CG  . TYR   B 42  ? 0.2150 0.2232 0.1264 -0.0008 -0.0255 0.0155  42  TYR   B CG  
4663 C  CD1 . TYR   B 42  ? 0.2077 0.2189 0.1067 -0.0091 -0.0083 0.0144  42  TYR   B CD1 
4664 C  CD2 . TYR   B 42  ? 0.2297 0.2381 0.1722 -0.0013 -0.0099 0.0188  42  TYR   B CD2 
4665 C  CE1 . TYR   B 42  ? 0.2235 0.2388 0.1225 -0.0071 -0.0064 0.0094  42  TYR   B CE1 
4666 C  CE2 . TYR   B 42  ? 0.2360 0.2523 0.1583 0.0032  0.0134  0.0382  42  TYR   B CE2 
4667 C  CZ  . TYR   B 42  ? 0.2429 0.2639 0.1454 0.0129  0.0180  0.0192  42  TYR   B CZ  
4668 O  OH  . TYR   B 42  ? 0.2775 0.2888 0.1767 0.0325  0.0225  0.0228  42  TYR   B OH  
4678 N  N   . LEU   B 43  ? 0.1630 0.1526 0.1113 0.0111  -0.0119 -0.0073 43  LEU   B N   
4679 C  CA  . LEU   B 43  ? 0.1587 0.1511 0.1125 0.0073  -0.0150 -0.0041 43  LEU   B CA  
4680 C  C   . LEU   B 43  ? 0.1590 0.1549 0.1244 0.0067  -0.0142 0.0053  43  LEU   B C   
4681 O  O   . LEU   B 43  ? 0.1607 0.1587 0.1483 0.0042  -0.0214 0.0146  43  LEU   B O   
4682 C  CB  . LEU   B 43  ? 0.1507 0.1386 0.1314 0.0007  -0.0221 -0.0059 43  LEU   B CB  
4683 C  CG  . LEU   B 43  ? 0.1565 0.1383 0.1472 -0.0021 -0.0254 0.0016  43  LEU   B CG  
4684 C  CD1 . LEU   B 43  ? 0.1668 0.1420 0.1761 -0.0059 -0.0481 -0.0025 43  LEU   B CD1 
4685 C  CD2 . LEU   B 43  ? 0.1537 0.1401 0.1531 -0.0049 -0.0265 -0.0064 43  LEU   B CD2 
4697 N  N   . LYS   B 44  ? 0.1626 0.1507 0.1262 0.0112  -0.0071 0.0078  44  LYS   B N   
4698 C  CA  . LYS   B 44  ? 0.1770 0.1568 0.1276 0.0153  -0.0115 0.0151  44  LYS   B CA  
4699 C  C   . LYS   B 44  ? 0.1743 0.1498 0.1270 0.0165  -0.0133 0.0080  44  LYS   B C   
4700 O  O   . LYS   B 44  ? 0.1937 0.1469 0.1494 0.0077  -0.0000 0.0015  44  LYS   B O   
4701 C  CB  . LYS   B 44  ? 0.2034 0.1821 0.1480 0.0210  -0.0263 0.0065  44  LYS   B CB  
4702 C  CG  . LYS   B 44  ? 0.2395 0.2129 0.1947 0.0111  -0.0498 0.0124  44  LYS   B CG  
4703 C  CD  . LYS   B 44  ? 0.2753 0.2381 0.2639 -0.0048 -0.0665 0.0056  44  LYS   B CD  
4704 C  CE  . LYS   B 44  ? 0.3056 0.2621 0.3278 -0.0102 -0.0720 0.0180  44  LYS   B CE  
4705 N  NZ  . LYS   B 44  ? 0.3189 0.2721 0.3578 -0.0087 -0.0770 0.0359  44  LYS   B NZ  
4719 N  N   . HIS   B 45  ? 0.1573 0.1511 0.1278 0.0065  -0.0120 0.0010  45  HIS   B N   
4720 C  CA  . HIS   B 45  ? 0.1662 0.1488 0.1387 0.0053  -0.0110 -0.0024 45  HIS   B CA  
4721 C  C   . HIS   B 45  ? 0.1886 0.1671 0.1794 0.0160  -0.0212 -0.0017 45  HIS   B C   
4722 O  O   . HIS   B 45  ? 0.2027 0.2082 0.2176 0.0458  0.0101  0.0009  45  HIS   B O   
4723 C  CB  . HIS   B 45  ? 0.1562 0.1523 0.1328 0.0012  -0.0067 -0.0016 45  HIS   B CB  
4724 C  CG  . HIS   B 45  ? 0.1568 0.1508 0.1261 0.0004  -0.0120 -0.0008 45  HIS   B CG  
4725 N  ND1 . HIS   B 45  ? 0.1583 0.1453 0.1363 0.0058  -0.0229 -0.0028 45  HIS   B ND1 
4726 C  CD2 . HIS   B 45  ? 0.1692 0.1483 0.1416 -0.0023 -0.0122 -0.0006 45  HIS   B CD2 
4727 C  CE1 . HIS   B 45  ? 0.1684 0.1378 0.1283 -0.0010 -0.0282 -0.0079 45  HIS   B CE1 
4728 N  NE2 . HIS   B 45  ? 0.1773 0.1402 0.1377 0.0003  -0.0190 -0.0029 45  HIS   B NE2 
4736 N  N   A GLY   B 46  ? 0.1948 0.1648 0.2064 0.0175  -0.0369 0.0115  46  GLY   B N   
4737 N  N   B GLY   B 46  ? 0.1971 0.1669 0.1998 0.0169  -0.0357 0.0157  46  GLY   B N   
4738 C  CA  A GLY   B 46  ? 0.2050 0.1743 0.2498 0.0153  -0.0367 0.0099  46  GLY   B CA  
4739 C  CA  B GLY   B 46  ? 0.2086 0.1776 0.2360 0.0134  -0.0357 0.0183  46  GLY   B CA  
4740 C  C   A GLY   B 46  ? 0.2025 0.1898 0.2882 0.0207  -0.0358 0.0039  46  GLY   B C   
4741 C  C   B GLY   B 46  ? 0.2087 0.1941 0.2701 0.0170  -0.0338 0.0170  46  GLY   B C   
4742 O  O   A GLY   B 46  ? 0.2033 0.2007 0.3538 0.0251  -0.0239 -0.0192 46  GLY   B O   
4743 O  O   B GLY   B 46  ? 0.2162 0.2091 0.3147 0.0143  -0.0195 0.0147  46  GLY   B O   
4750 N  N   . GLY   B 47  ? 0.2051 0.2042 0.2667 0.0092  -0.0212 -0.0006 47  GLY   B N   
4751 C  CA  . GLY   B 47  ? 0.1992 0.1794 0.2260 0.0010  -0.0180 -0.0032 47  GLY   B CA  
4752 C  C   . GLY   B 47  ? 0.1782 0.1536 0.1923 0.0003  -0.0050 0.0107  47  GLY   B C   
4753 O  O   . GLY   B 47  ? 0.1966 0.1448 0.1978 0.0007  -0.0122 0.0159  47  GLY   B O   
4758 N  N   . GLY   B 48  ? 0.1618 0.1431 0.1866 0.0047  -0.0100 0.0183  48  GLY   B N   
4759 C  CA  . GLY   B 48  ? 0.1560 0.1421 0.1784 -0.0014 -0.0066 0.0076  48  GLY   B CA  
4760 C  C   . GLY   B 48  ? 0.1518 0.1425 0.1605 0.0012  -0.0035 0.0031  48  GLY   B C   
4761 O  O   . GLY   B 48  ? 0.1464 0.1405 0.1844 0.0065  -0.0102 0.0079  48  GLY   B O   
4765 N  N   . VAL   B 49  ? 0.1522 0.1451 0.1463 0.0057  -0.0029 0.0058  49  VAL   B N   
4766 C  CA  . VAL   B 49  ? 0.1531 0.1519 0.1520 0.0084  -0.0120 -0.0039 49  VAL   B CA  
4767 C  C   . VAL   B 49  ? 0.1442 0.1441 0.1321 0.0123  -0.0020 -0.0040 49  VAL   B C   
4768 O  O   . VAL   B 49  ? 0.1482 0.1503 0.1498 0.0048  -0.0013 0.0009  49  VAL   B O   
4769 C  CB  . VAL   B 49  ? 0.1562 0.1662 0.1788 0.0012  -0.0233 -0.0051 49  VAL   B CB  
4770 C  CG1 . VAL   B 49  ? 0.1515 0.1773 0.1773 0.0110  -0.0346 0.0012  49  VAL   B CG1 
4771 C  CG2 . VAL   B 49  ? 0.1723 0.1826 0.1972 -0.0093 -0.0329 -0.0026 49  VAL   B CG2 
4781 N  N   . ALA   B 50  ? 0.1398 0.1399 0.1336 0.0018  -0.0034 0.0048  50  ALA   B N   
4782 C  CA  . ALA   B 50  ? 0.1392 0.1291 0.1391 0.0062  0.0008  0.0047  50  ALA   B CA  
4783 C  C   . ALA   B 50  ? 0.1455 0.1343 0.1317 0.0047  0.0041  -0.0022 50  ALA   B C   
4784 O  O   . ALA   B 50  ? 0.1458 0.1376 0.1289 0.0038  -0.0041 0.0026  50  ALA   B O   
4785 C  CB  . ALA   B 50  ? 0.1487 0.1313 0.1434 -0.0054 -0.0072 0.0139  50  ALA   B CB  
4791 N  N   . GLY   B 51  ? 0.1483 0.1426 0.1479 0.0148  -0.0102 0.0033  51  GLY   B N   
4792 C  CA  . GLY   B 51  ? 0.1525 0.1521 0.1693 0.0172  -0.0127 0.0035  51  GLY   B CA  
4793 C  C   . GLY   B 51  ? 0.1468 0.1490 0.1690 0.0221  -0.0035 0.0048  51  GLY   B C   
4794 O  O   . GLY   B 51  ? 0.1486 0.1571 0.1819 0.0098  -0.0052 -0.0009 51  GLY   B O   
4798 N  N   . ALA   B 52  ? 0.1463 0.1453 0.1575 0.0156  -0.0076 0.0009  52  ALA   B N   
4799 C  CA  . ALA   B 52  ? 0.1528 0.1470 0.1550 0.0177  0.0048  -0.0067 52  ALA   B CA  
4800 C  C   . ALA   B 52  ? 0.1450 0.1429 0.1496 0.0110  0.0070  -0.0074 52  ALA   B C   
4801 O  O   . ALA   B 52  ? 0.1399 0.1517 0.1726 0.0122  0.0041  0.0012  52  ALA   B O   
4802 C  CB  . ALA   B 52  ? 0.1627 0.1537 0.1637 0.0075  0.0001  -0.0091 52  ALA   B CB  
4808 N  N   . LEU   B 53  ? 0.1405 0.1444 0.1433 0.0138  0.0014  0.0088  53  LEU   B N   
4809 C  CA  . LEU   B 53  ? 0.1408 0.1521 0.1349 0.0120  -0.0058 0.0036  53  LEU   B CA  
4810 C  C   . LEU   B 53  ? 0.1458 0.1448 0.1425 0.0127  0.0010  0.0039  53  LEU   B C   
4811 O  O   . LEU   B 53  ? 0.1505 0.1486 0.1567 0.0017  0.0056  0.0115  53  LEU   B O   
4812 C  CB  . LEU   B 53  ? 0.1367 0.1563 0.1426 0.0075  0.0085  0.0132  53  LEU   B CB  
4813 C  CG  . LEU   B 53  ? 0.1394 0.1705 0.1540 0.0044  0.0109  0.0168  53  LEU   B CG  
4814 C  CD1 . LEU   B 53  ? 0.1474 0.1882 0.1679 0.0073  0.0061  0.0035  53  LEU   B CD1 
4815 C  CD2 . LEU   B 53  ? 0.1553 0.1980 0.1779 -0.0046 -0.0016 -0.0082 53  LEU   B CD2 
4827 N  N   . ASN   B 54  ? 0.1437 0.1342 0.1402 0.0055  -0.0010 0.0034  54  ASN   B N   
4828 C  CA  . ASN   B 54  ? 0.1420 0.1476 0.1488 0.0069  -0.0001 0.0020  54  ASN   B CA  
4829 C  C   . ASN   B 54  ? 0.1448 0.1553 0.1611 0.0036  0.0048  0.0003  54  ASN   B C   
4830 O  O   . ASN   B 54  ? 0.1369 0.1596 0.1689 -0.0050 -0.0003 -0.0003 54  ASN   B O   
4831 C  CB  . ASN   B 54  ? 0.1478 0.1599 0.1623 0.0060  0.0051  0.0047  54  ASN   B CB  
4832 C  CG  . ASN   B 54  ? 0.1442 0.1675 0.1554 0.0055  -0.0072 0.0090  54  ASN   B CG  
4833 O  OD1 . ASN   B 54  ? 0.1445 0.1615 0.1639 0.0011  -0.0123 -0.0103 54  ASN   B OD1 
4834 N  ND2 . ASN   B 54  ? 0.1589 0.1902 0.1853 0.0022  -0.0239 0.0189  54  ASN   B ND2 
4841 N  N   . LYS   B 55  ? 0.1426 0.1553 0.1749 0.0144  0.0029  0.0025  55  LYS   B N   
4842 C  CA  . LYS   B 55  ? 0.1482 0.1727 0.1946 0.0206  0.0002  -0.0042 55  LYS   B CA  
4843 C  C   . LYS   B 55  ? 0.1432 0.1756 0.1981 0.0153  0.0055  -0.0116 55  LYS   B C   
4844 O  O   . LYS   B 55  ? 0.1423 0.1872 0.2051 0.0150  0.0073  -0.0098 55  LYS   B O   
4845 C  CB  . LYS   B 55  ? 0.1634 0.1828 0.2370 0.0340  0.0217  -0.0054 55  LYS   B CB  
4846 C  CG  . LYS   B 55  ? 0.2060 0.2114 0.3292 0.0415  0.0325  0.0052  55  LYS   B CG  
4847 C  CD  . LYS   B 55  ? 0.2380 0.2324 0.4063 0.0531  0.0440  0.0203  55  LYS   B CD  
4848 C  CE  . LYS   B 55  ? 0.2579 0.2500 0.4732 0.0558  0.0536  0.0332  55  LYS   B CE  
4849 N  NZ  . LYS   B 55  ? 0.2640 0.2698 0.5128 0.0523  0.0434  0.0461  55  LYS   B NZ  
4863 N  N   . ALA   B 56  ? 0.1420 0.1799 0.1809 0.0120  0.0068  -0.0063 56  ALA   B N   
4864 C  CA  . ALA   B 56  ? 0.1555 0.1939 0.1767 0.0041  0.0107  -0.0061 56  ALA   B CA  
4865 C  C   . ALA   B 56  ? 0.1599 0.1873 0.1585 0.0038  0.0175  0.0020  56  ALA   B C   
4866 O  O   . ALA   B 56  ? 0.1688 0.1991 0.1836 0.0005  0.0264  0.0041  56  ALA   B O   
4867 C  CB  . ALA   B 56  ? 0.1676 0.2071 0.1846 -0.0068 0.0040  -0.0112 56  ALA   B CB  
4873 N  N   . THR   B 57  ? 0.1542 0.1746 0.1708 0.0051  0.0183  0.0006  57  THR   B N   
4874 C  CA  . THR   B 57  ? 0.1579 0.1753 0.1673 0.0030  0.0216  0.0013  57  THR   B CA  
4875 C  C   . THR   B 57  ? 0.1558 0.1846 0.1741 -0.0042 0.0245  0.0023  57  THR   B C   
4876 O  O   . THR   B 57  ? 0.1645 0.1849 0.1843 -0.0176 0.0164  -0.0004 57  THR   B O   
4877 C  CB  . THR   B 57  ? 0.1586 0.1611 0.1534 -0.0005 0.0133  0.0125  57  THR   B CB  
4878 O  OG1 . THR   B 57  ? 0.1514 0.1492 0.1618 -0.0022 0.0093  0.0076  57  THR   B OG1 
4879 C  CG2 . THR   B 57  ? 0.1592 0.1618 0.1593 0.0027  0.0140  0.0141  57  THR   B CG2 
4887 N  N   . ASN   B 58  ? 0.1442 0.2014 0.2107 -0.0094 0.0136  -0.0129 58  ASN   B N   
4888 C  CA  . ASN   B 58  ? 0.1644 0.2404 0.2553 -0.0226 0.0383  -0.0135 58  ASN   B CA  
4889 C  C   . ASN   B 58  ? 0.1438 0.2156 0.2057 -0.0124 0.0042  -0.0074 58  ASN   B C   
4890 O  O   . ASN   B 58  ? 0.1522 0.2235 0.2091 -0.0153 -0.0004 -0.0108 58  ASN   B O   
4891 C  CB  . ASN   B 58  ? 0.2345 0.3052 0.3707 -0.0386 0.0915  0.0003  58  ASN   B CB  
4892 C  CG  . ASN   B 58  ? 0.3230 0.3568 0.5113 -0.0409 0.1144  0.0310  58  ASN   B CG  
4893 O  OD1 . ASN   B 58  ? 0.3669 0.3821 0.5638 -0.0390 0.1177  0.0391  58  ASN   B OD1 
4894 N  ND2 . ASN   B 58  ? 0.3992 0.3992 0.5611 -0.0448 0.1218  0.0413  58  ASN   B ND2 
4901 N  N   . ASN   B 59  ? 0.1435 0.1972 0.1834 -0.0100 -0.0015 -0.0016 59  ASN   B N   
4902 C  CA  . ASN   B 59  ? 0.1469 0.2004 0.1725 -0.0067 -0.0091 0.0036  59  ASN   B CA  
4903 C  C   . ASN   B 59  ? 0.1425 0.1878 0.1586 -0.0100 -0.0114 -0.0034 59  ASN   B C   
4904 O  O   . ASN   B 59  ? 0.1474 0.1811 0.1648 -0.0090 -0.0070 -0.0023 59  ASN   B O   
4905 C  CB  . ASN   B 59  ? 0.1558 0.2181 0.1874 0.0035  -0.0186 0.0089  59  ASN   B CB  
4906 C  CG  . ASN   B 59  ? 0.1580 0.2282 0.1920 0.0088  -0.0310 0.0128  59  ASN   B CG  
4907 O  OD1 . ASN   B 59  ? 0.1611 0.2311 0.2012 0.0097  -0.0203 0.0250  59  ASN   B OD1 
4908 N  ND2 . ASN   B 59  ? 0.1644 0.2420 0.1943 0.0064  -0.0297 0.0047  59  ASN   B ND2 
4915 N  N   . ALA   B 60  ? 0.1426 0.1786 0.1610 -0.0142 -0.0030 -0.0024 60  ALA   B N   
4916 C  CA  . ALA   B 60  ? 0.1541 0.1689 0.1694 -0.0209 -0.0001 0.0080  60  ALA   B CA  
4917 C  C   . ALA   B 60  ? 0.1566 0.1580 0.1529 -0.0115 -0.0072 0.0107  60  ALA   B C   
4918 O  O   . ALA   B 60  ? 0.1614 0.1613 0.1714 -0.0161 -0.0056 -0.0029 60  ALA   B O   
4919 C  CB  . ALA   B 60  ? 0.1720 0.1689 0.1987 -0.0171 0.0080  0.0118  60  ALA   B CB  
4925 N  N   . MET   B 61  ? 0.1478 0.1486 0.1561 -0.0111 -0.0036 0.0042  61  MET   B N   
4926 C  CA  . MET   B 61  ? 0.1372 0.1480 0.1448 -0.0062 -0.0131 0.0080  61  MET   B CA  
4927 C  C   . MET   B 61  ? 0.1400 0.1467 0.1439 -0.0069 -0.0173 0.0047  61  MET   B C   
4928 O  O   . MET   B 61  ? 0.1458 0.1442 0.1343 0.0022  -0.0120 -0.0130 61  MET   B O   
4929 C  CB  . MET   B 61  ? 0.1381 0.1516 0.1371 0.0008  -0.0086 -0.0022 61  MET   B CB  
4930 C  CG  . MET   B 61  ? 0.1348 0.1469 0.1487 -0.0006 -0.0073 0.0002  61  MET   B CG  
4931 S  SD  . MET   B 61  ? 0.1392 0.1503 0.1662 -0.0031 -0.0057 -0.0101 61  MET   B SD  
4932 C  CE  . MET   B 61  ? 0.1469 0.1667 0.1855 -0.0013 -0.0163 -0.0158 61  MET   B CE  
4942 N  N   . GLN   B 62  ? 0.1440 0.1502 0.1352 -0.0022 -0.0238 0.0018  62  GLN   B N   
4943 C  CA  . GLN   B 62  ? 0.1456 0.1523 0.1408 -0.0017 -0.0163 0.0039  62  GLN   B CA  
4944 C  C   . GLN   B 62  ? 0.1452 0.1587 0.1445 -0.0060 -0.0239 -0.0017 62  GLN   B C   
4945 O  O   . GLN   B 62  ? 0.1529 0.1640 0.1455 -0.0016 -0.0203 -0.0050 62  GLN   B O   
4946 C  CB  . GLN   B 62  ? 0.1503 0.1595 0.1587 0.0090  -0.0071 0.0045  62  GLN   B CB  
4947 C  CG  . GLN   B 62  ? 0.1526 0.1610 0.1613 0.0109  -0.0242 0.0082  62  GLN   B CG  
4948 C  CD  . GLN   B 62  ? 0.1519 0.1600 0.1442 0.0068  -0.0276 0.0118  62  GLN   B CD  
4949 O  OE1 . GLN   B 62  ? 0.1517 0.1564 0.1654 0.0046  -0.0274 -0.0020 62  GLN   B OE1 
4950 N  NE2 . GLN   B 62  ? 0.1558 0.1680 0.1443 0.0062  -0.0221 -0.0038 62  GLN   B NE2 
4959 N  N   . VAL   B 63  ? 0.1443 0.1613 0.1625 -0.0046 -0.0220 -0.0114 63  VAL   B N   
4960 C  CA  . VAL   B 63  ? 0.1584 0.1685 0.1801 -0.0072 -0.0230 -0.0053 63  VAL   B CA  
4961 C  C   . VAL   B 63  ? 0.1565 0.1571 0.1614 -0.0105 -0.0218 -0.0184 63  VAL   B C   
4962 O  O   . VAL   B 63  ? 0.1613 0.1544 0.1695 -0.0044 -0.0354 -0.0120 63  VAL   B O   
4963 C  CB  . VAL   B 63  ? 0.1579 0.1776 0.2046 -0.0147 -0.0220 -0.0078 63  VAL   B CB  
4964 C  CG1 . VAL   B 63  ? 0.1659 0.1855 0.2187 -0.0242 -0.0181 -0.0058 63  VAL   B CG1 
4965 C  CG2 . VAL   B 63  ? 0.1535 0.2009 0.2205 -0.0089 -0.0249 -0.0105 63  VAL   B CG2 
4975 N  N   . GLU   B 64  ? 0.1528 0.1492 0.1449 -0.0032 -0.0256 -0.0067 64  GLU   B N   
4976 C  CA  . GLU   B 64  ? 0.1560 0.1447 0.1398 -0.0111 -0.0242 -0.0077 64  GLU   B CA  
4977 C  C   . GLU   B 64  ? 0.1568 0.1422 0.1341 -0.0041 -0.0319 -0.0100 64  GLU   B C   
4978 O  O   . GLU   B 64  ? 0.1635 0.1512 0.1334 -0.0037 -0.0290 -0.0064 64  GLU   B O   
4979 C  CB  . GLU   B 64  ? 0.1578 0.1535 0.1406 -0.0144 -0.0177 -0.0038 64  GLU   B CB  
4980 C  CG  . GLU   B 64  ? 0.1669 0.1567 0.1454 -0.0182 -0.0258 -0.0086 64  GLU   B CG  
4981 C  CD  . GLU   B 64  ? 0.1687 0.1702 0.1586 -0.0239 -0.0306 -0.0018 64  GLU   B CD  
4982 O  OE1 . GLU   B 64  ? 0.1701 0.1835 0.1619 -0.0316 -0.0164 -0.0241 64  GLU   B OE1 
4983 O  OE2 . GLU   B 64  ? 0.1830 0.1755 0.1701 -0.0279 -0.0409 -0.0081 64  GLU   B OE2 
4990 N  N   . SER   B 65  ? 0.1493 0.1375 0.1457 -0.0040 -0.0203 -0.0112 65  SER   B N   
4991 C  CA  . SER   B 65  ? 0.1436 0.1388 0.1447 0.0027  -0.0164 -0.0154 65  SER   B CA  
4992 C  C   . SER   B 65  ? 0.1485 0.1400 0.1506 0.0048  -0.0202 -0.0169 65  SER   B C   
4993 O  O   . SER   B 65  ? 0.1542 0.1519 0.1448 0.0057  -0.0195 -0.0207 65  SER   B O   
4994 C  CB  . SER   B 65  ? 0.1527 0.1480 0.1434 -0.0060 -0.0148 -0.0125 65  SER   B CB  
4995 O  OG  . SER   B 65  ? 0.1545 0.1439 0.1437 -0.0079 -0.0079 -0.0154 65  SER   B OG  
5001 N  N   . ASP   B 66  ? 0.1586 0.1490 0.1470 0.0012  -0.0285 -0.0156 66  ASP   B N   
5002 C  CA  . ASP   B 66  ? 0.1739 0.1574 0.1391 0.0071  -0.0288 -0.0134 66  ASP   B CA  
5003 C  C   . ASP   B 66  ? 0.1711 0.1578 0.1357 -0.0028 -0.0274 -0.0122 66  ASP   B C   
5004 O  O   . ASP   B 66  ? 0.1757 0.1682 0.1428 0.0019  -0.0258 -0.0177 66  ASP   B O   
5005 C  CB  . ASP   B 66  ? 0.1806 0.1659 0.1594 0.0072  -0.0441 -0.0165 66  ASP   B CB  
5006 C  CG  . ASP   B 66  ? 0.2036 0.1823 0.1841 0.0157  -0.0533 -0.0039 66  ASP   B CG  
5007 O  OD1 . ASP   B 66  ? 0.2315 0.1763 0.1899 0.0154  -0.0436 0.0006  66  ASP   B OD1 
5008 O  OD2 . ASP   B 66  ? 0.2133 0.2110 0.2452 0.0353  -0.0602 -0.0063 66  ASP   B OD2 
5013 N  N   . ASP   B 67  ? 0.1655 0.1522 0.1350 -0.0013 -0.0237 -0.0169 67  ASP   B N   
5014 C  CA  . ASP   B 67  ? 0.1799 0.1479 0.1396 -0.0053 -0.0261 -0.0102 67  ASP   B CA  
5015 C  C   . ASP   B 67  ? 0.1783 0.1496 0.1492 0.0011  -0.0185 -0.0137 67  ASP   B C   
5016 O  O   . ASP   B 67  ? 0.1863 0.1596 0.1648 0.0027  -0.0146 -0.0271 67  ASP   B O   
5017 C  CB  . ASP   B 67  ? 0.2007 0.1564 0.1642 -0.0122 -0.0337 -0.0093 67  ASP   B CB  
5018 C  CG  . ASP   B 67  ? 0.2362 0.1599 0.1811 -0.0075 -0.0645 -0.0079 67  ASP   B CG  
5019 O  OD1 . ASP   B 67  ? 0.2605 0.1694 0.1993 -0.0116 -0.0644 -0.0103 67  ASP   B OD1 
5020 O  OD2 . ASP   B 67  ? 0.2502 0.1694 0.2001 0.0114  -0.0662 -0.0021 67  ASP   B OD2 
5025 N  N   . TYR   B 68  ? 0.1718 0.1555 0.1424 0.0006  -0.0316 -0.0181 68  TYR   B N   
5026 C  CA  . TYR   B 68  ? 0.1677 0.1623 0.1545 0.0057  -0.0313 -0.0291 68  TYR   B CA  
5027 C  C   . TYR   B 68  ? 0.1621 0.1592 0.1630 0.0044  -0.0312 -0.0313 68  TYR   B C   
5028 O  O   . TYR   B 68  ? 0.1693 0.1710 0.1679 0.0083  -0.0314 -0.0417 68  TYR   B O   
5029 C  CB  . TYR   B 68  ? 0.1690 0.1869 0.1682 0.0129  -0.0453 -0.0336 68  TYR   B CB  
5030 C  CG  . TYR   B 68  ? 0.1844 0.2060 0.1820 0.0146  -0.0407 -0.0589 68  TYR   B CG  
5031 C  CD1 . TYR   B 68  ? 0.1885 0.2095 0.2057 0.0009  -0.0322 -0.0646 68  TYR   B CD1 
5032 C  CD2 . TYR   B 68  ? 0.1878 0.2223 0.1976 0.0224  -0.0504 -0.0599 68  TYR   B CD2 
5033 C  CE1 . TYR   B 68  ? 0.1957 0.2192 0.2319 0.0048  -0.0270 -0.0659 68  TYR   B CE1 
5034 C  CE2 . TYR   B 68  ? 0.1915 0.2202 0.2084 0.0255  -0.0314 -0.0757 68  TYR   B CE2 
5035 C  CZ  . TYR   B 68  ? 0.1905 0.2192 0.2261 0.0083  -0.0292 -0.0767 68  TYR   B CZ  
5036 O  OH  . TYR   B 68  ? 0.1889 0.2314 0.2558 0.0044  -0.0277 -0.0410 68  TYR   B OH  
5046 N  N   . ILE   B 69  ? 0.1640 0.1567 0.1534 0.0035  -0.0257 -0.0254 69  ILE   B N   
5047 C  CA  . ILE   B 69  ? 0.1652 0.1601 0.1547 0.0026  -0.0206 -0.0325 69  ILE   B CA  
5048 C  C   . ILE   B 69  ? 0.1644 0.1646 0.1532 0.0121  -0.0311 -0.0233 69  ILE   B C   
5049 O  O   . ILE   B 69  ? 0.1664 0.1787 0.1596 0.0087  -0.0203 -0.0263 69  ILE   B O   
5050 C  CB  . ILE   B 69  ? 0.1737 0.1649 0.1711 0.0012  0.0043  -0.0273 69  ILE   B CB  
5051 C  CG1 . ILE   B 69  ? 0.1778 0.1715 0.1875 -0.0061 0.0072  -0.0272 69  ILE   B CG1 
5052 C  CG2 . ILE   B 69  ? 0.1832 0.1764 0.1922 0.0031  -0.0007 -0.0181 69  ILE   B CG2 
5053 C  CD1 . ILE   B 69  ? 0.1801 0.1764 0.1981 -0.0125 -0.0048 -0.0301 69  ILE   B CD1 
5065 N  N   . ALA   B 70  ? 0.1607 0.1612 0.1547 0.0130  -0.0258 -0.0246 70  ALA   B N   
5066 C  CA  . ALA   B 70  ? 0.1635 0.1678 0.1428 0.0015  -0.0273 -0.0293 70  ALA   B CA  
5067 C  C   . ALA   B 70  ? 0.1729 0.1635 0.1617 -0.0038 -0.0350 -0.0377 70  ALA   B C   
5068 O  O   . ALA   B 70  ? 0.1810 0.1633 0.1660 0.0047  -0.0320 -0.0384 70  ALA   B O   
5069 C  CB  . ALA   B 70  ? 0.1658 0.1811 0.1511 0.0024  -0.0306 -0.0291 70  ALA   B CB  
5075 N  N   A THR   B 71  ? 0.1771 0.1624 0.1683 0.0044  -0.0457 -0.0347 71  THR   B N   
5076 N  N   B THR   B 71  ? 0.1791 0.1633 0.1689 0.0037  -0.0425 -0.0347 71  THR   B N   
5077 C  CA  A THR   B 71  ? 0.1906 0.1654 0.1844 0.0081  -0.0572 -0.0325 71  THR   B CA  
5078 C  CA  B THR   B 71  ? 0.1939 0.1658 0.1858 0.0061  -0.0504 -0.0338 71  THR   B CA  
5079 C  C   A THR   B 71  ? 0.1889 0.1682 0.1995 0.0192  -0.0552 -0.0424 71  THR   B C   
5080 C  C   B THR   B 71  ? 0.1897 0.1648 0.2070 0.0217  -0.0474 -0.0461 71  THR   B C   
5081 O  O   A THR   B 71  ? 0.1972 0.1779 0.2201 0.0181  -0.0551 -0.0466 71  THR   B O   
5082 O  O   B THR   B 71  ? 0.1964 0.1668 0.2365 0.0266  -0.0424 -0.0566 71  THR   B O   
5083 C  CB  A THR   B 71  ? 0.2083 0.1828 0.2030 0.0065  -0.0618 -0.0168 71  THR   B CB  
5084 C  CB  B THR   B 71  ? 0.2156 0.1869 0.2017 -0.0012 -0.0514 -0.0149 71  THR   B CB  
5085 O  OG1 A THR   B 71  ? 0.2172 0.2000 0.2275 0.0008  -0.0616 0.0026  71  THR   B OG1 
5086 O  OG1 B THR   B 71  ? 0.2267 0.2046 0.2179 -0.0132 -0.0476 0.0017  71  THR   B OG1 
5087 C  CG2 A THR   B 71  ? 0.2176 0.1813 0.2124 0.0117  -0.0593 -0.0089 71  THR   B CG2 
5088 C  CG2 B THR   B 71  ? 0.2256 0.1865 0.2135 0.0059  -0.0485 -0.0047 71  THR   B CG2 
5103 N  N   . ASN   B 72  ? 0.1750 0.1655 0.1959 0.0150  -0.0519 -0.0579 72  ASN   B N   
5104 C  CA  . ASN   B 72  ? 0.1736 0.1790 0.2061 0.0232  -0.0421 -0.0695 72  ASN   B CA  
5105 C  C   . ASN   B 72  ? 0.1685 0.1959 0.2102 0.0062  -0.0200 -0.0658 72  ASN   B C   
5106 O  O   . ASN   B 72  ? 0.1684 0.2126 0.2421 0.0067  -0.0140 -0.0647 72  ASN   B O   
5107 C  CB  . ASN   B 72  ? 0.1844 0.1953 0.2201 0.0170  -0.0606 -0.0546 72  ASN   B CB  
5108 C  CG  . ASN   B 72  ? 0.2030 0.2091 0.2351 0.0277  -0.0626 -0.0369 72  ASN   B CG  
5109 O  OD1 . ASN   B 72  ? 0.2295 0.2298 0.2343 0.0165  -0.0388 -0.0377 72  ASN   B OD1 
5110 N  ND2 . ASN   B 72  ? 0.2113 0.2192 0.2743 0.0438  -0.0497 -0.0110 72  ASN   B ND2 
5118 N  N   . GLY   B 73  ? 0.1740 0.1949 0.1925 0.0014  -0.0246 -0.0600 73  GLY   B N   
5119 C  CA  . GLY   B 73  ? 0.1712 0.2016 0.1727 -0.0006 -0.0174 -0.0530 73  GLY   B CA  
5120 C  C   . GLY   B 73  ? 0.1639 0.1977 0.1420 0.0030  -0.0216 -0.0393 73  GLY   B C   
5121 O  O   . GLY   B 73  ? 0.1643 0.1823 0.1543 0.0064  -0.0198 -0.0306 73  GLY   B O   
5125 N  N   . PRO   B 74  ? 0.1693 0.2057 0.1419 0.0021  -0.0257 -0.0340 74  PRO   B N   
5126 C  CA  . PRO   B 74  ? 0.1616 0.2036 0.1239 0.0048  -0.0161 -0.0254 74  PRO   B CA  
5127 C  C   . PRO   B 74  ? 0.1560 0.1887 0.1276 0.0053  -0.0098 -0.0195 74  PRO   B C   
5128 O  O   . PRO   B 74  ? 0.1609 0.1959 0.1642 0.0057  -0.0103 -0.0310 74  PRO   B O   
5129 C  CB  . PRO   B 74  ? 0.1819 0.2222 0.1356 0.0037  -0.0137 -0.0184 74  PRO   B CB  
5130 C  CG  . PRO   B 74  ? 0.2055 0.2338 0.1579 0.0049  -0.0106 -0.0140 74  PRO   B CG  
5131 C  CD  . PRO   B 74  ? 0.1964 0.2239 0.1519 0.0059  -0.0084 -0.0240 74  PRO   B CD  
5139 N  N   . LEU   B 75  ? 0.1499 0.1794 0.1183 0.0073  -0.0178 -0.0168 75  LEU   B N   
5140 C  CA  . LEU   B 75  ? 0.1535 0.1780 0.1241 0.0066  -0.0150 -0.0079 75  LEU   B CA  
5141 C  C   . LEU   B 75  ? 0.1613 0.1920 0.1292 0.0030  -0.0023 -0.0014 75  LEU   B C   
5142 O  O   . LEU   B 75  ? 0.1802 0.2031 0.1373 -0.0046 -0.0033 0.0053  75  LEU   B O   
5143 C  CB  . LEU   B 75  ? 0.1560 0.1759 0.1165 -0.0079 -0.0154 0.0084  75  LEU   B CB  
5144 C  CG  . LEU   B 75  ? 0.1896 0.1947 0.1364 -0.0310 -0.0179 0.0048  75  LEU   B CG  
5145 C  CD1 . LEU   B 75  ? 0.2223 0.2121 0.1520 -0.0379 0.0116  0.0006  75  LEU   B CD1 
5146 C  CD2 . LEU   B 75  ? 0.2360 0.2159 0.2014 -0.0171 -0.0053 0.0142  75  LEU   B CD2 
5158 N  N   . LYS   B 76  ? 0.1550 0.2050 0.1559 -0.0013 0.0059  0.0077  76  LYS   B N   
5159 C  CA  . LYS   B 76  ? 0.1704 0.2128 0.1815 -0.0076 0.0173  0.0019  76  LYS   B CA  
5160 C  C   . LYS   B 76  ? 0.1695 0.1992 0.1619 -0.0019 0.0146  0.0203  76  LYS   B C   
5161 O  O   . LYS   B 76  ? 0.1706 0.1825 0.1589 -0.0044 0.0131  0.0106  76  LYS   B O   
5162 C  CB  . LYS   B 76  ? 0.1862 0.2160 0.2325 -0.0100 0.0370  -0.0208 76  LYS   B CB  
5163 C  CG  . LYS   B 76  ? 0.1976 0.2328 0.2643 -0.0029 0.0256  -0.0277 76  LYS   B CG  
5164 C  CD  . LYS   B 76  ? 0.2003 0.2411 0.2939 0.0013  0.0183  -0.0393 76  LYS   B CD  
5165 C  CE  . LYS   B 76  ? 0.2051 0.2519 0.3346 0.0112  0.0056  -0.0498 76  LYS   B CE  
5166 N  NZ  . LYS   B 76  ? 0.2043 0.2549 0.3545 0.0092  -0.0097 -0.0663 76  LYS   B NZ  
5180 N  N   . VAL   B 77  ? 0.1756 0.2067 0.1604 -0.0012 0.0100  0.0274  77  VAL   B N   
5181 C  CA  . VAL   B 77  ? 0.1774 0.1989 0.1718 0.0068  0.0177  0.0563  77  VAL   B CA  
5182 C  C   . VAL   B 77  ? 0.1660 0.1770 0.1611 0.0114  0.0317  0.0356  77  VAL   B C   
5183 O  O   . VAL   B 77  ? 0.1775 0.1774 0.1607 0.0152  0.0309  0.0261  77  VAL   B O   
5184 C  CB  . VAL   B 77  ? 0.1932 0.2118 0.2089 0.0072  0.0289  0.0687  77  VAL   B CB  
5185 C  CG1 . VAL   B 77  ? 0.1992 0.2044 0.2315 0.0037  0.0348  0.0834  77  VAL   B CG1 
5186 C  CG2 . VAL   B 77  ? 0.2021 0.2288 0.2158 0.0064  0.0144  0.0705  77  VAL   B CG2 
5196 N  N   . GLY   B 78  ? 0.1607 0.1654 0.1595 0.0034  0.0205  0.0281  78  GLY   B N   
5197 C  CA  . GLY   B 78  ? 0.1588 0.1622 0.1623 0.0029  0.0267  0.0221  78  GLY   B CA  
5198 C  C   . GLY   B 78  ? 0.1528 0.1506 0.1614 0.0074  0.0230  0.0224  78  GLY   B C   
5199 O  O   . GLY   B 78  ? 0.1538 0.1521 0.1723 0.0128  0.0177  0.0285  78  GLY   B O   
5203 N  N   . GLY   B 79  ? 0.1471 0.1556 0.1499 0.0056  0.0212  0.0166  79  GLY   B N   
5204 C  CA  . GLY   B 79  ? 0.1492 0.1475 0.1516 0.0080  0.0201  0.0215  79  GLY   B CA  
5205 C  C   . GLY   B 79  ? 0.1417 0.1423 0.1515 0.0116  0.0139  0.0134  79  GLY   B C   
5206 O  O   . GLY   B 79  ? 0.1474 0.1395 0.1585 0.0098  0.0140  0.0199  79  GLY   B O   
5210 N  N   . SER   B 80  ? 0.1320 0.1395 0.1615 0.0057  0.0181  0.0168  80  SER   B N   
5211 C  CA  . SER   B 80  ? 0.1335 0.1343 0.1573 0.0034  0.0027  0.0089  80  SER   B CA  
5212 C  C   . SER   B 80  ? 0.1370 0.1269 0.1427 0.0041  -0.0032 0.0049  80  SER   B C   
5213 O  O   . SER   B 80  ? 0.1497 0.1344 0.1683 0.0058  0.0038  0.0008  80  SER   B O   
5214 C  CB  . SER   B 80  ? 0.1380 0.1353 0.1651 -0.0032 -0.0003 0.0119  80  SER   B CB  
5215 O  OG  . SER   B 80  ? 0.1456 0.1538 0.1744 -0.0028 -0.0088 0.0143  80  SER   B OG  
5221 N  N   . CYS   B 81  ? 0.1355 0.1227 0.1551 0.0031  -0.0031 -0.0002 81  CYS   B N   
5222 C  CA  . CYS   B 81  ? 0.1405 0.1213 0.1585 0.0006  -0.0103 -0.0033 81  CYS   B CA  
5223 C  C   . CYS   B 81  ? 0.1364 0.1173 0.1288 -0.0010 -0.0168 -0.0028 81  CYS   B C   
5224 O  O   . CYS   B 81  ? 0.1555 0.1210 0.1470 0.0047  -0.0034 -0.0007 81  CYS   B O   
5225 C  CB  . CYS   B 81  ? 0.1520 0.1368 0.1582 -0.0043 -0.0157 -0.0016 81  CYS   B CB  
5226 S  SG  . CYS   B 81  ? 0.1524 0.1521 0.1456 -0.0040 -0.0229 -0.0071 81  CYS   B SG  
5232 N  N   . VAL   B 82  ? 0.1450 0.1204 0.1492 0.0019  -0.0191 -0.0001 82  VAL   B N   
5233 C  CA  . VAL   B 82  ? 0.1441 0.1259 0.1440 -0.0031 -0.0117 0.0110  82  VAL   B CA  
5234 C  C   . VAL   B 82  ? 0.1511 0.1156 0.1520 -0.0054 -0.0084 0.0041  82  VAL   B C   
5235 O  O   . VAL   B 82  ? 0.1592 0.1231 0.1851 -0.0027 -0.0054 -0.0156 82  VAL   B O   
5236 C  CB  . VAL   B 82  ? 0.1552 0.1473 0.1559 -0.0068 -0.0158 0.0116  82  VAL   B CB  
5237 C  CG1 . VAL   B 82  ? 0.1713 0.1732 0.1610 0.0026  -0.0167 0.0229  82  VAL   B CG1 
5238 C  CG2 . VAL   B 82  ? 0.1608 0.1580 0.1625 -0.0132 -0.0305 0.0113  82  VAL   B CG2 
5248 N  N   . LEU   B 83  ? 0.1402 0.1199 0.1448 -0.0123 -0.0185 -0.0024 83  LEU   B N   
5249 C  CA  . LEU   B 83  ? 0.1415 0.1251 0.1364 -0.0139 -0.0175 -0.0034 83  LEU   B CA  
5250 C  C   . LEU   B 83  ? 0.1452 0.1197 0.1364 -0.0148 -0.0182 0.0048  83  LEU   B C   
5251 O  O   . LEU   B 83  ? 0.1514 0.1335 0.1264 -0.0247 -0.0181 -0.0012 83  LEU   B O   
5252 C  CB  . LEU   B 83  ? 0.1457 0.1346 0.1354 -0.0122 -0.0194 -0.0027 83  LEU   B CB  
5253 C  CG  . LEU   B 83  ? 0.1606 0.1577 0.1499 -0.0183 -0.0127 -0.0041 83  LEU   B CG  
5254 C  CD1 . LEU   B 83  ? 0.1823 0.1638 0.1519 -0.0169 -0.0198 0.0066  83  LEU   B CD1 
5255 C  CD2 . LEU   B 83  ? 0.1903 0.1644 0.1750 -0.0146 -0.0146 -0.0182 83  LEU   B CD2 
5267 N  N   . SER   B 84  ? 0.1472 0.1395 0.1509 -0.0223 -0.0188 0.0130  84  SER   B N   
5268 C  CA  . SER   B 84  ? 0.1484 0.1576 0.1446 -0.0271 -0.0161 0.0230  84  SER   B CA  
5269 C  C   . SER   B 84  ? 0.1413 0.1679 0.1194 -0.0223 -0.0224 0.0196  84  SER   B C   
5270 O  O   . SER   B 84  ? 0.1536 0.1530 0.1178 -0.0150 -0.0123 0.0081  84  SER   B O   
5271 C  CB  . SER   B 84  ? 0.1680 0.1617 0.1868 -0.0284 0.0030  0.0182  84  SER   B CB  
5272 O  OG  . SER   B 84  ? 0.1646 0.1733 0.2193 -0.0366 0.0039  0.0221  84  SER   B OG  
5278 N  N   . GLY   B 85  ? 0.1424 0.1875 0.1283 -0.0254 -0.0187 0.0229  85  GLY   B N   
5279 C  CA  . GLY   B 85  ? 0.1514 0.1995 0.1450 -0.0353 -0.0058 -0.0075 85  GLY   B CA  
5280 C  C   . GLY   B 85  ? 0.1485 0.1798 0.1298 -0.0429 -0.0114 0.0142  85  GLY   B C   
5281 O  O   . GLY   B 85  ? 0.1560 0.1812 0.1360 -0.0543 0.0129  -0.0065 85  GLY   B O   
5285 N  N   . HIS   B 86  ? 0.1428 0.1665 0.1418 -0.0349 -0.0151 0.0245  86  HIS   B N   
5286 C  CA  . HIS   B 86  ? 0.1500 0.1686 0.1375 -0.0352 -0.0179 0.0218  86  HIS   B CA  
5287 C  C   . HIS   B 86  ? 0.1525 0.1795 0.1345 -0.0469 0.0034  0.0318  86  HIS   B C   
5288 O  O   . HIS   B 86  ? 0.1626 0.1935 0.1392 -0.0392 0.0054  0.0285  86  HIS   B O   
5289 C  CB  . HIS   B 86  ? 0.1556 0.1734 0.1461 -0.0225 -0.0187 0.0118  86  HIS   B CB  
5290 C  CG  . HIS   B 86  ? 0.1533 0.1795 0.1456 -0.0097 -0.0150 0.0135  86  HIS   B CG  
5291 N  ND1 . HIS   B 86  ? 0.1705 0.2005 0.1593 -0.0286 -0.0194 0.0004  86  HIS   B ND1 
5292 C  CD2 . HIS   B 86  ? 0.1559 0.1845 0.1487 -0.0067 -0.0164 0.0074  86  HIS   B CD2 
5293 C  CE1 . HIS   B 86  ? 0.1768 0.1956 0.1429 -0.0153 -0.0071 -0.0070 86  HIS   B CE1 
5294 N  NE2 . HIS   B 86  ? 0.1708 0.1875 0.1322 -0.0012 -0.0104 0.0069  86  HIS   B NE2 
5302 N  N   . ASN   B 87  ? 0.1562 0.1815 0.1485 -0.0341 -0.0012 0.0190  87  ASN   B N   
5303 C  CA  . ASN   B 87  ? 0.1671 0.2030 0.1495 -0.0335 0.0261  0.0140  87  ASN   B CA  
5304 C  C   . ASN   B 87  ? 0.1826 0.1906 0.1366 -0.0311 0.0286  0.0166  87  ASN   B C   
5305 O  O   . ASN   B 87  ? 0.2089 0.2027 0.1563 -0.0274 0.0537  0.0060  87  ASN   B O   
5306 C  CB  . ASN   B 87  ? 0.1683 0.2336 0.1891 -0.0315 0.0322  0.0111  87  ASN   B CB  
5307 C  CG  . ASN   B 87  ? 0.1743 0.2485 0.1981 0.0004  0.0407  0.0335  87  ASN   B CG  
5308 O  OD1 . ASN   B 87  ? 0.1670 0.2337 0.1830 0.0097  0.0498  0.0474  87  ASN   B OD1 
5309 N  ND2 . ASN   B 87  ? 0.2089 0.2576 0.2316 0.0101  0.0527  0.0318  87  ASN   B ND2 
5316 N  N   . LEU   B 88  ? 0.1653 0.1726 0.1225 -0.0376 0.0189  0.0093  88  LEU   B N   
5317 C  CA  . LEU   B 88  ? 0.1847 0.1652 0.1282 -0.0367 0.0012  -0.0025 88  LEU   B CA  
5318 C  C   . LEU   B 88  ? 0.1817 0.1545 0.1275 -0.0440 -0.0046 -0.0030 88  LEU   B C   
5319 O  O   . LEU   B 88  ? 0.2048 0.1587 0.1637 -0.0292 -0.0234 -0.0074 88  LEU   B O   
5320 C  CB  . LEU   B 88  ? 0.1932 0.1768 0.1428 -0.0514 -0.0133 0.0103  88  LEU   B CB  
5321 C  CG  . LEU   B 88  ? 0.2284 0.2038 0.1709 -0.0408 -0.0215 0.0289  88  LEU   B CG  
5322 C  CD1 . LEU   B 88  ? 0.2325 0.2323 0.1882 -0.0543 -0.0161 0.0427  88  LEU   B CD1 
5323 C  CD2 . LEU   B 88  ? 0.2677 0.2286 0.2367 0.0009  -0.0325 0.0073  88  LEU   B CD2 
5335 N  N   . ALA   B 89  ? 0.1597 0.1570 0.1239 -0.0430 0.0099  -0.0067 89  ALA   B N   
5336 C  CA  . ALA   B 89  ? 0.1562 0.1523 0.1213 -0.0415 0.0024  0.0083  89  ALA   B CA  
5337 C  C   . ALA   B 89  ? 0.1679 0.1567 0.1192 -0.0458 0.0125  0.0058  89  ALA   B C   
5338 O  O   . ALA   B 89  ? 0.1489 0.1620 0.1459 -0.0439 0.0122  -0.0213 89  ALA   B O   
5339 C  CB  . ALA   B 89  ? 0.1443 0.1523 0.1270 -0.0380 0.0020  0.0146  89  ALA   B CB  
5345 N  N   . LYS   B 90  ? 0.2063 0.1431 0.1288 -0.0530 -0.0190 0.0199  90  LYS   B N   
5346 C  CA  . LYS   B 90  ? 0.2124 0.1418 0.1338 -0.0490 -0.0156 0.0155  90  LYS   B CA  
5347 C  C   . LYS   B 90  ? 0.1907 0.1352 0.1365 -0.0418 -0.0133 0.0076  90  LYS   B C   
5348 O  O   . LYS   B 90  ? 0.1969 0.1446 0.1462 -0.0503 -0.0118 0.0090  90  LYS   B O   
5349 C  CB  . LYS   B 90  ? 0.2207 0.1475 0.1538 -0.0418 -0.0137 0.0198  90  LYS   B CB  
5350 C  CG  . LYS   B 90  ? 0.2113 0.1596 0.1606 -0.0293 0.0103  0.0169  90  LYS   B CG  
5351 C  CD  . LYS   B 90  ? 0.2268 0.1824 0.2022 -0.0135 0.0319  -0.0032 90  LYS   B CD  
5352 C  CE  . LYS   B 90  ? 0.2405 0.1928 0.2526 -0.0149 0.0393  -0.0167 90  LYS   B CE  
5353 N  NZ  . LYS   B 90  ? 0.2426 0.1803 0.2470 -0.0263 0.0575  -0.0173 90  LYS   B NZ  
5367 N  N   . HIS   B 91  ? 0.1663 0.1252 0.1157 -0.0272 -0.0181 0.0138  91  HIS   B N   
5368 C  CA  . HIS   B 91  ? 0.1531 0.1259 0.1328 -0.0240 -0.0211 0.0101  91  HIS   B CA  
5369 C  C   . HIS   B 91  ? 0.1429 0.1254 0.1230 -0.0256 -0.0142 0.0116  91  HIS   B C   
5370 O  O   . HIS   B 91  ? 0.1668 0.1265 0.1209 -0.0279 -0.0190 0.0030  91  HIS   B O   
5371 C  CB  . HIS   B 91  ? 0.1766 0.1293 0.1733 -0.0116 -0.0124 0.0176  91  HIS   B CB  
5372 C  CG  . HIS   B 91  ? 0.2123 0.1462 0.2303 0.0027  0.0203  0.0252  91  HIS   B CG  
5373 N  ND1 . HIS   B 91  ? 0.2444 0.1511 0.2780 0.0020  0.0256  0.0053  91  HIS   B ND1 
5374 C  CD2 . HIS   B 91  ? 0.2219 0.1750 0.2717 0.0173  0.0042  0.0587  91  HIS   B CD2 
5375 C  CE1 . HIS   B 91  ? 0.2460 0.1659 0.2991 0.0164  0.0232  0.0182  91  HIS   B CE1 
5376 N  NE2 . HIS   B 91  ? 0.2344 0.1797 0.2956 0.0271  0.0142  0.0599  91  HIS   B NE2 
5384 N  N   . CYS   B 92  ? 0.1359 0.1250 0.1225 -0.0233 -0.0134 0.0061  92  CYS   B N   
5385 C  CA  . CYS   B 92  ? 0.1358 0.1271 0.1233 -0.0177 -0.0097 0.0048  92  CYS   B CA  
5386 C  C   . CYS   B 92  ? 0.1323 0.1198 0.1138 -0.0123 -0.0067 0.0050  92  CYS   B C   
5387 O  O   . CYS   B 92  ? 0.1397 0.1280 0.1281 -0.0161 -0.0046 -0.0013 92  CYS   B O   
5388 C  CB  . CYS   B 92  ? 0.1409 0.1304 0.1279 -0.0119 -0.0050 0.0033  92  CYS   B CB  
5389 S  SG  . CYS   B 92  ? 0.1369 0.1297 0.1349 -0.0115 -0.0090 0.0068  92  CYS   B SG  
5395 N  N   . LEU   B 93  ? 0.1285 0.1190 0.1153 -0.0136 -0.0080 0.0015  93  LEU   B N   
5396 C  CA  . LEU   B 93  ? 0.1269 0.1204 0.1292 -0.0060 -0.0140 0.0120  93  LEU   B CA  
5397 C  C   . LEU   B 93  ? 0.1261 0.1168 0.1155 -0.0017 -0.0135 0.0079  93  LEU   B C   
5398 O  O   . LEU   B 93  ? 0.1305 0.1188 0.1270 -0.0054 -0.0061 0.0048  93  LEU   B O   
5399 C  CB  . LEU   B 93  ? 0.1338 0.1176 0.1426 -0.0014 -0.0068 0.0121  93  LEU   B CB  
5400 C  CG  . LEU   B 93  ? 0.1253 0.1294 0.1587 -0.0055 -0.0038 0.0169  93  LEU   B CG  
5401 C  CD1 . LEU   B 93  ? 0.1278 0.1453 0.1649 0.0027  -0.0055 -0.0033 93  LEU   B CD1 
5402 C  CD2 . LEU   B 93  ? 0.1317 0.1303 0.1716 -0.0072 -0.0179 0.0096  93  LEU   B CD2 
5414 N  N   . HIS   B 94  ? 0.1293 0.1189 0.1163 -0.0071 -0.0121 0.0059  94  HIS   B N   
5415 C  CA  . HIS   B 94  ? 0.1336 0.1169 0.1161 -0.0012 -0.0127 0.0114  94  HIS   B CA  
5416 C  C   . HIS   B 94  ? 0.1299 0.1165 0.1262 0.0028  -0.0029 0.0117  94  HIS   B C   
5417 O  O   . HIS   B 94  ? 0.1289 0.1248 0.1677 -0.0060 0.0116  -0.0018 94  HIS   B O   
5418 C  CB  . HIS   B 94  ? 0.1316 0.1228 0.1332 0.0023  -0.0135 0.0071  94  HIS   B CB  
5419 C  CG  . HIS   B 94  ? 0.1320 0.1191 0.1198 -0.0037 -0.0184 0.0058  94  HIS   B CG  
5420 N  ND1 . HIS   B 94  ? 0.1341 0.1259 0.1223 -0.0048 -0.0140 0.0027  94  HIS   B ND1 
5421 C  CD2 . HIS   B 94  ? 0.1335 0.1251 0.1292 -0.0061 -0.0193 0.0059  94  HIS   B CD2 
5422 C  CE1 . HIS   B 94  ? 0.1324 0.1248 0.1255 -0.0070 -0.0150 0.0073  94  HIS   B CE1 
5423 N  NE2 . HIS   B 94  ? 0.1305 0.1345 0.1335 -0.0155 -0.0100 0.0065  94  HIS   B NE2 
5431 N  N   . VAL   B 95  ? 0.1241 0.1178 0.1292 0.0016  -0.0073 0.0082  95  VAL   B N   
5432 C  CA  . VAL   B 95  ? 0.1268 0.1250 0.1302 -0.0002 0.0071  0.0201  95  VAL   B CA  
5433 C  C   . VAL   B 95  ? 0.1347 0.1264 0.1303 0.0016  0.0142  0.0101  95  VAL   B C   
5434 O  O   . VAL   B 95  ? 0.1348 0.1235 0.1487 0.0101  0.0049  0.0186  95  VAL   B O   
5435 C  CB  . VAL   B 95  ? 0.1310 0.1239 0.1430 -0.0047 -0.0068 0.0101  95  VAL   B CB  
5436 C  CG1 . VAL   B 95  ? 0.1361 0.1392 0.1630 -0.0082 -0.0092 0.0168  95  VAL   B CG1 
5437 C  CG2 . VAL   B 95  ? 0.1414 0.1228 0.1340 -0.0007 -0.0151 0.0084  95  VAL   B CG2 
5447 N  N   . VAL   B 96  ? 0.1383 0.1286 0.1406 0.0086  0.0035  0.0154  96  VAL   B N   
5448 C  CA  . VAL   B 96  ? 0.1466 0.1393 0.1392 0.0075  0.0009  0.0250  96  VAL   B CA  
5449 C  C   . VAL   B 96  ? 0.1526 0.1413 0.1478 0.0084  0.0116  0.0223  96  VAL   B C   
5450 O  O   . VAL   B 96  ? 0.1543 0.1515 0.1611 -0.0005 0.0182  0.0106  96  VAL   B O   
5451 C  CB  . VAL   B 96  ? 0.1494 0.1639 0.1351 0.0079  0.0042  0.0135  96  VAL   B CB  
5452 C  CG1 . VAL   B 96  ? 0.1543 0.1755 0.1486 0.0110  0.0117  0.0192  96  VAL   B CG1 
5453 C  CG2 . VAL   B 96  ? 0.1677 0.1587 0.1301 0.0054  0.0043  0.0058  96  VAL   B CG2 
5463 N  N   . GLY   B 97  ? 0.1655 0.1439 0.1441 0.0018  0.0045  0.0244  97  GLY   B N   
5464 C  CA  . GLY   B 97  ? 0.1772 0.1464 0.1460 0.0026  0.0039  0.0259  97  GLY   B CA  
5465 C  C   . GLY   B 97  ? 0.2031 0.1590 0.1521 0.0087  0.0144  0.0147  97  GLY   B C   
5466 O  O   . GLY   B 97  ? 0.2173 0.1631 0.1474 0.0035  0.0093  0.0132  97  GLY   B O   
5470 N  N   . PRO   B 98  ? 0.2156 0.1634 0.1744 0.0145  0.0384  0.0336  98  PRO   B N   
5471 C  CA  . PRO   B 98  ? 0.2323 0.1801 0.1758 0.0268  0.0589  0.0383  98  PRO   B CA  
5472 C  C   . PRO   B 98  ? 0.2515 0.1782 0.1448 0.0460  0.0595  0.0581  98  PRO   B C   
5473 O  O   . PRO   B 98  ? 0.2410 0.1744 0.1711 0.0351  0.0534  0.0417  98  PRO   B O   
5474 C  CB  . PRO   B 98  ? 0.2211 0.1855 0.2067 0.0190  0.0652  0.0328  98  PRO   B CB  
5475 C  CG  . PRO   B 98  ? 0.2155 0.1760 0.2071 0.0147  0.0530  0.0501  98  PRO   B CG  
5476 C  CD  . PRO   B 98  ? 0.1997 0.1684 0.1974 0.0178  0.0458  0.0449  98  PRO   B CD  
5484 N  N   . ASN   B 99  ? 0.2714 0.2043 0.1480 0.0648  0.0652  0.0400  99  ASN   B N   
5485 C  CA  . ASN   B 99  ? 0.2965 0.2176 0.1636 0.0763  0.0518  0.0644  99  ASN   B CA  
5486 C  C   . ASN   B 99  ? 0.3247 0.2533 0.2123 0.0657  0.0719  0.0968  99  ASN   B C   
5487 O  O   . ASN   B 99  ? 0.3322 0.2540 0.2136 0.0751  0.0664  0.0875  99  ASN   B O   
5488 C  CB  . ASN   B 99  ? 0.3044 0.2124 0.1685 0.0771  0.0424  0.0592  99  ASN   B CB  
5489 C  CG  . ASN   B 99  ? 0.3096 0.2216 0.1874 0.0706  0.0348  0.0505  99  ASN   B CG  
5490 O  OD1 . ASN   B 99  ? 0.3097 0.2226 0.2194 0.0760  0.0371  0.0529  99  ASN   B OD1 
5491 N  ND2 . ASN   B 99  ? 0.3090 0.2229 0.1983 0.0704  0.0085  0.0399  99  ASN   B ND2 
5498 N  N   A VAL   B 100 ? 0.3434 0.2707 0.2611 0.0480  0.0719  0.1182  100 VAL   B N   
5499 N  N   B VAL   B 100 ? 0.3433 0.2703 0.2621 0.0479  0.0705  0.1183  100 VAL   B N   
5500 C  CA  A VAL   B 100 ? 0.3655 0.2913 0.3172 0.0333  0.0620  0.1348  100 VAL   B CA  
5501 C  CA  B VAL   B 100 ? 0.3651 0.2903 0.3184 0.0331  0.0598  0.1353  100 VAL   B CA  
5502 C  C   A VAL   B 100 ? 0.3851 0.2998 0.3098 0.0367  0.0538  0.1543  100 VAL   B C   
5503 C  C   B VAL   B 100 ? 0.3847 0.2986 0.3089 0.0362  0.0520  0.1546  100 VAL   B C   
5504 O  O   A VAL   B 100 ? 0.3899 0.3111 0.3206 0.0368  0.0584  0.1410  100 VAL   B O   
5505 O  O   B VAL   B 100 ? 0.3891 0.3084 0.3167 0.0355  0.0552  0.1413  100 VAL   B O   
5506 C  CB  A VAL   B 100 ? 0.3688 0.3009 0.3745 0.0143  0.0567  0.1385  100 VAL   B CB  
5507 C  CB  B VAL   B 100 ? 0.3681 0.2995 0.3767 0.0143  0.0538  0.1398  100 VAL   B CB  
5508 C  CG1 A VAL   B 100 ? 0.3708 0.3063 0.3958 0.0095  0.0537  0.1377  100 VAL   B CG1 
5509 C  CG1 B VAL   B 100 ? 0.3699 0.3046 0.3985 0.0098  0.0504  0.1400  100 VAL   B CG1 
5510 C  CG2 A VAL   B 100 ? 0.3695 0.3055 0.3898 0.0075  0.0551  0.1430  100 VAL   B CG2 
5511 C  CG2 B VAL   B 100 ? 0.3686 0.3039 0.3923 0.0073  0.0522  0.1443  100 VAL   B CG2 
5530 N  N   . ASN   B 101 ? 0.4003 0.3041 0.3044 0.0417  0.0374  0.1657  101 ASN   B N   
5531 C  CA  . ASN   B 101 ? 0.4369 0.3283 0.3230 0.0398  0.0129  0.1610  101 ASN   B CA  
5532 C  C   . ASN   B 101 ? 0.4900 0.3844 0.3499 0.0290  0.0028  0.1422  101 ASN   B C   
5533 O  O   . ASN   B 101 ? 0.4939 0.3933 0.3636 0.0323  0.0025  0.1202  101 ASN   B O   
5534 C  CB  . ASN   B 101 ? 0.4244 0.3089 0.3267 0.0365  0.0106  0.1463  101 ASN   B CB  
5535 C  CG  . ASN   B 101 ? 0.4112 0.2909 0.3281 0.0303  0.0143  0.1384  101 ASN   B CG  
5536 O  OD1 . ASN   B 101 ? 0.4087 0.2890 0.3507 0.0245  0.0271  0.1314  101 ASN   B OD1 
5537 N  ND2 . ASN   B 101 ? 0.4037 0.2877 0.3222 0.0290  0.0097  0.1262  101 ASN   B ND2 
5545 N  N   A LYS   B 102 ? 0.5131 0.4117 0.3728 0.0200  0.0044  0.1288  102 LYS   B N   
5546 N  N   B LYS   B 102 ? 0.5141 0.4117 0.3709 0.0216  0.0017  0.1303  102 LYS   B N   
5547 C  CA  A LYS   B 102 ? 0.5341 0.4406 0.4031 0.0100  0.0083  0.1079  102 LYS   B CA  
5548 C  CA  B LYS   B 102 ? 0.5360 0.4410 0.3995 0.0131  0.0031  0.1105  102 LYS   B CA  
5549 C  C   A LYS   B 102 ? 0.5381 0.4454 0.3777 0.0105  0.0115  0.1198  102 LYS   B C   
5550 C  C   B LYS   B 102 ? 0.5391 0.4455 0.3746 0.0122  0.0086  0.1220  102 LYS   B C   
5551 O  O   A LYS   B 102 ? 0.5434 0.4473 0.3728 0.0116  0.0032  0.1226  102 LYS   B O   
5552 O  O   B LYS   B 102 ? 0.5443 0.4474 0.3671 0.0134  -0.0002 0.1264  102 LYS   B O   
5553 C  CB  A LYS   B 102 ? 0.5487 0.4630 0.4605 0.0005  0.0139  0.0724  102 LYS   B CB  
5554 C  CB  B LYS   B 102 ? 0.5525 0.4640 0.4561 0.0063  0.0040  0.0761  102 LYS   B CB  
5555 C  CG  A LYS   B 102 ? 0.5609 0.4819 0.5173 -0.0069 0.0202  0.0386  102 LYS   B CG  
5556 C  CG  B LYS   B 102 ? 0.5664 0.4838 0.5132 0.0013  0.0058  0.0434  102 LYS   B CG  
5557 C  CD  A LYS   B 102 ? 0.5709 0.4974 0.5663 -0.0123 0.0264  0.0111  102 LYS   B CD  
5558 C  CD  B LYS   B 102 ? 0.5778 0.5000 0.5639 -0.0024 0.0084  0.0163  102 LYS   B CD  
5559 C  CE  A LYS   B 102 ? 0.5769 0.5077 0.6033 -0.0163 0.0315  -0.0084 102 LYS   B CE  
5560 C  CE  B LYS   B 102 ? 0.5848 0.5107 0.6032 -0.0050 0.0109  -0.0031 102 LYS   B CE  
5561 N  NZ  A LYS   B 102 ? 0.5799 0.5130 0.6235 -0.0180 0.0338  -0.0197 102 LYS   B NZ  
5562 N  NZ  B LYS   B 102 ? 0.5885 0.5164 0.6255 -0.0062 0.0118  -0.0140 102 LYS   B NZ  
5589 N  N   . GLY   B 103 ? 0.5337 0.4451 0.3666 0.0103  0.0263  0.1234  103 GLY   B N   
5590 C  CA  . GLY   B 103 ? 0.5223 0.4425 0.3710 0.0110  0.0580  0.1171  103 GLY   B CA  
5591 C  C   . GLY   B 103 ? 0.5075 0.4364 0.3664 0.0118  0.0880  0.1083  103 GLY   B C   
5592 O  O   . GLY   B 103 ? 0.5115 0.4409 0.3671 0.0101  0.0937  0.1109  103 GLY   B O   
5597 N  N   . GLU   B 104 ? 0.4855 0.4211 0.3532 0.0159  0.1104  0.0897  104 GLU   B N   
5598 C  CA  . GLU   B 104 ? 0.4628 0.4065 0.3440 0.0245  0.1227  0.0645  104 GLU   B CA  
5599 C  C   . GLU   B 104 ? 0.4640 0.4050 0.3703 0.0050  0.1583  0.0606  104 GLU   B C   
5600 O  O   . GLU   B 104 ? 0.4632 0.4047 0.3891 0.0011  0.1609  0.0605  104 GLU   B O   
5601 C  CB  . GLU   B 104 ? 0.4438 0.3920 0.3290 0.0533  0.0848  0.0331  104 GLU   B CB  
5602 C  CG  . GLU   B 104 ? 0.4261 0.3795 0.3107 0.0822  0.0404  -0.0006 104 GLU   B CG  
5603 C  CD  . GLU   B 104 ? 0.4112 0.3671 0.2872 0.1045  0.0051  -0.0257 104 GLU   B CD  
5604 O  OE1 . GLU   B 104 ? 0.4000 0.3554 0.2448 0.1182  0.0118  -0.0364 104 GLU   B OE1 
5605 O  OE2 . GLU   B 104 ? 0.4075 0.3696 0.2809 0.1098  -0.0263 -0.0388 104 GLU   B OE2 
5612 N  N   A ASP   B 105 ? 0.4636 0.4043 0.3780 -0.0023 0.1730  0.0569  105 ASP   B N   
5613 N  N   B ASP   B 105 ? 0.4628 0.4027 0.3740 -0.0021 0.1728  0.0582  105 ASP   B N   
5614 C  CA  A ASP   B 105 ? 0.4636 0.4028 0.3941 -0.0082 0.1818  0.0433  105 ASP   B CA  
5615 C  CA  B ASP   B 105 ? 0.4621 0.3997 0.3864 -0.0078 0.1813  0.0459  105 ASP   B CA  
5616 C  C   A ASP   B 105 ? 0.4490 0.3812 0.3556 -0.0144 0.1923  0.0397  105 ASP   B C   
5617 C  C   B ASP   B 105 ? 0.4475 0.3794 0.3504 -0.0141 0.1941  0.0406  105 ASP   B C   
5618 O  O   A ASP   B 105 ? 0.4453 0.3767 0.3357 -0.0141 0.2067  0.0410  105 ASP   B O   
5619 O  O   B ASP   B 105 ? 0.4421 0.3745 0.3276 -0.0136 0.2132  0.0415  105 ASP   B O   
5620 C  CB  A ASP   B 105 ? 0.4750 0.4195 0.4572 -0.0060 0.1767  0.0310  105 ASP   B CB  
5621 C  CB  B ASP   B 105 ? 0.4725 0.4139 0.4433 -0.0057 0.1743  0.0367  105 ASP   B CB  
5622 C  CG  A ASP   B 105 ? 0.4828 0.4319 0.5130 -0.0061 0.1750  0.0229  105 ASP   B CG  
5623 C  CG  B ASP   B 105 ? 0.4796 0.4238 0.4931 -0.0059 0.1711  0.0321  105 ASP   B CG  
5624 O  OD1 A ASP   B 105 ? 0.4834 0.4354 0.5237 -0.0098 0.1801  0.0260  105 ASP   B OD1 
5625 O  OD1 B ASP   B 105 ? 0.4807 0.4269 0.5046 -0.0096 0.1741  0.0355  105 ASP   B OD1 
5626 O  OD2 A ASP   B 105 ? 0.4864 0.4370 0.5449 -0.0036 0.1676  0.0155  105 ASP   B OD2 
5627 O  OD2 B ASP   B 105 ? 0.4811 0.4278 0.5154 -0.0043 0.1684  0.0282  105 ASP   B OD2 
5636 N  N   . ILE   B 106 ? 0.4353 0.3614 0.3503 -0.0202 0.1845  0.0376  106 ILE   B N   
5637 C  CA  . ILE   B 106 ? 0.4039 0.3219 0.3521 -0.0321 0.1794  0.0279  106 ILE   B CA  
5638 C  C   . ILE   B 106 ? 0.3586 0.3110 0.3419 -0.0280 0.1704  0.0090  106 ILE   B C   
5639 O  O   . ILE   B 106 ? 0.3473 0.2831 0.3371 -0.0430 0.1770  0.0134  106 ILE   B O   
5640 C  CB  . ILE   B 106 ? 0.4218 0.3028 0.3701 -0.0423 0.1741  0.0296  106 ILE   B CB  
5641 C  CG1 . ILE   B 106 ? 0.4314 0.2973 0.3743 -0.0366 0.1590  0.0199  106 ILE   B CG1 
5642 C  CG2 . ILE   B 106 ? 0.4276 0.3022 0.3907 -0.0484 0.1786  0.0309  106 ILE   B CG2 
5643 C  CD1 . ILE   B 106 ? 0.4368 0.2961 0.3695 -0.0332 0.1518  0.0193  106 ILE   B CD1 
5656 N  N   A GLN   B 107 ? 0.3448 0.3224 0.3507 -0.0244 0.1544  0.0036  107 GLN   B N   
5657 N  N   B GLN   B 107 ? 0.3448 0.3220 0.3488 -0.0245 0.1555  0.0039  107 GLN   B N   
5658 C  CA  A GLN   B 107 ? 0.3298 0.3321 0.3644 -0.0201 0.1303  0.0034  107 GLN   B CA  
5659 C  CA  B GLN   B 107 ? 0.3298 0.3315 0.3606 -0.0203 0.1325  0.0038  107 GLN   B CA  
5660 C  C   A GLN   B 107 ? 0.2962 0.3088 0.3327 -0.0087 0.1196  -0.0032 107 GLN   B C   
5661 C  C   B GLN   B 107 ? 0.2958 0.3088 0.3285 -0.0090 0.1234  -0.0028 107 GLN   B C   
5662 O  O   A GLN   B 107 ? 0.2886 0.3101 0.3492 -0.0010 0.1051  -0.0195 107 GLN   B O   
5663 O  O   B GLN   B 107 ? 0.2882 0.3111 0.3440 -0.0012 0.1113  -0.0192 107 GLN   B O   
5664 C  CB  A GLN   B 107 ? 0.3553 0.3660 0.4232 -0.0198 0.1039  0.0061  107 GLN   B CB  
5665 C  CB  B GLN   B 107 ? 0.3563 0.3647 0.4190 -0.0200 0.1045  0.0067  107 GLN   B CB  
5666 C  CG  A GLN   B 107 ? 0.3794 0.3949 0.4780 -0.0174 0.0760  0.0090  107 GLN   B CG  
5667 C  CG  B GLN   B 107 ? 0.3815 0.3932 0.4738 -0.0174 0.0747  0.0094  107 GLN   B CG  
5668 C  CD  A GLN   B 107 ? 0.3977 0.4168 0.5219 -0.0155 0.0550  0.0131  107 GLN   B CD  
5669 C  CD  B GLN   B 107 ? 0.4011 0.4145 0.5179 -0.0153 0.0518  0.0129  107 GLN   B CD  
5670 O  OE1 A GLN   B 107 ? 0.4042 0.4249 0.5383 -0.0131 0.0504  0.0142  107 GLN   B OE1 
5671 O  OE1 B GLN   B 107 ? 0.4080 0.4223 0.5340 -0.0140 0.0469  0.0145  107 GLN   B OE1 
5672 N  NE2 A GLN   B 107 ? 0.4054 0.4241 0.5373 -0.0143 0.0465  0.0153  107 GLN   B NE2 
5673 N  NE2 B GLN   B 107 ? 0.4091 0.4219 0.5333 -0.0140 0.0427  0.0145  107 GLN   B NE2 
5690 N  N   . LEU   B 108 ? 0.2683 0.2855 0.2951 0.0051  0.1180  0.0019  108 LEU   B N   
5691 C  CA  . LEU   B 108 ? 0.2364 0.2534 0.2422 0.0209  0.0905  0.0203  108 LEU   B CA  
5692 C  C   . LEU   B 108 ? 0.1986 0.2031 0.2314 0.0259  0.0563  0.0254  108 LEU   B C   
5693 O  O   . LEU   B 108 ? 0.1883 0.1881 0.2229 0.0295  0.0426  0.0252  108 LEU   B O   
5694 C  CB  . LEU   B 108 ? 0.2509 0.2760 0.2205 0.0255  0.0919  0.0289  108 LEU   B CB  
5695 C  CG  . LEU   B 108 ? 0.2648 0.3058 0.2338 0.0300  0.0743  0.0138  108 LEU   B CG  
5696 C  CD1 . LEU   B 108 ? 0.2763 0.3211 0.2307 0.0264  0.0669  0.0166  108 LEU   B CD1 
5697 C  CD2 . LEU   B 108 ? 0.2736 0.3140 0.2421 0.0333  0.0570  0.0032  108 LEU   B CD2 
5710 N  N   . LEU   B 109 ? 0.1819 0.1756 0.2227 0.0184  0.0472  0.0289  109 LEU   B N   
5711 C  CA  . LEU   B 109 ? 0.1593 0.1482 0.2301 0.0056  0.0421  0.0289  109 LEU   B CA  
5712 C  C   . LEU   B 109 ? 0.1476 0.1331 0.2293 -0.0003 0.0396  0.0287  109 LEU   B C   
5713 O  O   . LEU   B 109 ? 0.1446 0.1284 0.2245 0.0024  0.0398  0.0298  109 LEU   B O   
5714 C  CB  . LEU   B 109 ? 0.1688 0.1447 0.2280 0.0014  0.0316  0.0350  109 LEU   B CB  
5715 C  CG  . LEU   B 109 ? 0.1643 0.1376 0.2191 0.0084  0.0225  0.0224  109 LEU   B CG  
5716 C  CD1 . LEU   B 109 ? 0.1640 0.1465 0.2114 0.0025  0.0214  0.0263  109 LEU   B CD1 
5717 C  CD2 . LEU   B 109 ? 0.1810 0.1512 0.2358 0.0099  0.0235  0.0193  109 LEU   B CD2 
5729 N  N   . LYS   B 110 ? 0.1447 0.1353 0.2259 -0.0058 0.0366  0.0236  110 LYS   B N   
5730 C  CA  . LYS   B 110 ? 0.1462 0.1265 0.2319 -0.0037 0.0272  0.0145  110 LYS   B CA  
5731 C  C   . LYS   B 110 ? 0.1390 0.1293 0.2218 -0.0028 0.0270  0.0123  110 LYS   B C   
5732 O  O   . LYS   B 110 ? 0.1344 0.1302 0.2195 -0.0089 0.0234  0.0068  110 LYS   B O   
5733 C  CB  . LYS   B 110 ? 0.1475 0.1262 0.2522 -0.0050 0.0312  0.0085  110 LYS   B CB  
5734 C  CG  . LYS   B 110 ? 0.1413 0.1335 0.2562 -0.0039 0.0211  0.0173  110 LYS   B CG  
5735 C  CD  . LYS   B 110 ? 0.1543 0.1400 0.2651 -0.0088 0.0173  0.0180  110 LYS   B CD  
5736 C  CE  . LYS   B 110 ? 0.1544 0.1544 0.2751 -0.0033 0.0133  0.0175  110 LYS   B CE  
5737 N  NZ  . LYS   B 110 ? 0.1489 0.1680 0.2756 -0.0006 0.0090  0.0136  110 LYS   B NZ  
5751 N  N   . SER   B 111 ? 0.1464 0.1300 0.2248 -0.0013 0.0170  0.0108  111 SER   B N   
5752 C  CA  . SER   B 111 ? 0.1533 0.1354 0.2062 0.0018  0.0193  0.0169  111 SER   B CA  
5753 C  C   . SER   B 111 ? 0.1437 0.1308 0.2002 -0.0024 0.0150  0.0076  111 SER   B C   
5754 O  O   . SER   B 111 ? 0.1400 0.1328 0.2107 -0.0029 0.0093  0.0116  111 SER   B O   
5755 C  CB  . SER   B 111 ? 0.1692 0.1544 0.2099 0.0056  0.0374  0.0182  111 SER   B CB  
5756 O  OG  . SER   B 111 ? 0.1902 0.1848 0.2222 0.0118  0.0398  0.0275  111 SER   B OG  
5762 N  N   . ALA   B 112 ? 0.1344 0.1330 0.2094 0.0023  0.0238  0.0137  112 ALA   B N   
5763 C  CA  . ALA   B 112 ? 0.1330 0.1375 0.1970 -0.0026 0.0063  0.0074  112 ALA   B CA  
5764 C  C   . ALA   B 112 ? 0.1285 0.1331 0.1914 -0.0004 0.0085  0.0053  112 ALA   B C   
5765 O  O   . ALA   B 112 ? 0.1293 0.1317 0.2003 -0.0039 0.0169  0.0085  112 ALA   B O   
5766 C  CB  . ALA   B 112 ? 0.1331 0.1451 0.1957 0.0047  0.0119  0.0179  112 ALA   B CB  
5772 N  N   . TYR   B 113 ? 0.1248 0.1190 0.1938 0.0029  0.0096  0.0116  113 TYR   B N   
5773 C  CA  . TYR   B 113 ? 0.1234 0.1206 0.1944 -0.0028 0.0151  -0.0006 113 TYR   B CA  
5774 C  C   . TYR   B 113 ? 0.1207 0.1120 0.1960 -0.0071 0.0082  0.0040  113 TYR   B C   
5775 O  O   . TYR   B 113 ? 0.1251 0.1148 0.1879 -0.0051 0.0026  -0.0029 113 TYR   B O   
5776 C  CB  . TYR   B 113 ? 0.1269 0.1159 0.1906 -0.0037 0.0122  0.0119  113 TYR   B CB  
5777 C  CG  . TYR   B 113 ? 0.1284 0.1163 0.2058 -0.0015 0.0089  0.0180  113 TYR   B CG  
5778 C  CD1 . TYR   B 113 ? 0.1343 0.1246 0.2182 -0.0056 0.0083  0.0281  113 TYR   B CD1 
5779 C  CD2 . TYR   B 113 ? 0.1393 0.1197 0.2024 -0.0052 0.0071  0.0142  113 TYR   B CD2 
5780 C  CE1 . TYR   B 113 ? 0.1374 0.1245 0.2155 -0.0014 0.0236  0.0203  113 TYR   B CE1 
5781 C  CE2 . TYR   B 113 ? 0.1433 0.1143 0.2146 -0.0004 0.0072  0.0162  113 TYR   B CE2 
5782 C  CZ  . TYR   B 113 ? 0.1361 0.1212 0.2295 0.0055  0.0139  0.0080  113 TYR   B CZ  
5783 O  OH  . TYR   B 113 ? 0.1512 0.1137 0.2541 0.0089  0.0183  0.0084  113 TYR   B OH  
5793 N  N   . GLU   B 114 ? 0.1202 0.1131 0.1952 -0.0089 0.0105  0.0069  114 GLU   B N   
5794 C  CA  . GLU   B 114 ? 0.1202 0.1080 0.1985 -0.0002 0.0044  0.0086  114 GLU   B CA  
5795 C  C   . GLU   B 114 ? 0.1204 0.1114 0.1944 -0.0021 0.0103  0.0043  114 GLU   B C   
5796 O  O   . GLU   B 114 ? 0.1228 0.1141 0.1973 -0.0004 -0.0003 0.0062  114 GLU   B O   
5797 C  CB  . GLU   B 114 ? 0.1169 0.1157 0.2087 -0.0018 0.0125  0.0053  114 GLU   B CB  
5798 C  CG  . GLU   B 114 ? 0.1231 0.1193 0.2196 -0.0035 0.0078  -0.0014 114 GLU   B CG  
5799 C  CD  . GLU   B 114 ? 0.1245 0.1250 0.2199 -0.0090 0.0088  0.0102  114 GLU   B CD  
5800 O  OE1 . GLU   B 114 ? 0.1244 0.1394 0.2115 -0.0064 0.0120  0.0107  114 GLU   B OE1 
5801 O  OE2 . GLU   B 114 ? 0.1242 0.1459 0.2355 -0.0136 0.0121  0.0114  114 GLU   B OE2 
5808 N  N   . ASN   B 115 ? 0.1201 0.1156 0.1884 -0.0078 -0.0001 0.0060  115 ASN   B N   
5809 C  CA  . ASN   B 115 ? 0.1236 0.1223 0.1724 -0.0100 0.0060  0.0066  115 ASN   B CA  
5810 C  C   . ASN   B 115 ? 0.1217 0.1145 0.1787 -0.0066 -0.0022 0.0029  115 ASN   B C   
5811 O  O   . ASN   B 115 ? 0.1298 0.1189 0.1789 -0.0094 -0.0055 0.0084  115 ASN   B O   
5812 C  CB  . ASN   B 115 ? 0.1365 0.1355 0.1711 -0.0120 0.0048  0.0074  115 ASN   B CB  
5813 C  CG  . ASN   B 115 ? 0.1453 0.1331 0.1717 -0.0008 0.0020  0.0021  115 ASN   B CG  
5814 O  OD1 . ASN   B 115 ? 0.1763 0.1444 0.1921 -0.0049 0.0023  -0.0118 115 ASN   B OD1 
5815 N  ND2 . ASN   B 115 ? 0.1403 0.1419 0.1719 -0.0026 0.0009  0.0061  115 ASN   B ND2 
5822 N  N   . PHE   B 116 ? 0.1276 0.1128 0.1682 -0.0073 0.0005  0.0068  116 PHE   B N   
5823 C  CA  . PHE   B 116 ? 0.1238 0.1155 0.1720 -0.0088 -0.0045 0.0007  116 PHE   B CA  
5824 C  C   . PHE   B 116 ? 0.1305 0.1069 0.1753 -0.0101 -0.0116 0.0042  116 PHE   B C   
5825 O  O   . PHE   B 116 ? 0.1373 0.1140 0.1774 -0.0057 -0.0131 0.0080  116 PHE   B O   
5826 C  CB  . PHE   B 116 ? 0.1248 0.1143 0.1673 -0.0022 -0.0056 0.0032  116 PHE   B CB  
5827 C  CG  . PHE   B 116 ? 0.1172 0.1132 0.1707 -0.0087 -0.0093 0.0066  116 PHE   B CG  
5828 C  CD1 . PHE   B 116 ? 0.1273 0.1207 0.1875 0.0003  -0.0020 0.0026  116 PHE   B CD1 
5829 C  CD2 . PHE   B 116 ? 0.1266 0.1240 0.1682 -0.0043 -0.0050 0.0081  116 PHE   B CD2 
5830 C  CE1 . PHE   B 116 ? 0.1334 0.1246 0.1836 -0.0049 -0.0126 0.0115  116 PHE   B CE1 
5831 C  CE2 . PHE   B 116 ? 0.1255 0.1196 0.1729 -0.0003 -0.0018 0.0002  116 PHE   B CE2 
5832 C  CZ  . PHE   B 116 ? 0.1195 0.1257 0.1724 -0.0078 -0.0060 0.0089  116 PHE   B CZ  
5842 N  N   . ASN   B 117 ? 0.1285 0.1126 0.1844 -0.0075 -0.0152 0.0045  117 ASN   B N   
5843 C  CA  . ASN   B 117 ? 0.1350 0.1126 0.1823 -0.0019 -0.0125 0.0038  117 ASN   B CA  
5844 C  C   . ASN   B 117 ? 0.1386 0.1151 0.1902 -0.0025 -0.0191 0.0111  117 ASN   B C   
5845 O  O   . ASN   B 117 ? 0.1488 0.1260 0.2147 -0.0057 -0.0431 0.0198  117 ASN   B O   
5846 C  CB  . ASN   B 117 ? 0.1338 0.1131 0.1960 0.0041  -0.0129 0.0000  117 ASN   B CB  
5847 C  CG  . ASN   B 117 ? 0.1310 0.1171 0.2109 0.0011  -0.0058 -0.0010 117 ASN   B CG  
5848 O  OD1 . ASN   B 117 ? 0.1471 0.1220 0.2153 -0.0096 -0.0028 -0.0062 117 ASN   B OD1 
5849 N  ND2 . ASN   B 117 ? 0.1322 0.1233 0.2038 -0.0067 -0.0037 0.0023  117 ASN   B ND2 
5856 N  N   . GLN   B 118 ? 0.1412 0.1093 0.1749 -0.0063 -0.0184 0.0031  118 GLN   B N   
5857 C  CA  . GLN   B 118 ? 0.1423 0.1135 0.1942 0.0043  -0.0210 -0.0019 118 GLN   B CA  
5858 C  C   . GLN   B 118 ? 0.1447 0.1088 0.2069 0.0010  -0.0165 -0.0011 118 GLN   B C   
5859 O  O   . GLN   B 118 ? 0.1618 0.1145 0.2394 -0.0049 -0.0079 0.0077  118 GLN   B O   
5860 C  CB  . GLN   B 118 ? 0.1471 0.1175 0.2018 0.0033  -0.0268 0.0039  118 GLN   B CB  
5861 C  CG  . GLN   B 118 ? 0.1528 0.1263 0.2007 0.0107  -0.0152 -0.0075 118 GLN   B CG  
5862 C  CD  . GLN   B 118 ? 0.1587 0.1213 0.2129 0.0084  -0.0081 -0.0083 118 GLN   B CD  
5863 O  OE1 . GLN   B 118 ? 0.1605 0.1197 0.2314 0.0072  -0.0067 0.0040  118 GLN   B OE1 
5864 N  NE2 . GLN   B 118 ? 0.1640 0.1213 0.2175 0.0079  -0.0132 0.0077  118 GLN   B NE2 
5873 N  N   . HIS   B 119 ? 0.1459 0.1151 0.1851 -0.0138 -0.0152 0.0170  119 HIS   B N   
5874 C  CA  . HIS   B 119 ? 0.1552 0.1236 0.1679 -0.0116 -0.0261 0.0161  119 HIS   B CA  
5875 C  C   . HIS   B 119 ? 0.1584 0.1295 0.1702 -0.0081 -0.0358 0.0193  119 HIS   B C   
5876 O  O   . HIS   B 119 ? 0.1599 0.1357 0.1788 -0.0280 -0.0258 0.0137  119 HIS   B O   
5877 C  CB  . HIS   B 119 ? 0.1592 0.1422 0.1602 -0.0022 -0.0259 0.0040  119 HIS   B CB  
5878 C  CG  . HIS   B 119 ? 0.1646 0.1636 0.1849 0.0098  -0.0468 -0.0121 119 HIS   B CG  
5879 N  ND1 . HIS   B 119 ? 0.1749 0.1818 0.2212 0.0036  -0.0548 -0.0302 119 HIS   B ND1 
5880 C  CD2 . HIS   B 119 ? 0.1835 0.1850 0.1902 0.0356  -0.0559 -0.0144 119 HIS   B CD2 
5881 C  CE1 . HIS   B 119 ? 0.1908 0.1999 0.2191 0.0219  -0.0650 -0.0356 119 HIS   B CE1 
5882 N  NE2 . HIS   B 119 ? 0.2009 0.2103 0.2066 0.0338  -0.0548 -0.0324 119 HIS   B NE2 
5890 N  N   . GLU   B 120 ? 0.1809 0.1312 0.1740 -0.0146 -0.0450 0.0242  120 GLU   B N   
5891 C  CA  . GLU   B 120 ? 0.2126 0.1438 0.1919 -0.0092 -0.0619 0.0363  120 GLU   B CA  
5892 C  C   . GLU   B 120 ? 0.1884 0.1342 0.1673 -0.0197 -0.0505 0.0302  120 GLU   B C   
5893 O  O   . GLU   B 120 ? 0.1752 0.1463 0.1771 -0.0204 -0.0463 0.0169  120 GLU   B O   
5894 C  CB  . GLU   B 120 ? 0.2800 0.1895 0.2710 0.0065  -0.0841 0.0655  120 GLU   B CB  
5895 C  CG  . GLU   B 120 ? 0.3357 0.2661 0.3733 0.0184  -0.1007 0.0913  120 GLU   B CG  
5896 C  CD  . GLU   B 120 ? 0.3737 0.3346 0.4728 0.0212  -0.1062 0.1121  120 GLU   B CD  
5897 O  OE1 . GLU   B 120 ? 0.3911 0.3748 0.5057 0.0168  -0.0995 0.1256  120 GLU   B OE1 
5898 O  OE2 . GLU   B 120 ? 0.3971 0.3664 0.5246 0.0214  -0.1088 0.1064  120 GLU   B OE2 
5905 N  N   . VAL   B 121 ? 0.1763 0.1360 0.1602 -0.0235 -0.0368 0.0264  121 VAL   B N   
5906 C  CA  . VAL   B 121 ? 0.1721 0.1479 0.1475 -0.0215 -0.0350 0.0174  121 VAL   B CA  
5907 C  C   . VAL   B 121 ? 0.1608 0.1386 0.1509 -0.0277 -0.0266 0.0198  121 VAL   B C   
5908 O  O   . VAL   B 121 ? 0.1778 0.1379 0.1645 -0.0320 -0.0351 0.0169  121 VAL   B O   
5909 C  CB  . VAL   B 121 ? 0.1955 0.1839 0.1644 -0.0192 -0.0360 0.0193  121 VAL   B CB  
5910 C  CG1 . VAL   B 121 ? 0.1962 0.1952 0.2028 -0.0369 -0.0260 0.0189  121 VAL   B CG1 
5911 C  CG2 . VAL   B 121 ? 0.2229 0.2082 0.1755 -0.0038 -0.0269 0.0068  121 VAL   B CG2 
5921 N  N   . LEU   B 122 ? 0.1553 0.1312 0.1457 -0.0180 -0.0259 0.0143  122 LEU   B N   
5922 C  CA  . LEU   B 122 ? 0.1453 0.1399 0.1296 -0.0224 -0.0252 0.0149  122 LEU   B CA  
5923 C  C   . LEU   B 122 ? 0.1458 0.1280 0.1406 -0.0292 -0.0268 0.0180  122 LEU   B C   
5924 O  O   . LEU   B 122 ? 0.1583 0.1290 0.1704 -0.0363 -0.0356 0.0053  122 LEU   B O   
5925 C  CB  . LEU   B 122 ? 0.1620 0.1489 0.1663 -0.0072 -0.0237 0.0194  122 LEU   B CB  
5926 C  CG  . LEU   B 122 ? 0.1544 0.1577 0.1690 -0.0121 -0.0128 0.0176  122 LEU   B CG  
5927 C  CD1 . LEU   B 122 ? 0.1622 0.1775 0.1692 -0.0195 -0.0164 0.0100  122 LEU   B CD1 
5928 C  CD2 . LEU   B 122 ? 0.1535 0.1674 0.1476 -0.0078 -0.0124 0.0176  122 LEU   B CD2 
5940 N  N   . LEU   B 123 ? 0.1420 0.1264 0.1300 -0.0247 -0.0195 0.0159  123 LEU   B N   
5941 C  CA  . LEU   B 123 ? 0.1467 0.1233 0.1340 -0.0232 -0.0219 0.0083  123 LEU   B CA  
5942 C  C   . LEU   B 123 ? 0.1410 0.1164 0.1374 -0.0268 -0.0183 0.0075  123 LEU   B C   
5943 O  O   . LEU   B 123 ? 0.1547 0.1231 0.1327 -0.0335 -0.0174 0.0081  123 LEU   B O   
5944 C  CB  . LEU   B 123 ? 0.1494 0.1256 0.1503 -0.0269 -0.0140 -0.0008 123 LEU   B CB  
5945 C  CG  . LEU   B 123 ? 0.1527 0.1302 0.1566 -0.0161 -0.0047 0.0092  123 LEU   B CG  
5946 C  CD1 . LEU   B 123 ? 0.1649 0.1306 0.1677 -0.0208 -0.0011 -0.0094 123 LEU   B CD1 
5947 C  CD2 . LEU   B 123 ? 0.1614 0.1409 0.1690 -0.0202 0.0026  0.0209  123 LEU   B CD2 
5959 N  N   . ALA   B 124 ? 0.1368 0.1214 0.1317 -0.0171 -0.0116 0.0026  124 ALA   B N   
5960 C  CA  . ALA   B 124 ? 0.1268 0.1222 0.1446 -0.0125 -0.0093 0.0005  124 ALA   B CA  
5961 C  C   . ALA   B 124 ? 0.1275 0.1186 0.1497 -0.0190 -0.0088 0.0092  124 ALA   B C   
5962 O  O   . ALA   B 124 ? 0.1421 0.1179 0.1480 -0.0140 -0.0102 0.0012  124 ALA   B O   
5963 C  CB  . ALA   B 124 ? 0.1429 0.1209 0.1576 -0.0126 0.0010  -0.0002 124 ALA   B CB  
5969 N  N   . PRO   B 125 ? 0.1386 0.1244 0.1391 -0.0141 -0.0165 0.0156  125 PRO   B N   
5970 C  CA  . PRO   B 125 ? 0.1448 0.1190 0.1614 -0.0149 -0.0184 0.0217  125 PRO   B CA  
5971 C  C   . PRO   B 125 ? 0.1397 0.1155 0.1744 -0.0133 -0.0101 0.0104  125 PRO   B C   
5972 O  O   . PRO   B 125 ? 0.1403 0.1157 0.1852 -0.0076 0.0013  0.0185  125 PRO   B O   
5973 C  CB  . PRO   B 125 ? 0.1458 0.1405 0.1822 -0.0165 -0.0194 0.0289  125 PRO   B CB  
5974 C  CG  . PRO   B 125 ? 0.1516 0.1511 0.1530 -0.0258 -0.0214 0.0172  125 PRO   B CG  
5975 C  CD  . PRO   B 125 ? 0.1550 0.1355 0.1279 -0.0289 -0.0119 0.0064  125 PRO   B CD  
5983 N  N   . LEU   B 126 ? 0.1471 0.1162 0.1888 -0.0085 0.0087  0.0168  126 LEU   B N   
5984 C  CA  . LEU   B 126 ? 0.1522 0.1277 0.1933 -0.0139 0.0186  0.0171  126 LEU   B CA  
5985 C  C   . LEU   B 126 ? 0.1476 0.1386 0.1932 -0.0001 0.0117  0.0243  126 LEU   B C   
5986 O  O   . LEU   B 126 ? 0.1743 0.1729 0.2257 0.0228  -0.0040 -0.0020 126 LEU   B O   
5987 C  CB  . LEU   B 126 ? 0.1685 0.1308 0.2155 -0.0186 0.0248  0.0149  126 LEU   B CB  
5988 C  CG  . LEU   B 126 ? 0.1893 0.1458 0.2374 -0.0267 0.0248  -0.0041 126 LEU   B CG  
5989 C  CD1 . LEU   B 126 ? 0.2024 0.1462 0.2798 -0.0198 0.0212  -0.0090 126 LEU   B CD1 
5990 C  CD2 . LEU   B 126 ? 0.1855 0.1573 0.2307 -0.0377 0.0184  -0.0015 126 LEU   B CD2 
6002 N  N   . LEU   B 127 ? 0.1460 0.1235 0.2095 0.0011  0.0225  0.0128  127 LEU   B N   
6003 C  CA  . LEU   B 127 ? 0.1521 0.1327 0.2214 -0.0020 0.0243  0.0200  127 LEU   B CA  
6004 C  C   . LEU   B 127 ? 0.1482 0.1255 0.2199 -0.0014 0.0247  0.0218  127 LEU   B C   
6005 O  O   . LEU   B 127 ? 0.1505 0.1324 0.2205 -0.0143 0.0246  0.0236  127 LEU   B O   
6006 C  CB  . LEU   B 127 ? 0.1636 0.1280 0.2163 -0.0022 0.0275  0.0221  127 LEU   B CB  
6007 C  CG  . LEU   B 127 ? 0.1703 0.1321 0.2262 -0.0025 0.0293  0.0105  127 LEU   B CG  
6008 C  CD1 . LEU   B 127 ? 0.1767 0.1334 0.2284 0.0021  0.0162  0.0064  127 LEU   B CD1 
6009 C  CD2 . LEU   B 127 ? 0.1779 0.1420 0.2368 -0.0061 0.0258  0.0211  127 LEU   B CD2 
6021 N  N   . SER   B 128 ? 0.1543 0.1218 0.2183 0.0028  0.0095  0.0181  128 SER   B N   
6022 C  CA  . SER   B 128 ? 0.1659 0.1302 0.2267 0.0073  -0.0036 0.0267  128 SER   B CA  
6023 C  C   . SER   B 128 ? 0.1757 0.1368 0.2480 0.0059  -0.0269 0.0234  128 SER   B C   
6024 O  O   . SER   B 128 ? 0.1913 0.1386 0.2889 0.0043  -0.0234 0.0366  128 SER   B O   
6025 C  CB  . SER   B 128 ? 0.1705 0.1360 0.2114 0.0053  0.0038  0.0362  128 SER   B CB  
6026 O  OG  . SER   B 128 ? 0.1776 0.1589 0.2070 0.0090  0.0079  0.0443  128 SER   B OG  
6032 N  N   . ALA   B 129 ? 0.1900 0.1458 0.2654 0.0280  -0.0205 0.0093  129 ALA   B N   
6033 C  CA  . ALA   B 129 ? 0.2086 0.1569 0.2733 0.0356  -0.0173 -0.0084 129 ALA   B CA  
6034 C  C   . ALA   B 129 ? 0.1923 0.1482 0.2552 0.0248  0.0078  -0.0021 129 ALA   B C   
6035 O  O   . ALA   B 129 ? 0.1815 0.1540 0.2476 0.0194  -0.0026 0.0033  129 ALA   B O   
6036 C  CB  . ALA   B 129 ? 0.2332 0.1794 0.3048 0.0364  -0.0064 -0.0177 129 ALA   B CB  
6042 N  N   . GLY   B 130 ? 0.1892 0.1469 0.2626 0.0325  0.0184  -0.0051 130 GLY   B N   
6043 C  CA  . GLY   B 130 ? 0.1899 0.1526 0.2681 0.0293  0.0322  -0.0039 130 GLY   B CA  
6044 C  C   . GLY   B 130 ? 0.1903 0.1583 0.2586 0.0256  0.0250  0.0059  130 GLY   B C   
6045 O  O   . GLY   B 130 ? 0.2024 0.1750 0.2687 0.0185  0.0122  0.0093  130 GLY   B O   
6049 N  N   . ILE   B 131 ? 0.1899 0.1726 0.2626 0.0340  0.0233  0.0054  131 ILE   B N   
6050 C  CA  . ILE   B 131 ? 0.2086 0.1898 0.2670 0.0287  0.0109  0.0264  131 ILE   B CA  
6051 C  C   . ILE   B 131 ? 0.2236 0.1793 0.2338 0.0198  0.0127  0.0288  131 ILE   B C   
6052 O  O   . ILE   B 131 ? 0.2488 0.1953 0.2416 0.0184  -0.0020 0.0299  131 ILE   B O   
6053 C  CB  . ILE   B 131 ? 0.2085 0.2202 0.3021 0.0259  -0.0014 0.0254  131 ILE   B CB  
6054 C  CG1 . ILE   B 131 ? 0.2167 0.2359 0.3178 -0.0009 -0.0026 0.0281  131 ILE   B CG1 
6055 C  CG2 . ILE   B 131 ? 0.2023 0.2368 0.3229 0.0368  0.0015  0.0114  131 ILE   B CG2 
6056 C  CD1 . ILE   B 131 ? 0.2243 0.2558 0.3334 -0.0235 -0.0047 0.0265  131 ILE   B CD1 
6068 N  N   . PHE   B 132 ? 0.2130 0.1660 0.2104 0.0189  0.0292  0.0232  132 PHE   B N   
6069 C  CA  . PHE   B 132 ? 0.2218 0.1681 0.2197 0.0046  0.0481  0.0176  132 PHE   B CA  
6070 C  C   . PHE   B 132 ? 0.2395 0.1804 0.2462 0.0083  0.0580  0.0180  132 PHE   B C   
6071 O  O   . PHE   B 132 ? 0.2552 0.2049 0.2680 0.0025  0.0660  0.0151  132 PHE   B O   
6072 C  CB  . PHE   B 132 ? 0.2090 0.1660 0.1966 0.0041  0.0417  0.0171  132 PHE   B CB  
6073 C  CG  . PHE   B 132 ? 0.1985 0.1606 0.1911 0.0128  0.0285  0.0221  132 PHE   B CG  
6074 C  CD1 . PHE   B 132 ? 0.2104 0.1650 0.2283 0.0069  0.0275  0.0160  132 PHE   B CD1 
6075 C  CD2 . PHE   B 132 ? 0.1981 0.1677 0.1709 0.0240  0.0270  0.0279  132 PHE   B CD2 
6076 C  CE1 . PHE   B 132 ? 0.2154 0.1667 0.2352 0.0066  0.0184  0.0196  132 PHE   B CE1 
6077 C  CE2 . PHE   B 132 ? 0.2071 0.1695 0.1773 0.0124  0.0245  0.0231  132 PHE   B CE2 
6078 C  CZ  . PHE   B 132 ? 0.2130 0.1670 0.2097 0.0082  0.0087  0.0373  132 PHE   B CZ  
6088 N  N   . GLY   B 133 ? 0.2353 0.1626 0.2477 0.0009  0.0461  0.0308  133 GLY   B N   
6089 C  CA  . GLY   B 133 ? 0.2453 0.1731 0.2637 -0.0194 0.0382  0.0404  133 GLY   B CA  
6090 C  C   . GLY   B 133 ? 0.2511 0.1840 0.2708 -0.0348 0.0449  0.0486  133 GLY   B C   
6091 O  O   . GLY   B 133 ? 0.2707 0.2051 0.3046 -0.0460 0.0409  0.0584  133 GLY   B O   
6095 N  N   . ALA   B 134 ? 0.2358 0.1829 0.2589 -0.0321 0.0453  0.0308  134 ALA   B N   
6096 C  CA  . ALA   B 134 ? 0.2326 0.1795 0.2617 -0.0246 0.0478  0.0079  134 ALA   B CA  
6097 C  C   . ALA   B 134 ? 0.2413 0.1661 0.2601 -0.0217 0.0398  0.0195  134 ALA   B C   
6098 O  O   . ALA   B 134 ? 0.2451 0.1927 0.2647 -0.0117 0.0320  0.0177  134 ALA   B O   
6099 C  CB  . ALA   B 134 ? 0.2272 0.1840 0.2771 -0.0225 0.0337  -0.0002 134 ALA   B CB  
6105 N  N   . ASP   B 135 ? 0.2549 0.1635 0.2681 -0.0259 0.0192  0.0215  135 ASP   B N   
6106 C  CA  . ASP   B 135 ? 0.2733 0.1560 0.2850 -0.0193 0.0056  0.0339  135 ASP   B CA  
6107 C  C   . ASP   B 135 ? 0.2527 0.1456 0.2603 -0.0079 0.0053  0.0450  135 ASP   B C   
6108 O  O   . ASP   B 135 ? 0.2404 0.1439 0.2676 -0.0148 0.0070  0.0401  135 ASP   B O   
6109 C  CB  . ASP   B 135 ? 0.3008 0.1643 0.3183 -0.0378 -0.0009 0.0345  135 ASP   B CB  
6110 C  CG  . ASP   B 135 ? 0.3200 0.1689 0.3593 -0.0551 -0.0014 0.0331  135 ASP   B CG  
6111 O  OD1 . ASP   B 135 ? 0.3302 0.1637 0.3560 -0.0398 -0.0135 0.0286  135 ASP   B OD1 
6112 O  OD2 . ASP   B 135 ? 0.3371 0.2047 0.4163 -0.0651 0.0030  0.0163  135 ASP   B OD2 
6117 N  N   . PRO   B 136 ? 0.2412 0.1527 0.2637 0.0133  -0.0068 0.0303  136 PRO   B N   
6118 C  CA  . PRO   B 136 ? 0.2134 0.1456 0.2694 0.0182  -0.0067 0.0195  136 PRO   B CA  
6119 C  C   . PRO   B 136 ? 0.1854 0.1331 0.2744 0.0122  -0.0020 0.0174  136 PRO   B C   
6120 O  O   . PRO   B 136 ? 0.1712 0.1273 0.2623 0.0123  -0.0014 0.0155  136 PRO   B O   
6121 C  CB  . PRO   B 136 ? 0.2197 0.1682 0.2806 0.0308  -0.0070 0.0044  136 PRO   B CB  
6122 C  CG  . PRO   B 136 ? 0.2391 0.1729 0.2911 0.0298  -0.0020 0.0057  136 PRO   B CG  
6123 C  CD  . PRO   B 136 ? 0.2467 0.1648 0.2808 0.0344  -0.0015 0.0173  136 PRO   B CD  
6131 N  N   . ILE   B 137 ? 0.2001 0.1243 0.2864 0.0089  -0.0053 0.0147  137 ILE   B N   
6132 C  CA  . ILE   B 137 ? 0.2064 0.1231 0.3100 -0.0068 0.0007  0.0043  137 ILE   B CA  
6133 C  C   . ILE   B 137 ? 0.1959 0.1284 0.3008 -0.0095 0.0085  0.0134  137 ILE   B C   
6134 O  O   . ILE   B 137 ? 0.1862 0.1249 0.2984 -0.0138 0.0069  0.0125  137 ILE   B O   
6135 C  CB  . ILE   B 137 ? 0.2372 0.1297 0.3566 -0.0026 -0.0001 0.0024  137 ILE   B CB  
6136 C  CG1 . ILE   B 137 ? 0.2601 0.1480 0.3974 0.0053  0.0007  -0.0144 137 ILE   B CG1 
6137 C  CG2 . ILE   B 137 ? 0.2437 0.1302 0.3679 -0.0324 0.0033  0.0098  137 ILE   B CG2 
6138 C  CD1 . ILE   B 137 ? 0.2803 0.1742 0.4258 0.0149  -0.0032 -0.0117 137 ILE   B CD1 
6150 N  N   . HIS   B 138 ? 0.2013 0.1273 0.2925 -0.0098 0.0167  0.0193  138 HIS   B N   
6151 C  CA  . HIS   B 138 ? 0.2146 0.1364 0.2844 -0.0033 0.0325  0.0286  138 HIS   B CA  
6152 C  C   . HIS   B 138 ? 0.1923 0.1295 0.2741 -0.0075 0.0372  0.0362  138 HIS   B C   
6153 O  O   . HIS   B 138 ? 0.1828 0.1399 0.2844 0.0005  0.0398  0.0389  138 HIS   B O   
6154 C  CB  . HIS   B 138 ? 0.2449 0.1453 0.2915 -0.0084 0.0581  0.0273  138 HIS   B CB  
6155 C  CG  . HIS   B 138 ? 0.2679 0.1629 0.3003 -0.0114 0.0776  0.0342  138 HIS   B CG  
6156 N  ND1 . HIS   B 138 ? 0.2783 0.1814 0.3257 -0.0077 0.0804  0.0305  138 HIS   B ND1 
6157 C  CD2 . HIS   B 138 ? 0.2826 0.1695 0.2947 -0.0138 0.0845  0.0304  138 HIS   B CD2 
6158 C  CE1 . HIS   B 138 ? 0.2838 0.1824 0.3231 -0.0026 0.0850  0.0327  138 HIS   B CE1 
6159 N  NE2 . HIS   B 138 ? 0.2925 0.1752 0.3046 -0.0014 0.0891  0.0263  138 HIS   B NE2 
6167 N  N   . SER   B 139 ? 0.1834 0.1210 0.2753 -0.0002 0.0277  0.0210  139 SER   B N   
6168 C  CA  . SER   B 139 ? 0.1789 0.1173 0.2523 -0.0007 0.0194  0.0087  139 SER   B CA  
6169 C  C   . SER   B 139 ? 0.1473 0.1146 0.2510 -0.0065 0.0162  0.0062  139 SER   B C   
6170 O  O   . SER   B 139 ? 0.1496 0.1197 0.2532 -0.0028 0.0121  0.0096  139 SER   B O   
6171 C  CB  . SER   B 139 ? 0.1879 0.1137 0.2474 -0.0030 0.0177  0.0056  139 SER   B CB  
6172 O  OG  . SER   B 139 ? 0.1852 0.1194 0.2590 0.0006  -0.0065 0.0135  139 SER   B OG  
6178 N  N   . LEU   B 140 ? 0.1524 0.1124 0.2537 -0.0077 0.0160  0.0014  140 LEU   B N   
6179 C  CA  . LEU   B 140 ? 0.1510 0.1153 0.2509 -0.0023 0.0151  0.0034  140 LEU   B CA  
6180 C  C   . LEU   B 140 ? 0.1454 0.1189 0.2638 -0.0102 0.0062  0.0002  140 LEU   B C   
6181 O  O   . LEU   B 140 ? 0.1417 0.1252 0.2550 -0.0045 0.0014  0.0047  140 LEU   B O   
6182 C  CB  . LEU   B 140 ? 0.1472 0.1195 0.2501 -0.0092 0.0213  -0.0004 140 LEU   B CB  
6183 C  CG  . LEU   B 140 ? 0.1617 0.1204 0.2542 -0.0081 0.0088  0.0141  140 LEU   B CG  
6184 C  CD1 . LEU   B 140 ? 0.1691 0.1305 0.2670 -0.0154 0.0179  -0.0008 140 LEU   B CD1 
6185 C  CD2 . LEU   B 140 ? 0.1768 0.1309 0.2647 -0.0024 0.0020  -0.0005 140 LEU   B CD2 
6197 N  N   . ARG   B 141 ? 0.1440 0.1178 0.2764 -0.0128 0.0096  -0.0104 141 ARG   B N   
6198 C  CA  . ARG   B 141 ? 0.1432 0.1171 0.3109 -0.0148 0.0235  -0.0036 141 ARG   B CA  
6199 C  C   . ARG   B 141 ? 0.1367 0.1176 0.2963 -0.0124 0.0096  0.0021  141 ARG   B C   
6200 O  O   . ARG   B 141 ? 0.1424 0.1209 0.2973 -0.0101 -0.0048 -0.0126 141 ARG   B O   
6201 C  CB  . ARG   B 141 ? 0.1655 0.1297 0.3383 -0.0245 0.0303  -0.0077 141 ARG   B CB  
6202 C  CG  . ARG   B 141 ? 0.1977 0.1588 0.3595 -0.0341 0.0370  -0.0030 141 ARG   B CG  
6203 C  CD  . ARG   B 141 ? 0.2472 0.1842 0.3541 -0.0317 0.0322  -0.0121 141 ARG   B CD  
6204 N  NE  . ARG   B 141 ? 0.2713 0.1821 0.3411 -0.0463 0.0424  -0.0192 141 ARG   B NE  
6205 C  CZ  . ARG   B 141 ? 0.2932 0.1605 0.3264 -0.0429 0.0473  -0.0349 141 ARG   B CZ  
6206 N  NH1 . ARG   B 141 ? 0.3064 0.1528 0.3190 -0.0367 0.0500  -0.0361 141 ARG   B NH1 
6207 N  NH2 . ARG   B 141 ? 0.3028 0.1791 0.3353 -0.0270 0.0337  -0.0218 141 ARG   B NH2 
6221 N  N   . VAL   B 142 ? 0.1431 0.1175 0.2812 -0.0136 0.0162  -0.0027 142 VAL   B N   
6222 C  CA  . VAL   B 142 ? 0.1389 0.1169 0.2718 -0.0078 0.0204  -0.0064 142 VAL   B CA  
6223 C  C   . VAL   B 142 ? 0.1389 0.1151 0.2681 -0.0059 0.0102  -0.0024 142 VAL   B C   
6224 O  O   . VAL   B 142 ? 0.1445 0.1156 0.2749 -0.0027 0.0162  -0.0001 142 VAL   B O   
6225 C  CB  . VAL   B 142 ? 0.1507 0.1276 0.2704 -0.0002 0.0274  0.0070  142 VAL   B CB  
6226 C  CG1 . VAL   B 142 ? 0.1553 0.1254 0.2726 -0.0011 0.0282  0.0006  142 VAL   B CG1 
6227 C  CG2 . VAL   B 142 ? 0.1761 0.1313 0.2717 -0.0031 0.0237  0.0083  142 VAL   B CG2 
6237 N  N   . CYS   B 143 ? 0.1388 0.1169 0.2482 -0.0008 0.0085  0.0053  143 CYS   B N   
6238 C  CA  . CYS   B 143 ? 0.1375 0.1151 0.2485 -0.0104 0.0068  0.0071  143 CYS   B CA  
6239 C  C   . CYS   B 143 ? 0.1309 0.1182 0.2623 -0.0113 0.0024  0.0028  143 CYS   B C   
6240 O  O   . CYS   B 143 ? 0.1323 0.1220 0.2609 -0.0051 -0.0078 0.0022  143 CYS   B O   
6241 C  CB  . CYS   B 143 ? 0.1415 0.1179 0.2421 -0.0144 0.0014  0.0057  143 CYS   B CB  
6242 S  SG  . CYS   B 143 ? 0.1418 0.1415 0.2298 -0.0063 0.0037  0.0066  143 CYS   B SG  
6248 N  N   . VAL   B 144 ? 0.1314 0.1216 0.2800 -0.0061 -0.0076 -0.0042 144 VAL   B N   
6249 C  CA  . VAL   B 144 ? 0.1381 0.1315 0.2949 -0.0099 -0.0161 -0.0206 144 VAL   B CA  
6250 C  C   . VAL   B 144 ? 0.1405 0.1344 0.2997 -0.0051 -0.0075 0.0026  144 VAL   B C   
6251 O  O   . VAL   B 144 ? 0.1494 0.1585 0.3167 -0.0007 -0.0095 0.0207  144 VAL   B O   
6252 C  CB  . VAL   B 144 ? 0.1650 0.1394 0.3480 -0.0111 -0.0208 -0.0359 144 VAL   B CB  
6253 C  CG1 . VAL   B 144 ? 0.1937 0.1811 0.3662 -0.0018 -0.0335 -0.0312 144 VAL   B CG1 
6254 C  CG2 . VAL   B 144 ? 0.1805 0.1451 0.3454 -0.0046 -0.0407 -0.0459 144 VAL   B CG2 
6264 N  N   . ASP   B 145 ? 0.1391 0.1242 0.3033 -0.0102 -0.0007 -0.0180 145 ASP   B N   
6265 C  CA  . ASP   B 145 ? 0.1414 0.1317 0.3279 -0.0103 0.0090  -0.0055 145 ASP   B CA  
6266 C  C   . ASP   B 145 ? 0.1358 0.1316 0.3168 -0.0092 0.0077  -0.0042 145 ASP   B C   
6267 O  O   . ASP   B 145 ? 0.1337 0.1493 0.3731 -0.0128 0.0242  -0.0222 145 ASP   B O   
6268 C  CB  . ASP   B 145 ? 0.1494 0.1442 0.3777 -0.0178 0.0185  0.0035  145 ASP   B CB  
6269 C  CG  . ASP   B 145 ? 0.1685 0.1444 0.4272 -0.0294 0.0240  0.0014  145 ASP   B CG  
6270 O  OD1 . ASP   B 145 ? 0.1756 0.1419 0.4360 -0.0286 -0.0029 -0.0076 145 ASP   B OD1 
6271 O  OD2 . ASP   B 145 ? 0.1968 0.1615 0.4609 -0.0383 0.0427  0.0157  145 ASP   B OD2 
6276 N  N   . THR   B 146 ? 0.1322 0.1178 0.2740 -0.0094 -0.0050 -0.0011 146 THR   B N   
6277 C  CA  . THR   B 146 ? 0.1342 0.1157 0.2591 -0.0066 0.0091  0.0031  146 THR   B CA  
6278 C  C   . THR   B 146 ? 0.1324 0.1163 0.2360 -0.0061 0.0038  0.0011  146 THR   B C   
6279 O  O   . THR   B 146 ? 0.1430 0.1204 0.2403 -0.0054 -0.0023 0.0003  146 THR   B O   
6280 C  CB  . THR   B 146 ? 0.1388 0.1156 0.2613 -0.0014 0.0153  0.0047  146 THR   B CB  
6281 O  OG1 . THR   B 146 ? 0.1405 0.1220 0.2688 -0.0057 0.0179  0.0096  146 THR   B OG1 
6282 C  CG2 . THR   B 146 ? 0.1489 0.1325 0.2593 0.0031  0.0173  -0.0001 146 THR   B CG2 
6290 N  N   . VAL   B 147 ? 0.1389 0.1225 0.2173 -0.0067 0.0098  0.0058  147 VAL   B N   
6291 C  CA  . VAL   B 147 ? 0.1375 0.1199 0.2208 -0.0105 -0.0080 0.0027  147 VAL   B CA  
6292 C  C   . VAL   B 147 ? 0.1376 0.1175 0.2370 -0.0196 -0.0145 -0.0052 147 VAL   B C   
6293 O  O   . VAL   B 147 ? 0.1518 0.1233 0.2489 -0.0165 -0.0318 -0.0048 147 VAL   B O   
6294 C  CB  . VAL   B 147 ? 0.1337 0.1331 0.1960 -0.0080 -0.0095 -0.0001 147 VAL   B CB  
6295 C  CG1 . VAL   B 147 ? 0.1342 0.1438 0.1833 -0.0105 -0.0104 0.0010  147 VAL   B CG1 
6296 C  CG2 . VAL   B 147 ? 0.1392 0.1334 0.2076 -0.0141 -0.0041 0.0010  147 VAL   B CG2 
6306 N  N   . ARG   B 148 ? 0.1372 0.1302 0.2168 -0.0115 -0.0257 -0.0120 148 ARG   B N   
6307 C  CA  . ARG   B 148 ? 0.1412 0.1348 0.2146 -0.0102 -0.0321 -0.0138 148 ARG   B CA  
6308 C  C   . ARG   B 148 ? 0.1430 0.1407 0.2107 -0.0106 -0.0385 -0.0011 148 ARG   B C   
6309 O  O   . ARG   B 148 ? 0.1621 0.1701 0.2197 -0.0229 -0.0442 0.0101  148 ARG   B O   
6310 C  CB  . ARG   B 148 ? 0.1511 0.1421 0.2225 -0.0016 -0.0330 -0.0230 148 ARG   B CB  
6311 C  CG  . ARG   B 148 ? 0.1466 0.1565 0.2289 -0.0051 -0.0372 -0.0343 148 ARG   B CG  
6312 C  CD  . ARG   B 148 ? 0.1542 0.1755 0.2453 0.0060  -0.0333 -0.0394 148 ARG   B CD  
6313 N  NE  . ARG   B 148 ? 0.1626 0.1740 0.2390 0.0177  -0.0313 -0.0385 148 ARG   B NE  
6314 C  CZ  . ARG   B 148 ? 0.1542 0.1626 0.2267 0.0138  -0.0257 -0.0314 148 ARG   B CZ  
6315 N  NH1 . ARG   B 148 ? 0.1456 0.1657 0.2372 0.0019  -0.0123 -0.0343 148 ARG   B NH1 
6316 N  NH2 . ARG   B 148 ? 0.1709 0.1464 0.2268 0.0220  -0.0224 -0.0175 148 ARG   B NH2 
6330 N  N   . THR   B 149 ? 0.1474 0.1311 0.2106 -0.0105 -0.0368 0.0014  149 THR   B N   
6331 C  CA  . THR   B 149 ? 0.1545 0.1311 0.1986 -0.0138 -0.0291 0.0102  149 THR   B CA  
6332 C  C   . THR   B 149 ? 0.1558 0.1348 0.1856 -0.0203 -0.0374 0.0058  149 THR   B C   
6333 O  O   . THR   B 149 ? 0.1675 0.1322 0.1987 -0.0251 -0.0218 0.0052  149 THR   B O   
6334 C  CB  . THR   B 149 ? 0.1583 0.1340 0.2011 -0.0190 -0.0353 0.0043  149 THR   B CB  
6335 O  OG1 . THR   B 149 ? 0.1564 0.1363 0.1982 -0.0219 -0.0336 0.0088  149 THR   B OG1 
6336 C  CG2 . THR   B 149 ? 0.1737 0.1327 0.2124 -0.0183 -0.0295 0.0072  149 THR   B CG2 
6344 N  N   . ASN   B 150 ? 0.1610 0.1379 0.1705 -0.0197 -0.0418 0.0038  150 ASN   B N   
6345 C  CA  . ASN   B 150 ? 0.1720 0.1517 0.1633 -0.0260 -0.0368 -0.0002 150 ASN   B CA  
6346 C  C   . ASN   B 150 ? 0.1602 0.1446 0.1707 -0.0187 -0.0320 0.0004  150 ASN   B C   
6347 O  O   . ASN   B 150 ? 0.1613 0.1404 0.1920 -0.0242 -0.0438 0.0017  150 ASN   B O   
6348 C  CB  . ASN   B 150 ? 0.1986 0.1856 0.1810 -0.0284 -0.0455 0.0155  150 ASN   B CB  
6349 C  CG  . ASN   B 150 ? 0.2293 0.2243 0.2133 -0.0237 -0.0587 0.0248  150 ASN   B CG  
6350 O  OD1 . ASN   B 150 ? 0.2380 0.2447 0.2277 -0.0293 -0.0761 0.0203  150 ASN   B OD1 
6351 N  ND2 . ASN   B 150 ? 0.2459 0.2448 0.2503 -0.0161 -0.0559 0.0606  150 ASN   B ND2 
6358 N  N   . VAL   B 151 ? 0.1530 0.1407 0.1739 -0.0236 -0.0338 0.0063  151 VAL   B N   
6359 C  CA  . VAL   B 151 ? 0.1522 0.1433 0.1688 -0.0226 -0.0269 -0.0013 151 VAL   B CA  
6360 C  C   . VAL   B 151 ? 0.1585 0.1407 0.1657 -0.0321 -0.0282 0.0034  151 VAL   B C   
6361 O  O   . VAL   B 151 ? 0.1619 0.1464 0.1921 -0.0291 -0.0287 -0.0108 151 VAL   B O   
6362 C  CB  . VAL   B 151 ? 0.1675 0.1483 0.1859 -0.0061 -0.0209 -0.0044 151 VAL   B CB  
6363 C  CG1 . VAL   B 151 ? 0.1795 0.1524 0.2008 -0.0140 -0.0140 -0.0174 151 VAL   B CG1 
6364 C  CG2 . VAL   B 151 ? 0.1762 0.1651 0.1805 0.0051  -0.0202 0.0062  151 VAL   B CG2 
6374 N  N   . TYR   B 152 ? 0.1527 0.1302 0.1563 -0.0322 -0.0243 -0.0036 152 TYR   B N   
6375 C  CA  . TYR   B 152 ? 0.1572 0.1417 0.1560 -0.0333 -0.0215 -0.0097 152 TYR   B CA  
6376 C  C   . TYR   B 152 ? 0.1530 0.1292 0.1414 -0.0268 -0.0146 -0.0037 152 TYR   B C   
6377 O  O   . TYR   B 152 ? 0.1574 0.1317 0.1523 -0.0282 -0.0193 0.0043  152 TYR   B O   
6378 C  CB  . TYR   B 152 ? 0.1686 0.1601 0.1553 -0.0320 -0.0138 -0.0005 152 TYR   B CB  
6379 C  CG  . TYR   B 152 ? 0.1834 0.1736 0.1486 -0.0471 -0.0173 0.0066  152 TYR   B CG  
6380 C  CD1 . TYR   B 152 ? 0.1889 0.1861 0.1532 -0.0455 -0.0280 0.0117  152 TYR   B CD1 
6381 C  CD2 . TYR   B 152 ? 0.2043 0.1954 0.1515 -0.0426 -0.0103 -0.0012 152 TYR   B CD2 
6382 C  CE1 . TYR   B 152 ? 0.2081 0.2079 0.1676 -0.0417 -0.0299 0.0252  152 TYR   B CE1 
6383 C  CE2 . TYR   B 152 ? 0.2137 0.2150 0.1567 -0.0439 -0.0225 -0.0022 152 TYR   B CE2 
6384 C  CZ  . TYR   B 152 ? 0.2188 0.2274 0.1608 -0.0427 -0.0458 0.0178  152 TYR   B CZ  
6385 O  OH  . TYR   B 152 ? 0.2463 0.2637 0.1914 -0.0306 -0.0495 0.0248  152 TYR   B OH  
6395 N  N   . LEU   B 153 ? 0.1604 0.1260 0.1471 -0.0316 -0.0144 -0.0023 153 LEU   B N   
6396 C  CA  . LEU   B 153 ? 0.1598 0.1215 0.1471 -0.0221 -0.0056 -0.0021 153 LEU   B CA  
6397 C  C   . LEU   B 153 ? 0.1610 0.1190 0.1689 -0.0230 -0.0062 -0.0187 153 LEU   B C   
6398 O  O   . LEU   B 153 ? 0.1663 0.1446 0.1792 -0.0213 -0.0127 -0.0332 153 LEU   B O   
6399 C  CB  . LEU   B 153 ? 0.1559 0.1232 0.1643 -0.0294 -0.0075 -0.0070 153 LEU   B CB  
6400 C  CG  . LEU   B 153 ? 0.1497 0.1336 0.1913 -0.0241 -0.0018 -0.0039 153 LEU   B CG  
6401 C  CD1 . LEU   B 153 ? 0.1524 0.1443 0.2046 -0.0330 -0.0049 0.0152  153 LEU   B CD1 
6402 C  CD2 . LEU   B 153 ? 0.1455 0.1409 0.2006 -0.0233 0.0030  0.0063  153 LEU   B CD2 
6414 N  N   . ALA   B 154 ? 0.1537 0.1223 0.1823 -0.0076 -0.0117 -0.0161 154 ALA   B N   
6415 C  CA  . ALA   B 154 ? 0.1579 0.1291 0.1930 -0.0039 -0.0113 -0.0230 154 ALA   B CA  
6416 C  C   . ALA   B 154 ? 0.1720 0.1375 0.1957 -0.0001 -0.0167 -0.0261 154 ALA   B C   
6417 O  O   . ALA   B 154 ? 0.2066 0.1437 0.2069 0.0063  -0.0094 -0.0093 154 ALA   B O   
6418 C  CB  . ALA   B 154 ? 0.1592 0.1525 0.2132 -0.0062 -0.0101 -0.0246 154 ALA   B CB  
6424 N  N   . VAL   B 155 ? 0.1419 0.1285 0.2120 -0.0073 -0.0067 -0.0138 155 VAL   B N   
6425 C  CA  . VAL   B 155 ? 0.1436 0.1325 0.2372 -0.0043 -0.0134 -0.0129 155 VAL   B CA  
6426 C  C   . VAL   B 155 ? 0.1441 0.1379 0.2299 -0.0016 -0.0148 -0.0375 155 VAL   B C   
6427 O  O   . VAL   B 155 ? 0.1656 0.1600 0.2529 0.0105  -0.0102 -0.0482 155 VAL   B O   
6428 C  CB  . VAL   B 155 ? 0.1473 0.1452 0.2678 -0.0055 -0.0213 -0.0024 155 VAL   B CB  
6429 C  CG1 . VAL   B 155 ? 0.1535 0.1363 0.2661 -0.0077 -0.0142 -0.0010 155 VAL   B CG1 
6430 C  CG2 . VAL   B 155 ? 0.1453 0.1591 0.2893 -0.0020 -0.0207 0.0340  155 VAL   B CG2 
6440 N  N   . PHE   B 156 ? 0.1371 0.1405 0.2518 0.0034  -0.0175 -0.0288 156 PHE   B N   
6441 C  CA  . PHE   B 156 ? 0.1424 0.1462 0.2766 0.0060  -0.0070 -0.0268 156 PHE   B CA  
6442 C  C   . PHE   B 156 ? 0.1418 0.1562 0.3095 0.0130  -0.0108 -0.0434 156 PHE   B C   
6443 O  O   . PHE   B 156 ? 0.1668 0.1751 0.3393 0.0252  -0.0040 -0.0475 156 PHE   B O   
6444 C  CB  . PHE   B 156 ? 0.1436 0.1457 0.2628 0.0003  -0.0101 -0.0207 156 PHE   B CB  
6445 C  CG  . PHE   B 156 ? 0.1436 0.1525 0.2757 0.0035  -0.0100 0.0013  156 PHE   B CG  
6446 C  CD1 . PHE   B 156 ? 0.1509 0.1822 0.3098 0.0109  -0.0015 0.0245  156 PHE   B CD1 
6447 C  CD2 . PHE   B 156 ? 0.1541 0.1661 0.2776 0.0099  -0.0137 0.0034  156 PHE   B CD2 
6448 C  CE1 . PHE   B 156 ? 0.1584 0.1973 0.3201 0.0110  -0.0026 0.0275  156 PHE   B CE1 
6449 C  CE2 . PHE   B 156 ? 0.1604 0.1871 0.3067 0.0137  -0.0182 0.0095  156 PHE   B CE2 
6450 C  CZ  . PHE   B 156 ? 0.1506 0.1929 0.3150 0.0149  -0.0217 0.0112  156 PHE   B CZ  
6460 N  N   . ASP   B 157 ? 0.1422 0.1505 0.3360 0.0151  -0.0261 -0.0298 157 ASP   B N   
6461 C  CA  . ASP   B 157 ? 0.1527 0.1569 0.3644 0.0113  -0.0285 -0.0397 157 ASP   B CA  
6462 C  C   . ASP   B 157 ? 0.1560 0.1601 0.3644 0.0030  -0.0203 -0.0587 157 ASP   B C   
6463 O  O   . ASP   B 157 ? 0.1391 0.1538 0.3630 0.0005  -0.0229 -0.0452 157 ASP   B O   
6464 C  CB  . ASP   B 157 ? 0.1788 0.1703 0.3808 0.0062  -0.0506 -0.0226 157 ASP   B CB  
6465 C  CG  . ASP   B 157 ? 0.2164 0.1849 0.4046 0.0026  -0.0415 -0.0189 157 ASP   B CG  
6466 O  OD1 . ASP   B 157 ? 0.2226 0.1791 0.4170 0.0131  -0.0253 -0.0075 157 ASP   B OD1 
6467 O  OD2 . ASP   B 157 ? 0.2540 0.2089 0.4247 0.0019  -0.0265 -0.0192 157 ASP   B OD2 
6472 N  N   A LYS   B 158 ? 0.1619 0.1814 0.3598 0.0053  -0.0137 -0.0767 158 LYS   B N   
6473 N  N   B LYS   B 158 ? 0.1665 0.1887 0.3557 0.0099  -0.0128 -0.0746 158 LYS   B N   
6474 C  CA  A LYS   B 158 ? 0.1689 0.1934 0.3605 0.0056  -0.0079 -0.0913 158 LYS   B CA  
6475 C  CA  B LYS   B 158 ? 0.1793 0.2102 0.3542 0.0156  -0.0058 -0.0868 158 LYS   B CA  
6476 C  C   A LYS   B 158 ? 0.1676 0.1774 0.3661 0.0027  -0.0149 -0.0854 158 LYS   B C   
6477 C  C   B LYS   B 158 ? 0.1809 0.2010 0.3561 0.0160  -0.0132 -0.0808 158 LYS   B C   
6478 O  O   A LYS   B 158 ? 0.1669 0.1679 0.3681 -0.0065 -0.0154 -0.0924 158 LYS   B O   
6479 O  O   B LYS   B 158 ? 0.1845 0.2009 0.3543 0.0095  -0.0148 -0.0827 158 LYS   B O   
6480 C  CB  A LYS   B 158 ? 0.1936 0.2284 0.3612 0.0087  -0.0031 -0.1057 158 LYS   B CB  
6481 C  CB  B LYS   B 158 ? 0.2040 0.2465 0.3558 0.0201  0.0013  -0.1019 158 LYS   B CB  
6482 C  CG  A LYS   B 158 ? 0.2241 0.2638 0.3674 0.0075  -0.0022 -0.1145 158 LYS   B CG  
6483 C  CG  B LYS   B 158 ? 0.2337 0.2811 0.3618 0.0185  0.0053  -0.1105 158 LYS   B CG  
6484 C  CD  A LYS   B 158 ? 0.2452 0.2969 0.3738 0.0071  -0.0030 -0.1121 158 LYS   B CD  
6485 C  CD  B LYS   B 158 ? 0.2562 0.3146 0.3690 0.0153  0.0056  -0.1090 158 LYS   B CD  
6486 C  CE  A LYS   B 158 ? 0.2616 0.3212 0.3801 0.0094  -0.0076 -0.1069 158 LYS   B CE  
6487 C  CE  B LYS   B 158 ? 0.2731 0.3383 0.3758 0.0154  0.0031  -0.1050 158 LYS   B CE  
6488 N  NZ  A LYS   B 158 ? 0.2639 0.3325 0.3801 0.0086  -0.0104 -0.1053 158 LYS   B NZ  
6489 N  NZ  B LYS   B 158 ? 0.2782 0.3506 0.3769 0.0141  0.0030  -0.1027 158 LYS   B NZ  
6516 N  N   A ASN   B 159 ? 0.1735 0.1692 0.3818 0.0057  -0.0273 -0.0696 159 ASN   B N   
6517 N  N   B ASN   B 159 ? 0.1839 0.1916 0.3705 0.0182  -0.0250 -0.0688 159 ASN   B N   
6518 C  CA  A ASN   B 159 ? 0.1887 0.1595 0.3907 0.0177  -0.0423 -0.0565 159 ASN   B CA  
6519 C  CA  B ASN   B 159 ? 0.1926 0.1770 0.3805 0.0275  -0.0381 -0.0612 159 ASN   B CA  
6520 C  C   A ASN   B 159 ? 0.1764 0.1518 0.3782 0.0127  -0.0543 -0.0414 159 ASN   B C   
6521 C  C   B ASN   B 159 ? 0.1790 0.1615 0.3738 0.0196  -0.0470 -0.0492 159 ASN   B C   
6522 O  O   A ASN   B 159 ? 0.1784 0.1477 0.3827 -0.0029 -0.0665 -0.0280 159 ASN   B O   
6523 O  O   B ASN   B 159 ? 0.1794 0.1574 0.3781 0.0123  -0.0523 -0.0383 159 ASN   B O   
6524 C  CB  A ASN   B 159 ? 0.2106 0.1706 0.4138 0.0231  -0.0479 -0.0536 159 ASN   B CB  
6525 C  CB  B ASN   B 159 ? 0.2086 0.1899 0.3982 0.0347  -0.0453 -0.0586 159 ASN   B CB  
6526 C  CG  A ASN   B 159 ? 0.2370 0.1899 0.4331 0.0219  -0.0526 -0.0642 159 ASN   B CG  
6527 C  CG  B ASN   B 159 ? 0.2298 0.2102 0.4130 0.0362  -0.0523 -0.0648 159 ASN   B CG  
6528 O  OD1 A ASN   B 159 ? 0.2528 0.2035 0.4458 0.0266  -0.0492 -0.0673 159 ASN   B OD1 
6529 O  OD1 B ASN   B 159 ? 0.2416 0.2212 0.4209 0.0420  -0.0531 -0.0630 159 ASN   B OD1 
6530 N  ND2 A ASN   B 159 ? 0.2405 0.1994 0.4424 0.0181  -0.0559 -0.0635 159 ASN   B ND2 
6531 N  ND2 B ASN   B 159 ? 0.2319 0.2229 0.4249 0.0349  -0.0539 -0.0614 159 ASN   B ND2 
6544 N  N   . LEU   B 160 ? 0.1661 0.1552 0.3629 0.0103  -0.0509 -0.0416 160 LEU   B N   
6545 C  CA  . LEU   B 160 ? 0.1558 0.1549 0.3371 0.0120  -0.0419 -0.0169 160 LEU   B CA  
6546 C  C   . LEU   B 160 ? 0.1540 0.1487 0.3283 0.0008  -0.0192 -0.0325 160 LEU   B C   
6547 O  O   . LEU   B 160 ? 0.1373 0.1482 0.3302 -0.0011 -0.0278 -0.0133 160 LEU   B O   
6548 C  CB  . LEU   B 160 ? 0.1578 0.1644 0.3256 0.0045  -0.0452 -0.0131 160 LEU   B CB  
6549 C  CG  . LEU   B 160 ? 0.1610 0.1721 0.3139 0.0069  -0.0390 -0.0034 160 LEU   B CG  
6550 C  CD1 . LEU   B 160 ? 0.1791 0.1868 0.3186 -0.0010 -0.0231 -0.0008 160 LEU   B CD1 
6551 C  CD2 . LEU   B 160 ? 0.1635 0.1741 0.3142 0.0153  -0.0376 -0.0117 160 LEU   B CD2 
6564 N  N   A TYR   B 161 ? 0.1604 0.1505 0.3197 -0.0086 0.0019  -0.0432 161 TYR   B N   
6565 N  N   B TYR   B 161 ? 0.1638 0.1520 0.3192 -0.0072 0.0027  -0.0421 161 TYR   B N   
6566 C  CA  A TYR   B 161 ? 0.1634 0.1482 0.3067 -0.0183 0.0155  -0.0500 161 TYR   B CA  
6567 C  CA  B TYR   B 161 ? 0.1701 0.1508 0.3056 -0.0144 0.0172  -0.0472 161 TYR   B CA  
6568 C  C   A TYR   B 161 ? 0.1658 0.1480 0.3104 -0.0172 0.0173  -0.0420 161 TYR   B C   
6569 C  C   B TYR   B 161 ? 0.1693 0.1486 0.3101 -0.0147 0.0187  -0.0393 161 TYR   B C   
6570 O  O   A TYR   B 161 ? 0.1612 0.1495 0.3036 -0.0257 0.0118  -0.0331 161 TYR   B O   
6571 O  O   B TYR   B 161 ? 0.1655 0.1495 0.3044 -0.0219 0.0149  -0.0271 161 TYR   B O   
6572 C  CB  A TYR   B 161 ? 0.1781 0.1554 0.3017 -0.0345 0.0244  -0.0558 161 TYR   B CB  
6573 C  CB  B TYR   B 161 ? 0.1907 0.1610 0.2979 -0.0265 0.0265  -0.0507 161 TYR   B CB  
6574 C  CG  A TYR   B 161 ? 0.2020 0.1567 0.2891 -0.0394 0.0357  -0.0587 161 TYR   B CG  
6575 C  CG  B TYR   B 161 ? 0.2187 0.1658 0.2845 -0.0325 0.0367  -0.0504 161 TYR   B CG  
6576 C  CD1 A TYR   B 161 ? 0.2098 0.1526 0.2842 -0.0461 0.0405  -0.0611 161 TYR   B CD1 
6577 C  CD1 B TYR   B 161 ? 0.2254 0.1647 0.2767 -0.0404 0.0464  -0.0496 161 TYR   B CD1 
6578 C  CD2 A TYR   B 161 ? 0.2211 0.1629 0.2862 -0.0362 0.0332  -0.0551 161 TYR   B CD2 
6579 C  CD2 B TYR   B 161 ? 0.2374 0.1724 0.2792 -0.0295 0.0360  -0.0458 161 TYR   B CD2 
6580 C  CE1 A TYR   B 161 ? 0.2235 0.1680 0.2891 -0.0428 0.0397  -0.0562 161 TYR   B CE1 
6581 C  CE1 B TYR   B 161 ? 0.2384 0.1803 0.2801 -0.0395 0.0469  -0.0438 161 TYR   B CE1 
6582 C  CE2 A TYR   B 161 ? 0.2339 0.1767 0.2886 -0.0379 0.0348  -0.0510 161 TYR   B CE2 
6583 C  CE2 B TYR   B 161 ? 0.2487 0.1850 0.2799 -0.0317 0.0415  -0.0405 161 TYR   B CE2 
6584 C  CZ  A TYR   B 161 ? 0.2359 0.1821 0.2912 -0.0445 0.0361  -0.0446 161 TYR   B CZ  
6585 C  CZ  B TYR   B 161 ? 0.2521 0.1908 0.2791 -0.0385 0.0436  -0.0340 161 TYR   B CZ  
6586 O  OH  A TYR   B 161 ? 0.2561 0.2024 0.3065 -0.0417 0.0320  -0.0416 161 TYR   B OH  
6587 O  OH  B TYR   B 161 ? 0.2704 0.2067 0.2903 -0.0398 0.0435  -0.0328 161 TYR   B OH  
6606 N  N   . ASP   B 162 ? 0.1742 0.1457 0.3243 -0.0116 0.0062  -0.0530 162 ASP   B N   
6607 C  CA  . ASP   B 162 ? 0.1812 0.1587 0.3438 -0.0090 -0.0036 -0.0531 162 ASP   B CA  
6608 C  C   . ASP   B 162 ? 0.1767 0.1509 0.3371 -0.0122 -0.0085 -0.0371 162 ASP   B C   
6609 O  O   . ASP   B 162 ? 0.1767 0.1564 0.3386 -0.0243 -0.0269 -0.0232 162 ASP   B O   
6610 C  CB  . ASP   B 162 ? 0.1989 0.1674 0.3713 -0.0064 -0.0007 -0.0798 162 ASP   B CB  
6611 C  CG  . ASP   B 162 ? 0.2067 0.1868 0.4006 0.0019  -0.0016 -0.0910 162 ASP   B CG  
6612 O  OD1 . ASP   B 162 ? 0.2095 0.2054 0.3942 -0.0050 0.0048  -0.0892 162 ASP   B OD1 
6613 O  OD2 . ASP   B 162 ? 0.2175 0.2128 0.4237 0.0170  0.0017  -0.0878 162 ASP   B OD2 
6619 N  N   . LYS   B 163 ? 0.1746 0.1324 0.3239 -0.0097 -0.0172 -0.0253 163 LYS   B N   
6620 C  CA  . LYS   B 163 ? 0.1797 0.1406 0.3269 -0.0208 -0.0196 -0.0170 163 LYS   B CA  
6621 C  C   . LYS   B 163 ? 0.1526 0.1373 0.3059 -0.0207 -0.0193 -0.0041 163 LYS   B C   
6622 O  O   . LYS   B 163 ? 0.1548 0.1498 0.3232 -0.0270 -0.0230 0.0113  163 LYS   B O   
6623 C  CB  . LYS   B 163 ? 0.2277 0.1756 0.3605 -0.0189 -0.0190 -0.0034 163 LYS   B CB  
6624 C  CG  . LYS   B 163 ? 0.2988 0.2519 0.4192 -0.0198 -0.0053 -0.0045 163 LYS   B CG  
6625 C  CD  . LYS   B 163 ? 0.3667 0.3202 0.4831 -0.0225 0.0030  -0.0040 163 LYS   B CD  
6626 C  CE  . LYS   B 163 ? 0.4108 0.3647 0.5288 -0.0267 0.0071  -0.0032 163 LYS   B CE  
6627 N  NZ  . LYS   B 163 ? 0.4552 0.4081 0.5547 -0.0299 0.0091  -0.0041 163 LYS   B NZ  
6641 N  N   . LEU   B 164 ? 0.1420 0.1335 0.2776 -0.0111 -0.0221 0.0003  164 LEU   B N   
6642 C  CA  . LEU   B 164 ? 0.1429 0.1327 0.2697 -0.0125 -0.0285 0.0063  164 LEU   B CA  
6643 C  C   . LEU   B 164 ? 0.1509 0.1323 0.2785 -0.0190 -0.0341 0.0083  164 LEU   B C   
6644 O  O   . LEU   B 164 ? 0.1521 0.1597 0.2951 -0.0156 -0.0291 0.0145  164 LEU   B O   
6645 C  CB  . LEU   B 164 ? 0.1442 0.1300 0.2623 -0.0105 -0.0154 0.0036  164 LEU   B CB  
6646 C  CG  . LEU   B 164 ? 0.1510 0.1470 0.2681 -0.0131 -0.0092 0.0049  164 LEU   B CG  
6647 C  CD1 . LEU   B 164 ? 0.1641 0.1457 0.2672 -0.0196 -0.0246 -0.0043 164 LEU   B CD1 
6648 C  CD2 . LEU   B 164 ? 0.1648 0.1824 0.2851 -0.0123 0.0067  -0.0091 164 LEU   B CD2 
6660 N  N   . VAL   B 165 ? 0.1856 0.1369 0.2957 -0.0285 -0.0436 -0.0071 165 VAL   B N   
6661 C  CA  . VAL   B 165 ? 0.2299 0.1515 0.3103 -0.0396 -0.0678 -0.0047 165 VAL   B CA  
6662 C  C   . VAL   B 165 ? 0.2604 0.1630 0.3411 -0.0546 -0.0965 0.0071  165 VAL   B C   
6663 O  O   . VAL   B 165 ? 0.2846 0.1848 0.3508 -0.0581 -0.0953 0.0096  165 VAL   B O   
6664 C  CB  . VAL   B 165 ? 0.2520 0.1683 0.3100 -0.0236 -0.0410 -0.0121 165 VAL   B CB  
6665 C  CG1 . VAL   B 165 ? 0.2707 0.1700 0.3342 -0.0220 -0.0340 -0.0165 165 VAL   B CG1 
6666 C  CG2 . VAL   B 165 ? 0.2505 0.1777 0.2994 -0.0212 -0.0243 -0.0101 165 VAL   B CG2 
6676 N  N   . SER   B 166 ? 0.2688 0.1564 0.3860 -0.0514 -0.1052 -0.0083 166 SER   B N   
6677 C  CA  . SER   B 166 ? 0.2576 0.1557 0.4370 -0.0497 -0.0912 -0.0201 166 SER   B CA  
6678 C  C   . SER   B 166 ? 0.2451 0.1692 0.4517 -0.0489 -0.0842 0.0056  166 SER   B C   
6679 O  O   . SER   B 166 ? 0.2481 0.1871 0.4782 -0.0581 -0.0952 -0.0164 166 SER   B O   
6680 C  CB  . SER   B 166 ? 0.2538 0.1628 0.4690 -0.0382 -0.0822 -0.0284 166 SER   B CB  
6681 O  OG  . SER   B 166 ? 0.2410 0.1665 0.4898 -0.0293 -0.0794 -0.0140 166 SER   B OG  
6687 N  N   . SER   B 167 ? 0.2226 0.1577 0.4132 -0.0512 -0.0819 0.0447  167 SER   B N   
6688 C  CA  . SER   B 167 ? 0.2132 0.1641 0.3884 -0.0455 -0.0617 0.0533  167 SER   B CA  
6689 C  C   . SER   B 167 ? 0.2080 0.1777 0.3633 -0.0496 -0.0592 0.0667  167 SER   B C   
6690 O  O   . SER   B 167 ? 0.2062 0.1907 0.3655 -0.0553 -0.0582 0.0605  167 SER   B O   
6691 C  CB  . SER   B 167 ? 0.2022 0.1713 0.3955 -0.0394 -0.0354 0.0496  167 SER   B CB  
6692 O  OG  . SER   B 167 ? 0.1945 0.1818 0.4002 -0.0283 -0.0099 0.0418  167 SER   B OG  
6698 N  N   . PHE   B 168 ? 0.2150 0.1791 0.3478 -0.0488 -0.0431 0.0626  168 PHE   B N   
6699 C  CA  . PHE   B 168 ? 0.2193 0.1801 0.3183 -0.0489 -0.0345 0.0427  168 PHE   B CA  
6700 C  C   . PHE   B 168 ? 0.1977 0.1643 0.2644 -0.0240 -0.0215 0.0127  168 PHE   B C   
6701 O  O   . PHE   B 168 ? 0.2228 0.1532 0.2597 -0.0038 -0.0127 -0.0020 168 PHE   B O   
6702 C  CB  . PHE   B 168 ? 0.2269 0.1857 0.3242 -0.0662 -0.0460 0.0550  168 PHE   B CB  
6703 C  CG  . PHE   B 168 ? 0.2536 0.1710 0.3185 -0.0664 -0.0512 0.0309  168 PHE   B CG  
6704 C  CD1 . PHE   B 168 ? 0.2789 0.1648 0.3317 -0.0644 -0.0552 0.0222  168 PHE   B CD1 
6705 C  CD2 . PHE   B 168 ? 0.2455 0.1604 0.3157 -0.0610 -0.0488 0.0406  168 PHE   B CD2 
6706 C  CE1 . PHE   B 168 ? 0.2903 0.1739 0.3267 -0.0445 -0.0489 0.0319  168 PHE   B CE1 
6707 C  CE2 . PHE   B 168 ? 0.2698 0.1698 0.3185 -0.0403 -0.0530 0.0277  168 PHE   B CE2 
6708 C  CZ  . PHE   B 168 ? 0.2828 0.1587 0.3252 -0.0280 -0.0559 0.0462  168 PHE   B CZ  
6718 N  N   A LEU   B 169 ? 0.2145 0.1801 0.2673 -0.0068 -0.0086 0.0033  169 LEU   B N   
6719 N  N   B LEU   B 169 ? 0.2017 0.1735 0.2654 -0.0039 -0.0083 -0.0023 169 LEU   B N   
6720 C  CA  A LEU   B 169 ? 0.2465 0.2112 0.2959 -0.0017 -0.0036 -0.0193 169 LEU   B CA  
6721 C  CA  B LEU   B 169 ? 0.2245 0.1996 0.2927 0.0035  -0.0053 -0.0293 169 LEU   B CA  
6722 C  C   A LEU   B 169 ? 0.2645 0.2276 0.3350 0.0013  0.0017  -0.0369 169 LEU   B C   
6723 C  C   B LEU   B 169 ? 0.2399 0.2044 0.3299 0.0181  -0.0036 -0.0488 169 LEU   B C   
6724 O  O   A LEU   B 169 ? 0.2770 0.2368 0.3646 -0.0015 -0.0018 -0.0446 169 LEU   B O   
6725 O  O   B LEU   B 169 ? 0.2521 0.2109 0.3557 0.0213  -0.0006 -0.0532 169 LEU   B O   
6726 C  CB  A LEU   B 169 ? 0.2670 0.2375 0.3036 0.0006  -0.0076 -0.0075 169 LEU   B CB  
6727 C  CB  B LEU   B 169 ? 0.2421 0.2323 0.3010 -0.0023 -0.0083 -0.0164 169 LEU   B CB  
6728 C  CG  A LEU   B 169 ? 0.2925 0.2626 0.3224 0.0057  -0.0037 -0.0047 169 LEU   B CG  
6729 C  CG  B LEU   B 169 ? 0.2685 0.2624 0.3213 -0.0003 -0.0034 -0.0113 169 LEU   B CG  
6730 C  CD1 A LEU   B 169 ? 0.2994 0.2724 0.3236 0.0043  -0.0052 0.0018  169 LEU   B CD1 
6731 C  CD1 B LEU   B 169 ? 0.2757 0.2732 0.3238 -0.0017 -0.0042 -0.0023 169 LEU   B CD1 
6732 C  CD2 A LEU   B 169 ? 0.2962 0.2686 0.3224 0.0112  0.0048  -0.0102 169 LEU   B CD2 
6733 C  CD2 B LEU   B 169 ? 0.2703 0.2695 0.3189 0.0061  0.0076  -0.0185 169 LEU   B CD2 
6734 O  OXT A LEU   B 169 ? 0.2707 0.2400 0.3398 0.0085  0.0118  -0.0389 169 LEU   B OXT 
6735 O  OXT B LEU   B 169 ? 0.2511 0.2132 0.3429 0.0356  -0.0017 -0.0474 169 LEU   B OXT 
6758 S  S   B DMS   C .   ? 0.4292 0.4536 0.3494 -0.1241 -0.0146 0.1559  301 DMS   A S   
6759 O  O   B DMS   C .   ? 0.4329 0.4563 0.3501 -0.1204 -0.0121 0.1585  301 DMS   A O   
6760 C  C1  B DMS   C .   ? 0.4334 0.4574 0.3549 -0.1216 -0.0144 0.1556  301 DMS   A C1  
6761 C  C2  B DMS   C .   ? 0.4343 0.4575 0.3536 -0.1204 -0.0149 0.1539  301 DMS   A C2  
6768 N  N2  B A1BBQ D .   ? 0.1121 0.1198 0.1628 -0.0095 0.0112  0.0222  302 A1BBQ A N2  
6769 C  C3  B A1BBQ D .   ? 0.1361 0.1527 0.1762 -0.0043 -0.0072 0.0112  302 A1BBQ A C3  
6770 C  C6  B A1BBQ D .   ? 0.1620 0.1785 0.2436 0.0007  -0.0239 -0.0138 302 A1BBQ A C6  
6771 C  C9  B A1BBQ D .   ? 0.1135 0.1313 0.1469 -0.0021 0.0210  0.0138  302 A1BBQ A C9  
6772 C  C12 B A1BBQ D .   ? 0.1098 0.1264 0.1584 -0.0081 0.0015  0.0293  302 A1BBQ A C12 
6773 C  C1  B A1BBQ D .   ? 0.1365 0.1243 0.1810 -0.0023 0.0045  0.0313  302 A1BBQ A C1  
6774 C  C10 B A1BBQ D .   ? 0.1147 0.1267 0.1502 -0.0031 -0.0017 0.0114  302 A1BBQ A C10 
6775 C  C11 B A1BBQ D .   ? 0.1124 0.1233 0.1558 -0.0027 0.0009  0.0222  302 A1BBQ A C11 
6776 C  C13 B A1BBQ D .   ? 0.1059 0.1249 0.1459 -0.0128 -0.0106 0.0231  302 A1BBQ A C13 
6777 C  C2  B A1BBQ D .   ? 0.1220 0.1439 0.1635 -0.0039 -0.0024 0.0141  302 A1BBQ A C2  
6778 C  C4  B A1BBQ D .   ? 0.1460 0.1636 0.2152 0.0034  -0.0172 0.0082  302 A1BBQ A C4  
6779 C  C5  B A1BBQ D .   ? 0.1617 0.1789 0.2407 0.0008  -0.0225 -0.0001 302 A1BBQ A C5  
6780 C  C7  B A1BBQ D .   ? 0.1495 0.1628 0.2119 0.0035  -0.0097 -0.0027 302 A1BBQ A C7  
6781 C  C8  B A1BBQ D .   ? 0.1160 0.1218 0.1583 -0.0039 0.0066  0.0210  302 A1BBQ A C8  
6782 N  N1  B A1BBQ D .   ? 0.1220 0.1258 0.1615 -0.0024 -0.0063 0.0348  302 A1BBQ A N1  
6783 N  N3  B A1BBQ D .   ? 0.1177 0.1352 0.1475 -0.0093 0.0168  0.0228  302 A1BBQ A N3  
6784 N  N4  B A1BBQ D .   ? 0.1179 0.1284 0.1426 0.0003  -0.0125 0.0205  302 A1BBQ A N4  
6785 O  O1  B A1BBQ D .   ? 0.1314 0.1429 0.1376 -0.0058 -0.0013 0.0181  302 A1BBQ A O1  
6786 O  O2  B A1BBQ D .   ? 0.1712 0.1860 0.2488 0.0004  -0.0324 -0.0157 302 A1BBQ A O2  
6805 CL CL  B CL    E .   ? 0.1504 0.1311 0.2096 -0.0089 0.0144  -0.0234 303 CL    A CL  
6806 O  O   . HOH   F .   ? 0.6461 0.1943 0.4571 -0.0518 -0.1617 0.0207  401 HOH   A O   
6807 O  O   . HOH   F .   ? 0.4062 0.2073 0.2179 -0.0022 0.0426  0.0067  402 HOH   A O   
6808 O  O   . HOH   F .   ? 0.6526 0.4678 0.6239 -0.1098 0.1756  0.1982  403 HOH   A O   
6809 O  O   . HOH   F .   ? 0.5732 0.7173 0.6244 -0.1227 -0.1288 -0.1236 404 HOH   A O   
6810 O  O   A HOH   F .   ? 0.3477 0.5363 0.3279 -0.0708 -0.0092 0.0675  405 HOH   A O   
6811 O  O   . HOH   F .   ? 0.5480 0.4131 0.4871 0.1276  -0.1157 0.0236  406 HOH   A O   
6812 O  O   B HOH   F .   ? 0.2800 0.3513 0.4065 0.1611  -0.0427 -0.0431 407 HOH   A O   
6813 O  O   . HOH   F .   ? 0.4132 0.5723 0.3539 -0.1189 0.1334  0.0973  408 HOH   A O   
6814 O  O   A HOH   F .   ? 0.5170 0.4569 0.4670 -0.0020 0.0953  0.2611  409 HOH   A O   
6815 O  O   . HOH   F .   ? 0.2523 0.2569 0.3494 -0.0194 0.0832  0.0758  410 HOH   A O   
6816 O  O   . HOH   F .   ? 0.3425 0.2944 0.1626 -0.0656 0.0472  0.0416  411 HOH   A O   
6817 O  O   . HOH   F .   ? 0.5593 0.5305 0.4524 -0.1380 -0.1420 0.1019  412 HOH   A O   
6818 O  O   . HOH   F .   ? 0.5590 0.6993 0.5292 -0.0307 0.2950  -0.1190 413 HOH   A O   
6819 O  O   B HOH   F .   ? 0.1268 0.1420 0.2002 0.0021  0.0072  0.0384  414 HOH   A O   
6820 O  O   . HOH   F .   ? 0.6193 0.4998 0.3334 0.2492  -0.1147 0.0472  415 HOH   A O   
6821 O  O   . HOH   F .   ? 0.2957 0.6216 0.6171 0.0971  0.0608  0.1615  416 HOH   A O   
6822 O  O   . HOH   F .   ? 0.1559 0.4392 0.3626 -0.0151 0.0049  -0.0034 417 HOH   A O   
6823 O  O   . HOH   F .   ? 0.3774 0.3715 0.3852 -0.1614 -0.0149 0.1281  418 HOH   A O   
6824 O  O   B HOH   F .   ? 0.2931 0.2401 0.2824 -0.0544 0.1054  -0.0257 419 HOH   A O   
6825 O  O   B HOH   F .   ? 0.3610 0.2188 0.1674 -0.0929 0.0046  0.0202  420 HOH   A O   
6826 O  O   . HOH   F .   ? 0.5914 0.5092 0.4697 -0.1412 0.1376  0.1774  421 HOH   A O   
6827 O  O   B HOH   F .   ? 0.1301 0.2125 0.3070 0.0196  0.0087  0.0091  422 HOH   A O   
6828 O  O   . HOH   F .   ? 0.1794 0.4450 0.3087 0.0794  -0.0005 0.0441  423 HOH   A O   
6829 O  O   . HOH   F .   ? 0.4122 0.3557 0.5660 0.0053  0.1611  0.0289  424 HOH   A O   
6830 O  O   . HOH   F .   ? 0.2118 0.1819 0.3615 -0.0459 0.0214  -0.0215 425 HOH   A O   
6831 O  O   B HOH   F .   ? 0.3878 0.3699 0.2787 0.0348  0.0049  -0.0689 426 HOH   A O   
6832 O  O   . HOH   F .   ? 0.2715 0.6432 0.4471 -0.0472 -0.0549 0.1622  427 HOH   A O   
6833 O  O   . HOH   F .   ? 0.4470 0.5830 0.4919 0.1998  0.0643  -0.0625 428 HOH   A O   
6834 O  O   . HOH   F .   ? 0.5683 0.6612 0.3280 -0.0979 -0.0130 0.1338  429 HOH   A O   
6835 O  O   . HOH   F .   ? 0.4336 0.6755 0.3829 0.2033  -0.0293 -0.0401 430 HOH   A O   
6836 O  O   . HOH   F .   ? 0.1896 0.2391 0.2160 -0.0462 -0.0276 0.0927  431 HOH   A O   
6837 O  O   . HOH   F .   ? 0.6663 0.7060 0.4497 0.0830  -0.1374 -0.0374 432 HOH   A O   
6838 O  O   . HOH   F .   ? 0.2134 0.3324 0.3547 -0.0396 -0.0614 0.0962  433 HOH   A O   
6839 O  O   . HOH   F .   ? 0.2562 0.4347 0.3328 0.1133  -0.0932 -0.0586 434 HOH   A O   
6840 O  O   . HOH   F .   ? 0.2487 0.2940 0.3157 -0.0198 0.1043  -0.0205 435 HOH   A O   
6841 O  O   . HOH   F .   ? 0.1530 0.1524 0.2394 -0.0254 0.0003  0.0042  436 HOH   A O   
6842 O  O   . HOH   F .   ? 0.2266 0.2116 0.2682 0.0433  0.0243  0.0385  437 HOH   A O   
6843 O  O   . HOH   F .   ? 0.2245 0.1819 0.4322 0.0071  -0.0548 -0.0422 438 HOH   A O   
6844 O  O   . HOH   F .   ? 0.3996 0.3595 0.4215 -0.1606 -0.0635 0.1825  439 HOH   A O   
6845 O  O   . HOH   F .   ? 0.4674 0.2996 0.3469 -0.0506 -0.0263 -0.0245 440 HOH   A O   
6846 O  O   B HOH   F .   ? 0.2329 0.2027 0.3107 0.0218  -0.0232 -0.0354 441 HOH   A O   
6847 O  O   . HOH   F .   ? 0.3341 0.3869 0.4479 -0.0338 0.1914  0.0653  442 HOH   A O   
6848 O  O   . HOH   F .   ? 0.4667 0.2733 0.2634 -0.1147 0.0199  0.0543  443 HOH   A O   
6849 O  O   . HOH   F .   ? 0.5189 0.1981 0.5457 0.0589  -0.0653 -0.0053 444 HOH   A O   
6850 O  O   . HOH   F .   ? 0.6042 0.3818 0.2883 -0.0251 0.0292  0.1218  445 HOH   A O   
6851 O  O   . HOH   F .   ? 0.7201 0.4304 0.5431 -0.0084 -0.0918 0.0223  446 HOH   A O   
6852 O  O   . HOH   F .   ? 0.7838 0.5767 0.8074 -0.1092 0.0221  0.1756  447 HOH   A O   
6853 O  O   . HOH   F .   ? 0.8894 0.6309 0.7394 0.0132  -0.1281 0.0766  448 HOH   A O   
6854 O  O   . HOH   F .   ? 0.6177 0.1654 0.4170 0.0128  -0.0423 0.0352  449 HOH   A O   
6855 O  O   . HOH   F .   ? 0.1379 0.2159 0.2217 0.0079  -0.0143 0.0586  450 HOH   A O   
6856 O  O   A HOH   F .   ? 0.2238 0.5031 0.2448 0.1290  -0.0285 -0.0280 451 HOH   A O   
6857 O  O   . HOH   F .   ? 0.3793 0.5786 0.3564 0.0710  -0.0694 0.1321  452 HOH   A O   
6858 O  O   . HOH   F .   ? 0.2925 0.2806 0.5822 -0.0309 -0.1327 0.1790  453 HOH   A O   
6859 O  O   . HOH   F .   ? 0.3287 0.4353 0.1966 -0.0341 0.0586  0.0275  454 HOH   A O   
6860 O  O   . HOH   F .   ? 0.4375 0.8140 0.7194 -0.1119 -0.1454 0.0339  455 HOH   A O   
6861 O  O   . HOH   F .   ? 0.1856 0.1688 0.2244 0.0227  -0.0214 0.0105  456 HOH   A O   
6862 O  O   . HOH   F .   ? 0.2788 0.2935 0.4166 -0.0434 -0.0774 -0.0886 457 HOH   A O   
6863 O  O   . HOH   F .   ? 0.1916 0.2035 0.3965 0.0111  0.0944  -0.0149 458 HOH   A O   
6864 O  O   . HOH   F .   ? 0.3472 0.3705 0.2123 -0.1157 -0.0402 -0.0485 459 HOH   A O   
6865 O  O   . HOH   F .   ? 0.3209 0.3378 0.5559 0.0945  0.0760  -0.0210 460 HOH   A O   
6866 O  O   . HOH   F .   ? 0.1379 0.1574 0.1536 -0.0068 -0.0107 -0.0006 461 HOH   A O   
6867 O  O   B HOH   F .   ? 0.1985 0.2020 0.0904 -0.0248 -0.0296 0.0247  462 HOH   A O   
6868 O  O   . HOH   F .   ? 0.1368 0.1867 0.2565 0.0037  -0.0048 0.0091  463 HOH   A O   
6869 O  O   . HOH   F .   ? 0.1905 0.2244 0.3957 0.0150  0.0908  -0.0365 464 HOH   A O   
6870 O  O   . HOH   F .   ? 0.3375 0.4604 0.3080 0.0109  -0.0322 -0.0200 465 HOH   A O   
6871 O  O   . HOH   F .   ? 0.2170 0.3253 0.4320 -0.0251 0.0425  -0.0628 466 HOH   A O   
6872 O  O   . HOH   F .   ? 0.3927 0.4645 0.4103 0.2153  0.0420  0.0305  467 HOH   A O   
6873 O  O   . HOH   F .   ? 0.1500 0.1272 0.2385 -0.0095 0.0075  -0.0031 468 HOH   A O   
6874 O  O   A HOH   F .   ? 0.1037 0.1261 0.1489 0.0038  -0.0337 -0.0002 469 HOH   A O   
6875 O  O   . HOH   F .   ? 0.4739 0.2484 0.3574 -0.1583 0.1639  -0.0724 470 HOH   A O   
6876 O  O   . HOH   F .   ? 0.4181 0.2234 0.4740 -0.0975 0.0812  0.0441  471 HOH   A O   
6877 O  O   . HOH   F .   ? 0.1237 0.1219 0.1585 -0.0032 0.0042  0.0134  472 HOH   A O   
6878 O  O   . HOH   F .   ? 0.2611 0.1867 0.2212 -0.0413 0.0219  -0.0041 473 HOH   A O   
6879 O  O   A HOH   F .   ? 0.2501 0.3148 0.2261 0.0639  -0.0174 0.0913  474 HOH   A O   
6880 O  O   A HOH   F .   ? 0.1177 0.1178 0.1784 -0.0083 -0.0159 0.0163  475 HOH   A O   
6881 O  O   . HOH   F .   ? 0.1711 0.1710 0.2145 0.0128  -0.0241 0.0275  476 HOH   A O   
6882 O  O   . HOH   F .   ? 0.1912 0.2259 0.2208 -0.0145 -0.0408 0.0424  477 HOH   A O   
6883 O  O   . HOH   F .   ? 0.1548 0.2578 0.3407 -0.0135 0.0525  0.0490  478 HOH   A O   
6884 O  O   . HOH   F .   ? 0.3170 0.6155 0.3574 0.1454  0.0808  -0.0204 479 HOH   A O   
6885 O  O   . HOH   F .   ? 0.2159 0.1598 0.1565 -0.0090 0.0155  0.0215  480 HOH   A O   
6886 O  O   . HOH   F .   ? 0.3151 0.2904 0.1892 0.0379  0.0557  0.0157  481 HOH   A O   
6887 O  O   . HOH   F .   ? 0.1713 0.1765 0.2486 -0.0207 0.0153  0.0293  482 HOH   A O   
6888 O  O   . HOH   F .   ? 0.1868 0.2700 0.2666 0.0361  0.0413  0.1014  483 HOH   A O   
6889 O  O   B HOH   F .   ? 0.1818 0.2015 0.1669 0.0568  0.0008  0.0291  484 HOH   A O   
6890 O  O   B HOH   F .   ? 0.2745 0.4699 0.4001 0.0241  -0.0240 0.1595  485 HOH   A O   
6891 O  O   . HOH   F .   ? 0.2604 0.4118 0.3281 0.0668  0.0897  0.1861  486 HOH   A O   
6892 O  O   . HOH   F .   ? 0.5186 0.5147 0.5144 0.1659  -0.1341 -0.1606 487 HOH   A O   
6893 O  O   . HOH   F .   ? 0.2449 0.2395 0.4019 0.0352  -0.0748 0.0418  488 HOH   A O   
6894 O  O   . HOH   F .   ? 0.1609 0.1616 0.2392 -0.0173 0.0112  0.0349  489 HOH   A O   
6895 O  O   . HOH   F .   ? 0.1644 0.1302 0.1535 -0.0236 0.0167  -0.0016 490 HOH   A O   
6896 O  O   . HOH   F .   ? 0.3096 0.2399 0.5947 -0.0664 -0.0234 0.0134  491 HOH   A O   
6897 O  O   . HOH   F .   ? 0.2350 0.1883 0.1783 -0.0473 0.0146  0.0353  492 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2427 0.3888 0.4397 -0.0359 0.1391  -0.0878 493 HOH   A O   
6899 O  O   A HOH   F .   ? 0.3225 0.4253 0.3462 -0.0714 0.0072  0.0002  494 HOH   A O   
6900 O  O   . HOH   F .   ? 0.1708 0.1631 0.1747 -0.0016 0.0091  0.0184  495 HOH   A O   
6901 O  O   . HOH   F .   ? 0.3543 0.5287 0.3741 -0.0166 0.0009  0.0993  496 HOH   A O   
6902 O  O   . HOH   F .   ? 0.2566 0.3665 0.5123 -0.0142 0.1038  -0.0171 497 HOH   A O   
6903 O  O   . HOH   F .   ? 0.2941 0.2479 0.2230 -0.0432 -0.0932 0.0462  498 HOH   A O   
6904 O  O   . HOH   F .   ? 0.3065 0.3523 0.4420 -0.1108 0.1530  -0.0091 499 HOH   A O   
6905 O  O   . HOH   F .   ? 0.7297 0.7647 0.6834 -0.1316 0.0072  -0.0784 500 HOH   A O   
6906 O  O   A HOH   F .   ? 0.1435 0.2513 0.1874 0.0271  0.0453  0.1012  501 HOH   A O   
6907 O  O   . HOH   F .   ? 0.3169 0.2591 0.3129 -0.0141 -0.0445 0.0973  502 HOH   A O   
6908 O  O   . HOH   F .   ? 0.2790 0.4001 0.3776 -0.0512 0.0352  -0.0556 503 HOH   A O   
6909 O  O   . HOH   F .   ? 0.6028 0.3394 0.4087 -0.1391 -0.0198 0.0641  504 HOH   A O   
6910 O  O   . HOH   F .   ? 0.1744 0.1926 0.3955 0.0357  0.1011  0.0992  505 HOH   A O   
6911 O  O   . HOH   F .   ? 1.1452 1.0186 0.7941 -0.1156 -0.1302 -0.0816 506 HOH   A O   
6912 O  O   A HOH   F .   ? 0.3330 0.3628 0.2516 0.0198  -0.1172 -0.0282 507 HOH   A O   
6913 O  O   . HOH   F .   ? 0.2219 0.1819 0.3074 0.0119  -0.0436 0.0051  508 HOH   A O   
6914 O  O   B HOH   F .   ? 0.1392 0.1353 0.1822 -0.0137 -0.0159 -0.0008 509 HOH   A O   
6915 O  O   . HOH   F .   ? 0.5478 0.4861 0.3992 -0.0741 -0.1419 0.0033  510 HOH   A O   
6916 O  O   . HOH   F .   ? 0.2814 0.2877 0.3917 -0.0143 -0.0051 -0.0739 511 HOH   A O   
6917 O  O   A HOH   F .   ? 0.1161 0.1507 0.1025 0.0074  0.0162  0.0178  512 HOH   A O   
6918 O  O   . HOH   F .   ? 0.2458 0.3372 0.7135 -0.0412 -0.0090 -0.0466 513 HOH   A O   
6919 O  O   . HOH   F .   ? 0.1298 0.1373 0.1825 0.0014  -0.0230 0.0020  514 HOH   A O   
6920 O  O   . HOH   F .   ? 0.1591 0.2124 0.2952 -0.0294 -0.0179 0.0330  515 HOH   A O   
6921 O  O   . HOH   F .   ? 0.1491 0.1480 0.2025 0.0212  -0.0255 0.0138  516 HOH   A O   
6922 O  O   . HOH   F .   ? 0.2413 0.2135 0.2282 -0.0514 0.0090  0.0447  517 HOH   A O   
6923 O  O   . HOH   F .   ? 0.4759 0.5040 0.2367 -0.0012 0.0192  0.0571  518 HOH   A O   
6924 O  O   . HOH   F .   ? 0.2778 0.1942 0.2415 -0.0091 -0.0005 0.0244  519 HOH   A O   
6925 O  O   . HOH   F .   ? 0.2132 0.2244 0.2654 -0.0189 -0.0171 0.0865  520 HOH   A O   
6926 O  O   . HOH   F .   ? 0.1795 0.2602 0.4768 -0.0137 -0.0229 0.0116  521 HOH   A O   
6927 O  O   . HOH   F .   ? 0.5978 0.7257 0.6254 0.1173  -0.0427 0.0681  522 HOH   A O   
6928 O  O   A HOH   F .   ? 0.5206 0.4164 0.2440 -0.0976 0.0165  0.1174  523 HOH   A O   
6929 O  O   . HOH   F .   ? 0.4063 0.2339 0.4981 -0.0793 -0.2252 0.1258  524 HOH   A O   
6930 O  O   . HOH   F .   ? 0.1574 0.1670 0.3529 0.0001  0.0002  0.0238  525 HOH   A O   
6931 O  O   . HOH   F .   ? 0.1999 0.2793 0.2481 -0.0026 -0.0523 0.0607  526 HOH   A O   
6932 O  O   . HOH   F .   ? 0.4587 0.5103 0.6372 0.1611  -0.0288 0.0615  527 HOH   A O   
6933 O  O   . HOH   F .   ? 0.6230 0.7924 0.7777 0.0502  0.0046  -0.0566 528 HOH   A O   
6934 O  O   . HOH   F .   ? 0.3434 0.1217 0.2033 0.0097  -0.0698 0.0167  529 HOH   A O   
6935 O  O   . HOH   F .   ? 0.4729 0.3382 0.2444 -0.0647 0.0491  -0.0015 530 HOH   A O   
6936 O  O   A HOH   F .   ? 0.1695 0.1906 0.2828 0.0165  -0.0457 -0.0376 531 HOH   A O   
6937 O  O   . HOH   F .   ? 0.5543 0.7590 0.4105 0.0521  0.2680  -0.0616 532 HOH   A O   
6938 O  O   A HOH   F .   ? 0.4862 0.2977 0.3326 0.0068  0.1215  0.0684  533 HOH   A O   
6939 O  O   . HOH   F .   ? 0.2570 0.5621 0.1630 -0.0273 0.0494  -0.0054 534 HOH   A O   
6940 O  O   . HOH   F .   ? 0.4300 0.7305 0.3417 -0.0983 -0.0339 0.1359  535 HOH   A O   
6941 O  O   . HOH   F .   ? 0.6325 0.6136 0.6677 0.3502  0.1061  0.1236  536 HOH   A O   
6942 O  O   . HOH   F .   ? 0.2512 0.4058 0.2901 0.1698  0.0023  0.0149  537 HOH   A O   
6943 O  O   . HOH   F .   ? 0.3332 0.4363 0.5721 0.1125  0.0405  -0.1628 538 HOH   A O   
6944 O  O   A HOH   F .   ? 0.2941 0.4950 0.4086 0.0065  -0.0844 0.1379  539 HOH   A O   
6945 O  O   . HOH   F .   ? 0.3478 0.2546 0.1737 -0.0759 0.0254  0.0578  540 HOH   A O   
6946 O  O   A HOH   F .   ? 0.2305 0.1561 0.2544 0.0114  -0.0167 -0.0277 541 HOH   A O   
6947 O  O   A HOH   F .   ? 0.1982 0.1800 0.1415 0.0129  -0.0052 -0.0030 542 HOH   A O   
6948 O  O   . HOH   F .   ? 0.1922 0.1961 0.4737 -0.0207 -0.0910 0.0452  543 HOH   A O   
6949 O  O   . HOH   F .   ? 0.6541 0.4135 0.4676 0.1607  -0.1264 0.1113  544 HOH   A O   
6950 O  O   . HOH   F .   ? 0.2799 0.1674 0.2805 0.0250  -0.0011 0.0137  545 HOH   A O   
6951 O  O   . HOH   F .   ? 0.6263 0.6716 0.6424 -0.1451 0.1370  -0.1244 546 HOH   A O   
6952 O  O   . HOH   F .   ? 0.4116 0.3627 0.3066 0.2215  -0.0953 -0.0703 547 HOH   A O   
6953 O  O   . HOH   F .   ? 0.7966 0.7019 0.7705 0.0944  -0.0122 0.0076  548 HOH   A O   
6954 O  O   . HOH   F .   ? 0.6862 0.7722 0.5757 -0.1101 0.1213  0.2097  549 HOH   A O   
6955 O  O   A HOH   F .   ? 0.5015 0.2504 0.5840 0.0371  -0.0450 -0.0564 550 HOH   A O   
6956 O  O   B HOH   F .   ? 0.1867 0.1747 0.3811 0.0227  -0.0739 0.0066  551 HOH   A O   
6957 O  O   . HOH   F .   ? 0.2118 0.3043 0.2513 0.0029  -0.0033 -0.0482 552 HOH   A O   
6958 O  O   . HOH   F .   ? 0.7516 0.8892 0.5214 0.3249  -0.1188 0.1603  553 HOH   A O   
6959 O  O   . HOH   F .   ? 0.2303 0.2158 0.3210 0.0153  0.0495  0.0512  554 HOH   A O   
6960 O  O   . HOH   F .   ? 0.6769 0.5669 0.8092 0.0194  -0.1003 0.1940  555 HOH   A O   
6961 O  O   . HOH   F .   ? 0.4491 0.5102 0.5307 -0.0349 -0.1165 -0.1421 556 HOH   A O   
6962 O  O   . HOH   F .   ? 0.7942 0.8622 0.7106 -0.1302 0.1386  0.2090  557 HOH   A O   
6963 O  O   . HOH   F .   ? 0.2438 0.2680 0.3612 0.0435  0.0382  -0.0534 558 HOH   A O   
6964 O  O   A HOH   F .   ? 0.4458 0.4116 0.3193 0.1768  0.1313  0.1673  559 HOH   A O   
6965 O  O   . HOH   F .   ? 0.4876 0.3331 0.4039 0.0016  0.0116  0.0674  560 HOH   A O   
6966 O  O   . HOH   F .   ? 0.3924 0.4837 0.4432 0.1326  0.1336  0.0731  561 HOH   A O   
6967 O  O   . HOH   F .   ? 0.4337 0.3068 0.3751 0.0309  0.0586  0.0072  562 HOH   A O   
6968 O  O   . HOH   F .   ? 0.2720 0.2859 0.4740 -0.0313 0.0169  -0.1119 563 HOH   A O   
6969 O  O   . HOH   F .   ? 0.7343 0.7358 0.4747 -0.0744 -0.1085 -0.0251 564 HOH   A O   
6970 O  O   . HOH   F .   ? 0.2426 0.2733 0.2728 0.0528  -0.0231 0.0072  565 HOH   A O   
6971 O  O   . HOH   F .   ? 0.3524 0.5473 0.5172 -0.1639 0.1020  -0.1230 566 HOH   A O   
6972 O  O   . HOH   F .   ? 0.3433 0.5252 0.5273 0.0819  -0.1499 0.1178  567 HOH   A O   
6973 O  O   . HOH   F .   ? 0.2368 0.4663 0.4948 0.0315  -0.0221 -0.1830 568 HOH   A O   
6974 O  O   . HOH   F .   ? 0.3203 0.4424 0.3651 -0.1303 -0.0007 -0.0053 569 HOH   A O   
6975 O  O   . HOH   F .   ? 0.2740 0.2468 0.3070 -0.0882 0.0389  -0.0291 570 HOH   A O   
6976 O  O   . HOH   F .   ? 0.3588 0.6984 0.4428 -0.0619 -0.1097 0.2275  571 HOH   A O   
6977 O  O   . HOH   F .   ? 0.6984 0.7424 0.6264 0.1520  0.2004  0.2494  572 HOH   A O   
6978 O  O   . HOH   F .   ? 0.5564 0.3671 0.6820 0.0751  0.0490  0.2508  573 HOH   A O   
6979 O  O   . HOH   F .   ? 0.2894 0.1811 0.2428 0.0479  -0.0862 -0.0287 574 HOH   A O   
6980 O  O   . HOH   F .   ? 0.2732 0.2554 0.3284 0.0177  0.0558  -0.0075 575 HOH   A O   
6981 O  O   B HOH   F .   ? 0.3438 0.1745 0.4261 0.0239  0.1287  0.0254  576 HOH   A O   
6982 O  O   . HOH   F .   ? 0.6364 0.6283 0.4976 0.2341  -0.0414 -0.1004 577 HOH   A O   
6983 O  O   A HOH   F .   ? 0.4370 0.4391 0.3724 -0.0176 -0.1090 -0.1317 578 HOH   A O   
6984 O  O   . HOH   F .   ? 0.5075 0.4769 0.3884 0.0010  0.0644  0.0439  579 HOH   A O   
6985 O  O   . HOH   F .   ? 0.4505 0.5263 0.3692 0.0782  -0.1113 -0.1129 580 HOH   A O   
6986 O  O   . HOH   F .   ? 0.5233 0.8063 0.6789 -0.1490 -0.1384 -0.0195 581 HOH   A O   
6987 O  O   . HOH   F .   ? 0.4264 0.5174 0.2795 0.0190  -0.0394 0.0308  582 HOH   A O   
6988 O  O   . HOH   F .   ? 0.5234 0.4517 0.3952 -0.0365 -0.0347 -0.0284 583 HOH   A O   
6989 O  O   . HOH   F .   ? 0.6051 0.4069 0.4112 -0.0141 0.1057  0.0220  584 HOH   A O   
6990 O  O   . HOH   F .   ? 0.4177 0.4576 0.5083 -0.1844 -0.0597 -0.0352 585 HOH   A O   
6991 O  O   . HOH   F .   ? 0.4396 0.4658 0.5041 0.0317  -0.0301 -0.1407 586 HOH   A O   
6992 O  O   . HOH   F .   ? 0.6844 0.5990 0.7083 -0.1343 0.0349  -0.0861 587 HOH   A O   
6993 O  O   . HOH   F .   ? 0.2825 0.2967 0.2357 0.0551  0.0097  0.0238  588 HOH   A O   
6994 O  O   . HOH   F .   ? 0.4057 0.5048 0.4700 0.0601  0.1858  0.1942  589 HOH   A O   
6995 O  O   . HOH   F .   ? 0.6291 0.2805 0.3573 -0.0117 -0.1493 0.0594  590 HOH   A O   
6996 O  O   . HOH   F .   ? 0.3064 0.4900 0.3316 -0.0114 -0.0364 -0.0554 591 HOH   A O   
6997 O  O   . HOH   F .   ? 0.7899 0.3948 0.3269 -0.0862 -0.1219 0.0177  592 HOH   A O   
6998 O  O   . HOH   F .   ? 0.2684 0.2315 0.7004 0.0080  -0.1414 0.0231  593 HOH   A O   
6999 O  O   . HOH   F .   ? 0.6677 0.5277 0.6208 -0.1144 -0.0331 -0.1155 594 HOH   A O   
7000 O  O   . HOH   F .   ? 0.2605 0.4931 0.4122 0.0957  0.0982  0.2570  595 HOH   A O   
7001 O  O   . HOH   F .   ? 0.7497 0.6451 0.4955 -0.0864 0.1570  0.1658  596 HOH   A O   
7002 O  O   . HOH   F .   ? 0.5057 0.7269 0.5628 -0.0409 -0.1157 -0.0436 597 HOH   A O   
7003 O  O   . HOH   F .   ? 0.3830 0.3256 0.2325 -0.0750 0.0997  -0.0316 598 HOH   A O   
7004 O  O   . HOH   F .   ? 0.6333 0.5691 0.7937 0.1185  0.2577  -0.1109 599 HOH   A O   
7005 O  O   . HOH   F .   ? 0.5279 0.6190 0.3974 -0.0008 -0.0373 0.0022  600 HOH   A O   
7006 O  O   . HOH   F .   ? 0.2838 0.3290 0.5957 0.0354  0.0673  -0.1001 601 HOH   A O   
7007 O  O   . HOH   F .   ? 0.5061 0.4646 0.5114 -0.1384 0.0847  0.0860  602 HOH   A O   
7008 O  O   . HOH   F .   ? 0.3143 0.2043 0.6125 -0.0046 0.0794  0.0595  603 HOH   A O   
7009 O  O   . HOH   F .   ? 0.6190 0.2332 0.5090 -0.0817 0.1390  0.0268  604 HOH   A O   
7010 O  O   . HOH   F .   ? 0.4476 0.2836 0.4493 -0.0187 0.2109  0.0245  605 HOH   A O   
7011 O  O   B HOH   F .   ? 0.1774 0.1826 0.1942 0.0386  0.0234  0.0105  606 HOH   A O   
7012 O  O   . HOH   F .   ? 0.2324 0.3505 0.3823 0.0299  -0.0526 0.1028  607 HOH   A O   
7013 O  O   . HOH   F .   ? 0.7576 0.7560 0.6219 0.1410  -0.1375 0.0041  608 HOH   A O   
7014 O  O   . HOH   F .   ? 0.2831 0.4184 0.5079 0.0264  -0.0310 -0.0188 609 HOH   A O   
7015 O  O   . HOH   F .   ? 0.5290 0.7538 0.5369 0.1026  -0.0180 0.1354  610 HOH   A O   
7016 O  O   . HOH   F .   ? 0.4586 0.9173 0.6399 -0.1009 -0.0493 0.1429  611 HOH   A O   
7017 O  O   . HOH   F .   ? 0.5012 0.3417 0.5467 0.0143  -0.1290 0.2006  612 HOH   A O   
7018 O  O   . HOH   F .   ? 0.5268 0.6789 0.5500 0.3103  -0.0403 0.1375  613 HOH   A O   
7019 O  O   . HOH   F .   ? 0.3236 0.2490 0.4759 -0.0042 -0.0009 0.0772  614 HOH   A O   
7020 O  O   A HOH   F .   ? 0.3089 0.4576 0.2789 0.1354  0.0036  -0.0464 615 HOH   A O   
7021 O  O   . HOH   F .   ? 0.7286 0.6309 0.4786 -0.1210 -0.1051 -0.1301 616 HOH   A O   
7022 O  O   . HOH   F .   ? 0.2488 0.7758 0.3177 0.0869  -0.0157 -0.0216 617 HOH   A O   
7023 O  O   . HOH   F .   ? 0.5210 0.6803 0.5160 -0.0537 0.0467  0.1404  618 HOH   A O   
7024 O  O   . HOH   F .   ? 0.6662 0.5232 0.4813 0.1028  0.2011  0.0733  619 HOH   A O   
7025 O  O   . HOH   F .   ? 0.3723 0.4092 0.5876 -0.0686 -0.1010 0.2568  620 HOH   A O   
7026 O  O   . HOH   G .   ? 0.2280 0.2269 0.2852 0.0136  0.0813  0.0251  201 HOH   B O   
7027 O  O   . HOH   G .   ? 0.3560 0.3069 0.6696 -0.0081 0.0414  0.0025  202 HOH   B O   
7028 O  O   . HOH   G .   ? 0.3630 0.5913 0.4421 -0.0670 0.1883  -0.1858 203 HOH   B O   
7029 O  O   . HOH   G .   ? 0.7381 0.3494 0.4373 -0.0048 0.1493  -0.0336 204 HOH   B O   
7030 O  O   . HOH   G .   ? 0.4931 0.3598 0.4112 0.0382  -0.0453 -0.1803 205 HOH   B O   
7031 O  O   . HOH   G .   ? 0.6374 0.6429 0.6048 0.2136  -0.0316 0.0240  206 HOH   B O   
7032 O  O   . HOH   G .   ? 0.4110 0.4417 0.3590 0.2002  0.0058  0.0625  207 HOH   B O   
7033 O  O   . HOH   G .   ? 0.5708 0.4098 0.6209 0.0631  -0.0981 0.2611  208 HOH   B O   
7034 O  O   . HOH   G .   ? 0.5636 0.5727 0.3892 0.3243  -0.1168 -0.0590 209 HOH   B O   
7035 O  O   . HOH   G .   ? 0.3615 0.2651 0.5324 0.0722  -0.0760 -0.0640 210 HOH   B O   
7036 O  O   . HOH   G .   ? 0.3622 0.2823 0.3814 0.0621  -0.0306 -0.0504 211 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2047 0.2140 0.2954 -0.0022 0.0449  -0.0262 212 HOH   B O   
7038 O  O   . HOH   G .   ? 0.2721 0.6397 0.3635 0.0961  0.0350  0.2482  213 HOH   B O   
7039 O  O   . HOH   G .   ? 0.1632 0.1934 0.2741 -0.0259 -0.0052 0.0111  214 HOH   B O   
7040 O  O   . HOH   G .   ? 0.2984 0.2010 0.5535 0.0014  0.1840  0.0712  215 HOH   B O   
7041 O  O   . HOH   G .   ? 0.4693 0.4697 0.2197 0.0008  -0.0360 -0.1184 216 HOH   B O   
7042 O  O   . HOH   G .   ? 0.3565 0.5716 0.5251 0.2449  0.0282  -0.0684 217 HOH   B O   
7043 O  O   . HOH   G .   ? 0.5396 0.4677 0.4123 0.0886  0.1194  -0.1641 218 HOH   B O   
7044 O  O   . HOH   G .   ? 0.1951 0.2080 0.3075 -0.0261 0.0122  -0.0137 219 HOH   B O   
7045 O  O   . HOH   G .   ? 0.3496 0.4778 0.4879 -0.1170 -0.0329 -0.1407 220 HOH   B O   
7046 O  O   . HOH   G .   ? 0.2626 0.2613 0.5830 0.0646  -0.0943 0.0371  221 HOH   B O   
7047 O  O   . HOH   G .   ? 0.3077 0.4063 0.3119 0.0575  -0.0801 0.0331  222 HOH   B O   
7048 O  O   . HOH   G .   ? 0.3503 0.2301 0.5194 0.0062  0.2090  0.0300  223 HOH   B O   
7049 O  O   . HOH   G .   ? 0.2969 0.1799 0.6107 -0.0118 -0.1130 -0.0149 224 HOH   B O   
7050 O  O   . HOH   G .   ? 0.2431 0.1788 0.2632 -0.0206 0.0966  0.0037  225 HOH   B O   
7051 O  O   . HOH   G .   ? 0.5103 0.2967 0.4365 -0.1716 0.0126  -0.0208 226 HOH   B O   
7052 O  O   . HOH   G .   ? 0.3971 0.2873 0.4087 -0.0326 -0.0968 -0.0557 227 HOH   B O   
7053 O  O   . HOH   G .   ? 0.2207 0.2381 0.3593 -0.0390 0.0179  -0.0444 228 HOH   B O   
7054 O  O   . HOH   G .   ? 0.3986 0.3757 0.7246 0.0438  -0.1610 -0.1153 229 HOH   B O   
7055 O  O   . HOH   G .   ? 0.4840 0.4128 0.2897 0.0270  0.0307  -0.0860 230 HOH   B O   
7056 O  O   . HOH   G .   ? 0.2585 0.2261 0.2576 0.0839  -0.0898 -0.0788 231 HOH   B O   
7057 O  O   . HOH   G .   ? 0.3541 0.2399 0.4265 0.0291  -0.0743 -0.1304 232 HOH   B O   
7058 O  O   . HOH   G .   ? 0.3296 0.2752 0.2911 -0.0656 0.0196  -0.0492 233 HOH   B O   
7059 O  O   . HOH   G .   ? 0.5075 0.7382 0.4584 0.3105  0.0418  0.0377  234 HOH   B O   
7060 O  O   . HOH   G .   ? 0.2430 0.4042 0.3319 -0.0466 -0.0753 -0.0957 235 HOH   B O   
7061 O  O   . HOH   G .   ? 0.6828 0.4811 0.3259 -0.1146 0.0037  0.0257  236 HOH   B O   
7062 O  O   . HOH   G .   ? 0.4952 0.2121 0.2904 0.0209  -0.0816 0.0091  237 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2611 0.4457 0.2965 -0.0981 -0.0447 -0.0642 238 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2429 0.2867 0.3144 -0.0823 0.0281  -0.0420 239 HOH   B O   
7065 O  O   . HOH   G .   ? 0.3969 0.4100 0.5270 -0.1591 -0.0532 0.1091  240 HOH   B O   
7066 O  O   . HOH   G .   ? 0.3649 0.3069 0.2145 0.0292  0.0569  0.0372  241 HOH   B O   
7067 O  O   . HOH   G .   ? 0.3911 0.1858 0.1796 0.0381  -0.0899 -0.0042 242 HOH   B O   
7068 O  O   . HOH   G .   ? 0.2118 0.3687 0.2372 -0.0346 -0.0060 0.0584  243 HOH   B O   
7069 O  O   . HOH   G .   ? 0.2167 0.1325 0.3191 0.0121  -0.0611 -0.0172 244 HOH   B O   
7070 O  O   . HOH   G .   ? 0.2888 0.3162 0.2684 -0.0992 0.0230  -0.0317 245 HOH   B O   
7071 O  O   . HOH   G .   ? 0.2636 0.2653 0.3059 0.0240  0.0442  -0.0933 246 HOH   B O   
7072 O  O   . HOH   G .   ? 0.2433 0.3866 0.5474 0.0984  -0.0491 -0.0803 247 HOH   B O   
7073 O  O   . HOH   G .   ? 0.5480 0.2965 0.3784 -0.2172 0.0307  0.0056  248 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2814 0.2437 0.2822 0.0805  0.0709  0.0031  249 HOH   B O   
7075 O  O   . HOH   G .   ? 0.5613 0.5042 0.4828 0.1094  0.0412  -0.0607 250 HOH   B O   
7076 O  O   . HOH   G .   ? 0.1461 0.1451 0.1431 -0.0118 -0.0029 0.0045  251 HOH   B O   
7077 O  O   . HOH   G .   ? 0.1658 0.1381 0.5148 -0.0103 -0.0287 -0.0170 252 HOH   B O   
7078 O  O   . HOH   G .   ? 0.2370 0.3238 0.2069 -0.0735 0.0042  0.0561  253 HOH   B O   
7079 O  O   . HOH   G .   ? 0.3319 0.4142 0.2842 -0.0134 -0.0768 0.0427  254 HOH   B O   
7080 O  O   . HOH   G .   ? 0.2104 0.1982 0.2012 -0.0263 -0.0468 0.0138  255 HOH   B O   
7081 O  O   . HOH   G .   ? 0.1542 0.1289 0.1514 0.0012  -0.0055 0.0075  256 HOH   B O   
7082 O  O   . HOH   G .   ? 0.3418 0.3618 0.4950 0.1058  -0.0320 -0.0869 257 HOH   B O   
7083 O  O   . HOH   G .   ? 0.3710 0.4886 0.6483 0.0384  0.0599  -0.0467 258 HOH   B O   
7084 O  O   . HOH   G .   ? 0.4103 0.3467 0.2207 0.0220  0.0975  -0.0105 259 HOH   B O   
7085 O  O   . HOH   G .   ? 0.1603 0.1396 0.2688 -0.0146 0.0088  -0.0130 260 HOH   B O   
7086 O  O   . HOH   G .   ? 0.2792 0.2202 0.1918 0.0174  -0.0153 -0.0135 261 HOH   B O   
7087 O  O   . HOH   G .   ? 0.2168 0.1966 0.4720 0.0212  -0.0714 -0.0688 262 HOH   B O   
7088 O  O   . HOH   G .   ? 0.2148 0.1543 0.2179 -0.0334 -0.0120 0.0215  263 HOH   B O   
7089 O  O   . HOH   G .   ? 0.1640 0.1782 0.3084 -0.0313 -0.0116 0.0121  264 HOH   B O   
7090 O  O   . HOH   G .   ? 0.4281 0.2028 0.2597 0.1233  0.0502  0.0192  265 HOH   B O   
7091 O  O   . HOH   G .   ? 0.2258 0.1477 0.2028 -0.0316 -0.0475 0.0237  266 HOH   B O   
7092 O  O   . HOH   G .   ? 0.2934 0.3693 0.3526 0.0328  0.1326  0.0285  267 HOH   B O   
7093 O  O   . HOH   G .   ? 0.1355 0.1617 0.2162 -0.0097 -0.0001 0.0214  268 HOH   B O   
7094 O  O   . HOH   G .   ? 0.3101 0.4965 0.6815 -0.0090 -0.0177 -0.1428 269 HOH   B O   
7095 O  O   . HOH   G .   ? 0.4222 0.4963 0.4170 0.0186  -0.1482 -0.0025 270 HOH   B O   
7096 O  O   . HOH   G .   ? 0.5478 0.5718 0.3100 0.0864  0.0410  0.0282  271 HOH   B O   
7097 O  O   . HOH   G .   ? 0.2304 0.5443 0.4465 -0.0463 -0.0494 -0.1085 272 HOH   B O   
7098 O  O   . HOH   G .   ? 0.2392 0.2207 0.1728 0.0155  0.0054  -0.0058 273 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2413 0.2771 0.2315 -0.0206 -0.0806 0.0121  274 HOH   B O   
7100 O  O   . HOH   G .   ? 0.2239 0.2600 0.2296 0.0606  -0.0282 -0.0098 275 HOH   B O   
7101 O  O   . HOH   G .   ? 0.2361 0.2906 0.2063 -0.0538 -0.0768 -0.0283 276 HOH   B O   
7102 O  O   . HOH   G .   ? 0.2640 0.1941 0.2883 -0.0594 0.0418  -0.0019 277 HOH   B O   
7103 O  O   . HOH   G .   ? 0.1906 0.1756 0.1752 -0.0462 -0.0481 0.0118  278 HOH   B O   
7104 O  O   . HOH   G .   ? 0.3960 0.2427 0.4429 -0.0295 -0.0673 -0.0669 279 HOH   B O   
7105 O  O   . HOH   G .   ? 0.3568 0.2433 0.1938 0.0466  -0.0799 -0.0088 280 HOH   B O   
7106 O  O   . HOH   G .   ? 0.2258 0.3435 0.3190 -0.0431 0.0419  -0.1225 281 HOH   B O   
7107 O  O   . HOH   G .   ? 0.3877 0.2068 0.3794 -0.0707 -0.2007 0.0706  282 HOH   B O   
7108 O  O   . HOH   G .   ? 0.3269 0.4226 0.7174 -0.0877 -0.0676 -0.0499 283 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5430 0.6713 0.2800 -0.0452 -0.1249 -0.0105 284 HOH   B O   
7110 O  O   . HOH   G .   ? 0.3231 0.2070 0.4754 0.0194  0.0631  0.0233  285 HOH   B O   
7111 O  O   . HOH   G .   ? 0.1668 0.1531 0.3509 -0.0198 0.0069  -0.0070 286 HOH   B O   
7112 O  O   . HOH   G .   ? 0.2802 0.4695 0.5466 -0.1233 -0.1500 0.0841  287 HOH   B O   
7113 O  O   . HOH   G .   ? 0.1624 0.2081 0.1540 -0.0181 -0.0208 0.0083  288 HOH   B O   
7114 O  O   . HOH   G .   ? 0.1707 0.1544 0.1776 0.0043  0.0158  0.0034  289 HOH   B O   
7115 O  O   . HOH   G .   ? 0.2416 0.2593 0.3035 0.0215  -0.0692 0.0271  290 HOH   B O   
7116 O  O   . HOH   G .   ? 0.2812 0.6090 0.7947 0.1538  -0.0497 -0.1235 291 HOH   B O   
7117 O  O   . HOH   G .   ? 0.4632 0.3575 0.3880 -0.0980 0.0937  -0.0663 292 HOH   B O   
7118 O  O   . HOH   G .   ? 0.1800 0.1987 0.2924 0.0151  0.0091  0.0026  293 HOH   B O   
7119 O  O   . HOH   G .   ? 0.6179 0.4720 0.5182 0.2399  -0.0206 0.0426  294 HOH   B O   
7120 O  O   . HOH   G .   ? 0.6269 0.3837 0.2851 0.2702  0.1072  0.0741  295 HOH   B O   
7121 O  O   . HOH   G .   ? 0.4202 0.3718 0.2277 0.0587  -0.0772 0.0814  296 HOH   B O   
7122 O  O   . HOH   G .   ? 0.1675 0.1485 0.3350 0.0105  0.0080  -0.0031 297 HOH   B O   
7123 O  O   . HOH   G .   ? 0.2349 0.1755 0.2507 -0.0315 -0.0121 -0.0122 298 HOH   B O   
7124 O  O   . HOH   G .   ? 0.5645 0.3633 0.4644 -0.0385 0.1681  -0.1614 299 HOH   B O   
7125 O  O   . HOH   G .   ? 0.3331 0.2993 0.2666 -0.0500 0.0291  -0.1303 300 HOH   B O   
7126 O  O   . HOH   G .   ? 0.1736 0.3596 0.5034 0.0098  -0.0105 -0.1818 301 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4584 0.5021 0.2448 -0.0020 0.1185  0.0998  302 HOH   B O   
7128 O  O   . HOH   G .   ? 0.2210 0.3333 0.5913 0.0886  -0.0539 -0.1472 303 HOH   B O   
7129 O  O   . HOH   G .   ? 0.1803 0.1622 0.2472 0.0162  0.0059  0.0311  304 HOH   B O   
7130 O  O   . HOH   G .   ? 0.3128 0.2817 0.5132 -0.0440 -0.0539 0.1164  305 HOH   B O   
7131 O  O   . HOH   G .   ? 0.2847 0.5933 0.2131 0.1206  -0.0396 -0.0678 306 HOH   B O   
7132 O  O   . HOH   G .   ? 0.2006 0.3092 0.4898 -0.0003 -0.0748 -0.0220 307 HOH   B O   
7133 O  O   . HOH   G .   ? 0.2160 0.1559 0.3315 0.0418  -0.0967 -0.0067 308 HOH   B O   
7134 O  O   . HOH   G .   ? 0.3670 0.2025 0.2871 0.1093  0.0737  0.0190  309 HOH   B O   
7135 O  O   . HOH   G .   ? 0.4999 0.3890 0.2727 0.0397  -0.0128 -0.0551 310 HOH   B O   
7136 O  O   . HOH   G .   ? 0.3484 0.4448 0.4038 -0.1525 0.1371  -0.0784 311 HOH   B O   
7137 O  O   . HOH   G .   ? 0.2283 0.1957 0.1813 -0.0169 0.0219  0.0093  312 HOH   B O   
7138 O  O   . HOH   G .   ? 0.2961 0.1866 0.3477 0.0608  0.0929  0.0432  313 HOH   B O   
7139 O  O   . HOH   G .   ? 0.4265 0.2748 0.2356 -0.1707 0.0716  -0.0259 314 HOH   B O   
7140 O  O   . HOH   G .   ? 0.2606 0.1545 0.2655 -0.0217 -0.0302 0.0390  315 HOH   B O   
7141 O  O   . HOH   G .   ? 0.6438 0.4735 0.6279 0.1415  0.2064  0.0023  316 HOH   B O   
7142 O  O   . HOH   G .   ? 0.3195 0.3119 0.3701 -0.0705 0.1397  -0.1142 317 HOH   B O   
7143 O  O   . HOH   G .   ? 0.2343 0.5530 0.5385 -0.0684 0.0111  0.0212  318 HOH   B O   
7144 O  O   . HOH   G .   ? 0.4279 0.3639 0.1918 0.0865  -0.0576 -0.0095 319 HOH   B O   
7145 O  O   . HOH   G .   ? 0.3462 0.7383 0.3820 0.1215  -0.0879 0.0085  320 HOH   B O   
7146 O  O   . HOH   G .   ? 0.1608 0.1913 0.2764 -0.0306 -0.0070 0.0006  321 HOH   B O   
7147 O  O   . HOH   G .   ? 0.1651 0.2572 0.2217 -0.0158 -0.0173 0.0610  322 HOH   B O   
7148 O  O   . HOH   G .   ? 0.3209 0.2342 0.2332 0.0277  -0.0296 0.0305  323 HOH   B O   
7149 O  O   . HOH   G .   ? 0.1621 0.1629 0.2978 -0.0177 -0.0076 -0.0170 324 HOH   B O   
7150 O  O   . HOH   G .   ? 0.5132 0.3660 0.5907 0.1035  0.0153  0.0593  325 HOH   B O   
7151 O  O   . HOH   G .   ? 0.2889 0.3229 0.5947 -0.0772 -0.1936 0.1789  326 HOH   B O   
7152 O  O   . HOH   G .   ? 0.5705 0.3771 0.4017 0.0500  0.1605  0.1478  327 HOH   B O   
7153 O  O   . HOH   G .   ? 0.2712 0.1936 0.4926 0.0009  -0.0104 0.0289  328 HOH   B O   
7154 O  O   . HOH   G .   ? 0.1782 0.1897 0.2814 0.0319  0.0318  0.0267  329 HOH   B O   
7155 O  O   . HOH   G .   ? 0.5567 0.5681 0.7057 0.2074  -0.1058 0.2084  330 HOH   B O   
7156 O  O   . HOH   G .   ? 0.5038 0.3434 0.5640 0.1561  0.2561  0.1974  331 HOH   B O   
7157 O  O   . HOH   G .   ? 0.2154 0.2436 0.5526 -0.0547 -0.0093 0.1395  332 HOH   B O   
7158 O  O   . HOH   G .   ? 0.5604 0.5509 0.5140 -0.1088 -0.1066 0.1520  333 HOH   B O   
7159 O  O   . HOH   G .   ? 0.1990 0.2973 0.3144 0.0596  -0.0107 -0.0780 334 HOH   B O   
7160 O  O   . HOH   G .   ? 0.4293 0.4234 0.4504 -0.0108 0.0837  0.0939  335 HOH   B O   
7161 O  O   . HOH   G .   ? 0.8613 0.2365 0.3310 0.0371  -0.1088 -0.0107 336 HOH   B O   
7162 O  O   . HOH   G .   ? 0.1782 0.1481 0.2353 0.0071  -0.0209 0.0077  337 HOH   B O   
7163 O  O   . HOH   G .   ? 0.6853 0.4304 0.6114 -0.1097 -0.1222 -0.1241 338 HOH   B O   
7164 O  O   . HOH   G .   ? 0.3758 0.4303 0.9067 -0.0170 -0.1090 0.2251  339 HOH   B O   
7165 O  O   . HOH   G .   ? 0.2460 0.1838 0.3689 0.0318  -0.0732 -0.0503 340 HOH   B O   
7166 O  O   . HOH   G .   ? 0.4340 0.7118 0.3765 -0.0824 -0.0955 0.1958  341 HOH   B O   
7167 O  O   . HOH   G .   ? 0.5007 0.5811 0.3461 0.0329  -0.1057 0.0611  342 HOH   B O   
7168 O  O   . HOH   G .   ? 0.4724 0.2502 0.4103 0.0528  0.0613  0.0856  343 HOH   B O   
7169 O  O   . HOH   G .   ? 0.5206 0.3511 0.2980 0.0794  -0.1216 -0.0591 344 HOH   B O   
7170 O  O   . HOH   G .   ? 0.7587 0.6188 0.4008 0.0789  -0.0685 0.2076  345 HOH   B O   
7171 O  O   . HOH   G .   ? 0.4531 0.5413 0.3933 -0.1329 -0.0916 -0.0660 346 HOH   B O   
7172 O  O   . HOH   G .   ? 0.2091 0.1965 0.3410 -0.0179 0.0630  -0.0144 347 HOH   B O   
7173 O  O   . HOH   G .   ? 0.3072 0.4996 0.5345 -0.1422 0.0295  -0.0263 348 HOH   B O   
7174 O  O   . HOH   G .   ? 0.4379 0.6614 0.5875 0.0162  -0.1084 0.0243  349 HOH   B O   
7175 O  O   . HOH   G .   ? 0.5732 0.5733 0.5962 -0.1267 0.0826  0.1592  350 HOH   B O   
7176 O  O   . HOH   G .   ? 0.4901 0.6214 0.7559 0.0474  0.1531  -0.0181 351 HOH   B O   
7177 O  O   . HOH   G .   ? 0.3347 0.2232 0.4584 -0.0369 -0.0859 -0.0477 352 HOH   B O   
7178 O  O   . HOH   G .   ? 0.2191 0.5994 0.2935 0.1344  -0.0573 -0.1264 353 HOH   B O   
7179 O  O   . HOH   G .   ? 0.4088 0.2210 0.3815 -0.0992 0.0793  -0.1035 354 HOH   B O   
7180 O  O   . HOH   G .   ? 0.4495 0.5348 0.4873 0.1546  -0.1018 0.1491  355 HOH   B O   
7181 O  O   . HOH   G .   ? 0.5345 0.2644 0.5549 -0.0953 0.1812  0.0453  356 HOH   B O   
7182 O  O   . HOH   G .   ? 0.2385 0.4095 0.5233 0.0030  0.0227  -0.0039 357 HOH   B O   
7183 O  O   . HOH   G .   ? 0.3728 0.2721 0.3830 -0.0732 -0.0597 -0.0382 358 HOH   B O   
7184 O  O   . HOH   G .   ? 0.4834 0.3664 0.4089 -0.0020 0.1322  -0.0544 359 HOH   B O   
7185 O  O   . HOH   G .   ? 0.5919 0.3668 0.5338 0.0417  -0.1495 -0.0806 360 HOH   B O   
7186 O  O   . HOH   G .   ? 0.5054 0.4052 0.6430 0.0372  0.1103  0.1362  361 HOH   B O   
7187 O  O   . HOH   G .   ? 0.2218 0.4185 0.6402 -0.0902 -0.0804 -0.0622 362 HOH   B O   
7188 O  O   . HOH   G .   ? 0.4304 0.5001 0.4457 0.1910  -0.0257 0.0276  363 HOH   B O   
7189 O  O   . HOH   G .   ? 0.6659 0.2474 0.3161 -0.0090 0.0181  0.0728  364 HOH   B O   
7190 O  O   . HOH   G .   ? 0.5300 0.4920 0.4964 0.0613  -0.0070 0.0634  365 HOH   B O   
7191 O  O   . HOH   G .   ? 0.4976 0.5927 0.4965 -0.0546 -0.0037 -0.1210 366 HOH   B O   
7192 O  O   . HOH   G .   ? 0.5833 0.7201 0.3666 0.2045  -0.1148 0.1434  367 HOH   B O   
7193 O  O   . HOH   G .   ? 0.3251 0.3442 0.5718 0.0607  -0.1830 -0.0059 368 HOH   B O   
7194 O  O   . HOH   G .   ? 0.6879 0.5259 0.4366 0.1934  0.0975  0.1142  369 HOH   B O   
7195 O  O   . HOH   G .   ? 0.4205 0.6380 0.5215 0.2737  0.1254  0.1754  370 HOH   B O   
7196 O  O   . HOH   G .   ? 0.7313 0.3738 0.2920 -0.1001 -0.1163 -0.0567 371 HOH   B O   
7197 O  O   . HOH   G .   ? 0.4906 0.3024 0.3279 0.0447  -0.1147 0.0002  372 HOH   B O   
7198 O  O   . HOH   G .   ? 0.4858 0.2972 0.6410 -0.1173 0.0048  0.0115  373 HOH   B O   
7199 O  O   . HOH   G .   ? 0.3972 0.6323 0.5694 0.0567  -0.0417 0.0193  374 HOH   B O   
7200 O  O   . HOH   G .   ? 0.3813 0.4995 0.4413 -0.0564 -0.0259 0.0236  375 HOH   B O   
7201 O  O   . HOH   G .   ? 0.8600 0.8677 0.6182 0.2573  -0.1344 -0.0230 376 HOH   B O   
7202 O  O   . HOH   G .   ? 0.2351 0.3623 0.4415 0.0160  -0.0364 -0.0772 377 HOH   B O   
7203 O  O   . HOH   G .   ? 0.4053 0.6402 0.2249 -0.0949 -0.0290 -0.0040 378 HOH   B O   
7204 O  O   . HOH   G .   ? 0.4298 0.7833 0.5662 0.1505  -0.0096 0.2265  379 HOH   B O   
7205 O  O   . HOH   G .   ? 0.4999 0.7616 0.3932 -0.1338 0.0038  -0.1412 380 HOH   B O   
7206 O  O   . HOH   G .   ? 0.6361 0.3694 0.5714 -0.0815 -0.1274 0.0153  381 HOH   B O   
7207 O  O   . HOH   G .   ? 0.5544 0.7208 0.7109 -0.0674 0.2573  0.1096  382 HOH   B O   
7208 O  O   . HOH   G .   ? 0.4660 0.8828 0.6024 0.1661  0.1869  0.1102  383 HOH   B O   
7209 O  O   . HOH   G .   ? 0.2842 0.2649 0.2963 0.0138  0.0052  0.0080  384 HOH   B O   
7210 O  O   . HOH   G .   ? 0.7532 0.3857 0.4312 -0.0005 0.0908  -0.1295 385 HOH   B O   
7211 O  O   . HOH   G .   ? 0.6436 0.4113 0.6159 -0.1045 0.0341  0.0127  386 HOH   B O   
7212 O  O   . HOH   G .   ? 0.5303 0.4587 0.3604 0.0130  0.1015  -0.0387 387 HOH   B O   
7213 O  O   . HOH   G .   ? 0.4544 0.3270 0.4954 -0.1706 0.0130  0.0572  388 HOH   B O   
7214 O  O   . HOH   G .   ? 0.7489 0.5278 0.3858 0.2113  0.0466  0.0058  389 HOH   B O   
7215 O  O   . HOH   G .   ? 0.2498 0.4057 0.4142 -0.0574 -0.1098 -0.0256 390 HOH   B O   
7216 O  O   . HOH   G .   ? 0.4150 0.2343 0.3274 0.0825  -0.0407 0.0128  391 HOH   B O   
7217 O  O   . HOH   G .   ? 0.5714 0.4504 0.5812 0.0861  0.1083  0.0220  392 HOH   B O   
7218 O  O   . HOH   G .   ? 0.4105 0.2157 0.5199 -0.0522 -0.0115 0.0764  393 HOH   B O   
7219 O  O   . HOH   G .   ? 0.2361 0.5538 0.6414 -0.1498 -0.0717 -0.0289 394 HOH   B O   
7220 O  O   . HOH   G .   ? 0.3345 0.4264 0.4066 -0.0319 0.0553  -0.1094 395 HOH   B O   
7221 O  O   . HOH   G .   ? 0.3974 0.7161 0.3965 0.0542  -0.0121 -0.1284 396 HOH   B O   
7222 O  O   . HOH   G .   ? 0.2192 0.2681 0.6337 -0.0615 -0.0849 0.0576  397 HOH   B O   
7223 O  O   . HOH   G .   ? 0.4281 0.4936 0.3632 -0.0150 0.0375  0.0418  398 HOH   B O   
7224 O  O   . HOH   G .   ? 0.5484 0.6213 0.6519 0.1054  -0.1200 0.2764  399 HOH   B O   
7225 O  O   . HOH   G .   ? 0.5269 0.3848 0.2992 -0.1799 -0.0716 0.0919  400 HOH   B O   
7226 O  O   . HOH   G .   ? 0.5863 0.5881 0.3634 0.1540  -0.0050 -0.0378 401 HOH   B O   
# 
