data_7HFK
# 
_entry.id   7HFK 
# 
_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   7HFK         pdb_00007hfk 10.2210/pdb7hfk/pdb 
WWPDB D_1001407410 ?            ?                   
# 
_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                        7HFK 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                    18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 
'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' 248.281   1   ?                      ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                35.453    1   ?                      ? ? ? 
4 water       nat water                                                         18.015    407 ?                      ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' A1BBL 
3 'CHLORIDE ION'                                                CL    
4 water                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BBL non-polymer         . '4-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' ? 'C12 H16 N4 O2'  248.281 
ALA   'L-peptide linking' y ALANINE                                                       ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                      ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                    ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                               ? 'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                      ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                     ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                               ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                       ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                     ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                         ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                        ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                    ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                 ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                       ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                        ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                     ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                      ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                        ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BBL 1   201 201  A1BBL LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 1289 HOH   HOH A . 
E 4 HOH   2   302 229  HOH   HOH A . 
E 4 HOH   3   303 196  HOH   HOH A . 
E 4 HOH   4   304 292  HOH   HOH A . 
E 4 HOH   5   305 93   HOH   HOH A . 
E 4 HOH   6   306 625  HOH   HOH A . 
E 4 HOH   7   307 1301 HOH   HOH A . 
E 4 HOH   8   308 247  HOH   HOH A . 
E 4 HOH   9   309 1310 HOH   HOH A . 
E 4 HOH   10  310 109  HOH   HOH A . 
E 4 HOH   11  311 409  HOH   HOH A . 
E 4 HOH   12  312 86   HOH   HOH A . 
E 4 HOH   13  313 209  HOH   HOH A . 
E 4 HOH   14  314 192  HOH   HOH A . 
E 4 HOH   15  315 136  HOH   HOH A . 
E 4 HOH   16  316 661  HOH   HOH A . 
E 4 HOH   17  317 124  HOH   HOH A . 
E 4 HOH   18  318 76   HOH   HOH A . 
E 4 HOH   19  319 493  HOH   HOH A . 
E 4 HOH   20  320 36   HOH   HOH A . 
E 4 HOH   21  321 469  HOH   HOH A . 
E 4 HOH   22  322 105  HOH   HOH A . 
E 4 HOH   23  323 1295 HOH   HOH A . 
E 4 HOH   24  324 164  HOH   HOH A . 
E 4 HOH   25  325 18   HOH   HOH A . 
E 4 HOH   26  326 393  HOH   HOH A . 
E 4 HOH   27  327 1290 HOH   HOH A . 
E 4 HOH   28  328 218  HOH   HOH A . 
E 4 HOH   29  329 15   HOH   HOH A . 
E 4 HOH   30  330 225  HOH   HOH A . 
E 4 HOH   31  331 165  HOH   HOH A . 
E 4 HOH   32  332 21   HOH   HOH A . 
E 4 HOH   33  333 155  HOH   HOH A . 
E 4 HOH   34  334 140  HOH   HOH A . 
E 4 HOH   35  335 964  HOH   HOH A . 
E 4 HOH   36  336 56   HOH   HOH A . 
E 4 HOH   37  337 153  HOH   HOH A . 
E 4 HOH   38  338 39   HOH   HOH A . 
E 4 HOH   39  339 320  HOH   HOH A . 
E 4 HOH   40  340 630  HOH   HOH A . 
E 4 HOH   41  341 241  HOH   HOH A . 
E 4 HOH   42  342 939  HOH   HOH A . 
E 4 HOH   43  343 42   HOH   HOH A . 
E 4 HOH   44  344 33   HOH   HOH A . 
E 4 HOH   45  345 17   HOH   HOH A . 
E 4 HOH   46  346 236  HOH   HOH A . 
E 4 HOH   47  347 337  HOH   HOH A . 
E 4 HOH   48  348 1300 HOH   HOH A . 
E 4 HOH   49  349 1094 HOH   HOH A . 
E 4 HOH   50  350 662  HOH   HOH A . 
E 4 HOH   51  351 1313 HOH   HOH A . 
E 4 HOH   52  352 199  HOH   HOH A . 
E 4 HOH   53  353 354  HOH   HOH A . 
E 4 HOH   54  354 92   HOH   HOH A . 
E 4 HOH   55  355 396  HOH   HOH A . 
E 4 HOH   56  356 1283 HOH   HOH A . 
E 4 HOH   57  357 151  HOH   HOH A . 
E 4 HOH   58  358 66   HOH   HOH A . 
E 4 HOH   59  359 1308 HOH   HOH A . 
E 4 HOH   60  360 2    HOH   HOH A . 
E 4 HOH   61  361 26   HOH   HOH A . 
E 4 HOH   62  362 5    HOH   HOH A . 
E 4 HOH   63  363 102  HOH   HOH A . 
E 4 HOH   64  364 169  HOH   HOH A . 
E 4 HOH   65  365 19   HOH   HOH A . 
E 4 HOH   66  366 81   HOH   HOH A . 
E 4 HOH   67  367 45   HOH   HOH A . 
E 4 HOH   68  368 366  HOH   HOH A . 
E 4 HOH   69  369 27   HOH   HOH A . 
E 4 HOH   70  370 132  HOH   HOH A . 
E 4 HOH   71  371 57   HOH   HOH A . 
E 4 HOH   72  372 46   HOH   HOH A . 
E 4 HOH   73  373 3    HOH   HOH A . 
E 4 HOH   74  374 83   HOH   HOH A . 
E 4 HOH   75  375 162  HOH   HOH A . 
E 4 HOH   76  376 154  HOH   HOH A . 
E 4 HOH   77  377 139  HOH   HOH A . 
E 4 HOH   78  378 138  HOH   HOH A . 
E 4 HOH   79  379 4    HOH   HOH A . 
E 4 HOH   80  380 35   HOH   HOH A . 
E 4 HOH   81  381 78   HOH   HOH A . 
E 4 HOH   82  382 49   HOH   HOH A . 
E 4 HOH   83  383 159  HOH   HOH A . 
E 4 HOH   84  384 186  HOH   HOH A . 
E 4 HOH   85  385 148  HOH   HOH A . 
E 4 HOH   86  386 461  HOH   HOH A . 
E 4 HOH   87  387 6    HOH   HOH A . 
E 4 HOH   88  388 116  HOH   HOH A . 
E 4 HOH   89  389 134  HOH   HOH A . 
E 4 HOH   90  390 296  HOH   HOH A . 
E 4 HOH   91  391 24   HOH   HOH A . 
E 4 HOH   92  392 381  HOH   HOH A . 
E 4 HOH   93  393 12   HOH   HOH A . 
E 4 HOH   94  394 278  HOH   HOH A . 
E 4 HOH   95  395 1309 HOH   HOH A . 
E 4 HOH   96  396 85   HOH   HOH A . 
E 4 HOH   97  397 96   HOH   HOH A . 
E 4 HOH   98  398 58   HOH   HOH A . 
E 4 HOH   99  399 67   HOH   HOH A . 
E 4 HOH   100 400 303  HOH   HOH A . 
E 4 HOH   101 401 351  HOH   HOH A . 
E 4 HOH   102 402 8    HOH   HOH A . 
E 4 HOH   103 403 74   HOH   HOH A . 
E 4 HOH   104 404 333  HOH   HOH A . 
E 4 HOH   105 405 125  HOH   HOH A . 
E 4 HOH   106 406 121  HOH   HOH A . 
E 4 HOH   107 407 1068 HOH   HOH A . 
E 4 HOH   108 408 68   HOH   HOH A . 
E 4 HOH   109 409 123  HOH   HOH A . 
E 4 HOH   110 410 195  HOH   HOH A . 
E 4 HOH   111 411 34   HOH   HOH A . 
E 4 HOH   112 412 7    HOH   HOH A . 
E 4 HOH   113 413 53   HOH   HOH A . 
E 4 HOH   114 414 25   HOH   HOH A . 
E 4 HOH   115 415 1315 HOH   HOH A . 
E 4 HOH   116 416 115  HOH   HOH A . 
E 4 HOH   117 417 1275 HOH   HOH A . 
E 4 HOH   118 418 95   HOH   HOH A . 
E 4 HOH   119 419 51   HOH   HOH A . 
E 4 HOH   120 420 281  HOH   HOH A . 
E 4 HOH   121 421 405  HOH   HOH A . 
E 4 HOH   122 422 122  HOH   HOH A . 
E 4 HOH   123 423 397  HOH   HOH A . 
E 4 HOH   124 424 212  HOH   HOH A . 
E 4 HOH   125 425 582  HOH   HOH A . 
E 4 HOH   126 426 1279 HOH   HOH A . 
E 4 HOH   127 427 156  HOH   HOH A . 
E 4 HOH   128 428 1222 HOH   HOH A . 
E 4 HOH   129 429 1286 HOH   HOH A . 
E 4 HOH   130 430 16   HOH   HOH A . 
E 4 HOH   131 431 70   HOH   HOH A . 
E 4 HOH   132 432 73   HOH   HOH A . 
E 4 HOH   133 433 80   HOH   HOH A . 
E 4 HOH   134 434 71   HOH   HOH A . 
E 4 HOH   135 435 94   HOH   HOH A . 
E 4 HOH   136 436 188  HOH   HOH A . 
E 4 HOH   137 437 944  HOH   HOH A . 
E 4 HOH   138 438 1238 HOH   HOH A . 
E 4 HOH   139 439 952  HOH   HOH A . 
E 4 HOH   140 440 40   HOH   HOH A . 
E 4 HOH   141 441 1189 HOH   HOH A . 
E 4 HOH   142 442 104  HOH   HOH A . 
E 4 HOH   143 443 1296 HOH   HOH A . 
E 4 HOH   144 444 97   HOH   HOH A . 
E 4 HOH   145 445 576  HOH   HOH A . 
E 4 HOH   146 446 79   HOH   HOH A . 
E 4 HOH   147 447 1134 HOH   HOH A . 
E 4 HOH   148 448 330  HOH   HOH A . 
E 4 HOH   149 449 1119 HOH   HOH A . 
E 4 HOH   150 450 509  HOH   HOH A . 
E 4 HOH   151 451 107  HOH   HOH A . 
E 4 HOH   152 452 408  HOH   HOH A . 
E 4 HOH   153 453 163  HOH   HOH A . 
E 4 HOH   154 454 726  HOH   HOH A . 
E 4 HOH   155 455 756  HOH   HOH A . 
E 4 HOH   156 456 280  HOH   HOH A . 
E 4 HOH   157 457 126  HOH   HOH A . 
E 4 HOH   158 458 319  HOH   HOH A . 
E 4 HOH   159 459 556  HOH   HOH A . 
E 4 HOH   160 460 361  HOH   HOH A . 
E 4 HOH   161 461 1307 HOH   HOH A . 
E 4 HOH   162 462 63   HOH   HOH A . 
E 4 HOH   163 463 801  HOH   HOH A . 
E 4 HOH   164 464 342  HOH   HOH A . 
E 4 HOH   165 465 370  HOH   HOH A . 
E 4 HOH   166 466 250  HOH   HOH A . 
E 4 HOH   167 467 1276 HOH   HOH A . 
E 4 HOH   168 468 135  HOH   HOH A . 
E 4 HOH   169 469 1306 HOH   HOH A . 
E 4 HOH   170 470 1287 HOH   HOH A . 
E 4 HOH   171 471 267  HOH   HOH A . 
E 4 HOH   172 472 224  HOH   HOH A . 
E 4 HOH   173 473 674  HOH   HOH A . 
E 4 HOH   174 474 521  HOH   HOH A . 
E 4 HOH   175 475 318  HOH   HOH A . 
E 4 HOH   176 476 919  HOH   HOH A . 
E 4 HOH   177 477 202  HOH   HOH A . 
E 4 HOH   178 478 695  HOH   HOH A . 
E 4 HOH   179 479 315  HOH   HOH A . 
E 4 HOH   180 480 331  HOH   HOH A . 
E 4 HOH   181 481 805  HOH   HOH A . 
E 4 HOH   182 482 711  HOH   HOH A . 
E 4 HOH   183 483 1314 HOH   HOH A . 
E 4 HOH   184 484 309  HOH   HOH A . 
E 4 HOH   185 485 981  HOH   HOH A . 
E 4 HOH   186 486 152  HOH   HOH A . 
E 4 HOH   187 487 1299 HOH   HOH A . 
E 4 HOH   188 488 941  HOH   HOH A . 
E 4 HOH   189 489 263  HOH   HOH A . 
E 4 HOH   190 490 208  HOH   HOH A . 
E 4 HOH   191 491 180  HOH   HOH A . 
E 4 HOH   192 492 1071 HOH   HOH A . 
E 4 HOH   193 493 363  HOH   HOH A . 
E 4 HOH   194 494 356  HOH   HOH A . 
E 4 HOH   195 495 1284 HOH   HOH A . 
E 4 HOH   196 496 326  HOH   HOH A . 
E 4 HOH   197 497 371  HOH   HOH A . 
E 4 HOH   198 498 313  HOH   HOH A . 
E 4 HOH   199 499 376  HOH   HOH A . 
E 4 HOH   200 500 185  HOH   HOH A . 
E 4 HOH   201 501 429  HOH   HOH A . 
E 4 HOH   202 502 772  HOH   HOH A . 
E 4 HOH   203 503 1074 HOH   HOH A . 
E 4 HOH   204 504 1292 HOH   HOH A . 
E 4 HOH   205 505 346  HOH   HOH A . 
E 4 HOH   206 506 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 240  HOH   HOH B . 
F 4 HOH   4   204 205  HOH   HOH B . 
F 4 HOH   5   205 398  HOH   HOH B . 
F 4 HOH   6   206 758  HOH   HOH B . 
F 4 HOH   7   207 364  HOH   HOH B . 
F 4 HOH   8   208 50   HOH   HOH B . 
F 4 HOH   9   209 172  HOH   HOH B . 
F 4 HOH   10  210 1249 HOH   HOH B . 
F 4 HOH   11  211 120  HOH   HOH B . 
F 4 HOH   12  212 353  HOH   HOH B . 
F 4 HOH   13  213 900  HOH   HOH B . 
F 4 HOH   14  214 358  HOH   HOH B . 
F 4 HOH   15  215 332  HOH   HOH B . 
F 4 HOH   16  216 232  HOH   HOH B . 
F 4 HOH   17  217 75   HOH   HOH B . 
F 4 HOH   18  218 743  HOH   HOH B . 
F 4 HOH   19  219 416  HOH   HOH B . 
F 4 HOH   20  220 531  HOH   HOH B . 
F 4 HOH   21  221 264  HOH   HOH B . 
F 4 HOH   22  222 452  HOH   HOH B . 
F 4 HOH   23  223 444  HOH   HOH B . 
F 4 HOH   24  224 82   HOH   HOH B . 
F 4 HOH   25  225 654  HOH   HOH B . 
F 4 HOH   26  226 127  HOH   HOH B . 
F 4 HOH   27  227 54   HOH   HOH B . 
F 4 HOH   28  228 60   HOH   HOH B . 
F 4 HOH   29  229 1278 HOH   HOH B . 
F 4 HOH   30  230 723  HOH   HOH B . 
F 4 HOH   31  231 110  HOH   HOH B . 
F 4 HOH   32  232 300  HOH   HOH B . 
F 4 HOH   33  233 1140 HOH   HOH B . 
F 4 HOH   34  234 325  HOH   HOH B . 
F 4 HOH   35  235 131  HOH   HOH B . 
F 4 HOH   36  236 1    HOH   HOH B . 
F 4 HOH   37  237 69   HOH   HOH B . 
F 4 HOH   38  238 391  HOH   HOH B . 
F 4 HOH   39  239 166  HOH   HOH B . 
F 4 HOH   40  240 287  HOH   HOH B . 
F 4 HOH   41  241 133  HOH   HOH B . 
F 4 HOH   42  242 128  HOH   HOH B . 
F 4 HOH   43  243 343  HOH   HOH B . 
F 4 HOH   44  244 231  HOH   HOH B . 
F 4 HOH   45  245 129  HOH   HOH B . 
F 4 HOH   46  246 272  HOH   HOH B . 
F 4 HOH   47  247 14   HOH   HOH B . 
F 4 HOH   48  248 52   HOH   HOH B . 
F 4 HOH   49  249 150  HOH   HOH B . 
F 4 HOH   50  250 1312 HOH   HOH B . 
F 4 HOH   51  251 30   HOH   HOH B . 
F 4 HOH   52  252 9    HOH   HOH B . 
F 4 HOH   53  253 47   HOH   HOH B . 
F 4 HOH   54  254 144  HOH   HOH B . 
F 4 HOH   55  255 41   HOH   HOH B . 
F 4 HOH   56  256 72   HOH   HOH B . 
F 4 HOH   57  257 103  HOH   HOH B . 
F 4 HOH   58  258 271  HOH   HOH B . 
F 4 HOH   59  259 181  HOH   HOH B . 
F 4 HOH   60  260 347  HOH   HOH B . 
F 4 HOH   61  261 31   HOH   HOH B . 
F 4 HOH   62  262 221  HOH   HOH B . 
F 4 HOH   63  263 62   HOH   HOH B . 
F 4 HOH   64  264 143  HOH   HOH B . 
F 4 HOH   65  265 59   HOH   HOH B . 
F 4 HOH   66  266 276  HOH   HOH B . 
F 4 HOH   67  267 252  HOH   HOH B . 
F 4 HOH   68  268 1106 HOH   HOH B . 
F 4 HOH   69  269 243  HOH   HOH B . 
F 4 HOH   70  270 10   HOH   HOH B . 
F 4 HOH   71  271 20   HOH   HOH B . 
F 4 HOH   72  272 77   HOH   HOH B . 
F 4 HOH   73  273 242  HOH   HOH B . 
F 4 HOH   74  274 61   HOH   HOH B . 
F 4 HOH   75  275 147  HOH   HOH B . 
F 4 HOH   76  276 1277 HOH   HOH B . 
F 4 HOH   77  277 117  HOH   HOH B . 
F 4 HOH   78  278 11   HOH   HOH B . 
F 4 HOH   79  279 84   HOH   HOH B . 
F 4 HOH   80  280 302  HOH   HOH B . 
F 4 HOH   81  281 216  HOH   HOH B . 
F 4 HOH   82  282 114  HOH   HOH B . 
F 4 HOH   83  283 235  HOH   HOH B . 
F 4 HOH   84  284 1305 HOH   HOH B . 
F 4 HOH   85  285 22   HOH   HOH B . 
F 4 HOH   86  286 175  HOH   HOH B . 
F 4 HOH   87  287 99   HOH   HOH B . 
F 4 HOH   88  288 43   HOH   HOH B . 
F 4 HOH   89  289 299  HOH   HOH B . 
F 4 HOH   90  290 297  HOH   HOH B . 
F 4 HOH   91  291 106  HOH   HOH B . 
F 4 HOH   92  292 13   HOH   HOH B . 
F 4 HOH   93  293 282  HOH   HOH B . 
F 4 HOH   94  294 89   HOH   HOH B . 
F 4 HOH   95  295 207  HOH   HOH B . 
F 4 HOH   96  296 311  HOH   HOH B . 
F 4 HOH   97  297 88   HOH   HOH B . 
F 4 HOH   98  298 215  HOH   HOH B . 
F 4 HOH   99  299 316  HOH   HOH B . 
F 4 HOH   100 300 160  HOH   HOH B . 
F 4 HOH   101 301 112  HOH   HOH B . 
F 4 HOH   102 302 197  HOH   HOH B . 
F 4 HOH   103 303 137  HOH   HOH B . 
F 4 HOH   104 304 960  HOH   HOH B . 
F 4 HOH   105 305 118  HOH   HOH B . 
F 4 HOH   106 306 220  HOH   HOH B . 
F 4 HOH   107 307 1066 HOH   HOH B . 
F 4 HOH   108 308 32   HOH   HOH B . 
F 4 HOH   109 309 177  HOH   HOH B . 
F 4 HOH   110 310 101  HOH   HOH B . 
F 4 HOH   111 311 717  HOH   HOH B . 
F 4 HOH   112 312 23   HOH   HOH B . 
F 4 HOH   113 313 142  HOH   HOH B . 
F 4 HOH   114 314 170  HOH   HOH B . 
F 4 HOH   115 315 100  HOH   HOH B . 
F 4 HOH   116 316 1285 HOH   HOH B . 
F 4 HOH   117 317 1291 HOH   HOH B . 
F 4 HOH   118 318 37   HOH   HOH B . 
F 4 HOH   119 319 387  HOH   HOH B . 
F 4 HOH   120 320 44   HOH   HOH B . 
F 4 HOH   121 321 38   HOH   HOH B . 
F 4 HOH   122 322 91   HOH   HOH B . 
F 4 HOH   123 323 445  HOH   HOH B . 
F 4 HOH   124 324 48   HOH   HOH B . 
F 4 HOH   125 325 704  HOH   HOH B . 
F 4 HOH   126 326 141  HOH   HOH B . 
F 4 HOH   127 327 28   HOH   HOH B . 
F 4 HOH   128 328 635  HOH   HOH B . 
F 4 HOH   129 329 29   HOH   HOH B . 
F 4 HOH   130 330 55   HOH   HOH B . 
F 4 HOH   131 331 98   HOH   HOH B . 
F 4 HOH   132 332 182  HOH   HOH B . 
F 4 HOH   133 333 234  HOH   HOH B . 
F 4 HOH   134 334 161  HOH   HOH B . 
F 4 HOH   135 335 1274 HOH   HOH B . 
F 4 HOH   136 336 1294 HOH   HOH B . 
F 4 HOH   137 337 362  HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 1293 HOH   HOH B . 
F 4 HOH   140 340 334  HOH   HOH B . 
F 4 HOH   141 341 341  HOH   HOH B . 
F 4 HOH   142 342 178  HOH   HOH B . 
F 4 HOH   143 343 87   HOH   HOH B . 
F 4 HOH   144 344 619  HOH   HOH B . 
F 4 HOH   145 345 1126 HOH   HOH B . 
F 4 HOH   146 346 339  HOH   HOH B . 
F 4 HOH   147 347 90   HOH   HOH B . 
F 4 HOH   148 348 1280 HOH   HOH B . 
F 4 HOH   149 349 463  HOH   HOH B . 
F 4 HOH   150 350 1304 HOH   HOH B . 
F 4 HOH   151 351 191  HOH   HOH B . 
F 4 HOH   152 352 623  HOH   HOH B . 
F 4 HOH   153 353 1046 HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 304  HOH   HOH B . 
F 4 HOH   156 356 1077 HOH   HOH B . 
F 4 HOH   157 357 203  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 541  HOH   HOH B . 
F 4 HOH   160 360 718  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 291  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 479  HOH   HOH B . 
F 4 HOH   166 366 615  HOH   HOH B . 
F 4 HOH   167 367 340  HOH   HOH B . 
F 4 HOH   168 368 898  HOH   HOH B . 
F 4 HOH   169 369 1316 HOH   HOH B . 
F 4 HOH   170 370 310  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 190  HOH   HOH B . 
F 4 HOH   173 373 373  HOH   HOH B . 
F 4 HOH   174 374 1303 HOH   HOH B . 
F 4 HOH   175 375 431  HOH   HOH B . 
F 4 HOH   176 376 1173 HOH   HOH B . 
F 4 HOH   177 377 149  HOH   HOH B . 
F 4 HOH   178 378 418  HOH   HOH B . 
F 4 HOH   179 379 1163 HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 183  HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 424  HOH   HOH B . 
F 4 HOH   184 384 491  HOH   HOH B . 
F 4 HOH   185 385 1298 HOH   HOH B . 
F 4 HOH   186 386 176  HOH   HOH B . 
F 4 HOH   187 387 350  HOH   HOH B . 
F 4 HOH   188 388 470  HOH   HOH B . 
F 4 HOH   189 389 265  HOH   HOH B . 
F 4 HOH   190 390 248  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 410  HOH   HOH B . 
F 4 HOH   193 393 360  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 314  HOH   HOH B . 
F 4 HOH   196 396 157  HOH   HOH B . 
F 4 HOH   197 397 274  HOH   HOH B . 
F 4 HOH   198 398 566  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFK 
_cell.length_a           88.740 
_cell.length_b           88.740 
_cell.length_c           39.315 
_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                         7HFK 
_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          7HFK 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.32 
_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                     7HFK 
_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            0.990 
_reflns.number_obs                   169248 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.055 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.800 
_reflns.B_iso_Wilson_estimate        12.620 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.060 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1075690 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.990 1.010  ? 32586 7617 ? 1.552 ? ? ? 4.300 ? 0.700  ? ? ? ? ? ? 91.000 1.765 0.820 0.575 
1 2 5.420 44.370 ? 7660  1128 ? 0.047 ? ? ? 6.800 ? 40.200 ? ? ? ? ? ? 99.900 0.051 0.019 0.998 
# 
_refine.entry_id                                 7HFK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3700 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3600 
_refine.ls_number_reflns_obs                     169053 
_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                          0.1540 
_refine.ls_R_factor_R_work                       0.1532 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1699 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8148 
_refine.ls_number_reflns_R_work                  160905 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.7432 
_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                            0.1300 
_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                                80.980 
_refine.B_iso_min                                9.520 
_refine.pdbx_overall_phase_error                 22.5500 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        44.3700 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             407 
_refine_hist.number_atoms_total               2984 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           18.24 
_refine_hist.pdbx_B_iso_mean_solvent          32.14 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9900 1.0000  30 88.0000  4732 . 0.4648 0.4659 . 227 0.0000 4959 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 96.0000  5119 . 0.4078 0.3878 . 268 0.0000 5387 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5373 . 0.3597 0.3701 . 233 0.0000 5606 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5382 . 0.3427 0.3454 . 286 0.0000 5668 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5320 . 0.3120 0.3091 . 284 0.0000 5604 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5346 . 0.2764 0.2849 . 320 0.0000 5666 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5370 . 0.2488 0.2739 . 274 0.0000 5644 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5376 . 0.2240 0.2588 . 240 0.0000 5616 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5354 . 0.2045 0.2182 . 287 0.0000 5641 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5375 . 0.1802 0.2158 . 240 0.0000 5615 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5450 . 0.1743 0.1713 . 265 0.0000 5715 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5317 . 0.1585 0.1946 . 272 0.0000 5589 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5416 . 0.1532 0.2006 . 269 0.0000 5685 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5321 . 0.1432 0.1733 . 297 0.0000 5618 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5402 . 0.1448 0.1681 . 259 0.0000 5661 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5383 . 0.1469 0.1706 . 260 0.0000 5643 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5368 . 0.1418 0.1671 . 280 0.0000 5648 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5380 . 0.1453 0.1766 . 273 0.0000 5653 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5364 . 0.1414 0.1732 . 283 0.0000 5647 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5419 . 0.1340 0.1596 . 259 0.0000 5678 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5401 . 0.1279 0.1339 . 268 0.0000 5669 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5380 . 0.1237 0.1282 . 289 0.0000 5669 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5375 . 0.1249 0.1489 . 272 0.0000 5647 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5404 . 0.1316 0.1514 . 265 0.0000 5669 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5443 . 0.1429 0.1485 . 259 0.0000 5702 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5413 . 0.1362 0.1388 . 297 0.0000 5710 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5404 . 0.1425 0.1473 . 274 0.0000 5678 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5424 . 0.1386 0.1533 . 300 0.0000 5724 . 'X-RAY DIFFRACTION' 
2.4400 3.0700  30 100.0000 5490 . 0.1501 0.1758 . 278 0.0000 5768 . 'X-RAY DIFFRACTION' 
3.0800 44.3700 30 100.0000 5604 . 0.1502 0.1707 . 270 0.0000 5874 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFK 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004314' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFK 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFK A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFK 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 7HFK SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFK MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFK SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFK MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 39  ? VAL A 34  ALA A 39  
AA2 2 HIS A 91  ? VAL A 96  ? HIS A 91  VAL A 96  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFK 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HD1 A HIS 91  ? ? O A HOH 306 ? ? 1.58 
2 1 O   B HOH 220 ? ? O B HOH 302 ? ? 2.17 
# 
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  ? ? 55.81   -132.76 
2 1 SER A 128 ? B 70.88   -6.75   
3 1 PHE A 156 ? B -92.84  55.48   
4 1 ASP A 157 ? B -173.24 113.14  
5 1 HIS B 86  ? ? 58.09   -127.54 
# 
_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 504 ? 6.01 . 
2 1 O ? A HOH 505 ? 6.04 . 
3 1 O ? A HOH 506 ? 7.60 . 
4 1 O ? B HOH 401 ? 6.59 . 
# 
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 
A1BBL N2   N  Y N 1   
A1BBL C3   C  Y N 2   
A1BBL C6   C  Y N 3   
A1BBL C9   C  N N 4   
A1BBL C12  C  N N 5   
A1BBL C1   C  N N 6   
A1BBL C10  C  N N 7   
A1BBL C11  C  N N 8   
A1BBL C2   C  N N 9   
A1BBL C4   C  Y N 10  
A1BBL C5   C  Y N 11  
A1BBL C7   C  Y N 12  
A1BBL C8   C  Y N 13  
A1BBL N1   N  N N 14  
A1BBL N3   N  Y N 15  
A1BBL N4   N  Y N 16  
A1BBL O1   O  N N 17  
A1BBL O2   O  N N 18  
A1BBL H9   H  N N 19  
A1BBL H10  H  N N 20  
A1BBL H15  H  N N 21  
A1BBL H16  H  N N 22  
A1BBL H12  H  N N 23  
A1BBL H11  H  N N 24  
A1BBL H13  H  N N 25  
A1BBL H14  H  N N 26  
A1BBL H3   H  N N 27  
A1BBL H2   H  N N 28  
A1BBL H5   H  N N 29  
A1BBL H6   H  N N 30  
A1BBL H7   H  N N 31  
A1BBL H4   H  N N 32  
A1BBL H8   H  N N 33  
A1BBL H1   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
LEU   N    N  N N 218 
LEU   CA   C  N S 219 
LEU   C    C  N N 220 
LEU   O    O  N N 221 
LEU   CB   C  N N 222 
LEU   CG   C  N N 223 
LEU   CD1  C  N N 224 
LEU   CD2  C  N N 225 
LEU   OXT  O  N N 226 
LEU   H    H  N N 227 
LEU   H2   H  N N 228 
LEU   HA   H  N N 229 
LEU   HB2  H  N N 230 
LEU   HB3  H  N N 231 
LEU   HG   H  N N 232 
LEU   HD11 H  N N 233 
LEU   HD12 H  N N 234 
LEU   HD13 H  N N 235 
LEU   HD21 H  N N 236 
LEU   HD22 H  N N 237 
LEU   HD23 H  N N 238 
LEU   HXT  H  N N 239 
LYS   N    N  N N 240 
LYS   CA   C  N S 241 
LYS   C    C  N N 242 
LYS   O    O  N N 243 
LYS   CB   C  N N 244 
LYS   CG   C  N N 245 
LYS   CD   C  N N 246 
LYS   CE   C  N N 247 
LYS   NZ   N  N N 248 
LYS   OXT  O  N N 249 
LYS   H    H  N N 250 
LYS   H2   H  N N 251 
LYS   HA   H  N N 252 
LYS   HB2  H  N N 253 
LYS   HB3  H  N N 254 
LYS   HG2  H  N N 255 
LYS   HG3  H  N N 256 
LYS   HD2  H  N N 257 
LYS   HD3  H  N N 258 
LYS   HE2  H  N N 259 
LYS   HE3  H  N N 260 
LYS   HZ1  H  N N 261 
LYS   HZ2  H  N N 262 
LYS   HZ3  H  N N 263 
LYS   HXT  H  N N 264 
MET   N    N  N N 265 
MET   CA   C  N S 266 
MET   C    C  N N 267 
MET   O    O  N N 268 
MET   CB   C  N N 269 
MET   CG   C  N N 270 
MET   SD   S  N N 271 
MET   CE   C  N N 272 
MET   OXT  O  N N 273 
MET   H    H  N N 274 
MET   H2   H  N N 275 
MET   HA   H  N N 276 
MET   HB2  H  N N 277 
MET   HB3  H  N N 278 
MET   HG2  H  N N 279 
MET   HG3  H  N N 280 
MET   HE1  H  N N 281 
MET   HE2  H  N N 282 
MET   HE3  H  N N 283 
MET   HXT  H  N N 284 
PHE   N    N  N N 285 
PHE   CA   C  N S 286 
PHE   C    C  N N 287 
PHE   O    O  N N 288 
PHE   CB   C  N N 289 
PHE   CG   C  Y N 290 
PHE   CD1  C  Y N 291 
PHE   CD2  C  Y N 292 
PHE   CE1  C  Y N 293 
PHE   CE2  C  Y N 294 
PHE   CZ   C  Y N 295 
PHE   OXT  O  N N 296 
PHE   H    H  N N 297 
PHE   H2   H  N N 298 
PHE   HA   H  N N 299 
PHE   HB2  H  N N 300 
PHE   HB3  H  N N 301 
PHE   HD1  H  N N 302 
PHE   HD2  H  N N 303 
PHE   HE1  H  N N 304 
PHE   HE2  H  N N 305 
PHE   HZ   H  N N 306 
PHE   HXT  H  N N 307 
PRO   N    N  N N 308 
PRO   CA   C  N S 309 
PRO   C    C  N N 310 
PRO   O    O  N N 311 
PRO   CB   C  N N 312 
PRO   CG   C  N N 313 
PRO   CD   C  N N 314 
PRO   OXT  O  N N 315 
PRO   H    H  N N 316 
PRO   HA   H  N N 317 
PRO   HB2  H  N N 318 
PRO   HB3  H  N N 319 
PRO   HG2  H  N N 320 
PRO   HG3  H  N N 321 
PRO   HD2  H  N N 322 
PRO   HD3  H  N N 323 
PRO   HXT  H  N N 324 
SER   N    N  N N 325 
SER   CA   C  N S 326 
SER   C    C  N N 327 
SER   O    O  N N 328 
SER   CB   C  N N 329 
SER   OG   O  N N 330 
SER   OXT  O  N N 331 
SER   H    H  N N 332 
SER   H2   H  N N 333 
SER   HA   H  N N 334 
SER   HB2  H  N N 335 
SER   HB3  H  N N 336 
SER   HG   H  N N 337 
SER   HXT  H  N N 338 
THR   N    N  N N 339 
THR   CA   C  N S 340 
THR   C    C  N N 341 
THR   O    O  N N 342 
THR   CB   C  N R 343 
THR   OG1  O  N N 344 
THR   CG2  C  N N 345 
THR   OXT  O  N N 346 
THR   H    H  N N 347 
THR   H2   H  N N 348 
THR   HA   H  N N 349 
THR   HB   H  N N 350 
THR   HG1  H  N N 351 
THR   HG21 H  N N 352 
THR   HG22 H  N N 353 
THR   HG23 H  N N 354 
THR   HXT  H  N N 355 
TYR   N    N  N N 356 
TYR   CA   C  N S 357 
TYR   C    C  N N 358 
TYR   O    O  N N 359 
TYR   CB   C  N N 360 
TYR   CG   C  Y N 361 
TYR   CD1  C  Y N 362 
TYR   CD2  C  Y N 363 
TYR   CE1  C  Y N 364 
TYR   CE2  C  Y N 365 
TYR   CZ   C  Y N 366 
TYR   OH   O  N N 367 
TYR   OXT  O  N N 368 
TYR   H    H  N N 369 
TYR   H2   H  N N 370 
TYR   HA   H  N N 371 
TYR   HB2  H  N N 372 
TYR   HB3  H  N N 373 
TYR   HD1  H  N N 374 
TYR   HD2  H  N N 375 
TYR   HE1  H  N N 376 
TYR   HE2  H  N N 377 
TYR   HH   H  N N 378 
TYR   HXT  H  N N 379 
VAL   N    N  N N 380 
VAL   CA   C  N S 381 
VAL   C    C  N N 382 
VAL   O    O  N N 383 
VAL   CB   C  N N 384 
VAL   CG1  C  N N 385 
VAL   CG2  C  N N 386 
VAL   OXT  O  N N 387 
VAL   H    H  N N 388 
VAL   H2   H  N N 389 
VAL   HA   H  N N 390 
VAL   HB   H  N N 391 
VAL   HG11 H  N N 392 
VAL   HG12 H  N N 393 
VAL   HG13 H  N N 394 
VAL   HG21 H  N N 395 
VAL   HG22 H  N N 396 
VAL   HG23 H  N N 397 
VAL   HXT  H  N N 398 
# 
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 
A1BBL O2  C10  sing N N 1   
A1BBL O2  C11  sing N N 2   
A1BBL C10 C9   sing N N 3   
A1BBL C11 C12  sing N N 4   
A1BBL C9  C1   sing N N 5   
A1BBL C12 C1   sing N N 6   
A1BBL C1  C2   sing N N 7   
A1BBL C1  O1   sing N N 8   
A1BBL C2  N1   sing N N 9   
A1BBL N1  C3   sing N N 10  
A1BBL C3  C6   doub Y N 11  
A1BBL C3  N2   sing Y N 12  
A1BBL C7  C6   sing Y N 13  
A1BBL C7  C8   doub Y N 14  
A1BBL C6  C5   sing Y N 15  
A1BBL N2  C4   doub Y N 16  
A1BBL C8  N4   sing Y N 17  
A1BBL C4  N3   sing Y N 18  
A1BBL C5  N4   sing Y N 19  
A1BBL C5  N3   doub Y N 20  
A1BBL C9  H9   sing N N 21  
A1BBL C9  H10  sing N N 22  
A1BBL C12 H15  sing N N 23  
A1BBL C12 H16  sing N N 24  
A1BBL C10 H12  sing N N 25  
A1BBL C10 H11  sing N N 26  
A1BBL C11 H13  sing N N 27  
A1BBL C11 H14  sing N N 28  
A1BBL C2  H3   sing N N 29  
A1BBL C2  H2   sing N N 30  
A1BBL C4  H5   sing N N 31  
A1BBL C7  H6   sing N N 32  
A1BBL C8  H7   sing N N 33  
A1BBL N1  H4   sing N N 34  
A1BBL N4  H8   sing N N 35  
A1BBL O1  H1   sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TYR   N   CA   sing N N 342 
TYR   N   H    sing N N 343 
TYR   N   H2   sing N N 344 
TYR   CA  C    sing N N 345 
TYR   CA  CB   sing N N 346 
TYR   CA  HA   sing N N 347 
TYR   C   O    doub N N 348 
TYR   C   OXT  sing N N 349 
TYR   CB  CG   sing N N 350 
TYR   CB  HB2  sing N N 351 
TYR   CB  HB3  sing N N 352 
TYR   CG  CD1  doub Y N 353 
TYR   CG  CD2  sing Y N 354 
TYR   CD1 CE1  sing Y N 355 
TYR   CD1 HD1  sing N N 356 
TYR   CD2 CE2  doub Y N 357 
TYR   CD2 HD2  sing N N 358 
TYR   CE1 CZ   doub Y N 359 
TYR   CE1 HE1  sing N N 360 
TYR   CE2 CZ   sing Y N 361 
TYR   CE2 HE2  sing N N 362 
TYR   CZ  OH   sing N N 363 
TYR   OH  HH   sing N N 364 
TYR   OXT HXT  sing N N 365 
VAL   N   CA   sing N N 366 
VAL   N   H    sing N N 367 
VAL   N   H2   sing N N 368 
VAL   CA  C    sing N N 369 
VAL   CA  CB   sing N N 370 
VAL   CA  HA   sing N N 371 
VAL   C   O    doub N N 372 
VAL   C   OXT  sing N N 373 
VAL   CB  CG1  sing N N 374 
VAL   CB  CG2  sing N N 375 
VAL   CB  HB   sing N N 376 
VAL   CG1 HG11 sing N N 377 
VAL   CG1 HG12 sing N N 378 
VAL   CG1 HG13 sing N N 379 
VAL   CG2 HG21 sing N N 380 
VAL   CG2 HG22 sing N N 381 
VAL   CG2 HG23 sing N N 382 
VAL   OXT HXT  sing N N 383 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HFK 
_atom_sites.fract_transf_matrix[1][1]   0.011269 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011269 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025436 
_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   ? 19.668 -16.158 22.207  0.70 63.65 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.614 -16.131 22.284  0.30 62.56 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.680 -15.099 22.367  0.70 63.16 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.650 -15.052 22.460  0.30 62.23 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.313 -13.739 22.085  0.70 61.63 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.293 -13.711 22.129  0.30 61.04 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.397 -13.435 22.581  0.70 62.31 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.371 -13.392 22.630  0.30 61.56 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.039 -15.140 23.769  0.70 63.76 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.069 -15.048 23.887  0.30 62.74 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.019 -14.022 23.920  0.70 63.90 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.060 -13.920 24.046  0.30 62.86 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.389 -16.494 24.018  0.70 63.90 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.430 -16.391 24.207  0.30 62.87 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.972 -15.233 21.721  0.70 75.76 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.914 -15.187 21.846  0.30 74.63 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.728 -15.011 24.439  0.70 76.47 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.786 -14.900 24.523  0.30 75.24 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.500 -14.176 24.725  0.70 76.65 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.573 -14.047 24.875  0.30 75.40 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.485 -13.174 23.985  0.70 76.65 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.531 -13.073 24.067  0.30 75.40 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.434 -14.022 23.146  0.70 76.65 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.445 -13.940 23.296  0.30 75.40 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.937 -16.474 24.876  0.70 76.64 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.007 -16.340 25.078  0.30 75.41 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.749 -16.671 23.311  0.70 76.64 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.767 -16.594 23.529  0.30 75.41 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.076 -17.179 24.022  0.70 76.64 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.118 -17.075 24.213  0.30 75.41 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.628 -12.928 21.281  1.00 58.98 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.075 -11.583 20.943  1.00 53.87 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.944 -10.593 21.207  1.00 49.18 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.819 -10.975 21.543  1.00 49.25 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.625 -11.493 19.508  1.00 53.15 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.612 -11.896 18.461  1.00 52.36 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.463 -11.454 18.484  1.00 52.07 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.038 -12.742 17.527  1.00 52.16 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.880 -13.145 20.913  0.70 70.74 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.900 -13.163 20.884  0.30 70.74 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.803 -11.349 21.529  1.00 64.61 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.897 -10.578 19.330  1.00 63.74 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.392 -12.085 19.426  1.00 63.74 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.505 -13.001 16.905  1.00 62.56 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.849 -13.031 17.546  1.00 62.56 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.253 -9.306  21.057  0.70 46.61 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.254 -9.306  21.049  0.30 46.64 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.340 -8.235  21.438  0.70 43.97 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.353 -8.226  21.429  0.30 43.99 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.477 -7.738  20.283  0.70 40.48 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.489 -7.729  20.276  0.30 40.62 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.843 -6.685  20.412  0.70 40.38 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.864 -6.671  20.400  0.30 40.69 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.118 -7.066  22.049  0.70 44.80 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.142 -7.057  22.028  0.30 44.63 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.103 -6.582  21.154  0.70 45.27 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.078 -6.539  21.099  0.30 44.98 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.993 -9.025  20.725  0.70 55.90 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 18.992 -9.031  20.709  0.30 55.93 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.747 -8.572  22.126  0.70 52.73 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.758 -8.552  22.119  0.30 52.76 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.497 -6.346  22.252  0.70 53.72 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.521 -6.352  22.277  0.30 53.51 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.550 -7.367  22.864  0.70 53.72 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.617 -7.369  22.814  0.30 53.51 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.521 -5.943  21.506  0.70 54.29 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.501 -5.900  21.445  0.30 53.93 ?  5   SER   A HG   1 
ATOM   68   N  N    . PHE   A 1 6   ? 16.438 -8.456  19.163  1.00 37.12 ?  6   PHE   A N    1 
ATOM   69   C  CA   . PHE   A 1 6   ? 15.535 -8.087  18.082  1.00 30.63 ?  6   PHE   A CA   1 
ATOM   70   C  C    . PHE   A 1 6   ? 14.108 -8.459  18.464  1.00 29.75 ?  6   PHE   A C    1 
ATOM   71   O  O    . PHE   A 1 6   ? 13.856 -9.544  18.995  1.00 30.43 ?  6   PHE   A O    1 
ATOM   72   C  CB   . PHE   A 1 6   ? 15.928 -8.798  16.789  1.00 26.55 ?  6   PHE   A CB   1 
ATOM   73   C  CG   . PHE   A 1 6   ? 17.197 -8.275  16.169  1.00 23.50 ?  6   PHE   A CG   1 
ATOM   74   C  CD1  . PHE   A 1 6   ? 17.207 -7.071  15.483  1.00 22.21 ?  6   PHE   A CD1  1 
ATOM   75   C  CD2  . PHE   A 1 6   ? 18.374 -8.994  16.266  1.00 23.22 ?  6   PHE   A CD2  1 
ATOM   76   C  CE1  . PHE   A 1 6   ? 18.374 -6.589  14.909  1.00 21.70 ?  6   PHE   A CE1  1 
ATOM   77   C  CE2  . PHE   A 1 6   ? 19.539 -8.525  15.694  1.00 22.79 ?  6   PHE   A CE2  1 
ATOM   78   C  CZ   . PHE   A 1 6   ? 19.540 -7.317  15.014  1.00 21.93 ?  6   PHE   A CZ   1 
ATOM   79   H  H    A PHE   A 1 6   ? 16.921 -9.151  19.007  0.70 44.51 ?  6   PHE   A H    1 
ATOM   80   H  H    B PHE   A 1 6   ? 16.910 -9.160  19.014  0.30 44.51 ?  6   PHE   A H    1 
ATOM   81   H  HA   . PHE   A 1 6   ? 15.575 -7.133  17.937  1.00 36.72 ?  6   PHE   A HA   1 
ATOM   82   H  HB2  . PHE   A 1 6   ? 16.056 -9.742  16.977  1.00 31.82 ?  6   PHE   A HB2  1 
ATOM   83   H  HB3  . PHE   A 1 6   ? 15.215 -8.687  16.142  1.00 31.82 ?  6   PHE   A HB3  1 
ATOM   84   H  HD1  . PHE   A 1 6   ? 16.420 -6.580  15.411  1.00 26.61 ?  6   PHE   A HD1  1 
ATOM   85   H  HD2  . PHE   A 1 6   ? 18.380 -9.805  16.724  1.00 27.83 ?  6   PHE   A HD2  1 
ATOM   86   H  HE1  . PHE   A 1 6   ? 18.368 -5.779  14.451  1.00 26.00 ?  6   PHE   A HE1  1 
ATOM   87   H  HE2  . PHE   A 1 6   ? 20.327 -9.014  15.770  1.00 27.31 ?  6   PHE   A HE2  1 
ATOM   88   H  HZ   . PHE   A 1 6   ? 20.323 -6.997  14.631  1.00 26.27 ?  6   PHE   A HZ   1 
ATOM   89   N  N    . SER   A 1 7   ? 13.167 -7.554  18.195  1.00 28.61 ?  7   SER   A N    1 
ATOM   90   C  CA   . SER   A 1 7   ? 11.796 -7.694  18.672  1.00 28.82 ?  7   SER   A CA   1 
ATOM   91   C  C    . SER   A 1 7   ? 10.804 -7.425  17.549  1.00 25.94 ?  7   SER   A C    1 
ATOM   92   O  O    . SER   A 1 7   ? 11.016 -6.543  16.714  1.00 25.69 ?  7   SER   A O    1 
ATOM   93   C  CB   . SER   A 1 7   ? 11.540 -6.708  19.820  1.00 31.33 ?  7   SER   A CB   1 
ATOM   94   O  OG   . SER   A 1 7   ? 10.204 -6.791  20.275  1.00 32.57 ?  7   SER   A OG   1 
ATOM   95   H  H    . SER   A 1 7   ? 13.304 -6.845  17.728  1.00 34.30 ?  7   SER   A H    1 
ATOM   96   H  HA   . SER   A 1 7   ? 11.658 -8.595  19.005  1.00 34.54 ?  7   SER   A HA   1 
ATOM   97   H  HB2  . SER   A 1 7   ? 12.139 -6.917  20.556  1.00 37.56 ?  7   SER   A HB2  1 
ATOM   98   H  HB3  . SER   A 1 7   ? 11.712 -5.807  19.503  1.00 37.56 ?  7   SER   A HB3  1 
ATOM   99   H  HG   . SER   A 1 7   ? 10.081 -6.245  20.901  1.00 39.04 ?  7   SER   A HG   1 
ATOM   100  N  N    . GLY   A 1 8   ? 9.710  -8.183  17.540  1.00 23.84 ?  8   GLY   A N    1 
ATOM   101  C  CA   . GLY   A 1 8   ? 8.635  -7.919  16.608  1.00 22.28 ?  8   GLY   A CA   1 
ATOM   102  C  C    . GLY   A 1 8   ? 8.838  -8.439  15.205  1.00 20.59 ?  8   GLY   A C    1 
ATOM   103  O  O    . GLY   A 1 8   ? 8.116  -8.014  14.298  1.00 20.80 ?  8   GLY   A O    1 
ATOM   104  H  H    . GLY   A 1 8   ? 9.575  -8.847  18.066  1.00 28.57 ?  8   GLY   A H    1 
ATOM   105  H  HA2  . GLY   A 1 8   ? 7.822  -8.309  16.958  1.00 26.70 ?  8   GLY   A HA2  1 
ATOM   106  H  HA3  . GLY   A 1 8   ? 8.506  -6.960  16.547  1.00 26.70 ?  8   GLY   A HA3  1 
ATOM   107  N  N    . TYR   A 1 9   ? 9.794  -9.343  14.992  1.00 18.63 ?  9   TYR   A N    1 
ATOM   108  C  CA   . TYR   A 1 9   ? 10.062 -9.875  13.664  1.00 17.25 ?  9   TYR   A CA   1 
ATOM   109  C  C    . TYR   A 1 9   ? 9.198  -11.099 13.386  1.00 16.54 ?  9   TYR   A C    1 
ATOM   110  O  O    . TYR   A 1 9   ? 8.923  -11.913 14.273  1.00 18.31 ?  9   TYR   A O    1 
ATOM   111  C  CB   . TYR   A 1 9   ? 11.539 -10.267 13.513  1.00 17.32 ?  9   TYR   A CB   1 
ATOM   112  C  CG   . TYR   A 1 9   ? 12.458 -9.076  13.345  1.00 17.22 ?  9   TYR   A CG   1 
ATOM   113  C  CD1  . TYR   A 1 9   ? 12.774 -8.274  14.428  1.00 17.80 ?  9   TYR   A CD1  1 
ATOM   114  C  CD2  . TYR   A 1 9   ? 12.969 -8.735  12.100  1.00 16.54 ?  9   TYR   A CD2  1 
ATOM   115  C  CE1  . TYR   A 1 9   ? 13.586 -7.169  14.284  1.00 18.44 ?  9   TYR   A CE1  1 
ATOM   116  C  CE2  . TYR   A 1 9   ? 13.783 -7.634  11.945  1.00 17.18 ?  9   TYR   A CE2  1 
ATOM   117  C  CZ   . TYR   A 1 9   ? 14.081 -6.849  13.035  1.00 18.11 ?  9   TYR   A CZ   1 
ATOM   118  O  OH   . TYR   A 1 9   ? 14.884 -5.750  12.871  1.00 19.31 ?  9   TYR   A OH   1 
ATOM   119  H  H    . TYR   A 1 9   ? 10.300 -9.670  15.606  1.00 22.31 ?  9   TYR   A H    1 
ATOM   120  H  HA   . TYR   A 1 9   ? 9.858  -9.195  13.005  1.00 20.67 ?  9   TYR   A HA   1 
ATOM   121  H  HB2  . TYR   A 1 9   ? 11.817 -10.763 14.300  1.00 20.74 ?  9   TYR   A HB2  1 
ATOM   122  H  HB3  . TYR   A 1 9   ? 11.622 -10.827 12.724  1.00 20.74 ?  9   TYR   A HB3  1 
ATOM   123  H  HD1  . TYR   A 1 9   ? 12.418 -8.490  15.270  1.00 21.33 ?  9   TYR   A HD1  1 
ATOM   124  H  HD2  . TYR   A 1 9   ? 12.762 -9.261  11.360  1.00 19.81 ?  9   TYR   A HD2  1 
ATOM   125  H  HE1  . TYR   A 1 9   ? 13.781 -6.645  15.025  1.00 22.09 ?  9   TYR   A HE1  1 
ATOM   126  H  HE2  . TYR   A 1 9   ? 14.125 -7.420  11.109  1.00 20.58 ?  9   TYR   A HE2  1 
ATOM   127  H  HH   . TYR   A 1 9   ? 15.004 -5.375  13.612  1.00 23.14 ?  9   TYR   A HH   1 
ATOM   128  N  N    . LEU   A 1 10  ? 8.792  -11.233 12.126  1.00 16.00 ?  10  LEU   A N    1 
ATOM   129  C  CA   . LEU   A 1 10  ? 8.179  -12.454 11.629  1.00 16.09 ?  10  LEU   A CA   1 
ATOM   130  C  C    . LEU   A 1 10  ? 9.295  -13.387 11.174  1.00 15.39 ?  10  LEU   A C    1 
ATOM   131  O  O    . LEU   A 1 10  ? 10.246 -12.957 10.512  1.00 15.24 ?  10  LEU   A O    1 
ATOM   132  C  CB   . LEU   A 1 10  ? 7.268  -12.121 10.446  1.00 17.66 ?  10  LEU   A CB   1 
ATOM   133  C  CG   . LEU   A 1 10  ? 6.568  -13.307 9.778   1.00 19.91 ?  10  LEU   A CG   1 
ATOM   134  C  CD1  . LEU   A 1 10  ? 5.490  -13.872 10.684  1.00 21.95 ?  10  LEU   A CD1  1 
ATOM   135  C  CD2  . LEU   A 1 10  ? 6.004  -12.918 8.422   1.00 22.31 ?  10  LEU   A CD2  1 
ATOM   136  H  H    . LEU   A 1 10  ? 8.878  -10.619 11.521  1.00 19.16 ?  10  LEU   A H    1 
ATOM   137  H  HA   . LEU   A 1 10  ? 7.653  -12.873 12.334  1.00 19.27 ?  10  LEU   A HA   1 
ATOM   138  H  HB2  . LEU   A 1 10  ? 6.574  -11.513 10.750  1.00 21.16 ?  10  LEU   A HB2  1 
ATOM   139  H  HB3  . LEU   A 1 10  ? 7.802  -11.682 9.766   1.00 21.16 ?  10  LEU   A HB3  1 
ATOM   140  H  HG   . LEU   A 1 10  ? 7.221  -14.011 9.635   1.00 23.86 ?  10  LEU   A HG   1 
ATOM   141  H  HD11 . LEU   A 1 10  ? 5.114  -14.666 10.272  1.00 26.30 ?  10  LEU   A HD11 1 
ATOM   142  H  HD12 . LEU   A 1 10  ? 5.879  -14.100 11.544  1.00 26.30 ?  10  LEU   A HD12 1 
ATOM   143  H  HD13 . LEU   A 1 10  ? 4.796  -13.203 10.805  1.00 26.30 ?  10  LEU   A HD13 1 
ATOM   144  H  HD21 . LEU   A 1 10  ? 5.569  -13.693 8.034   1.00 26.73 ?  10  LEU   A HD21 1 
ATOM   145  H  HD22 . LEU   A 1 10  ? 5.365  -12.202 8.544   1.00 26.73 ?  10  LEU   A HD22 1 
ATOM   146  H  HD23 . LEU   A 1 10  ? 6.733  -12.626 7.855   1.00 26.73 ?  10  LEU   A HD23 1 
ATOM   147  N  N    . LYS   A 1 11  ? 9.192  -14.659 11.554  1.00 15.57 ?  11  LYS   A N    1 
ATOM   148  C  CA   . LYS   A 1 11  ? 10.194 -15.656 11.200  1.00 15.37 ?  11  LYS   A CA   1 
ATOM   149  C  C    . LYS   A 1 11  ? 9.835  -16.237 9.839   1.00 15.74 ?  11  LYS   A C    1 
ATOM   150  O  O    . LYS   A 1 11  ? 8.747  -16.791 9.673   1.00 17.42 ?  11  LYS   A O    1 
ATOM   151  C  CB   . LYS   A 1 11  ? 10.244 -16.740 12.277  1.00 15.12 ?  11  LYS   A CB   1 
ATOM   152  C  CG   . LYS   A 1 11  ? 11.275 -17.837 12.069  1.00 14.95 ?  11  LYS   A CG   1 
ATOM   153  C  CD   . LYS   A 1 11  ? 11.370 -18.711 13.325  1.00 15.51 ?  11  LYS   A CD   1 
ATOM   154  C  CE   . LYS   A 1 11  ? 12.357 -19.864 13.178  1.00 15.60 ?  11  LYS   A CE   1 
ATOM   155  N  NZ   . LYS   A 1 11  ? 13.730 -19.374 12.918  1.00 15.87 ?  11  LYS   A NZ   1 
ATOM   156  H  H    . LYS   A 1 11  ? 8.534  -14.972 12.018  1.00 18.65 ?  11  LYS   A H    1 
ATOM   157  H  HA   . LYS   A 1 11  ? 11.064 -15.228 11.137  1.00 18.41 ?  11  LYS   A HA   1 
ATOM   158  H  HB2  . LYS   A 1 11  ? 10.443 -16.312 13.125  1.00 18.11 ?  11  LYS   A HB2  1 
ATOM   159  H  HB3  . LYS   A 1 11  ? 9.375  -17.160 12.322  1.00 18.11 ?  11  LYS   A HB3  1 
ATOM   160  H  HG2  . LYS   A 1 11  ? 11.010 -18.393 11.321  1.00 17.91 ?  11  LYS   A HG2  1 
ATOM   161  H  HG3  . LYS   A 1 11  ? 12.146 -17.438 11.904  1.00 17.91 ?  11  LYS   A HG3  1 
ATOM   162  H  HD2  . LYS   A 1 11  ? 11.655 -18.164 14.072  1.00 18.58 ?  11  LYS   A HD2  1 
ATOM   163  H  HD3  . LYS   A 1 11  ? 10.493 -19.090 13.509  1.00 18.58 ?  11  LYS   A HD3  1 
ATOM   164  H  HE2  . LYS   A 1 11  ? 12.371 -20.382 13.999  1.00 18.69 ?  11  LYS   A HE2  1 
ATOM   165  H  HE3  . LYS   A 1 11  ? 12.089 -20.425 12.433  1.00 18.69 ?  11  LYS   A HE3  1 
ATOM   166  H  HZ1  . LYS   A 1 11  ? 14.269 -20.063 12.746  1.00 19.01 ?  11  LYS   A HZ1  1 
ATOM   167  H  HZ2  . LYS   A 1 11  ? 13.730 -18.827 12.216  1.00 19.01 ?  11  LYS   A HZ2  1 
ATOM   168  H  HZ3  . LYS   A 1 11  ? 14.038 -18.938 13.627  1.00 19.01 ?  11  LYS   A HZ3  1 
ATOM   169  N  N    . LEU   A 1 12  ? 10.732 -16.105 8.862   1.00 15.03 ?  12  LEU   A N    1 
ATOM   170  C  CA   . LEU   A 1 12  ? 10.471 -16.679 7.544   1.00 15.30 ?  12  LEU   A CA   1 
ATOM   171  C  C    . LEU   A 1 12  ? 11.060 -18.075 7.396   1.00 14.94 ?  12  LEU   A C    1 
ATOM   172  O  O    . LEU   A 1 12  ? 10.437 -18.950 6.785   1.00 15.52 ?  12  LEU   A O    1 
ATOM   173  C  CB   . LEU   A 1 12  ? 11.031 -15.784 6.436   1.00 16.14 ?  12  LEU   A CB   1 
ATOM   174  C  CG   . LEU   A 1 12  ? 10.358 -14.426 6.245   1.00 17.33 ?  12  LEU   A CG   1 
ATOM   175  C  CD1  . LEU   A 1 12  ? 11.084 -13.642 5.169   1.00 18.16 ?  12  LEU   A CD1  1 
ATOM   176  C  CD2  . LEU   A 1 12  ? 8.887  -14.596 5.891   1.00 18.30 ?  12  LEU   A CD2  1 
ATOM   177  H  H    . LEU   A 1 12  ? 11.491 -15.701 8.934   1.00 18.00 ?  12  LEU   A H    1 
ATOM   178  H  HA   . LEU   A 1 12  ? 9.515  -16.751 7.413   1.00 18.32 ?  12  LEU   A HA   1 
ATOM   179  H  HB2  . LEU   A 1 12  ? 11.967 -15.613 6.627   1.00 19.33 ?  12  LEU   A HB2  1 
ATOM   180  H  HB3  . LEU   A 1 12  ? 10.960 -16.262 5.594   1.00 19.33 ?  12  LEU   A HB3  1 
ATOM   181  H  HG   . LEU   A 1 12  ? 10.411 -13.927 7.072   1.00 20.76 ?  12  LEU   A HG   1 
ATOM   182  H  HD11 . LEU   A 1 12  ? 10.652 -12.785 5.051   1.00 21.76 ?  12  LEU   A HD11 1 
ATOM   183  H  HD12 . LEU   A 1 12  ? 12.009 -13.511 5.446   1.00 21.76 ?  12  LEU   A HD12 1 
ATOM   184  H  HD13 . LEU   A 1 12  ? 11.062 -14.144 4.338   1.00 21.76 ?  12  LEU   A HD13 1 
ATOM   185  H  HD21 . LEU   A 1 12  ? 8.523  -13.738 5.624   1.00 21.92 ?  12  LEU   A HD21 1 
ATOM   186  H  HD22 . LEU   A 1 12  ? 8.806  -15.230 5.159   1.00 21.92 ?  12  LEU   A HD22 1 
ATOM   187  H  HD23 . LEU   A 1 12  ? 8.408  -14.931 6.667   1.00 21.92 ?  12  LEU   A HD23 1 
ATOM   188  N  N    . THR   A 1 13  ? 12.274 -18.279 7.903   1.00 14.84 ?  13  THR   A N    1 
ATOM   189  C  CA   . THR   A 1 13  ? 12.975 -19.554 7.808   1.00 15.23 ?  13  THR   A CA   1 
ATOM   190  C  C    . THR   A 1 13  ? 13.745 -19.774 9.103   1.00 15.29 ?  13  THR   A C    1 
ATOM   191  O  O    . THR   A 1 13  ? 13.647 -18.995 10.056  1.00 14.95 ?  13  THR   A O    1 
ATOM   192  C  CB   . THR   A 1 13  ? 13.949 -19.586 6.624   1.00 15.87 ?  13  THR   A CB   1 
ATOM   193  O  OG1  . THR   A 1 13  ? 15.008 -18.664 6.882   1.00 16.27 ?  13  THR   A OG1  1 
ATOM   194  C  CG2  . THR   A 1 13  ? 13.267 -19.228 5.311   1.00 16.49 ?  13  THR   A CG2  1 
ATOM   195  H  H    . THR   A 1 13  ? 12.731 -17.673 8.310   1.00 17.77 ?  13  THR   A H    1 
ATOM   196  H  HA   . THR   A 1 13  ? 12.339 -20.274 7.697   1.00 18.24 ?  13  THR   A HA   1 
ATOM   197  H  HB   . THR   A 1 13  ? 14.323 -20.477 6.532   1.00 19.00 ?  13  THR   A HB   1 
ATOM   198  H  HG1  . THR   A 1 13  ? 15.675 -19.069 7.196   1.00 19.48 ?  13  THR   A HG1  1 
ATOM   199  H  HG21 . THR   A 1 13  ? 13.879 -19.373 4.569   1.00 19.75 ?  13  THR   A HG21 1 
ATOM   200  H  HG22 . THR   A 1 13  ? 12.487 -19.790 5.184   1.00 19.75 ?  13  THR   A HG22 1 
ATOM   201  H  HG23 . THR   A 1 13  ? 12.995 -18.301 5.319   1.00 19.75 ?  13  THR   A HG23 1 
ATOM   202  N  N    . ASP   A 1 14  ? 14.555 -20.832 9.114   1.00 16.06 ?  14  ASP   A N    1 
ATOM   203  C  CA   . ASP   A 1 14  ? 15.397 -21.111 10.266  1.00 16.97 ?  14  ASP   A CA   1 
ATOM   204  C  C    . ASP   A 1 14  ? 16.225 -19.894 10.675  1.00 15.80 ?  14  ASP   A C    1 
ATOM   205  O  O    . ASP   A 1 14  ? 16.456 -19.668 11.868  1.00 16.77 ?  14  ASP   A O    1 
ATOM   206  C  CB   . ASP   A 1 14  ? 16.327 -22.274 9.940   1.00 19.81 ?  14  ASP   A CB   1 
ATOM   207  C  CG   . ASP   A 1 14  ? 17.254 -22.585 11.075  1.00 23.83 ?  14  ASP   A CG   1 
ATOM   208  O  OD1  . ASP   A 1 14  ? 16.756 -22.959 12.159  1.00 25.91 ?  14  ASP   A OD1  1 
ATOM   209  O  OD2  . ASP   A 1 14  ? 18.478 -22.434 10.887  1.00 27.21 -1 14  ASP   A OD2  1 
ATOM   210  H  H    . ASP   A 1 14  ? 14.641 -21.394 8.468   1.00 19.24 ?  14  ASP   A H    1 
ATOM   211  H  HA   . ASP   A 1 14  ? 14.843 -21.371 11.018  1.00 20.32 ?  14  ASP   A HA   1 
ATOM   212  H  HB2  . ASP   A 1 14  ? 15.795 -23.070 9.759   1.00 23.73 ?  14  ASP   A HB2  1 
ATOM   213  H  HB3  . ASP   A 1 14  ? 16.856 -22.053 9.153   1.00 23.73 ?  14  ASP   A HB3  1 
ATOM   214  N  N    . ASN   A 1 15  ? 16.674 -19.091 9.705   1.00 15.04 ?  15  ASN   A N    1 
ATOM   215  C  CA   . ASN   A 1 15  ? 17.661 -18.052 9.976   1.00 15.60 ?  15  ASN   A CA   1 
ATOM   216  C  C    . ASN   A 1 15  ? 17.295 -16.664 9.463   1.00 15.67 ?  15  ASN   A C    1 
ATOM   217  O  O    . ASN   A 1 15  ? 18.077 -15.734 9.682   1.00 16.78 ?  15  ASN   A O    1 
ATOM   218  C  CB   . ASN   A 1 15  ? 19.036 -18.452 9.405   1.00 15.35 ?  15  ASN   A CB   1 
ATOM   219  C  CG   . ASN   A 1 15  ? 19.028 -18.554 7.894   1.00 15.64 ?  15  ASN   A CG   1 
ATOM   220  O  OD1  . ASN   A 1 15  ? 18.323 -19.390 7.319   1.00 16.89 ?  15  ASN   A OD1  1 
ATOM   221  N  ND2  . ASN   A 1 15  ? 19.808 -17.699 7.238   1.00 15.58 ?  15  ASN   A ND2  1 
ATOM   222  H  H    . ASN   A 1 15  ? 16.416 -19.120 8.892   1.00 18.01 ?  15  ASN   A H    1 
ATOM   223  H  HA   . ASN   A 1 15  ? 17.774 -17.980 10.938  1.00 18.68 ?  15  ASN   A HA   1 
ATOM   224  H  HB2  . ASN   A 1 15  ? 19.697 -17.781 9.661   1.00 18.39 ?  15  ASN   A HB2  1 
ATOM   225  H  HB3  . ASN   A 1 15  ? 19.297 -19.316 9.766   1.00 18.39 ?  15  ASN   A HB3  1 
ATOM   226  H  HD21 . ASN   A 1 15  ? 19.833 -17.715 6.379   1.00 18.65 ?  15  ASN   A HD21 1 
ATOM   227  H  HD22 . ASN   A 1 15  ? 20.286 -17.124 7.668   1.00 18.65 ?  15  ASN   A HD22 1 
ATOM   228  N  N    . VAL   A 1 16  ? 16.151 -16.488 8.802   1.00 15.43 ?  16  VAL   A N    1 
ATOM   229  C  CA   . VAL   A 1 16  ? 15.761 -15.210 8.218   1.00 15.08 ?  16  VAL   A CA   1 
ATOM   230  C  C    . VAL   A 1 16  ? 14.484 -14.719 8.886   1.00 14.97 ?  16  VAL   A C    1 
ATOM   231  O  O    . VAL   A 1 16  ? 13.485 -15.448 8.967   1.00 14.96 ?  16  VAL   A O    1 
ATOM   232  C  CB   . VAL   A 1 16  ? 15.599 -15.299 6.691   1.00 15.45 ?  16  VAL   A CB   1 
ATOM   233  C  CG1  . VAL   A 1 16  ? 15.140 -13.954 6.118   1.00 16.20 ?  16  VAL   A CG1  1 
ATOM   234  C  CG2  . VAL   A 1 16  ? 16.897 -15.751 6.039   1.00 16.55 ?  16  VAL   A CG2  1 
ATOM   235  H  H    . VAL   A 1 16  ? 15.576 -17.113 8.687   1.00 18.47 ?  16  VAL   A H    1 
ATOM   236  H  HA   . VAL   A 1 16  ? 16.465 -14.561 8.401   1.00 18.06 ?  16  VAL   A HA   1 
ATOM   237  H  HB   . VAL   A 1 16  ? 14.926 -15.962 6.491   1.00 18.51 ?  16  VAL   A HB   1 
ATOM   238  H  HG11 . VAL   A 1 16  ? 15.235 -13.979 5.154   1.00 19.40 ?  16  VAL   A HG11 1 
ATOM   239  H  HG12 . VAL   A 1 16  ? 14.207 -13.818 6.353   1.00 19.40 ?  16  VAL   A HG12 1 
ATOM   240  H  HG13 . VAL   A 1 16  ? 15.685 -13.248 6.490   1.00 19.40 ?  16  VAL   A HG13 1 
ATOM   241  H  HG21 . VAL   A 1 16  ? 16.798 -15.722 5.075   1.00 19.82 ?  16  VAL   A HG21 1 
ATOM   242  H  HG22 . VAL   A 1 16  ? 17.618 -15.156 6.311   1.00 19.82 ?  16  VAL   A HG22 1 
ATOM   243  H  HG23 . VAL   A 1 16  ? 17.102 -16.657 6.323   1.00 19.82 ?  16  VAL   A HG23 1 
ATOM   244  N  N    . TYR   A 1 17  ? 14.523 -13.460 9.323   1.00 14.60 ?  17  TYR   A N    1 
ATOM   245  C  CA   . TYR   A 1 17  ? 13.440 -12.768 10.010  1.00 14.29 ?  17  TYR   A CA   1 
ATOM   246  C  C    . TYR   A 1 17  ? 13.173 -11.445 9.300   1.00 14.69 ?  17  TYR   A C    1 
ATOM   247  O  O    . TYR   A 1 17  ? 14.080 -10.881 8.687   1.00 15.19 ?  17  TYR   A O    1 
ATOM   248  C  CB   . TYR   A 1 17  ? 13.855 -12.507 11.460  1.00 14.87 ?  17  TYR   A CB   1 
ATOM   249  C  CG   . TYR   A 1 17  ? 14.075 -13.770 12.263  1.00 15.63 ?  17  TYR   A CG   1 
ATOM   250  C  CD1  . TYR   A 1 17  ? 15.263 -14.500 12.169  1.00 16.65 ?  17  TYR   A CD1  1 
ATOM   251  C  CD2  . TYR   A 1 17  ? 13.083 -14.251 13.104  1.00 16.23 ?  17  TYR   A CD2  1 
ATOM   252  C  CE1  . TYR   A 1 17  ? 15.448 -15.674 12.899  1.00 17.20 ?  17  TYR   A CE1  1 
ATOM   253  C  CE2  . TYR   A 1 17  ? 13.260 -15.421 13.835  1.00 16.76 ?  17  TYR   A CE2  1 
ATOM   254  C  CZ   . TYR   A 1 17  ? 14.443 -16.126 13.733  1.00 17.39 ?  17  TYR   A CZ   1 
ATOM   255  O  OH   . TYR   A 1 17  ? 14.616 -17.279 14.467  1.00 18.53 ?  17  TYR   A OH   1 
ATOM   256  H  H    . TYR   A 1 17  ? 15.215 -12.951 9.207   1.00 17.48 ?  17  TYR   A H    1 
ATOM   257  H  HA   . TYR   A 1 17  ? 12.639 -13.315 9.992   1.00 17.11 ?  17  TYR   A HA   1 
ATOM   258  H  HB2  . TYR   A 1 17  ? 14.684 -12.004 11.457  1.00 17.80 ?  17  TYR   A HB2  1 
ATOM   259  H  HB3  . TYR   A 1 17  ? 13.159 -11.998 11.890  1.00 17.80 ?  17  TYR   A HB3  1 
ATOM   260  H  HD1  . TYR   A 1 17  ? 15.944 -14.199 11.604  1.00 19.94 ?  17  TYR   A HD1  1 
ATOM   261  H  HD2  . TYR   A 1 17  ? 12.284 -13.787 13.178  1.00 19.44 ?  17  TYR   A HD2  1 
ATOM   262  H  HE1  . TYR   A 1 17  ? 16.253 -16.147 12.832  1.00 20.60 ?  17  TYR   A HE1  1 
ATOM   263  H  HE2  . TYR   A 1 17  ? 12.588 -15.720 14.400  1.00 20.07 ?  17  TYR   A HE2  1 
ATOM   264  H  HH   . TYR   A 1 17  ? 13.891 -17.503 14.820  1.00 22.20 ?  17  TYR   A HH   1 
ATOM   265  N  N    A ILE   A 1 18  ? 11.926 -10.963 9.341   0.70 14.64 ?  18  ILE   A N    1 
ATOM   266  N  N    B ILE   A 1 18  ? 11.952 -10.917 9.452   0.30 14.19 ?  18  ILE   A N    1 
ATOM   267  C  CA   A ILE   A 1 18  ? 11.538 -9.786  8.561   0.70 14.70 ?  18  ILE   A CA   1 
ATOM   268  C  CA   B ILE   A 1 18  ? 11.547 -9.692  8.767   0.30 13.99 ?  18  ILE   A CA   1 
ATOM   269  C  C    A ILE   A 1 18  ? 10.571 -8.915  9.359   0.70 15.34 ?  18  ILE   A C    1 
ATOM   270  C  C    B ILE   A 1 18  ? 10.635 -8.849  9.652   0.30 14.22 ?  18  ILE   A C    1 
ATOM   271  O  O    A ILE   A 1 18  ? 9.714  -9.424  10.090  0.70 15.38 ?  18  ILE   A O    1 
ATOM   272  O  O    B ILE   A 1 18  ? 9.936  -9.363  10.532  0.30 14.20 ?  18  ILE   A O    1 
ATOM   273  C  CB   A ILE   A 1 18  ? 10.983 -10.198 7.177   0.70 14.66 ?  18  ILE   A CB   1 
ATOM   274  C  CB   B ILE   A 1 18  ? 10.862 -10.011 7.420   0.30 13.92 ?  18  ILE   A CB   1 
ATOM   275  C  CG1  A ILE   A 1 18  ? 10.871 -9.004  6.233   0.70 15.32 ?  18  ILE   A CG1  1 
ATOM   276  C  CG1  B ILE   A 1 18  ? 10.898 -8.798  6.489   0.30 14.48 ?  18  ILE   A CG1  1 
ATOM   277  C  CG2  A ILE   A 1 18  ? 9.656  -10.927 7.316   0.70 14.26 ?  18  ILE   A CG2  1 
ATOM   278  C  CG2  B ILE   A 1 18  ? 9.433  -10.493 7.648   0.30 14.03 ?  18  ILE   A CG2  1 
ATOM   279  C  CD1  A ILE   A 1 18  ? 10.628 -9.412  4.795   0.70 17.34 ?  18  ILE   A CD1  1 
ATOM   280  C  CD1  B ILE   A 1 18  ? 10.623 -9.150  5.044   0.30 15.28 ?  18  ILE   A CD1  1 
ATOM   281  H  H    A ILE   A 1 18  ? 11.290 -11.316 9.803   0.70 17.53 ?  18  ILE   A H    1 
ATOM   282  H  H    B ILE   A 1 18  ? 11.343 -11.259 9.953   0.30 16.99 ?  18  ILE   A H    1 
ATOM   283  H  HA   A ILE   A 1 18  ? 12.334 -9.264  8.396   0.70 17.60 ?  18  ILE   A HA   1 
ATOM   284  H  HA   B ILE   A 1 18  ? 12.343 -9.172  8.579   0.30 16.75 ?  18  ILE   A HA   1 
ATOM   285  H  HB   A ILE   A 1 18  ? 11.611 -10.824 6.778   0.70 17.56 ?  18  ILE   A HB   1 
ATOM   286  H  HB   B ILE   A 1 18  ? 11.354 -10.724 6.999   0.30 16.67 ?  18  ILE   A HB   1 
ATOM   287  H  HG12 A ILE   A 1 18  ? 10.131 -8.448  6.513   0.70 18.35 ?  18  ILE   A HG12 1 
ATOM   288  H  HG12 B ILE   A 1 18  ? 10.228 -8.158  6.772   0.30 17.33 ?  18  ILE   A HG12 1 
ATOM   289  H  HG13 A ILE   A 1 18  ? 11.699 -8.503  6.261   0.70 18.35 ?  18  ILE   A HG13 1 
ATOM   290  H  HG13 B ILE   A 1 18  ? 11.779 -8.393  6.531   0.30 17.33 ?  18  ILE   A HG13 1 
ATOM   291  H  HG21 A ILE   A 1 18  ? 9.414  -11.317 6.457   0.70 17.07 ?  18  ILE   A HG21 1 
ATOM   292  H  HG21 B ILE   A 1 18  ? 9.108  -10.904 6.832   0.30 16.80 ?  18  ILE   A HG21 1 
ATOM   293  H  HG22 A ILE   A 1 18  ? 9.749  -11.632 7.976   0.70 17.07 ?  18  ILE   A HG22 1 
ATOM   294  H  HG22 B ILE   A 1 18  ? 9.435  -11.144 8.367   0.30 16.80 ?  18  ILE   A HG22 1 
ATOM   295  H  HG23 A ILE   A 1 18  ? 8.974  -10.300 7.594   0.70 17.07 ?  18  ILE   A HG23 1 
ATOM   296  H  HG23 B ILE   A 1 18  ? 8.869  -9.740  7.885   0.30 16.80 ?  18  ILE   A HG23 1 
ATOM   297  H  HD11 A ILE   A 1 18  ? 10.647 -8.617  4.237   0.70 20.77 ?  18  ILE   A HD11 1 
ATOM   298  H  HD11 B ILE   A 1 18  ? 10.648 -8.343  4.507   0.30 18.30 ?  18  ILE   A HD11 1 
ATOM   299  H  HD12 A ILE   A 1 18  ? 11.323 -10.027 4.518   0.70 20.77 ?  18  ILE   A HD12 1 
ATOM   300  H  HD12 B ILE   A 1 18  ? 11.300 -9.773  4.733   0.30 18.30 ?  18  ILE   A HD12 1 
ATOM   301  H  HD13 A ILE   A 1 18  ? 9.760  -9.839  4.730   0.70 20.77 ?  18  ILE   A HD13 1 
ATOM   302  H  HD13 B ILE   A 1 18  ? 9.745  -9.560  4.979   0.30 18.30 ?  18  ILE   A HD13 1 
ATOM   303  N  N    A LYS   A 1 19  ? 10.711 -7.596  9.213   0.70 15.81 ?  19  LYS   A N    1 
ATOM   304  N  N    B LYS   A 1 19  ? 10.628 -7.539  9.385   0.30 14.77 ?  19  LYS   A N    1 
ATOM   305  C  CA   A LYS   A 1 19  ? 9.890  -6.640  9.945   0.70 16.76 ?  19  LYS   A CA   1 
ATOM   306  C  CA   B LYS   A 1 19  ? 9.842  -6.587  10.166  0.30 15.87 ?  19  LYS   A CA   1 
ATOM   307  C  C    A LYS   A 1 19  ? 9.675  -5.401  9.088   0.70 16.49 ?  19  LYS   A C    1 
ATOM   308  C  C    B LYS   A 1 19  ? 9.713  -5.285  9.386   0.30 15.91 ?  19  LYS   A C    1 
ATOM   309  O  O    A LYS   A 1 19  ? 10.546 -5.022  8.300   0.70 15.51 ?  19  LYS   A O    1 
ATOM   310  O  O    B LYS   A 1 19  ? 10.717 -4.755  8.906   0.30 15.75 ?  19  LYS   A O    1 
ATOM   311  C  CB   A LYS   A 1 19  ? 10.593 -6.230  11.247  0.70 17.67 ?  19  LYS   A CB   1 
ATOM   312  C  CB   B LYS   A 1 19  ? 10.538 -6.337  11.509  0.30 16.88 ?  19  LYS   A CB   1 
ATOM   313  C  CG   A LYS   A 1 19  ? 9.813  -5.293  12.163  0.70 18.99 ?  19  LYS   A CG   1 
ATOM   314  C  CG   B LYS   A 1 19  ? 9.877  -5.320  12.421  0.30 17.66 ?  19  LYS   A CG   1 
ATOM   315  C  CD   A LYS   A 1 19  ? 10.661 -4.965  13.391  0.70 19.68 ?  19  LYS   A CD   1 
ATOM   316  C  CD   B LYS   A 1 19  ? 10.500 -5.424  13.803  0.30 18.18 ?  19  LYS   A CD   1 
ATOM   317  C  CE   A LYS   A 1 19  ? 9.945  -4.058  14.379  0.70 20.81 ?  19  LYS   A CE   1 
ATOM   318  C  CE   B LYS   A 1 19  ? 10.478 -4.114  14.565  0.30 18.29 ?  19  LYS   A CE   1 
ATOM   319  N  NZ   A LYS   A 1 19  ? 10.824 -3.728  15.539  0.70 21.18 ?  19  LYS   A NZ   1 
ATOM   320  N  NZ   B LYS   A 1 19  ? 11.361 -4.183  15.768  0.30 18.15 ?  19  LYS   A NZ   1 
ATOM   321  H  H    A LYS   A 1 19  ? 11.296 -7.236  8.692   0.70 18.94 ?  19  LYS   A H    1 
ATOM   322  H  H    B LYS   A 1 19  ? 11.083 -7.175  8.748   0.30 17.69 ?  19  LYS   A H    1 
ATOM   323  H  HA   A LYS   A 1 19  ? 9.034  -7.044  10.157  0.70 20.08 ?  19  LYS   A HA   1 
ATOM   324  H  HA   B LYS   A 1 19  ? 8.961  -6.949  10.330  0.30 19.00 ?  19  LYS   A HA   1 
ATOM   325  H  HB2  A LYS   A 1 19  ? 10.787 -7.035  11.755  0.70 21.17 ?  19  LYS   A HB2  1 
ATOM   326  H  HB2  B LYS   A 1 19  ? 10.576 -7.176  11.995  0.30 20.22 ?  19  LYS   A HB2  1 
ATOM   327  H  HB3  A LYS   A 1 19  ? 11.424 -5.789  11.017  0.70 21.17 ?  19  LYS   A HB3  1 
ATOM   328  H  HB3  B LYS   A 1 19  ? 11.440 -6.025  11.335  0.30 20.22 ?  19  LYS   A HB3  1 
ATOM   329  H  HG2  A LYS   A 1 19  ? 9.615  -4.468  11.695  0.70 22.75 ?  19  LYS   A HG2  1 
ATOM   330  H  HG2  B LYS   A 1 19  ? 10.027 -4.426  12.075  0.30 21.16 ?  19  LYS   A HG2  1 
ATOM   331  H  HG3  A LYS   A 1 19  ? 8.996  -5.727  12.455  0.70 22.75 ?  19  LYS   A HG3  1 
ATOM   332  H  HG3  B LYS   A 1 19  ? 8.929  -5.510  12.489  0.30 21.16 ?  19  LYS   A HG3  1 
ATOM   333  H  HD2  A LYS   A 1 19  ? 10.881 -5.794  13.850  0.70 23.58 ?  19  LYS   A HD2  1 
ATOM   334  H  HD2  B LYS   A 1 19  ? 10.013 -6.084  14.320  0.30 21.78 ?  19  LYS   A HD2  1 
ATOM   335  H  HD3  A LYS   A 1 19  ? 11.472 -4.521  13.104  0.70 23.58 ?  19  LYS   A HD3  1 
ATOM   336  H  HD3  B LYS   A 1 19  ? 11.426 -5.696  13.705  0.30 21.78 ?  19  LYS   A HD3  1 
ATOM   337  H  HE2  A LYS   A 1 19  ? 9.704  -3.230  13.937  0.70 24.93 ?  19  LYS   A HE2  1 
ATOM   338  H  HE2  B LYS   A 1 19  ? 10.796 -3.402  13.988  0.30 21.91 ?  19  LYS   A HE2  1 
ATOM   339  H  HE3  A LYS   A 1 19  ? 9.155  -4.506  14.715  0.70 24.93 ?  19  LYS   A HE3  1 
ATOM   340  H  HE3  B LYS   A 1 19  ? 9.573  -3.930  14.860  0.30 21.91 ?  19  LYS   A HE3  1 
ATOM   341  H  HZ1  A LYS   A 1 19  ? 10.390 -3.206  16.113  0.70 25.38 ?  19  LYS   A HZ1  1 
ATOM   342  H  HZ1  B LYS   A 1 19  ? 11.344 -3.406  16.202  0.30 21.74 ?  19  LYS   A HZ1  1 
ATOM   343  H  HZ2  A LYS   A 1 19  ? 11.070 -4.476  15.958  0.70 25.38 ?  19  LYS   A HZ2  1 
ATOM   344  H  HZ2  B LYS   A 1 19  ? 11.080 -4.827  16.315  0.30 21.74 ?  19  LYS   A HZ2  1 
ATOM   345  H  HZ3  A LYS   A 1 19  ? 11.555 -3.304  15.258  0.70 25.38 ?  19  LYS   A HZ3  1 
ATOM   346  H  HZ3  B LYS   A 1 19  ? 12.198 -4.358  15.521  0.30 21.74 ?  19  LYS   A HZ3  1 
ATOM   347  N  N    A ASN   A 1 20  ? 8.511  -4.771  9.255   0.70 17.91 ?  20  ASN   A N    1 
ATOM   348  N  N    B ASN   A 1 20  ? 8.484  -4.780  9.251   0.30 16.31 ?  20  ASN   A N    1 
ATOM   349  C  CA   A ASN   A 1 20  ? 8.275  -3.440  8.708   0.70 19.33 ?  20  ASN   A CA   1 
ATOM   350  C  CA   B ASN   A 1 20  ? 8.231  -3.486  8.608   0.30 16.64 ?  20  ASN   A CA   1 
ATOM   351  C  C    A ASN   A 1 20  ? 8.896  -2.446  9.680   0.70 19.73 ?  20  ASN   A C    1 
ATOM   352  C  C    B ASN   A 1 20  ? 8.799  -2.380  9.488   0.30 16.97 ?  20  ASN   A C    1 
ATOM   353  O  O    A ASN   A 1 20  ? 8.393  -2.251  10.790  0.70 20.62 ?  20  ASN   A O    1 
ATOM   354  O  O    B ASN   A 1 20  ? 8.181  -1.971  10.474  0.30 17.78 ?  20  ASN   A O    1 
ATOM   355  C  CB   A ASN   A 1 20  ? 6.779  -3.193  8.517   0.70 20.48 ?  20  ASN   A CB   1 
ATOM   356  C  CB   B ASN   A 1 20  ? 6.732  -3.293  8.385   0.30 16.63 ?  20  ASN   A CB   1 
ATOM   357  C  CG   A ASN   A 1 20  ? 6.455  -1.746  8.154   0.70 21.66 ?  20  ASN   A CG   1 
ATOM   358  C  CG   B ASN   A 1 20  ? 6.371  -1.897  7.860   0.30 16.80 ?  20  ASN   A CG   1 
ATOM   359  O  OD1  A ASN   A 1 20  ? 5.571  -1.126  8.755   0.70 23.28 ?  20  ASN   A OD1  1 
ATOM   360  O  OD1  B ASN   A 1 20  ? 5.235  -1.434  8.039   0.30 17.04 ?  20  ASN   A OD1  1 
ATOM   361  N  ND2  A ASN   A 1 20  ? 7.162  -1.207  7.165   0.70 22.38 ?  20  ASN   A ND2  1 
ATOM   362  N  ND2  B ASN   A 1 20  ? 7.323  -1.231  7.205   0.30 17.43 ?  20  ASN   A ND2  1 
ATOM   363  H  H    A ASN   A 1 20  ? 7.847  -5.098  9.692   0.70 21.45 ?  20  ASN   A H    1 
ATOM   364  H  H    B ASN   A 1 20  ? 7.772  -5.186  9.510   0.30 19.54 ?  20  ASN   A H    1 
ATOM   365  H  HA   A ASN   A 1 20  ? 8.714  -3.359  7.849   0.70 23.16 ?  20  ASN   A HA   1 
ATOM   366  H  HA   B ASN   A 1 20  ? 8.683  -3.459  7.750   0.30 19.93 ?  20  ASN   A HA   1 
ATOM   367  H  HB2  A ASN   A 1 20  ? 6.457  -3.763  7.798   0.70 24.54 ?  20  ASN   A HB2  1 
ATOM   368  H  HB2  B ASN   A 1 20  ? 6.424  -3.942  7.738   0.30 19.92 ?  20  ASN   A HB2  1 
ATOM   369  H  HB3  A ASN   A 1 20  ? 6.317  -3.409  9.340   0.70 24.54 ?  20  ASN   A HB3  1 
ATOM   370  H  HB3  B ASN   A 1 20  ? 6.273  -3.422  9.229   0.30 19.92 ?  20  ASN   A HB3  1 
ATOM   371  H  HD21 A ASN   A 1 20  ? 7.015  -0.397  6.925   0.70 26.81 ?  20  ASN   A HD21 1 
ATOM   372  H  HD21 B ASN   A 1 20  ? 7.159  -0.446  6.899   0.30 20.88 ?  20  ASN   A HD21 1 
ATOM   373  H  HD22 A ASN   A 1 20  ? 7.773  -1.669  6.769   0.70 26.81 ?  20  ASN   A HD22 1 
ATOM   374  H  HD22 B ASN   A 1 20  ? 8.102  -1.579  7.091   0.30 20.88 ?  20  ASN   A HD22 1 
ATOM   375  N  N    A ALA   A 1 21  ? 10.024 -1.857  9.295   0.70 19.77 ?  21  ALA   A N    1 
ATOM   376  N  N    B ALA   A 1 21  ? 9.975  -1.871  9.123   0.30 16.79 ?  21  ALA   A N    1 
ATOM   377  C  CA   A ALA   A 1 21  ? 10.722 -0.964  10.207  0.70 19.74 ?  21  ALA   A CA   1 
ATOM   378  C  CA   B ALA   A 1 21  ? 10.641 -0.873  9.949   0.30 16.79 ?  21  ALA   A CA   1 
ATOM   379  C  C    A ALA   A 1 21  ? 11.676 -0.079  9.426   0.70 19.04 ?  21  ALA   A C    1 
ATOM   380  C  C    B ALA   A 1 21  ? 11.693 -0.146  9.129   0.30 16.03 ?  21  ALA   A C    1 
ATOM   381  O  O    A ALA   A 1 21  ? 12.119 -0.425  8.328   0.70 19.38 ?  21  ALA   A O    1 
ATOM   382  O  O    B ALA   A 1 21  ? 12.182 -0.655  8.116   0.30 16.05 ?  21  ALA   A O    1 
ATOM   383  C  CB   A ALA   A 1 21  ? 11.486 -1.745  11.280  0.70 20.75 ?  21  ALA   A CB   1 
ATOM   384  C  CB   B ALA   A 1 21  ? 11.288 -1.507  11.184  0.30 17.50 ?  21  ALA   A CB   1 
ATOM   385  H  H    A ALA   A 1 21  ? 10.402 -1.963  8.529   0.70 23.68 ?  21  ALA   A H    1 
ATOM   386  H  H    B ALA   A 1 21  ? 10.397 -2.080  8.401   0.30 20.10 ?  21  ALA   A H    1 
ATOM   387  H  HA   A ALA   A 1 21  ? 10.072 -0.395  10.649  0.70 23.66 ?  21  ALA   A HA   1 
ATOM   388  H  HA   B ALA   A 1 21  ? 9.987  -0.226  10.248  0.30 20.11 ?  21  ALA   A HA   1 
ATOM   389  H  HB1  A ALA   A 1 21  ? 11.873 -1.112  11.903  0.70 24.86 ?  21  ALA   A HB1  1 
ATOM   390  H  HB1  B ALA   A 1 21  ? 11.714 -0.811  11.708  0.30 20.97 ?  21  ALA   A HB1  1 
ATOM   391  H  HB2  A ALA   A 1 21  ? 10.862 -2.326  11.745  0.70 24.86 ?  21  ALA   A HB2  1 
ATOM   392  H  HB2  B ALA   A 1 21  ? 10.601 -1.945  11.712  0.30 20.97 ?  21  ALA   A HB2  1 
ATOM   393  H  HB3  A ALA   A 1 21  ? 12.177 -2.270  10.856  0.70 24.86 ?  21  ALA   A HB3  1 
ATOM   394  H  HB3  B ALA   A 1 21  ? 11.948 -2.158  10.898  0.30 20.97 ?  21  ALA   A HB3  1 
ATOM   395  N  N    A ASP   A 1 22  ? 11.968 1.077   10.017  0.70 18.57 ?  22  ASP   A N    1 
ATOM   396  N  N    B ASP   A 1 22  ? 12.013 1.067   9.578   0.30 15.85 ?  22  ASP   A N    1 
ATOM   397  C  CA   A ASP   A 1 22  ? 12.992 1.991   9.524   0.70 18.15 ?  22  ASP   A CA   1 
ATOM   398  C  CA   B ASP   A 1 22  ? 13.167 1.810   9.085   0.30 15.71 ?  22  ASP   A CA   1 
ATOM   399  C  C    A ASP   A 1 22  ? 14.328 1.522   10.089  0.70 16.59 ?  22  ASP   A C    1 
ATOM   400  C  C    B ASP   A 1 22  ? 14.424 1.218   9.713   0.30 14.59 ?  22  ASP   A C    1 
ATOM   401  O  O    A ASP   A 1 22  ? 14.535 1.551   11.307  0.70 17.16 ?  22  ASP   A O    1 
ATOM   402  O  O    B ASP   A 1 22  ? 14.528 1.135   10.941  0.30 14.85 ?  22  ASP   A O    1 
ATOM   403  C  CB   A ASP   A 1 22  ? 12.655 3.405   9.991   0.70 20.21 ?  22  ASP   A CB   1 
ATOM   404  C  CB   B ASP   A 1 22  ? 13.025 3.282   9.475   0.30 17.07 ?  22  ASP   A CB   1 
ATOM   405  C  CG   A ASP   A 1 22  ? 13.680 4.440   9.548   0.70 21.79 ?  22  ASP   A CG   1 
ATOM   406  C  CG   B ASP   A 1 22  ? 14.128 4.162   8.907   0.30 18.05 ?  22  ASP   A CG   1 
ATOM   407  O  OD1  A ASP   A 1 22  ? 14.789 4.083   9.100   0.70 21.82 ?  22  ASP   A OD1  1 
ATOM   408  O  OD1  B ASP   A 1 22  ? 15.119 3.625   8.370   0.30 17.99 ?  22  ASP   A OD1  1 
ATOM   409  O  OD2  A ASP   A 1 22  ? 13.360 5.640   9.653   0.70 23.22 -1 22  ASP   A OD2  1 
ATOM   410  O  OD2  B ASP   A 1 22  ? 14.001 5.403   8.999   0.30 18.98 -1 22  ASP   A OD2  1 
ATOM   411  H  H    A ASP   A 1 22  ? 11.569 1.364   10.725  0.70 22.25 ?  22  ASP   A H    1 
ATOM   412  H  H    B ASP   A 1 22  ? 11.556 1.490   10.173  0.30 18.99 ?  22  ASP   A H    1 
ATOM   413  H  HA   A ASP   A 1 22  ? 13.025 1.967   8.555   0.70 21.75 ?  22  ASP   A HA   1 
ATOM   414  H  HA   B ASP   A 1 22  ? 13.227 1.731   8.119   0.30 18.82 ?  22  ASP   A HA   1 
ATOM   415  H  HB2  A ASP   A 1 22  ? 11.787 3.660   9.632   0.70 24.21 ?  22  ASP   A HB2  1 
ATOM   416  H  HB2  B ASP   A 1 22  ? 12.181 3.618   9.147   0.30 20.45 ?  22  ASP   A HB2  1 
ATOM   417  H  HB3  A ASP   A 1 22  ? 12.617 3.416   10.963  0.70 24.21 ?  22  ASP   A HB3  1 
ATOM   418  H  HB3  B ASP   A 1 22  ? 13.061 3.352   10.442  0.30 20.45 ?  22  ASP   A HB3  1 
ATOM   419  N  N    A ILE   A 1 23  ? 15.227 1.069   9.209   0.70 16.02 ?  23  ILE   A N    1 
ATOM   420  N  N    B ILE   A 1 23  ? 15.370 0.790   8.872   0.30 14.22 ?  23  ILE   A N    1 
ATOM   421  C  CA   A ILE   A 1 23  ? 16.485 0.469   9.649   0.70 15.46 ?  23  ILE   A CA   1 
ATOM   422  C  CA   B ILE   A 1 23  ? 16.610 0.206   9.379   0.30 13.85 ?  23  ILE   A CA   1 
ATOM   423  C  C    A ILE   A 1 23  ? 17.282 1.431   10.521  0.70 15.54 ?  23  ILE   A C    1 
ATOM   424  C  C    B ILE   A 1 23  ? 17.346 1.190   10.276  0.30 14.51 ?  23  ILE   A C    1 
ATOM   425  O  O    A ILE   A 1 23  ? 17.996 1.002   11.435  0.70 15.96 ?  23  ILE   A O    1 
ATOM   426  O  O    B ILE   A 1 23  ? 18.062 0.783   11.198  0.30 14.60 ?  23  ILE   A O    1 
ATOM   427  C  CB   A ILE   A 1 23  ? 17.287 -0.041  8.431   0.70 15.22 ?  23  ILE   A CB   1 
ATOM   428  C  CB   B ILE   A 1 23  ? 17.502 -0.309  8.226   0.30 13.31 ?  23  ILE   A CB   1 
ATOM   429  C  CG1  A ILE   A 1 23  ? 18.466 -0.907  8.887   0.70 15.01 ?  23  ILE   A CG1  1 
ATOM   430  C  CG1  B ILE   A 1 23  ? 18.567 -1.270  8.767   0.30 13.14 ?  23  ILE   A CG1  1 
ATOM   431  C  CG2  A ILE   A 1 23  ? 17.734 1.123   7.548   0.70 15.36 ?  23  ILE   A CG2  1 
ATOM   432  C  CG2  B ILE   A 1 23  ? 18.168 0.848   7.485   0.30 13.04 ?  23  ILE   A CG2  1 
ATOM   433  C  CD1  A ILE   A 1 23  ? 19.161 -1.638  7.761   0.70 15.42 ?  23  ILE   A CD1  1 
ATOM   434  C  CD1  B ILE   A 1 23  ? 19.431 -1.912  7.690   0.30 13.32 ?  23  ILE   A CD1  1 
ATOM   435  H  H    A ILE   A 1 23  ? 15.123 1.101   8.360   0.70 19.19 ?  23  ILE   A H    1 
ATOM   436  H  H    B ILE   A 1 23  ? 15.316 0.816   8.024   0.30 17.02 ?  23  ILE   A H    1 
ATOM   437  H  HA   A ILE   A 1 23  ? 16.278 -0.304  10.193  0.70 18.51 ?  23  ILE   A HA   1 
ATOM   438  H  HA   B ILE   A 1 23  ? 16.377 -0.561  9.921   0.30 16.58 ?  23  ILE   A HA   1 
ATOM   439  H  HB   A ILE   A 1 23  ? 16.699 -0.600  7.901   0.70 18.23 ?  23  ILE   A HB   1 
ATOM   440  H  HB   B ILE   A 1 23  ? 16.946 -0.794  7.599   0.30 15.93 ?  23  ILE   A HB   1 
ATOM   441  H  HG12 A ILE   A 1 23  ? 19.121 -0.343  9.321   0.70 17.98 ?  23  ILE   A HG12 1 
ATOM   442  H  HG12 B ILE   A 1 23  ? 19.156 -0.785  9.365   0.30 15.72 ?  23  ILE   A HG12 1 
ATOM   443  H  HG13 A ILE   A 1 23  ? 18.138 -1.574  9.511   0.70 17.98 ?  23  ILE   A HG13 1 
ATOM   444  H  HG13 B ILE   A 1 23  ? 18.125 -1.986  9.253   0.30 15.72 ?  23  ILE   A HG13 1 
ATOM   445  H  HG21 A ILE   A 1 23  ? 18.114 0.771   6.726   0.70 18.40 ?  23  ILE   A HG21 1 
ATOM   446  H  HG21 B ILE   A 1 23  ? 18.518 0.520   6.640   0.30 15.61 ?  23  ILE   A HG21 1 
ATOM   447  H  HG22 A ILE   A 1 23  ? 16.962 1.676   7.339   0.70 18.40 ?  23  ILE   A HG22 1 
ATOM   448  H  HG22 B ILE   A 1 23  ? 17.509 1.538   7.324   0.30 15.61 ?  23  ILE   A HG22 1 
ATOM   449  H  HG23 A ILE   A 1 23  ? 18.397 1.648   8.020   0.70 18.40 ?  23  ILE   A HG23 1 
ATOM   450  H  HG23 B ILE   A 1 23  ? 18.891 1.198   8.027   0.30 15.61 ?  23  ILE   A HG23 1 
ATOM   451  H  HD11 A ILE   A 1 23  ? 19.851 -2.207  8.134   0.70 18.46 ?  23  ILE   A HD11 1 
ATOM   452  H  HD11 B ILE   A 1 23  ? 20.009 -2.575  8.101   0.30 15.95 ?  23  ILE   A HD11 1 
ATOM   453  H  HD12 A ILE   A 1 23  ? 18.509 -2.175  7.284   0.70 18.46 ?  23  ILE   A HD12 1 
ATOM   454  H  HD12 B ILE   A 1 23  ? 18.855 -2.338  7.036   0.30 15.95 ?  23  ILE   A HD12 1 
ATOM   455  H  HD13 A ILE   A 1 23  ? 19.556 -0.987  7.160   0.70 18.46 ?  23  ILE   A HD13 1 
ATOM   456  H  HD13 B ILE   A 1 23  ? 19.967 -1.226  7.263   0.30 15.95 ?  23  ILE   A HD13 1 
ATOM   457  N  N    A VAL   A 1 24  ? 17.159 2.737   10.276  0.70 15.93 ?  24  VAL   A N    1 
ATOM   458  N  N    B VAL   A 1 24  ? 17.178 2.492   10.032  0.30 15.58 ?  24  VAL   A N    1 
ATOM   459  C  CA   A VAL   A 1 24  ? 17.841 3.718   11.117  0.70 17.05 ?  24  VAL   A CA   1 
ATOM   460  C  CA   B VAL   A 1 24  ? 17.838 3.501   10.855  0.30 16.87 ?  24  VAL   A CA   1 
ATOM   461  C  C    A VAL   A 1 24  ? 17.323 3.642   12.546  0.70 18.04 ?  24  VAL   A C    1 
ATOM   462  C  C    B VAL   A 1 24  ? 17.266 3.497   12.267  0.30 18.05 ?  24  VAL   A C    1 
ATOM   463  O  O    A VAL   A 1 24  ? 18.098 3.571   13.509  0.70 18.74 ?  24  VAL   A O    1 
ATOM   464  O  O    B VAL   A 1 24  ? 18.009 3.531   13.255  0.30 18.59 ?  24  VAL   A O    1 
ATOM   465  C  CB   A VAL   A 1 24  ? 17.679 5.133   10.535  0.70 17.58 ?  24  VAL   A CB   1 
ATOM   466  C  CB   B VAL   A 1 24  ? 17.726 4.886   10.194  0.30 17.39 ?  24  VAL   A CB   1 
ATOM   467  C  CG1  A VAL   A 1 24  ? 18.157 6.182   11.533  0.70 18.42 ?  24  VAL   A CG1  1 
ATOM   468  C  CG1  B VAL   A 1 24  ? 18.367 5.949   11.070  0.30 17.99 ?  24  VAL   A CG1  1 
ATOM   469  C  CG2  A VAL   A 1 24  ? 18.426 5.256   9.218   0.70 17.97 ?  24  VAL   A CG2  1 
ATOM   470  C  CG2  B VAL   A 1 24  ? 18.362 4.860   8.818   0.30 17.51 ?  24  VAL   A CG2  1 
ATOM   471  H  H    A VAL   A 1 24  ? 16.691 3.074   9.640   0.70 19.08 ?  24  VAL   A H    1 
ATOM   472  H  H    B VAL   A 1 24  ? 16.694 2.813   9.400   0.30 18.66 ?  24  VAL   A H    1 
ATOM   473  H  HA   A VAL   A 1 24  ? 18.787 3.512   11.135  0.70 20.42 ?  24  VAL   A HA   1 
ATOM   474  H  HA   B VAL   A 1 24  ? 18.779 3.282   10.922  0.30 20.21 ?  24  VAL   A HA   1 
ATOM   475  H  HB   A VAL   A 1 24  ? 16.740 5.296   10.358  0.70 21.06 ?  24  VAL   A HB   1 
ATOM   476  H  HB   B VAL   A 1 24  ? 16.788 5.111   10.086  0.30 20.83 ?  24  VAL   A HB   1 
ATOM   477  H  HG11 A VAL   A 1 24  ? 18.320 7.011   11.061  0.70 22.06 ?  24  VAL   A HG11 1 
ATOM   478  H  HG11 B VAL   A 1 24  ? 18.452 6.768   10.559  0.30 21.55 ?  24  VAL   A HG11 1 
ATOM   479  H  HG12 A VAL   A 1 24  ? 17.472 6.312   12.206  0.70 22.06 ?  24  VAL   A HG12 1 
ATOM   480  H  HG12 B VAL   A 1 24  ? 17.805 6.102   11.846  0.30 21.55 ?  24  VAL   A HG12 1 
ATOM   481  H  HG13 A VAL   A 1 24  ? 18.978 5.869   11.946  0.70 22.06 ?  24  VAL   A HG13 1 
ATOM   482  H  HG13 B VAL   A 1 24  ? 19.242 5.640   11.349  0.30 21.55 ?  24  VAL   A HG13 1 
ATOM   483  H  HG21 A VAL   A 1 24  ? 18.291 6.146   8.857   0.70 21.53 ?  24  VAL   A HG21 1 
ATOM   484  H  HG21 B VAL   A 1 24  ? 18.523 5.769   8.527   0.30 20.97 ?  24  VAL   A HG21 1 
ATOM   485  H  HG22 A VAL   A 1 24  ? 19.373 5.104   9.375   0.70 21.53 ?  24  VAL   A HG22 1 
ATOM   486  H  HG22 B VAL   A 1 24  ? 19.201 4.376   8.871   0.30 20.97 ?  24  VAL   A HG22 1 
ATOM   487  H  HG23 A VAL   A 1 24  ? 18.086 4.592   8.596   0.70 21.53 ?  24  VAL   A HG23 1 
ATOM   488  H  HG23 B VAL   A 1 24  ? 17.763 4.412   8.203   0.30 20.97 ?  24  VAL   A HG23 1 
ATOM   489  N  N    A GLU   A 1 25  ? 15.999 3.670   12.706  0.70 19.45 ?  25  GLU   A N    1 
ATOM   490  N  N    B GLU   A 1 25  ? 15.937 3.456   12.386  0.30 19.22 ?  25  GLU   A N    1 
ATOM   491  C  CA   A GLU   A 1 25  ? 15.417 3.596   14.041  0.70 21.24 ?  25  GLU   A CA   1 
ATOM   492  C  CA   B GLU   A 1 25  ? 15.327 3.434   13.711  0.30 20.67 ?  25  GLU   A CA   1 
ATOM   493  C  C    A GLU   A 1 25  ? 15.654 2.228   14.669  0.70 20.11 ?  25  GLU   A C    1 
ATOM   494  C  C    B GLU   A 1 25  ? 15.569 2.108   14.417  0.30 20.40 ?  25  GLU   A C    1 
ATOM   495  O  O    A GLU   A 1 25  ? 15.906 2.131   15.875  0.70 20.77 ?  25  GLU   A O    1 
ATOM   496  O  O    B GLU   A 1 25  ? 15.723 2.080   15.643  0.30 20.68 ?  25  GLU   A O    1 
ATOM   497  C  CB   A GLU   A 1 25  ? 13.927 3.943   13.989  0.70 24.14 ?  25  GLU   A CB   1 
ATOM   498  C  CB   B GLU   A 1 25  ? 13.830 3.737   13.617  0.30 22.56 ?  25  GLU   A CB   1 
ATOM   499  C  CG   A GLU   A 1 25  ? 13.658 5.389   13.584  0.70 27.88 ?  25  GLU   A CG   1 
ATOM   500  C  CG   B GLU   A 1 25  ? 13.527 5.177   13.226  0.30 24.91 ?  25  GLU   A CG   1 
ATOM   501  C  CD   A GLU   A 1 25  ? 14.379 6.393   14.470  0.70 31.15 ?  25  GLU   A CD   1 
ATOM   502  C  CD   B GLU   A 1 25  ? 14.313 6.193   14.032  0.30 26.86 ?  25  GLU   A CD   1 
ATOM   503  O  OE1  A GLU   A 1 25  ? 14.479 6.152   15.693  0.70 32.29 ?  25  GLU   A OE1  1 
ATOM   504  O  OE1  B GLU   A 1 25  ? 14.444 6.009   15.261  0.30 27.81 ?  25  GLU   A OE1  1 
ATOM   505  O  OE2  A GLU   A 1 25  ? 14.863 7.414   13.939  0.70 32.52 -1 25  GLU   A OE2  1 
ATOM   506  O  OE2  B GLU   A 1 25  ? 14.811 7.167   13.432  0.30 27.52 -1 25  GLU   A OE2  1 
ATOM   507  H  H    A GLU   A 1 25  ? 15.426 3.734   12.068  0.70 23.31 ?  25  GLU   A H    1 
ATOM   508  H  H    B GLU   A 1 25  ? 15.381 3.442   11.730  0.30 23.03 ?  25  GLU   A H    1 
ATOM   509  H  HA   A GLU   A 1 25  ? 15.851 4.248   14.610  0.70 25.45 ?  25  GLU   A HA   1 
ATOM   510  H  HA   B GLU   A 1 25  ? 15.743 4.118   14.252  0.30 24.76 ?  25  GLU   A HA   1 
ATOM   511  H  HB2  A GLU   A 1 25  ? 13.487 3.370   13.340  0.70 28.93 ?  25  GLU   A HB2  1 
ATOM   512  H  HB2  B GLU   A 1 25  ? 13.432 3.159   12.942  0.30 27.04 ?  25  GLU   A HB2  1 
ATOM   513  H  HB3  A GLU   A 1 25  ? 13.535 3.808   14.866  0.70 28.93 ?  25  GLU   A HB3  1 
ATOM   514  H  HB3  B GLU   A 1 25  ? 13.417 3.567   14.478  0.30 27.04 ?  25  GLU   A HB3  1 
ATOM   515  H  HG2  A GLU   A 1 25  ? 13.969 5.523   12.676  0.70 33.41 ?  25  GLU   A HG2  1 
ATOM   516  H  HG2  B GLU   A 1 25  ? 13.750 5.303   12.294  0.30 29.86 ?  25  GLU   A HG2  1 
ATOM   517  H  HG3  A GLU   A 1 25  ? 12.703 5.559   13.638  0.70 33.41 ?  25  GLU   A HG3  1 
ATOM   518  H  HG3  B GLU   A 1 25  ? 12.590 5.355   13.380  0.30 29.86 ?  25  GLU   A HG3  1 
ATOM   519  N  N    A GLU   A 1 26  ? 15.603 1.161   13.866  0.70 19.31 ?  26  GLU   A N    1 
ATOM   520  N  N    B GLU   A 1 26  ? 15.604 1.005   13.669  0.30 20.15 ?  26  GLU   A N    1 
ATOM   521  C  CA   A GLU   A 1 26  ? 15.913 -0.169  14.386  0.70 19.58 ?  26  GLU   A CA   1 
ATOM   522  C  CA   B GLU   A 1 26  ? 15.935 -0.282  14.271  0.30 20.21 ?  26  GLU   A CA   1 
ATOM   523  C  C    A GLU   A 1 26  ? 17.332 -0.216  14.938  0.70 18.25 ?  26  GLU   A C    1 
ATOM   524  C  C    B GLU   A 1 26  ? 17.364 -0.294  14.797  0.30 19.90 ?  26  GLU   A C    1 
ATOM   525  O  O    A GLU   A 1 26  ? 17.569 -0.705  16.047  0.70 18.46 ?  26  GLU   A O    1 
ATOM   526  O  O    B GLU   A 1 26  ? 17.647 -0.900  15.837  0.30 19.82 ?  26  GLU   A O    1 
ATOM   527  C  CB   A GLU   A 1 26  ? 15.759 -1.220  13.284  0.70 21.68 ?  26  GLU   A CB   1 
ATOM   528  C  CB   B GLU   A 1 26  ? 15.747 -1.400  13.248  0.30 20.61 ?  26  GLU   A CB   1 
ATOM   529  C  CG   A GLU   A 1 26  ? 14.382 -1.847  13.145  0.70 24.17 ?  26  GLU   A CG   1 
ATOM   530  C  CG   B GLU   A 1 26  ? 14.306 -1.801  13.029  0.30 21.14 ?  26  GLU   A CG   1 
ATOM   531  C  CD   A GLU   A 1 26  ? 13.967 -2.680  14.357  0.70 25.30 ?  26  GLU   A CD   1 
ATOM   532  C  CD   B GLU   A 1 26  ? 13.641 -2.295  14.292  0.30 21.15 ?  26  GLU   A CD   1 
ATOM   533  O  OE1  A GLU   A 1 26  ? 14.346 -3.872  14.474  0.70 25.83 ?  26  GLU   A OE1  1 
ATOM   534  O  OE1  B GLU   A 1 26  ? 14.314 -2.981  15.089  0.30 21.21 ?  26  GLU   A OE1  1 
ATOM   535  O  OE2  A GLU   A 1 26  ? 13.246 -2.129  15.204  0.70 26.03 -1 26  GLU   A OE2  1 
ATOM   536  O  OE2  B GLU   A 1 26  ? 12.452 -1.978  14.492  0.30 20.89 -1 26  GLU   A OE2  1 
ATOM   537  H  H    A GLU   A 1 26  ? 15.395 1.185   13.032  0.70 23.14 ?  26  GLU   A H    1 
ATOM   538  H  H    B GLU   A 1 26  ? 15.431 0.979   12.829  0.30 24.14 ?  26  GLU   A H    1 
ATOM   539  H  HA   A GLU   A 1 26  ? 15.296 -0.382  15.103  0.70 23.45 ?  26  GLU   A HA   1 
ATOM   540  H  HA   B GLU   A 1 26  ? 15.339 -0.441  15.018  0.30 24.22 ?  26  GLU   A HA   1 
ATOM   541  H  HB2  A GLU   A 1 26  ? 15.975 -0.803  12.435  0.70 25.97 ?  26  GLU   A HB2  1 
ATOM   542  H  HB2  B GLU   A 1 26  ? 16.103 -1.103  12.394  0.30 24.69 ?  26  GLU   A HB2  1 
ATOM   543  H  HB3  A GLU   A 1 26  ? 16.387 -1.935  13.461  0.70 25.97 ?  26  GLU   A HB3  1 
ATOM   544  H  HB3  B GLU   A 1 26  ? 16.234 -2.182  13.550  0.30 24.69 ?  26  GLU   A HB3  1 
ATOM   545  H  HG2  A GLU   A 1 26  ? 13.733 -1.135  13.020  0.70 28.96 ?  26  GLU   A HG2  1 
ATOM   546  H  HG2  B GLU   A 1 26  ? 13.808 -1.034  12.718  0.30 25.33 ?  26  GLU   A HG2  1 
ATOM   547  H  HG3  A GLU   A 1 26  ? 14.379 -2.434  12.375  0.70 28.96 ?  26  GLU   A HG3  1 
ATOM   548  H  HG3  B GLU   A 1 26  ? 14.273 -2.516  12.378  0.30 25.33 ?  26  GLU   A HG3  1 
ATOM   549  N  N    A ALA   A 1 27  ? 18.298 0.289   14.167  0.70 17.00 ?  27  ALA   A N    1 
ATOM   550  N  N    B ALA   A 1 27  ? 18.282 0.359   14.086  0.30 19.85 ?  27  ALA   A N    1 
ATOM   551  C  CA   A ALA   A 1 27  ? 19.690 0.248   14.606  0.70 17.09 ?  27  ALA   A CA   1 
ATOM   552  C  CA   B ALA   A 1 27  ? 19.669 0.387   14.536  0.30 20.24 ?  27  ALA   A CA   1 
ATOM   553  C  C    A ALA   A 1 27  ? 19.892 1.051   15.885  0.70 18.79 ?  27  ALA   A C    1 
ATOM   554  C  C    B ALA   A 1 27  ? 19.820 1.203   15.814  0.30 21.56 ?  27  ALA   A C    1 
ATOM   555  O  O    A ALA   A 1 27  ? 20.580 0.601   16.807  0.70 19.04 ?  27  ALA   A O    1 
ATOM   556  O  O    B ALA   A 1 27  ? 20.507 0.778   16.750  0.30 21.41 ?  27  ALA   A O    1 
ATOM   557  C  CB   A ALA   A 1 27  ? 20.611 0.762   13.496  0.70 16.75 ?  27  ALA   A CB   1 
ATOM   558  C  CB   B ALA   A 1 27  ? 20.569 0.936   13.429  0.30 19.89 ?  27  ALA   A CB   1 
ATOM   559  H  H    A ALA   A 1 27  ? 18.174 0.653   13.401  0.70 20.36 ?  27  ALA   A H    1 
ATOM   560  H  H    B ALA   A 1 27  ? 18.129 0.781   13.354  0.30 23.78 ?  27  ALA   A H    1 
ATOM   561  H  HA   A ALA   A 1 27  ? 19.931 -0.672  14.790  0.70 20.47 ?  27  ALA   A HA   1 
ATOM   562  H  HA   B ALA   A 1 27  ? 19.951 -0.520  14.726  0.30 24.26 ?  27  ALA   A HA   1 
ATOM   563  H  HB1  A ALA   A 1 27  ? 21.531 0.725   13.808  0.70 20.06 ?  27  ALA   A HB1  1 
ATOM   564  H  HB1  B ALA   A 1 27  ? 21.487 0.934   13.742  0.30 23.83 ?  27  ALA   A HB1  1 
ATOM   565  H  HB2  A ALA   A 1 27  ? 20.506 0.201   12.713  0.70 20.06 ?  27  ALA   A HB2  1 
ATOM   566  H  HB2  B ALA   A 1 27  ? 20.486 0.369   12.645  0.30 23.83 ?  27  ALA   A HB2  1 
ATOM   567  H  HB3  A ALA   A 1 27  ? 20.372 1.677   13.285  0.70 20.06 ?  27  ALA   A HB3  1 
ATOM   568  H  HB3  B ALA   A 1 27  ? 20.292 1.840   13.215  0.30 23.83 ?  27  ALA   A HB3  1 
ATOM   569  N  N    A LYS   A 1 28  ? 19.294 2.240   15.967  0.70 21.67 ?  28  LYS   A N    1 
ATOM   570  N  N    B LYS   A 1 28  ? 19.176 2.371   15.879  0.30 23.41 ?  28  LYS   A N    1 
ATOM   571  C  CA   A LYS   A 1 28  ? 19.451 3.056   17.167  0.70 24.97 ?  28  LYS   A CA   1 
ATOM   572  C  CA   B LYS   A 1 28  ? 19.313 3.219   17.060  0.30 25.56 ?  28  LYS   A CA   1 
ATOM   573  C  C    A LYS   A 1 28  ? 18.887 2.365   18.401  0.70 26.48 ?  28  LYS   A C    1 
ATOM   574  C  C    B LYS   A 1 28  ? 18.725 2.564   18.304  0.30 26.46 ?  28  LYS   A C    1 
ATOM   575  O  O    A LYS   A 1 28  ? 19.403 2.558   19.507  0.70 27.63 ?  28  LYS   A O    1 
ATOM   576  O  O    B LYS   A 1 28  ? 19.199 2.822   19.416  0.30 26.81 ?  28  LYS   A O    1 
ATOM   577  C  CB   A LYS   A 1 28  ? 18.820 4.435   16.961  0.70 27.34 ?  28  LYS   A CB   1 
ATOM   578  C  CB   B LYS   A 1 28  ? 18.665 4.582   16.816  0.30 27.12 ?  28  LYS   A CB   1 
ATOM   579  C  CG   A LYS   A 1 28  ? 19.651 5.340   16.064  0.70 29.67 ?  28  LYS   A CG   1 
ATOM   580  C  CG   B LYS   A 1 28  ? 19.499 5.497   15.937  0.30 28.72 ?  28  LYS   A CG   1 
ATOM   581  C  CD   A LYS   A 1 28  ? 19.190 6.785   16.112  0.70 32.05 ?  28  LYS   A CD   1 
ATOM   582  C  CD   B LYS   A 1 28  ? 19.005 6.934   15.977  0.30 30.34 ?  28  LYS   A CD   1 
ATOM   583  C  CE   A LYS   A 1 28  ? 17.891 6.981   15.360  0.70 33.80 ?  28  LYS   A CE   1 
ATOM   584  C  CE   B LYS   A 1 28  ? 17.707 7.103   15.211  0.30 31.60 ?  28  LYS   A CE   1 
ATOM   585  N  NZ   A LYS   A 1 28  ? 17.543 8.425   15.251  0.70 34.94 ?  28  LYS   A NZ   1 
ATOM   586  N  NZ   B LYS   A 1 28  ? 17.346 8.541   15.068  0.30 32.35 ?  28  LYS   A NZ   1 
ATOM   587  H  H    A LYS   A 1 28  ? 18.803 2.585   15.360  0.70 25.96 ?  28  LYS   A H    1 
ATOM   588  H  H    B LYS   A 1 28  ? 18.666 2.688   15.265  0.30 28.05 ?  28  LYS   A H    1 
ATOM   589  H  HA   A LYS   A 1 28  ? 20.394 3.192   17.331  0.70 29.93 ?  28  LYS   A HA   1 
ATOM   590  H  HA   B LYS   A 1 28  ? 20.255 3.367   17.225  0.30 30.63 ?  28  LYS   A HA   1 
ATOM   591  H  HB2  A LYS   A 1 28  ? 17.950 4.327   16.548  0.70 32.77 ?  28  LYS   A HB2  1 
ATOM   592  H  HB2  B LYS   A 1 28  ? 17.809 4.449   16.381  0.30 32.51 ?  28  LYS   A HB2  1 
ATOM   593  H  HB3  A LYS   A 1 28  ? 18.727 4.875   17.820  0.70 32.77 ?  28  LYS   A HB3  1 
ATOM   594  H  HB3  B LYS   A 1 28  ? 18.537 5.023   17.671  0.30 32.51 ?  28  LYS   A HB3  1 
ATOM   595  H  HG2  A LYS   A 1 28  ? 20.576 5.311   16.352  0.70 35.57 ?  28  LYS   A HG2  1 
ATOM   596  H  HG2  B LYS   A 1 28  ? 20.418 5.485   16.247  0.30 34.43 ?  28  LYS   A HG2  1 
ATOM   597  H  HG3  A LYS   A 1 28  ? 19.577 5.032   15.147  0.70 35.57 ?  28  LYS   A HG3  1 
ATOM   598  H  HG3  B LYS   A 1 28  ? 19.452 5.187   15.020  0.30 34.43 ?  28  LYS   A HG3  1 
ATOM   599  H  HD2  A LYS   A 1 28  ? 19.048 7.047   17.035  0.70 38.42 ?  28  LYS   A HD2  1 
ATOM   600  H  HD2  B LYS   A 1 28  ? 18.848 7.193   16.900  0.30 36.37 ?  28  LYS   A HD2  1 
ATOM   601  H  HD3  A LYS   A 1 28  ? 19.865 7.350   15.704  0.70 38.42 ?  28  LYS   A HD3  1 
ATOM   602  H  HD3  B LYS   A 1 28  ? 19.672 7.512   15.576  0.30 36.37 ?  28  LYS   A HD3  1 
ATOM   603  H  HE2  A LYS   A 1 28  ? 17.983 6.620   14.464  0.70 40.53 ?  28  LYS   A HE2  1 
ATOM   604  H  HE2  B LYS   A 1 28  ? 17.808 6.724   14.324  0.30 37.88 ?  28  LYS   A HE2  1 
ATOM   605  H  HE3  A LYS   A 1 28  ? 17.176 6.529   15.834  0.70 40.53 ?  28  LYS   A HE3  1 
ATOM   606  H  HE3  B LYS   A 1 28  ? 16.992 6.654   15.689  0.30 37.88 ?  28  LYS   A HE3  1 
ATOM   607  H  HZ1  A LYS   A 1 28  ? 16.779 8.521   14.807  0.70 41.89 ?  28  LYS   A HZ1  1 
ATOM   608  H  HZ1  B LYS   A 1 28  ? 16.584 8.620   14.616  0.30 38.78 ?  28  LYS   A HZ1  1 
ATOM   609  H  HZ2  A LYS   A 1 28  ? 17.453 8.778   16.063  0.70 41.89 ?  28  LYS   A HZ2  1 
ATOM   610  H  HZ2  B LYS   A 1 28  ? 17.246 8.910   15.871  0.30 38.78 ?  28  LYS   A HZ2  1 
ATOM   611  H  HZ3  A LYS   A 1 28  ? 18.187 8.861   14.817  0.70 41.89 ?  28  LYS   A HZ3  1 
ATOM   612  H  HZ3  B LYS   A 1 28  ? 17.989 8.973   14.629  0.30 38.78 ?  28  LYS   A HZ3  1 
ATOM   613  N  N    A LYS   A 1 29  ? 17.850 1.542   18.233  0.70 27.31 ?  29  LYS   A N    1 
ATOM   614  N  N    B LYS   A 1 29  ? 17.701 1.726   18.143  0.30 27.23 ?  29  LYS   A N    1 
ATOM   615  C  CA   A LYS   A 1 29  ? 17.254 0.843   19.368  0.70 28.82 ?  29  LYS   A CA   1 
ATOM   616  C  CA   B LYS   A 1 29  ? 17.092 1.063   19.291  0.30 28.16 ?  29  LYS   A CA   1 
ATOM   617  C  C    A LYS   A 1 29  ? 18.071 -0.384  19.758  0.70 28.14 ?  29  LYS   A C    1 
ATOM   618  C  C    B LYS   A 1 29  ? 17.880 -0.175  19.703  0.30 27.31 ?  29  LYS   A C    1 
ATOM   619  O  O    A LYS   A 1 29  ? 18.402 -0.573  20.934  0.70 29.11 ?  29  LYS   A O    1 
ATOM   620  O  O    B LYS   A 1 29  ? 18.165 -0.372  20.889  0.30 27.62 ?  29  LYS   A O    1 
ATOM   621  C  CB   A LYS   A 1 29  ? 15.820 0.431   19.028  0.70 31.28 ?  29  LYS   A CB   1 
ATOM   622  C  CB   B LYS   A 1 29  ? 15.647 0.684   18.964  0.30 29.95 ?  29  LYS   A CB   1 
ATOM   623  C  CG   A LYS   A 1 29  ? 15.086 -0.287  20.153  0.70 34.03 ?  29  LYS   A CG   1 
ATOM   624  C  CG   B LYS   A 1 29  ? 14.891 0.039   20.116  0.30 31.71 ?  29  LYS   A CG   1 
ATOM   625  C  CD   A LYS   A 1 29  ? 14.760 0.663   21.292  0.70 36.59 ?  29  LYS   A CD   1 
ATOM   626  C  CD   B LYS   A 1 29  ? 14.635 1.035   21.235  0.30 33.22 ?  29  LYS   A CD   1 
ATOM   627  C  CE   A LYS   A 1 29  ? 13.875 -0.002  22.334  0.70 38.36 ?  29  LYS   A CE   1 
ATOM   628  C  CE   B LYS   A 1 29  ? 13.772 0.429   22.328  0.30 34.26 ?  29  LYS   A CE   1 
ATOM   629  N  NZ   A LYS   A 1 29  ? 13.453 0.960   23.389  0.70 39.39 ?  29  LYS   A NZ   1 
ATOM   630  N  NZ   B LYS   A 1 29  ? 13.480 1.412   23.405  0.30 34.85 ?  29  LYS   A NZ   1 
ATOM   631  H  H    A LYS   A 1 29  ? 17.475 1.373   17.479  0.70 32.74 ?  29  LYS   A H    1 
ATOM   632  H  H    B LYS   A 1 29  ? 17.338 1.535   17.388  0.30 32.63 ?  29  LYS   A H    1 
ATOM   633  H  HA   A LYS   A 1 29  ? 17.222 1.440   20.132  0.70 34.55 ?  29  LYS   A HA   1 
ATOM   634  H  HA   B LYS   A 1 29  ? 17.083 1.674   20.043  0.30 33.76 ?  29  LYS   A HA   1 
ATOM   635  H  HB2  A LYS   A 1 29  ? 15.310 1.227   18.811  0.70 37.50 ?  29  LYS   A HB2  1 
ATOM   636  H  HB2  B LYS   A 1 29  ? 15.167 1.486   18.710  0.30 35.90 ?  29  LYS   A HB2  1 
ATOM   637  H  HB3  A LYS   A 1 29  ? 15.839 -0.165  18.264  0.70 37.50 ?  29  LYS   A HB3  1 
ATOM   638  H  HB3  B LYS   A 1 29  ? 15.651 0.055   18.226  0.30 35.90 ?  29  LYS   A HB3  1 
ATOM   639  H  HG2  A LYS   A 1 29  ? 14.253 -0.647  19.812  0.70 40.80 ?  29  LYS   A HG2  1 
ATOM   640  H  HG2  B LYS   A 1 29  ? 14.035 -0.282  19.794  0.30 38.02 ?  29  LYS   A HG2  1 
ATOM   641  H  HG3  A LYS   A 1 29  ? 15.639 -1.005  20.503  0.70 40.80 ?  29  LYS   A HG3  1 
ATOM   642  H  HG3  B LYS   A 1 29  ? 15.409 -0.699  20.476  0.30 38.02 ?  29  LYS   A HG3  1 
ATOM   643  H  HD2  A LYS   A 1 29  ? 15.583 0.941   21.724  0.70 43.87 ?  29  LYS   A HD2  1 
ATOM   644  H  HD2  B LYS   A 1 29  ? 15.480 1.302   21.628  0.30 39.82 ?  29  LYS   A HD2  1 
ATOM   645  H  HD3  A LYS   A 1 29  ? 14.289 1.434   20.940  0.70 43.87 ?  29  LYS   A HD3  1 
ATOM   646  H  HD3  B LYS   A 1 29  ? 14.172 1.808   20.875  0.30 39.82 ?  29  LYS   A HD3  1 
ATOM   647  H  HE2  A LYS   A 1 29  ? 13.078 -0.349  21.903  0.70 45.99 ?  29  LYS   A HE2  1 
ATOM   648  H  HE2  B LYS   A 1 29  ? 12.929 0.137   21.946  0.30 41.08 ?  29  LYS   A HE2  1 
ATOM   649  H  HE3  A LYS   A 1 29  ? 14.367 -0.722  22.759  0.70 45.99 ?  29  LYS   A HE3  1 
ATOM   650  H  HE3  B LYS   A 1 29  ? 14.239 -0.325  22.723  0.30 41.08 ?  29  LYS   A HE3  1 
ATOM   651  H  HZ1  A LYS   A 1 29  ? 12.937 0.549   23.986  0.70 47.23 ?  29  LYS   A HZ1  1 
ATOM   652  H  HZ1  B LYS   A 1 29  ? 12.975 1.034   24.033  0.30 41.79 ?  29  LYS   A HZ1  1 
ATOM   653  H  HZ2  A LYS   A 1 29  ? 14.168 1.290   23.803  0.70 47.23 ?  29  LYS   A HZ2  1 
ATOM   654  H  HZ2  B LYS   A 1 29  ? 14.240 1.692   23.775  0.30 41.79 ?  29  LYS   A HZ2  1 
ATOM   655  H  HZ3  A LYS   A 1 29  ? 12.995 1.630   23.024  0.70 47.23 ?  29  LYS   A HZ3  1 
ATOM   656  H  HZ3  B LYS   A 1 29  ? 13.047 2.113   23.067  0.30 41.79 ?  29  LYS   A HZ3  1 
ATOM   657  N  N    A VAL   A 1 30  ? 18.387 -1.238  18.784  0.70 26.14 ?  30  VAL   A N    1 
ATOM   658  N  N    B VAL   A 1 30  ? 18.231 -1.024  18.737  0.30 26.20 ?  30  VAL   A N    1 
ATOM   659  C  CA   A VAL   A 1 30  ? 19.042 -2.507  19.080  0.70 24.88 ?  30  VAL   A CA   1 
ATOM   660  C  CA   B VAL   A 1 30  ? 18.875 -2.295  19.055  0.30 25.23 ?  30  VAL   A CA   1 
ATOM   661  C  C    A VAL   A 1 30  ? 20.539 -2.327  19.301  0.70 23.34 ?  30  VAL   A C    1 
ATOM   662  C  C    B VAL   A 1 30  ? 20.371 -2.114  19.282  0.30 24.58 ?  30  VAL   A C    1 
ATOM   663  O  O    A VAL   A 1 30  ? 21.140 -3.045  20.108  0.70 23.64 ?  30  VAL   A O    1 
ATOM   664  O  O    B VAL   A 1 30  ? 20.963 -2.777  20.140  0.30 24.38 ?  30  VAL   A O    1 
ATOM   665  C  CB   A VAL   A 1 30  ? 18.765 -3.513  17.948  0.70 25.00 ?  30  VAL   A CB   1 
ATOM   666  C  CB   B VAL   A 1 30  ? 18.586 -3.321  17.942  0.30 25.01 ?  30  VAL   A CB   1 
ATOM   667  C  CG1  A VAL   A 1 30  ? 19.554 -4.803  18.162  0.70 25.32 ?  30  VAL   A CG1  1 
ATOM   668  C  CG1  B VAL   A 1 30  ? 19.311 -4.632  18.218  0.30 25.06 ?  30  VAL   A CG1  1 
ATOM   669  C  CG2  A VAL   A 1 30  ? 17.275 -3.804  17.843  0.70 25.20 ?  30  VAL   A CG2  1 
ATOM   670  C  CG2  B VAL   A 1 30  ? 17.088 -3.553  17.807  0.30 25.04 ?  30  VAL   A CG2  1 
ATOM   671  H  H    A VAL   A 1 30  ? 18.222 -1.112  17.952  0.70 31.33 ?  30  VAL   A H    1 
ATOM   672  H  H    B VAL   A 1 30  ? 18.101 -0.892  17.897  0.30 31.40 ?  30  VAL   A H    1 
ATOM   673  H  HA   A VAL   A 1 30  ? 18.657 -2.874  19.893  0.70 29.82 ?  30  VAL   A HA   1 
ATOM   674  H  HA   B VAL   A 1 30  ? 18.488 -2.640  19.874  0.30 30.24 ?  30  VAL   A HA   1 
ATOM   675  H  HB   A VAL   A 1 30  ? 19.057 -3.128  17.107  0.70 29.96 ?  30  VAL   A HB   1 
ATOM   676  H  HB   B VAL   A 1 30  ? 18.914 -2.974  17.098  0.30 29.97 ?  30  VAL   A HB   1 
ATOM   677  H  HG11 A VAL   A 1 30  ? 19.202 -5.489  17.573  0.70 30.35 ?  30  VAL   A HG11 1 
ATOM   678  H  HG11 B VAL   A 1 30  ? 18.957 -5.318  17.630  0.30 30.04 ?  30  VAL   A HG11 1 
ATOM   679  H  HG12 A VAL   A 1 30  ? 20.490 -4.644  17.958  0.70 30.35 ?  30  VAL   A HG12 1 
ATOM   680  H  HG12 B VAL   A 1 30  ? 20.260 -4.514  18.050  0.30 30.04 ?  30  VAL   A HG12 1 
ATOM   681  H  HG13 A VAL   A 1 30  ? 19.458 -5.083  19.086  0.70 30.35 ?  30  VAL   A HG13 1 
ATOM   682  H  HG13 B VAL   A 1 30  ? 19.166 -4.885  19.143  0.30 30.04 ?  30  VAL   A HG13 1 
ATOM   683  H  HG21 A VAL   A 1 30  ? 17.134 -4.467  17.148  0.70 30.20 ?  30  VAL   A HG21 1 
ATOM   684  H  HG21 B VAL   A 1 30  ? 16.934 -4.244  17.143  0.30 30.01 ?  30  VAL   A HG21 1 
ATOM   685  H  HG22 A VAL   A 1 30  ? 16.961 -4.143  18.694  0.70 30.20 ?  30  VAL   A HG22 1 
ATOM   686  H  HG22 B VAL   A 1 30  ? 16.735 -3.835  18.665  0.30 30.01 ?  30  VAL   A HG22 1 
ATOM   687  H  HG23 A VAL   A 1 30  ? 16.812 -2.984  17.618  0.70 30.20 ?  30  VAL   A HG23 1 
ATOM   688  H  HG23 B VAL   A 1 30  ? 16.666 -2.727  17.529  0.30 30.01 ?  30  VAL   A HG23 1 
ATOM   689  N  N    A LYS   A 1 31  ? 21.162 -1.382  18.606  0.70 22.80 ?  31  LYS   A N    1 
ATOM   690  N  N    B LYS   A 1 31  ? 20.999 -1.216  18.532  0.30 24.62 ?  31  LYS   A N    1 
ATOM   691  C  CA   A LYS   A 1 31  ? 22.614 -1.266  18.550  0.70 23.63 ?  31  LYS   A CA   1 
ATOM   692  C  CA   B LYS   A 1 31  ? 22.452 -1.107  18.473  0.30 25.11 ?  31  LYS   A CA   1 
ATOM   693  C  C    A LYS   A 1 31  ? 23.232 -2.625  18.211  0.70 20.93 ?  31  LYS   A C    1 
ATOM   694  C  C    B LYS   A 1 31  ? 23.076 -2.482  18.216  0.30 22.96 ?  31  LYS   A C    1 
ATOM   695  O  O    A LYS   A 1 31  ? 24.014 -3.173  18.996  0.70 21.25 ?  31  LYS   A O    1 
ATOM   696  O  O    B LYS   A 1 31  ? 23.812 -3.004  19.059  0.30 23.18 ?  31  LYS   A O    1 
ATOM   697  C  CB   A LYS   A 1 31  ? 23.195 -0.710  19.842  0.70 28.09 ?  31  LYS   A CB   1 
ATOM   698  C  CB   B LYS   A 1 31  ? 23.028 -0.476  19.732  0.30 28.01 ?  31  LYS   A CB   1 
ATOM   699  C  CG   A LYS   A 1 31  ? 22.507 0.546   20.342  0.70 32.68 ?  31  LYS   A CG   1 
ATOM   700  C  CG   B LYS   A 1 31  ? 22.374 0.829   20.136  0.30 30.96 ?  31  LYS   A CG   1 
ATOM   701  C  CD   A LYS   A 1 31  ? 23.514 1.614   20.737  0.70 36.22 ?  31  LYS   A CD   1 
ATOM   702  C  CD   B LYS   A 1 31  ? 23.401 1.813   20.667  0.30 33.37 ?  31  LYS   A CD   1 
ATOM   703  C  CE   A LYS   A 1 31  ? 22.884 2.657   21.645  0.70 38.60 ?  31  LYS   A CE   1 
ATOM   704  C  CE   B LYS   A 1 31  ? 22.757 2.867   21.548  0.30 35.06 ?  31  LYS   A CE   1 
ATOM   705  N  NZ   A LYS   A 1 31  ? 21.647 3.245   21.064  0.70 39.89 ?  31  LYS   A NZ   1 
ATOM   706  N  NZ   B LYS   A 1 31  ? 21.529 3.443   20.935  0.30 35.99 ?  31  LYS   A NZ   1 
ATOM   707  H  H    A LYS   A 1 31  ? 20.750 -0.786  18.150  0.70 27.32 ?  31  LYS   A H    1 
ATOM   708  H  H    B LYS   A 1 31  ? 20.595 -0.644  18.041  0.30 29.51 ?  31  LYS   A H    1 
ATOM   709  H  HA   A LYS   A 1 31  ? 22.839 -0.652  17.840  0.70 28.32 ?  31  LYS   A HA   1 
ATOM   710  H  HA   B LYS   A 1 31  ? 22.683 -0.535  17.732  0.30 30.10 ?  31  LYS   A HA   1 
ATOM   711  H  HB2  A LYS   A 1 31  ? 23.121 -1.387  20.527  0.70 33.68 ?  31  LYS   A HB2  1 
ATOM   712  H  HB2  B LYS   A 1 31  ? 22.902 -1.096  20.459  0.30 33.58 ?  31  LYS   A HB2  1 
ATOM   713  H  HB3  A LYS   A 1 31  ? 24.131 -0.495  19.693  0.70 33.68 ?  31  LYS   A HB3  1 
ATOM   714  H  HB3  B LYS   A 1 31  ? 23.978 -0.310  19.599  0.30 33.58 ?  31  LYS   A HB3  1 
ATOM   715  H  HG2  A LYS   A 1 31  ? 21.944 0.906   19.640  0.70 39.17 ?  31  LYS   A HG2  1 
ATOM   716  H  HG2  B LYS   A 1 31  ? 21.940 1.223   19.364  0.30 37.11 ?  31  LYS   A HG2  1 
ATOM   717  H  HG3  A LYS   A 1 31  ? 21.973 0.330   21.123  0.70 39.17 ?  31  LYS   A HG3  1 
ATOM   718  H  HG3  B LYS   A 1 31  ? 21.724 0.658   20.837  0.30 37.11 ?  31  LYS   A HG3  1 
ATOM   719  H  HD2  A LYS   A 1 31  ? 24.252 1.202   21.213  0.70 43.42 ?  31  LYS   A HD2  1 
ATOM   720  H  HD2  B LYS   A 1 31  ? 24.061 1.335   21.195  0.30 40.00 ?  31  LYS   A HD2  1 
ATOM   721  H  HD3  A LYS   A 1 31  ? 23.838 2.062   19.938  0.70 43.42 ?  31  LYS   A HD3  1 
ATOM   722  H  HD3  B LYS   A 1 31  ? 23.830 2.260   19.920  0.30 40.00 ?  31  LYS   A HD3  1 
ATOM   723  H  HE2  A LYS   A 1 31  ? 22.651 2.241   22.490  0.70 46.28 ?  31  LYS   A HE2  1 
ATOM   724  H  HE2  B LYS   A 1 31  ? 22.515 2.464   22.396  0.30 42.03 ?  31  LYS   A HE2  1 
ATOM   725  H  HE3  A LYS   A 1 31  ? 23.519 3.376   21.791  0.70 46.28 ?  31  LYS   A HE3  1 
ATOM   726  H  HE3  B LYS   A 1 31  ? 23.388 3.588   21.692  0.30 42.03 ?  31  LYS   A HE3  1 
ATOM   727  H  HZ1  A LYS   A 1 31  ? 21.327 3.875   21.605  0.70 47.83 ?  31  LYS   A HZ1  1 
ATOM   728  H  HZ1  B LYS   A 1 31  ? 21.223 4.110   21.438  0.30 43.15 ?  31  LYS   A HZ1  1 
ATOM   729  H  HZ2  A LYS   A 1 31  ? 21.826 3.608   20.272  0.70 47.83 ?  31  LYS   A HZ2  1 
ATOM   730  H  HZ2  B LYS   A 1 31  ? 21.713 3.753   20.122  0.30 43.15 ?  31  LYS   A HZ2  1 
ATOM   731  H  HZ3  A LYS   A 1 31  ? 21.029 2.613   20.959  0.70 47.83 ?  31  LYS   A HZ3  1 
ATOM   732  H  HZ3  B LYS   A 1 31  ? 20.899 2.817   20.869  0.30 43.15 ?  31  LYS   A HZ3  1 
ATOM   733  N  N    A PRO   A 1 32  ? 22.902 -3.188  17.053  0.70 18.83 ?  32  PRO   A N    1 
ATOM   734  N  N    B PRO   A 1 32  ? 22.802 -3.087  17.064  0.30 20.93 ?  32  PRO   A N    1 
ATOM   735  C  CA   A PRO   A 1 32  ? 23.378 -4.531  16.724  0.70 18.72 ?  32  PRO   A CA   1 
ATOM   736  C  CA   B PRO   A 1 32  ? 23.287 -4.445  16.808  0.30 20.00 ?  32  PRO   A CA   1 
ATOM   737  C  C    A PRO   A 1 32  ? 24.879 -4.553  16.501  0.70 18.54 ?  32  PRO   A C    1 
ATOM   738  C  C    B PRO   A 1 32  ? 24.793 -4.463  16.610  0.30 19.10 ?  32  PRO   A C    1 
ATOM   739  O  O    A PRO   A 1 32  ? 25.521 -3.530  16.254  0.70 18.24 ?  32  PRO   A O    1 
ATOM   740  O  O    B PRO   A 1 32  ? 25.456 -3.430  16.500  0.30 18.92 ?  32  PRO   A O    1 
ATOM   741  C  CB   A PRO   A 1 32  ? 22.645 -4.845  15.418  0.70 18.81 ?  32  PRO   A CB   1 
ATOM   742  C  CB   B PRO   A 1 32  ? 22.559 -4.831  15.520  0.30 20.10 ?  32  PRO   A CB   1 
ATOM   743  C  CG   A PRO   A 1 32  ? 22.477 -3.509  14.779  0.70 18.53 ?  32  PRO   A CG   1 
ATOM   744  C  CG   B PRO   A 1 32  ? 22.384 -3.536  14.807  0.30 20.20 ?  32  PRO   A CG   1 
ATOM   745  C  CD   A PRO   A 1 32  ? 22.184 -2.575  15.923  0.70 18.24 ?  32  PRO   A CD   1 
ATOM   746  C  CD   B PRO   A 1 32  ? 22.120 -2.519  15.888  0.30 20.37 ?  32  PRO   A CD   1 
ATOM   747  H  HA   A PRO   A 1 32  ? 23.123 -5.167  17.414  0.70 22.42 ?  32  PRO   A HA   1 
ATOM   748  H  HA   B PRO   A 1 32  ? 23.038 -5.047  17.526  0.30 23.96 ?  32  PRO   A HA   1 
ATOM   749  H  HB2  A PRO   A 1 32  ? 23.193 -5.430  14.867  0.70 22.54 ?  32  PRO   A HB2  1 
ATOM   750  H  HB2  B PRO   A 1 32  ? 23.104 -5.443  15.000  0.30 24.08 ?  32  PRO   A HB2  1 
ATOM   751  H  HB3  A PRO   A 1 32  ? 21.787 -5.254  15.608  0.70 22.54 ?  32  PRO   A HB3  1 
ATOM   752  H  HB3  B PRO   A 1 32  ? 21.699 -5.228  15.732  0.30 24.08 ?  32  PRO   A HB3  1 
ATOM   753  H  HG2  A PRO   A 1 32  ? 23.298 -3.261  14.327  0.70 22.20 ?  32  PRO   A HG2  1 
ATOM   754  H  HG2  B PRO   A 1 32  ? 23.197 -3.320  14.323  0.30 24.20 ?  32  PRO   A HG2  1 
ATOM   755  H  HG3  A PRO   A 1 32  ? 21.735 -3.541  14.156  0.70 22.20 ?  32  PRO   A HG3  1 
ATOM   756  H  HG3  B PRO   A 1 32  ? 21.631 -3.597  14.199  0.30 24.20 ?  32  PRO   A HG3  1 
ATOM   757  H  HD2  A PRO   A 1 32  ? 22.539 -1.693  15.727  0.70 21.85 ?  32  PRO   A HD2  1 
ATOM   758  H  HD2  B PRO   A 1 32  ? 22.509 -1.664  15.645  0.30 24.41 ?  32  PRO   A HD2  1 
ATOM   759  H  HD3  A PRO   A 1 32  ? 21.233 -2.548  16.097  0.70 21.85 ?  32  PRO   A HD3  1 
ATOM   760  H  HD3  B PRO   A 1 32  ? 21.168 -2.445  16.051  0.30 24.41 ?  32  PRO   A HD3  1 
ATOM   761  N  N    A THR   A 1 33  ? 25.433 -5.762  16.568  0.70 18.72 ?  33  THR   A N    1 
ATOM   762  N  N    B THR   A 1 33  ? 25.335 -5.680  16.565  0.30 18.67 ?  33  THR   A N    1 
ATOM   763  C  CA   A THR   A 1 33  ? 26.845 -5.938  16.253  0.70 18.78 ?  33  THR   A CA   1 
ATOM   764  C  CA   B THR   A 1 33  ? 26.755 -5.840  16.275  0.30 18.28 ?  33  THR   A CA   1 
ATOM   765  C  C    A THR   A 1 33  ? 27.147 -5.479  14.833  0.70 17.43 ?  33  THR   A C    1 
ATOM   766  C  C    B THR   A 1 33  ? 27.074 -5.380  14.857  0.30 17.00 ?  33  THR   A C    1 
ATOM   767  O  O    A THR   A 1 33  ? 28.186 -4.851  14.582  0.70 17.38 ?  33  THR   A O    1 
ATOM   768  O  O    B THR   A 1 33  ? 28.056 -4.662  14.631  0.30 16.87 ?  33  THR   A O    1 
ATOM   769  C  CB   A THR   A 1 33  ? 27.238 -7.403  16.442  0.70 20.59 ?  33  THR   A CB   1 
ATOM   770  C  CB   B THR   A 1 33  ? 27.163 -7.300  16.480  0.30 19.39 ?  33  THR   A CB   1 
ATOM   771  O  OG1  A THR   A 1 33  ? 26.958 -7.804  17.788  0.70 22.24 ?  33  THR   A OG1  1 
ATOM   772  O  OG1  B THR   A 1 33  ? 26.836 -7.704  17.815  0.30 20.30 ?  33  THR   A OG1  1 
ATOM   773  C  CG2  A THR   A 1 33  ? 28.718 -7.603  16.162  0.70 21.17 ?  33  THR   A CG2  1 
ATOM   774  C  CG2  B THR   A 1 33  ? 28.658 -7.477  16.253  0.30 19.75 ?  33  THR   A CG2  1 
ATOM   775  H  H    A THR   A 1 33  ? 25.018 -6.485  16.785  0.70 22.43 ?  33  THR   A H    1 
ATOM   776  H  H    B THR   A 1 33  ? 24.910 -6.416  16.702  0.30 22.36 ?  33  THR   A H    1 
ATOM   777  H  HA   A THR   A 1 33  ? 27.376 -5.403  16.863  0.70 22.50 ?  33  THR   A HA   1 
ATOM   778  H  HA   B THR   A 1 33  ? 27.269 -5.296  16.890  0.30 21.90 ?  33  THR   A HA   1 
ATOM   779  H  HB   A THR   A 1 33  ? 26.729 -7.958  15.828  0.70 24.67 ?  33  THR   A HB   1 
ATOM   780  H  HB   B THR   A 1 33  ? 26.688 -7.863  15.847  0.30 23.23 ?  33  THR   A HB   1 
ATOM   781  H  HG1  A THR   A 1 33  ? 27.394 -7.331  18.327  0.70 26.65 ?  33  THR   A HG1  1 
ATOM   782  H  HG1  B THR   A 1 33  ? 27.248 -7.226  18.370  0.30 24.32 ?  33  THR   A HG1  1 
ATOM   783  H  HG21 A THR   A 1 33  ? 28.991 -8.488  16.450  0.70 25.37 ?  33  THR   A HG21 1 
ATOM   784  H  HG21 B THR   A 1 33  ? 28.935 -8.359  16.547  0.30 23.66 ?  33  THR   A HG21 1 
ATOM   785  H  HG22 A THR   A 1 33  ? 28.892 -7.514  15.213  0.70 25.37 ?  33  THR   A HG22 1 
ATOM   786  H  HG22 B THR   A 1 33  ? 28.867 -7.381  15.311  0.30 23.66 ?  33  THR   A HG22 1 
ATOM   787  H  HG23 A THR   A 1 33  ? 29.236 -6.941  16.644  0.70 25.37 ?  33  THR   A HG23 1 
ATOM   788  H  HG23 B THR   A 1 33  ? 29.150 -6.809  16.756  0.30 23.66 ?  33  THR   A HG23 1 
ATOM   789  N  N    . VAL   A 1 34  ? 26.248 -5.779  13.891  1.00 16.02 ?  34  VAL   A N    1 
ATOM   790  C  CA   . VAL   A 1 34  ? 26.440 -5.447  12.484  1.00 14.79 ?  34  VAL   A CA   1 
ATOM   791  C  C    . VAL   A 1 34  ? 25.141 -4.890  11.913  1.00 14.10 ?  34  VAL   A C    1 
ATOM   792  O  O    . VAL   A 1 34  ? 24.100 -5.558  11.957  1.00 14.55 ?  34  VAL   A O    1 
ATOM   793  C  CB   . VAL   A 1 34  ? 26.892 -6.663  11.653  1.00 15.22 ?  34  VAL   A CB   1 
ATOM   794  C  CG1  . VAL   A 1 34  ? 27.051 -6.269  10.187  1.00 15.26 ?  34  VAL   A CG1  1 
ATOM   795  C  CG2  . VAL   A 1 34  ? 28.185 -7.273  12.205  1.00 16.11 ?  34  VAL   A CG2  1 
ATOM   796  H  H    A VAL   A 1 34  ? 25.506 -6.189  14.050  0.70 19.18 ?  34  VAL   A H    1 
ATOM   797  H  H    B VAL   A 1 34  ? 25.545 -6.259  14.033  0.30 19.18 ?  34  VAL   A H    1 
ATOM   798  H  HA   . VAL   A 1 34  ? 27.120 -4.757  12.408  1.00 17.71 ?  34  VAL   A HA   1 
ATOM   799  H  HB   . VAL   A 1 34  ? 26.205 -7.344  11.700  1.00 18.23 ?  34  VAL   A HB   1 
ATOM   800  H  HG11 . VAL   A 1 34  ? 27.546 -6.966  9.727   1.00 18.28 ?  34  VAL   A HG11 1 
ATOM   801  H  HG12 . VAL   A 1 34  ? 26.173 -6.172  9.787   1.00 18.28 ?  34  VAL   A HG12 1 
ATOM   802  H  HG13 . VAL   A 1 34  ? 27.536 -5.432  10.136  1.00 18.28 ?  34  VAL   A HG13 1 
ATOM   803  H  HG21 . VAL   A 1 34  ? 28.469 -7.996  11.622  1.00 19.29 ?  34  VAL   A HG21 1 
ATOM   804  H  HG22 . VAL   A 1 34  ? 28.871 -6.586  12.235  1.00 19.29 ?  34  VAL   A HG22 1 
ATOM   805  H  HG23 . VAL   A 1 34  ? 28.019 -7.614  13.096  1.00 19.29 ?  34  VAL   A HG23 1 
ATOM   806  N  N    . VAL   A 1 35  ? 25.215 -3.688  11.347  1.00 13.48 ?  35  VAL   A N    1 
ATOM   807  C  CA   . VAL   A 1 35  ? 24.187 -3.171  10.454  1.00 12.87 ?  35  VAL   A CA   1 
ATOM   808  C  C    . VAL   A 1 35  ? 24.742 -3.174  9.037   1.00 12.29 ?  35  VAL   A C    1 
ATOM   809  O  O    . VAL   A 1 35  ? 25.893 -2.787  8.811   1.00 12.88 ?  35  VAL   A O    1 
ATOM   810  C  CB   . VAL   A 1 35  ? 23.658 -1.779  10.864  1.00 13.44 ?  35  VAL   A CB   1 
ATOM   811  C  CG1  . VAL   A 1 35  ? 24.723 -0.694  10.733  1.00 14.08 ?  35  VAL   A CG1  1 
ATOM   812  C  CG2  . VAL   A 1 35  ? 22.427 -1.421  10.034  1.00 13.91 ?  35  VAL   A CG2  1 
ATOM   813  H  H    . VAL   A 1 35  ? 25.868 -3.140  11.460  1.00 16.14 ?  35  VAL   A H    1 
ATOM   814  H  HA   . VAL   A 1 35  ? 23.429 -3.779  10.472  1.00 15.41 ?  35  VAL   A HA   1 
ATOM   815  H  HB   . VAL   A 1 35  ? 23.381 -1.808  11.791  1.00 16.09 ?  35  VAL   A HB   1 
ATOM   816  H  HG11 . VAL   A 1 35  ? 24.383 0.131   11.113  1.00 16.86 ?  35  VAL   A HG11 1 
ATOM   817  H  HG12 . VAL   A 1 35  ? 25.517 -0.977  11.211  1.00 16.86 ?  35  VAL   A HG12 1 
ATOM   818  H  HG13 . VAL   A 1 35  ? 24.932 -0.564  9.794   1.00 16.86 ?  35  VAL   A HG13 1 
ATOM   819  H  HG21 . VAL   A 1 35  ? 22.068 -0.578  10.346  1.00 16.66 ?  35  VAL   A HG21 1 
ATOM   820  H  HG22 . VAL   A 1 35  ? 22.686 -1.345  9.100   1.00 16.66 ?  35  VAL   A HG22 1 
ATOM   821  H  HG23 . VAL   A 1 35  ? 21.765 -2.123  10.135  1.00 16.66 ?  35  VAL   A HG23 1 
ATOM   822  N  N    . VAL   A 1 36  ? 23.932 -3.632  8.087   1.00 11.71 ?  36  VAL   A N    1 
ATOM   823  C  CA   . VAL   A 1 36  ? 24.312 -3.646  6.682   1.00 11.21 ?  36  VAL   A CA   1 
ATOM   824  C  C    . VAL   A 1 36  ? 23.859 -2.355  6.020   1.00 11.51 ?  36  VAL   A C    1 
ATOM   825  O  O    . VAL   A 1 36  ? 22.698 -1.953  6.150   1.00 12.20 ?  36  VAL   A O    1 
ATOM   826  C  CB   . VAL   A 1 36  ? 23.712 -4.859  5.962   1.00 11.27 ?  36  VAL   A CB   1 
ATOM   827  C  CG1  . VAL   A 1 36  ? 23.974 -4.791  4.481   1.00 12.05 ?  36  VAL   A CG1  1 
ATOM   828  C  CG2  . VAL   A 1 36  ? 24.255 -6.155  6.545   1.00 12.14 ?  36  VAL   A CG2  1 
ATOM   829  H  H    . VAL   A 1 36  ? 23.135 -3.937  8.234   1.00 14.01 ?  36  VAL   A H    1 
ATOM   830  H  HA   . VAL   A 1 36  ? 25.277 -3.706  6.615   1.00 13.41 ?  36  VAL   A HA   1 
ATOM   831  H  HB   . VAL   A 1 36  ? 22.747 -4.856  6.093   1.00 13.49 ?  36  VAL   A HB   1 
ATOM   832  H  HG11 . VAL   A 1 36  ? 23.835 -5.669  4.093   1.00 14.42 ?  36  VAL   A HG11 1 
ATOM   833  H  HG12 . VAL   A 1 36  ? 23.360 -4.155  4.076   1.00 14.42 ?  36  VAL   A HG12 1 
ATOM   834  H  HG13 . VAL   A 1 36  ? 24.889 -4.507  4.336   1.00 14.42 ?  36  VAL   A HG13 1 
ATOM   835  H  HG21 . VAL   A 1 36  ? 23.859 -6.910  6.071   1.00 14.53 ?  36  VAL   A HG21 1 
ATOM   836  H  HG22 . VAL   A 1 36  ? 25.217 -6.173  6.445   1.00 14.53 ?  36  VAL   A HG22 1 
ATOM   837  H  HG23 . VAL   A 1 36  ? 24.018 -6.209  7.487   1.00 14.53 ?  36  VAL   A HG23 1 
ATOM   838  N  N    . ASN   A 1 37  ? 24.778 -1.720  5.294   1.00 10.62 ?  37  ASN   A N    1 
ATOM   839  C  CA   . ASN   A 1 37  ? 24.453 -0.602  4.424   1.00 10.41 ?  37  ASN   A CA   1 
ATOM   840  C  C    . ASN   A 1 37  ? 24.326 -1.069  2.983   1.00 10.71 ?  37  ASN   A C    1 
ATOM   841  O  O    . ASN   A 1 37  ? 25.113 -1.903  2.513   1.00 11.19 ?  37  ASN   A O    1 
ATOM   842  C  CB   . ASN   A 1 37  ? 25.537 0.469   4.503   1.00 11.20 ?  37  ASN   A CB   1 
ATOM   843  C  CG   . ASN   A 1 37  ? 25.216 1.670   3.656   1.00 11.49 ?  37  ASN   A CG   1 
ATOM   844  O  OD1  . ASN   A 1 37  ? 24.040 2.004   3.474   1.00 12.16 ?  37  ASN   A OD1  1 
ATOM   845  N  ND2  . ASN   A 1 37  ? 26.249 2.324   3.129   1.00 11.85 ?  37  ASN   A ND2  1 
ATOM   846  H  H    . ASN   A 1 37  ? 25.617 -1.920  5.296   1.00 12.71 ?  37  ASN   A H    1 
ATOM   847  H  HA   . ASN   A 1 37  ? 23.614 -0.205  4.699   1.00 12.46 ?  37  ASN   A HA   1 
ATOM   848  H  HB2  . ASN   A 1 37  ? 25.623 0.771   5.423   1.00 13.41 ?  37  ASN   A HB2  1 
ATOM   849  H  HB3  . ASN   A 1 37  ? 26.381 0.099   4.196   1.00 13.41 ?  37  ASN   A HB3  1 
ATOM   850  H  HD21 . ASN   A 1 37  ? 26.109 3.013   2.630   1.00 14.18 ?  37  ASN   A HD21 1 
ATOM   851  H  HD22 . ASN   A 1 37  ? 27.046 2.062   3.274   1.00 14.18 ?  37  ASN   A HD22 1 
ATOM   852  N  N    A ALA   A 1 38  ? 23.310 -0.532  2.302   0.70 11.09 ?  38  ALA   A N    1 
ATOM   853  N  N    B ALA   A 1 38  ? 23.322 -0.549  2.279   0.30 10.93 ?  38  ALA   A N    1 
ATOM   854  C  CA   A ALA   A 1 38  ? 23.124 -0.654  0.857   0.70 11.20 ?  38  ALA   A CA   1 
ATOM   855  C  CA   B ALA   A 1 38  ? 23.177 -0.817  0.848   0.30 11.30 ?  38  ALA   A CA   1 
ATOM   856  C  C    A ALA   A 1 38  ? 24.061 0.333   0.163   0.70 11.20 ?  38  ALA   A C    1 
ATOM   857  C  C    B ALA   A 1 38  ? 23.989 0.230   0.087   0.30 11.33 ?  38  ALA   A C    1 
ATOM   858  O  O    A ALA   A 1 38  ? 23.678 1.435   -0.239  0.70 10.95 ?  38  ALA   A O    1 
ATOM   859  O  O    B ALA   A 1 38  ? 23.473 1.228   -0.423  0.30 11.25 ?  38  ALA   A O    1 
ATOM   860  C  CB   A ALA   A 1 38  ? 21.670 -0.373  0.490   0.70 11.84 ?  38  ALA   A CB   1 
ATOM   861  C  CB   B ALA   A 1 38  ? 21.710 -0.820  0.444   0.30 11.61 ?  38  ALA   A CB   1 
ATOM   862  H  H    A ALA   A 1 38  ? 22.703 -0.049  2.674   0.70 13.27 ?  38  ALA   A H    1 
ATOM   863  H  H    B ALA   A 1 38  ? 22.715 -0.030  2.605   0.30 13.08 ?  38  ALA   A H    1 
ATOM   864  H  HA   A ALA   A 1 38  ? 23.354 -1.549  0.572   0.70 13.40 ?  38  ALA   A HA   1 
ATOM   865  H  HA   B ALA   A 1 38  ? 23.547 -1.694  0.653   0.30 13.53 ?  38  ALA   A HA   1 
ATOM   866  H  HB1  A ALA   A 1 38  ? 21.565 -0.462  -0.470  0.70 14.17 ?  38  ALA   A HB1  1 
ATOM   867  H  HB1  B ALA   A 1 38  ? 21.654 -0.884  -0.521  0.30 13.90 ?  38  ALA   A HB1  1 
ATOM   868  H  HB2  A ALA   A 1 38  ? 21.103 -1.011  0.948   0.70 14.17 ?  38  ALA   A HB2  1 
ATOM   869  H  HB2  B ALA   A 1 38  ? 21.269 -1.581  0.854   0.30 13.90 ?  38  ALA   A HB2  1 
ATOM   870  H  HB3  A ALA   A 1 38  ? 21.444 0.530   0.765   0.70 14.17 ?  38  ALA   A HB3  1 
ATOM   871  H  HB3  B ALA   A 1 38  ? 21.301 0.005   0.742   0.30 13.90 ?  38  ALA   A HB3  1 
ATOM   872  N  N    A ALA   A 1 39  ? 25.317 -0.081  0.018   0.70 11.33 ?  39  ALA   A N    1 
ATOM   873  N  N    B ALA   A 1 39  ? 25.294 -0.017  0.014   0.30 11.48 ?  39  ALA   A N    1 
ATOM   874  C  CA   A ALA   A 1 39  ? 26.383 0.780   -0.465  0.70 10.77 ?  39  ALA   A CA   1 
ATOM   875  C  CA   B ALA   A 1 39  ? 26.236 0.960   -0.504  0.30 11.62 ?  39  ALA   A CA   1 
ATOM   876  C  C    A ALA   A 1 39  ? 26.494 0.738   -1.986  0.70 10.90 ?  39  ALA   A C    1 
ATOM   877  C  C    B ALA   A 1 39  ? 26.452 0.793   -2.004  0.30 11.07 ?  39  ALA   A C    1 
ATOM   878  O  O    A ALA   A 1 39  ? 25.982 -0.164  -2.655  0.70 11.73 ?  39  ALA   A O    1 
ATOM   879  O  O    B ALA   A 1 39  ? 26.117 -0.234  -2.601  0.30 11.09 ?  39  ALA   A O    1 
ATOM   880  C  CB   A ALA   A 1 39  ? 27.707 0.354   0.175   0.70 10.97 ?  39  ALA   A CB   1 
ATOM   881  C  CB   B ALA   A 1 39  ? 27.580 0.825   0.211   0.30 12.32 ?  39  ALA   A CB   1 
ATOM   882  H  H    A ALA   A 1 39  ? 25.579 -0.885  0.198   0.70 13.56 ?  39  ALA   A H    1 
ATOM   883  H  H    B ALA   A 1 39  ? 25.663 -0.758  0.265   0.30 13.73 ?  39  ALA   A H    1 
ATOM   884  H  HA   A ALA   A 1 39  ? 26.197 1.693   -0.197  0.70 12.89 ?  39  ALA   A HA   1 
ATOM   885  H  HA   B ALA   A 1 39  ? 25.887 1.848   -0.334  0.30 13.90 ?  39  ALA   A HA   1 
ATOM   886  H  HB1  A ALA   A 1 39  ? 28.414 0.937   -0.147  0.70 13.13 ?  39  ALA   A HB1  1 
ATOM   887  H  HB1  B ALA   A 1 39  ? 28.191 1.488   -0.148  0.30 14.74 ?  39  ALA   A HB1  1 
ATOM   888  H  HB2  A ALA   A 1 39  ? 27.633 0.436   1.143   0.70 13.13 ?  39  ALA   A HB2  1 
ATOM   889  H  HB2  B ALA   A 1 39  ? 27.447 0.974   1.159   0.30 14.74 ?  39  ALA   A HB2  1 
ATOM   890  H  HB3  A ALA   A 1 39  ? 27.897 -0.563  -0.064  0.70 13.13 ?  39  ALA   A HB3  1 
ATOM   891  H  HB3  B ALA   A 1 39  ? 27.929 -0.066  0.058   0.30 14.74 ?  39  ALA   A HB3  1 
ATOM   892  N  N    A ASN   A 1 40  ? 27.193 1.736   -2.528  0.70 11.36 ?  40  ASN   A N    1 
ATOM   893  N  N    B ASN   A 1 40  ? 27.034 1.829   -2.607  0.30 10.95 ?  40  ASN   A N    1 
ATOM   894  C  CA   A ASN   A 1 40  ? 27.718 1.690   -3.887  0.70 12.01 ?  40  ASN   A CA   1 
ATOM   895  C  CA   B ASN   A 1 40  ? 27.589 1.752   -3.948  0.30 11.06 ?  40  ASN   A CA   1 
ATOM   896  C  C    A ASN   A 1 40  ? 29.244 1.593   -3.832  0.70 11.34 ?  40  ASN   A C    1 
ATOM   897  C  C    B ASN   A 1 40  ? 29.107 1.590   -3.852  0.30 10.70 ?  40  ASN   A C    1 
ATOM   898  O  O    A ASN   A 1 40  ? 29.853 1.725   -2.768  0.70 11.83 ?  40  ASN   A O    1 
ATOM   899  O  O    B ASN   A 1 40  ? 29.695 1.627   -2.768  0.30 10.77 ?  40  ASN   A O    1 
ATOM   900  C  CB   A ASN   A 1 40  ? 27.219 2.868   -4.740  0.70 12.99 ?  40  ASN   A CB   1 
ATOM   901  C  CB   B ASN   A 1 40  ? 27.195 2.973   -4.786  0.30 11.64 ?  40  ASN   A CB   1 
ATOM   902  C  CG   A ASN   A 1 40  ? 27.591 4.221   -4.171  0.70 13.63 ?  40  ASN   A CG   1 
ATOM   903  C  CG   B ASN   A 1 40  ? 27.572 4.284   -4.125  0.30 12.16 ?  40  ASN   A CG   1 
ATOM   904  O  OD1  A ASN   A 1 40  ? 28.757 4.484   -3.873  0.70 14.21 ?  40  ASN   A OD1  1 
ATOM   905  O  OD1  B ASN   A 1 40  ? 28.751 4.576   -3.924  0.30 12.28 ?  40  ASN   A OD1  1 
ATOM   906  N  ND2  A ASN   A 1 40  ? 26.598 5.096   -4.027  0.70 14.32 ?  40  ASN   A ND2  1 
ATOM   907  N  ND2  B ASN   A 1 40  ? 26.568 5.090   -3.798  0.30 12.98 ?  40  ASN   A ND2  1 
ATOM   908  H  H    A ASN   A 1 40  ? 27.382 2.466   -2.115  0.70 13.59 ?  40  ASN   A H    1 
ATOM   909  H  H    B ASN   A 1 40  ? 27.122 2.605   -2.246  0.30 13.10 ?  40  ASN   A H    1 
ATOM   910  H  HA   A ASN   A 1 40  ? 27.394 0.876   -4.306  0.70 14.37 ?  40  ASN   A HA   1 
ATOM   911  H  HA   B ASN   A 1 40  ? 27.239 0.959   -4.392  0.30 13.24 ?  40  ASN   A HA   1 
ATOM   912  H  HB2  A ASN   A 1 40  ? 27.607 2.794   -5.630  0.70 15.55 ?  40  ASN   A HB2  1 
ATOM   913  H  HB2  B ASN   A 1 40  ? 27.651 2.927   -5.642  0.30 13.93 ?  40  ASN   A HB2  1 
ATOM   914  H  HB3  A ASN   A 1 40  ? 26.252 2.822   -4.802  0.70 15.55 ?  40  ASN   A HB3  1 
ATOM   915  H  HB3  B ASN   A 1 40  ? 26.235 2.966   -4.923  0.30 13.93 ?  40  ASN   A HB3  1 
ATOM   916  H  HD21 A ASN   A 1 40  ? 26.754 5.881   -3.710  0.70 17.15 ?  40  ASN   A HD21 1 
ATOM   917  H  HD21 B ASN   A 1 40  ? 26.730 5.845   -3.420  0.30 15.54 ?  40  ASN   A HD21 1 
ATOM   918  H  HD22 A ASN   A 1 40  ? 25.792 4.873   -4.235  0.70 17.15 ?  40  ASN   A HD22 1 
ATOM   919  H  HD22 B ASN   A 1 40  ? 25.755 4.856   -3.960  0.30 15.54 ?  40  ASN   A HD22 1 
ATOM   920  N  N    A VAL   A 1 41  ? 29.858 1.316   -4.987  0.70 11.96 ?  41  VAL   A N    1 
ATOM   921  N  N    B VAL   A 1 41  ? 29.746 1.415   -5.011  0.30 11.06 ?  41  VAL   A N    1 
ATOM   922  C  CA   A VAL   A 1 41  ? 31.293 1.026   -5.007  0.70 12.44 ?  41  VAL   A CA   1 
ATOM   923  C  CA   B VAL   A 1 41  ? 31.164 1.051   -5.038  0.30 11.49 ?  41  VAL   A CA   1 
ATOM   924  C  C    A VAL   A 1 41  ? 32.136 2.195   -4.542  0.70 12.00 ?  41  VAL   A C    1 
ATOM   925  C  C    B VAL   A 1 41  ? 32.056 2.170   -4.507  0.30 11.62 ?  41  VAL   A C    1 
ATOM   926  O  O    A VAL   A 1 41  ? 33.296 1.996   -4.160  0.70 12.19 ?  41  VAL   A O    1 
ATOM   927  O  O    B VAL   A 1 41  ? 33.160 1.908   -4.012  0.30 11.98 ?  41  VAL   A O    1 
ATOM   928  C  CB   A VAL   A 1 41  ? 31.809 0.533   -6.381  0.70 12.88 ?  41  VAL   A CB   1 
ATOM   929  C  CB   B VAL   A 1 41  ? 31.580 0.595   -6.452  0.30 11.88 ?  41  VAL   A CB   1 
ATOM   930  C  CG1  A VAL   A 1 41  ? 31.156 -0.781  -6.773  0.70 12.96 ?  41  VAL   A CG1  1 
ATOM   931  C  CG1  B VAL   A 1 41  ? 30.770 -0.626  -6.879  0.30 12.68 ?  41  VAL   A CG1  1 
ATOM   932  C  CG2  A VAL   A 1 41  ? 31.657 1.593   -7.465  0.70 13.91 ?  41  VAL   A CG2  1 
ATOM   933  C  CG2  B VAL   A 1 41  ? 31.428 1.723   -7.466  0.30 12.34 ?  41  VAL   A CG2  1 
ATOM   934  H  H    A VAL   A 1 41  ? 29.474 1.272   -5.751  0.70 14.31 ?  41  VAL   A H    1 
ATOM   935  H  H    B VAL   A 1 41  ? 29.379 1.486   -5.785  0.30 13.23 ?  41  VAL   A H    1 
ATOM   936  H  HA   A VAL   A 1 41  ? 31.461 0.299   -4.383  0.70 14.89 ?  41  VAL   A HA   1 
ATOM   937  H  HA   B VAL   A 1 41  ? 31.289 0.294   -4.451  0.30 13.76 ?  41  VAL   A HA   1 
ATOM   938  H  HB   A VAL   A 1 41  ? 32.761 0.353   -6.296  0.70 15.42 ?  41  VAL   A HB   1 
ATOM   939  H  HB   B VAL   A 1 41  ? 32.514 0.332   -6.436  0.30 14.22 ?  41  VAL   A HB   1 
ATOM   940  H  HG11 A VAL   A 1 41  ? 31.507 -1.071  -7.629  0.70 15.51 ?  41  VAL   A HG11 1 
ATOM   941  H  HG11 B VAL   A 1 41  ? 30.959 -0.824  -7.810  0.30 15.18 ?  41  VAL   A HG11 1 
ATOM   942  H  HG12 A VAL   A 1 41  ? 31.347 -1.448  -6.094  0.70 15.51 ?  41  VAL   A HG12 1 
ATOM   943  H  HG12 B VAL   A 1 41  ? 31.021 -1.382  -6.324  0.30 15.18 ?  41  VAL   A HG12 1 
ATOM   944  H  HG13 A VAL   A 1 41  ? 30.195 -0.648  -6.840  0.70 15.51 ?  41  VAL   A HG13 1 
ATOM   945  H  HG13 B VAL   A 1 41  ? 29.826 -0.440  -6.769  0.30 15.18 ?  41  VAL   A HG13 1 
ATOM   946  H  HG21 A VAL   A 1 41  ? 31.899 1.203   -8.322  0.70 16.66 ?  41  VAL   A HG21 1 
ATOM   947  H  HG21 B VAL   A 1 41  ? 31.660 1.385   -8.348  0.30 14.77 ?  41  VAL   A HG21 1 
ATOM   948  H  HG22 A VAL   A 1 41  ? 30.738 1.893   -7.485  0.70 16.66 ?  41  VAL   A HG22 1 
ATOM   949  H  HG22 B VAL   A 1 41  ? 30.512 2.031   -7.462  0.30 14.77 ?  41  VAL   A HG22 1 
ATOM   950  H  HG23 A VAL   A 1 41  ? 32.248 2.336   -7.265  0.70 16.66 ?  41  VAL   A HG23 1 
ATOM   951  H  HG23 B VAL   A 1 41  ? 32.027 2.445   -7.224  0.30 14.77 ?  41  VAL   A HG23 1 
ATOM   952  N  N    . TYR   A 1 42  ? 31.606 3.418   -4.608  1.00 11.96 ?  42  TYR   A N    1 
ATOM   953  C  CA   . TYR   A 1 42  ? 32.344 4.603   -4.184  1.00 11.79 ?  42  TYR   A CA   1 
ATOM   954  C  C    . TYR   A 1 42  ? 32.089 4.972   -2.734  1.00 11.61 ?  42  TYR   A C    1 
ATOM   955  O  O    . TYR   A 1 42  ? 32.643 5.969   -2.252  1.00 12.36 ?  42  TYR   A O    1 
ATOM   956  C  CB   . TYR   A 1 42  ? 31.992 5.797   -5.094  1.00 12.46 ?  42  TYR   A CB   1 
ATOM   957  C  CG   . TYR   A 1 42  ? 32.167 5.489   -6.563  1.00 13.08 ?  42  TYR   A CG   1 
ATOM   958  C  CD1  . TYR   A 1 42  ? 33.428 5.296   -7.103  1.00 13.77 ?  42  TYR   A CD1  1 
ATOM   959  C  CD2  . TYR   A 1 42  ? 31.072 5.356   -7.406  1.00 14.40 ?  42  TYR   A CD2  1 
ATOM   960  C  CE1  . TYR   A 1 42  ? 33.594 4.988   -8.435  1.00 14.23 ?  42  TYR   A CE1  1 
ATOM   961  C  CE2  . TYR   A 1 42  ? 31.233 5.066   -8.745  1.00 15.42 ?  42  TYR   A CE2  1 
ATOM   962  C  CZ   . TYR   A 1 42  ? 32.498 4.875   -9.254  1.00 15.18 ?  42  TYR   A CZ   1 
ATOM   963  O  OH   . TYR   A 1 42  ? 32.662 4.578   -10.585 1.00 17.26 ?  42  TYR   A OH   1 
ATOM   964  H  H    A TYR   A 1 42  ? 30.816 3.584   -4.902  0.70 14.31 ?  42  TYR   A H    1 
ATOM   965  H  H    B TYR   A 1 42  ? 30.834 3.609   -4.932  0.30 14.31 ?  42  TYR   A H    1 
ATOM   966  H  HA   . TYR   A 1 42  ? 33.294 4.434   -4.280  1.00 14.11 ?  42  TYR   A HA   1 
ATOM   967  H  HB2  . TYR   A 1 42  ? 31.063 6.041   -4.947  1.00 14.92 ?  42  TYR   A HB2  1 
ATOM   968  H  HB3  . TYR   A 1 42  ? 32.569 6.544   -4.874  1.00 14.92 ?  42  TYR   A HB3  1 
ATOM   969  H  HD1  . TYR   A 1 42  ? 34.174 5.362   -6.554  1.00 16.49 ?  42  TYR   A HD1  1 
ATOM   970  H  HD2  . TYR   A 1 42  ? 30.214 5.483   -7.065  1.00 17.24 ?  42  TYR   A HD2  1 
ATOM   971  H  HE1  . TYR   A 1 42  ? 34.448 4.863   -8.784  1.00 17.03 ?  42  TYR   A HE1  1 
ATOM   972  H  HE2  . TYR   A 1 42  ? 30.488 4.983   -9.300  1.00 18.46 ?  42  TYR   A HE2  1 
ATOM   973  H  HH   . TYR   A 1 42  ? 33.481 4.483   -10.762 1.00 20.68 ?  42  TYR   A HH   1 
ATOM   974  N  N    . LEU   A 1 43  ? 31.224 4.223   -2.050  1.00 11.31 ?  43  LEU   A N    1 
ATOM   975  C  CA   . LEU   A 1 43  ? 30.775 4.564   -0.704  1.00 11.31 ?  43  LEU   A CA   1 
ATOM   976  C  C    . LEU   A 1 43  ? 30.288 6.010   -0.618  1.00 11.48 ?  43  LEU   A C    1 
ATOM   977  O  O    . LEU   A 1 43  ? 30.548 6.716   0.357   1.00 12.60 ?  43  LEU   A O    1 
ATOM   978  C  CB   . LEU   A 1 43  ? 31.823 4.254   0.364   1.00 11.67 ?  43  LEU   A CB   1 
ATOM   979  C  CG   . LEU   A 1 43  ? 32.324 2.809   0.456   1.00 12.05 ?  43  LEU   A CG   1 
ATOM   980  C  CD1  . LEU   A 1 43  ? 33.356 2.699   1.565   1.00 12.98 ?  43  LEU   A CD1  1 
ATOM   981  C  CD2  . LEU   A 1 43  ? 31.171 1.828   0.689   1.00 12.49 ?  43  LEU   A CD2  1 
ATOM   982  H  H    . LEU   A 1 43  ? 30.872 3.494   -2.351  1.00 13.54 ?  43  LEU   A H    1 
ATOM   983  H  HA   . LEU   A 1 43  ? 30.008 3.999   -0.504  1.00 13.53 ?  43  LEU   A HA   1 
ATOM   984  H  HB2  . LEU   A 1 43  ? 32.594 4.816   0.204   1.00 13.97 ?  43  LEU   A HB2  1 
ATOM   985  H  HB3  . LEU   A 1 43  ? 31.441 4.472   1.230   1.00 13.97 ?  43  LEU   A HB3  1 
ATOM   986  H  HG   . LEU   A 1 43  ? 32.759 2.569   -0.381  1.00 14.42 ?  43  LEU   A HG   1 
ATOM   987  H  HD11 . LEU   A 1 43  ? 33.672 1.785   1.616   1.00 15.54 ?  43  LEU   A HD11 1 
ATOM   988  H  HD12 . LEU   A 1 43  ? 34.096 3.296   1.367   1.00 15.54 ?  43  LEU   A HD12 1 
ATOM   989  H  HD13 . LEU   A 1 43  ? 32.941 2.956   2.404   1.00 15.54 ?  43  LEU   A HD13 1 
ATOM   990  H  HD21 . LEU   A 1 43  ? 31.535 0.945   0.846   1.00 14.95 ?  43  LEU   A HD21 1 
ATOM   991  H  HD22 . LEU   A 1 43  ? 30.665 2.123   1.463   1.00 14.95 ?  43  LEU   A HD22 1 
ATOM   992  H  HD23 . LEU   A 1 43  ? 30.602 1.821   -0.095  1.00 14.95 ?  43  LEU   A HD23 1 
ATOM   993  N  N    A LYS   A 1 44  ? 29.574 6.448   -1.656  0.70 11.13 ?  44  LYS   A N    1 
ATOM   994  N  N    B LYS   A 1 44  ? 29.545 6.439   -1.638  0.30 12.17 ?  44  LYS   A N    1 
ATOM   995  C  CA   A LYS   A 1 44  ? 28.935 7.764   -1.674  0.70 11.60 ?  44  LYS   A CA   1 
ATOM   996  C  CA   B LYS   A 1 44  ? 28.898 7.750   -1.643  0.30 13.39 ?  44  LYS   A CA   1 
ATOM   997  C  C    A LYS   A 1 44  ? 27.505 7.585   -1.189  0.70 11.00 ?  44  LYS   A C    1 
ATOM   998  C  C    B LYS   A 1 44  ? 27.480 7.574   -1.117  0.30 12.84 ?  44  LYS   A C    1 
ATOM   999  O  O    A LYS   A 1 44  ? 26.645 7.069   -1.909  0.70 11.85 ?  44  LYS   A O    1 
ATOM   1000 O  O    B LYS   A 1 44  ? 26.598 7.074   -1.819  0.30 12.93 ?  44  LYS   A O    1 
ATOM   1001 C  CB   A LYS   A 1 44  ? 28.992 8.375   -3.067  0.70 13.81 ?  44  LYS   A CB   1 
ATOM   1002 C  CB   B LYS   A 1 44  ? 28.921 8.355   -3.044  0.30 15.48 ?  44  LYS   A CB   1 
ATOM   1003 C  CG   A LYS   A 1 44  ? 30.374 8.829   -3.493  0.70 17.29 ?  44  LYS   A CG   1 
ATOM   1004 C  CG   B LYS   A 1 44  ? 30.269 8.934   -3.445  0.30 17.68 ?  44  LYS   A CG   1 
ATOM   1005 C  CD   A LYS   A 1 44  ? 31.037 9.728   -2.458  0.70 22.40 ?  44  LYS   A CD   1 
ATOM   1006 C  CD   B LYS   A 1 44  ? 30.739 9.987   -2.447  0.30 20.08 ?  44  LYS   A CD   1 
ATOM   1007 C  CE   A LYS   A 1 44  ? 32.339 10.301  -2.979  0.70 25.56 ?  44  LYS   A CE   1 
ATOM   1008 C  CE   B LYS   A 1 44  ? 32.093 10.547  -2.824  0.30 21.56 ?  44  LYS   A CE   1 
ATOM   1009 N  NZ   A LYS   A 1 44  ? 33.127 10.948  -1.898  0.70 27.31 ?  44  LYS   A NZ   1 
ATOM   1010 N  NZ   B LYS   A 1 44  ? 33.056 10.464  -1.690  0.30 22.10 ?  44  LYS   A NZ   1 
ATOM   1011 H  H    A LYS   A 1 44  ? 29.451 5.990   -2.377  0.70 13.32 ?  44  LYS   A H    1 
ATOM   1012 H  H    B LYS   A 1 44  ? 29.397 5.979   -2.352  0.30 14.56 ?  44  LYS   A H    1 
ATOM   1013 H  HA   A LYS   A 1 44  ? 29.385 8.345   -1.045  0.70 13.88 ?  44  LYS   A HA   1 
ATOM   1014 H  HA   B LYS   A 1 44  ? 29.361 8.336   -1.028  0.30 16.03 ?  44  LYS   A HA   1 
ATOM   1015 H  HB2  A LYS   A 1 44  ? 28.685 7.718   -3.710  0.70 16.54 ?  44  LYS   A HB2  1 
ATOM   1016 H  HB2  B LYS   A 1 44  ? 28.695 7.665   -3.690  0.30 18.53 ?  44  LYS   A HB2  1 
ATOM   1017 H  HB3  A LYS   A 1 44  ? 28.408 9.150   -3.087  0.70 16.54 ?  44  LYS   A HB3  1 
ATOM   1018 H  HB3  B LYS   A 1 44  ? 28.269 9.072   -3.091  0.30 18.53 ?  44  LYS   A HB3  1 
ATOM   1019 H  HG2  A LYS   A 1 44  ? 30.941 8.052   -3.625  0.70 20.70 ?  44  LYS   A HG2  1 
ATOM   1020 H  HG2  B LYS   A 1 44  ? 30.929 8.223   -3.474  0.30 21.18 ?  44  LYS   A HG2  1 
ATOM   1021 H  HG3  A LYS   A 1 44  ? 30.304 9.331   -4.323  0.70 20.70 ?  44  LYS   A HG3  1 
ATOM   1022 H  HG3  B LYS   A 1 44  ? 30.193 9.356   -4.318  0.30 21.18 ?  44  LYS   A HG3  1 
ATOM   1023 H  HD2  A LYS   A 1 44  ? 30.437 10.458  -2.238  0.70 26.84 ?  44  LYS   A HD2  1 
ATOM   1024 H  HD2  B LYS   A 1 44  ? 30.092 10.709  -2.421  0.30 24.06 ?  44  LYS   A HD2  1 
ATOM   1025 H  HD3  A LYS   A 1 44  ? 31.238 9.206   -1.663  0.70 26.84 ?  44  LYS   A HD3  1 
ATOM   1026 H  HD3  B LYS   A 1 44  ? 30.832 9.587   -1.568  0.30 24.06 ?  44  LYS   A HD3  1 
ATOM   1027 H  HE2  A LYS   A 1 44  ? 32.873 9.584   -3.357  0.70 30.63 ?  44  LYS   A HE2  1 
ATOM   1028 H  HE2  B LYS   A 1 44  ? 32.454 10.036  -3.564  0.30 25.84 ?  44  LYS   A HE2  1 
ATOM   1029 H  HE3  A LYS   A 1 44  ? 32.145 10.966  -3.656  0.70 30.63 ?  44  LYS   A HE3  1 
ATOM   1030 H  HE3  B LYS   A 1 44  ? 31.993 11.476  -3.071  0.30 25.84 ?  44  LYS   A HE3  1 
ATOM   1031 H  HZ1  A LYS   A 1 44  ? 33.886 11.273  -2.229  0.70 32.74 ?  44  LYS   A HZ1  1 
ATOM   1032 H  HZ1  B LYS   A 1 44  ? 33.842 10.800  -1.935  0.30 26.49 ?  44  LYS   A HZ1  1 
ATOM   1033 H  HZ2  A LYS   A 1 44  ? 32.658 11.615  -1.539  0.70 32.74 ?  44  LYS   A HZ2  1 
ATOM   1034 H  HZ2  B LYS   A 1 44  ? 32.747 10.928  -0.995  0.30 26.49 ?  44  LYS   A HZ2  1 
ATOM   1035 H  HZ3  A LYS   A 1 44  ? 33.317 10.354  -1.263  0.70 32.74 ?  44  LYS   A HZ3  1 
ATOM   1036 H  HZ3  B LYS   A 1 44  ? 33.166 9.616   -1.444  0.30 26.49 ?  44  LYS   A HZ3  1 
ATOM   1037 N  N    A HIS   A 1 45  ? 27.270 7.961   0.064   0.70 10.88 ?  45  HIS   A N    1 
ATOM   1038 N  N    B HIS   A 1 45  ? 27.265 7.975   0.135   0.30 12.70 ?  45  HIS   A N    1 
ATOM   1039 C  CA   A HIS   A 1 45  ? 26.035 7.608   0.764   0.70 10.52 ?  45  HIS   A CA   1 
ATOM   1040 C  CA   B HIS   A 1 45  ? 26.000 7.732   0.826   0.30 12.38 ?  45  HIS   A CA   1 
ATOM   1041 C  C    A HIS   A 1 45  ? 25.003 8.728   0.605   0.70 11.50 ?  45  HIS   A C    1 
ATOM   1042 C  C    B HIS   A 1 45  ? 25.086 8.928   0.604   0.30 13.19 ?  45  HIS   A C    1 
ATOM   1043 O  O    A HIS   A 1 45  ? 24.652 9.453   1.542   0.70 12.02 ?  45  HIS   A O    1 
ATOM   1044 O  O    B HIS   A 1 45  ? 25.064 9.876   1.389   0.30 13.75 ?  45  HIS   A O    1 
ATOM   1045 C  CB   A HIS   A 1 45  ? 26.339 7.338   2.226   0.70 10.57 ?  45  HIS   A CB   1 
ATOM   1046 C  CB   B HIS   A 1 45  ? 26.248 7.505   2.309   0.30 11.54 ?  45  HIS   A CB   1 
ATOM   1047 C  CG   A HIS   A 1 45  ? 27.453 6.362   2.435   0.70 10.66 ?  45  HIS   A CG   1 
ATOM   1048 C  CG   B HIS   A 1 45  ? 27.369 6.558   2.591   0.30 10.85 ?  45  HIS   A CG   1 
ATOM   1049 N  ND1  A HIS   A 1 45  ? 27.436 5.078   1.924   0.70 10.72 ?  45  HIS   A ND1  1 
ATOM   1050 N  ND1  B HIS   A 1 45  ? 27.384 5.260   2.126   0.30 10.88 ?  45  HIS   A ND1  1 
ATOM   1051 C  CD2  A HIS   A 1 45  ? 28.624 6.491   3.102   0.70 11.19 ?  45  HIS   A CD2  1 
ATOM   1052 C  CD2  B HIS   A 1 45  ? 28.518 6.724   3.289   0.30 9.98  ?  45  HIS   A CD2  1 
ATOM   1053 C  CE1  A HIS   A 1 45  ? 28.550 4.461   2.280   0.70 11.22 ?  45  HIS   A CE1  1 
ATOM   1054 C  CE1  B HIS   A 1 45  ? 28.494 4.668   2.528   0.30 9.81  ?  45  HIS   A CE1  1 
ATOM   1055 N  NE2  A HIS   A 1 45  ? 29.289 5.297   2.989   0.70 11.29 ?  45  HIS   A NE2  1 
ATOM   1056 N  NE2  B HIS   A 1 45  ? 29.200 5.534   3.234   0.30 9.52  ?  45  HIS   A NE2  1 
ATOM   1057 H  H    A HIS   A 1 45  ? 27.812 8.433   0.535   0.70 13.02 ?  45  HIS   A H    1 
ATOM   1058 H  H    B HIS   A 1 45  ? 27.845 8.400   0.610   0.30 15.21 ?  45  HIS   A H    1 
ATOM   1059 H  HA   A HIS   A 1 45  ? 25.667 6.796   0.378   0.70 12.59 ?  45  HIS   A HA   1 
ATOM   1060 H  HA   B HIS   A 1 45  ? 25.575 6.945   0.455   0.30 14.82 ?  45  HIS   A HA   1 
ATOM   1061 H  HB2  A HIS   A 1 45  ? 26.587 8.167   2.657   0.70 12.64 ?  45  HIS   A HB2  1 
ATOM   1062 H  HB2  B HIS   A 1 45  ? 26.460 8.356   2.724   0.30 13.82 ?  45  HIS   A HB2  1 
ATOM   1063 H  HB3  A HIS   A 1 45  ? 25.543 6.971   2.651   0.70 12.64 ?  45  HIS   A HB3  1 
ATOM   1064 H  HB3  B HIS   A 1 45  ? 25.440 7.140   2.705   0.30 13.82 ?  45  HIS   A HB3  1 
ATOM   1065 H  HD2  A HIS   A 1 45  ? 28.927 7.250   3.549   0.70 13.39 ?  45  HIS   A HD2  1 
ATOM   1066 H  HD2  B HIS   A 1 45  ? 28.792 7.504   3.722   0.30 11.94 ?  45  HIS   A HD2  1 
ATOM   1067 H  HE1  A HIS   A 1 45  ? 28.780 3.581   2.073   0.70 13.43 ?  45  HIS   A HE1  1 
ATOM   1068 H  HE1  B HIS   A 1 45  ? 28.737 3.794   2.345   0.30 11.74 ?  45  HIS   A HE1  1 
ATOM   1069 H  HE2  A HIS   A 1 45  ? 30.065 5.120   3.331   0.70 13.51 ?  45  HIS   A HE2  1 
ATOM   1070 H  HE2  B HIS   A 1 45  ? 29.961 5.381   3.601   0.30 11.38 ?  45  HIS   A HE2  1 
ATOM   1071 N  N    A GLY   A 1 46  ? 24.509 8.859   -0.621  0.70 12.78 ?  46  GLY   A N    1 
ATOM   1072 N  N    B GLY   A 1 46  ? 24.311 8.880   -0.473  0.30 13.22 ?  46  GLY   A N    1 
ATOM   1073 C  CA   A GLY   A 1 46  ? 23.726 10.030  -0.973  0.70 13.36 ?  46  GLY   A CA   1 
ATOM   1074 C  CA   B GLY   A 1 46  ? 23.447 9.993   -0.809  0.30 12.61 ?  46  GLY   A CA   1 
ATOM   1075 C  C    A GLY   A 1 46  ? 22.231 9.906   -0.765  0.70 13.32 ?  46  GLY   A C    1 
ATOM   1076 C  C    B GLY   A 1 46  ? 22.002 9.817   -0.388  0.30 11.43 ?  46  GLY   A C    1 
ATOM   1077 O  O    A GLY   A 1 46  ? 21.557 10.908  -0.495  0.70 13.40 ?  46  GLY   A O    1 
ATOM   1078 O  O    B GLY   A 1 46  ? 21.389 10.765  0.113   0.30 11.63 ?  46  GLY   A O    1 
ATOM   1079 H  H    A GLY   A 1 46  ? 24.598 8.280   -1.251  0.70 15.30 ?  46  GLY   A H    1 
ATOM   1080 H  H    B GLY   A 1 46  ? 24.272 8.221   -1.021  0.30 15.83 ?  46  GLY   A H    1 
ATOM   1081 H  HA2  A GLY   A 1 46  ? 24.039 10.782  -0.444  0.70 16.00 ?  46  GLY   A HA2  1 
ATOM   1082 H  HA2  B GLY   A 1 46  ? 23.781 10.800  -0.384  0.30 15.09 ?  46  GLY   A HA2  1 
ATOM   1083 H  HA3  A GLY   A 1 46  ? 23.880 10.235  -1.905  0.70 16.00 ?  46  GLY   A HA3  1 
ATOM   1084 H  HA3  B GLY   A 1 46  ? 23.469 10.130  -1.767  0.30 15.09 ?  46  GLY   A HA3  1 
ATOM   1085 N  N    A GLY   A 1 47  ? 21.698 8.697   -0.904  0.70 13.19 ?  47  GLY   A N    1 
ATOM   1086 N  N    B GLY   A 1 47  ? 21.443 8.623   -0.578  0.30 11.11 ?  47  GLY   A N    1 
ATOM   1087 C  CA   A GLY   A 1 47  ? 20.262 8.505   -0.872  0.70 13.10 ?  47  GLY   A CA   1 
ATOM   1088 C  CA   B GLY   A 1 47  ? 20.025 8.412   -0.373  0.30 10.81 ?  47  GLY   A CA   1 
ATOM   1089 C  C    A GLY   A 1 47  ? 19.945 7.065   -0.538  0.70 12.45 ?  47  GLY   A C    1 
ATOM   1090 C  C    B GLY   A 1 47  ? 19.708 6.973   -0.024  0.30 9.99  ?  47  GLY   A C    1 
ATOM   1091 O  O    A GLY   A 1 47  ? 20.836 6.239   -0.326  0.70 12.87 ?  47  GLY   A O    1 
ATOM   1092 O  O    B GLY   A 1 47  ? 20.602 6.136   0.137   0.30 9.83  ?  47  GLY   A O    1 
ATOM   1093 H  H    A GLY   A 1 47  ? 22.149 7.976   -1.008  0.70 15.79 ?  47  GLY   A H    1 
ATOM   1094 H  H    B GLY   A 1 47  ? 21.873 7.921   -0.819  0.30 13.30 ?  47  GLY   A H    1 
ATOM   1095 H  HA2  A GLY   A 1 47  ? 19.858 9.091   -0.208  0.70 15.68 ?  47  GLY   A HA2  1 
ATOM   1096 H  HA2  B GLY   A 1 47  ? 19.711 8.977   0.348   0.30 12.94 ?  47  GLY   A HA2  1 
ATOM   1097 H  HA3  A GLY   A 1 47  ? 19.884 8.709   -1.742  0.70 15.68 ?  47  GLY   A HA3  1 
ATOM   1098 H  HA3  B GLY   A 1 47  ? 19.541 8.651   -1.182  0.30 12.94 ?  47  GLY   A HA3  1 
ATOM   1099 N  N    A GLY   A 1 48  ? 18.654 6.761   -0.512  0.70 12.25 ?  48  GLY   A N    1 
ATOM   1100 N  N    B GLY   A 1 48  ? 18.406 6.694   0.085   0.30 9.98  ?  48  GLY   A N    1 
ATOM   1101 C  CA   A GLY   A 1 48  ? 18.245 5.429   -0.133  0.70 12.54 ?  48  GLY   A CA   1 
ATOM   1102 C  CA   B GLY   A 1 48  ? 17.963 5.370   0.491   0.30 9.66  ?  48  GLY   A CA   1 
ATOM   1103 C  C    A GLY   A 1 48  ? 18.637 5.125   1.298   0.70 12.07 ?  48  GLY   A C    1 
ATOM   1104 C  C    B GLY   A 1 48  ? 18.558 4.987   1.831   0.30 9.80  ?  48  GLY   A C    1 
ATOM   1105 O  O    A GLY   A 1 48  ? 18.784 6.020   2.141   0.70 12.09 ?  48  GLY   A O    1 
ATOM   1106 O  O    B GLY   A 1 48  ? 18.711 5.814   2.738   0.30 9.90  ?  48  GLY   A O    1 
ATOM   1107 H  H    A GLY   A 1 48  ? 18.018 7.296   -0.707  0.70 14.66 ?  48  GLY   A H    1 
ATOM   1108 H  H    B GLY   A 1 48  ? 17.754 7.254   -0.068  0.30 11.94 ?  48  GLY   A H    1 
ATOM   1109 H  HA2  A GLY   A 1 48  ? 17.288 5.343   -0.213  0.70 15.01 ?  48  GLY   A HA2  1 
ATOM   1110 H  HA2  B GLY   A 1 48  ? 16.990 5.346   0.554   0.30 11.55 ?  48  GLY   A HA2  1 
ATOM   1111 H  HA3  A GLY   A 1 48  ? 18.674 4.775   -0.704  0.70 15.01 ?  48  GLY   A HA3  1 
ATOM   1112 H  HA3  B GLY   A 1 48  ? 18.239 4.715   -0.173  0.30 11.55 ?  48  GLY   A HA3  1 
ATOM   1113 N  N    A VAL   A 1 49  ? 18.809 3.831   1.579   0.70 12.15 ?  49  VAL   A N    1 
ATOM   1114 N  N    B VAL   A 1 49  ? 18.897 3.704   1.958   0.30 10.06 ?  49  VAL   A N    1 
ATOM   1115 C  CA   A VAL   A 1 49  ? 19.254 3.407   2.903   0.70 12.33 ?  49  VAL   A CA   1 
ATOM   1116 C  CA   B VAL   A 1 49  ? 19.498 3.201   3.190   0.30 10.17 ?  49  VAL   A CA   1 
ATOM   1117 C  C    A VAL   A 1 49  ? 20.581 4.063   3.271   0.70 11.38 ?  49  VAL   A C    1 
ATOM   1118 C  C    B VAL   A 1 49  ? 20.757 3.987   3.535   0.30 9.76  ?  49  VAL   A C    1 
ATOM   1119 O  O    A VAL   A 1 49  ? 20.776 4.476   4.417   0.70 11.77 ?  49  VAL   A O    1 
ATOM   1120 O  O    B VAL   A 1 49  ? 20.950 4.411   4.681   0.30 9.71  ?  49  VAL   A O    1 
ATOM   1121 C  CB   A VAL   A 1 49  ? 19.338 1.868   2.972   0.70 13.50 ?  49  VAL   A CB   1 
ATOM   1122 C  CB   B VAL   A 1 49  ? 19.788 1.695   3.059   0.30 10.17 ?  49  VAL   A CB   1 
ATOM   1123 C  CG1  A VAL   A 1 49  ? 20.079 1.412   4.234   0.70 14.16 ?  49  VAL   A CG1  1 
ATOM   1124 C  CG1  B VAL   A 1 49  ? 20.602 1.217   4.243   0.30 9.89  ?  49  VAL   A CG1  1 
ATOM   1125 C  CG2  A VAL   A 1 49  ? 17.943 1.257   2.917   0.70 14.90 ?  49  VAL   A CG2  1 
ATOM   1126 C  CG2  B VAL   A 1 49  ? 18.495 0.909   2.939   0.30 10.49 ?  49  VAL   A CG2  1 
ATOM   1127 H  H    A VAL   A 1 49  ? 18.681 3.182   1.030   0.70 14.55 ?  49  VAL   A H    1 
ATOM   1128 H  H    B VAL   A 1 49  ? 18.789 3.113   1.346   0.30 12.03 ?  49  VAL   A H    1 
ATOM   1129 H  HA   A VAL   A 1 49  ? 18.602 3.682   3.563   0.70 14.76 ?  49  VAL   A HA   1 
ATOM   1130 H  HA   B VAL   A 1 49  ? 18.870 3.319   3.915   0.30 12.17 ?  49  VAL   A HA   1 
ATOM   1131 H  HB   A VAL   A 1 49  ? 19.840 1.539   2.211   0.70 16.16 ?  49  VAL   A HB   1 
ATOM   1132 H  HB   B VAL   A 1 49  ? 20.308 1.540   2.254   0.30 12.17 ?  49  VAL   A HB   1 
ATOM   1133 H  HG11 A VAL   A 1 49  ? 19.883 0.476   4.397   0.70 16.95 ?  49  VAL   A HG11 1 
ATOM   1134 H  HG11 B VAL   A 1 49  ? 20.529 0.252   4.308   0.30 11.83 ?  49  VAL   A HG11 1 
ATOM   1135 H  HG12 A VAL   A 1 49  ? 21.032 1.533   4.109   0.70 16.95 ?  49  VAL   A HG12 1 
ATOM   1136 H  HG12 B VAL   A 1 49  ? 21.533 1.466   4.112   0.30 11.83 ?  49  VAL   A HG12 1 
ATOM   1137 H  HG13 A VAL   A 1 49  ? 19.772 1.945   4.988   0.70 16.95 ?  49  VAL   A HG13 1 
ATOM   1138 H  HG13 B VAL   A 1 49  ? 20.260 1.629   5.051   0.30 11.83 ?  49  VAL   A HG13 1 
ATOM   1139 H  HG21 A VAL   A 1 49  ? 18.018 0.291   2.962   0.70 17.84 ?  49  VAL   A HG21 1 
ATOM   1140 H  HG21 B VAL   A 1 49  ? 18.706 -0.031  2.829   0.30 12.55 ?  49  VAL   A HG21 1 
ATOM   1141 H  HG22 A VAL   A 1 49  ? 17.428 1.584   3.672   0.70 17.84 ?  49  VAL   A HG22 1 
ATOM   1142 H  HG22 B VAL   A 1 49  ? 17.972 1.040   3.744   0.30 12.55 ?  49  VAL   A HG22 1 
ATOM   1143 H  HG23 A VAL   A 1 49  ? 17.522 1.520   2.087   0.70 17.84 ?  49  VAL   A HG23 1 
ATOM   1144 H  HG23 B VAL   A 1 49  ? 18.001 1.228   2.167   0.30 12.55 ?  49  VAL   A HG23 1 
ATOM   1145 N  N    A ALA   A 1 50  ? 21.529 4.121   2.327   0.70 11.30 ?  50  ALA   A N    1 
ATOM   1146 N  N    B ALA   A 1 50  ? 21.641 4.176   2.552   0.30 9.58  ?  50  ALA   A N    1 
ATOM   1147 C  CA   A ALA   A 1 50  ? 22.851 4.665   2.628   0.70 11.08 ?  50  ALA   A CA   1 
ATOM   1148 C  CA   B ALA   A 1 50  ? 22.944 4.770   2.833   0.30 9.56  ?  50  ALA   A CA   1 
ATOM   1149 C  C    A ALA   A 1 50  ? 22.767 6.128   3.035   0.70 11.18 ?  50  ALA   A C    1 
ATOM   1150 C  C    B ALA   A 1 50  ? 22.805 6.216   3.287   0.30 9.63  ?  50  ALA   A C    1 
ATOM   1151 O  O    A ALA   A 1 50  ? 23.411 6.554   3.999   0.70 11.49 ?  50  ALA   A O    1 
ATOM   1152 O  O    B ALA   A 1 50  ? 23.404 6.622   4.290   0.30 9.52  ?  50  ALA   A O    1 
ATOM   1153 C  CB   A ALA   A 1 50  ? 23.765 4.508   1.415   0.70 11.53 ?  50  ALA   A CB   1 
ATOM   1154 C  CB   B ALA   A 1 50  ? 23.840 4.672   1.599   0.30 9.54  ?  50  ALA   A CB   1 
ATOM   1155 H  H    A ALA   A 1 50  ? 21.430 3.848   1.521   0.70 13.53 ?  50  ALA   A H    1 
ATOM   1156 H  H    B ALA   A 1 50  ? 21.505 3.983   1.722   0.30 11.46 ?  50  ALA   A H    1 
ATOM   1157 H  HA   A ALA   A 1 50  ? 23.241 4.173   3.369   0.70 13.26 ?  50  ALA   A HA   1 
ATOM   1158 H  HA   B ALA   A 1 50  ? 23.363 4.279   3.550   0.30 11.43 ?  50  ALA   A HA   1 
ATOM   1159 H  HB1  A ALA   A 1 50  ? 24.637 4.877   1.630   0.70 13.80 ?  50  ALA   A HB1  1 
ATOM   1160 H  HB1  B ALA   A 1 50  ? 24.700 5.069   1.802   0.30 11.41 ?  50  ALA   A HB1  1 
ATOM   1161 H  HB2  A ALA   A 1 50  ? 23.846 3.567   1.202   0.70 13.80 ?  50  ALA   A HB2  1 
ATOM   1162 H  HB2  B ALA   A 1 50  ? 23.953 3.736   1.368   0.30 11.41 ?  50  ALA   A HB2  1 
ATOM   1163 H  HB3  A ALA   A 1 50  ? 23.378 4.988   0.668   0.70 13.80 ?  50  ALA   A HB3  1 
ATOM   1164 H  HB3  B ALA   A 1 50  ? 23.420 5.145   0.864   0.30 11.41 ?  50  ALA   A HB3  1 
ATOM   1165 N  N    A GLY   A 1 51  ? 21.999 6.923   2.293   0.70 11.05 ?  51  GLY   A N    1 
ATOM   1166 N  N    B GLY   A 1 51  ? 22.018 7.009   2.560   0.30 9.97  ?  51  GLY   A N    1 
ATOM   1167 C  CA   A GLY   A 1 51  ? 21.842 8.316   2.665   0.70 11.56 ?  51  GLY   A CA   1 
ATOM   1168 C  CA   B GLY   A 1 51  ? 21.831 8.394   2.953   0.30 10.26 ?  51  GLY   A CA   1 
ATOM   1169 C  C    A GLY   A 1 51  ? 21.228 8.473   4.040   0.70 11.40 ?  51  GLY   A C    1 
ATOM   1170 C  C    B GLY   A 1 51  ? 21.206 8.519   4.328   0.30 10.62 ?  51  GLY   A C    1 
ATOM   1171 O  O    A GLY   A 1 51  ? 21.607 9.368   4.800   0.70 12.18 ?  51  GLY   A O    1 
ATOM   1172 O  O    B GLY   A 1 51  ? 21.564 9.406   5.107   0.30 10.80 ?  51  GLY   A O    1 
ATOM   1173 H  H    A GLY   A 1 51  ? 21.578 6.686   1.584   0.70 13.22 ?  51  GLY   A H    1 
ATOM   1174 H  H    B GLY   A 1 51  ? 21.586 6.771   1.854   0.30 11.93 ?  51  GLY   A H    1 
ATOM   1175 H  HA2  A GLY   A 1 51  ? 22.707 8.754   2.665   0.70 13.84 ?  51  GLY   A HA2  1 
ATOM   1176 H  HA2  B GLY   A 1 51  ? 22.690 8.847   2.958   0.30 12.27 ?  51  GLY   A HA2  1 
ATOM   1177 H  HA3  A GLY   A 1 51  ? 21.269 8.762   2.022   0.70 13.84 ?  51  GLY   A HA3  1 
ATOM   1178 H  HA3  B GLY   A 1 51  ? 21.257 8.840   2.306   0.30 12.27 ?  51  GLY   A HA3  1 
ATOM   1179 N  N    A ALA   A 1 52  ? 20.254 7.618   4.371   0.70 11.35 ?  52  ALA   A N    1 
ATOM   1180 N  N    B ALA   A 1 52  ? 20.268 7.625   4.648   0.30 10.99 ?  52  ALA   A N    1 
ATOM   1181 C  CA   A ALA   A 1 52  ? 19.607 7.694   5.676   0.70 11.98 ?  52  ALA   A CA   1 
ATOM   1182 C  CA   B ALA   A 1 52  ? 19.591 7.695   5.937   0.30 11.20 ?  52  ALA   A CA   1 
ATOM   1183 C  C    A ALA   A 1 52  ? 20.551 7.266   6.799   0.70 11.58 ?  52  ALA   A C    1 
ATOM   1184 C  C    B ALA   A 1 52  ? 20.513 7.264   7.073   0.30 10.60 ?  52  ALA   A C    1 
ATOM   1185 O  O    A ALA   A 1 52  ? 20.638 7.932   7.834   0.70 12.41 ?  52  ALA   A O    1 
ATOM   1186 O  O    B ALA   A 1 52  ? 20.546 7.904   8.131   0.30 10.83 ?  52  ALA   A O    1 
ATOM   1187 C  CB   A ALA   A 1 52  ? 18.324 6.859   5.675   0.70 13.15 ?  52  ALA   A CB   1 
ATOM   1188 C  CB   B ALA   A 1 52  ? 18.322 6.847   5.900   0.30 12.03 ?  52  ALA   A CB   1 
ATOM   1189 H  H    A ALA   A 1 52  ? 19.970 6.982   3.868   0.70 13.58 ?  52  ALA   A H    1 
ATOM   1190 H  H    B ALA   A 1 52  ? 20.023 6.975   4.143   0.30 13.15 ?  52  ALA   A H    1 
ATOM   1191 H  HA   A ALA   A 1 52  ? 19.358 8.613   5.843   0.70 14.34 ?  52  ALA   A HA   1 
ATOM   1192 H  HA   B ALA   A 1 52  ? 19.334 8.615   6.095   0.30 13.41 ?  52  ALA   A HA   1 
ATOM   1193 H  HB1  A ALA   A 1 52  ? 17.902 6.925   6.548   0.70 15.74 ?  52  ALA   A HB1  1 
ATOM   1194 H  HB1  B ALA   A 1 52  ? 17.855 6.949   6.741   0.30 14.40 ?  52  ALA   A HB1  1 
ATOM   1195 H  HB2  A ALA   A 1 52  ? 17.724 7.207   4.995   0.70 15.74 ?  52  ALA   A HB2  1 
ATOM   1196 H  HB2  B ALA   A 1 52  ? 17.762 7.156   5.169   0.30 14.40 ?  52  ALA   A HB2  1 
ATOM   1197 H  HB3  A ALA   A 1 52  ? 18.543 5.936   5.483   0.70 15.74 ?  52  ALA   A HB3  1 
ATOM   1198 H  HB3  B ALA   A 1 52  ? 18.566 5.920   5.759   0.30 14.40 ?  52  ALA   A HB3  1 
ATOM   1199 N  N    A LEU   A 1 53  ? 21.272 6.155   6.620   0.70 11.40 ?  53  LEU   A N    1 
ATOM   1200 N  N    B LEU   A 1 53  ? 21.268 6.179   6.881   0.30 10.49 ?  53  LEU   A N    1 
ATOM   1201 C  CA   A LEU   A 1 53  ? 22.220 5.735   7.652   0.70 11.95 ?  53  LEU   A CA   1 
ATOM   1202 C  CA   B LEU   A 1 53  ? 22.263 5.797   7.878   0.30 10.68 ?  53  LEU   A CA   1 
ATOM   1203 C  C    A LEU   A 1 53  ? 23.277 6.805   7.876   0.70 11.42 ?  53  LEU   A C    1 
ATOM   1204 C  C    B LEU   A 1 53  ? 23.299 6.900   8.052   0.30 10.67 ?  53  LEU   A C    1 
ATOM   1205 O  O    A LEU   A 1 53  ? 23.616 7.128   9.018   0.70 12.48 ?  53  LEU   A O    1 
ATOM   1206 O  O    B LEU   A 1 53  ? 23.572 7.343   9.173   0.30 11.05 ?  53  LEU   A O    1 
ATOM   1207 C  CB   A LEU   A 1 53  ? 22.882 4.405   7.279   0.70 12.37 ?  53  LEU   A CB   1 
ATOM   1208 C  CB   B LEU   A 1 53  ? 22.940 4.479   7.484   0.30 10.76 ?  53  LEU   A CB   1 
ATOM   1209 C  CG   A LEU   A 1 53  ? 22.010 3.146   7.331   0.70 13.28 ?  53  LEU   A CG   1 
ATOM   1210 C  CG   B LEU   A 1 53  ? 22.127 3.180   7.551   0.30 11.41 ?  53  LEU   A CG   1 
ATOM   1211 C  CD1  A LEU   A 1 53  ? 22.734 1.965   6.709   0.70 13.35 ?  53  LEU   A CD1  1 
ATOM   1212 C  CD1  B LEU   A 1 53  ? 22.964 2.004   7.061   0.30 11.67 ?  53  LEU   A CD1  1 
ATOM   1213 C  CD2  A LEU   A 1 53  ? 21.607 2.808   8.758   0.70 14.78 ?  53  LEU   A CD2  1 
ATOM   1214 C  CD2  B LEU   A 1 53  ? 21.618 2.908   8.958   0.30 12.39 ?  53  LEU   A CD2  1 
ATOM   1215 H  H    A LEU   A 1 53  ? 21.239 5.642   5.933   0.70 13.65 ?  53  LEU   A H    1 
ATOM   1216 H  H    B LEU   A 1 53  ? 21.221 5.660   6.195   0.30 12.55 ?  53  LEU   A H    1 
ATOM   1217 H  HA   A LEU   A 1 53  ? 21.745 5.608   8.487   0.70 14.30 ?  53  LEU   A HA   1 
ATOM   1218 H  HA   B LEU   A 1 53  ? 21.820 5.671   8.727   0.30 12.77 ?  53  LEU   A HA   1 
ATOM   1219 H  HB2  A LEU   A 1 53  ? 23.222 4.478   6.374   0.70 14.80 ?  53  LEU   A HB2  1 
ATOM   1220 H  HB2  B LEU   A 1 53  ? 23.249 4.565   6.568   0.30 12.88 ?  53  LEU   A HB2  1 
ATOM   1221 H  HB3  A LEU   A 1 53  ? 23.628 4.256   7.885   0.70 14.80 ?  53  LEU   A HB3  1 
ATOM   1222 H  HB3  B LEU   A 1 53  ? 23.707 4.355   8.063   0.30 12.88 ?  53  LEU   A HB3  1 
ATOM   1223 H  HG   A LEU   A 1 53  ? 21.202 3.301   6.818   0.70 15.90 ?  53  LEU   A HG   1 
ATOM   1224 H  HG   B LEU   A 1 53  ? 21.361 3.257   6.962   0.30 13.65 ?  53  LEU   A HG   1 
ATOM   1225 H  HD11 A LEU   A 1 53  ? 22.160 1.184   6.755   0.70 15.99 ?  53  LEU   A HD11 1 
ATOM   1226 H  HD11 B LEU   A 1 53  ? 22.432 1.193   7.111   0.30 13.97 ?  53  LEU   A HD11 1 
ATOM   1227 H  HD12 A LEU   A 1 53  ? 22.939 2.172   5.785   0.70 15.99 ?  53  LEU   A HD12 1 
ATOM   1228 H  HD12 B LEU   A 1 53  ? 23.232 2.165   6.142   0.30 13.97 ?  53  LEU   A HD12 1 
ATOM   1229 H  HD13 A LEU   A 1 53  ? 23.554 1.803   7.203   0.70 15.99 ?  53  LEU   A HD13 1 
ATOM   1230 H  HD13 B LEU   A 1 53  ? 23.750 1.917   7.624   0.30 13.97 ?  53  LEU   A HD13 1 
ATOM   1231 H  HD21 A LEU   A 1 53  ? 21.106 1.976   8.756   0.70 17.70 ?  53  LEU   A HD21 1 
ATOM   1232 H  HD21 B LEU   A 1 53  ? 20.960 2.195   8.918   0.30 14.83 ?  53  LEU   A HD21 1 
ATOM   1233 H  HD22 A LEU   A 1 53  ? 22.405 2.713   9.299   0.70 17.70 ?  53  LEU   A HD22 1 
ATOM   1234 H  HD22 B LEU   A 1 53  ? 22.362 2.640   9.515   0.30 14.83 ?  53  LEU   A HD22 1 
ATOM   1235 H  HD23 A LEU   A 1 53  ? 21.052 3.524   9.107   0.70 17.70 ?  53  LEU   A HD23 1 
ATOM   1236 H  HD23 B LEU   A 1 53  ? 21.209 3.710   9.312   0.30 14.83 ?  53  LEU   A HD23 1 
ATOM   1237 N  N    A ASN   A 1 54  ? 23.805 7.370   6.798   0.70 11.21 ?  54  ASN   A N    1 
ATOM   1238 N  N    B ASN   A 1 54  ? 23.873 7.370   6.945   0.30 11.02 ?  54  ASN   A N    1 
ATOM   1239 C  CA   A ASN   A 1 54  ? 24.861 8.357   6.961   0.70 11.11 ?  54  ASN   A CA   1 
ATOM   1240 C  CA   B ASN   A 1 54  ? 24.907 8.391   7.048   0.30 11.16 ?  54  ASN   A CA   1 
ATOM   1241 C  C    A ASN   A 1 54  ? 24.353 9.595   7.702   0.70 11.73 ?  54  ASN   A C    1 
ATOM   1242 C  C    B ASN   A 1 54  ? 24.372 9.653   7.710   0.30 11.32 ?  54  ASN   A C    1 
ATOM   1243 O  O    A ASN   A 1 54  ? 25.045 10.134  8.575   0.70 12.32 ?  54  ASN   A O    1 
ATOM   1244 O  O    B ASN   A 1 54  ? 25.059 10.267  8.535   0.30 11.35 ?  54  ASN   A O    1 
ATOM   1245 C  CB   A ASN   A 1 54  ? 25.435 8.726   5.604   0.70 11.14 ?  54  ASN   A CB   1 
ATOM   1246 C  CB   B ASN   A 1 54  ? 25.483 8.715   5.675   0.30 11.43 ?  54  ASN   A CB   1 
ATOM   1247 C  CG   A ASN   A 1 54  ? 26.474 9.806   5.721   0.70 11.41 ?  54  ASN   A CG   1 
ATOM   1248 C  CG   B ASN   A 1 54  ? 26.457 9.867   5.733   0.30 11.63 ?  54  ASN   A CG   1 
ATOM   1249 O  OD1  A ASN   A 1 54  ? 27.457 9.657   6.460   0.70 11.43 ?  54  ASN   A OD1  1 
ATOM   1250 O  OD1  B ASN   A 1 54  ? 27.534 9.745   6.317   0.30 11.79 ?  54  ASN   A OD1  1 
ATOM   1251 N  ND2  A ASN   A 1 54  ? 26.266 10.910  5.023   0.70 11.87 ?  54  ASN   A ND2  1 
ATOM   1252 N  ND2  B ASN   A 1 54  ? 26.079 11.001  5.156   0.30 11.78 ?  54  ASN   A ND2  1 
ATOM   1253 H  H    A ASN   A 1 54  ? 23.567 7.213   5.988   0.70 13.41 ?  54  ASN   A H    1 
ATOM   1254 H  H    B ASN   A 1 54  ? 23.679 7.127   6.145   0.30 13.18 ?  54  ASN   A H    1 
ATOM   1255 H  HA   A ASN   A 1 54  ? 25.570 7.969   7.489   0.70 13.29 ?  54  ASN   A HA   1 
ATOM   1256 H  HA   B ASN   A 1 54  ? 25.624 8.054   7.602   0.30 13.35 ?  54  ASN   A HA   1 
ATOM   1257 H  HB2  A ASN   A 1 54  ? 25.853 7.937   5.212   0.70 13.33 ?  54  ASN   A HB2  1 
ATOM   1258 H  HB2  B ASN   A 1 54  ? 25.957 7.938   5.340   0.30 13.68 ?  54  ASN   A HB2  1 
ATOM   1259 H  HB3  A ASN   A 1 54  ? 24.726 9.046   5.027   0.70 13.33 ?  54  ASN   A HB3  1 
ATOM   1260 H  HB3  B ASN   A 1 54  ? 24.764 8.956   5.074   0.30 13.68 ?  54  ASN   A HB3  1 
ATOM   1261 H  HD21 A ASN   A 1 54  ? 26.835 11.552  5.060   0.70 14.20 ?  54  ASN   A HD21 1 
ATOM   1262 H  HD21 B ASN   A 1 54  ? 26.599 11.687  5.172   0.30 14.10 ?  54  ASN   A HD21 1 
ATOM   1263 H  HD22 A ASN   A 1 54  ? 25.565 10.981  4.531   0.70 14.20 ?  54  ASN   A HD22 1 
ATOM   1264 H  HD22 B ASN   A 1 54  ? 25.317 11.049  4.761   0.30 14.10 ?  54  ASN   A HD22 1 
ATOM   1265 N  N    . LYS   A 1 55  ? 23.153 10.069  7.356   1.00 11.49 ?  55  LYS   A N    1 
ATOM   1266 C  CA   . LYS   A 1 55  ? 22.573 11.231  8.020   1.00 12.39 ?  55  LYS   A CA   1 
ATOM   1267 C  C    . LYS   A 1 55  ? 22.468 11.003  9.522   1.00 12.53 ?  55  LYS   A C    1 
ATOM   1268 O  O    . LYS   A 1 55  ? 22.752 11.905  10.321  1.00 13.54 ?  55  LYS   A O    1 
ATOM   1269 C  CB   . LYS   A 1 55  ? 21.204 11.532  7.411   1.00 13.23 ?  55  LYS   A CB   1 
ATOM   1270 C  CG   . LYS   A 1 55  ? 20.477 12.719  8.029   1.00 14.94 ?  55  LYS   A CG   1 
ATOM   1271 C  CD   . LYS   A 1 55  ? 19.136 12.941  7.335   1.00 16.60 ?  55  LYS   A CD   1 
ATOM   1272 C  CE   . LYS   A 1 55  ? 18.315 14.049  7.985   1.00 18.46 ?  55  LYS   A CE   1 
ATOM   1273 N  NZ   . LYS   A 1 55  ? 16.985 14.198  7.328   1.00 19.33 ?  55  LYS   A NZ   1 
ATOM   1274 H  H    A LYS   A 1 55  ? 22.653 9.734   6.743   0.70 13.75 ?  55  LYS   A H    1 
ATOM   1275 H  H    B LYS   A 1 55  ? 22.653 9.706   6.759   0.30 13.75 ?  55  LYS   A H    1 
ATOM   1276 H  HA   . LYS   A 1 55  ? 23.141 12.004  7.874   1.00 14.83 ?  55  LYS   A HA   1 
ATOM   1277 H  HB2  . LYS   A 1 55  ? 21.317 11.721  6.468   1.00 15.84 ?  55  LYS   A HB2  1 
ATOM   1278 H  HB3  . LYS   A 1 55  ? 20.636 10.754  7.524   1.00 15.84 ?  55  LYS   A HB3  1 
ATOM   1279 H  HG2  . LYS   A 1 55  ? 20.307 12.545  8.969   1.00 17.88 ?  55  LYS   A HG2  1 
ATOM   1280 H  HG3  . LYS   A 1 55  ? 21.013 13.519  7.923   1.00 17.88 ?  55  LYS   A HG3  1 
ATOM   1281 H  HD2  . LYS   A 1 55  ? 19.299 13.181  6.410   1.00 19.88 ?  55  LYS   A HD2  1 
ATOM   1282 H  HD3  . LYS   A 1 55  ? 18.623 12.116  7.377   1.00 19.88 ?  55  LYS   A HD3  1 
ATOM   1283 H  HE2  . LYS   A 1 55  ? 18.173 13.834  8.919   1.00 22.11 ?  55  LYS   A HE2  1 
ATOM   1284 H  HE3  . LYS   A 1 55  ? 18.794 14.888  7.901   1.00 22.11 ?  55  LYS   A HE3  1 
ATOM   1285 H  HZ1  . LYS   A 1 55  ? 16.404 14.566  7.895   1.00 23.16 ?  55  LYS   A HZ1  1 
ATOM   1286 H  HZ2  . LYS   A 1 55  ? 17.052 14.723  6.610   1.00 23.16 ?  55  LYS   A HZ2  1 
ATOM   1287 H  HZ3  . LYS   A 1 55  ? 16.672 13.403  7.076   1.00 23.16 ?  55  LYS   A HZ3  1 
ATOM   1288 N  N    . ALA   A 1 56  ? 22.078 9.789   9.925   1.00 12.91 ?  56  ALA   A N    1 
ATOM   1289 C  CA   . ALA   A 1 56  ? 21.949 9.474   11.340  1.00 13.52 ?  56  ALA   A CA   1 
ATOM   1290 C  C    . ALA   A 1 56  ? 23.288 9.502   12.070  1.00 13.42 ?  56  ALA   A C    1 
ATOM   1291 O  O    . ALA   A 1 56  ? 23.302 9.693   13.289  1.00 14.51 ?  56  ALA   A O    1 
ATOM   1292 C  CB   . ALA   A 1 56  ? 21.241 8.126   11.523  1.00 14.45 ?  56  ALA   A CB   1 
ATOM   1293 H  H    . ALA   A 1 56  ? 21.886 9.142   9.396   1.00 15.46 ?  56  ALA   A H    1 
ATOM   1294 H  HA   . ALA   A 1 56  ? 21.397 10.141  11.757  1.00 16.19 ?  56  ALA   A HA   1 
ATOM   1295 H  HB1  . ALA   A 1 56  ? 21.165 7.929   12.471  1.00 17.30 ?  56  ALA   A HB1  1 
ATOM   1296 H  HB2  . ALA   A 1 56  ? 20.353 8.185   11.130  1.00 17.30 ?  56  ALA   A HB2  1 
ATOM   1297 H  HB3  . ALA   A 1 56  ? 21.749 7.430   11.080  1.00 17.30 ?  56  ALA   A HB3  1 
ATOM   1298 N  N    . THR   A 1 57  ? 24.408 9.315   11.358  1.00 12.65 ?  57  THR   A N    1 
ATOM   1299 C  CA   . THR   A 1 57  ? 25.749 9.444   11.934  1.00 12.68 ?  57  THR   A CA   1 
ATOM   1300 C  C    . THR   A 1 57  ? 26.304 10.860  11.855  1.00 12.89 ?  57  THR   A C    1 
ATOM   1301 O  O    . THR   A 1 57  ? 27.487 11.065  12.150  1.00 13.47 ?  57  THR   A O    1 
ATOM   1302 C  CB   . THR   A 1 57  ? 26.757 8.488   11.268  1.00 12.12 ?  57  THR   A CB   1 
ATOM   1303 O  OG1  . THR   A 1 57  ? 27.146 8.977   9.971   1.00 12.20 ?  57  THR   A OG1  1 
ATOM   1304 C  CG2  . THR   A 1 57  ? 26.220 7.066   11.158  1.00 12.20 ?  57  THR   A CG2  1 
ATOM   1305 H  H    . THR   A 1 57  ? 24.415 9.095   10.525  1.00 15.14 ?  57  THR   A H    1 
ATOM   1306 H  HA   . THR   A 1 57  ? 25.706 9.188   12.874  1.00 15.18 ?  57  THR   A HA   1 
ATOM   1307 H  HB   . THR   A 1 57  ? 27.557 8.446   11.825  1.00 14.51 ?  57  THR   A HB   1 
ATOM   1308 H  HG1  . THR   A 1 57  ? 26.467 9.058   9.481   1.00 14.60 ?  57  THR   A HG1  1 
ATOM   1309 H  HG21 . THR   A 1 57  ? 26.921 6.459   10.863  1.00 14.61 ?  57  THR   A HG21 1 
ATOM   1310 H  HG22 . THR   A 1 57  ? 25.887 6.764   12.017  1.00 14.61 ?  57  THR   A HG22 1 
ATOM   1311 H  HG23 . THR   A 1 57  ? 25.494 7.033   10.514  1.00 14.61 ?  57  THR   A HG23 1 
ATOM   1312 N  N    . ASN   A 1 58  ? 25.496 11.836  11.446  1.00 13.30 ?  58  ASN   A N    1 
ATOM   1313 C  CA   . ASN   A 1 58  ? 25.964 13.213  11.354  1.00 14.29 ?  58  ASN   A CA   1 
ATOM   1314 C  C    . ASN   A 1 58  ? 27.111 13.340  10.346  1.00 13.04 ?  58  ASN   A C    1 
ATOM   1315 O  O    . ASN   A 1 58  ? 27.995 14.183  10.497  1.00 13.83 ?  58  ASN   A O    1 
ATOM   1316 C  CB   . ASN   A 1 58  ? 26.351 13.743  12.749  1.00 16.50 ?  58  ASN   A CB   1 
ATOM   1317 C  CG   . ASN   A 1 58  ? 26.782 15.199  12.749  1.00 19.59 ?  58  ASN   A CG   1 
ATOM   1318 O  OD1  . ASN   A 1 58  ? 26.152 16.041  12.117  1.00 21.14 ?  58  ASN   A OD1  1 
ATOM   1319 N  ND2  . ASN   A 1 58  ? 27.855 15.506  13.484  1.00 20.43 ?  58  ASN   A ND2  1 
ATOM   1320 H  H    . ASN   A 1 58  ? 24.676 11.717  11.218  1.00 15.92 ?  58  ASN   A H    1 
ATOM   1321 H  HA   . ASN   A 1 58  ? 25.232 13.752  11.032  1.00 17.11 ?  58  ASN   A HA   1 
ATOM   1322 H  HB2  . ASN   A 1 58  ? 25.579 13.662  13.341  1.00 19.77 ?  58  ASN   A HB2  1 
ATOM   1323 H  HB3  . ASN   A 1 58  ? 27.084 13.222  13.103  1.00 19.77 ?  58  ASN   A HB3  1 
ATOM   1324 H  HD21 . ASN   A 1 58  ? 28.135 16.320  13.516  1.00 24.48 ?  58  ASN   A HD21 1 
ATOM   1325 H  HD22 . ASN   A 1 58  ? 28.264 14.891  13.919  1.00 24.48 ?  58  ASN   A HD22 1 
ATOM   1326 N  N    . ASN   A 1 59  ? 27.096 12.513  9.298   1.00 12.21 ?  59  ASN   A N    1 
ATOM   1327 C  CA   . ASN   A 1 59  ? 28.076 12.482  8.202   1.00 12.23 ?  59  ASN   A CA   1 
ATOM   1328 C  C    . ASN   A 1 59  ? 29.388 11.800  8.592   1.00 11.70 ?  59  ASN   A C    1 
ATOM   1329 O  O    . ASN   A 1 59  ? 30.311 11.759  7.769   1.00 11.92 ?  59  ASN   A O    1 
ATOM   1330 C  CB   . ASN   A 1 59  ? 28.372 13.866  7.589   1.00 12.13 ?  59  ASN   A CB   1 
ATOM   1331 C  CG   . ASN   A 1 59  ? 28.726 13.792  6.115   1.00 12.37 ?  59  ASN   A CG   1 
ATOM   1332 O  OD1  . ASN   A 1 59  ? 28.018 13.164  5.324   1.00 12.87 ?  59  ASN   A OD1  1 
ATOM   1333 N  ND2  . ASN   A 1 59  ? 29.821 14.452  5.731   1.00 13.09 ?  59  ASN   A ND2  1 
ATOM   1334 H  H    . ASN   A 1 59  ? 26.487 11.913  9.191   1.00 14.61 ?  59  ASN   A H    1 
ATOM   1335 H  HA   . ASN   A 1 59  ? 27.693 11.953  7.489   1.00 14.63 ?  59  ASN   A HA   1 
ATOM   1336 H  HB2  . ASN   A 1 59  ? 27.590 14.434  7.674   1.00 14.52 ?  59  ASN   A HB2  1 
ATOM   1337 H  HB3  . ASN   A 1 59  ? 29.125 14.270  8.051   1.00 14.52 ?  59  ASN   A HB3  1 
ATOM   1338 H  HD21 . ASN   A 1 59  ? 30.066 14.443  4.902   1.00 15.67 ?  59  ASN   A HD21 1 
ATOM   1339 H  HD22 . ASN   A 1 59  ? 30.296 14.884  6.307   1.00 15.67 ?  59  ASN   A HD22 1 
ATOM   1340 N  N    . ALA   A 1 60  ? 29.506 11.265  9.806   1.00 11.69 ?  60  ALA   A N    1 
ATOM   1341 C  CA   . ALA   A 1 60  ? 30.742 10.584  10.175  1.00 11.94 ?  60  ALA   A CA   1 
ATOM   1342 C  C    . ALA   A 1 60  ? 30.977 9.344   9.323   1.00 12.06 ?  60  ALA   A C    1 
ATOM   1343 O  O    . ALA   A 1 60  ? 32.128 9.027   8.999   1.00 12.48 ?  60  ALA   A O    1 
ATOM   1344 C  CB   . ALA   A 1 60  ? 30.740 10.239  11.662  1.00 12.65 ?  60  ALA   A CB   1 
ATOM   1345 H  H    . ALA   A 1 60  ? 28.908 11.286  10.420  1.00 14.00 ?  60  ALA   A H    1 
ATOM   1346 H  HA   . ALA   A 1 60  ? 31.489 11.193  10.023  1.00 14.29 ?  60  ALA   A HA   1 
ATOM   1347 H  HB1  . ALA   A 1 60  ? 31.568 9.792   11.889  1.00 15.15 ?  60  ALA   A HB1  1 
ATOM   1348 H  HB2  . ALA   A 1 60  ? 30.657 11.060  12.181  1.00 15.15 ?  60  ALA   A HB2  1 
ATOM   1349 H  HB3  . ALA   A 1 60  ? 29.985 9.659   11.849  1.00 15.15 ?  60  ALA   A HB3  1 
ATOM   1350 N  N    . MET   A 1 61  ? 29.908 8.645   8.937   1.00 11.47 ?  61  MET   A N    1 
ATOM   1351 C  CA   . MET   A 1 61  ? 30.051 7.504   8.037   1.00 11.59 ?  61  MET   A CA   1 
ATOM   1352 C  C    . MET   A 1 61  ? 30.688 7.922   6.715   1.00 11.44 ?  61  MET   A C    1 
ATOM   1353 O  O    . MET   A 1 61  ? 31.589 7.244   6.209   1.00 11.77 ?  61  MET   A O    1 
ATOM   1354 C  CB   . MET   A 1 61  ? 28.686 6.852   7.811   1.00 11.81 ?  61  MET   A CB   1 
ATOM   1355 C  CG   . MET   A 1 61  ? 28.700 5.677   6.843   1.00 12.35 ?  61  MET   A CG   1 
ATOM   1356 S  SD   . MET   A 1 61  ? 27.076 4.943   6.610   1.00 12.98 ?  61  MET   A SD   1 
ATOM   1357 C  CE   . MET   A 1 61  ? 26.914 4.058   8.167   1.00 14.95 ?  61  MET   A CE   1 
ATOM   1358 H  H    . MET   A 1 61  ? 29.100 8.808   9.181   1.00 13.73 ?  61  MET   A H    1 
ATOM   1359 H  HA   . MET   A 1 61  ? 30.622 6.843   8.460   1.00 13.87 ?  61  MET   A HA   1 
ATOM   1360 H  HB2  . MET   A 1 61  ? 28.350 6.529   8.660   1.00 14.13 ?  61  MET   A HB2  1 
ATOM   1361 H  HB3  . MET   A 1 61  ? 28.079 7.517   7.451   1.00 14.13 ?  61  MET   A HB3  1 
ATOM   1362 H  HG2  . MET   A 1 61  ? 29.006 5.968   5.973   1.00 14.78 ?  61  MET   A HG2  1 
ATOM   1363 H  HG3  . MET   A 1 61  ? 29.282 4.980   7.186   1.00 14.78 ?  61  MET   A HG3  1 
ATOM   1364 H  HE1  . MET   A 1 61  ? 26.068 3.584   8.175   1.00 17.90 ?  61  MET   A HE1  1 
ATOM   1365 H  HE2  . MET   A 1 61  ? 27.648 3.434   8.251   1.00 17.90 ?  61  MET   A HE2  1 
ATOM   1366 H  HE3  . MET   A 1 61  ? 26.939 4.698   8.900   1.00 17.90 ?  61  MET   A HE3  1 
ATOM   1367 N  N    . GLN   A 1 62  ? 30.253 9.055   6.156   1.00 11.34 ?  62  GLN   A N    1 
ATOM   1368 C  CA   . GLN   A 1 62  ? 30.817 9.519   4.892   1.00 11.48 ?  62  GLN   A CA   1 
ATOM   1369 C  C    . GLN   A 1 62  ? 32.286 9.899   5.041   1.00 11.53 ?  62  GLN   A C    1 
ATOM   1370 O  O    . GLN   A 1 62  ? 33.098 9.582   4.167   1.00 11.80 ?  62  GLN   A O    1 
ATOM   1371 C  CB   . GLN   A 1 62  ? 30.022 10.706  4.354   1.00 11.45 ?  62  GLN   A CB   1 
ATOM   1372 C  CG   . GLN   A 1 62  ? 30.399 11.070  2.930   1.00 11.64 ?  62  GLN   A CG   1 
ATOM   1373 C  CD   . GLN   A 1 62  ? 30.074 9.941   1.983   1.00 11.69 ?  62  GLN   A CD   1 
ATOM   1374 O  OE1  . GLN   A 1 62  ? 28.898 9.636   1.764   1.00 12.55 ?  62  GLN   A OE1  1 
ATOM   1375 N  NE2  . GLN   A 1 62  ? 31.097 9.263   1.468   1.00 12.29 ?  62  GLN   A NE2  1 
ATOM   1376 H  H    . GLN   A 1 62  ? 29.641 9.558   6.487   1.00 13.57 ?  62  GLN   A H    1 
ATOM   1377 H  HA   . GLN   A 1 62  ? 30.764 8.798   4.250   1.00 13.73 ?  62  GLN   A HA   1 
ATOM   1378 H  HB2  . GLN   A 1 62  ? 29.078 10.486  4.374   1.00 13.70 ?  62  GLN   A HB2  1 
ATOM   1379 H  HB3  . GLN   A 1 62  ? 30.194 11.480  4.914   1.00 13.70 ?  62  GLN   A HB3  1 
ATOM   1380 H  HG2  . GLN   A 1 62  ? 29.888 11.843  2.650   1.00 13.93 ?  62  GLN   A HG2  1 
ATOM   1381 H  HG3  . GLN   A 1 62  ? 31.346 11.246  2.875   1.00 13.93 ?  62  GLN   A HG3  1 
ATOM   1382 H  HE21 . GLN   A 1 62  ? 31.904 9.494   1.659   1.00 14.71 ?  62  GLN   A HE21 1 
ATOM   1383 H  HE22 . GLN   A 1 62  ? 30.956 8.605   0.931   1.00 14.71 ?  62  GLN   A HE22 1 
ATOM   1384 N  N    . VAL   A 1 63  ? 32.642 10.583  6.133   1.00 12.08 ?  63  VAL   A N    1 
ATOM   1385 C  CA   . VAL   A 1 63  ? 34.034 10.969  6.355   1.00 12.56 ?  63  VAL   A CA   1 
ATOM   1386 C  C    . VAL   A 1 63  ? 34.924 9.731   6.428   1.00 11.88 ?  63  VAL   A C    1 
ATOM   1387 O  O    . VAL   A 1 63  ? 35.985 9.662   5.789   1.00 12.82 ?  63  VAL   A O    1 
ATOM   1388 C  CB   . VAL   A 1 63  ? 34.137 11.856  7.611   1.00 14.35 ?  63  VAL   A CB   1 
ATOM   1389 C  CG1  . VAL   A 1 63  ? 35.577 12.078  8.004   1.00 15.89 ?  63  VAL   A CG1  1 
ATOM   1390 C  CG2  . VAL   A 1 63  ? 33.441 13.201  7.362   1.00 14.38 ?  63  VAL   A CG2  1 
ATOM   1391 H  H    . VAL   A 1 63  ? 32.096 10.831  6.752   1.00 14.46 ?  63  VAL   A H    1 
ATOM   1392 H  HA   . VAL   A 1 63  ? 34.331 11.498  5.603   1.00 15.03 ?  63  VAL   A HA   1 
ATOM   1393 H  HB   . VAL   A 1 63  ? 33.685 11.424  8.352   1.00 17.18 ?  63  VAL   A HB   1 
ATOM   1394 H  HG11 . VAL   A 1 63  ? 35.619 12.820  8.630   1.00 19.03 ?  63  VAL   A HG11 1 
ATOM   1395 H  HG12 . VAL   A 1 63  ? 35.917 11.275  8.419   1.00 19.03 ?  63  VAL   A HG12 1 
ATOM   1396 H  HG13 . VAL   A 1 63  ? 36.087 12.291  7.208   1.00 19.03 ?  63  VAL   A HG13 1 
ATOM   1397 H  HG21 . VAL   A 1 63  ? 33.519 13.754  8.157   1.00 17.22 ?  63  VAL   A HG21 1 
ATOM   1398 H  HG22 . VAL   A 1 63  ? 33.872 13.646  6.611   1.00 17.22 ?  63  VAL   A HG22 1 
ATOM   1399 H  HG23 . VAL   A 1 63  ? 32.507 13.045  7.159   1.00 17.22 ?  63  VAL   A HG23 1 
ATOM   1400 N  N    . GLU   A 1 64  ? 34.495 8.724   7.195   1.00 11.95 ?  64  GLU   A N    1 
ATOM   1401 C  CA   . GLU   A 1 64  ? 35.260 7.489   7.297   1.00 12.12 ?  64  GLU   A CA   1 
ATOM   1402 C  C    . GLU   A 1 64  ? 35.360 6.806   5.941   1.00 11.66 ?  64  GLU   A C    1 
ATOM   1403 O  O    . GLU   A 1 64  ? 36.412 6.264   5.574   1.00 12.24 ?  64  GLU   A O    1 
ATOM   1404 C  CB   . GLU   A 1 64  ? 34.577 6.579   8.319   1.00 12.73 ?  64  GLU   A CB   1 
ATOM   1405 C  CG   . GLU   A 1 64  ? 35.232 5.228   8.459   1.00 13.20 ?  64  GLU   A CG   1 
ATOM   1406 C  CD   . GLU   A 1 64  ? 34.359 4.233   9.194   1.00 14.16 ?  64  GLU   A CD   1 
ATOM   1407 O  OE1  . GLU   A 1 64  ? 33.119 4.325   9.068   1.00 14.88 ?  64  GLU   A OE1  1 
ATOM   1408 O  OE2  . GLU   A 1 64  ? 34.922 3.341   9.873   1.00 14.63 -1 64  GLU   A OE2  1 
ATOM   1409 H  H    . GLU   A 1 64  ? 33.761 8.730   7.652   1.00 14.30 ?  64  GLU   A H    1 
ATOM   1410 H  HA   . GLU   A 1 64  ? 36.156 7.697   7.616   1.00 14.51 ?  64  GLU   A HA   1 
ATOM   1411 H  HB2  . GLU   A 1 64  ? 34.609 7.017   9.193   1.00 15.24 ?  64  GLU   A HB2  1 
ATOM   1412 H  HB3  . GLU   A 1 64  ? 33.657 6.454   8.053   1.00 15.24 ?  64  GLU   A HB3  1 
ATOM   1413 H  HG2  . GLU   A 1 64  ? 35.413 4.864   7.574   1.00 15.80 ?  64  GLU   A HG2  1 
ATOM   1414 H  HG3  . GLU   A 1 64  ? 36.059 5.328   8.948   1.00 15.80 ?  64  GLU   A HG3  1 
ATOM   1415 N  N    . SER   A 1 65  ? 34.246 6.787   5.205   1.00 11.33 ?  65  SER   A N    1 
ATOM   1416 C  CA   . SER   A 1 65  ? 34.196 6.132   3.903   1.00 11.37 ?  65  SER   A CA   1 
ATOM   1417 C  C    . SER   A 1 65  ? 35.124 6.793   2.892   1.00 11.62 ?  65  SER   A C    1 
ATOM   1418 O  O    . SER   A 1 65  ? 35.769 6.107   2.088   1.00 12.52 ?  65  SER   A O    1 
ATOM   1419 C  CB   . SER   A 1 65  ? 32.769 6.140   3.367   1.00 11.58 ?  65  SER   A CB   1 
ATOM   1420 O  OG   . SER   A 1 65  ? 31.909 5.334   4.167   1.00 11.97 ?  65  SER   A OG   1 
ATOM   1421 H  H    . SER   A 1 65  ? 33.504 7.149   5.445   1.00 13.56 ?  65  SER   A H    1 
ATOM   1422 H  HA   . SER   A 1 65  ? 34.479 5.211   4.005   1.00 13.60 ?  65  SER   A HA   1 
ATOM   1423 H  HB2  . SER   A 1 65  ? 32.439 7.049   3.366   1.00 13.86 ?  65  SER   A HB2  1 
ATOM   1424 H  HB3  . SER   A 1 65  ? 32.779 5.788   2.463   1.00 13.86 ?  65  SER   A HB3  1 
ATOM   1425 H  HG   . SER   A 1 65  ? 31.898 5.627   4.957   1.00 14.33 ?  65  SER   A HG   1 
ATOM   1426 N  N    . ASP   A 1 66  ? 35.192 8.126   2.899   1.00 11.85 ?  66  ASP   A N    1 
ATOM   1427 C  CA   . ASP   A 1 66  ? 36.064 8.816   1.954   1.00 12.64 ?  66  ASP   A CA   1 
ATOM   1428 C  C    . ASP   A 1 66  ? 37.529 8.471   2.209   1.00 12.74 ?  66  ASP   A C    1 
ATOM   1429 O  O    . ASP   A 1 66  ? 38.309 8.296   1.264   1.00 13.37 ?  66  ASP   A O    1 
ATOM   1430 C  CB   . ASP   A 1 66  ? 35.837 10.323  2.034   1.00 14.08 ?  66  ASP   A CB   1 
ATOM   1431 C  CG   . ASP   A 1 66  ? 34.509 10.775  1.404   1.00 15.70 ?  66  ASP   A CG   1 
ATOM   1432 O  OD1  . ASP   A 1 66  ? 33.807 9.971   0.747   1.00 16.21 ?  66  ASP   A OD1  1 
ATOM   1433 O  OD2  . ASP   A 1 66  ? 34.199 11.978  1.551   1.00 18.66 -1 66  ASP   A OD2  1 
ATOM   1434 H  H    . ASP   A 1 66  ? 34.741 8.647   3.423   1.00 14.18 ?  66  ASP   A H    1 
ATOM   1435 H  HA   . ASP   A 1 66  ? 35.839 8.528   1.056   1.00 15.13 ?  66  ASP   A HA   1 
ATOM   1436 H  HB2  . ASP   A 1 66  ? 35.822 10.591  2.965   1.00 16.86 ?  66  ASP   A HB2  1 
ATOM   1437 H  HB3  . ASP   A 1 66  ? 36.559 10.774  1.570   1.00 16.86 ?  66  ASP   A HB3  1 
ATOM   1438 N  N    . ASP   A 1 67  ? 37.917 8.354   3.480   1.00 12.71 ?  67  ASP   A N    1 
ATOM   1439 C  CA   . ASP   A 1 67  ? 39.272 7.912   3.795   1.00 13.38 ?  67  ASP   A CA   1 
ATOM   1440 C  C    . ASP   A 1 67  ? 39.503 6.479   3.328   1.00 13.70 ?  67  ASP   A C    1 
ATOM   1441 O  O    . ASP   A 1 67  ? 40.567 6.158   2.785   1.00 14.25 ?  67  ASP   A O    1 
ATOM   1442 C  CB   . ASP   A 1 67  ? 39.529 8.059   5.295   1.00 14.66 ?  67  ASP   A CB   1 
ATOM   1443 C  CG   . ASP   A 1 67  ? 40.829 7.416   5.735   1.00 15.82 ?  67  ASP   A CG   1 
ATOM   1444 O  OD1  . ASP   A 1 67  ? 41.892 8.071   5.648   1.00 18.37 ?  67  ASP   A OD1  1 
ATOM   1445 O  OD2  . ASP   A 1 67  ? 40.775 6.244   6.173   1.00 16.01 -1 67  ASP   A OD2  1 
ATOM   1446 H  H    . ASP   A 1 67  ? 37.424 8.529   4.164   1.00 15.21 ?  67  ASP   A H    1 
ATOM   1447 H  HA   . ASP   A 1 67  ? 39.902 8.481   3.327   1.00 16.02 ?  67  ASP   A HA   1 
ATOM   1448 H  HB2  . ASP   A 1 67  ? 39.568 9.002   5.515   1.00 17.56 ?  67  ASP   A HB2  1 
ATOM   1449 H  HB3  . ASP   A 1 67  ? 38.805 7.634   5.782   1.00 17.56 ?  67  ASP   A HB3  1 
ATOM   1450 N  N    . TYR   A 1 68  ? 38.511 5.601   3.513   1.00 13.13 ?  68  TYR   A N    1 
ATOM   1451 C  CA   . TYR   A 1 68  ? 38.640 4.219   3.047   1.00 13.37 ?  68  TYR   A CA   1 
ATOM   1452 C  C    . TYR   A 1 68  ? 38.875 4.162   1.538   1.00 13.08 ?  68  TYR   A C    1 
ATOM   1453 O  O    . TYR   A 1 68  ? 39.759 3.435   1.064   1.00 13.63 ?  68  TYR   A O    1 
ATOM   1454 C  CB   . TYR   A 1 68  ? 37.397 3.398   3.440   1.00 13.78 ?  68  TYR   A CB   1 
ATOM   1455 C  CG   . TYR   A 1 68  ? 37.428 2.006   2.822   1.00 15.10 ?  68  TYR   A CG   1 
ATOM   1456 C  CD1  . TYR   A 1 68  ? 36.971 1.805   1.525   1.00 16.61 ?  68  TYR   A CD1  1 
ATOM   1457 C  CD2  . TYR   A 1 68  ? 37.974 0.926   3.498   1.00 16.86 ?  68  TYR   A CD2  1 
ATOM   1458 C  CE1  . TYR   A 1 68  ? 37.043 0.590   0.917   1.00 18.05 ?  68  TYR   A CE1  1 
ATOM   1459 C  CE2  . TYR   A 1 68  ? 38.033 -0.336  2.893   1.00 18.12 ?  68  TYR   A CE2  1 
ATOM   1460 C  CZ   . TYR   A 1 68  ? 37.572 -0.479  1.600   1.00 18.29 ?  68  TYR   A CZ   1 
ATOM   1461 O  OH   . TYR   A 1 68  ? 37.649 -1.693  0.970   1.00 20.06 ?  68  TYR   A OH   1 
ATOM   1462 H  H    . TYR   A 1 68  ? 37.762 5.776   3.907   1.00 15.72 ?  68  TYR   A H    1 
ATOM   1463 H  HA   . TYR   A 1 68  ? 39.403 3.816   3.483   1.00 16.00 ?  68  TYR   A HA   1 
ATOM   1464 H  HB2  . TYR   A 1 68  ? 37.366 3.300   4.406   1.00 16.50 ?  68  TYR   A HB2  1 
ATOM   1465 H  HB3  . TYR   A 1 68  ? 36.597 3.851   3.125   1.00 16.50 ?  68  TYR   A HB3  1 
ATOM   1466 H  HD1  . TYR   A 1 68  ? 36.626 2.527   1.053   1.00 19.89 ?  68  TYR   A HD1  1 
ATOM   1467 H  HD2  . TYR   A 1 68  ? 38.300 1.037   4.361   1.00 20.20 ?  68  TYR   A HD2  1 
ATOM   1468 H  HE1  . TYR   A 1 68  ? 36.727 0.480   0.050   1.00 21.62 ?  68  TYR   A HE1  1 
ATOM   1469 H  HE2  . TYR   A 1 68  ? 38.405 -1.063  3.339   1.00 21.70 ?  68  TYR   A HE2  1 
ATOM   1470 H  HH   . TYR   A 1 68  ? 37.982 -2.269  1.489   1.00 24.03 ?  68  TYR   A HH   1 
ATOM   1471 N  N    . ILE   A 1 69  ? 38.091 4.922   0.764   1.00 12.46 ?  69  ILE   A N    1 
ATOM   1472 C  CA   . ILE   A 1 69  ? 38.229 4.902   -0.690  1.00 12.59 ?  69  ILE   A CA   1 
ATOM   1473 C  C    . ILE   A 1 69  ? 39.557 5.514   -1.124  1.00 12.62 ?  69  ILE   A C    1 
ATOM   1474 O  O    . ILE   A 1 69  ? 40.201 5.027   -2.061  1.00 13.27 ?  69  ILE   A O    1 
ATOM   1475 C  CB   . ILE   A 1 69  ? 37.031 5.607   -1.357  1.00 13.24 ?  69  ILE   A CB   1 
ATOM   1476 C  CG1  . ILE   A 1 69  ? 35.718 4.872   -1.073  1.00 14.00 ?  69  ILE   A CG1  1 
ATOM   1477 C  CG2  . ILE   A 1 69  ? 37.268 5.769   -2.859  1.00 14.60 ?  69  ILE   A CG2  1 
ATOM   1478 C  CD1  . ILE   A 1 69  ? 35.560 3.578   -1.834  1.00 15.07 ?  69  ILE   A CD1  1 
ATOM   1479 H  H    . ILE   A 1 69  ? 37.478 5.451   1.059   1.00 14.91 ?  69  ILE   A H    1 
ATOM   1480 H  HA   . ILE   A 1 69  ? 38.229 3.979   -0.983  1.00 15.07 ?  69  ILE   A HA   1 
ATOM   1481 H  HB   . ILE   A 1 69  ? 36.962 6.491   -0.974  1.00 15.85 ?  69  ILE   A HB   1 
ATOM   1482 H  HG12 . ILE   A 1 69  ? 35.675 4.667   -0.123  1.00 16.76 ?  69  ILE   A HG12 1 
ATOM   1483 H  HG13 . ILE   A 1 69  ? 34.980 5.454   -1.314  1.00 16.76 ?  69  ILE   A HG13 1 
ATOM   1484 H  HG21 . ILE   A 1 69  ? 36.420 5.964   -3.292  1.00 17.48 ?  69  ILE   A HG21 1 
ATOM   1485 H  HG22 . ILE   A 1 69  ? 37.885 6.506   -3.006  1.00 17.48 ?  69  ILE   A HG22 1 
ATOM   1486 H  HG23 . ILE   A 1 69  ? 37.639 4.949   -3.217  1.00 17.48 ?  69  ILE   A HG23 1 
ATOM   1487 H  HD11 . ILE   A 1 69  ? 34.774 3.116   -1.504  1.00 18.05 ?  69  ILE   A HD11 1 
ATOM   1488 H  HD12 . ILE   A 1 69  ? 35.453 3.777   -2.777  1.00 18.05 ?  69  ILE   A HD12 1 
ATOM   1489 H  HD13 . ILE   A 1 69  ? 36.347 3.029   -1.697  1.00 18.05 ?  69  ILE   A HD13 1 
ATOM   1490 N  N    . ALA   A 1 70  ? 39.978 6.592   -0.466  1.00 13.17 ?  70  ALA   A N    1 
ATOM   1491 C  CA   . ALA   A 1 70  ? 41.252 7.210   -0.818  1.00 14.25 ?  70  ALA   A CA   1 
ATOM   1492 C  C    . ALA   A 1 70  ? 42.412 6.239   -0.636  1.00 14.87 ?  70  ALA   A C    1 
ATOM   1493 O  O    . ALA   A 1 70  ? 43.408 6.313   -1.363  1.00 16.64 ?  70  ALA   A O    1 
ATOM   1494 C  CB   . ALA   A 1 70  ? 41.468 8.473   0.021   1.00 14.70 ?  70  ALA   A CB   1 
ATOM   1495 H  H    . ALA   A 1 70  ? 39.553 6.985   0.169   1.00 15.77 ?  70  ALA   A H    1 
ATOM   1496 H  HA   . ALA   A 1 70  ? 41.227 7.483   -1.751  1.00 17.06 ?  70  ALA   A HA   1 
ATOM   1497 H  HB1  . ALA   A 1 70  ? 42.323 8.872   -0.222  1.00 17.60 ?  70  ALA   A HB1  1 
ATOM   1498 H  HB2  . ALA   A 1 70  ? 40.752 9.099   -0.149  1.00 17.60 ?  70  ALA   A HB2  1 
ATOM   1499 H  HB3  . ALA   A 1 70  ? 41.481 8.226   0.961   1.00 17.60 ?  70  ALA   A HB3  1 
ATOM   1500 N  N    . THR   A 1 71  ? 42.301 5.319   0.317   1.00 14.58 ?  71  THR   A N    1 
ATOM   1501 C  CA   . THR   A 1 71  ? 43.351 4.346   0.589   1.00 16.18 ?  71  THR   A CA   1 
ATOM   1502 C  C    . THR   A 1 71  ? 43.243 3.107   -0.286  1.00 15.80 ?  71  THR   A C    1 
ATOM   1503 O  O    . THR   A 1 71  ? 44.263 2.576   -0.744  1.00 17.94 ?  71  THR   A O    1 
ATOM   1504 C  CB   . THR   A 1 71  ? 43.271 3.916   2.055   1.00 18.89 ?  71  THR   A CB   1 
ATOM   1505 O  OG1  . THR   A 1 71  ? 43.525 5.046   2.895   1.00 20.60 ?  71  THR   A OG1  1 
ATOM   1506 C  CG2  . THR   A 1 71  ? 44.270 2.794   2.367   1.00 20.10 ?  71  THR   A CG2  1 
ATOM   1507 H  H    . THR   A 1 71  ? 41.609 5.232   0.817   1.00 17.45 ?  71  THR   A H    1 
ATOM   1508 H  HA   . THR   A 1 71  ? 44.214 4.752   0.431   1.00 19.37 ?  71  THR   A HA   1 
ATOM   1509 H  HB   . THR   A 1 71  ? 42.379 3.579   2.239   1.00 22.63 ?  71  THR   A HB   1 
ATOM   1510 H  HG1  . THR   A 1 71  ? 42.957 5.641   2.750   1.00 24.68 ?  71  THR   A HG1  1 
ATOM   1511 H  HG21 . THR   A 1 71  ? 44.399 2.727   3.327   1.00 24.09 ?  71  THR   A HG21 1 
ATOM   1512 H  HG22 . THR   A 1 71  ? 43.939 1.945   2.036   1.00 24.09 ?  71  THR   A HG22 1 
ATOM   1513 H  HG23 . THR   A 1 71  ? 45.125 2.986   1.950   1.00 24.09 ?  71  THR   A HG23 1 
ATOM   1514 N  N    . ASN   A 1 72  ? 42.022 2.624   -0.515  1.00 14.70 ?  72  ASN   A N    1 
ATOM   1515 C  CA   . ASN   A 1 72  ? 41.803 1.295   -1.066  1.00 14.75 ?  72  ASN   A CA   1 
ATOM   1516 C  C    . ASN   A 1 72  ? 41.193 1.278   -2.454  1.00 15.09 ?  72  ASN   A C    1 
ATOM   1517 O  O    . ASN   A 1 72  ? 41.193 0.219   -3.096  1.00 16.06 ?  72  ASN   A O    1 
ATOM   1518 C  CB   . ASN   A 1 72  ? 40.904 0.484   -0.127  1.00 15.79 ?  72  ASN   A CB   1 
ATOM   1519 C  CG   . ASN   A 1 72  ? 41.516 0.317   1.242   1.00 16.92 ?  72  ASN   A CG   1 
ATOM   1520 O  OD1  . ASN   A 1 72  ? 41.070 0.918   2.216   1.00 18.74 ?  72  ASN   A OD1  1 
ATOM   1521 N  ND2  . ASN   A 1 72  ? 42.560 -0.479  1.319   1.00 17.73 ?  72  ASN   A ND2  1 
ATOM   1522 H  H    . ASN   A 1 72  ? 41.289 3.055   -0.354  1.00 17.60 ?  72  ASN   A H    1 
ATOM   1523 H  HA   . ASN   A 1 72  ? 42.654 0.841   -1.121  1.00 17.66 ?  72  ASN   A HA   1 
ATOM   1524 H  HB2  . ASN   A 1 72  ? 40.052 0.940   -0.029  1.00 18.91 ?  72  ASN   A HB2  1 
ATOM   1525 H  HB3  . ASN   A 1 72  ? 40.764 -0.399  -0.507  1.00 18.91 ?  72  ASN   A HB3  1 
ATOM   1526 H  HD21 . ASN   A 1 72  ? 42.945 -0.604  2.079   1.00 21.24 ?  72  ASN   A HD21 1 
ATOM   1527 H  HD22 . ASN   A 1 72  ? 42.851 -0.876  0.617   1.00 21.24 ?  72  ASN   A HD22 1 
ATOM   1528 N  N    . GLY   A 1 73  ? 40.640 2.388   -2.917  1.00 14.59 ?  73  GLY   A N    1 
ATOM   1529 C  CA   . GLY   A 1 73  ? 39.915 2.392   -4.158  1.00 14.50 ?  73  GLY   A CA   1 
ATOM   1530 C  C    . GLY   A 1 73  ? 38.521 1.821   -3.988  1.00 13.91 ?  73  GLY   A C    1 
ATOM   1531 O  O    . GLY   A 1 73  ? 38.124 1.388   -2.899  1.00 14.18 ?  73  GLY   A O    1 
ATOM   1532 H  H    . GLY   A 1 73  ? 40.672 3.159   -2.526  1.00 17.47 ?  73  GLY   A H    1 
ATOM   1533 H  HA2  . GLY   A 1 73  ? 39.844 3.305   -4.487  1.00 17.36 ?  73  GLY   A HA2  1 
ATOM   1534 H  HA3  . GLY   A 1 73  ? 40.390 1.864   -4.816  1.00 17.36 ?  73  GLY   A HA3  1 
ATOM   1535 N  N    . PRO   A 1 74  ? 37.746 1.832   -5.072  1.00 14.28 ?  74  PRO   A N    1 
ATOM   1536 C  CA   . PRO   A 1 74  ? 36.346 1.405   -4.993  1.00 14.18 ?  74  PRO   A CA   1 
ATOM   1537 C  C    . PRO   A 1 74  ? 36.192 -0.074  -4.670  1.00 13.67 ?  74  PRO   A C    1 
ATOM   1538 O  O    . PRO   A 1 74  ? 37.056 -0.908  -4.961  1.00 14.71 ?  74  PRO   A O    1 
ATOM   1539 C  CB   . PRO   A 1 74  ? 35.808 1.696   -6.401  1.00 16.14 ?  74  PRO   A CB   1 
ATOM   1540 C  CG   . PRO   A 1 74  ? 36.752 2.679   -6.995  1.00 18.71 ?  74  PRO   A CG   1 
ATOM   1541 C  CD   . PRO   A 1 74  ? 38.088 2.350   -6.407  1.00 16.15 ?  74  PRO   A CD   1 
ATOM   1542 H  HA   . PRO   A 1 74  ? 35.859 1.935   -4.342  1.00 16.98 ?  74  PRO   A HA   1 
ATOM   1543 H  HB2  . PRO   A 1 74  ? 35.793 0.874   -6.919  1.00 19.33 ?  74  PRO   A HB2  1 
ATOM   1544 H  HB3  . PRO   A 1 74  ? 34.916 2.073   -6.337  1.00 19.33 ?  74  PRO   A HB3  1 
ATOM   1545 H  HG2  . PRO   A 1 74  ? 36.769 2.572   -7.958  1.00 22.41 ?  74  PRO   A HG2  1 
ATOM   1546 H  HG3  . PRO   A 1 74  ? 36.484 3.575   -6.751  1.00 22.41 ?  74  PRO   A HG3  1 
ATOM   1547 H  HD2  . PRO   A 1 74  ? 38.537 1.665   -6.934  1.00 19.34 ?  74  PRO   A HD2  1 
ATOM   1548 H  HD3  . PRO   A 1 74  ? 38.631 3.152   -6.339  1.00 19.34 ?  74  PRO   A HD3  1 
ATOM   1549 N  N    . LEU   A 1 75  ? 35.046 -0.396  -4.082  1.00 13.01 ?  75  LEU   A N    1 
ATOM   1550 C  CA   . LEU   A 1 75  ? 34.645 -1.785  -3.940  1.00 12.33 ?  75  LEU   A CA   1 
ATOM   1551 C  C    . LEU   A 1 75  ? 34.264 -2.360  -5.302  1.00 12.59 ?  75  LEU   A C    1 
ATOM   1552 O  O    . LEU   A 1 75  ? 34.128 -1.645  -6.299  1.00 14.18 ?  75  LEU   A O    1 
ATOM   1553 C  CB   . LEU   A 1 75  ? 33.454 -1.909  -2.991  1.00 12.58 ?  75  LEU   A CB   1 
ATOM   1554 C  CG   . LEU   A 1 75  ? 33.662 -1.506  -1.533  1.00 14.36 ?  75  LEU   A CG   1 
ATOM   1555 C  CD1  . LEU   A 1 75  ? 32.386 -1.755  -0.742  1.00 16.57 ?  75  LEU   A CD1  1 
ATOM   1556 C  CD2  . LEU   A 1 75  ? 34.813 -2.224  -0.889  1.00 17.42 ?  75  LEU   A CD2  1 
ATOM   1557 H  H    . LEU   A 1 75  ? 34.489 0.169   -3.756  1.00 15.57 ?  75  LEU   A H    1 
ATOM   1558 H  HA   . LEU   A 1 75  ? 35.386 -2.301  -3.587  1.00 14.76 ?  75  LEU   A HA   1 
ATOM   1559 H  HB2  . LEU   A 1 75  ? 32.738 -1.363  -3.338  1.00 15.06 ?  75  LEU   A HB2  1 
ATOM   1560 H  HB3  . LEU   A 1 75  ? 33.175 -2.842  -2.991  1.00 15.06 ?  75  LEU   A HB3  1 
ATOM   1561 H  HG   . LEU   A 1 75  ? 33.860 -0.558  -1.499  1.00 17.19 ?  75  LEU   A HG   1 
ATOM   1562 H  HD11 . LEU   A 1 75  ? 32.533 -1.492  0.180   1.00 19.84 ?  75  LEU   A HD11 1 
ATOM   1563 H  HD12 . LEU   A 1 75  ? 31.674 -1.227  -1.130  1.00 19.84 ?  75  LEU   A HD12 1 
ATOM   1564 H  HD13 . LEU   A 1 75  ? 32.168 -2.698  -0.788  1.00 19.84 ?  75  LEU   A HD13 1 
ATOM   1565 H  HD21 . LEU   A 1 75  ? 34.860 -1.975  0.048   1.00 20.86 ?  75  LEU   A HD21 1 
ATOM   1566 H  HD22 . LEU   A 1 75  ? 34.677 -3.182  -0.968  1.00 20.86 ?  75  LEU   A HD22 1 
ATOM   1567 H  HD23 . LEU   A 1 75  ? 35.641 -1.973  -1.335  1.00 20.86 ?  75  LEU   A HD23 1 
ATOM   1568 N  N    . LYS   A 1 76  ? 34.092 -3.681  -5.326  1.00 13.18 ?  76  LYS   A N    1 
ATOM   1569 C  CA   . LYS   A 1 76  ? 33.494 -4.401  -6.444  1.00 13.69 ?  76  LYS   A CA   1 
ATOM   1570 C  C    . LYS   A 1 76  ? 31.983 -4.483  -6.252  1.00 12.65 ?  76  LYS   A C    1 
ATOM   1571 O  O    . LYS   A 1 76  ? 31.495 -4.591  -5.128  1.00 12.83 ?  76  LYS   A O    1 
ATOM   1572 C  CB   . LYS   A 1 76  ? 34.039 -5.837  -6.501  1.00 15.19 ?  76  LYS   A CB   1 
ATOM   1573 C  CG   . LYS   A 1 76  ? 35.548 -5.934  -6.697  1.00 16.38 ?  76  LYS   A CG   1 
ATOM   1574 C  CD   . LYS   A 1 76  ? 36.068 -7.339  -6.488  1.00 18.12 ?  76  LYS   A CD   1 
ATOM   1575 C  CE   . LYS   A 1 76  ? 37.570 -7.402  -6.681  1.00 20.02 ?  76  LYS   A CE   1 
ATOM   1576 N  NZ   . LYS   A 1 76  ? 38.095 -8.758  -6.442  1.00 20.87 ?  76  LYS   A NZ   1 
ATOM   1577 H  H    . LYS   A 1 76  ? 34.321 -4.201  -4.677  1.00 15.77 ?  76  LYS   A H    1 
ATOM   1578 H  HA   . LYS   A 1 76  ? 33.691 -3.950  -7.280  1.00 16.38 ?  76  LYS   A HA   1 
ATOM   1579 H  HB2  . LYS   A 1 76  ? 33.818 -6.285  -5.670  1.00 18.19 ?  76  LYS   A HB2  1 
ATOM   1580 H  HB3  . LYS   A 1 76  ? 33.615 -6.298  -7.243  1.00 18.19 ?  76  LYS   A HB3  1 
ATOM   1581 H  HG2  . LYS   A 1 76  ? 35.770 -5.659  -7.601  1.00 19.62 ?  76  LYS   A HG2  1 
ATOM   1582 H  HG3  . LYS   A 1 76  ? 35.990 -5.351  -6.057  1.00 19.62 ?  76  LYS   A HG3  1 
ATOM   1583 H  HD2  . LYS   A 1 76  ? 35.863 -7.629  -5.585  1.00 21.71 ?  76  LYS   A HD2  1 
ATOM   1584 H  HD3  . LYS   A 1 76  ? 35.652 -7.935  -7.134  1.00 21.71 ?  76  LYS   A HD3  1 
ATOM   1585 H  HE2  . LYS   A 1 76  ? 37.787 -7.151  -7.592  1.00 23.99 ?  76  LYS   A HE2  1 
ATOM   1586 H  HE3  . LYS   A 1 76  ? 37.998 -6.801  -6.054  1.00 23.99 ?  76  LYS   A HE3  1 
ATOM   1587 H  HZ1  . LYS   A 1 76  ? 38.978 -8.780  -6.562  1.00 25.00 ?  76  LYS   A HZ1  1 
ATOM   1588 H  HZ2  . LYS   A 1 76  ? 37.913 -9.024  -5.610  1.00 25.00 ?  76  LYS   A HZ2  1 
ATOM   1589 H  HZ3  . LYS   A 1 76  ? 37.721 -9.343  -7.010  1.00 25.00 ?  76  LYS   A HZ3  1 
ATOM   1590 N  N    . VAL   A 1 77  ? 31.240 -4.451  -7.361  1.00 13.12 ?  77  VAL   A N    1 
ATOM   1591 C  CA   . VAL   A 1 77  ? 29.833 -4.837  -7.283  1.00 12.86 ?  77  VAL   A CA   1 
ATOM   1592 C  C    . VAL   A 1 77  ? 29.769 -6.291  -6.839  1.00 12.96 ?  77  VAL   A C    1 
ATOM   1593 O  O    . VAL   A 1 77  ? 30.426 -7.165  -7.422  1.00 13.52 ?  77  VAL   A O    1 
ATOM   1594 C  CB   . VAL   A 1 77  ? 29.118 -4.630  -8.626  1.00 13.97 ?  77  VAL   A CB   1 
ATOM   1595 C  CG1  . VAL   A 1 77  ? 27.653 -5.051  -8.520  1.00 14.55 ?  77  VAL   A CG1  1 
ATOM   1596 C  CG2  . VAL   A 1 77  ? 29.220 -3.180  -9.064  1.00 15.43 ?  77  VAL   A CG2  1 
ATOM   1597 H  H    . VAL   A 1 77  ? 31.518 -4.210  -8.139  1.00 15.70 ?  77  VAL   A H    1 
ATOM   1598 H  HA   . VAL   A 1 77  ? 29.387 -4.293  -6.616  1.00 15.40 ?  77  VAL   A HA   1 
ATOM   1599 H  HB   . VAL   A 1 77  ? 29.542 -5.179  -9.305  1.00 16.72 ?  77  VAL   A HB   1 
ATOM   1600 H  HG11 . VAL   A 1 77  ? 27.184 -4.761  -9.316  1.00 17.42 ?  77  VAL   A HG11 1 
ATOM   1601 H  HG12 . VAL   A 1 77  ? 27.606 -6.015  -8.440  1.00 17.42 ?  77  VAL   A HG12 1 
ATOM   1602 H  HG13 . VAL   A 1 77  ? 27.265 -4.632  -7.735  1.00 17.42 ?  77  VAL   A HG13 1 
ATOM   1603 H  HG21 . VAL   A 1 77  ? 28.703 -3.059  -9.875  1.00 18.48 ?  77  VAL   A HG21 1 
ATOM   1604 H  HG22 . VAL   A 1 77  ? 28.869 -2.616  -8.358  1.00 18.48 ?  77  VAL   A HG22 1 
ATOM   1605 H  HG23 . VAL   A 1 77  ? 30.151 -2.966  -9.228  1.00 18.48 ?  77  VAL   A HG23 1 
ATOM   1606 N  N    . GLY   A 1 78  ? 28.985 -6.560  -5.794  1.00 12.51 ?  78  GLY   A N    1 
ATOM   1607 C  CA   . GLY   A 1 78  ? 28.964 -7.851  -5.140  1.00 12.85 ?  78  GLY   A CA   1 
ATOM   1608 C  C    . GLY   A 1 78  ? 29.869 -7.935  -3.930  1.00 12.84 ?  78  GLY   A C    1 
ATOM   1609 O  O    . GLY   A 1 78  ? 29.808 -8.936  -3.199  1.00 13.40 ?  78  GLY   A O    1 
ATOM   1610 H  H    . GLY   A 1 78  ? 28.439 -5.988  -5.449  1.00 14.98 ?  78  GLY   A H    1 
ATOM   1611 H  HA2  . GLY   A 1 78  ? 28.060 -8.046  -4.862  1.00 15.38 ?  78  GLY   A HA2  1 
ATOM   1612 H  HA3  . GLY   A 1 78  ? 29.240 -8.528  -5.781  1.00 15.38 ?  78  GLY   A HA3  1 
ATOM   1613 N  N    . GLY   A 1 79  ? 30.718 -6.923  -3.709  1.00 12.59 ?  79  GLY   A N    1 
ATOM   1614 C  CA   . GLY   A 1 79  ? 31.678 -6.935  -2.632  1.00 12.58 ?  79  GLY   A CA   1 
ATOM   1615 C  C    . GLY   A 1 79  ? 31.217 -6.137  -1.421  1.00 11.71 ?  79  GLY   A C    1 
ATOM   1616 O  O    . GLY   A 1 79  ? 30.097 -5.633  -1.349  1.00 13.03 ?  79  GLY   A O    1 
ATOM   1617 H  H    . GLY   A 1 79  ? 30.750 -6.207  -4.187  1.00 15.07 ?  79  GLY   A H    1 
ATOM   1618 H  HA2  . GLY   A 1 79  ? 31.835 -7.859  -2.357  1.00 15.06 ?  79  GLY   A HA2  1 
ATOM   1619 H  HA3  . GLY   A 1 79  ? 32.516 -6.568  -2.943  1.00 15.06 ?  79  GLY   A HA3  1 
ATOM   1620 N  N    . SER   A 1 80  ? 32.122 -6.041  -0.448  1.00 12.82 ?  80  SER   A N    1 
ATOM   1621 C  CA   . SER   A 1 80  ? 31.798 -5.416  0.823   1.00 12.70 ?  80  SER   A CA   1 
ATOM   1622 C  C    . SER   A 1 80  ? 33.066 -4.967  1.529   1.00 12.40 ?  80  SER   A C    1 
ATOM   1623 O  O    . SER   A 1 80  ? 34.180 -5.394  1.201   1.00 13.61 ?  80  SER   A O    1 
ATOM   1624 C  CB   . SER   A 1 80  ? 31.026 -6.374  1.741   1.00 13.54 ?  80  SER   A CB   1 
ATOM   1625 O  OG   . SER   A 1 80  ? 31.864 -7.414  2.230   1.00 14.91 ?  80  SER   A OG   1 
ATOM   1626 H  H    . SER   A 1 80  ? 32.933 -6.316  -0.506  1.00 15.35 ?  80  SER   A H    1 
ATOM   1627 H  HA   . SER   A 1 80  ? 31.241 -4.639  0.652   1.00 15.20 ?  80  SER   A HA   1 
ATOM   1628 H  HB2  . SER   A 1 80  ? 30.674 -5.875  2.494   1.00 16.21 ?  80  SER   A HB2  1 
ATOM   1629 H  HB3  . SER   A 1 80  ? 30.297 -6.772  1.239   1.00 16.21 ?  80  SER   A HB3  1 
ATOM   1630 H  HG   . SER   A 1 80  ? 32.175 -7.858  1.590   1.00 17.85 ?  80  SER   A HG   1 
ATOM   1631 N  N    . CYS   A 1 81  ? 32.871 -4.116  2.531   1.00 12.30 ?  81  CYS   A N    1 
ATOM   1632 C  CA   . CYS   A 1 81  ? 33.918 -3.821  3.497   1.00 12.30 ?  81  CYS   A CA   1 
ATOM   1633 C  C    . CYS   A 1 81  ? 33.264 -3.582  4.851   1.00 12.11 ?  81  CYS   A C    1 
ATOM   1634 O  O    . CYS   A 1 81  ? 32.097 -3.178  4.935   1.00 13.20 ?  81  CYS   A O    1 
ATOM   1635 C  CB   . CYS   A 1 81  ? 34.789 -2.632  3.077   1.00 13.11 ?  81  CYS   A CB   1 
ATOM   1636 S  SG   . CYS   A 1 81  ? 33.890 -1.059  3.088   1.00 12.79 ?  81  CYS   A SG   1 
ATOM   1637 H  H    . CYS   A 1 81  ? 32.133 -3.697  2.683   1.00 14.72 ?  81  CYS   A H    1 
ATOM   1638 H  HA   . CYS   A 1 81  ? 34.498 -4.592  3.580   1.00 14.72 ?  81  CYS   A HA   1 
ATOM   1639 H  HB2  . CYS   A 1 81  ? 35.540 -2.557  3.689   1.00 15.69 ?  81  CYS   A HB2  1 
ATOM   1640 H  HB3  . CYS   A 1 81  ? 35.116 -2.785  2.175   1.00 15.69 ?  81  CYS   A HB3  1 
ATOM   1641 H  HG   . CYS   A 1 81  ? 34.636 -0.181  2.752   1.00 15.31 ?  81  CYS   A HG   1 
ATOM   1642 N  N    . VAL   A 1 82  ? 34.030 -3.846  5.909   1.00 12.78 ?  82  VAL   A N    1 
ATOM   1643 C  CA   . VAL   A 1 82  ? 33.602 -3.609  7.280   1.00 13.04 ?  82  VAL   A CA   1 
ATOM   1644 C  C    . VAL   A 1 82  ? 34.200 -2.296  7.755   1.00 13.06 ?  82  VAL   A C    1 
ATOM   1645 O  O    . VAL   A 1 82  ? 35.425 -2.122  7.746   1.00 13.75 ?  82  VAL   A O    1 
ATOM   1646 C  CB   . VAL   A 1 82  ? 34.021 -4.757  8.211   1.00 14.46 ?  82  VAL   A CB   1 
ATOM   1647 C  CG1  . VAL   A 1 82  ? 33.587 -4.458  9.634   1.00 15.54 ?  82  VAL   A CG1  1 
ATOM   1648 C  CG2  . VAL   A 1 82  ? 33.442 -6.081  7.739   1.00 15.41 ?  82  VAL   A CG2  1 
ATOM   1649 H  H    . VAL   A 1 82  ? 34.823 -4.189  5.853   1.00 15.30 ?  82  VAL   A H    1 
ATOM   1650 H  HA   . VAL   A 1 82  ? 32.636 -3.532  7.302   1.00 15.61 ?  82  VAL   A HA   1 
ATOM   1651 H  HB   . VAL   A 1 82  ? 34.987 -4.830  8.204   1.00 17.31 ?  82  VAL   A HB   1 
ATOM   1652 H  HG11 . VAL   A 1 82  ? 33.658 -5.268  10.161  1.00 18.61 ?  82  VAL   A HG11 1 
ATOM   1653 H  HG12 . VAL   A 1 82  ? 34.162 -3.770  10.007  1.00 18.61 ?  82  VAL   A HG12 1 
ATOM   1654 H  HG13 . VAL   A 1 82  ? 32.666 -4.150  9.626   1.00 18.61 ?  82  VAL   A HG13 1 
ATOM   1655 H  HG21 . VAL   A 1 82  ? 33.693 -6.777  8.366   1.00 18.46 ?  82  VAL   A HG21 1 
ATOM   1656 H  HG22 . VAL   A 1 82  ? 32.475 -6.006  7.698   1.00 18.46 ?  82  VAL   A HG22 1 
ATOM   1657 H  HG23 . VAL   A 1 82  ? 33.795 -6.285  6.859   1.00 18.46 ?  82  VAL   A HG23 1 
ATOM   1658 N  N    . LEU   A 1 83  ? 33.341 -1.375  8.173   1.00 12.70 ?  83  LEU   A N    1 
ATOM   1659 C  CA   . LEU   A 1 83  ? 33.759 -0.105  8.747   1.00 12.61 ?  83  LEU   A CA   1 
ATOM   1660 C  C    . LEU   A 1 83  ? 33.042 0.080   10.079  1.00 12.61 ?  83  LEU   A C    1 
ATOM   1661 O  O    . LEU   A 1 83  ? 32.307 -0.802  10.540  1.00 13.45 ?  83  LEU   A O    1 
ATOM   1662 C  CB   . LEU   A 1 83  ? 33.503 1.049   7.768   1.00 12.96 ?  83  LEU   A CB   1 
ATOM   1663 C  CG   . LEU   A 1 83  ? 34.411 1.043   6.533   1.00 13.74 ?  83  LEU   A CG   1 
ATOM   1664 C  CD1  . LEU   A 1 83  ? 33.980 2.098   5.530   1.00 14.00 ?  83  LEU   A CD1  1 
ATOM   1665 C  CD2  . LEU   A 1 83  ? 35.884 1.251   6.925   1.00 14.24 ?  83  LEU   A CD2  1 
ATOM   1666 H  H    . LEU   A 1 83  ? 32.488 -1.456  8.118   1.00 15.20 ?  83  LEU   A H    1 
ATOM   1667 H  HA   . LEU   A 1 83  ? 34.712 -0.125  8.922   1.00 15.10 ?  83  LEU   A HA   1 
ATOM   1668 H  HB2  . LEU   A 1 83  ? 32.584 1.002   7.449   1.00 15.51 ?  83  LEU   A HB2  1 
ATOM   1669 H  HB3  . LEU   A 1 83  ? 33.639 1.897   8.222   1.00 15.51 ?  83  LEU   A HB3  1 
ATOM   1670 H  HG   . LEU   A 1 83  ? 34.342 0.179   6.099   1.00 16.46 ?  83  LEU   A HG   1 
ATOM   1671 H  HD11 . LEU   A 1 83  ? 34.572 2.064   4.761   1.00 16.76 ?  83  LEU   A HD11 1 
ATOM   1672 H  HD12 . LEU   A 1 83  ? 33.069 1.916   5.254   1.00 16.76 ?  83  LEU   A HD12 1 
ATOM   1673 H  HD13 . LEU   A 1 83  ? 34.032 2.971   5.948   1.00 16.76 ?  83  LEU   A HD13 1 
ATOM   1674 H  HD21 . LEU   A 1 83  ? 36.406 1.428   6.124   1.00 17.05 ?  83  LEU   A HD21 1 
ATOM   1675 H  HD22 . LEU   A 1 83  ? 35.947 2.011   7.529   1.00 17.05 ?  83  LEU   A HD22 1 
ATOM   1676 H  HD23 . LEU   A 1 83  ? 36.215 0.454   7.364   1.00 17.05 ?  83  LEU   A HD23 1 
ATOM   1677 N  N    . SER   A 1 84  ? 33.250 1.232   10.705  1.00 13.32 ?  84  SER   A N    1 
ATOM   1678 C  CA   . SER   A 1 84  ? 32.600 1.490   11.981  1.00 13.38 ?  84  SER   A CA   1 
ATOM   1679 C  C    . SER   A 1 84  ? 31.083 1.579   11.824  1.00 13.26 ?  84  SER   A C    1 
ATOM   1680 O  O    . SER   A 1 84  ? 30.564 2.019   10.797  1.00 13.35 ?  84  SER   A O    1 
ATOM   1681 C  CB   . SER   A 1 84  ? 33.104 2.806   12.559  1.00 14.74 ?  84  SER   A CB   1 
ATOM   1682 O  OG   . SER   A 1 84  ? 32.459 3.098   13.782  1.00 15.74 ?  84  SER   A OG   1 
ATOM   1683 H  H    . SER   A 1 84  ? 33.747 1.874   10.413  1.00 15.95 ?  84  SER   A H    1 
ATOM   1684 H  HA   . SER   A 1 84  ? 32.808 0.773   12.595  1.00 16.01 ?  84  SER   A HA   1 
ATOM   1685 H  HB2  . SER   A 1 84  ? 34.063 2.740   12.700  1.00 17.66 ?  84  SER   A HB2  1 
ATOM   1686 H  HB3  . SER   A 1 84  ? 32.908 3.522   11.939  1.00 17.66 ?  84  SER   A HB3  1 
ATOM   1687 H  HG   . SER   A 1 84  ? 32.768 3.809   14.107  1.00 18.85 ?  84  SER   A HG   1 
ATOM   1688 N  N    . GLY   A 1 85  ? 30.368 1.165   12.868  1.00 14.23 ?  85  GLY   A N    1 
ATOM   1689 C  CA   . GLY   A 1 85  ? 28.941 1.395   12.948  1.00 14.85 ?  85  GLY   A CA   1 
ATOM   1690 C  C    . GLY   A 1 85  ? 28.559 2.713   13.583  1.00 14.58 ?  85  GLY   A C    1 
ATOM   1691 O  O    . GLY   A 1 85  ? 27.365 3.021   13.675  1.00 15.43 ?  85  GLY   A O    1 
ATOM   1692 H  H    . GLY   A 1 85  ? 30.696 0.741   13.541  1.00 17.04 ?  85  GLY   A H    1 
ATOM   1693 H  HA2  . GLY   A 1 85  ? 28.567 1.368   12.052  1.00 17.78 ?  85  GLY   A HA2  1 
ATOM   1694 H  HA3  . GLY   A 1 85  ? 28.535 0.685   13.464  1.00 17.78 ?  85  GLY   A HA3  1 
ATOM   1695 N  N    . HIS   A 1 86  ? 29.537 3.497   14.028  1.00 14.25 ?  86  HIS   A N    1 
ATOM   1696 C  CA   . HIS   A 1 86  ? 29.305 4.840   14.579  1.00 14.98 ?  86  HIS   A CA   1 
ATOM   1697 C  C    . HIS   A 1 86  ? 28.309 4.722   15.728  1.00 15.82 ?  86  HIS   A C    1 
ATOM   1698 O  O    . HIS   A 1 86  ? 28.490 3.853   16.596  1.00 17.21 ?  86  HIS   A O    1 
ATOM   1699 C  CB   . HIS   A 1 86  ? 28.936 5.808   13.461  1.00 14.84 ?  86  HIS   A CB   1 
ATOM   1700 C  CG   . HIS   A 1 86  ? 30.001 5.908   12.427  1.00 14.89 ?  86  HIS   A CG   1 
ATOM   1701 N  ND1  . HIS   A 1 86  ? 31.082 6.754   12.559  1.00 15.86 ?  86  HIS   A ND1  1 
ATOM   1702 C  CD2  . HIS   A 1 86  ? 30.198 5.216   11.282  1.00 14.68 ?  86  HIS   A CD2  1 
ATOM   1703 C  CE1  . HIS   A 1 86  ? 31.881 6.599   11.519  1.00 15.87 ?  86  HIS   A CE1  1 
ATOM   1704 N  NE2  . HIS   A 1 86  ? 31.376 5.663   10.738  1.00 15.06 ?  86  HIS   A NE2  1 
ATOM   1705 H  H    . HIS   A 1 86  ? 30.366 3.282   14.019  1.00 17.06 ?  86  HIS   A H    1 
ATOM   1706 H  HA   . HIS   A 1 86  ? 30.133 5.161   14.956  1.00 17.93 ?  86  HIS   A HA   1 
ATOM   1707 H  HB2  . HIS   A 1 86  ? 28.119 5.509   13.026  1.00 17.77 ?  86  HIS   A HB2  1 
ATOM   1708 H  HB3  . HIS   A 1 86  ? 28.796 6.698   13.834  1.00 17.77 ?  86  HIS   A HB3  1 
ATOM   1709 H  HD2  . HIS   A 1 86  ? 29.643 4.558   10.927  1.00 17.57 ?  86  HIS   A HD2  1 
ATOM   1710 H  HE1  . HIS   A 1 86  ? 32.669 7.070   11.362  1.00 19.01 ?  86  HIS   A HE1  1 
ATOM   1711 H  HE2  . HIS   A 1 86  ? 31.717 5.397   9.990   1.00 18.04 ?  86  HIS   A HE2  1 
ATOM   1712 N  N    . ASN   A 1 87  ? 27.282 5.564   15.783  1.00 16.55 ?  87  ASN   A N    1 
ATOM   1713 C  CA   . ASN   A 1 87  ? 26.283 5.541   16.839  1.00 17.66 ?  87  ASN   A CA   1 
ATOM   1714 C  C    . ASN   A 1 87  ? 25.164 4.545   16.577  1.00 18.56 ?  87  ASN   A C    1 
ATOM   1715 O  O    . ASN   A 1 87  ? 24.220 4.489   17.369  1.00 20.87 ?  87  ASN   A O    1 
ATOM   1716 C  CB   . ASN   A 1 87  ? 25.678 6.942   17.008  1.00 18.46 ?  87  ASN   A CB   1 
ATOM   1717 C  CG   . ASN   A 1 87  ? 25.174 7.527   15.694  1.00 18.87 ?  87  ASN   A CG   1 
ATOM   1718 O  OD1  . ASN   A 1 87  ? 25.803 7.380   14.650  1.00 19.37 ?  87  ASN   A OD1  1 
ATOM   1719 N  ND2  . ASN   A 1 87  ? 24.036 8.196   15.747  1.00 20.09 ?  87  ASN   A ND2  1 
ATOM   1720 H  H    . ASN   A 1 87  ? 27.137 6.176   15.202  1.00 19.83 ?  87  ASN   A H    1 
ATOM   1721 H  HA   . ASN   A 1 87  ? 26.707 5.293   17.679  1.00 21.15 ?  87  ASN   A HA   1 
ATOM   1722 H  HB2  . ASN   A 1 87  ? 24.925 6.887   17.624  1.00 22.11 ?  87  ASN   A HB2  1 
ATOM   1723 H  HB3  . ASN   A 1 87  ? 26.354 7.534   17.366  1.00 22.11 ?  87  ASN   A HB3  1 
ATOM   1724 H  HD21 . ASN   A 1 87  ? 23.712 8.544   15.032  1.00 24.07 ?  87  ASN   A HD21 1 
ATOM   1725 H  HD22 . ASN   A 1 87  ? 23.626 8.289   16.497  1.00 24.07 ?  87  ASN   A HD22 1 
ATOM   1726 N  N    . LEU   A 1 88  ? 25.241 3.758   15.508  1.00 17.47 ?  88  LEU   A N    1 
ATOM   1727 C  CA   . LEU   A 1 88  ? 24.135 2.897   15.107  1.00 17.15 ?  88  LEU   A CA   1 
ATOM   1728 C  C    . LEU   A 1 88  ? 24.355 1.422   15.403  1.00 16.88 ?  88  LEU   A C    1 
ATOM   1729 O  O    . LEU   A 1 88  ? 23.381 0.689   15.566  1.00 17.69 ?  88  LEU   A O    1 
ATOM   1730 C  CB   . LEU   A 1 88  ? 23.881 3.054   13.607  1.00 17.57 ?  88  LEU   A CB   1 
ATOM   1731 C  CG   . LEU   A 1 88  ? 23.607 4.482   13.130  1.00 18.95 ?  88  LEU   A CG   1 
ATOM   1732 C  CD1  . LEU   A 1 88  ? 23.445 4.520   11.620  1.00 19.44 ?  88  LEU   A CD1  1 
ATOM   1733 C  CD2  . LEU   A 1 88  ? 22.376 5.062   13.811  1.00 20.32 ?  88  LEU   A CD2  1 
ATOM   1734 H  H    . LEU   A 1 88  ? 25.938 3.695   15.004  1.00 20.93 ?  88  LEU   A H    1 
ATOM   1735 H  HA   . LEU   A 1 88  ? 23.336 3.181   15.576  1.00 20.54 ?  88  LEU   A HA   1 
ATOM   1736 H  HB2  . LEU   A 1 88  ? 24.656 2.734   13.128  1.00 21.04 ?  88  LEU   A HB2  1 
ATOM   1737 H  HB3  . LEU   A 1 88  ? 23.106 2.522   13.373  1.00 21.04 ?  88  LEU   A HB3  1 
ATOM   1738 H  HG   . LEU   A 1 88  ? 24.365 5.043   13.356  1.00 22.70 ?  88  LEU   A HG   1 
ATOM   1739 H  HD11 . LEU   A 1 88  ? 23.304 5.439   11.338  1.00 23.29 ?  88  LEU   A HD11 1 
ATOM   1740 H  HD12 . LEU   A 1 88  ? 24.246 4.166   11.205  1.00 23.29 ?  88  LEU   A HD12 1 
ATOM   1741 H  HD13 . LEU   A 1 88  ? 22.677 3.980   11.371  1.00 23.29 ?  88  LEU   A HD13 1 
ATOM   1742 H  HD21 . LEU   A 1 88  ? 22.167 5.917   13.402  1.00 24.35 ?  88  LEU   A HD21 1 
ATOM   1743 H  HD22 . LEU   A 1 88  ? 21.638 4.448   13.695  1.00 24.35 ?  88  LEU   A HD22 1 
ATOM   1744 H  HD23 . LEU   A 1 88  ? 22.570 5.182   14.752  1.00 24.35 ?  88  LEU   A HD23 1 
ATOM   1745 N  N    . ALA   A 1 89  ? 25.605 0.980   15.466  1.00 16.26 ?  89  ALA   A N    1 
ATOM   1746 C  CA   . ALA   A 1 89  ? 25.956 -0.428  15.573  1.00 15.92 ?  89  ALA   A CA   1 
ATOM   1747 C  C    . ALA   A 1 89  ? 27.434 -0.482  15.920  1.00 16.36 ?  89  ALA   A C    1 
ATOM   1748 O  O    . ALA   A 1 89  ? 28.144 0.521   15.823  1.00 17.15 ?  89  ALA   A O    1 
ATOM   1749 C  CB   . ALA   A 1 89  ? 25.713 -1.145  14.247  1.00 15.82 ?  89  ALA   A CB   1 
ATOM   1750 H  H    . ALA   A 1 89  ? 26.288 1.501   15.441  1.00 19.48 ?  89  ALA   A H    1 
ATOM   1751 H  HA   . ALA   A 1 89  ? 25.437 -0.850  16.274  1.00 19.06 ?  89  ALA   A HA   1 
ATOM   1752 H  HB1  . ALA   A 1 89  ? 25.965 -2.077  14.342  1.00 18.95 ?  89  ALA   A HB1  1 
ATOM   1753 H  HB2  . ALA   A 1 89  ? 24.772 -1.080  14.015  1.00 18.95 ?  89  ALA   A HB2  1 
ATOM   1754 H  HB3  . ALA   A 1 89  ? 26.251 -0.727  13.556  1.00 18.95 ?  89  ALA   A HB3  1 
ATOM   1755 N  N    . LYS   A 1 90  ? 27.909 -1.658  16.319  1.00 17.19 ?  90  LYS   A N    1 
ATOM   1756 C  CA   . LYS   A 1 90  ? 29.350 -1.808  16.484  1.00 18.30 ?  90  LYS   A CA   1 
ATOM   1757 C  C    . LYS   A 1 90  ? 30.065 -1.635  15.147  1.00 16.64 ?  90  LYS   A C    1 
ATOM   1758 O  O    . LYS   A 1 90  ? 31.003 -0.830  15.021  1.00 17.82 ?  90  LYS   A O    1 
ATOM   1759 C  CB   . LYS   A 1 90  ? 29.677 -3.161  17.114  1.00 22.33 ?  90  LYS   A CB   1 
ATOM   1760 C  CG   . LYS   A 1 90  ? 31.158 -3.332  17.429  1.00 28.32 ?  90  LYS   A CG   1 
ATOM   1761 C  CD   . LYS   A 1 90  ? 31.397 -4.523  18.345  1.00 34.52 ?  90  LYS   A CD   1 
ATOM   1762 C  CE   . LYS   A 1 90  ? 32.807 -4.520  18.924  1.00 39.18 ?  90  LYS   A CE   1 
ATOM   1763 N  NZ   . LYS   A 1 90  ? 33.835 -4.965  17.944  1.00 42.10 ?  90  LYS   A NZ   1 
ATOM   1764 H  H    . LYS   A 1 90  ? 27.434 -2.349  16.498  1.00 20.59 ?  90  LYS   A H    1 
ATOM   1765 H  HA   . LYS   A 1 90  ? 29.670 -1.114  17.078  1.00 21.92 ?  90  LYS   A HA   1 
ATOM   1766 H  HB2  . LYS   A 1 90  ? 29.180 -3.247  17.947  1.00 26.76 ?  90  LYS   A HB2  1 
ATOM   1767 H  HB3  . LYS   A 1 90  ? 29.414 -3.867  16.504  1.00 26.76 ?  90  LYS   A HB3  1 
ATOM   1768 H  HG2  . LYS   A 1 90  ? 31.645 -3.477  16.603  1.00 33.94 ?  90  LYS   A HG2  1 
ATOM   1769 H  HG3  . LYS   A 1 90  ? 31.483 -2.534  17.874  1.00 33.94 ?  90  LYS   A HG3  1 
ATOM   1770 H  HD2  . LYS   A 1 90  ? 30.767 -4.491  19.082  1.00 41.39 ?  90  LYS   A HD2  1 
ATOM   1771 H  HD3  . LYS   A 1 90  ? 31.279 -5.343  17.840  1.00 41.39 ?  90  LYS   A HD3  1 
ATOM   1772 H  HE2  . LYS   A 1 90  ? 33.032 -3.618  19.204  1.00 46.97 ?  90  LYS   A HE2  1 
ATOM   1773 H  HE3  . LYS   A 1 90  ? 32.837 -5.120  19.685  1.00 46.97 ?  90  LYS   A HE3  1 
ATOM   1774 H  HZ1  . LYS   A 1 90  ? 33.655 -5.793  17.670  1.00 50.48 ?  90  LYS   A HZ1  1 
ATOM   1775 H  HZ2  . LYS   A 1 90  ? 33.841 -4.422  17.240  1.00 50.48 ?  90  LYS   A HZ2  1 
ATOM   1776 H  HZ3  . LYS   A 1 90  ? 34.641 -4.956  18.323  1.00 50.48 ?  90  LYS   A HZ3  1 
ATOM   1777 N  N    . HIS   A 1 91  ? 29.599 -2.355  14.126  1.00 14.30 ?  91  HIS   A N    1 
ATOM   1778 C  CA   . HIS   A 1 91  ? 30.184 -2.345  12.799  1.00 13.82 ?  91  HIS   A CA   1 
ATOM   1779 C  C    . HIS   A 1 91  ? 29.109 -2.067  11.766  1.00 12.65 ?  91  HIS   A C    1 
ATOM   1780 O  O    . HIS   A 1 91  ? 27.941 -2.428  11.947  1.00 13.95 ?  91  HIS   A O    1 
ATOM   1781 C  CB   . HIS   A 1 91  ? 30.789 -3.709  12.447  1.00 16.32 ?  91  HIS   A CB   1 
ATOM   1782 C  CG   . HIS   A 1 91  ? 31.786 -4.207  13.442  1.00 20.17 ?  91  HIS   A CG   1 
ATOM   1783 N  ND1  . HIS   A 1 91  ? 33.068 -3.709  13.523  1.00 22.12 ?  91  HIS   A ND1  1 
ATOM   1784 C  CD2  . HIS   A 1 91  ? 31.697 -5.171  14.389  1.00 22.05 ?  91  HIS   A CD2  1 
ATOM   1785 C  CE1  . HIS   A 1 91  ? 33.724 -4.339  14.482  1.00 23.07 ?  91  HIS   A CE1  1 
ATOM   1786 N  NE2  . HIS   A 1 91  ? 32.914 -5.232  15.023  1.00 23.21 ?  91  HIS   A NE2  1 
ATOM   1787 H  H    . HIS   A 1 91  ? 28.907 -2.884  14.188  1.00 17.12 ?  91  HIS   A H    1 
ATOM   1788 H  HA   . HIS   A 1 91  ? 30.870 -1.673  12.741  1.00 16.55 ?  91  HIS   A HA   1 
ATOM   1789 H  HB2  . HIS   A 1 91  ? 30.078 -4.369  12.392  1.00 19.55 ?  91  HIS   A HB2  1 
ATOM   1790 H  HB3  . HIS   A 1 91  ? 31.237 -3.641  11.589  1.00 19.55 ?  91  HIS   A HB3  1 
ATOM   1791 H  HD1  . HIS   A 1 91  ? 33.392 -3.085  13.023  1.00 26.51 ?  91  HIS   A HD1  1 
ATOM   1792 H  HD2  . HIS   A 1 91  ? 30.956 -5.692  14.581  1.00 26.42 ?  91  HIS   A HD2  1 
ATOM   1793 H  HE1  . HIS   A 1 91  ? 34.610 -4.176  14.729  1.00 27.65 ?  91  HIS   A HE1  1 
ATOM   1794 N  N    . CYS   A 1 92  ? 29.525 -1.463  10.660  1.00 12.48 ?  92  CYS   A N    1 
ATOM   1795 C  CA   . CYS   A 1 92  ? 28.705 -1.395  9.460   1.00 12.27 ?  92  CYS   A CA   1 
ATOM   1796 C  C    . CYS   A 1 92  ? 29.358 -2.220  8.361   1.00 11.76 ?  92  CYS   A C    1 
ATOM   1797 O  O    . CYS   A 1 92  ? 30.514 -1.970  7.991   1.00 12.82 ?  92  CYS   A O    1 
ATOM   1798 C  CB   . CYS   A 1 92  ? 28.499 0.044   8.993   1.00 12.88 ?  92  CYS   A CB   1 
ATOM   1799 S  SG   . CYS   A 1 92  ? 27.484 0.159   7.481   1.00 12.03 ?  92  CYS   A SG   1 
ATOM   1800 H  H    . CYS   A 1 92  ? 30.294 -1.080  10.583  1.00 14.93 ?  92  CYS   A H    1 
ATOM   1801 H  HA   . CYS   A 1 92  ? 27.836 -1.777  9.649   1.00 14.69 ?  92  CYS   A HA   1 
ATOM   1802 H  HB2  . CYS   A 1 92  ? 28.049 0.544   9.696   1.00 15.42 ?  92  CYS   A HB2  1 
ATOM   1803 H  HB3  . CYS   A 1 92  ? 29.361 0.444   8.805   1.00 15.42 ?  92  CYS   A HB3  1 
ATOM   1804 H  HG   . CYS   A 1 92  ? 27.351 1.319   7.191   1.00 14.40 ?  92  CYS   A HG   1 
ATOM   1805 N  N    . LEU   A 1 93  ? 28.619 -3.202  7.859   1.00 11.78 ?  93  LEU   A N    1 
ATOM   1806 C  CA   . LEU   A 1 93  ? 29.023 -3.960  6.683   1.00 11.41 ?  93  LEU   A CA   1 
ATOM   1807 C  C    . LEU   A 1 93  ? 28.437 -3.268  5.456   1.00 11.08 ?  93  LEU   A C    1 
ATOM   1808 O  O    . LEU   A 1 93  ? 27.225 -3.328  5.220   1.00 11.40 ?  93  LEU   A O    1 
ATOM   1809 C  CB   . LEU   A 1 93  ? 28.542 -5.404  6.799   1.00 12.21 ?  93  LEU   A CB   1 
ATOM   1810 C  CG   . LEU   A 1 93  ? 28.937 -6.302  5.630   1.00 12.31 ?  93  LEU   A CG   1 
ATOM   1811 C  CD1  . LEU   A 1 93  ? 30.441 -6.568  5.619   1.00 13.18 ?  93  LEU   A CD1  1 
ATOM   1812 C  CD2  . LEU   A 1 93  ? 28.161 -7.614  5.697   1.00 13.41 ?  93  LEU   A CD2  1 
ATOM   1813 H  H    . LEU   A 1 93  ? 27.865 -3.450  8.194   1.00 14.10 ?  93  LEU   A H    1 
ATOM   1814 H  HA   . LEU   A 1 93  ? 29.990 -3.953  6.617   1.00 13.65 ?  93  LEU   A HA   1 
ATOM   1815 H  HB2  . LEU   A 1 93  ? 28.921 -5.787  7.609   1.00 14.61 ?  93  LEU   A HB2  1 
ATOM   1816 H  HB3  . LEU   A 1 93  ? 27.577 -5.401  6.864   1.00 14.61 ?  93  LEU   A HB3  1 
ATOM   1817 H  HG   . LEU   A 1 93  ? 28.703 -5.861  4.803   1.00 14.74 ?  93  LEU   A HG   1 
ATOM   1818 H  HD11 . LEU   A 1 93  ? 30.647 -7.181  4.898   1.00 15.77 ?  93  LEU   A HD11 1 
ATOM   1819 H  HD12 . LEU   A 1 93  ? 30.912 -5.732  5.491   1.00 15.77 ?  93  LEU   A HD12 1 
ATOM   1820 H  HD13 . LEU   A 1 93  ? 30.699 -6.965  6.471   1.00 15.77 ?  93  LEU   A HD13 1 
ATOM   1821 H  HD21 . LEU   A 1 93  ? 28.423 -8.172  4.951   1.00 16.05 ?  93  LEU   A HD21 1 
ATOM   1822 H  HD22 . LEU   A 1 93  ? 28.365 -8.060  6.535   1.00 16.05 ?  93  LEU   A HD22 1 
ATOM   1823 H  HD23 . LEU   A 1 93  ? 27.209 -7.422  5.650   1.00 16.05 ?  93  LEU   A HD23 1 
ATOM   1824 N  N    . HIS   A 1 94  ? 29.291 -2.573  4.699   1.00 11.09 ?  94  HIS   A N    1 
ATOM   1825 C  CA   . HIS   A 1 94  ? 28.876 -1.905  3.466   1.00 11.36 ?  94  HIS   A CA   1 
ATOM   1826 C  C    . HIS   A 1 94  ? 28.890 -2.940  2.354   1.00 11.08 ?  94  HIS   A C    1 
ATOM   1827 O  O    . HIS   A 1 94  ? 29.956 -3.454  2.008   1.00 12.59 ?  94  HIS   A O    1 
ATOM   1828 C  CB   . HIS   A 1 94  ? 29.833 -0.762  3.134   1.00 11.24 ?  94  HIS   A CB   1 
ATOM   1829 C  CG   . HIS   A 1 94  ? 29.819 0.337   4.145   1.00 11.26 ?  94  HIS   A CG   1 
ATOM   1830 N  ND1  . HIS   A 1 94  ? 28.933 1.395   4.093   1.00 11.33 ?  94  HIS   A ND1  1 
ATOM   1831 C  CD2  . HIS   A 1 94  ? 30.559 0.511   5.263   1.00 12.23 ?  94  HIS   A CD2  1 
ATOM   1832 C  CE1  . HIS   A 1 94  ? 29.145 2.178   5.134   1.00 11.52 ?  94  HIS   A CE1  1 
ATOM   1833 N  NE2  . HIS   A 1 94  ? 30.132 1.671   5.853   1.00 11.78 ?  94  HIS   A NE2  1 
ATOM   1834 H  H    . HIS   A 1 94  ? 30.123 -2.470  4.883   1.00 13.27 ?  94  HIS   A H    1 
ATOM   1835 H  HA   . HIS   A 1 94  ? 27.971 -1.552  3.563   1.00 13.60 ?  94  HIS   A HA   1 
ATOM   1836 H  HB2  . HIS   A 1 94  ? 30.728 -1.110  3.086   1.00 13.45 ?  94  HIS   A HB2  1 
ATOM   1837 H  HB3  . HIS   A 1 94  ? 29.571 -0.379  2.280   1.00 13.45 ?  94  HIS   A HB3  1 
ATOM   1838 H  HD2  . HIS   A 1 94  ? 31.242 -0.036  5.564   1.00 14.64 ?  94  HIS   A HD2  1 
ATOM   1839 H  HE1  . HIS   A 1 94  ? 28.676 2.965   5.318   1.00 13.79 ?  94  HIS   A HE1  1 
ATOM   1840 H  HE2  . HIS   A 1 94  ? 30.444 2.021   6.572   1.00 14.09 ?  94  HIS   A HE2  1 
ATOM   1841 N  N    . VAL   A 1 95  ? 27.722 -3.265  1.803   1.00 10.47 ?  95  VAL   A N    1 
ATOM   1842 C  CA   . VAL   A 1 95  ? 27.587 -4.307  0.788   1.00 10.66 ?  95  VAL   A CA   1 
ATOM   1843 C  C    . VAL   A 1 95  ? 27.038 -3.674  -0.479  1.00 10.69 ?  95  VAL   A C    1 
ATOM   1844 O  O    . VAL   A 1 95  ? 26.039 -2.949  -0.425  1.00 11.63 ?  95  VAL   A O    1 
ATOM   1845 C  CB   . VAL   A 1 95  ? 26.652 -5.441  1.245   1.00 11.62 ?  95  VAL   A CB   1 
ATOM   1846 C  CG1  . VAL   A 1 95  ? 26.557 -6.487  0.145   1.00 12.43 ?  95  VAL   A CG1  1 
ATOM   1847 C  CG2  . VAL   A 1 95  ? 27.148 -6.049  2.540   1.00 11.69 ?  95  VAL   A CG2  1 
ATOM   1848 H  H    . VAL   A 1 95  ? 26.972 -2.899  2.017   1.00 12.53 ?  95  VAL   A H    1 
ATOM   1849 H  HA   . VAL   A 1 95  ? 28.453 -4.685  0.591   1.00 12.75 ?  95  VAL   A HA   1 
ATOM   1850 H  HB   . VAL   A 1 95  ? 25.764 -5.086  1.400   1.00 13.91 ?  95  VAL   A HB   1 
ATOM   1851 H  HG11 . VAL   A 1 95  ? 26.179 -7.303  0.512   1.00 14.88 ?  95  VAL   A HG11 1 
ATOM   1852 H  HG12 . VAL   A 1 95  ? 25.986 -6.155  -0.567  1.00 14.88 ?  95  VAL   A HG12 1 
ATOM   1853 H  HG13 . VAL   A 1 95  ? 27.446 -6.667  -0.202  1.00 14.88 ?  95  VAL   A HG13 1 
ATOM   1854 H  HG21 . VAL   A 1 95  ? 26.591 -6.813  2.766   1.00 13.99 ?  95  VAL   A HG21 1 
ATOM   1855 H  HG22 . VAL   A 1 95  ? 28.067 -6.335  2.426   1.00 13.99 ?  95  VAL   A HG22 1 
ATOM   1856 H  HG23 . VAL   A 1 95  ? 27.092 -5.384  3.244   1.00 13.99 ?  95  VAL   A HG23 1 
ATOM   1857 N  N    A VAL   A 1 96  ? 27.677 -3.964  -1.613  0.70 10.39 ?  96  VAL   A N    1 
ATOM   1858 N  N    B VAL   A 1 96  ? 27.667 -3.957  -1.615  0.30 10.35 ?  96  VAL   A N    1 
ATOM   1859 C  CA   A VAL   A 1 96  ? 27.283 -3.425  -2.909  0.70 11.35 ?  96  VAL   A CA   1 
ATOM   1860 C  CA   B VAL   A 1 96  ? 27.253 -3.384  -2.891  0.30 10.72 ?  96  VAL   A CA   1 
ATOM   1861 C  C    A VAL   A 1 96  ? 26.472 -4.483  -3.647  0.70 12.07 ?  96  VAL   A C    1 
ATOM   1862 C  C    B VAL   A 1 96  ? 26.480 -4.438  -3.675  0.30 11.24 ?  96  VAL   A C    1 
ATOM   1863 O  O    A VAL   A 1 96  ? 27.024 -5.447  -4.184  0.70 13.08 ?  96  VAL   A O    1 
ATOM   1864 O  O    B VAL   A 1 96  ? 27.065 -5.348  -4.270  0.30 11.64 ?  96  VAL   A O    1 
ATOM   1865 C  CB   A VAL   A 1 96  ? 28.491 -2.985  -3.735  0.70 11.45 ?  96  VAL   A CB   1 
ATOM   1866 C  CB   B VAL   A 1 96  ? 28.437 -2.835  -3.687  0.30 10.57 ?  96  VAL   A CB   1 
ATOM   1867 C  CG1  A VAL   A 1 96  ? 28.003 -2.332  -5.013  0.70 11.97 ?  96  VAL   A CG1  1 
ATOM   1868 C  CG1  B VAL   A 1 96  ? 27.941 -2.253  -4.996  0.30 10.70 ?  96  VAL   A CG1  1 
ATOM   1869 C  CG2  A VAL   A 1 96  ? 29.387 -2.042  -2.940  0.70 11.58 ?  96  VAL   A CG2  1 
ATOM   1870 C  CG2  B VAL   A 1 96  ? 29.167 -1.776  -2.880  0.30 10.39 ?  96  VAL   A CG2  1 
ATOM   1871 H  H    A VAL   A 1 96  ? 28.363 -4.490  -1.653  0.70 12.43 ?  96  VAL   A H    1 
ATOM   1872 H  H    B VAL   A 1 96  ? 28.351 -4.483  -1.670  0.30 12.38 ?  96  VAL   A H    1 
ATOM   1873 H  HA   A VAL   A 1 96  ? 26.718 -2.654  -2.769  0.70 13.58 ?  96  VAL   A HA   1 
ATOM   1874 H  HA   B VAL   A 1 96  ? 26.651 -2.649  -2.718  0.30 12.83 ?  96  VAL   A HA   1 
ATOM   1875 H  HB   A VAL   A 1 96  ? 29.014 -3.764  -3.979  0.70 13.71 ?  96  VAL   A HB   1 
ATOM   1876 H  HB   B VAL   A 1 96  ? 29.059 -3.553  -3.885  0.30 12.64 ?  96  VAL   A HB   1 
ATOM   1877 H  HG11 A VAL   A 1 96  ? 28.753 -1.893  -5.449  0.70 14.33 ?  96  VAL   A HG11 1 
ATOM   1878 H  HG11 B VAL   A 1 96  ? 28.654 -1.732  -5.396  0.30 12.80 ?  96  VAL   A HG11 1 
ATOM   1879 H  HG12 A VAL   A 1 96  ? 27.632 -3.007  -5.599  0.70 14.33 ?  96  VAL   A HG12 1 
ATOM   1880 H  HG12 B VAL   A 1 96  ? 27.686 -2.975  -5.591  0.30 12.80 ?  96  VAL   A HG12 1 
ATOM   1881 H  HG13 A VAL   A 1 96  ? 27.324 -1.672  -4.793  0.70 14.33 ?  96  VAL   A HG13 1 
ATOM   1882 H  HG13 B VAL   A 1 96  ? 27.177 -1.681  -4.818  0.30 12.80 ?  96  VAL   A HG13 1 
ATOM   1883 H  HG21 A VAL   A 1 96  ? 30.093 -1.717  -3.517  0.70 13.86 ?  96  VAL   A HG21 1 
ATOM   1884 H  HG21 B VAL   A 1 96  ? 29.878 -1.402  -3.421  0.30 12.43 ?  96  VAL   A HG21 1 
ATOM   1885 H  HG22 A VAL   A 1 96  ? 28.853 -1.302  -2.614  0.70 13.86 ?  96  VAL   A HG22 1 
ATOM   1886 H  HG22 B VAL   A 1 96  ? 28.536 -1.080  -2.634  0.30 12.43 ?  96  VAL   A HG22 1 
ATOM   1887 H  HG23 A VAL   A 1 96  ? 29.768 -2.530  -2.191  0.70 13.86 ?  96  VAL   A HG23 1 
ATOM   1888 H  HG23 B VAL   A 1 96  ? 29.535 -2.185  -2.082  0.30 12.43 ?  96  VAL   A HG23 1 
ATOM   1889 N  N    . GLY   A 1 97  ? 25.156 -4.308  -3.691  1.00 11.65 ?  97  GLY   A N    1 
ATOM   1890 C  CA   . GLY   A 1 97  ? 24.329 -5.079  -4.582  1.00 12.03 ?  97  GLY   A CA   1 
ATOM   1891 C  C    . GLY   A 1 97  ? 24.350 -4.441  -5.958  1.00 12.36 ?  97  GLY   A C    1 
ATOM   1892 O  O    . GLY   A 1 97  ? 24.645 -3.246  -6.101  1.00 13.02 ?  97  GLY   A O    1 
ATOM   1893 H  H    A GLY   A 1 97  ? 24.722 -3.741  -3.206  0.70 13.94 ?  97  GLY   A H    1 
ATOM   1894 H  H    B GLY   A 1 97  ? 24.716 -3.759  -3.191  0.30 13.94 ?  97  GLY   A H    1 
ATOM   1895 H  HA2  . GLY   A 1 97  ? 24.670 -5.987  -4.636  1.00 14.39 ?  97  GLY   A HA2  1 
ATOM   1896 H  HA3  . GLY   A 1 97  ? 23.417 -5.104  -4.251  1.00 14.39 ?  97  GLY   A HA3  1 
ATOM   1897 N  N    . PRO   A 1 98  ? 24.034 -5.212  -6.996  1.00 12.78 ?  98  PRO   A N    1 
ATOM   1898 C  CA   . PRO   A 1 98  ? 23.963 -4.632  -8.338  1.00 14.13 ?  98  PRO   A CA   1 
ATOM   1899 C  C    . PRO   A 1 98  ? 22.852 -3.598  -8.439  1.00 14.74 ?  98  PRO   A C    1 
ATOM   1900 O  O    . PRO   A 1 98  ? 21.761 -3.757  -7.878  1.00 14.44 ?  98  PRO   A O    1 
ATOM   1901 C  CB   . PRO   A 1 98  ? 23.682 -5.845  -9.237  1.00 14.61 ?  98  PRO   A CB   1 
ATOM   1902 C  CG   . PRO   A 1 98  ? 23.038 -6.850  -8.330  1.00 14.50 ?  98  PRO   A CG   1 
ATOM   1903 C  CD   . PRO   A 1 98  ? 23.742 -6.657  -7.006  1.00 13.19 ?  98  PRO   A CD   1 
ATOM   1904 H  HA   . PRO   A 1 98  ? 24.816 -4.239  -8.584  1.00 16.91 ?  98  PRO   A HA   1 
ATOM   1905 H  HB2  . PRO   A 1 98  ? 23.073 -5.590  -9.946  1.00 17.49 ?  98  PRO   A HB2  1 
ATOM   1906 H  HB3  . PRO   A 1 98  ? 24.511 -6.191  -9.599  1.00 17.49 ?  98  PRO   A HB3  1 
ATOM   1907 H  HG2  . PRO   A 1 98  ? 22.093 -6.663  -8.246  1.00 17.36 ?  98  PRO   A HG2  1 
ATOM   1908 H  HG3  . PRO   A 1 98  ? 23.188 -7.746  -8.673  1.00 17.36 ?  98  PRO   A HG3  1 
ATOM   1909 H  HD2  . PRO   A 1 98  ? 23.157 -6.900  -6.268  1.00 15.79 ?  98  PRO   A HD2  1 
ATOM   1910 H  HD3  . PRO   A 1 98  ? 24.566 -7.177  -6.980  1.00 15.79 ?  98  PRO   A HD3  1 
ATOM   1911 N  N    A ASN   A 1 99  ? 23.135 -2.492  -9.131  0.70 15.60 ?  99  ASN   A N    1 
ATOM   1912 N  N    B ASN   A 1 99  ? 23.156 -2.561  -9.198  0.30 14.78 ?  99  ASN   A N    1 
ATOM   1913 C  CA   A ASN   A 1 99  ? 22.158 -1.417  -9.324  0.70 16.69 ?  99  ASN   A CA   1 
ATOM   1914 C  CA   B ASN   A 1 99  ? 22.203 -1.552  -9.617  0.30 15.10 ?  99  ASN   A CA   1 
ATOM   1915 C  C    A ASN   A 1 99  ? 21.546 -1.556  -10.712 0.70 17.67 ?  99  ASN   A C    1 
ATOM   1916 C  C    B ASN   A 1 99  ? 21.734 -1.936  -11.016 0.30 15.15 ?  99  ASN   A C    1 
ATOM   1917 O  O    A ASN   A 1 99  ? 22.190 -1.244  -11.720 0.70 18.55 ?  99  ASN   A O    1 
ATOM   1918 O  O    B ASN   A 1 99  ? 22.497 -1.840  -11.984 0.30 14.51 ?  99  ASN   A O    1 
ATOM   1919 C  CB   A ASN   A 1 99  ? 22.784 -0.032  -9.148  0.70 17.12 ?  99  ASN   A CB   1 
ATOM   1920 C  CB   B ASN   A 1 99  ? 22.904 -0.199  -9.632  0.30 15.72 ?  99  ASN   A CB   1 
ATOM   1921 C  CG   A ASN   A 1 99  ? 21.736 1.102   -9.096  0.70 17.63 ?  99  ASN   A CG   1 
ATOM   1922 C  CG   B ASN   A 1 99  ? 21.962 0.940   -9.912  0.30 15.92 ?  99  ASN   A CG   1 
ATOM   1923 O  OD1  A ASN   A 1 99  ? 20.716 1.058   -9.781  0.70 18.05 ?  99  ASN   A OD1  1 
ATOM   1924 O  OD1  B ASN   A 1 99  ? 20.951 0.772   -10.590 0.30 16.09 ?  99  ASN   A OD1  1 
ATOM   1925 N  ND2  A ASN   A 1 99  ? 22.004 2.120   -8.282  0.70 17.51 ?  99  ASN   A ND2  1 
ATOM   1926 N  ND2  B ASN   A 1 99  ? 22.288 2.115   -9.388  0.30 16.25 ?  99  ASN   A ND2  1 
ATOM   1927 H  H    A ASN   A 1 99  ? 23.906 -2.335  -9.487  0.70 18.68 ?  99  ASN   A H    1 
ATOM   1928 H  H    B ASN   A 1 99  ? 23.953 -2.410  -9.490  0.30 17.70 ?  99  ASN   A H    1 
ATOM   1929 H  HA   A ASN   A 1 99  ? 21.447 -1.517  -8.676  0.70 19.99 ?  99  ASN   A HA   1 
ATOM   1930 H  HA   B ASN   A 1 99  ? 21.445 -1.527  -9.009  0.30 18.09 ?  99  ASN   A HA   1 
ATOM   1931 H  HB2  A ASN   A 1 99  ? 23.288 -0.018  -8.327  0.70 20.51 ?  99  ASN   A HB2  1 
ATOM   1932 H  HB2  B ASN   A 1 99  ? 23.316 -0.046  -8.766  0.30 18.82 ?  99  ASN   A HB2  1 
ATOM   1933 H  HB3  A ASN   A 1 99  ? 23.373 0.140   -9.905  0.70 20.51 ?  99  ASN   A HB3  1 
ATOM   1934 H  HB3  B ASN   A 1 99  ? 23.581 -0.202  -10.325 0.30 18.82 ?  99  ASN   A HB3  1 
ATOM   1935 H  HD21 A ASN   A 1 99  ? 21.456 2.779   -8.215  0.70 20.97 ?  99  ASN   A HD21 1 
ATOM   1936 H  HD21 B ASN   A 1 99  ? 21.783 2.800   -9.516  0.30 19.46 ?  99  ASN   A HD21 1 
ATOM   1937 H  HD22 A ASN   A 1 99  ? 22.730 2.117   -7.817  0.70 20.97 ?  99  ASN   A HD22 1 
ATOM   1938 H  HD22 B ASN   A 1 99  ? 23.011 2.197   -8.926  0.30 19.46 ?  99  ASN   A HD22 1 
ATOM   1939 N  N    A VAL   A 1 100 ? 20.284 -1.994  -10.755 0.70 18.26 ?  100 VAL   A N    1 
ATOM   1940 N  N    B VAL   A 1 100 ? 20.483 -2.386  -11.117 0.30 16.20 ?  100 VAL   A N    1 
ATOM   1941 C  CA   A VAL   A 1 100 ? 19.619 -2.254  -12.030 0.70 20.13 ?  100 VAL   A CA   1 
ATOM   1942 C  CA   B VAL   A 1 100 ? 19.939 -2.792  -12.408 0.30 17.37 ?  100 VAL   A CA   1 
ATOM   1943 C  C    A VAL   A 1 100 ? 19.519 -0.977  -12.852 0.70 21.51 ?  100 VAL   A C    1 
ATOM   1944 C  C    B VAL   A 1 100 ? 19.792 -1.599  -13.343 0.30 17.14 ?  100 VAL   A C    1 
ATOM   1945 O  O    A VAL   A 1 100 ? 19.617 -1.010  -14.084 0.70 22.20 ?  100 VAL   A O    1 
ATOM   1946 O  O    B VAL   A 1 100 ? 19.802 -1.763  -14.570 0.30 17.41 ?  100 VAL   A O    1 
ATOM   1947 C  CB   A VAL   A 1 100 ? 18.243 -2.920  -11.797 0.70 21.34 ?  100 VAL   A CB   1 
ATOM   1948 C  CB   B VAL   A 1 100 ? 18.614 -3.549  -12.204 0.30 19.20 ?  100 VAL   A CB   1 
ATOM   1949 C  CG1  A VAL   A 1 100 ? 17.495 -3.107  -13.111 0.70 22.30 ?  100 VAL   A CG1  1 
ATOM   1950 C  CG1  B VAL   A 1 100 ? 17.733 -3.476  -13.447 0.30 19.81 ?  100 VAL   A CG1  1 
ATOM   1951 C  CG2  A VAL   A 1 100 ? 18.423 -4.264  -11.104 0.70 21.36 ?  100 VAL   A CG2  1 
ATOM   1952 C  CG2  B VAL   A 1 100 ? 18.901 -4.992  -11.833 0.30 19.90 ?  100 VAL   A CG2  1 
ATOM   1953 H  H    A VAL   A 1 100 ? 19.785 -2.131  -10.066 0.70 21.88 ?  100 VAL   A H    1 
ATOM   1954 H  H    B VAL   A 1 100 ? 19.938 -2.471  -10.460 0.30 19.40 ?  100 VAL   A H    1 
ATOM   1955 H  HA   A VAL   A 1 100 ? 20.150 -2.885  -12.537 0.70 24.12 ?  100 VAL   A HA   1 
ATOM   1956 H  HA   B VAL   A 1 100 ? 20.562 -3.403  -12.826 0.30 20.81 ?  100 VAL   A HA   1 
ATOM   1957 H  HB   A VAL   A 1 100 ? 17.701 -2.360  -11.221 0.70 25.57 ?  100 VAL   A HB   1 
ATOM   1958 H  HB   B VAL   A 1 100 ? 18.130 -3.135  -11.474 0.30 23.00 ?  100 VAL   A HB   1 
ATOM   1959 H  HG11 A VAL   A 1 100 ? 16.740 -3.702  -12.966 0.70 26.72 ?  100 VAL   A HG11 1 
ATOM   1960 H  HG11 B VAL   A 1 100 ? 17.025 -4.134  -13.363 0.30 23.74 ?  100 VAL   A HG11 1 
ATOM   1961 H  HG12 A VAL   A 1 100 ? 17.177 -2.246  -13.421 0.70 26.72 ?  100 VAL   A HG12 1 
ATOM   1962 H  HG12 B VAL   A 1 100 ? 17.345 -2.587  -13.516 0.30 23.74 ?  100 VAL   A HG12 1 
ATOM   1963 H  HG13 A VAL   A 1 100 ? 18.096 -3.497  -13.765 0.70 26.72 ?  100 VAL   A HG13 1 
ATOM   1964 H  HG13 B VAL   A 1 100 ? 18.269 -3.667  -14.231 0.30 23.74 ?  100 VAL   A HG13 1 
ATOM   1965 H  HG21 A VAL   A 1 100 ? 17.556 -4.690  -11.002 0.70 25.59 ?  100 VAL   A HG21 1 
ATOM   1966 H  HG21 B VAL   A 1 100 ? 18.064 -5.436  -11.640 0.30 23.84 ?  100 VAL   A HG21 1 
ATOM   1967 H  HG22 A VAL   A 1 100 ? 19.002 -4.824  -11.645 0.70 25.59 ?  100 VAL   A HG22 1 
ATOM   1968 H  HG22 B VAL   A 1 100 ? 19.345 -5.426  -12.579 0.30 23.84 ?  100 VAL   A HG22 1 
ATOM   1969 H  HG23 A VAL   A 1 100 ? 18.823 -4.119  -10.233 0.70 25.59 ?  100 VAL   A HG23 1 
ATOM   1970 H  HG23 B VAL   A 1 100 ? 19.475 -5.005  -11.053 0.30 23.84 ?  100 VAL   A HG23 1 
ATOM   1971 N  N    A ASN   A 1 101 ? 19.330 0.163   -12.196 0.70 22.71 ?  101 ASN   A N    1 
ATOM   1972 N  N    B ASN   A 1 101 ? 19.642 -0.390  -12.793 0.30 17.26 ?  101 ASN   A N    1 
ATOM   1973 C  CA   A ASN   A 1 101 ? 19.270 1.430   -12.911 0.70 24.17 ?  101 ASN   A CA   1 
ATOM   1974 C  CA   B ASN   A 1 101 ? 19.595 0.814   -13.618 0.30 18.16 ?  101 ASN   A CA   1 
ATOM   1975 C  C    A ASN   A 1 101 ? 20.626 1.862   -13.465 0.70 26.64 ?  101 ASN   A C    1 
ATOM   1976 C  C    B ASN   A 1 101 ? 20.928 1.106   -14.297 0.30 19.77 ?  101 ASN   A C    1 
ATOM   1977 O  O    A ASN   A 1 101 ? 20.699 2.905   -14.126 0.70 27.78 ?  101 ASN   A O    1 
ATOM   1978 O  O    B ASN   A 1 101 ? 20.943 1.789   -15.326 0.30 19.88 ?  101 ASN   A O    1 
ATOM   1979 C  CB   A ASN   A 1 101 ? 18.669 2.501   -12.000 0.70 22.84 ?  101 ASN   A CB   1 
ATOM   1980 C  CB   B ASN   A 1 101 ? 19.153 2.021   -12.780 0.30 17.85 ?  101 ASN   A CB   1 
ATOM   1981 C  CG   A ASN   A 1 101 ? 17.304 2.102   -11.452 0.70 22.08 ?  101 ASN   A CG   1 
ATOM   1982 C  CG   B ASN   A 1 101 ? 17.890 1.744   -11.980 0.30 18.31 ?  101 ASN   A CG   1 
ATOM   1983 O  OD1  A ASN   A 1 101 ? 16.444 1.604   -12.183 0.70 22.53 ?  101 ASN   A OD1  1 
ATOM   1984 O  OD1  B ASN   A 1 101 ? 16.943 1.134   -12.479 0.30 19.42 ?  101 ASN   A OD1  1 
ATOM   1985 N  ND2  A ASN   A 1 101 ? 17.105 2.307   -10.158 0.70 22.18 ?  101 ASN   A ND2  1 
ATOM   1986 N  ND2  B ASN   A 1 101 ? 17.876 2.182   -10.727 0.30 18.23 ?  101 ASN   A ND2  1 
ATOM   1987 H  H    A ASN   A 1 101 ? 19.231 0.224   -11.347 0.70 27.21 ?  101 ASN   A H    1 
ATOM   1988 H  H    B ASN   A 1 101 ? 19.549 -0.239  -11.951 0.30 20.67 ?  101 ASN   A H    1 
ATOM   1989 H  HA   A ASN   A 1 101 ? 18.670 1.324   -13.666 0.70 28.96 ?  101 ASN   A HA   1 
ATOM   1990 H  HA   B ASN   A 1 101 ? 18.939 0.694   -14.318 0.30 21.75 ?  101 ASN   A HA   1 
ATOM   1991 H  HB2  A ASN   A 1 101 ? 19.264 2.650   -11.251 0.70 27.37 ?  101 ASN   A HB2  1 
ATOM   1992 H  HB2  B ASN   A 1 101 ? 19.857 2.259   -12.156 0.30 21.39 ?  101 ASN   A HB2  1 
ATOM   1993 H  HB3  A ASN   A 1 101 ? 18.561 3.321   -12.509 0.70 27.37 ?  101 ASN   A HB3  1 
ATOM   1994 H  HB3  B ASN   A 1 101 ? 18.972 2.774   -13.371 0.30 21.39 ?  101 ASN   A HB3  1 
ATOM   1995 H  HD21 A ASN   A 1 101 ? 16.353 2.096   -9.803  0.70 26.58 ?  101 ASN   A HD21 1 
ATOM   1996 H  HD21 B ASN   A 1 101 ? 17.185 2.048   -10.233 0.30 21.84 ?  101 ASN   A HD21 1 
ATOM   1997 H  HD22 A ASN   A 1 101 ? 17.729 2.654   -9.677  0.70 26.58 ?  101 ASN   A HD22 1 
ATOM   1998 H  HD22 B ASN   A 1 101 ? 18.557 2.600   -10.409 0.30 21.84 ?  101 ASN   A HD22 1 
ATOM   1999 N  N    A LYS   A 1 102 ? 21.687 1.088   -13.217 0.70 28.18 ?  102 LYS   A N    1 
ATOM   2000 N  N    B LYS   A 1 102 ? 22.039 0.609   -13.750 0.30 21.51 ?  102 LYS   A N    1 
ATOM   2001 C  CA   A LYS   A 1 102 ? 22.980 1.276   -13.863 0.70 29.50 ?  102 LYS   A CA   1 
ATOM   2002 C  CA   B LYS   A 1 102 ? 23.359 0.778   -14.347 0.30 23.35 ?  102 LYS   A CA   1 
ATOM   2003 C  C    A LYS   A 1 102 ? 23.315 0.161   -14.846 0.70 29.78 ?  102 LYS   A C    1 
ATOM   2004 C  C    B LYS   A 1 102 ? 23.740 -0.380  -15.265 0.30 23.63 ?  102 LYS   A C    1 
ATOM   2005 O  O    A LYS   A 1 102 ? 24.413 0.164   -15.411 0.70 30.31 ?  102 LYS   A O    1 
ATOM   2006 O  O    B LYS   A 1 102 ? 24.912 -0.504  -15.635 0.30 23.73 ?  102 LYS   A O    1 
ATOM   2007 C  CB   A LYS   A 1 102 ? 24.100 1.360   -12.818 0.70 30.96 ?  102 LYS   A CB   1 
ATOM   2008 C  CB   B LYS   A 1 102 ? 24.429 0.930   -13.259 0.30 25.02 ?  102 LYS   A CB   1 
ATOM   2009 C  CG   A LYS   A 1 102 ? 23.968 2.496   -11.824 0.70 32.08 ?  102 LYS   A CG   1 
ATOM   2010 C  CG   B LYS   A 1 102 ? 24.539 2.322   -12.654 0.30 26.64 ?  102 LYS   A CG   1 
ATOM   2011 C  CD   A LYS   A 1 102 ? 25.124 2.482   -10.831 0.70 33.33 ?  102 LYS   A CD   1 
ATOM   2012 C  CD   B LYS   A 1 102 ? 25.777 2.438   -11.770 0.30 28.18 ?  102 LYS   A CD   1 
ATOM   2013 C  CE   A LYS   A 1 102 ? 25.042 3.647   -9.858  0.70 34.38 ?  102 LYS   A CE   1 
ATOM   2014 C  CE   B LYS   A 1 102 ? 25.955 3.851   -11.230 0.30 29.31 ?  102 LYS   A CE   1 
ATOM   2015 N  NZ   A LYS   A 1 102 ? 26.122 3.586   -8.831  0.70 34.91 ?  102 LYS   A NZ   1 
ATOM   2016 N  NZ   B LYS   A 1 102 ? 27.132 3.960   -10.320 0.30 29.92 ?  102 LYS   A NZ   1 
ATOM   2017 H  H    A LYS   A 1 102 ? 21.678 0.430   -12.661 0.70 33.78 ?  102 LYS   A H    1 
ATOM   2018 H  H    B LYS   A 1 102 ? 22.050 0.156   -13.019 0.30 25.77 ?  102 LYS   A H    1 
ATOM   2019 H  HA   A LYS   A 1 102 ? 22.965 2.112   -14.352 0.70 35.36 ?  102 LYS   A HA   1 
ATOM   2020 H  HA   B LYS   A 1 102 ? 23.360 1.598   -14.868 0.30 27.98 ?  102 LYS   A HA   1 
ATOM   2021 H  HB2  A LYS   A 1 102 ? 24.118 0.532   -12.314 0.70 37.12 ?  102 LYS   A HB2  1 
ATOM   2022 H  HB2  B LYS   A 1 102 ? 24.229 0.315   -12.538 0.30 29.99 ?  102 LYS   A HB2  1 
ATOM   2023 H  HB3  A LYS   A 1 102 ? 24.945 1.476   -13.281 0.70 37.12 ?  102 LYS   A HB3  1 
ATOM   2024 H  HB3  B LYS   A 1 102 ? 25.296 0.713   -13.639 0.30 29.99 ?  102 LYS   A HB3  1 
ATOM   2025 H  HG2  A LYS   A 1 102 ? 23.981 3.342   -12.298 0.70 38.45 ?  102 LYS   A HG2  1 
ATOM   2026 H  HG2  B LYS   A 1 102 ? 24.611 2.980   -13.363 0.30 31.93 ?  102 LYS   A HG2  1 
ATOM   2027 H  HG3  A LYS   A 1 102 ? 23.139 2.396   -11.331 0.70 38.45 ?  102 LYS   A HG3  1 
ATOM   2028 H  HG3  B LYS   A 1 102 ? 23.759 2.500   -12.106 0.30 31.93 ?  102 LYS   A HG3  1 
ATOM   2029 H  HD2  A LYS   A 1 102 ? 25.098 1.656   -10.321 0.70 39.96 ?  102 LYS   A HD2  1 
ATOM   2030 H  HD2  B LYS   A 1 102 ? 25.691 1.835   -11.015 0.30 33.78 ?  102 LYS   A HD2  1 
ATOM   2031 H  HD3  A LYS   A 1 102 ? 25.963 2.547   -11.316 0.70 39.96 ?  102 LYS   A HD3  1 
ATOM   2032 H  HD3  B LYS   A 1 102 ? 26.565 2.212   -12.290 0.30 33.78 ?  102 LYS   A HD3  1 
ATOM   2033 H  HE2  A LYS   A 1 102 ? 25.135 4.480   -10.349 0.70 41.22 ?  102 LYS   A HE2  1 
ATOM   2034 H  HE2  B LYS   A 1 102 ? 26.091 4.461   -11.972 0.30 35.14 ?  102 LYS   A HE2  1 
ATOM   2035 H  HE3  A LYS   A 1 102 ? 24.186 3.623   -9.402  0.70 41.22 ?  102 LYS   A HE3  1 
ATOM   2036 H  HE3  B LYS   A 1 102 ? 25.163 4.104   -10.731 0.30 35.14 ?  102 LYS   A HE3  1 
ATOM   2037 H  HZ1  A LYS   A 1 102 ? 26.053 4.277   -8.275  0.70 41.86 ?  102 LYS   A HZ1  1 
ATOM   2038 H  HZ1  B LYS   A 1 102 ? 27.211 4.795   -10.021 0.30 35.87 ?  102 LYS   A HZ1  1 
ATOM   2039 H  HZ2  A LYS   A 1 102 ? 26.055 2.831   -8.364  0.70 41.86 ?  102 LYS   A HZ2  1 
ATOM   2040 H  HZ2  B LYS   A 1 102 ? 27.031 3.413   -9.625  0.30 35.87 ?  102 LYS   A HZ2  1 
ATOM   2041 H  HZ3  A LYS   A 1 102 ? 26.919 3.612   -9.226  0.70 41.86 ?  102 LYS   A HZ3  1 
ATOM   2042 H  HZ3  B LYS   A 1 102 ? 27.876 3.738   -10.755 0.30 35.87 ?  102 LYS   A HZ3  1 
ATOM   2043 N  N    A GLY   A 1 103 ? 22.412 -0.797  -15.055 0.70 29.93 ?  103 GLY   A N    1 
ATOM   2044 N  N    B GLY   A 1 103 ? 22.786 -1.232  -15.633 0.30 23.98 ?  103 GLY   A N    1 
ATOM   2045 C  CA   A GLY   A 1 103 ? 22.664 -1.904  -15.958 0.70 29.86 ?  103 GLY   A CA   1 
ATOM   2046 C  CA   B GLY   A 1 103 ? 23.094 -2.361  -16.489 0.30 24.24 ?  103 GLY   A CA   1 
ATOM   2047 C  C    A GLY   A 1 103 ? 23.471 -3.047  -15.380 0.70 29.43 ?  103 GLY   A C    1 
ATOM   2048 C  C    B GLY   A 1 103 ? 23.901 -3.455  -15.831 0.30 24.27 ?  103 GLY   A C    1 
ATOM   2049 O  O    A GLY   A 1 103 ? 23.948 -3.894  -16.144 0.70 30.42 ?  103 GLY   A O    1 
ATOM   2050 O  O    B GLY   A 1 103 ? 24.508 -4.271  -16.531 0.30 24.81 ?  103 GLY   A O    1 
ATOM   2051 H  H    A GLY   A 1 103 ? 21.637 -0.821  -14.687 0.70 35.88 ?  103 GLY   A H    1 
ATOM   2052 H  H    B GLY   A 1 103 ? 21.962 -1.168  -15.401 0.30 28.73 ?  103 GLY   A H    1 
ATOM   2053 H  HA2  A GLY   A 1 103 ? 21.815 -2.257  -16.273 0.70 35.79 ?  103 GLY   A HA2  1 
ATOM   2054 H  HA2  B GLY   A 1 103 ? 22.267 -2.743  -16.823 0.30 29.04 ?  103 GLY   A HA2  1 
ATOM   2055 H  HA3  A GLY   A 1 103 ? 23.146 -1.562  -16.728 0.70 35.79 ?  103 GLY   A HA3  1 
ATOM   2056 H  HA3  B GLY   A 1 103 ? 23.609 -2.041  -17.246 0.30 29.04 ?  103 GLY   A HA3  1 
ATOM   2057 N  N    A GLU   A 1 104 ? 23.631 -3.112  -14.062 0.70 27.21 ?  104 GLU   A N    1 
ATOM   2058 N  N    B GLU   A 1 104 ? 23.925 -3.502  -14.505 0.30 23.30 ?  104 GLU   A N    1 
ATOM   2059 C  CA   A GLU   A 1 104 ? 24.511 -4.099  -13.451 0.70 25.13 ?  104 GLU   A CA   1 
ATOM   2060 C  CA   B GLU   A 1 104 ? 24.782 -4.437  -13.794 0.30 22.56 ?  104 GLU   A CA   1 
ATOM   2061 C  C    A GLU   A 1 104 ? 23.833 -5.464  -13.336 0.70 25.19 ?  104 GLU   A C    1 
ATOM   2062 C  C    B GLU   A 1 104 ? 24.108 -5.797  -13.636 0.30 22.01 ?  104 GLU   A C    1 
ATOM   2063 O  O    A GLU   A 1 104 ? 22.619 -5.573  -13.138 0.70 24.92 ?  104 GLU   A O    1 
ATOM   2064 O  O    B GLU   A 1 104 ? 22.880 -5.913  -13.613 0.30 21.41 ?  104 GLU   A O    1 
ATOM   2065 C  CB   A GLU   A 1 104 ? 25.005 -3.592  -12.094 0.70 22.94 ?  104 GLU   A CB   1 
ATOM   2066 C  CB   B GLU   A 1 104 ? 25.181 -3.862  -12.435 0.30 22.63 ?  104 GLU   A CB   1 
ATOM   2067 C  CG   A GLU   A 1 104 ? 25.917 -2.372  -12.259 0.70 22.01 ?  104 GLU   A CG   1 
ATOM   2068 C  CG   B GLU   A 1 104 ? 25.999 -2.582  -12.563 0.30 23.08 ?  104 GLU   A CG   1 
ATOM   2069 C  CD   A GLU   A 1 104 ? 26.311 -1.664  -10.970 0.70 20.64 ?  104 GLU   A CD   1 
ATOM   2070 C  CD   B GLU   A 1 104 ? 26.187 -1.853  -11.245 0.30 23.37 ?  104 GLU   A CD   1 
ATOM   2071 O  OE1  A GLU   A 1 104 ? 25.732 -1.926  -9.899  0.70 19.39 ?  104 GLU   A OE1  1 
ATOM   2072 O  OE1  B GLU   A 1 104 ? 25.807 -2.402  -10.191 0.30 23.69 ?  104 GLU   A OE1  1 
ATOM   2073 O  OE2  A GLU   A 1 104 ? 27.221 -0.808  -11.049 0.70 21.24 -1 104 GLU   A OE2  1 
ATOM   2074 O  OE2  B GLU   A 1 104 ? 26.708 -0.718  -11.269 0.30 23.50 -1 104 GLU   A OE2  1 
ATOM   2075 H  H    A GLU   A 1 104 ? 23.244 -2.585  -13.506 0.70 32.61 ?  104 GLU   A H    1 
ATOM   2076 H  H    B GLU   A 1 104 ? 23.454 -2.990  -13.996 0.30 27.92 ?  104 GLU   A H    1 
ATOM   2077 H  HA   A GLU   A 1 104 ? 25.286 -4.203  -14.022 0.70 30.11 ?  104 GLU   A HA   1 
ATOM   2078 H  HA   B GLU   A 1 104 ? 25.593 -4.557  -14.312 0.30 27.03 ?  104 GLU   A HA   1 
ATOM   2079 H  HB2  A GLU   A 1 104 ? 24.244 -3.336  -11.552 0.70 27.49 ?  104 GLU   A HB2  1 
ATOM   2080 H  HB2  B GLU   A 1 104 ? 24.380 -3.660  -11.929 0.30 27.12 ?  104 GLU   A HB2  1 
ATOM   2081 H  HB3  A GLU   A 1 104 ? 25.510 -4.296  -11.660 0.70 27.49 ?  104 GLU   A HB3  1 
ATOM   2082 H  HB3  B GLU   A 1 104 ? 25.719 -4.518  -11.965 0.30 27.12 ?  104 GLU   A HB3  1 
ATOM   2083 H  HG2  A GLU   A 1 104 ? 26.734 -2.656  -12.693 0.70 26.37 ?  104 GLU   A HG2  1 
ATOM   2084 H  HG2  B GLU   A 1 104 ? 26.874 -2.803  -12.920 0.30 27.65 ?  104 GLU   A HG2  1 
ATOM   2085 H  HG3  A GLU   A 1 104 ? 25.461 -1.720  -12.814 0.70 26.37 ?  104 GLU   A HG3  1 
ATOM   2086 H  HG3  B GLU   A 1 104 ? 25.543 -1.976  -13.170 0.30 27.65 ?  104 GLU   A HG3  1 
ATOM   2087 N  N    A ASP   A 1 105 ? 24.645 -6.512  -13.461 0.70 25.93 ?  105 ASP   A N    1 
ATOM   2088 N  N    B ASP   A 1 105 ? 24.942 -6.828  -13.517 0.30 22.67 ?  105 ASP   A N    1 
ATOM   2089 C  CA   A ASP   A 1 105 ? 24.147 -7.875  -13.614 0.70 26.91 ?  105 ASP   A CA   1 
ATOM   2090 C  CA   B ASP   A 1 105 ? 24.491 -8.211  -13.615 0.30 23.61 ?  105 ASP   A CA   1 
ATOM   2091 C  C    A ASP   A 1 105 ? 23.487 -8.356  -12.323 0.70 24.42 ?  105 ASP   A C    1 
ATOM   2092 C  C    B ASP   A 1 105 ? 23.647 -8.597  -12.406 0.30 23.58 ?  105 ASP   A C    1 
ATOM   2093 O  O    A ASP   A 1 105 ? 24.145 -8.485  -11.285 0.70 22.63 ?  105 ASP   A O    1 
ATOM   2094 O  O    B ASP   A 1 105 ? 24.078 -8.451  -11.258 0.30 23.06 ?  105 ASP   A O    1 
ATOM   2095 C  CB   A ASP   A 1 105 ? 25.314 -8.785  -13.993 0.70 30.15 ?  105 ASP   A CB   1 
ATOM   2096 C  CB   B ASP   A 1 105 ? 25.715 -9.122  -13.699 0.30 24.63 ?  105 ASP   A CB   1 
ATOM   2097 C  CG   A ASP   A 1 105 ? 24.893 -10.222 -14.200 0.70 32.94 ?  105 ASP   A CG   1 
ATOM   2098 C  CG   B ASP   A 1 105 ? 25.360 -10.557 -14.028 0.30 25.54 ?  105 ASP   A CG   1 
ATOM   2099 O  OD1  A ASP   A 1 105 ? 23.674 -10.474 -14.304 0.70 33.72 ?  105 ASP   A OD1  1 
ATOM   2100 O  OD1  B ASP   A 1 105 ? 24.157 -10.878 -14.123 0.30 25.62 ?  105 ASP   A OD1  1 
ATOM   2101 O  OD2  A ASP   A 1 105 ? 25.782 -11.099 -14.256 0.70 34.31 -1 105 ASP   A OD2  1 
ATOM   2102 O  OD2  B ASP   A 1 105 ? 26.296 -11.371 -14.187 0.30 25.89 -1 105 ASP   A OD2  1 
ATOM   2103 H  H    A ASP   A 1 105 ? 25.501 -6.452  -13.460 0.70 31.08 ?  105 ASP   A H    1 
ATOM   2104 H  H    B ASP   A 1 105 ? 25.782 -6.743  -13.375 0.30 27.16 ?  105 ASP   A H    1 
ATOM   2105 H  HA   A ASP   A 1 105 ? 23.489 -7.903  -14.330 0.70 32.26 ?  105 ASP   A HA   1 
ATOM   2106 H  HA   B ASP   A 1 105 ? 23.960 -8.329  -14.420 0.30 28.29 ?  105 ASP   A HA   1 
ATOM   2107 H  HB2  A ASP   A 1 105 ? 25.711 -8.463  -14.821 0.70 36.14 ?  105 ASP   A HB2  1 
ATOM   2108 H  HB2  B ASP   A 1 105 ? 26.317 -8.780  -14.381 0.30 29.52 ?  105 ASP   A HB2  1 
ATOM   2109 H  HB3  A ASP   A 1 105 ? 25.973 -8.762  -13.283 0.70 36.14 ?  105 ASP   A HB3  1 
ATOM   2110 H  HB3  B ASP   A 1 105 ? 26.161 -9.127  -12.840 0.30 29.52 ?  105 ASP   A HB3  1 
ATOM   2111 N  N    A ILE   A 1 106 ? 22.183 -8.637  -12.396 0.70 23.58 ?  106 ILE   A N    1 
ATOM   2112 N  N    B ILE   A 1 106 ? 22.446 -9.119  -12.669 0.30 24.15 ?  106 ILE   A N    1 
ATOM   2113 C  CA   A ILE   A 1 106 ? 21.430 -9.053  -11.218 0.70 22.47 ?  106 ILE   A CA   1 
ATOM   2114 C  CA   B ILE   A 1 106 ? 21.571 -9.537  -11.578 0.30 24.65 ?  106 ILE   A CA   1 
ATOM   2115 C  C    A ILE   A 1 106 ? 21.957 -10.355 -10.636 0.70 21.64 ?  106 ILE   A C    1 
ATOM   2116 C  C    B ILE   A 1 106 ? 22.181 -10.700 -10.812 0.30 24.77 ?  106 ILE   A C    1 
ATOM   2117 O  O    A ILE   A 1 106 ? 21.755 -10.625 -9.448  0.70 20.88 ?  106 ILE   A O    1 
ATOM   2118 O  O    B ILE   A 1 106 ? 21.927 -10.863 -9.612  0.30 24.72 ?  106 ILE   A O    1 
ATOM   2119 C  CB   A ILE   A 1 106 ? 19.922 -9.127  -11.548 0.70 23.38 ?  106 ILE   A CB   1 
ATOM   2120 C  CB   B ILE   A 1 106 ? 20.165 -9.879  -12.109 0.30 25.13 ?  106 ILE   A CB   1 
ATOM   2121 C  CG1  A ILE   A 1 106 ? 19.086 -9.211  -10.267 0.70 23.82 ?  106 ILE   A CG1  1 
ATOM   2122 C  CG1  B ILE   A 1 106 ? 19.133 -9.819  -10.983 0.30 25.21 ?  106 ILE   A CG1  1 
ATOM   2123 C  CG2  A ILE   A 1 106 ? 19.627 -10.317 -12.443 0.70 23.93 ?  106 ILE   A CG2  1 
ATOM   2124 C  CG2  B ILE   A 1 106 ? 20.146 -11.276 -12.703 0.30 25.35 ?  106 ILE   A CG2  1 
ATOM   2125 C  CD1  A ILE   A 1 106 ? 19.211 -7.997  -9.370  0.70 23.99 ?  106 ILE   A CD1  1 
ATOM   2126 C  CD1  B ILE   A 1 106 ? 19.028 -8.469  -10.320 0.30 25.32 ?  106 ILE   A CD1  1 
ATOM   2127 H  H    A ILE   A 1 106 ? 21.718 -8.580  -13.113 0.70 28.26 ?  106 ILE   A H    1 
ATOM   2128 H  H    B ILE   A 1 106 ? 22.126 -9.245  -13.455 0.30 28.94 ?  106 ILE   A H    1 
ATOM   2129 H  HA   A ILE   A 1 106 ? 21.551 -8.378  -10.538 0.70 26.92 ?  106 ILE   A HA   1 
ATOM   2130 H  HA   B ILE   A 1 106 ? 21.491 -8.800  -10.960 0.30 29.54 ?  106 ILE   A HA   1 
ATOM   2131 H  HB   A ILE   A 1 106 ? 19.674 -8.316  -12.022 0.70 28.02 ?  106 ILE   A HB   1 
ATOM   2132 H  HB   B ILE   A 1 106 ? 19.920 -9.242  -12.800 0.30 30.12 ?  106 ILE   A HB   1 
ATOM   2133 H  HG12 A ILE   A 1 106 ? 18.152 -9.298  -10.511 0.70 28.54 ?  106 ILE   A HG12 1 
ATOM   2134 H  HG12 B ILE   A 1 106 ? 18.261 -10.039 -11.349 0.30 30.22 ?  106 ILE   A HG12 1 
ATOM   2135 H  HG13 A ILE   A 1 106 ? 19.367 -9.985  -9.758  0.70 28.54 ?  106 ILE   A HG13 1 
ATOM   2136 H  HG13 B ILE   A 1 106 ? 19.376 -10.468 -10.305 0.30 30.22 ?  106 ILE   A HG13 1 
ATOM   2137 H  HG21 A ILE   A 1 106 ? 18.731 -10.222 -12.800 0.70 28.68 ?  106 ILE   A HG21 1 
ATOM   2138 H  HG21 B ILE   A 1 106 ? 19.322 -11.397 -13.197 0.30 30.39 ?  106 ILE   A HG21 1 
ATOM   2139 H  HG22 A ILE   A 1 106 ? 20.274 -10.330 -13.165 0.70 28.68 ?  106 ILE   A HG22 1 
ATOM   2140 H  HG22 B ILE   A 1 106 ? 20.908 -11.380 -13.292 0.30 30.39 ?  106 ILE   A HG22 1 
ATOM   2141 H  HG23 A ILE   A 1 106 ? 19.694 -11.128 -11.919 0.70 28.68 ?  106 ILE   A HG23 1 
ATOM   2142 H  HG23 B ILE   A 1 106 ? 20.190 -11.929 -11.985 0.30 30.39 ?  106 ILE   A HG23 1 
ATOM   2143 H  HD11 A ILE   A 1 106 ? 18.490 -8.008  -8.724  0.70 28.75 ?  106 ILE   A HD11 1 
ATOM   2144 H  HD11 B ILE   A 1 106 ? 18.166 -8.402  -9.887  0.30 30.34 ?  106 ILE   A HD11 1 
ATOM   2145 H  HD12 A ILE   A 1 106 ? 20.066 -8.029  -8.910  0.70 28.75 ?  106 ILE   A HD12 1 
ATOM   2146 H  HD12 B ILE   A 1 106 ? 19.738 -8.386  -9.664  0.30 30.34 ?  106 ILE   A HD12 1 
ATOM   2147 H  HD13 A ILE   A 1 106 ? 19.157 -7.195  -9.913  0.70 28.75 ?  106 ILE   A HD13 1 
ATOM   2148 H  HD13 B ILE   A 1 106 ? 19.115 -7.781  -10.997 0.30 30.34 ?  106 ILE   A HD13 1 
ATOM   2149 N  N    A GLN   A 1 107 ? 22.650 -11.166 -11.443 0.70 22.93 ?  107 GLN   A N    1 
ATOM   2150 N  N    B GLN   A 1 107 ? 22.993 -11.525 -11.480 0.30 25.06 ?  107 GLN   A N    1 
ATOM   2151 C  CA   A GLN   A 1 107 ? 23.277 -12.378 -10.926 0.70 25.33 ?  107 GLN   A CA   1 
ATOM   2152 C  CA   B GLN   A 1 107 ? 23.615 -12.662 -10.815 0.30 25.79 ?  107 GLN   A CA   1 
ATOM   2153 C  C    A GLN   A 1 107 ? 24.253 -12.073 -9.794  0.70 22.37 ?  107 GLN   A C    1 
ATOM   2154 C  C    B GLN   A 1 107 ? 24.523 -12.223 -9.678  0.30 23.14 ?  107 GLN   A C    1 
ATOM   2155 O  O    A GLN   A 1 107 ? 24.486 -12.931 -8.937  0.70 23.63 ?  107 GLN   A O    1 
ATOM   2156 O  O    B GLN   A 1 107 ? 24.840 -13.031 -8.797  0.30 23.38 ?  107 GLN   A O    1 
ATOM   2157 C  CB   A GLN   A 1 107 ? 23.974 -13.124 -12.072 0.70 30.47 ?  107 GLN   A CB   1 
ATOM   2158 C  CB   B GLN   A 1 107 ? 24.413 -13.485 -11.829 0.30 29.05 ?  107 GLN   A CB   1 
ATOM   2159 C  CG   A GLN   A 1 107 ? 23.072 -13.386 -13.278 0.70 35.79 ?  107 GLN   A CG   1 
ATOM   2160 C  CG   B GLN   A 1 107 ? 23.586 -13.982 -13.005 0.30 32.15 ?  107 GLN   A CG   1 
ATOM   2161 C  CD   A GLN   A 1 107 ? 21.808 -14.138 -12.908 0.70 40.16 ?  107 GLN   A CD   1 
ATOM   2162 C  CD   B GLN   A 1 107 ? 22.478 -14.925 -12.580 0.30 34.73 ?  107 GLN   A CD   1 
ATOM   2163 O  OE1  A GLN   A 1 107 ? 21.855 -15.154 -12.214 0.70 41.65 ?  107 GLN   A OE1  1 
ATOM   2164 O  OE1  B GLN   A 1 107 ? 22.658 -15.750 -11.684 0.30 35.59 ?  107 GLN   A OE1  1 
ATOM   2165 N  NE2  A GLN   A 1 107 ? 20.666 -13.636 -13.365 0.70 41.68 ?  107 GLN   A NE2  1 
ATOM   2166 N  NE2  B GLN   A 1 107 ? 21.320 -14.803 -13.219 0.30 35.56 ?  107 GLN   A NE2  1 
ATOM   2167 H  H    A GLN   A 1 107 ? 22.775 -11.032 -12.285 0.70 27.48 ?  107 GLN   A H    1 
ATOM   2168 H  H    B GLN   A 1 107 ? 23.205 -11.438 -12.308 0.30 30.03 ?  107 GLN   A H    1 
ATOM   2169 H  HA   A GLN   A 1 107 ? 22.589 -12.963 -10.579 0.70 30.36 ?  107 GLN   A HA   1 
ATOM   2170 H  HA   B GLN   A 1 107 ? 22.924 -13.230 -10.446 0.30 30.91 ?  107 GLN   A HA   1 
ATOM   2171 H  HB2  A GLN   A 1 107 ? 24.729 -12.601 -12.383 0.70 36.53 ?  107 GLN   A HB2  1 
ATOM   2172 H  HB2  B GLN   A 1 107 ? 25.131 -12.937 -12.183 0.30 34.82 ?  107 GLN   A HB2  1 
ATOM   2173 H  HB3  A GLN   A 1 107 ? 24.281 -13.987 -11.752 0.70 36.53 ?  107 GLN   A HB3  1 
ATOM   2174 H  HB3  B GLN   A 1 107 ? 24.783 -14.262 -11.381 0.30 34.82 ?  107 GLN   A HB3  1 
ATOM   2175 H  HG2  A GLN   A 1 107 ? 22.809 -12.539 -13.674 0.70 42.91 ?  107 GLN   A HG2  1 
ATOM   2176 H  HG2  B GLN   A 1 107 ? 23.180 -13.222 -13.452 0.30 38.55 ?  107 GLN   A HG2  1 
ATOM   2177 H  HG3  A GLN   A 1 107 ? 23.558 -13.915 -13.931 0.70 42.91 ?  107 GLN   A HG3  1 
ATOM   2178 H  HG3  B GLN   A 1 107 ? 24.165 -14.458 -13.620 0.30 38.55 ?  107 GLN   A HG3  1 
ATOM   2179 H  HE21 A GLN   A 1 107 ? 20.669 -12.923 -13.845 0.70 49.97 ?  107 GLN   A HE21 1 
ATOM   2180 H  HE21 B GLN   A 1 107 ? 21.231 -14.212 -13.838 0.30 42.63 ?  107 GLN   A HE21 1 
ATOM   2181 H  HE22 A GLN   A 1 107 ? 19.923 -14.027 -13.181 0.70 49.97 ?  107 GLN   A HE22 1 
ATOM   2182 H  HE22 B GLN   A 1 107 ? 20.660 -15.314 -13.014 0.30 42.63 ?  107 GLN   A HE22 1 
ATOM   2183 N  N    A LEU   A 1 108 ? 24.803 -10.857 -9.749  0.70 18.64 ?  108 LEU   A N    1 
ATOM   2184 N  N    B LEU   A 1 108 ? 24.946 -10.959 -9.677  0.30 20.48 ?  108 LEU   A N    1 
ATOM   2185 C  CA   A LEU   A 1 108 ? 25.723 -10.472 -8.684  0.70 16.46 ?  108 LEU   A CA   1 
ATOM   2186 C  CA   B LEU   A 1 108 ? 25.786 -10.443 -8.609  0.30 18.10 ?  108 LEU   A CA   1 
ATOM   2187 C  C    A LEU   A 1 108 ? 25.024 -10.292 -7.343  0.70 14.67 ?  108 LEU   A C    1 
ATOM   2188 C  C    B LEU   A 1 108 ? 25.025 -10.229 -7.309  0.30 15.90 ?  108 LEU   A C    1 
ATOM   2189 O  O    A LEU   A 1 108 ? 25.697 -10.152 -6.321  0.70 14.80 ?  108 LEU   A O    1 
ATOM   2190 O  O    B LEU   A 1 108 ? 25.660 -9.983  -6.279  0.30 15.85 ?  108 LEU   A O    1 
ATOM   2191 C  CB   A LEU   A 1 108 ? 26.478 -9.196  -9.072  0.70 16.95 ?  108 LEU   A CB   1 
ATOM   2192 C  CB   B LEU   A 1 108 ? 26.467 -9.146  -9.057  0.30 18.31 ?  108 LEU   A CB   1 
ATOM   2193 C  CG   A LEU   A 1 108 ? 27.493 -9.385  -10.200 0.70 18.47 ?  108 LEU   A CG   1 
ATOM   2194 C  CG   B LEU   A 1 108 ? 27.484 -9.326  -10.187 0.30 18.93 ?  108 LEU   A CG   1 
ATOM   2195 C  CD1  A LEU   A 1 108 ? 27.938 -8.048  -10.771 0.70 19.22 ?  108 LEU   A CD1  1 
ATOM   2196 C  CD1  B LEU   A 1 108 ? 28.034 -7.985  -10.650 0.30 19.21 ?  108 LEU   A CD1  1 
ATOM   2197 C  CD2  A LEU   A 1 108 ? 28.702 -10.172 -9.717  0.70 19.79 ?  108 LEU   A CD2  1 
ATOM   2198 C  CD2  B LEU   A 1 108 ? 28.618 -10.242 -9.751  0.30 19.53 ?  108 LEU   A CD2  1 
ATOM   2199 H  H    A LEU   A 1 108 ? 24.654 -10.245 -10.326 0.70 22.33 ?  108 LEU   A H    1 
ATOM   2200 H  H    B LEU   A 1 108 ? 24.764 -10.388 -10.289 0.30 24.54 ?  108 LEU   A H    1 
ATOM   2201 H  HA   A LEU   A 1 108 ? 26.376 -11.182 -8.575  0.70 19.72 ?  108 LEU   A HA   1 
ATOM   2202 H  HA   B LEU   A 1 108 ? 26.479 -11.091 -8.425  0.30 21.68 ?  108 LEU   A HA   1 
ATOM   2203 H  HB2  A LEU   A 1 108 ? 25.836 -8.533  -9.364  0.70 20.30 ?  108 LEU   A HB2  1 
ATOM   2204 H  HB2  B LEU   A 1 108 ? 25.788 -8.528  -9.370  0.30 21.93 ?  108 LEU   A HB2  1 
ATOM   2205 H  HB3  A LEU   A 1 108 ? 26.957 -8.875  -8.296  0.70 20.30 ?  108 LEU   A HB3  1 
ATOM   2206 H  HB3  B LEU   A 1 108 ? 26.935 -8.763  -8.300  0.30 21.93 ?  108 LEU   A HB3  1 
ATOM   2207 H  HG   A LEU   A 1 108 ? 27.080 -9.891  -10.917 0.70 22.13 ?  108 LEU   A HG   1 
ATOM   2208 H  HG   B LEU   A 1 108 ? 27.043 -9.743  -10.943 0.30 22.68 ?  108 LEU   A HG   1 
ATOM   2209 H  HD11 A LEU   A 1 108 ? 28.569 -8.206  -11.492 0.70 23.03 ?  108 LEU   A HD11 1 
ATOM   2210 H  HD11 B LEU   A 1 108 ? 28.640 -8.132  -11.394 0.30 23.01 ?  108 LEU   A HD11 1 
ATOM   2211 H  HD12 A LEU   A 1 108 ? 27.162 -7.575  -11.108 0.70 23.03 ?  108 LEU   A HD12 1 
ATOM   2212 H  HD12 B LEU   A 1 108 ? 27.297 -7.421  -10.931 0.30 23.01 ?  108 LEU   A HD12 1 
ATOM   2213 H  HD13 A LEU   A 1 108 ? 28.362 -7.531  -10.068 0.70 23.03 ?  108 LEU   A HD13 1 
ATOM   2214 H  HD13 B LEU   A 1 108 ? 28.510 -7.568  -9.915  0.30 23.01 ?  108 LEU   A HD13 1 
ATOM   2215 H  HD21 A LEU   A 1 108 ? 29.372 -10.185 -10.419 0.70 23.71 ?  108 LEU   A HD21 1 
ATOM   2216 H  HD21 B LEU   A 1 108 ? 29.350 -10.160 -10.382 0.30 23.40 ?  108 LEU   A HD21 1 
ATOM   2217 H  HD22 A LEU   A 1 108 ? 29.061 -9.742  -8.925  0.70 23.71 ?  108 LEU   A HD22 1 
ATOM   2218 H  HD22 B LEU   A 1 108 ? 28.912 -9.976  -8.866  0.30 23.40 ?  108 LEU   A HD22 1 
ATOM   2219 H  HD23 A LEU   A 1 108 ? 28.427 -11.078 -9.506  0.70 23.71 ?  108 LEU   A HD23 1 
ATOM   2220 H  HD23 B LEU   A 1 108 ? 28.295 -11.156 -9.733  0.30 23.40 ?  108 LEU   A HD23 1 
ATOM   2221 N  N    . LEU   A 1 109 ? 23.692 -10.333 -7.314  1.00 14.63 ?  109 LEU   A N    1 
ATOM   2222 C  CA   . LEU   A 1 109 ? 22.975 -10.205 -6.052  1.00 14.08 ?  109 LEU   A CA   1 
ATOM   2223 C  C    . LEU   A 1 109 ? 23.320 -11.356 -5.108  1.00 13.49 ?  109 LEU   A C    1 
ATOM   2224 O  O    . LEU   A 1 109 ? 23.459 -11.158 -3.897  1.00 13.69 ?  109 LEU   A O    1 
ATOM   2225 C  CB   . LEU   A 1 109 ? 21.474 -10.127 -6.316  1.00 14.59 ?  109 LEU   A CB   1 
ATOM   2226 C  CG   . LEU   A 1 109 ? 20.583 -9.836  -5.109  1.00 15.09 ?  109 LEU   A CG   1 
ATOM   2227 C  CD1  . LEU   A 1 109 ? 21.036 -8.584  -4.381  1.00 15.40 ?  109 LEU   A CD1  1 
ATOM   2228 C  CD2  . LEU   A 1 109 ? 19.127 -9.707  -5.546  1.00 15.84 ?  109 LEU   A CD2  1 
ATOM   2229 H  H    A LEU   A 1 109 ? 23.184 -10.436 -8.002  0.70 17.51 ?  109 LEU   A H    1 
ATOM   2230 H  H    B LEU   A 1 109 ? 23.198 -10.478 -8.005  0.30 17.51 ?  109 LEU   A H    1 
ATOM   2231 H  HA   . LEU   A 1 109 ? 23.250 -9.380  -5.627  1.00 16.86 ?  109 LEU   A HA   1 
ATOM   2232 H  HB2  . LEU   A 1 109 ? 21.317 -9.420  -6.962  1.00 17.47 ?  109 LEU   A HB2  1 
ATOM   2233 H  HB3  . LEU   A 1 109 ? 21.184 -10.972 -6.686  1.00 17.47 ?  109 LEU   A HB3  1 
ATOM   2234 H  HG   . LEU   A 1 109 ? 20.638 -10.575 -4.488  1.00 18.07 ?  109 LEU   A HG   1 
ATOM   2235 H  HD11 . LEU   A 1 109 ? 20.348 -8.297  -3.766  1.00 18.44 ?  109 LEU   A HD11 1 
ATOM   2236 H  HD12 . LEU   A 1 109 ? 21.856 -8.778  -3.896  1.00 18.44 ?  109 LEU   A HD12 1 
ATOM   2237 H  HD13 . LEU   A 1 109 ? 21.206 -7.882  -5.036  1.00 18.44 ?  109 LEU   A HD13 1 
ATOM   2238 H  HD21 . LEU   A 1 109 ? 18.589 -9.412  -4.789  1.00 18.97 ?  109 LEU   A HD21 1 
ATOM   2239 H  HD22 . LEU   A 1 109 ? 19.062 -9.054  -6.263  1.00 18.97 ?  109 LEU   A HD22 1 
ATOM   2240 H  HD23 . LEU   A 1 109 ? 18.807 -10.569 -5.858  1.00 18.97 ?  109 LEU   A HD23 1 
ATOM   2241 N  N    . LYS   A 1 110 ? 23.463 -12.574 -5.636  1.00 13.42 ?  110 LYS   A N    1 
ATOM   2242 C  CA   . LYS   A 1 110 ? 23.839 -13.689 -4.772  1.00 13.49 ?  110 LYS   A CA   1 
ATOM   2243 C  C    . LYS   A 1 110 ? 25.218 -13.464 -4.163  1.00 12.86 ?  110 LYS   A C    1 
ATOM   2244 O  O    . LYS   A 1 110 ? 25.415 -13.670 -2.961  1.00 13.30 ?  110 LYS   A O    1 
ATOM   2245 C  CB   . LYS   A 1 110 ? 23.770 -15.014 -5.534  1.00 14.56 ?  110 LYS   A CB   1 
ATOM   2246 C  CG   . LYS   A 1 110 ? 23.949 -16.226 -4.626  1.00 14.76 ?  110 LYS   A CG   1 
ATOM   2247 C  CD   . LYS   A 1 110 ? 23.736 -17.548 -5.351  1.00 15.48 ?  110 LYS   A CD   1 
ATOM   2248 C  CE   . LYS   A 1 110 ? 23.848 -18.736 -4.399  1.00 16.17 ?  110 LYS   A CE   1 
ATOM   2249 N  NZ   . LYS   A 1 110 ? 22.659 -18.883 -3.517  1.00 16.33 ?  110 LYS   A NZ   1 
ATOM   2250 H  H    . LYS   A 1 110 ? 23.348 -12.775 -6.461  1.00 16.07 ?  110 LYS   A H    1 
ATOM   2251 H  HA   . LYS   A 1 110 ? 23.199 -13.744 -4.040  1.00 16.15 ?  110 LYS   A HA   1 
ATOM   2252 H  HB2  . LYS   A 1 110 ? 22.902 -15.089 -5.963  1.00 17.43 ?  110 LYS   A HB2  1 
ATOM   2253 H  HB3  . LYS   A 1 110 ? 24.473 -15.034 -6.198  1.00 17.43 ?  110 LYS   A HB3  1 
ATOM   2254 H  HG2  . LYS   A 1 110 ? 24.846 -16.222 -4.264  1.00 17.68 ?  110 LYS   A HG2  1 
ATOM   2255 H  HG3  . LYS   A 1 110 ? 23.300 -16.177 -3.904  1.00 17.68 ?  110 LYS   A HG3  1 
ATOM   2256 H  HD2  . LYS   A 1 110 ? 22.853 -17.560 -5.746  1.00 18.54 ?  110 LYS   A HD2  1 
ATOM   2257 H  HD3  . LYS   A 1 110 ? 24.415 -17.643 -6.040  1.00 18.54 ?  110 LYS   A HD3  1 
ATOM   2258 H  HE2  . LYS   A 1 110 ? 23.949 -19.548 -4.917  1.00 19.36 ?  110 LYS   A HE2  1 
ATOM   2259 H  HE3  . LYS   A 1 110 ? 24.632 -18.610 -3.830  1.00 19.36 ?  110 LYS   A HE3  1 
ATOM   2260 H  HZ1  . LYS   A 1 110 ? 22.762 -19.582 -2.978  1.00 19.56 ?  110 LYS   A HZ1  1 
ATOM   2261 H  HZ2  . LYS   A 1 110 ? 22.551 -18.149 -3.024  1.00 19.56 ?  110 LYS   A HZ2  1 
ATOM   2262 H  HZ3  . LYS   A 1 110 ? 21.929 -19.005 -4.014  1.00 19.56 ?  110 LYS   A HZ3  1 
ATOM   2263 N  N    . SER   A 1 111 ? 26.178 -13.013 -4.975  1.00 13.20 ?  111 SER   A N    1 
ATOM   2264 C  CA   . SER   A 1 111 ? 27.509 -12.718 -4.455  1.00 13.21 ?  111 SER   A CA   1 
ATOM   2265 C  C    . SER   A 1 111 ? 27.446 -11.667 -3.351  1.00 12.95 ?  111 SER   A C    1 
ATOM   2266 O  O    . SER   A 1 111 ? 28.143 -11.771 -2.335  1.00 13.60 ?  111 SER   A O    1 
ATOM   2267 C  CB   . SER   A 1 111 ? 28.405 -12.228 -5.594  1.00 14.44 ?  111 SER   A CB   1 
ATOM   2268 O  OG   . SER   A 1 111 ? 28.485 -13.204 -6.620  1.00 16.23 ?  111 SER   A OG   1 
ATOM   2269 H  H    . SER   A 1 111 ? 26.077 -12.872 -5.816  1.00 15.80 ?  111 SER   A H    1 
ATOM   2270 H  HA   . SER   A 1 111 ? 27.896 -13.531 -4.089  1.00 15.82 ?  111 SER   A HA   1 
ATOM   2271 H  HB2  . SER   A 1 111 ? 28.023 -11.423 -5.973  1.00 17.29 ?  111 SER   A HB2  1 
ATOM   2272 H  HB3  . SER   A 1 111 ? 29.290 -12.047 -5.244  1.00 17.29 ?  111 SER   A HB3  1 
ATOM   2273 H  HG   . SER   A 1 111 ? 29.002 -12.932 -7.234  1.00 19.44 ?  111 SER   A HG   1 
ATOM   2274 N  N    . ALA   A 1 112 ? 26.605 -10.647 -3.534  1.00 12.79 ?  112 ALA   A N    1 
ATOM   2275 C  CA   . ALA   A 1 112 ? 26.455 -9.610  -2.516  1.00 12.67 ?  112 ALA   A CA   1 
ATOM   2276 C  C    . ALA   A 1 112 ? 25.958 -10.206 -1.203  1.00 12.48 ?  112 ALA   A C    1 
ATOM   2277 O  O    . ALA   A 1 112 ? 26.499 -9.918  -0.129  1.00 12.88 ?  112 ALA   A O    1 
ATOM   2278 C  CB   . ALA   A 1 112 ? 25.498 -8.528  -3.017  1.00 13.11 ?  112 ALA   A CB   1 
ATOM   2279 H  H    . ALA   A 1 112 ? 26.124 -10.528 -4.238  1.00 15.31 ?  112 ALA   A H    1 
ATOM   2280 H  HA   . ALA   A 1 112 ? 27.319 -9.191  -2.358  1.00 15.16 ?  112 ALA   A HA   1 
ATOM   2281 H  HB1  . ALA   A 1 112 ? 25.428 -7.827  -2.343  1.00 15.69 ?  112 ALA   A HB1  1 
ATOM   2282 H  HB2  . ALA   A 1 112 ? 25.840 -8.148  -3.843  1.00 15.69 ?  112 ALA   A HB2  1 
ATOM   2283 H  HB3  . ALA   A 1 112 ? 24.624 -8.919  -3.172  1.00 15.69 ?  112 ALA   A HB3  1 
ATOM   2284 N  N    . TYR   A 1 113 ? 24.925 -11.055 -1.269  1.00 12.59 ?  113 TYR   A N    1 
ATOM   2285 C  CA   . TYR   A 1 113 ? 24.412 -11.662 -0.046  1.00 12.39 ?  113 TYR   A CA   1 
ATOM   2286 C  C    . TYR   A 1 113 ? 25.419 -12.601 0.613   1.00 12.05 ?  113 TYR   A C    1 
ATOM   2287 O  O    . TYR   A 1 113 ? 25.371 -12.781 1.835   1.00 12.65 ?  113 TYR   A O    1 
ATOM   2288 C  CB   . TYR   A 1 113 ? 23.105 -12.406 -0.327  1.00 12.81 ?  113 TYR   A CB   1 
ATOM   2289 C  CG   . TYR   A 1 113 ? 21.883 -11.520 -0.244  1.00 12.85 ?  113 TYR   A CG   1 
ATOM   2290 C  CD1  . TYR   A 1 113 ? 21.509 -10.930 0.958   1.00 13.01 ?  113 TYR   A CD1  1 
ATOM   2291 C  CD2  . TYR   A 1 113 ? 21.077 -11.296 -1.357  1.00 13.20 ?  113 TYR   A CD2  1 
ATOM   2292 C  CE1  . TYR   A 1 113 ? 20.378 -10.139 1.048   1.00 13.51 ?  113 TYR   A CE1  1 
ATOM   2293 C  CE2  . TYR   A 1 113 ? 19.926 -10.499 -1.273  1.00 13.23 ?  113 TYR   A CE2  1 
ATOM   2294 C  CZ   . TYR   A 1 113 ? 19.591 -9.930  -0.066  1.00 13.09 ?  113 TYR   A CZ   1 
ATOM   2295 O  OH   . TYR   A 1 113 ? 18.462 -9.144  0.049   1.00 13.76 ?  113 TYR   A OH   1 
ATOM   2296 H  H    . TYR   A 1 113 ? 24.530 -11.289 -1.994  1.00 15.07 ?  113 TYR   A H    1 
ATOM   2297 H  HA   . TYR   A 1 113 ? 24.224 -10.960 0.586   1.00 14.83 ?  113 TYR   A HA   1 
ATOM   2298 H  HB2  . TYR   A 1 113 ? 23.141 -12.774 -1.225  1.00 15.33 ?  113 TYR   A HB2  1 
ATOM   2299 H  HB3  . TYR   A 1 113 ? 23.006 -13.118 0.319   1.00 15.33 ?  113 TYR   A HB3  1 
ATOM   2300 H  HD1  . TYR   A 1 113 ? 22.028 -11.072 1.715   1.00 15.57 ?  113 TYR   A HD1  1 
ATOM   2301 H  HD2  . TYR   A 1 113 ? 21.298 -11.693 -2.169  1.00 15.80 ?  113 TYR   A HD2  1 
ATOM   2302 H  HE1  . TYR   A 1 113 ? 20.144 -9.755  1.859   1.00 16.18 ?  113 TYR   A HE1  1 
ATOM   2303 H  HE2  . TYR   A 1 113 ? 19.391 -10.360 -2.022  1.00 15.84 ?  113 TYR   A HE2  1 
ATOM   2304 H  HH   . TYR   A 1 113 ? 18.074 -9.103  -0.702  1.00 16.48 ?  113 TYR   A HH   1 
ATOM   2305 N  N    . GLU   A 1 114 ? 26.326 -13.218 -0.158  1.00 12.21 ?  114 GLU   A N    1 
ATOM   2306 C  CA   . GLU   A 1 114 ? 27.308 -14.115 0.454   1.00 12.71 ?  114 GLU   A CA   1 
ATOM   2307 C  C    . GLU   A 1 114 ? 28.149 -13.397 1.504   1.00 12.38 ?  114 GLU   A C    1 
ATOM   2308 O  O    . GLU   A 1 114 ? 28.634 -14.028 2.451   1.00 12.93 ?  114 GLU   A O    1 
ATOM   2309 C  CB   . GLU   A 1 114 ? 28.194 -14.764 -0.623  1.00 12.90 ?  114 GLU   A CB   1 
ATOM   2310 C  CG   . GLU   A 1 114 ? 27.435 -15.804 -1.422  1.00 13.58 ?  114 GLU   A CG   1 
ATOM   2311 C  CD   . GLU   A 1 114 ? 28.155 -16.334 -2.652  1.00 14.16 ?  114 GLU   A CD   1 
ATOM   2312 O  OE1  . GLU   A 1 114 ? 29.115 -15.700 -3.139  1.00 14.47 ?  114 GLU   A OE1  1 
ATOM   2313 O  OE2  . GLU   A 1 114 ? 27.726 -17.395 -3.151  1.00 15.18 -1 114 GLU   A OE2  1 
ATOM   2314 H  H    . GLU   A 1 114 ? 26.396 -13.127 -1.016  1.00 14.61 ?  114 GLU   A H    1 
ATOM   2315 H  HA   . GLU   A 1 114 ? 26.830 -14.825 0.900   1.00 15.21 ?  114 GLU   A HA   1 
ATOM   2316 H  HB2  . GLU   A 1 114 ? 28.508 -14.081 -1.238  1.00 15.44 ?  114 GLU   A HB2  1 
ATOM   2317 H  HB3  . GLU   A 1 114 ? 28.945 -15.202 -0.196  1.00 15.44 ?  114 GLU   A HB3  1 
ATOM   2318 H  HG2  . GLU   A 1 114 ? 27.254 -16.562 -0.847  1.00 16.26 ?  114 GLU   A HG2  1 
ATOM   2319 H  HG3  . GLU   A 1 114 ? 26.594 -15.414 -1.716  1.00 16.26 ?  114 GLU   A HG3  1 
ATOM   2320 N  N    . ASN   A 1 115 ? 28.332 -12.080 1.367   1.00 12.31 ?  115 ASN   A N    1 
ATOM   2321 C  CA   . ASN   A 1 115 ? 29.091 -11.347 2.374   1.00 12.86 ?  115 ASN   A CA   1 
ATOM   2322 C  C    . ASN   A 1 115 ? 28.469 -11.473 3.758   1.00 12.87 ?  115 ASN   A C    1 
ATOM   2323 O  O    . ASN   A 1 115 ? 29.177 -11.398 4.769   1.00 13.64 ?  115 ASN   A O    1 
ATOM   2324 C  CB   . ASN   A 1 115 ? 29.198 -9.870  1.990   1.00 13.06 ?  115 ASN   A CB   1 
ATOM   2325 C  CG   . ASN   A 1 115 ? 30.004 -9.653  0.736   1.00 13.40 ?  115 ASN   A CG   1 
ATOM   2326 O  OD1  . ASN   A 1 115 ? 31.225 -9.746  0.761   1.00 16.57 ?  115 ASN   A OD1  1 
ATOM   2327 N  ND2  . ASN   A 1 115 ? 29.336 -9.350  -0.364  1.00 13.10 ?  115 ASN   A ND2  1 
ATOM   2328 H  H    . ASN   A 1 115 ? 28.035 -11.599 0.718   1.00 14.73 ?  115 ASN   A H    1 
ATOM   2329 H  HA   . ASN   A 1 115 ? 29.987 -11.710 2.421   1.00 15.40 ?  115 ASN   A HA   1 
ATOM   2330 H  HB2  . ASN   A 1 115 ? 28.305 -9.519  1.846   1.00 15.63 ?  115 ASN   A HB2  1 
ATOM   2331 H  HB3  . ASN   A 1 115 ? 29.629 -9.389  2.714   1.00 15.63 ?  115 ASN   A HB3  1 
ATOM   2332 H  HD21 . ASN   A 1 115 ? 29.756 -9.216  -1.103  1.00 15.68 ?  115 ASN   A HD21 1 
ATOM   2333 H  HD22 . ASN   A 1 115 ? 28.477 -9.302  -0.346  1.00 15.68 ?  115 ASN   A HD22 1 
ATOM   2334 N  N    . PHE   A 1 116 ? 27.142 -11.645 3.831   1.00 12.78 ?  116 PHE   A N    1 
ATOM   2335 C  CA   . PHE   A 1 116 ? 26.477 -11.747 5.128   1.00 12.79 ?  116 PHE   A CA   1 
ATOM   2336 C  C    . PHE   A 1 116 ? 26.953 -12.974 5.903   1.00 13.00 ?  116 PHE   A C    1 
ATOM   2337 O  O    . PHE   A 1 116 ? 26.884 -12.990 7.134   1.00 13.52 ?  116 PHE   A O    1 
ATOM   2338 C  CB   . PHE   A 1 116 ? 24.953 -11.881 4.973   1.00 12.82 ?  116 PHE   A CB   1 
ATOM   2339 C  CG   . PHE   A 1 116 ? 24.198 -10.631 4.515   1.00 12.78 ?  116 PHE   A CG   1 
ATOM   2340 C  CD1  . PHE   A 1 116 ? 24.777 -9.607  3.782   1.00 12.86 ?  116 PHE   A CD1  1 
ATOM   2341 C  CD2  . PHE   A 1 116 ? 22.842 -10.535 4.818   1.00 12.94 ?  116 PHE   A CD2  1 
ATOM   2342 C  CE1  . PHE   A 1 116 ? 24.014 -8.524  3.368   1.00 13.05 ?  116 PHE   A CE1  1 
ATOM   2343 C  CE2  . PHE   A 1 116 ? 22.087 -9.451  4.416   1.00 12.91 ?  116 PHE   A CE2  1 
ATOM   2344 C  CZ   . PHE   A 1 116 ? 22.668 -8.454  3.687   1.00 12.66 ?  116 PHE   A CZ   1 
ATOM   2345 H  H    . PHE   A 1 116 ? 26.612 -11.700 3.153   1.00 15.30 ?  116 PHE   A H    1 
ATOM   2346 H  HA   . PHE   A 1 116 ? 26.664 -10.954 5.656   1.00 15.31 ?  116 PHE   A HA   1 
ATOM   2347 H  HB2  . PHE   A 1 116 ? 24.774 -12.583 4.326   1.00 15.35 ?  116 PHE   A HB2  1 
ATOM   2348 H  HB3  . PHE   A 1 116 ? 24.583 -12.146 5.835   1.00 15.35 ?  116 PHE   A HB3  1 
ATOM   2349 H  HD1  . PHE   A 1 116 ? 25.676 -9.664  3.559   1.00 15.39 ?  116 PHE   A HD1  1 
ATOM   2350 H  HD2  . PHE   A 1 116 ? 22.432 -11.222 5.307   1.00 15.49 ?  116 PHE   A HD2  1 
ATOM   2351 H  HE1  . PHE   A 1 116 ? 24.418 -7.844  2.881   1.00 15.62 ?  116 PHE   A HE1  1 
ATOM   2352 H  HE2  . PHE   A 1 116 ? 21.181 -9.411  4.632   1.00 15.45 ?  116 PHE   A HE2  1 
ATOM   2353 H  HZ   . PHE   A 1 116 ? 22.170 -7.719  3.419   1.00 15.15 ?  116 PHE   A HZ   1 
ATOM   2354 N  N    . ASN   A 1 117 ? 27.408 -14.019 5.205   1.00 13.08 ?  117 ASN   A N    1 
ATOM   2355 C  CA   . ASN   A 1 117 ? 27.773 -15.264 5.875   1.00 13.38 ?  117 ASN   A CA   1 
ATOM   2356 C  C    . ASN   A 1 117 ? 29.031 -15.144 6.715   1.00 14.13 ?  117 ASN   A C    1 
ATOM   2357 O  O    . ASN   A 1 117 ? 29.331 -16.065 7.482   1.00 14.79 ?  117 ASN   A O    1 
ATOM   2358 C  CB   . ASN   A 1 117 ? 27.898 -16.391 4.856   1.00 13.53 ?  117 ASN   A CB   1 
ATOM   2359 C  CG   . ASN   A 1 117 ? 26.554 -16.783 4.306   1.00 13.55 ?  117 ASN   A CG   1 
ATOM   2360 O  OD1  . ASN   A 1 117 ? 25.567 -16.795 5.041   1.00 14.54 ?  117 ASN   A OD1  1 
ATOM   2361 N  ND2  . ASN   A 1 117 ? 26.482 -17.032 3.015   1.00 13.13 ?  117 ASN   A ND2  1 
ATOM   2362 H  H    . ASN   A 1 117 ? 27.499 -14.032 4.349   1.00 15.66 ?  117 ASN   A H    1 
ATOM   2363 H  HA   . ASN   A 1 117 ? 27.051 -15.499 6.478   1.00 16.02 ?  117 ASN   A HA   1 
ATOM   2364 H  HB2  . ASN   A 1 117 ? 28.458 -16.092 4.120   1.00 16.20 ?  117 ASN   A HB2  1 
ATOM   2365 H  HB3  . ASN   A 1 117 ? 28.291 -17.163 5.286   1.00 16.20 ?  117 ASN   A HB3  1 
ATOM   2366 H  HD21 . ASN   A 1 117 ? 25.737 -17.257 2.664   1.00 15.71 ?  117 ASN   A HD21 1 
ATOM   2367 H  HD22 . ASN   A 1 117 ? 27.198 -17.001 2.534   1.00 15.71 ?  117 ASN   A HD22 1 
ATOM   2368 N  N    . GLN   A 1 118 ? 29.759 -14.034 6.607   1.00 13.75 ?  118 GLN   A N    1 
ATOM   2369 C  CA   . GLN   A 1 118 ? 30.931 -13.796 7.438   1.00 14.49 ?  118 GLN   A CA   1 
ATOM   2370 C  C    . GLN   A 1 118 ? 30.581 -13.227 8.807   1.00 14.81 ?  118 GLN   A C    1 
ATOM   2371 O  O    . GLN   A 1 118 ? 31.493 -12.940 9.589   1.00 16.07 ?  118 GLN   A O    1 
ATOM   2372 C  CB   . GLN   A 1 118 ? 31.922 -12.883 6.706   1.00 14.68 ?  118 GLN   A CB   1 
ATOM   2373 C  CG   . GLN   A 1 118 ? 32.402 -13.465 5.381   1.00 14.73 ?  118 GLN   A CG   1 
ATOM   2374 C  CD   . GLN   A 1 118 ? 33.256 -14.713 5.564   1.00 14.90 ?  118 GLN   A CD   1 
ATOM   2375 O  OE1  . GLN   A 1 118 ? 34.114 -14.772 6.452   1.00 15.80 ?  118 GLN   A OE1  1 
ATOM   2376 N  NE2  . GLN   A 1 118 ? 33.020 -15.719 4.724   1.00 15.11 ?  118 GLN   A NE2  1 
ATOM   2377 H  H    . GLN   A 1 118 ? 29.586 -13.387 6.055   1.00 16.47 ?  118 GLN   A H    1 
ATOM   2378 H  HA   . GLN   A 1 118 ? 31.371 -14.647 7.581   1.00 17.35 ?  118 GLN   A HA   1 
ATOM   2379 H  HB2  . GLN   A 1 118 ? 31.490 -12.034 6.525   1.00 17.58 ?  118 GLN   A HB2  1 
ATOM   2380 H  HB3  . GLN   A 1 118 ? 32.696 -12.747 7.273   1.00 17.58 ?  118 GLN   A HB3  1 
ATOM   2381 H  HG2  . GLN   A 1 118 ? 31.633 -13.701 4.837   1.00 17.64 ?  118 GLN   A HG2  1 
ATOM   2382 H  HG3  . GLN   A 1 118 ? 32.938 -12.799 4.920   1.00 17.64 ?  118 GLN   A HG3  1 
ATOM   2383 H  HE21 . GLN   A 1 118 ? 32.405 -15.642 4.120   1.00 18.09 ?  118 GLN   A HE21 1 
ATOM   2384 H  HE22 . GLN   A 1 118 ? 33.469 -16.445 4.785   1.00 18.09 ?  118 GLN   A HE22 1 
ATOM   2385 N  N    . HIS   A 1 119 ? 29.290 -13.064 9.110   1.00 14.14 ?  119 HIS   A N    1 
ATOM   2386 C  CA   . HIS   A 1 119 ? 28.828 -12.447 10.348  1.00 14.62 ?  119 HIS   A CA   1 
ATOM   2387 C  C    . HIS   A 1 119 ? 27.687 -13.267 10.921  1.00 14.99 ?  119 HIS   A C    1 
ATOM   2388 O  O    . HIS   A 1 119 ? 26.744 -13.612 10.200  1.00 15.07 ?  119 HIS   A O    1 
ATOM   2389 C  CB   . HIS   A 1 119 ? 28.375 -11.017 10.060  1.00 14.90 ?  119 HIS   A CB   1 
ATOM   2390 C  CG   . HIS   A 1 119 ? 29.457 -10.217 9.435   1.00 15.98 ?  119 HIS   A CG   1 
ATOM   2391 N  ND1  . HIS   A 1 119 ? 30.427 -9.592  10.182  1.00 17.92 ?  119 HIS   A ND1  1 
ATOM   2392 C  CD2  . HIS   A 1 119 ? 29.793 -10.041 8.138   1.00 16.82 ?  119 HIS   A CD2  1 
ATOM   2393 C  CE1  . HIS   A 1 119 ? 31.292 -9.017  9.367   1.00 17.62 ?  119 HIS   A CE1  1 
ATOM   2394 N  NE2  . HIS   A 1 119 ? 30.939 -9.285  8.121   1.00 17.86 ?  119 HIS   A NE2  1 
ATOM   2395 H  H    . HIS   A 1 119 ? 28.642 -13.321 8.599   1.00 16.93 ?  119 HIS   A H    1 
ATOM   2396 H  HA   . HIS   A 1 119 ? 29.551 -12.428 10.993  1.00 17.51 ?  119 HIS   A HA   1 
ATOM   2397 H  HB2  . HIS   A 1 119 ? 27.617 -11.044 9.452   1.00 17.85 ?  119 HIS   A HB2  1 
ATOM   2398 H  HB3  . HIS   A 1 119 ? 28.120 -10.595 10.894  1.00 17.85 ?  119 HIS   A HB3  1 
ATOM   2399 H  HD2  . HIS   A 1 119 ? 29.337 -10.372 7.395   1.00 20.14 ?  119 HIS   A HD2  1 
ATOM   2400 H  HE1  . HIS   A 1 119 ? 32.025 -8.510  9.623   1.00 21.11 ?  119 HIS   A HE1  1 
ATOM   2401 H  HE2  . HIS   A 1 119 ? 31.344 -9.007  7.414   1.00 21.39 ?  119 HIS   A HE2  1 
ATOM   2402 N  N    A GLU   A 1 120 ? 27.764 -13.565 12.220  0.70 15.72 ?  120 GLU   A N    1 
ATOM   2403 N  N    B GLU   A 1 120 ? 27.765 -13.565 12.220  0.30 16.42 ?  120 GLU   A N    1 
ATOM   2404 C  CA   A GLU   A 1 120 ? 26.805 -14.491 12.821  0.70 17.40 ?  120 GLU   A CA   1 
ATOM   2405 C  CA   B GLU   A 1 120 ? 26.802 -14.483 12.823  0.30 18.32 ?  120 GLU   A CA   1 
ATOM   2406 C  C    A GLU   A 1 120 ? 25.393 -13.922 12.888  0.70 16.27 ?  120 GLU   A C    1 
ATOM   2407 C  C    B GLU   A 1 120 ? 25.391 -13.907 12.822  0.30 17.01 ?  120 GLU   A C    1 
ATOM   2408 O  O    A GLU   A 1 120 ? 24.420 -14.689 12.815  0.70 16.34 ?  120 GLU   A O    1 
ATOM   2409 O  O    B GLU   A 1 120 ? 24.418 -14.638 12.596  0.30 17.26 ?  120 GLU   A O    1 
ATOM   2410 C  CB   A GLU   A 1 120 ? 27.263 -14.899 14.222  0.70 21.24 ?  120 GLU   A CB   1 
ATOM   2411 C  CB   B GLU   A 1 120 ? 27.238 -14.851 14.242  0.30 21.96 ?  120 GLU   A CB   1 
ATOM   2412 C  CG   A GLU   A 1 120 ? 28.460 -15.835 14.229  0.70 26.42 ?  120 GLU   A CG   1 
ATOM   2413 C  CG   B GLU   A 1 120 ? 28.442 -15.777 14.297  0.30 25.69 ?  120 GLU   A CG   1 
ATOM   2414 C  CD   A GLU   A 1 120 ? 28.604 -16.591 15.533  0.70 30.99 ?  120 GLU   A CD   1 
ATOM   2415 C  CD   B GLU   A 1 120 ? 28.474 -16.613 15.561  0.30 28.92 ?  120 GLU   A CD   1 
ATOM   2416 O  OE1  A GLU   A 1 120 ? 28.257 -16.023 16.591  0.70 32.62 ?  120 GLU   A OE1  1 
ATOM   2417 O  OE1  B GLU   A 1 120 ? 28.234 -16.054 16.653  0.30 30.01 ?  120 GLU   A OE1  1 
ATOM   2418 O  OE2  A GLU   A 1 120 ? 29.059 -17.755 15.499  0.70 32.82 -1 120 GLU   A OE2  1 
ATOM   2419 O  OE2  B GLU   A 1 120 ? 28.725 -17.833 15.462  0.30 30.16 -1 120 GLU   A OE2  1 
ATOM   2420 H  H    A GLU   A 1 120 ? 28.361 -13.263 12.763  0.70 18.83 ?  120 GLU   A H    1 
ATOM   2421 H  H    B GLU   A 1 120 ? 28.354 -13.252 12.764  0.30 19.66 ?  120 GLU   A H    1 
ATOM   2422 H  HA   A GLU   A 1 120 ? 26.770 -15.295 12.283  0.70 20.84 ?  120 GLU   A HA   1 
ATOM   2423 H  HA   B GLU   A 1 120 ? 26.783 -15.299 12.304  0.30 21.95 ?  120 GLU   A HA   1 
ATOM   2424 H  HB2  A GLU   A 1 120 ? 27.506 -14.104 14.719  0.70 25.44 ?  120 GLU   A HB2  1 
ATOM   2425 H  HB2  B GLU   A 1 120 ? 27.470 -14.040 14.721  0.30 26.31 ?  120 GLU   A HB2  1 
ATOM   2426 H  HB3  A GLU   A 1 120 ? 26.530 -15.354 14.671  0.70 25.44 ?  120 GLU   A HB3  1 
ATOM   2427 H  HB3  B GLU   A 1 120 ? 26.503 -15.298 14.691  0.30 26.31 ?  120 GLU   A HB3  1 
ATOM   2428 H  HG2  A GLU   A 1 120 ? 28.366 -16.476 13.508  0.70 31.67 ?  120 GLU   A HG2  1 
ATOM   2429 H  HG2  B GLU   A 1 120 ? 28.417 -16.376 13.535  0.30 30.79 ?  120 GLU   A HG2  1 
ATOM   2430 H  HG3  A GLU   A 1 120 ? 29.268 -15.316 14.115  0.70 31.67 ?  120 GLU   A HG3  1 
ATOM   2431 H  HG3  B GLU   A 1 120 ? 29.253 -15.245 14.276  0.30 30.79 ?  120 GLU   A HG3  1 
ATOM   2432 N  N    . VAL   A 1 121 ? 25.258 -12.607 13.075  1.00 15.98 ?  121 VAL   A N    1 
ATOM   2433 C  CA   . VAL   A 1 121 ? 23.957 -11.947 13.183  1.00 16.09 ?  121 VAL   A CA   1 
ATOM   2434 C  C    . VAL   A 1 121 ? 24.062 -10.573 12.532  1.00 15.07 ?  121 VAL   A C    1 
ATOM   2435 O  O    . VAL   A 1 121 ? 25.028 -9.842  12.774  1.00 15.46 ?  121 VAL   A O    1 
ATOM   2436 C  CB   . VAL   A 1 121 ? 23.512 -11.782 14.656  1.00 18.83 ?  121 VAL   A CB   1 
ATOM   2437 C  CG1  . VAL   A 1 121 ? 22.116 -11.173 14.726  1.00 19.10 ?  121 VAL   A CG1  1 
ATOM   2438 C  CG2  . VAL   A 1 121 ? 23.520 -13.095 15.412  1.00 20.68 ?  121 VAL   A CG2  1 
ATOM   2439 H  H    A VAL   A 1 121 ? 25.920 -12.064 13.155  0.70 19.13 ?  121 VAL   A H    1 
ATOM   2440 H  H    B VAL   A 1 121 ? 25.921 -12.070 13.187  0.30 19.13 ?  121 VAL   A H    1 
ATOM   2441 H  HA   . VAL   A 1 121 ? 23.286 -12.467 12.719  1.00 19.27 ?  121 VAL   A HA   1 
ATOM   2442 H  HB   . VAL   A 1 121 ? 24.118 -11.177 15.109  1.00 22.56 ?  121 VAL   A HB   1 
ATOM   2443 H  HG11 . VAL   A 1 121 ? 21.793 -11.215 15.643  1.00 22.88 ?  121 VAL   A HG11 1 
ATOM   2444 H  HG12 . VAL   A 1 121 ? 22.153 -10.249 14.436  1.00 22.88 ?  121 VAL   A HG12 1 
ATOM   2445 H  HG13 . VAL   A 1 121 ? 21.518 -11.678 14.150  1.00 22.88 ?  121 VAL   A HG13 1 
ATOM   2446 H  HG21 . VAL   A 1 121 ? 23.177 -12.945 16.316  1.00 24.78 ?  121 VAL   A HG21 1 
ATOM   2447 H  HG22 . VAL   A 1 121 ? 22.946 -13.731 14.955  1.00 24.78 ?  121 VAL   A HG22 1 
ATOM   2448 H  HG23 . VAL   A 1 121 ? 24.423 -13.433 15.460  1.00 24.78 ?  121 VAL   A HG23 1 
ATOM   2449 N  N    . LEU   A 1 122 ? 23.053 -10.196 11.742  1.00 13.69 ?  122 LEU   A N    1 
ATOM   2450 C  CA   . LEU   A 1 122 ? 23.061 -8.904  11.065  1.00 13.50 ?  122 LEU   A CA   1 
ATOM   2451 C  C    . LEU   A 1 122 ? 21.665 -8.308  11.005  1.00 13.63 ?  122 LEU   A C    1 
ATOM   2452 O  O    . LEU   A 1 122 ? 20.673 -9.025  10.865  1.00 14.72 ?  122 LEU   A O    1 
ATOM   2453 C  CB   . LEU   A 1 122 ? 23.488 -9.016  9.599   1.00 14.69 ?  122 LEU   A CB   1 
ATOM   2454 C  CG   . LEU   A 1 122 ? 24.708 -9.855  9.249   1.00 14.80 ?  122 LEU   A CG   1 
ATOM   2455 C  CD1  . LEU   A 1 122 ? 24.300 -11.302 9.015   1.00 15.39 ?  122 LEU   A CD1  1 
ATOM   2456 C  CD2  . LEU   A 1 122 ? 25.402 -9.291  8.025   1.00 14.48 ?  122 LEU   A CD2  1 
ATOM   2457 H  H    . LEU   A 1 122 ? 22.347 -10.670 11.589  1.00 16.39 ?  122 LEU   A H    1 
ATOM   2458 H  HA   . LEU   A 1 122 ? 23.658 -8.288  11.525  1.00 16.16 ?  122 LEU   A HA   1 
ATOM   2459 H  HB2  . LEU   A 1 122 ? 22.756 -9.392  9.101   1.00 17.59 ?  122 LEU   A HB2  1 
ATOM   2460 H  HB3  . LEU   A 1 122 ? 23.679 -8.125  9.273   1.00 17.59 ?  122 LEU   A HB3  1 
ATOM   2461 H  HG   . LEU   A 1 122 ? 25.350 -9.842  9.983   1.00 17.72 ?  122 LEU   A HG   1 
ATOM   2462 H  HD11 . LEU   A 1 122 ? 25.081 -11.830 8.779   1.00 18.44 ?  122 LEU   A HD11 1 
ATOM   2463 H  HD12 . LEU   A 1 122 ? 23.903 -11.655 9.828   1.00 18.44 ?  122 LEU   A HD12 1 
ATOM   2464 H  HD13 . LEU   A 1 122 ? 23.652 -11.336 8.293   1.00 18.44 ?  122 LEU   A HD13 1 
ATOM   2465 H  HD21 . LEU   A 1 122 ? 26.157 -9.863  7.786   1.00 17.34 ?  122 LEU   A HD21 1 
ATOM   2466 H  HD22 . LEU   A 1 122 ? 24.772 -9.262  7.289   1.00 17.34 ?  122 LEU   A HD22 1 
ATOM   2467 H  HD23 . LEU   A 1 122 ? 25.724 -8.398  8.223   1.00 17.34 ?  122 LEU   A HD23 1 
ATOM   2468 N  N    A LEU   A 1 123 ? 21.603 -6.985  11.136  0.70 13.01 ?  123 LEU   A N    1 
ATOM   2469 N  N    B LEU   A 1 123 ? 21.613 -6.979  11.059  0.30 13.31 ?  123 LEU   A N    1 
ATOM   2470 C  CA   A LEU   A 1 123 ? 20.440 -6.190  10.765  0.70 12.53 ?  123 LEU   A CA   1 
ATOM   2471 C  CA   B LEU   A 1 123 ? 20.426 -6.202  10.722  0.30 13.18 ?  123 LEU   A CA   1 
ATOM   2472 C  C    A LEU   A 1 123 ? 20.684 -5.675  9.357   0.70 12.25 ?  123 LEU   A C    1 
ATOM   2473 C  C    B LEU   A 1 123 ? 20.640 -5.620  9.326   0.30 12.61 ?  123 LEU   A C    1 
ATOM   2474 O  O    A LEU   A 1 123 ? 21.769 -5.161  9.078   0.70 12.26 ?  123 LEU   A O    1 
ATOM   2475 O  O    B LEU   A 1 123 ? 21.560 -4.819  9.129   0.30 12.56 ?  123 LEU   A O    1 
ATOM   2476 C  CB   A LEU   A 1 123 ? 20.297 -5.002  11.716  0.70 13.24 ?  123 LEU   A CB   1 
ATOM   2477 C  CB   B LEU   A 1 123 ? 20.243 -5.084  11.750  0.30 13.93 ?  123 LEU   A CB   1 
ATOM   2478 C  CG   A LEU   A 1 123 ? 19.255 -3.940  11.353  0.70 14.07 ?  123 LEU   A CG   1 
ATOM   2479 C  CG   B LEU   A 1 123 ? 19.206 -4.013  11.408  0.30 14.51 ?  123 LEU   A CG   1 
ATOM   2480 C  CD1  A LEU   A 1 123 ? 17.849 -4.534  11.360  0.70 14.78 ?  123 LEU   A CD1  1 
ATOM   2481 C  CD1  B LEU   A 1 123 ? 17.815 -4.625  11.298  0.30 14.79 ?  123 LEU   A CD1  1 
ATOM   2482 C  CD2  A LEU   A 1 123 ? 19.344 -2.745  12.296  0.70 14.94 ?  123 LEU   A CD2  1 
ATOM   2483 C  CD2  B LEU   A 1 123 ? 19.227 -2.888  12.433  0.30 15.09 ?  123 LEU   A CD2  1 
ATOM   2484 H  H    A LEU   A 1 123 ? 22.254 -6.507  11.437  0.70 15.57 ?  123 LEU   A H    1 
ATOM   2485 H  H    B LEU   A 1 123 ? 22.280 -6.488  11.300  0.30 15.94 ?  123 LEU   A H    1 
ATOM   2486 H  HA   A LEU   A 1 123 ? 19.636 -6.730  10.778  0.70 15.00 ?  123 LEU   A HA   1 
ATOM   2487 H  HA   B LEU   A 1 123 ? 19.640 -6.770  10.725  0.30 15.78 ?  123 LEU   A HA   1 
ATOM   2488 H  HB2  A LEU   A 1 123 ? 20.057 -5.348  12.589  0.70 15.85 ?  123 LEU   A HB2  1 
ATOM   2489 H  HB2  B LEU   A 1 123 ? 19.978 -5.483  12.598  0.30 16.68 ?  123 LEU   A HB2  1 
ATOM   2490 H  HB3  A LEU   A 1 123 ? 21.152 -4.553  11.770  0.70 15.85 ?  123 LEU   A HB3  1 
ATOM   2491 H  HB3  B LEU   A 1 123 ? 21.096 -4.633  11.868  0.30 16.68 ?  123 LEU   A HB3  1 
ATOM   2492 H  HG   A LEU   A 1 123 ? 19.428 -3.615  10.456  0.70 16.85 ?  123 LEU   A HG   1 
ATOM   2493 H  HG   B LEU   A 1 123 ? 19.427 -3.625  10.549  0.30 17.37 ?  123 LEU   A HG   1 
ATOM   2494 H  HD11 A LEU   A 1 123 ? 17.208 -3.836  11.157  0.70 17.69 ?  123 LEU   A HD11 1 
ATOM   2495 H  HD11 B LEU   A 1 123 ? 17.172 -3.916  11.142  0.30 17.71 ?  123 LEU   A HD11 1 
ATOM   2496 H  HD12 A LEU   A 1 123 ? 17.799 -5.234  10.688  0.70 17.69 ?  123 LEU   A HD12 1 
ATOM   2497 H  HD12 B LEU   A 1 123 ? 17.803 -5.250  10.556  0.30 17.71 ?  123 LEU   A HD12 1 
ATOM   2498 H  HD13 A LEU   A 1 123 ? 17.668 -4.907  12.237  0.70 17.69 ?  123 LEU   A HD13 1 
ATOM   2499 H  HD13 B LEU   A 1 123 ? 17.605 -5.087  12.124  0.30 17.71 ?  123 LEU   A HD13 1 
ATOM   2500 H  HD21 A LEU   A 1 123 ? 18.671 -2.092  12.044  0.70 17.90 ?  123 LEU   A HD21 1 
ATOM   2501 H  HD21 B LEU   A 1 123 ? 18.560 -2.228  12.187  0.30 18.07 ?  123 LEU   A HD21 1 
ATOM   2502 H  HD22 A LEU   A 1 123 ? 19.181 -3.049  13.204  0.70 17.90 ?  123 LEU   A HD22 1 
ATOM   2503 H  HD22 B LEU   A 1 123 ? 19.025 -3.253  13.308  0.30 18.07 ?  123 LEU   A HD22 1 
ATOM   2504 H  HD23 A LEU   A 1 123 ? 20.227 -2.356  12.229  0.70 17.90 ?  123 LEU   A HD23 1 
ATOM   2505 H  HD23 B LEU   A 1 123 ? 20.108 -2.483  12.438  0.30 18.07 ?  123 LEU   A HD23 1 
ATOM   2506 N  N    A ALA   A 1 124 ? 19.691 -5.790  8.476   0.70 11.92 ?  124 ALA   A N    1 
ATOM   2507 N  N    B ALA   A 1 124 ? 19.809 -6.012  8.363   0.30 11.98 ?  124 ALA   A N    1 
ATOM   2508 C  CA   A ALA   A 1 124 ? 19.968 -5.511  7.076   0.70 11.80 ?  124 ALA   A CA   1 
ATOM   2509 C  CA   B ALA   A 1 124 ? 20.100 -5.747  6.961   0.30 11.96 ?  124 ALA   A CA   1 
ATOM   2510 C  C    A ALA   A 1 124 ? 18.732 -5.052  6.323   0.70 11.86 ?  124 ALA   A C    1 
ATOM   2511 C  C    B ALA   A 1 124 ? 18.868 -5.323  6.176   0.30 11.41 ?  124 ALA   A C    1 
ATOM   2512 O  O    A ALA   A 1 124 ? 17.604 -5.415  6.684   0.70 12.79 ?  124 ALA   A O    1 
ATOM   2513 O  O    B ALA   A 1 124 ? 17.734 -5.622  6.566   0.30 11.69 ?  124 ALA   A O    1 
ATOM   2514 C  CB   A ALA   A 1 124 ? 20.545 -6.741  6.369   0.70 11.85 ?  124 ALA   A CB   1 
ATOM   2515 C  CB   B ALA   A 1 124 ? 20.722 -6.972  6.278   0.30 12.31 ?  124 ALA   A CB   1 
ATOM   2516 H  H    A ALA   A 1 124 ? 18.874 -6.009  8.657   0.70 14.27 ?  124 ALA   A H    1 
ATOM   2517 H  H    B ALA   A 1 124 ? 19.073 -6.438  8.504   0.30 14.34 ?  124 ALA   A H    1 
ATOM   2518 H  HA   A ALA   A 1 124 ? 20.636 -4.805  7.039   0.70 14.12 ?  124 ALA   A HA   1 
ATOM   2519 H  HA   B ALA   A 1 124 ? 20.733 -5.023  6.911   0.30 14.31 ?  124 ALA   A HA   1 
ATOM   2520 H  HB1  A ALA   A 1 124 ? 20.727 -6.515  5.442   0.70 14.18 ?  124 ALA   A HB1  1 
ATOM   2521 H  HB1  B ALA   A 1 124 ? 20.899 -6.761  5.346   0.30 14.74 ?  124 ALA   A HB1  1 
ATOM   2522 H  HB2  A ALA   A 1 124 ? 21.373 -6.998  6.811   0.70 14.18 ?  124 ALA   A HB2  1 
ATOM   2523 H  HB2  B ALA   A 1 124 ? 21.553 -7.192  6.728   0.30 14.74 ?  124 ALA   A HB2  1 
ATOM   2524 H  HB3  A ALA   A 1 124 ? 19.904 -7.461  6.418   0.70 14.18 ?  124 ALA   A HB3  1 
ATOM   2525 H  HB3  B ALA   A 1 124 ? 20.105 -7.718  6.336   0.30 14.74 ?  124 ALA   A HB3  1 
ATOM   2526 N  N    A PRO   A 1 125 ? 18.921 -4.283  5.259   0.70 11.62 ?  125 PRO   A N    1 
ATOM   2527 N  N    B PRO   A 1 125 ? 19.069 -4.625  5.037   0.30 10.83 ?  125 PRO   A N    1 
ATOM   2528 C  CA   A PRO   A 1 125 ? 17.868 -4.059  4.273   0.70 12.20 ?  125 PRO   A CA   1 
ATOM   2529 C  CA   B PRO   A 1 125 ? 17.971 -4.353  4.104   0.30 11.17 ?  125 PRO   A CA   1 
ATOM   2530 C  C    A PRO   A 1 125 ? 17.939 -5.160  3.221   0.70 12.18 ?  125 PRO   A C    1 
ATOM   2531 C  C    B PRO   A 1 125 ? 17.991 -5.310  2.923   0.30 11.26 ?  125 PRO   A C    1 
ATOM   2532 O  O    A PRO   A 1 125 ? 18.904 -5.927  3.154   0.70 12.35 ?  125 PRO   A O    1 
ATOM   2533 O  O    B PRO   A 1 125 ? 18.978 -6.021  2.710   0.30 11.14 ?  125 PRO   A O    1 
ATOM   2534 C  CB   A PRO   A 1 125 ? 18.310 -2.726  3.654   0.70 12.97 ?  125 PRO   A CB   1 
ATOM   2535 C  CB   B PRO   A 1 125 ? 18.296 -2.936  3.629   0.30 11.38 ?  125 PRO   A CB   1 
ATOM   2536 C  CG   A PRO   A 1 125 ? 19.823 -2.895  3.584   0.70 13.65 ?  125 PRO   A CG   1 
ATOM   2537 C  CG   B PRO   A 1 125 ? 19.814 -2.955  3.550   0.30 11.18 ?  125 PRO   A CG   1 
ATOM   2538 C  CD   A PRO   A 1 125 ? 20.177 -3.600  4.882   0.70 12.71 ?  125 PRO   A CD   1 
ATOM   2539 C  CD   B PRO   A 1 125 ? 20.299 -3.923  4.625   0.30 10.08 ?  125 PRO   A CD   1 
ATOM   2540 H  HA   A PRO   A 1 125 ? 16.981 -4.004  4.674   0.70 14.61 ?  125 PRO   A HA   1 
ATOM   2541 H  HA   B PRO   A 1 125 ? 17.111 -4.380  4.546   0.30 13.37 ?  125 PRO   A HA   1 
ATOM   2542 H  HB2  A PRO   A 1 125 ? 17.912 -2.623  2.774   0.70 15.52 ?  125 PRO   A HB2  1 
ATOM   2543 H  HB2  B PRO   A 1 125 ? 17.898 -2.779  2.754   0.30 13.62 ?  125 PRO   A HB2  1 
ATOM   2544 H  HB3  A PRO   A 1 125 ? 18.054 -1.993  4.240   0.70 15.52 ?  125 PRO   A HB3  1 
ATOM   2545 H  HB3  B PRO   A 1 125 ? 17.979 -2.292  4.278   0.30 13.62 ?  125 PRO   A HB3  1 
ATOM   2546 H  HG2  A PRO   A 1 125 ? 20.061 -3.443  2.817   0.70 16.34 ?  125 PRO   A HG2  1 
ATOM   2547 H  HG2  B PRO   A 1 125 ? 20.085 -3.260  2.671   0.30 13.38 ?  125 PRO   A HG2  1 
ATOM   2548 H  HG3  A PRO   A 1 125 ? 20.250 -2.026  3.532   0.70 16.34 ?  125 PRO   A HG3  1 
ATOM   2549 H  HG3  B PRO   A 1 125 ? 20.150 -2.062  3.719   0.30 13.38 ?  125 PRO   A HG3  1 
ATOM   2550 H  HD2  A PRO   A 1 125 ? 20.888 -4.240  4.741   0.70 15.21 ?  125 PRO   A HD2  1 
ATOM   2551 H  HD2  B PRO   A 1 125 ? 20.942 -4.546  4.251   0.30 12.05 ?  125 PRO   A HD2  1 
ATOM   2552 H  HD3  A PRO   A 1 125 ? 20.415 -2.949  5.565   0.70 15.21 ?  125 PRO   A HD3  1 
ATOM   2553 H  HD3  B PRO   A 1 125 ? 20.673 -3.430  5.372   0.30 12.05 ?  125 PRO   A HD3  1 
ATOM   2554 N  N    A LEU   A 1 126 ? 16.909 -5.209  2.378   0.70 12.95 ?  126 LEU   A N    1 
ATOM   2555 N  N    B LEU   A 1 126 ? 16.920 -5.312  2.134   0.30 11.72 ?  126 LEU   A N    1 
ATOM   2556 C  CA   A LEU   A 1 126 ? 16.970 -6.070  1.204   0.70 13.20 ?  126 LEU   A CA   1 
ATOM   2557 C  CA   B LEU   A 1 126 ? 16.877 -6.077  0.892   0.30 12.00 ?  126 LEU   A CA   1 
ATOM   2558 C  C    A LEU   A 1 126 ? 17.923 -5.466  0.176   0.70 13.03 ?  126 LEU   A C    1 
ATOM   2559 C  C    B LEU   A 1 126 ? 17.808 -5.432  -0.126  0.30 11.66 ?  126 LEU   A C    1 
ATOM   2560 O  O    A LEU   A 1 126 ? 17.756 -4.319  -0.244  0.70 13.59 ?  126 LEU   A O    1 
ATOM   2561 O  O    B LEU   A 1 126 ? 17.509 -4.365  -0.673  0.30 11.63 ?  126 LEU   A O    1 
ATOM   2562 C  CB   A LEU   A 1 126 ? 15.585 -6.289  0.606   0.70 14.08 ?  126 LEU   A CB   1 
ATOM   2563 C  CB   B LEU   A 1 126 ? 15.447 -6.110  0.372   0.30 12.57 ?  126 LEU   A CB   1 
ATOM   2564 C  CG   A LEU   A 1 126 ? 14.681 -7.299  1.319   0.70 14.82 ?  126 LEU   A CG   1 
ATOM   2565 C  CG   B LEU   A 1 126 ? 14.501 -6.905  1.265   0.30 12.50 ?  126 LEU   A CG   1 
ATOM   2566 C  CD1  A LEU   A 1 126 ? 13.261 -7.190  0.804   0.70 15.67 ?  126 LEU   A CD1  1 
ATOM   2567 C  CD1  B LEU   A 1 126 ? 13.089 -6.727  0.773   0.30 13.05 ?  126 LEU   A CD1  1 
ATOM   2568 C  CD2  A LEU   A 1 126 ? 15.202 -8.727  1.145   0.70 14.56 ?  126 LEU   A CD2  1 
ATOM   2569 C  CD2  B LEU   A 1 126 ? 14.889 -8.378  1.273   0.30 12.35 ?  126 LEU   A CD2  1 
ATOM   2570 H  H    A LEU   A 1 126 ? 16.182 -4.748  2.453   0.70 15.50 ?  126 LEU   A H    1 
ATOM   2571 H  H    B LEU   A 1 126 ? 16.201 -4.869  2.294   0.30 14.03 ?  126 LEU   A H    1 
ATOM   2572 H  HA   A LEU   A 1 126 ? 17.323 -6.922  1.460   0.70 15.80 ?  126 LEU   A HA   1 
ATOM   2573 H  HA   B LEU   A 1 126 ? 17.169 -6.989  1.052   0.30 14.36 ?  126 LEU   A HA   1 
ATOM   2574 H  HB2  A LEU   A 1 126 ? 15.109 -5.441  0.604   0.70 16.86 ?  126 LEU   A HB2  1 
ATOM   2575 H  HB2  B LEU   A 1 126 ? 15.106 -5.202  0.319   0.30 15.04 ?  126 LEU   A HB2  1 
ATOM   2576 H  HB3  A LEU   A 1 126 ? 15.688 -6.595  -0.309  0.70 16.86 ?  126 LEU   A HB3  1 
ATOM   2577 H  HB3  B LEU   A 1 126 ? 15.433 -6.518  -0.507  0.30 15.04 ?  126 LEU   A HB3  1 
ATOM   2578 H  HG   A LEU   A 1 126 ? 14.673 -7.103  2.266   0.70 17.74 ?  126 LEU   A HG   1 
ATOM   2579 H  HG   B LEU   A 1 126 ? 14.554 -6.567  2.175   0.30 14.97 ?  126 LEU   A HG   1 
ATOM   2580 H  HD11 A LEU   A 1 126 ? 12.708 -7.844  1.261   0.70 18.77 ?  126 LEU   A HD11 1 
ATOM   2581 H  HD11 B LEU   A 1 126 ? 12.490 -7.235  1.342   0.30 15.62 ?  126 LEU   A HD11 1 
ATOM   2582 H  HD12 A LEU   A 1 126 ? 12.932 -6.296  0.982   0.70 18.77 ?  126 LEU   A HD12 1 
ATOM   2583 H  HD12 B LEU   A 1 126 ? 12.860 -5.786  0.804   0.30 15.62 ?  126 LEU   A HD12 1 
ATOM   2584 H  HD13 A LEU   A 1 126 ? 13.256 -7.362  -0.151  0.70 18.77 ?  126 LEU   A HD13 1 
ATOM   2585 H  HD13 B LEU   A 1 126 ? 13.033 -7.052  -0.140  0.30 15.62 ?  126 LEU   A HD13 1 
ATOM   2586 H  HD21 A LEU   A 1 126 ? 14.569 -9.346  1.539   0.70 17.44 ?  126 LEU   A HD21 1 
ATOM   2587 H  HD21 B LEU   A 1 126 ? 14.164 -8.891  1.656   0.30 14.78 ?  126 LEU   A HD21 1 
ATOM   2588 H  HD22 A LEU   A 1 126 ? 15.303 -8.915  0.198   0.70 17.44 ?  126 LEU   A HD22 1 
ATOM   2589 H  HD22 B LEU   A 1 126 ? 15.053 -8.661  0.360   0.30 14.78 ?  126 LEU   A HD22 1 
ATOM   2590 H  HD23 A LEU   A 1 126 ? 16.062 -8.807  1.590   0.70 17.44 ?  126 LEU   A HD23 1 
ATOM   2591 H  HD23 B LEU   A 1 126 ? 15.694 -8.489  1.803   0.30 14.78 ?  126 LEU   A HD23 1 
ATOM   2592 N  N    A LEU   A 1 127 ? 18.929 -6.238  -0.219  0.70 12.71 ?  127 LEU   A N    1 
ATOM   2593 N  N    B LEU   A 1 127 ? 18.938 -6.078  -0.384  0.30 11.12 ?  127 LEU   A N    1 
ATOM   2594 C  CA   A LEU   A 1 127 ? 19.927 -5.751  -1.160  0.70 12.68 ?  127 LEU   A CA   1 
ATOM   2595 C  CA   B LEU   A 1 127 ? 19.915 -5.511  -1.297  0.30 11.11 ?  127 LEU   A CA   1 
ATOM   2596 C  C    A LEU   A 1 127 ? 19.302 -5.524  -2.528  0.70 12.33 ?  127 LEU   A C    1 
ATOM   2597 C  C    B LEU   A 1 127 ? 19.376 -5.468  -2.727  0.30 11.37 ?  127 LEU   A C    1 
ATOM   2598 O  O    A LEU   A 1 127 ? 18.456 -6.299  -2.988  0.70 12.83 ?  127 LEU   A O    1 
ATOM   2599 O  O    B LEU   A 1 127 ? 18.566 -6.302  -3.146  0.30 11.73 ?  127 LEU   A O    1 
ATOM   2600 C  CB   A LEU   A 1 127 ? 21.074 -6.753  -1.288  0.70 12.81 ?  127 LEU   A CB   1 
ATOM   2601 C  CB   B LEU   A 1 127 ? 21.210 -6.319  -1.246  0.30 11.25 ?  127 LEU   A CB   1 
ATOM   2602 C  CG   A LEU   A 1 127 ? 21.917 -6.977  -0.036  0.70 12.97 ?  127 LEU   A CG   1 
ATOM   2603 C  CG   B LEU   A 1 127 ? 21.961 -6.301  0.088   0.30 12.07 ?  127 LEU   A CG   1 
ATOM   2604 C  CD1  A LEU   A 1 127 ? 23.011 -7.988  -0.319  0.70 13.29 ?  127 LEU   A CD1  1 
ATOM   2605 C  CD1  B LEU   A 1 127 ? 23.082 -7.323  0.063   0.30 12.47 ?  127 LEU   A CD1  1 
ATOM   2606 C  CD2  A LEU   A 1 127 ? 22.526 -5.676  0.455   0.70 13.49 ?  127 LEU   A CD2  1 
ATOM   2607 C  CD2  B LEU   A 1 127 ? 22.503 -4.907  0.382   0.30 12.61 ?  127 LEU   A CD2  1 
ATOM   2608 H  H    A LEU   A 1 127 ? 19.055 -7.040  0.046   0.70 15.21 ?  127 LEU   A H    1 
ATOM   2609 H  H    B LEU   A 1 127 ? 19.164 -6.832  -0.027  0.30 13.30 ?  127 LEU   A H    1 
ATOM   2610 H  HA   A LEU   A 1 127 ? 20.285 -4.909  -0.850  0.70 15.18 ?  127 LEU   A HA   1 
ATOM   2611 H  HA   B LEU   A 1 127 ? 20.113 -4.603  -1.015  0.30 13.30 ?  127 LEU   A HA   1 
ATOM   2612 H  HB2  A LEU   A 1 127 ? 20.701 -7.612  -1.544  0.70 15.33 ?  127 LEU   A HB2  1 
ATOM   2613 H  HB2  B LEU   A 1 127 ? 21.000 -7.243  -1.445  0.30 13.46 ?  127 LEU   A HB2  1 
ATOM   2614 H  HB3  A LEU   A 1 127 ? 21.672 -6.444  -1.988  0.70 15.33 ?  127 LEU   A HB3  1 
ATOM   2615 H  HB3  B LEU   A 1 127 ? 21.810 -5.968  -1.919  0.30 13.46 ?  127 LEU   A HB3  1 
ATOM   2616 H  HG   A LEU   A 1 127 ? 21.353 -7.332  0.667   0.70 15.53 ?  127 LEU   A HG   1 
ATOM   2617 H  HG   B LEU   A 1 127 ? 21.350 -6.542  0.802   0.30 14.44 ?  127 LEU   A HG   1 
ATOM   2618 H  HD11 A LEU   A 1 127 ? 23.499 -8.165  0.504   0.70 15.91 ?  127 LEU   A HD11 1 
ATOM   2619 H  HD11 B LEU   A 1 127 ? 23.587 -7.257  0.888   0.30 14.93 ?  127 LEU   A HD11 1 
ATOM   2620 H  HD12 A LEU   A 1 127 ? 22.607 -8.811  -0.642  0.70 15.91 ?  127 LEU   A HD12 1 
ATOM   2621 H  HD12 B LEU   A 1 127 ? 22.697 -8.210  -0.021  0.30 14.93 ?  127 LEU   A HD12 1 
ATOM   2622 H  HD13 A LEU   A 1 127 ? 23.611 -7.631  -0.988  0.70 15.91 ?  127 LEU   A HD13 1 
ATOM   2623 H  HD13 B LEU   A 1 127 ? 23.658 -7.139  -0.694  0.30 14.93 ?  127 LEU   A HD13 1 
ATOM   2624 H  HD21 A LEU   A 1 127 ? 23.175 -5.875  1.150   0.70 16.15 ?  127 LEU   A HD21 1 
ATOM   2625 H  HD21 B LEU   A 1 127 ? 23.056 -4.945  1.179   0.30 15.09 ?  127 LEU   A HD21 1 
ATOM   2626 H  HD22 A LEU   A 1 127 ? 22.971 -5.236  -0.290  0.70 16.15 ?  127 LEU   A HD22 1 
ATOM   2627 H  HD22 B LEU   A 1 127 ? 23.036 -4.610  -0.374  0.30 15.09 ?  127 LEU   A HD22 1 
ATOM   2628 H  HD23 A LEU   A 1 127 ? 21.827 -5.109  0.804   0.70 16.15 ?  127 LEU   A HD23 1 
ATOM   2629 H  HD23 B LEU   A 1 127 ? 21.761 -4.301  0.522   0.30 15.09 ?  127 LEU   A HD23 1 
ATOM   2630 N  N    A SER   A 1 128 ? 19.740 -4.450  -3.176  0.70 12.18 ?  128 SER   A N    1 
ATOM   2631 N  N    B SER   A 1 128 ? 19.844 -4.464  -3.467  0.30 11.32 ?  128 SER   A N    1 
ATOM   2632 C  CA   A SER   A 1 128 ? 19.333 -4.036  -4.512  0.70 12.04 ?  128 SER   A CA   1 
ATOM   2633 C  CA   B SER   A 1 128 ? 19.499 -4.213  -4.864  0.30 11.00 ?  128 SER   A CA   1 
ATOM   2634 C  C    A SER   A 1 128 ? 17.876 -3.586  -4.596  0.70 12.12 ?  128 SER   A C    1 
ATOM   2635 C  C    B SER   A 1 128 ? 18.069 -3.718  -5.071  0.30 11.12 ?  128 SER   A C    1 
ATOM   2636 O  O    A SER   A 1 128 ? 17.404 -3.288  -5.692  0.70 12.98 ?  128 SER   A O    1 
ATOM   2637 O  O    B SER   A 1 128 ? 17.713 -3.336  -6.189  0.30 11.28 ?  128 SER   A O    1 
ATOM   2638 C  CB   A SER   A 1 128 ? 19.671 -5.066  -5.598  0.70 12.08 ?  128 SER   A CB   1 
ATOM   2639 C  CB   B SER   A 1 128 ? 19.815 -5.419  -5.754  0.30 11.22 ?  128 SER   A CB   1 
ATOM   2640 O  OG   A SER   A 1 128 ? 21.079 -5.267  -5.678  0.70 12.63 ?  128 SER   A OG   1 
ATOM   2641 O  OG   B SER   A 1 128 ? 21.215 -5.634  -5.817  0.30 11.33 ?  128 SER   A OG   1 
ATOM   2642 H  H    A SER   A 1 128 ? 20.325 -3.909  -2.843  0.70 14.58 ?  128 SER   A H    1 
ATOM   2643 H  H    B SER   A 1 128 ? 20.411 -3.898  -3.162  0.30 13.54 ?  128 SER   A H    1 
ATOM   2644 H  HA   A SER   A 1 128 ? 19.855 -3.252  -4.730  0.70 14.41 ?  128 SER   A HA   1 
ATOM   2645 H  HA   B SER   A 1 128 ? 20.072 -3.501  -5.166  0.30 13.16 ?  128 SER   A HA   1 
ATOM   2646 H  HB2  A SER   A 1 128 ? 19.234 -5.903  -5.386  0.70 14.46 ?  128 SER   A HB2  1 
ATOM   2647 H  HB2  B SER   A 1 128 ? 19.385 -6.209  -5.400  0.30 13.43 ?  128 SER   A HB2  1 
ATOM   2648 H  HB3  A SER   A 1 128 ? 19.356 -4.734  -6.456  0.70 14.46 ?  128 SER   A HB3  1 
ATOM   2649 H  HB3  B SER   A 1 128 ? 19.487 -5.237  -6.653  0.30 13.43 ?  128 SER   A HB3  1 
ATOM   2650 H  HG   A SER   A 1 128 ? 21.464 -4.542  -5.840  0.70 15.11 ?  128 SER   A HG   1 
ATOM   2651 H  HG   B SER   A 1 128 ? 21.593 -4.949  -6.121  0.30 13.56 ?  128 SER   A HG   1 
ATOM   2652 N  N    A ALA   A 1 129 ? 17.166 -3.500  -3.472  0.70 12.57 ?  129 ALA   A N    1 
ATOM   2653 N  N    B ALA   A 1 129 ? 17.256 -3.698  -4.013  0.30 11.30 ?  129 ALA   A N    1 
ATOM   2654 C  CA   A ALA   A 1 129 ? 15.803 -2.991  -3.458  0.70 12.91 ?  129 ALA   A CA   1 
ATOM   2655 C  CA   B ALA   A 1 129 ? 15.888 -3.197  -4.086  0.30 11.74 ?  129 ALA   A CA   1 
ATOM   2656 C  C    A ALA   A 1 129 ? 15.819 -1.462  -3.506  0.70 13.11 ?  129 ALA   A C    1 
ATOM   2657 C  C    B ALA   A 1 129 ? 15.872 -1.700  -3.760  0.30 12.72 ?  129 ALA   A C    1 
ATOM   2658 O  O    A ALA   A 1 129 ? 16.875 -0.825  -3.586  0.70 13.48 ?  129 ALA   A O    1 
ATOM   2659 O  O    B ALA   A 1 129 ? 16.910 -1.034  -3.783  0.30 12.78 ?  129 ALA   A O    1 
ATOM   2660 C  CB   A ALA   A 1 129 ? 15.046 -3.527  -2.241  0.70 13.50 ?  129 ALA   A CB   1 
ATOM   2661 C  CB   B ALA   A 1 129 ? 14.978 -4.034  -3.179  0.30 11.51 ?  129 ALA   A CB   1 
ATOM   2662 H  H    A ALA   A 1 129 ? 17.462 -3.727  -2.698  0.70 15.04 ?  129 ALA   A H    1 
ATOM   2663 H  H    B ALA   A 1 129 ? 17.477 -3.988  -3.231  0.30 13.52 ?  129 ALA   A H    1 
ATOM   2664 H  HA   A ALA   A 1 129 ? 15.347 -3.302  -4.249  0.70 15.46 ?  129 ALA   A HA   1 
ATOM   2665 H  HA   B ALA   A 1 129 ? 15.570 -3.305  -4.990  0.30 14.05 ?  129 ALA   A HA   1 
ATOM   2666 H  HB1  A ALA   A 1 129 ? 14.142 -3.179  -2.254  0.70 16.16 ?  129 ALA   A HB1  1 
ATOM   2667 H  HB1  B ALA   A 1 129 ? 14.071 -3.701  -3.255  0.30 13.77 ?  129 ALA   A HB1  1 
ATOM   2668 H  HB2  A ALA   A 1 129 ? 15.030 -4.496  -2.283  0.70 16.16 ?  129 ALA   A HB2  1 
ATOM   2669 H  HB2  B ALA   A 1 129 ? 15.016 -4.961  -3.464  0.30 13.77 ?  129 ALA   A HB2  1 
ATOM   2670 H  HB3  A ALA   A 1 129 ? 15.500 -3.239  -1.432  0.70 16.16 ?  129 ALA   A HB3  1 
ATOM   2671 H  HB3  B ALA   A 1 129 ? 15.286 -3.957  -2.263  0.30 13.77 ?  129 ALA   A HB3  1 
ATOM   2672 N  N    A GLY   A 1 130 ? 14.633 -0.866  -3.476  0.70 14.09 ?  130 GLY   A N    1 
ATOM   2673 N  N    B GLY   A 1 130 ? 14.696 -1.153  -3.464  0.30 13.37 ?  130 GLY   A N    1 
ATOM   2674 C  CA   A GLY   A 1 130 ? 14.554 0.585   -3.510  0.70 14.37 ?  130 GLY   A CA   1 
ATOM   2675 C  CA   B GLY   A 1 130 ? 14.615 0.265   -3.161  0.30 13.56 ?  130 GLY   A CA   1 
ATOM   2676 C  C    A GLY   A 1 130 ? 15.218 1.151   -4.751  0.70 14.21 ?  130 GLY   A C    1 
ATOM   2677 C  C    B GLY   A 1 130 ? 15.063 1.086   -4.352  0.30 13.34 ?  130 GLY   A C    1 
ATOM   2678 O  O    A GLY   A 1 130 ? 14.990 0.686   -5.875  0.70 14.63 ?  130 GLY   A O    1 
ATOM   2679 O  O    B GLY   A 1 130 ? 14.762 0.762   -5.506  0.30 13.35 ?  130 GLY   A O    1 
ATOM   2680 H  H    A GLY   A 1 130 ? 13.873 -1.272  -3.434  0.70 16.87 ?  130 GLY   A H    1 
ATOM   2681 H  H    B GLY   A 1 130 ? 13.948 -1.576  -3.446  0.30 16.01 ?  130 GLY   A H    1 
ATOM   2682 H  HA2  A GLY   A 1 130 ? 13.621 0.858   -3.501  0.70 17.20 ?  130 GLY   A HA2  1 
ATOM   2683 H  HA2  B GLY   A 1 130 ? 13.700 0.495   -2.926  0.30 16.23 ?  130 GLY   A HA2  1 
ATOM   2684 H  HA3  A GLY   A 1 130 ? 14.990 0.953   -2.726  0.70 17.20 ?  130 GLY   A HA3  1 
ATOM   2685 H  HA3  B GLY   A 1 130 ? 15.190 0.471   -2.409  0.30 16.23 ?  130 GLY   A HA3  1 
ATOM   2686 N  N    A ILE   A 1 131 ? 16.061 2.170   -4.548  0.70 13.84 ?  131 ILE   A N    1 
ATOM   2687 N  N    B ILE   A 1 131 ? 15.814 2.158   -4.078  0.30 13.28 ?  131 ILE   A N    1 
ATOM   2688 C  CA   A ILE   A 1 131 ? 16.637 2.918   -5.665  0.70 13.43 ?  131 ILE   A CA   1 
ATOM   2689 C  CA   B ILE   A 1 131 ? 16.332 3.002   -5.150  0.30 13.46 ?  131 ILE   A CA   1 
ATOM   2690 C  C    A ILE   A 1 131 ? 17.642 2.124   -6.482  0.70 13.25 ?  131 ILE   A C    1 
ATOM   2691 C  C    B ILE   A 1 131 ? 17.335 2.280   -6.041  0.30 13.13 ?  131 ILE   A C    1 
ATOM   2692 O  O    A ILE   A 1 131 ? 18.056 2.599   -7.545  0.70 13.61 ?  131 ILE   A O    1 
ATOM   2693 O  O    B ILE   A 1 131 ? 17.743 2.831   -7.068  0.30 12.62 ?  131 ILE   A O    1 
ATOM   2694 C  CB   A ILE   A 1 131 ? 17.239 4.274   -5.239  0.70 14.31 ?  131 ILE   A CB   1 
ATOM   2695 C  CB   B ILE   A 1 131 ? 16.937 4.312   -4.600  0.30 14.25 ?  131 ILE   A CB   1 
ATOM   2696 C  CG1  A ILE   A 1 131 ? 18.505 4.096   -4.391  0.70 15.62 ?  131 ILE   A CG1  1 
ATOM   2697 C  CG1  B ILE   A 1 131 ? 18.173 4.027   -3.742  0.30 14.96 ?  131 ILE   A CG1  1 
ATOM   2698 C  CG2  A ILE   A 1 131 ? 16.204 5.110   -4.497  0.70 14.67 ?  131 ILE   A CG2  1 
ATOM   2699 C  CG2  B ILE   A 1 131 ? 15.892 5.087   -3.801  0.30 14.56 ?  131 ILE   A CG2  1 
ATOM   2700 C  CD1  A ILE   A 1 131 ? 19.145 5.426   -3.973  0.70 16.55 ?  131 ILE   A CD1  1 
ATOM   2701 C  CD1  B ILE   A 1 131 ? 18.894 5.281   -3.266  0.30 15.46 ?  131 ILE   A CD1  1 
ATOM   2702 H  H    A ILE   A 1 131 ? 16.310 2.448   -3.775  0.70 16.57 ?  131 ILE   A H    1 
ATOM   2703 H  H    B ILE   A 1 131 ? 16.026 2.417   -3.285  0.30 15.90 ?  131 ILE   A H    1 
ATOM   2704 H  HA   A ILE   A 1 131 ? 15.916 3.120   -6.272  0.70 16.08 ?  131 ILE   A HA   1 
ATOM   2705 H  HA   B ILE   A 1 131 ? 15.582 3.259   -5.710  0.30 16.12 ?  131 ILE   A HA   1 
ATOM   2706 H  HB   A ILE   A 1 131 ? 17.484 4.754   -6.045  0.70 17.13 ?  131 ILE   A HB   1 
ATOM   2707 H  HB   B ILE   A 1 131 ? 17.204 4.863   -5.352  0.30 17.06 ?  131 ILE   A HB   1 
ATOM   2708 H  HG12 A ILE   A 1 131 ? 18.277 3.608   -3.586  0.70 18.71 ?  131 ILE   A HG12 1 
ATOM   2709 H  HG12 B ILE   A 1 131 ? 17.899 3.527   -2.958  0.30 17.91 ?  131 ILE   A HG12 1 
ATOM   2710 H  HG13 A ILE   A 1 131 ? 19.164 3.603   -4.903  0.70 18.71 ?  131 ILE   A HG13 1 
ATOM   2711 H  HG13 B ILE   A 1 131 ? 18.804 3.507   -4.261  0.30 17.91 ?  131 ILE   A HG13 1 
ATOM   2712 H  HG21 A ILE   A 1 131 ? 16.525 6.020   -4.424  0.70 17.56 ?  131 ILE   A HG21 1 
ATOM   2713 H  HG21 B ILE   A 1 131 ? 16.266 5.941   -3.531  0.30 17.43 ?  131 ILE   A HG21 1 
ATOM   2714 H  HG22 A ILE   A 1 131 ? 15.371 5.090   -4.994  0.70 17.56 ?  131 ILE   A HG22 1 
ATOM   2715 H  HG22 B ILE   A 1 131 ? 15.114 5.234   -4.361  0.30 17.43 ?  131 ILE   A HG22 1 
ATOM   2716 H  HG23 A ILE   A 1 131 ? 16.069 4.731   -3.614  0.70 17.56 ?  131 ILE   A HG23 1 
ATOM   2717 H  HG23 B ILE   A 1 131 ? 15.645 4.571   -3.018  0.30 17.43 ?  131 ILE   A HG23 1 
ATOM   2718 H  HD11 A ILE   A 1 131 ? 20.010 5.247   -3.574  0.70 19.83 ?  131 ILE   A HD11 1 
ATOM   2719 H  HD11 B ILE   A 1 131 ? 19.736 5.023   -2.859  0.30 18.51 ?  131 ILE   A HD11 1 
ATOM   2720 H  HD12 A ILE   A 1 131 ? 19.251 5.985   -4.758  0.70 19.83 ?  131 ILE   A HD12 1 
ATOM   2721 H  HD12 B ILE   A 1 131 ? 19.060 5.858   -4.029  0.30 18.51 ?  131 ILE   A HD12 1 
ATOM   2722 H  HD13 A ILE   A 1 131 ? 18.568 5.867   -3.329  0.70 19.83 ?  131 ILE   A HD13 1 
ATOM   2723 H  HD13 B ILE   A 1 131 ? 18.340 5.741   -2.618  0.30 18.51 ?  131 ILE   A HD13 1 
ATOM   2724 N  N    A PHE   A 1 132 ? 18.039 0.928   -6.031  0.70 12.71 ?  132 PHE   A N    1 
ATOM   2725 N  N    B PHE   A 1 132 ? 17.746 1.062   -5.680  0.30 13.09 ?  132 PHE   A N    1 
ATOM   2726 C  CA   A PHE   A 1 132 ? 18.899 0.070   -6.843  0.70 13.14 ?  132 PHE   A CA   1 
ATOM   2727 C  CA   B PHE   A 1 132 ? 18.669 0.307   -6.520  0.30 13.37 ?  132 PHE   A CA   1 
ATOM   2728 C  C    A PHE   A 1 132 ? 18.123 -0.703  -7.911  0.70 14.02 ?  132 PHE   A C    1 
ATOM   2729 C  C    B PHE   A 1 132 ? 17.983 -0.386  -7.696  0.30 13.98 ?  132 PHE   A C    1 
ATOM   2730 O  O    A PHE   A 1 132 ? 18.745 -1.359  -8.753  0.70 15.02 ?  132 PHE   A O    1 
ATOM   2731 O  O    B PHE   A 1 132 ? 18.675 -0.826  -8.621  0.30 14.65 ?  132 PHE   A O    1 
ATOM   2732 C  CB   A PHE   A 1 132 ? 19.702 -0.900  -5.965  0.70 12.51 ?  132 PHE   A CB   1 
ATOM   2733 C  CB   B PHE   A 1 132 ? 19.468 -0.695  -5.680  0.30 12.98 ?  132 PHE   A CB   1 
ATOM   2734 C  CG   A PHE   A 1 132 ? 20.905 -0.283  -5.277  0.70 12.40 ?  132 PHE   A CG   1 
ATOM   2735 C  CG   B PHE   A 1 132 ? 20.699 -0.109  -5.029  0.30 12.88 ?  132 PHE   A CG   1 
ATOM   2736 C  CD1  A PHE   A 1 132 ? 20.765 0.752   -4.366  0.70 12.99 ?  132 PHE   A CD1  1 
ATOM   2737 C  CD1  B PHE   A 1 132 ? 20.590 0.818   -4.004  0.30 13.27 ?  132 PHE   A CD1  1 
ATOM   2738 C  CD2  A PHE   A 1 132 ? 22.174 -0.788  -5.510  0.70 13.16 ?  132 PHE   A CD2  1 
ATOM   2739 C  CD2  B PHE   A 1 132 ? 21.964 -0.504  -5.432  0.30 12.96 ?  132 PHE   A CD2  1 
ATOM   2740 C  CE1  A PHE   A 1 132 ? 21.884 1.294   -3.729  0.70 13.38 ?  132 PHE   A CE1  1 
ATOM   2741 C  CE1  B PHE   A 1 132 ? 21.723 1.352   -3.404  0.30 13.65 ?  132 PHE   A CE1  1 
ATOM   2742 C  CE2  A PHE   A 1 132 ? 23.281 -0.262  -4.876  0.70 13.78 ?  132 PHE   A CE2  1 
ATOM   2743 C  CE2  B PHE   A 1 132 ? 23.098 0.024   -4.835  0.30 13.45 ?  132 PHE   A CE2  1 
ATOM   2744 C  CZ   A PHE   A 1 132 ? 23.136 0.786   -3.984  0.70 13.30 ?  132 PHE   A CZ   1 
ATOM   2745 C  CZ   B PHE   A 1 132 ? 22.975 0.953   -3.819  0.30 13.45 ?  132 PHE   A CZ   1 
ATOM   2746 H  H    A PHE   A 1 132 ? 17.832 0.593   -5.262  0.70 15.21 ?  132 PHE   A H    1 
ATOM   2747 H  H    B PHE   A 1 132 ? 17.508 0.660   -4.958  0.30 15.67 ?  132 PHE   A H    1 
ATOM   2748 H  HA   A PHE   A 1 132 ? 19.542 0.630   -7.300  0.70 15.73 ?  132 PHE   A HA   1 
ATOM   2749 H  HA   B PHE   A 1 132 ? 19.306 0.936   -6.890  0.30 16.00 ?  132 PHE   A HA   1 
ATOM   2750 H  HB2  A PHE   A 1 132 ? 19.124 -1.246  -5.271  0.70 14.97 ?  132 PHE   A HB2  1 
ATOM   2751 H  HB2  B PHE   A 1 132 ? 18.900 -1.041  -4.977  0.30 15.54 ?  132 PHE   A HB2  1 
ATOM   2752 H  HB3  A PHE   A 1 132 ? 20.030 -1.632  -6.515  0.70 14.97 ?  132 PHE   A HB3  1 
ATOM   2753 H  HB3  B PHE   A 1 132 ? 19.755 -1.418  -6.256  0.30 15.54 ?  132 PHE   A HB3  1 
ATOM   2754 H  HD1  A PHE   A 1 132 ? 19.924 1.103   -4.184  0.70 15.55 ?  132 PHE   A HD1  1 
ATOM   2755 H  HD1  B PHE   A 1 132 ? 19.748 1.093   -3.720  0.30 15.88 ?  132 PHE   A HD1  1 
ATOM   2756 H  HD2  A PHE   A 1 132 ? 22.285 -1.491  -6.108  0.70 15.75 ?  132 PHE   A HD2  1 
ATOM   2757 H  HD2  B PHE   A 1 132 ? 22.053 -1.127  -6.117  0.30 15.51 ?  132 PHE   A HD2  1 
ATOM   2758 H  HE1  A PHE   A 1 132 ? 21.783 1.996   -3.123  0.70 16.02 ?  132 PHE   A HE1  1 
ATOM   2759 H  HE1  B PHE   A 1 132 ? 21.637 1.976   -2.720  0.30 16.34 ?  132 PHE   A HE1  1 
ATOM   2760 H  HE2  A PHE   A 1 132 ? 24.130 -0.604  -5.054  0.70 16.50 ?  132 PHE   A HE2  1 
ATOM   2761 H  HE2  B PHE   A 1 132 ? 23.942 -0.247  -5.119  0.30 16.10 ?  132 PHE   A HE2  1 
ATOM   2762 H  HZ   A PHE   A 1 132 ? 23.883 1.146   -3.557  0.70 15.92 ?  132 PHE   A HZ   1 
ATOM   2763 H  HZ   B PHE   A 1 132 ? 23.736 1.308   -3.417  0.30 16.10 ?  132 PHE   A HZ   1 
ATOM   2764 N  N    A GLY   A 1 133 ? 16.791 -0.648  -7.897  0.70 14.45 ?  133 GLY   A N    1 
ATOM   2765 N  N    B GLY   A 1 133 ? 16.654 -0.502  -7.694  0.30 14.06 ?  133 GLY   A N    1 
ATOM   2766 C  CA   A GLY   A 1 133 ? 16.004 -1.027  -9.052  0.70 15.00 ?  133 GLY   A CA   1 
ATOM   2767 C  CA   B GLY   A 1 133 ? 15.913 -0.817  -8.898  0.30 14.39 ?  133 GLY   A CA   1 
ATOM   2768 C  C    A GLY   A 1 133 ? 15.655 -2.491  -9.214  0.70 15.26 ?  133 GLY   A C    1 
ATOM   2769 C  C    B GLY   A 1 133 ? 15.429 -2.245  -9.051  0.30 14.45 ?  133 GLY   A C    1 
ATOM   2770 O  O    A GLY   A 1 133 ? 14.998 -2.831  -10.204 0.70 15.67 ?  133 GLY   A O    1 
ATOM   2771 O  O    B GLY   A 1 133 ? 14.611 -2.497  -9.945  0.30 14.35 ?  133 GLY   A O    1 
ATOM   2772 H  H    A GLY   A 1 133 ? 16.322 -0.392  -7.221  0.70 17.30 ?  133 GLY   A H    1 
ATOM   2773 H  H    B GLY   A 1 133 ? 16.160 -0.395  -6.998  0.30 16.84 ?  133 GLY   A H    1 
ATOM   2774 H  HA2  A GLY   A 1 133 ? 15.170 -0.537  -9.028  0.70 17.96 ?  133 GLY   A HA2  1 
ATOM   2775 H  HA2  B GLY   A 1 133 ? 15.129 -0.253  -8.934  0.30 17.24 ?  133 GLY   A HA2  1 
ATOM   2776 H  HA3  A GLY   A 1 133 ? 16.482 -0.759  -9.851  0.70 17.96 ?  133 GLY   A HA3  1 
ATOM   2777 H  HA3  B GLY   A 1 133 ? 16.463 -0.613  -9.672  0.30 17.24 ?  133 GLY   A HA3  1 
ATOM   2778 N  N    A ALA   A 1 134 ? 16.059 -3.371  -8.299  0.70 14.68 ?  134 ALA   A N    1 
ATOM   2779 N  N    B ALA   A 1 134 ? 15.897 -3.187  -8.238  0.30 14.59 ?  134 ALA   A N    1 
ATOM   2780 C  CA   A ALA   A 1 134 ? 15.721 -4.781  -8.438  0.70 15.12 ?  134 ALA   A CA   1 
ATOM   2781 C  CA   B ALA   A 1 134 ? 15.472 -4.568  -8.413  0.30 14.65 ?  134 ALA   A CA   1 
ATOM   2782 C  C    A ALA   A 1 134 ? 14.348 -5.078  -7.835  0.70 15.42 ?  134 ALA   A C    1 
ATOM   2783 C  C    B ALA   A 1 134 ? 14.188 -4.851  -7.638  0.30 14.52 ?  134 ALA   A C    1 
ATOM   2784 O  O    A ALA   A 1 134 ? 13.779 -4.280  -7.086  0.70 16.45 ?  134 ALA   A O    1 
ATOM   2785 O  O    B ALA   A 1 134 ? 13.813 -4.129  -6.711  0.30 14.97 ?  134 ALA   A O    1 
ATOM   2786 C  CB   A ALA   A 1 134 ? 16.794 -5.659  -7.791  0.70 15.97 ?  134 ALA   A CB   1 
ATOM   2787 C  CB   B ALA   A 1 134 ? 16.561 -5.547  -7.980  0.30 15.01 ?  134 ALA   A CB   1 
ATOM   2788 H  H    A ALA   A 1 134 ? 16.532 -3.176  -7.602  0.70 17.57 ?  134 ALA   A H    1 
ATOM   2789 H  H    B ALA   A 1 134 ? 16.453 -3.054  -7.593  0.30 17.47 ?  134 ALA   A H    1 
ATOM   2790 H  HA   A ALA   A 1 134 ? 15.695 -5.001  -9.381  0.70 18.11 ?  134 ALA   A HA   1 
ATOM   2791 H  HA   B ALA   A 1 134 ? 15.294 -4.717  -9.355  0.30 17.55 ?  134 ALA   A HA   1 
ATOM   2792 H  HB1  A ALA   A 1 134 ? 16.553 -6.589  -7.910  0.70 19.12 ?  134 ALA   A HB1  1 
ATOM   2793 H  HB1  B ALA   A 1 134 ? 16.246 -6.452  -8.140  0.30 17.97 ?  134 ALA   A HB1  1 
ATOM   2794 H  HB2  A ALA   A 1 134 ? 17.650 -5.483  -8.222  0.70 19.12 ?  134 ALA   A HB2  1 
ATOM   2795 H  HB2  B ALA   A 1 134 ? 17.360 -5.378  -8.501  0.30 17.97 ?  134 ALA   A HB2  1 
ATOM   2796 H  HB3  A ALA   A 1 134 ? 16.853 -5.446  -6.848  0.70 19.12 ?  134 ALA   A HB3  1 
ATOM   2797 H  HB3  B ALA   A 1 134 ? 16.742 -5.420  -7.038  0.30 17.97 ?  134 ALA   A HB3  1 
ATOM   2798 N  N    A ASP   A 1 135 ? 13.815 -6.243  -8.189  0.70 15.71 ?  135 ASP   A N    1 
ATOM   2799 N  N    B ASP   A 1 135 ? 13.519 -5.925  -8.039  0.30 14.60 ?  135 ASP   A N    1 
ATOM   2800 C  CA   A ASP   A 1 135 ? 12.546 -6.715  -7.639  0.70 16.35 ?  135 ASP   A CA   1 
ATOM   2801 C  CA   B ASP   A 1 135 ? 12.277 -6.351  -7.409  0.30 14.88 ?  135 ASP   A CA   1 
ATOM   2802 C  C    A ASP   A 1 135 ? 12.767 -7.166  -6.201  0.70 15.88 ?  135 ASP   A C    1 
ATOM   2803 C  C    B ASP   A 1 135 ? 12.564 -6.849  -5.998  0.30 14.55 ?  135 ASP   A C    1 
ATOM   2804 O  O    A ASP   A 1 135 ? 13.538 -8.105  -5.972  0.70 15.57 ?  135 ASP   A O    1 
ATOM   2805 O  O    B ASP   A 1 135 ? 13.322 -7.816  -5.837  0.30 14.49 ?  135 ASP   A O    1 
ATOM   2806 C  CB   A ASP   A 1 135 ? 12.056 -7.888  -8.489  0.70 18.60 ?  135 ASP   A CB   1 
ATOM   2807 C  CB   B ASP   A 1 135 ? 11.672 -7.475  -8.243  0.30 15.60 ?  135 ASP   A CB   1 
ATOM   2808 C  CG   A ASP   A 1 135 ? 10.791 -8.550  -7.942  0.70 20.69 ?  135 ASP   A CG   1 
ATOM   2809 C  CG   B ASP   A 1 135 ? 10.299 -7.899  -7.748  0.30 16.48 ?  135 ASP   A CG   1 
ATOM   2810 O  OD1  A ASP   A 1 135 ? 10.236 -8.092  -6.922  0.70 20.68 ?  135 ASP   A OD1  1 
ATOM   2811 O  OD1  B ASP   A 1 135 ? 9.898  -7.475  -6.642  0.30 16.64 ?  135 ASP   A OD1  1 
ATOM   2812 O  OD2  A ASP   A 1 135 ? 10.354 -9.548  -8.550  0.70 23.02 -1 135 ASP   A OD2  1 
ATOM   2813 O  OD2  B ASP   A 1 135 ? 9.619  -8.657  -8.469  0.30 17.21 -1 135 ASP   A OD2  1 
ATOM   2814 H  H    A ASP   A 1 135 ? 14.174 -6.784  -8.753  0.70 18.81 ?  135 ASP   A H    1 
ATOM   2815 H  H    B ASP   A 1 135 ? 13.765 -6.430  -8.687  0.30 17.48 ?  135 ASP   A H    1 
ATOM   2816 H  HA   A ASP   A 1 135 ? 11.891 -6.001  -7.673  0.70 19.58 ?  135 ASP   A HA   1 
ATOM   2817 H  HA   B ASP   A 1 135 ? 11.647 -5.610  -7.386  0.30 17.81 ?  135 ASP   A HA   1 
ATOM   2818 H  HB2  A ASP   A 1 135 ? 11.868 -7.568  -9.385  0.70 22.28 ?  135 ASP   A HB2  1 
ATOM   2819 H  HB2  B ASP   A 1 135 ? 11.595 -7.176  -9.166  0.30 18.68 ?  135 ASP   A HB2  1 
ATOM   2820 H  HB3  A ASP   A 1 135 ? 12.747 -8.565  -8.516  0.70 22.28 ?  135 ASP   A HB3  1 
ATOM   2821 H  HB3  B ASP   A 1 135 ? 12.261 -8.248  -8.200  0.30 18.68 ?  135 ASP   A HB3  1 
ATOM   2822 N  N    A PRO   A 1 136 ? 12.132 -6.536  -5.209  0.70 15.83 ?  136 PRO   A N    1 
ATOM   2823 N  N    B PRO   A 1 136 ? 11.996 -6.235  -4.956  0.30 14.51 ?  136 PRO   A N    1 
ATOM   2824 C  CA   A PRO   A 1 136 ? 12.364 -6.953  -3.814  0.70 16.31 ?  136 PRO   A CA   1 
ATOM   2825 C  CA   B PRO   A 1 136 ? 12.267 -6.717  -3.590  0.30 14.92 ?  136 PRO   A CA   1 
ATOM   2826 C  C    A PRO   A 1 136 ? 11.922 -8.373  -3.503  0.70 15.75 ?  136 PRO   A C    1 
ATOM   2827 C  C    B PRO   A 1 136 ? 11.853 -8.160  -3.357  0.30 14.93 ?  136 PRO   A C    1 
ATOM   2828 O  O    A PRO   A 1 136 ? 12.519 -9.014  -2.629  0.70 15.71 ?  136 PRO   A O    1 
ATOM   2829 O  O    B PRO   A 1 136 ? 12.430 -8.827  -2.488  0.30 14.59 ?  136 PRO   A O    1 
ATOM   2830 C  CB   A PRO   A 1 136 ? 11.575 -5.916  -3.004  0.70 17.26 ?  136 PRO   A CB   1 
ATOM   2831 C  CB   B PRO   A 1 136 ? 11.471 -5.739  -2.713  0.30 15.28 ?  136 PRO   A CB   1 
ATOM   2832 C  CG   A PRO   A 1 136 ? 10.533 -5.408  -3.955  0.70 18.17 ?  136 PRO   A CG   1 
ATOM   2833 C  CG   B PRO   A 1 136 ? 10.414 -5.184  -3.620  0.30 15.63 ?  136 PRO   A CG   1 
ATOM   2834 C  CD   A PRO   A 1 136 ? 11.176 -5.421  -5.305  0.70 17.05 ?  136 PRO   A CD   1 
ATOM   2835 C  CD   B PRO   A 1 136 ? 11.078 -5.084  -4.959  0.30 14.96 ?  136 PRO   A CD   1 
ATOM   2836 H  HA   A PRO   A 1 136 ? 13.305 -6.870  -3.594  0.70 19.54 ?  136 PRO   A HA   1 
ATOM   2837 H  HA   B PRO   A 1 136 ? 13.211 -6.618  -3.385  0.30 17.87 ?  136 PRO   A HA   1 
ATOM   2838 H  HB2  A PRO   A 1 136 ? 11.163 -6.343  -2.236  0.70 20.67 ?  136 PRO   A HB2  1 
ATOM   2839 H  HB2  B PRO   A 1 136 ? 11.074 -6.207  -1.963  0.30 18.30 ?  136 PRO   A HB2  1 
ATOM   2840 H  HB3  A PRO   A 1 136 ? 12.167 -5.201  -2.724  0.70 20.67 ?  136 PRO   A HB3  1 
ATOM   2841 H  HB3  B PRO   A 1 136 ? 12.056 -5.030  -2.410  0.30 18.30 ?  136 PRO   A HB3  1 
ATOM   2842 H  HG2  A PRO   A 1 136 ? 9.762  -5.996  -3.939  0.70 21.76 ?  136 PRO   A HG2  1 
ATOM   2843 H  HG2  B PRO   A 1 136 ? 9.660  -5.794  -3.658  0.30 18.72 ?  136 PRO   A HG2  1 
ATOM   2844 H  HG3  A PRO   A 1 136 ? 10.281 -4.505  -3.710  0.70 21.76 ?  136 PRO   A HG3  1 
ATOM   2845 H  HG3  B PRO   A 1 136 ? 10.134 -4.309  -3.310  0.30 18.72 ?  136 PRO   A HG3  1 
ATOM   2846 H  HD2  A PRO   A 1 136 ? 10.515 -5.606  -5.994  0.70 20.42 ?  136 PRO   A HD2  1 
ATOM   2847 H  HD2  B PRO   A 1 136 ? 10.420 -5.174  -5.669  0.30 17.91 ?  136 PRO   A HD2  1 
ATOM   2848 H  HD3  A PRO   A 1 136 ? 11.643 -4.589  -5.475  0.70 20.42 ?  136 PRO   A HD3  1 
ATOM   2849 H  HD3  B PRO   A 1 136 ? 11.572 -4.250  -5.038  0.30 17.91 ?  136 PRO   A HD3  1 
ATOM   2850 N  N    A ILE   A 1 137 ? 10.876 -8.880  -4.159  0.70 15.93 ?  137 ILE   A N    1 
ATOM   2851 N  N    B ILE   A 1 137 ? 10.862 -8.659  -4.100  0.30 15.45 ?  137 ILE   A N    1 
ATOM   2852 C  CA   A ILE   A 1 137 ? 10.505 -10.282 -3.971  0.70 16.15 ?  137 ILE   A CA   1 
ATOM   2853 C  CA   B ILE   A 1 137 ? 10.462 -10.059 -3.972  0.30 16.04 ?  137 ILE   A CA   1 
ATOM   2854 C  C    A ILE   A 1 137 ? 11.666 -11.184 -4.364  0.70 15.94 ?  137 ILE   A C    1 
ATOM   2855 C  C    B ILE   A 1 137 ? 11.619 -10.975 -4.351  0.30 16.06 ?  137 ILE   A C    1 
ATOM   2856 O  O    A ILE   A 1 137 ? 11.985 -12.160 -3.672  0.70 16.26 ?  137 ILE   A O    1 
ATOM   2857 O  O    B ILE   A 1 137 ? 11.900 -11.967 -3.667  0.30 16.40 ?  137 ILE   A O    1 
ATOM   2858 C  CB   A ILE   A 1 137 ? 9.223  -10.611 -4.759  0.70 17.69 ?  137 ILE   A CB   1 
ATOM   2859 C  CB   B ILE   A 1 137 ? 9.211  -10.333 -4.831  0.30 16.84 ?  137 ILE   A CB   1 
ATOM   2860 C  CG1  A ILE   A 1 137 ? 8.035  -9.800  -4.225  0.70 19.37 ?  137 ILE   A CG1  1 
ATOM   2861 C  CG1  B ILE   A 1 137 ? 8.052  -9.418  -4.416  0.30 17.52 ?  137 ILE   A CG1  1 
ATOM   2862 C  CG2  A ILE   A 1 137 ? 8.917  -12.103 -4.682  0.70 18.19 ?  137 ILE   A CG2  1 
ATOM   2863 C  CG2  B ILE   A 1 137 ? 8.803  -11.799 -4.737  0.30 16.95 ?  137 ILE   A CG2  1 
ATOM   2864 C  CD1  A ILE   A 1 137 ? 6.741  -10.015 -4.986  0.70 20.95 ?  137 ILE   A CD1  1 
ATOM   2865 C  CD1  B ILE   A 1 137 ? 6.794  -9.606  -5.248  0.30 18.02 ?  137 ILE   A CD1  1 
ATOM   2866 H  H    A ILE   A 1 137 ? 10.373 -8.446  -4.702  0.70 19.07 ?  137 ILE   A H    1 
ATOM   2867 H  H    B ILE   A 1 137 ? 10.411 -8.208  -4.677  0.30 18.50 ?  137 ILE   A H    1 
ATOM   2868 H  HA   A ILE   A 1 137 ? 10.320 -10.439 -3.035  0.70 19.34 ?  137 ILE   A HA   1 
ATOM   2869 H  HA   B ILE   A 1 137 ? 10.230 -10.235 -3.049  0.30 19.21 ?  137 ILE   A HA   1 
ATOM   2870 H  HB   A ILE   A 1 137 ? 9.356  -10.374 -5.689  0.70 21.19 ?  137 ILE   A HB   1 
ATOM   2871 H  HB   B ILE   A 1 137 ? 9.427  -10.138 -5.755  0.30 20.17 ?  137 ILE   A HB   1 
ATOM   2872 H  HG12 A ILE   A 1 137 ? 7.880  -10.041 -3.299  0.70 23.21 ?  137 ILE   A HG12 1 
ATOM   2873 H  HG12 B ILE   A 1 137 ? 7.823  -9.598  -3.491  0.30 20.99 ?  137 ILE   A HG12 1 
ATOM   2874 H  HG13 A ILE   A 1 137 ? 8.255  -8.852  -4.281  0.70 23.21 ?  137 ILE   A HG13 1 
ATOM   2875 H  HG13 B ILE   A 1 137 ? 8.328  -8.493  -4.513  0.30 20.99 ?  137 ILE   A HG13 1 
ATOM   2876 H  HG21 A ILE   A 1 137 ? 8.176  -12.310 -5.271  0.70 21.78 ?  137 ILE   A HG21 1 
ATOM   2877 H  HG21 B ILE   A 1 137 ? 8.001  -11.944 -5.263  0.30 20.31 ?  137 ILE   A HG21 1 
ATOM   2878 H  HG22 A ILE   A 1 137 ? 9.688  -12.609 -4.964  0.70 21.78 ?  137 ILE   A HG22 1 
ATOM   2879 H  HG22 B ILE   A 1 137 ? 9.520  -12.350 -5.085  0.30 20.31 ?  137 ILE   A HG22 1 
ATOM   2880 H  HG23 A ILE   A 1 137 ? 8.686  -12.325 -3.768  0.70 21.78 ?  137 ILE   A HG23 1 
ATOM   2881 H  HG23 B ILE   A 1 137 ? 8.634  -12.019 -3.809  0.30 20.31 ?  137 ILE   A HG23 1 
ATOM   2882 H  HD11 A ILE   A 1 137 ? 6.012  -9.740  -4.416  0.70 25.11 ?  137 ILE   A HD11 1 
ATOM   2883 H  HD11 B ILE   A 1 137 ? 6.197  -8.858  -5.095  0.30 21.59 ?  137 ILE   A HD11 1 
ATOM   2884 H  HD12 A ILE   A 1 137 ? 6.756  -9.479  -5.795  0.70 25.11 ?  137 ILE   A HD12 1 
ATOM   2885 H  HD12 B ILE   A 1 137 ? 7.039  -9.648  -6.186  0.30 21.59 ?  137 ILE   A HD12 1 
ATOM   2886 H  HD13 A ILE   A 1 137 ? 6.633  -10.950 -5.211  0.70 25.11 ?  137 ILE   A HD13 1 
ATOM   2887 H  HD13 B ILE   A 1 137 ? 6.360  -10.435 -4.985  0.30 21.59 ?  137 ILE   A HD13 1 
ATOM   2888 N  N    A HIS   A 1 138 ? 12.315 -10.870 -5.486  0.70 16.10 ?  138 HIS   A N    1 
ATOM   2889 N  N    B HIS   A 1 138 ? 12.303 -10.656 -5.450  0.30 15.94 ?  138 HIS   A N    1 
ATOM   2890 C  CA   A HIS   A 1 138 ? 13.504 -11.613 -5.883  0.70 16.10 ?  138 HIS   A CA   1 
ATOM   2891 C  CA   B HIS   A 1 138 ? 13.424 -11.473 -5.903  0.30 15.51 ?  138 HIS   A CA   1 
ATOM   2892 C  C    A HIS   A 1 138 ? 14.629 -11.445 -4.867  0.70 15.45 ?  138 HIS   A C    1 
ATOM   2893 C  C    B HIS   A 1 138 ? 14.588 -11.408 -4.920  0.30 15.13 ?  138 HIS   A C    1 
ATOM   2894 O  O    A HIS   A 1 138 ? 15.288 -12.426 -4.496  0.70 15.59 ?  138 HIS   A O    1 
ATOM   2895 O  O    B HIS   A 1 138 ? 15.232 -12.425 -4.635  0.30 15.27 ?  138 HIS   A O    1 
ATOM   2896 C  CB   A HIS   A 1 138 ? 13.950 -11.189 -7.281  0.70 17.02 ?  138 HIS   A CB   1 
ATOM   2897 C  CB   B HIS   A 1 138 ? 13.849 -10.998 -7.292  0.30 15.63 ?  138 HIS   A CB   1 
ATOM   2898 C  CG   A HIS   A 1 138 ? 15.194 -11.879 -7.743  0.70 17.88 ?  138 HIS   A CG   1 
ATOM   2899 C  CG   B HIS   A 1 138 ? 15.144 -11.580 -7.759  0.30 15.98 ?  138 HIS   A CG   1 
ATOM   2900 N  ND1  A HIS   A 1 138 ? 15.257 -13.241 -7.951  0.70 18.82 ?  138 HIS   A ND1  1 
ATOM   2901 N  ND1  B HIS   A 1 138 ? 15.298 -12.917 -8.053  0.30 16.44 ?  138 HIS   A ND1  1 
ATOM   2902 C  CD2  A HIS   A 1 138 ? 16.430 -11.399 -8.016  0.70 18.35 ?  138 HIS   A CD2  1 
ATOM   2903 C  CD2  B HIS   A 1 138 ? 16.348 -11.003 -7.984  0.30 16.06 ?  138 HIS   A CD2  1 
ATOM   2904 C  CE1  A HIS   A 1 138 ? 16.475 -13.567 -8.345  0.70 19.25 ?  138 HIS   A CE1  1 
ATOM   2905 C  CE1  B HIS   A 1 138 ? 16.542 -13.140 -8.437  0.30 16.41 ?  138 HIS   A CE1  1 
ATOM   2906 N  NE2  A HIS   A 1 138 ? 17.207 -12.469 -8.390  0.70 18.87 ?  138 HIS   A NE2  1 
ATOM   2907 N  NE2  B HIS   A 1 138 ? 17.200 -11.995 -8.404  0.30 16.24 ?  138 HIS   A NE2  1 
ATOM   2908 H  H    A HIS   A 1 138 ? 12.082 -10.243 -6.035  0.70 19.28 ?  138 HIS   A H    1 
ATOM   2909 H  H    B HIS   A 1 138 ? 12.135 -9.974  -5.950  0.30 19.08 ?  138 HIS   A H    1 
ATOM   2910 H  HA   A HIS   A 1 138 ? 13.280 -12.554 -5.926  0.70 19.28 ?  138 HIS   A HA   1 
ATOM   2911 H  HA   B HIS   A 1 138 ? 13.136 -12.395 -5.975  0.30 18.57 ?  138 HIS   A HA   1 
ATOM   2912 H  HB2  A HIS   A 1 138 ? 13.240 -11.396 -7.915  0.70 20.38 ?  138 HIS   A HB2  1 
ATOM   2913 H  HB2  B HIS   A 1 138 ? 13.163 -11.249 -7.932  0.30 18.71 ?  138 HIS   A HB2  1 
ATOM   2914 H  HB3  A HIS   A 1 138 ? 14.119 -10.233 -7.283  0.70 20.38 ?  138 HIS   A HB3  1 
ATOM   2915 H  HB3  B HIS   A 1 138 ? 13.945 -10.033 -7.278  0.30 18.71 ?  138 HIS   A HB3  1 
ATOM   2916 H  HD1  A HIS   A 1 138 ? 14.604 -13.790 -7.849  0.70 22.55 ?  138 HIS   A HD1  1 
ATOM   2917 H  HD2  A HIS   A 1 138 ? 16.698 -10.510 -7.964  0.70 21.98 ?  138 HIS   A HD2  1 
ATOM   2918 H  HD2  B HIS   A 1 138 ? 16.558 -10.104 -7.875  0.30 19.23 ?  138 HIS   A HD2  1 
ATOM   2919 H  HE1  A HIS   A 1 138 ? 16.768 -14.424 -8.549  0.70 23.06 ?  138 HIS   A HE1  1 
ATOM   2920 H  HE1  B HIS   A 1 138 ? 16.893 -13.963 -8.687  0.30 19.66 ?  138 HIS   A HE1  1 
ATOM   2921 H  HE2  B HIS   A 1 138 ? 18.026 -11.888 -8.613  0.30 19.45 ?  138 HIS   A HE2  1 
ATOM   2922 N  N    . SER   A 1 139 ? 14.862 -10.217 -4.390  1.00 14.81 ?  139 SER   A N    1 
ATOM   2923 C  CA   . SER   A 1 139 ? 15.930 -10.033 -3.417  1.00 14.77 ?  139 SER   A CA   1 
ATOM   2924 C  C    . SER   A 1 139 ? 15.701 -10.878 -2.169  1.00 14.40 ?  139 SER   A C    1 
ATOM   2925 O  O    . SER   A 1 139 ? 16.647 -11.470 -1.634  1.00 14.59 ?  139 SER   A O    1 
ATOM   2926 C  CB   . SER   A 1 139 ? 16.057 -8.554  -3.055  1.00 14.44 ?  139 SER   A CB   1 
ATOM   2927 O  OG   . SER   A 1 139 ? 17.137 -8.382  -2.154  1.00 14.85 ?  139 SER   A OG   1 
ATOM   2928 H  H    A SER   A 1 139 ? 14.436 -9.504  -4.605  0.70 17.74 ?  139 SER   A H    1 
ATOM   2929 H  H    B SER   A 1 139 ? 14.439 -9.495  -4.579  0.30 17.74 ?  139 SER   A H    1 
ATOM   2930 H  HA   . SER   A 1 139 ? 16.774 -10.313 -3.813  1.00 17.68 ?  139 SER   A HA   1 
ATOM   2931 H  HB2  . SER   A 1 139 ? 16.233 -8.035  -3.856  1.00 17.28 ?  139 SER   A HB2  1 
ATOM   2932 H  HB3  . SER   A 1 139 ? 15.240 -8.251  -2.631  1.00 17.28 ?  139 SER   A HB3  1 
ATOM   2933 H  HG   . SER   A 1 139 ? 17.216 -7.564  -1.940  1.00 17.78 ?  139 SER   A HG   1 
ATOM   2934 N  N    . LEU   A 1 140 ? 14.458 -10.947 -1.691  1.00 14.31 ?  140 LEU   A N    1 
ATOM   2935 C  CA   . LEU   A 1 140 ? 14.178 -11.762 -0.513  1.00 14.23 ?  140 LEU   A CA   1 
ATOM   2936 C  C    . LEU   A 1 140 ? 14.441 -13.238 -0.792  1.00 14.40 ?  140 LEU   A C    1 
ATOM   2937 O  O    . LEU   A 1 140 ? 14.992 -13.951 0.057   1.00 14.92 ?  140 LEU   A O    1 
ATOM   2938 C  CB   . LEU   A 1 140 ? 12.737 -11.536 -0.063  1.00 14.34 ?  140 LEU   A CB   1 
ATOM   2939 C  CG   . LEU   A 1 140 ? 12.262 -12.399 1.107   1.00 15.23 ?  140 LEU   A CG   1 
ATOM   2940 C  CD1  . LEU   A 1 140 ? 13.158 -12.225 2.328   1.00 15.66 ?  140 LEU   A CD1  1 
ATOM   2941 C  CD2  . LEU   A 1 140 ? 10.800 -12.068 1.451   1.00 15.77 ?  140 LEU   A CD2  1 
ATOM   2942 H  H    . LEU   A 1 140 ? 13.781 -10.533 -2.020  1.00 17.13 ?  140 LEU   A H    1 
ATOM   2943 H  HA   . LEU   A 1 140 ? 14.762 -11.489 0.208   1.00 17.04 ?  140 LEU   A HA   1 
ATOM   2944 H  HB2  . LEU   A 1 140 ? 12.642 -10.614 0.208   1.00 17.17 ?  140 LEU   A HB2  1 
ATOM   2945 H  HB3  . LEU   A 1 140 ? 12.150 -11.720 -0.812  1.00 17.17 ?  140 LEU   A HB3  1 
ATOM   2946 H  HG   . LEU   A 1 140 ? 12.286 -13.335 0.844   1.00 18.24 ?  140 LEU   A HG   1 
ATOM   2947 H  HD11 . LEU   A 1 140 ? 12.769 -12.706 3.077   1.00 18.76 ?  140 LEU   A HD11 1 
ATOM   2948 H  HD12 . LEU   A 1 140 ? 14.035 -12.590 2.125   1.00 18.76 ?  140 LEU   A HD12 1 
ATOM   2949 H  HD13 . LEU   A 1 140 ? 13.227 -11.284 2.537   1.00 18.76 ?  140 LEU   A HD13 1 
ATOM   2950 H  HD21 . LEU   A 1 140 ? 10.497 -12.655 2.162   1.00 18.88 ?  140 LEU   A HD21 1 
ATOM   2951 H  HD22 . LEU   A 1 140 ? 10.745 -11.143 1.742   1.00 18.88 ?  140 LEU   A HD22 1 
ATOM   2952 H  HD23 . LEU   A 1 140 ? 10.248 -12.197 0.661   1.00 18.88 ?  140 LEU   A HD23 1 
ATOM   2953 N  N    . ARG   A 1 141 ? 14.066 -13.708 -1.984  1.00 14.72 ?  141 ARG   A N    1 
ATOM   2954 C  CA   . ARG   A 1 141 ? 14.307 -15.099 -2.350  1.00 15.92 ?  141 ARG   A CA   1 
ATOM   2955 C  C    . ARG   A 1 141 ? 15.801 -15.404 -2.354  1.00 15.16 ?  141 ARG   A C    1 
ATOM   2956 O  O    . ARG   A 1 141 ? 16.247 -16.419 -1.807  1.00 15.29 ?  141 ARG   A O    1 
ATOM   2957 C  CB   . ARG   A 1 141 ? 13.696 -15.363 -3.728  1.00 17.67 ?  141 ARG   A CB   1 
ATOM   2958 C  CG   . ARG   A 1 141 ? 13.713 -16.812 -4.178  1.00 20.50 ?  141 ARG   A CG   1 
ATOM   2959 C  CD   . ARG   A 1 141 ? 12.673 -17.606 -3.443  1.00 23.22 ?  141 ARG   A CD   1 
ATOM   2960 N  NE   . ARG   A 1 141 ? 13.267 -18.395 -2.376  1.00 24.42 ?  141 ARG   A NE   1 
ATOM   2961 C  CZ   . ARG   A 1 141 ? 12.573 -18.950 -1.389  1.00 25.25 ?  141 ARG   A CZ   1 
ATOM   2962 N  NH1  . ARG   A 1 141 ? 11.280 -18.715 -1.233  1.00 24.79 ?  141 ARG   A NH1  1 
ATOM   2963 N  NH2  . ARG   A 1 141 ? 13.198 -19.745 -0.525  1.00 26.27 ?  141 ARG   A NH2  1 
ATOM   2964 H  H    . ARG   A 1 141 ? 13.676 -13.241 -2.597  1.00 17.63 ?  141 ARG   A H    1 
ATOM   2965 H  HA   . ARG   A 1 141 ? 13.878 -15.681 -1.709  1.00 19.07 ?  141 ARG   A HA   1 
ATOM   2966 H  HB2  . ARG   A 1 141 ? 12.771 -15.068 -3.720  1.00 21.16 ?  141 ARG   A HB2  1 
ATOM   2967 H  HB3  . ARG   A 1 141 ? 14.190 -14.851 -4.388  1.00 21.16 ?  141 ARG   A HB3  1 
ATOM   2968 H  HG2  . ARG   A 1 141 ? 13.522 -16.857 -5.129  1.00 24.56 ?  141 ARG   A HG2  1 
ATOM   2969 H  HG3  . ARG   A 1 141 ? 14.585 -17.199 -3.994  1.00 24.56 ?  141 ARG   A HG3  1 
ATOM   2970 H  HD2  . ARG   A 1 141 ? 12.029 -17.003 -3.039  1.00 27.83 ?  141 ARG   A HD2  1 
ATOM   2971 H  HD3  . ARG   A 1 141 ? 12.223 -18.201 -4.067  1.00 27.83 ?  141 ARG   A HD3  1 
ATOM   2972 H  HE   . ARG   A 1 141 ? 14.092 -18.617 -2.453  1.00 29.27 ?  141 ARG   A HE   1 
ATOM   2973 H  HH11 . ARG   A 1 141 ? 10.859 -18.214 -1.790  1.00 29.71 ?  141 ARG   A HH11 1 
ATOM   2974 H  HH12 . ARG   A 1 141 ? 10.852 -19.079 -0.580  1.00 29.71 ?  141 ARG   A HH12 1 
ATOM   2975 H  HH21 . ARG   A 1 141 ? 14.037 -19.905 -0.616  1.00 31.48 ?  141 ARG   A HH21 1 
ATOM   2976 H  HH22 . ARG   A 1 141 ? 12.762 -20.098 0.129   1.00 31.48 ?  141 ARG   A HH22 1 
ATOM   2977 N  N    . VAL   A 1 142 ? 16.598 -14.531 -2.973  1.00 14.61 ?  142 VAL   A N    1 
ATOM   2978 C  CA   . VAL   A 1 142 ? 18.044 -14.736 -2.987  1.00 14.72 ?  142 VAL   A CA   1 
ATOM   2979 C  C    . VAL   A 1 142 ? 18.598 -14.718 -1.569  1.00 13.94 ?  142 VAL   A C    1 
ATOM   2980 O  O    . VAL   A 1 142 ? 19.464 -15.526 -1.213  1.00 14.38 ?  142 VAL   A O    1 
ATOM   2981 C  CB   . VAL   A 1 142 ? 18.741 -13.712 -3.901  1.00 14.96 ?  142 VAL   A CB   1 
ATOM   2982 C  CG1  . VAL   A 1 142 ? 20.256 -13.922 -3.870  1.00 14.58 ?  142 VAL   A CG1  1 
ATOM   2983 C  CG2  . VAL   A 1 142 ? 18.236 -13.834 -5.330  1.00 15.96 ?  142 VAL   A CG2  1 
ATOM   2984 H  H    . VAL   A 1 142 ? 16.333 -13.821 -3.389  1.00 17.50 ?  142 VAL   A H    1 
ATOM   2985 H  HA   . VAL   A 1 142 ? 18.226 -15.609 -3.359  1.00 17.63 ?  142 VAL   A HA   1 
ATOM   2986 H  HB   . VAL   A 1 142 ? 18.555 -12.809 -3.591  1.00 17.92 ?  142 VAL   A HB   1 
ATOM   2987 H  HG11 . VAL   A 1 142 ? 20.664 -13.410 -4.590  1.00 17.46 ?  142 VAL   A HG11 1 
ATOM   2988 H  HG12 . VAL   A 1 142 ? 20.604 -13.612 -3.017  1.00 17.46 ?  142 VAL   A HG12 1 
ATOM   2989 H  HG13 . VAL   A 1 142 ? 20.448 -14.862 -3.986  1.00 17.46 ?  142 VAL   A HG13 1 
ATOM   2990 H  HG21 . VAL   A 1 142 ? 18.712 -13.194 -5.888  1.00 19.12 ?  142 VAL   A HG21 1 
ATOM   2991 H  HG22 . VAL   A 1 142 ? 18.408 -14.734 -5.644  1.00 19.12 ?  142 VAL   A HG22 1 
ATOM   2992 H  HG23 . VAL   A 1 142 ? 17.289 -13.646 -5.345  1.00 19.12 ?  142 VAL   A HG23 1 
ATOM   2993 N  N    . CYS   A 1 143 ? 18.123 -13.788 -0.740  1.00 13.65 ?  143 CYS   A N    1 
ATOM   2994 C  CA   . CYS   A 1 143 ? 18.576 -13.738 0.645   1.00 13.96 ?  143 CYS   A CA   1 
ATOM   2995 C  C    . CYS   A 1 143 ? 18.349 -15.078 1.337   1.00 14.06 ?  143 CYS   A C    1 
ATOM   2996 O  O    . CYS   A 1 143 ? 19.267 -15.658 1.926   1.00 14.32 ?  143 CYS   A O    1 
ATOM   2997 C  CB   . CYS   A 1 143 ? 17.844 -12.620 1.381   1.00 14.40 ?  143 CYS   A CB   1 
ATOM   2998 S  SG   . CYS   A 1 143 ? 18.316 -12.444 3.097   1.00 14.93 ?  143 CYS   A SG   1 
ATOM   2999 H  H    . CYS   A 1 143 ? 17.540 -13.193 -0.951  1.00 16.35 ?  143 CYS   A H    1 
ATOM   3000 H  HA   . CYS   A 1 143 ? 19.521 -13.551 0.665   1.00 16.71 ?  143 CYS   A HA   1 
ATOM   3001 H  HB2  . CYS   A 1 143 ? 18.022 -11.780 0.930   1.00 17.24 ?  143 CYS   A HB2  1 
ATOM   3002 H  HB3  . CYS   A 1 143 ? 16.891 -12.801 1.355   1.00 17.24 ?  143 CYS   A HB3  1 
ATOM   3003 H  HG   . CYS   A 1 143 ? 17.731 -11.509 3.564   1.00 17.88 ?  143 CYS   A HG   1 
ATOM   3004 N  N    . VAL   A 1 144 ? 17.123 -15.591 1.264   1.00 14.60 ?  144 VAL   A N    1 
ATOM   3005 C  CA   . VAL   A 1 144 ? 16.785 -16.825 1.962   1.00 16.01 ?  144 VAL   A CA   1 
ATOM   3006 C  C    . VAL   A 1 144 ? 17.607 -17.991 1.440   1.00 15.56 ?  144 VAL   A C    1 
ATOM   3007 O  O    . VAL   A 1 144 ? 17.963 -18.905 2.196   1.00 16.22 ?  144 VAL   A O    1 
ATOM   3008 C  CB   . VAL   A 1 144 ? 15.271 -17.078 1.831   1.00 18.56 ?  144 VAL   A CB   1 
ATOM   3009 C  CG1  . VAL   A 1 144 ? 14.921 -18.514 2.170   1.00 20.03 ?  144 VAL   A CG1  1 
ATOM   3010 C  CG2  . VAL   A 1 144 ? 14.517 -16.087 2.705   1.00 18.33 ?  144 VAL   A CG2  1 
ATOM   3011 H  H    . VAL   A 1 144 ? 16.467 -15.246 0.819   1.00 17.48 ?  144 VAL   A H    1 
ATOM   3012 H  HA   . VAL   A 1 144 ? 16.978 -16.720 2.903   1.00 19.18 ?  144 VAL   A HA   1 
ATOM   3013 H  HB   . VAL   A 1 144 ? 15.000 -16.921 0.909   1.00 22.24 ?  144 VAL   A HB   1 
ATOM   3014 H  HG11 . VAL   A 1 144 ? 13.966 -18.574 2.352   1.00 24.00 ?  144 VAL   A HG11 1 
ATOM   3015 H  HG12 . VAL   A 1 144 ? 15.143 -19.086 1.418   1.00 24.00 ?  144 VAL   A HG12 1 
ATOM   3016 H  HG13 . VAL   A 1 144 ? 15.419 -18.784 2.955   1.00 24.00 ?  144 VAL   A HG13 1 
ATOM   3017 H  HG21 . VAL   A 1 144 ? 13.559 -16.249 2.622   1.00 21.95 ?  144 VAL   A HG21 1 
ATOM   3018 H  HG22 . VAL   A 1 144 ? 14.788 -16.205 3.628   1.00 21.95 ?  144 VAL   A HG22 1 
ATOM   3019 H  HG23 . VAL   A 1 144 ? 14.719 -15.184 2.412   1.00 21.95 ?  144 VAL   A HG23 1 
ATOM   3020 N  N    . ASP   A 1 145 ? 17.877 -18.012 0.139   1.00 15.67 ?  145 ASP   A N    1 
ATOM   3021 C  CA   . ASP   A 1 145 ? 18.598 -19.120 -0.478  1.00 16.15 ?  145 ASP   A CA   1 
ATOM   3022 C  C    . ASP   A 1 145 ? 20.118 -18.966 -0.426  1.00 15.99 ?  145 ASP   A C    1 
ATOM   3023 O  O    . ASP   A 1 145 ? 20.830 -19.859 -0.899  1.00 17.84 ?  145 ASP   A O    1 
ATOM   3024 C  CB   . ASP   A 1 145 ? 18.169 -19.272 -1.939  1.00 17.41 ?  145 ASP   A CB   1 
ATOM   3025 C  CG   . ASP   A 1 145 ? 16.728 -19.734 -2.083  1.00 19.63 ?  145 ASP   A CG   1 
ATOM   3026 O  OD1  . ASP   A 1 145 ? 16.145 -20.258 -1.104  1.00 20.42 ?  145 ASP   A OD1  1 
ATOM   3027 O  OD2  . ASP   A 1 145 ? 16.181 -19.559 -3.188  1.00 21.49 -1 145 ASP   A OD2  1 
ATOM   3028 H  H    . ASP   A 1 145 ? 17.633 -17.404 -0.416  1.00 18.77 ?  145 ASP   A H    1 
ATOM   3029 H  HA   . ASP   A 1 145 ? 18.364 -19.944 -0.020  1.00 19.34 ?  145 ASP   A HA   1 
ATOM   3030 H  HB2  . ASP   A 1 145 ? 18.267 -18.414 -2.386  1.00 20.85 ?  145 ASP   A HB2  1 
ATOM   3031 H  HB3  . ASP   A 1 145 ? 18.741 -19.931 -2.368  1.00 20.85 ?  145 ASP   A HB3  1 
ATOM   3032 N  N    . THR   A 1 146 ? 20.636 -17.867 0.122   1.00 14.62 ?  146 THR   A N    1 
ATOM   3033 C  CA   . THR   A 1 146 ? 22.073 -17.611 0.142   1.00 13.98 ?  146 THR   A CA   1 
ATOM   3034 C  C    . THR   A 1 146 ? 22.617 -17.428 1.547   1.00 13.98 ?  146 THR   A C    1 
ATOM   3035 O  O    . THR   A 1 146 ? 23.695 -17.949 1.862   1.00 14.91 ?  146 THR   A O    1 
ATOM   3036 C  CB   . THR   A 1 146 ? 22.396 -16.362 -0.697  1.00 14.27 ?  146 THR   A CB   1 
ATOM   3037 O  OG1  . THR   A 1 146 ? 21.882 -16.532 -2.021  1.00 14.87 ?  146 THR   A OG1  1 
ATOM   3038 C  CG2  . THR   A 1 146 ? 23.896 -16.119 -0.755  1.00 14.10 ?  146 THR   A CG2  1 
ATOM   3039 H  H    . THR   A 1 146 ? 20.166 -17.242 0.490   1.00 17.51 ?  146 THR   A H    1 
ATOM   3040 H  HA   . THR   A 1 146 ? 22.535 -18.361 -0.254  1.00 16.74 ?  146 THR   A HA   1 
ATOM   3041 H  HB   . THR   A 1 146 ? 21.977 -15.586 -0.291  1.00 17.08 ?  146 THR   A HB   1 
ATOM   3042 H  HG1  . THR   A 1 146 ? 21.050 -16.622 -1.997  1.00 17.80 ?  146 THR   A HG1  1 
ATOM   3043 H  HG21 . THR   A 1 146 ? 24.097 -15.466 -1.442  1.00 16.89 ?  146 THR   A HG21 1 
ATOM   3044 H  HG22 . THR   A 1 146 ? 24.211 -15.781 0.100   1.00 16.89 ?  146 THR   A HG22 1 
ATOM   3045 H  HG23 . THR   A 1 146 ? 24.358 -16.945 -0.959  1.00 16.89 ?  146 THR   A HG23 1 
ATOM   3046 N  N    . VAL   A 1 147 ? 21.942 -16.637 2.372   1.00 14.00 ?  147 VAL   A N    1 
ATOM   3047 C  CA   . VAL   A 1 147 ? 22.423 -16.338 3.713   1.00 14.19 ?  147 VAL   A CA   1 
ATOM   3048 C  C    . VAL   A 1 147 ? 22.105 -17.506 4.639   1.00 14.48 ?  147 VAL   A C    1 
ATOM   3049 O  O    . VAL   A 1 147 ? 20.963 -17.988 4.692   1.00 14.99 ?  147 VAL   A O    1 
ATOM   3050 C  CB   . VAL   A 1 147 ? 21.793 -15.032 4.221   1.00 14.22 ?  147 VAL   A CB   1 
ATOM   3051 C  CG1  . VAL   A 1 147 ? 22.300 -14.705 5.604   1.00 15.19 ?  147 VAL   A CG1  1 
ATOM   3052 C  CG2  . VAL   A 1 147 ? 22.051 -13.883 3.237   1.00 14.58 ?  147 VAL   A CG2  1 
ATOM   3053 H  H    . VAL   A 1 147 ? 21.193 -16.255 2.179   1.00 16.76 ?  147 VAL   A H    1 
ATOM   3054 H  HA   . VAL   A 1 147 ? 23.385 -16.218 3.688   1.00 16.99 ?  147 VAL   A HA   1 
ATOM   3055 H  HB   . VAL   A 1 147 ? 20.833 -15.157 4.285   1.00 17.03 ?  147 VAL   A HB   1 
ATOM   3056 H  HG11 . VAL   A 1 147 ? 22.031 -13.802 5.830   1.00 18.19 ?  147 VAL   A HG11 1 
ATOM   3057 H  HG12 . VAL   A 1 147 ? 21.908 -15.332 6.238   1.00 18.19 ?  147 VAL   A HG12 1 
ATOM   3058 H  HG13 . VAL   A 1 147 ? 23.262 -14.782 5.613   1.00 18.19 ?  147 VAL   A HG13 1 
ATOM   3059 H  HG21 . VAL   A 1 147 ? 21.720 -13.057 3.627   1.00 17.46 ?  147 VAL   A HG21 1 
ATOM   3060 H  HG22 . VAL   A 1 147 ? 22.997 -13.818 3.066   1.00 17.46 ?  147 VAL   A HG22 1 
ATOM   3061 H  HG23 . VAL   A 1 147 ? 21.571 -14.068 2.410   1.00 17.46 ?  147 VAL   A HG23 1 
ATOM   3062 N  N    . ARG   A 1 148 ? 23.124 -17.957 5.372   1.00 14.45 ?  148 ARG   A N    1 
ATOM   3063 C  CA   . ARG   A 1 148 ? 22.999 -19.029 6.347   1.00 14.87 ?  148 ARG   A CA   1 
ATOM   3064 C  C    . ARG   A 1 148 ? 23.111 -18.550 7.782   1.00 14.91 ?  148 ARG   A C    1 
ATOM   3065 O  O    . ARG   A 1 148 ? 22.691 -19.268 8.698   1.00 16.62 ?  148 ARG   A O    1 
ATOM   3066 C  CB   . ARG   A 1 148 ? 24.054 -20.116 6.095   1.00 15.67 ?  148 ARG   A CB   1 
ATOM   3067 C  CG   . ARG   A 1 148 ? 23.927 -20.758 4.734   1.00 16.57 ?  148 ARG   A CG   1 
ATOM   3068 C  CD   . ARG   A 1 148 ? 25.027 -21.790 4.487   1.00 17.29 ?  148 ARG   A CD   1 
ATOM   3069 N  NE   . ARG   A 1 148 ? 26.359 -21.197 4.513   1.00 17.18 ?  148 ARG   A NE   1 
ATOM   3070 C  CZ   . ARG   A 1 148 ? 26.873 -20.473 3.528   1.00 16.22 ?  148 ARG   A CZ   1 
ATOM   3071 N  NH1  . ARG   A 1 148 ? 26.214 -20.271 2.401   1.00 16.55 ?  148 ARG   A NH1  1 
ATOM   3072 N  NH2  . ARG   A 1 148 ? 28.085 -19.942 3.677   1.00 16.61 ?  148 ARG   A NH2  1 
ATOM   3073 H  H    . ARG   A 1 148 ? 23.924 -17.643 5.306   1.00 17.30 ?  148 ARG   A H    1 
ATOM   3074 H  HA   . ARG   A 1 148 ? 22.128 -19.435 6.246   1.00 17.81 ?  148 ARG   A HA   1 
ATOM   3075 H  HB2  . ARG   A 1 148 ? 24.937 -19.726 6.162   1.00 18.76 ?  148 ARG   A HB2  1 
ATOM   3076 H  HB3  . ARG   A 1 148 ? 23.947 -20.815 6.762   1.00 18.76 ?  148 ARG   A HB3  1 
ATOM   3077 H  HG2  . ARG   A 1 148 ? 23.064 -21.196 4.676   1.00 19.85 ?  148 ARG   A HG2  1 
ATOM   3078 H  HG3  . ARG   A 1 148 ? 23.994 -20.062 4.059   1.00 19.85 ?  148 ARG   A HG3  1 
ATOM   3079 H  HD2  . ARG   A 1 148 ? 24.980 -22.464 5.181   1.00 20.71 ?  148 ARG   A HD2  1 
ATOM   3080 H  HD3  . ARG   A 1 148 ? 24.884 -22.189 3.618   1.00 20.71 ?  148 ARG   A HD3  1 
ATOM   3081 H  HE   . ARG   A 1 148 ? 26.840 -21.326 5.211   1.00 20.57 ?  148 ARG   A HE   1 
ATOM   3082 H  HH11 . ARG   A 1 148 ? 25.429 -20.598 2.292   1.00 19.82 ?  148 ARG   A HH11 1 
ATOM   3083 H  HH12 . ARG   A 1 148 ? 26.570 -19.791 1.778   1.00 19.82 ?  148 ARG   A HH12 1 
ATOM   3084 H  HH21 . ARG   A 1 148 ? 28.523 -20.067 4.406   1.00 19.90 ?  148 ARG   A HH21 1 
ATOM   3085 H  HH22 . ARG   A 1 148 ? 28.430 -19.470 3.045   1.00 19.90 ?  148 ARG   A HH22 1 
ATOM   3086 N  N    . THR   A 1 149 ? 23.656 -17.353 7.990   1.00 14.86 ?  149 THR   A N    1 
ATOM   3087 C  CA   . THR   A 1 149 ? 23.718 -16.743 9.303   1.00 14.99 ?  149 THR   A CA   1 
ATOM   3088 C  C    . THR   A 1 149 ? 22.388 -16.045 9.590   1.00 14.92 ?  149 THR   A C    1 
ATOM   3089 O  O    . THR   A 1 149 ? 21.464 -16.042 8.765   1.00 15.10 ?  149 THR   A O    1 
ATOM   3090 C  CB   . THR   A 1 149 ? 24.917 -15.802 9.364   1.00 15.45 ?  149 THR   A CB   1 
ATOM   3091 O  OG1  . THR   A 1 149 ? 24.794 -14.874 8.285   1.00 15.21 ?  149 THR   A OG1  1 
ATOM   3092 C  CG2  . THR   A 1 149 ? 26.235 -16.591 9.241   1.00 15.81 ?  149 THR   A CG2  1 
ATOM   3093 H  H    . THR   A 1 149 ? 24.009 -16.859 7.369   1.00 17.79 ?  149 THR   A H    1 
ATOM   3094 H  HA   . THR   A 1 149 ? 23.842 -17.442 9.965   1.00 17.95 ?  149 THR   A HA   1 
ATOM   3095 H  HB   . THR   A 1 149 ? 24.912 -15.330 10.210  1.00 18.50 ?  149 THR   A HB   1 
ATOM   3096 H  HG1  . THR   A 1 149 ? 25.443 -14.341 8.292   1.00 18.22 ?  149 THR   A HG1  1 
ATOM   3097 H  HG21 . THR   A 1 149 ? 26.991 -15.987 9.299   1.00 18.94 ?  149 THR   A HG21 1 
ATOM   3098 H  HG22 . THR   A 1 149 ? 26.302 -17.248 9.954   1.00 18.94 ?  149 THR   A HG22 1 
ATOM   3099 H  HG23 . THR   A 1 149 ? 26.270 -17.054 8.387   1.00 18.94 ?  149 THR   A HG23 1 
ATOM   3100 N  N    . ASN   A 1 150 ? 22.251 -15.511 10.799  1.00 15.31 ?  150 ASN   A N    1 
ATOM   3101 C  CA   . ASN   A 1 150 ? 20.964 -14.995 11.267  1.00 15.79 ?  150 ASN   A CA   1 
ATOM   3102 C  C    . ASN   A 1 150 ? 20.795 -13.557 10.790  1.00 14.76 ?  150 ASN   A C    1 
ATOM   3103 O  O    . ASN   A 1 150 ? 21.550 -12.667 11.194  1.00 16.01 ?  150 ASN   A O    1 
ATOM   3104 C  CB   . ASN   A 1 150 ? 20.887 -15.093 12.786  1.00 18.11 ?  150 ASN   A CB   1 
ATOM   3105 C  CG   . ASN   A 1 150 ? 20.798 -16.522 13.258  1.00 21.72 ?  150 ASN   A CG   1 
ATOM   3106 O  OD1  . ASN   A 1 150 ? 20.215 -17.362 12.579  1.00 22.94 ?  150 ASN   A OD1  1 
ATOM   3107 N  ND2  . ASN   A 1 150 ? 21.391 -16.813 14.412  1.00 23.89 ?  150 ASN   A ND2  1 
ATOM   3108 H  H    . ASN   A 1 150 ? 22.892 -15.434 11.372  1.00 18.34 ?  150 ASN   A H    1 
ATOM   3109 H  HA   . ASN   A 1 150 ? 20.251 -15.533 10.891  1.00 18.91 ?  150 ASN   A HA   1 
ATOM   3110 H  HB2  . ASN   A 1 150 ? 21.682 -14.700 13.175  1.00 21.69 ?  150 ASN   A HB2  1 
ATOM   3111 H  HB3  . ASN   A 1 150 ? 20.095 -14.627 13.096  1.00 21.69 ?  150 ASN   A HB3  1 
ATOM   3112 H  HD21 . ASN   A 1 150 ? 21.369 -17.618 14.727  1.00 28.63 ?  150 ASN   A HD21 1 
ATOM   3113 H  HD22 . ASN   A 1 150 ? 21.797 -16.197 14.855  1.00 28.63 ?  150 ASN   A HD22 1 
ATOM   3114 N  N    . VAL   A 1 151 ? 19.811 -13.329 9.926   1.00 14.39 ?  151 VAL   A N    1 
ATOM   3115 C  CA   . VAL   A 1 151 ? 19.594 -12.022 9.325   1.00 14.82 ?  151 VAL   A CA   1 
ATOM   3116 C  C    . VAL   A 1 151 ? 18.201 -11.514 9.681   1.00 14.61 ?  151 VAL   A C    1 
ATOM   3117 O  O    . VAL   A 1 151 ? 17.193 -12.228 9.542   1.00 15.72 ?  151 VAL   A O    1 
ATOM   3118 C  CB   . VAL   A 1 151 ? 19.883 -12.017 7.808   1.00 15.94 ?  151 VAL   A CB   1 
ATOM   3119 C  CG1  . VAL   A 1 151 ? 19.071 -13.053 7.064   1.00 16.65 ?  151 VAL   A CG1  1 
ATOM   3120 C  CG2  . VAL   A 1 151 ? 19.681 -10.612 7.222   1.00 15.67 ?  151 VAL   A CG2  1 
ATOM   3121 H  H    . VAL   A 1 151 ? 19.252 -13.929 9.664   1.00 17.23 ?  151 VAL   A H    1 
ATOM   3122 H  HA   . VAL   A 1 151 ? 20.237 -11.407 9.722   1.00 17.75 ?  151 VAL   A HA   1 
ATOM   3123 H  HB   . VAL   A 1 151 ? 20.821 -12.241 7.676   1.00 19.09 ?  151 VAL   A HB   1 
ATOM   3124 H  HG11 . VAL   A 1 151 ? 19.267 -12.997 6.115   1.00 19.94 ?  151 VAL   A HG11 1 
ATOM   3125 H  HG12 . VAL   A 1 151 ? 19.311 -13.940 7.393   1.00 19.94 ?  151 VAL   A HG12 1 
ATOM   3126 H  HG13 . VAL   A 1 151 ? 18.128 -12.893 7.218   1.00 19.94 ?  151 VAL   A HG13 1 
ATOM   3127 H  HG21 . VAL   A 1 151 ? 19.994 -10.604 6.300   1.00 18.76 ?  151 VAL   A HG21 1 
ATOM   3128 H  HG22 . VAL   A 1 151 ? 18.738 -10.387 7.249   1.00 18.76 ?  151 VAL   A HG22 1 
ATOM   3129 H  HG23 . VAL   A 1 151 ? 20.190 -9.971  7.744   1.00 18.76 ?  151 VAL   A HG23 1 
ATOM   3130 N  N    . TYR   A 1 152 ? 18.177 -10.266 10.146  1.00 14.58 ?  152 TYR   A N    1 
ATOM   3131 C  CA   . TYR   A 1 152 ? 16.983 -9.536  10.535  1.00 13.99 ?  152 TYR   A CA   1 
ATOM   3132 C  C    . TYR   A 1 152 ? 16.784 -8.428  9.512   1.00 13.65 ?  152 TYR   A C    1 
ATOM   3133 O  O    . TYR   A 1 152 ? 17.559 -7.465  9.468   1.00 14.53 ?  152 TYR   A O    1 
ATOM   3134 C  CB   . TYR   A 1 152 ? 17.161 -9.001  11.952  1.00 14.83 ?  152 TYR   A CB   1 
ATOM   3135 C  CG   . TYR   A 1 152 ? 17.122 -10.119 12.960  1.00 15.59 ?  152 TYR   A CG   1 
ATOM   3136 C  CD1  . TYR   A 1 152 ? 18.250 -10.880 13.243  1.00 17.09 ?  152 TYR   A CD1  1 
ATOM   3137 C  CD2  . TYR   A 1 152 ? 15.938 -10.448 13.600  1.00 15.83 ?  152 TYR   A CD2  1 
ATOM   3138 C  CE1  . TYR   A 1 152 ? 18.205 -11.929 14.146  1.00 18.50 ?  152 TYR   A CE1  1 
ATOM   3139 C  CE2  . TYR   A 1 152 ? 15.881 -11.500 14.507  1.00 17.27 ?  152 TYR   A CE2  1 
ATOM   3140 C  CZ   . TYR   A 1 152 ? 17.020 -12.236 14.776  1.00 18.67 ?  152 TYR   A CZ   1 
ATOM   3141 O  OH   . TYR   A 1 152 ? 16.977 -13.285 15.675  1.00 21.27 ?  152 TYR   A OH   1 
ATOM   3142 H  H    . TYR   A 1 152 ? 18.898 -9.776  10.220  1.00 17.46 ?  152 TYR   A H    1 
ATOM   3143 H  HA   . TYR   A 1 152 ? 16.221 -10.132 10.511  1.00 16.75 ?  152 TYR   A HA   1 
ATOM   3144 H  HB2  . TYR   A 1 152 ? 18.023 -8.568  12.021  1.00 17.76 ?  152 TYR   A HB2  1 
ATOM   3145 H  HB3  . TYR   A 1 152 ? 16.447 -8.386  12.152  1.00 17.76 ?  152 TYR   A HB3  1 
ATOM   3146 H  HD1  . TYR   A 1 152 ? 19.049 -10.683 12.813  1.00 20.47 ?  152 TYR   A HD1  1 
ATOM   3147 H  HD2  . TYR   A 1 152 ? 15.162 -9.957  13.414  1.00 18.96 ?  152 TYR   A HD2  1 
ATOM   3148 H  HE1  . TYR   A 1 152 ? 18.969 -12.422 14.331  1.00 22.16 ?  152 TYR   A HE1  1 
ATOM   3149 H  HE2  . TYR   A 1 152 ? 15.076 -11.698 14.936  1.00 20.69 ?  152 TYR   A HE2  1 
ATOM   3150 H  HH   . TYR   A 1 152 ? 16.203 -13.343 16.003  1.00 25.49 ?  152 TYR   A HH   1 
ATOM   3151 N  N    . LEU   A 1 153 ? 15.769 -8.593  8.673   1.00 14.03 ?  153 LEU   A N    1 
ATOM   3152 C  CA   . LEU   A 1 153 ? 15.517 -7.700  7.555   1.00 13.96 ?  153 LEU   A CA   1 
ATOM   3153 C  C    . LEU   A 1 153 ? 14.517 -6.627  7.947   1.00 14.34 ?  153 LEU   A C    1 
ATOM   3154 O  O    . LEU   A 1 153 ? 13.429 -6.935  8.443   1.00 15.78 ?  153 LEU   A O    1 
ATOM   3155 C  CB   . LEU   A 1 153 ? 14.953 -8.483  6.371   1.00 13.83 ?  153 LEU   A CB   1 
ATOM   3156 C  CG   . LEU   A 1 153 ? 15.897 -9.491  5.721   1.00 14.19 ?  153 LEU   A CG   1 
ATOM   3157 C  CD1  . LEU   A 1 153 ? 15.113 -10.379 4.762   1.00 14.74 ?  153 LEU   A CD1  1 
ATOM   3158 C  CD2  . LEU   A 1 153 ? 17.028 -8.772  5.000   1.00 14.54 ?  153 LEU   A CD2  1 
ATOM   3159 H  H    . LEU   A 1 153 ? 15.185 -9.227  8.742   1.00 16.79 ?  153 LEU   A H    1 
ATOM   3160 H  HA   . LEU   A 1 153 ? 16.346 -7.283  7.294   1.00 16.71 ?  153 LEU   A HA   1 
ATOM   3161 H  HB2  . LEU   A 1 153 ? 14.169 -8.966  6.675   1.00 16.56 ?  153 LEU   A HB2  1 
ATOM   3162 H  HB3  . LEU   A 1 153 ? 14.691 -7.844  5.688   1.00 16.56 ?  153 LEU   A HB3  1 
ATOM   3163 H  HG   . LEU   A 1 153 ? 16.286 -10.051 6.414   1.00 16.99 ?  153 LEU   A HG   1 
ATOM   3164 H  HD11 . LEU   A 1 153 ? 15.704 -11.058 4.411   1.00 17.64 ?  153 LEU   A HD11 1 
ATOM   3165 H  HD12 . LEU   A 1 153 ? 14.378 -10.787 5.241   1.00 17.64 ?  153 LEU   A HD12 1 
ATOM   3166 H  HD13 . LEU   A 1 153 ? 14.772 -9.827  4.038   1.00 17.64 ?  153 LEU   A HD13 1 
ATOM   3167 H  HD21 . LEU   A 1 153 ? 17.575 -9.429  4.548   1.00 17.41 ?  153 LEU   A HD21 1 
ATOM   3168 H  HD22 . LEU   A 1 153 ? 16.644 -8.155  4.358   1.00 17.41 ?  153 LEU   A HD22 1 
ATOM   3169 H  HD23 . LEU   A 1 153 ? 17.559 -8.286  5.650   1.00 17.41 ?  153 LEU   A HD23 1 
ATOM   3170 N  N    A ALA   A 1 154 ? 14.907 -5.373  7.746   0.70 14.29 ?  154 ALA   A N    1 
ATOM   3171 N  N    B ALA   A 1 154 ? 14.862 -5.372  7.673   0.30 14.27 ?  154 ALA   A N    1 
ATOM   3172 C  CA   A ALA   A 1 154 ? 14.046 -4.220  7.965   0.70 15.07 ?  154 ALA   A CA   1 
ATOM   3173 C  CA   B ALA   A 1 154 ? 13.987 -4.229  7.917   0.30 14.73 ?  154 ALA   A CA   1 
ATOM   3174 C  C    A ALA   A 1 154 ? 13.553 -3.731  6.611   0.70 15.45 ?  154 ALA   A C    1 
ATOM   3175 C  C    B ALA   A 1 154 ? 13.531 -3.667  6.575   0.30 15.28 ?  154 ALA   A C    1 
ATOM   3176 O  O    A ALA   A 1 154 ? 14.359 -3.389  5.737   0.70 16.08 ?  154 ALA   A O    1 
ATOM   3177 O  O    B ALA   A 1 154 ? 14.357 -3.207  5.779   0.30 15.41 ?  154 ALA   A O    1 
ATOM   3178 C  CB   A ALA   A 1 154 ? 14.822 -3.107  8.671   0.70 15.48 ?  154 ALA   A CB   1 
ATOM   3179 C  CB   B ALA   A 1 154 ? 14.724 -3.157  8.721   0.30 14.86 ?  154 ALA   A CB   1 
ATOM   3180 H  H    A ALA   A 1 154 ? 15.699 -5.158  7.479   0.70 17.11 ?  154 ALA   A H    1 
ATOM   3181 H  H    B ALA   A 1 154 ? 15.622 -5.151  7.335   0.30 17.09 ?  154 ALA   A H    1 
ATOM   3182 H  HA   A ALA   A 1 154 ? 13.286 -4.469  8.512   0.70 18.05 ?  154 ALA   A HA   1 
ATOM   3183 H  HA   B ALA   A 1 154 ? 13.208 -4.513  8.423   0.30 17.63 ?  154 ALA   A HA   1 
ATOM   3184 H  HB1  A ALA   A 1 154 ? 14.233 -2.346  8.805   0.70 18.53 ?  154 ALA   A HB1  1 
ATOM   3185 H  HB1  B ALA   A 1 154 ? 14.125 -2.409  8.872   0.30 17.80 ?  154 ALA   A HB1  1 
ATOM   3186 H  HB2  A ALA   A 1 154 ? 15.140 -3.432  9.527   0.70 18.53 ?  154 ALA   A HB2  1 
ATOM   3187 H  HB2  B ALA   A 1 154 ? 15.005 -3.532  9.571   0.30 17.80 ?  154 ALA   A HB2  1 
ATOM   3188 H  HB3  A ALA   A 1 154 ? 15.575 -2.844  8.117   0.70 18.53 ?  154 ALA   A HB3  1 
ATOM   3189 H  HB3  B ALA   A 1 154 ? 15.500 -2.863  8.218   0.30 17.80 ?  154 ALA   A HB3  1 
ATOM   3190 N  N    A VAL   A 1 155 ? 12.234 -3.700  6.445   0.70 15.61 ?  155 VAL   A N    1 
ATOM   3191 N  N    B VAL   A 1 155 ? 12.220 -3.693  6.336   0.30 15.82 ?  155 VAL   A N    1 
ATOM   3192 C  CA   A VAL   A 1 155 ? 11.584 -3.231  5.226   0.70 16.04 ?  155 VAL   A CA   1 
ATOM   3193 C  CA   B VAL   A 1 155 ? 11.623 -3.285  5.065   0.30 16.51 ?  155 VAL   A CA   1 
ATOM   3194 C  C    A VAL   A 1 155 ? 10.840 -1.954  5.590   0.70 17.25 ?  155 VAL   A C    1 
ATOM   3195 C  C    B VAL   A 1 155 ? 10.898 -1.958  5.277   0.30 17.60 ?  155 VAL   A C    1 
ATOM   3196 O  O    A VAL   A 1 155 ? 9.893  -1.992  6.384   0.70 18.02 ?  155 VAL   A O    1 
ATOM   3197 O  O    B VAL   A 1 155 ? 9.962  -1.876  6.082   0.30 17.92 ?  155 VAL   A O    1 
ATOM   3198 C  CB   A VAL   A 1 155 ? 10.644 -4.295  4.643   0.70 16.00 ?  155 VAL   A CB   1 
ATOM   3199 C  CB   B VAL   A 1 155 ? 10.672 -4.365  4.526   0.30 16.25 ?  155 VAL   A CB   1 
ATOM   3200 C  CG1  A VAL   A 1 155 ? 9.903  -3.753  3.431   0.70 16.58 ?  155 VAL   A CG1  1 
ATOM   3201 C  CG1  B VAL   A 1 155 ? 10.015 -3.913  3.229   0.30 16.21 ?  155 VAL   A CG1  1 
ATOM   3202 C  CG2  A VAL   A 1 155 ? 11.434 -5.548  4.271   0.70 16.61 ?  155 VAL   A CG2  1 
ATOM   3203 C  CG2  B VAL   A 1 155 ? 11.421 -5.677  4.318   0.30 16.44 ?  155 VAL   A CG2  1 
ATOM   3204 H  H    A VAL   A 1 155 ? 11.678 -3.963  7.048   0.70 18.69 ?  155 VAL   A H    1 
ATOM   3205 H  H    B VAL   A 1 155 ? 11.642 -3.959  6.914   0.30 18.95 ?  155 VAL   A H    1 
ATOM   3206 H  HA   A VAL   A 1 155 ? 12.256 -3.018  4.562   0.70 19.21 ?  155 VAL   A HA   1 
ATOM   3207 H  HA   B VAL   A 1 155 ? 12.328 -3.150  4.411   0.30 19.78 ?  155 VAL   A HA   1 
ATOM   3208 H  HB   A VAL   A 1 155 ? 9.987  -4.543  5.315   0.70 19.17 ?  155 VAL   A HB   1 
ATOM   3209 H  HB   B VAL   A 1 155 ? 9.972  -4.526  5.178   0.30 19.46 ?  155 VAL   A HB   1 
ATOM   3210 H  HG11 A VAL   A 1 155 ? 9.453  -4.487  2.982   0.70 19.85 ?  155 VAL   A HG11 1 
ATOM   3211 H  HG11 B VAL   A 1 155 ? 9.555  -4.668  2.827   0.30 19.42 ?  155 VAL   A HG11 1 
ATOM   3212 H  HG12 A VAL   A 1 155 ? 9.247  -3.099  3.724   0.70 19.85 ?  155 VAL   A HG12 1 
ATOM   3213 H  HG12 B VAL   A 1 155 ? 9.378  -3.209  3.425   0.30 19.42 ?  155 VAL   A HG12 1 
ATOM   3214 H  HG13 A VAL   A 1 155 ? 10.539 -3.339  2.830   0.70 19.85 ?  155 VAL   A HG13 1 
ATOM   3215 H  HG13 B VAL   A 1 155 ? 10.699 -3.585  2.626   0.30 19.42 ?  155 VAL   A HG13 1 
ATOM   3216 H  HG21 A VAL   A 1 155 ? 10.835 -6.197  3.873   0.70 19.89 ?  155 VAL   A HG21 1 
ATOM   3217 H  HG21 B VAL   A 1 155 ? 10.876 -6.270  3.777   0.30 19.69 ?  155 VAL   A HG21 1 
ATOM   3218 H  HG22 A VAL   A 1 155 ? 12.128 -5.306  3.636   0.70 19.89 ?  155 VAL   A HG22 1 
ATOM   3219 H  HG22 B VAL   A 1 155 ? 12.259 -5.493  3.863   0.30 19.69 ?  155 VAL   A HG22 1 
ATOM   3220 H  HG23 A VAL   A 1 155 ? 11.839 -5.919  5.072   0.70 19.89 ?  155 VAL   A HG23 1 
ATOM   3221 H  HG23 B VAL   A 1 155 ? 11.598 -6.082  5.182   0.30 19.69 ?  155 VAL   A HG23 1 
ATOM   3222 N  N    A PHE   A 1 156 ? 11.277 -0.822  5.028   0.70 18.01 ?  156 PHE   A N    1 
ATOM   3223 N  N    B PHE   A 1 156 ? 11.324 -0.925  4.544   0.30 18.96 ?  156 PHE   A N    1 
ATOM   3224 C  CA   A PHE   A 1 156 ? 10.731 0.479   5.418   0.70 19.14 ?  156 PHE   A CA   1 
ATOM   3225 C  CA   B PHE   A 1 156 ? 10.803 0.440   4.695   0.30 20.46 ?  156 PHE   A CA   1 
ATOM   3226 C  C    A PHE   A 1 156 ? 9.275  0.635   5.001   0.70 19.35 ?  156 PHE   A C    1 
ATOM   3227 C  C    B PHE   A 1 156 ? 9.644  0.697   3.725   0.30 21.39 ?  156 PHE   A C    1 
ATOM   3228 O  O    A PHE   A 1 156 ? 8.462  1.182   5.757   0.70 19.93 ?  156 PHE   A O    1 
ATOM   3229 O  O    B PHE   A 1 156 ? 9.652  1.634   2.927   0.30 22.40 ?  156 PHE   A O    1 
ATOM   3230 C  CB   A PHE   A 1 156 ? 11.568 1.589   4.786   0.70 20.15 ?  156 PHE   A CB   1 
ATOM   3231 C  CB   B PHE   A 1 156 ? 11.934 1.447   4.489   0.30 21.20 ?  156 PHE   A CB   1 
ATOM   3232 C  CG   A PHE   A 1 156 ? 11.063 2.973   5.088   0.70 21.60 ?  156 PHE   A CG   1 
ATOM   3233 C  CG   B PHE   A 1 156 ? 11.600 2.871   4.896   0.30 22.01 ?  156 PHE   A CG   1 
ATOM   3234 C  CD1  A PHE   A 1 156 ? 10.974 3.405   6.400   0.70 22.55 ?  156 PHE   A CD1  1 
ATOM   3235 C  CD1  B PHE   A 1 156 ? 11.762 3.285   6.209   0.30 22.41 ?  156 PHE   A CD1  1 
ATOM   3236 C  CD2  A PHE   A 1 156 ? 10.682 3.836   4.069   0.70 22.47 ?  156 PHE   A CD2  1 
ATOM   3237 C  CD2  B PHE   A 1 156 ? 11.172 3.804   3.961   0.30 22.55 ?  156 PHE   A CD2  1 
ATOM   3238 C  CE1  A PHE   A 1 156 ? 10.514 4.668   6.694   0.70 23.41 ?  156 PHE   A CE1  1 
ATOM   3239 C  CE1  B PHE   A 1 156 ? 11.476 4.589   6.587   0.30 22.63 ?  156 PHE   A CE1  1 
ATOM   3240 C  CE2  A PHE   A 1 156 ? 10.224 5.107   4.357   0.70 23.40 ?  156 PHE   A CE2  1 
ATOM   3241 C  CE2  B PHE   A 1 156 ? 10.885 5.111   4.335   0.30 22.71 ?  156 PHE   A CE2  1 
ATOM   3242 C  CZ   A PHE   A 1 156 ? 10.144 5.525   5.671   0.70 23.82 ?  156 PHE   A CZ   1 
ATOM   3243 C  CZ   B PHE   A 1 156 ? 11.038 5.502   5.648   0.30 22.59 ?  156 PHE   A CZ   1 
ATOM   3244 H  H    A PHE   A 1 156 ? 11.897 -0.787  4.432   0.70 21.57 ?  156 PHE   A H    1 
ATOM   3245 H  H    B PHE   A 1 156 ? 11.941 -0.994  3.950   0.30 22.72 ?  156 PHE   A H    1 
ATOM   3246 H  HA   A PHE   A 1 156 ? 10.787 0.570   6.383   0.70 22.93 ?  156 PHE   A HA   1 
ATOM   3247 H  HA   B PHE   A 1 156 ? 10.465 0.549   5.596   0.30 24.51 ?  156 PHE   A HA   1 
ATOM   3248 H  HB2  A PHE   A 1 156 ? 12.478 1.522   5.121   0.70 24.14 ?  156 PHE   A HB2  1 
ATOM   3249 H  HB2  B PHE   A 1 156 ? 12.691 1.170   5.025   0.30 25.41 ?  156 PHE   A HB2  1 
ATOM   3250 H  HB3  A PHE   A 1 156 ? 11.563 1.471   3.825   0.70 24.14 ?  156 PHE   A HB3  1 
ATOM   3251 H  HB3  B PHE   A 1 156 ? 12.182 1.456   3.551   0.30 25.41 ?  156 PHE   A HB3  1 
ATOM   3252 H  HD1  A PHE   A 1 156 ? 11.228 2.827   7.092   0.70 27.02 ?  156 PHE   A HD1  1 
ATOM   3253 H  HD1  B PHE   A 1 156 ? 12.055 2.678   6.847   0.30 26.86 ?  156 PHE   A HD1  1 
ATOM   3254 H  HD2  A PHE   A 1 156 ? 10.743 3.546   3.186   0.70 26.93 ?  156 PHE   A HD2  1 
ATOM   3255 H  HD2  B PHE   A 1 156 ? 11.065 3.551   3.076   0.30 27.02 ?  156 PHE   A HD2  1 
ATOM   3256 H  HE1  A PHE   A 1 156 ? 10.461 4.947   7.580   0.70 28.05 ?  156 PHE   A HE1  1 
ATOM   3257 H  HE1  B PHE   A 1 156 ? 11.582 4.850   7.474   0.30 27.12 ?  156 PHE   A HE1  1 
ATOM   3258 H  HE2  A PHE   A 1 156 ? 9.974  5.670   3.669   0.70 28.04 ?  156 PHE   A HE2  1 
ATOM   3259 H  HE2  B PHE   A 1 156 ? 10.591 5.723   3.700   0.30 27.22 ?  156 PHE   A HE2  1 
ATOM   3260 H  HZ   A PHE   A 1 156 ? 9.832  6.374   5.870   0.70 28.54 ?  156 PHE   A HZ   1 
ATOM   3261 H  HZ   B PHE   A 1 156 ? 10.847 6.377   5.902   0.30 27.07 ?  156 PHE   A HZ   1 
ATOM   3262 N  N    A ASP   A 1 157 ? 8.940  0.210   3.790   0.70 19.47 ?  157 ASP   A N    1 
ATOM   3263 N  N    B ASP   A 1 157 ? 8.630  -0.165  3.807   0.30 21.07 ?  157 ASP   A N    1 
ATOM   3264 C  CA   A ASP   A 1 157 ? 7.622  0.456   3.226   0.70 20.72 ?  157 ASP   A CA   1 
ATOM   3265 C  CA   B ASP   A 1 157 ? 7.412  0.007   3.020   0.30 20.58 ?  157 ASP   A CA   1 
ATOM   3266 C  C    A ASP   A 1 157 ? 6.637  -0.586  3.745   0.70 20.54 ?  157 ASP   A C    1 
ATOM   3267 C  C    B ASP   A 1 157 ? 6.368  -1.021  3.435   0.30 19.30 ?  157 ASP   A C    1 
ATOM   3268 O  O    A ASP   A 1 157 ? 6.813  -1.788  3.504   0.70 20.04 ?  157 ASP   A O    1 
ATOM   3269 O  O    B ASP   A 1 157 ? 6.547  -2.222  3.209   0.30 18.93 ?  157 ASP   A O    1 
ATOM   3270 C  CB   A ASP   A 1 157 ? 7.718  0.377   1.709   0.70 22.22 ?  157 ASP   A CB   1 
ATOM   3271 C  CB   B ASP   A 1 157 ? 7.697  -0.135  1.524   0.30 21.26 ?  157 ASP   A CB   1 
ATOM   3272 C  CG   A ASP   A 1 157 ? 6.486  0.902   1.028   0.70 24.57 ?  157 ASP   A CG   1 
ATOM   3273 C  CG   B ASP   A 1 157 ? 6.592  0.426   0.661   0.30 22.14 ?  157 ASP   A CG   1 
ATOM   3274 O  OD1  A ASP   A 1 157 ? 6.338  2.137   0.934   0.70 26.61 ?  157 ASP   A OD1  1 
ATOM   3275 O  OD1  B ASP   A 1 157 ? 6.611  1.650   0.407   0.30 22.61 ?  157 ASP   A OD1  1 
ATOM   3276 O  OD2  A ASP   A 1 157 ? 5.648  0.080   0.608   0.70 24.55 -1 157 ASP   A OD2  1 
ATOM   3277 O  OD2  B ASP   A 1 157 ? 5.715  -0.355  0.230   0.30 22.40 -1 157 ASP   A OD2  1 
ATOM   3278 H  H    A ASP   A 1 157 ? 9.477  -0.217  3.264   0.70 23.33 ?  157 ASP   A H    1 
ATOM   3279 H  H    B ASP   A 1 157 ? 8.625  -0.862  4.314   0.30 25.25 ?  157 ASP   A H    1 
ATOM   3280 H  HA   A ASP   A 1 157 ? 7.319  1.343   3.482   0.70 24.83 ?  157 ASP   A HA   1 
ATOM   3281 H  HA   B ASP   A 1 157 ? 7.053  0.892   3.183   0.30 24.66 ?  157 ASP   A HA   1 
ATOM   3282 H  HB2  A ASP   A 1 157 ? 8.495  0.883   1.415   0.70 26.63 ?  157 ASP   A HB2  1 
ATOM   3283 H  HB2  B ASP   A 1 157 ? 8.500  0.340   1.295   0.30 25.47 ?  157 ASP   A HB2  1 
ATOM   3284 H  HB3  A ASP   A 1 157 ? 7.815  -0.550  1.450   0.70 26.63 ?  157 ASP   A HB3  1 
ATOM   3285 H  HB3  B ASP   A 1 157 ? 7.787  -1.072  1.312   0.30 25.47 ?  157 ASP   A HB3  1 
ATOM   3286 N  N    A LYS   A 1 158 ? 5.597  -0.129  4.453   0.70 22.10 ?  158 LYS   A N    1 
ATOM   3287 N  N    B LYS   A 1 158 ? 5.272  -0.553  4.034   0.30 18.81 ?  158 LYS   A N    1 
ATOM   3288 C  CA   A LYS   A 1 158 ? 4.632  -1.067  5.018   0.70 23.24 ?  158 LYS   A CA   1 
ATOM   3289 C  CA   B LYS   A 1 158 ? 4.249  -1.456  4.555   0.30 18.73 ?  158 LYS   A CA   1 
ATOM   3290 C  C    A LYS   A 1 158 ? 3.905  -1.828  3.919   0.70 22.39 ?  158 LYS   A C    1 
ATOM   3291 C  C    B LYS   A 1 158 ? 3.668  -2.338  3.453   0.30 17.46 ?  158 LYS   A C    1 
ATOM   3292 O  O    A LYS   A 1 158 ? 3.702  -3.043  4.025   0.70 22.08 ?  158 LYS   A O    1 
ATOM   3293 O  O    B LYS   A 1 158 ? 3.576  -3.563  3.601   0.30 16.59 ?  158 LYS   A O    1 
ATOM   3294 C  CB   A LYS   A 1 158 ? 3.644  -0.335  5.930   0.70 25.18 ?  158 LYS   A CB   1 
ATOM   3295 C  CB   B LYS   A 1 158 ? 3.156  -0.627  5.236   0.30 20.33 ?  158 LYS   A CB   1 
ATOM   3296 C  CG   A LYS   A 1 158 ? 2.438  -1.172  6.376   0.70 27.13 ?  158 LYS   A CG   1 
ATOM   3297 C  CG   B LYS   A 1 158 ? 1.883  -1.384  5.572   0.30 21.85 ?  158 LYS   A CG   1 
ATOM   3298 C  CD   A LYS   A 1 158 ? 2.836  -2.437  7.146   0.70 28.55 ?  158 LYS   A CD   1 
ATOM   3299 C  CD   B LYS   A 1 158 ? 2.169  -2.595  6.433   0.30 23.28 ?  158 LYS   A CD   1 
ATOM   3300 C  CE   A LYS   A 1 158 ? 1.597  -3.149  7.698   0.70 29.30 ?  158 LYS   A CE   1 
ATOM   3301 C  CE   B LYS   A 1 158 ? 1.068  -2.817  7.450   0.30 24.33 ?  158 LYS   A CE   1 
ATOM   3302 N  NZ   A LYS   A 1 158 ? 1.869  -4.528  8.201   0.70 29.80 ?  158 LYS   A NZ   1 
ATOM   3303 N  NZ   B LYS   A 1 158 ? 1.124  -4.188  8.020   0.30 24.92 ?  158 LYS   A NZ   1 
ATOM   3304 H  H    A LYS   A 1 158 ? 5.437  0.700   4.616   0.70 26.48 ?  158 LYS   A H    1 
ATOM   3305 H  H    B LYS   A 1 158 ? 5.106  0.280   4.156   0.30 22.53 ?  158 LYS   A H    1 
ATOM   3306 H  HA   A LYS   A 1 158 ? 5.106  -1.713  5.564   0.70 27.85 ?  158 LYS   A HA   1 
ATOM   3307 H  HA   B LYS   A 1 158 ? 4.647  -2.033  5.225   0.30 22.44 ?  158 LYS   A HA   1 
ATOM   3308 H  HB2  A LYS   A 1 158 ? 4.110  -0.049  6.733   0.70 30.17 ?  158 LYS   A HB2  1 
ATOM   3309 H  HB2  B LYS   A 1 158 ? 3.511  -0.272  6.069   0.30 24.36 ?  158 LYS   A HB2  1 
ATOM   3310 H  HB3  A LYS   A 1 158 ? 3.302  0.442   5.461   0.70 30.17 ?  158 LYS   A HB3  1 
ATOM   3311 H  HB3  B LYS   A 1 158 ? 2.914  0.107   4.651   0.30 24.36 ?  158 LYS   A HB3  1 
ATOM   3312 H  HG2  A LYS   A 1 158 ? 1.884  -0.633  6.961   0.70 32.52 ?  158 LYS   A HG2  1 
ATOM   3313 H  HG2  B LYS   A 1 158 ? 1.287  -0.798  6.064   0.30 26.19 ?  158 LYS   A HG2  1 
ATOM   3314 H  HG3  A LYS   A 1 158 ? 1.925  -1.440  5.597   0.70 32.52 ?  158 LYS   A HG3  1 
ATOM   3315 H  HG3  B LYS   A 1 158 ? 1.455  -1.681  4.753   0.30 26.19 ?  158 LYS   A HG3  1 
ATOM   3316 H  HD2  A LYS   A 1 158 ? 3.297  -3.046  6.549   0.70 34.22 ?  158 LYS   A HD2  1 
ATOM   3317 H  HD2  B LYS   A 1 158 ? 2.227  -3.383  5.871   0.30 27.89 ?  158 LYS   A HD2  1 
ATOM   3318 H  HD3  A LYS   A 1 158 ? 3.409  -2.193  7.890   0.70 34.22 ?  158 LYS   A HD3  1 
ATOM   3319 H  HD3  B LYS   A 1 158 ? 3.003  -2.460  6.910   0.30 27.89 ?  158 LYS   A HD3  1 
ATOM   3320 H  HE2  A LYS   A 1 158 ? 1.232  -2.629  8.430   0.70 35.12 ?  158 LYS   A HE2  1 
ATOM   3321 H  HE2  B LYS   A 1 158 ? 1.175  -2.178  8.175   0.30 29.16 ?  158 LYS   A HE2  1 
ATOM   3322 H  HE3  A LYS   A 1 158 ? 0.941  -3.216  6.992   0.70 35.12 ?  158 LYS   A HE3  1 
ATOM   3323 H  HE3  B LYS   A 1 158 ? 0.209  -2.693  7.020   0.30 29.16 ?  158 LYS   A HE3  1 
ATOM   3324 H  HZ1  A LYS   A 1 158 ? 1.118  -4.892  8.511   0.70 35.72 ?  158 LYS   A HZ1  1 
ATOM   3325 H  HZ1  B LYS   A 1 158 ? 0.471  -4.296  8.613   0.30 29.86 ?  158 LYS   A HZ1  1 
ATOM   3326 H  HZ2  A LYS   A 1 158 ? 2.184  -5.035  7.540   0.70 35.72 ?  158 LYS   A HZ2  1 
ATOM   3327 H  HZ2  B LYS   A 1 158 ? 1.027  -4.788  7.369   0.30 29.86 ?  158 LYS   A HZ2  1 
ATOM   3328 H  HZ3  A LYS   A 1 158 ? 2.470  -4.503  8.857   0.70 35.72 ?  158 LYS   A HZ3  1 
ATOM   3329 H  HZ3  B LYS   A 1 158 ? 1.907  -4.319  8.421   0.30 29.86 ?  158 LYS   A HZ3  1 
ATOM   3330 N  N    A ASN   A 1 159 ? 3.507  -1.136  2.852   0.70 22.62 ?  159 ASN   A N    1 
ATOM   3331 N  N    B ASN   A 1 159 ? 3.264  -1.729  2.339   0.30 17.83 ?  159 ASN   A N    1 
ATOM   3332 C  CA   A ASN   A 1 159 ? 2.861  -1.833  1.747   0.70 22.85 ?  159 ASN   A CA   1 
ATOM   3333 C  CA   B ASN   A 1 159 ? 2.605  -2.491  1.285   0.30 18.69 ?  159 ASN   A CA   1 
ATOM   3334 C  C    A ASN   A 1 159 ? 3.772  -2.912  1.171   0.70 21.40 ?  159 ASN   A C    1 
ATOM   3335 C  C    B ASN   A 1 159 ? 3.552  -3.502  0.637   0.30 17.12 ?  159 ASN   A C    1 
ATOM   3336 O  O    A ASN   A 1 159 ? 3.330  -4.036  0.912   0.70 20.55 ?  159 ASN   A O    1 
ATOM   3337 O  O    B ASN   A 1 159 ? 3.124  -4.606  0.273   0.30 17.13 ?  159 ASN   A O    1 
ATOM   3338 C  CB   A ASN   A 1 159 ? 2.410  -0.831  0.681   0.70 25.46 ?  159 ASN   A CB   1 
ATOM   3339 C  CB   B ASN   A 1 159 ? 1.982  -1.519  0.280   0.30 21.46 ?  159 ASN   A CB   1 
ATOM   3340 C  CG   A ASN   A 1 159 ? 1.129  -0.108  1.067   0.70 28.67 ?  159 ASN   A CG   1 
ATOM   3341 C  CG   B ASN   A 1 159 ? 1.225  -0.386  0.964   0.30 24.24 ?  159 ASN   A CG   1 
ATOM   3342 O  OD1  A ASN   A 1 159 ? 0.267  -0.679  1.731   0.70 30.13 ?  159 ASN   A OD1  1 
ATOM   3343 O  OD1  B ASN   A 1 159 ? 1.644  0.769   0.912   0.30 25.19 ?  159 ASN   A OD1  1 
ATOM   3344 N  ND2  A ASN   A 1 159 ? 1.000  1.146   0.651   0.70 29.81 ?  159 ASN   A ND2  1 
ATOM   3345 N  ND2  B ASN   A 1 159 ? 0.112  -0.719  1.622   0.30 25.25 ?  159 ASN   A ND2  1 
ATOM   3346 H  H    A ASN   A 1 159 ? 3.596  -0.286  2.753   0.70 27.11 ?  159 ASN   A H    1 
ATOM   3347 H  H    B ASN   A 1 159 ? 3.355  -0.886  2.179   0.30 21.35 ?  159 ASN   A H    1 
ATOM   3348 H  HA   A ASN   A 1 159 ? 2.067  -2.273  2.085   0.70 27.38 ?  159 ASN   A HA   1 
ATOM   3349 H  HA   B ASN   A 1 159 ? 1.879  -2.990  1.681   0.30 22.39 ?  159 ASN   A HA   1 
ATOM   3350 H  HB2  A ASN   A 1 159 ? 3.097  -0.162  0.556   0.70 30.51 ?  159 ASN   A HB2  1 
ATOM   3351 H  HB2  B ASN   A 1 159 ? 2.679  -1.116  -0.259  0.30 25.72 ?  159 ASN   A HB2  1 
ATOM   3352 H  HB3  A ASN   A 1 159 ? 2.248  -1.305  -0.150  0.70 30.51 ?  159 ASN   A HB3  1 
ATOM   3353 H  HB3  B ASN   A 1 159 ? 1.353  -1.992  -0.280  0.30 25.72 ?  159 ASN   A HB3  1 
ATOM   3354 H  HD21 A ASN   A 1 159 ? 0.290  1.589   0.843   0.70 35.74 ?  159 ASN   A HD21 1 
ATOM   3355 H  HD21 B ASN   A 1 159 ? -0.353 -0.117  2.034   0.30 30.26 ?  159 ASN   A HD21 1 
ATOM   3356 H  HD22 A ASN   A 1 159 ? 1.624  1.511   0.194   0.70 35.74 ?  159 ASN   A HD22 1 
ATOM   3357 H  HD22 B ASN   A 1 159 ? -0.149 -1.538  1.636   0.30 30.26 ?  159 ASN   A HD22 1 
ATOM   3358 N  N    A LEU   A 1 160 ? 5.057  -2.608  1.000   0.70 20.39 ?  160 LEU   A N    1 
ATOM   3359 N  N    B LEU   A 1 160 ? 4.841  -3.166  0.520   0.30 16.21 ?  160 LEU   A N    1 
ATOM   3360 C  CA   A LEU   A 1 160 ? 5.961  -3.621  0.464   0.70 19.42 ?  160 LEU   A CA   1 
ATOM   3361 C  CA   B LEU   A 1 160 ? 5.816  -4.138  0.026   0.30 16.27 ?  160 LEU   A CA   1 
ATOM   3362 C  C    A LEU   A 1 160 ? 6.136  -4.777  1.441   0.70 18.95 ?  160 LEU   A C    1 
ATOM   3363 C  C    B LEU   A 1 160 ? 6.050  -5.245  1.049   0.30 15.56 ?  160 LEU   A C    1 
ATOM   3364 O  O    A LEU   A 1 160 ? 6.175  -5.944  1.033   0.70 19.91 ?  160 LEU   A O    1 
ATOM   3365 O  O    B LEU   A 1 160 ? 6.085  -6.432  0.702   0.30 15.36 ?  160 LEU   A O    1 
ATOM   3366 C  CB   A LEU   A 1 160 ? 7.311  -3.005  0.113   0.70 19.14 ?  160 LEU   A CB   1 
ATOM   3367 C  CB   B LEU   A 1 160 ? 7.133  -3.437  -0.310  0.30 17.50 ?  160 LEU   A CB   1 
ATOM   3368 C  CG   A LEU   A 1 160 ? 8.342  -4.035  -0.350  0.70 19.36 ?  160 LEU   A CG   1 
ATOM   3369 C  CG   B LEU   A 1 160 ? 7.178  -2.599  -1.589  0.30 19.20 ?  160 LEU   A CG   1 
ATOM   3370 C  CD1  A LEU   A 1 160 ? 7.869  -4.760  -1.590  0.70 19.90 ?  160 LEU   A CD1  1 
ATOM   3371 C  CD1  B LEU   A 1 160 ? 8.510  -1.884  -1.733  0.30 19.66 ?  160 LEU   A CD1  1 
ATOM   3372 C  CD2  A LEU   A 1 160 ? 9.657  -3.352  -0.619  0.70 19.25 ?  160 LEU   A CD2  1 
ATOM   3373 C  CD2  B LEU   A 1 160 ? 6.911  -3.478  -2.799  0.30 19.82 ?  160 LEU   A CD2  1 
ATOM   3374 H  H    A LEU   A 1 160 ? 5.421  -1.842  1.186   0.70 24.42 ?  160 LEU   A H    1 
ATOM   3375 H  H    B LEU   A 1 160 ? 5.175  -2.395  0.723   0.30 19.41 ?  160 LEU   A H    1 
ATOM   3376 H  HA   A LEU   A 1 160 ? 5.575  -3.965  -0.352  0.70 23.26 ?  160 LEU   A HA   1 
ATOM   3377 H  HA   B LEU   A 1 160 ? 5.474  -4.542  -0.783  0.30 19.49 ?  160 LEU   A HA   1 
ATOM   3378 H  HB2  A LEU   A 1 160 ? 7.195  -2.350  -0.603  0.70 22.94 ?  160 LEU   A HB2  1 
ATOM   3379 H  HB2  B LEU   A 1 160 ? 7.358  -2.851  0.428   0.30 20.96 ?  160 LEU   A HB2  1 
ATOM   3380 H  HB3  A LEU   A 1 160 ? 7.672  -2.568  0.898   0.70 22.94 ?  160 LEU   A HB3  1 
ATOM   3381 H  HB3  B LEU   A 1 160 ? 7.822  -4.112  -0.394  0.30 20.96 ?  160 LEU   A HB3  1 
ATOM   3382 H  HG   A LEU   A 1 160 ? 8.487  -4.689  0.350   0.70 23.19 ?  160 LEU   A HG   1 
ATOM   3383 H  HG   B LEU   A 1 160 ? 6.490  -1.922  -1.545  0.30 23.01 ?  160 LEU   A HG   1 
ATOM   3384 H  HD11 A LEU   A 1 160 ? 8.594  -5.298  -1.935  0.70 23.84 ?  160 LEU   A HD11 1 
ATOM   3385 H  HD11 B LEU   A 1 160 ? 8.504  -1.366  -2.554  0.30 23.55 ?  160 LEU   A HD11 1 
ATOM   3386 H  HD12 A LEU   A 1 160 ? 7.116  -5.326  -1.357  0.70 23.84 ?  160 LEU   A HD12 1 
ATOM   3387 H  HD12 B LEU   A 1 160 ? 8.636  -1.295  -0.972  0.30 23.55 ?  160 LEU   A HD12 1 
ATOM   3388 H  HD13 A LEU   A 1 160 ? 7.597  -4.104  -2.252  0.70 23.84 ?  160 LEU   A HD13 1 
ATOM   3389 H  HD13 B LEU   A 1 160 ? 9.222  -2.542  -1.763  0.30 23.55 ?  160 LEU   A HD13 1 
ATOM   3390 H  HD21 A LEU   A 1 160 ? 10.305 -4.016  -0.905  0.70 23.06 ?  160 LEU   A HD21 1 
ATOM   3391 H  HD21 B LEU   A 1 160 ? 7.121  -2.980  -3.603  0.30 23.75 ?  160 LEU   A HD21 1 
ATOM   3392 H  HD22 A LEU   A 1 160 ? 9.533  -2.690  -1.318  0.70 23.06 ?  160 LEU   A HD22 1 
ATOM   3393 H  HD22 B LEU   A 1 160 ? 7.471  -4.269  -2.743  0.30 23.75 ?  160 LEU   A HD22 1 
ATOM   3394 H  HD23 A LEU   A 1 160 ? 9.963  -2.921  0.194   0.70 23.06 ?  160 LEU   A HD23 1 
ATOM   3395 H  HD23 B LEU   A 1 160 ? 5.976  -3.735  -2.802  0.30 23.75 ?  160 LEU   A HD23 1 
ATOM   3396 N  N    A TYR   A 1 161 ? 6.242  -4.472  2.733   0.70 18.37 ?  161 TYR   A N    1 
ATOM   3397 N  N    B TYR   A 1 161 ? 6.228  -4.867  2.317   0.30 15.39 ?  161 TYR   A N    1 
ATOM   3398 C  CA   A TYR   A 1 161 ? 6.377  -5.525  3.731   0.70 18.27 ?  161 TYR   A CA   1 
ATOM   3399 C  CA   B TYR   A 1 161 ? 6.355  -5.844  3.395   0.30 15.61 ?  161 TYR   A CA   1 
ATOM   3400 C  C    A TYR   A 1 161 ? 5.248  -6.550  3.627   0.70 19.09 ?  161 TYR   A C    1 
ATOM   3401 C  C    B TYR   A 1 161 ? 5.175  -6.808  3.392   0.30 16.25 ?  161 TYR   A C    1 
ATOM   3402 O  O    A TYR   A 1 161 ? 5.487  -7.762  3.666   0.70 19.01 ?  161 TYR   A O    1 
ATOM   3403 O  O    B TYR   A 1 161 ? 5.354  -8.031  3.386   0.30 15.82 ?  161 TYR   A O    1 
ATOM   3404 C  CB   A TYR   A 1 161 ? 6.430  -4.919  5.132   0.70 18.60 ?  161 TYR   A CB   1 
ATOM   3405 C  CB   B TYR   A 1 161 ? 6.447  -5.100  4.732   0.30 15.66 ?  161 TYR   A CB   1 
ATOM   3406 C  CG   A TYR   A 1 161 ? 6.336  -5.970  6.199   0.70 18.38 ?  161 TYR   A CG   1 
ATOM   3407 C  CG   B TYR   A 1 161 ? 6.338  -5.968  5.971   0.30 16.12 ?  161 TYR   A CG   1 
ATOM   3408 C  CD1  A TYR   A 1 161 ? 7.449  -6.707  6.567   0.70 18.01 ?  161 TYR   A CD1  1 
ATOM   3409 C  CD1  B TYR   A 1 161 ? 7.467  -6.527  6.554   0.30 16.34 ?  161 TYR   A CD1  1 
ATOM   3410 C  CD2  A TYR   A 1 161 ? 5.124  -6.250  6.818   0.70 18.20 ?  161 TYR   A CD2  1 
ATOM   3411 C  CD2  B TYR   A 1 161 ? 5.106  -6.205  6.575   0.30 16.33 ?  161 TYR   A CD2  1 
ATOM   3412 C  CE1  A TYR   A 1 161 ? 7.365  -7.688  7.526   0.70 17.97 ?  161 TYR   A CE1  1 
ATOM   3413 C  CE1  B TYR   A 1 161 ? 7.374  -7.314  7.689   0.30 16.58 ?  161 TYR   A CE1  1 
ATOM   3414 C  CE2  A TYR   A 1 161 ? 5.029  -7.229  7.781   0.70 18.26 ?  161 TYR   A CE2  1 
ATOM   3415 C  CE2  B TYR   A 1 161 ? 5.004  -6.992  7.713   0.30 16.54 ?  161 TYR   A CE2  1 
ATOM   3416 C  CZ   A TYR   A 1 161 ? 6.155  -7.942  8.131   0.70 18.21 ?  161 TYR   A CZ   1 
ATOM   3417 C  CZ   B TYR   A 1 161 ? 6.142  -7.543  8.265   0.30 16.93 ?  161 TYR   A CZ   1 
ATOM   3418 O  OH   A TYR   A 1 161 ? 6.068  -8.912  9.093   0.70 18.38 ?  161 TYR   A OH   1 
ATOM   3419 O  OH   B TYR   A 1 161 ? 6.052  -8.325  9.395   0.30 17.77 ?  161 TYR   A OH   1 
ATOM   3420 H  H    A TYR   A 1 161 ? 6.230  -3.670  3.049   0.70 22.00 ?  161 TYR   A H    1 
ATOM   3421 H  H    B TYR   A 1 161 ? 6.276  -4.056  2.576   0.30 18.43 ?  161 TYR   A H    1 
ATOM   3422 H  HA   A TYR   A 1 161 ? 7.202  -5.989  3.578   0.70 21.88 ?  161 TYR   A HA   1 
ATOM   3423 H  HA   B TYR   A 1 161 ? 7.167  -6.361  3.276   0.30 18.70 ?  161 TYR   A HA   1 
ATOM   3424 H  HB2  A TYR   A 1 161 ? 7.268  -4.447  5.242   0.70 22.28 ?  161 TYR   A HB2  1 
ATOM   3425 H  HB2  B TYR   A 1 161 ? 7.300  -4.644  4.769   0.30 18.75 ?  161 TYR   A HB2  1 
ATOM   3426 H  HB3  A TYR   A 1 161 ? 5.684  -4.302  5.246   0.70 22.28 ?  161 TYR   A HB3  1 
ATOM   3427 H  HB3  B TYR   A 1 161 ? 5.729  -4.447  4.768   0.30 18.75 ?  161 TYR   A HB3  1 
ATOM   3428 H  HD1  A TYR   A 1 161 ? 8.263  -6.537  6.155   0.70 21.57 ?  161 TYR   A HD1  1 
ATOM   3429 H  HD1  B TYR   A 1 161 ? 8.299  -6.376  6.170   0.30 19.57 ?  161 TYR   A HD1  1 
ATOM   3430 H  HD2  A TYR   A 1 161 ? 4.360  -5.771  6.581   0.70 21.80 ?  161 TYR   A HD2  1 
ATOM   3431 H  HD2  B TYR   A 1 161 ? 4.335  -5.836  6.207   0.30 19.56 ?  161 TYR   A HD2  1 
ATOM   3432 H  HE1  A TYR   A 1 161 ? 8.116  -8.177  7.768   0.70 21.53 ?  161 TYR   A HE1  1 
ATOM   3433 H  HE1  B TYR   A 1 161 ? 8.138  -7.685  8.067   0.30 19.85 ?  161 TYR   A HE1  1 
ATOM   3434 H  HE2  A TYR   A 1 161 ? 4.206  -7.407  8.191   0.70 21.87 ?  161 TYR   A HE2  1 
ATOM   3435 H  HE2  B TYR   A 1 161 ? 4.170  -7.145  8.105   0.30 19.82 ?  161 TYR   A HE2  1 
ATOM   3436 H  HH   A TYR   A 1 161 ? 6.807  -9.281  9.211   0.70 22.02 ?  161 TYR   A HH   1 
ATOM   3437 H  HH   B TYR   A 1 161 ? 6.810  -8.596  9.626   0.30 21.28 ?  161 TYR   A HH   1 
ATOM   3438 N  N    A ASP   A 1 162 ? 4.001  -6.082  3.497   0.70 20.25 ?  162 ASP   A N    1 
ATOM   3439 N  N    B ASP   A 1 162 ? 3.953  -6.266  3.391   0.30 17.58 ?  162 ASP   A N    1 
ATOM   3440 C  CA   A ASP   A 1 162 ? 2.873  -7.014  3.460   0.70 21.12 ?  162 ASP   A CA   1 
ATOM   3441 C  CA   B ASP   A 1 162 ? 2.760  -7.104  3.315   0.30 18.90 ?  162 ASP   A CA   1 
ATOM   3442 C  C    A ASP   A 1 162 ? 2.921  -7.890  2.213   0.70 21.02 ?  162 ASP   A C    1 
ATOM   3443 C  C    B ASP   A 1 162 ? 2.808  -8.012  2.095   0.30 19.44 ?  162 ASP   A C    1 
ATOM   3444 O  O    A ASP   A 1 162 ? 2.569  -9.075  2.265   0.70 22.01 ?  162 ASP   A O    1 
ATOM   3445 O  O    B ASP   A 1 162 ? 2.474  -9.200  2.178   0.30 19.69 ?  162 ASP   A O    1 
ATOM   3446 C  CB   A ASP   A 1 162 ? 1.537  -6.265  3.531   0.70 22.24 ?  162 ASP   A CB   1 
ATOM   3447 C  CB   B ASP   A 1 162 ? 1.506  -6.227  3.272   0.30 19.97 ?  162 ASP   A CB   1 
ATOM   3448 C  CG   A ASP   A 1 162 ? 1.266  -5.641  4.893   0.70 23.64 ?  162 ASP   A CG   1 
ATOM   3449 C  CG   B ASP   A 1 162 ? 1.170  -5.608  4.614   0.30 20.97 ?  162 ASP   A CG   1 
ATOM   3450 O  OD1  A ASP   A 1 162 ? 1.883  -6.060  5.892   0.70 24.56 ?  162 ASP   A OD1  1 
ATOM   3451 O  OD1  B ASP   A 1 162 ? 1.860  -5.908  5.608   0.30 21.57 ?  162 ASP   A OD1  1 
ATOM   3452 O  OD2  A ASP   A 1 162 ? 0.389  -4.746  4.964   0.70 24.84 -1 162 ASP   A OD2  1 
ATOM   3453 O  OD2  B ASP   A 1 162 ? 0.195  -4.826  4.672   0.30 21.31 -1 162 ASP   A OD2  1 
ATOM   3454 H  H    A ASP   A 1 162 ? 3.777  -5.253  3.424   0.70 24.26 ?  162 ASP   A H    1 
ATOM   3455 H  H    B ASP   A 1 162 ? 3.793  -5.425  3.430   0.30 21.06 ?  162 ASP   A H    1 
ATOM   3456 H  HA   A ASP   A 1 162 ? 2.920  -7.601  4.229   0.70 25.30 ?  162 ASP   A HA   1 
ATOM   3457 H  HA   B ASP   A 1 162 ? 2.709  -7.664  4.103   0.30 22.65 ?  162 ASP   A HA   1 
ATOM   3458 H  HB2  A ASP   A 1 162 ? 1.530  -5.554  2.877   0.70 26.65 ?  162 ASP   A HB2  1 
ATOM   3459 H  HB2  B ASP   A 1 162 ? 1.637  -5.510  2.631   0.30 23.92 ?  162 ASP   A HB2  1 
ATOM   3460 H  HB3  A ASP   A 1 162 ? 0.809  -6.887  3.356   0.70 26.65 ?  162 ASP   A HB3  1 
ATOM   3461 H  HB3  B ASP   A 1 162 ? 0.743  -6.766  3.016   0.30 23.92 ?  162 ASP   A HB3  1 
ATOM   3462 N  N    A LYS   A 1 163 ? 3.360  -7.330  1.084   0.70 21.64 ?  163 LYS   A N    1 
ATOM   3463 N  N    B LYS   A 1 163 ? 3.221  -7.468  0.950   0.30 20.16 ?  163 LYS   A N    1 
ATOM   3464 C  CA   A LYS   A 1 163 ? 3.447  -8.108  -0.148  0.70 22.31 ?  163 LYS   A CA   1 
ATOM   3465 C  CA   B LYS   A 1 163 ? 3.353  -8.284  -0.250  0.30 21.03 ?  163 LYS   A CA   1 
ATOM   3466 C  C    A LYS   A 1 163 ? 4.539  -9.170  -0.063  0.70 21.80 ?  163 LYS   A C    1 
ATOM   3467 C  C    B LYS   A 1 163 ? 4.456  -9.324  -0.091  0.30 20.34 ?  163 LYS   A C    1 
ATOM   3468 O  O    A LYS   A 1 163 ? 4.380  -10.274 -0.595  0.70 22.69 ?  163 LYS   A O    1 
ATOM   3469 O  O    B LYS   A 1 163 ? 4.283  -10.486 -0.476  0.30 21.00 ?  163 LYS   A O    1 
ATOM   3470 C  CB   A LYS   A 1 163 ? 3.694  -7.173  -1.332  0.70 24.99 ?  163 LYS   A CB   1 
ATOM   3471 C  CB   B LYS   A 1 163 ? 3.639  -7.388  -1.449  0.30 22.90 ?  163 LYS   A CB   1 
ATOM   3472 C  CG   A LYS   A 1 163 ? 3.761  -7.881  -2.672  0.70 28.13 ?  163 LYS   A CG   1 
ATOM   3473 C  CG   B LYS   A 1 163 ? 2.441  -7.126  -2.359  0.30 24.81 ?  163 LYS   A CG   1 
ATOM   3474 C  CD   A LYS   A 1 163 ? 4.098  -6.914  -3.790  0.70 31.66 ?  163 LYS   A CD   1 
ATOM   3475 C  CD   B LYS   A 1 163 ? 2.865  -6.362  -3.609  0.30 26.56 ?  163 LYS   A CD   1 
ATOM   3476 C  CE   A LYS   A 1 163 ? 4.055  -7.604  -5.143  0.70 34.34 ?  163 LYS   A CE   1 
ATOM   3477 C  CE   B LYS   A 1 163 ? 4.189  -6.891  -4.161  0.30 28.00 ?  163 LYS   A CE   1 
ATOM   3478 N  NZ   A LYS   A 1 163 ? 4.698  -6.789  -6.209  0.70 35.55 ?  163 LYS   A NZ   1 
ATOM   3479 N  NZ   B LYS   A 1 163 ? 4.573  -6.256  -5.435  0.30 28.75 ?  163 LYS   A NZ   1 
ATOM   3480 H  H    A LYS   A 1 163 ? 3.609  -6.510  1.011   0.70 25.94 ?  163 LYS   A H    1 
ATOM   3481 H  H    B LYS   A 1 163 ? 3.432  -6.640  0.843   0.30 24.15 ?  163 LYS   A H    1 
ATOM   3482 H  HA   A LYS   A 1 163 ? 2.601  -8.557  -0.295  0.70 26.74 ?  163 LYS   A HA   1 
ATOM   3483 H  HA   B LYS   A 1 163 ? 2.524  -8.749  -0.422  0.30 25.20 ?  163 LYS   A HA   1 
ATOM   3484 H  HB2  A LYS   A 1 163 ? 2.969  -6.527  -1.376  0.70 29.95 ?  163 LYS   A HB2  1 
ATOM   3485 H  HB2  B LYS   A 1 163 ? 3.969  -6.521  -1.153  0.30 27.44 ?  163 LYS   A HB2  1 
ATOM   3486 H  HB3  A LYS   A 1 163 ? 4.535  -6.712  -1.197  0.70 29.95 ?  163 LYS   A HB3  1 
ATOM   3487 H  HB3  B LYS   A 1 163 ? 4.320  -7.845  -1.955  0.30 27.44 ?  163 LYS   A HB3  1 
ATOM   3488 H  HG2  A LYS   A 1 163 ? 4.452  -8.562  -2.644  0.70 33.71 ?  163 LYS   A HG2  1 
ATOM   3489 H  HG2  B LYS   A 1 163 ? 2.051  -7.970  -2.636  0.30 29.73 ?  163 LYS   A HG2  1 
ATOM   3490 H  HG3  A LYS   A 1 163 ? 2.900  -8.285  -2.864  0.70 33.71 ?  163 LYS   A HG3  1 
ATOM   3491 H  HG3  B LYS   A 1 163 ? 1.780  -6.591  -1.885  0.30 29.73 ?  163 LYS   A HG3  1 
ATOM   3492 H  HD2  A LYS   A 1 163 ? 3.450  -6.191  -3.795  0.70 37.96 ?  163 LYS   A HD2  1 
ATOM   3493 H  HD2  B LYS   A 1 163 ? 2.185  -6.466  -4.295  0.30 31.84 ?  163 LYS   A HD2  1 
ATOM   3494 H  HD3  A LYS   A 1 163 ? 4.992  -6.563  -3.653  0.70 37.96 ?  163 LYS   A HD3  1 
ATOM   3495 H  HD3  B LYS   A 1 163 ? 2.978  -5.424  -3.387  0.30 31.84 ?  163 LYS   A HD3  1 
ATOM   3496 H  HE2  A LYS   A 1 163 ? 4.517  -8.454  -5.087  0.70 41.17 ?  163 LYS   A HE2  1 
ATOM   3497 H  HE2  B LYS   A 1 163 ? 4.901  -6.688  -3.531  0.30 33.56 ?  163 LYS   A HE2  1 
ATOM   3498 H  HE3  A LYS   A 1 163 ? 3.130  -7.749  -5.392  0.70 41.17 ?  163 LYS   A HE3  1 
ATOM   3499 H  HE3  B LYS   A 1 163 ? 4.117  -7.856  -4.284  0.30 33.56 ?  163 LYS   A HE3  1 
ATOM   3500 H  HZ1  A LYS   A 1 163 ? 4.658  -7.220  -6.986  0.70 42.62 ?  163 LYS   A HZ1  1 
ATOM   3501 H  HZ1  B LYS   A 1 163 ? 5.347  -6.593  -5.715  0.30 34.47 ?  163 LYS   A HZ1  1 
ATOM   3502 H  HZ2  A LYS   A 1 163 ? 4.278  -6.008  -6.287  0.70 42.62 ?  163 LYS   A HZ2  1 
ATOM   3503 H  HZ2  B LYS   A 1 163 ? 3.949  -6.407  -6.046  0.30 34.47 ?  163 LYS   A HZ2  1 
ATOM   3504 H  HZ3  A LYS   A 1 163 ? 5.551  -6.639  -6.004  0.70 42.62 ?  163 LYS   A HZ3  1 
ATOM   3505 H  HZ3  B LYS   A 1 163 ? 4.663  -5.379  -5.316  0.30 34.47 ?  163 LYS   A HZ3  1 
ATOM   3506 N  N    A LEU   A 1 164 ? 5.663  -8.847  0.581   0.70 20.27 ?  164 LEU   A N    1 
ATOM   3507 N  N    B LEU   A 1 164 ? 5.597  -8.922  0.474   0.30 19.13 ?  164 LEU   A N    1 
ATOM   3508 C  CA   A LEU   A 1 164 ? 6.755  -9.811  0.714   0.70 19.49 ?  164 LEU   A CA   1 
ATOM   3509 C  CA   B LEU   A 1 164 ? 6.707  -9.851  0.662   0.30 18.31 ?  164 LEU   A CA   1 
ATOM   3510 C  C    A LEU   A 1 164 ? 6.333  -11.002 1.562   0.70 19.71 ?  164 LEU   A C    1 
ATOM   3511 C  C    B LEU   A 1 164 ? 6.292  -11.024 1.539   0.30 18.72 ?  164 LEU   A C    1 
ATOM   3512 O  O    A LEU   A 1 164 ? 6.668  -12.151 1.254   0.70 20.44 ?  164 LEU   A O    1 
ATOM   3513 O  O    B LEU   A 1 164 ? 6.587  -12.184 1.228   0.30 18.91 ?  164 LEU   A O    1 
ATOM   3514 C  CB   A LEU   A 1 164 ? 7.965  -9.127  1.349   0.70 19.20 ?  164 LEU   A CB   1 
ATOM   3515 C  CB   B LEU   A 1 164 ? 7.895  -9.113  1.279   0.30 17.42 ?  164 LEU   A CB   1 
ATOM   3516 C  CG   A LEU   A 1 164 ? 8.676  -8.063  0.510   0.70 19.05 ?  164 LEU   A CG   1 
ATOM   3517 C  CG   B LEU   A 1 164 ? 8.715  -8.250  0.320   0.30 16.61 ?  164 LEU   A CG   1 
ATOM   3518 C  CD1  A LEU   A 1 164 ? 9.641  -7.235  1.361   0.70 18.66 ?  164 LEU   A CD1  1 
ATOM   3519 C  CD1  B LEU   A 1 164 ? 9.510  -7.204  1.084   0.30 16.26 ?  164 LEU   A CD1  1 
ATOM   3520 C  CD2  A LEU   A 1 164 ? 9.416  -8.725  -0.642  0.70 19.17 ?  164 LEU   A CD2  1 
ATOM   3521 C  CD2  B LEU   A 1 164 ? 9.645  -9.123  -0.507  0.30 16.15 ?  164 LEU   A CD2  1 
ATOM   3522 H  H    A LEU   A 1 164 ? 5.818  -8.085  0.947   0.70 24.29 ?  164 LEU   A H    1 
ATOM   3523 H  H    B LEU   A 1 164 ? 5.747  -8.126  0.764   0.30 22.92 ?  164 LEU   A H    1 
ATOM   3524 H  HA   A LEU   A 1 164 ? 7.008  -10.136 -0.163  0.70 23.35 ?  164 LEU   A HA   1 
ATOM   3525 H  HA   B LEU   A 1 164 ? 6.982  -10.198 -0.200  0.30 21.93 ?  164 LEU   A HA   1 
ATOM   3526 H  HB2  A LEU   A 1 164 ? 7.677  -8.700  2.169   0.70 23.00 ?  164 LEU   A HB2  1 
ATOM   3527 H  HB2  B LEU   A 1 164 ? 7.565  -8.531  1.980   0.30 20.86 ?  164 LEU   A HB2  1 
ATOM   3528 H  HB3  A LEU   A 1 164 ? 8.623  -9.809  1.559   0.70 23.00 ?  164 LEU   A HB3  1 
ATOM   3529 H  HB3  B LEU   A 1 164 ? 8.498  -9.770  1.662   0.30 20.86 ?  164 LEU   A HB3  1 
ATOM   3530 H  HG   A LEU   A 1 164 ? 8.017  -7.458  0.139   0.70 22.82 ?  164 LEU   A HG   1 
ATOM   3531 H  HG   B LEU   A 1 164 ? 8.116  -7.790  -0.287  0.30 19.90 ?  164 LEU   A HG   1 
ATOM   3532 H  HD11 A LEU   A 1 164 ? 10.072 -6.570  0.799   0.70 22.36 ?  164 LEU   A HD11 1 
ATOM   3533 H  HD11 B LEU   A 1 164 ? 10.028 -6.678  0.456   0.30 19.48 ?  164 LEU   A HD11 1 
ATOM   3534 H  HD12 A LEU   A 1 164 ? 9.143  -6.792  2.068   0.70 22.36 ?  164 LEU   A HD12 1 
ATOM   3535 H  HD12 B LEU   A 1 164 ? 8.892  -6.629  1.565   0.30 19.48 ?  164 LEU   A HD12 1 
ATOM   3536 H  HD13 A LEU   A 1 164 ? 10.310 -7.822  1.748   0.70 22.36 ?  164 LEU   A HD13 1 
ATOM   3537 H  HD13 B LEU   A 1 164 ? 10.101 -7.650  1.710   0.30 19.48 ?  164 LEU   A HD13 1 
ATOM   3538 H  HD21 A LEU   A 1 164 ? 9.911  -8.046  -1.130  0.70 22.97 ?  164 LEU   A HD21 1 
ATOM   3539 H  HD21 B LEU   A 1 164 ? 10.145 -8.560  -1.119  0.30 19.34 ?  164 LEU   A HD21 1 
ATOM   3540 H  HD22 A LEU   A 1 164 ? 10.028 -9.387  -0.286  0.70 22.97 ?  164 LEU   A HD22 1 
ATOM   3541 H  HD22 B LEU   A 1 164 ? 10.255 -9.587  0.088   0.30 19.34 ?  164 LEU   A HD22 1 
ATOM   3542 H  HD23 A LEU   A 1 164 ? 8.771  -9.148  -1.228  0.70 22.97 ?  164 LEU   A HD23 1 
ATOM   3543 H  HD23 B LEU   A 1 164 ? 9.116  -9.765  -1.005  0.30 19.34 ?  164 LEU   A HD23 1 
ATOM   3544 N  N    . VAL   A 1 165 ? 5.605  -10.740 2.644   1.00 19.00 ?  165 VAL   A N    1 
ATOM   3545 C  CA   . VAL   A 1 165 ? 5.152  -11.808 3.527   1.00 18.99 ?  165 VAL   A CA   1 
ATOM   3546 C  C    . VAL   A 1 165 ? 4.108  -12.671 2.827   1.00 19.50 ?  165 VAL   A C    1 
ATOM   3547 O  O    . VAL   A 1 165 ? 4.202  -13.903 2.815   1.00 19.53 ?  165 VAL   A O    1 
ATOM   3548 C  CB   . VAL   A 1 165 ? 4.600  -11.197 4.830   1.00 19.53 ?  165 VAL   A CB   1 
ATOM   3549 C  CG1  . VAL   A 1 165 ? 3.855  -12.239 5.648   1.00 20.40 ?  165 VAL   A CG1  1 
ATOM   3550 C  CG2  . VAL   A 1 165 ? 5.722  -10.561 5.639   1.00 19.73 ?  165 VAL   A CG2  1 
ATOM   3551 H  H    A VAL   A 1 165 ? 5.358  -9.958  2.888   0.70 22.76 ?  165 VAL   A H    1 
ATOM   3552 H  H    B VAL   A 1 165 ? 5.387  -9.954  2.900   0.30 22.76 ?  165 VAL   A H    1 
ATOM   3553 H  HA   . VAL   A 1 165 ? 5.901  -12.378 3.757   1.00 22.75 ?  165 VAL   A HA   1 
ATOM   3554 H  HB   . VAL   A 1 165 ? 3.971  -10.496 4.602   1.00 23.40 ?  165 VAL   A HB   1 
ATOM   3555 H  HG11 . VAL   A 1 165 ? 3.759  -11.912 6.557   1.00 24.44 ?  165 VAL   A HG11 1 
ATOM   3556 H  HG12 . VAL   A 1 165 ? 2.977  -12.379 5.257   1.00 24.44 ?  165 VAL   A HG12 1 
ATOM   3557 H  HG13 . VAL   A 1 165 ? 4.359  -13.063 5.645   1.00 24.44 ?  165 VAL   A HG13 1 
ATOM   3558 H  HG21 . VAL   A 1 165 ? 5.356  -10.183 6.455   1.00 23.64 ?  165 VAL   A HG21 1 
ATOM   3559 H  HG22 . VAL   A 1 165 ? 6.384  -11.237 5.857   1.00 23.64 ?  165 VAL   A HG22 1 
ATOM   3560 H  HG23 . VAL   A 1 165 ? 6.136  -9.857  5.110   1.00 23.64 ?  165 VAL   A HG23 1 
ATOM   3561 N  N    A SER   A 1 166 ? 3.107  -12.032 2.218   0.70 20.05 ?  166 SER   A N    1 
ATOM   3562 N  N    B SER   A 1 166 ? 3.094  -12.036 2.237   0.30 20.32 ?  166 SER   A N    1 
ATOM   3563 C  CA   A SER   A 1 166 ? 1.971  -12.767 1.670   0.70 21.85 ?  166 SER   A CA   1 
ATOM   3564 C  CA   B SER   A 1 166 ? 1.986  -12.786 1.652   0.30 21.75 ?  166 SER   A CA   1 
ATOM   3565 C  C    A SER   A 1 166 ? 2.356  -13.618 0.471   0.70 22.42 ?  166 SER   A C    1 
ATOM   3566 C  C    B SER   A 1 166 ? 2.452  -13.677 0.507   0.30 22.52 ?  166 SER   A C    1 
ATOM   3567 O  O    A SER   A 1 166 ? 1.678  -14.614 0.184   0.70 23.53 ?  166 SER   A O    1 
ATOM   3568 O  O    B SER   A 1 166 ? 1.956  -14.798 0.345   0.30 23.16 ?  166 SER   A O    1 
ATOM   3569 C  CB   A SER   A 1 166 ? 0.866  -11.795 1.256   0.70 23.92 ?  166 SER   A CB   1 
ATOM   3570 C  CB   B SER   A 1 166 ? 0.891  -11.821 1.189   0.30 22.77 ?  166 SER   A CB   1 
ATOM   3571 O  OG   A SER   A 1 166 ? 0.337  -11.101 2.373   0.70 26.57 ?  166 SER   A OG   1 
ATOM   3572 O  OG   B SER   A 1 166 ? 0.401  -11.051 2.275   0.30 24.05 ?  166 SER   A OG   1 
ATOM   3573 H  H    A SER   A 1 166 ? 3.054  -11.186 2.121   0.70 24.02 ?  166 SER   A H    1 
ATOM   3574 H  H    B SER   A 1 166 ? 3.021  -11.186 2.168   0.30 24.34 ?  166 SER   A H    1 
ATOM   3575 H  HA   A SER   A 1 166 ? 1.604  -13.357 2.348   0.70 26.19 ?  166 SER   A HA   1 
ATOM   3576 H  HA   B SER   A 1 166 ? 1.596  -13.367 2.323   0.30 26.06 ?  166 SER   A HA   1 
ATOM   3577 H  HB2  A SER   A 1 166 ? 1.225  -11.167 0.608   0.70 28.66 ?  166 SER   A HB2  1 
ATOM   3578 H  HB2  B SER   A 1 166 ? 1.252  -11.221 0.519   0.30 27.29 ?  166 SER   A HB2  1 
ATOM   3579 H  HB3  A SER   A 1 166 ? 0.134  -12.294 0.855   0.70 28.66 ?  166 SER   A HB3  1 
ATOM   3580 H  HB3  B SER   A 1 166 ? 0.150  -12.326 0.815   0.30 27.29 ?  166 SER   A HB3  1 
ATOM   3581 H  HG   A SER   A 1 166 ? -0.236 -10.542 2.117   0.70 31.85 ?  166 SER   A HG   1 
ATOM   3582 H  HG   B SER   A 1 166 ? 1.019  -10.588 2.609   0.30 28.82 ?  166 SER   A HG   1 
ATOM   3583 N  N    A SER   A 1 167 ? 3.406  -13.231 -0.253  0.70 22.07 ?  167 SER   A N    1 
ATOM   3584 N  N    B SER   A 1 167 ? 3.414  -13.209 -0.286  0.30 22.64 ?  167 SER   A N    1 
ATOM   3585 C  CA   A SER   A 1 167 ? 3.863  -13.967 -1.421  0.70 23.28 ?  167 SER   A CA   1 
ATOM   3586 C  CA   B SER   A 1 167 ? 3.879  -13.964 -1.441  0.30 23.27 ?  167 SER   A CA   1 
ATOM   3587 C  C    A SER   A 1 167 ? 5.032  -14.890 -1.111  0.70 23.84 ?  167 SER   A C    1 
ATOM   3588 C  C    B SER   A 1 167 ? 5.040  -14.892 -1.114  0.30 23.71 ?  167 SER   A C    1 
ATOM   3589 O  O    A SER   A 1 167 ? 5.526  -15.564 -2.019  0.70 24.30 ?  167 SER   A O    1 
ATOM   3590 O  O    B SER   A 1 167 ? 5.539  -15.573 -2.015  0.30 23.87 ?  167 SER   A O    1 
ATOM   3591 C  CB   A SER   A 1 167 ? 4.259  -12.991 -2.539  0.70 23.84 ?  167 SER   A CB   1 
ATOM   3592 C  CB   B SER   A 1 167 ? 4.291  -13.016 -2.575  0.30 23.50 ?  167 SER   A CB   1 
ATOM   3593 O  OG   A SER   A 1 167 ? 5.343  -12.171 -2.134  0.70 24.31 ?  167 SER   A OG   1 
ATOM   3594 O  OG   B SER   A 1 167 ? 5.376  -12.195 -2.183  0.30 23.69 ?  167 SER   A OG   1 
ATOM   3595 H  H    A SER   A 1 167 ? 3.862  -12.519 -0.093  0.70 26.44 ?  167 SER   A H    1 
ATOM   3596 H  H    B SER   A 1 167 ? 3.822  -12.459 -0.171  0.30 27.13 ?  167 SER   A H    1 
ATOM   3597 H  HA   A SER   A 1 167 ? 3.135  -14.511 -1.754  0.70 27.90 ?  167 SER   A HA   1 
ATOM   3598 H  HA   B SER   A 1 167 ? 3.148  -14.509 -1.771  0.30 27.89 ?  167 SER   A HA   1 
ATOM   3599 H  HB2  A SER   A 1 167 ? 4.521  -13.500 -3.324  0.70 28.57 ?  167 SER   A HB2  1 
ATOM   3600 H  HB2  B SER   A 1 167 ? 4.557  -13.546 -3.346  0.30 28.16 ?  167 SER   A HB2  1 
ATOM   3601 H  HB3  A SER   A 1 167 ? 3.488  -12.434 -2.759  0.70 28.57 ?  167 SER   A HB3  1 
ATOM   3602 H  HB3  B SER   A 1 167 ? 3.533  -12.456 -2.810  0.30 28.16 ?  167 SER   A HB3  1 
ATOM   3603 H  HG   A SER   A 1 167 ? 5.109  -11.708 -1.472  0.70 29.13 ?  167 SER   A HG   1 
ATOM   3604 H  HG   B SER   A 1 167 ? 5.152  -11.728 -1.522  0.30 28.40 ?  167 SER   A HG   1 
ATOM   3605 N  N    . PHE   A 1 168 ? 5.482  -14.939 0.140   1.00 24.15 ?  168 PHE   A N    1 
ATOM   3606 C  CA   . PHE   A 1 168 ? 6.661  -15.730 0.474   1.00 26.21 ?  168 PHE   A CA   1 
ATOM   3607 C  C    . PHE   A 1 168 ? 6.371  -17.217 0.368   1.00 33.21 ?  168 PHE   A C    1 
ATOM   3608 O  O    . PHE   A 1 168 ? 5.378  -17.712 0.911   1.00 32.96 ?  168 PHE   A O    1 
ATOM   3609 C  CB   . PHE   A 1 168 ? 7.166  -15.422 1.880   1.00 23.11 ?  168 PHE   A CB   1 
ATOM   3610 C  CG   . PHE   A 1 168 ? 8.441  -16.152 2.214   1.00 20.56 ?  168 PHE   A CG   1 
ATOM   3611 C  CD1  . PHE   A 1 168 ? 9.621  -15.791 1.597   1.00 19.93 ?  168 PHE   A CD1  1 
ATOM   3612 C  CD2  . PHE   A 1 168 ? 8.461  -17.214 3.104   1.00 19.69 ?  168 PHE   A CD2  1 
ATOM   3613 C  CE1  . PHE   A 1 168 ? 10.797 -16.454 1.870   1.00 19.51 ?  168 PHE   A CE1  1 
ATOM   3614 C  CE2  . PHE   A 1 168 ? 9.648  -17.882 3.384   1.00 19.82 ?  168 PHE   A CE2  1 
ATOM   3615 C  CZ   . PHE   A 1 168 ? 10.812 -17.497 2.765   1.00 19.66 ?  168 PHE   A CZ   1 
ATOM   3616 H  H    A PHE   A 1 168 ? 5.133  -14.522 0.804   0.70 28.94 ?  168 PHE   A H    1 
ATOM   3617 H  H    B PHE   A 1 168 ? 5.133  -14.518 0.802   0.30 28.94 ?  168 PHE   A H    1 
ATOM   3618 H  HA   . PHE   A 1 168 ? 7.370  -15.519 -0.153  1.00 31.41 ?  168 PHE   A HA   1 
ATOM   3619 H  HB2  . PHE   A 1 168 ? 7.341  -14.471 1.951   1.00 27.70 ?  168 PHE   A HB2  1 
ATOM   3620 H  HB3  . PHE   A 1 168 ? 6.493  -15.686 2.524   1.00 27.70 ?  168 PHE   A HB3  1 
ATOM   3621 H  HD1  . PHE   A 1 168 ? 9.631  -15.086 0.991   1.00 23.88 ?  168 PHE   A HD1  1 
ATOM   3622 H  HD2  . PHE   A 1 168 ? 7.674  -17.478 3.524   1.00 23.59 ?  168 PHE   A HD2  1 
ATOM   3623 H  HE1  . PHE   A 1 168 ? 11.593 -16.197 1.454   1.00 23.37 ?  168 PHE   A HE1  1 
ATOM   3624 H  HE2  . PHE   A 1 168 ? 9.651  -18.593 3.988   1.00 23.75 ?  168 PHE   A HE2  1 
ATOM   3625 H  HZ   . PHE   A 1 168 ? 11.610 -17.947 2.950   1.00 23.55 ?  168 PHE   A HZ   1 
ATOM   3626 N  N    A LEU   A 1 169 ? 7.249  -17.933 -0.325  0.70 37.46 ?  169 LEU   A N    1 
ATOM   3627 N  N    B LEU   A 1 169 ? 7.252  -17.936 -0.318  0.30 36.81 ?  169 LEU   A N    1 
ATOM   3628 C  CA   A LEU   A 1 169 ? 7.102  -19.369 -0.482  0.70 42.03 ?  169 LEU   A CA   1 
ATOM   3629 C  CA   B LEU   A 1 169 ? 7.102  -19.373 -0.464  0.30 40.36 ?  169 LEU   A CA   1 
ATOM   3630 C  C    A LEU   A 1 169 ? 8.053  -20.084 0.470   0.70 44.22 ?  169 LEU   A C    1 
ATOM   3631 C  C    B LEU   A 1 169 ? 7.957  -20.102 0.565   0.30 41.86 ?  169 LEU   A C    1 
ATOM   3632 O  O    A LEU   A 1 169 ? 7.642  -20.569 1.525   0.70 45.03 ?  169 LEU   A O    1 
ATOM   3633 O  O    B LEU   A 1 169 ? 7.441  -20.641 1.545   0.30 42.37 ?  169 LEU   A O    1 
ATOM   3634 C  CB   A LEU   A 1 169 ? 7.387  -19.780 -1.929  0.70 43.84 ?  169 LEU   A CB   1 
ATOM   3635 C  CB   B LEU   A 1 169 ? 7.491  -19.808 -1.879  0.30 42.00 ?  169 LEU   A CB   1 
ATOM   3636 C  CG   A LEU   A 1 169 ? 7.009  -21.211 -2.315  0.70 45.29 ?  169 LEU   A CG   1 
ATOM   3637 C  CG   B LEU   A 1 169 ? 7.049  -21.209 -2.306  0.30 43.29 ?  169 LEU   A CG   1 
ATOM   3638 C  CD1  A LEU   A 1 169 ? 5.573  -21.513 -1.916  0.70 45.86 ?  169 LEU   A CD1  1 
ATOM   3639 C  CD1  B LEU   A 1 169 ? 5.612  -21.468 -1.882  0.30 43.75 ?  169 LEU   A CD1  1 
ATOM   3640 C  CD2  A LEU   A 1 169 ? 7.203  -21.424 -3.808  0.70 45.72 ?  169 LEU   A CD2  1 
ATOM   3641 C  CD2  B LEU   A 1 169 ? 7.194  -21.368 -3.812  0.30 43.69 ?  169 LEU   A CD2  1 
ATOM   3642 O  OXT  A LEU   A 1 169 ? 9.254  -20.180 0.213   0.70 44.68 -1 169 LEU   A OXT  1 
ATOM   3643 O  OXT  B LEU   A 1 169 ? 9.181  -20.162 0.448   0.30 42.26 -1 169 LEU   A OXT  1 
ATOM   3644 H  H    A LEU   A 1 169 ? 7.944  -17.607 -0.714  0.70 44.91 ?  169 LEU   A H    1 
ATOM   3645 H  H    B LEU   A 1 169 ? 7.945  -17.611 -0.711  0.30 44.14 ?  169 LEU   A H    1 
ATOM   3646 H  HA   A LEU   A 1 169 ? 6.193  -19.618 -0.259  0.70 50.40 ?  169 LEU   A HA   1 
ATOM   3647 H  HA   B LEU   A 1 169 ? 6.174  -19.600 -0.306  0.30 48.40 ?  169 LEU   A HA   1 
ATOM   3648 H  HB2  A LEU   A 1 169 ? 6.896  -19.186 -2.517  0.70 52.57 ?  169 LEU   A HB2  1 
ATOM   3649 H  HB2  B LEU   A 1 169 ? 7.105  -19.181 -2.509  0.30 50.36 ?  169 LEU   A HB2  1 
ATOM   3650 H  HB3  A LEU   A 1 169 ? 8.338  -19.680 -2.091  0.70 52.57 ?  169 LEU   A HB3  1 
ATOM   3651 H  HB3  B LEU   A 1 169 ? 8.459  -19.779 -1.950  0.30 50.36 ?  169 LEU   A HB3  1 
ATOM   3652 H  HG   A LEU   A 1 169 ? 7.590  -21.832 -1.846  0.70 54.31 ?  169 LEU   A HG   1 
ATOM   3653 H  HG   B LEU   A 1 169 ? 7.617  -21.869 -1.877  0.30 51.91 ?  169 LEU   A HG   1 
ATOM   3654 H  HD11 A LEU   A 1 169 ? 5.279  -22.311 -2.378  0.70 55.00 ?  169 LEU   A HD11 1 
ATOM   3655 H  HD11 B LEU   A 1 169 ? 5.265  -22.215 -2.388  0.30 52.46 ?  169 LEU   A HD11 1 
ATOM   3656 H  HD12 A LEU   A 1 169 ? 5.535  -21.652 -0.956  0.70 55.00 ?  169 LEU   A HD12 1 
ATOM   3657 H  HD12 B LEU   A 1 169 ? 5.594  -21.671 -0.933  0.30 52.46 ?  169 LEU   A HD12 1 
ATOM   3658 H  HD13 A LEU   A 1 169 ? 5.014  -20.760 -2.165  0.70 55.00 ?  169 LEU   A HD13 1 
ATOM   3659 H  HD13 B LEU   A 1 169 ? 5.084  -20.672 -2.061  0.30 52.46 ?  169 LEU   A HD13 1 
ATOM   3660 H  HD21 A LEU   A 1 169 ? 6.966  -22.338 -4.031  0.70 54.82 ?  169 LEU   A HD21 1 
ATOM   3661 H  HD21 B LEU   A 1 169 ? 6.924  -22.265 -4.062  0.30 52.39 ?  169 LEU   A HD21 1 
ATOM   3662 H  HD22 A LEU   A 1 169 ? 6.629  -20.808 -4.291  0.70 54.82 ?  169 LEU   A HD22 1 
ATOM   3663 H  HD22 B LEU   A 1 169 ? 6.625  -20.716 -4.253  0.30 52.39 ?  169 LEU   A HD22 1 
ATOM   3664 H  HD23 A LEU   A 1 169 ? 8.131  -21.258 -4.034  0.70 54.82 ?  169 LEU   A HD23 1 
ATOM   3665 H  HD23 B LEU   A 1 169 ? 8.120  -21.219 -4.058  0.30 52.39 ?  169 LEU   A HD23 1 
ATOM   3666 N  N    A SER   B 1 1   ? 50.855 -9.248  -23.714 0.70 27.28 ?  1   SER   B N    1 
ATOM   3667 N  N    B SER   B 1 1   ? 50.831 -9.263  -23.664 0.30 25.82 ?  1   SER   B N    1 
ATOM   3668 C  CA   A SER   B 1 1   ? 51.368 -10.302 -22.818 0.70 27.37 ?  1   SER   B CA   1 
ATOM   3669 C  CA   B SER   B 1 1   ? 51.335 -10.263 -22.699 0.30 25.84 ?  1   SER   B CA   1 
ATOM   3670 C  C    A SER   B 1 1   ? 50.300 -11.362 -22.555 0.70 26.32 ?  1   SER   B C    1 
ATOM   3671 C  C    B SER   B 1 1   ? 50.302 -11.358 -22.491 0.30 25.42 ?  1   SER   B C    1 
ATOM   3672 O  O    A SER   B 1 1   ? 49.097 -11.158 -22.791 0.70 26.55 ?  1   SER   B O    1 
ATOM   3673 O  O    B SER   B 1 1   ? 49.103 -11.158 -22.709 0.30 25.52 ?  1   SER   B O    1 
ATOM   3674 C  CB   A SER   B 1 1   ? 51.847 -9.700  -21.497 0.70 28.47 ?  1   SER   B CB   1 
ATOM   3675 C  CB   B SER   B 1 1   ? 51.659 -9.604  -21.362 0.30 26.22 ?  1   SER   B CB   1 
ATOM   3676 O  OG   A SER   B 1 1   ? 50.753 -9.405  -20.649 0.70 30.19 ?  1   SER   B OG   1 
ATOM   3677 O  OG   B SER   B 1 1   ? 50.493 -9.478  -20.567 0.30 26.90 ?  1   SER   B OG   1 
ATOM   3678 H  H1   A SER   B 1 1   ? 50.755 -9.584  -24.530 0.70 32.70 ?  1   SER   B H1   1 
ATOM   3679 H  H1   B SER   B 1 1   ? 50.760 -9.642  -24.464 0.30 30.95 ?  1   SER   B H1   1 
ATOM   3680 H  H2   A SER   B 1 1   ? 50.075 -8.963  -23.406 0.70 32.70 ?  1   SER   B H2   1 
ATOM   3681 H  H2   B SER   B 1 1   ? 50.038 -8.974  -23.394 0.30 30.95 ?  1   SER   B H2   1 
ATOM   3682 H  H3   A SER   B 1 1   ? 51.437 -8.576  -23.734 0.70 32.70 ?  1   SER   B H3   1 
ATOM   3683 H  H3   B SER   B 1 1   ? 51.405 -8.587  -23.702 0.30 30.95 ?  1   SER   B H3   1 
ATOM   3684 H  HA   A SER   B 1 1   ? 52.126 -10.722 -23.253 0.70 32.81 ?  1   SER   B HA   1 
ATOM   3685 H  HA   B SER   B 1 1   ? 52.141 -10.657 -23.059 0.30 30.97 ?  1   SER   B HA   1 
ATOM   3686 H  HB2  A SER   B 1 1   ? 52.416 -10.344 -21.054 0.70 34.13 ?  1   SER   B HB2  1 
ATOM   3687 H  HB2  B SER   B 1 1   ? 52.306 -10.154 -20.898 0.30 31.42 ?  1   SER   B HB2  1 
ATOM   3688 H  HB3  A SER   B 1 1   ? 52.347 -8.887  -21.683 0.70 34.13 ?  1   SER   B HB3  1 
ATOM   3689 H  HB3  B SER   B 1 1   ? 52.027 -8.721  -21.526 0.30 31.42 ?  1   SER   B HB3  1 
ATOM   3690 H  HG   A SER   B 1 1   ? 51.034 -9.031  -19.948 0.70 36.19 ?  1   SER   B HG   1 
ATOM   3691 H  HG   B SER   B 1 1   ? 50.681 -9.074  -19.854 0.30 32.24 ?  1   SER   B HG   1 
ATOM   3692 N  N    A MET   B 1 2   ? 50.762 -12.505 -22.065 0.70 25.62 ?  2   MET   B N    1 
ATOM   3693 N  N    B MET   B 1 2   ? 50.778 -12.519 -22.060 0.30 24.98 ?  2   MET   B N    1 
ATOM   3694 C  CA   A MET   B 1 2   ? 49.937 -13.692 -21.893 0.70 25.78 ?  2   MET   B CA   1 
ATOM   3695 C  CA   B MET   B 1 2   ? 49.939 -13.693 -21.879 0.30 24.76 ?  2   MET   B CA   1 
ATOM   3696 C  C    A MET   B 1 2   ? 49.664 -13.889 -20.407 0.70 23.78 ?  2   MET   B C    1 
ATOM   3697 C  C    B MET   B 1 2   ? 49.665 -13.884 -20.397 0.30 23.16 ?  2   MET   B C    1 
ATOM   3698 O  O    A MET   B 1 2   ? 50.584 -14.155 -19.630 0.70 24.18 ?  2   MET   B O    1 
ATOM   3699 O  O    B MET   B 1 2   ? 50.588 -14.136 -19.615 0.30 23.41 ?  2   MET   B O    1 
ATOM   3700 C  CB   A MET   B 1 2   ? 50.667 -14.893 -22.479 0.70 29.29 ?  2   MET   B CB   1 
ATOM   3701 C  CB   B MET   B 1 2   ? 50.641 -14.912 -22.453 0.30 26.64 ?  2   MET   B CB   1 
ATOM   3702 C  CG   A MET   B 1 2   ? 49.827 -16.153 -22.596 0.70 32.70 ?  2   MET   B CG   1 
ATOM   3703 C  CG   B MET   B 1 2   ? 49.726 -16.094 -22.743 0.30 28.28 ?  2   MET   B CG   1 
ATOM   3704 S  SD   A MET   B 1 2   ? 50.640 -17.382 -23.634 0.70 36.10 ?  2   MET   B SD   1 
ATOM   3705 S  SD   B MET   B 1 2   ? 50.533 -17.309 -23.793 0.30 29.78 ?  2   MET   B SD   1 
ATOM   3706 C  CE   A MET   B 1 2   ? 51.168 -16.331 -24.978 0.70 36.52 ?  2   MET   B CE   1 
ATOM   3707 C  CE   B MET   B 1 2   ? 51.654 -16.242 -24.685 0.30 30.09 ?  2   MET   B CE   1 
ATOM   3708 H  H    A MET   B 1 2   ? 51.583 -12.626 -21.827 0.70 30.71 ?  2   MET   B H    1 
ATOM   3709 H  H    B MET   B 1 2   ? 51.607 -12.660 -21.869 0.30 29.94 ?  2   MET   B H    1 
ATOM   3710 H  HA   A MET   B 1 2   ? 49.103 -13.583 -22.374 0.70 30.90 ?  2   MET   B HA   1 
ATOM   3711 H  HA   B MET   B 1 2   ? 49.108 -13.584 -22.365 0.30 29.67 ?  2   MET   B HA   1 
ATOM   3712 H  HB2  A MET   B 1 2   ? 50.971 -14.621 -23.356 0.70 35.11 ?  2   MET   B HB2  1 
ATOM   3713 H  HB2  B MET   B 1 2   ? 51.018 -14.572 -23.271 0.30 31.94 ?  2   MET   B HB2  1 
ATOM   3714 H  HB3  A MET   B 1 2   ? 51.429 -15.113 -21.927 0.70 35.11 ?  2   MET   B HB3  1 
ATOM   3715 H  HB3  B MET   B 1 2   ? 51.345 -15.227 -21.865 0.30 31.94 ?  2   MET   B HB3  1 
ATOM   3716 H  HG2  A MET   B 1 2   ? 49.694 -16.533 -21.708 0.70 39.20 ?  2   MET   B HG2  1 
ATOM   3717 H  HG2  B MET   B 1 2   ? 49.481 -16.527 -21.906 0.30 33.90 ?  2   MET   B HG2  1 
ATOM   3718 H  HG3  A MET   B 1 2   ? 48.970 -15.939 -22.998 0.70 39.20 ?  2   MET   B HG3  1 
ATOM   3719 H  HG3  B MET   B 1 2   ? 48.933 -15.789 -23.205 0.30 33.90 ?  2   MET   B HG3  1 
ATOM   3720 H  HE1  A MET   B 1 2   ? 51.313 -16.877 -25.750 0.70 43.79 ?  2   MET   B HE1  1 
ATOM   3721 H  HE1  B MET   B 1 2   ? 52.042 -16.759 -25.374 0.30 36.07 ?  2   MET   B HE1  1 
ATOM   3722 H  HE2  A MET   B 1 2   ? 50.467 -15.677 -25.153 0.70 43.79 ?  2   MET   B HE2  1 
ATOM   3723 H  HE2  B MET   B 1 2   ? 51.149 -15.496 -25.066 0.30 36.07 ?  2   MET   B HE2  1 
ATOM   3724 H  HE3  A MET   B 1 2   ? 51.991 -15.873 -24.728 0.70 43.79 ?  2   MET   B HE3  1 
ATOM   3725 H  HE3  B MET   B 1 2   ? 52.356 -15.909 -24.088 0.30 36.07 ?  2   MET   B HE3  1 
ATOM   3726 N  N    . VAL   B 1 3   ? 48.398 -13.762 -20.018 1.00 21.28 ?  3   VAL   B N    1 
ATOM   3727 C  CA   . VAL   B 1 3   ? 47.975 -13.966 -18.641 1.00 20.06 ?  3   VAL   B CA   1 
ATOM   3728 C  C    . VAL   B 1 3   ? 46.742 -14.857 -18.655 1.00 18.47 ?  3   VAL   B C    1 
ATOM   3729 O  O    . VAL   B 1 3   ? 46.025 -14.953 -19.654 1.00 18.73 ?  3   VAL   B O    1 
ATOM   3730 C  CB   . VAL   B 1 3   ? 47.679 -12.639 -17.907 1.00 21.41 ?  3   VAL   B CB   1 
ATOM   3731 C  CG1  . VAL   B 1 3   ? 48.943 -11.777 -17.795 1.00 22.06 ?  3   VAL   B CG1  1 
ATOM   3732 C  CG2  . VAL   B 1 3   ? 46.554 -11.891 -18.604 1.00 21.68 ?  3   VAL   B CG2  1 
ATOM   3733 H  H    A VAL   B 1 3   ? 47.754 -13.567 -20.556 0.70 25.50 ?  3   VAL   B H    1 
ATOM   3734 H  H    B VAL   B 1 3   ? 47.756 -13.569 -20.558 0.30 25.50 ?  3   VAL   B H    1 
ATOM   3735 H  HA   . VAL   B 1 3   ? 48.678 -14.430 -18.161 1.00 24.03 ?  3   VAL   B HA   1 
ATOM   3736 H  HB   . VAL   B 1 3   ? 47.382 -12.853 -17.008 1.00 25.65 ?  3   VAL   B HB   1 
ATOM   3737 H  HG11 . VAL   B 1 3   ? 48.717 -10.960 -17.324 1.00 26.44 ?  3   VAL   B HG11 1 
ATOM   3738 H  HG12 . VAL   B 1 3   ? 49.616 -12.271 -17.305 1.00 26.44 ?  3   VAL   B HG12 1 
ATOM   3739 H  HG13 . VAL   B 1 3   ? 49.259 -11.572 -18.686 1.00 26.44 ?  3   VAL   B HG13 1 
ATOM   3740 H  HG21 . VAL   B 1 3   ? 46.483 -11.006 -18.221 1.00 25.98 ?  3   VAL   B HG21 1 
ATOM   3741 H  HG22 . VAL   B 1 3   ? 46.751 -11.831 -19.551 1.00 25.98 ?  3   VAL   B HG22 1 
ATOM   3742 H  HG23 . VAL   B 1 3   ? 45.720 -12.376 -18.473 1.00 25.98 ?  3   VAL   B HG23 1 
ATOM   3743 N  N    . ASN   B 1 4   ? 46.504 -15.516 -17.526 1.00 16.69 ?  4   ASN   B N    1 
ATOM   3744 C  CA   . ASN   B 1 4   ? 45.365 -16.422 -17.394 1.00 16.18 ?  4   ASN   B CA   1 
ATOM   3745 C  C    . ASN   B 1 4   ? 45.300 -17.392 -18.569 1.00 16.27 ?  4   ASN   B C    1 
ATOM   3746 O  O    . ASN   B 1 4   ? 44.239 -17.634 -19.138 1.00 16.79 ?  4   ASN   B O    1 
ATOM   3747 C  CB   . ASN   B 1 4   ? 44.051 -15.650 -17.240 1.00 15.50 ?  4   ASN   B CB   1 
ATOM   3748 C  CG   . ASN   B 1 4   ? 43.995 -14.849 -15.947 1.00 14.94 ?  4   ASN   B CG   1 
ATOM   3749 O  OD1  . ASN   B 1 4   ? 44.287 -15.356 -14.870 1.00 14.58 ?  4   ASN   B OD1  1 
ATOM   3750 N  ND2  . ASN   B 1 4   ? 43.653 -13.573 -16.060 1.00 16.19 ?  4   ASN   B ND2  1 
ATOM   3751 H  H    . ASN   B 1 4   ? 46.996 -15.464 -16.827 1.00 19.99 ?  4   ASN   B H    1 
ATOM   3752 H  HA   . ASN   B 1 4   ? 45.493 -16.952 -16.594 1.00 19.38 ?  4   ASN   B HA   1 
ATOM   3753 H  HB2  . ASN   B 1 4   ? 43.960 -15.034 -17.985 1.00 18.57 ?  4   ASN   B HB2  1 
ATOM   3754 H  HB3  . ASN   B 1 4   ? 43.315 -16.280 -17.238 1.00 18.57 ?  4   ASN   B HB3  1 
ATOM   3755 H  HD21 . ASN   B 1 4   ? 43.617 -13.073 -15.358 1.00 19.39 ?  4   ASN   B HD21 1 
ATOM   3756 H  HD22 . ASN   B 1 4   ? 43.467 -13.238 -16.831 1.00 19.39 ?  4   ASN   B HD22 1 
ATOM   3757 N  N    . SER   B 1 5   ? 46.456 -17.946 -18.940 1.00 17.18 ?  5   SER   B N    1 
ATOM   3758 C  CA   . SER   B 1 5   ? 46.550 -18.867 -20.071 1.00 19.46 ?  5   SER   B CA   1 
ATOM   3759 C  C    . SER   B 1 5   ? 46.499 -20.288 -19.527 1.00 21.15 ?  5   SER   B C    1 
ATOM   3760 O  O    . SER   B 1 5   ? 47.499 -20.991 -19.443 1.00 23.21 ?  5   SER   B O    1 
ATOM   3761 C  CB   . SER   B 1 5   ? 47.825 -18.607 -20.871 1.00 21.06 ?  5   SER   B CB   1 
ATOM   3762 O  OG   . SER   B 1 5   ? 48.986 -18.771 -20.074 1.00 24.18 ?  5   SER   B OG   1 
ATOM   3763 H  H    . SER   B 1 5   ? 47.209 -17.815 -18.546 1.00 20.58 ?  5   SER   B H    1 
ATOM   3764 H  HA   . SER   B 1 5   ? 45.793 -18.740 -20.660 1.00 23.31 ?  5   SER   B HA   1 
ATOM   3765 H  HB2  . SER   B 1 5   ? 47.868 -19.231 -21.616 1.00 25.24 ?  5   SER   B HB2  1 
ATOM   3766 H  HB3  . SER   B 1 5   ? 47.795 -17.698 -21.208 1.00 25.24 ?  5   SER   B HB3  1 
ATOM   3767 H  HG   . SER   B 1 5   ? 49.025 -19.557 -19.783 1.00 28.98 ?  5   SER   B HG   1 
ATOM   3768 N  N    A PHE   B 1 6   ? 45.294 -20.712 -19.156 0.70 22.14 ?  6   PHE   B N    1 
ATOM   3769 N  N    B PHE   B 1 6   ? 45.293 -20.667 -19.107 0.30 21.18 ?  6   PHE   B N    1 
ATOM   3770 C  CA   A PHE   B 1 6   ? 45.087 -22.055 -18.633 0.70 22.50 ?  6   PHE   B CA   1 
ATOM   3771 C  CA   B PHE   B 1 6   ? 45.024 -22.015 -18.631 0.30 21.06 ?  6   PHE   B CA   1 
ATOM   3772 C  C    A PHE   B 1 6   ? 45.003 -23.048 -19.784 0.70 26.03 ?  6   PHE   B C    1 
ATOM   3773 C  C    B PHE   B 1 6   ? 44.851 -22.932 -19.832 0.30 22.30 ?  6   PHE   B C    1 
ATOM   3774 O  O    A PHE   B 1 6   ? 44.308 -22.804 -20.775 0.70 27.89 ?  6   PHE   B O    1 
ATOM   3775 O  O    B PHE   B 1 6   ? 44.141 -22.590 -20.783 0.30 23.28 ?  6   PHE   B O    1 
ATOM   3776 C  CB   A PHE   B 1 6   ? 43.806 -22.103 -17.801 0.70 20.54 ?  6   PHE   B CB   1 
ATOM   3777 C  CB   B PHE   B 1 6   ? 43.743 -22.023 -17.796 0.30 20.16 ?  6   PHE   B CB   1 
ATOM   3778 C  CG   A PHE   B 1 6   ? 43.851 -21.239 -16.573 0.70 18.84 ?  6   PHE   B CG   1 
ATOM   3779 C  CG   B PHE   B 1 6   ? 43.808 -21.156 -16.568 0.30 19.37 ?  6   PHE   B CG   1 
ATOM   3780 C  CD1  A PHE   B 1 6   ? 44.364 -21.730 -15.386 0.70 17.59 ?  6   PHE   B CD1  1 
ATOM   3781 C  CD1  B PHE   B 1 6   ? 44.309 -21.658 -15.380 0.30 18.90 ?  6   PHE   B CD1  1 
ATOM   3782 C  CD2  A PHE   B 1 6   ? 43.383 -19.936 -16.611 0.70 18.20 ?  6   PHE   B CD2  1 
ATOM   3783 C  CD2  B PHE   B 1 6   ? 43.358 -19.845 -16.600 0.30 19.02 ?  6   PHE   B CD2  1 
ATOM   3784 C  CE1  A PHE   B 1 6   ? 44.401 -20.936 -14.250 0.70 17.26 ?  6   PHE   B CE1  1 
ATOM   3785 C  CE1  B PHE   B 1 6   ? 44.366 -20.868 -14.245 0.30 18.71 ?  6   PHE   B CE1  1 
ATOM   3786 C  CE2  A PHE   B 1 6   ? 43.418 -19.139 -15.487 0.70 18.28 ?  6   PHE   B CE2  1 
ATOM   3787 C  CE2  B PHE   B 1 6   ? 43.412 -19.050 -15.471 0.30 18.98 ?  6   PHE   B CE2  1 
ATOM   3788 C  CZ   A PHE   B 1 6   ? 43.938 -19.630 -14.307 0.70 17.53 ?  6   PHE   B CZ   1 
ATOM   3789 C  CZ   B PHE   B 1 6   ? 43.920 -19.560 -14.293 0.30 18.69 ?  6   PHE   B CZ   1 
ATOM   3790 H  H    A PHE   B 1 6   ? 44.578 -20.237 -19.197 0.70 26.53 ?  6   PHE   B H    1 
ATOM   3791 H  H    B PHE   B 1 6   ? 44.606 -20.154 -19.092 0.30 25.38 ?  6   PHE   B H    1 
ATOM   3792 H  HA   A PHE   B 1 6   ? 45.831 -22.304 -18.069 0.70 26.96 ?  6   PHE   B HA   1 
ATOM   3793 H  HA   B PHE   B 1 6   ? 45.760 -22.337 -18.090 0.30 25.24 ?  6   PHE   B HA   1 
ATOM   3794 H  HB2  A PHE   B 1 6   ? 43.063 -21.806 -18.352 0.70 24.60 ?  6   PHE   B HB2  1 
ATOM   3795 H  HB2  B PHE   B 1 6   ? 43.010 -21.703 -18.347 0.30 24.16 ?  6   PHE   B HB2  1 
ATOM   3796 H  HB3  A PHE   B 1 6   ? 43.653 -23.021 -17.518 0.70 24.60 ?  6   PHE   B HB3  1 
ATOM   3797 H  HB3  B PHE   B 1 6   ? 43.561 -22.932 -17.508 0.30 24.16 ?  6   PHE   B HB3  1 
ATOM   3798 H  HD1  A PHE   B 1 6   ? 44.684 -22.605 -15.350 0.70 21.07 ?  6   PHE   B HD1  1 
ATOM   3799 H  HD1  B PHE   B 1 6   ? 44.615 -22.535 -15.346 0.30 22.64 ?  6   PHE   B HD1  1 
ATOM   3800 H  HD2  A PHE   B 1 6   ? 43.034 -19.601 -17.406 0.70 21.81 ?  6   PHE   B HD2  1 
ATOM   3801 H  HD2  B PHE   B 1 6   ? 43.015 -19.497 -17.392 0.30 22.78 ?  6   PHE   B HD2  1 
ATOM   3802 H  HE1  A PHE   B 1 6   ? 44.754 -21.272 -13.460 0.70 20.68 ?  6   PHE   B HE1  1 
ATOM   3803 H  HE1  B PHE   B 1 6   ? 44.711 -21.213 -13.454 0.30 22.41 ?  6   PHE   B HE1  1 
ATOM   3804 H  HE2  A PHE   B 1 6   ? 43.101 -18.267 -15.527 0.70 21.90 ?  6   PHE   B HE2  1 
ATOM   3805 H  HE2  B PHE   B 1 6   ? 43.108 -18.171 -15.505 0.30 22.74 ?  6   PHE   B HE2  1 
ATOM   3806 H  HZ   A PHE   B 1 6   ? 43.961 -19.098 -13.547 0.70 20.99 ?  6   PHE   B HZ   1 
ATOM   3807 H  HZ   B PHE   B 1 6   ? 43.958 -19.028 -13.532 0.30 22.39 ?  6   PHE   B HZ   1 
ATOM   3808 N  N    A SER   B 1 7   ? 45.713 -24.168 -19.650 0.70 27.79 ?  7   SER   B N    1 
ATOM   3809 N  N    B SER   B 1 7   ? 45.506 -24.091 -19.792 0.30 22.56 ?  7   SER   B N    1 
ATOM   3810 C  CA   A SER   B 1 7   ? 45.827 -25.151 -20.717 0.70 30.46 ?  7   SER   B CA   1 
ATOM   3811 C  CA   B SER   B 1 7   ? 45.478 -25.030 -20.903 0.30 23.55 ?  7   SER   B CA   1 
ATOM   3812 C  C    A SER   B 1 7   ? 45.744 -26.555 -20.139 0.70 29.91 ?  7   SER   B C    1 
ATOM   3813 C  C    B SER   B 1 7   ? 45.448 -26.452 -20.362 0.30 23.24 ?  7   SER   B C    1 
ATOM   3814 O  O    A SER   B 1 7   ? 46.355 -26.849 -19.108 0.70 30.40 ?  7   SER   B O    1 
ATOM   3815 O  O    B SER   B 1 7   ? 46.086 -26.756 -19.351 0.30 23.56 ?  7   SER   B O    1 
ATOM   3816 C  CB   A SER   B 1 7   ? 47.152 -24.986 -21.476 0.70 32.81 ?  7   SER   B CB   1 
ATOM   3817 C  CB   B SER   B 1 7   ? 46.703 -24.834 -21.811 0.30 24.44 ?  7   SER   B CB   1 
ATOM   3818 O  OG   A SER   B 1 7   ? 47.247 -25.903 -22.552 0.70 34.49 ?  7   SER   B OG   1 
ATOM   3819 O  OG   B SER   B 1 7   ? 46.523 -25.470 -23.065 0.30 25.09 ?  7   SER   B OG   1 
ATOM   3820 H  H    A SER   B 1 7   ? 46.144 -24.384 -18.935 0.70 33.32 ?  7   SER   B H    1 
ATOM   3821 H  H    B SER   B 1 7   ? 45.986 -24.357 -19.126 0.30 27.03 ?  7   SER   B H    1 
ATOM   3822 H  HA   A SER   B 1 7   ? 45.100 -25.038 -21.344 0.70 36.51 ?  7   SER   B HA   1 
ATOM   3823 H  HA   B SER   B 1 7   ? 44.684 -24.888 -21.434 0.30 28.22 ?  7   SER   B HA   1 
ATOM   3824 H  HB2  A SER   B 1 7   ? 47.204 -24.081 -21.827 0.70 39.33 ?  7   SER   B HB2  1 
ATOM   3825 H  HB2  B SER   B 1 7   ? 46.839 -23.882 -21.963 0.30 29.29 ?  7   SER   B HB2  1 
ATOM   3826 H  HB3  A SER   B 1 7   ? 47.890 -25.144 -20.867 0.70 39.33 ?  7   SER   B HB3  1 
ATOM   3827 H  HB3  B SER   B 1 7   ? 47.488 -25.207 -21.377 0.30 29.29 ?  7   SER   B HB3  1 
ATOM   3828 H  HG   A SER   B 1 7   ? 47.973 -25.795 -22.961 0.70 41.35 ?  7   SER   B HG   1 
ATOM   3829 H  HG   B SER   B 1 7   ? 47.205 -25.354 -23.547 0.30 30.08 ?  7   SER   B HG   1 
ATOM   3830 N  N    A GLY   B 1 8   ? 44.984 -27.416 -20.812 0.70 29.32 ?  8   GLY   B N    1 
ATOM   3831 N  N    B GLY   B 1 8   ? 44.694 -27.318 -21.036 0.30 22.93 ?  8   GLY   B N    1 
ATOM   3832 C  CA   A GLY   B 1 8   ? 44.922 -28.811 -20.437 0.70 28.30 ?  8   GLY   B CA   1 
ATOM   3833 C  CA   B GLY   B 1 8   ? 44.656 -28.717 -20.669 0.30 22.57 ?  8   GLY   B CA   1 
ATOM   3834 C  C    A GLY   B 1 8   ? 43.992 -29.126 -19.296 0.70 26.95 ?  8   GLY   B C    1 
ATOM   3835 C  C    B GLY   B 1 8   ? 43.782 -29.049 -19.486 0.30 21.97 ?  8   GLY   B C    1 
ATOM   3836 O  O    A GLY   B 1 8   ? 44.151 -30.172 -18.657 0.70 28.15 ?  8   GLY   B O    1 
ATOM   3837 O  O    B GLY   B 1 8   ? 43.962 -30.110 -18.879 0.30 22.64 ?  8   GLY   B O    1 
ATOM   3838 H  H    A GLY   B 1 8   ? 44.497 -27.210 -21.488 0.70 35.15 ?  8   GLY   B H    1 
ATOM   3839 H  H    B GLY   B 1 8   ? 44.208 -27.111 -21.709 0.30 27.48 ?  8   GLY   B H    1 
ATOM   3840 H  HA2  A GLY   B 1 8   ? 44.638 -29.331 -21.204 0.70 33.93 ?  8   GLY   B HA2  1 
ATOM   3841 H  HA2  B GLY   B 1 8   ? 44.326 -29.227 -21.420 0.30 27.05 ?  8   GLY   B HA2  1 
ATOM   3842 H  HA3  A GLY   B 1 8   ? 45.806 -29.111 -20.180 0.70 33.93 ?  8   GLY   B HA3  1 
ATOM   3843 H  HA3  B GLY   B 1 8   ? 45.559 -29.017 -20.472 0.30 27.05 ?  8   GLY   B HA3  1 
ATOM   3844 N  N    A TYR   B 1 9   ? 43.012 -28.269 -19.022 0.70 24.87 ?  9   TYR   B N    1 
ATOM   3845 N  N    B TYR   B 1 9   ? 42.823 -28.193 -19.147 0.30 20.85 ?  9   TYR   B N    1 
ATOM   3846 C  CA   A TYR   B 1 9   ? 42.065 -28.532 -17.951 0.70 22.68 ?  9   TYR   B CA   1 
ATOM   3847 C  CA   B TYR   B 1 9   ? 41.934 -28.457 -18.026 0.30 19.73 ?  9   TYR   B CA   1 
ATOM   3848 C  C    A TYR   B 1 9   ? 40.875 -29.323 -18.459 0.70 21.93 ?  9   TYR   B C    1 
ATOM   3849 C  C    B TYR   B 1 9   ? 40.713 -29.239 -18.482 0.30 20.07 ?  9   TYR   B C    1 
ATOM   3850 O  O    A TYR   B 1 9   ? 40.469 -29.209 -19.620 0.70 23.06 ?  9   TYR   B O    1 
ATOM   3851 O  O    B TYR   B 1 9   ? 40.210 -29.058 -19.595 0.30 20.61 ?  9   TYR   B O    1 
ATOM   3852 C  CB   A TYR   B 1 9   ? 41.579 -27.238 -17.304 0.70 21.89 ?  9   TYR   B CB   1 
ATOM   3853 C  CB   B TYR   B 1 9   ? 41.468 -27.157 -17.376 0.30 18.68 ?  9   TYR   B CB   1 
ATOM   3854 C  CG   A TYR   B 1 9   ? 42.616 -26.635 -16.387 0.70 21.36 ?  9   TYR   B CG   1 
ATOM   3855 C  CG   B TYR   B 1 9   ? 42.500 -26.527 -16.476 0.30 17.90 ?  9   TYR   B CG   1 
ATOM   3856 C  CD1  A TYR   B 1 9   ? 43.741 -26.006 -16.903 0.70 21.47 ?  9   TYR   B CD1  1 
ATOM   3857 C  CD1  B TYR   B 1 9   ? 43.560 -25.809 -17.006 0.30 17.66 ?  9   TYR   B CD1  1 
ATOM   3858 C  CD2  A TYR   B 1 9   ? 42.483 -26.705 -15.008 0.70 20.82 ?  9   TYR   B CD2  1 
ATOM   3859 C  CD2  B TYR   B 1 9   ? 42.418 -26.649 -15.095 0.30 17.17 ?  9   TYR   B CD2  1 
ATOM   3860 C  CE1  A TYR   B 1 9   ? 44.705 -25.459 -16.073 0.70 21.58 ?  9   TYR   B CE1  1 
ATOM   3861 C  CE1  B TYR   B 1 9   ? 44.514 -25.229 -16.191 0.30 17.38 ?  9   TYR   B CE1  1 
ATOM   3862 C  CE2  A TYR   B 1 9   ? 43.444 -26.161 -14.166 0.70 20.97 ?  9   TYR   B CE2  1 
ATOM   3863 C  CE2  B TYR   B 1 9   ? 43.371 -26.074 -14.268 0.30 16.98 ?  9   TYR   B CE2  1 
ATOM   3864 C  CZ   A TYR   B 1 9   ? 44.553 -25.535 -14.705 0.70 21.57 ?  9   TYR   B CZ   1 
ATOM   3865 C  CZ   B TYR   B 1 9   ? 44.417 -25.361 -14.824 0.30 17.13 ?  9   TYR   B CZ   1 
ATOM   3866 O  OH   A TYR   B 1 9   ? 45.513 -24.997 -13.879 0.70 22.06 ?  9   TYR   B OH   1 
ATOM   3867 O  OH   B TYR   B 1 9   ? 45.368 -24.783 -14.015 0.30 17.42 ?  9   TYR   B OH   1 
ATOM   3868 H  H    A TYR   B 1 9   ? 42.862 -27.540 -19.450 0.70 29.80 ?  9   TYR   B H    1 
ATOM   3869 H  H    B TYR   B 1 9   ? 42.656 -27.459 -19.560 0.30 24.99 ?  9   TYR   B H    1 
ATOM   3870 H  HA   A TYR   B 1 9   ? 42.492 -29.061 -17.267 0.70 27.18 ?  9   TYR   B HA   1 
ATOM   3871 H  HA   B TYR   B 1 9   ? 42.398 -28.980 -17.356 0.30 23.64 ?  9   TYR   B HA   1 
ATOM   3872 H  HB2  A TYR   B 1 9   ? 41.365 -26.588 -17.994 0.70 26.23 ?  9   TYR   B HB2  1 
ATOM   3873 H  HB2  B TYR   B 1 9   ? 41.236 -26.513 -18.064 0.30 22.38 ?  9   TYR   B HB2  1 
ATOM   3874 H  HB3  A TYR   B 1 9   ? 40.789 -27.432 -16.775 0.70 26.23 ?  9   TYR   B HB3  1 
ATOM   3875 H  HB3  B TYR   B 1 9   ? 40.696 -27.359 -16.834 0.30 22.38 ?  9   TYR   B HB3  1 
ATOM   3876 H  HD1  A TYR   B 1 9   ? 43.846 -25.953 -17.827 0.70 25.72 ?  9   TYR   B HD1  1 
ATOM   3877 H  HD1  B TYR   B 1 9   ? 43.635 -25.718 -17.927 0.30 21.16 ?  9   TYR   B HD1  1 
ATOM   3878 H  HD2  A TYR   B 1 9   ? 41.731 -27.125 -14.642 0.70 24.95 ?  9   TYR   B HD2  1 
ATOM   3879 H  HD2  B TYR   B 1 9   ? 41.712 -27.127 -14.718 0.30 20.57 ?  9   TYR   B HD2  1 
ATOM   3880 H  HE1  A TYR   B 1 9   ? 45.447 -25.047 -16.438 0.70 25.85 ?  9   TYR   B HE1  1 
ATOM   3881 H  HE1  B TYR   B 1 9   ? 45.221 -24.756 -16.562 0.30 20.82 ?  9   TYR   B HE1  1 
ATOM   3882 H  HE2  A TYR   B 1 9   ? 43.333 -26.218 -13.243 0.70 25.13 ?  9   TYR   B HE2  1 
ATOM   3883 H  HE2  B TYR   B 1 9   ? 43.300 -26.165 -13.343 0.30 20.34 ?  9   TYR   B HE2  1 
ATOM   3884 H  HH   A TYR   B 1 9   ? 46.121 -24.661 -14.340 0.70 26.44 ?  9   TYR   B HH   1 
ATOM   3885 H  HH   B TYR   B 1 9   ? 45.939 -24.394 -14.486 0.30 20.87 ?  9   TYR   B HH   1 
ATOM   3886 N  N    A LEU   B 1 10  ? 40.331 -30.144 -17.567 0.70 20.59 ?  10  LEU   B N    1 
ATOM   3887 N  N    B LEU   B 1 10  ? 40.237 -30.112 -17.598 0.30 20.20 ?  10  LEU   B N    1 
ATOM   3888 C  CA   A LEU   B 1 10  ? 39.130 -30.919 -17.817 0.70 20.23 ?  10  LEU   B CA   1 
ATOM   3889 C  CA   B LEU   B 1 10  ? 39.023 -30.875 -17.835 0.30 20.79 ?  10  LEU   B CA   1 
ATOM   3890 C  C    A LEU   B 1 10  ? 37.943 -30.150 -17.264 0.70 19.84 ?  10  LEU   B C    1 
ATOM   3891 C  C    B LEU   B 1 10  ? 37.836 -30.090 -17.294 0.30 20.96 ?  10  LEU   B C    1 
ATOM   3892 O  O    A LEU   B 1 10  ? 37.953 -29.739 -16.099 0.70 19.45 ?  10  LEU   B O    1 
ATOM   3893 O  O    B LEU   B 1 10  ? 37.857 -29.635 -16.146 0.30 20.51 ?  10  LEU   B O    1 
ATOM   3894 C  CB   A LEU   B 1 10  ? 39.229 -32.274 -17.114 0.70 21.11 ?  10  LEU   B CB   1 
ATOM   3895 C  CB   B LEU   B 1 10  ? 39.109 -32.227 -17.129 0.30 21.62 ?  10  LEU   B CB   1 
ATOM   3896 C  CG   A LEU   B 1 10  ? 38.115 -33.267 -17.441 0.70 22.52 ?  10  LEU   B CG   1 
ATOM   3897 C  CG   B LEU   B 1 10  ? 38.016 -33.232 -17.491 0.30 22.46 ?  10  LEU   B CG   1 
ATOM   3898 C  CD1  A LEU   B 1 10  ? 38.237 -33.742 -18.882 0.70 23.49 ?  10  LEU   B CD1  1 
ATOM   3899 C  CD1  B LEU   B 1 10  ? 38.272 -33.816 -18.871 0.30 22.88 ?  10  LEU   B CD1  1 
ATOM   3900 C  CD2  A LEU   B 1 10  ? 38.124 -34.446 -16.481 0.70 23.12 ?  10  LEU   B CD2  1 
ATOM   3901 C  CD2  B LEU   B 1 10  ? 37.923 -34.328 -16.444 0.30 22.78 ?  10  LEU   B CD2  1 
ATOM   3902 H  H    A LEU   B 1 10  ? 40.640 -30.266 -16.772 0.70 24.67 ?  10  LEU   B H    1 
ATOM   3903 H  H    B LEU   B 1 10  ? 40.603 -30.280 -16.836 0.30 24.20 ?  10  LEU   B H    1 
ATOM   3904 H  HA   A LEU   B 1 10  ? 39.000 -31.060 -18.764 0.70 24.24 ?  10  LEU   B HA   1 
ATOM   3905 H  HA   B LEU   B 1 10  ? 38.899 -31.021 -18.785 0.30 24.91 ?  10  LEU   B HA   1 
ATOM   3906 H  HB2  A LEU   B 1 10  ? 40.068 -32.688 -17.364 0.70 25.29 ?  10  LEU   B HB2  1 
ATOM   3907 H  HB2  B LEU   B 1 10  ? 39.961 -32.634 -17.351 0.30 25.91 ?  10  LEU   B HB2  1 
ATOM   3908 H  HB3  A LEU   B 1 10  ? 39.212 -32.130 -16.152 0.70 25.29 ?  10  LEU   B HB3  1 
ATOM   3909 H  HB3  B LEU   B 1 10  ? 39.060 -32.078 -16.172 0.30 25.91 ?  10  LEU   B HB3  1 
ATOM   3910 H  HG   A LEU   B 1 10  ? 37.257 -32.822 -17.348 0.70 26.99 ?  10  LEU   B HG   1 
ATOM   3911 H  HG   B LEU   B 1 10  ? 37.161 -32.774 -17.515 0.30 26.92 ?  10  LEU   B HG   1 
ATOM   3912 H  HD11 A LEU   B 1 10  ? 37.589 -34.444 -19.038 0.70 28.15 ?  10  LEU   B HD11 1 
ATOM   3913 H  HD11 B LEU   B 1 10  ? 37.585 -34.471 -19.069 0.30 27.41 ?  10  LEU   B HD11 1 
ATOM   3914 H  HD12 A LEU   B 1 10  ? 38.064 -32.993 -19.475 0.70 28.15 ?  10  LEU   B HD12 1 
ATOM   3915 H  HD12 B LEU   B 1 10  ? 38.246 -33.101 -19.526 0.30 27.41 ?  10  LEU   B HD12 1 
ATOM   3916 H  HD13 A LEU   B 1 10  ? 39.134 -34.079 -19.026 0.70 28.15 ?  10  LEU   B HD13 1 
ATOM   3917 H  HD13 B LEU   B 1 10  ? 39.145 -34.239 -18.877 0.30 27.41 ?  10  LEU   B HD13 1 
ATOM   3918 H  HD21 A LEU   B 1 10  ? 37.405 -35.051 -16.721 0.70 27.70 ?  10  LEU   B HD21 1 
ATOM   3919 H  HD21 B LEU   B 1 10  ? 37.228 -34.953 -16.704 0.30 27.29 ?  10  LEU   B HD21 1 
ATOM   3920 H  HD22 A LEU   B 1 10  ? 38.977 -34.898 -16.549 0.70 27.70 ?  10  LEU   B HD22 1 
ATOM   3921 H  HD22 B LEU   B 1 10  ? 38.777 -34.784 -16.391 0.30 27.29 ?  10  LEU   B HD22 1 
ATOM   3922 H  HD23 A LEU   B 1 10  ? 37.992 -34.116 -15.579 0.70 27.70 ?  10  LEU   B HD23 1 
ATOM   3923 H  HD23 B LEU   B 1 10  ? 37.706 -33.927 -15.588 0.30 27.29 ?  10  LEU   B HD23 1 
ATOM   3924 N  N    A LYS   B 1 11  ? 36.922 -29.973 -18.096 0.70 20.90 ?  11  LYS   B N    1 
ATOM   3925 N  N    B LYS   B 1 11  ? 36.811 -29.930 -18.125 0.30 21.88 ?  11  LYS   B N    1 
ATOM   3926 C  CA   A LYS   B 1 11  ? 35.710 -29.289 -17.682 0.70 23.15 ?  11  LYS   B CA   1 
ATOM   3927 C  CA   B LYS   B 1 11  ? 35.606 -29.213 -17.730 0.30 23.26 ?  11  LYS   B CA   1 
ATOM   3928 C  C    A LYS   B 1 11  ? 34.892 -30.215 -16.789 0.70 21.66 ?  11  LYS   B C    1 
ATOM   3929 C  C    B LYS   B 1 11  ? 34.734 -30.118 -16.867 0.30 21.70 ?  11  LYS   B C    1 
ATOM   3930 O  O    A LYS   B 1 11  ? 34.638 -31.374 -17.144 0.70 22.48 ?  11  LYS   B O    1 
ATOM   3931 O  O    B LYS   B 1 11  ? 34.268 -31.165 -17.331 0.30 21.86 ?  11  LYS   B O    1 
ATOM   3932 C  CB   A LYS   B 1 11  ? 34.911 -28.896 -18.927 0.70 27.11 ?  11  LYS   B CB   1 
ATOM   3933 C  CB   B LYS   B 1 11  ? 34.843 -28.789 -18.982 0.30 26.23 ?  11  LYS   B CB   1 
ATOM   3934 C  CG   A LYS   B 1 11  ? 33.885 -27.799 -18.719 0.70 30.62 ?  11  LYS   B CG   1 
ATOM   3935 C  CG   B LYS   B 1 11  ? 33.745 -27.776 -18.739 0.30 28.96 ?  11  LYS   B CG   1 
ATOM   3936 C  CD   A LYS   B 1 11  ? 33.156 -27.500 -20.023 0.70 33.37 ?  11  LYS   B CD   1 
ATOM   3937 C  CD   B LYS   B 1 11  ? 33.008 -27.461 -20.031 0.30 31.14 ?  11  LYS   B CD   1 
ATOM   3938 C  CE   A LYS   B 1 11  ? 32.145 -26.378 -19.860 0.70 35.37 ?  11  LYS   B CE   1 
ATOM   3939 C  CE   B LYS   B 1 11  ? 32.011 -26.333 -19.842 0.30 32.70 ?  11  LYS   B CE   1 
ATOM   3940 N  NZ   A LYS   B 1 11  ? 32.805 -25.069 -19.605 0.70 36.48 ?  11  LYS   B NZ   1 
ATOM   3941 N  NZ   B LYS   B 1 11  ? 32.687 -25.050 -19.506 0.30 33.54 ?  11  LYS   B NZ   1 
ATOM   3942 H  H    A LYS   B 1 11  ? 36.895 -30.255 -18.911 0.70 25.04 ?  11  LYS   B H    1 
ATOM   3943 H  H    B LYS   B 1 11  ? 36.792 -30.221 -18.937 0.30 26.21 ?  11  LYS   B H    1 
ATOM   3944 H  HA   A LYS   B 1 11  ? 35.930 -28.485 -17.187 0.70 27.74 ?  11  LYS   B HA   1 
ATOM   3945 H  HA   B LYS   B 1 11  ? 35.844 -28.420 -17.223 0.30 27.88 ?  11  LYS   B HA   1 
ATOM   3946 H  HB2  A LYS   B 1 11  ? 35.532 -28.582 -19.607 0.70 32.49 ?  11  LYS   B HB2  1 
ATOM   3947 H  HB2  B LYS   B 1 11  ? 35.469 -28.398 -19.611 0.30 31.43 ?  11  LYS   B HB2  1 
ATOM   3948 H  HB3  A LYS   B 1 11  ? 34.438 -29.674 -19.257 0.70 32.49 ?  11  LYS   B HB3  1 
ATOM   3949 H  HB3  B LYS   B 1 11  ? 34.433 -29.576 -19.375 0.30 31.43 ?  11  LYS   B HB3  1 
ATOM   3950 H  HG2  A LYS   B 1 11  ? 33.233 -28.086 -18.063 0.70 36.71 ?  11  LYS   B HG2  1 
ATOM   3951 H  HG2  B LYS   B 1 11  ? 33.109 -28.138 -18.104 0.30 34.72 ?  11  LYS   B HG2  1 
ATOM   3952 H  HG3  A LYS   B 1 11  ? 34.331 -26.989 -18.426 0.70 36.71 ?  11  LYS   B HG3  1 
ATOM   3953 H  HG3  B LYS   B 1 11  ? 34.136 -26.956 -18.400 0.30 34.72 ?  11  LYS   B HG3  1 
ATOM   3954 H  HD2  A LYS   B 1 11  ? 33.802 -27.231 -20.696 0.70 40.01 ?  11  LYS   B HD2  1 
ATOM   3955 H  HD2  B LYS   B 1 11  ? 33.650 -27.191 -20.707 0.30 37.33 ?  11  LYS   B HD2  1 
ATOM   3956 H  HD3  A LYS   B 1 11  ? 32.684 -28.296 -20.314 0.70 40.01 ?  11  LYS   B HD3  1 
ATOM   3957 H  HD3  B LYS   B 1 11  ? 32.525 -28.250 -20.323 0.30 37.33 ?  11  LYS   B HD3  1 
ATOM   3958 H  HE2  A LYS   B 1 11  ? 31.621 -26.301 -20.673 0.70 42.41 ?  11  LYS   B HE2  1 
ATOM   3959 H  HE2  B LYS   B 1 11  ? 31.513 -26.207 -20.665 0.30 39.20 ?  11  LYS   B HE2  1 
ATOM   3960 H  HE3  A LYS   B 1 11  ? 31.567 -26.580 -19.108 0.70 42.41 ?  11  LYS   B HE3  1 
ATOM   3961 H  HE3  B LYS   B 1 11  ? 31.408 -26.561 -19.117 0.30 39.20 ?  11  LYS   B HE3  1 
ATOM   3962 H  HZ1  A LYS   B 1 11  ? 32.191 -24.431 -19.520 0.70 43.74 ?  11  LYS   B HZ1  1 
ATOM   3963 H  HZ1  B LYS   B 1 11  ? 32.088 -24.393 -19.466 0.30 40.21 ?  11  LYS   B HZ1  1 
ATOM   3964 H  HZ2  A LYS   B 1 11  ? 33.284 -25.111 -18.856 0.70 43.74 ?  11  LYS   B HZ2  1 
ATOM   3965 H  HZ2  B LYS   B 1 11  ? 33.095 -25.118 -18.718 0.30 40.21 ?  11  LYS   B HZ2  1 
ATOM   3966 H  HZ3  A LYS   B 1 11  ? 33.344 -24.863 -20.283 0.70 43.74 ?  11  LYS   B HZ3  1 
ATOM   3967 H  HZ3  B LYS   B 1 11  ? 33.291 -24.852 -20.129 0.30 40.21 ?  11  LYS   B HZ3  1 
ATOM   3968 N  N    . LEU   B 1 12  ? 34.502 -29.715 -15.617 1.00 20.11 ?  12  LEU   B N    1 
ATOM   3969 C  CA   . LEU   B 1 12  ? 33.567 -30.424 -14.747 1.00 18.78 ?  12  LEU   B CA   1 
ATOM   3970 C  C    . LEU   B 1 12  ? 32.180 -29.811 -14.812 1.00 18.74 ?  12  LEU   B C    1 
ATOM   3971 O  O    . LEU   B 1 12  ? 31.192 -30.524 -14.974 1.00 19.52 ?  12  LEU   B O    1 
ATOM   3972 C  CB   . LEU   B 1 12  ? 34.052 -30.444 -13.293 1.00 18.13 ?  12  LEU   B CB   1 
ATOM   3973 C  CG   . LEU   B 1 12  ? 35.390 -31.127 -13.033 1.00 17.98 ?  12  LEU   B CG   1 
ATOM   3974 C  CD1  . LEU   B 1 12  ? 35.736 -31.070 -11.560 1.00 18.15 ?  12  LEU   B CD1  1 
ATOM   3975 C  CD2  . LEU   B 1 12  ? 35.372 -32.565 -13.525 1.00 18.36 ?  12  LEU   B CD2  1 
ATOM   3976 H  H    A LEU   B 1 12  ? 34.770 -28.960 -15.299 0.70 24.10 ?  12  LEU   B H    1 
ATOM   3977 H  H    B LEU   B 1 12  ? 34.855 -29.018 -15.257 0.30 24.10 ?  12  LEU   B H    1 
ATOM   3978 H  HA   . LEU   B 1 12  ? 33.485 -31.337 -15.047 1.00 22.49 ?  12  LEU   B HA   1 
ATOM   3979 H  HB2  . LEU   B 1 12  ? 34.124 -29.530 -12.983 1.00 21.72 ?  12  LEU   B HB2  1 
ATOM   3980 H  HB3  . LEU   B 1 12  ? 33.383 -30.910 -12.761 1.00 21.72 ?  12  LEU   B HB3  1 
ATOM   3981 H  HG   . LEU   B 1 12  ? 36.077 -30.649 -13.521 1.00 21.54 ?  12  LEU   B HG   1 
ATOM   3982 H  HD11 . LEU   B 1 12  ? 36.594 -31.503 -11.423 1.00 21.74 ?  12  LEU   B HD11 1 
ATOM   3983 H  HD12 . LEU   B 1 12  ? 35.790 -30.140 -11.282 1.00 21.74 ?  12  LEU   B HD12 1 
ATOM   3984 H  HD13 . LEU   B 1 12  ? 35.049 -31.527 -11.053 1.00 21.74 ?  12  LEU   B HD13 1 
ATOM   3985 H  HD21 . LEU   B 1 12  ? 36.181 -33.007 -13.229 1.00 21.99 ?  12  LEU   B HD21 1 
ATOM   3986 H  HD22 . LEU   B 1 12  ? 34.594 -33.014 -13.160 1.00 21.99 ?  12  LEU   B HD22 1 
ATOM   3987 H  HD23 . LEU   B 1 12  ? 35.329 -32.567 -14.495 1.00 21.99 ?  12  LEU   B HD23 1 
ATOM   3988 N  N    . THR   B 1 13  ? 32.097 -28.495 -14.681 1.00 18.83 ?  13  THR   B N    1 
ATOM   3989 C  CA   . THR   B 1 13  ? 30.879 -27.737 -14.891 1.00 18.84 ?  13  THR   B CA   1 
ATOM   3990 C  C    . THR   B 1 13  ? 31.235 -26.560 -15.792 1.00 21.33 ?  13  THR   B C    1 
ATOM   3991 O  O    . THR   B 1 13  ? 32.387 -26.395 -16.213 1.00 22.26 ?  13  THR   B O    1 
ATOM   3992 C  CB   . THR   B 1 13  ? 30.295 -27.238 -13.564 1.00 18.44 ?  13  THR   B CB   1 
ATOM   3993 O  OG1  . THR   B 1 13  ? 31.155 -26.228 -13.028 1.00 18.01 ?  13  THR   B OG1  1 
ATOM   3994 C  CG2  . THR   B 1 13  ? 30.172 -28.374 -12.558 1.00 19.01 ?  13  THR   B CG2  1 
ATOM   3995 H  H    . THR   B 1 13  ? 32.759 -28.001 -14.450 1.00 22.55 ?  13  THR   B H    1 
ATOM   3996 H  HA   . THR   B 1 13  ? 30.210 -28.291 -15.328 1.00 22.57 ?  13  THR   B HA   1 
ATOM   3997 H  HB   . THR   B 1 13  ? 29.402 -26.864 -13.714 1.00 22.09 ?  13  THR   B HB   1 
ATOM   3998 H  HG1  . THR   B 1 13  ? 30.861 -25.459 -13.239 1.00 21.57 ?  13  THR   B HG1  1 
ATOM   3999 H  HG21 . THR   B 1 13  ? 29.658 -28.081 -11.787 1.00 22.78 ?  13  THR   B HG21 1 
ATOM   4000 H  HG22 . THR   B 1 13  ? 29.722 -29.128 -12.966 1.00 22.78 ?  13  THR   B HG22 1 
ATOM   4001 H  HG23 . THR   B 1 13  ? 31.052 -28.648 -12.264 1.00 22.78 ?  13  THR   B HG23 1 
ATOM   4002 N  N    A ASP   B 1 14  ? 30.238 -25.726 -16.086 0.70 22.44 ?  14  ASP   B N    1 
ATOM   4003 N  N    B ASP   B 1 14  ? 30.238 -25.719 -16.078 0.30 22.27 ?  14  ASP   B N    1 
ATOM   4004 C  CA   A ASP   B 1 14  ? 30.490 -24.585 -16.956 0.70 23.90 ?  14  ASP   B CA   1 
ATOM   4005 C  CA   B ASP   B 1 14  ? 30.469 -24.573 -16.950 0.30 23.32 ?  14  ASP   B CA   1 
ATOM   4006 C  C    A ASP   B 1 14  ? 31.593 -23.688 -16.410 0.70 21.98 ?  14  ASP   B C    1 
ATOM   4007 C  C    B ASP   B 1 14  ? 31.505 -23.608 -16.393 0.30 21.52 ?  14  ASP   B C    1 
ATOM   4008 O  O    A ASP   B 1 14  ? 32.298 -23.040 -17.193 0.70 23.30 ?  14  ASP   B O    1 
ATOM   4009 O  O    B ASP   B 1 14  ? 32.054 -22.809 -17.160 0.30 21.99 ?  14  ASP   B O    1 
ATOM   4010 C  CB   A ASP   B 1 14  ? 29.206 -23.786 -17.175 0.70 27.52 ?  14  ASP   B CB   1 
ATOM   4011 C  CB   B ASP   B 1 14  ? 29.164 -23.819 -17.205 0.30 26.13 ?  14  ASP   B CB   1 
ATOM   4012 C  CG   A ASP   B 1 14  ? 28.226 -24.496 -18.082 0.70 30.96 ?  14  ASP   B CG   1 
ATOM   4013 C  CG   B ASP   B 1 14  ? 28.257 -24.540 -18.183 0.30 28.59 ?  14  ASP   B CG   1 
ATOM   4014 O  OD1  A ASP   B 1 14  ? 28.610 -25.499 -18.725 0.70 31.99 ?  14  ASP   B OD1  1 
ATOM   4015 O  OD1  B ASP   B 1 14  ? 28.778 -25.275 -19.048 0.30 29.38 ?  14  ASP   B OD1  1 
ATOM   4016 O  OD2  A ASP   B 1 14  ? 27.059 -24.058 -18.142 0.70 32.47 -1 14  ASP   B OD2  1 
ATOM   4017 O  OD2  B ASP   B 1 14  ? 27.022 -24.376 -18.087 0.30 29.49 -1 14  ASP   B OD2  1 
ATOM   4018 H  H    A ASP   B 1 14  ? 29.430 -25.789 -15.799 0.70 26.89 ?  14  ASP   B H    1 
ATOM   4019 H  H    B ASP   B 1 14  ? 29.432 -25.789 -15.787 0.30 26.69 ?  14  ASP   B H    1 
ATOM   4020 H  HA   A ASP   B 1 14  ? 30.791 -24.907 -17.815 0.70 28.64 ?  14  ASP   B HA   1 
ATOM   4021 H  HA   B ASP   B 1 14  ? 30.798 -24.894 -17.801 0.30 27.94 ?  14  ASP   B HA   1 
ATOM   4022 H  HB2  A ASP   B 1 14  ? 28.764 -23.650 -16.326 0.70 32.98 ?  14  ASP   B HB2  1 
ATOM   4023 H  HB2  B ASP   B 1 14  ? 28.686 -23.724 -16.368 0.30 31.32 ?  14  ASP   B HB2  1 
ATOM   4024 H  HB3  A ASP   B 1 14  ? 29.427 -22.931 -17.579 0.70 32.98 ?  14  ASP   B HB3  1 
ATOM   4025 H  HB3  B ASP   B 1 14  ? 29.376 -22.940 -17.566 0.30 31.32 ?  14  ASP   B HB3  1 
ATOM   4026 N  N    . ASN   B 1 15  ? 31.771 -23.643 -15.083 1.00 19.81 ?  15  ASN   B N    1 
ATOM   4027 C  CA   . ASN   B 1 15  ? 32.747 -22.737 -14.475 1.00 17.19 ?  15  ASN   B CA   1 
ATOM   4028 C  C    . ASN   B 1 15  ? 33.841 -23.401 -13.646 1.00 15.99 ?  15  ASN   B C    1 
ATOM   4029 O  O    . ASN   B 1 15  ? 34.726 -22.689 -13.158 1.00 15.71 ?  15  ASN   B O    1 
ATOM   4030 C  CB   . ASN   B 1 15  ? 32.051 -21.682 -13.599 1.00 17.08 ?  15  ASN   B CB   1 
ATOM   4031 C  CG   . ASN   B 1 15  ? 31.438 -22.283 -12.354 1.00 16.85 ?  15  ASN   B CG   1 
ATOM   4032 O  OD1  . ASN   B 1 15  ? 30.487 -23.067 -12.441 1.00 18.73 ?  15  ASN   B OD1  1 
ATOM   4033 N  ND2  . ASN   B 1 15  ? 31.981 -21.952 -11.195 1.00 16.00 ?  15  ASN   B ND2  1 
ATOM   4034 H  H    A ASN   B 1 15  ? 31.329 -24.117 -14.514 0.70 23.74 ?  15  ASN   B H    1 
ATOM   4035 H  H    B ASN   B 1 15  ? 31.376 -24.161 -14.519 0.30 23.74 ?  15  ASN   B H    1 
ATOM   4036 H  HA   . ASN   B 1 15  ? 33.193 -22.248 -15.177 1.00 20.59 ?  15  ASN   B HA   1 
ATOM   4037 H  HB2  . ASN   B 1 15  ? 32.706 -21.009 -13.324 1.00 20.46 ?  15  ASN   B HB2  1 
ATOM   4038 H  HB3  . ASN   B 1 15  ? 31.342 -21.251 -14.105 1.00 20.46 ?  15  ASN   B HB3  1 
ATOM   4039 H  HD21 . ASN   B 1 15  ? 31.667 -22.261 -10.456 1.00 19.16 ?  15  ASN   B HD21 1 
ATOM   4040 H  HD22 . ASN   B 1 15  ? 32.657 -21.402 -11.164 1.00 19.16 ?  15  ASN   B HD22 1 
ATOM   4041 N  N    . VAL   B 1 16  ? 33.810 -24.715 -13.448 1.00 15.57 ?  16  VAL   B N    1 
ATOM   4042 C  CA   . VAL   B 1 16  ? 34.821 -25.411 -12.655 1.00 15.35 ?  16  VAL   B CA   1 
ATOM   4043 C  C    . VAL   B 1 16  ? 35.603 -26.343 -13.565 1.00 15.27 ?  16  VAL   B C    1 
ATOM   4044 O  O    . VAL   B 1 16  ? 35.023 -27.233 -14.208 1.00 16.31 ?  16  VAL   B O    1 
ATOM   4045 C  CB   . VAL   B 1 16  ? 34.206 -26.183 -11.477 1.00 15.40 ?  16  VAL   B CB   1 
ATOM   4046 C  CG1  . VAL   B 1 16  ? 35.291 -26.915 -10.694 1.00 15.51 ?  16  VAL   B CG1  1 
ATOM   4047 C  CG2  . VAL   B 1 16  ? 33.419 -25.241 -10.569 1.00 15.85 ?  16  VAL   B CG2  1 
ATOM   4048 H  H    . VAL   B 1 16  ? 33.184 -25.235 -13.752 1.00 18.65 ?  16  VAL   B H    1 
ATOM   4049 H  HA   . VAL   B 1 16  ? 35.428 -24.758 -12.285 1.00 18.38 ?  16  VAL   B HA   1 
ATOM   4050 H  HB   . VAL   B 1 16  ? 33.583 -26.848 -11.817 1.00 18.44 ?  16  VAL   B HB   1 
ATOM   4051 H  HG11 . VAL   B 1 16  ? 34.915 -27.229 -9.853  1.00 18.57 ?  16  VAL   B HG11 1 
ATOM   4052 H  HG12 . VAL   B 1 16  ? 35.602 -27.669 -11.215 1.00 18.57 ?  16  VAL   B HG12 1 
ATOM   4053 H  HG13 . VAL   B 1 16  ? 36.018 -26.301 -10.519 1.00 18.57 ?  16  VAL   B HG13 1 
ATOM   4054 H  HG21 . VAL   B 1 16  ? 33.093 -25.737 -9.798  1.00 18.99 ?  16  VAL   B HG21 1 
ATOM   4055 H  HG22 . VAL   B 1 16  ? 33.997 -24.522 -10.278 1.00 18.99 ?  16  VAL   B HG22 1 
ATOM   4056 H  HG23 . VAL   B 1 16  ? 32.664 -24.879 -11.064 1.00 18.99 ?  16  VAL   B HG23 1 
ATOM   4057 N  N    . TYR   B 1 17  ? 36.919 -26.159 -13.573 1.00 15.82 ?  17  TYR   B N    1 
ATOM   4058 C  CA   . TYR   B 1 17  ? 37.857 -26.914 -14.383 1.00 16.45 ?  17  TYR   B CA   1 
ATOM   4059 C  C    . TYR   B 1 17  ? 38.912 -27.533 -13.475 1.00 15.52 ?  17  TYR   B C    1 
ATOM   4060 O  O    . TYR   B 1 17  ? 39.215 -27.005 -12.401 1.00 15.74 ?  17  TYR   B O    1 
ATOM   4061 C  CB   . TYR   B 1 17  ? 38.561 -25.999 -15.391 1.00 20.18 ?  17  TYR   B CB   1 
ATOM   4062 C  CG   . TYR   B 1 17  ? 37.641 -25.235 -16.311 1.00 24.31 ?  17  TYR   B CG   1 
ATOM   4063 C  CD1  . TYR   B 1 17  ? 37.098 -24.015 -15.932 1.00 26.44 ?  17  TYR   B CD1  1 
ATOM   4064 C  CD2  . TYR   B 1 17  ? 37.320 -25.734 -17.567 1.00 26.87 ?  17  TYR   B CD2  1 
ATOM   4065 C  CE1  . TYR   B 1 17  ? 36.254 -23.313 -16.777 1.00 28.49 ?  17  TYR   B CE1  1 
ATOM   4066 C  CE2  . TYR   B 1 17  ? 36.482 -25.042 -18.418 1.00 28.75 ?  17  TYR   B CE2  1 
ATOM   4067 C  CZ   . TYR   B 1 17  ? 35.949 -23.833 -18.018 1.00 29.73 ?  17  TYR   B CZ   1 
ATOM   4068 O  OH   . TYR   B 1 17  ? 35.114 -23.142 -18.864 1.00 30.88 ?  17  TYR   B OH   1 
ATOM   4069 H  H    . TYR   B 1 17  ? 37.307 -25.555 -13.093 1.00 18.95 ?  17  TYR   B H    1 
ATOM   4070 H  HA   . TYR   B 1 17  ? 37.382 -27.613 -14.866 1.00 19.70 ?  17  TYR   B HA   1 
ATOM   4071 H  HB2  . TYR   B 1 17  ? 39.111 -25.361 -14.915 1.00 24.18 ?  17  TYR   B HB2  1 
ATOM   4072 H  HB3  . TYR   B 1 17  ? 39.110 -26.554 -15.953 1.00 24.18 ?  17  TYR   B HB3  1 
ATOM   4073 H  HD1  . TYR   B 1 17  ? 37.302 -23.663 -15.097 1.00 31.69 ?  17  TYR   B HD1  1 
ATOM   4074 H  HD2  . TYR   B 1 17  ? 37.673 -26.549 -17.842 1.00 32.21 ?  17  TYR   B HD2  1 
ATOM   4075 H  HE1  . TYR   B 1 17  ? 35.896 -22.497 -16.511 1.00 34.15 ?  17  TYR   B HE1  1 
ATOM   4076 H  HE2  . TYR   B 1 17  ? 36.272 -25.392 -19.256 1.00 34.47 ?  17  TYR   B HE2  1 
ATOM   4077 H  HH   . TYR   B 1 17  ? 35.012 -23.570 -19.581 1.00 37.02 ?  17  TYR   B HH   1 
ATOM   4078 N  N    . ILE   B 1 18  ? 39.505 -28.640 -13.915 1.00 15.36 ?  18  ILE   B N    1 
ATOM   4079 C  CA   . ILE   B 1 18  ? 40.434 -29.374 -13.065 1.00 15.32 ?  18  ILE   B CA   1 
ATOM   4080 C  C    . ILE   B 1 18  ? 41.579 -29.934 -13.898 1.00 15.75 ?  18  ILE   B C    1 
ATOM   4081 O  O    . ILE   B 1 18  ? 41.410 -30.308 -15.061 1.00 16.52 ?  18  ILE   B O    1 
ATOM   4082 C  CB   . ILE   B 1 18  ? 39.692 -30.476 -12.264 1.00 15.65 ?  18  ILE   B CB   1 
ATOM   4083 C  CG1  . ILE   B 1 18  ? 40.561 -31.025 -11.132 1.00 16.19 ?  18  ILE   B CG1  1 
ATOM   4084 C  CG2  . ILE   B 1 18  ? 39.182 -31.593 -13.189 1.00 16.22 ?  18  ILE   B CG2  1 
ATOM   4085 C  CD1  . ILE   B 1 18  ? 39.777 -31.829 -10.107 1.00 17.33 ?  18  ILE   B CD1  1 
ATOM   4086 H  H    . ILE   B 1 18  ? 39.377 -28.979 -14.691 1.00 18.40 ?  18  ILE   B H    1 
ATOM   4087 H  HA   . ILE   B 1 18  ? 40.802 -28.755 -12.416 1.00 18.35 ?  18  ILE   B HA   1 
ATOM   4088 H  HB   . ILE   B 1 18  ? 38.908 -30.074 -11.852 1.00 18.74 ?  18  ILE   B HB   1 
ATOM   4089 H  HG12 . ILE   B 1 18  ? 41.238 -31.602 -11.508 1.00 19.39 ?  18  ILE   B HG12 1 
ATOM   4090 H  HG13 . ILE   B 1 18  ? 40.973 -30.279 -10.670 1.00 19.39 ?  18  ILE   B HG13 1 
ATOM   4091 H  HG21 . ILE   B 1 18  ? 38.599 -32.184 -12.683 1.00 19.43 ?  18  ILE   B HG21 1 
ATOM   4092 H  HG22 . ILE   B 1 18  ? 38.683 -31.191 -13.919 1.00 19.43 ?  18  ILE   B HG22 1 
ATOM   4093 H  HG23 . ILE   B 1 18  ? 39.936 -32.089 -13.535 1.00 19.43 ?  18  ILE   B HG23 1 
ATOM   4094 H  HD11 . ILE   B 1 18  ? 40.380 -32.111 -9.401  1.00 20.76 ?  18  ILE   B HD11 1 
ATOM   4095 H  HD12 . ILE   B 1 18  ? 39.073 -31.272 -9.737  1.00 20.76 ?  18  ILE   B HD12 1 
ATOM   4096 H  HD13 . ILE   B 1 18  ? 39.390 -32.605 -10.541 1.00 20.76 ?  18  ILE   B HD13 1 
ATOM   4097 N  N    . LYS   B 1 19  ? 42.762 -29.979 -13.290 1.00 16.14 ?  19  LYS   B N    1 
ATOM   4098 C  CA   . LYS   B 1 19  ? 43.966 -30.451 -13.958 1.00 17.29 ?  19  LYS   B CA   1 
ATOM   4099 C  C    . LYS   B 1 19  ? 44.880 -31.124 -12.941 1.00 17.02 ?  19  LYS   B C    1 
ATOM   4100 O  O    . LYS   B 1 19  ? 44.973 -30.692 -11.791 1.00 16.83 ?  19  LYS   B O    1 
ATOM   4101 C  CB   . LYS   B 1 19  ? 44.716 -29.285 -14.614 1.00 19.42 ?  19  LYS   B CB   1 
ATOM   4102 C  CG   . LYS   B 1 19  ? 45.882 -29.696 -15.491 1.00 21.88 ?  19  LYS   B CG   1 
ATOM   4103 C  CD   . LYS   B 1 19  ? 46.614 -28.474 -16.023 1.00 24.40 ?  19  LYS   B CD   1 
ATOM   4104 C  CE   . LYS   B 1 19  ? 47.789 -28.854 -16.901 1.00 26.64 ?  19  LYS   B CE   1 
ATOM   4105 N  NZ   . LYS   B 1 19  ? 48.510 -27.653 -17.404 1.00 27.67 ?  19  LYS   B NZ   1 
ATOM   4106 H  H    . LYS   B 1 19  ? 42.878 -29.736 -12.477 1.00 19.33 ?  19  LYS   B H    1 
ATOM   4107 H  HA   . LYS   B 1 19  ? 43.715 -31.096 -14.647 1.00 20.71 ?  19  LYS   B HA   1 
ATOM   4108 H  HB2  . LYS   B 1 19  ? 44.091 -28.799 -15.172 1.00 23.27 ?  19  LYS   B HB2  1 
ATOM   4109 H  HB3  . LYS   B 1 19  ? 45.050 -28.706 -13.912 1.00 23.27 ?  19  LYS   B HB3  1 
ATOM   4110 H  HG2  . LYS   B 1 19  ? 46.498 -30.231 -14.971 1.00 26.21 ?  19  LYS   B HG2  1 
ATOM   4111 H  HG3  . LYS   B 1 19  ? 45.541 -30.209 -16.245 1.00 26.21 ?  19  LYS   B HG3  1 
ATOM   4112 H  HD2  . LYS   B 1 19  ? 45.998 -27.939 -16.550 1.00 29.24 ?  19  LYS   B HD2  1 
ATOM   4113 H  HD3  . LYS   B 1 19  ? 46.947 -27.956 -15.273 1.00 29.24 ?  19  LYS   B HD3  1 
ATOM   4114 H  HE2  . LYS   B 1 19  ? 48.412 -29.392 -16.386 1.00 31.93 ?  19  LYS   B HE2  1 
ATOM   4115 H  HE3  . LYS   B 1 19  ? 47.466 -29.360 -17.665 1.00 31.93 ?  19  LYS   B HE3  1 
ATOM   4116 H  HZ1  . LYS   B 1 19  ? 49.183 -27.901 -17.933 1.00 33.17 ?  19  LYS   B HZ1  1 
ATOM   4117 H  HZ2  . LYS   B 1 19  ? 47.954 -27.136 -17.869 1.00 33.17 ?  19  LYS   B HZ2  1 
ATOM   4118 H  HZ3  . LYS   B 1 19  ? 48.837 -27.186 -16.721 1.00 33.17 ?  19  LYS   B HZ3  1 
ATOM   4119 N  N    . ASN   B 1 20  ? 45.556 -32.185 -13.369 1.00 18.05 ?  20  ASN   B N    1 
ATOM   4120 C  CA   . ASN   B 1 20  ? 46.597 -32.806 -12.553 1.00 19.13 ?  20  ASN   B CA   1 
ATOM   4121 C  C    . ASN   B 1 20  ? 47.874 -31.993 -12.753 1.00 19.56 ?  20  ASN   B C    1 
ATOM   4122 O  O    . ASN   B 1 20  ? 48.503 -32.069 -13.815 1.00 21.59 ?  20  ASN   B O    1 
ATOM   4123 C  CB   . ASN   B 1 20  ? 46.764 -34.267 -12.982 1.00 21.14 ?  20  ASN   B CB   1 
ATOM   4124 C  CG   . ASN   B 1 20  ? 47.937 -34.976 -12.305 1.00 22.88 ?  20  ASN   B CG   1 
ATOM   4125 O  OD1  . ASN   B 1 20  ? 48.603 -35.815 -12.926 1.00 24.82 ?  20  ASN   B OD1  1 
ATOM   4126 N  ND2  . ASN   B 1 20  ? 48.179 -34.671 -11.035 1.00 22.93 ?  20  ASN   B ND2  1 
ATOM   4127 H  H    . ASN   B 1 20  ? 45.433 -32.557 -14.133 1.00 21.62 ?  20  ASN   B H    1 
ATOM   4128 H  HA   . ASN   B 1 20  ? 46.331 -32.772 -11.618 1.00 22.92 ?  20  ASN   B HA   1 
ATOM   4129 H  HB2  . ASN   B 1 20  ? 45.946 -34.747 -12.759 1.00 25.32 ?  20  ASN   B HB2  1 
ATOM   4130 H  HB3  . ASN   B 1 20  ? 46.906 -34.290 -13.937 1.00 25.32 ?  20  ASN   B HB3  1 
ATOM   4131 H  HD21 . ASN   B 1 20  ? 48.826 -35.047 -10.616 1.00 27.48 ?  20  ASN   B HD21 1 
ATOM   4132 H  HD22 . ASN   B 1 20  ? 47.693 -34.082 -10.624 1.00 27.48 ?  20  ASN   B HD22 1 
ATOM   4133 N  N    A ALA   B 1 21  ? 48.252 -31.198 -11.749 0.70 19.08 ?  21  ALA   B N    1 
ATOM   4134 N  N    B ALA   B 1 21  ? 48.253 -31.206 -11.746 0.30 19.00 ?  21  ALA   B N    1 
ATOM   4135 C  CA   A ALA   B 1 21  ? 49.383 -30.295 -11.906 0.70 19.53 ?  21  ALA   B CA   1 
ATOM   4136 C  CA   B ALA   B 1 21  ? 49.394 -30.314 -11.906 0.30 18.94 ?  21  ALA   B CA   1 
ATOM   4137 C  C    A ALA   B 1 21  ? 49.856 -29.791 -10.548 0.70 18.87 ?  21  ALA   B C    1 
ATOM   4138 C  C    B ALA   B 1 21  ? 49.858 -29.796 -10.551 0.30 18.39 ?  21  ALA   B C    1 
ATOM   4139 O  O    A ALA   B 1 21  ? 49.120 -29.808 -9.558  0.70 18.72 ?  21  ALA   B O    1 
ATOM   4140 O  O    B ALA   B 1 21  ? 49.114 -29.804 -9.567  0.30 18.24 ?  21  ALA   B O    1 
ATOM   4141 C  CB   A ALA   B 1 21  ? 49.019 -29.122 -12.818 0.70 20.75 ?  21  ALA   B CB   1 
ATOM   4142 C  CB   B ALA   B 1 21  ? 49.052 -29.145 -12.832 0.30 19.53 ?  21  ALA   B CB   1 
ATOM   4143 H  H    A ALA   B 1 21  ? 47.870 -31.168 -10.976 0.70 22.85 ?  21  ALA   B H    1 
ATOM   4144 H  H    B ALA   B 1 21  ? 47.870 -31.172 -10.975 0.30 22.76 ?  21  ALA   B H    1 
ATOM   4145 H  HA   A ALA   B 1 21  ? 50.113 -30.784 -12.320 0.70 23.40 ?  21  ALA   B HA   1 
ATOM   4146 H  HA   B ALA   B 1 21  ? 50.123 -30.811 -12.304 0.30 22.70 ?  21  ALA   B HA   1 
ATOM   4147 H  HB1  A ALA   B 1 21  ? 49.817 -28.602 -12.979 0.70 24.87 ?  21  ALA   B HB1  1 
ATOM   4148 H  HB1  B ALA   B 1 21  ? 49.847 -28.607 -12.953 0.30 23.40 ?  21  ALA   B HB1  1 
ATOM   4149 H  HB2  A ALA   B 1 21  ? 48.677 -29.474 -13.656 0.70 24.87 ?  21  ALA   B HB2  1 
ATOM   4150 H  HB2  B ALA   B 1 21  ? 48.756 -29.499 -13.685 0.30 23.40 ?  21  ALA   B HB2  1 
ATOM   4151 H  HB3  A ALA   B 1 21  ? 48.341 -28.585 -12.383 0.70 24.87 ?  21  ALA   B HB3  1 
ATOM   4152 H  HB3  B ALA   B 1 21  ? 48.346 -28.619 -12.428 0.30 23.40 ?  21  ALA   B HB3  1 
ATOM   4153 N  N    . ASP   B 1 22  ? 51.113 -29.347 -10.531 1.00 17.94 ?  22  ASP   B N    1 
ATOM   4154 C  CA   . ASP   B 1 22  ? 51.721 -28.682 -9.378  1.00 17.13 ?  22  ASP   B CA   1 
ATOM   4155 C  C    . ASP   B 1 22  ? 51.329 -27.205 -9.436  1.00 15.75 ?  22  ASP   B C    1 
ATOM   4156 O  O    . ASP   B 1 22  ? 51.644 -26.523 -10.414 1.00 15.93 ?  22  ASP   B O    1 
ATOM   4157 C  CB   . ASP   B 1 22  ? 53.240 -28.866 -9.527  1.00 18.37 ?  22  ASP   B CB   1 
ATOM   4158 C  CG   . ASP   B 1 22  ? 54.073 -28.118 -8.491  1.00 20.07 ?  22  ASP   B CG   1 
ATOM   4159 O  OD1  . ASP   B 1 22  ? 53.720 -26.999 -8.086  1.00 20.04 ?  22  ASP   B OD1  1 
ATOM   4160 O  OD2  . ASP   B 1 22  ? 55.145 -28.646 -8.118  1.00 22.08 -1 22  ASP   B OD2  1 
ATOM   4161 H  H    A ASP   B 1 22  ? 51.652 -29.421 -11.201 0.70 21.49 ?  22  ASP   B H    1 
ATOM   4162 H  H    B ASP   B 1 22  ? 51.653 -29.423 -11.200 0.30 21.49 ?  22  ASP   B H    1 
ATOM   4163 H  HA   . ASP   B 1 22  ? 51.416 -29.085 -8.547  1.00 20.52 ?  22  ASP   B HA   1 
ATOM   4164 H  HB2  . ASP   B 1 22  ? 53.455 -29.805 -9.449  1.00 22.00 ?  22  ASP   B HB2  1 
ATOM   4165 H  HB3  . ASP   B 1 22  ? 53.507 -28.536 -10.399 1.00 22.00 ?  22  ASP   B HB3  1 
ATOM   4166 N  N    . ILE   B 1 23  ? 50.626 -26.718 -8.406  1.00 14.82 ?  23  ILE   B N    1 
ATOM   4167 C  CA   . ILE   B 1 23  ? 50.047 -25.371 -8.463  1.00 14.28 ?  23  ILE   B CA   1 
ATOM   4168 C  C    . ILE   B 1 23  ? 51.112 -24.288 -8.597  1.00 13.76 ?  23  ILE   B C    1 
ATOM   4169 O  O    . ILE   B 1 23  ? 50.851 -23.241 -9.195  1.00 13.23 ?  23  ILE   B O    1 
ATOM   4170 C  CB   . ILE   B 1 23  ? 49.109 -25.127 -7.264  1.00 14.28 ?  23  ILE   B CB   1 
ATOM   4171 C  CG1  . ILE   B 1 23  ? 48.294 -23.847 -7.458  1.00 14.76 ?  23  ILE   B CG1  1 
ATOM   4172 C  CG2  . ILE   B 1 23  ? 49.883 -25.125 -5.958  1.00 15.18 ?  23  ILE   B CG2  1 
ATOM   4173 C  CD1  . ILE   B 1 23  ? 47.184 -23.684 -6.435  1.00 15.34 ?  23  ILE   B CD1  1 
ATOM   4174 H  H    . ILE   B 1 23  ? 50.467 -27.146 -7.680  1.00 17.75 ?  23  ILE   B H    1 
ATOM   4175 H  HA   . ILE   B 1 23  ? 49.498 -25.319 -9.258  1.00 17.10 ?  23  ILE   B HA   1 
ATOM   4176 H  HB   . ILE   B 1 23  ? 48.484 -25.870 -7.232  1.00 17.10 ?  23  ILE   B HB   1 
ATOM   4177 H  HG12 . ILE   B 1 23  ? 48.889 -23.084 -7.379  1.00 17.67 ?  23  ILE   B HG12 1 
ATOM   4178 H  HG13 . ILE   B 1 23  ? 47.892 -23.862 -8.340  1.00 17.67 ?  23  ILE   B HG13 1 
ATOM   4179 H  HG21 . ILE   B 1 23  ? 49.255 -25.117 -5.220  1.00 18.18 ?  23  ILE   B HG21 1 
ATOM   4180 H  HG22 . ILE   B 1 23  ? 50.429 -25.929 -5.914  1.00 18.18 ?  23  ILE   B HG22 1 
ATOM   4181 H  HG23 . ILE   B 1 23  ? 50.448 -24.341 -5.926  1.00 18.18 ?  23  ILE   B HG23 1 
ATOM   4182 H  HD11 . ILE   B 1 23  ? 46.661 -22.902 -6.663  1.00 18.37 ?  23  ILE   B HD11 1 
ATOM   4183 H  HD12 . ILE   B 1 23  ? 46.624 -24.477 -6.454  1.00 18.37 ?  23  ILE   B HD12 1 
ATOM   4184 H  HD13 . ILE   B 1 23  ? 47.579 -23.578 -5.557  1.00 18.37 ?  23  ILE   B HD13 1 
ATOM   4185 N  N    . VAL   B 1 24  ? 52.309 -24.498 -8.041  1.00 13.83 ?  24  VAL   B N    1 
ATOM   4186 C  CA   . VAL   B 1 24  ? 53.384 -23.515 -8.201  1.00 14.43 ?  24  VAL   B CA   1 
ATOM   4187 C  C    . VAL   B 1 24  ? 53.837 -23.462 -9.653  1.00 14.48 ?  24  VAL   B C    1 
ATOM   4188 O  O    . VAL   B 1 24  ? 53.970 -22.382 -10.244 1.00 15.02 ?  24  VAL   B O    1 
ATOM   4189 C  CB   . VAL   B 1 24  ? 54.561 -23.829 -7.255  1.00 15.13 ?  24  VAL   B CB   1 
ATOM   4190 C  CG1  . VAL   B 1 24  ? 55.776 -22.955 -7.580  1.00 15.74 ?  24  VAL   B CG1  1 
ATOM   4191 C  CG2  . VAL   B 1 24  ? 54.146 -23.644 -5.813  1.00 15.98 ?  24  VAL   B CG2  1 
ATOM   4192 H  H    . VAL   B 1 24  ? 52.522 -25.187 -7.577  1.00 16.56 ?  24  VAL   B H    1 
ATOM   4193 H  HA   . VAL   B 1 24  ? 53.046 -22.638 -7.965  1.00 17.28 ?  24  VAL   B HA   1 
ATOM   4194 H  HB   . VAL   B 1 24  ? 54.824 -24.755 -7.368  1.00 18.11 ?  24  VAL   B HB   1 
ATOM   4195 H  HG11 . VAL   B 1 24  ? 56.381 -22.961 -6.820  1.00 18.85 ?  24  VAL   B HG11 1 
ATOM   4196 H  HG12 . VAL   B 1 24  ? 56.225 -23.315 -8.360  1.00 18.85 ?  24  VAL   B HG12 1 
ATOM   4197 H  HG13 . VAL   B 1 24  ? 55.477 -22.049 -7.754  1.00 18.85 ?  24  VAL   B HG13 1 
ATOM   4198 H  HG21 . VAL   B 1 24  ? 54.873 -23.919 -5.233  1.00 19.13 ?  24  VAL   B HG21 1 
ATOM   4199 H  HG22 . VAL   B 1 24  ? 53.942 -22.706 -5.661  1.00 19.13 ?  24  VAL   B HG22 1 
ATOM   4200 H  HG23 . VAL   B 1 24  ? 53.360 -24.184 -5.637  1.00 19.13 ?  24  VAL   B HG23 1 
ATOM   4201 N  N    . GLU   B 1 25  ? 54.113 -24.631 -10.240 1.00 15.50 ?  25  GLU   B N    1 
ATOM   4202 C  CA   . GLU   B 1 25  ? 54.504 -24.669 -11.644 1.00 17.29 ?  25  GLU   B CA   1 
ATOM   4203 C  C    . GLU   B 1 25  ? 53.393 -24.131 -12.532 1.00 15.74 ?  25  GLU   B C    1 
ATOM   4204 O  O    . GLU   B 1 25  ? 53.660 -23.420 -13.510 1.00 16.92 ?  25  GLU   B O    1 
ATOM   4205 C  CB   . GLU   B 1 25  ? 54.906 -26.089 -12.040 1.00 22.28 ?  25  GLU   B CB   1 
ATOM   4206 C  CG   . GLU   B 1 25  ? 56.210 -26.536 -11.388 1.00 27.88 ?  25  GLU   B CG   1 
ATOM   4207 C  CD   . GLU   B 1 25  ? 57.313 -25.488 -11.457 1.00 32.95 ?  25  GLU   B CD   1 
ATOM   4208 O  OE1  . GLU   B 1 25  ? 57.684 -25.079 -12.578 1.00 34.88 ?  25  GLU   B OE1  1 
ATOM   4209 O  OE2  . GLU   B 1 25  ? 57.802 -25.058 -10.386 1.00 34.62 -1 25  GLU   B OE2  1 
ATOM   4210 H  H    . GLU   B 1 25  ? 54.077 -25.396 -9.853  1.00 18.56 ?  25  GLU   B H    1 
ATOM   4211 H  HA   . GLU   B 1 25  ? 55.258 -24.081 -11.773 1.00 20.71 ?  25  GLU   B HA   1 
ATOM   4212 H  HB2  . GLU   B 1 25  ? 54.208 -26.707 -11.761 1.00 26.69 ?  25  GLU   B HB2  1 
ATOM   4213 H  HB3  . GLU   B 1 25  ? 55.017 -26.131 -13.003 1.00 26.69 ?  25  GLU   B HB3  1 
ATOM   4214 H  HG2  . GLU   B 1 25  ? 56.051 -26.715 -10.454 1.00 33.42 ?  25  GLU   B HG2  1 
ATOM   4215 H  HG3  . GLU   B 1 25  ? 56.532 -27.329 -11.840 1.00 33.42 ?  25  GLU   B HG3  1 
ATOM   4216 N  N    A GLU   B 1 26  ? 52.140 -24.451 -12.203 0.70 14.90 ?  26  GLU   B N    1 
ATOM   4217 N  N    B GLU   B 1 26  ? 52.138 -24.451 -12.203 0.30 15.22 ?  26  GLU   B N    1 
ATOM   4218 C  CA   A GLU   B 1 26  ? 51.012 -23.938 -12.974 0.70 15.79 ?  26  GLU   B CA   1 
ATOM   4219 C  CA   B GLU   B 1 26  ? 51.012 -23.938 -12.978 0.30 15.47 ?  26  GLU   B CA   1 
ATOM   4220 C  C    A GLU   B 1 26  ? 50.952 -22.421 -12.904 0.70 14.82 ?  26  GLU   B C    1 
ATOM   4221 C  C    B GLU   B 1 26  ? 50.949 -22.420 -12.904 0.30 14.63 ?  26  GLU   B C    1 
ATOM   4222 O  O    A GLU   B 1 26  ? 50.755 -21.749 -13.921 0.70 15.98 ?  26  GLU   B O    1 
ATOM   4223 O  O    B GLU   B 1 26  ? 50.756 -21.745 -13.921 0.30 15.15 ?  26  GLU   B O    1 
ATOM   4224 C  CB   A GLU   B 1 26  ? 49.702 -24.526 -12.448 0.70 18.11 ?  26  GLU   B CB   1 
ATOM   4225 C  CB   B GLU   B 1 26  ? 49.701 -24.541 -12.470 0.30 16.72 ?  26  GLU   B CB   1 
ATOM   4226 C  CG   A GLU   B 1 26  ? 49.278 -25.811 -13.117 0.70 22.06 ?  26  GLU   B CG   1 
ATOM   4227 C  CG   B GLU   B 1 26  ? 49.244 -25.769 -13.233 0.30 18.73 ?  26  GLU   B CG   1 
ATOM   4228 C  CD   A GLU   B 1 26  ? 49.004 -25.644 -14.609 0.70 24.12 ?  26  GLU   B CD   1 
ATOM   4229 C  CD   B GLU   B 1 26  ? 48.898 -25.466 -14.693 0.30 19.09 ?  26  GLU   B CD   1 
ATOM   4230 O  OE1  A GLU   B 1 26  ? 48.163 -24.801 -14.988 0.70 25.01 ?  26  GLU   B OE1  1 
ATOM   4231 O  OE1  B GLU   B 1 26  ? 47.774 -24.982 -14.968 0.30 19.45 ?  26  GLU   B OE1  1 
ATOM   4232 O  OE2  A GLU   B 1 26  ? 49.635 -26.366 -15.403 0.70 25.25 -1 26  GLU   B OE2  1 
ATOM   4233 O  OE2  B GLU   B 1 26  ? 49.755 -25.706 -15.564 0.30 19.34 -1 26  GLU   B OE2  1 
ATOM   4234 H  H    A GLU   B 1 26  ? 51.914 -24.959 -11.542 0.70 17.84 ?  26  GLU   B H    1 
ATOM   4235 H  H    B GLU   B 1 26  ? 51.914 -24.955 -11.540 0.30 18.23 ?  26  GLU   B H    1 
ATOM   4236 H  HA   A GLU   B 1 26  ? 51.116 -24.196 -13.903 0.70 18.90 ?  26  GLU   B HA   1 
ATOM   4237 H  HA   B GLU   B 1 26  ? 51.126 -24.189 -13.906 0.30 18.52 ?  26  GLU   B HA   1 
ATOM   4238 H  HB2  A GLU   B 1 26  ? 49.801 -24.702 -11.499 0.70 21.69 ?  26  GLU   B HB2  1 
ATOM   4239 H  HB2  B GLU   B 1 26  ? 49.812 -24.791 -11.539 0.30 20.03 ?  26  GLU   B HB2  1 
ATOM   4240 H  HB3  A GLU   B 1 26  ? 48.995 -23.872 -12.583 0.70 21.69 ?  26  GLU   B HB3  1 
ATOM   4241 H  HB3  B GLU   B 1 26  ? 49.001 -23.871 -12.546 0.30 20.03 ?  26  GLU   B HB3  1 
ATOM   4242 H  HG2  A GLU   B 1 26  ? 49.989 -26.452 -13.009 0.70 26.43 ?  26  GLU   B HG2  1 
ATOM   4243 H  HG2  B GLU   B 1 26  ? 49.955 -26.429 -13.188 0.30 22.44 ?  26  GLU   B HG2  1 
ATOM   4244 H  HG3  A GLU   B 1 26  ? 48.466 -26.125 -12.692 0.70 26.43 ?  26  GLU   B HG3  1 
ATOM   4245 H  HG3  B GLU   B 1 26  ? 48.442 -26.111 -12.817 0.30 22.44 ?  26  GLU   B HG3  1 
ATOM   4246 N  N    . ALA   B 1 27  ? 51.099 -21.864 -11.700 1.00 13.93 ?  27  ALA   B N    1 
ATOM   4247 C  CA   . ALA   B 1 27  ? 51.063 -20.415 -11.553 1.00 13.97 ?  27  ALA   B CA   1 
ATOM   4248 C  C    . ALA   B 1 27  ? 52.128 -19.753 -12.416 1.00 15.25 ?  27  ALA   B C    1 
ATOM   4249 O  O    . ALA   B 1 27  ? 51.858 -18.764 -13.107 1.00 16.10 ?  27  ALA   B O    1 
ATOM   4250 C  CB   . ALA   B 1 27  ? 51.222 -20.037 -10.081 1.00 14.12 ?  27  ALA   B CB   1 
ATOM   4251 H  H    A ALA   B 1 27  ? 51.215 -22.298 -10.968 0.70 16.68 ?  27  ALA   B H    1 
ATOM   4252 H  H    B ALA   B 1 27  ? 51.220 -22.298 -10.969 0.30 16.68 ?  27  ALA   B H    1 
ATOM   4253 H  HA   . ALA   B 1 27  ? 50.202 -20.089 -11.847 1.00 16.73 ?  27  ALA   B HA   1 
ATOM   4254 H  HB1  . ALA   B 1 27  ? 51.189 -19.074 -9.994  1.00 16.90 ?  27  ALA   B HB1  1 
ATOM   4255 H  HB2  . ALA   B 1 27  ? 50.495 -20.439 -9.573  1.00 16.90 ?  27  ALA   B HB2  1 
ATOM   4256 H  HB3  . ALA   B 1 27  ? 52.071 -20.373 -9.755  1.00 16.90 ?  27  ALA   B HB3  1 
ATOM   4257 N  N    . LYS   B 1 28  ? 53.346 -20.295 -12.410 1.00 16.70 ?  28  LYS   B N    1 
ATOM   4258 C  CA   . LYS   B 1 28  ? 54.417 -19.677 -13.183 1.00 18.87 ?  28  LYS   B CA   1 
ATOM   4259 C  C    . LYS   B 1 28  ? 54.171 -19.778 -14.680 1.00 19.39 ?  28  LYS   B C    1 
ATOM   4260 O  O    . LYS   B 1 28  ? 54.590 -18.889 -15.433 1.00 20.43 ?  28  LYS   B O    1 
ATOM   4261 C  CB   . LYS   B 1 28  ? 55.771 -20.269 -12.786 1.00 22.18 ?  28  LYS   B CB   1 
ATOM   4262 C  CG   . LYS   B 1 28  ? 56.173 -19.892 -11.363 1.00 25.95 ?  28  LYS   B CG   1 
ATOM   4263 C  CD   . LYS   B 1 28  ? 57.600 -20.292 -11.017 1.00 30.74 ?  28  LYS   B CD   1 
ATOM   4264 C  CE   . LYS   B 1 28  ? 57.703 -21.767 -10.709 1.00 34.24 ?  28  LYS   B CE   1 
ATOM   4265 N  NZ   . LYS   B 1 28  ? 59.058 -22.128 -10.206 1.00 36.52 ?  28  LYS   B NZ   1 
ATOM   4266 H  H    . LYS   B 1 28  ? 53.572 -21.003 -11.979 1.00 20.00 ?  28  LYS   B H    1 
ATOM   4267 H  HA   . LYS   B 1 28  ? 54.443 -18.737 -12.971 1.00 22.60 ?  28  LYS   B HA   1 
ATOM   4268 H  HB2  . LYS   B 1 28  ? 55.729 -21.236 -12.842 1.00 26.57 ?  28  LYS   B HB2  1 
ATOM   4269 H  HB3  . LYS   B 1 28  ? 56.454 -19.932 -13.391 1.00 26.57 ?  28  LYS   B HB3  1 
ATOM   4270 H  HG2  . LYS   B 1 28  ? 56.096 -18.928 -11.263 1.00 31.10 ?  28  LYS   B HG2  1 
ATOM   4271 H  HG3  . LYS   B 1 28  ? 55.576 -20.336 -10.743 1.00 31.10 ?  28  LYS   B HG3  1 
ATOM   4272 H  HD2  . LYS   B 1 28  ? 58.177 -20.093 -11.771 1.00 36.85 ?  28  LYS   B HD2  1 
ATOM   4273 H  HD3  . LYS   B 1 28  ? 57.887 -19.793 -10.235 1.00 36.85 ?  28  LYS   B HD3  1 
ATOM   4274 H  HE2  . LYS   B 1 28  ? 57.053 -21.996 -10.026 1.00 41.05 ?  28  LYS   B HE2  1 
ATOM   4275 H  HE3  . LYS   B 1 28  ? 57.532 -22.274 -11.517 1.00 41.05 ?  28  LYS   B HE3  1 
ATOM   4276 H  HZ1  . LYS   B 1 28  ? 59.095 -23.000 -10.032 1.00 43.78 ?  28  LYS   B HZ1  1 
ATOM   4277 H  HZ2  . LYS   B 1 28  ? 59.672 -21.929 -10.818 1.00 43.78 ?  28  LYS   B HZ2  1 
ATOM   4278 H  HZ3  . LYS   B 1 28  ? 59.236 -21.676 -9.460  1.00 43.78 ?  28  LYS   B HZ3  1 
ATOM   4279 N  N    . LYS   B 1 29  ? 53.463 -20.816 -15.130 1.00 20.55 ?  29  LYS   B N    1 
ATOM   4280 C  CA   . LYS   B 1 29  ? 53.195 -20.981 -16.554 1.00 23.30 ?  29  LYS   B CA   1 
ATOM   4281 C  C    . LYS   B 1 29  ? 51.946 -20.230 -17.007 1.00 22.09 ?  29  LYS   B C    1 
ATOM   4282 O  O    . LYS   B 1 29  ? 51.952 -19.619 -18.081 1.00 23.53 ?  29  LYS   B O    1 
ATOM   4283 C  CB   . LYS   B 1 29  ? 53.066 -22.469 -16.898 1.00 28.30 ?  29  LYS   B CB   1 
ATOM   4284 C  CG   . LYS   B 1 29  ? 52.880 -22.751 -18.380 1.00 33.09 ?  29  LYS   B CG   1 
ATOM   4285 C  CD   . LYS   B 1 29  ? 53.092 -24.227 -18.700 1.00 36.92 ?  29  LYS   B CD   1 
ATOM   4286 C  CE   . LYS   B 1 29  ? 51.957 -25.093 -18.174 1.00 39.58 ?  29  LYS   B CE   1 
ATOM   4287 N  NZ   . LYS   B 1 29  ? 52.196 -26.541 -18.445 1.00 41.11 ?  29  LYS   B NZ   1 
ATOM   4288 H  H    . LYS   B 1 29  ? 53.115 -21.437 -14.632 1.00 24.62 ?  29  LYS   B H    1 
ATOM   4289 H  HA   . LYS   B 1 29  ? 53.945 -20.630 -17.051 1.00 27.92 ?  29  LYS   B HA   1 
ATOM   4290 H  HB2  . LYS   B 1 29  ? 53.877 -22.923 -16.615 1.00 33.92 ?  29  LYS   B HB2  1 
ATOM   4291 H  HB3  . LYS   B 1 29  ? 52.304 -22.837 -16.431 1.00 33.92 ?  29  LYS   B HB3  1 
ATOM   4292 H  HG2  . LYS   B 1 29  ? 51.977 -22.510 -18.640 1.00 39.67 ?  29  LYS   B HG2  1 
ATOM   4293 H  HG3  . LYS   B 1 29  ? 53.524 -22.234 -18.890 1.00 39.67 ?  29  LYS   B HG3  1 
ATOM   4294 H  HD2  . LYS   B 1 29  ? 53.139 -24.343 -19.661 1.00 44.26 ?  29  LYS   B HD2  1 
ATOM   4295 H  HD3  . LYS   B 1 29  ? 53.917 -24.528 -18.286 1.00 44.26 ?  29  LYS   B HD3  1 
ATOM   4296 H  HE2  . LYS   B 1 29  ? 51.879 -24.974 -17.215 1.00 47.46 ?  29  LYS   B HE2  1 
ATOM   4297 H  HE3  . LYS   B 1 29  ? 51.130 -24.835 -18.611 1.00 47.46 ?  29  LYS   B HE3  1 
ATOM   4298 H  HZ1  . LYS   B 1 29  ? 51.519 -27.026 -18.129 1.00 49.30 ?  29  LYS   B HZ1  1 
ATOM   4299 H  HZ2  . LYS   B 1 29  ? 52.266 -26.679 -19.321 1.00 49.30 ?  29  LYS   B HZ2  1 
ATOM   4300 H  HZ3  . LYS   B 1 29  ? 52.949 -26.803 -18.050 1.00 49.30 ?  29  LYS   B HZ3  1 
ATOM   4301 N  N    . VAL   B 1 30  ? 50.877 -20.272 -16.206 1.00 20.18 ?  30  VAL   B N    1 
ATOM   4302 C  CA   . VAL   B 1 30  ? 49.593 -19.679 -16.584 1.00 19.99 ?  30  VAL   B CA   1 
ATOM   4303 C  C    . VAL   B 1 30  ? 49.589 -18.168 -16.413 1.00 17.98 ?  30  VAL   B C    1 
ATOM   4304 O  O    . VAL   B 1 30  ? 48.828 -17.459 -17.097 1.00 18.76 ?  30  VAL   B O    1 
ATOM   4305 C  CB   . VAL   B 1 30  ? 48.484 -20.303 -15.717 1.00 21.61 ?  30  VAL   B CB   1 
ATOM   4306 C  CG1  . VAL   B 1 30  ? 47.190 -19.515 -15.832 1.00 22.74 ?  30  VAL   B CG1  1 
ATOM   4307 C  CG2  . VAL   B 1 30  ? 48.277 -21.767 -16.085 1.00 22.46 ?  30  VAL   B CG2  1 
ATOM   4308 H  H    . VAL   B 1 30  ? 50.864 -20.666 -15.435 1.00 24.17 ?  30  VAL   B H    1 
ATOM   4309 H  HA   . VAL   B 1 30  ? 49.401 -19.894 -17.510 1.00 23.95 ?  30  VAL   B HA   1 
ATOM   4310 H  HB   . VAL   B 1 30  ? 48.758 -20.278 -14.787 1.00 25.90 ?  30  VAL   B HB   1 
ATOM   4311 H  HG11 . VAL   B 1 30  ? 46.453 -20.131 -15.719 1.00 27.25 ?  30  VAL   B HG11 1 
ATOM   4312 H  HG12 . VAL   B 1 30  ? 47.166 -18.839 -15.140 1.00 27.25 ?  30  VAL   B HG12 1 
ATOM   4313 H  HG13 . VAL   B 1 30  ? 47.137 -19.116 -16.708 1.00 27.25 ?  30  VAL   B HG13 1 
ATOM   4314 H  HG21 . VAL   B 1 30  ? 47.582 -22.147 -15.518 1.00 26.92 ?  30  VAL   B HG21 1 
ATOM   4315 H  HG22 . VAL   B 1 30  ? 48.003 -21.826 -17.016 1.00 26.92 ?  30  VAL   B HG22 1 
ATOM   4316 H  HG23 . VAL   B 1 30  ? 49.106 -22.250 -15.954 1.00 26.92 ?  30  VAL   B HG23 1 
ATOM   4317 N  N    A LYS   B 1 31  ? 50.407 -17.652 -15.503 0.70 17.31 ?  31  LYS   B N    1 
ATOM   4318 N  N    B LYS   B 1 31  ? 50.407 -17.659 -15.500 0.30 17.97 ?  31  LYS   B N    1 
ATOM   4319 C  CA   A LYS   B 1 31  ? 50.416 -16.239 -15.141 0.70 17.82 ?  31  LYS   B CA   1 
ATOM   4320 C  CA   B LYS   B 1 31  ? 50.417 -16.249 -15.135 0.30 18.44 ?  31  LYS   B CA   1 
ATOM   4321 C  C    A LYS   B 1 31  ? 49.023 -15.738 -14.745 0.70 15.98 ?  31  LYS   B C    1 
ATOM   4322 C  C    B LYS   B 1 31  ? 49.015 -15.761 -14.759 0.30 16.44 ?  31  LYS   B C    1 
ATOM   4323 O  O    A LYS   B 1 31  ? 48.486 -14.817 -15.366 0.70 16.32 ?  31  LYS   B O    1 
ATOM   4324 O  O    B LYS   B 1 31  ? 48.462 -14.871 -15.414 0.30 16.36 ?  31  LYS   B O    1 
ATOM   4325 C  CB   A LYS   B 1 31  ? 51.028 -15.387 -16.246 0.70 20.79 ?  31  LYS   B CB   1 
ATOM   4326 C  CB   B LYS   B 1 31  ? 51.027 -15.399 -16.240 0.30 21.06 ?  31  LYS   B CB   1 
ATOM   4327 C  CG   A LYS   B 1 31  ? 52.476 -15.778 -16.548 0.70 23.98 ?  31  LYS   B CG   1 
ATOM   4328 C  CG   B LYS   B 1 31  ? 52.453 -15.827 -16.568 0.30 23.55 ?  31  LYS   B CG   1 
ATOM   4329 C  CD   A LYS   B 1 31  ? 53.069 -14.983 -17.695 0.70 27.47 ?  31  LYS   B CD   1 
ATOM   4330 C  CD   B LYS   B 1 31  ? 53.052 -15.030 -17.708 0.30 25.83 ?  31  LYS   B CD   1 
ATOM   4331 C  CE   A LYS   B 1 31  ? 54.554 -15.253 -17.834 0.70 29.97 ?  31  LYS   B CE   1 
ATOM   4332 C  CE   B LYS   B 1 31  ? 54.554 -15.240 -17.784 0.30 27.47 ?  31  LYS   B CE   1 
ATOM   4333 N  NZ   A LYS   B 1 31  ? 55.304 -14.833 -16.616 0.70 31.33 ?  31  LYS   B NZ   1 
ATOM   4334 N  NZ   B LYS   B 1 31  ? 55.225 -14.808 -16.526 0.30 28.37 ?  31  LYS   B NZ   1 
ATOM   4335 H  H    A LYS   B 1 31  ? 50.992 -18.123 -15.077 0.70 20.74 ?  31  LYS   B H    1 
ATOM   4336 H  H    B LYS   B 1 31  ? 50.987 -18.130 -15.071 0.30 21.52 ?  31  LYS   B H    1 
ATOM   4337 H  HA   A LYS   B 1 31  ? 50.980 -16.146 -14.366 0.70 21.35 ?  31  LYS   B HA   1 
ATOM   4338 H  HA   B LYS   B 1 31  ? 50.977 -16.152 -14.357 0.30 22.09 ?  31  LYS   B HA   1 
ATOM   4339 H  HB2  A LYS   B 1 31  ? 50.509 -15.497 -17.059 0.70 24.91 ?  31  LYS   B HB2  1 
ATOM   4340 H  HB2  B LYS   B 1 31  ? 50.495 -15.483 -17.045 0.30 25.24 ?  31  LYS   B HB2  1 
ATOM   4341 H  HB3  A LYS   B 1 31  ? 51.016 -14.461 -15.964 0.70 24.91 ?  31  LYS   B HB3  1 
ATOM   4342 H  HB3  B LYS   B 1 31  ? 51.051 -14.474 -15.949 0.30 25.24 ?  31  LYS   B HB3  1 
ATOM   4343 H  HG2  A LYS   B 1 31  ? 53.012 -15.619 -15.755 0.70 28.73 ?  31  LYS   B HG2  1 
ATOM   4344 H  HG2  B LYS   B 1 31  ? 53.006 -15.701 -15.781 0.30 28.22 ?  31  LYS   B HG2  1 
ATOM   4345 H  HG3  A LYS   B 1 31  ? 52.506 -16.720 -16.783 0.70 28.73 ?  31  LYS   B HG3  1 
ATOM   4346 H  HG3  B LYS   B 1 31  ? 52.454 -16.763 -16.826 0.30 28.22 ?  31  LYS   B HG3  1 
ATOM   4347 H  HD2  A LYS   B 1 31  ? 52.627 -15.243 -18.519 0.70 32.92 ?  31  LYS   B HD2  1 
ATOM   4348 H  HD2  B LYS   B 1 31  ? 52.659 -15.323 -18.545 0.30 30.96 ?  31  LYS   B HD2  1 
ATOM   4349 H  HD3  A LYS   B 1 31  ? 52.939 -14.039 -17.525 0.70 32.92 ?  31  LYS   B HD3  1 
ATOM   4350 H  HD3  B LYS   B 1 31  ? 52.882 -14.088 -17.564 0.30 30.96 ?  31  LYS   B HD3  1 
ATOM   4351 H  HE2  A LYS   B 1 31  ? 54.696 -16.204 -17.967 0.70 35.92 ?  31  LYS   B HE2  1 
ATOM   4352 H  HE2  B LYS   B 1 31  ? 54.740 -16.184 -17.920 0.30 32.93 ?  31  LYS   B HE2  1 
ATOM   4353 H  HE3  A LYS   B 1 31  ? 54.898 -14.754 -18.590 0.70 35.92 ?  31  LYS   B HE3  1 
ATOM   4354 H  HE3  B LYS   B 1 31  ? 54.914 -14.718 -18.517 0.30 32.93 ?  31  LYS   B HE3  1 
ATOM   4355 H  HZ1  A LYS   B 1 31  ? 56.179 -14.905 -16.758 0.70 37.55 ?  31  LYS   B HZ1  1 
ATOM   4356 H  HZ1  B LYS   B 1 31  ? 56.105 -14.774 -16.646 0.30 34.00 ?  31  LYS   B HZ1  1 
ATOM   4357 H  HZ2  A LYS   B 1 31  ? 55.110 -13.988 -16.416 0.70 37.55 ?  31  LYS   B HZ2  1 
ATOM   4358 H  HZ2  B LYS   B 1 31  ? 54.933 -14.002 -16.288 0.30 34.00 ?  31  LYS   B HZ2  1 
ATOM   4359 H  HZ3  A LYS   B 1 31  ? 55.080 -15.351 -15.926 0.70 37.55 ?  31  LYS   B HZ3  1 
ATOM   4360 H  HZ3  B LYS   B 1 31  ? 55.045 -15.384 -15.870 0.30 34.00 ?  31  LYS   B HZ3  1 
ATOM   4361 N  N    . PRO   B 1 32  ? 48.418 -16.326 -13.710 1.00 14.99 ?  32  PRO   B N    1 
ATOM   4362 C  CA   . PRO   B 1 32  ? 47.049 -15.955 -13.340 1.00 14.47 ?  32  PRO   B CA   1 
ATOM   4363 C  C    . PRO   B 1 32  ? 46.984 -14.613 -12.634 1.00 14.44 ?  32  PRO   B C    1 
ATOM   4364 O  O    . PRO   B 1 32  ? 47.923 -14.192 -11.952 1.00 15.26 ?  32  PRO   B O    1 
ATOM   4365 C  CB   . PRO   B 1 32  ? 46.654 -17.067 -12.360 1.00 14.57 ?  32  PRO   B CB   1 
ATOM   4366 C  CG   . PRO   B 1 32  ? 47.965 -17.413 -11.693 1.00 14.70 ?  32  PRO   B CG   1 
ATOM   4367 C  CD   . PRO   B 1 32  ? 49.011 -17.292 -12.761 1.00 14.84 ?  32  PRO   B CD   1 
ATOM   4368 H  HA   . PRO   B 1 32  ? 46.457 -15.974 -14.119 1.00 17.33 ?  32  PRO   B HA   1 
ATOM   4369 H  HB2  . PRO   B 1 32  ? 46.012 -16.729 -11.715 1.00 17.45 ?  32  PRO   B HB2  1 
ATOM   4370 H  HB3  . PRO   B 1 32  ? 46.294 -17.833 -12.838 1.00 17.45 ?  32  PRO   B HB3  1 
ATOM   4371 H  HG2  . PRO   B 1 32  ? 48.139 -16.787 -10.972 1.00 17.60 ?  32  PRO   B HG2  1 
ATOM   4372 H  HG3  . PRO   B 1 32  ? 47.930 -18.322 -11.351 1.00 17.60 ?  32  PRO   B HG3  1 
ATOM   4373 H  HD2  . PRO   B 1 32  ? 49.829 -16.934 -12.387 1.00 17.77 ?  32  PRO   B HD2  1 
ATOM   4374 H  HD3  . PRO   B 1 32  ? 49.154 -18.150 -13.184 1.00 17.77 ?  32  PRO   B HD3  1 
ATOM   4375 N  N    . THR   B 1 33  ? 45.830 -13.953 -12.782 1.00 13.83 ?  33  THR   B N    1 
ATOM   4376 C  CA   . THR   B 1 33  ? 45.556 -12.773 -11.971 1.00 14.30 ?  33  THR   B CA   1 
ATOM   4377 C  C    . THR   B 1 33  ? 45.516 -13.126 -10.489 1.00 13.75 ?  33  THR   B C    1 
ATOM   4378 O  O    . THR   B 1 33  ? 46.011 -12.356 -9.650  1.00 14.73 ?  33  THR   B O    1 
ATOM   4379 C  CB   . THR   B 1 33  ? 44.244 -12.114 -12.407 1.00 15.33 ?  33  THR   B CB   1 
ATOM   4380 O  OG1  . THR   B 1 33  ? 44.258 -11.892 -13.819 1.00 15.40 ?  33  THR   B OG1  1 
ATOM   4381 C  CG2  . THR   B 1 33  ? 44.045 -10.804 -11.688 1.00 16.65 ?  33  THR   B CG2  1 
ATOM   4382 H  H    . THR   B 1 33  ? 45.202 -14.179 -13.333 1.00 16.56 ?  33  THR   B H    1 
ATOM   4383 H  HA   . THR   B 1 33  ? 46.271 -12.140 -12.113 1.00 17.12 ?  33  THR   B HA   1 
ATOM   4384 H  HB   . THR   B 1 33  ? 43.502 -12.711 -12.186 1.00 18.36 ?  33  THR   B HB   1 
ATOM   4385 H  HG1  . THR   B 1 33  ? 43.542 -11.522 -14.058 1.00 18.44 ?  33  THR   B HG1  1 
ATOM   4386 H  HG21 . THR   B 1 33  ? 43.287 -10.338 -12.059 1.00 19.94 ?  33  THR   B HG21 1 
ATOM   4387 H  HG22 . THR   B 1 33  ? 43.893 -10.964 -10.743 1.00 19.94 ?  33  THR   B HG22 1 
ATOM   4388 H  HG23 . THR   B 1 33  ? 44.840 -10.255 -11.790 1.00 19.94 ?  33  THR   B HG23 1 
ATOM   4389 N  N    . VAL   B 1 34  ? 44.939 -14.285 -10.145 1.00 12.79 ?  34  VAL   B N    1 
ATOM   4390 C  CA   . VAL   B 1 34  ? 44.737 -14.679 -8.754  1.00 12.55 ?  34  VAL   B CA   1 
ATOM   4391 C  C    . VAL   B 1 34  ? 45.151 -16.130 -8.583  1.00 11.75 ?  34  VAL   B C    1 
ATOM   4392 O  O    . VAL   B 1 34  ? 44.624 -17.014 -9.269  1.00 12.66 ?  34  VAL   B O    1 
ATOM   4393 C  CB   . VAL   B 1 34  ? 43.261 -14.529 -8.322  1.00 13.74 ?  34  VAL   B CB   1 
ATOM   4394 C  CG1  . VAL   B 1 34  ? 43.080 -14.959 -6.878  1.00 14.60 ?  34  VAL   B CG1  1 
ATOM   4395 C  CG2  . VAL   B 1 34  ? 42.775 -13.101 -8.528  1.00 14.48 ?  34  VAL   B CG2  1 
ATOM   4396 H  H    . VAL   B 1 34  ? 44.664 -14.875 -10.709 1.00 15.31 ?  34  VAL   B H    1 
ATOM   4397 H  HA   . VAL   B 1 34  ? 45.282 -14.131 -8.169  1.00 15.02 ?  34  VAL   B HA   1 
ATOM   4398 H  HB   . VAL   B 1 34  ? 42.714 -15.109 -8.878  1.00 16.45 ?  34  VAL   B HB   1 
ATOM   4399 H  HG11 . VAL   B 1 34  ? 42.218 -14.641 -6.561  1.00 17.48 ?  34  VAL   B HG11 1 
ATOM   4400 H  HG12 . VAL   B 1 34  ? 43.110 -15.927 -6.825  1.00 17.48 ?  34  VAL   B HG12 1 
ATOM   4401 H  HG13 . VAL   B 1 34  ? 43.789 -14.573 -6.342  1.00 17.48 ?  34  VAL   B HG13 1 
ATOM   4402 H  HG21 . VAL   B 1 34  ? 41.854 -13.035 -8.228  1.00 17.33 ?  34  VAL   B HG21 1 
ATOM   4403 H  HG22 . VAL   B 1 34  ? 43.335 -12.499 -8.018  1.00 17.33 ?  34  VAL   B HG22 1 
ATOM   4404 H  HG23 . VAL   B 1 34  ? 42.827 -12.881 -9.474  1.00 17.33 ?  34  VAL   B HG23 1 
ATOM   4405 N  N    . VAL   B 1 35  ? 46.049 -16.388 -7.633  1.00 10.95 ?  35  VAL   B N    1 
ATOM   4406 C  CA   . VAL   B 1 35  ? 46.274 -17.730 -7.113  1.00 11.12 ?  35  VAL   B CA   1 
ATOM   4407 C  C    . VAL   B 1 35  ? 45.733 -17.781 -5.694  1.00 10.66 ?  35  VAL   B C    1 
ATOM   4408 O  O    . VAL   B 1 35  ? 45.950 -16.857 -4.902  1.00 11.12 ?  35  VAL   B O    1 
ATOM   4409 C  CB   . VAL   B 1 35  ? 47.755 -18.167 -7.191  1.00 12.36 ?  35  VAL   B CB   1 
ATOM   4410 C  CG1  . VAL   B 1 35  ? 48.652 -17.338 -6.260  1.00 13.02 ?  35  VAL   B CG1  1 
ATOM   4411 C  CG2  . VAL   B 1 35  ? 47.894 -19.666 -6.896  1.00 12.73 ?  35  VAL   B CG2  1 
ATOM   4412 H  H    . VAL   B 1 35  ? 46.548 -15.787 -7.266  1.00 13.10 ?  35  VAL   B H    1 
ATOM   4413 H  HA   . VAL   B 1 35  ? 45.760 -18.358 -7.638  1.00 13.31 ?  35  VAL   B HA   1 
ATOM   4414 H  HB   . VAL   B 1 35  ? 48.068 -18.025 -8.098  1.00 14.79 ?  35  VAL   B HB   1 
ATOM   4415 H  HG11 . VAL   B 1 35  ? 49.576 -17.557 -6.447  1.00 15.59 ?  35  VAL   B HG11 1 
ATOM   4416 H  HG12 . VAL   B 1 35  ? 48.485 -16.403 -6.421  1.00 15.59 ?  35  VAL   B HG12 1 
ATOM   4417 H  HG13 . VAL   B 1 35  ? 48.436 -17.566 -5.340  1.00 15.59 ?  35  VAL   B HG13 1 
ATOM   4418 H  HG21 . VAL   B 1 35  ? 48.819 -19.936 -6.990  1.00 15.24 ?  35  VAL   B HG21 1 
ATOM   4419 H  HG22 . VAL   B 1 35  ? 47.588 -19.850 -5.990  1.00 15.24 ?  35  VAL   B HG22 1 
ATOM   4420 H  HG23 . VAL   B 1 35  ? 47.343 -20.173 -7.527  1.00 15.24 ?  35  VAL   B HG23 1 
ATOM   4421 N  N    . VAL   B 1 36  ? 45.018 -18.859 -5.379  1.00 10.77 ?  36  VAL   B N    1 
ATOM   4422 C  CA   . VAL   B 1 36  ? 44.471 -19.059 -4.047  1.00 10.58 ?  36  VAL   B CA   1 
ATOM   4423 C  C    . VAL   B 1 36  ? 45.478 -19.817 -3.191  1.00 9.86  ?  36  VAL   B C    1 
ATOM   4424 O  O    . VAL   B 1 36  ? 46.021 -20.852 -3.607  1.00 11.43 ?  36  VAL   B O    1 
ATOM   4425 C  CB   . VAL   B 1 36  ? 43.131 -19.818 -4.126  1.00 11.06 ?  36  VAL   B CB   1 
ATOM   4426 C  CG1  . VAL   B 1 36  ? 42.629 -20.188 -2.730  1.00 11.56 ?  36  VAL   B CG1  1 
ATOM   4427 C  CG2  . VAL   B 1 36  ? 42.104 -18.992 -4.876  1.00 11.61 ?  36  VAL   B CG2  1 
ATOM   4428 H  H    . VAL   B 1 36  ? 44.855 -19.505 -5.922  1.00 12.89 ?  36  VAL   B H    1 
ATOM   4429 H  HA   . VAL   B 1 36  ? 44.304 -18.197 -3.634  1.00 12.65 ?  36  VAL   B HA   1 
ATOM   4430 H  HB   . VAL   B 1 36  ? 43.266 -20.639 -4.618  1.00 13.24 ?  36  VAL   B HB   1 
ATOM   4431 H  HG11 . VAL   B 1 36  ? 41.692 -20.421 -2.782  1.00 13.84 ?  36  VAL   B HG11 1 
ATOM   4432 H  HG12 . VAL   B 1 36  ? 43.142 -20.939 -2.396  1.00 13.84 ?  36  VAL   B HG12 1 
ATOM   4433 H  HG13 . VAL   B 1 36  ? 42.745 -19.420 -2.141  1.00 13.84 ?  36  VAL   B HG13 1 
ATOM   4434 H  HG21 . VAL   B 1 36  ? 41.264 -19.476 -4.898  1.00 13.89 ?  36  VAL   B HG21 1 
ATOM   4435 H  HG22 . VAL   B 1 36  ? 41.987 -18.143 -4.425  1.00 13.89 ?  36  VAL   B HG22 1 
ATOM   4436 H  HG23 . VAL   B 1 36  ? 42.421 -18.843 -5.784  1.00 13.89 ?  36  VAL   B HG23 1 
ATOM   4437 N  N    . ASN   B 1 37  ? 45.695 -19.325 -1.976  1.00 10.31 ?  37  ASN   B N    1 
ATOM   4438 C  CA   . ASN   B 1 37  ? 46.441 -20.051 -0.963  1.00 10.76 ?  37  ASN   B CA   1 
ATOM   4439 C  C    . ASN   B 1 37  ? 45.492 -20.719 0.024   1.00 11.22 ?  37  ASN   B C    1 
ATOM   4440 O  O    . ASN   B 1 37  ? 44.486 -20.136 0.438   1.00 11.60 ?  37  ASN   B O    1 
ATOM   4441 C  CB   . ASN   B 1 37  ? 47.370 -19.111 -0.203  1.00 10.70 ?  37  ASN   B CB   1 
ATOM   4442 C  CG   . ASN   B 1 37  ? 48.215 -19.831 0.812   1.00 11.13 ?  37  ASN   B CG   1 
ATOM   4443 O  OD1  . ASN   B 1 37  ? 48.555 -21.005 0.638   1.00 12.18 ?  37  ASN   B OD1  1 
ATOM   4444 N  ND2  . ASN   B 1 37  ? 48.566 -19.130 1.885   1.00 11.65 ?  37  ASN   B ND2  1 
ATOM   4445 H  H    . ASN   B 1 37  ? 45.409 -18.557 -1.706  1.00 12.34 ?  37  ASN   B H    1 
ATOM   4446 H  HA   . ASN   B 1 37  ? 46.974 -20.739 -1.378  1.00 12.87 ?  37  ASN   B HA   1 
ATOM   4447 H  HB2  . ASN   B 1 37  ? 47.967 -18.682 -0.836  1.00 12.80 ?  37  ASN   B HB2  1 
ATOM   4448 H  HB3  . ASN   B 1 37  ? 46.844 -18.444 0.264   1.00 12.80 ?  37  ASN   B HB3  1 
ATOM   4449 H  HD21 . ASN   B 1 37  ? 49.064 -19.489 2.489   1.00 13.94 ?  37  ASN   B HD21 1 
ATOM   4450 H  HD22 . ASN   B 1 37  ? 48.324 -18.314 1.968   1.00 13.94 ?  37  ASN   B HD22 1 
ATOM   4451 N  N    . ALA   B 1 38  ? 45.841 -21.952 0.402   1.00 11.43 ?  38  ALA   B N    1 
ATOM   4452 C  CA   . ALA   B 1 38  ? 45.189 -22.696 1.481   1.00 12.00 ?  38  ALA   B CA   1 
ATOM   4453 C  C    . ALA   B 1 38  ? 45.777 -22.211 2.804   1.00 11.69 ?  38  ALA   B C    1 
ATOM   4454 O  O    . ALA   B 1 38  ? 46.674 -22.828 3.394   1.00 12.47 ?  38  ALA   B O    1 
ATOM   4455 C  CB   . ALA   B 1 38  ? 45.415 -24.190 1.299   1.00 13.09 ?  38  ALA   B CB   1 
ATOM   4456 H  H    . ALA   B 1 38  ? 46.498 -22.386 0.054   1.00 13.67 ?  38  ALA   B H    1 
ATOM   4457 H  HA   . ALA   B 1 38  ? 44.240 -22.515 1.482   1.00 14.36 ?  38  ALA   B HA   1 
ATOM   4458 H  HB1  . ALA   B 1 38  ? 44.968 -24.667 2.027   1.00 15.68 ?  38  ALA   B HB1  1 
ATOM   4459 H  HB2  . ALA   B 1 38  ? 45.035 -24.463 0.453   1.00 15.68 ?  38  ALA   B HB2  1 
ATOM   4460 H  HB3  . ALA   B 1 38  ? 46.362 -24.378 1.322   1.00 15.68 ?  38  ALA   B HB3  1 
ATOM   4461 N  N    . ALA   B 1 39  ? 45.268 -21.065 3.259   1.00 11.40 ?  39  ALA   B N    1 
ATOM   4462 C  CA   . ALA   B 1 39  ? 45.814 -20.330 4.388   1.00 11.61 ?  39  ALA   B CA   1 
ATOM   4463 C  C    . ALA   B 1 39  ? 45.197 -20.780 5.711   1.00 11.62 ?  39  ALA   B C    1 
ATOM   4464 O  O    . ALA   B 1 39  ? 44.161 -21.446 5.758   1.00 12.83 ?  39  ALA   B O    1 
ATOM   4465 C  CB   . ALA   B 1 39  ? 45.572 -18.832 4.194   1.00 11.83 ?  39  ALA   B CB   1 
ATOM   4466 H  H    . ALA   B 1 39  ? 44.581 -20.684 2.917   1.00 13.64 ?  39  ALA   B H    1 
ATOM   4467 H  HA   . ALA   B 1 39  ? 46.774 -20.475 4.437   1.00 13.90 ?  39  ALA   B HA   1 
ATOM   4468 H  HB1  . ALA   B 1 39  ? 45.941 -18.347 4.949   1.00 14.16 ?  39  ALA   B HB1  1 
ATOM   4469 H  HB2  . ALA   B 1 39  ? 46.006 -18.545 3.374   1.00 14.16 ?  39  ALA   B HB2  1 
ATOM   4470 H  HB3  . ALA   B 1 39  ? 44.617 -18.672 4.134   1.00 14.16 ?  39  ALA   B HB3  1 
ATOM   4471 N  N    . ASN   B 1 40  ? 45.841 -20.371 6.800   1.00 12.23 ?  40  ASN   B N    1 
ATOM   4472 C  CA   . ASN   B 1 40  ? 45.280 -20.417 8.140   1.00 13.00 ?  40  ASN   B CA   1 
ATOM   4473 C  C    . ASN   B 1 40  ? 45.083 -18.987 8.655   1.00 12.62 ?  40  ASN   B C    1 
ATOM   4474 O  O    . ASN   B 1 40  ? 45.496 -18.008 8.026   1.00 12.55 ?  40  ASN   B O    1 
ATOM   4475 C  CB   . ASN   B 1 40  ? 46.141 -21.282 9.078   1.00 13.83 ?  40  ASN   B CB   1 
ATOM   4476 C  CG   . ASN   B 1 40  ? 47.592 -20.865 9.096   1.00 14.85 ?  40  ASN   B CG   1 
ATOM   4477 O  OD1  . ASN   B 1 40  ? 47.901 -19.681 9.175   1.00 16.86 ?  40  ASN   B OD1  1 
ATOM   4478 N  ND2  . ASN   B 1 40  ? 48.491 -21.832 9.031   1.00 14.97 ?  40  ASN   B ND2  1 
ATOM   4479 H  H    . ASN   B 1 40  ? 46.639 -20.045 6.780   1.00 14.64 ?  40  ASN   B H    1 
ATOM   4480 H  HA   . ASN   B 1 40  ? 44.402 -20.821 8.093   1.00 15.57 ?  40  ASN   B HA   1 
ATOM   4481 H  HB2  . ASN   B 1 40  ? 45.793 -21.207 9.979   1.00 16.56 ?  40  ASN   B HB2  1 
ATOM   4482 H  HB3  . ASN   B 1 40  ? 46.094 -22.203 8.779   1.00 16.56 ?  40  ASN   B HB3  1 
ATOM   4483 H  HD21 . ASN   B 1 40  ? 49.329 -21.646 9.037   1.00 17.92 ?  40  ASN   B HD21 1 
ATOM   4484 H  HD22 . ASN   B 1 40  ? 48.234 -22.653 8.972   1.00 17.92 ?  40  ASN   B HD22 1 
ATOM   4485 N  N    . VAL   B 1 41  ? 44.434 -18.861 9.814   1.00 13.28 ?  41  VAL   B N    1 
ATOM   4486 C  CA   . VAL   B 1 41  ? 43.968 -17.543 10.261  1.00 13.82 ?  41  VAL   B CA   1 
ATOM   4487 C  C    . VAL   B 1 41  ? 45.113 -16.577 10.538  1.00 13.32 ?  41  VAL   B C    1 
ATOM   4488 O  O    . VAL   B 1 41  ? 44.927 -15.357 10.448  1.00 13.82 ?  41  VAL   B O    1 
ATOM   4489 C  CB   . VAL   B 1 41  ? 43.018 -17.632 11.474  1.00 15.50 ?  41  VAL   B CB   1 
ATOM   4490 C  CG1  . VAL   B 1 41  ? 41.696 -18.283 11.089  1.00 15.86 ?  41  VAL   B CG1  1 
ATOM   4491 C  CG2  . VAL   B 1 41  ? 43.692 -18.345 12.646  1.00 16.84 ?  41  VAL   B CG2  1 
ATOM   4492 H  H    . VAL   B 1 41  ? 44.254 -19.504 10.346  1.00 15.90 ?  41  VAL   B H    1 
ATOM   4493 H  HA   . VAL   B 1 41  ? 43.449 -17.156 9.543   1.00 16.54 ?  41  VAL   B HA   1 
ATOM   4494 H  HB   . VAL   B 1 41  ? 42.814 -16.732 11.773  1.00 18.56 ?  41  VAL   B HB   1 
ATOM   4495 H  HG11 . VAL   B 1 41  ? 41.108 -18.294 11.863  1.00 19.00 ?  41  VAL   B HG11 1 
ATOM   4496 H  HG12 . VAL   B 1 41  ? 41.289 -17.771 10.374  1.00 19.00 ?  41  VAL   B HG12 1 
ATOM   4497 H  HG13 . VAL   B 1 41  ? 41.865 -19.191 10.792  1.00 19.00 ?  41  VAL   B HG13 1 
ATOM   4498 H  HG21 . VAL   B 1 41  ? 43.087 -18.355 13.405  1.00 20.18 ?  41  VAL   B HG21 1 
ATOM   4499 H  HG22 . VAL   B 1 41  ? 43.903 -19.258 12.386  1.00 20.18 ?  41  VAL   B HG22 1 
ATOM   4500 H  HG23 . VAL   B 1 41  ? 44.506 -17.874 12.881  1.00 20.18 ?  41  VAL   B HG23 1 
ATOM   4501 N  N    . TYR   B 1 42  ? 46.288 -17.085 10.911  1.00 13.73 ?  42  TYR   B N    1 
ATOM   4502 C  CA   . TYR   B 1 42  ? 47.439 -16.238 11.190  1.00 13.75 ?  42  TYR   B CA   1 
ATOM   4503 C  C    . TYR   B 1 42  ? 48.412 -16.170 10.018  1.00 13.17 ?  42  TYR   B C    1 
ATOM   4504 O  O    . TYR   B 1 42  ? 49.501 -15.602 10.160  1.00 14.52 ?  42  TYR   B O    1 
ATOM   4505 C  CB   . TYR   B 1 42  ? 48.121 -16.653 12.500  1.00 15.54 ?  42  TYR   B CB   1 
ATOM   4506 C  CG   . TYR   B 1 42  ? 47.549 -15.930 13.718  1.00 15.73 ?  42  TYR   B CG   1 
ATOM   4507 C  CD1  . TYR   B 1 42  ? 47.783 -14.575 13.905  1.00 14.78 ?  42  TYR   B CD1  1 
ATOM   4508 C  CD2  . TYR   B 1 42  ? 46.773 -16.593 14.666  1.00 16.71 ?  42  TYR   B CD2  1 
ATOM   4509 C  CE1  . TYR   B 1 42  ? 47.272 -13.898 14.989  1.00 15.40 ?  42  TYR   B CE1  1 
ATOM   4510 C  CE2  . TYR   B 1 42  ? 46.255 -15.915 15.770  1.00 16.92 ?  42  TYR   B CE2  1 
ATOM   4511 C  CZ   . TYR   B 1 42  ? 46.514 -14.560 15.923  1.00 16.85 ?  42  TYR   B CZ   1 
ATOM   4512 O  OH   . TYR   B 1 42  ? 46.034 -13.844 17.004  1.00 19.03 ?  42  TYR   B OH   1 
ATOM   4513 H  H    . TYR   B 1 42  ? 46.443 -17.929 10.998  1.00 16.44 ?  42  TYR   B H    1 
ATOM   4514 H  HA   . TYR   B 1 42  ? 47.110 -15.337 11.323  1.00 16.46 ?  42  TYR   B HA   1 
ATOM   4515 H  HB2  . TYR   B 1 42  ? 47.998 -17.607 12.630  1.00 18.61 ?  42  TYR   B HB2  1 
ATOM   4516 H  HB3  . TYR   B 1 42  ? 49.067 -16.446 12.440  1.00 18.61 ?  42  TYR   B HB3  1 
ATOM   4517 H  HD1  . TYR   B 1 42  ? 48.300 -14.112 13.277  1.00 17.69 ?  42  TYR   B HD1  1 
ATOM   4518 H  HD2  . TYR   B 1 42  ? 46.600 -17.505 14.556  1.00 20.01 ?  42  TYR   B HD2  1 
ATOM   4519 H  HE1  . TYR   B 1 42  ? 47.451 -12.993 15.091  1.00 18.44 ?  42  TYR   B HE1  1 
ATOM   4520 H  HE2  . TYR   B 1 42  ? 45.740 -16.374 16.394  1.00 20.26 ?  42  TYR   B HE2  1 
ATOM   4521 H  HH   . TYR   B 1 42  ? 46.277 -13.046 16.938  1.00 22.80 ?  42  TYR   B HH   1 
ATOM   4522 N  N    . LEU   B 1 43  ? 48.019 -16.680 8.852   1.00 12.33 ?  43  LEU   B N    1 
ATOM   4523 C  CA   . LEU   B 1 43  ? 48.833 -16.619 7.640   1.00 12.19 ?  43  LEU   B CA   1 
ATOM   4524 C  C    . LEU   B 1 43  ? 50.247 -17.127 7.898   1.00 12.70 ?  43  LEU   B C    1 
ATOM   4525 O  O    . LEU   B 1 43  ? 51.229 -16.526 7.458   1.00 13.54 ?  43  LEU   B O    1 
ATOM   4526 C  CB   . LEU   B 1 43  ? 48.853 -15.218 7.021   1.00 12.33 ?  43  LEU   B CB   1 
ATOM   4527 C  CG   . LEU   B 1 43  ? 47.494 -14.601 6.665   1.00 12.93 ?  43  LEU   B CG   1 
ATOM   4528 C  CD1  . LEU   B 1 43  ? 47.692 -13.210 6.072   1.00 14.23 ?  43  LEU   B CD1  1 
ATOM   4529 C  CD2  . LEU   B 1 43  ? 46.723 -15.498 5.709   1.00 12.94 ?  43  LEU   B CD2  1 
ATOM   4530 H  H    . LEU   B 1 43  ? 47.269 -17.085 8.735   1.00 14.76 ?  43  LEU   B H    1 
ATOM   4531 H  HA   . LEU   B 1 43  ? 48.437 -17.213 6.983   1.00 14.60 ?  43  LEU   B HA   1 
ATOM   4532 H  HB2  . LEU   B 1 43  ? 49.290 -14.619 7.640   1.00 14.76 ?  43  LEU   B HB2  1 
ATOM   4533 H  HB3  . LEU   B 1 43  ? 49.370 -15.263 6.197   1.00 14.76 ?  43  LEU   B HB3  1 
ATOM   4534 H  HG   . LEU   B 1 43  ? 46.972 -14.508 7.474   1.00 15.48 ?  43  LEU   B HG   1 
ATOM   4535 H  HD11 . LEU   B 1 43  ? 46.823 -12.834 5.855   1.00 17.03 ?  43  LEU   B HD11 1 
ATOM   4536 H  HD12 . LEU   B 1 43  ? 48.140 -12.650 6.725   1.00 17.03 ?  43  LEU   B HD12 1 
ATOM   4537 H  HD13 . LEU   B 1 43  ? 48.231 -13.280 5.270   1.00 17.03 ?  43  LEU   B HD13 1 
ATOM   4538 H  HD21 . LEU   B 1 43  ? 45.920 -15.035 5.419   1.00 15.49 ?  43  LEU   B HD21 1 
ATOM   4539 H  HD22 . LEU   B 1 43  ? 47.280 -15.706 4.945   1.00 15.49 ?  43  LEU   B HD22 1 
ATOM   4540 H  HD23 . LEU   B 1 43  ? 46.479 -16.318 6.173   1.00 15.49 ?  43  LEU   B HD23 1 
ATOM   4541 N  N    . LYS   B 1 44  ? 50.347 -18.250 8.612   1.00 12.57 ?  44  LYS   B N    1 
ATOM   4542 C  CA   . LYS   B 1 44  ? 51.614 -18.923 8.867   1.00 13.46 ?  44  LYS   B CA   1 
ATOM   4543 C  C    . LYS   B 1 44  ? 51.731 -20.039 7.841   1.00 13.28 ?  44  LYS   B C    1 
ATOM   4544 O  O    . LYS   B 1 44  ? 51.046 -21.060 7.931   1.00 14.29 ?  44  LYS   B O    1 
ATOM   4545 C  CB   . LYS   B 1 44  ? 51.649 -19.433 10.303  1.00 15.31 ?  44  LYS   B CB   1 
ATOM   4546 C  CG   . LYS   B 1 44  ? 51.899 -18.325 11.314  1.00 18.57 ?  44  LYS   B CG   1 
ATOM   4547 C  CD   . LYS   B 1 44  ? 53.096 -17.481 10.857  1.00 22.39 ?  44  LYS   B CD   1 
ATOM   4548 C  CE   . LYS   B 1 44  ? 53.656 -16.599 11.941  1.00 25.46 ?  44  LYS   B CE   1 
ATOM   4549 N  NZ   . LYS   B 1 44  ? 54.807 -15.783 11.479  1.00 26.30 ?  44  LYS   B NZ   1 
ATOM   4550 H  H    . LYS   B 1 44  ? 49.673 -18.637 8.982   1.00 15.04 ?  44  LYS   B H    1 
ATOM   4551 H  HA   . LYS   B 1 44  ? 52.347 -18.317 8.699   1.00 16.11 ?  44  LYS   B HA   1 
ATOM   4552 H  HB2  . LYS   B 1 44  ? 50.788 -19.842 10.517  1.00 18.34 ?  44  LYS   B HB2  1 
ATOM   4553 H  HB3  . LYS   B 1 44  ? 52.354 -20.092 10.394  1.00 18.34 ?  44  LYS   B HB3  1 
ATOM   4554 H  HG2  . LYS   B 1 44  ? 51.119 -17.758 11.378  1.00 22.25 ?  44  LYS   B HG2  1 
ATOM   4555 H  HG3  . LYS   B 1 44  ? 52.110 -18.719 12.180  1.00 22.25 ?  44  LYS   B HG3  1 
ATOM   4556 H  HD2  . LYS   B 1 44  ? 53.798 -18.081 10.536  1.00 26.83 ?  44  LYS   B HD2  1 
ATOM   4557 H  HD3  . LYS   B 1 44  ? 52.807 -16.901 10.134  1.00 26.83 ?  44  LYS   B HD3  1 
ATOM   4558 H  HE2  . LYS   B 1 44  ? 52.964 -15.989 12.218  1.00 30.51 ?  44  LYS   B HE2  1 
ATOM   4559 H  HE3  . LYS   B 1 44  ? 53.948 -17.153 12.679  1.00 30.51 ?  44  LYS   B HE3  1 
ATOM   4560 H  HZ1  . LYS   B 1 44  ? 55.092 -15.265 12.143  1.00 31.52 ?  44  LYS   B HZ1  1 
ATOM   4561 H  HZ2  . LYS   B 1 44  ? 55.472 -16.310 11.215  1.00 31.52 ?  44  LYS   B HZ2  1 
ATOM   4562 H  HZ3  . LYS   B 1 44  ? 54.559 -15.266 10.796  1.00 31.52 ?  44  LYS   B HZ3  1 
ATOM   4563 N  N    . HIS   B 1 45  ? 52.574 -19.816 6.837   1.00 12.93 ?  45  HIS   B N    1 
ATOM   4564 C  CA   . HIS   B 1 45  ? 52.607 -20.652 5.637   1.00 13.29 ?  45  HIS   B CA   1 
ATOM   4565 C  C    . HIS   B 1 45  ? 53.630 -21.770 5.807   1.00 15.37 ?  45  HIS   B C    1 
ATOM   4566 O  O    . HIS   B 1 45  ? 54.702 -21.776 5.210   1.00 17.87 ?  45  HIS   B O    1 
ATOM   4567 C  CB   . HIS   B 1 45  ? 52.920 -19.800 4.419   1.00 12.85 ?  45  HIS   B CB   1 
ATOM   4568 C  CG   . HIS   B 1 45  ? 52.051 -18.599 4.311   1.00 12.89 ?  45  HIS   B CG   1 
ATOM   4569 N  ND1  . HIS   B 1 45  ? 50.674 -18.680 4.280   1.00 12.86 ?  45  HIS   B ND1  1 
ATOM   4570 C  CD2  . HIS   B 1 45  ? 52.364 -17.286 4.234   1.00 13.06 ?  45  HIS   B CD2  1 
ATOM   4571 C  CE1  . HIS   B 1 45  ? 50.182 -17.459 4.180   1.00 12.28 ?  45  HIS   B CE1  1 
ATOM   4572 N  NE2  . HIS   B 1 45  ? 51.183 -16.596 4.151   1.00 12.91 ?  45  HIS   B NE2  1 
ATOM   4573 H  H    . HIS   B 1 45  ? 53.138 -19.166 6.820   1.00 15.48 ?  45  HIS   B H    1 
ATOM   4574 H  HA   . HIS   B 1 45  ? 51.732 -21.055 5.503   1.00 15.91 ?  45  HIS   B HA   1 
ATOM   4575 H  HB2  . HIS   B 1 45  ? 53.841 -19.505 4.468   1.00 15.38 ?  45  HIS   B HB2  1 
ATOM   4576 H  HB3  . HIS   B 1 45  ? 52.792 -20.340 3.616   1.00 15.38 ?  45  HIS   B HB3  1 
ATOM   4577 H  HD2  . HIS   B 1 45  ? 53.220 -16.920 4.236   1.00 15.63 ?  45  HIS   B HD2  1 
ATOM   4578 H  HE1  . HIS   B 1 45  ? 49.279 -17.240 4.135   1.00 14.69 ?  45  HIS   B HE1  1 
ATOM   4579 H  HE2  . HIS   B 1 45  ? 51.106 -15.741 4.096   1.00 15.45 ?  45  HIS   B HE2  1 
ATOM   4580 N  N    A GLY   B 1 46  ? 53.252 -22.750 6.620   0.70 16.06 ?  46  GLY   B N    1 
ATOM   4581 N  N    B GLY   B 1 46  ? 53.262 -22.736 6.640   0.30 16.08 ?  46  GLY   B N    1 
ATOM   4582 C  CA   A GLY   B 1 46  ? 54.172 -23.805 7.008   0.70 17.82 ?  46  GLY   B CA   1 
ATOM   4583 C  CA   B GLY   B 1 46  ? 54.174 -23.804 6.991   0.30 17.17 ?  46  GLY   B CA   1 
ATOM   4584 C  C    A GLY   B 1 46  ? 54.214 -25.030 6.115   0.70 19.24 ?  46  GLY   B C    1 
ATOM   4585 C  C    B GLY   B 1 46  ? 54.201 -24.961 6.012   0.30 18.28 ?  46  GLY   B C    1 
ATOM   4586 O  O    A GLY   B 1 46  ? 55.294 -25.469 5.709   0.70 21.75 ?  46  GLY   B O    1 
ATOM   4587 O  O    B GLY   B 1 46  ? 55.244 -25.261 5.421   0.30 19.21 ?  46  GLY   B O    1 
ATOM   4588 H  H    A GLY   B 1 46  ? 52.469 -22.812 6.975   0.70 19.24 ?  46  GLY   B H    1 
ATOM   4589 H  H    B GLY   B 1 46  ? 52.488 -22.784 7.019   0.30 19.26 ?  46  GLY   B H    1 
ATOM   4590 H  HA2  A GLY   B 1 46  ? 55.066 -23.434 7.048   0.70 21.35 ?  46  GLY   B HA2  1 
ATOM   4591 H  HA2  B GLY   B 1 46  ? 55.070 -23.440 7.054   0.30 20.57 ?  46  GLY   B HA2  1 
ATOM   4592 H  HA3  A GLY   B 1 46  ? 53.935 -24.105 7.900   0.70 21.35 ?  46  GLY   B HA3  1 
ATOM   4593 H  HA3  B GLY   B 1 46  ? 53.927 -24.147 7.865   0.30 20.57 ?  46  GLY   B HA3  1 
ATOM   4594 N  N    . GLY   B 1 47  ? 53.057 -25.614 5.816   1.00 18.93 ?  47  GLY   B N    1 
ATOM   4595 C  CA   . GLY   B 1 47  ? 53.000 -26.884 5.121   1.00 16.94 ?  47  GLY   B CA   1 
ATOM   4596 C  C    . GLY   B 1 47  ? 52.088 -26.864 3.909   1.00 15.28 ?  47  GLY   B C    1 
ATOM   4597 O  O    . GLY   B 1 47  ? 51.441 -25.861 3.611   1.00 15.35 ?  47  GLY   B O    1 
ATOM   4598 H  H    A GLY   B 1 47  ? 52.283 -25.297 6.027   0.70 22.68 ?  47  GLY   B H    1 
ATOM   4599 H  H    B GLY   B 1 47  ? 52.287 -25.333 6.087   0.30 22.68 ?  47  GLY   B H    1 
ATOM   4600 H  HA2  . GLY   B 1 47  ? 53.887 -27.135 4.823   1.00 20.29 ?  47  GLY   B HA2  1 
ATOM   4601 H  HA3  . GLY   B 1 47  ? 52.681 -27.567 5.733   1.00 20.29 ?  47  GLY   B HA3  1 
ATOM   4602 N  N    . GLY   B 1 48  ? 52.033 -28.008 3.227   1.00 14.27 ?  48  GLY   B N    1 
ATOM   4603 C  CA   . GLY   B 1 48  ? 51.100 -28.144 2.125   1.00 14.08 ?  48  GLY   B CA   1 
ATOM   4604 C  C    . GLY   B 1 48  ? 51.243 -27.036 1.104   1.00 13.54 ?  48  GLY   B C    1 
ATOM   4605 O  O    . GLY   B 1 48  ? 52.346 -26.570 0.799   1.00 13.71 ?  48  GLY   B O    1 
ATOM   4606 H  H    . GLY   B 1 48  ? 52.519 -28.692 3.378   1.00 17.09 ?  48  GLY   B H    1 
ATOM   4607 H  HA2  . GLY   B 1 48  ? 51.246 -28.996 1.683   1.00 16.86 ?  48  GLY   B HA2  1 
ATOM   4608 H  HA3  . GLY   B 1 48  ? 50.189 -28.129 2.462   1.00 16.86 ?  48  GLY   B HA3  1 
ATOM   4609 N  N    . VAL   B 1 49  ? 50.101 -26.607 0.564   1.00 13.01 ?  49  VAL   B N    1 
ATOM   4610 C  CA   . VAL   B 1 49  ? 50.099 -25.585 -0.478  1.00 12.85 ?  49  VAL   B CA   1 
ATOM   4611 C  C    . VAL   B 1 49  ? 50.760 -24.301 0.015   1.00 11.98 ?  49  VAL   B C    1 
ATOM   4612 O  O    . VAL   B 1 49  ? 51.556 -23.682 -0.702  1.00 12.81 ?  49  VAL   B O    1 
ATOM   4613 C  CB   . VAL   B 1 49  ? 48.658 -25.328 -0.970  1.00 14.11 ?  49  VAL   B CB   1 
ATOM   4614 C  CG1  . VAL   B 1 49  ? 48.589 -24.067 -1.831  1.00 14.52 ?  49  VAL   B CG1  1 
ATOM   4615 C  CG2  . VAL   B 1 49  ? 48.130 -26.529 -1.741  1.00 15.50 ?  49  VAL   B CG2  1 
ATOM   4616 H  H    . VAL   B 1 49  ? 49.314 -26.884 0.784   1.00 15.57 ?  49  VAL   B H    1 
ATOM   4617 H  HA   . VAL   B 1 49  ? 50.606 -25.906 -1.237  1.00 15.39 ?  49  VAL   B HA   1 
ATOM   4618 H  HB   . VAL   B 1 49  ? 48.079 -25.192 -0.205  1.00 16.89 ?  49  VAL   B HB   1 
ATOM   4619 H  HG11 . VAL   B 1 49  ? 47.763 -24.076 -2.343  1.00 17.39 ?  49  VAL   B HG11 1 
ATOM   4620 H  HG12 . VAL   B 1 49  ? 48.608 -23.285 -1.256  1.00 17.39 ?  49  VAL   B HG12 1 
ATOM   4621 H  HG13 . VAL   B 1 49  ? 49.347 -24.054 -2.436  1.00 17.39 ?  49  VAL   B HG13 1 
ATOM   4622 H  HG21 . VAL   B 1 49  ? 47.222 -26.343 -2.035  1.00 18.56 ?  49  VAL   B HG21 1 
ATOM   4623 H  HG22 . VAL   B 1 49  ? 48.699 -26.683 -2.512  1.00 18.56 ?  49  VAL   B HG22 1 
ATOM   4624 H  HG23 . VAL   B 1 49  ? 48.138 -27.303 -1.160  1.00 18.56 ?  49  VAL   B HG23 1 
ATOM   4625 N  N    . ALA   B 1 50  ? 50.418 -23.860 1.227   1.00 12.10 ?  50  ALA   B N    1 
ATOM   4626 C  CA   . ALA   B 1 50  ? 50.941 -22.582 1.704   1.00 11.62 ?  50  ALA   B CA   1 
ATOM   4627 C  C    . ALA   B 1 50  ? 52.458 -22.612 1.813   1.00 12.15 ?  50  ALA   B C    1 
ATOM   4628 O  O    . ALA   B 1 50  ? 53.138 -21.641 1.453   1.00 12.26 ?  50  ALA   B O    1 
ATOM   4629 C  CB   . ALA   B 1 50  ? 50.318 -22.226 3.051   1.00 11.96 ?  50  ALA   B CB   1 
ATOM   4630 H  H    . ALA   B 1 50  ? 49.890 -24.264 1.774   1.00 14.49 ?  50  ALA   B H    1 
ATOM   4631 H  HA   . ALA   B 1 50  ? 50.707 -21.886 1.073   1.00 13.91 ?  50  ALA   B HA   1 
ATOM   4632 H  HB1  . ALA   B 1 50  ? 50.681 -21.375 3.351   1.00 14.32 ?  50  ALA   B HB1  1 
ATOM   4633 H  HB2  . ALA   B 1 50  ? 49.357 -22.155 2.945   1.00 14.32 ?  50  ALA   B HB2  1 
ATOM   4634 H  HB3  . ALA   B 1 50  ? 50.532 -22.920 3.692   1.00 14.32 ?  50  ALA   B HB3  1 
ATOM   4635 N  N    . GLY   B 1 51  ? 53.007 -23.706 2.331   1.00 12.86 ?  51  GLY   B N    1 
ATOM   4636 C  CA   . GLY   B 1 51  ? 54.452 -23.808 2.408   1.00 13.30 ?  51  GLY   B CA   1 
ATOM   4637 C  C    . GLY   B 1 51  ? 55.099 -23.760 1.039   1.00 13.36 ?  51  GLY   B C    1 
ATOM   4638 O  O    . GLY   B 1 51  ? 56.138 -23.122 0.854   1.00 14.04 ?  51  GLY   B O    1 
ATOM   4639 H  H    . GLY   B 1 51  ? 52.579 -24.389 2.630   1.00 15.40 ?  51  GLY   B H    1 
ATOM   4640 H  HA2  . GLY   B 1 51  ? 54.802 -23.074 2.937   1.00 15.93 ?  51  GLY   B HA2  1 
ATOM   4641 H  HA3  . GLY   B 1 51  ? 54.700 -24.643 2.835   1.00 15.93 ?  51  GLY   B HA3  1 
ATOM   4642 N  N    . ALA   B 1 52  ? 54.490 -24.421 0.056   1.00 12.82 ?  52  ALA   B N    1 
ATOM   4643 C  CA   . ALA   B 1 52  ? 55.050 -24.435 -1.289  1.00 13.03 ?  52  ALA   B CA   1 
ATOM   4644 C  C    . ALA   B 1 52  ? 54.979 -23.057 -1.939  1.00 12.85 ?  52  ALA   B C    1 
ATOM   4645 O  O    . ALA   B 1 52  ? 55.954 -22.604 -2.558  1.00 13.36 ?  52  ALA   B O    1 
ATOM   4646 C  CB   . ALA   B 1 52  ? 54.339 -25.479 -2.142  1.00 13.70 ?  52  ALA   B CB   1 
ATOM   4647 H  H    . ALA   B 1 52  ? 53.751 -24.852 0.141   1.00 15.34 ?  52  ALA   B H    1 
ATOM   4648 H  HA   . ALA   B 1 52  ? 55.984 -24.682 -1.229  1.00 15.60 ?  52  ALA   B HA   1 
ATOM   4649 H  HB1  . ALA   B 1 52  ? 54.730 -25.474 -3.029  1.00 16.41 ?  52  ALA   B HB1  1 
ATOM   4650 H  HB2  . ALA   B 1 52  ? 54.459 -26.350 -1.731  1.00 16.41 ?  52  ALA   B HB2  1 
ATOM   4651 H  HB3  . ALA   B 1 52  ? 53.398 -25.259 -2.189  1.00 16.41 ?  52  ALA   B HB3  1 
ATOM   4652 N  N    . LEU   B 1 53  ? 53.831 -22.379 -1.831  1.00 12.21 ?  53  LEU   B N    1 
ATOM   4653 C  CA   . LEU   B 1 53  ? 53.726 -21.034 -2.396  1.00 12.30 ?  53  LEU   B CA   1 
ATOM   4654 C  C    . LEU   B 1 53  ? 54.736 -20.098 -1.745  1.00 12.13 ?  53  LEU   B C    1 
ATOM   4655 O  O    . LEU   B 1 53  ? 55.443 -19.347 -2.432  1.00 12.85 ?  53  LEU   B O    1 
ATOM   4656 C  CB   . LEU   B 1 53  ? 52.310 -20.485 -2.224  1.00 12.98 ?  53  LEU   B CB   1 
ATOM   4657 C  CG   . LEU   B 1 53  ? 51.170 -21.214 -2.940  1.00 13.05 ?  53  LEU   B CG   1 
ATOM   4658 C  CD1  . LEU   B 1 53  ? 49.835 -20.587 -2.597  1.00 14.40 ?  53  LEU   B CD1  1 
ATOM   4659 C  CD2  . LEU   B 1 53  ? 51.369 -21.231 -4.445  1.00 14.78 ?  53  LEU   B CD2  1 
ATOM   4660 H  H    . LEU   B 1 53  ? 53.119 -22.663 -1.446  1.00 14.61 ?  53  LEU   B H    1 
ATOM   4661 H  HA   . LEU   B 1 53  ? 53.927 -21.074 -3.348  1.00 14.72 ?  53  LEU   B HA   1 
ATOM   4662 H  HB2  . LEU   B 1 53  ? 52.102 -20.493 -1.279  1.00 15.53 ?  53  LEU   B HB2  1 
ATOM   4663 H  HB3  . LEU   B 1 53  ? 52.303 -19.571 -2.545  1.00 15.53 ?  53  LEU   B HB3  1 
ATOM   4664 H  HG   . LEU   B 1 53  ? 51.141 -22.132 -2.632  1.00 15.63 ?  53  LEU   B HG   1 
ATOM   4665 H  HD11 . LEU   B 1 53  ? 49.128 -21.071 -3.059  1.00 17.25 ?  53  LEU   B HD11 1 
ATOM   4666 H  HD12 . LEU   B 1 53  ? 49.693 -20.645 -1.636  1.00 17.25 ?  53  LEU   B HD12 1 
ATOM   4667 H  HD13 . LEU   B 1 53  ? 49.835 -19.660 -2.875  1.00 17.25 ?  53  LEU   B HD13 1 
ATOM   4668 H  HD21 . LEU   B 1 53  ? 50.642 -21.722 -4.858  1.00 17.70 ?  53  LEU   B HD21 1 
ATOM   4669 H  HD22 . LEU   B 1 53  ? 51.380 -20.319 -4.775  1.00 17.70 ?  53  LEU   B HD22 1 
ATOM   4670 H  HD23 . LEU   B 1 53  ? 52.214 -21.666 -4.646  1.00 17.70 ?  53  LEU   B HD23 1 
ATOM   4671 N  N    . ASN   B 1 54  ? 54.819 -20.125 -0.417  1.00 11.83 ?  54  ASN   B N    1 
ATOM   4672 C  CA   . ASN   B 1 54  ? 55.738 -19.215 0.255   1.00 12.29 ?  54  ASN   B CA   1 
ATOM   4673 C  C    . ASN   B 1 54  ? 57.182 -19.496 -0.141  1.00 13.00 ?  54  ASN   B C    1 
ATOM   4674 O  O    . ASN   B 1 54  ? 57.964 -18.565 -0.370  1.00 13.72 ?  54  ASN   B O    1 
ATOM   4675 C  CB   . ASN   B 1 54  ? 55.584 -19.294 1.765   1.00 13.25 ?  54  ASN   B CB   1 
ATOM   4676 C  CG   . ASN   B 1 54  ? 56.560 -18.375 2.473   1.00 13.51 ?  54  ASN   B CG   1 
ATOM   4677 O  OD1  . ASN   B 1 54  ? 56.570 -17.166 2.231   1.00 13.75 ?  54  ASN   B OD1  1 
ATOM   4678 N  ND2  . ASN   B 1 54  ? 57.403 -18.941 3.331   1.00 15.05 ?  54  ASN   B ND2  1 
ATOM   4679 H  H    . ASN   B 1 54  ? 54.371 -20.648 0.100   1.00 14.15 ?  54  ASN   B H    1 
ATOM   4680 H  HA   . ASN   B 1 54  ? 55.528 -18.310 -0.017  1.00 14.71 ?  54  ASN   B HA   1 
ATOM   4681 H  HB2  . ASN   B 1 54  ? 54.682 -19.021 2.012   1.00 15.86 ?  54  ASN   B HB2  1 
ATOM   4682 H  HB3  . ASN   B 1 54  ? 55.749 -20.200 2.064   1.00 15.86 ?  54  ASN   B HB3  1 
ATOM   4683 H  HD21 . ASN   B 1 54  ? 57.985 -18.460 3.751   1.00 18.02 ?  54  ASN   B HD21 1 
ATOM   4684 H  HD22 . ASN   B 1 54  ? 57.380 -19.791 3.468   1.00 18.02 ?  54  ASN   B HD22 1 
ATOM   4685 N  N    . LYS   B 1 55  ? 57.564 -20.773 -0.202  1.00 13.65 ?  55  LYS   B N    1 
ATOM   4686 C  CA   . LYS   B 1 55  ? 58.919 -21.121 -0.617  1.00 14.53 ?  55  LYS   B CA   1 
ATOM   4687 C  C    . LYS   B 1 55  ? 59.218 -20.584 -2.010  1.00 14.51 ?  55  LYS   B C    1 
ATOM   4688 O  O    . LYS   B 1 55  ? 60.319 -20.086 -2.264  1.00 15.25 ?  55  LYS   B O    1 
ATOM   4689 C  CB   . LYS   B 1 55  ? 59.102 -22.639 -0.566  1.00 16.77 ?  55  LYS   B CB   1 
ATOM   4690 C  CG   . LYS   B 1 55  ? 60.474 -23.111 -1.012  1.00 20.76 ?  55  LYS   B CG   1 
ATOM   4691 C  CD   . LYS   B 1 55  ? 60.637 -24.613 -0.846  1.00 24.41 ?  55  LYS   B CD   1 
ATOM   4692 C  CE   . LYS   B 1 55  ? 60.697 -25.019 0.626   1.00 27.22 ?  55  LYS   B CE   1 
ATOM   4693 N  NZ   . LYS   B 1 55  ? 61.022 -26.455 0.804   1.00 28.57 ?  55  LYS   B NZ   1 
ATOM   4694 H  H    . LYS   B 1 55  ? 57.060 -21.444 -0.015  1.00 16.34 ?  55  LYS   B H    1 
ATOM   4695 H  HA   . LYS   B 1 55  ? 59.551 -20.724 -0.001  1.00 17.40 ?  55  LYS   B HA   1 
ATOM   4696 H  HB2  . LYS   B 1 55  ? 58.966 -22.933 0.350   1.00 20.08 ?  55  LYS   B HB2  1 
ATOM   4697 H  HB3  . LYS   B 1 55  ? 58.442 -23.055 -1.142  1.00 20.08 ?  55  LYS   B HB3  1 
ATOM   4698 H  HG2  . LYS   B 1 55  ? 60.595 -22.897 -1.950  1.00 24.88 ?  55  LYS   B HG2  1 
ATOM   4699 H  HG3  . LYS   B 1 55  ? 61.151 -22.670 -0.477  1.00 24.88 ?  55  LYS   B HG3  1 
ATOM   4700 H  HD2  . LYS   B 1 55  ? 59.881 -25.067 -1.253  1.00 29.26 ?  55  LYS   B HD2  1 
ATOM   4701 H  HD3  . LYS   B 1 55  ? 61.464 -24.895 -1.269  1.00 29.26 ?  55  LYS   B HD3  1 
ATOM   4702 H  HE2  . LYS   B 1 55  ? 61.381 -24.488 1.068   1.00 32.63 ?  55  LYS   B HE2  1 
ATOM   4703 H  HE3  . LYS   B 1 55  ? 59.832 -24.847 1.034   1.00 32.63 ?  55  LYS   B HE3  1 
ATOM   4704 H  HZ1  . LYS   B 1 55  ? 61.032 -26.654 1.672   1.00 34.24 ?  55  LYS   B HZ1  1 
ATOM   4705 H  HZ2  . LYS   B 1 55  ? 60.408 -26.954 0.399   1.00 34.24 ?  55  LYS   B HZ2  1 
ATOM   4706 H  HZ3  . LYS   B 1 55  ? 61.819 -26.629 0.455   1.00 34.24 ?  55  LYS   B HZ3  1 
ATOM   4707 N  N    . ALA   B 1 56  ? 58.249 -20.666 -2.926  1.00 14.16 ?  56  ALA   B N    1 
ATOM   4708 C  CA   . ALA   B 1 56  ? 58.474 -20.171 -4.279  1.00 15.07 ?  56  ALA   B CA   1 
ATOM   4709 C  C    . ALA   B 1 56  ? 58.748 -18.674 -4.284  1.00 14.71 ?  56  ALA   B C    1 
ATOM   4710 O  O    . ALA   B 1 56  ? 59.487 -18.180 -5.146  1.00 15.60 ?  56  ALA   B O    1 
ATOM   4711 C  CB   . ALA   B 1 56  ? 57.273 -20.496 -5.168  1.00 16.33 ?  56  ALA   B CB   1 
ATOM   4712 H  H    . ALA   B 1 56  ? 57.463 -20.991 -2.786  1.00 16.96 ?  56  ALA   B H    1 
ATOM   4713 H  HA   . ALA   B 1 56  ? 59.248 -20.614 -4.651  1.00 18.05 ?  56  ALA   B HA   1 
ATOM   4714 H  HB1  . ALA   B 1 56  ? 57.444 -20.162 -6.064  1.00 19.56 ?  56  ALA   B HB1  1 
ATOM   4715 H  HB2  . ALA   B 1 56  ? 57.152 -21.459 -5.194  1.00 19.56 ?  56  ALA   B HB2  1 
ATOM   4716 H  HB3  . ALA   B 1 56  ? 56.482 -20.073 -4.803  1.00 19.56 ?  56  ALA   B HB3  1 
ATOM   4717 N  N    . THR   B 1 57  ? 58.173 -17.936 -3.331  1.00 14.14 ?  57  THR   B N    1 
ATOM   4718 C  CA   . THR   B 1 57  ? 58.416 -16.501 -3.218  1.00 14.35 ?  57  THR   B CA   1 
ATOM   4719 C  C    . THR   B 1 57  ? 59.665 -16.172 -2.407  1.00 15.00 ?  57  THR   B C    1 
ATOM   4720 O  O    . THR   B 1 57  ? 59.903 -14.996 -2.109  1.00 15.37 ?  57  THR   B O    1 
ATOM   4721 C  CB   . THR   B 1 57  ? 57.216 -15.767 -2.594  1.00 13.48 ?  57  THR   B CB   1 
ATOM   4722 O  OG1  . THR   B 1 57  ? 57.189 -15.975 -1.173  1.00 13.98 ?  57  THR   B OG1  1 
ATOM   4723 C  CG2  . THR   B 1 57  ? 55.892 -16.190 -3.236  1.00 13.37 ?  57  THR   B CG2  1 
ATOM   4724 H  H    . THR   B 1 57  ? 57.624 -18.244 -2.740  1.00 16.93 ?  57  THR   B H    1 
ATOM   4725 H  HA   . THR   B 1 57  ? 58.540 -16.143 -4.111  1.00 17.18 ?  57  THR   B HA   1 
ATOM   4726 H  HB   . THR   B 1 57  ? 57.320 -14.816 -2.767  1.00 16.14 ?  57  THR   B HB   1 
ATOM   4727 H  HG1  . THR   B 1 57  ? 57.115 -16.790 -1.008  1.00 16.74 ?  57  THR   B HG1  1 
ATOM   4728 H  HG21 . THR   B 1 57  ? 55.166 -15.649 -2.898  1.00 16.01 ?  57  THR   B HG21 1 
ATOM   4729 H  HG22 . THR   B 1 57  ? 55.941 -16.085 -4.203  1.00 16.01 ?  57  THR   B HG22 1 
ATOM   4730 H  HG23 . THR   B 1 57  ? 55.710 -17.123 -3.038  1.00 16.01 ?  57  THR   B HG23 1 
ATOM   4731 N  N    . ASN   B 1 58  ? 60.461 -17.174 -2.041  1.00 15.88 ?  58  ASN   B N    1 
ATOM   4732 C  CA   . ASN   B 1 58  ? 61.659 -16.960 -1.230  1.00 19.19 ?  58  ASN   B CA   1 
ATOM   4733 C  C    . ASN   B 1 58  ? 61.323 -16.240 0.077   1.00 16.71 ?  58  ASN   B C    1 
ATOM   4734 O  O    . ASN   B 1 58  ? 62.064 -15.365 0.539   1.00 17.37 ?  58  ASN   B O    1 
ATOM   4735 C  CB   . ASN   B 1 58  ? 62.754 -16.222 -2.007  1.00 27.84 ?  58  ASN   B CB   1 
ATOM   4736 C  CG   . ASN   B 1 58  ? 64.128 -16.404 -1.390  1.00 37.15 ?  58  ASN   B CG   1 
ATOM   4737 O  OD1  . ASN   B 1 58  ? 64.415 -17.435 -0.782  1.00 39.95 ?  58  ASN   B OD1  1 
ATOM   4738 N  ND2  . ASN   B 1 58  ? 64.983 -15.402 -1.541  1.00 43.66 ?  58  ASN   B ND2  1 
ATOM   4739 H  H    . ASN   B 1 58  ? 60.323 -18.001 -2.249  1.00 19.02 ?  58  ASN   B H    1 
ATOM   4740 H  HA   . ASN   B 1 58  ? 62.016 -17.836 -1.006  1.00 22.99 ?  58  ASN   B HA   1 
ATOM   4741 H  HB2  . ASN   B 1 58  ? 62.784 -16.562 -2.917  1.00 33.37 ?  58  ASN   B HB2  1 
ATOM   4742 H  HB3  . ASN   B 1 58  ? 62.552 -15.275 -2.013  1.00 33.37 ?  58  ASN   B HB3  1 
ATOM   4743 H  HD21 . ASN   B 1 58  ? 65.774 -15.459 -1.210  1.00 52.35 ?  58  ASN   B HD21 1 
ATOM   4744 H  HD22 . ASN   B 1 58  ? 64.744 -14.697 -1.970  1.00 52.35 ?  58  ASN   B HD22 1 
ATOM   4745 N  N    . ASN   B 1 59  ? 60.195 -16.620 0.682   1.00 15.49 ?  59  ASN   B N    1 
ATOM   4746 C  CA   . ASN   B 1 59  ? 59.718 -16.143 1.981   1.00 15.60 ?  59  ASN   B CA   1 
ATOM   4747 C  C    . ASN   B 1 59  ? 59.126 -14.738 1.921   1.00 14.52 ?  59  ASN   B C    1 
ATOM   4748 O  O    . ASN   B 1 59  ? 58.699 -14.229 2.965   1.00 14.80 ?  59  ASN   B O    1 
ATOM   4749 C  CB   . ASN   B 1 59  ? 60.792 -16.194 3.083   1.00 16.84 ?  59  ASN   B CB   1 
ATOM   4750 C  CG   . ASN   B 1 59  ? 60.206 -16.365 4.470   1.00 17.39 ?  59  ASN   B CG   1 
ATOM   4751 O  OD1  . ASN   B 1 59  ? 59.376 -17.247 4.710   1.00 17.70 ?  59  ASN   B OD1  1 
ATOM   4752 N  ND2  . ASN   B 1 59  ? 60.628 -15.515 5.392   1.00 18.07 ?  59  ASN   B ND2  1 
ATOM   4753 H  H    . ASN   B 1 59  ? 59.655 -17.204 0.338   1.00 18.55 ?  59  ASN   B H    1 
ATOM   4754 H  HA   . ASN   B 1 59  ? 59.005 -16.738 2.266   1.00 18.68 ?  59  ASN   B HA   1 
ATOM   4755 H  HB2  . ASN   B 1 59  ? 61.380 -16.945 2.925   1.00 20.17 ?  59  ASN   B HB2  1 
ATOM   4756 H  HB3  . ASN   B 1 59  ? 61.292 -15.366 3.078   1.00 20.17 ?  59  ASN   B HB3  1 
ATOM   4757 H  HD21 . ASN   B 1 59  ? 60.318 -15.565 6.194   1.00 21.64 ?  59  ASN   B HD21 1 
ATOM   4758 H  HD22 . ASN   B 1 59  ? 61.202 -14.910 5.189   1.00 21.64 ?  59  ASN   B HD22 1 
ATOM   4759 N  N    . ALA   B 1 60  ? 59.069 -14.097 0.748   1.00 14.25 ?  60  ALA   B N    1 
ATOM   4760 C  CA   . ALA   B 1 60  ? 58.467 -12.768 0.664   1.00 14.12 ?  60  ALA   B CA   1 
ATOM   4761 C  C    . ALA   B 1 60  ? 56.999 -12.797 1.071   1.00 13.43 ?  60  ALA   B C    1 
ATOM   4762 O  O    . ALA   B 1 60  ? 56.491 -11.842 1.677   1.00 14.45 ?  60  ALA   B O    1 
ATOM   4763 C  CB   . ALA   B 1 60  ? 58.615 -12.211 -0.752  1.00 14.97 ?  60  ALA   B CB   1 
ATOM   4764 H  H    . ALA   B 1 60  ? 59.378 -14.406 0.005   1.00 17.06 ?  60  ALA   B H    1 
ATOM   4765 H  HA   . ALA   B 1 60  ? 58.934 -12.174 1.269   1.00 16.90 ?  60  ALA   B HA   1 
ATOM   4766 H  HB1  . ALA   B 1 60  ? 58.210 -11.333 -0.787  1.00 17.93 ?  60  ALA   B HB1  1 
ATOM   4767 H  HB2  . ALA   B 1 60  ? 59.559 -12.151 -0.973  1.00 17.93 ?  60  ALA   B HB2  1 
ATOM   4768 H  HB3  . ALA   B 1 60  ? 58.169 -12.809 -1.375  1.00 17.93 ?  60  ALA   B HB3  1 
ATOM   4769 N  N    . MET   B 1 61  ? 56.292 -13.877 0.729   1.00 12.84 ?  61  MET   B N    1 
ATOM   4770 C  CA   . MET   B 1 61  ? 54.895 -13.994 1.117   1.00 12.41 ?  61  MET   B CA   1 
ATOM   4771 C  C    . MET   B 1 61  ? 54.752 -13.998 2.635   1.00 12.52 ?  61  MET   B C    1 
ATOM   4772 O  O    . MET   B 1 61  ? 53.848 -13.347 3.178   1.00 12.55 ?  61  MET   B O    1 
ATOM   4773 C  CB   . MET   B 1 61  ? 54.309 -15.259 0.482   1.00 12.60 ?  61  MET   B CB   1 
ATOM   4774 C  CG   . MET   B 1 61  ? 52.875 -15.566 0.898   1.00 12.86 ?  61  MET   B CG   1 
ATOM   4775 S  SD   . MET   B 1 61  ? 52.230 -17.066 0.151   1.00 13.00 ?  61  MET   B SD   1 
ATOM   4776 C  CE   . MET   B 1 61  ? 51.971 -16.517 -1.532  1.00 14.70 ?  61  MET   B CE   1 
ATOM   4777 H  H    . MET   B 1 61  ? 56.599 -14.549 0.273   1.00 15.37 ?  61  MET   B H    1 
ATOM   4778 H  HA   . MET   B 1 61  ? 54.411 -13.239 0.757   1.00 14.85 ?  61  MET   B HA   1 
ATOM   4779 H  HB2  . MET   B 1 61  ? 54.318 -15.154 -0.488  1.00 15.08 ?  61  MET   B HB2  1 
ATOM   4780 H  HB3  . MET   B 1 61  ? 54.858 -16.019 0.727   1.00 15.08 ?  61  MET   B HB3  1 
ATOM   4781 H  HG2  . MET   B 1 61  ? 52.843 -15.678 1.858   1.00 15.39 ?  61  MET   B HG2  1 
ATOM   4782 H  HG3  . MET   B 1 61  ? 52.306 -14.830 0.626   1.00 15.39 ?  61  MET   B HG3  1 
ATOM   4783 H  HE1  . MET   B 1 61  ? 51.598 -17.251 -2.047  1.00 17.60 ?  61  MET   B HE1  1 
ATOM   4784 H  HE2  . MET   B 1 61  ? 51.354 -15.770 -1.528  1.00 17.60 ?  61  MET   B HE2  1 
ATOM   4785 H  HE3  . MET   B 1 61  ? 52.820 -16.244 -1.914  1.00 17.60 ?  61  MET   B HE3  1 
ATOM   4786 N  N    . GLN   B 1 62  ? 55.628 -14.718 3.342   1.00 12.56 ?  62  GLN   B N    1 
ATOM   4787 C  CA   . GLN   B 1 62  ? 55.525 -14.765 4.797   1.00 12.65 ?  62  GLN   B CA   1 
ATOM   4788 C  C    . GLN   B 1 62  ? 55.803 -13.403 5.422   1.00 13.07 ?  62  GLN   B C    1 
ATOM   4789 O  O    . GLN   B 1 62  ? 55.120 -13.000 6.370   1.00 13.42 ?  62  GLN   B O    1 
ATOM   4790 C  CB   . GLN   B 1 62  ? 56.482 -15.810 5.371   1.00 13.17 ?  62  GLN   B CB   1 
ATOM   4791 C  CG   . GLN   B 1 62  ? 56.249 -16.064 6.848   1.00 13.62 ?  62  GLN   B CG   1 
ATOM   4792 C  CD   . GLN   B 1 62  ? 54.874 -16.668 7.092   1.00 13.36 ?  62  GLN   B CD   1 
ATOM   4793 O  OE1  . GLN   B 1 62  ? 54.624 -17.819 6.734   1.00 13.76 ?  62  GLN   B OE1  1 
ATOM   4794 N  NE2  . GLN   B 1 62  ? 53.957 -15.882 7.652   1.00 13.86 ?  62  GLN   B NE2  1 
ATOM   4795 H  H    . GLN   B 1 62  ? 56.274 -15.182 3.007   1.00 15.03 ?  62  GLN   B H    1 
ATOM   4796 H  HA   . GLN   B 1 62  ? 54.622 -15.024 5.036   1.00 15.14 ?  62  GLN   B HA   1 
ATOM   4797 H  HB2  . GLN   B 1 62  ? 56.362 -16.652 4.901   1.00 15.77 ?  62  GLN   B HB2  1 
ATOM   4798 H  HB3  . GLN   B 1 62  ? 57.398 -15.502 5.263   1.00 15.77 ?  62  GLN   B HB3  1 
ATOM   4799 H  HG2  . GLN   B 1 62  ? 56.917 -16.688 7.174   1.00 16.31 ?  62  GLN   B HG2  1 
ATOM   4800 H  HG3  . GLN   B 1 62  ? 56.303 -15.228 7.332   1.00 16.31 ?  62  GLN   B HG3  1 
ATOM   4801 H  HE21 . GLN   B 1 62  ? 54.158 -15.084 7.882   1.00 16.59 ?  62  GLN   B HE21 1 
ATOM   4802 H  HE22 . GLN   B 1 62  ? 53.165 -16.191 7.795   1.00 16.59 ?  62  GLN   B HE22 1 
ATOM   4803 N  N    . VAL   B 1 63  ? 56.814 -12.691 4.924   1.00 13.64 ?  63  VAL   B N    1 
ATOM   4804 C  CA   . VAL   B 1 63  ? 57.119 -11.371 5.471   1.00 14.43 ?  63  VAL   B CA   1 
ATOM   4805 C  C    . VAL   B 1 63  ? 55.926 -10.438 5.285   1.00 13.62 ?  63  VAL   B C    1 
ATOM   4806 O  O    . VAL   B 1 63  ? 55.515 -9.725  6.212   1.00 14.27 ?  63  VAL   B O    1 
ATOM   4807 C  CB   . VAL   B 1 63  ? 58.411 -10.817 4.845   1.00 15.43 ?  63  VAL   B CB   1 
ATOM   4808 C  CG1  . VAL   B 1 63  ? 58.642 -9.374  5.282   1.00 16.12 ?  63  VAL   B CG1  1 
ATOM   4809 C  CG2  . VAL   B 1 63  ? 59.594 -11.695 5.243   1.00 15.76 ?  63  VAL   B CG2  1 
ATOM   4810 H  H    . VAL   B 1 63  ? 57.325 -12.946 4.275   1.00 16.33 ?  63  VAL   B H    1 
ATOM   4811 H  HA   . VAL   B 1 63  ? 57.275 -11.465 6.421   1.00 17.28 ?  63  VAL   B HA   1 
ATOM   4812 H  HB   . VAL   B 1 63  ? 58.339 -10.839 3.877   1.00 18.48 ?  63  VAL   B HB   1 
ATOM   4813 H  HG11 . VAL   B 1 63  ? 59.558 -9.130  5.087   1.00 19.31 ?  63  VAL   B HG11 1 
ATOM   4814 H  HG12 . VAL   B 1 63  ? 58.032 -8.799  4.798   1.00 19.31 ?  63  VAL   B HG12 1 
ATOM   4815 H  HG13 . VAL   B 1 63  ? 58.478 -9.309  6.237   1.00 19.31 ?  63  VAL   B HG13 1 
ATOM   4816 H  HG21 . VAL   B 1 63  ? 60.408 -11.324 4.867   1.00 18.88 ?  63  VAL   B HG21 1 
ATOM   4817 H  HG22 . VAL   B 1 63  ? 59.660 -11.714 6.214   1.00 18.88 ?  63  VAL   B HG22 1 
ATOM   4818 H  HG23 . VAL   B 1 63  ? 59.454 -12.594 4.907   1.00 18.88 ?  63  VAL   B HG23 1 
ATOM   4819 N  N    . GLU   B 1 64  ? 55.350 -10.439 4.084   1.00 13.30 ?  64  GLU   B N    1 
ATOM   4820 C  CA   . GLU   B 1 64  ? 54.188 -9.598  3.808   1.00 13.02 ?  64  GLU   B CA   1 
ATOM   4821 C  C    . GLU   B 1 64  ? 53.003 -9.995  4.681   1.00 12.78 ?  64  GLU   B C    1 
ATOM   4822 O  O    . GLU   B 1 64  ? 52.251 -9.130  5.172   1.00 13.19 ?  64  GLU   B O    1 
ATOM   4823 C  CB   . GLU   B 1 64  ? 53.835 -9.735  2.328   1.00 13.11 ?  64  GLU   B CB   1 
ATOM   4824 C  CG   . GLU   B 1 64  ? 52.575 -8.995  1.890   1.00 13.39 ?  64  GLU   B CG   1 
ATOM   4825 C  CD   . GLU   B 1 64  ? 52.042 -9.487  0.547   1.00 14.33 ?  64  GLU   B CD   1 
ATOM   4826 O  OE1  . GLU   B 1 64  ? 52.226 -10.693 0.226   1.00 15.48 ?  64  GLU   B OE1  1 
ATOM   4827 O  OE2  . GLU   B 1 64  ? 51.417 -8.669  -0.175  1.00 15.26 -1 64  GLU   B OE2  1 
ATOM   4828 H  H    . GLU   B 1 64  ? 55.618 -10.909 3.409   1.00 15.92 ?  64  GLU   B H    1 
ATOM   4829 H  HA   . GLU   B 1 64  ? 54.405 -8.673  3.986   1.00 15.59 ?  64  GLU   B HA   1 
ATOM   4830 H  HB2  . GLU   B 1 64  ? 54.568 -9.379  1.795   1.00 15.69 ?  64  GLU   B HB2  1 
ATOM   4831 H  HB3  . GLU   B 1 64  ? 53.707 -10.670 2.119   1.00 15.69 ?  64  GLU   B HB3  1 
ATOM   4832 H  HG2  . GLU   B 1 64  ? 51.871 -9.122  2.551   1.00 16.03 ?  64  GLU   B HG2  1 
ATOM   4833 H  HG3  . GLU   B 1 64  ? 52.772 -8.048  1.804   1.00 16.03 ?  64  GLU   B HG3  1 
ATOM   4834 N  N    . SER   B 1 65  ? 52.832 -11.302 4.887   1.00 12.36 ?  65  SER   B N    1 
ATOM   4835 C  CA   . SER   B 1 65  ? 51.723 -11.812 5.682   1.00 12.09 ?  65  SER   B CA   1 
ATOM   4836 C  C    . SER   B 1 65  ? 51.850 -11.412 7.144   1.00 12.60 ?  65  SER   B C    1 
ATOM   4837 O  O    . SER   B 1 65  ? 50.851 -11.039 7.775   1.00 12.85 ?  65  SER   B O    1 
ATOM   4838 C  CB   . SER   B 1 65  ? 51.643 -13.335 5.551   1.00 12.46 ?  65  SER   B CB   1 
ATOM   4839 O  OG   . SER   B 1 65  ? 51.284 -13.735 4.239   1.00 12.87 ?  65  SER   B OG   1 
ATOM   4840 H  H    . SER   B 1 65  ? 53.354 -11.923 4.582   1.00 14.79 ?  65  SER   B H    1 
ATOM   4841 H  HA   . SER   B 1 65  ? 50.894 -11.439 5.342   1.00 14.47 ?  65  SER   B HA   1 
ATOM   4842 H  HB2  . SER   B 1 65  ? 52.506 -13.715 5.762   1.00 14.91 ?  65  SER   B HB2  1 
ATOM   4843 H  HB3  . SER   B 1 65  ? 50.974 -13.667 6.173   1.00 14.91 ?  65  SER   B HB3  1 
ATOM   4844 H  HG   . SER   B 1 65  ? 51.845 -13.446 3.682   1.00 15.41 ?  65  SER   B HG   1 
ATOM   4845 N  N    . ASP   B 1 66  ? 53.059 -11.496 7.712   1.00 12.76 ?  66  ASP   B N    1 
ATOM   4846 C  CA   . ASP   B 1 66  ? 53.238 -11.101 9.107   1.00 13.05 ?  66  ASP   B CA   1 
ATOM   4847 C  C    . ASP   B 1 66  ? 52.922 -9.620  9.301   1.00 13.48 ?  66  ASP   B C    1 
ATOM   4848 O  O    . ASP   B 1 66  ? 52.348 -9.225  10.323  1.00 13.93 ?  66  ASP   B O    1 
ATOM   4849 C  CB   . ASP   B 1 66  ? 54.666 -11.407 9.569   1.00 14.55 ?  66  ASP   B CB   1 
ATOM   4850 C  CG   . ASP   B 1 66  ? 54.936 -12.899 9.730   1.00 16.35 ?  66  ASP   B CG   1 
ATOM   4851 O  OD1  . ASP   B 1 66  ? 53.988 -13.715 9.633   1.00 17.04 ?  66  ASP   B OD1  1 
ATOM   4852 O  OD2  . ASP   B 1 66  ? 56.111 -13.262 9.971   1.00 19.03 -1 66  ASP   B OD2  1 
ATOM   4853 H  H    . ASP   B 1 66  ? 53.768 -11.790 7.328   1.00 15.27 ?  66  ASP   B H    1 
ATOM   4854 H  HA   . ASP   B 1 66  ? 52.633 -11.608 9.671   1.00 15.62 ?  66  ASP   B HA   1 
ATOM   4855 H  HB2  . ASP   B 1 66  ? 55.294 -11.055 8.919   1.00 17.42 ?  66  ASP   B HB2  1 
ATOM   4856 H  HB3  . ASP   B 1 66  ? 54.820 -10.987 10.435  1.00 17.42 ?  66  ASP   B HB3  1 
ATOM   4857 N  N    . ASP   B 1 67  ? 53.294 -8.781  8.332   1.00 13.12 ?  67  ASP   B N    1 
ATOM   4858 C  CA   . ASP   B 1 67  ? 52.948 -7.368  8.408   1.00 13.44 ?  67  ASP   B CA   1 
ATOM   4859 C  C    . ASP   B 1 67  ? 51.437 -7.161  8.322   1.00 13.80 ?  67  ASP   B C    1 
ATOM   4860 O  O    . ASP   B 1 67  ? 50.871 -6.352  9.070   1.00 14.32 ?  67  ASP   B O    1 
ATOM   4861 C  CB   . ASP   B 1 67  ? 53.668 -6.610  7.299   1.00 14.70 ?  67  ASP   B CB   1 
ATOM   4862 C  CG   . ASP   B 1 67  ? 53.238 -5.167  7.228   1.00 16.42 ?  67  ASP   B CG   1 
ATOM   4863 O  OD1  . ASP   B 1 67  ? 53.742 -4.328  8.016   1.00 17.76 ?  67  ASP   B OD1  1 
ATOM   4864 O  OD2  . ASP   B 1 67  ? 52.358 -4.890  6.399   1.00 17.57 -1 67  ASP   B OD2  1 
ATOM   4865 H  H    . ASP   B 1 67  ? 53.746 -9.008  7.635   1.00 15.70 ?  67  ASP   B H    1 
ATOM   4866 H  HA   . ASP   B 1 67  ? 53.251 -7.014  9.257   1.00 16.09 ?  67  ASP   B HA   1 
ATOM   4867 H  HB2  . ASP   B 1 67  ? 54.625 -6.637  7.462   1.00 17.60 ?  67  ASP   B HB2  1 
ATOM   4868 H  HB3  . ASP   B 1 67  ? 53.470 -7.033  6.444   1.00 17.60 ?  67  ASP   B HB3  1 
ATOM   4869 N  N    . TYR   B 1 68  ? 50.763 -7.895  7.431   1.00 13.61 ?  68  TYR   B N    1 
ATOM   4870 C  CA   . TYR   B 1 68  ? 49.305 -7.822  7.360   1.00 14.07 ?  68  TYR   B CA   1 
ATOM   4871 C  C    . TYR   B 1 68  ? 48.673 -8.166  8.706   1.00 13.51 ?  68  TYR   B C    1 
ATOM   4872 O  O    . TYR   B 1 68  ? 47.734 -7.493  9.155   1.00 14.18 ?  68  TYR   B O    1 
ATOM   4873 C  CB   . TYR   B 1 68  ? 48.775 -8.759  6.264   1.00 14.82 ?  68  TYR   B CB   1 
ATOM   4874 C  CG   . TYR   B 1 68  ? 47.268 -8.910  6.320   1.00 15.82 ?  68  TYR   B CG   1 
ATOM   4875 C  CD1  . TYR   B 1 68  ? 46.679 -9.868  7.137   1.00 16.42 ?  68  TYR   B CD1  1 
ATOM   4876 C  CD2  . TYR   B 1 68  ? 46.435 -8.075  5.590   1.00 16.72 ?  68  TYR   B CD2  1 
ATOM   4877 C  CE1  . TYR   B 1 68  ? 45.315 -9.992  7.224   1.00 17.33 ?  68  TYR   B CE1  1 
ATOM   4878 C  CE2  . TYR   B 1 68  ? 45.055 -8.204  5.665   1.00 17.52 ?  68  TYR   B CE2  1 
ATOM   4879 C  CZ   . TYR   B 1 68  ? 44.512 -9.161  6.486   1.00 17.55 ?  68  TYR   B CZ   1 
ATOM   4880 O  OH   . TYR   B 1 68  ? 43.142 -9.282  6.578   1.00 18.68 ?  68  TYR   B OH   1 
ATOM   4881 H  H    . TYR   B 1 68  ? 51.123 -8.446  6.869   1.00 16.30 ?  68  TYR   B H    1 
ATOM   4882 H  HA   . TYR   B 1 68  ? 49.051 -6.916  7.133   1.00 16.85 ?  68  TYR   B HA   1 
ATOM   4883 H  HB2  . TYR   B 1 68  ? 49.006 -8.391  5.397   1.00 17.75 ?  68  TYR   B HB2  1 
ATOM   4884 H  HB3  . TYR   B 1 68  ? 49.172 -9.634  6.374   1.00 17.75 ?  68  TYR   B HB3  1 
ATOM   4885 H  HD1  . TYR   B 1 68  ? 47.220 -10.437 7.638   1.00 19.67 ?  68  TYR   B HD1  1 
ATOM   4886 H  HD2  . TYR   B 1 68  ? 46.809 -7.419  5.049   1.00 20.02 ?  68  TYR   B HD2  1 
ATOM   4887 H  HE1  . TYR   B 1 68  ? 44.934 -10.652 7.763   1.00 20.76 ?  68  TYR   B HE1  1 
ATOM   4888 H  HE2  . TYR   B 1 68  ? 44.501 -7.637  5.175   1.00 20.99 ?  68  TYR   B HE2  1 
ATOM   4889 H  HH   . TYR   B 1 68  ? 42.755 -8.730  6.065   1.00 22.38 ?  68  TYR   B HH   1 
ATOM   4890 N  N    . ILE   B 1 69  ? 49.158 -9.230  9.352   1.00 13.47 ?  69  ILE   B N    1 
ATOM   4891 C  CA   . ILE   B 1 69  ? 48.609 -9.649  10.641  1.00 13.96 ?  69  ILE   B CA   1 
ATOM   4892 C  C    . ILE   B 1 69  ? 48.856 -8.593  11.713  1.00 13.74 ?  69  ILE   B C    1 
ATOM   4893 O  O    . ILE   B 1 69  ? 47.983 -8.315  12.543  1.00 13.89 ?  69  ILE   B O    1 
ATOM   4894 C  CB   . ILE   B 1 69  ? 49.191 -11.018 11.041  1.00 14.34 ?  69  ILE   B CB   1 
ATOM   4895 C  CG1  . ILE   B 1 69  ? 48.662 -12.134 10.130  1.00 14.58 ?  69  ILE   B CG1  1 
ATOM   4896 C  CG2  . ILE   B 1 69  ? 48.914 -11.316 12.505  1.00 15.39 ?  69  ILE   B CG2  1 
ATOM   4897 C  CD1  . ILE   B 1 69  ? 47.184 -12.443 10.300  1.00 15.39 ?  69  ILE   B CD1  1 
ATOM   4898 H  H    . ILE   B 1 69  ? 49.805 -9.720  9.067   1.00 16.12 ?  69  ILE   B H    1 
ATOM   4899 H  HA   . ILE   B 1 69  ? 47.654 -9.751  10.547  1.00 16.71 ?  69  ILE   B HA   1 
ATOM   4900 H  HB   . ILE   B 1 69  ? 50.157 -10.975 10.926  1.00 17.17 ?  69  ILE   B HB   1 
ATOM   4901 H  HG12 . ILE   B 1 69  ? 48.807 -11.871 9.206   1.00 17.46 ?  69  ILE   B HG12 1 
ATOM   4902 H  HG13 . ILE   B 1 69  ? 49.160 -12.945 10.318  1.00 17.46 ?  69  ILE   B HG13 1 
ATOM   4903 H  HG21 . ILE   B 1 69  ? 49.049 -12.266 12.661  1.00 18.43 ?  69  ILE   B HG21 1 
ATOM   4904 H  HG22 . ILE   B 1 69  ? 49.524 -10.805 13.058  1.00 18.43 ?  69  ILE   B HG22 1 
ATOM   4905 H  HG23 . ILE   B 1 69  ? 47.997 -11.078 12.707  1.00 18.43 ?  69  ILE   B HG23 1 
ATOM   4906 H  HD11 . ILE   B 1 69  ? 46.950 -13.166 9.700   1.00 18.43 ?  69  ILE   B HD11 1 
ATOM   4907 H  HD12 . ILE   B 1 69  ? 47.020 -12.707 11.218  1.00 18.43 ?  69  ILE   B HD12 1 
ATOM   4908 H  HD13 . ILE   B 1 69  ? 46.669 -11.653 10.083  1.00 18.43 ?  69  ILE   B HD13 1 
ATOM   4909 N  N    . ALA   B 1 70  ? 50.052 -8.002  11.731  1.00 13.72 ?  70  ALA   B N    1 
ATOM   4910 C  CA   . ALA   B 1 70  ? 50.332 -6.952  12.710  1.00 13.55 ?  70  ALA   B CA   1 
ATOM   4911 C  C    . ALA   B 1 70  ? 49.317 -5.823  12.603  1.00 14.30 ?  70  ALA   B C    1 
ATOM   4912 O  O    . ALA   B 1 70  ? 48.864 -5.282  13.617  1.00 14.90 ?  70  ALA   B O    1 
ATOM   4913 C  CB   . ALA   B 1 70  ? 51.750 -6.412  12.518  1.00 13.93 ?  70  ALA   B CB   1 
ATOM   4914 H  H    . ALA   B 1 70  ? 50.702 -8.186  11.203  1.00 16.43 ?  70  ALA   B H    1 
ATOM   4915 H  HA   . ALA   B 1 70  ? 50.278 -7.327  13.603  1.00 16.22 ?  70  ALA   B HA   1 
ATOM   4916 H  HB1  . ALA   B 1 70  ? 51.940 -5.759  13.212  1.00 16.68 ?  70  ALA   B HB1  1 
ATOM   4917 H  HB2  . ALA   B 1 70  ? 52.385 -7.144  12.576  1.00 16.68 ?  70  ALA   B HB2  1 
ATOM   4918 H  HB3  . ALA   B 1 70  ? 51.817 -5.991  11.644  1.00 16.68 ?  70  ALA   B HB3  1 
ATOM   4919 N  N    . THR   B 1 71  ? 48.944 -5.461  11.379  1.00 14.63 ?  71  THR   B N    1 
ATOM   4920 C  CA   . THR   B 1 71  ? 48.036 -4.338  11.169  1.00 15.55 ?  71  THR   B CA   1 
ATOM   4921 C  C    . THR   B 1 71  ? 46.570 -4.716  11.382  1.00 16.19 ?  71  THR   B C    1 
ATOM   4922 O  O    . THR   B 1 71  ? 45.785 -3.902  11.886  1.00 17.56 ?  71  THR   B O    1 
ATOM   4923 C  CB   . THR   B 1 71  ? 48.239 -3.785  9.757   1.00 17.32 ?  71  THR   B CB   1 
ATOM   4924 O  OG1  . THR   B 1 71  ? 49.560 -3.243  9.640   1.00 19.63 ?  71  THR   B OG1  1 
ATOM   4925 C  CG2  . THR   B 1 71  ? 47.211 -2.711  9.438   1.00 18.23 ?  71  THR   B CG2  1 
ATOM   4926 H  H    . THR   B 1 71  ? 49.201 -5.855  10.657  1.00 17.52 ?  71  THR   B H    1 
ATOM   4927 H  HA   . THR   B 1 71  ? 48.259 -3.637  11.800  1.00 18.63 ?  71  THR   B HA   1 
ATOM   4928 H  HB   . THR   B 1 71  ? 48.145 -4.500  9.112   1.00 20.75 ?  71  THR   B HB   1 
ATOM   4929 H  HG1  . THR   B 1 71  ? 49.679 -2.917  8.871   1.00 23.52 ?  71  THR   B HG1  1 
ATOM   4930 H  HG21 . THR   B 1 71  ? 47.509 -2.181  8.680   1.00 21.84 ?  71  THR   B HG21 1 
ATOM   4931 H  HG22 . THR   B 1 71  ? 46.360 -3.117  9.221   1.00 21.84 ?  71  THR   B HG22 1 
ATOM   4932 H  HG23 . THR   B 1 71  ? 47.097 -2.121  10.202  1.00 21.84 ?  71  THR   B HG23 1 
ATOM   4933 N  N    . ASN   B 1 72  ? 46.181 -5.938  11.006  1.00 15.46 ?  72  ASN   B N    1 
ATOM   4934 C  CA   . ASN   B 1 72  ? 44.779 -6.307  10.880  1.00 15.86 ?  72  ASN   B CA   1 
ATOM   4935 C  C    . ASN   B 1 72  ? 44.312 -7.400  11.830  1.00 16.20 ?  72  ASN   B C    1 
ATOM   4936 O  O    . ASN   B 1 72  ? 43.098 -7.563  11.997  1.00 17.18 ?  72  ASN   B O    1 
ATOM   4937 C  CB   . ASN   B 1 72  ? 44.471 -6.745  9.439   1.00 16.66 ?  72  ASN   B CB   1 
ATOM   4938 C  CG   . ASN   B 1 72  ? 44.743 -5.652  8.430   1.00 17.96 ?  72  ASN   B CG   1 
ATOM   4939 O  OD1  . ASN   B 1 72  ? 45.762 -5.659  7.739   1.00 19.36 ?  72  ASN   B OD1  1 
ATOM   4940 N  ND2  . ASN   B 1 72  ? 43.851 -4.684  8.365   1.00 19.36 ?  72  ASN   B ND2  1 
ATOM   4941 H  H    . ASN   B 1 72  ? 46.727 -6.586  10.819  1.00 18.52 ?  72  ASN   B H    1 
ATOM   4942 H  HA   . ASN   B 1 72  ? 44.246 -5.521  11.062  1.00 18.99 ?  72  ASN   B HA   1 
ATOM   4943 H  HB2  . ASN   B 1 72  ? 45.033 -7.507  9.213   1.00 19.95 ?  72  ASN   B HB2  1 
ATOM   4944 H  HB3  . ASN   B 1 72  ? 43.539 -6.987  9.373   1.00 19.95 ?  72  ASN   B HB3  1 
ATOM   4945 H  HD21 . ASN   B 1 72  ? 43.954 -4.036  7.805   1.00 23.19 ?  72  ASN   B HD21 1 
ATOM   4946 H  HD22 . ASN   B 1 72  ? 43.147 -4.710  8.861   1.00 23.19 ?  72  ASN   B HD22 1 
ATOM   4947 N  N    . GLY   B 1 73  ? 45.217 -8.152  12.448  1.00 16.06 ?  73  GLY   B N    1 
ATOM   4948 C  CA   . GLY   B 1 73  ? 44.823 -9.286  13.247  1.00 15.53 ?  73  GLY   B CA   1 
ATOM   4949 C  C    . GLY   B 1 73  ? 44.490 -10.476 12.375  1.00 14.19 ?  73  GLY   B C    1 
ATOM   4950 O  O    . GLY   B 1 73  ? 44.485 -10.395 11.143  1.00 14.02 ?  73  GLY   B O    1 
ATOM   4951 H  H    . GLY   B 1 73  ? 46.068 -8.020  12.419  1.00 19.24 ?  73  GLY   B H    1 
ATOM   4952 H  HA2  . GLY   B 1 73  ? 45.543 -9.530  13.849  1.00 18.60 ?  73  GLY   B HA2  1 
ATOM   4953 H  HA3  . GLY   B 1 73  ? 44.041 -9.057  13.777  1.00 18.60 ?  73  GLY   B HA3  1 
ATOM   4954 N  N    . PRO   B 1 74  ? 44.180 -11.602 13.012  1.00 14.38 ?  74  PRO   B N    1 
ATOM   4955 C  CA   . PRO   B 1 74  ? 43.929 -12.835 12.263  1.00 14.16 ?  74  PRO   B CA   1 
ATOM   4956 C  C    . PRO   B 1 74  ? 42.633 -12.778 11.466  1.00 13.49 ?  74  PRO   B C    1 
ATOM   4957 O  O    . PRO   B 1 74  ? 41.694 -12.040 11.786  1.00 15.09 ?  74  PRO   B O    1 
ATOM   4958 C  CB   . PRO   B 1 74  ? 43.846 -13.899 13.363  1.00 15.30 ?  74  PRO   B CB   1 
ATOM   4959 C  CG   . PRO   B 1 74  ? 43.391 -13.144 14.570  1.00 16.66 ?  74  PRO   B CG   1 
ATOM   4960 C  CD   . PRO   B 1 74  ? 44.058 -11.802 14.464  1.00 15.96 ?  74  PRO   B CD   1 
ATOM   4961 H  HA   . PRO   B 1 74  ? 44.676 -13.032 11.670  1.00 16.95 ?  74  PRO   B HA   1 
ATOM   4962 H  HB2  . PRO   B 1 74  ? 43.197 -14.577 13.114  1.00 18.33 ?  74  PRO   B HB2  1 
ATOM   4963 H  HB3  . PRO   B 1 74  ? 44.719 -14.293 13.510  1.00 18.33 ?  74  PRO   B HB3  1 
ATOM   4964 H  HG2  . PRO   B 1 74  ? 42.425 -13.049 14.550  1.00 19.95 ?  74  PRO   B HG2  1 
ATOM   4965 H  HG3  . PRO   B 1 74  ? 43.675 -13.607 15.371  1.00 19.95 ?  74  PRO   B HG3  1 
ATOM   4966 H  HD2  . PRO   B 1 74  ? 43.494 -11.116 14.860  1.00 19.11 ?  74  PRO   B HD2  1 
ATOM   4967 H  HD3  . PRO   B 1 74  ? 44.933 -11.826 14.878  1.00 19.11 ?  74  PRO   B HD3  1 
ATOM   4968 N  N    . LEU   B 1 75  ? 42.604 -13.578 10.409  1.00 13.00 ?  75  LEU   B N    1 
ATOM   4969 C  CA   . LEU   B 1 75  ? 41.394 -13.792 9.641   1.00 13.24 ?  75  LEU   B CA   1 
ATOM   4970 C  C    . LEU   B 1 75  ? 40.415 -14.642 10.445  1.00 13.87 ?  75  LEU   B C    1 
ATOM   4971 O  O    . LEU   B 1 75  ? 40.757 -15.239 11.468  1.00 15.04 ?  75  LEU   B O    1 
ATOM   4972 C  CB   . LEU   B 1 75  ? 41.717 -14.518 8.337   1.00 13.02 ?  75  LEU   B CB   1 
ATOM   4973 C  CG   . LEU   B 1 75  ? 42.551 -13.754 7.306   1.00 14.96 ?  75  LEU   B CG   1 
ATOM   4974 C  CD1  . LEU   B 1 75  ? 42.811 -14.610 6.066   1.00 16.90 ?  75  LEU   B CD1  1 
ATOM   4975 C  CD2  . LEU   B 1 75  ? 41.908 -12.443 6.927   1.00 17.88 ?  75  LEU   B CD2  1 
ATOM   4976 H  H    . LEU   B 1 75  ? 43.283 -14.022 10.119  1.00 15.56 ?  75  LEU   B H    1 
ATOM   4977 H  HA   . LEU   B 1 75  ? 40.979 -12.944 9.439   1.00 15.85 ?  75  LEU   B HA   1 
ATOM   4978 H  HB2  . LEU   B 1 75  ? 42.207 -15.331 8.557   1.00 15.59 ?  75  LEU   B HB2  1 
ATOM   4979 H  HB3  . LEU   B 1 75  ? 40.882 -14.760 7.909   1.00 15.59 ?  75  LEU   B HB3  1 
ATOM   4980 H  HG   . LEU   B 1 75  ? 43.414 -13.553 7.702   1.00 17.91 ?  75  LEU   B HG   1 
ATOM   4981 H  HD11 . LEU   B 1 75  ? 43.347 -14.097 5.437   1.00 20.24 ?  75  LEU   B HD11 1 
ATOM   4982 H  HD12 . LEU   B 1 75  ? 43.295 -15.411 6.328   1.00 20.24 ?  75  LEU   B HD12 1 
ATOM   4983 H  HD13 . LEU   B 1 75  ? 41.966 -14.850 5.662   1.00 20.24 ?  75  LEU   B HD13 1 
ATOM   4984 H  HD21 . LEU   B 1 75  ? 42.411 -12.046 6.202   1.00 21.42 ?  75  LEU   B HD21 1 
ATOM   4985 H  HD22 . LEU   B 1 75  ? 40.995 -12.610 6.649   1.00 21.42 ?  75  LEU   B HD22 1 
ATOM   4986 H  HD23 . LEU   B 1 75  ? 41.918 -11.854 7.699   1.00 21.42 ?  75  LEU   B HD23 1 
ATOM   4987 N  N    . LYS   B 1 76  ? 39.175 -14.691 9.961   1.00 15.21 ?  76  LYS   B N    1 
ATOM   4988 C  CA   . LYS   B 1 76  ? 38.185 -15.647 10.439  1.00 16.22 ?  76  LYS   B CA   1 
ATOM   4989 C  C    . LYS   B 1 76  ? 38.298 -16.930 9.623   1.00 15.28 ?  76  LYS   B C    1 
ATOM   4990 O  O    . LYS   B 1 76  ? 38.581 -16.893 8.426   1.00 15.10 ?  76  LYS   B O    1 
ATOM   4991 C  CB   . LYS   B 1 76  ? 36.768 -15.094 10.235  1.00 17.68 ?  76  LYS   B CB   1 
ATOM   4992 C  CG   . LYS   B 1 76  ? 36.476 -13.728 10.869  1.00 19.39 ?  76  LYS   B CG   1 
ATOM   4993 C  CD   . LYS   B 1 76  ? 35.094 -13.192 10.457  1.00 20.56 ?  76  LYS   B CD   1 
ATOM   4994 C  CE   . LYS   B 1 76  ? 34.787 -11.848 11.097  1.00 22.41 ?  76  LYS   B CE   1 
ATOM   4995 N  NZ   . LYS   B 1 76  ? 33.520 -11.241 10.600  1.00 23.32 ?  76  LYS   B NZ   1 
ATOM   4996 H  H    . LYS   B 1 76  ? 38.884 -14.182 9.333   1.00 18.21 ?  76  LYS   B H    1 
ATOM   4997 H  HA   . LYS   B 1 76  ? 38.329 -15.850 11.377  1.00 19.42 ?  76  LYS   B HA   1 
ATOM   4998 H  HB2  . LYS   B 1 76  ? 36.609 -15.010 9.282   1.00 21.18 ?  76  LYS   B HB2  1 
ATOM   4999 H  HB3  . LYS   B 1 76  ? 36.138 -15.728 10.612  1.00 21.18 ?  76  LYS   B HB3  1 
ATOM   5000 H  HG2  . LYS   B 1 76  ? 36.495 -13.814 11.836  1.00 23.24 ?  76  LYS   B HG2  1 
ATOM   5001 H  HG3  . LYS   B 1 76  ? 37.150 -13.091 10.579  1.00 23.24 ?  76  LYS   B HG3  1 
ATOM   5002 H  HD2  . LYS   B 1 76  ? 35.070 -13.082 9.493   1.00 24.63 ?  76  LYS   B HD2  1 
ATOM   5003 H  HD3  . LYS   B 1 76  ? 34.412 -13.823 10.736  1.00 24.63 ?  76  LYS   B HD3  1 
ATOM   5004 H  HE2  . LYS   B 1 76  ? 34.707 -11.967 12.055  1.00 26.86 ?  76  LYS   B HE2  1 
ATOM   5005 H  HE3  . LYS   B 1 76  ? 35.512 -11.233 10.898  1.00 26.86 ?  76  LYS   B HE3  1 
ATOM   5006 H  HZ1  . LYS   B 1 76  ? 33.379 -10.457 10.999  1.00 27.95 ?  76  LYS   B HZ1  1 
ATOM   5007 H  HZ2  . LYS   B 1 76  ? 33.566 -11.111 9.720   1.00 27.95 ?  76  LYS   B HZ2  1 
ATOM   5008 H  HZ3  . LYS   B 1 76  ? 32.833 -11.780 10.775  1.00 27.95 ?  76  LYS   B HZ3  1 
ATOM   5009 N  N    . VAL   B 1 77  ? 38.059 -18.073 10.271  1.00 16.07 ?  77  VAL   B N    1 
ATOM   5010 C  CA   . VAL   B 1 77  ? 37.859 -19.299 9.507   1.00 16.17 ?  77  VAL   B CA   1 
ATOM   5011 C  C    . VAL   B 1 77  ? 36.672 -19.080 8.582   1.00 15.08 ?  77  VAL   B C    1 
ATOM   5012 O  O    . VAL   B 1 77  ? 35.604 -18.635 9.019   1.00 15.08 ?  77  VAL   B O    1 
ATOM   5013 C  CB   . VAL   B 1 77  ? 37.650 -20.500 10.441  1.00 17.80 ?  77  VAL   B CB   1 
ATOM   5014 C  CG1  . VAL   B 1 77  ? 37.367 -21.752 9.618   1.00 18.03 ?  77  VAL   B CG1  1 
ATOM   5015 C  CG2  . VAL   B 1 77  ? 38.867 -20.701 11.344  1.00 19.02 ?  77  VAL   B CG2  1 
ATOM   5016 H  H    . VAL   B 1 77  ? 38.008 -18.161 11.120  1.00 19.25 ?  77  VAL   B H    1 
ATOM   5017 H  HA   . VAL   B 1 77  ? 38.637 -19.469 8.957   1.00 19.36 ?  77  VAL   B HA   1 
ATOM   5018 H  HB   . VAL   B 1 77  ? 36.876 -20.330 11.004  1.00 21.33 ?  77  VAL   B HB   1 
ATOM   5019 H  HG11 . VAL   B 1 77  ? 37.401 -22.524 10.204  1.00 21.60 ?  77  VAL   B HG11 1 
ATOM   5020 H  HG12 . VAL   B 1 77  ? 36.484 -21.682 9.220   1.00 21.60 ?  77  VAL   B HG12 1 
ATOM   5021 H  HG13 . VAL   B 1 77  ? 38.038 -21.831 8.926   1.00 21.60 ?  77  VAL   B HG13 1 
ATOM   5022 H  HG21 . VAL   B 1 77  ? 38.725 -21.491 11.883  1.00 22.78 ?  77  VAL   B HG21 1 
ATOM   5023 H  HG22 . VAL   B 1 77  ? 39.651 -20.807 10.788  1.00 22.78 ?  77  VAL   B HG22 1 
ATOM   5024 H  HG23 . VAL   B 1 77  ? 38.963 -19.921 11.913  1.00 22.78 ?  77  VAL   B HG23 1 
ATOM   5025 N  N    . GLY   B 1 78  ? 36.856 -19.368 7.295   1.00 14.46 ?  78  GLY   B N    1 
ATOM   5026 C  CA   . GLY   B 1 78  ? 35.883 -19.050 6.276   1.00 14.25 ?  78  GLY   B CA   1 
ATOM   5027 C  C    . GLY   B 1 78  ? 36.122 -17.736 5.566   1.00 13.71 ?  78  GLY   B C    1 
ATOM   5028 O  O    . GLY   B 1 78  ? 35.431 -17.455 4.575   1.00 14.07 ?  78  GLY   B O    1 
ATOM   5029 H  H    . GLY   B 1 78  ? 37.555 -19.766 6.989   1.00 17.31 ?  78  GLY   B H    1 
ATOM   5030 H  HA2  . GLY   B 1 78  ? 35.883 -19.746 5.607   1.00 17.06 ?  78  GLY   B HA2  1 
ATOM   5031 H  HA3  . GLY   B 1 78  ? 35.002 -19.014 6.678   1.00 17.06 ?  78  GLY   B HA3  1 
ATOM   5032 N  N    . GLY   B 1 79  ? 37.063 -16.920 6.053   1.00 13.41 ?  79  GLY   B N    1 
ATOM   5033 C  CA   . GLY   B 1 79  ? 37.364 -15.630 5.468   1.00 12.99 ?  79  GLY   B CA   1 
ATOM   5034 C  C    . GLY   B 1 79  ? 38.585 -15.660 4.563   1.00 12.55 ?  79  GLY   B C    1 
ATOM   5035 O  O    . GLY   B 1 79  ? 39.192 -16.699 4.317   1.00 13.10 ?  79  GLY   B O    1 
ATOM   5036 H  H    . GLY   B 1 79  ? 37.550 -17.095 6.742   1.00 16.05 ?  79  GLY   B H    1 
ATOM   5037 H  HA2  . GLY   B 1 79  ? 36.607 -15.325 4.942   1.00 15.55 ?  79  GLY   B HA2  1 
ATOM   5038 H  HA3  . GLY   B 1 79  ? 37.523 -14.978 6.172   1.00 15.55 ?  79  GLY   B HA3  1 
ATOM   5039 N  N    . SER   B 1 80  ? 38.952 -14.470 4.082   1.00 12.40 ?  80  SER   B N    1 
ATOM   5040 C  CA   . SER   B 1 80  ? 40.054 -14.339 3.138   1.00 12.33 ?  80  SER   B CA   1 
ATOM   5041 C  C    . SER   B 1 80  ? 40.639 -12.934 3.195   1.00 12.14 ?  80  SER   B C    1 
ATOM   5042 O  O    . SER   B 1 80  ? 40.032 -11.999 3.723   1.00 13.25 ?  80  SER   B O    1 
ATOM   5043 C  CB   . SER   B 1 80  ? 39.612 -14.630 1.702   1.00 12.58 ?  80  SER   B CB   1 
ATOM   5044 O  OG   . SER   B 1 80  ? 38.774 -13.606 1.203   1.00 13.51 ?  80  SER   B OG   1 
ATOM   5045 H  H    . SER   B 1 80  ? 38.587 -13.723 4.293   1.00 14.84 ?  80  SER   B H    1 
ATOM   5046 H  HA   . SER   B 1 80  ? 40.749 -14.968 3.377   1.00 14.75 ?  80  SER   B HA   1 
ATOM   5047 H  HB2  . SER   B 1 80  ? 40.394 -14.688 1.131   1.00 15.06 ?  80  SER   B HB2  1 
ATOM   5048 H  HB3  . SER   B 1 80  ? 39.124 -15.464 1.683   1.00 15.06 ?  80  SER   B HB3  1 
ATOM   5049 H  HG   . SER   B 1 80  ? 38.082 -13.532 1.685   1.00 16.17 ?  80  SER   B HG   1 
ATOM   5050 N  N    . CYS   B 1 81  ? 41.827 -12.792 2.607   1.00 11.75 ?  81  CYS   B N    1 
ATOM   5051 C  CA   . CYS   B 1 81  ? 42.380 -11.480 2.303   1.00 11.82 ?  81  CYS   B CA   1 
ATOM   5052 C  C    . CYS   B 1 81  ? 43.155 -11.568 0.997   1.00 11.13 ?  81  CYS   B C    1 
ATOM   5053 O  O    . CYS   B 1 81  ? 43.649 -12.638 0.620   1.00 12.32 ?  81  CYS   B O    1 
ATOM   5054 C  CB   . CYS   B 1 81  ? 43.265 -10.935 3.432   1.00 12.74 ?  81  CYS   B CB   1 
ATOM   5055 S  SG   . CYS   B 1 81  ? 44.791 -11.872 3.659   1.00 12.73 ?  81  CYS   B SG   1 
ATOM   5056 H  H    . CYS   B 1 81  ? 42.339 -13.445 2.368   1.00 14.06 ?  81  CYS   B H    1 
ATOM   5057 H  HA   . CYS   B 1 81  ? 41.651 -10.854 2.177   1.00 14.15 ?  81  CYS   B HA   1 
ATOM   5058 H  HB2  . CYS   B 1 81  ? 43.506 -10.016 3.235   1.00 15.24 ?  81  CYS   B HB2  1 
ATOM   5059 H  HB3  . CYS   B 1 81  ? 42.766 -10.966 4.270   1.00 15.24 ?  81  CYS   B HB3  1 
ATOM   5060 H  HG   . CYS   B 1 81  ? 45.419 -11.385 4.562   1.00 15.24 ?  81  CYS   B HG   1 
ATOM   5061 N  N    . VAL   B 1 82  ? 43.267 -10.425 0.322   1.00 11.63 ?  82  VAL   B N    1 
ATOM   5062 C  CA   . VAL   B 1 82  ? 44.022 -10.302 -0.920  1.00 11.57 ?  82  VAL   B CA   1 
ATOM   5063 C  C    . VAL   B 1 82  ? 45.366 -9.662  -0.611  1.00 12.10 ?  82  VAL   B C    1 
ATOM   5064 O  O    . VAL   B 1 82  ? 45.421 -8.542  -0.084  1.00 13.13 ?  82  VAL   B O    1 
ATOM   5065 C  CB   . VAL   B 1 82  ? 43.270 -9.465  -1.967  1.00 12.95 ?  82  VAL   B CB   1 
ATOM   5066 C  CG1  . VAL   B 1 82  ? 44.118 -9.337  -3.235  1.00 14.29 ?  82  VAL   B CG1  1 
ATOM   5067 C  CG2  . VAL   B 1 82  ? 41.908 -10.060 -2.266  1.00 14.37 ?  82  VAL   B CG2  1 
ATOM   5068 H  H    . VAL   B 1 82  ? 42.892 -9.682  0.568   1.00 13.91 ?  82  VAL   B H    1 
ATOM   5069 H  HA   . VAL   B 1 82  ? 44.179 -11.183 -1.286  1.00 13.84 ?  82  VAL   B HA   1 
ATOM   5070 H  HB   . VAL   B 1 82  ? 43.136 -8.572  -1.617  1.00 15.50 ?  82  VAL   B HB   1 
ATOM   5071 H  HG11 . VAL   B 1 82  ? 43.559 -9.018  -3.959  1.00 17.11 ?  82  VAL   B HG11 1 
ATOM   5072 H  HG12 . VAL   B 1 82  ? 44.841 -8.705  -3.076  1.00 17.11 ?  82  VAL   B HG12 1 
ATOM   5073 H  HG13 . VAL   B 1 82  ? 44.487 -10.206 -3.461  1.00 17.11 ?  82  VAL   B HG13 1 
ATOM   5074 H  HG21 . VAL   B 1 82  ? 41.480 -9.535  -2.961  1.00 17.21 ?  82  VAL   B HG21 1 
ATOM   5075 H  HG22 . VAL   B 1 82  ? 42.021 -10.975 -2.564  1.00 17.21 ?  82  VAL   B HG22 1 
ATOM   5076 H  HG23 . VAL   B 1 82  ? 41.372 -10.037 -1.458  1.00 17.21 ?  82  VAL   B HG23 1 
ATOM   5077 N  N    . LEU   B 1 83  ? 46.441 -10.347 -0.983  1.00 11.68 ?  83  LEU   B N    1 
ATOM   5078 C  CA   . LEU   B 1 83  ? 47.799 -9.834  -0.868  1.00 11.58 ?  83  LEU   B CA   1 
ATOM   5079 C  C    . LEU   B 1 83  ? 48.496 -9.986  -2.218  1.00 11.56 ?  83  LEU   B C    1 
ATOM   5080 O  O    . LEU   B 1 83  ? 47.891 -10.418 -3.202  1.00 11.58 ?  83  LEU   B O    1 
ATOM   5081 C  CB   . LEU   B 1 83  ? 48.546 -10.516 0.284   1.00 12.42 ?  83  LEU   B CB   1 
ATOM   5082 C  CG   . LEU   B 1 83  ? 48.045 -10.165 1.692   1.00 13.26 ?  83  LEU   B CG   1 
ATOM   5083 C  CD1  . LEU   B 1 83  ? 48.676 -11.032 2.760   1.00 13.90 ?  83  LEU   B CD1  1 
ATOM   5084 C  CD2  . LEU   B 1 83  ? 48.259 -8.685  2.015   1.00 14.24 ?  83  LEU   B CD2  1 
ATOM   5085 H  H    . LEU   B 1 83  ? 46.397 -11.144 -1.315  1.00 13.98 ?  83  LEU   B H    1 
ATOM   5086 H  HA   . LEU   B 1 83  ? 47.753 -8.890  -0.674  1.00 13.86 ?  83  LEU   B HA   1 
ATOM   5087 H  HB2  . LEU   B 1 83  ? 48.471 -11.475 0.180   1.00 14.86 ?  83  LEU   B HB2  1 
ATOM   5088 H  HB3  . LEU   B 1 83  ? 49.481 -10.257 0.235   1.00 14.86 ?  83  LEU   B HB3  1 
ATOM   5089 H  HG   . LEU   B 1 83  ? 47.093 -10.325 1.717   1.00 15.88 ?  83  LEU   B HG   1 
ATOM   5090 H  HD11 . LEU   B 1 83  ? 48.319 -10.778 3.628   1.00 16.64 ?  83  LEU   B HD11 1 
ATOM   5091 H  HD12 . LEU   B 1 83  ? 48.459 -11.964 2.580   1.00 16.64 ?  83  LEU   B HD12 1 
ATOM   5092 H  HD13 . LEU   B 1 83  ? 49.637 -10.911 2.749   1.00 16.64 ?  83  LEU   B HD13 1 
ATOM   5093 H  HD21 . LEU   B 1 83  ? 48.050 -8.533  2.951   1.00 17.05 ?  83  LEU   B HD21 1 
ATOM   5094 H  HD22 . LEU   B 1 83  ? 49.185 -8.451  1.843   1.00 17.05 ?  83  LEU   B HD22 1 
ATOM   5095 H  HD23 . LEU   B 1 83  ? 47.674 -8.149  1.456   1.00 17.05 ?  83  LEU   B HD23 1 
ATOM   5096 N  N    . SER   B 1 84  ? 49.775 -9.614  -2.276  1.00 12.69 ?  84  SER   B N    1 
ATOM   5097 C  CA   . SER   B 1 84  ? 50.513 -9.754  -3.522  1.00 12.88 ?  84  SER   B CA   1 
ATOM   5098 C  C    . SER   B 1 84  ? 50.673 -11.221 -3.904  1.00 11.90 ?  84  SER   B C    1 
ATOM   5099 O  O    . SER   B 1 84  ? 50.791 -12.102 -3.049  1.00 12.06 ?  84  SER   B O    1 
ATOM   5100 C  CB   . SER   B 1 84  ? 51.909 -9.147  -3.381  1.00 14.66 ?  84  SER   B CB   1 
ATOM   5101 O  OG   . SER   B 1 84  ? 52.650 -9.368  -4.567  1.00 15.66 ?  84  SER   B OG   1 
ATOM   5102 H  H    . SER   B 1 84  ? 50.220 -9.271  -1.624  1.00 15.20 ?  84  SER   B H    1 
ATOM   5103 H  HA   . SER   B 1 84  ? 50.046 -9.296  -4.237  1.00 15.42 ?  84  SER   B HA   1 
ATOM   5104 H  HB2  . SER   B 1 84  ? 51.831 -8.192  -3.230  1.00 17.56 ?  84  SER   B HB2  1 
ATOM   5105 H  HB3  . SER   B 1 84  ? 52.366 -9.565  -2.632  1.00 17.56 ?  84  SER   B HB3  1 
ATOM   5106 H  HG   . SER   B 1 84  ? 53.428 -9.036  -4.483  1.00 18.75 ?  84  SER   B HG   1 
ATOM   5107 N  N    . GLY   B 1 85  ? 50.732 -11.468 -5.206  1.00 12.86 ?  85  GLY   B N    1 
ATOM   5108 C  CA   . GLY   B 1 85  ? 51.092 -12.771 -5.711  1.00 13.75 ?  85  GLY   B CA   1 
ATOM   5109 C  C    . GLY   B 1 85  ? 52.562 -12.955 -6.023  1.00 13.14 ?  85  GLY   B C    1 
ATOM   5110 O  O    . GLY   B 1 85  ? 52.949 -14.038 -6.468  1.00 13.72 ?  85  GLY   B O    1 
ATOM   5111 H  H    . GLY   B 1 85  ? 50.570 -10.898 -5.820  1.00 15.39 ?  85  GLY   B H    1 
ATOM   5112 H  HA2  . GLY   B 1 85  ? 50.841 -13.450 -5.059  1.00 16.46 ?  85  GLY   B HA2  1 
ATOM   5113 H  HA3  . GLY   B 1 85  ? 50.603 -12.949 -6.524  1.00 16.46 ?  85  GLY   B HA3  1 
ATOM   5114 N  N    . HIS   B 1 86  ? 53.408 -11.945 -5.823  1.00 13.34 ?  86  HIS   B N    1 
ATOM   5115 C  CA   . HIS   B 1 86  ? 54.870 -12.108 -5.913  1.00 13.13 ?  86  HIS   B CA   1 
ATOM   5116 C  C    . HIS   B 1 86  ? 55.246 -12.630 -7.299  1.00 13.10 ?  86  HIS   B C    1 
ATOM   5117 O  O    . HIS   B 1 86  ? 54.860 -12.020 -8.310  1.00 14.26 ?  86  HIS   B O    1 
ATOM   5118 C  CB   . HIS   B 1 86  ? 55.372 -12.933 -4.726  1.00 13.63 ?  86  HIS   B CB   1 
ATOM   5119 C  CG   . HIS   B 1 86  ? 55.047 -12.320 -3.404  1.00 13.80 ?  86  HIS   B CG   1 
ATOM   5120 N  ND1  . HIS   B 1 86  ? 55.865 -11.396 -2.791  1.00 15.53 ?  86  HIS   B ND1  1 
ATOM   5121 C  CD2  . HIS   B 1 86  ? 53.967 -12.462 -2.599  1.00 14.40 ?  86  HIS   B CD2  1 
ATOM   5122 C  CE1  . HIS   B 1 86  ? 55.304 -11.002 -1.661  1.00 15.17 ?  86  HIS   B CE1  1 
ATOM   5123 N  NE2  . HIS   B 1 86  ? 54.150 -11.628 -1.523  1.00 14.67 ?  86  HIS   B NE2  1 
ATOM   5124 H  H    . HIS   B 1 86  ? 53.163 -11.148 -5.631  1.00 15.97 ?  86  HIS   B H    1 
ATOM   5125 H  HA   . HIS   B 1 86  ? 55.277 -11.234 -5.823  1.00 15.72 ?  86  HIS   B HA   1 
ATOM   5126 H  HB2  . HIS   B 1 86  ? 54.966 -13.815 -4.757  1.00 16.32 ?  86  HIS   B HB2  1 
ATOM   5127 H  HB3  . HIS   B 1 86  ? 56.340 -13.018 -4.783  1.00 16.32 ?  86  HIS   B HB3  1 
ATOM   5128 H  HD2  . HIS   B 1 86  ? 53.230 -13.013 -2.752  1.00 17.24 ?  86  HIS   B HD2  1 
ATOM   5129 H  HE1  . HIS   B 1 86  ? 55.669 -10.396 -1.058  1.00 18.17 ?  86  HIS   B HE1  1 
ATOM   5130 H  HE2  . HIS   B 1 86  ? 53.610 -11.546 -0.857  1.00 17.56 ?  86  HIS   B HE2  1 
ATOM   5131 N  N    . ASN   B 1 87  ? 56.013 -13.716 -7.400  1.00 14.00 ?  87  ASN   B N    1 
ATOM   5132 C  CA   . ASN   B 1 87  ? 56.405 -14.303 -8.674  1.00 14.75 ?  87  ASN   B CA   1 
ATOM   5133 C  C    . ASN   B 1 87  ? 55.417 -15.337 -9.173  1.00 14.61 ?  87  ASN   B C    1 
ATOM   5134 O  O    . ASN   B 1 87  ? 55.723 -16.040 -10.140 1.00 16.11 ?  87  ASN   B O    1 
ATOM   5135 C  CB   . ASN   B 1 87  ? 57.796 -14.943 -8.562  1.00 16.24 ?  87  ASN   B CB   1 
ATOM   5136 C  CG   . ASN   B 1 87  ? 57.856 -16.045 -7.508  1.00 17.30 ?  87  ASN   B CG   1 
ATOM   5137 O  OD1  . ASN   B 1 87  ? 57.208 -15.958 -6.460  1.00 16.32 ?  87  ASN   B OD1  1 
ATOM   5138 N  ND2  . ASN   B 1 87  ? 58.632 -17.099 -7.792  1.00 19.07 ?  87  ASN   B ND2  1 
ATOM   5139 H  H    . ASN   B 1 87  ? 56.319 -14.148 -6.723  1.00 16.76 ?  87  ASN   B H    1 
ATOM   5140 H  HA   . ASN   B 1 87  ? 56.456 -13.606 -9.336  1.00 17.66 ?  87  ASN   B HA   1 
ATOM   5141 H  HB2  . ASN   B 1 87  ? 58.038 -15.335 -9.421  1.00 19.45 ?  87  ASN   B HB2  1 
ATOM   5142 H  HB3  . ASN   B 1 87  ? 58.440 -14.261 -8.320  1.00 19.45 ?  87  ASN   B HB3  1 
ATOM   5143 H  HD21 . ASN   B 1 87  ? 58.712 -17.744 -7.229  1.00 22.85 ?  87  ASN   B HD21 1 
ATOM   5144 H  HD22 . ASN   B 1 87  ? 59.075 -17.128 -8.536  1.00 22.85 ?  87  ASN   B HD22 1 
ATOM   5145 N  N    . LEU   B 1 88  ? 54.244 -15.436 -8.548  1.00 13.33 ?  88  LEU   B N    1 
ATOM   5146 C  CA   . LEU   B 1 88  ? 53.258 -16.456 -8.872  1.00 13.68 ?  88  LEU   B CA   1 
ATOM   5147 C  C    . LEU   B 1 88  ? 52.033 -15.933 -9.599  1.00 13.71 ?  88  LEU   B C    1 
ATOM   5148 O  O    . LEU   B 1 88  ? 51.436 -16.672 -10.391 1.00 15.42 ?  88  LEU   B O    1 
ATOM   5149 C  CB   . LEU   B 1 88  ? 52.781 -17.130 -7.583  1.00 14.97 ?  88  LEU   B CB   1 
ATOM   5150 C  CG   . LEU   B 1 88  ? 53.901 -17.822 -6.817  1.00 16.92 ?  88  LEU   B CG   1 
ATOM   5151 C  CD1  . LEU   B 1 88  ? 53.436 -18.176 -5.417  1.00 18.31 ?  88  LEU   B CD1  1 
ATOM   5152 C  CD2  . LEU   B 1 88  ? 54.336 -19.061 -7.573  1.00 19.73 ?  88  LEU   B CD2  1 
ATOM   5153 H  H    . LEU   B 1 88  ? 53.993 -14.914 -7.908  1.00 15.96 ?  88  LEU   B H    1 
ATOM   5154 H  HA   . LEU   B 1 88  ? 53.664 -17.131 -9.427  1.00 16.38 ?  88  LEU   B HA   1 
ATOM   5155 H  HB2  . LEU   B 1 88  ? 52.386 -16.463 -6.997  1.00 17.92 ?  88  LEU   B HB2  1 
ATOM   5156 H  HB3  . LEU   B 1 88  ? 52.113 -17.803 -7.805  1.00 17.92 ?  88  LEU   B HB3  1 
ATOM   5157 H  HG   . LEU   B 1 88  ? 54.658 -17.221 -6.745  1.00 20.27 ?  88  LEU   B HG   1 
ATOM   5158 H  HD11 . LEU   B 1 88  ? 54.085 -18.772 -5.011  1.00 21.93 ?  88  LEU   B HD11 1 
ATOM   5159 H  HD12 . LEU   B 1 88  ? 53.359 -17.363 -4.894  1.00 21.93 ?  88  LEU   B HD12 1 
ATOM   5160 H  HD13 . LEU   B 1 88  ? 52.574 -18.615 -5.475  1.00 21.93 ?  88  LEU   B HD13 1 
ATOM   5161 H  HD21 . LEU   B 1 88  ? 54.961 -19.558 -7.025  1.00 23.64 ?  88  LEU   B HD21 1 
ATOM   5162 H  HD22 . LEU   B 1 88  ? 53.556 -19.604 -7.764  1.00 23.64 ?  88  LEU   B HD22 1 
ATOM   5163 H  HD23 . LEU   B 1 88  ? 54.764 -18.791 -8.401  1.00 23.64 ?  88  LEU   B HD23 1 
ATOM   5164 N  N    . ALA   B 1 89  ? 51.625 -14.701 -9.323  1.00 13.03 ?  89  ALA   B N    1 
ATOM   5165 C  CA   . ALA   B 1 89  ? 50.341 -14.193 -9.778  1.00 12.44 ?  89  ALA   B CA   1 
ATOM   5166 C  C    . ALA   B 1 89  ? 50.327 -12.705 -9.480  1.00 12.76 ?  89  ALA   B C    1 
ATOM   5167 O  O    . ALA   B 1 89  ? 51.148 -12.207 -8.709  1.00 13.06 ?  89  ALA   B O    1 
ATOM   5168 C  CB   . ALA   B 1 89  ? 49.193 -14.864 -9.029  1.00 12.59 ?  89  ALA   B CB   1 
ATOM   5169 H  H    . ALA   B 1 89  ? 52.073 -14.126 -8.868  1.00 15.60 ?  89  ALA   B H    1 
ATOM   5170 H  HA   . ALA   B 1 89  ? 50.232 -14.332 -10.738 1.00 14.89 ?  89  ALA   B HA   1 
ATOM   5171 H  HB1  . ALA   B 1 89  ? 48.352 -14.518 -9.366  1.00 15.07 ?  89  ALA   B HB1  1 
ATOM   5172 H  HB2  . ALA   B 1 89  ? 49.242 -15.821 -9.182  1.00 15.07 ?  89  ALA   B HB2  1 
ATOM   5173 H  HB3  . ALA   B 1 89  ? 49.283 -14.671 -8.087  1.00 15.07 ?  89  ALA   B HB3  1 
ATOM   5174 N  N    . LYS   B 1 90  ? 49.370 -11.992 -10.069 1.00 13.55 ?  90  LYS   B N    1 
ATOM   5175 C  CA   . LYS   B 1 90  ? 49.188 -10.604 -9.655  1.00 13.28 ?  90  LYS   B CA   1 
ATOM   5176 C  C    . LYS   B 1 90  ? 48.852 -10.531 -8.170  1.00 12.83 ?  90  LYS   B C    1 
ATOM   5177 O  O    . LYS   B 1 90  ? 49.490 -9.784  -7.409  1.00 13.60 ?  90  LYS   B O    1 
ATOM   5178 C  CB   . LYS   B 1 90  ? 48.123 -9.929  -10.520 1.00 14.80 ?  90  LYS   B CB   1 
ATOM   5179 C  CG   . LYS   B 1 90  ? 47.784 -8.505  -10.101 1.00 15.15 ?  90  LYS   B CG   1 
ATOM   5180 C  CD   . LYS   B 1 90  ? 48.966 -7.580  -10.169 1.00 16.91 ?  90  LYS   B CD   1 
ATOM   5181 C  CE   . LYS   B 1 90  ? 48.493 -6.186  -9.838  1.00 18.57 ?  90  LYS   B CE   1 
ATOM   5182 N  NZ   . LYS   B 1 90  ? 49.607 -5.218  -9.814  1.00 18.19 ?  90  LYS   B NZ   1 
ATOM   5183 H  H    . LYS   B 1 90  ? 48.839 -12.274 -10.687 1.00 16.22 ?  90  LYS   B H    1 
ATOM   5184 H  HA   . LYS   B 1 90  ? 50.018 -10.127 -9.796  1.00 15.90 ?  90  LYS   B HA   1 
ATOM   5185 H  HB2  . LYS   B 1 90  ? 48.437 -9.891  -11.441 1.00 17.72 ?  90  LYS   B HB2  1 
ATOM   5186 H  HB3  . LYS   B 1 90  ? 47.305 -10.449 -10.482 1.00 17.72 ?  90  LYS   B HB3  1 
ATOM   5187 H  HG2  . LYS   B 1 90  ? 47.095 -8.155  -10.692 1.00 18.15 ?  90  LYS   B HG2  1 
ATOM   5188 H  HG3  . LYS   B 1 90  ? 47.451 -8.508  -9.186  1.00 18.15 ?  90  LYS   B HG3  1 
ATOM   5189 H  HD2  . LYS   B 1 90  ? 49.633 -7.841  -9.517  1.00 20.25 ?  90  LYS   B HD2  1 
ATOM   5190 H  HD3  . LYS   B 1 90  ? 49.336 -7.577  -11.065 1.00 20.25 ?  90  LYS   B HD3  1 
ATOM   5191 H  HE2  . LYS   B 1 90  ? 47.857 -5.886  -10.511 1.00 22.25 ?  90  LYS   B HE2  1 
ATOM   5192 H  HE3  . LYS   B 1 90  ? 48.077 -6.177  -8.962  1.00 22.25 ?  90  LYS   B HE3  1 
ATOM   5193 H  HZ1  . LYS   B 1 90  ? 49.308 -4.399  -9.620  1.00 21.79 ?  90  LYS   B HZ1  1 
ATOM   5194 H  HZ2  . LYS   B 1 90  ? 50.208 -5.454  -9.202  1.00 21.79 ?  90  LYS   B HZ2  1 
ATOM   5195 H  HZ3  . LYS   B 1 90  ? 50.008 -5.189  -10.612 1.00 21.79 ?  90  LYS   B HZ3  1 
ATOM   5196 N  N    . HIS   B 1 91  ? 47.876 -11.340 -7.737  1.00 11.80 ?  91  HIS   B N    1 
ATOM   5197 C  CA   . HIS   B 1 91  ? 47.396 -11.365 -6.369  1.00 11.68 ?  91  HIS   B CA   1 
ATOM   5198 C  C    . HIS   B 1 91  ? 47.391 -12.791 -5.847  1.00 10.95 ?  91  HIS   B C    1 
ATOM   5199 O  O    . HIS   B 1 91  ? 47.160 -13.747 -6.599  1.00 11.93 ?  91  HIS   B O    1 
ATOM   5200 C  CB   . HIS   B 1 91  ? 45.942 -10.880 -6.265  1.00 13.40 ?  91  HIS   B CB   1 
ATOM   5201 C  CG   . HIS   B 1 91  ? 45.742 -9.458  -6.668  1.00 16.35 ?  91  HIS   B CG   1 
ATOM   5202 N  ND1  . HIS   B 1 91  ? 46.359 -8.401  -6.031  1.00 18.59 ?  91  HIS   B ND1  1 
ATOM   5203 C  CD2  . HIS   B 1 91  ? 44.962 -8.914  -7.629  1.00 18.56 ?  91  HIS   B CD2  1 
ATOM   5204 C  CE1  . HIS   B 1 91  ? 45.981 -7.267  -6.595  1.00 19.52 ?  91  HIS   B CE1  1 
ATOM   5205 N  NE2  . HIS   B 1 91  ? 45.131 -7.551  -7.566  1.00 19.97 ?  91  HIS   B NE2  1 
ATOM   5206 H  H    . HIS   B 1 91  ? 47.468 -11.902 -8.247  1.00 14.12 ?  91  HIS   B H    1 
ATOM   5207 H  HA   . HIS   B 1 91  ? 47.963 -10.808 -5.802  1.00 13.98 ?  91  HIS   B HA   1 
ATOM   5208 H  HB2  . HIS   B 1 91  ? 45.388 -11.430 -6.840  1.00 16.05 ?  91  HIS   B HB2  1 
ATOM   5209 H  HB3  . HIS   B 1 91  ? 45.646 -10.970 -5.344  1.00 16.05 ?  91  HIS   B HB3  1 
ATOM   5210 H  HD2  . HIS   B 1 91  ? 44.420 -9.371  -8.231  1.00 22.23 ?  91  HIS   B HD2  1 
ATOM   5211 H  HE1  . HIS   B 1 91  ? 46.262 -6.417  -6.343  1.00 23.39 ?  91  HIS   B HE1  1 
ATOM   5212 H  HE2  . HIS   B 1 91  ? 44.754 -6.971  -8.078  1.00 23.93 ?  91  HIS   B HE2  1 
ATOM   5213 N  N    . CYS   B 1 92  ? 47.569 -12.919 -4.543  1.00 10.90 ?  92  CYS   B N    1 
ATOM   5214 C  CA   . CYS   B 1 92  ? 47.262 -14.154 -3.832  1.00 11.07 ?  92  CYS   B CA   1 
ATOM   5215 C  C    . CYS   B 1 92  ? 46.038 -13.912 -2.958  1.00 10.56 ?  92  CYS   B C    1 
ATOM   5216 O  O    . CYS   B 1 92  ? 46.034 -13.003 -2.118  1.00 11.68 ?  92  CYS   B O    1 
ATOM   5217 C  CB   . CYS   B 1 92  ? 48.435 -14.616 -2.972  1.00 11.57 ?  92  CYS   B CB   1 
ATOM   5218 S  SG   . CYS   B 1 92  ? 48.074 -16.153 -2.073  1.00 11.37 ?  92  CYS   B SG   1 
ATOM   5219 H  H    . CYS   B 1 92  ? 47.891 -12.299 -4.036  1.00 13.04 ?  92  CYS   B H    1 
ATOM   5220 H  HA   . CYS   B 1 92  ? 47.063 -14.852 -4.477  1.00 13.24 ?  92  CYS   B HA   1 
ATOM   5221 H  HB2  . CYS   B 1 92  ? 49.204 -14.768 -3.540  1.00 13.84 ?  92  CYS   B HB2  1 
ATOM   5222 H  HB3  . CYS   B 1 92  ? 48.633 -13.924 -2.320  1.00 13.84 ?  92  CYS   B HB3  1 
ATOM   5223 H  HG   . CYS   B 1 92  ? 49.046 -16.467 -1.443  1.00 13.61 ?  92  CYS   B HG   1 
ATOM   5224 N  N    . LEU   B 1 93  ? 45.003 -14.726 -3.163  1.00 10.76 ?  93  LEU   B N    1 
ATOM   5225 C  CA   . LEU   B 1 93  ? 43.827 -14.735 -2.304  1.00 10.57 ?  93  LEU   B CA   1 
ATOM   5226 C  C    . LEU   B 1 93  ? 44.054 -15.796 -1.235  1.00 10.13 ?  93  LEU   B C    1 
ATOM   5227 O  O    . LEU   B 1 93  ? 44.005 -16.998 -1.521  1.00 11.13 ?  93  LEU   B O    1 
ATOM   5228 C  CB   . LEU   B 1 93  ? 42.569 -15.024 -3.117  1.00 11.39 ?  93  LEU   B CB   1 
ATOM   5229 C  CG   . LEU   B 1 93  ? 41.271 -15.029 -2.304  1.00 11.97 ?  93  LEU   B CG   1 
ATOM   5230 C  CD1  . LEU   B 1 93  ? 40.912 -13.642 -1.811  1.00 12.76 ?  93  LEU   B CD1  1 
ATOM   5231 C  CD2  . LEU   B 1 93  ? 40.142 -15.632 -3.122  1.00 12.30 ?  93  LEU   B CD2  1 
ATOM   5232 H  H    . LEU   B 1 93  ? 44.963 -15.307 -3.808  1.00 12.87 ?  93  LEU   B H    1 
ATOM   5233 H  HA   . LEU   B 1 93  ? 43.735 -13.874 -1.876  1.00 12.65 ?  93  LEU   B HA   1 
ATOM   5234 H  HB2  . LEU   B 1 93  ? 42.481 -14.337 -3.800  1.00 13.63 ?  93  LEU   B HB2  1 
ATOM   5235 H  HB3  . LEU   B 1 93  ? 42.656 -15.890 -3.533  1.00 13.63 ?  93  LEU   B HB3  1 
ATOM   5236 H  HG   . LEU   B 1 93  ? 41.393 -15.587 -1.524  1.00 14.33 ?  93  LEU   B HG   1 
ATOM   5237 H  HD11 . LEU   B 1 93  ? 40.061 -13.681 -1.350  1.00 15.28 ?  93  LEU   B HD11 1 
ATOM   5238 H  HD12 . LEU   B 1 93  ? 41.604 -13.334 -1.205  1.00 15.28 ?  93  LEU   B HD12 1 
ATOM   5239 H  HD13 . LEU   B 1 93  ? 40.850 -13.042 -2.573  1.00 15.28 ?  93  LEU   B HD13 1 
ATOM   5240 H  HD21 . LEU   B 1 93  ? 39.323 -15.615 -2.597  1.00 14.73 ?  93  LEU   B HD21 1 
ATOM   5241 H  HD22 . LEU   B 1 93  ? 40.021 -15.113 -3.933  1.00 14.73 ?  93  LEU   B HD22 1 
ATOM   5242 H  HD23 . LEU   B 1 93  ? 40.367 -16.548 -3.347  1.00 14.73 ?  93  LEU   B HD23 1 
ATOM   5243 N  N    . HIS   B 1 94  ? 44.328 -15.360 -0.012  1.00 10.15 ?  94  HIS   B N    1 
ATOM   5244 C  CA   . HIS   B 1 94  ? 44.543 -16.266 1.109   1.00 10.63 ?  94  HIS   B CA   1 
ATOM   5245 C  C    . HIS   B 1 94  ? 43.181 -16.613 1.686   1.00 11.30 ?  94  HIS   B C    1 
ATOM   5246 O  O    . HIS   B 1 94  ? 42.507 -15.733 2.226   1.00 12.43 ?  94  HIS   B O    1 
ATOM   5247 C  CB   . HIS   B 1 94  ? 45.418 -15.599 2.167   1.00 11.02 ?  94  HIS   B CB   1 
ATOM   5248 C  CG   . HIS   B 1 94  ? 46.797 -15.292 1.695   1.00 11.16 ?  94  HIS   B CG   1 
ATOM   5249 N  ND1  . HIS   B 1 94  ? 47.825 -16.207 1.771   1.00 11.45 ?  94  HIS   B ND1  1 
ATOM   5250 C  CD2  . HIS   B 1 94  ? 47.303 -14.179 1.112   1.00 11.23 ?  94  HIS   B CD2  1 
ATOM   5251 C  CE1  . HIS   B 1 94  ? 48.915 -15.650 1.271   1.00 11.56 ?  94  HIS   B CE1  1 
ATOM   5252 N  NE2  . HIS   B 1 94  ? 48.627 -14.423 0.864   1.00 11.52 ?  94  HIS   B NE2  1 
ATOM   5253 H  H    . HIS   B 1 94  ? 44.401 -14.524 0.194   1.00 12.14 ?  94  HIS   B H    1 
ATOM   5254 H  HA   . HIS   B 1 94  ? 44.970 -17.076 0.799   1.00 12.72 ?  94  HIS   B HA   1 
ATOM   5255 H  HB2  . HIS   B 1 94  ? 45.003 -14.765 2.433   1.00 13.19 ?  94  HIS   B HB2  1 
ATOM   5256 H  HB3  . HIS   B 1 94  ? 45.490 -16.194 2.926   1.00 13.19 ?  94  HIS   B HB3  1 
ATOM   5257 H  HD2  . HIS   B 1 94  ? 46.842 -13.393 0.924   1.00 13.44 ?  94  HIS   B HD2  1 
ATOM   5258 H  HE1  . HIS   B 1 94  ? 49.746 -16.066 1.207   1.00 13.84 ?  94  HIS   B HE1  1 
ATOM   5259 H  HE2  . HIS   B 1 94  ? 49.180 -13.879 0.501   1.00 13.79 ?  94  HIS   B HE2  1 
ATOM   5260 N  N    . VAL   B 1 95  ? 42.750 -17.868 1.543   1.00 11.03 ?  95  VAL   B N    1 
ATOM   5261 C  CA   . VAL   B 1 95  ? 41.418 -18.302 1.970   1.00 11.06 ?  95  VAL   B CA   1 
ATOM   5262 C  C    . VAL   B 1 95  ? 41.580 -19.337 3.073   1.00 11.20 ?  95  VAL   B C    1 
ATOM   5263 O  O    . VAL   B 1 95  ? 42.350 -20.293 2.921   1.00 12.17 ?  95  VAL   B O    1 
ATOM   5264 C  CB   . VAL   B 1 95  ? 40.601 -18.913 0.813   1.00 11.40 ?  95  VAL   B CB   1 
ATOM   5265 C  CG1  . VAL   B 1 95  ? 39.234 -19.360 1.305   1.00 12.92 ?  95  VAL   B CG1  1 
ATOM   5266 C  CG2  . VAL   B 1 95  ? 40.469 -17.926 -0.322  1.00 11.43 ?  95  VAL   B CG2  1 
ATOM   5267 H  H    . VAL   B 1 95  ? 43.216 -18.497 1.185   1.00 13.20 ?  95  VAL   B H    1 
ATOM   5268 H  HA   . VAL   B 1 95  ? 40.926 -17.548 2.326   1.00 13.23 ?  95  VAL   B HA   1 
ATOM   5269 H  HB   . VAL   B 1 95  ? 41.065 -19.692 0.475   1.00 13.64 ?  95  VAL   B HB   1 
ATOM   5270 H  HG11 . VAL   B 1 95  ? 38.663 -19.539 0.538   1.00 15.47 ?  95  VAL   B HG11 1 
ATOM   5271 H  HG12 . VAL   B 1 95  ? 39.331 -20.173 1.831   1.00 15.47 ?  95  VAL   B HG12 1 
ATOM   5272 H  HG13 . VAL   B 1 95  ? 38.841 -18.660 1.847   1.00 15.47 ?  95  VAL   B HG13 1 
ATOM   5273 H  HG21 . VAL   B 1 95  ? 39.898 -18.313 -1.005  1.00 13.68 ?  95  VAL   B HG21 1 
ATOM   5274 H  HG22 . VAL   B 1 95  ? 40.064 -17.111 0.021   1.00 13.68 ?  95  VAL   B HG22 1 
ATOM   5275 H  HG23 . VAL   B 1 95  ? 41.343 -17.741 -0.679  1.00 13.68 ?  95  VAL   B HG23 1 
ATOM   5276 N  N    . VAL   B 1 96  ? 40.854 -19.156 4.172   1.00 11.72 ?  96  VAL   B N    1 
ATOM   5277 C  CA   . VAL   B 1 96  ? 40.936 -20.065 5.316   1.00 12.11 ?  96  VAL   B CA   1 
ATOM   5278 C  C    . VAL   B 1 96  ? 39.750 -21.027 5.275   1.00 12.93 ?  96  VAL   B C    1 
ATOM   5279 O  O    . VAL   B 1 96  ? 38.635 -20.675 5.669   1.00 13.72 ?  96  VAL   B O    1 
ATOM   5280 C  CB   . VAL   B 1 96  ? 40.986 -19.312 6.650   1.00 13.00 ?  96  VAL   B CB   1 
ATOM   5281 C  CG1  . VAL   B 1 96  ? 41.142 -20.301 7.797   1.00 13.88 ?  96  VAL   B CG1  1 
ATOM   5282 C  CG2  . VAL   B 1 96  ? 42.112 -18.287 6.662   1.00 13.87 ?  96  VAL   B CG2  1 
ATOM   5283 H  H    . VAL   B 1 96  ? 40.300 -18.507 4.286   1.00 14.03 ?  96  VAL   B H    1 
ATOM   5284 H  HA   . VAL   B 1 96  ? 41.749 -20.589 5.246   1.00 14.49 ?  96  VAL   B HA   1 
ATOM   5285 H  HB   . VAL   B 1 96  ? 40.150 -18.838 6.779   1.00 15.56 ?  96  VAL   B HB   1 
ATOM   5286 H  HG11 . VAL   B 1 96  ? 41.348 -19.814 8.612   1.00 16.62 ?  96  VAL   B HG11 1 
ATOM   5287 H  HG12 . VAL   B 1 96  ? 40.314 -20.794 7.911   1.00 16.62 ?  96  VAL   B HG12 1 
ATOM   5288 H  HG13 . VAL   B 1 96  ? 41.867 -20.915 7.592   1.00 16.62 ?  96  VAL   B HG13 1 
ATOM   5289 H  HG21 . VAL   B 1 96  ? 42.154 -17.869 7.539   1.00 16.60 ?  96  VAL   B HG21 1 
ATOM   5290 H  HG22 . VAL   B 1 96  ? 42.950 -18.729 6.466   1.00 16.60 ?  96  VAL   B HG22 1 
ATOM   5291 H  HG23 . VAL   B 1 96  ? 41.931 -17.609 5.987   1.00 16.60 ?  96  VAL   B HG23 1 
ATOM   5292 N  N    . GLY   B 1 97  ? 39.980 -22.253 4.808   1.00 13.22 ?  97  GLY   B N    1 
ATOM   5293 C  CA   . GLY   B 1 97  ? 39.026 -23.321 4.993   1.00 14.06 ?  97  GLY   B CA   1 
ATOM   5294 C  C    . GLY   B 1 97  ? 39.191 -23.925 6.369   1.00 15.59 ?  97  GLY   B C    1 
ATOM   5295 O  O    . GLY   B 1 97  ? 40.248 -23.802 7.002   1.00 16.34 ?  97  GLY   B O    1 
ATOM   5296 H  H    . GLY   B 1 97  ? 40.690 -22.477 4.372   1.00 15.83 ?  97  GLY   B H    1 
ATOM   5297 H  HA2  . GLY   B 1 97  ? 38.126 -22.963 4.897   1.00 16.83 ?  97  GLY   B HA2  1 
ATOM   5298 H  HA3  . GLY   B 1 97  ? 39.164 -24.003 4.318   1.00 16.83 ?  97  GLY   B HA3  1 
ATOM   5299 N  N    . PRO   B 1 98  ? 38.153 -24.601 6.858   1.00 16.79 ?  98  PRO   B N    1 
ATOM   5300 C  CA   . PRO   B 1 98  ? 38.267 -25.277 8.155   1.00 17.82 ?  98  PRO   B CA   1 
ATOM   5301 C  C    . PRO   B 1 98  ? 39.279 -26.411 8.106   1.00 17.63 ?  98  PRO   B C    1 
ATOM   5302 O  O    . PRO   B 1 98  ? 39.370 -27.148 7.123   1.00 17.46 ?  98  PRO   B O    1 
ATOM   5303 C  CB   . PRO   B 1 98  ? 36.849 -25.806 8.404   1.00 18.39 ?  98  PRO   B CB   1 
ATOM   5304 C  CG   . PRO   B 1 98  ? 36.240 -25.928 7.055   1.00 18.14 ?  98  PRO   B CG   1 
ATOM   5305 C  CD   . PRO   B 1 98  ? 36.817 -24.779 6.261   1.00 17.05 ?  98  PRO   B CD   1 
ATOM   5306 H  HA   . PRO   B 1 98  ? 38.514 -24.648 8.846   1.00 21.35 ?  98  PRO   B HA   1 
ATOM   5307 H  HB2  . PRO   B 1 98  ? 36.897 -26.672 8.840   1.00 22.02 ?  98  PRO   B HB2  1 
ATOM   5308 H  HB3  . PRO   B 1 98  ? 36.358 -25.173 8.948   1.00 22.02 ?  98  PRO   B HB3  1 
ATOM   5309 H  HG2  . PRO   B 1 98  ? 36.490 -26.780 6.661   1.00 21.73 ?  98  PRO   B HG2  1 
ATOM   5310 H  HG3  . PRO   B 1 98  ? 35.278 -25.850 7.125   1.00 21.73 ?  98  PRO   B HG3  1 
ATOM   5311 H  HD2  . PRO   B 1 98  ? 36.888 -25.026 5.321   1.00 20.42 ?  98  PRO   B HD2  1 
ATOM   5312 H  HD3  . PRO   B 1 98  ? 36.281 -23.983 6.379   1.00 20.42 ?  98  PRO   B HD3  1 
ATOM   5313 N  N    . ASN   B 1 99  ? 40.054 -26.530 9.181   1.00 19.16 ?  99  ASN   B N    1 
ATOM   5314 C  CA   . ASN   B 1 99  ? 41.049 -27.591 9.337   1.00 20.35 ?  99  ASN   B CA   1 
ATOM   5315 C  C    . ASN   B 1 99  ? 40.448 -28.665 10.238  1.00 23.05 ?  99  ASN   B C    1 
ATOM   5316 O  O    . ASN   B 1 99  ? 40.421 -28.518 11.463  1.00 24.10 ?  99  ASN   B O    1 
ATOM   5317 C  CB   . ASN   B 1 99  ? 42.333 -27.023 9.935   1.00 20.46 ?  99  ASN   B CB   1 
ATOM   5318 C  CG   . ASN   B 1 99  ? 43.480 -28.019 9.921   1.00 20.83 ?  99  ASN   B CG   1 
ATOM   5319 O  OD1  . ASN   B 1 99  ? 43.287 -29.205 10.153  1.00 21.41 ?  99  ASN   B OD1  1 
ATOM   5320 N  ND2  . ASN   B 1 99  ? 44.680 -27.537 9.644   1.00 21.09 ?  99  ASN   B ND2  1 
ATOM   5321 H  H    . ASN   B 1 99  ? 40.017 -25.999 9.853   1.00 22.95 ?  99  ASN   B H    1 
ATOM   5322 H  HA   . ASN   B 1 99  ? 41.248 -27.990 8.477   1.00 24.38 ?  99  ASN   B HA   1 
ATOM   5323 H  HB2  . ASN   B 1 99  ? 42.597 -26.249 9.426   1.00 24.51 ?  99  ASN   B HB2  1 
ATOM   5324 H  HB3  . ASN   B 1 99  ? 42.161 -26.777 10.860  1.00 24.51 ?  99  ASN   B HB3  1 
ATOM   5325 H  HD21 . ASN   B 1 99  ? 45.359 -28.056 9.622   1.00 25.26 ?  99  ASN   B HD21 1 
ATOM   5326 H  HD22 . ASN   B 1 99  ? 44.771 -26.694 9.488   1.00 25.26 ?  99  ASN   B HD22 1 
ATOM   5327 N  N    . VAL   B 1 100 ? 39.966 -29.751 9.624   1.00 25.56 ?  100 VAL   B N    1 
ATOM   5328 C  CA   . VAL   B 1 100 ? 39.346 -30.830 10.390  1.00 28.72 ?  100 VAL   B CA   1 
ATOM   5329 C  C    . VAL   B 1 100 ? 40.359 -31.492 11.314  1.00 29.59 ?  100 VAL   B C    1 
ATOM   5330 O  O    . VAL   B 1 100 ? 40.007 -31.958 12.405  1.00 30.46 ?  100 VAL   B O    1 
ATOM   5331 C  CB   . VAL   B 1 100 ? 38.662 -31.837 9.442   1.00 31.06 ?  100 VAL   B CB   1 
ATOM   5332 C  CG1  . VAL   B 1 100 ? 38.207 -33.073 10.203  1.00 31.98 ?  100 VAL   B CG1  1 
ATOM   5333 C  CG2  . VAL   B 1 100 ? 37.477 -31.175 8.748   1.00 31.78 ?  100 VAL   B CG2  1 
ATOM   5334 H  H    . VAL   B 1 100 ? 39.978 -29.881 8.772   1.00 30.64 ?  100 VAL   B H    1 
ATOM   5335 H  HA   . VAL   B 1 100 ? 38.646 -30.451 10.943  1.00 34.43 ?  100 VAL   B HA   1 
ATOM   5336 H  HB   . VAL   B 1 100 ? 39.294 -32.120 8.762   1.00 37.24 ?  100 VAL   B HB   1 
ATOM   5337 H  HG11 . VAL   B 1 100 ? 37.583 -33.572 9.650   1.00 38.34 ?  100 VAL   B HG11 1 
ATOM   5338 H  HG12 . VAL   B 1 100 ? 38.978 -33.625 10.407  1.00 38.34 ?  100 VAL   B HG12 1 
ATOM   5339 H  HG13 . VAL   B 1 100 ? 37.769 -32.795 11.023  1.00 38.34 ?  100 VAL   B HG13 1 
ATOM   5340 H  HG21 . VAL   B 1 100 ? 37.051 -31.822 8.165   1.00 38.10 ?  100 VAL   B HG21 1 
ATOM   5341 H  HG22 . VAL   B 1 100 ? 36.849 -30.871 9.422   1.00 38.10 ?  100 VAL   B HG22 1 
ATOM   5342 H  HG23 . VAL   B 1 100 ? 37.799 -30.422 8.230   1.00 38.10 ?  100 VAL   B HG23 1 
ATOM   5343 N  N    A ASN   B 1 101 ? 41.629 -31.550 10.906  0.70 29.68 ?  101 ASN   B N    1 
ATOM   5344 N  N    B ASN   B 1 101 ? 41.623 -31.562 10.892  0.30 30.40 ?  101 ASN   B N    1 
ATOM   5345 C  CA   A ASN   B 1 101 ? 42.667 -32.074 11.789  0.70 30.54 ?  101 ASN   B CA   1 
ATOM   5346 C  CA   B ASN   B 1 101 ? 42.671 -32.095 11.755  0.30 31.54 ?  101 ASN   B CA   1 
ATOM   5347 C  C    A ASN   B 1 101 ? 42.868 -31.216 13.032  0.70 33.23 ?  101 ASN   B C    1 
ATOM   5348 C  C    B ASN   B 1 101 ? 42.901 -31.236 12.991  0.30 33.75 ?  101 ASN   B C    1 
ATOM   5349 O  O    A ASN   B 1 101 ? 43.526 -31.669 13.978  0.70 33.91 ?  101 ASN   B O    1 
ATOM   5350 O  O    B ASN   B 1 101 ? 43.570 -31.693 13.925  0.30 33.83 ?  101 ASN   B O    1 
ATOM   5351 C  CB   A ASN   B 1 101 ? 43.984 -32.241 11.026  0.70 29.62 ?  101 ASN   B CB   1 
ATOM   5352 C  CB   B ASN   B 1 101 ? 43.975 -32.261 10.968  0.30 30.74 ?  101 ASN   B CB   1 
ATOM   5353 C  CG   A ASN   B 1 101 ? 43.940 -33.393 10.037  0.70 28.64 ?  101 ASN   B CG   1 
ATOM   5354 C  CG   B ASN   B 1 101 ? 43.913 -33.407 9.974   0.30 30.09 ?  101 ASN   B CG   1 
ATOM   5355 O  OD1  A ASN   B 1 101 ? 43.231 -34.373 10.246  0.70 28.98 ?  101 ASN   B OD1  1 
ATOM   5356 O  OD1  B ASN   B 1 101 ? 43.198 -34.386 10.183  0.30 30.05 ?  101 ASN   B OD1  1 
ATOM   5357 N  ND2  A ASN   B 1 101 ? 44.693 -33.274 8.950   0.70 28.11 ?  101 ASN   B ND2  1 
ATOM   5358 N  ND2  B ASN   B 1 101 ? 44.665 -33.289 8.886   0.30 29.74 ?  101 ASN   B ND2  1 
ATOM   5359 H  H    A ASN   B 1 101 ? 41.902 -31.309 10.130  0.70 35.57 ?  101 ASN   B H    1 
ATOM   5360 H  H    B ASN   B 1 101 ? 41.888 -31.317 10.113  0.30 36.45 ?  101 ASN   B H    1 
ATOM   5361 H  HA   A ASN   B 1 101 ? 42.394 -32.953 12.090  0.70 36.62 ?  101 ASN   B HA   1 
ATOM   5362 H  HA   B ASN   B 1 101 ? 42.400 -32.973 12.058  0.30 37.81 ?  101 ASN   B HA   1 
ATOM   5363 H  HB2  A ASN   B 1 101 ? 44.175 -31.430 10.534  0.70 35.51 ?  101 ASN   B HB2  1 
ATOM   5364 H  HB2  B ASN   B 1 101 ? 44.158 -31.448 10.474  0.30 36.85 ?  101 ASN   B HB2  1 
ATOM   5365 H  HB3  A ASN   B 1 101 ? 44.695 -32.421 11.662  0.70 35.51 ?  101 ASN   B HB3  1 
ATOM   5366 H  HB3  B ASN   B 1 101 ? 44.697 -32.444 11.589  0.30 36.85 ?  101 ASN   B HB3  1 
ATOM   5367 H  HD21 A ASN   B 1 101 ? 44.699 -33.900 8.361   0.70 33.69 ?  101 ASN   B HD21 1 
ATOM   5368 H  HD21 B ASN   B 1 101 ? 44.664 -33.913 8.293   0.30 35.65 ?  101 ASN   B HD21 1 
ATOM   5369 H  HD22 A ASN   B 1 101 ? 45.173 -32.571 8.836   0.70 33.69 ?  101 ASN   B HD22 1 
ATOM   5370 H  HD22 B ASN   B 1 101 ? 45.152 -32.590 8.774   0.30 35.65 ?  101 ASN   B HD22 1 
ATOM   5371 N  N    A LYS   B 1 102 ? 42.326 -29.997 13.049  0.70 36.37 ?  102 LYS   B N    1 
ATOM   5372 N  N    B LYS   B 1 102 ? 42.371 -30.013 13.019  0.30 36.18 ?  102 LYS   B N    1 
ATOM   5373 C  CA   A LYS   B 1 102 ? 42.261 -29.165 14.243  0.70 39.65 ?  102 LYS   B CA   1 
ATOM   5374 C  CA   B LYS   B 1 102 ? 42.368 -29.177 14.211  0.30 38.64 ?  102 LYS   B CA   1 
ATOM   5375 C  C    A LYS   B 1 102 ? 40.869 -29.152 14.861  0.70 39.89 ?  102 LYS   B C    1 
ATOM   5376 C  C    B LYS   B 1 102 ? 41.003 -29.136 14.888  0.30 39.30 ?  102 LYS   B C    1 
ATOM   5377 O  O    A LYS   B 1 102 ? 40.596 -28.324 15.736  0.70 39.90 ?  102 LYS   B O    1 
ATOM   5378 O  O    B LYS   B 1 102 ? 40.812 -28.363 15.831  0.30 39.32 ?  102 LYS   B O    1 
ATOM   5379 C  CB   A LYS   B 1 102 ? 42.675 -27.729 13.918  0.70 42.69 ?  102 LYS   B CB   1 
ATOM   5380 C  CB   B LYS   B 1 102 ? 42.825 -27.756 13.869  0.30 40.39 ?  102 LYS   B CB   1 
ATOM   5381 C  CG   A LYS   B 1 102 ? 44.125 -27.549 13.515  0.70 45.45 ?  102 LYS   B CG   1 
ATOM   5382 C  CG   B LYS   B 1 102 ? 44.294 -27.636 13.497  0.30 42.00 ?  102 LYS   B CG   1 
ATOM   5383 C  CD   A LYS   B 1 102 ? 44.373 -26.102 13.127  0.70 47.88 ?  102 LYS   B CD   1 
ATOM   5384 C  CD   B LYS   B 1 102 ? 44.643 -26.202 13.128  0.30 43.47 ?  102 LYS   B CD   1 
ATOM   5385 C  CE   A LYS   B 1 102 ? 45.836 -25.825 12.837  0.70 49.55 ?  102 LYS   B CE   1 
ATOM   5386 C  CE   B LYS   B 1 102 ? 46.130 -26.032 12.867  0.30 44.51 ?  102 LYS   B CE   1 
ATOM   5387 N  NZ   A LYS   B 1 102 ? 46.044 -24.401 12.443  0.70 50.49 ?  102 LYS   B NZ   1 
ATOM   5388 N  NZ   B LYS   B 1 102 ? 46.462 -24.631 12.479  0.30 45.13 ?  102 LYS   B NZ   1 
ATOM   5389 H  H    A LYS   B 1 102 ? 41.974 -29.620 12.360  0.70 43.60 ?  102 LYS   B H    1 
ATOM   5390 H  H    B LYS   B 1 102 ? 41.999 -29.640 12.340  0.30 43.37 ?  102 LYS   B H    1 
ATOM   5391 H  HA   A LYS   B 1 102 ? 42.880 -29.511 14.903  0.70 47.54 ?  102 LYS   B HA   1 
ATOM   5392 H  HA   B LYS   B 1 102 ? 43.001 -29.541 14.846  0.30 46.33 ?  102 LYS   B HA   1 
ATOM   5393 H  HB2  A LYS   B 1 102 ? 42.127 -27.409 13.185  0.70 51.19 ?  102 LYS   B HB2  1 
ATOM   5394 H  HB2  B LYS   B 1 102 ? 42.306 -27.432 13.118  0.30 48.43 ?  102 LYS   B HB2  1 
ATOM   5395 H  HB3  A LYS   B 1 102 ? 42.521 -27.178 14.702  0.70 51.19 ?  102 LYS   B HB3  1 
ATOM   5396 H  HB3  B LYS   B 1 102 ? 42.673 -27.187 14.641  0.30 48.43 ?  102 LYS   B HB3  1 
ATOM   5397 H  HG2  A LYS   B 1 102 ? 44.701 -27.772 14.264  0.70 54.50 ?  102 LYS   B HG2  1 
ATOM   5398 H  HG2  B LYS   B 1 102 ? 44.842 -27.898 14.253  0.30 50.36 ?  102 LYS   B HG2  1 
ATOM   5399 H  HG3  A LYS   B 1 102 ? 44.323 -28.114 12.752  0.70 54.50 ?  102 LYS   B HG3  1 
ATOM   5400 H  HG3  B LYS   B 1 102 ? 44.481 -28.202 12.732  0.30 50.36 ?  102 LYS   B HG3  1 
ATOM   5401 H  HD2  A LYS   B 1 102 ? 43.862 -25.896 12.328  0.70 57.42 ?  102 LYS   B HD2  1 
ATOM   5402 H  HD2  B LYS   B 1 102 ? 44.164 -25.953 12.322  0.30 52.13 ?  102 LYS   B HD2  1 
ATOM   5403 H  HD3  A LYS   B 1 102 ? 44.095 -25.526 13.856  0.70 57.42 ?  102 LYS   B HD3  1 
ATOM   5404 H  HD3  B LYS   B 1 102 ? 44.395 -25.614 13.859  0.30 52.13 ?  102 LYS   B HD3  1 
ATOM   5405 H  HE2  A LYS   B 1 102 ? 46.361 -26.002 13.634  0.70 59.42 ?  102 LYS   B HE2  1 
ATOM   5406 H  HE2  B LYS   B 1 102 ? 46.623 -26.249 13.674  0.30 53.37 ?  102 LYS   B HE2  1 
ATOM   5407 H  HE3  A LYS   B 1 102 ? 46.131 -26.391 12.106  0.70 59.42 ?  102 LYS   B HE3  1 
ATOM   5408 H  HE3  B LYS   B 1 102 ? 46.396 -26.619 12.142  0.30 53.37 ?  102 LYS   B HE3  1 
ATOM   5409 H  HZ1  A LYS   B 1 102 ? 46.905 -24.254 12.276  0.70 60.55 ?  102 LYS   B HZ1  1 
ATOM   5410 H  HZ1  B LYS   B 1 102 ? 47.336 -24.556 12.331  0.30 54.11 ?  102 LYS   B HZ1  1 
ATOM   5411 H  HZ2  A LYS   B 1 102 ? 45.571 -24.216 11.711  0.70 60.55 ?  102 LYS   B HZ2  1 
ATOM   5412 H  HZ2  B LYS   B 1 102 ? 46.023 -24.409 11.737  0.30 54.11 ?  102 LYS   B HZ2  1 
ATOM   5413 H  HZ3  A LYS   B 1 102 ? 45.780 -23.862 13.101  0.70 60.55 ?  102 LYS   B HZ3  1 
ATOM   5414 H  HZ3  B LYS   B 1 102 ? 46.229 -24.072 13.131  0.30 54.11 ?  102 LYS   B HZ3  1 
ATOM   5415 N  N    A GLY   B 1 103 ? 39.979 -30.034 14.413  0.70 40.33 ?  103 GLY   B N    1 
ATOM   5416 N  N    B GLY   B 1 103 ? 40.050 -29.944 14.424  0.30 40.01 ?  103 GLY   B N    1 
ATOM   5417 C  CA   A GLY   B 1 103 ? 38.636 -30.110 14.949  0.70 40.83 ?  103 GLY   B CA   1 
ATOM   5418 C  CA   B GLY   B 1 103 ? 38.736 -30.014 15.030  0.30 40.62 ?  103 GLY   B CA   1 
ATOM   5419 C  C    A GLY   B 1 103 ? 37.692 -29.023 14.492  0.70 40.94 ?  103 GLY   B C    1 
ATOM   5420 C  C    B GLY   B 1 103 ? 37.750 -28.971 14.558  0.30 40.91 ?  103 GLY   B C    1 
ATOM   5421 O  O    A GLY   B 1 103 ? 36.560 -28.965 14.985  0.70 41.29 ?  103 GLY   B O    1 
ATOM   5422 O  O    B GLY   B 1 103 ? 36.642 -28.901 15.102  0.30 41.36 ?  103 GLY   B O    1 
ATOM   5423 H  H    A GLY   B 1 103 ? 40.136 -30.604 13.794  0.70 48.36 ?  103 GLY   B H    1 
ATOM   5424 H  H    B GLY   B 1 103 ? 40.147 -30.466 13.750  0.30 47.97 ?  103 GLY   B H    1 
ATOM   5425 H  HA2  A GLY   B 1 103 ? 38.252 -30.967 14.700  0.70 48.96 ?  103 GLY   B HA2  1 
ATOM   5426 H  HA2  B GLY   B 1 103 ? 38.362 -30.894 14.857  0.30 48.70 ?  103 GLY   B HA2  1 
ATOM   5427 H  HA3  A GLY   B 1 103 ? 38.679 -30.074 15.916  0.70 48.96 ?  103 GLY   B HA3  1 
ATOM   5428 H  HA3  B GLY   B 1 103 ? 38.826 -29.912 15.988  0.30 48.70 ?  103 GLY   B HA3  1 
ATOM   5429 N  N    . GLU   B 1 104 ? 38.111 -28.160 13.569  1.00 40.32 ?  104 GLU   B N    1 
ATOM   5430 C  CA   . GLU   B 1 104 ? 37.241 -27.090 13.105  1.00 38.92 ?  104 GLU   B CA   1 
ATOM   5431 C  C    . GLU   B 1 104 ? 36.062 -27.651 12.310  1.00 38.73 ?  104 GLU   B C    1 
ATOM   5432 O  O    . GLU   B 1 104 ? 36.103 -28.765 11.779  1.00 39.08 ?  104 GLU   B O    1 
ATOM   5433 C  CB   . GLU   B 1 104 ? 38.038 -26.089 12.269  1.00 37.72 ?  104 GLU   B CB   1 
ATOM   5434 C  CG   . GLU   B 1 104 ? 39.151 -25.420 13.065  1.00 36.51 ?  104 GLU   B CG   1 
ATOM   5435 C  CD   . GLU   B 1 104 ? 40.055 -24.531 12.229  1.00 35.28 ?  104 GLU   B CD   1 
ATOM   5436 O  OE1  . GLU   B 1 104 ? 40.040 -24.642 10.986  1.00 33.81 ?  104 GLU   B OE1  1 
ATOM   5437 O  OE2  . GLU   B 1 104 ? 40.791 -23.718 12.827  1.00 35.13 -1 104 GLU   B OE2  1 
ATOM   5438 H  H    A GLU   B 1 104 ? 38.887 -28.172 13.201  0.70 48.35 ?  104 GLU   B H    1 
ATOM   5439 H  H    B GLU   B 1 104 ? 38.863 -28.201 13.156  0.30 48.35 ?  104 GLU   B H    1 
ATOM   5440 H  HA   . GLU   B 1 104 ? 36.885 -26.621 13.874  1.00 46.66 ?  104 GLU   B HA   1 
ATOM   5441 H  HB2  . GLU   B 1 104 ? 38.439 -26.552 11.518  1.00 45.22 ?  104 GLU   B HB2  1 
ATOM   5442 H  HB3  . GLU   B 1 104 ? 37.437 -25.396 11.949  1.00 45.22 ?  104 GLU   B HB3  1 
ATOM   5443 H  HG2  . GLU   B 1 104 ? 38.752 -24.875 13.761  1.00 43.77 ?  104 GLU   B HG2  1 
ATOM   5444 H  HG3  . GLU   B 1 104 ? 39.709 -26.106 13.460  1.00 43.77 ?  104 GLU   B HG3  1 
ATOM   5445 N  N    . ASP   B 1 105 ? 34.998 -26.852 12.233  1.00 37.77 ?  105 ASP   B N    1 
ATOM   5446 C  CA   . ASP   B 1 105 ? 33.728 -27.305 11.681  1.00 37.36 ?  105 ASP   B CA   1 
ATOM   5447 C  C    . ASP   B 1 105 ? 33.795 -27.346 10.160  1.00 34.33 ?  105 ASP   B C    1 
ATOM   5448 O  O    . ASP   B 1 105 ? 33.992 -26.311 9.513   1.00 33.44 ?  105 ASP   B O    1 
ATOM   5449 C  CB   . ASP   B 1 105 ? 32.603 -26.372 12.121  1.00 40.13 ?  105 ASP   B CB   1 
ATOM   5450 C  CG   . ASP   B 1 105 ? 31.238 -26.865 11.690  1.00 42.48 ?  105 ASP   B CG   1 
ATOM   5451 O  OD1  . ASP   B 1 105 ? 31.155 -27.990 11.156  1.00 42.73 ?  105 ASP   B OD1  1 
ATOM   5452 O  OD2  . ASP   B 1 105 ? 30.246 -26.128 11.883  1.00 44.00 -1 105 ASP   B OD2  1 
ATOM   5453 H  H    . ASP   B 1 105 ? 34.988 -26.034 12.500  1.00 45.29 ?  105 ASP   B H    1 
ATOM   5454 H  HA   . ASP   B 1 105 ? 33.533 -28.199 12.004  1.00 44.80 ?  105 ASP   B HA   1 
ATOM   5455 H  HB2  . ASP   B 1 105 ? 32.614 -26.296 13.087  1.00 48.12 ?  105 ASP   B HB2  1 
ATOM   5456 H  HB3  . ASP   B 1 105 ? 32.737 -25.502 11.716  1.00 48.12 ?  105 ASP   B HB3  1 
ATOM   5457 N  N    A ILE   B 1 106 ? 33.603 -28.540 9.593   0.70 33.14 ?  106 ILE   B N    1 
ATOM   5458 N  N    B ILE   B 1 106 ? 33.613 -28.539 9.590   0.30 33.83 ?  106 ILE   B N    1 
ATOM   5459 C  CA   A ILE   B 1 106 ? 33.585 -28.709 8.145   0.70 31.78 ?  106 ILE   B CA   1 
ATOM   5460 C  CA   B ILE   B 1 106 ? 33.638 -28.697 8.141   0.30 33.27 ?  106 ILE   B CA   1 
ATOM   5461 C  C    A ILE   B 1 106 ? 32.500 -27.864 7.487   0.70 30.17 ?  106 ILE   B C    1 
ATOM   5462 C  C    B ILE   B 1 106 ? 32.536 -27.886 7.471   0.30 32.33 ?  106 ILE   B C    1 
ATOM   5463 O  O    A ILE   B 1 106 ? 32.601 -27.549 6.297   0.70 29.39 ?  106 ILE   B O    1 
ATOM   5464 O  O    B ILE   B 1 106 ? 32.613 -27.611 6.268   0.30 32.28 ?  106 ILE   B O    1 
ATOM   5465 C  CB   A ILE   B 1 106 ? 33.442 -30.211 7.801   0.70 32.18 ?  106 ILE   B CB   1 
ATOM   5466 C  CB   B ILE   B 1 106 ? 33.557 -30.197 7.778   0.30 33.64 ?  106 ILE   B CB   1 
ATOM   5467 C  CG1  A ILE   B 1 106 ? 33.658 -30.459 6.305   0.70 32.33 ?  106 ILE   B CG1  1 
ATOM   5468 C  CG1  B ILE   B 1 106 ? 33.806 -30.416 6.283   0.30 33.69 ?  106 ILE   B CG1  1 
ATOM   5469 C  CG2  A ILE   B 1 106 ? 32.077 -30.732 8.234   0.70 32.76 ?  106 ILE   B CG2  1 
ATOM   5470 C  CG2  B ILE   B 1 106 ? 32.207 -30.772 8.183   0.30 33.97 ?  106 ILE   B CG2  1 
ATOM   5471 C  CD1  A ILE   B 1 106 ? 35.025 -30.051 5.814   0.70 32.32 ?  106 ILE   B CD1  1 
ATOM   5472 C  CD1  B ILE   B 1 106 ? 35.140 -29.889 5.803   0.30 33.68 ?  106 ILE   B CD1  1 
ATOM   5473 H  H    A ILE   B 1 106 ? 33.481 -29.269 10.031  0.70 39.73 ?  106 ILE   B H    1 
ATOM   5474 H  H    B ILE   B 1 106 ? 33.472 -29.268 10.022  0.30 40.56 ?  106 ILE   B H    1 
ATOM   5475 H  HA   A ILE   B 1 106 ? 34.434 -28.408 7.794   0.70 38.09 ?  106 ILE   B HA   1 
ATOM   5476 H  HA   B ILE   B 1 106 ? 34.485 -28.359 7.817   0.30 39.88 ?  106 ILE   B HA   1 
ATOM   5477 H  HB   A ILE   B 1 106 ? 34.119 -30.702 8.290   0.70 38.57 ?  106 ILE   B HB   1 
ATOM   5478 H  HB   B ILE   B 1 106 ? 34.245 -30.668 8.271   0.30 40.33 ?  106 ILE   B HB   1 
ATOM   5479 H  HG12 A ILE   B 1 106 ? 33.555 -31.409 6.128   0.70 38.76 ?  106 ILE   B HG12 1 
ATOM   5480 H  HG12 B ILE   B 1 106 ? 33.785 -31.370 6.100   0.30 40.39 ?  106 ILE   B HG12 1 
ATOM   5481 H  HG13 A ILE   B 1 106 ? 32.999 -29.960 5.801   0.70 38.76 ?  106 ILE   B HG13 1 
ATOM   5482 H  HG13 B ILE   B 1 106 ? 33.110 -29.972 5.777   0.30 40.39 ?  106 ILE   B HG13 1 
ATOM   5483 H  HG21 A ILE   B 1 106 ? 32.064 -31.697 8.140   0.70 39.27 ?  106 ILE   B HG21 1 
ATOM   5484 H  HG21 B ILE   B 1 106 ? 32.227 -31.735 8.065   0.30 40.72 ?  106 ILE   B HG21 1 
ATOM   5485 H  HG22 A ILE   B 1 106 ? 31.926 -30.489 9.161   0.70 39.27 ?  106 ILE   B HG22 1 
ATOM   5486 H  HG22 B ILE   B 1 106 ? 32.039 -30.557 9.114   0.30 40.72 ?  106 ILE   B HG22 1 
ATOM   5487 H  HG23 A ILE   B 1 106 ? 31.392 -30.336 7.672   0.70 39.27 ?  106 ILE   B HG23 1 
ATOM   5488 H  HG23 B ILE   B 1 106 ? 31.515 -30.386 7.624   0.30 40.72 ?  106 ILE   B HG23 1 
ATOM   5489 H  HD11 A ILE   B 1 106 ? 35.175 -30.442 4.940   0.70 38.75 ?  106 ILE   B HD11 1 
ATOM   5490 H  HD11 B ILE   B 1 106 ? 35.335 -30.273 4.935   0.30 40.38 ?  106 ILE   B HD11 1 
ATOM   5491 H  HD12 A ILE   B 1 106 ? 35.063 -29.083 5.754   0.70 38.75 ?  106 ILE   B HD12 1 
ATOM   5492 H  HD12 B ILE   B 1 106 ? 35.091 -28.923 5.734   0.30 40.38 ?  106 ILE   B HD12 1 
ATOM   5493 H  HD13 A ILE   B 1 106 ? 35.694 -30.371 6.440   0.70 38.75 ?  106 ILE   B HD13 1 
ATOM   5494 H  HD13 B ILE   B 1 106 ? 35.826 -30.143 6.439   0.30 40.38 ?  106 ILE   B HD13 1 
ATOM   5495 N  N    A GLN   B 1 107 ? 31.463 -27.477 8.236   0.70 29.84 ?  107 GLN   B N    1 
ATOM   5496 N  N    B GLN   B 1 107 ? 31.509 -27.489 8.226   0.30 31.57 ?  107 GLN   B N    1 
ATOM   5497 C  CA   A GLN   B 1 107 ? 30.381 -26.682 7.662   0.70 29.47 ?  107 GLN   B CA   1 
ATOM   5498 C  CA   B GLN   B 1 107 ? 30.412 -26.709 7.662   0.30 30.63 ?  107 GLN   B CA   1 
ATOM   5499 C  C    A GLN   B 1 107 ? 30.860 -25.327 7.160   0.70 26.66 ?  107 GLN   B C    1 
ATOM   5500 C  C    B GLN   B 1 107 ? 30.867 -25.342 7.162   0.30 27.49 ?  107 GLN   B C    1 
ATOM   5501 O  O    A GLN   B 1 107 ? 30.204 -24.739 6.296   0.70 26.69 ?  107 GLN   B O    1 
ATOM   5502 O  O    B GLN   B 1 107 ? 30.195 -24.756 6.307   0.30 27.51 ?  107 GLN   B O    1 
ATOM   5503 C  CB   A GLN   B 1 107 ? 29.265 -26.487 8.692   0.70 32.96 ?  107 GLN   B CB   1 
ATOM   5504 C  CB   B GLN   B 1 107 ? 29.308 -26.550 8.711   0.30 33.04 ?  107 GLN   B CB   1 
ATOM   5505 C  CG   A GLN   B 1 107 ? 27.922 -26.045 8.108   0.70 36.32 ?  107 GLN   B CG   1 
ATOM   5506 C  CG   B GLN   B 1 107 ? 27.952 -26.134 8.154   0.30 35.22 ?  107 GLN   B CG   1 
ATOM   5507 C  CD   A GLN   B 1 107 ? 27.801 -24.536 7.971   0.70 38.88 ?  107 GLN   B CD   1 
ATOM   5508 C  CD   B GLN   B 1 107 ? 27.793 -24.629 8.046   0.30 36.96 ?  107 GLN   B CD   1 
ATOM   5509 O  OE1  A GLN   B 1 107 ? 28.612 -23.784 8.511   0.70 39.83 ?  107 GLN   B OE1  1 
ATOM   5510 O  OE1  B GLN   B 1 107 ? 28.559 -23.866 8.635   0.30 37.57 ?  107 GLN   B OE1  1 
ATOM   5511 N  NE2  A GLN   B 1 107 ? 26.777 -24.087 7.247   0.70 39.81 ?  107 GLN   B NE2  1 
ATOM   5512 N  NE2  B GLN   B 1 107 ? 26.790 -24.194 7.292   0.30 37.58 ?  107 GLN   B NE2  1 
ATOM   5513 H  H    A GLN   B 1 107 ? 31.366 -27.653 9.065   0.70 35.78 ?  107 GLN   B H    1 
ATOM   5514 H  H    B GLN   B 1 107 ? 31.420 -27.667 9.060   0.30 37.85 ?  107 GLN   B H    1 
ATOM   5515 H  HA   A GLN   B 1 107 ? 30.008 -27.160 6.904   0.70 35.32 ?  107 GLN   B HA   1 
ATOM   5516 H  HA   B GLN   B 1 107 ? 30.038 -27.194 6.911   0.30 36.72 ?  107 GLN   B HA   1 
ATOM   5517 H  HB2  A GLN   B 1 107 ? 29.121 -27.325 9.147   0.70 39.52 ?  107 GLN   B HB2  1 
ATOM   5518 H  HB2  B GLN   B 1 107 ? 29.187 -27.398 9.162   0.30 39.60 ?  107 GLN   B HB2  1 
ATOM   5519 H  HB3  A GLN   B 1 107 ? 29.546 -25.810 9.328   0.70 39.52 ?  107 GLN   B HB3  1 
ATOM   5520 H  HB3  B GLN   B 1 107 ? 29.583 -25.877 9.353   0.30 39.60 ?  107 GLN   B HB3  1 
ATOM   5521 H  HG2  A GLN   B 1 107 ? 27.814 -26.433 7.226   0.70 43.54 ?  107 GLN   B HG2  1 
ATOM   5522 H  HG2  B GLN   B 1 107 ? 27.845 -26.510 7.267   0.30 42.23 ?  107 GLN   B HG2  1 
ATOM   5523 H  HG3  A GLN   B 1 107 ? 27.209 -26.353 8.693   0.70 43.54 ?  107 GLN   B HG3  1 
ATOM   5524 H  HG3  B GLN   B 1 107 ? 27.254 -26.471 8.741   0.30 42.23 ?  107 GLN   B HG3  1 
ATOM   5525 H  HE21 A GLN   B 1 107 ? 26.229 -24.643 6.883   0.70 47.74 ?  107 GLN   B HE21 1 
ATOM   5526 H  HE21 B GLN   B 1 107 ? 26.275 -24.757 6.894   0.30 45.06 ?  107 GLN   B HE21 1 
ATOM   5527 H  HE22 A GLN   B 1 107 ? 26.661 -23.241 7.143   0.70 47.74 ?  107 GLN   B HE22 1 
ATOM   5528 H  HE22 B GLN   B 1 107 ? 26.655 -23.350 7.201   0.30 45.06 ?  107 GLN   B HE22 1 
ATOM   5529 N  N    . LEU   B 1 108 ? 31.991 -24.824 7.667   1.00 24.48 ?  108 LEU   B N    1 
ATOM   5530 C  CA   . LEU   B 1 108 ? 32.512 -23.523 7.242   1.00 21.25 ?  108 LEU   B CA   1 
ATOM   5531 C  C    . LEU   B 1 108 ? 33.149 -23.552 5.862   1.00 18.04 ?  108 LEU   B C    1 
ATOM   5532 O  O    . LEU   B 1 108 ? 33.572 -22.497 5.369   1.00 17.19 ?  108 LEU   B O    1 
ATOM   5533 C  CB   . LEU   B 1 108 ? 33.501 -22.993 8.282   1.00 22.08 ?  108 LEU   B CB   1 
ATOM   5534 C  CG   . LEU   B 1 108 ? 32.862 -22.432 9.555   1.00 23.77 ?  108 LEU   B CG   1 
ATOM   5535 C  CD1  . LEU   B 1 108 ? 33.848 -22.454 10.706  1.00 24.61 ?  108 LEU   B CD1  1 
ATOM   5536 C  CD2  . LEU   B 1 108 ? 32.367 -21.013 9.314   1.00 24.24 ?  108 LEU   B CD2  1 
ATOM   5537 H  H    A LEU   B 1 108 ? 32.461 -25.213 8.268   0.70 29.34 ?  108 LEU   B H    1 
ATOM   5538 H  H    B LEU   B 1 108 ? 32.465 -25.207 8.269   0.30 29.34 ?  108 LEU   B H    1 
ATOM   5539 H  HA   . LEU   B 1 108 ? 31.775 -22.901 7.202   1.00 25.46 ?  108 LEU   B HA   1 
ATOM   5540 H  HB2  . LEU   B 1 108 ? 34.086 -23.715 8.551   1.00 26.46 ?  108 LEU   B HB2  1 
ATOM   5541 H  HB3  . LEU   B 1 108 ? 34.017 -22.281 7.881   1.00 26.46 ?  108 LEU   B HB3  1 
ATOM   5542 H  HG   . LEU   B 1 108 ? 32.097 -22.977 9.802   1.00 28.48 ?  108 LEU   B HG   1 
ATOM   5543 H  HD11 . LEU   B 1 108 ? 33.407 -22.128 11.507  1.00 29.50 ?  108 LEU   B HD11 1 
ATOM   5544 H  HD12 . LEU   B 1 108 ? 34.150 -23.365 10.842  1.00 29.50 ?  108 LEU   B HD12 1 
ATOM   5545 H  HD13 . LEU   B 1 108 ? 34.600 -21.883 10.487  1.00 29.50 ?  108 LEU   B HD13 1 
ATOM   5546 H  HD21 . LEU   B 1 108 ? 31.964 -20.674 10.129  1.00 29.05 ?  108 LEU   B HD21 1 
ATOM   5547 H  HD22 . LEU   B 1 108 ? 33.120 -20.455 9.062   1.00 29.05 ?  108 LEU   B HD22 1 
ATOM   5548 H  HD23 . LEU   B 1 108 ? 31.710 -21.024 8.600   1.00 29.05 ?  108 LEU   B HD23 1 
ATOM   5549 N  N    . LEU   B 1 109 ? 33.207 -24.723 5.229   1.00 16.77 ?  109 LEU   B N    1 
ATOM   5550 C  CA   . LEU   B 1 109 ? 33.826 -24.837 3.915   1.00 15.50 ?  109 LEU   B CA   1 
ATOM   5551 C  C    . LEU   B 1 109 ? 33.055 -24.056 2.853   1.00 14.84 ?  109 LEU   B C    1 
ATOM   5552 O  O    . LEU   B 1 109 ? 33.667 -23.476 1.948   1.00 14.48 ?  109 LEU   B O    1 
ATOM   5553 C  CB   . LEU   B 1 109 ? 33.951 -26.314 3.544   1.00 15.62 ?  109 LEU   B CB   1 
ATOM   5554 C  CG   . LEU   B 1 109 ? 34.725 -26.672 2.278   1.00 15.15 ?  109 LEU   B CG   1 
ATOM   5555 C  CD1  . LEU   B 1 109 ? 36.096 -26.012 2.287   1.00 14.82 ?  109 LEU   B CD1  1 
ATOM   5556 C  CD2  . LEU   B 1 109 ? 34.852 -28.190 2.146   1.00 15.70 ?  109 LEU   B CD2  1 
ATOM   5557 H  H    . LEU   B 1 109 ? 32.912 -25.464 5.541   1.00 20.08 ?  109 LEU   B H    1 
ATOM   5558 H  HA   . LEU   B 1 109 ? 34.725 -24.470 3.958   1.00 18.57 ?  109 LEU   B HA   1 
ATOM   5559 H  HB2  . LEU   B 1 109 ? 34.392 -26.775 4.274   1.00 18.70 ?  109 LEU   B HB2  1 
ATOM   5560 H  HB3  . LEU   B 1 109 ? 33.059 -26.675 3.435   1.00 18.70 ?  109 LEU   B HB3  1 
ATOM   5561 H  HG   . LEU   B 1 109 ? 34.238 -26.356 1.500   1.00 18.14 ?  109 LEU   B HG   1 
ATOM   5562 H  HD11 . LEU   B 1 109 ? 36.635 -26.389 1.570   1.00 17.75 ?  109 LEU   B HD11 1 
ATOM   5563 H  HD12 . LEU   B 1 109 ? 35.988 -25.063 2.157   1.00 17.75 ?  109 LEU   B HD12 1 
ATOM   5564 H  HD13 . LEU   B 1 109 ? 36.523 -26.191 3.141   1.00 17.75 ?  109 LEU   B HD13 1 
ATOM   5565 H  HD21 . LEU   B 1 109 ? 35.424 -28.397 1.386   1.00 18.81 ?  109 LEU   B HD21 1 
ATOM   5566 H  HD22 . LEU   B 1 109 ? 35.242 -28.548 2.957   1.00 18.81 ?  109 LEU   B HD22 1 
ATOM   5567 H  HD23 . LEU   B 1 109 ? 33.971 -28.575 2.004   1.00 18.81 ?  109 LEU   B HD23 1 
ATOM   5568 N  N    . LYS   B 1 110 ? 31.719 -24.034 2.929   1.00 14.73 ?  110 LYS   B N    1 
ATOM   5569 C  CA   . LYS   B 1 110 ? 30.965 -23.281 1.932   1.00 14.79 ?  110 LYS   B CA   1 
ATOM   5570 C  C    . LYS   B 1 110 ? 31.295 -21.789 2.020   1.00 14.55 ?  110 LYS   B C    1 
ATOM   5571 O  O    . LYS   B 1 110 ? 31.550 -21.135 1.000   1.00 14.38 ?  110 LYS   B O    1 
ATOM   5572 C  CB   . LYS   B 1 110 ? 29.460 -23.539 2.077   1.00 15.50 ?  110 LYS   B CB   1 
ATOM   5573 C  CG   . LYS   B 1 110 ? 28.645 -22.914 0.945   1.00 15.69 ?  110 LYS   B CG   1 
ATOM   5574 C  CD   . LYS   B 1 110 ? 27.183 -23.352 0.985   1.00 15.75 ?  110 LYS   B CD   1 
ATOM   5575 C  CE   . LYS   B 1 110 ? 26.406 -22.816 -0.210  1.00 16.70 ?  110 LYS   B CE   1 
ATOM   5576 N  NZ   . LYS   B 1 110 ? 26.734 -23.538 -1.470  1.00 17.16 ?  110 LYS   B NZ   1 
ATOM   5577 H  H    . LYS   B 1 110 ? 31.253 -24.439 3.523   1.00 17.63 ?  110 LYS   B H    1 
ATOM   5578 H  HA   . LYS   B 1 110 ? 31.232 -23.585 1.050   1.00 17.71 ?  110 LYS   B HA   1 
ATOM   5579 H  HB2  . LYS   B 1 110 ? 29.305 -24.499 2.066   1.00 18.56 ?  110 LYS   B HB2  1 
ATOM   5580 H  HB3  . LYS   B 1 110 ? 29.155 -23.163 2.914   1.00 18.56 ?  110 LYS   B HB3  1 
ATOM   5581 H  HG2  . LYS   B 1 110 ? 28.670 -21.950 1.029   1.00 18.79 ?  110 LYS   B HG2  1 
ATOM   5582 H  HG3  . LYS   B 1 110 ? 29.016 -23.188 0.093   1.00 18.79 ?  110 LYS   B HG3  1 
ATOM   5583 H  HD2  . LYS   B 1 110 ? 27.137 -24.326 0.968   1.00 18.86 ?  110 LYS   B HD2  1 
ATOM   5584 H  HD3  . LYS   B 1 110 ? 26.767 -23.017 1.797   1.00 18.86 ?  110 LYS   B HD3  1 
ATOM   5585 H  HE2  . LYS   B 1 110 ? 25.457 -22.915 -0.044  1.00 20.01 ?  110 LYS   B HE2  1 
ATOM   5586 H  HE3  . LYS   B 1 110 ? 26.630 -21.881 -0.334  1.00 20.01 ?  110 LYS   B HE3  1 
ATOM   5587 H  HZ1  . LYS   B 1 110 ? 26.266 -23.199 -2.145  1.00 20.56 ?  110 LYS   B HZ1  1 
ATOM   5588 H  HZ2  . LYS   B 1 110 ? 27.602 -23.461 -1.649  1.00 20.56 ?  110 LYS   B HZ2  1 
ATOM   5589 H  HZ3  . LYS   B 1 110 ? 26.534 -24.403 -1.384  1.00 20.56 ?  110 LYS   B HZ3  1 
ATOM   5590 N  N    . SER   B 1 111 ? 31.311 -21.236 3.240   1.00 14.68 ?  111 SER   B N    1 
ATOM   5591 C  CA   . SER   B 1 111 ? 31.705 -19.840 3.422   1.00 14.69 ?  111 SER   B CA   1 
ATOM   5592 C  C    . SER   B 1 111 ? 33.079 -19.578 2.821   1.00 13.99 ?  111 SER   B C    1 
ATOM   5593 O  O    . SER   B 1 111 ? 33.301 -18.543 2.173   1.00 14.49 ?  111 SER   B O    1 
ATOM   5594 C  CB   . SER   B 1 111 ? 31.712 -19.496 4.912   1.00 15.58 ?  111 SER   B CB   1 
ATOM   5595 O  OG   . SER   B 1 111 ? 30.408 -19.481 5.448   1.00 16.97 ?  111 SER   B OG   1 
ATOM   5596 H  H    . SER   B 1 111 ? 31.113 -21.658 3.970   1.00 17.58 ?  111 SER   B H    1 
ATOM   5597 H  HA   . SER   B 1 111 ? 31.063 -19.272 2.983   1.00 17.59 ?  111 SER   B HA   1 
ATOM   5598 H  HB2  . SER   B 1 111 ? 32.233 -20.164 5.392   1.00 18.65 ?  111 SER   B HB2  1 
ATOM   5599 H  HB3  . SER   B 1 111 ? 32.104 -18.623 5.034   1.00 18.65 ?  111 SER   B HB3  1 
ATOM   5600 H  HG   . SER   B 1 111 ? 30.430 -19.293 6.275   1.00 20.33 ?  111 SER   B HG   1 
ATOM   5601 N  N    . ALA   B 1 112 ? 34.019 -20.500 3.031   1.00 14.05 ?  112 ALA   B N    1 
ATOM   5602 C  CA   . ALA   B 1 112 ? 35.361 -20.319 2.488   1.00 13.48 ?  112 ALA   B CA   1 
ATOM   5603 C  C    . ALA   B 1 112 ? 35.331 -20.229 0.963   1.00 13.12 ?  112 ALA   B C    1 
ATOM   5604 O  O    . ALA   B 1 112 ? 35.958 -19.346 0.364   1.00 13.38 ?  112 ALA   B O    1 
ATOM   5605 C  CB   . ALA   B 1 112 ? 36.265 -21.460 2.961   1.00 13.59 ?  112 ALA   B CB   1 
ATOM   5606 H  H    . ALA   B 1 112 ? 33.908 -21.233 3.488   1.00 16.82 ?  112 ALA   B H    1 
ATOM   5607 H  HA   . ALA   B 1 112 ? 35.724 -19.491 2.832   1.00 16.14 ?  112 ALA   B HA   1 
ATOM   5608 H  HB1  . ALA   B 1 112 ? 37.158 -21.322 2.597   1.00 16.27 ?  112 ALA   B HB1  1 
ATOM   5609 H  HB2  . ALA   B 1 112 ? 36.308 -21.451 3.933   1.00 16.27 ?  112 ALA   B HB2  1 
ATOM   5610 H  HB3  . ALA   B 1 112 ? 35.909 -22.303 2.652   1.00 16.27 ?  112 ALA   B HB3  1 
ATOM   5611 N  N    . TYR   B 1 113 ? 34.598 -21.135 0.312   1.00 12.80 ?  113 TYR   B N    1 
ATOM   5612 C  CA   . TYR   B 1 113 ? 34.528 -21.099 -1.144  1.00 12.86 ?  113 TYR   B CA   1 
ATOM   5613 C  C    . TYR   B 1 113 ? 33.815 -19.851 -1.664  1.00 12.85 ?  113 TYR   B C    1 
ATOM   5614 O  O    . TYR   B 1 113 ? 34.088 -19.420 -2.791  1.00 12.95 ?  113 TYR   B O    1 
ATOM   5615 C  CB   . TYR   B 1 113 ? 33.865 -22.365 -1.692  1.00 13.13 ?  113 TYR   B CB   1 
ATOM   5616 C  CG   . TYR   B 1 113 ? 34.828 -23.509 -1.935  1.00 13.20 ?  113 TYR   B CG   1 
ATOM   5617 C  CD1  . TYR   B 1 113 ? 35.827 -23.417 -2.899  1.00 13.91 ?  113 TYR   B CD1  1 
ATOM   5618 C  CD2  . TYR   B 1 113 ? 34.722 -24.690 -1.224  1.00 13.60 ?  113 TYR   B CD2  1 
ATOM   5619 C  CE1  . TYR   B 1 113 ? 36.706 -24.446 -3.129  1.00 13.77 ?  113 TYR   B CE1  1 
ATOM   5620 C  CE2  . TYR   B 1 113 ? 35.598 -25.739 -1.451  1.00 13.96 ?  113 TYR   B CE2  1 
ATOM   5621 C  CZ   . TYR   B 1 113 ? 36.576 -25.616 -2.414  1.00 13.96 ?  113 TYR   B CZ   1 
ATOM   5622 O  OH   . TYR   B 1 113 ? 37.455 -26.636 -2.668  1.00 15.11 ?  113 TYR   B OH   1 
ATOM   5623 H  H    . TYR   B 1 113 ? 34.131 -21.761 0.686   1.00 15.32 ?  113 TYR   B H    1 
ATOM   5624 H  HA   . TYR   B 1 113 ? 35.428 -21.075 -1.481  1.00 15.40 ?  113 TYR   B HA   1 
ATOM   5625 H  HB2  . TYR   B 1 113 ? 33.195 -22.673 -1.058  1.00 15.72 ?  113 TYR   B HB2  1 
ATOM   5626 H  HB3  . TYR   B 1 113 ? 33.434 -22.151 -2.537  1.00 15.72 ?  113 TYR   B HB3  1 
ATOM   5627 H  HD1  . TYR   B 1 113 ? 35.913 -22.627 -3.387  1.00 16.65 ?  113 TYR   B HD1  1 
ATOM   5628 H  HD2  . TYR   B 1 113 ? 34.052 -24.779 -0.588  1.00 16.28 ?  113 TYR   B HD2  1 
ATOM   5629 H  HE1  . TYR   B 1 113 ? 37.366 -24.362 -3.778  1.00 16.49 ?  113 TYR   B HE1  1 
ATOM   5630 H  HE2  . TYR   B 1 113 ? 35.509 -26.533 -0.973  1.00 16.72 ?  113 TYR   B HE2  1 
ATOM   5631 H  HH   . TYR   B 1 113 ? 37.277 -27.298 -2.180  1.00 18.10 ?  113 TYR   B HH   1 
ATOM   5632 N  N    . GLU   B 1 114 ? 32.890 -19.275 -0.886  1.00 13.20 ?  114 GLU   B N    1 
ATOM   5633 C  CA   . GLU   B 1 114 ? 32.203 -18.068 -1.342  1.00 13.24 ?  114 GLU   B CA   1 
ATOM   5634 C  C    . GLU   B 1 114 ? 33.186 -16.944 -1.643  1.00 12.86 ?  114 GLU   B C    1 
ATOM   5635 O  O    . GLU   B 1 114 ? 32.906 -16.090 -2.487  1.00 13.19 ?  114 GLU   B O    1 
ATOM   5636 C  CB   . GLU   B 1 114 ? 31.145 -17.640 -0.323  1.00 13.63 ?  114 GLU   B CB   1 
ATOM   5637 C  CG   . GLU   B 1 114 ? 29.925 -18.557 -0.402  1.00 13.98 ?  114 GLU   B CG   1 
ATOM   5638 C  CD   . GLU   B 1 114 ? 28.907 -18.380 0.712   1.00 13.80 ?  114 GLU   B CD   1 
ATOM   5639 O  OE1  . GLU   B 1 114 ? 29.192 -17.758 1.756   1.00 14.15 ?  114 GLU   B OE1  1 
ATOM   5640 O  OE2  . GLU   B 1 114 ? 27.788 -18.921 0.551   1.00 15.01 -1 114 GLU   B OE2  1 
ATOM   5641 H  H    . GLU   B 1 114 ? 32.638 -19.571 -0.115  1.00 15.80 ?  114 GLU   B H    1 
ATOM   5642 H  HA   . GLU   B 1 114 ? 31.739 -18.272 -2.164  1.00 15.85 ?  114 GLU   B HA   1 
ATOM   5643 H  HB2  . GLU   B 1 114 ? 31.511 -17.700 0.575   1.00 16.32 ?  114 GLU   B HB2  1 
ATOM   5644 H  HB3  . GLU   B 1 114 ? 30.857 -16.736 -0.512  1.00 16.32 ?  114 GLU   B HB3  1 
ATOM   5645 H  HG2  . GLU   B 1 114 ? 29.470 -18.391 -1.239  1.00 16.74 ?  114 GLU   B HG2  1 
ATOM   5646 H  HG3  . GLU   B 1 114 ? 30.229 -19.478 -0.371  1.00 16.74 ?  114 GLU   B HG3  1 
ATOM   5647 N  N    . ASN   B 1 115 ? 34.357 -16.937 -0.999  1.00 12.74 ?  115 ASN   B N    1 
ATOM   5648 C  CA   . ASN   B 1 115 ? 35.344 -15.900 -1.305  1.00 12.50 ?  115 ASN   B CA   1 
ATOM   5649 C  C    . ASN   B 1 115 ? 35.750 -15.927 -2.773  1.00 12.32 ?  115 ASN   B C    1 
ATOM   5650 O  O    . ASN   B 1 115 ? 36.135 -14.887 -3.329  1.00 12.85 ?  115 ASN   B O    1 
ATOM   5651 C  CB   . ASN   B 1 115 ? 36.581 -16.068 -0.420  1.00 13.14 ?  115 ASN   B CB   1 
ATOM   5652 C  CG   . ASN   B 1 115 ? 36.306 -15.807 1.047   1.00 13.70 ?  115 ASN   B CG   1 
ATOM   5653 O  OD1  . ASN   B 1 115 ? 36.312 -14.662 1.498   1.00 15.51 ?  115 ASN   B OD1  1 
ATOM   5654 N  ND2  . ASN   B 1 115 ? 36.131 -16.874 1.815   1.00 13.81 ?  115 ASN   B ND2  1 
ATOM   5655 H  H    . ASN   B 1 115 ? 34.599 -17.499 -0.387  1.00 15.25 ?  115 ASN   B H    1 
ATOM   5656 H  HA   . ASN   B 1 115 ? 34.960 -15.031 -1.117  1.00 14.96 ?  115 ASN   B HA   1 
ATOM   5657 H  HB2  . ASN   B 1 115 ? 36.913 -16.976 -0.511  1.00 15.73 ?  115 ASN   B HB2  1 
ATOM   5658 H  HB3  . ASN   B 1 115 ? 37.262 -15.440 -0.712  1.00 15.73 ?  115 ASN   B HB3  1 
ATOM   5659 H  HD21 . ASN   B 1 115 ? 35.982 -16.777 2.657   1.00 16.54 ?  115 ASN   B HD21 1 
ATOM   5660 H  HD22 . ASN   B 1 115 ? 36.147 -17.662 1.471   1.00 16.54 ?  115 ASN   B HD22 1 
ATOM   5661 N  N    . PHE   B 1 116 ? 35.735 -17.109 -3.401  1.00 12.24 ?  116 PHE   B N    1 
ATOM   5662 C  CA   . PHE   B 1 116 ? 36.159 -17.203 -4.793  1.00 12.65 ?  116 PHE   B CA   1 
ATOM   5663 C  C    . PHE   B 1 116 ? 35.255 -16.375 -5.698  1.00 12.25 ?  116 PHE   B C    1 
ATOM   5664 O  O    . PHE   B 1 116 ? 35.685 -15.947 -6.774  1.00 12.83 ?  116 PHE   B O    1 
ATOM   5665 C  CB   . PHE   B 1 116 ? 36.126 -18.648 -5.314  1.00 12.02 ?  116 PHE   B CB   1 
ATOM   5666 C  CG   . PHE   B 1 116 ? 37.188 -19.602 -4.756  1.00 12.01 ?  116 PHE   B CG   1 
ATOM   5667 C  CD1  . PHE   B 1 116 ? 37.830 -19.418 -3.538  1.00 12.63 ?  116 PHE   B CD1  1 
ATOM   5668 C  CD2  . PHE   B 1 116 ? 37.497 -20.741 -5.489  1.00 12.26 ?  116 PHE   B CD2  1 
ATOM   5669 C  CE1  . PHE   B 1 116 ? 38.759 -20.361 -3.079  1.00 12.79 ?  116 PHE   B CE1  1 
ATOM   5670 C  CE2  . PHE   B 1 116 ? 38.422 -21.672 -5.037  1.00 12.28 ?  116 PHE   B CE2  1 
ATOM   5671 C  CZ   . PHE   B 1 116 ? 39.045 -21.489 -3.835  1.00 12.23 ?  116 PHE   B CZ   1 
ATOM   5672 H  H    . PHE   B 1 116 ? 35.483 -17.854 -3.050  1.00 14.65 ?  116 PHE   B H    1 
ATOM   5673 H  HA   . PHE   B 1 116 ? 37.063 -16.871 -4.876  1.00 15.14 ?  116 PHE   B HA   1 
ATOM   5674 H  HB2  . PHE   B 1 116 ? 35.252 -19.026 -5.104  1.00 14.39 ?  116 PHE   B HB2  1 
ATOM   5675 H  HB3  . PHE   B 1 116 ? 36.234 -18.626 -6.278  1.00 14.39 ?  116 PHE   B HB3  1 
ATOM   5676 H  HD1  . PHE   B 1 116 ? 37.623 -18.671 -3.017  1.00 15.12 ?  116 PHE   B HD1  1 
ATOM   5677 H  HD2  . PHE   B 1 116 ? 37.069 -20.890 -6.304  1.00 14.68 ?  116 PHE   B HD2  1 
ATOM   5678 H  HE1  . PHE   B 1 116 ? 39.183 -20.224 -2.262  1.00 15.31 ?  116 PHE   B HE1  1 
ATOM   5679 H  HE2  . PHE   B 1 116 ? 38.614 -22.423 -5.551  1.00 14.70 ?  116 PHE   B HE2  1 
ATOM   5680 H  HZ   . PHE   B 1 116 ? 39.671 -22.097 -3.534  1.00 14.64 ?  116 PHE   B HZ   1 
ATOM   5681 N  N    . ASN   B 1 117 ? 33.990 -16.171 -5.306  1.00 12.79 ?  117 ASN   B N    1 
ATOM   5682 C  CA   . ASN   B 1 117 ? 33.043 -15.470 -6.173  1.00 13.21 ?  117 ASN   B CA   1 
ATOM   5683 C  C    . ASN   B 1 117 ? 33.355 -13.991 -6.326  1.00 13.59 ?  117 ASN   B C    1 
ATOM   5684 O  O    . ASN   B 1 117 ? 32.748 -13.337 -7.179  1.00 14.64 ?  117 ASN   B O    1 
ATOM   5685 C  CB   . ASN   B 1 117 ? 31.621 -15.692 -5.680  1.00 13.55 ?  117 ASN   B CB   1 
ATOM   5686 C  CG   . ASN   B 1 117 ? 31.174 -17.098 -5.930  1.00 13.81 ?  117 ASN   B CG   1 
ATOM   5687 O  OD1  . ASN   B 1 117 ? 31.531 -17.687 -6.951  1.00 14.45 ?  117 ASN   B OD1  1 
ATOM   5688 N  ND2  . ASN   B 1 117 ? 30.435 -17.669 -4.994  1.00 13.45 ?  117 ASN   B ND2  1 
ATOM   5689 H  H    . ASN   B 1 117 ? 33.666 -16.422 -4.546  1.00 15.32 ?  117 ASN   B H    1 
ATOM   5690 H  HA   . ASN   B 1 117 ? 33.103 -15.867 -7.050  1.00 15.81 ?  117 ASN   B HA   1 
ATOM   5691 H  HB2  . ASN   B 1 117 ? 31.579 -15.526 -4.722  1.00 16.23 ?  117 ASN   B HB2  1 
ATOM   5692 H  HB3  . ASN   B 1 117 ? 31.023 -15.086 -6.147  1.00 16.23 ?  117 ASN   B HB3  1 
ATOM   5693 H  HD21 . ASN   B 1 117 ? 30.153 -18.475 -5.099  1.00 16.10 ?  117 ASN   B HD21 1 
ATOM   5694 H  HD22 . ASN   B 1 117 ? 30.211 -17.226 -4.290  1.00 16.10 ?  117 ASN   B HD22 1 
ATOM   5695 N  N    . GLN   B 1 118 ? 34.294 -13.468 -5.550  1.00 13.26 ?  118 GLN   B N    1 
ATOM   5696 C  CA   . GLN   B 1 118 ? 34.724 -12.082 -5.685  1.00 13.74 ?  118 GLN   B CA   1 
ATOM   5697 C  C    . GLN   B 1 118 ? 35.792 -11.888 -6.758  1.00 13.81 ?  118 GLN   B C    1 
ATOM   5698 O  O    . GLN   B 1 118 ? 36.267 -10.758 -6.936  1.00 15.14 ?  118 GLN   B O    1 
ATOM   5699 C  CB   . GLN   B 1 118 ? 35.195 -11.552 -4.324  1.00 14.36 ?  118 GLN   B CB   1 
ATOM   5700 C  CG   . GLN   B 1 118 ? 34.103 -11.593 -3.258  1.00 14.59 ?  118 GLN   B CG   1 
ATOM   5701 C  CD   . GLN   B 1 118 ? 32.939 -10.684 -3.590  1.00 14.70 ?  118 GLN   B CD   1 
ATOM   5702 O  OE1  . GLN   B 1 118 ? 33.130 -9.547  -4.036  1.00 15.22 ?  118 GLN   B OE1  1 
ATOM   5703 N  NE2  . GLN   B 1 118 ? 31.723 -11.177 -3.385  1.00 15.15 ?  118 GLN   B NE2  1 
ATOM   5704 H  H    . GLN   B 1 118 ? 34.709 -13.895 -4.932  1.00 15.87 ?  118 GLN   B H    1 
ATOM   5705 H  HA   . GLN   B 1 118 ? 33.963 -11.551 -5.956  1.00 16.45 ?  118 GLN   B HA   1 
ATOM   5706 H  HB2  . GLN   B 1 118 ? 35.940 -12.082 -4.013  1.00 17.19 ?  118 GLN   B HB2  1 
ATOM   5707 H  HB3  . GLN   B 1 118 ? 35.469 -10.622 -4.425  1.00 17.19 ?  118 GLN   B HB3  1 
ATOM   5708 H  HG2  . GLN   B 1 118 ? 33.768 -12.505 -3.186  1.00 17.47 ?  118 GLN   B HG2  1 
ATOM   5709 H  HG3  . GLN   B 1 118 ? 34.473 -11.310 -2.409  1.00 17.47 ?  118 GLN   B HG3  1 
ATOM   5710 H  HE21 . GLN   B 1 118 ? 31.626 -11.976 -3.069  1.00 18.15 ?  118 GLN   B HE21 1 
ATOM   5711 H  HE22 . GLN   B 1 118 ? 31.032 -10.701 -3.561  1.00 18.15 ?  118 GLN   B HE22 1 
ATOM   5712 N  N    . HIS   B 1 119 ? 36.144 -12.948 -7.495  1.00 13.31 ?  119 HIS   B N    1 
ATOM   5713 C  CA   . HIS   B 1 119 ? 37.195 -12.898 -8.505  1.00 13.41 ?  119 HIS   B CA   1 
ATOM   5714 C  C    . HIS   B 1 119 ? 36.707 -13.622 -9.747  1.00 13.49 ?  119 HIS   B C    1 
ATOM   5715 O  O    . HIS   B 1 119 ? 36.198 -14.737 -9.650  1.00 14.11 ?  119 HIS   B O    1 
ATOM   5716 C  CB   . HIS   B 1 119 ? 38.469 -13.534 -7.953  1.00 13.40 ?  119 HIS   B CB   1 
ATOM   5717 C  CG   . HIS   B 1 119 ? 38.943 -12.847 -6.719  1.00 14.25 ?  119 HIS   B CG   1 
ATOM   5718 N  ND1  . HIS   B 1 119 ? 39.739 -11.722 -6.758  1.00 15.99 ?  119 HIS   B ND1  1 
ATOM   5719 C  CD2  . HIS   B 1 119 ? 38.648 -13.057 -5.416  1.00 15.54 ?  119 HIS   B CD2  1 
ATOM   5720 C  CE1  . HIS   B 1 119 ? 39.948 -11.297 -5.526  1.00 16.99 ?  119 HIS   B CE1  1 
ATOM   5721 N  NE2  . HIS   B 1 119 ? 39.288 -12.081 -4.693  1.00 17.10 ?  119 HIS   B NE2  1 
ATOM   5722 H  H    . HIS   B 1 119 ? 35.774 -13.726 -7.428  1.00 15.93 ?  119 HIS   B H    1 
ATOM   5723 H  HA   . HIS   B 1 119 ? 37.380 -11.971 -8.734  1.00 16.06 ?  119 HIS   B HA   1 
ATOM   5724 H  HB2  . HIS   B 1 119 ? 38.290 -14.463 -7.738  1.00 16.04 ?  119 HIS   B HB2  1 
ATOM   5725 H  HB3  . HIS   B 1 119 ? 39.167 -13.475 -8.625  1.00 16.04 ?  119 HIS   B HB3  1 
ATOM   5726 H  HD2  . HIS   B 1 119 ? 38.120 -13.741 -5.073  1.00 18.61 ?  119 HIS   B HD2  1 
ATOM   5727 H  HE1  . HIS   B 1 119 ? 40.481 -10.574 -5.284  1.00 20.35 ?  119 HIS   B HE1  1 
ATOM   5728 H  HE2  . HIS   B 1 119 ? 39.296 -12.018 -3.835  1.00 20.49 ?  119 HIS   B HE2  1 
ATOM   5729 N  N    A GLU   B 1 120 ? 36.861 -12.993 -10.912 0.70 13.83 ?  120 GLU   B N    1 
ATOM   5730 N  N    B GLU   B 1 120 ? 36.868 -12.992 -10.913 0.30 14.75 ?  120 GLU   B N    1 
ATOM   5731 C  CA   A GLU   B 1 120 ? 36.278 -13.562 -12.122 0.70 15.67 ?  120 GLU   B CA   1 
ATOM   5732 C  CA   B GLU   B 1 120 ? 36.289 -13.550 -12.132 0.30 16.60 ?  120 GLU   B CA   1 
ATOM   5733 C  C    A GLU   B 1 120 ? 36.950 -14.867 -12.536 0.70 13.96 ?  120 GLU   B C    1 
ATOM   5734 C  C    B GLU   B 1 120 ? 36.956 -14.857 -12.548 0.30 14.89 ?  120 GLU   B C    1 
ATOM   5735 O  O    A GLU   B 1 120 ? 36.285 -15.748 -13.098 0.70 14.42 ?  120 GLU   B O    1 
ATOM   5736 O  O    B GLU   B 1 120 ? 36.296 -15.726 -13.130 0.30 14.96 ?  120 GLU   B O    1 
ATOM   5737 C  CB   A GLU   B 1 120 ? 36.300 -12.540 -13.258 0.70 20.30 ?  120 GLU   B CB   1 
ATOM   5738 C  CB   B GLU   B 1 120 ? 36.345 -12.524 -13.265 0.30 20.58 ?  120 GLU   B CB   1 
ATOM   5739 C  CG   A GLU   B 1 120 ? 35.264 -11.436 -13.092 0.70 26.15 ?  120 GLU   B CG   1 
ATOM   5740 C  CG   B GLU   B 1 120 ? 35.441 -11.319 -13.044 0.30 24.67 ?  120 GLU   B CG   1 
ATOM   5741 C  CD   A GLU   B 1 120 ? 35.141 -10.547 -14.311 0.70 31.06 ?  120 GLU   B CD   1 
ATOM   5742 C  CD   B GLU   B 1 120 ? 35.379 -10.405 -14.253 0.30 28.18 ?  120 GLU   B CD   1 
ATOM   5743 O  OE1  A GLU   B 1 120 ? 36.163 -10.326 -14.997 0.70 32.88 ?  120 GLU   B OE1  1 
ATOM   5744 O  OE1  B GLU   B 1 120 ? 36.278 -10.499 -15.115 0.30 29.52 ?  120 GLU   B OE1  1 
ATOM   5745 O  OE2  A GLU   B 1 120 ? 34.017 -10.072 -14.583 0.70 33.34 -1 120 GLU   B OE2  1 
ATOM   5746 O  OE2  B GLU   B 1 120 ? 34.437 -9.588  -14.337 0.30 29.40 -1 120 GLU   B OE2  1 
ATOM   5747 H  H    A GLU   B 1 120 ? 37.283 -12.245 -11.024 0.70 16.56 ?  120 GLU   B H    1 
ATOM   5748 H  H    B GLU   B 1 120 ? 37.298 -12.251 -11.022 0.30 17.67 ?  120 GLU   B H    1 
ATOM   5749 H  HA   A GLU   B 1 120 ? 35.351 -13.763 -11.940 0.70 18.77 ?  120 GLU   B HA   1 
ATOM   5750 H  HA   B GLU   B 1 120 ? 35.357 -13.742 -11.963 0.30 19.88 ?  120 GLU   B HA   1 
ATOM   5751 H  HB2  A GLU   B 1 120 ? 37.172 -12.119 -13.294 0.70 24.32 ?  120 GLU   B HB2  1 
ATOM   5752 H  HB2  B GLU   B 1 120 ? 37.254 -12.198 -13.352 0.30 24.66 ?  120 GLU   B HB2  1 
ATOM   5753 H  HB3  A GLU   B 1 120 ? 36.116 -12.993 -14.095 0.70 24.32 ?  120 GLU   B HB3  1 
ATOM   5754 H  HB3  B GLU   B 1 120 ? 36.069 -12.954 -14.090 0.30 24.66 ?  120 GLU   B HB3  1 
ATOM   5755 H  HG2  A GLU   B 1 120 ? 34.394 -11.839 -12.935 0.70 31.35 ?  120 GLU   B HG2  1 
ATOM   5756 H  HG2  B GLU   B 1 120 ? 34.544 -11.632 -12.832 0.30 29.57 ?  120 GLU   B HG2  1 
ATOM   5757 H  HG3  A GLU   B 1 120 ? 35.511 -10.876 -12.342 0.70 31.35 ?  120 GLU   B HG3  1 
ATOM   5758 H  HG3  B GLU   B 1 120 ? 35.788 -10.793 -12.309 0.30 29.57 ?  120 GLU   B HG3  1 
ATOM   5759 N  N    . VAL   B 1 121 ? 38.248 -15.016 -12.269 1.00 13.99 ?  121 VAL   B N    1 
ATOM   5760 C  CA   . VAL   B 1 121 ? 38.991 -16.224 -12.628 1.00 13.54 ?  121 VAL   B CA   1 
ATOM   5761 C  C    . VAL   B 1 121 ? 40.107 -16.436 -11.614 1.00 12.77 ?  121 VAL   B C    1 
ATOM   5762 O  O    . VAL   B 1 121 ? 40.787 -15.481 -11.224 1.00 13.46 ?  121 VAL   B O    1 
ATOM   5763 C  CB   . VAL   B 1 121 ? 39.506 -16.162 -14.085 1.00 15.69 ?  121 VAL   B CB   1 
ATOM   5764 C  CG1  . VAL   B 1 121 ? 40.376 -14.930 -14.317 1.00 16.95 ?  121 VAL   B CG1  1 
ATOM   5765 C  CG2  . VAL   B 1 121 ? 40.244 -17.442 -14.458 1.00 17.40 ?  121 VAL   B CG2  1 
ATOM   5766 H  H    A VAL   B 1 121 ? 38.731 -14.420 -11.877 0.70 16.75 ?  121 VAL   B H    1 
ATOM   5767 H  H    B VAL   B 1 121 ? 38.729 -14.424 -11.869 0.30 16.75 ?  121 VAL   B H    1 
ATOM   5768 H  HA   . VAL   B 1 121 ? 38.383 -16.979 -12.569 1.00 16.21 ?  121 VAL   B HA   1 
ATOM   5769 H  HB   . VAL   B 1 121 ? 38.740 -16.089 -14.677 1.00 18.79 ?  121 VAL   B HB   1 
ATOM   5770 H  HG11 . VAL   B 1 121 ? 40.687 -14.931 -15.236 1.00 20.30 ?  121 VAL   B HG11 1 
ATOM   5771 H  HG12 . VAL   B 1 121 ? 39.850 -14.133 -14.147 1.00 20.30 ?  121 VAL   B HG12 1 
ATOM   5772 H  HG13 . VAL   B 1 121 ? 41.135 -14.960 -13.713 1.00 20.30 ?  121 VAL   B HG13 1 
ATOM   5773 H  HG21 . VAL   B 1 121 ? 40.456 -17.420 -15.406 1.00 20.85 ?  121 VAL   B HG21 1 
ATOM   5774 H  HG22 . VAL   B 1 121 ? 41.064 -17.499 -13.941 1.00 20.85 ?  121 VAL   B HG22 1 
ATOM   5775 H  HG23 . VAL   B 1 121 ? 39.677 -18.204 -14.265 1.00 20.85 ?  121 VAL   B HG23 1 
ATOM   5776 N  N    . LEU   B 1 122 ? 40.284 -17.689 -11.182 1.00 12.37 ?  122 LEU   B N    1 
ATOM   5777 C  CA   . LEU   B 1 122 ? 41.260 -18.044 -10.156 1.00 12.05 ?  122 LEU   B CA   1 
ATOM   5778 C  C    . LEU   B 1 122 ? 41.916 -19.375 -10.483 1.00 11.91 ?  122 LEU   B C    1 
ATOM   5779 O  O    . LEU   B 1 122 ? 41.253 -20.298 -10.982 1.00 13.01 ?  122 LEU   B O    1 
ATOM   5780 C  CB   . LEU   B 1 122 ? 40.613 -18.279 -8.777  1.00 13.78 ?  122 LEU   B CB   1 
ATOM   5781 C  CG   . LEU   B 1 122 ? 39.573 -17.269 -8.292  1.00 14.01 ?  122 LEU   B CG   1 
ATOM   5782 C  CD1  . LEU   B 1 122 ? 38.184 -17.639 -8.789  1.00 14.61 ?  122 LEU   B CD1  1 
ATOM   5783 C  CD2  . LEU   B 1 122 ? 39.597 -17.165 -6.782  1.00 13.37 ?  122 LEU   B CD2  1 
ATOM   5784 H  H    . LEU   B 1 122 ? 39.835 -18.370 -11.468 1.00 14.80 ?  122 LEU   B H    1 
ATOM   5785 H  HA   . LEU   B 1 122 ? 41.935 -17.353 -10.074 1.00 14.42 ?  122 LEU   B HA   1 
ATOM   5786 H  HB2  . LEU   B 1 122 ? 40.173 -19.142 -8.793  1.00 16.50 ?  122 LEU   B HB2  1 
ATOM   5787 H  HB3  . LEU   B 1 122 ? 41.315 -18.291 -8.110  1.00 16.50 ?  122 LEU   B HB3  1 
ATOM   5788 H  HG   . LEU   B 1 122 ? 39.792 -16.393 -8.652  1.00 16.77 ?  122 LEU   B HG   1 
ATOM   5789 H  HD11 . LEU   B 1 122 ? 37.539 -17.014 -8.419  1.00 17.50 ?  122 LEU   B HD11 1 
ATOM   5790 H  HD12 . LEU   B 1 122 ? 38.169 -17.585 -9.760  1.00 17.50 ?  122 LEU   B HD12 1 
ATOM   5791 H  HD13 . LEU   B 1 122 ? 37.974 -18.539 -8.505  1.00 17.50 ?  122 LEU   B HD13 1 
ATOM   5792 H  HD21 . LEU   B 1 122 ? 38.910 -16.541 -6.493  1.00 16.00 ?  122 LEU   B HD21 1 
ATOM   5793 H  HD22 . LEU   B 1 122 ? 39.429 -18.040 -6.400  1.00 16.00 ?  122 LEU   B HD22 1 
ATOM   5794 H  HD23 . LEU   B 1 122 ? 40.469 -16.844 -6.500  1.00 16.00 ?  122 LEU   B HD23 1 
ATOM   5795 N  N    . LEU   B 1 123 ? 43.200 -19.492 -10.120 1.00 11.67 ?  123 LEU   B N    1 
ATOM   5796 C  CA   . LEU   B 1 123 ? 43.903 -20.764 -10.002 1.00 11.78 ?  123 LEU   B CA   1 
ATOM   5797 C  C    . LEU   B 1 123 ? 43.879 -21.157 -8.529  1.00 11.42 ?  123 LEU   B C    1 
ATOM   5798 O  O    . LEU   B 1 123 ? 44.233 -20.335 -7.676  1.00 11.92 ?  123 LEU   B O    1 
ATOM   5799 C  CB   . LEU   B 1 123 ? 45.351 -20.592 -10.469 1.00 12.50 ?  123 LEU   B CB   1 
ATOM   5800 C  CG   . LEU   B 1 123 ? 46.292 -21.780 -10.225 1.00 12.67 ?  123 LEU   B CG   1 
ATOM   5801 C  CD1  . LEU   B 1 123 ? 45.857 -23.034 -10.986 1.00 13.30 ?  123 LEU   B CD1  1 
ATOM   5802 C  CD2  . LEU   B 1 123 ? 47.700 -21.387 -10.612 1.00 13.35 ?  123 LEU   B CD2  1 
ATOM   5803 H  H    . LEU   B 1 123 ? 43.693 -18.814 -9.907  1.00 13.97 ?  123 LEU   B H    1 
ATOM   5804 H  HA   . LEU   B 1 123 ? 43.456 -21.447 -10.526 1.00 14.09 ?  123 LEU   B HA   1 
ATOM   5805 H  HB2  . LEU   B 1 123 ? 45.335 -20.424 -11.423 1.00 14.96 ?  123 LEU   B HB2  1 
ATOM   5806 H  HB3  . LEU   B 1 123 ? 45.725 -19.827 -10.010 1.00 14.96 ?  123 LEU   B HB3  1 
ATOM   5807 H  HG   . LEU   B 1 123 ? 46.289 -21.996 -9.279  1.00 15.16 ?  123 LEU   B HG   1 
ATOM   5808 H  HD11 . LEU   B 1 123 ? 46.490 -23.745 -10.803 1.00 15.92 ?  123 LEU   B HD11 1 
ATOM   5809 H  HD12 . LEU   B 1 123 ? 44.970 -23.296 -10.688 1.00 15.92 ?  123 LEU   B HD12 1 
ATOM   5810 H  HD13 . LEU   B 1 123 ? 45.843 -22.837 -11.935 1.00 15.92 ?  123 LEU   B HD13 1 
ATOM   5811 H  HD21 . LEU   B 1 123 ? 48.288 -22.141 -10.460 1.00 15.99 ?  123 LEU   B HD21 1 
ATOM   5812 H  HD22 . LEU   B 1 123 ? 47.710 -21.140 -11.550 1.00 15.99 ?  123 LEU   B HD22 1 
ATOM   5813 H  HD23 . LEU   B 1 123 ? 47.974 -20.633 -10.068 1.00 15.99 ?  123 LEU   B HD23 1 
ATOM   5814 N  N    . ALA   B 1 124 ? 43.445 -22.388 -8.222  1.00 11.00 ?  124 ALA   B N    1 
ATOM   5815 C  CA   . ALA   B 1 124 ? 43.191 -22.712 -6.825  1.00 11.37 ?  124 ALA   B CA   1 
ATOM   5816 C  C    . ALA   B 1 124 ? 43.461 -24.172 -6.492  1.00 10.94 ?  124 ALA   B C    1 
ATOM   5817 O  O    . ALA   B 1 124 ? 43.322 -25.049 -7.356  1.00 11.93 ?  124 ALA   B O    1 
ATOM   5818 C  CB   . ALA   B 1 124 ? 41.735 -22.399 -6.454  1.00 11.99 ?  124 ALA   B CB   1 
ATOM   5819 H  H    . ALA   B 1 124 ? 43.290 -23.031 -8.781  1.00 13.16 ?  124 ALA   B H    1 
ATOM   5820 H  HA   . ALA   B 1 124 ? 43.762 -22.162 -6.275  1.00 13.60 ?  124 ALA   B HA   1 
ATOM   5821 H  HB1  . ALA   B 1 124 ? 41.584 -22.618 -5.520  1.00 14.35 ?  124 ALA   B HB1  1 
ATOM   5822 H  HB2  . ALA   B 1 124 ? 41.569 -21.452 -6.598  1.00 14.35 ?  124 ALA   B HB2  1 
ATOM   5823 H  HB3  . ALA   B 1 124 ? 41.140 -22.924 -7.015  1.00 14.35 ?  124 ALA   B HB3  1 
ATOM   5824 N  N    . PRO   B 1 125 ? 43.762 -24.462 -5.232  1.00 11.40 ?  125 PRO   B N    1 
ATOM   5825 C  CA   . PRO   B 1 125 ? 43.700 -25.829 -4.710  1.00 12.05 ?  125 PRO   B CA   1 
ATOM   5826 C  C    . PRO   B 1 125 ? 42.302 -26.101 -4.152  1.00 12.56 ?  125 PRO   B C    1 
ATOM   5827 O  O    . PRO   B 1 125 ? 41.507 -25.183 -3.947  1.00 12.86 ?  125 PRO   B O    1 
ATOM   5828 C  CB   . PRO   B 1 125 ? 44.694 -25.761 -3.546  1.00 13.09 ?  125 PRO   B CB   1 
ATOM   5829 C  CG   . PRO   B 1 125 ? 44.466 -24.370 -2.983  1.00 12.94 ?  125 PRO   B CG   1 
ATOM   5830 C  CD   . PRO   B 1 125 ? 44.099 -23.494 -4.175  1.00 12.18 ?  125 PRO   B CD   1 
ATOM   5831 H  HA   . PRO   B 1 125 ? 43.970 -26.501 -5.363  1.00 14.42 ?  125 PRO   B HA   1 
ATOM   5832 H  HB2  . PRO   B 1 125 ? 44.481 -26.443 -2.884  1.00 15.67 ?  125 PRO   B HB2  1 
ATOM   5833 H  HB3  . PRO   B 1 125 ? 45.603 -25.866 -3.869  1.00 15.67 ?  125 PRO   B HB3  1 
ATOM   5834 H  HG2  . PRO   B 1 125 ? 43.740 -24.386 -2.342  1.00 15.50 ?  125 PRO   B HG2  1 
ATOM   5835 H  HG3  . PRO   B 1 125 ? 45.283 -24.047 -2.563  1.00 15.50 ?  125 PRO   B HG3  1 
ATOM   5836 H  HD2  . PRO   B 1 125 ? 43.333 -22.944 -3.974  1.00 14.58 ?  125 PRO   B HD2  1 
ATOM   5837 H  HD3  . PRO   B 1 125 ? 44.866 -22.954 -4.444  1.00 14.58 ?  125 PRO   B HD3  1 
ATOM   5838 N  N    . LEU   B 1 126 ? 42.040 -27.373 -3.848  1.00 13.14 ?  126 LEU   B N    1 
ATOM   5839 C  CA   . LEU   B 1 126 ? 40.821 -27.735 -3.134  1.00 13.58 ?  126 LEU   B CA   1 
ATOM   5840 C  C    . LEU   B 1 126 ? 40.942 -27.345 -1.667  1.00 13.94 ?  126 LEU   B C    1 
ATOM   5841 O  O    . LEU   B 1 126 ? 41.838 -27.812 -0.957  1.00 16.21 ?  126 LEU   B O    1 
ATOM   5842 C  CB   . LEU   B 1 126 ? 40.574 -29.232 -3.254  1.00 14.62 ?  126 LEU   B CB   1 
ATOM   5843 C  CG   . LEU   B 1 126 ? 40.040 -29.727 -4.599  1.00 15.63 ?  126 LEU   B CG   1 
ATOM   5844 C  CD1  . LEU   B 1 126 ? 40.069 -31.232 -4.657  1.00 17.18 ?  126 LEU   B CD1  1 
ATOM   5845 C  CD2  . LEU   B 1 126 ? 38.625 -29.220 -4.844  1.00 16.16 ?  126 LEU   B CD2  1 
ATOM   5846 H  H    . LEU   B 1 126 ? 42.561 -28.038 -4.025  1.00 15.73 ?  126 LEU   B H    1 
ATOM   5847 H  HA   . LEU   B 1 126 ? 40.072 -27.259 -3.521  1.00 16.26 ?  126 LEU   B HA   1 
ATOM   5848 H  HB2  . LEU   B 1 126 ? 41.412 -29.689 -3.094  1.00 17.51 ?  126 LEU   B HB2  1 
ATOM   5849 H  HB3  . LEU   B 1 126 ? 39.930 -29.485 -2.579  1.00 17.51 ?  126 LEU   B HB3  1 
ATOM   5850 H  HG   . LEU   B 1 126 ? 40.606 -29.384 -5.311  1.00 18.72 ?  126 LEU   B HG   1 
ATOM   5851 H  HD11 . LEU   B 1 126 ? 39.723 -31.521 -5.517  1.00 20.58 ?  126 LEU   B HD11 1 
ATOM   5852 H  HD12 . LEU   B 1 126 ? 40.981 -31.535 -4.546  1.00 20.58 ?  126 LEU   B HD12 1 
ATOM   5853 H  HD13 . LEU   B 1 126 ? 39.511 -31.584 -3.944  1.00 20.58 ?  126 LEU   B HD13 1 
ATOM   5854 H  HD21 . LEU   B 1 126 ? 38.272 -29.637 -5.647  1.00 19.35 ?  126 LEU   B HD21 1 
ATOM   5855 H  HD22 . LEU   B 1 126 ? 38.068 -29.451 -4.083  1.00 19.35 ?  126 LEU   B HD22 1 
ATOM   5856 H  HD23 . LEU   B 1 126 ? 38.642 -28.255 -4.957  1.00 19.35 ?  126 LEU   B HD23 1 
ATOM   5857 N  N    . LEU   B 1 127 ? 40.013 -26.519 -1.199  1.00 13.66 ?  127 LEU   B N    1 
ATOM   5858 C  CA   . LEU   B 1 127 ? 40.078 -26.028 0.167   1.00 14.21 ?  127 LEU   B CA   1 
ATOM   5859 C  C    . LEU   B 1 127 ? 39.792 -27.142 1.167   1.00 14.17 ?  127 LEU   B C    1 
ATOM   5860 O  O    . LEU   B 1 127 ? 38.971 -28.034 0.935   1.00 14.57 ?  127 LEU   B O    1 
ATOM   5861 C  CB   . LEU   B 1 127 ? 39.077 -24.892 0.382   1.00 14.76 ?  127 LEU   B CB   1 
ATOM   5862 C  CG   . LEU   B 1 127 ? 39.260 -23.634 -0.462  1.00 15.58 ?  127 LEU   B CG   1 
ATOM   5863 C  CD1  . LEU   B 1 127 ? 38.129 -22.661 -0.146  1.00 15.84 ?  127 LEU   B CD1  1 
ATOM   5864 C  CD2  . LEU   B 1 127 ? 40.624 -23.000 -0.231  1.00 16.25 ?  127 LEU   B CD2  1 
ATOM   5865 H  H    . LEU   B 1 127 ? 39.334 -26.221 -1.652  1.00 16.36 ?  127 LEU   B H    1 
ATOM   5866 H  HA   . LEU   B 1 127 ? 40.969 -25.678 0.334   1.00 17.01 ?  127 LEU   B HA   1 
ATOM   5867 H  HB2  . LEU   B 1 127 ? 38.187 -25.241 0.193   1.00 17.67 ?  127 LEU   B HB2  1 
ATOM   5868 H  HB3  . LEU   B 1 127 ? 39.118 -24.628 1.314   1.00 17.67 ?  127 LEU   B HB3  1 
ATOM   5869 H  HG   . LEU   B 1 127 ? 39.189 -23.872 -1.396  1.00 18.66 ?  127 LEU   B HG   1 
ATOM   5870 H  HD11 . LEU   B 1 127 ? 38.254 -21.852 -0.675  1.00 18.97 ?  127 LEU   B HD11 1 
ATOM   5871 H  HD12 . LEU   B 1 127 ? 37.280 -23.068 -0.362  1.00 18.97 ?  127 LEU   B HD12 1 
ATOM   5872 H  HD13 . LEU   B 1 127 ? 38.159 -22.434 0.800   1.00 18.97 ?  127 LEU   B HD13 1 
ATOM   5873 H  HD21 . LEU   B 1 127 ? 40.661 -22.155 -0.697  1.00 19.46 ?  127 LEU   B HD21 1 
ATOM   5874 H  HD22 . LEU   B 1 127 ? 40.750 -22.863 0.722   1.00 19.46 ?  127 LEU   B HD22 1 
ATOM   5875 H  HD23 . LEU   B 1 127 ? 41.308 -23.601 -0.569  1.00 19.46 ?  127 LEU   B HD23 1 
ATOM   5876 N  N    . SER   B 1 128 ? 40.468 -27.055 2.306   1.00 14.25 ?  128 SER   B N    1 
ATOM   5877 C  CA   . SER   B 1 128 ? 40.338 -27.958 3.439   1.00 14.79 ?  128 SER   B CA   1 
ATOM   5878 C  C    . SER   B 1 128 ? 40.814 -29.373 3.130   1.00 16.37 ?  128 SER   B C    1 
ATOM   5879 O  O    . SER   B 1 128 ? 40.705 -30.243 3.992   1.00 17.81 ?  128 SER   B O    1 
ATOM   5880 C  CB   . SER   B 1 128 ? 38.930 -27.947 4.054   1.00 15.05 ?  128 SER   B CB   1 
ATOM   5881 O  OG   . SER   B 1 128 ? 38.643 -26.663 4.606   1.00 15.55 ?  128 SER   B OG   1 
ATOM   5882 H  H    . SER   B 1 128 ? 41.045 -26.431 2.453   1.00 17.06 ?  128 SER   B H    1 
ATOM   5883 H  HA   . SER   B 1 128 ? 40.931 -27.627 4.125   1.00 17.71 ?  128 SER   B HA   1 
ATOM   5884 H  HB2  . SER   B 1 128 ? 38.276 -28.157 3.371   1.00 18.02 ?  128 SER   B HB2  1 
ATOM   5885 H  HB3  . SER   B 1 128 ? 38.891 -28.618 4.764   1.00 18.02 ?  128 SER   B HB3  1 
ATOM   5886 H  HG   . SER   B 1 128 ? 39.211 -26.479 5.202   1.00 18.63 ?  128 SER   B HG   1 
ATOM   5887 N  N    . ALA   B 1 129 ? 41.394 -29.613 1.951   1.00 17.52 ?  129 ALA   B N    1 
ATOM   5888 C  CA   . ALA   B 1 129 ? 41.932 -30.919 1.603   1.00 18.67 ?  129 ALA   B CA   1 
ATOM   5889 C  C    . ALA   B 1 129 ? 43.338 -31.084 2.168   1.00 17.67 ?  129 ALA   B C    1 
ATOM   5890 O  O    . ALA   B 1 129 ? 43.899 -30.181 2.803   1.00 17.50 ?  129 ALA   B O    1 
ATOM   5891 C  CB   . ALA   B 1 129 ? 41.956 -31.095 0.086   1.00 20.41 ?  129 ALA   B CB   1 
ATOM   5892 H  H    . ALA   B 1 129 ? 41.490 -29.029 1.325   1.00 20.99 ?  129 ALA   B H    1 
ATOM   5893 H  HA   . ALA   B 1 129 ? 41.368 -31.611 1.978   1.00 22.36 ?  129 ALA   B HA   1 
ATOM   5894 H  HB1  . ALA   B 1 129 ? 42.305 -31.978 -0.127  1.00 24.45 ?  129 ALA   B HB1  1 
ATOM   5895 H  HB2  . ALA   B 1 129 ? 41.054 -31.007 -0.255  1.00 24.45 ?  129 ALA   B HB2  1 
ATOM   5896 H  HB3  . ALA   B 1 129 ? 42.527 -30.414 -0.303  1.00 24.45 ?  129 ALA   B HB3  1 
ATOM   5897 N  N    . GLY   B 1 130 ? 43.916 -32.257 1.915   1.00 17.48 ?  130 GLY   B N    1 
ATOM   5898 C  CA   . GLY   B 1 130 ? 45.310 -32.477 2.251   1.00 17.60 ?  130 GLY   B CA   1 
ATOM   5899 C  C    . GLY   B 1 130 ? 45.536 -32.400 3.741   1.00 17.52 ?  130 GLY   B C    1 
ATOM   5900 O  O    . GLY   B 1 130 ? 44.835 -33.043 4.535   1.00 18.34 ?  130 GLY   B O    1 
ATOM   5901 H  H    . GLY   B 1 130 ? 43.534 -32.933 1.544   1.00 20.94 ?  130 GLY   B H    1 
ATOM   5902 H  HA2  . GLY   B 1 130 ? 45.593 -33.356 1.945   1.00 21.08 ?  130 GLY   B HA2  1 
ATOM   5903 H  HA3  . GLY   B 1 130 ? 45.867 -31.810 1.817   1.00 21.08 ?  130 GLY   B HA3  1 
ATOM   5904 N  N    . ILE   B 1 131 ? 46.523 -31.582 4.128   1.00 17.75 ?  131 ILE   B N    1 
ATOM   5905 C  CA   . ILE   B 1 131 ? 46.910 -31.460 5.526   1.00 18.76 ?  131 ILE   B CA   1 
ATOM   5906 C  C    . ILE   B 1 131 ? 45.807 -30.862 6.379   1.00 17.96 ?  131 ILE   B C    1 
ATOM   5907 O  O    . ILE   B 1 131 ? 45.896 -30.925 7.607   1.00 19.39 ?  131 ILE   B O    1 
ATOM   5908 C  CB   . ILE   B 1 131 ? 48.233 -30.677 5.699   1.00 20.21 ?  131 ILE   B CB   1 
ATOM   5909 C  CG1  . ILE   B 1 131 ? 48.043 -29.188 5.371   1.00 21.14 ?  131 ILE   B CG1  1 
ATOM   5910 C  CG2  . ILE   B 1 131 ? 49.337 -31.289 4.831   1.00 21.07 ?  131 ILE   B CG2  1 
ATOM   5911 C  CD1  . ILE   B 1 131 ? 49.246 -28.324 5.690   1.00 22.27 ?  131 ILE   B CD1  1 
ATOM   5912 H  H    . ILE   B 1 131 ? 46.981 -31.078 3.605   1.00 21.26 ?  131 ILE   B H    1 
ATOM   5913 H  HA   . ILE   B 1 131 ? 47.067 -32.349 5.873   1.00 22.47 ?  131 ILE   B HA   1 
ATOM   5914 H  HB   . ILE   B 1 131 ? 48.511 -30.745 6.626   1.00 24.22 ?  131 ILE   B HB   1 
ATOM   5915 H  HG12 . ILE   B 1 131 ? 47.854 -29.102 4.424   1.00 25.33 ?  131 ILE   B HG12 1 
ATOM   5916 H  HG13 . ILE   B 1 131 ? 47.295 -28.840 5.884   1.00 25.33 ?  131 ILE   B HG13 1 
ATOM   5917 H  HG21 . ILE   B 1 131 ? 50.182 -30.879 5.060   1.00 25.25 ?  131 ILE   B HG21 1 
ATOM   5918 H  HG22 . ILE   B 1 131 ? 49.370 -32.242 4.997   1.00 25.25 ?  131 ILE   B HG22 1 
ATOM   5919 H  HG23 . ILE   B 1 131 ? 49.127 -31.122 3.898   1.00 25.25 ?  131 ILE   B HG23 1 
ATOM   5920 H  HD11 . ILE   B 1 131 ? 49.013 -27.395 5.537   1.00 26.68 ?  131 ILE   B HD11 1 
ATOM   5921 H  HD12 . ILE   B 1 131 ? 49.487 -28.456 6.621   1.00 26.68 ?  131 ILE   B HD12 1 
ATOM   5922 H  HD13 . ILE   B 1 131 ? 49.980 -28.583 5.116   1.00 26.68 ?  131 ILE   B HD13 1 
ATOM   5923 N  N    . PHE   B 1 132 ? 44.771 -30.284 5.762   1.00 16.99 ?  132 PHE   B N    1 
ATOM   5924 C  CA   . PHE   B 1 132 ? 43.626 -29.772 6.503   1.00 17.53 ?  132 PHE   B CA   1 
ATOM   5925 C  C    . PHE   B 1 132 ? 42.609 -30.859 6.855   1.00 19.05 ?  132 PHE   B C    1 
ATOM   5926 O  O    . PHE   B 1 132 ? 41.726 -30.602 7.678   1.00 20.90 ?  132 PHE   B O    1 
ATOM   5927 C  CB   . PHE   B 1 132 ? 42.930 -28.658 5.711   1.00 16.26 ?  132 PHE   B CB   1 
ATOM   5928 C  CG   . PHE   B 1 132 ? 43.619 -27.308 5.790   1.00 16.10 ?  132 PHE   B CG   1 
ATOM   5929 C  CD1  . PHE   B 1 132 ? 44.916 -27.129 5.334   1.00 17.49 ?  132 PHE   B CD1  1 
ATOM   5930 C  CD2  . PHE   B 1 132 ? 42.933 -26.204 6.279   1.00 16.00 ?  132 PHE   B CD2  1 
ATOM   5931 C  CE1  . PHE   B 1 132 ? 45.529 -25.884 5.401   1.00 17.59 ?  132 PHE   B CE1  1 
ATOM   5932 C  CE2  . PHE   B 1 132 ? 43.537 -24.952 6.340   1.00 16.43 ?  132 PHE   B CE2  1 
ATOM   5933 C  CZ   . PHE   B 1 132 ? 44.831 -24.798 5.900   1.00 17.16 ?  132 PHE   B CZ   1 
ATOM   5934 H  H    . PHE   B 1 132 ? 44.707 -30.184 4.910   1.00 20.36 ?  132 PHE   B H    1 
ATOM   5935 H  HA   . PHE   B 1 132 ? 43.943 -29.387 7.333   1.00 21.00 ?  132 PHE   B HA   1 
ATOM   5936 H  HB2  . PHE   B 1 132 ? 42.901 -28.918 4.779   1.00 19.48 ?  132 PHE   B HB2  1 
ATOM   5937 H  HB3  . PHE   B 1 132 ? 42.026 -28.553 6.052   1.00 19.48 ?  132 PHE   B HB3  1 
ATOM   5938 H  HD1  . PHE   B 1 132 ? 45.387 -27.862 5.004   1.00 20.95 ?  132 PHE   B HD1  1 
ATOM   5939 H  HD2  . PHE   B 1 132 ? 42.054 -26.304 6.581   1.00 19.16 ?  132 PHE   B HD2  1 
ATOM   5940 H  HE1  . PHE   B 1 132 ? 46.402 -25.784 5.103   1.00 21.07 ?  132 PHE   B HE1  1 
ATOM   5941 H  HE2  . PHE   B 1 132 ? 43.067 -24.222 6.682   1.00 19.68 ?  132 PHE   B HE2  1 
ATOM   5942 H  HZ   . PHE   B 1 132 ? 45.241 -23.962 5.946   1.00 20.55 ?  132 PHE   B HZ   1 
ATOM   5943 N  N    . GLY   B 1 133 ? 42.687 -32.047 6.241   1.00 18.40 ?  133 GLY   B N    1 
ATOM   5944 C  CA   . GLY   B 1 133 ? 41.983 -33.216 6.741   1.00 19.63 ?  133 GLY   B CA   1 
ATOM   5945 C  C    . GLY   B 1 133 ? 40.581 -33.476 6.221   1.00 20.50 ?  133 GLY   B C    1 
ATOM   5946 O  O    . GLY   B 1 133 ? 39.989 -34.488 6.610   1.00 22.18 ?  133 GLY   B O    1 
ATOM   5947 H  H    . GLY   B 1 133 ? 43.147 -32.189 5.529   1.00 22.04 ?  133 GLY   B H    1 
ATOM   5948 H  HA2  . GLY   B 1 133 ? 42.519 -33.999 6.539   1.00 23.52 ?  133 GLY   B HA2  1 
ATOM   5949 H  HA3  . GLY   B 1 133 ? 41.927 -33.144 7.708   1.00 23.52 ?  133 GLY   B HA3  1 
ATOM   5950 N  N    . ALA   B 1 134 ? 40.022 -32.621 5.370   1.00 19.48 ?  134 ALA   B N    1 
ATOM   5951 C  CA   . ALA   B 1 134 ? 38.693 -32.915 4.853   1.00 19.29 ?  134 ALA   B CA   1 
ATOM   5952 C  C    . ALA   B 1 134 ? 38.780 -33.878 3.673   1.00 19.20 ?  134 ALA   B C    1 
ATOM   5953 O  O    . ALA   B 1 134 ? 39.828 -34.044 3.046   1.00 20.03 ?  134 ALA   B O    1 
ATOM   5954 C  CB   . ALA   B 1 134 ? 37.978 -31.636 4.424   1.00 19.47 ?  134 ALA   B CB   1 
ATOM   5955 H  H    . ALA   B 1 134 ? 40.376 -31.884 5.095   1.00 23.33 ?  134 ALA   B H    1 
ATOM   5956 H  HA   . ALA   B 1 134 ? 38.168 -33.336 5.555   1.00 23.11 ?  134 ALA   B HA   1 
ATOM   5957 H  HB1  . ALA   B 1 134 ? 37.088 -31.868 4.116   1.00 23.33 ?  134 ALA   B HB1  1 
ATOM   5958 H  HB2  . ALA   B 1 134 ? 37.920 -31.037 5.184   1.00 23.33 ?  134 ALA   B HB2  1 
ATOM   5959 H  HB3  . ALA   B 1 134 ? 38.480 -31.221 3.709   1.00 23.33 ?  134 ALA   B HB3  1 
ATOM   5960 N  N    . ASP   B 1 135 ? 37.653 -34.507 3.376   1.00 19.59 ?  135 ASP   B N    1 
ATOM   5961 C  CA   . ASP   B 1 135 ? 37.561 -35.387 2.223   1.00 20.32 ?  135 ASP   B CA   1 
ATOM   5962 C  C    . ASP   B 1 135 ? 37.643 -34.544 0.956   1.00 18.82 ?  135 ASP   B C    1 
ATOM   5963 O  O    . ASP   B 1 135 ? 36.781 -33.678 0.744   1.00 18.81 ?  135 ASP   B O    1 
ATOM   5964 C  CB   . ASP   B 1 135 ? 36.231 -36.127 2.278   1.00 22.21 ?  135 ASP   B CB   1 
ATOM   5965 C  CG   . ASP   B 1 135 ? 36.075 -37.143 1.164   1.00 24.23 ?  135 ASP   B CG   1 
ATOM   5966 O  OD1  . ASP   B 1 135 ? 36.922 -37.172 0.250   1.00 24.14 ?  135 ASP   B OD1  1 
ATOM   5967 O  OD2  . ASP   B 1 135 ? 35.104 -37.927 1.208   1.00 26.96 -1 135 ASP   B OD2  1 
ATOM   5968 H  H    . ASP   B 1 135 ? 36.927 -34.440 3.831   1.00 23.47 ?  135 ASP   B H    1 
ATOM   5969 H  HA   . ASP   B 1 135 ? 38.287 -36.034 2.247   1.00 24.35 ?  135 ASP   B HA   1 
ATOM   5970 H  HB2  . ASP   B 1 135 ? 36.164 -36.582 3.135   1.00 26.62 ?  135 ASP   B HB2  1 
ATOM   5971 H  HB3  . ASP   B 1 135 ? 35.514 -35.486 2.185   1.00 26.62 ?  135 ASP   B HB3  1 
ATOM   5972 N  N    . PRO   B 1 136 ? 38.642 -34.745 0.096   1.00 18.76 ?  136 PRO   B N    1 
ATOM   5973 C  CA   . PRO   B 1 136 ? 38.718 -33.918 -1.120  1.00 17.93 ?  136 PRO   B CA   1 
ATOM   5974 C  C    . PRO   B 1 136 ? 37.521 -34.079 -2.036  1.00 17.24 ?  136 PRO   B C    1 
ATOM   5975 O  O    . PRO   B 1 136 ? 37.178 -33.133 -2.753  1.00 16.54 ?  136 PRO   B O    1 
ATOM   5976 C  CB   . PRO   B 1 136 ? 40.025 -34.381 -1.780  1.00 18.46 ?  136 PRO   B CB   1 
ATOM   5977 C  CG   . PRO   B 1 136 ? 40.235 -35.772 -1.247  1.00 19.70 ?  136 PRO   B CG   1 
ATOM   5978 C  CD   . PRO   B 1 136 ? 39.738 -35.727 0.164   1.00 19.67 ?  136 PRO   B CD   1 
ATOM   5979 H  HA   . PRO   B 1 136 ? 38.803 -32.984 -0.885  1.00 21.47 ?  136 PRO   B HA   1 
ATOM   5980 H  HB2  . PRO   B 1 136 ? 39.926 -34.396 -2.746  1.00 22.12 ?  136 PRO   B HB2  1 
ATOM   5981 H  HB3  . PRO   B 1 136 ? 40.753 -33.799 -1.516  1.00 22.12 ?  136 PRO   B HB3  1 
ATOM   5982 H  HG2  . PRO   B 1 136 ? 39.718 -36.409 -1.769  1.00 23.60 ?  136 PRO   B HG2  1 
ATOM   5983 H  HG3  . PRO   B 1 136 ? 41.178 -35.999 -1.270  1.00 23.60 ?  136 PRO   B HG3  1 
ATOM   5984 H  HD2  . PRO   B 1 136 ? 39.399 -36.593 0.436   1.00 23.56 ?  136 PRO   B HD2  1 
ATOM   5985 H  HD3  . PRO   B 1 136 ? 40.435 -35.411 0.764   1.00 23.56 ?  136 PRO   B HD3  1 
ATOM   5986 N  N    . ILE   B 1 137 ? 36.873 -35.247 -2.036  1.00 17.67 ?  137 ILE   B N    1 
ATOM   5987 C  CA   . ILE   B 1 137 ? 35.649 -35.425 -2.813  1.00 18.06 ?  137 ILE   B CA   1 
ATOM   5988 C  C    . ILE   B 1 137 ? 34.575 -34.458 -2.327  1.00 17.40 ?  137 ILE   B C    1 
ATOM   5989 O  O    . ILE   B 1 137 ? 33.853 -33.840 -3.125  1.00 17.01 ?  137 ILE   B O    1 
ATOM   5990 C  CB   . ILE   B 1 137 ? 35.183 -36.894 -2.740  1.00 20.39 ?  137 ILE   B CB   1 
ATOM   5991 C  CG1  . ILE   B 1 137 ? 36.172 -37.801 -3.476  1.00 22.43 ?  137 ILE   B CG1  1 
ATOM   5992 C  CG2  . ILE   B 1 137 ? 33.781 -37.046 -3.313  1.00 20.89 ?  137 ILE   B CG2  1 
ATOM   5993 C  CD1  . ILE   B 1 137 ? 35.879 -39.283 -3.326  1.00 24.71 ?  137 ILE   B CD1  1 
ATOM   5994 H  H    . ILE   B 1 137 ? 37.124 -35.949 -1.606  1.00 21.17 ?  137 ILE   B H    1 
ATOM   5995 H  HA   . ILE   B 1 137 ? 35.834 -35.224 -3.745  1.00 21.63 ?  137 ILE   B HA   1 
ATOM   5996 H  HB   . ILE   B 1 137 ? 35.159 -37.163 -1.811  1.00 24.44 ?  137 ILE   B HB   1 
ATOM   5997 H  HG12 . ILE   B 1 137 ? 36.147 -37.598 -4.423  1.00 26.88 ?  137 ILE   B HG12 1 
ATOM   5998 H  HG13 . ILE   B 1 137 ? 37.061 -37.647 -3.127  1.00 26.88 ?  137 ILE   B HG13 1 
ATOM   5999 H  HG21 . ILE   B 1 137 ? 33.550 -37.991 -3.365  1.00 25.03 ?  137 ILE   B HG21 1 
ATOM   6000 H  HG22 . ILE   B 1 137 ? 33.146 -36.600 -2.732  1.00 25.03 ?  137 ILE   B HG22 1 
ATOM   6001 H  HG23 . ILE   B 1 137 ? 33.755 -36.657 -4.199  1.00 25.03 ?  137 ILE   B HG23 1 
ATOM   6002 H  HD11 . ILE   B 1 137 ? 36.582 -39.779 -3.770  1.00 29.61 ?  137 ILE   B HD11 1 
ATOM   6003 H  HD12 . ILE   B 1 137 ? 35.858 -39.511 -2.382  1.00 29.61 ?  137 ILE   B HD12 1 
ATOM   6004 H  HD13 . ILE   B 1 137 ? 35.026 -39.492 -3.737  1.00 29.61 ?  137 ILE   B HD13 1 
ATOM   6005 N  N    . HIS   B 1 138 ? 34.461 -34.305 -1.010  1.00 17.71 ?  138 HIS   B N    1 
ATOM   6006 C  CA   . HIS   B 1 138 ? 33.516 -33.338 -0.463  1.00 17.84 ?  138 HIS   B CA   1 
ATOM   6007 C  C    . HIS   B 1 138 ? 33.919 -31.908 -0.801  1.00 17.12 ?  138 HIS   B C    1 
ATOM   6008 O  O    . HIS   B 1 138 ? 33.063 -31.070 -1.110  1.00 17.84 ?  138 HIS   B O    1 
ATOM   6009 C  CB   . HIS   B 1 138 ? 33.418 -33.513 1.047   1.00 19.06 ?  138 HIS   B CB   1 
ATOM   6010 C  CG   . HIS   B 1 138 ? 32.502 -32.528 1.697   1.00 20.75 ?  138 HIS   B CG   1 
ATOM   6011 N  ND1  . HIS   B 1 138 ? 31.155 -32.472 1.413   1.00 22.22 ?  138 HIS   B ND1  1 
ATOM   6012 C  CD2  . HIS   B 1 138 ? 32.741 -31.542 2.592   1.00 21.35 ?  138 HIS   B CD2  1 
ATOM   6013 C  CE1  . HIS   B 1 138 ? 30.599 -31.504 2.120   1.00 22.63 ?  138 HIS   B CE1  1 
ATOM   6014 N  NE2  . HIS   B 1 138 ? 31.539 -30.927 2.847   1.00 21.87 ?  138 HIS   B NE2  1 
ATOM   6015 H  H    . HIS   B 1 138 ? 34.920 -34.739 -0.424  1.00 21.21 ?  138 HIS   B H    1 
ATOM   6016 H  HA   . HIS   B 1 138 ? 32.643 -33.511 -0.844  1.00 21.37 ?  138 HIS   B HA   1 
ATOM   6017 H  HB2  . HIS   B 1 138 ? 33.083 -34.406 1.241   1.00 22.83 ?  138 HIS   B HB2  1 
ATOM   6018 H  HB3  . HIS   B 1 138 ? 34.300 -33.404 1.436   1.00 22.83 ?  138 HIS   B HB3  1 
ATOM   6019 H  HD1  . HIS   B 1 138 ? 30.741 -32.998 0.869   1.00 26.63 ?  138 HIS   B HD1  1 
ATOM   6020 H  HD2  . HIS   B 1 138 ? 33.558 -31.333 2.979   1.00 25.58 ?  138 HIS   B HD2  1 
ATOM   6021 H  HE1  . HIS   B 1 138 ? 29.696 -31.281 2.112   1.00 27.12 ?  138 HIS   B HE1  1 
ATOM   6022 N  N    . SER   B 1 139 ? 35.212 -31.603 -0.739  1.00 16.34 ?  139 SER   B N    1 
ATOM   6023 C  CA   . SER   B 1 139 ? 35.644 -30.253 -1.061  1.00 15.48 ?  139 SER   B CA   1 
ATOM   6024 C  C    . SER   B 1 139 ? 35.303 -29.910 -2.502  1.00 14.72 ?  139 SER   B C    1 
ATOM   6025 O  O    . SER   B 1 139 ? 34.854 -28.797 -2.789  1.00 14.73 ?  139 SER   B O    1 
ATOM   6026 C  CB   . SER   B 1 139 ? 37.140 -30.116 -0.801  1.00 16.16 ?  139 SER   B CB   1 
ATOM   6027 O  OG   . SER   B 1 139 ? 37.547 -28.784 -1.031  1.00 16.43 ?  139 SER   B OG   1 
ATOM   6028 H  H    . SER   B 1 139 ? 35.843 -32.148 -0.532  1.00 19.57 ?  139 SER   B H    1 
ATOM   6029 H  HA   . SER   B 1 139 ? 35.173 -29.628 -0.492  1.00 18.53 ?  139 SER   B HA   1 
ATOM   6030 H  HB2  . SER   B 1 139 ? 37.321 -30.362 0.122   1.00 19.36 ?  139 SER   B HB2  1 
ATOM   6031 H  HB3  . SER   B 1 139 ? 37.627 -30.694 -1.404  1.00 19.36 ?  139 SER   B HB3  1 
ATOM   6032 H  HG   . SER   B 1 139 ? 38.369 -28.701 -0.859  1.00 19.68 ?  139 SER   B HG   1 
ATOM   6033 N  N    . LEU   B 1 140 ? 35.483 -30.860 -3.420  1.00 14.87 ?  140 LEU   B N    1 
ATOM   6034 C  CA   . LEU   B 1 140 ? 35.119 -30.610 -4.809  1.00 14.55 ?  140 LEU   B CA   1 
ATOM   6035 C  C    . LEU   B 1 140 ? 33.617 -30.382 -4.942  1.00 14.92 ?  140 LEU   B C    1 
ATOM   6036 O  O    . LEU   B 1 140 ? 33.180 -29.497 -5.684  1.00 14.92 ?  140 LEU   B O    1 
ATOM   6037 C  CB   . LEU   B 1 140 ? 35.589 -31.771 -5.689  1.00 14.62 ?  140 LEU   B CB   1 
ATOM   6038 C  CG   . LEU   B 1 140 ? 35.217 -31.664 -7.159  1.00 15.10 ?  140 LEU   B CG   1 
ATOM   6039 C  CD1  . LEU   B 1 140 ? 35.798 -30.394 -7.754  1.00 15.95 ?  140 LEU   B CD1  1 
ATOM   6040 C  CD2  . LEU   B 1 140 ? 35.686 -32.894 -7.903  1.00 16.38 ?  140 LEU   B CD2  1 
ATOM   6041 H  H    . LEU   B 1 140 ? 35.815 -31.635 -3.272  1.00 17.80 ?  140 LEU   B H    1 
ATOM   6042 H  HA   . LEU   B 1 140 ? 35.570 -29.809 -5.118  1.00 17.43 ?  140 LEU   B HA   1 
ATOM   6043 H  HB2  . LEU   B 1 140 ? 36.560 -31.827 -5.641  1.00 17.51 ?  140 LEU   B HB2  1 
ATOM   6044 H  HB3  . LEU   B 1 140 ? 35.203 -32.595 -5.356  1.00 17.51 ?  140 LEU   B HB3  1 
ATOM   6045 H  HG   . LEU   B 1 140 ? 34.253 -31.609 -7.239  1.00 18.08 ?  140 LEU   B HG   1 
ATOM   6046 H  HD11 . LEU   B 1 140 ? 35.691 -30.420 -8.716  1.00 19.10 ?  140 LEU   B HD11 1 
ATOM   6047 H  HD12 . LEU   B 1 140 ? 35.327 -29.627 -7.389  1.00 19.10 ?  140 LEU   B HD12 1 
ATOM   6048 H  HD13 . LEU   B 1 140 ? 36.740 -30.342 -7.526  1.00 19.10 ?  140 LEU   B HD13 1 
ATOM   6049 H  HD21 . LEU   B 1 140 ? 35.438 -32.806 -8.837  1.00 19.62 ?  140 LEU   B HD21 1 
ATOM   6050 H  HD22 . LEU   B 1 140 ? 36.645 -32.966 -7.817  1.00 19.62 ?  140 LEU   B HD22 1 
ATOM   6051 H  HD23 . LEU   B 1 140 ? 35.253 -33.670 -7.517  1.00 19.62 ?  140 LEU   B HD23 1 
ATOM   6052 N  N    . ARG   B 1 141 ? 32.814 -31.169 -4.217  1.00 15.31 ?  141 ARG   B N    1 
ATOM   6053 C  CA   . ARG   B 1 141 ? 31.365 -30.993 -4.203  1.00 16.15 ?  141 ARG   B CA   1 
ATOM   6054 C  C    . ARG   B 1 141 ? 30.989 -29.580 -3.781  1.00 15.84 ?  141 ARG   B C    1 
ATOM   6055 O  O    . ARG   B 1 141 ? 30.186 -28.907 -4.443  1.00 16.26 ?  141 ARG   B O    1 
ATOM   6056 C  CB   . ARG   B 1 141 ? 30.774 -32.015 -3.223  1.00 17.58 ?  141 ARG   B CB   1 
ATOM   6057 C  CG   . ARG   B 1 141 ? 29.304 -31.897 -2.925  1.00 19.43 ?  141 ARG   B CG   1 
ATOM   6058 C  CD   . ARG   B 1 141 ? 28.523 -32.546 -4.001  1.00 21.02 ?  141 ARG   B CD   1 
ATOM   6059 N  NE   . ARG   B 1 141 ? 28.236 -31.629 -5.093  1.00 21.11 ?  141 ARG   B NE   1 
ATOM   6060 C  CZ   . ARG   B 1 141 ? 28.228 -31.967 -6.375  1.00 20.77 ?  141 ARG   B CZ   1 
ATOM   6061 N  NH1  . ARG   B 1 141 ? 28.668 -33.146 -6.784  1.00 20.38 ?  141 ARG   B NH1  1 
ATOM   6062 N  NH2  . ARG   B 1 141 ? 27.757 -31.103 -7.269  1.00 21.81 ?  141 ARG   B NH2  1 
ATOM   6063 H  H    . ARG   B 1 141 ? 33.094 -31.808 -3.717  1.00 18.34 ?  141 ARG   B H    1 
ATOM   6064 H  HA   . ARG   B 1 141 ? 31.006 -31.151 -5.084  1.00 19.34 ?  141 ARG   B HA   1 
ATOM   6065 H  HB2  . ARG   B 1 141 ? 30.941 -32.898 -3.580  1.00 21.06 ?  141 ARG   B HB2  1 
ATOM   6066 H  HB3  . ARG   B 1 141 ? 31.243 -31.921 -2.379  1.00 21.06 ?  141 ARG   B HB3  1 
ATOM   6067 H  HG2  . ARG   B 1 141 ? 29.113 -32.340 -2.088  1.00 23.27 ?  141 ARG   B HG2  1 
ATOM   6068 H  HG3  . ARG   B 1 141 ? 29.044 -30.959 -2.874  1.00 23.27 ?  141 ARG   B HG3  1 
ATOM   6069 H  HD2  . ARG   B 1 141 ? 29.027 -33.301 -4.349  1.00 25.19 ?  141 ARG   B HD2  1 
ATOM   6070 H  HD3  . ARG   B 1 141 ? 27.686 -32.857 -3.634  1.00 25.19 ?  141 ARG   B HD3  1 
ATOM   6071 H  HE   . ARG   B 1 141 ? 28.042 -30.814 -4.891  1.00 25.29 ?  141 ARG   B HE   1 
ATOM   6072 H  HH11 . ARG   B 1 141 ? 28.959 -33.724 -6.219  1.00 24.42 ?  141 ARG   B HH11 1 
ATOM   6073 H  HH12 . ARG   B 1 141 ? 28.657 -33.337 -7.621  1.00 24.42 ?  141 ARG   B HH12 1 
ATOM   6074 H  HH21 . ARG   B 1 141 ? 27.479 -30.327 -7.017  1.00 26.13 ?  141 ARG   B HH21 1 
ATOM   6075 H  HH22 . ARG   B 1 141 ? 27.768 -31.300 -8.107  1.00 26.13 ?  141 ARG   B HH22 1 
ATOM   6076 N  N    . VAL   B 1 142 ? 31.529 -29.132 -2.649  1.00 16.01 ?  142 VAL   B N    1 
ATOM   6077 C  CA   . VAL   B 1 142 ? 31.207 -27.796 -2.169  1.00 15.22 ?  142 VAL   B CA   1 
ATOM   6078 C  C    . VAL   B 1 142 ? 31.681 -26.743 -3.165  1.00 15.00 ?  142 VAL   B C    1 
ATOM   6079 O  O    . VAL   B 1 142 ? 30.979 -25.760 -3.430  1.00 15.58 ?  142 VAL   B O    1 
ATOM   6080 C  CB   . VAL   B 1 142 ? 31.764 -27.567 -0.750  1.00 15.76 ?  142 VAL   B CB   1 
ATOM   6081 C  CG1  . VAL   B 1 142 ? 31.443 -26.151 -0.273  1.00 15.41 ?  142 VAL   B CG1  1 
ATOM   6082 C  CG2  . VAL   B 1 142 ? 31.206 -28.599 0.216   1.00 16.33 ?  142 VAL   B CG2  1 
ATOM   6083 H  H    . VAL   B 1 142 ? 32.073 -29.569 -2.148  1.00 19.18 ?  142 VAL   B H    1 
ATOM   6084 H  HA   . VAL   B 1 142 ? 30.247 -27.713 -2.106  1.00 18.22 ?  142 VAL   B HA   1 
ATOM   6085 H  HB   . VAL   B 1 142 ? 32.732 -27.663 -0.766  1.00 18.88 ?  142 VAL   B HB   1 
ATOM   6086 H  HG11 . VAL   B 1 142 ? 31.638 -26.088 0.675   1.00 18.45 ?  142 VAL   B HG11 1 
ATOM   6087 H  HG12 . VAL   B 1 142 ? 31.996 -25.520 -0.764  1.00 18.45 ?  142 VAL   B HG12 1 
ATOM   6088 H  HG13 . VAL   B 1 142 ? 30.508 -25.971 -0.434  1.00 18.45 ?  142 VAL   B HG13 1 
ATOM   6089 H  HG21 . VAL   B 1 142 ? 31.533 -28.403 1.109   1.00 19.56 ?  142 VAL   B HG21 1 
ATOM   6090 H  HG22 . VAL   B 1 142 ? 30.240 -28.554 0.198   1.00 19.56 ?  142 VAL   B HG22 1 
ATOM   6091 H  HG23 . VAL   B 1 142 ? 31.505 -29.480 -0.058  1.00 19.56 ?  142 VAL   B HG23 1 
ATOM   6092 N  N    . CYS   B 1 143 ? 32.867 -26.938 -3.747  1.00 14.65 ?  143 CYS   B N    1 
ATOM   6093 C  CA   . CYS   B 1 143 ? 33.353 -26.002 -4.757  1.00 14.75 ?  143 CYS   B CA   1 
ATOM   6094 C  C    . CYS   B 1 143 ? 32.348 -25.861 -5.896  1.00 14.89 ?  143 CYS   B C    1 
ATOM   6095 O  O    . CYS   B 1 143 ? 31.951 -24.751 -6.267  1.00 15.21 ?  143 CYS   B O    1 
ATOM   6096 C  CB   . CYS   B 1 143 ? 34.705 -26.482 -5.290  1.00 14.91 ?  143 CYS   B CB   1 
ATOM   6097 S  SG   . CYS   B 1 143 ? 35.456 -25.389 -6.524  1.00 15.18 ?  143 CYS   B SG   1 
ATOM   6098 H  H    . CYS   B 1 143 ? 33.401 -27.585 -3.572  1.00 17.54 ?  143 CYS   B H    1 
ATOM   6099 H  HA   . CYS   B 1 143 ? 33.479 -25.126 -4.352  1.00 17.67 ?  143 CYS   B HA   1 
ATOM   6100 H  HB2  . CYS   B 1 143 ? 35.327 -26.558 -4.549  1.00 17.85 ?  143 CYS   B HB2  1 
ATOM   6101 H  HB3  . CYS   B 1 143 ? 34.585 -27.347 -5.702  1.00 17.85 ?  143 CYS   B HB3  1 
ATOM   6102 H  HG   . CYS   B 1 143 ? 36.530 -25.818 -6.832  1.00 18.17 ?  143 CYS   B HG   1 
ATOM   6103 N  N    . VAL   B 1 144 ? 31.943 -26.985 -6.482  1.00 15.52 ?  144 VAL   B N    1 
ATOM   6104 C  CA   . VAL   B 1 144 ? 31.036 -26.928 -7.623  1.00 16.52 ?  144 VAL   B CA   1 
ATOM   6105 C  C    . VAL   B 1 144 ? 29.693 -26.324 -7.248  1.00 16.50 ?  144 VAL   B C    1 
ATOM   6106 O  O    . VAL   B 1 144 ? 29.082 -25.610 -8.053  1.00 17.82 ?  144 VAL   B O    1 
ATOM   6107 C  CB   . VAL   B 1 144 ? 30.883 -28.336 -8.201  1.00 18.52 ?  144 VAL   B CB   1 
ATOM   6108 C  CG1  . VAL   B 1 144 ? 29.600 -28.472 -9.015  1.00 20.92 ?  144 VAL   B CG1  1 
ATOM   6109 C  CG2  . VAL   B 1 144 ? 32.111 -28.718 -9.008  1.00 18.90 ?  144 VAL   B CG2  1 
ATOM   6110 H  H    . VAL   B 1 144 ? 32.176 -27.776 -6.245  1.00 18.59 ?  144 VAL   B H    1 
ATOM   6111 H  HA   . VAL   B 1 144 ? 31.423 -26.366 -8.309  1.00 19.78 ?  144 VAL   B HA   1 
ATOM   6112 H  HB   . VAL   B 1 144 ? 30.819 -28.965 -7.464  1.00 22.19 ?  144 VAL   B HB   1 
ATOM   6113 H  HG11 . VAL   B 1 144 ? 29.677 -29.258 -9.584  1.00 25.07 ?  144 VAL   B HG11 1 
ATOM   6114 H  HG12 . VAL   B 1 144 ? 28.850 -28.581 -8.411  1.00 25.07 ?  144 VAL   B HG12 1 
ATOM   6115 H  HG13 . VAL   B 1 144 ? 29.485 -27.683 -9.561  1.00 25.07 ?  144 VAL   B HG13 1 
ATOM   6116 H  HG21 . VAL   B 1 144 ? 31.998 -29.615 -9.354  1.00 22.64 ?  144 VAL   B HG21 1 
ATOM   6117 H  HG22 . VAL   B 1 144 ? 32.211 -28.090 -9.743  1.00 22.64 ?  144 VAL   B HG22 1 
ATOM   6118 H  HG23 . VAL   B 1 144 ? 32.890 -28.678 -8.433  1.00 22.64 ?  144 VAL   B HG23 1 
ATOM   6119 N  N    . ASP   B 1 145 ? 29.226 -26.566 -6.029  1.00 16.46 ?  145 ASP   B N    1 
ATOM   6120 C  CA   . ASP   B 1 145 ? 27.923 -26.088 -5.594  1.00 17.20 ?  145 ASP   B CA   1 
ATOM   6121 C  C    . ASP   B 1 145 ? 27.957 -24.664 -5.061  1.00 16.95 ?  145 ASP   B C    1 
ATOM   6122 O  O    . ASP   B 1 145 ? 26.900 -24.118 -4.724  1.00 18.39 ?  145 ASP   B O    1 
ATOM   6123 C  CB   . ASP   B 1 145 ? 27.345 -27.000 -4.505  1.00 19.08 ?  145 ASP   B CB   1 
ATOM   6124 C  CG   . ASP   B 1 145 ? 26.967 -28.372 -5.017  1.00 20.90 ?  145 ASP   B CG   1 
ATOM   6125 O  OD1  . ASP   B 1 145 ? 26.855 -28.558 -6.249  1.00 21.09 ?  145 ASP   B OD1  1 
ATOM   6126 O  OD2  . ASP   B 1 145 ? 26.773 -29.268 -4.171  1.00 23.21 -1 145 ASP   B OD2  1 
ATOM   6127 H  H    . ASP   B 1 145 ? 29.659 -26.991 -5.423  1.00 19.71 ?  145 ASP   B H    1 
ATOM   6128 H  HA   . ASP   B 1 145 ? 27.321 -26.084 -6.349  1.00 20.60 ?  145 ASP   B HA   1 
ATOM   6129 H  HB2  . ASP   B 1 145 ? 28.004 -27.112 -3.810  1.00 22.86 ?  145 ASP   B HB2  1 
ATOM   6130 H  HB3  . ASP   B 1 145 ? 26.545 -26.581 -4.146  1.00 22.86 ?  145 ASP   B HB3  1 
ATOM   6131 N  N    . THR   B 1 146 ? 29.137 -24.050 -4.972  1.00 15.32 ?  146 THR   B N    1 
ATOM   6132 C  CA   . THR   B 1 146 ? 29.274 -22.727 -4.375  1.00 15.03 ?  146 THR   B CA   1 
ATOM   6133 C  C    . THR   B 1 146 ? 29.900 -21.703 -5.305  1.00 14.65 ?  146 THR   B C    1 
ATOM   6134 O  O    . THR   B 1 146 ? 29.445 -20.542 -5.352  1.00 14.78 ?  146 THR   B O    1 
ATOM   6135 C  CB   . THR   B 1 146 ? 30.106 -22.829 -3.090  1.00 15.11 ?  146 THR   B CB   1 
ATOM   6136 O  OG1  . THR   B 1 146 ? 29.520 -23.813 -2.221  1.00 15.49 ?  146 THR   B OG1  1 
ATOM   6137 C  CG2  . THR   B 1 146 ? 30.187 -21.490 -2.388  1.00 15.19 ?  146 THR   B CG2  1 
ATOM   6138 H  H    . THR   B 1 146 ? 29.881 -24.379 -5.255  1.00 18.35 ?  146 THR   B H    1 
ATOM   6139 H  HA   . THR   B 1 146 ? 28.405 -22.395 -4.130  1.00 18.00 ?  146 THR   B HA   1 
ATOM   6140 H  HB   . THR   B 1 146 ? 31.015 -23.098 -3.314  1.00 18.10 ?  146 THR   B HB   1 
ATOM   6141 H  HG1  . THR   B 1 146 ? 29.550 -24.570 -2.587  1.00 18.55 ?  146 THR   B HG1  1 
ATOM   6142 H  HG21 . THR   B 1 146 ? 30.525 -21.604 -1.488  1.00 18.19 ?  146 THR   B HG21 1 
ATOM   6143 H  HG22 . THR   B 1 146 ? 30.787 -20.895 -2.873  1.00 18.19 ?  146 THR   B HG22 1 
ATOM   6144 H  HG23 . THR   B 1 146 ? 29.309 -21.085 -2.349  1.00 18.19 ?  146 THR   B HG23 1 
ATOM   6145 N  N    . VAL   B 1 147 ? 30.965 -22.078 -6.009  1.00 14.24 ?  147 VAL   B N    1 
ATOM   6146 C  CA   . VAL   B 1 147 ? 31.684 -21.133 -6.852  1.00 13.83 ?  147 VAL   B CA   1 
ATOM   6147 C  C    . VAL   B 1 147 ? 30.947 -20.997 -8.172  1.00 14.33 ?  147 VAL   B C    1 
ATOM   6148 O  O    . VAL   B 1 147 ? 30.576 -21.999 -8.800  1.00 15.44 ?  147 VAL   B O    1 
ATOM   6149 C  CB   . VAL   B 1 147 ? 33.139 -21.580 -7.055  1.00 13.62 ?  147 VAL   B CB   1 
ATOM   6150 C  CG1  . VAL   B 1 147 ? 33.895 -20.551 -7.872  1.00 13.57 ?  147 VAL   B CG1  1 
ATOM   6151 C  CG2  . VAL   B 1 147 ? 33.816 -21.796 -5.707  1.00 13.90 ?  147 VAL   B CG2  1 
ATOM   6152 H  H    . VAL   B 1 147 ? 31.288 -22.880 -6.021  1.00 17.05 ?  147 VAL   B H    1 
ATOM   6153 H  HA   . VAL   B 1 147 ? 31.696 -20.270 -6.419  1.00 16.56 ?  147 VAL   B HA   1 
ATOM   6154 H  HB   . VAL   B 1 147 ? 33.155 -22.423 -7.543  1.00 16.31 ?  147 VAL   B HB   1 
ATOM   6155 H  HG11 . VAL   B 1 147 ? 34.839 -20.768 -7.864  1.00 16.25 ?  147 VAL   B HG11 1 
ATOM   6156 H  HG12 . VAL   B 1 147 ? 33.562 -20.554 -8.783  1.00 16.25 ?  147 VAL   B HG12 1 
ATOM   6157 H  HG13 . VAL   B 1 147 ? 33.757 -19.673 -7.475  1.00 16.25 ?  147 VAL   B HG13 1 
ATOM   6158 H  HG21 . VAL   B 1 147 ? 34.758 -21.974 -5.851  1.00 16.64 ?  147 VAL   B HG21 1 
ATOM   6159 H  HG22 . VAL   B 1 147 ? 33.707 -20.995 -5.172  1.00 16.64 ?  147 VAL   B HG22 1 
ATOM   6160 H  HG23 . VAL   B 1 147 ? 33.400 -22.551 -5.262  1.00 16.64 ?  147 VAL   B HG23 1 
ATOM   6161 N  N    . ARG   B 1 148 ? 30.749 -19.749 -8.595  1.00 14.32 ?  148 ARG   B N    1 
ATOM   6162 C  CA   . ARG   B 1 148 ? 30.118 -19.429 -9.862  1.00 14.61 ?  148 ARG   B CA   1 
ATOM   6163 C  C    . ARG   B 1 148 ? 31.062 -18.729 -10.825 1.00 14.33 ?  148 ARG   B C    1 
ATOM   6164 O  O    . ARG   B 1 148 ? 30.778 -18.706 -12.027 1.00 15.77 ?  148 ARG   B O    1 
ATOM   6165 C  CB   . ARG   B 1 148 ? 28.876 -18.554 -9.631  1.00 14.98 ?  148 ARG   B CB   1 
ATOM   6166 C  CG   . ARG   B 1 148 ? 27.821 -19.267 -8.801  1.00 15.52 ?  148 ARG   B CG   1 
ATOM   6167 C  CD   . ARG   B 1 148 ? 26.596 -18.391 -8.507  1.00 16.56 ?  148 ARG   B CD   1 
ATOM   6168 N  NE   . ARG   B 1 148 ? 26.953 -17.184 -7.772  1.00 16.56 ?  148 ARG   B NE   1 
ATOM   6169 C  CZ   . ARG   B 1 148 ? 27.265 -17.150 -6.482  1.00 15.69 ?  148 ARG   B CZ   1 
ATOM   6170 N  NH1  . ARG   B 1 148 ? 27.224 -18.240 -5.729  1.00 15.75 ?  148 ARG   B NH1  1 
ATOM   6171 N  NH2  . ARG   B 1 148 ? 27.651 -15.996 -5.939  1.00 15.74 ?  148 ARG   B NH2  1 
ATOM   6172 H  H    . ARG   B 1 148 ? 30.991 -19.047 -8.152  1.00 17.15 ?  148 ARG   B H    1 
ATOM   6173 H  HA   . ARG   B 1 148 ? 29.824 -20.250 -10.283 1.00 17.49 ?  148 ARG   B HA   1 
ATOM   6174 H  HB2  . ARG   B 1 148 ? 29.140 -17.749 -9.155  1.00 17.94 ?  148 ARG   B HB2  1 
ATOM   6175 H  HB3  . ARG   B 1 148 ? 28.483 -18.322 -10.485 1.00 17.94 ?  148 ARG   B HB3  1 
ATOM   6176 H  HG2  . ARG   B 1 148 ? 27.521 -20.054 -9.285  1.00 18.58 ?  148 ARG   B HG2  1 
ATOM   6177 H  HG3  . ARG   B 1 148 ? 28.212 -19.532 -7.952  1.00 18.58 ?  148 ARG   B HG3  1 
ATOM   6178 H  HD2  . ARG   B 1 148 ? 26.191 -18.127 -9.346  1.00 19.84 ?  148 ARG   B HD2  1 
ATOM   6179 H  HD3  . ARG   B 1 148 ? 25.968 -18.898 -7.971  1.00 19.84 ?  148 ARG   B HD3  1 
ATOM   6180 H  HE   . ARG   B 1 148 ? 26.989 -16.448 -8.209  1.00 19.84 ?  148 ARG   B HE   1 
ATOM   6181 H  HH11 . ARG   B 1 148 ? 26.976 -18.994 -6.068  1.00 18.86 ?  148 ARG   B HH11 1 
ATOM   6182 H  HH12 . ARG   B 1 148 ? 27.422 -18.196 -4.893  1.00 18.86 ?  148 ARG   B HH12 1 
ATOM   6183 H  HH21 . ARG   B 1 148 ? 27.694 -15.289 -6.422  1.00 18.85 ?  148 ARG   B HH21 1 
ATOM   6184 H  HH22 . ARG   B 1 148 ? 27.855 -15.962 -5.104  1.00 18.85 ?  148 ARG   B HH22 1 
ATOM   6185 N  N    . THR   B 1 149 ? 32.172 -18.180 -10.337 1.00 14.50 ?  149 THR   B N    1 
ATOM   6186 C  CA   . THR   B 1 149 ? 33.217 -17.620 -11.179 1.00 14.49 ?  149 THR   B CA   1 
ATOM   6187 C  C    . THR   B 1 149 ? 34.095 -18.759 -11.700 1.00 14.31 ?  149 THR   B C    1 
ATOM   6188 O  O    . THR   B 1 149 ? 33.900 -19.931 -11.366 1.00 14.80 ?  149 THR   B O    1 
ATOM   6189 C  CB   . THR   B 1 149 ? 33.996 -16.578 -10.389 1.00 14.60 ?  149 THR   B CB   1 
ATOM   6190 O  OG1  . THR   B 1 149 ? 34.459 -17.177 -9.175  1.00 14.34 ?  149 THR   B OG1  1 
ATOM   6191 C  CG2  . THR   B 1 149 ? 33.118 -15.357 -10.094 1.00 15.42 ?  149 THR   B CG2  1 
ATOM   6192 H  H    . THR   B 1 149 ? 32.333 -18.118 -9.495  1.00 17.36 ?  149 THR   B H    1 
ATOM   6193 H  HA   . THR   B 1 149 ? 32.809 -17.175 -11.936 1.00 17.35 ?  149 THR   B HA   1 
ATOM   6194 H  HB   . THR   B 1 149 ? 34.764 -16.293 -10.899 1.00 17.48 ?  149 THR   B HB   1 
ATOM   6195 H  HG1  . THR   B 1 149 ? 34.869 -16.606 -8.705  1.00 17.17 ?  149 THR   B HG1  1 
ATOM   6196 H  HG21 . THR   B 1 149 ? 33.631 -14.692 -9.596  1.00 18.47 ?  149 THR   B HG21 1 
ATOM   6197 H  HG22 . THR   B 1 149 ? 32.822 -14.954 -10.927 1.00 18.47 ?  149 THR   B HG22 1 
ATOM   6198 H  HG23 . THR   B 1 149 ? 32.347 -15.611 -9.572  1.00 18.47 ?  149 THR   B HG23 1 
ATOM   6199 N  N    . ASN   B 1 150 ? 35.049 -18.430 -12.557 1.00 14.06 ?  150 ASN   B N    1 
ATOM   6200 C  CA   . ASN   B 1 150 ? 35.817 -19.450 -13.263 1.00 14.68 ?  150 ASN   B CA   1 
ATOM   6201 C  C    . ASN   B 1 150 ? 36.983 -19.908 -12.395 1.00 13.99 ?  150 ASN   B C    1 
ATOM   6202 O  O    . ASN   B 1 150 ? 37.929 -19.151 -12.167 1.00 14.46 ?  150 ASN   B O    1 
ATOM   6203 C  CB   . ASN   B 1 150 ? 36.278 -18.920 -14.614 1.00 16.44 ?  150 ASN   B CB   1 
ATOM   6204 C  CG   . ASN   B 1 150 ? 35.127 -18.700 -15.558 1.00 19.11 ?  150 ASN   B CG   1 
ATOM   6205 O  OD1  . ASN   B 1 150 ? 34.212 -19.510 -15.616 1.00 19.95 ?  150 ASN   B OD1  1 
ATOM   6206 N  ND2  . ASN   B 1 150 ? 35.149 -17.596 -16.286 1.00 20.79 ?  150 ASN   B ND2  1 
ATOM   6207 H  H    . ASN   B 1 150 ? 35.276 -17.621 -12.743 1.00 16.84 ?  150 ASN   B H    1 
ATOM   6208 H  HA   . ASN   B 1 150 ? 35.237 -20.215 -13.426 1.00 17.57 ?  150 ASN   B HA   1 
ATOM   6209 H  HB2  . ASN   B 1 150 ? 36.725 -18.067 -14.484 1.00 19.69 ?  150 ASN   B HB2  1 
ATOM   6210 H  HB3  . ASN   B 1 150 ? 36.880 -19.558 -15.018 1.00 19.69 ?  150 ASN   B HB3  1 
ATOM   6211 H  HD21 . ASN   B 1 150 ? 34.510 -17.425 -16.842 1.00 24.91 ?  150 ASN   B HD21 1 
ATOM   6212 H  HD22 . ASN   B 1 150 ? 35.807 -17.043 -16.217 1.00 24.91 ?  150 ASN   B HD22 1 
ATOM   6213 N  N    . VAL   B 1 151 ? 36.925 -21.145 -11.913 1.00 13.64 ?  151 VAL   B N    1 
ATOM   6214 C  CA   . VAL   B 1 151 ? 37.947 -21.679 -11.022 1.00 13.63 ?  151 VAL   B CA   1 
ATOM   6215 C  C    . VAL   B 1 151 ? 38.647 -22.852 -11.697 1.00 13.22 ?  151 VAL   B C    1 
ATOM   6216 O  O    . VAL   B 1 151 ? 38.000 -23.781 -12.199 1.00 14.60 ?  151 VAL   B O    1 
ATOM   6217 C  CB   . VAL   B 1 151 ? 37.390 -22.025 -9.624  1.00 14.69 ?  151 VAL   B CB   1 
ATOM   6218 C  CG1  . VAL   B 1 151 ? 36.219 -23.011 -9.707  1.00 15.56 ?  151 VAL   B CG1  1 
ATOM   6219 C  CG2  . VAL   B 1 151 ? 38.503 -22.534 -8.715  1.00 14.91 ?  151 VAL   B CG2  1 
ATOM   6220 H  H    . VAL   B 1 151 ? 36.287 -21.698 -12.092 1.00 16.33 ?  151 VAL   B H    1 
ATOM   6221 H  HA   . VAL   B 1 151 ? 38.611 -20.983 -10.889 1.00 16.31 ?  151 VAL   B HA   1 
ATOM   6222 H  HB   . VAL   B 1 151 ? 37.043 -21.208 -9.225  1.00 17.59 ?  151 VAL   B HB   1 
ATOM   6223 H  HG11 . VAL   B 1 151 ? 35.905 -23.204 -8.808  1.00 18.63 ?  151 VAL   B HG11 1 
ATOM   6224 H  HG12 . VAL   B 1 151 ? 35.499 -22.610 -10.224 1.00 18.63 ?  151 VAL   B HG12 1 
ATOM   6225 H  HG13 . VAL   B 1 151 ? 36.519 -23.825 -10.135 1.00 18.63 ?  151 VAL   B HG13 1 
ATOM   6226 H  HG21 . VAL   B 1 151 ? 38.153 -22.617 -7.812  1.00 17.85 ?  151 VAL   B HG21 1 
ATOM   6227 H  HG22 . VAL   B 1 151 ? 38.797 -23.401 -9.034  1.00 17.85 ?  151 VAL   B HG22 1 
ATOM   6228 H  HG23 . VAL   B 1 151 ? 39.235 -21.904 -8.731  1.00 17.85 ?  151 VAL   B HG23 1 
ATOM   6229 N  N    . TYR   B 1 152 ? 39.975 -22.772 -11.724 1.00 12.96 ?  152 TYR   B N    1 
ATOM   6230 C  CA   . TYR   B 1 152 ? 40.866 -23.759 -12.314 1.00 13.29 ?  152 TYR   B CA   1 
ATOM   6231 C  C    . TYR   B 1 152 ? 41.595 -24.442 -11.161 1.00 12.63 ?  152 TYR   B C    1 
ATOM   6232 O  O    . TYR   B 1 152 ? 42.456 -23.832 -10.516 1.00 13.20 ?  152 TYR   B O    1 
ATOM   6233 C  CB   . TYR   B 1 152 ? 41.835 -23.062 -13.271 1.00 14.24 ?  152 TYR   B CB   1 
ATOM   6234 C  CG   . TYR   B 1 152 ? 41.158 -22.586 -14.536 1.00 14.70 ?  152 TYR   B CG   1 
ATOM   6235 C  CD1  . TYR   B 1 152 ? 40.526 -21.346 -14.593 1.00 15.05 ?  152 TYR   B CD1  1 
ATOM   6236 C  CD2  . TYR   B 1 152 ? 41.134 -23.384 -15.668 1.00 15.83 ?  152 TYR   B CD2  1 
ATOM   6237 C  CE1  . TYR   B 1 152 ? 39.886 -20.926 -15.747 1.00 16.73 ?  152 TYR   B CE1  1 
ATOM   6238 C  CE2  . TYR   B 1 152 ? 40.503 -22.974 -16.822 1.00 16.89 ?  152 TYR   B CE2  1 
ATOM   6239 C  CZ   . TYR   B 1 152 ? 39.887 -21.740 -16.860 1.00 17.36 ?  152 TYR   B CZ   1 
ATOM   6240 O  OH   . TYR   B 1 152 ? 39.260 -21.334 -18.015 1.00 20.09 ?  152 TYR   B OH   1 
ATOM   6241 H  H    . TYR   B 1 152 ? 40.409 -22.104 -11.384 1.00 15.51 ?  152 TYR   B H    1 
ATOM   6242 H  HA   . TYR   B 1 152 ? 40.349 -24.418 -12.805 1.00 15.91 ?  152 TYR   B HA   1 
ATOM   6243 H  HB2  . TYR   B 1 152 ? 42.211 -22.286 -12.823 1.00 17.05 ?  152 TYR   B HB2  1 
ATOM   6244 H  HB3  . TYR   B 1 152 ? 42.542 -23.672 -13.516 1.00 17.05 ?  152 TYR   B HB3  1 
ATOM   6245 H  HD1  . TYR   B 1 152 ? 40.521 -20.794 -13.842 1.00 18.02 ?  152 TYR   B HD1  1 
ATOM   6246 H  HD2  . TYR   B 1 152 ? 41.545 -24.217 -15.645 1.00 18.96 ?  152 TYR   B HD2  1 
ATOM   6247 H  HE1  . TYR   B 1 152 ? 39.469 -20.092 -15.781 1.00 20.03 ?  152 TYR   B HE1  1 
ATOM   6248 H  HE2  . TYR   B 1 152 ? 40.501 -23.523 -17.574 1.00 20.23 ?  152 TYR   B HE2  1 
ATOM   6249 H  HH   . TYR   B 1 152 ? 38.924 -20.570 -17.904 1.00 24.07 ?  152 TYR   B HH   1 
ATOM   6250 N  N    . LEU   B 1 153 ? 41.217 -25.691 -10.885 1.00 12.94 ?  153 LEU   B N    1 
ATOM   6251 C  CA   . LEU   B 1 153 ? 41.734 -26.444 -9.751  1.00 12.80 ?  153 LEU   B CA   1 
ATOM   6252 C  C    . LEU   B 1 153 ? 42.959 -27.246 -10.155 1.00 13.05 ?  153 LEU   B C    1 
ATOM   6253 O  O    . LEU   B 1 153 ? 42.932 -27.978 -11.148 1.00 14.10 ?  153 LEU   B O    1 
ATOM   6254 C  CB   . LEU   B 1 153 ? 40.663 -27.402 -9.224  1.00 13.04 ?  153 LEU   B CB   1 
ATOM   6255 C  CG   . LEU   B 1 153 ? 39.409 -26.748 -8.646  1.00 13.66 ?  153 LEU   B CG   1 
ATOM   6256 C  CD1  . LEU   B 1 153 ? 38.302 -27.777 -8.481  1.00 14.65 ?  153 LEU   B CD1  1 
ATOM   6257 C  CD2  . LEU   B 1 153 ? 39.721 -26.082 -7.310  1.00 14.20 ?  153 LEU   B CD2  1 
ATOM   6258 H  H    . LEU   B 1 153 ? 40.627 -26.127 -11.348 1.00 15.50 ?  153 LEU   B H    1 
ATOM   6259 H  HA   . LEU   B 1 153 ? 41.968 -25.828 -9.044  1.00 15.32 ?  153 LEU   B HA   1 
ATOM   6260 H  HB2  . LEU   B 1 153 ? 40.377 -27.979 -9.947  1.00 15.61 ?  153 LEU   B HB2  1 
ATOM   6261 H  HB3  . LEU   B 1 153 ? 41.056 -27.939 -8.516  1.00 15.61 ?  153 LEU   B HB3  1 
ATOM   6262 H  HG   . LEU   B 1 153 ? 39.095 -26.056 -9.254  1.00 16.35 ?  153 LEU   B HG   1 
ATOM   6263 H  HD11 . LEU   B 1 153 ? 37.498 -27.321 -8.179  1.00 17.54 ?  153 LEU   B HD11 1 
ATOM   6264 H  HD12 . LEU   B 1 153 ? 38.144 -28.197 -9.335  1.00 17.54 ?  153 LEU   B HD12 1 
ATOM   6265 H  HD13 . LEU   B 1 153 ? 38.582 -28.428 -7.826  1.00 17.54 ?  153 LEU   B HD13 1 
ATOM   6266 H  HD21 . LEU   B 1 153 ? 38.906 -25.709 -6.939  1.00 17.00 ?  153 LEU   B HD21 1 
ATOM   6267 H  HD22 . LEU   B 1 153 ? 40.081 -26.752 -6.703  1.00 17.00 ?  153 LEU   B HD22 1 
ATOM   6268 H  HD23 . LEU   B 1 153 ? 40.375 -25.380 -7.448  1.00 17.00 ?  153 LEU   B HD23 1 
ATOM   6269 N  N    . ALA   B 1 154 ? 44.014 -27.136 -9.357  1.00 12.87 ?  154 ALA   B N    1 
ATOM   6270 C  CA   . ALA   B 1 154 ? 45.242 -27.891 -9.550  1.00 14.10 ?  154 ALA   B CA   1 
ATOM   6271 C  C    . ALA   B 1 154 ? 45.319 -28.972 -8.478  1.00 14.52 ?  154 ALA   B C    1 
ATOM   6272 O  O    . ALA   B 1 154 ? 45.272 -28.677 -7.276  1.00 16.21 ?  154 ALA   B O    1 
ATOM   6273 C  CB   . ALA   B 1 154 ? 46.460 -26.972 -9.490  1.00 15.06 ?  154 ALA   B CB   1 
ATOM   6274 H  H    . ALA   B 1 154 ? 44.034 -26.606 -8.677  1.00 15.40 ?  154 ALA   B H    1 
ATOM   6275 H  HA   . ALA   B 1 154 ? 45.219 -28.317 -10.420 1.00 16.88 ?  154 ALA   B HA   1 
ATOM   6276 H  HB1  . ALA   B 1 154 ? 47.259 -27.503 -9.620  1.00 18.03 ?  154 ALA   B HB1  1 
ATOM   6277 H  HB2  . ALA   B 1 154 ? 46.388 -26.302 -10.190 1.00 18.03 ?  154 ALA   B HB2  1 
ATOM   6278 H  HB3  . ALA   B 1 154 ? 46.486 -26.538 -8.622  1.00 18.03 ?  154 ALA   B HB3  1 
ATOM   6279 N  N    . VAL   B 1 155 ? 45.422 -30.220 -8.914  1.00 14.13 ?  155 VAL   B N    1 
ATOM   6280 C  CA   . VAL   B 1 155 ? 45.527 -31.369 -8.022  1.00 14.89 ?  155 VAL   B CA   1 
ATOM   6281 C  C    . VAL   B 1 155 ? 46.860 -32.048 -8.309  1.00 14.65 ?  155 VAL   B C    1 
ATOM   6282 O  O    . VAL   B 1 155 ? 47.091 -32.536 -9.424  1.00 16.37 ?  155 VAL   B O    1 
ATOM   6283 C  CB   . VAL   B 1 155 ? 44.361 -32.353 -8.210  1.00 15.97 ?  155 VAL   B CB   1 
ATOM   6284 C  CG1  . VAL   B 1 155 ? 44.543 -33.563 -7.311  1.00 15.98 ?  155 VAL   B CG1  1 
ATOM   6285 C  CG2  . VAL   B 1 155 ? 43.031 -31.658 -7.932  1.00 16.80 ?  155 VAL   B CG2  1 
ATOM   6286 H  H    . VAL   B 1 155 ? 45.437 -30.434 -9.749  1.00 16.92 ?  155 VAL   B H    1 
ATOM   6287 H  HA   . VAL   B 1 155 ? 45.524 -31.066 -7.101  1.00 17.83 ?  155 VAL   B HA   1 
ATOM   6288 H  HB   . VAL   B 1 155 ? 44.348 -32.659 -9.131  1.00 19.13 ?  155 VAL   B HB   1 
ATOM   6289 H  HG11 . VAL   B 1 155 ? 43.710 -34.058 -7.276  1.00 19.14 ?  155 VAL   B HG11 1 
ATOM   6290 H  HG12 . VAL   B 1 155 ? 45.245 -34.125 -7.674  1.00 19.14 ?  155 VAL   B HG12 1 
ATOM   6291 H  HG13 . VAL   B 1 155 ? 44.785 -33.261 -6.421  1.00 19.14 ?  155 VAL   B HG13 1 
ATOM   6292 H  HG21 . VAL   B 1 155 ? 42.309 -32.305 -8.021  1.00 20.12 ?  155 VAL   B HG21 1 
ATOM   6293 H  HG22 . VAL   B 1 155 ? 43.040 -31.300 -7.030  1.00 20.12 ?  155 VAL   B HG22 1 
ATOM   6294 H  HG23 . VAL   B 1 155 ? 42.904 -30.939 -8.571  1.00 20.12 ?  155 VAL   B HG23 1 
ATOM   6295 N  N    . PHE   B 1 156 ? 47.729 -32.094 -7.299  1.00 15.13 ?  156 PHE   B N    1 
ATOM   6296 C  CA   . PHE   B 1 156 ? 49.107 -32.545 -7.512  1.00 16.00 ?  156 PHE   B CA   1 
ATOM   6297 C  C    . PHE   B 1 156 ? 49.206 -34.044 -7.793  1.00 17.29 ?  156 PHE   B C    1 
ATOM   6298 O  O    . PHE   B 1 156 ? 49.912 -34.470 -8.718  1.00 19.06 ?  156 PHE   B O    1 
ATOM   6299 C  CB   . PHE   B 1 156 ? 49.943 -32.181 -6.288  1.00 15.67 ?  156 PHE   B CB   1 
ATOM   6300 C  CG   . PHE   B 1 156 ? 51.365 -32.644 -6.356  1.00 16.34 ?  156 PHE   B CG   1 
ATOM   6301 C  CD1  . PHE   B 1 156 ? 52.238 -32.129 -7.299  1.00 17.89 ?  156 PHE   B CD1  1 
ATOM   6302 C  CD2  . PHE   B 1 156 ? 51.836 -33.580 -5.457  1.00 16.87 ?  156 PHE   B CD2  1 
ATOM   6303 C  CE1  . PHE   B 1 156 ? 53.554 -32.547 -7.347  1.00 18.42 ?  156 PHE   B CE1  1 
ATOM   6304 C  CE2  . PHE   B 1 156 ? 53.150 -33.997 -5.502  1.00 18.13 ?  156 PHE   B CE2  1 
ATOM   6305 C  CZ   . PHE   B 1 156 ? 54.002 -33.484 -6.452  1.00 18.30 ?  156 PHE   B CZ   1 
ATOM   6306 H  H    . PHE   B 1 156 ? 47.546 -31.873 -6.489  1.00 18.12 ?  156 PHE   B H    1 
ATOM   6307 H  HA   . PHE   B 1 156 ? 49.472 -32.074 -8.274  1.00 19.17 ?  156 PHE   B HA   1 
ATOM   6308 H  HB2  . PHE   B 1 156 ? 49.949 -31.213 -6.197  1.00 18.77 ?  156 PHE   B HB2  1 
ATOM   6309 H  HB3  . PHE   B 1 156 ? 49.537 -32.578 -5.502  1.00 18.77 ?  156 PHE   B HB3  1 
ATOM   6310 H  HD1  . PHE   B 1 156 ? 51.936 -31.490 -7.908  1.00 21.44 ?  156 PHE   B HD1  1 
ATOM   6311 H  HD2  . PHE   B 1 156 ? 51.257 -33.930 -4.816  1.00 20.21 ?  156 PHE   B HD2  1 
ATOM   6312 H  HE1  . PHE   B 1 156 ? 54.132 -32.199 -7.987  1.00 22.07 ?  156 PHE   B HE1  1 
ATOM   6313 H  HE2  . PHE   B 1 156 ? 53.452 -34.637 -4.895  1.00 21.72 ?  156 PHE   B HE2  1 
ATOM   6314 H  HZ   . PHE   B 1 156 ? 54.887 -33.771 -6.481  1.00 21.92 ?  156 PHE   B HZ   1 
ATOM   6315 N  N    A ASP   B 1 157 ? 48.534 -34.859 -6.989  0.70 17.31 ?  157 ASP   B N    1 
ATOM   6316 N  N    B ASP   B 1 157 ? 48.527 -34.861 -6.998  0.30 17.40 ?  157 ASP   B N    1 
ATOM   6317 C  CA   A ASP   B 1 157 ? 48.683 -36.307 -7.046  0.70 18.41 ?  157 ASP   B CA   1 
ATOM   6318 C  CA   B ASP   B 1 157 ? 48.630 -36.308 -7.134  0.30 18.00 ?  157 ASP   B CA   1 
ATOM   6319 C  C    A ASP   B 1 157 ? 47.754 -36.874 -8.114  0.70 18.42 ?  157 ASP   B C    1 
ATOM   6320 C  C    B ASP   B 1 157 ? 47.738 -36.783 -8.275  0.30 18.60 ?  157 ASP   B C    1 
ATOM   6321 O  O    A ASP   B 1 157 ? 46.529 -36.763 -8.000  0.70 17.85 ?  157 ASP   B O    1 
ATOM   6322 O  O    B ASP   B 1 157 ? 46.524 -36.552 -8.261  0.30 18.51 ?  157 ASP   B O    1 
ATOM   6323 C  CB   A ASP   B 1 157 ? 48.351 -36.892 -5.676  0.70 20.34 ?  157 ASP   B CB   1 
ATOM   6324 C  CB   B ASP   B 1 157 ? 48.220 -36.973 -5.824  0.30 18.38 ?  157 ASP   B CB   1 
ATOM   6325 C  CG   A ASP   B 1 157 ? 48.477 -38.400 -5.634  0.70 22.92 ?  157 ASP   B CG   1 
ATOM   6326 C  CG   B ASP   B 1 157 ? 48.439 -38.476 -5.840  0.30 18.98 ?  157 ASP   B CG   1 
ATOM   6327 O  OD1  A ASP   B 1 157 ? 48.869 -39.010 -6.653  0.70 23.83 ?  157 ASP   B OD1  1 
ATOM   6328 O  OD1  B ASP   B 1 157 ? 48.792 -39.023 -6.909  0.30 18.94 ?  157 ASP   B OD1  1 
ATOM   6329 O  OD2  A ASP   B 1 157 ? 48.179 -38.976 -4.569  0.70 24.75 -1 157 ASP   B OD2  1 
ATOM   6330 O  OD2  B ASP   B 1 157 ? 48.258 -39.114 -4.783  0.30 19.97 -1 157 ASP   B OD2  1 
ATOM   6331 H  H    A ASP   B 1 157 ? 47.978 -34.592 -6.392  0.70 20.74 ?  157 ASP   B H    1 
ATOM   6332 H  H    B ASP   B 1 157 ? 48.006 -34.602 -6.366  0.30 20.84 ?  157 ASP   B H    1 
ATOM   6333 H  HA   A ASP   B 1 157 ? 49.597 -36.539 -7.272  0.70 22.05 ?  157 ASP   B HA   1 
ATOM   6334 H  HA   B ASP   B 1 157 ? 49.548 -36.552 -7.332  0.30 21.57 ?  157 ASP   B HA   1 
ATOM   6335 H  HB2  A ASP   B 1 157 ? 48.947 -36.505 -5.013  0.70 24.37 ?  157 ASP   B HB2  1 
ATOM   6336 H  HB2  B ASP   B 1 157 ? 48.734 -36.578 -5.097  0.30 22.02 ?  157 ASP   B HB2  1 
ATOM   6337 H  HB3  A ASP   B 1 157 ? 47.435 -36.669 -5.454  0.70 24.37 ?  157 ASP   B HB3  1 
ATOM   6338 H  HB3  B ASP   B 1 157 ? 47.273 -36.812 -5.674  0.30 22.02 ?  157 ASP   B HB3  1 
ATOM   6339 N  N    A LYS   B 1 158 ? 48.342 -37.504 -9.138  0.70 19.75 ?  158 LYS   B N    1 
ATOM   6340 N  N    B LYS   B 1 158 ? 48.339 -37.457 -9.261  0.30 19.65 ?  158 LYS   B N    1 
ATOM   6341 C  CA   A LYS   B 1 158 ? 47.565 -38.124 -10.213 0.70 21.14 ?  158 LYS   B CA   1 
ATOM   6342 C  CA   B LYS   B 1 158 ? 47.558 -38.028 -10.355 0.30 20.89 ?  158 LYS   B CA   1 
ATOM   6343 C  C    A LYS   B 1 158 ? 46.507 -39.085 -9.676  0.70 21.37 ?  158 LYS   B C    1 
ATOM   6344 C  C    B LYS   B 1 158 ? 46.508 -39.006 -9.842  0.30 20.87 ?  158 LYS   B C    1 
ATOM   6345 O  O    A LYS   B 1 158 ? 45.391 -39.157 -10.206 0.70 21.53 ?  158 LYS   B O    1 
ATOM   6346 O  O    B LYS   B 1 158 ? 45.421 -39.112 -10.424 0.30 20.91 ?  158 LYS   B O    1 
ATOM   6347 C  CB   A LYS   B 1 158 ? 48.519 -38.852 -11.169 0.70 23.12 ?  158 LYS   B CB   1 
ATOM   6348 C  CB   B LYS   B 1 158 ? 48.496 -38.722 -11.346 0.30 22.39 ?  158 LYS   B CB   1 
ATOM   6349 C  CG   A LYS   B 1 158 ? 47.850 -39.774 -12.179 0.70 25.44 ?  158 LYS   B CG   1 
ATOM   6350 C  CG   B LYS   B 1 158 ? 47.814 -39.637 -12.355 0.30 23.88 ?  158 LYS   B CG   1 
ATOM   6351 C  CD   A LYS   B 1 158 ? 46.990 -39.014 -13.170 0.70 27.35 ?  158 LYS   B CD   1 
ATOM   6352 C  CD   B LYS   B 1 158 ? 46.907 -38.872 -13.302 0.30 25.29 ?  158 LYS   B CD   1 
ATOM   6353 C  CE   A LYS   B 1 158 ? 46.385 -39.956 -14.201 0.70 29.01 ?  158 LYS   B CE   1 
ATOM   6354 C  CE   B LYS   B 1 158 ? 46.323 -39.795 -14.360 0.30 26.40 ?  158 LYS   B CE   1 
ATOM   6355 N  NZ   A LYS   B 1 158 ? 45.335 -39.292 -15.024 0.70 29.68 ?  158 LYS   B NZ   1 
ATOM   6356 N  NZ   B LYS   B 1 158 ? 45.273 -39.122 -15.174 0.30 26.91 ?  158 LYS   B NZ   1 
ATOM   6357 H  H    A LYS   B 1 158 ? 49.192 -37.589 -9.226  0.70 23.66 ?  158 LYS   B H    1 
ATOM   6358 H  H    B LYS   B 1 158 ? 49.186 -37.600 -9.314  0.30 23.54 ?  158 LYS   B H    1 
ATOM   6359 H  HA   A LYS   B 1 158 ? 47.113 -37.430 -10.715 0.70 25.33 ?  158 LYS   B HA   1 
ATOM   6360 H  HA   B LYS   B 1 158 ? 47.102 -37.313 -10.825 0.30 25.03 ?  158 LYS   B HA   1 
ATOM   6361 H  HB2  A LYS   B 1 158 ? 49.020 -38.186 -11.671 0.70 27.71 ?  158 LYS   B HB2  1 
ATOM   6362 H  HB2  B LYS   B 1 158 ? 48.972 -38.041 -11.848 0.30 26.83 ?  158 LYS   B HB2  1 
ATOM   6363 H  HB3  A LYS   B 1 158 ? 49.134 -39.388 -10.644 0.70 27.71 ?  158 LYS   B HB3  1 
ATOM   6364 H  HB3  B LYS   B 1 158 ? 49.130 -39.258 -10.847 0.30 26.83 ?  158 LYS   B HB3  1 
ATOM   6365 H  HG2  A LYS   B 1 158 ? 48.540 -40.236 -12.680 0.70 30.49 ?  158 LYS   B HG2  1 
ATOM   6366 H  HG2  B LYS   B 1 158 ? 48.497 -40.073 -12.886 0.30 28.62 ?  158 LYS   B HG2  1 
ATOM   6367 H  HG3  A LYS   B 1 158 ? 47.292 -40.423 -11.721 0.70 30.49 ?  158 LYS   B HG3  1 
ATOM   6368 H  HG3  B LYS   B 1 158 ? 47.284 -40.306 -11.892 0.30 28.62 ?  158 LYS   B HG3  1 
ATOM   6369 H  HD2  A LYS   B 1 158 ? 46.267 -38.572 -12.699 0.70 32.78 ?  158 LYS   B HD2  1 
ATOM   6370 H  HD2  B LYS   B 1 158 ? 46.176 -38.478 -12.802 0.30 30.31 ?  158 LYS   B HD2  1 
ATOM   6371 H  HD3  A LYS   B 1 158 ? 47.537 -38.363 -13.638 0.70 32.78 ?  158 LYS   B HD3  1 
ATOM   6372 H  HD3  B LYS   B 1 158 ? 47.421 -38.180 -13.749 0.30 30.31 ?  158 LYS   B HD3  1 
ATOM   6373 H  HE2  A LYS   B 1 158 ? 47.083 -40.266 -14.798 0.70 34.78 ?  158 LYS   B HE2  1 
ATOM   6374 H  HE2  B LYS   B 1 158 ? 47.032 -40.082 -14.958 0.30 31.64 ?  158 LYS   B HE2  1 
ATOM   6375 H  HE3  A LYS   B 1 158 ? 45.981 -40.712 -13.746 0.70 34.78 ?  158 LYS   B HE3  1 
ATOM   6376 H  HE3  B LYS   B 1 158 ? 45.923 -40.565 -13.925 0.30 31.64 ?  158 LYS   B HE3  1 
ATOM   6377 H  HZ1  A LYS   B 1 158 ? 45.000 -39.867 -15.615 0.70 35.58 ?  158 LYS   B HZ1  1 
ATOM   6378 H  HZ1  B LYS   B 1 158 ? 44.951 -39.686 -15.782 0.30 32.25 ?  158 LYS   B HZ1  1 
ATOM   6379 H  HZ2  A LYS   B 1 158 ? 44.676 -39.000 -14.500 0.70 35.58 ?  158 LYS   B HZ2  1 
ATOM   6380 H  HZ2  B LYS   B 1 158 ? 44.607 -38.853 -14.648 0.30 32.25 ?  158 LYS   B HZ2  1 
ATOM   6381 H  HZ3  A LYS   B 1 158 ? 45.684 -38.599 -15.460 0.70 35.58 ?  158 LYS   B HZ3  1 
ATOM   6382 H  HZ3  B LYS   B 1 158 ? 45.618 -38.414 -15.589 0.30 32.25 ?  158 LYS   B HZ3  1 
ATOM   6383 N  N    A ASN   B 1 159 ? 46.843 -39.855 -8.639  0.70 21.32 ?  159 ASN   B N    1 
ATOM   6384 N  N    B ASN   B 1 159 ? 46.812 -39.732 -8.764  0.30 20.85 ?  159 ASN   B N    1 
ATOM   6385 C  CA   A ASN   B 1 159 ? 45.881 -40.821 -8.118  0.70 21.65 ?  159 ASN   B CA   1 
ATOM   6386 C  CA   B ASN   B 1 159 ? 45.872 -40.725 -8.254  0.30 20.84 ?  159 ASN   B CA   1 
ATOM   6387 C  C    A ASN   B 1 159 ? 44.692 -40.130 -7.454  0.70 20.61 ?  159 ASN   B C    1 
ATOM   6388 C  C    B ASN   B 1 159 ? 44.682 -40.067 -7.558  0.30 20.23 ?  159 ASN   B C    1 
ATOM   6389 O  O    A ASN   B 1 159 ? 43.557 -40.622 -7.539  0.70 20.88 ?  159 ASN   B O    1 
ATOM   6390 O  O    B ASN   B 1 159 ? 43.543 -40.532 -7.697  0.30 20.21 ?  159 ASN   B O    1 
ATOM   6391 C  CB   A ASN   B 1 159 ? 46.577 -41.788 -7.163  0.70 23.45 ?  159 ASN   B CB   1 
ATOM   6392 C  CB   B ASN   B 1 159 ? 46.597 -41.708 -7.334  0.30 21.48 ?  159 ASN   B CB   1 
ATOM   6393 C  CG   A ASN   B 1 159 ? 47.593 -42.660 -7.865  0.70 25.43 ?  159 ASN   B CG   1 
ATOM   6394 C  CG   B ASN   B 1 159 ? 47.589 -42.577 -8.082  0.30 22.18 ?  159 ASN   B CG   1 
ATOM   6395 O  OD1  A ASN   B 1 159 ? 47.347 -43.155 -8.971  0.70 26.30 ?  159 ASN   B OD1  1 
ATOM   6396 O  OD1  B ASN   B 1 159 ? 47.325 -43.013 -9.205  0.30 22.47 ?  159 ASN   B OD1  1 
ATOM   6397 N  ND2  A ASN   B 1 159 ? 48.746 -42.856 -7.228  0.70 26.21 ?  159 ASN   B ND2  1 
ATOM   6398 N  ND2  B ASN   B 1 159 ? 48.741 -42.830 -7.466  0.30 22.57 ?  159 ASN   B ND2  1 
ATOM   6399 H  H    A ASN   B 1 159 ? 47.597 -39.831 -8.231  0.70 25.54 ?  159 ASN   B H    1 
ATOM   6400 H  H    B ASN   B 1 159 ? 47.548 -39.673 -8.324  0.30 24.98 ?  159 ASN   B H    1 
ATOM   6401 H  HA   A ASN   B 1 159 ? 45.542 -41.342 -8.862  0.70 25.94 ?  159 ASN   B HA   1 
ATOM   6402 H  HA   B ASN   B 1 159 ? 45.529 -41.234 -9.004  0.30 24.97 ?  159 ASN   B HA   1 
ATOM   6403 H  HB2  A ASN   B 1 159 ? 47.035 -41.282 -6.474  0.70 28.10 ?  159 ASN   B HB2  1 
ATOM   6404 H  HB2  B ASN   B 1 159 ? 47.084 -41.214 -6.657  0.30 25.74 ?  159 ASN   B HB2  1 
ATOM   6405 H  HB3  A ASN   B 1 159 ? 45.913 -42.370 -6.766  0.70 28.10 ?  159 ASN   B HB3  1 
ATOM   6406 H  HB3  B ASN   B 1 159 ? 45.945 -42.293 -6.916  0.30 25.74 ?  159 ASN   B HB3  1 
ATOM   6407 H  HD21 A ASN   B 1 159 ? 49.362 -43.348 -7.581  0.70 31.42 ?  159 ASN   B HD21 1 
ATOM   6408 H  HD21 B ASN   B 1 159 ? 49.339 -43.321 -7.847  0.30 27.05 ?  159 ASN   B HD21 1 
ATOM   6409 H  HD22 A ASN   B 1 159 ? 48.878 -42.508 -6.451  0.70 31.42 ?  159 ASN   B HD22 1 
ATOM   6410 H  HD22 B ASN   B 1 159 ? 48.890 -42.511 -6.680  0.30 27.05 ?  159 ASN   B HD22 1 
ATOM   6411 N  N    . LEU   B 1 160 ? 44.914 -38.980 -6.815  1.00 19.88 ?  160 LEU   B N    1 
ATOM   6412 C  CA   . LEU   B 1 160 ? 43.790 -38.240 -6.255  1.00 18.98 ?  160 LEU   B CA   1 
ATOM   6413 C  C    . LEU   B 1 160 ? 42.990 -37.579 -7.364  1.00 18.23 ?  160 LEU   B C    1 
ATOM   6414 O  O    . LEU   B 1 160 ? 41.753 -37.576 -7.326  1.00 18.23 ?  160 LEU   B O    1 
ATOM   6415 C  CB   . LEU   B 1 160 ? 44.265 -37.211 -5.233  1.00 18.56 ?  160 LEU   B CB   1 
ATOM   6416 C  CG   . LEU   B 1 160 ? 43.133 -36.318 -4.712  1.00 18.32 ?  160 LEU   B CG   1 
ATOM   6417 C  CD1  . LEU   B 1 160 ? 42.018 -37.152 -4.083  1.00 19.02 ?  160 LEU   B CD1  1 
ATOM   6418 C  CD2  . LEU   B 1 160 ? 43.671 -35.305 -3.719  1.00 18.50 ?  160 LEU   B CD2  1 
ATOM   6419 H  H    A LEU   B 1 160 ? 45.686 -38.620 -6.697  0.70 23.82 ?  160 LEU   B H    1 
ATOM   6420 H  H    B LEU   B 1 160 ? 45.691 -38.658 -6.637  0.30 23.82 ?  160 LEU   B H    1 
ATOM   6421 H  HA   . LEU   B 1 160 ? 43.208 -38.867 -5.799  1.00 22.74 ?  160 LEU   B HA   1 
ATOM   6422 H  HB2  . LEU   B 1 160 ? 44.657 -37.681 -4.476  1.00 22.23 ?  160 LEU   B HB2  1 
ATOM   6423 H  HB3  . LEU   B 1 160 ? 44.936 -36.644 -5.648  1.00 22.23 ?  160 LEU   B HB3  1 
ATOM   6424 H  HG   . LEU   B 1 160 ? 42.752 -35.827 -5.456  1.00 21.94 ?  160 LEU   B HG   1 
ATOM   6425 H  HD11 . LEU   B 1 160 ? 41.398 -36.560 -3.637  1.00 22.79 ?  160 LEU   B HD11 1 
ATOM   6426 H  HD12 . LEU   B 1 160 ? 41.558 -37.651 -4.779  1.00 22.79 ?  160 LEU   B HD12 1 
ATOM   6427 H  HD13 . LEU   B 1 160 ? 42.409 -37.770 -3.442  1.00 22.79 ?  160 LEU   B HD13 1 
ATOM   6428 H  HD21 . LEU   B 1 160 ? 42.944 -34.728 -3.440  1.00 22.16 ?  160 LEU   B HD21 1 
ATOM   6429 H  HD22 . LEU   B 1 160 ? 44.034 -35.777 -2.955  1.00 22.16 ?  160 LEU   B HD22 1 
ATOM   6430 H  HD23 . LEU   B 1 160 ? 44.365 -34.783 -4.149  1.00 22.16 ?  160 LEU   B HD23 1 
ATOM   6431 N  N    A TYR   B 1 161 ? 43.678 -37.021 -8.364  0.70 18.35 ?  161 TYR   B N    1 
ATOM   6432 N  N    B TYR   B 1 161 ? 43.674 -37.029 -8.372  0.30 18.04 ?  161 TYR   B N    1 
ATOM   6433 C  CA   A TYR   B 1 161 ? 42.996 -36.452 -9.521  0.70 18.05 ?  161 TYR   B CA   1 
ATOM   6434 C  CA   B TYR   B 1 161 ? 42.977 -36.447 -9.515  0.30 17.78 ?  161 TYR   B CA   1 
ATOM   6435 C  C    A TYR   B 1 161 ? 42.042 -37.469 -10.134 0.70 18.04 ?  161 TYR   B C    1 
ATOM   6436 C  C    B TYR   B 1 161 ? 42.041 -37.466 -10.152 0.30 17.86 ?  161 TYR   B C    1 
ATOM   6437 O  O    A TYR   B 1 161 ? 40.868 -37.171 -10.379 0.70 17.90 ?  161 TYR   B O    1 
ATOM   6438 O  O    B TYR   B 1 161 ? 40.879 -37.162 -10.446 0.30 17.65 ?  161 TYR   B O    1 
ATOM   6439 C  CB   A TYR   B 1 161 ? 44.036 -35.983 -10.549 0.70 18.23 ?  161 TYR   B CB   1 
ATOM   6440 C  CB   B TYR   B 1 161 ? 43.995 -35.929 -10.538 0.30 17.78 ?  161 TYR   B CB   1 
ATOM   6441 C  CG   A TYR   B 1 161 ? 43.457 -35.506 -11.862 0.70 18.62 ?  161 TYR   B CG   1 
ATOM   6442 C  CG   B TYR   B 1 161 ? 43.384 -35.459 -11.845 0.30 18.09 ?  161 TYR   B CG   1 
ATOM   6443 C  CD1  A TYR   B 1 161 ? 43.081 -34.181 -12.030 0.70 18.48 ?  161 TYR   B CD1  1 
ATOM   6444 C  CD1  B TYR   B 1 161 ? 42.968 -34.143 -12.005 0.30 18.11 ?  161 TYR   B CD1  1 
ATOM   6445 C  CD2  A TYR   B 1 161 ? 43.277 -36.379 -12.930 0.70 19.13 ?  161 TYR   B CD2  1 
ATOM   6446 C  CD2  B TYR   B 1 161 ? 43.224 -36.331 -12.916 0.30 18.29 ?  161 TYR   B CD2  1 
ATOM   6447 C  CE1  A TYR   B 1 161 ? 42.552 -33.734 -13.221 0.70 19.58 ?  161 TYR   B CE1  1 
ATOM   6448 C  CE1  B TYR   B 1 161 ? 42.408 -33.709 -13.194 0.30 18.64 ?  161 TYR   B CE1  1 
ATOM   6449 C  CE2  A TYR   B 1 161 ? 42.743 -35.942 -14.127 0.70 20.19 ?  161 TYR   B CE2  1 
ATOM   6450 C  CE2  B TYR   B 1 161 ? 42.665 -35.906 -14.108 0.30 18.85 ?  161 TYR   B CE2  1 
ATOM   6451 C  CZ   A TYR   B 1 161 ? 42.382 -34.619 -14.266 0.70 20.48 ?  161 TYR   B CZ   1 
ATOM   6452 C  CZ   B TYR   B 1 161 ? 42.260 -34.594 -14.242 0.30 19.10 ?  161 TYR   B CZ   1 
ATOM   6453 O  OH   A TYR   B 1 161 ? 41.851 -34.177 -15.453 0.70 22.68 ?  161 TYR   B OH   1 
ATOM   6454 O  OH   B TYR   B 1 161 ? 41.703 -34.171 -15.427 0.30 20.22 ?  161 TYR   B OH   1 
ATOM   6455 H  H    A TYR   B 1 161 ? 44.533 -36.976 -8.400  0.70 21.99 ?  161 TYR   B H    1 
ATOM   6456 H  H    B TYR   B 1 161 ? 44.529 -36.990 -8.419  0.30 21.61 ?  161 TYR   B H    1 
ATOM   6457 H  HA   A TYR   B 1 161 ? 42.478 -35.683 -9.238  0.70 21.62 ?  161 TYR   B HA   1 
ATOM   6458 H  HA   B TYR   B 1 161 ? 42.443 -35.697 -9.213  0.30 21.29 ?  161 TYR   B HA   1 
ATOM   6459 H  HB2  A TYR   B 1 161 ? 44.538 -35.249 -10.166 0.70 21.84 ?  161 TYR   B HB2  1 
ATOM   6460 H  HB2  B TYR   B 1 161 ? 44.470 -35.179 -10.149 0.30 21.29 ?  161 TYR   B HB2  1 
ATOM   6461 H  HB3  A TYR   B 1 161 ? 44.632 -36.722 -10.744 0.70 21.84 ?  161 TYR   B HB3  1 
ATOM   6462 H  HB3  B TYR   B 1 161 ? 44.619 -36.642 -10.744 0.30 21.29 ?  161 TYR   B HB3  1 
ATOM   6463 H  HD1  A TYR   B 1 161 ? 43.194 -33.580 -11.327 0.70 22.14 ?  161 TYR   B HD1  1 
ATOM   6464 H  HD1  B TYR   B 1 161 ? 43.066 -33.543 -11.301 0.30 21.69 ?  161 TYR   B HD1  1 
ATOM   6465 H  HD2  A TYR   B 1 161 ? 43.514 -37.273 -12.839 0.70 22.92 ?  161 TYR   B HD2  1 
ATOM   6466 H  HD2  B TYR   B 1 161 ? 43.494 -37.217 -12.831 0.30 21.90 ?  161 TYR   B HD2  1 
ATOM   6467 H  HE1  A TYR   B 1 161 ? 42.305 -32.838 -13.315 0.70 23.46 ?  161 TYR   B HE1  1 
ATOM   6468 H  HE1  B TYR   B 1 161 ? 42.135 -32.823 -13.286 0.30 22.33 ?  161 TYR   B HE1  1 
ATOM   6469 H  HE2  A TYR   B 1 161 ? 42.623 -36.531 -14.834 0.70 24.19 ?  161 TYR   B HE2  1 
ATOM   6470 H  HE2  B TYR   B 1 161 ? 42.565 -36.500 -14.815 0.30 22.58 ?  161 TYR   B HE2  1 
ATOM   6471 H  HH   A TYR   B 1 161 ? 41.805 -34.810 -16.001 0.70 27.18 ?  161 TYR   B HH   1 
ATOM   6472 H  HH   B TYR   B 1 161 ? 41.668 -34.810 -15.971 0.30 24.23 ?  161 TYR   B HH   1 
ATOM   6473 N  N    . ASP   B 1 162 ? 42.529 -38.690 -10.365 1.00 18.52 ?  162 ASP   B N    1 
ATOM   6474 C  CA   . ASP   B 1 162 ? 41.691 -39.723 -10.962 1.00 19.35 ?  162 ASP   B CA   1 
ATOM   6475 C  C    . ASP   B 1 162 ? 40.497 -40.053 -10.074 1.00 18.77 ?  162 ASP   B C    1 
ATOM   6476 O  O    . ASP   B 1 162 ? 39.385 -40.265 -10.572 1.00 19.29 ?  162 ASP   B O    1 
ATOM   6477 C  CB   . ASP   B 1 162 ? 42.512 -40.988 -11.208 1.00 20.71 ?  162 ASP   B CB   1 
ATOM   6478 C  CG   . ASP   B 1 162 ? 43.516 -40.836 -12.335 1.00 22.25 ?  162 ASP   B CG   1 
ATOM   6479 O  OD1  . ASP   B 1 162 ? 43.399 -39.887 -13.132 1.00 22.77 ?  162 ASP   B OD1  1 
ATOM   6480 O  OD2  . ASP   B 1 162 ? 44.411 -41.698 -12.439 1.00 23.89 -1 162 ASP   B OD2  1 
ATOM   6481 H  H    A ASP   B 1 162 ? 43.331 -38.938 -10.189 0.70 22.18 ?  162 ASP   B H    1 
ATOM   6482 H  H    B ASP   B 1 162 ? 43.328 -38.940 -10.177 0.30 22.18 ?  162 ASP   B H    1 
ATOM   6483 H  HA   . ASP   B 1 162 ? 41.354 -39.410 -11.814 1.00 23.18 ?  162 ASP   B HA   1 
ATOM   6484 H  HB2  . ASP   B 1 162 ? 43.009 -41.207 -10.404 1.00 24.81 ?  162 ASP   B HB2  1 
ATOM   6485 H  HB3  . ASP   B 1 162 ? 41.914 -41.716 -11.438 1.00 24.81 ?  162 ASP   B HB3  1 
ATOM   6486 N  N    . LYS   B 1 163 ? 40.709 -40.128 -8.759  1.00 18.24 ?  163 LYS   B N    1 
ATOM   6487 C  CA   . LYS   B 1 163 ? 39.594 -40.406 -7.858  1.00 19.12 ?  163 LYS   B CA   1 
ATOM   6488 C  C    . LYS   B 1 163 ? 38.559 -39.287 -7.905  1.00 17.59 ?  163 LYS   B C    1 
ATOM   6489 O  O    . LYS   B 1 163 ? 37.345 -39.546 -7.887  1.00 18.12 ?  163 LYS   B O    1 
ATOM   6490 C  CB   . LYS   B 1 163 ? 40.097 -40.595 -6.429  1.00 23.35 ?  163 LYS   B CB   1 
ATOM   6491 C  CG   . LYS   B 1 163 ? 39.009 -41.051 -5.478  1.00 30.05 ?  163 LYS   B CG   1 
ATOM   6492 C  CD   . LYS   B 1 163 ? 39.524 -41.289 -4.072  1.00 36.17 ?  163 LYS   B CD   1 
ATOM   6493 C  CE   . LYS   B 1 163 ? 38.441 -41.938 -3.220  1.00 40.88 ?  163 LYS   B CE   1 
ATOM   6494 N  NZ   . LYS   B 1 163 ? 38.615 -41.676 -1.766  1.00 44.06 ?  163 LYS   B NZ   1 
ATOM   6495 H  H    . LYS   B 1 163 ? 41.474 -40.024 -8.374  1.00 21.85 ?  163 LYS   B H    1 
ATOM   6496 H  HA   . LYS   B 1 163 ? 39.161 -41.222 -8.136  1.00 22.91 ?  163 LYS   B HA   1 
ATOM   6497 H  HB2  . LYS   B 1 163 ? 40.797 -41.267 -6.428  1.00 27.99 ?  163 LYS   B HB2  1 
ATOM   6498 H  HB3  . LYS   B 1 163 ? 40.447 -39.752 -6.100  1.00 27.99 ?  163 LYS   B HB3  1 
ATOM   6499 H  HG2  . LYS   B 1 163 ? 38.320 -40.371 -5.431  1.00 36.03 ?  163 LYS   B HG2  1 
ATOM   6500 H  HG3  . LYS   B 1 163 ? 38.632 -41.884 -5.805  1.00 36.03 ?  163 LYS   B HG3  1 
ATOM   6501 H  HD2  . LYS   B 1 163 ? 40.290 -41.886 -4.103  1.00 43.37 ?  163 LYS   B HD2  1 
ATOM   6502 H  HD3  . LYS   B 1 163 ? 39.770 -40.443 -3.668  1.00 43.37 ?  163 LYS   B HD3  1 
ATOM   6503 H  HE2  . LYS   B 1 163 ? 37.574 -41.601 -3.492  1.00 49.02 ?  163 LYS   B HE2  1 
ATOM   6504 H  HE3  . LYS   B 1 163 ? 38.474 -42.897 -3.355  1.00 49.02 ?  163 LYS   B HE3  1 
ATOM   6505 H  HZ1  . LYS   B 1 163 ? 37.962 -42.070 -1.307  1.00 52.83 ?  163 LYS   B HZ1  1 
ATOM   6506 H  HZ2  . LYS   B 1 163 ? 39.397 -41.998 -1.492  1.00 52.83 ?  163 LYS   B HZ2  1 
ATOM   6507 H  HZ3  . LYS   B 1 163 ? 38.590 -40.800 -1.610  1.00 52.83 ?  163 LYS   B HZ3  1 
ATOM   6508 N  N    . LEU   B 1 164 ? 39.024 -38.034 -7.972  1.00 16.61 ?  164 LEU   B N    1 
ATOM   6509 C  CA   . LEU   B 1 164 ? 38.116 -36.893 -8.011  1.00 16.27 ?  164 LEU   B CA   1 
ATOM   6510 C  C    . LEU   B 1 164 ? 37.308 -36.870 -9.305  1.00 16.70 ?  164 LEU   B C    1 
ATOM   6511 O  O    . LEU   B 1 164 ? 36.086 -36.663 -9.284  1.00 17.63 ?  164 LEU   B O    1 
ATOM   6512 C  CB   . LEU   B 1 164 ? 38.911 -35.596 -7.849  1.00 15.63 ?  164 LEU   B CB   1 
ATOM   6513 C  CG   . LEU   B 1 164 ? 39.464 -35.326 -6.452  1.00 16.18 ?  164 LEU   B CG   1 
ATOM   6514 C  CD1  . LEU   B 1 164 ? 40.535 -34.258 -6.525  1.00 16.08 ?  164 LEU   B CD1  1 
ATOM   6515 C  CD2  . LEU   B 1 164 ? 38.364 -34.903 -5.494  1.00 18.00 ?  164 LEU   B CD2  1 
ATOM   6516 H  H    . LEU   B 1 164 ? 39.862 -37.818 -7.997  1.00 19.89 ?  164 LEU   B H    1 
ATOM   6517 H  HA   . LEU   B 1 164 ? 37.496 -36.959 -7.274  1.00 19.49 ?  164 LEU   B HA   1 
ATOM   6518 H  HB2  . LEU   B 1 164 ? 39.667 -35.617 -8.458  1.00 18.72 ?  164 LEU   B HB2  1 
ATOM   6519 H  HB3  . LEU   B 1 164 ? 38.335 -34.850 -8.078  1.00 18.72 ?  164 LEU   B HB3  1 
ATOM   6520 H  HG   . LEU   B 1 164 ? 39.874 -36.132 -6.107  1.00 19.38 ?  164 LEU   B HG   1 
ATOM   6521 H  HD11 . LEU   B 1 164 ? 40.874 -34.081 -5.630  1.00 19.26 ?  164 LEU   B HD11 1 
ATOM   6522 H  HD12 . LEU   B 1 164 ? 41.264 -34.572 -7.089  1.00 19.26 ?  164 LEU   B HD12 1 
ATOM   6523 H  HD13 . LEU   B 1 164 ? 40.159 -33.446 -6.898  1.00 19.26 ?  164 LEU   B HD13 1 
ATOM   6524 H  HD21 . LEU   B 1 164 ? 38.753 -34.694 -4.631  1.00 21.56 ?  164 LEU   B HD21 1 
ATOM   6525 H  HD22 . LEU   B 1 164 ? 37.914 -34.120 -5.851  1.00 21.56 ?  164 LEU   B HD22 1 
ATOM   6526 H  HD23 . LEU   B 1 164 ? 37.730 -35.632 -5.402  1.00 21.56 ?  164 LEU   B HD23 1 
ATOM   6527 N  N    . VAL   B 1 165 ? 37.976 -37.047 -10.446 1.00 18.39 ?  165 VAL   B N    1 
ATOM   6528 C  CA   . VAL   B 1 165 ? 37.293 -36.978 -11.733 1.00 20.12 ?  165 VAL   B CA   1 
ATOM   6529 C  C    . VAL   B 1 165 ? 36.359 -38.168 -11.900 1.00 22.38 ?  165 VAL   B C    1 
ATOM   6530 O  O    . VAL   B 1 165 ? 35.179 -38.017 -12.245 1.00 23.86 ?  165 VAL   B O    1 
ATOM   6531 C  CB   . VAL   B 1 165 ? 38.313 -36.912 -12.883 1.00 20.80 ?  165 VAL   B CB   1 
ATOM   6532 C  CG1  . VAL   B 1 165 ? 37.611 -37.036 -14.211 1.00 21.85 ?  165 VAL   B CG1  1 
ATOM   6533 C  CG2  . VAL   B 1 165 ? 39.120 -35.628 -12.817 1.00 20.41 ?  165 VAL   B CG2  1 
ATOM   6534 H  H    . VAL   B 1 165 ? 38.820 -37.206 -10.500 1.00 22.03 ?  165 VAL   B H    1 
ATOM   6535 H  HA   . VAL   B 1 165 ? 36.758 -36.171 -11.766 1.00 24.11 ?  165 VAL   B HA   1 
ATOM   6536 H  HB   . VAL   B 1 165 ? 38.935 -37.650 -12.799 1.00 24.92 ?  165 VAL   B HB   1 
ATOM   6537 H  HG11 . VAL   B 1 165 ? 38.188 -36.703 -14.908 1.00 26.18 ?  165 VAL   B HG11 1 
ATOM   6538 H  HG12 . VAL   B 1 165 ? 37.416 -37.974 -14.367 1.00 26.18 ?  165 VAL   B HG12 1 
ATOM   6539 H  HG13 . VAL   B 1 165 ? 36.787 -36.528 -14.182 1.00 26.18 ?  165 VAL   B HG13 1 
ATOM   6540 H  HG21 . VAL   B 1 165 ? 39.737 -35.603 -13.567 1.00 24.46 ?  165 VAL   B HG21 1 
ATOM   6541 H  HG22 . VAL   B 1 165 ? 38.514 -34.870 -12.865 1.00 24.46 ?  165 VAL   B HG22 1 
ATOM   6542 H  HG23 . VAL   B 1 165 ? 39.614 -35.604 -11.983 1.00 24.46 ?  165 VAL   B HG23 1 
ATOM   6543 N  N    . SER   B 1 166 ? 36.887 -39.377 -11.672 1.00 23.57 ?  166 SER   B N    1 
ATOM   6544 C  CA   . SER   B 1 166 ? 36.125 -40.590 -11.928 1.00 25.15 ?  166 SER   B CA   1 
ATOM   6545 C  C    . SER   B 1 166 ? 34.882 -40.677 -11.054 1.00 25.43 ?  166 SER   B C    1 
ATOM   6546 O  O    . SER   B 1 166 ? 33.904 -41.299 -11.460 1.00 26.77 ?  166 SER   B O    1 
ATOM   6547 C  CB   . SER   B 1 166 ? 37.003 -41.845 -11.785 1.00 26.11 ?  166 SER   B CB   1 
ATOM   6548 O  OG   . SER   B 1 166 ? 37.403 -42.062 -10.443 1.00 26.34 ?  166 SER   B OG   1 
ATOM   6549 H  H    . SER   B 1 166 ? 37.687 -39.516 -11.399 1.00 28.25 ?  166 SER   B H    1 
ATOM   6550 H  HA   . SER   B 1 166 ? 35.809 -40.574 -12.844 1.00 30.15 ?  166 SER   B HA   1 
ATOM   6551 H  HB2  . SER   B 1 166 ? 36.502 -42.620 -12.089 1.00 31.30 ?  166 SER   B HB2  1 
ATOM   6552 H  HB3  . SER   B 1 166 ? 37.795 -41.735 -12.338 1.00 31.30 ?  166 SER   B HB3  1 
ATOM   6553 H  HG   . SER   B 1 166 ? 37.852 -41.405 -10.169 1.00 31.57 ?  166 SER   B HG   1 
ATOM   6554 N  N    . SER   B 1 167 ? 34.873 -40.055 -9.877  1.00 23.31 ?  167 SER   B N    1 
ATOM   6555 C  CA   . SER   B 1 167 ? 33.720 -40.114 -8.982  1.00 22.81 ?  167 SER   B CA   1 
ATOM   6556 C  C    . SER   B 1 167 ? 32.808 -38.892 -9.067  1.00 22.27 ?  167 SER   B C    1 
ATOM   6557 O  O    . SER   B 1 167 ? 31.732 -38.900 -8.461  1.00 22.78 ?  167 SER   B O    1 
ATOM   6558 C  CB   . SER   B 1 167 ? 34.172 -40.294 -7.526  1.00 22.57 ?  167 SER   B CB   1 
ATOM   6559 O  OG   . SER   B 1 167 ? 34.871 -39.146 -7.065  1.00 22.71 ?  167 SER   B OG   1 
ATOM   6560 H  H    . SER   B 1 167 ? 35.511 -39.582 -9.579  1.00 27.93 ?  167 SER   B H    1 
ATOM   6561 H  HA   . SER   B 1 167 ? 33.177 -40.885 -9.215  1.00 27.34 ?  167 SER   B HA   1 
ATOM   6562 H  HB2  . SER   B 1 167 ? 33.383 -40.437 -6.968  1.00 27.05 ?  167 SER   B HB2  1 
ATOM   6563 H  HB3  . SER   B 1 167 ? 34.747 -41.074 -7.475  1.00 27.05 ?  167 SER   B HB3  1 
ATOM   6564 H  HG   . SER   B 1 167 ? 35.551 -39.033 -7.533  1.00 27.21 ?  167 SER   B HG   1 
ATOM   6565 N  N    . PHE   B 1 168 ? 33.194 -37.842 -9.794  1.00 22.01 ?  168 PHE   B N    1 
ATOM   6566 C  CA   . PHE   B 1 168 ? 32.359 -36.641 -9.860  1.00 20.81 ?  168 PHE   B CA   1 
ATOM   6567 C  C    . PHE   B 1 168 ? 31.071 -36.904 -10.633 1.00 17.99 ?  168 PHE   B C    1 
ATOM   6568 O  O    . PHE   B 1 168 ? 30.010 -36.330 -10.315 1.00 18.44 ?  168 PHE   B O    1 
ATOM   6569 C  CB   . PHE   B 1 168 ? 33.131 -35.496 -10.510 1.00 21.76 ?  168 PHE   B CB   1 
ATOM   6570 C  CG   . PHE   B 1 168 ? 32.310 -34.262 -10.705 1.00 21.53 ?  168 PHE   B CG   1 
ATOM   6571 C  CD1  . PHE   B 1 168 ? 31.925 -33.498 -9.614  1.00 22.42 ?  168 PHE   B CD1  1 
ATOM   6572 C  CD2  . PHE   B 1 168 ? 31.907 -33.872 -11.969 1.00 20.76 ?  168 PHE   B CD2  1 
ATOM   6573 C  CE1  . PHE   B 1 168 ? 31.154 -32.365 -9.778  1.00 22.31 ?  168 PHE   B CE1  1 
ATOM   6574 C  CE2  . PHE   B 1 168 ? 31.145 -32.724 -12.147 1.00 21.88 ?  168 PHE   B CE2  1 
ATOM   6575 C  CZ   . PHE   B 1 168 ? 30.763 -31.972 -11.047 1.00 21.70 ?  168 PHE   B CZ   1 
ATOM   6576 H  H    . PHE   B 1 168 ? 33.921 -37.795 -10.246 1.00 26.38 ?  168 PHE   B H    1 
ATOM   6577 H  HA   . PHE   B 1 168 ? 32.115 -36.368 -8.963  1.00 24.93 ?  168 PHE   B HA   1 
ATOM   6578 H  HB2  . PHE   B 1 168 ? 33.882 -35.264 -9.943  1.00 26.07 ?  168 PHE   B HB2  1 
ATOM   6579 H  HB3  . PHE   B 1 168 ? 33.446 -35.780 -11.380 1.00 26.07 ?  168 PHE   B HB3  1 
ATOM   6580 H  HD1  . PHE   B 1 168 ? 32.183 -33.758 -8.762  1.00 26.86 ?  168 PHE   B HD1  1 
ATOM   6581 H  HD2  . PHE   B 1 168 ? 32.160 -34.369 -12.710 1.00 24.87 ?  168 PHE   B HD2  1 
ATOM   6582 H  HE1  . PHE   B 1 168 ? 30.904 -31.862 -9.039  1.00 26.73 ?  168 PHE   B HE1  1 
ATOM   6583 H  HE2  . PHE   B 1 168 ? 30.879 -32.471 -13.003 1.00 26.22 ?  168 PHE   B HE2  1 
ATOM   6584 H  HZ   . PHE   B 1 168 ? 30.245 -31.208 -11.164 1.00 26.00 ?  168 PHE   B HZ   1 
ATOM   6585 N  N    . LEU   B 1 169 ? 31.142 -37.775 -11.637 1.00 18.69 ?  169 LEU   B N    1 
ATOM   6586 C  CA   . LEU   B 1 169 ? 29.980 -38.124 -12.444 1.00 21.14 ?  169 LEU   B CA   1 
ATOM   6587 C  C    . LEU   B 1 169 ? 29.957 -39.575 -12.905 1.00 23.85 ?  169 LEU   B C    1 
ATOM   6588 O  O    . LEU   B 1 169 ? 29.051 -39.995 -13.628 1.00 26.09 ?  169 LEU   B O    1 
ATOM   6589 C  CB   . LEU   B 1 169 ? 29.917 -37.221 -13.673 1.00 22.55 ?  169 LEU   B CB   1 
ATOM   6590 C  CG   . LEU   B 1 169 ? 28.679 -36.336 -13.780 1.00 24.89 ?  169 LEU   B CG   1 
ATOM   6591 C  CD1  . LEU   B 1 169 ? 28.584 -35.767 -15.177 1.00 25.50 ?  169 LEU   B CD1  1 
ATOM   6592 C  CD2  . LEU   B 1 169 ? 27.415 -37.102 -13.423 1.00 25.11 ?  169 LEU   B CD2  1 
ATOM   6593 O  OXT  . LEU   B 1 169 ? 30.841 -40.357 -12.578 1.00 25.05 -1 169 LEU   B OXT  1 
ATOM   6594 H  H    . LEU   B 1 169 ? 31.865 -38.174 -11.879 1.00 22.40 ?  169 LEU   B H    1 
ATOM   6595 H  HA   . LEU   B 1 169 ? 29.194 -37.978 -11.905 1.00 25.33 ?  169 LEU   B HA   1 
ATOM   6596 H  HB2  . LEU   B 1 169 ? 30.690 -36.635 -13.672 1.00 27.02 ?  169 LEU   B HB2  1 
ATOM   6597 H  HB3  . LEU   B 1 169 ? 29.937 -37.778 -14.468 1.00 27.02 ?  169 LEU   B HB3  1 
ATOM   6598 H  HG   . LEU   B 1 169 ? 28.763 -35.593 -13.159 1.00 29.83 ?  169 LEU   B HG   1 
ATOM   6599 H  HD11 . LEU   B 1 169 ? 27.815 -35.179 -15.226 1.00 30.56 ?  169 LEU   B HD11 1 
ATOM   6600 H  HD12 . LEU   B 1 169 ? 29.394 -35.270 -15.368 1.00 30.56 ?  169 LEU   B HD12 1 
ATOM   6601 H  HD13 . LEU   B 1 169 ? 28.485 -36.497 -15.806 1.00 30.56 ?  169 LEU   B HD13 1 
ATOM   6602 H  HD21 . LEU   B 1 169 ? 26.662 -36.707 -13.883 1.00 30.09 ?  169 LEU   B HD21 1 
ATOM   6603 H  HD22 . LEU   B 1 169 ? 27.522 -38.029 -13.698 1.00 30.09 ?  169 LEU   B HD22 1 
ATOM   6604 H  HD23 . LEU   B 1 169 ? 27.280 -37.058 -12.463 1.00 30.09 ?  169 LEU   B HD23 1 
HETATM 6605 N  N2   B A1BBL C 2 .   ? 15.053 0.048   3.888   0.30 15.20 ?  201 A1BBL A N2   1 
HETATM 6606 C  C3   B A1BBL C 2 .   ? 15.213 1.207   3.171   0.30 14.98 ?  201 A1BBL A C3   1 
HETATM 6607 C  C6   B A1BBL C 2 .   ? 15.382 2.468   3.867   0.30 14.56 ?  201 A1BBL A C6   1 
HETATM 6608 C  C9   B A1BBL C 2 .   ? 14.036 -2.281  0.048   0.30 18.44 ?  201 A1BBL A C9   1 
HETATM 6609 C  C12  B A1BBL C 2 .   ? 12.749 -0.168  0.379   0.30 18.39 ?  201 A1BBL A C12  1 
HETATM 6610 C  C1   B A1BBL C 2 .   ? 13.875 -1.045  0.969   0.30 17.48 ?  201 A1BBL A C1   1 
HETATM 6611 C  C10  B A1BBL C 2 .   ? 12.687 -2.937  -0.255  0.30 19.45 ?  201 A1BBL A C10  1 
HETATM 6612 C  C11  B A1BBL C 2 .   ? 11.485 -0.955  0.025   0.30 19.52 ?  201 A1BBL A C11  1 
HETATM 6613 C  C2   B A1BBL C 2 .   ? 15.235 -0.251  1.077   0.30 15.84 ?  201 A1BBL A C2   1 
HETATM 6614 C  C4   B A1BBL C 2 .   ? 15.070 0.147   5.254   0.30 15.41 ?  201 A1BBL A C4   1 
HETATM 6615 C  C5   B A1BBL C 2 .   ? 15.371 2.381   5.292   0.30 14.57 ?  201 A1BBL A C5   1 
HETATM 6616 C  C7   B A1BBL C 2 .   ? 15.583 3.865   3.600   0.30 14.17 ?  201 A1BBL A C7   1 
HETATM 6617 C  C8   B A1BBL C 2 .   ? 15.669 4.543   4.807   0.30 13.50 ?  201 A1BBL A C8   1 
HETATM 6618 N  N1   B A1BBL C 2 .   ? 15.197 1.055   1.794   0.30 15.14 ?  201 A1BBL A N1   1 
HETATM 6619 N  N3   B A1BBL C 2 .   ? 15.209 1.234   6.017   0.30 15.23 ?  201 A1BBL A N3   1 
HETATM 6620 N  N4   B A1BBL C 2 .   ? 15.552 3.636   5.867   0.30 14.38 ?  201 A1BBL A N4   1 
HETATM 6621 O  O1   B A1BBL C 2 .   ? 13.446 -1.458  2.232   0.30 17.64 ?  201 A1BBL A O1   1 
HETATM 6622 O  O2   B A1BBL C 2 .   ? 11.797 -2.022  -0.837  0.30 19.94 ?  201 A1BBL A O2   1 
HETATM 6623 H  H9   B A1BBL C 2 .   ? 14.524 -2.012  -0.911  0.30 22.09 ?  201 A1BBL A H9   1 
HETATM 6624 H  H10  B A1BBL C 2 .   ? 14.694 -3.046  0.493   0.30 22.09 ?  201 A1BBL A H10  1 
HETATM 6625 H  H15  B A1BBL C 2 .   ? 12.479 0.629   1.098   0.30 22.03 ?  201 A1BBL A H15  1 
HETATM 6626 H  H16  B A1BBL C 2 .   ? 13.094 0.379   -0.519  0.30 22.03 ?  201 A1BBL A H16  1 
HETATM 6627 H  H12  B A1BBL C 2 .   ? 12.781 -3.745  -1.000  0.30 23.30 ?  201 A1BBL A H12  1 
HETATM 6628 H  H11  B A1BBL C 2 .   ? 12.234 -3.450  0.621   0.30 23.30 ?  201 A1BBL A H11  1 
HETATM 6629 H  H13  B A1BBL C 2 .   ? 11.031 -1.438  0.917   0.30 23.39 ?  201 A1BBL A H13  1 
HETATM 6630 H  H14  B A1BBL C 2 .   ? 10.672 -0.311  -0.374  0.30 23.39 ?  201 A1BBL A H14  1 
HETATM 6631 H  H3   B A1BBL C 2 .   ? 15.628 -0.093  0.049   0.30 18.97 ?  201 A1BBL A H3   1 
HETATM 6632 H  H2   B A1BBL C 2 .   ? 15.953 -0.927  1.559   0.30 18.97 ?  201 A1BBL A H2   1 
HETATM 6633 H  H5   B A1BBL C 2 .   ? 14.936 -0.773  5.862   0.30 18.45 ?  201 A1BBL A H5   1 
HETATM 6634 H  H6   B A1BBL C 2 .   ? 15.639 4.357   2.649   0.30 16.96 ?  201 A1BBL A H6   1 
HETATM 6635 H  H7   B A1BBL C 2 .   ? 15.804 5.590   5.063   0.30 16.16 ?  201 A1BBL A H7   1 
HETATM 6636 H  H4   B A1BBL C 2 .   ? 15.156 1.895   1.240   0.30 18.13 ?  201 A1BBL A H4   1 
HETATM 6637 H  H8   B A1BBL C 2 .   ? 15.568 3.867   6.847   0.30 17.22 ?  201 A1BBL A H8   1 
HETATM 6638 H  H1   B A1BBL C 2 .   ? 14.157 -1.972  2.614   0.30 21.14 ?  201 A1BBL A H1   1 
HETATM 6639 CL CL   B CL    D 3 .   ? 15.959 2.687   -0.992  0.30 17.11 ?  202 CL    A CL   1 
HETATM 6640 O  O    . HOH   E 4 .   ? 18.621 -2.400  -16.441 1.00 48.56 ?  301 HOH   A O    1 
HETATM 6641 O  O    . HOH   E 4 .   ? 11.988 0.266   14.725  1.00 36.79 ?  302 HOH   A O    1 
HETATM 6642 O  O    . HOH   E 4 .   ? 4.710  3.755   0.514   1.00 31.97 ?  303 HOH   A O    1 
HETATM 6643 O  O    . HOH   E 4 .   ? 14.612 -4.665  20.461  1.00 46.15 ?  304 HOH   A O    1 
HETATM 6644 O  O    . HOH   E 4 .   ? 26.869 11.438  1.576   1.00 18.06 ?  305 HOH   A O    1 
HETATM 6645 O  O    . HOH   E 4 .   ? 34.280 -1.869  12.532  1.00 38.76 ?  306 HOH   A O    1 
HETATM 6646 O  O    . HOH   E 4 .   ? 11.781 -10.859 -10.092 1.00 48.13 ?  307 HOH   A O    1 
HETATM 6647 O  O    . HOH   E 4 .   ? 0.656  -4.704  0.043   1.00 33.93 ?  308 HOH   A O    1 
HETATM 6648 O  O    . HOH   E 4 .   ? 28.658 -10.587 -14.101 1.00 40.89 ?  309 HOH   A O    1 
HETATM 6649 O  O    . HOH   E 4 .   ? 28.940 0.454   -9.760  1.00 23.40 ?  310 HOH   A O    1 
HETATM 6650 O  O    . HOH   E 4 .   ? -0.419 -3.065  3.011   1.00 40.33 ?  311 HOH   A O    1 
HETATM 6651 O  O    . HOH   E 4 .   ? 6.880  -8.138  11.745  1.00 23.78 ?  312 HOH   A O    1 
HETATM 6652 O  O    . HOH   E 4 .   ? 15.080 -12.219 18.605  1.00 42.34 ?  313 HOH   A O    1 
HETATM 6653 O  O    . HOH   E 4 .   ? 14.133 -4.550  -11.845 1.00 32.92 ?  314 HOH   A O    1 
HETATM 6654 O  O    . HOH   E 4 .   ? 14.690 -13.900 16.617  1.00 29.82 ?  315 HOH   A O    1 
HETATM 6655 O  O    . HOH   E 4 .   ? 9.174  -10.068 19.214  1.00 44.66 ?  316 HOH   A O    1 
HETATM 6656 O  O    . HOH   E 4 .   ? 30.226 -13.294 -8.519  1.00 26.11 ?  317 HOH   A O    1 
HETATM 6657 O  O    . HOH   E 4 .   ? 42.385 10.512  4.951   1.00 20.49 ?  318 HOH   A O    1 
HETATM 6658 O  O    . HOH   E 4 .   ? 7.591  -6.306  -6.541  1.00 41.87 ?  319 HOH   A O    1 
HETATM 6659 O  O    . HOH   E 4 .   ? 17.646 -1.789  0.307   1.00 21.81 ?  320 HOH   A O    1 
HETATM 6660 O  O    . HOH   E 4 .   ? 38.167 10.283  7.062   1.00 52.23 ?  321 HOH   A O    1 
HETATM 6661 O  O    . HOH   E 4 .   ? 7.930  -12.656 -0.973  1.00 23.97 ?  322 HOH   A O    1 
HETATM 6662 O  O    . HOH   E 4 .   ? 28.233 -6.292  19.508  1.00 43.16 ?  323 HOH   A O    1 
HETATM 6663 O  O    . HOH   E 4 .   ? 37.465 2.828   10.243  1.00 27.27 ?  324 HOH   A O    1 
HETATM 6664 O  O    . HOH   E 4 .   ? 22.725 12.506  1.550   1.00 16.23 ?  325 HOH   A O    1 
HETATM 6665 O  O    . HOH   E 4 .   ? 3.567  -9.237  9.870   1.00 34.53 ?  326 HOH   A O    1 
HETATM 6666 O  O    . HOH   E 4 .   ? -0.616 -8.609  2.104   1.00 43.57 ?  327 HOH   A O    1 
HETATM 6667 O  O    . HOH   E 4 .   ? 43.352 7.683   2.678   1.00 42.50 ?  328 HOH   A O    1 
HETATM 6668 O  O    . HOH   E 4 .   ? 26.524 -19.344 -1.792  1.00 16.13 ?  329 HOH   A O    1 
HETATM 6669 O  O    . HOH   E 4 .   ? 34.063 -1.176  -8.921  1.00 28.86 ?  330 HOH   A O    1 
HETATM 6670 O  O    . HOH   E 4 .   ? 44.314 7.219   6.399   1.00 27.91 ?  331 HOH   A O    1 
HETATM 6671 O  O    . HOH   E 4 .   ? 14.554 -3.787  2.950   1.00 18.46 ?  332 HOH   A O    1 
HETATM 6672 O  O    . HOH   E 4 .   ? 13.563 -15.294 -7.605  1.00 27.15 ?  333 HOH   A O    1 
HETATM 6673 O  O    . HOH   E 4 .   ? 31.052 -18.112 7.771   1.00 20.12 ?  334 HOH   A O    1 
HETATM 6674 O  O    . HOH   E 4 .   ? 28.346 -0.155  -13.405 1.00 41.33 ?  335 HOH   A O    1 
HETATM 6675 O  O    . HOH   E 4 .   ? 18.501 9.468   8.917   1.00 23.22 ?  336 HOH   A O    1 
HETATM 6676 O  O    . HOH   E 4 .   ? 17.169 -18.049 14.875  1.00 30.61 ?  337 HOH   A O    1 
HETATM 6677 O  O    . HOH   E 4 .   ? 13.353 -1.466  -6.656  1.00 18.88 ?  338 HOH   A O    1 
HETATM 6678 O  O    . HOH   E 4 .   ? 20.677 -19.831 -5.097  1.00 28.37 ?  339 HOH   A O    1 
HETATM 6679 O  O    . HOH   E 4 .   ? 18.698 -19.398 13.519  1.00 36.91 ?  340 HOH   A O    1 
HETATM 6680 O  O    . HOH   E 4 .   ? 27.344 13.786  2.773   1.00 31.52 ?  341 HOH   A O    1 
HETATM 6681 O  O    . HOH   E 4 .   ? 37.193 -2.768  9.698   1.00 44.92 ?  342 HOH   A O    1 
HETATM 6682 O  O    . HOH   E 4 .   ? 38.527 4.982   7.015   1.00 16.27 ?  343 HOH   A O    1 
HETATM 6683 O  O    A HOH   E 4 .   ? 14.255 0.555   6.729   0.70 20.76 ?  344 HOH   A O    1 
HETATM 6684 O  O    . HOH   E 4 .   ? 21.284 -2.424  -2.236  1.00 17.72 ?  345 HOH   A O    1 
HETATM 6685 O  O    . HOH   E 4 .   ? 36.268 -5.122  -0.514  1.00 31.34 ?  346 HOH   A O    1 
HETATM 6686 O  O    . HOH   E 4 .   ? 18.938 -22.009 6.931   1.00 34.97 ?  347 HOH   A O    1 
HETATM 6687 O  O    . HOH   E 4 .   ? 22.295 5.346   19.087  1.00 46.17 ?  348 HOH   A O    1 
HETATM 6688 O  O    . HOH   E 4 .   ? -1.542 -4.382  7.497   1.00 56.60 ?  349 HOH   A O    1 
HETATM 6689 O  O    . HOH   E 4 .   ? 8.169  -21.647 3.972   1.00 49.60 ?  350 HOH   A O    1 
HETATM 6690 O  O    . HOH   E 4 .   ? 15.840 2.125   24.569  1.00 46.86 ?  351 HOH   A O    1 
HETATM 6691 O  O    . HOH   E 4 .   ? 23.850 -15.786 -9.229  1.00 36.14 ?  352 HOH   A O    1 
HETATM 6692 O  O    . HOH   E 4 .   ? 42.558 4.293   5.487   1.00 34.35 ?  353 HOH   A O    1 
HETATM 6693 O  O    . HOH   E 4 .   ? 39.776 -1.051  -5.165  1.00 22.13 ?  354 HOH   A O    1 
HETATM 6694 O  O    . HOH   E 4 .   ? 22.083 -19.287 11.363  1.00 37.02 ?  355 HOH   A O    1 
HETATM 6695 O  O    . HOH   E 4 .   ? 14.975 4.007   17.633  1.00 43.80 ?  356 HOH   A O    1 
HETATM 6696 O  O    . HOH   E 4 .   ? 19.944 -12.600 -8.884  1.00 27.72 ?  357 HOH   A O    1 
HETATM 6697 O  O    . HOH   E 4 .   ? 35.778 -12.634 6.826   1.00 17.02 ?  358 HOH   A O    1 
HETATM 6698 O  O    . HOH   E 4 .   ? 27.554 -6.152  -14.000 1.00 38.89 ?  359 HOH   A O    1 
HETATM 6699 O  O    . HOH   E 4 .   ? 24.043 -2.137  -2.119  1.00 12.17 ?  360 HOH   A O    1 
HETATM 6700 O  O    . HOH   E 4 .   ? 25.726 -0.829  -7.382  1.00 17.42 ?  361 HOH   A O    1 
HETATM 6701 O  O    . HOH   E 4 .   ? 30.765 3.084   8.274   1.00 13.64 ?  362 HOH   A O    1 
HETATM 6702 O  O    . HOH   E 4 .   ? 31.624 8.192   14.845  1.00 27.05 ?  363 HOH   A O    1 
HETATM 6703 O  O    . HOH   E 4 .   ? 14.379 -21.328 -4.293  1.00 28.05 ?  364 HOH   A O    1 
HETATM 6704 O  O    . HOH   E 4 .   ? 31.118 -13.938 -2.445  1.00 15.52 ?  365 HOH   A O    1 
HETATM 6705 O  O    . HOH   E 4 .   ? 31.958 -9.339  -6.695  1.00 24.29 ?  366 HOH   A O    1 
HETATM 6706 O  O    . HOH   E 4 .   ? 33.625 -7.161  4.337   1.00 17.56 ?  367 HOH   A O    1 
HETATM 6707 O  O    . HOH   E 4 .   ? 21.140 10.270  14.905  1.00 37.90 ?  368 HOH   A O    1 
HETATM 6708 O  O    . HOH   E 4 .   ? 24.418 3.558   -1.851  1.00 16.49 ?  369 HOH   A O    1 
HETATM 6709 O  O    . HOH   E 4 .   ? 10.946 1.606   12.534  1.00 25.56 ?  370 HOH   A O    1 
HETATM 6710 O  O    . HOH   E 4 .   ? 9.893  -21.406 5.624   1.00 20.40 ?  371 HOH   A O    1 
HETATM 6711 O  O    . HOH   E 4 .   ? 27.385 -10.544 14.068  1.00 18.81 ?  372 HOH   A O    1 
HETATM 6712 O  O    . HOH   E 4 .   ? 26.938 4.156   -0.658  1.00 13.82 ?  373 HOH   A O    1 
HETATM 6713 O  O    . HOH   E 4 .   ? 30.510 1.931   16.702  1.00 24.94 ?  374 HOH   A O    1 
HETATM 6714 O  O    . HOH   E 4 .   ? 37.256 11.983  4.902   1.00 28.70 ?  375 HOH   A O    1 
HETATM 6715 O  O    . HOH   E 4 .   ? 24.652 -17.473 12.728  1.00 25.61 ?  376 HOH   A O    1 
HETATM 6716 O  O    . HOH   E 4 .   ? 17.171 -17.840 -5.158  1.00 28.02 ?  377 HOH   A O    1 
HETATM 6717 O  O    . HOH   E 4 .   ? 21.841 -21.917 8.419   1.00 29.55 ?  378 HOH   A O    1 
HETATM 6718 O  O    . HOH   E 4 .   ? 18.976 -0.736  -1.730  1.00 15.29 ?  379 HOH   A O    1 
HETATM 6719 O  O    . HOH   E 4 .   ? 24.142 -7.729  14.393  1.00 18.05 ?  380 HOH   A O    1 
HETATM 6720 O  O    . HOH   E 4 .   ? 20.092 4.531   -7.571  1.00 24.14 ?  381 HOH   A O    1 
HETATM 6721 O  O    . HOH   E 4 .   ? 17.013 -19.299 4.837   1.00 16.83 ?  382 HOH   A O    1 
HETATM 6722 O  O    . HOH   E 4 .   ? 44.003 8.514   -3.004  1.00 30.00 ?  383 HOH   A O    1 
HETATM 6723 O  O    . HOH   E 4 .   ? 16.539 -22.124 0.962   1.00 28.56 ?  384 HOH   A O    1 
HETATM 6724 O  O    . HOH   E 4 .   ? 13.906 -4.964  17.378  1.00 27.90 ?  385 HOH   A O    1 
HETATM 6725 O  O    . HOH   E 4 .   ? 22.633 -11.900 21.825  1.00 51.08 ?  386 HOH   A O    1 
HETATM 6726 O  O    . HOH   E 4 .   ? 21.352 3.079   -0.329  1.00 14.23 ?  387 HOH   A O    1 
HETATM 6727 O  O    . HOH   E 4 .   ? 37.576 -2.100  5.914   1.00 28.52 ?  388 HOH   A O    1 
HETATM 6728 O  O    . HOH   E 4 .   ? 31.888 -7.293  -9.841  1.00 22.68 ?  389 HOH   A O    1 
HETATM 6729 O  O    . HOH   E 4 .   ? 15.437 11.900  7.915   1.00 41.53 ?  390 HOH   A O    1 
HETATM 6730 O  O    . HOH   E 4 .   ? 6.381  -5.615  10.955  1.00 22.13 ?  391 HOH   A O    1 
HETATM 6731 O  O    . HOH   E 4 .   ? 5.135  2.622   4.965   1.00 31.82 ?  392 HOH   A O    1 
HETATM 6732 O  O    . HOH   E 4 .   ? 23.454 11.386  4.029   1.00 13.57 ?  393 HOH   A O    1 
HETATM 6733 O  O    . HOH   E 4 .   ? 16.228 16.651  8.552   1.00 36.12 ?  394 HOH   A O    1 
HETATM 6734 O  O    . HOH   E 4 .   ? 10.349 -22.247 -1.410  1.00 52.94 ?  395 HOH   A O    1 
HETATM 6735 O  O    . HOH   E 4 .   ? 24.573 1.983   -7.057  1.00 21.63 ?  396 HOH   A O    1 
HETATM 6736 O  O    . HOH   E 4 .   ? 15.221 -8.056  -9.885  1.00 24.25 ?  397 HOH   A O    1 
HETATM 6737 O  O    . HOH   E 4 .   ? 32.744 -9.273  5.910   1.00 20.58 ?  398 HOH   A O    1 
HETATM 6738 O  O    . HOH   E 4 .   ? 20.530 -20.040 2.755   1.00 20.48 ?  399 HOH   A O    1 
HETATM 6739 O  O    A HOH   E 4 .   ? 15.784 -0.964  5.203   0.70 24.70 ?  400 HOH   A O    1 
HETATM 6740 O  O    . HOH   E 4 .   ? 6.636  -3.415  12.732  1.00 31.83 ?  401 HOH   A O    1 
HETATM 6741 O  O    . HOH   E 4 .   ? 27.955 0.792   -7.161  1.00 15.72 ?  402 HOH   A O    1 
HETATM 6742 O  O    . HOH   E 4 .   ? 15.211 -21.518 14.171  1.00 19.71 ?  403 HOH   A O    1 
HETATM 6743 O  O    . HOH   E 4 .   ? 21.847 -13.894 -8.209  1.00 47.05 ?  404 HOH   A O    1 
HETATM 6744 O  O    . HOH   E 4 .   ? 32.726 -4.220  -9.845  1.00 29.48 ?  405 HOH   A O    1 
HETATM 6745 O  O    . HOH   E 4 .   ? 30.009 -10.066 13.017  1.00 25.80 ?  406 HOH   A O    1 
HETATM 6746 O  O    . HOH   E 4 .   ? 40.942 -8.261  -6.779  1.00 36.98 ?  407 HOH   A O    1 
HETATM 6747 O  O    . HOH   E 4 .   ? 38.094 -1.352  -1.920  1.00 20.00 ?  408 HOH   A O    1 
HETATM 6748 O  O    . HOH   E 4 .   ? 30.292 -12.909 13.505  1.00 21.62 ?  409 HOH   A O    1 
HETATM 6749 O  O    . HOH   E 4 .   ? 14.586 -0.636  -12.192 1.00 28.34 ?  410 HOH   A O    1 
HETATM 6750 O  O    . HOH   E 4 .   ? 14.081 -23.071 7.310   1.00 20.25 ?  411 HOH   A O    1 
HETATM 6751 O  O    . HOH   E 4 .   ? 16.009 6.907   2.810   1.00 18.81 ?  412 HOH   A O    1 
HETATM 6752 O  O    . HOH   E 4 .   ? 35.148 -5.238  -3.094  1.00 18.49 ?  413 HOH   A O    1 
HETATM 6753 O  O    . HOH   E 4 .   ? 23.962 -20.305 -1.323  1.00 19.04 ?  414 HOH   A O    1 
HETATM 6754 O  O    . HOH   E 4 .   ? 27.156 2.318   18.697  1.00 36.48 ?  415 HOH   A O    1 
HETATM 6755 O  O    A HOH   E 4 .   ? 11.056 -0.406  1.858   0.70 23.12 ?  416 HOH   A O    1 
HETATM 6756 O  O    . HOH   E 4 .   ? 14.451 -24.634 11.468  1.00 39.28 ?  417 HOH   A O    1 
HETATM 6757 O  O    . HOH   E 4 .   ? 36.719 -4.928  5.412   1.00 24.95 ?  418 HOH   A O    1 
HETATM 6758 O  O    . HOH   E 4 .   ? 10.415 -13.819 -1.819  1.00 19.13 ?  419 HOH   A O    1 
HETATM 6759 O  O    . HOH   E 4 .   ? 30.893 6.191   -12.295 1.00 29.34 ?  420 HOH   A O    1 
HETATM 6760 O  O    . HOH   E 4 .   ? 8.937  -11.984 17.217  1.00 42.77 ?  421 HOH   A O    1 
HETATM 6761 O  O    . HOH   E 4 .   ? 24.039 3.923   -4.893  1.00 22.51 ?  422 HOH   A O    1 
HETATM 6762 O  O    . HOH   E 4 .   ? 41.654 1.415   5.066   1.00 39.19 ?  423 HOH   A O    1 
HETATM 6763 O  O    . HOH   E 4 .   ? 26.930 -3.160  19.485  1.00 36.58 ?  424 HOH   A O    1 
HETATM 6764 O  O    . HOH   E 4 .   ? 16.219 -14.259 20.187  1.00 51.58 ?  425 HOH   A O    1 
HETATM 6765 O  O    . HOH   E 4 .   ? 45.004 -0.553  3.013   1.00 43.55 ?  426 HOH   A O    1 
HETATM 6766 O  O    . HOH   E 4 .   ? 32.476 -10.639 3.316   1.00 32.66 ?  427 HOH   A O    1 
HETATM 6767 O  O    . HOH   E 4 .   ? 22.582 8.191   18.352  1.00 47.34 ?  428 HOH   A O    1 
HETATM 6768 O  O    . HOH   E 4 .   ? 21.229 -9.159  21.230  1.00 53.20 ?  429 HOH   A O    1 
HETATM 6769 O  O    . HOH   E 4 .   ? 18.860 1.954   -0.759  1.00 15.14 ?  430 HOH   A O    1 
HETATM 6770 O  O    . HOH   E 4 .   ? 11.684 -10.805 16.853  1.00 29.68 ?  431 HOH   A O    1 
HETATM 6771 O  O    . HOH   E 4 .   ? 37.750 -8.799  -3.425  1.00 22.55 ?  432 HOH   A O    1 
HETATM 6772 O  O    . HOH   E 4 .   ? 23.434 -20.945 1.342   1.00 20.78 ?  433 HOH   A O    1 
HETATM 6773 O  O    . HOH   E 4 .   ? 23.446 -8.033  17.018  1.00 23.44 ?  434 HOH   A O    1 
HETATM 6774 O  O    . HOH   E 4 .   ? 34.409 -8.069  -0.582  1.00 28.78 ?  435 HOH   A O    1 
HETATM 6775 O  O    . HOH   E 4 .   ? 23.216 7.600   -3.331  1.00 30.20 ?  436 HOH   A O    1 
HETATM 6776 O  O    . HOH   E 4 .   ? 18.348 -15.994 16.205  1.00 40.64 ?  437 HOH   A O    1 
HETATM 6777 O  O    . HOH   E 4 .   ? 18.541 4.854   -15.182 1.00 53.75 ?  438 HOH   A O    1 
HETATM 6778 O  O    . HOH   E 4 .   ? 9.494  -16.312 -2.144  1.00 43.56 ?  439 HOH   A O    1 
HETATM 6779 O  O    A HOH   E 4 .   ? 16.250 2.922   -1.511  0.70 16.40 ?  440 HOH   A O    1 
HETATM 6780 O  O    . HOH   E 4 .   ? 20.566 -17.708 24.821  1.00 54.33 ?  441 HOH   A O    1 
HETATM 6781 O  O    . HOH   E 4 .   ? 31.342 -12.792 0.017   1.00 20.92 ?  442 HOH   A O    1 
HETATM 6782 O  O    . HOH   E 4 .   ? 18.914 -10.781 23.886  1.00 80.98 ?  443 HOH   A O    1 
HETATM 6783 O  O    . HOH   E 4 .   ? 30.541 14.732  2.674   1.00 21.19 ?  444 HOH   A O    1 
HETATM 6784 O  O    . HOH   E 4 .   ? 21.470 -14.827 17.800  1.00 50.93 ?  445 HOH   A O    1 
HETATM 6785 O  O    A HOH   E 4 .   ? 14.014 -0.361  3.391   0.70 17.23 ?  446 HOH   A O    1 
HETATM 6786 O  O    . HOH   E 4 .   ? 29.828 -1.997  -12.754 1.00 51.60 ?  447 HOH   A O    1 
HETATM 6787 O  O    . HOH   E 4 .   ? 29.844 -16.088 10.799  1.00 37.20 ?  448 HOH   A O    1 
HETATM 6788 O  O    . HOH   E 4 .   ? 27.684 6.976   -6.601  1.00 41.74 ?  449 HOH   A O    1 
HETATM 6789 O  O    . HOH   E 4 .   ? 32.411 -15.930 10.850  1.00 30.54 ?  450 HOH   A O    1 
HETATM 6790 O  O    . HOH   E 4 .   ? 25.413 8.256   -4.859  1.00 28.15 ?  451 HOH   A O    1 
HETATM 6791 O  O    . HOH   E 4 .   ? 23.209 -22.316 -3.264  1.00 39.34 ?  452 HOH   A O    1 
HETATM 6792 O  O    . HOH   E 4 .   ? 19.909 -17.398 -5.092  1.00 25.24 ?  453 HOH   A O    1 
HETATM 6793 O  O    . HOH   E 4 .   ? 24.821 5.650   20.626  1.00 55.25 ?  454 HOH   A O    1 
HETATM 6794 O  O    . HOH   E 4 .   ? 24.557 14.643  7.736   1.00 38.82 ?  455 HOH   A O    1 
HETATM 6795 O  O    . HOH   E 4 .   ? 21.991 5.196   -6.199  1.00 33.28 ?  456 HOH   A O    1 
HETATM 6796 O  O    . HOH   E 4 .   ? 15.767 -21.554 3.632   1.00 23.96 ?  457 HOH   A O    1 
HETATM 6797 O  O    . HOH   E 4 .   ? 18.737 10.856  11.216  1.00 34.77 ?  458 HOH   A O    1 
HETATM 6798 O  O    . HOH   E 4 .   ? 39.675 -7.014  -3.521  1.00 46.42 ?  459 HOH   A O    1 
HETATM 6799 O  O    . HOH   E 4 .   ? 26.966 11.632  -1.383  1.00 33.57 ?  460 HOH   A O    1 
HETATM 6800 O  O    . HOH   E 4 .   ? 12.306 1.609   17.208  1.00 41.37 ?  461 HOH   A O    1 
HETATM 6801 O  O    . HOH   E 4 .   ? 23.437 13.700  5.537   1.00 19.89 ?  462 HOH   A O    1 
HETATM 6802 O  O    . HOH   E 4 .   ? 27.419 -11.415 16.522  1.00 39.72 ?  463 HOH   A O    1 
HETATM 6803 O  O    . HOH   E 4 .   ? 10.995 -15.044 -6.080  1.00 36.27 ?  464 HOH   A O    1 
HETATM 6804 O  O    . HOH   E 4 .   ? 18.159 -16.196 -8.946  1.00 42.52 ?  465 HOH   A O    1 
HETATM 6805 O  O    . HOH   E 4 .   ? 25.875 10.796  -3.754  1.00 25.79 ?  466 HOH   A O    1 
HETATM 6806 O  O    . HOH   E 4 .   ? 11.983 -13.383 16.304  1.00 53.53 ?  467 HOH   A O    1 
HETATM 6807 O  O    . HOH   E 4 .   ? 23.167 11.870  -4.068  1.00 21.38 ?  468 HOH   A O    1 
HETATM 6808 O  O    . HOH   E 4 .   ? 35.046 7.502   12.205  1.00 53.86 ?  469 HOH   A O    1 
HETATM 6809 O  O    . HOH   E 4 .   ? 28.763 8.965   17.483  1.00 37.63 ?  470 HOH   A O    1 
HETATM 6810 O  O    . HOH   E 4 .   ? 14.066 -10.294 -10.996 1.00 32.71 ?  471 HOH   A O    1 
HETATM 6811 O  O    . HOH   E 4 .   ? 15.776 -17.237 -7.001  1.00 32.92 ?  472 HOH   A O    1 
HETATM 6812 O  O    . HOH   E 4 .   ? 41.075 -3.921  -0.480  1.00 40.26 ?  473 HOH   A O    1 
HETATM 6813 O  O    . HOH   E 4 .   ? 28.604 -4.649  -12.342 1.00 41.46 ?  474 HOH   A O    1 
HETATM 6814 O  O    . HOH   E 4 .   ? 44.418 10.375  -1.698  1.00 35.24 ?  475 HOH   A O    1 
HETATM 6815 O  O    . HOH   E 4 .   ? 30.744 0.757   19.129  1.00 41.18 ?  476 HOH   A O    1 
HETATM 6816 O  O    . HOH   E 4 .   ? 16.861 -20.514 16.035  1.00 31.68 ?  477 HOH   A O    1 
HETATM 6817 O  O    . HOH   E 4 .   ? 17.364 -18.719 19.686  1.00 50.32 ?  478 HOH   A O    1 
HETATM 6818 O  O    . HOH   E 4 .   ? 31.483 -0.571  -10.596 1.00 30.58 ?  479 HOH   A O    1 
HETATM 6819 O  O    . HOH   E 4 .   ? 39.177 2.405   7.330   1.00 29.50 ?  480 HOH   A O    1 
HETATM 6820 O  O    . HOH   E 4 .   ? 18.427 -23.195 1.939   1.00 49.71 ?  481 HOH   A O    1 
HETATM 6821 O  O    . HOH   E 4 .   ? 16.031 -6.750  -11.877 1.00 47.63 ?  482 HOH   A O    1 
HETATM 6822 O  O    . HOH   E 4 .   ? 28.753 -7.958  -15.266 1.00 52.61 ?  483 HOH   A O    1 
HETATM 6823 O  O    . HOH   E 4 .   ? 41.748 9.547   -3.810  1.00 31.76 ?  484 HOH   A O    1 
HETATM 6824 O  O    . HOH   E 4 .   ? 25.810 -18.861 -11.836 1.00 41.15 ?  485 HOH   A O    1 
HETATM 6825 O  O    . HOH   E 4 .   ? 20.126 -22.327 4.264   1.00 33.68 ?  486 HOH   A O    1 
HETATM 6826 O  O    . HOH   E 4 .   ? 23.225 -12.844 19.188  1.00 54.72 ?  487 HOH   A O    1 
HETATM 6827 O  O    . HOH   E 4 .   ? 13.978 -25.257 8.854   1.00 34.41 ?  488 HOH   A O    1 
HETATM 6828 O  O    . HOH   E 4 .   ? 40.597 -0.301  -7.796  1.00 33.74 ?  489 HOH   A O    1 
HETATM 6829 O  O    . HOH   E 4 .   ? 16.224 -23.413 5.749   1.00 31.91 ?  490 HOH   A O    1 
HETATM 6830 O  O    . HOH   E 4 .   ? 37.397 -6.596  7.632   1.00 26.71 ?  491 HOH   A O    1 
HETATM 6831 O  O    . HOH   E 4 .   ? 30.756 -5.826  -11.909 1.00 50.47 ?  492 HOH   A O    1 
HETATM 6832 O  O    . HOH   E 4 .   ? 39.518 -0.102  6.634   1.00 32.55 ?  493 HOH   A O    1 
HETATM 6833 O  O    . HOH   E 4 .   ? 30.814 5.739   -14.765 1.00 33.43 ?  494 HOH   A O    1 
HETATM 6834 O  O    . HOH   E 4 .   ? 8.223  -3.129  -5.819  1.00 60.41 ?  495 HOH   A O    1 
HETATM 6835 O  O    . HOH   E 4 .   ? 20.587 -16.132 -7.419  1.00 29.86 ?  496 HOH   A O    1 
HETATM 6836 O  O    . HOH   E 4 .   ? 28.979 14.485  0.839   1.00 49.62 ?  497 HOH   A O    1 
HETATM 6837 O  O    . HOH   E 4 .   ? 37.942 13.976  6.623   1.00 36.68 ?  498 HOH   A O    1 
HETATM 6838 O  O    . HOH   E 4 .   ? 14.787 8.434   4.914   1.00 33.87 ?  499 HOH   A O    1 
HETATM 6839 O  O    . HOH   E 4 .   ? 22.104 -24.006 4.493   1.00 26.35 ?  500 HOH   A O    1 
HETATM 6840 O  O    . HOH   E 4 .   ? 36.452 -6.464  10.226  1.00 50.00 ?  501 HOH   A O    1 
HETATM 6841 O  O    . HOH   E 4 .   ? 17.295 -6.653  -14.146 1.00 44.66 ?  502 HOH   A O    1 
HETATM 6842 O  O    . HOH   E 4 .   ? 24.092 9.082   -7.279  1.00 38.70 ?  503 HOH   A O    1 
HETATM 6843 O  O    . HOH   E 4 .   ? 15.747 -12.327 27.296  1.00 43.75 ?  504 HOH   A O    1 
HETATM 6844 O  O    . HOH   E 4 .   ? 16.282 -21.226 18.720  1.00 38.97 ?  505 HOH   A O    1 
HETATM 6845 O  O    . HOH   E 4 .   ? 14.669 -22.750 19.748  1.00 34.66 ?  506 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 4 .   ? 29.920 -22.482 5.538   1.00 20.37 ?  201 HOH   B O    1 
HETATM 6847 O  O    . HOH   F 4 .   ? 41.643 -35.975 -17.163 1.00 34.33 ?  202 HOH   B O    1 
HETATM 6848 O  O    . HOH   F 4 .   ? 27.766 -29.172 -1.850  1.00 36.29 ?  203 HOH   B O    1 
HETATM 6849 O  O    . HOH   F 4 .   ? 31.140 -28.733 4.548   1.00 29.50 ?  204 HOH   B O    1 
HETATM 6850 O  O    . HOH   F 4 .   ? 27.930 -41.678 -15.163 1.00 35.33 ?  205 HOH   B O    1 
HETATM 6851 O  O    . HOH   F 4 .   ? 41.367 -7.812  5.449   1.00 41.92 ?  206 HOH   B O    1 
HETATM 6852 O  O    . HOH   F 4 .   ? 59.139 -18.664 6.854   1.00 39.10 ?  207 HOH   B O    1 
HETATM 6853 O  O    . HOH   F 4 .   ? 30.220 -40.985 -8.020  1.00 19.13 ?  208 HOH   B O    1 
HETATM 6854 O  O    . HOH   F 4 .   ? 34.928 -24.715 13.738  1.00 43.01 ?  209 HOH   B O    1 
HETATM 6855 O  O    . HOH   F 4 .   ? 38.070 -39.471 -0.235  1.00 41.75 ?  210 HOH   B O    1 
HETATM 6856 O  O    . HOH   F 4 .   ? 54.509 -9.437  -8.612  1.00 19.34 ?  211 HOH   B O    1 
HETATM 6857 O  O    . HOH   F 4 .   ? 50.125 -3.422  7.081   1.00 36.37 ?  212 HOH   B O    1 
HETATM 6858 O  O    . HOH   F 4 .   ? 49.386 -22.778 -19.828 1.00 54.05 ?  213 HOH   B O    1 
HETATM 6859 O  O    . HOH   F 4 .   ? 48.050 -6.941  15.488  1.00 30.04 ?  214 HOH   B O    1 
HETATM 6860 O  O    . HOH   F 4 .   ? 56.703 -30.754 -7.803  1.00 29.85 ?  215 HOH   B O    1 
HETATM 6861 O  O    . HOH   F 4 .   ? 30.026 -26.297 4.167   1.00 27.67 ?  216 HOH   B O    1 
HETATM 6862 O  O    . HOH   F 4 .   ? 34.572 -36.410 -7.133  1.00 20.29 ?  217 HOH   B O    1 
HETATM 6863 O  O    . HOH   F 4 .   ? 56.373 -19.746 7.204   1.00 30.94 ?  218 HOH   B O    1 
HETATM 6864 O  O    . HOH   F 4 .   ? 42.880 -20.262 -20.641 1.00 37.82 ?  219 HOH   B O    1 
HETATM 6865 O  O    . HOH   F 4 .   ? 53.028 -13.420 -20.366 1.00 37.37 ?  220 HOH   B O    1 
HETATM 6866 O  O    . HOH   F 4 .   ? 58.216 -12.917 8.364   1.00 31.50 ?  221 HOH   B O    1 
HETATM 6867 O  O    . HOH   F 4 .   ? 57.759 -24.450 5.026   1.00 40.38 ?  222 HOH   B O    1 
HETATM 6868 O  O    . HOH   F 4 .   ? 44.426 -7.173  1.993   1.00 35.72 ?  223 HOH   B O    1 
HETATM 6869 O  O    . HOH   F 4 .   ? 41.521 -39.165 -14.918 1.00 22.48 ?  224 HOH   B O    1 
HETATM 6870 O  O    . HOH   F 4 .   ? 47.426 -7.289  -3.824  1.00 42.95 ?  225 HOH   B O    1 
HETATM 6871 O  O    . HOH   F 4 .   ? 41.398 -9.650  13.007  1.00 21.99 ?  226 HOH   B O    1 
HETATM 6872 O  O    . HOH   F 4 .   ? 57.382 -16.273 -12.258 1.00 18.14 ?  227 HOH   B O    1 
HETATM 6873 O  O    . HOH   F 4 .   ? 51.661 -6.477  4.325   1.00 20.65 ?  228 HOH   B O    1 
HETATM 6874 O  O    . HOH   F 4 .   ? 37.068 -19.755 -18.178 1.00 48.10 ?  229 HOH   B O    1 
HETATM 6875 O  O    . HOH   F 4 .   ? 45.184 -35.005 6.857   1.00 43.98 ?  230 HOH   B O    1 
HETATM 6876 O  O    . HOH   F 4 .   ? 35.113 -8.016  -3.007  1.00 18.83 ?  231 HOH   B O    1 
HETATM 6877 O  O    . HOH   F 4 .   ? 25.431 -25.899 -1.217  1.00 33.82 ?  232 HOH   B O    1 
HETATM 6878 O  O    . HOH   F 4 .   ? 57.160 -26.902 -7.611  1.00 36.77 ?  233 HOH   B O    1 
HETATM 6879 O  O    . HOH   F 4 .   ? 46.368 -1.548  13.106  1.00 28.95 ?  234 HOH   B O    1 
HETATM 6880 O  O    . HOH   F 4 .   ? 50.783 -6.048  0.183   1.00 29.14 ?  235 HOH   B O    1 
HETATM 6881 O  O    . HOH   F 4 .   ? 50.785 -12.989 -0.475  1.00 12.61 ?  236 HOH   B O    1 
HETATM 6882 O  O    . HOH   F 4 .   ? 32.768 -43.766 -11.261 1.00 24.83 ?  237 HOH   B O    1 
HETATM 6883 O  O    . HOH   F 4 .   ? 50.973 -39.943 -8.256  1.00 34.96 ?  238 HOH   B O    1 
HETATM 6884 O  O    . HOH   F 4 .   ? 44.883 -43.578 -10.520 1.00 27.81 ?  239 HOH   B O    1 
HETATM 6885 O  O    . HOH   F 4 .   ? 46.943 -29.563 9.727   1.00 30.72 ?  240 HOH   B O    1 
HETATM 6886 O  O    . HOH   F 4 .   ? 44.555 -27.763 -0.694  1.00 22.83 ?  241 HOH   B O    1 
HETATM 6887 O  O    . HOH   F 4 .   ? 40.585 -16.086 14.066  1.00 23.71 ?  242 HOH   B O    1 
HETATM 6888 O  O    . HOH   F 4 .   ? 55.342 -16.489 -14.344 1.00 32.43 ?  243 HOH   B O    1 
HETATM 6889 O  O    . HOH   F 4 .   ? 51.565 -13.832 10.917  1.00 28.81 ?  244 HOH   B O    1 
HETATM 6890 O  O    . HOH   F 4 .   ? 43.000 -43.230 -8.193  1.00 30.53 ?  245 HOH   B O    1 
HETATM 6891 O  O    . HOH   F 4 .   ? 39.323 -10.843 6.113   1.00 25.51 ?  246 HOH   B O    1 
HETATM 6892 O  O    . HOH   F 4 .   ? 42.610 -25.375 2.684   1.00 16.61 ?  247 HOH   B O    1 
HETATM 6893 O  O    . HOH   F 4 .   ? 57.666 -24.360 -3.799  1.00 21.17 ?  248 HOH   B O    1 
HETATM 6894 O  O    . HOH   F 4 .   ? 58.201 -10.673 -4.049  1.00 21.46 ?  249 HOH   B O    1 
HETATM 6895 O  O    . HOH   F 4 .   ? 48.535 -36.554 -15.574 1.00 44.93 ?  250 HOH   B O    1 
HETATM 6896 O  O    . HOH   F 4 .   ? 39.563 -11.128 0.301   1.00 17.21 ?  251 HOH   B O    1 
HETATM 6897 O  O    . HOH   F 4 .   ? 42.673 -22.856 3.874   1.00 12.87 ?  252 HOH   B O    1 
HETATM 6898 O  O    . HOH   F 4 .   ? 29.715 -25.176 -10.699 1.00 18.54 ?  253 HOH   B O    1 
HETATM 6899 O  O    . HOH   F 4 .   ? 34.310 -18.350 11.449  1.00 28.26 ?  254 HOH   B O    1 
HETATM 6900 O  O    . HOH   F 4 .   ? 38.500 -11.063 -2.242  1.00 19.94 ?  255 HOH   B O    1 
HETATM 6901 O  O    . HOH   F 4 .   ? 41.961 -23.538 9.325   1.00 23.14 ?  256 HOH   B O    1 
HETATM 6902 O  O    . HOH   F 4 .   ? 27.107 -31.794 -9.875  1.00 23.17 ?  257 HOH   B O    1 
HETATM 6903 O  O    . HOH   F 4 .   ? 31.808 -17.890 -14.474 1.00 31.59 ?  258 HOH   B O    1 
HETATM 6904 O  O    . HOH   F 4 .   ? 28.427 -19.695 -13.129 1.00 25.81 ?  259 HOH   B O    1 
HETATM 6905 O  O    . HOH   F 4 .   ? 38.974 -11.944 12.372  1.00 37.05 ?  260 HOH   B O    1 
HETATM 6906 O  O    . HOH   F 4 .   ? 40.393 -12.738 -11.525 1.00 16.34 ?  261 HOH   B O    1 
HETATM 6907 O  O    . HOH   F 4 .   ? 30.424 -42.260 -10.583 1.00 30.75 ?  262 HOH   B O    1 
HETATM 6908 O  O    . HOH   F 4 .   ? 33.564 -16.943 8.139   1.00 20.61 ?  263 HOH   B O    1 
HETATM 6909 O  O    . HOH   F 4 .   ? 43.099 -32.341 -17.156 1.00 25.88 ?  264 HOH   B O    1 
HETATM 6910 O  O    . HOH   F 4 .   ? 48.078 -22.779 5.815   1.00 18.24 ?  265 HOH   B O    1 
HETATM 6911 O  O    . HOH   F 4 .   ? 29.863 -34.130 -0.436  1.00 36.26 ?  266 HOH   B O    1 
HETATM 6912 O  O    . HOH   F 4 .   ? 47.837 -24.546 -17.865 1.00 34.55 ?  267 HOH   B O    1 
HETATM 6913 O  O    . HOH   F 4 .   ? 57.026 -12.086 12.351  1.00 40.88 ?  268 HOH   B O    1 
HETATM 6914 O  O    . HOH   F 4 .   ? 28.411 -30.878 -14.763 1.00 32.93 ?  269 HOH   B O    1 
HETATM 6915 O  O    . HOH   F 4 .   ? 30.893 -15.729 2.707   1.00 15.14 ?  270 HOH   B O    1 
HETATM 6916 O  O    . HOH   F 4 .   ? 49.330 -28.724 -6.919  1.00 17.00 ?  271 HOH   B O    1 
HETATM 6917 O  O    . HOH   F 4 .   ? 28.261 -34.331 -9.303  1.00 20.63 ?  272 HOH   B O    1 
HETATM 6918 O  O    . HOH   F 4 .   ? 56.180 -23.589 -14.767 1.00 29.01 ?  273 HOH   B O    1 
HETATM 6919 O  O    . HOH   F 4 .   ? 57.497 -9.227  1.339   1.00 19.98 ?  274 HOH   B O    1 
HETATM 6920 O  O    . HOH   F 4 .   ? 42.474 -34.683 3.814   1.00 27.39 ?  275 HOH   B O    1 
HETATM 6921 O  O    . HOH   F 4 .   ? 34.913 -33.274 -19.226 1.00 32.28 ?  276 HOH   B O    1 
HETATM 6922 O  O    . HOH   F 4 .   ? 42.368 -9.935  9.309   1.00 20.90 ?  277 HOH   B O    1 
HETATM 6923 O  O    . HOH   F 4 .   ? 43.441 -15.793 -12.196 1.00 15.04 ?  278 HOH   B O    1 
HETATM 6924 O  O    . HOH   F 4 .   ? 56.949 -8.581  8.380   1.00 19.95 ?  279 HOH   B O    1 
HETATM 6925 O  O    . HOH   F 4 .   ? 49.672 -0.456  10.178  1.00 32.20 ?  280 HOH   B O    1 
HETATM 6926 O  O    . HOH   F 4 .   ? 59.805 -15.326 8.107   1.00 35.58 ?  281 HOH   B O    1 
HETATM 6927 O  O    . HOH   F 4 .   ? 46.602 -31.250 -4.827  1.00 28.01 ?  282 HOH   B O    1 
HETATM 6928 O  O    . HOH   F 4 .   ? 27.595 -26.676 -15.611 1.00 33.31 ?  283 HOH   B O    1 
HETATM 6929 O  O    . HOH   F 4 .   ? 41.173 -5.532  11.451  1.00 48.01 ?  284 HOH   B O    1 
HETATM 6930 O  O    . HOH   F 4 .   ? 48.432 -25.057 3.118   1.00 14.75 ?  285 HOH   B O    1 
HETATM 6931 O  O    . HOH   F 4 .   ? 34.498 -12.765 2.620   1.00 26.59 ?  286 HOH   B O    1 
HETATM 6932 O  O    . HOH   F 4 .   ? 45.265 -33.378 -15.954 1.00 25.60 ?  287 HOH   B O    1 
HETATM 6933 O  O    . HOH   F 4 .   ? 27.982 -22.893 -7.970  1.00 18.78 ?  288 HOH   B O    1 
HETATM 6934 O  O    . HOH   F 4 .   ? 45.863 -40.363 -3.600  1.00 31.46 ?  289 HOH   B O    1 
HETATM 6935 O  O    . HOH   F 4 .   ? 35.208 -33.693 4.649   1.00 32.60 ?  290 HOH   B O    1 
HETATM 6936 O  O    . HOH   F 4 .   ? 33.567 -15.287 -13.944 1.00 22.46 ?  291 HOH   B O    1 
HETATM 6937 O  O    . HOH   F 4 .   ? 48.732 -20.024 5.939   1.00 14.79 ?  292 HOH   B O    1 
HETATM 6938 O  O    . HOH   F 4 .   ? 36.040 -43.512 -8.349  1.00 43.22 ?  293 HOH   B O    1 
HETATM 6939 O  O    . HOH   F 4 .   ? 47.076 -33.963 -4.655  1.00 19.46 ?  294 HOH   B O    1 
HETATM 6940 O  O    . HOH   F 4 .   ? 48.613 -12.089 -14.390 1.00 25.58 ?  295 HOH   B O    1 
HETATM 6941 O  O    . HOH   F 4 .   ? 37.468 -17.881 13.112  1.00 33.71 ?  296 HOH   B O    1 
HETATM 6942 O  O    . HOH   F 4 .   ? 52.491 -10.368 12.995  1.00 22.28 ?  297 HOH   B O    1 
HETATM 6943 O  O    . HOH   F 4 .   ? 52.989 -15.946 -12.743 1.00 25.50 ?  298 HOH   B O    1 
HETATM 6944 O  O    . HOH   F 4 .   ? 52.582 -35.626 -8.807  1.00 31.31 ?  299 HOH   B O    1 
HETATM 6945 O  O    . HOH   F 4 .   ? 42.743 -12.204 -18.464 1.00 27.21 ?  300 HOH   B O    1 
HETATM 6946 O  O    . HOH   F 4 .   ? 44.649 -27.476 2.012   1.00 16.87 ?  301 HOH   B O    1 
HETATM 6947 O  O    . HOH   F 4 .   ? 53.691 -12.573 -22.246 1.00 36.45 ?  302 HOH   B O    1 
HETATM 6948 O  O    . HOH   F 4 .   ? 51.221 -37.585 -9.737  1.00 28.37 ?  303 HOH   B O    1 
HETATM 6949 O  O    . HOH   F 4 .   ? 38.402 -12.143 -16.271 1.00 49.85 ?  304 HOH   B O    1 
HETATM 6950 O  O    . HOH   F 4 .   ? 52.480 -29.239 -13.116 1.00 25.51 ?  305 HOH   B O    1 
HETATM 6951 O  O    . HOH   F 4 .   ? 49.942 -24.707 5.844   1.00 35.73 ?  306 HOH   B O    1 
HETATM 6952 O  O    . HOH   F 4 .   ? 36.813 -12.757 -1.432  1.00 28.61 ?  307 HOH   B O    1 
HETATM 6953 O  O    . HOH   F 4 .   ? 40.297 -10.854 -9.504  1.00 18.27 ?  308 HOH   B O    1 
HETATM 6954 O  O    . HOH   F 4 .   ? 37.033 -30.589 -20.977 1.00 31.77 ?  309 HOH   B O    1 
HETATM 6955 O  O    . HOH   F 4 .   ? 53.450 -30.223 4.542   1.00 19.61 ?  310 HOH   B O    1 
HETATM 6956 O  O    . HOH   F 4 .   ? 33.808 -31.067 11.089  1.00 37.18 ?  311 HOH   B O    1 
HETATM 6957 O  O    . HOH   F 4 .   ? 43.260 -21.418 10.690  1.00 17.21 ?  312 HOH   B O    1 
HETATM 6958 O  O    . HOH   F 4 .   ? 44.068 -29.354 -4.659  1.00 23.38 ?  313 HOH   B O    1 
HETATM 6959 O  O    . HOH   F 4 .   ? 62.741 -13.551 4.774   1.00 27.31 ?  314 HOH   B O    1 
HETATM 6960 O  O    . HOH   F 4 .   ? 44.741 -24.587 9.579   1.00 22.47 ?  315 HOH   B O    1 
HETATM 6961 O  O    . HOH   F 4 .   ? 51.703 -6.010  -7.892  1.00 41.15 ?  316 HOH   B O    1 
HETATM 6962 O  O    . HOH   F 4 .   ? 48.144 -32.675 -16.687 1.00 45.73 ?  317 HOH   B O    1 
HETATM 6963 O  O    . HOH   F 4 .   ? 37.894 -10.222 -10.734 1.00 19.42 ?  318 HOH   B O    1 
HETATM 6964 O  O    . HOH   F 4 .   ? 42.477 -9.760  -14.850 1.00 41.03 ?  319 HOH   B O    1 
HETATM 6965 O  O    . HOH   F 4 .   ? 38.361 -12.673 7.943   1.00 18.70 ?  320 HOH   B O    1 
HETATM 6966 O  O    . HOH   F 4 .   ? 25.982 -21.495 -3.492  1.00 18.33 ?  321 HOH   B O    1 
HETATM 6967 O  O    . HOH   F 4 .   ? 41.830 -8.066  1.421   1.00 24.65 ?  322 HOH   B O    1 
HETATM 6968 O  O    . HOH   F 4 .   ? 45.697 -36.303 -16.036 1.00 37.06 ?  323 HOH   B O    1 
HETATM 6969 O  O    . HOH   F 4 .   ? 32.856 -34.604 -5.829  1.00 18.09 ?  324 HOH   B O    1 
HETATM 6970 O  O    . HOH   F 4 .   ? 62.880 -20.219 -0.740  1.00 37.82 ?  325 HOH   B O    1 
HETATM 6971 O  O    . HOH   F 4 .   ? 57.544 -21.920 3.474   1.00 32.05 ?  326 HOH   B O    1 
HETATM 6972 O  O    . HOH   F 4 .   ? 26.374 -21.064 -6.201  1.00 18.39 ?  327 HOH   B O    1 
HETATM 6973 O  O    . HOH   F 4 .   ? 37.296 -35.620 7.288   1.00 34.14 ?  328 HOH   B O    1 
HETATM 6974 O  O    . HOH   F 4 .   ? 36.773 -12.401 4.291   1.00 18.01 ?  329 HOH   B O    1 
HETATM 6975 O  O    . HOH   F 4 .   ? 43.194 -34.554 0.095   1.00 23.48 ?  330 HOH   B O    1 
HETATM 6976 O  O    . HOH   F 4 .   ? 47.284 -24.464 8.173   1.00 27.04 ?  331 HOH   B O    1 
HETATM 6977 O  O    . HOH   F 4 .   ? 38.464 -9.357  -13.279 1.00 30.39 ?  332 HOH   B O    1 
HETATM 6978 O  O    . HOH   F 4 .   ? 42.895 -43.523 -14.352 1.00 44.24 ?  333 HOH   B O    1 
HETATM 6979 O  O    . HOH   F 4 .   ? 59.956 -17.341 -10.549 1.00 37.19 ?  334 HOH   B O    1 
HETATM 6980 O  O    . HOH   F 4 .   ? 51.455 -33.096 -11.001 1.00 48.40 ?  335 HOH   B O    1 
HETATM 6981 O  O    . HOH   F 4 .   ? 44.165 -1.711  7.623   1.00 51.71 ?  336 HOH   B O    1 
HETATM 6982 O  O    . HOH   F 4 .   ? 28.905 -42.804 -12.347 1.00 44.45 ?  337 HOH   B O    1 
HETATM 6983 O  O    . HOH   F 4 .   ? 47.494 -27.446 1.999   1.00 16.43 ?  338 HOH   B O    1 
HETATM 6984 O  O    . HOH   F 4 .   ? 37.119 -15.216 -16.589 1.00 42.83 ?  339 HOH   B O    1 
HETATM 6985 O  O    . HOH   F 4 .   ? 27.750 -14.702 -9.523  1.00 40.42 ?  340 HOH   B O    1 
HETATM 6986 O  O    . HOH   F 4 .   ? 43.509 -15.390 18.055  1.00 30.08 ?  341 HOH   B O    1 
HETATM 6987 O  O    . HOH   F 4 .   ? 37.077 -45.097 -9.687  1.00 36.53 ?  342 HOH   B O    1 
HETATM 6988 O  O    . HOH   F 4 .   ? 34.472 -10.360 7.721   1.00 22.78 ?  343 HOH   B O    1 
HETATM 6989 O  O    . HOH   F 4 .   ? 46.834 -19.913 12.304  1.00 29.19 ?  344 HOH   B O    1 
HETATM 6990 O  O    . HOH   F 4 .   ? 41.333 -24.644 15.873  1.00 44.52 ?  345 HOH   B O    1 
HETATM 6991 O  O    . HOH   F 4 .   ? 39.627 -23.633 -20.375 1.00 37.74 ?  346 HOH   B O    1 
HETATM 6992 O  O    . HOH   F 4 .   ? 33.014 -14.674 1.067   1.00 24.44 ?  347 HOH   B O    1 
HETATM 6993 O  O    . HOH   F 4 .   ? 44.190 -37.395 -17.819 1.00 36.63 ?  348 HOH   B O    1 
HETATM 6994 O  O    . HOH   F 4 .   ? 39.899 -44.147 -11.231 1.00 46.29 ?  349 HOH   B O    1 
HETATM 6995 O  O    . HOH   F 4 .   ? 38.646 -22.472 15.083  1.00 43.99 ?  350 HOH   B O    1 
HETATM 6996 O  O    . HOH   F 4 .   ? 40.411 -43.476 -9.147  1.00 26.71 ?  351 HOH   B O    1 
HETATM 6997 O  O    . HOH   F 4 .   ? 33.712 -9.618  -8.871  1.00 32.60 ?  352 HOH   B O    1 
HETATM 6998 O  O    . HOH   F 4 .   ? 62.549 -20.067 -4.863  1.00 47.12 ?  353 HOH   B O    1 
HETATM 6999 O  O    . HOH   F 4 .   ? 27.826 -26.642 -0.483  1.00 32.09 ?  354 HOH   B O    1 
HETATM 7000 O  O    . HOH   F 4 .   ? 55.672 -8.216  10.760  1.00 24.69 ?  355 HOH   B O    1 
HETATM 7001 O  O    . HOH   F 4 .   ? 33.951 -7.908  11.530  1.00 38.59 ?  356 HOH   B O    1 
HETATM 7002 O  O    . HOH   F 4 .   ? 23.267 -23.661 6.807   1.00 34.91 ?  357 HOH   B O    1 
HETATM 7003 O  O    . HOH   F 4 .   ? 56.652 -7.260  2.935   1.00 29.05 ?  358 HOH   B O    1 
HETATM 7004 O  O    . HOH   F 4 .   ? 36.135 -8.500  -9.810  1.00 35.05 ?  359 HOH   B O    1 
HETATM 7005 O  O    . HOH   F 4 .   ? 56.877 -21.650 -16.462 1.00 40.71 ?  360 HOH   B O    1 
HETATM 7006 O  O    . HOH   F 4 .   ? 61.538 -19.924 1.785   1.00 38.40 ?  361 HOH   B O    1 
HETATM 7007 O  O    . HOH   F 4 .   ? 40.267 -8.801  9.862   1.00 36.72 ?  362 HOH   B O    1 
HETATM 7008 O  O    . HOH   F 4 .   ? 40.515 -11.291 -13.876 1.00 35.03 ?  363 HOH   B O    1 
HETATM 7009 O  O    . HOH   F 4 .   ? 27.145 -25.871 -11.318 1.00 34.10 ?  364 HOH   B O    1 
HETATM 7010 O  O    . HOH   F 4 .   ? 43.230 -12.661 -21.135 1.00 40.32 ?  365 HOH   B O    1 
HETATM 7011 O  O    . HOH   F 4 .   ? 48.358 -26.405 8.798   1.00 43.17 ?  366 HOH   B O    1 
HETATM 7012 O  O    . HOH   F 4 .   ? 36.188 -8.679  8.953   1.00 34.93 ?  367 HOH   B O    1 
HETATM 7013 O  O    . HOH   F 4 .   ? 32.683 -23.638 13.992  1.00 39.64 ?  368 HOH   B O    1 
HETATM 7014 O  O    . HOH   F 4 .   ? 54.239 -5.763  2.890   1.00 38.63 ?  369 HOH   B O    1 
HETATM 7015 O  O    . HOH   F 4 .   ? 52.097 -12.964 13.251  1.00 28.80 ?  370 HOH   B O    1 
HETATM 7016 O  O    . HOH   F 4 .   ? 39.831 -7.094  7.807   1.00 39.34 ?  371 HOH   B O    1 
HETATM 7017 O  O    . HOH   F 4 .   ? 56.026 -7.832  -0.644  1.00 37.01 ?  372 HOH   B O    1 
HETATM 7018 O  O    . HOH   F 4 .   ? 59.040 -10.395 9.143   1.00 42.75 ?  373 HOH   B O    1 
HETATM 7019 O  O    . HOH   F 4 .   ? 41.887 -9.975  -17.433 1.00 60.20 ?  374 HOH   B O    1 
HETATM 7020 O  O    . HOH   F 4 .   ? 63.101 -12.400 7.004   1.00 35.43 ?  375 HOH   B O    1 
HETATM 7021 O  O    . HOH   F 4 .   ? 41.864 -6.742  -4.864  1.00 46.19 ?  376 HOH   B O    1 
HETATM 7022 O  O    . HOH   F 4 .   ? 38.009 -10.530 10.030  1.00 29.09 ?  377 HOH   B O    1 
HETATM 7023 O  O    . HOH   F 4 .   ? 40.205 -7.722  3.111   1.00 41.63 ?  378 HOH   B O    1 
HETATM 7024 O  O    . HOH   F 4 .   ? 44.184 -5.612  -3.521  1.00 39.28 ?  379 HOH   B O    1 
HETATM 7025 O  O    . HOH   F 4 .   ? 42.659 -17.037 -23.151 1.00 42.81 ?  380 HOH   B O    1 
HETATM 7026 O  O    . HOH   F 4 .   ? 36.522 -22.894 13.255  1.00 35.58 ?  381 HOH   B O    1 
HETATM 7027 O  O    . HOH   F 4 .   ? 39.631 -14.096 15.563  1.00 48.39 ?  382 HOH   B O    1 
HETATM 7028 O  O    . HOH   F 4 .   ? 60.488 -22.240 2.894   1.00 49.62 ?  383 HOH   B O    1 
HETATM 7029 O  O    . HOH   F 4 .   ? 46.812 -5.439  2.891   1.00 39.68 ?  384 HOH   B O    1 
HETATM 7030 O  O    . HOH   F 4 .   ? 41.110 -9.701  15.765  1.00 53.17 ?  385 HOH   B O    1 
HETATM 7031 O  O    . HOH   F 4 .   ? 52.900 -29.926 7.276   1.00 23.39 ?  386 HOH   B O    1 
HETATM 7032 O  O    . HOH   F 4 .   ? 23.232 -23.802 1.479   1.00 35.28 ?  387 HOH   B O    1 
HETATM 7033 O  O    . HOH   F 4 .   ? 35.515 -33.733 7.414   1.00 43.35 ?  388 HOH   B O    1 
HETATM 7034 O  O    . HOH   F 4 .   ? 35.256 -20.427 13.298  1.00 35.75 ?  389 HOH   B O    1 
HETATM 7035 O  O    . HOH   F 4 .   ? 23.951 -20.941 -7.665  1.00 30.64 ?  390 HOH   B O    1 
HETATM 7036 O  O    . HOH   F 4 .   ? 40.753 -6.640  -0.881  1.00 27.36 ?  391 HOH   B O    1 
HETATM 7037 O  O    . HOH   F 4 .   ? 28.044 -27.069 2.276   1.00 29.13 ?  392 HOH   B O    1 
HETATM 7038 O  O    . HOH   F 4 .   ? 44.145 -31.722 -3.721  1.00 43.65 ?  393 HOH   B O    1 
HETATM 7039 O  O    . HOH   F 4 .   ? 26.611 -27.903 -13.416 1.00 39.02 ?  394 HOH   B O    1 
HETATM 7040 O  O    . HOH   F 4 .   ? 50.692 -30.912 8.725   1.00 31.09 ?  395 HOH   B O    1 
HETATM 7041 O  O    . HOH   F 4 .   ? 26.825 -30.652 -12.608 1.00 29.05 ?  396 HOH   B O    1 
HETATM 7042 O  O    . HOH   F 4 .   ? 24.625 -20.646 -10.496 1.00 42.19 ?  397 HOH   B O    1 
HETATM 7043 O  O    . HOH   F 4 .   ? 34.399 -33.524 9.628   1.00 37.83 ?  398 HOH   B O    1 
HETATM 7044 O  O    . HOH   F 4 .   ? 45.763 -20.063 15.243  1.00 42.88 ?  399 HOH   B O    1 
HETATM 7045 O  O    . HOH   F 4 .   ? 57.777 -6.551  -2.353  1.00 34.92 ?  400 HOH   B O    1 
HETATM 7046 O  O    . HOH   F 4 .   ? 40.842 -11.805 -22.242 1.00 39.09 ?  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   ? 0.7866 0.7814 0.8506 -0.0023 -0.0413 0.0850  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7820 0.7774 0.8178 -0.0053 -0.0288 0.0596  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7831 0.7781 0.8388 -0.0035 -0.0401 0.0839  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7788 0.7745 0.8110 -0.0063 -0.0288 0.0608  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.7643 0.7618 0.8157 -0.0104 -0.0364 0.0831  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.7621 0.7599 0.7971 -0.0120 -0.0300 0.0703  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.7683 0.7649 0.8342 -0.0091 -0.0383 0.0854  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.7661 0.7629 0.8099 -0.0111 -0.0312 0.0709  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7944 0.7880 0.8401 0.0006  -0.0406 0.0834  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7886 0.7833 0.8117 -0.0029 -0.0266 0.0537  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7978 0.7910 0.8392 0.0021  -0.0404 0.0833  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7915 0.7859 0.8112 -0.0018 -0.0257 0.0513  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7978 0.7909 0.8393 0.0022  -0.0404 0.0837  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7916 0.7860 0.8112 -0.0017 -0.0257 0.0515  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.7389 0.7401 0.7620 -0.0195 -0.0283 0.0790  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.6876 0.6962 0.6631 -0.0376 -0.0175 0.0808  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.6187 0.6469 0.6029 -0.0593 0.0070  0.0531  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.6210 0.6488 0.6014 -0.0587 0.0046  0.0552  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.7006 0.6981 0.6206 -0.0357 -0.0297 0.1088  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.7107 0.6985 0.5803 -0.0355 -0.0392 0.1329  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.7154 0.6987 0.5645 -0.0360 -0.0423 0.1415  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.7136 0.6990 0.5693 -0.0350 -0.0416 0.1421  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.5817 0.6200 0.5694 -0.0721 0.0215  0.0391  5   SER   A N   
47   N  N   B SER   A 5   ? 0.5816 0.6191 0.5714 -0.0702 0.0195  0.0386  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.5437 0.5916 0.5354 -0.0841 0.0384  0.0267  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.5436 0.5898 0.5381 -0.0814 0.0343  0.0258  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.5016 0.5546 0.4819 -0.0974 0.0574  0.0253  5   SER   A C   
51   C  C   B SER   A 5   ? 0.5018 0.5539 0.4876 -0.0956 0.0533  0.0243  5   SER   A C   
52   O  O   A SER   A 5   ? 0.5031 0.5577 0.4735 -0.0959 0.0631  0.0204  5   SER   A O   
53   O  O   B SER   A 5   ? 0.5034 0.5566 0.4861 -0.0949 0.0553  0.0195  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.5478 0.5990 0.5553 -0.0823 0.0370  0.0187  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.5469 0.5952 0.5535 -0.0788 0.0313  0.0183  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.5499 0.6027 0.5675 -0.0809 0.0367  0.0148  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.5486 0.5980 0.5623 -0.0772 0.0296  0.0146  5   SER   A OG  
68   N  N   . PHE   A 6   ? 0.4570 0.5140 0.4394 -0.1106 0.0699  0.0308  6   PHE   A N   
69   C  CA  . PHE   A 6   ? 0.3710 0.4343 0.3586 -0.1341 0.0868  0.0448  6   PHE   A CA  
70   C  C   . PHE   A 6   ? 0.3511 0.4215 0.3577 -0.1441 0.1040  0.0415  6   PHE   A C   
71   O  O   . PHE   A 6   ? 0.3553 0.4278 0.3733 -0.1417 0.1058  0.0494  6   PHE   A O   
72   C  CB  . PHE   A 6   ? 0.3198 0.3762 0.3126 -0.1310 0.0630  0.0461  6   PHE   A CB  
73   C  CG  . PHE   A 6   ? 0.2799 0.3324 0.2805 -0.1150 0.0441  0.0410  6   PHE   A CG  
74   C  CD1 . PHE   A 6   ? 0.2586 0.3160 0.2691 -0.0989 0.0391  0.0350  6   PHE   A CD1 
75   C  CD2 . PHE   A 6   ? 0.2761 0.3209 0.2854 -0.0953 0.0410  0.0364  6   PHE   A CD2 
76   C  CE1 . PHE   A 6   ? 0.2485 0.3059 0.2701 -0.0931 0.0416  0.0295  6   PHE   A CE1 
77   C  CE2 . PHE   A 6   ? 0.2676 0.3114 0.2870 -0.0863 0.0400  0.0301  6   PHE   A CE2 
78   C  CZ  . PHE   A 6   ? 0.2544 0.3019 0.2769 -0.0901 0.0404  0.0272  6   PHE   A CZ  
89   N  N   . SER   A 7   ? 0.3328 0.4036 0.3507 -0.1456 0.1086  0.0246  7   SER   A N   
90   C  CA  . SER   A 7   ? 0.3327 0.3971 0.3652 -0.1307 0.1029  -0.0023 7   SER   A CA  
91   C  C   . SER   A 7   ? 0.2937 0.3541 0.3377 -0.1154 0.1014  -0.0051 7   SER   A C   
92   O  O   . SER   A 7   ? 0.2935 0.3435 0.3390 -0.1183 0.1029  -0.0000 7   SER   A O   
93   C  CB  . SER   A 7   ? 0.3633 0.4252 0.4020 -0.1258 0.1021  -0.0085 7   SER   A CB  
94   O  OG  . SER   A 7   ? 0.3683 0.4317 0.4375 -0.1163 0.0978  -0.0100 7   SER   A OG  
100  N  N   . GLY   A 8   ? 0.2606 0.3220 0.3232 -0.1011 0.0909  -0.0081 8   GLY   A N   
101  C  CA  . GLY   A 8   ? 0.2388 0.2910 0.3169 -0.0732 0.0830  -0.0050 8   GLY   A CA  
102  C  C   . GLY   A 8   ? 0.2128 0.2634 0.3062 -0.0525 0.0621  -0.0016 8   GLY   A C   
103  O  O   . GLY   A 8   ? 0.2065 0.2572 0.3268 -0.0295 0.0601  -0.0212 8   GLY   A O   
107  N  N   . TYR   A 9   ? 0.1850 0.2408 0.2820 -0.0424 0.0510  0.0224  9   TYR   A N   
108  C  CA  . TYR   A 9   ? 0.1678 0.2227 0.2651 -0.0333 0.0389  0.0314  9   TYR   A CA  
109  C  C   . TYR   A 9   ? 0.1717 0.2025 0.2543 -0.0178 0.0456  0.0553  9   TYR   A C   
110  O  O   . TYR   A 9   ? 0.1969 0.2182 0.2807 -0.0272 0.0359  0.0520  9   TYR   A O   
111  C  CB  . TYR   A 9   ? 0.1666 0.2296 0.2617 -0.0232 0.0312  0.0259  9   TYR   A CB  
112  C  CG  . TYR   A 9   ? 0.1641 0.2369 0.2533 -0.0145 0.0381  0.0203  9   TYR   A CG  
113  C  CD1 . TYR   A 9   ? 0.1682 0.2491 0.2591 -0.0259 0.0423  0.0101  9   TYR   A CD1 
114  C  CD2 . TYR   A 9   ? 0.1555 0.2309 0.2422 -0.0118 0.0320  0.0243  9   TYR   A CD2 
115  C  CE1 . TYR   A 9   ? 0.1755 0.2541 0.2712 -0.0287 0.0419  0.0020  9   TYR   A CE1 
116  C  CE2 . TYR   A 9   ? 0.1615 0.2379 0.2536 -0.0165 0.0346  0.0185  9   TYR   A CE2 
117  C  CZ  . TYR   A 9   ? 0.1689 0.2455 0.2736 -0.0334 0.0488  0.0144  9   TYR   A CZ  
118  O  OH  . TYR   A 9   ? 0.1783 0.2541 0.3013 -0.0489 0.0482  0.0099  9   TYR   A OH  
128  N  N   . LEU   A 10  ? 0.1653 0.1835 0.2591 -0.0188 0.0358  0.0490  10  LEU   A N   
129  C  CA  . LEU   A 10  ? 0.1558 0.1809 0.2747 -0.0244 0.0173  0.0569  10  LEU   A CA  
130  C  C   . LEU   A 10  ? 0.1511 0.1731 0.2606 -0.0250 0.0137  0.0543  10  LEU   A C   
131  O  O   . LEU   A 10  ? 0.1623 0.1668 0.2498 -0.0238 0.0349  0.0515  10  LEU   A O   
132  C  CB  . LEU   A 10  ? 0.1639 0.1952 0.3120 -0.0290 0.0005  0.0781  10  LEU   A CB  
133  C  CG  . LEU   A 10  ? 0.1919 0.2101 0.3547 -0.0250 -0.0283 0.0966  10  LEU   A CG  
134  C  CD1 . LEU   A 10  ? 0.2180 0.2270 0.3890 -0.0336 -0.0194 0.0839  10  LEU   A CD1 
135  C  CD2 . LEU   A 10  ? 0.2239 0.2359 0.3879 -0.0214 -0.0104 0.0784  10  LEU   A CD2 
147  N  N   . LYS   A 11  ? 0.1525 0.1759 0.2632 -0.0310 0.0252  0.0566  11  LYS   A N   
148  C  CA  . LYS   A 11  ? 0.1556 0.1718 0.2567 -0.0344 0.0142  0.0572  11  LYS   A CA  
149  C  C   . LYS   A 11  ? 0.1533 0.1830 0.2616 -0.0430 0.0151  0.0488  11  LYS   A C   
150  O  O   . LYS   A 11  ? 0.1632 0.2274 0.2712 -0.0651 0.0170  0.0422  11  LYS   A O   
151  C  CB  . LYS   A 11  ? 0.1668 0.1654 0.2424 -0.0307 0.0069  0.0390  11  LYS   A CB  
152  C  CG  . LYS   A 11  ? 0.1825 0.1591 0.2266 -0.0330 0.0064  0.0452  11  LYS   A CG  
153  C  CD  . LYS   A 11  ? 0.1929 0.1709 0.2255 -0.0270 -0.0009 0.0380  11  LYS   A CD  
154  C  CE  . LYS   A 11  ? 0.2009 0.1698 0.2221 -0.0219 0.0052  0.0472  11  LYS   A CE  
155  N  NZ  . LYS   A 11  ? 0.2006 0.1658 0.2368 -0.0072 0.0025  0.0409  11  LYS   A NZ  
169  N  N   . LEU   A 12  ? 0.1412 0.1705 0.2592 -0.0322 0.0065  0.0420  12  LEU   A N   
170  C  CA  . LEU   A 12  ? 0.1476 0.1834 0.2502 -0.0313 0.0004  0.0548  12  LEU   A CA  
171  C  C   . LEU   A 12  ? 0.1532 0.1731 0.2414 -0.0329 0.0112  0.0517  12  LEU   A C   
172  O  O   . LEU   A 12  ? 0.1640 0.1768 0.2488 -0.0348 0.0080  0.0389  12  LEU   A O   
173  C  CB  . LEU   A 12  ? 0.1549 0.1866 0.2716 -0.0221 -0.0034 0.0619  12  LEU   A CB  
174  C  CG  . LEU   A 12  ? 0.1637 0.1951 0.2996 -0.0188 0.0081  0.0705  12  LEU   A CG  
175  C  CD1 . LEU   A 12  ? 0.1845 0.2017 0.3040 -0.0038 0.0287  0.0794  12  LEU   A CD1 
176  C  CD2 . LEU   A 12  ? 0.1636 0.2010 0.3307 -0.0205 -0.0001 0.0715  12  LEU   A CD2 
188  N  N   . THR   A 13  ? 0.1499 0.1670 0.2470 -0.0268 0.0159  0.0381  13  THR   A N   
189  C  CA  . THR   A 13  ? 0.1570 0.1660 0.2557 -0.0269 0.0202  0.0403  13  THR   A CA  
190  C  C   . THR   A 13  ? 0.1547 0.1653 0.2609 -0.0319 0.0179  0.0402  13  THR   A C   
191  O  O   . THR   A 13  ? 0.1521 0.1649 0.2511 -0.0237 0.0172  0.0446  13  THR   A O   
192  C  CB  . THR   A 13  ? 0.1650 0.1805 0.2573 -0.0223 0.0195  0.0489  13  THR   A CB  
193  O  OG1 . THR   A 13  ? 0.1597 0.1814 0.2770 -0.0306 0.0196  0.0499  13  THR   A OG1 
194  C  CG2 . THR   A 13  ? 0.1735 0.1986 0.2545 -0.0208 0.0227  0.0362  13  THR   A CG2 
202  N  N   . ASP   A 14  ? 0.1698 0.1671 0.2735 -0.0312 0.0088  0.0606  14  ASP   A N   
203  C  CA  . ASP   A 14  ? 0.1718 0.1756 0.2972 -0.0303 0.0009  0.0661  14  ASP   A CA  
204  C  C   . ASP   A 14  ? 0.1653 0.1731 0.2620 -0.0271 -0.0030 0.0659  14  ASP   A C   
205  O  O   . ASP   A 14  ? 0.1777 0.1895 0.2700 -0.0389 -0.0008 0.0667  14  ASP   A O   
206  C  CB  . ASP   A 14  ? 0.2058 0.2003 0.3466 -0.0437 -0.0090 0.1002  14  ASP   A CB  
207  C  CG  . ASP   A 14  ? 0.2346 0.2571 0.4137 -0.0478 -0.0113 0.1086  14  ASP   A CG  
208  O  OD1 . ASP   A 14  ? 0.2587 0.2847 0.4409 -0.0238 -0.0345 0.1105  14  ASP   A OD1 
209  O  OD2 . ASP   A 14  ? 0.2818 0.2914 0.4605 -0.0361 -0.0148 0.0872  14  ASP   A OD2 
214  N  N   . ASN   A 15  ? 0.1525 0.1587 0.2602 -0.0255 0.0060  0.0627  15  ASN   A N   
215  C  CA  . ASN   A 15  ? 0.1511 0.1581 0.2835 -0.0224 -0.0041 0.0545  15  ASN   A CA  
216  C  C   . ASN   A 15  ? 0.1440 0.1561 0.2953 -0.0222 -0.0002 0.0521  15  ASN   A C   
217  O  O   . ASN   A 15  ? 0.1440 0.1625 0.3309 -0.0269 -0.0164 0.0540  15  ASN   A O   
218  C  CB  . ASN   A 15  ? 0.1455 0.1613 0.2767 -0.0144 0.0005  0.0556  15  ASN   A CB  
219  C  CG  . ASN   A 15  ? 0.1408 0.1682 0.2851 -0.0118 0.0122  0.0428  15  ASN   A CG  
220  O  OD1 . ASN   A 15  ? 0.1565 0.1716 0.3137 -0.0284 -0.0016 0.0402  15  ASN   A OD1 
221  N  ND2 . ASN   A 15  ? 0.1453 0.1716 0.2749 -0.0179 0.0082  0.0383  15  ASN   A ND2 
228  N  N   . VAL   A 16  ? 0.1470 0.1546 0.2845 -0.0184 0.0014  0.0594  16  VAL   A N   
229  C  CA  . VAL   A 16  ? 0.1429 0.1570 0.2733 -0.0180 0.0079  0.0549  16  VAL   A CA  
230  C  C   . VAL   A 16  ? 0.1410 0.1581 0.2698 -0.0205 0.0012  0.0535  16  VAL   A C   
231  O  O   . VAL   A 16  ? 0.1322 0.1561 0.2802 -0.0282 0.0114  0.0424  16  VAL   A O   
232  C  CB  . VAL   A 16  ? 0.1569 0.1707 0.2596 -0.0016 0.0256  0.0638  16  VAL   A CB  
233  C  CG1 . VAL   A 16  ? 0.1670 0.1847 0.2637 0.0050  0.0313  0.0612  16  VAL   A CG1 
234  C  CG2 . VAL   A 16  ? 0.1648 0.1891 0.2749 0.0054  0.0389  0.0613  16  VAL   A CG2 
244  N  N   . TYR   A 17  ? 0.1417 0.1521 0.2608 -0.0152 0.0198  0.0593  17  TYR   A N   
245  C  CA  . TYR   A 17  ? 0.1453 0.1546 0.2432 -0.0214 0.0163  0.0551  17  TYR   A CA  
246  C  C   . TYR   A 17  ? 0.1495 0.1559 0.2528 -0.0200 0.0150  0.0475  17  TYR   A C   
247  O  O   . TYR   A 17  ? 0.1395 0.1650 0.2727 -0.0216 0.0250  0.0606  17  TYR   A O   
248  C  CB  . TYR   A 17  ? 0.1617 0.1623 0.2408 -0.0258 0.0104  0.0484  17  TYR   A CB  
249  C  CG  . TYR   A 17  ? 0.1822 0.1677 0.2438 -0.0322 -0.0062 0.0436  17  TYR   A CG  
250  C  CD1 . TYR   A 17  ? 0.1980 0.1793 0.2551 -0.0166 -0.0070 0.0473  17  TYR   A CD1 
251  C  CD2 . TYR   A 17  ? 0.1984 0.1729 0.2453 -0.0501 -0.0015 0.0429  17  TYR   A CD2 
252  C  CE1 . TYR   A 17  ? 0.2156 0.1782 0.2597 -0.0228 -0.0158 0.0424  17  TYR   A CE1 
253  C  CE2 . TYR   A 17  ? 0.2197 0.1743 0.2428 -0.0503 -0.0067 0.0306  17  TYR   A CE2 
254  C  CZ  . TYR   A 17  ? 0.2317 0.1735 0.2556 -0.0377 -0.0232 0.0473  17  TYR   A CZ  
255  O  OH  . TYR   A 17  ? 0.2528 0.1814 0.2700 -0.0387 -0.0191 0.0482  17  TYR   A OH  
265  N  N   A ILE   A 18  ? 0.1418 0.1544 0.2600 -0.0153 0.0222  0.0526  18  ILE   A N   
266  N  N   B ILE   A 18  ? 0.1544 0.1623 0.2224 -0.0165 0.0161  0.0527  18  ILE   A N   
267  C  CA  A ILE   A 18  ? 0.1399 0.1519 0.2666 -0.0135 0.0301  0.0450  18  ILE   A CA  
268  C  CA  B ILE   A 18  ? 0.1623 0.1683 0.2009 -0.0113 0.0171  0.0478  18  ILE   A CA  
269  C  C   A ILE   A 18  ? 0.1423 0.1622 0.2783 -0.0241 0.0348  0.0423  18  ILE   A C   
270  C  C   B ILE   A 18  ? 0.1645 0.1820 0.1939 -0.0112 0.0121  0.0482  18  ILE   A C   
271  O  O   A ILE   A 18  ? 0.1330 0.1720 0.2794 -0.0368 0.0257  0.0389  18  ILE   A O   
272  O  O   B ILE   A 18  ? 0.1629 0.1884 0.1881 -0.0172 0.0052  0.0523  18  ILE   A O   
273  C  CB  A ILE   A 18  ? 0.1567 0.1542 0.2461 -0.0009 0.0234  0.0503  18  ILE   A CB  
274  C  CB  B ILE   A 18  ? 0.1746 0.1667 0.1876 -0.0056 0.0216  0.0483  18  ILE   A CB  
275  C  CG1 A ILE   A 18  ? 0.1676 0.1709 0.2437 0.0008  0.0063  0.0569  18  ILE   A CG1 
276  C  CG1 B ILE   A 18  ? 0.1842 0.1745 0.1914 -0.0086 0.0168  0.0603  18  ILE   A CG1 
277  C  CG2 A ILE   A 18  ? 0.1541 0.1432 0.2444 0.0011  0.0261  0.0420  18  ILE   A CG2 
278  C  CG2 B ILE   A 18  ? 0.1801 0.1671 0.1859 -0.0105 0.0278  0.0455  18  ILE   A CG2 
279  C  CD1 A ILE   A 18  ? 0.1976 0.1956 0.2656 0.0087  0.0069  0.0655  18  ILE   A CD1 
280  C  CD1 B ILE   A 18  ? 0.1981 0.1848 0.1976 -0.0077 0.0141  0.0592  18  ILE   A CD1 
303  N  N   A LYS   A 19  ? 0.1467 0.1657 0.2884 -0.0127 0.0570  0.0482  19  LYS   A N   
304  N  N   B LYS   A 19  ? 0.1685 0.1881 0.2046 -0.0021 0.0265  0.0423  19  LYS   A N   
305  C  CA  A LYS   A 19  ? 0.1663 0.1775 0.2931 -0.0068 0.0559  0.0437  19  LYS   A CA  
306  C  CA  B LYS   A 19  ? 0.1792 0.1967 0.2270 0.0038  0.0240  0.0361  19  LYS   A CA  
307  C  C   A LYS   A 19  ? 0.1524 0.1684 0.3058 0.0000  0.0492  0.0362  19  LYS   A C   
308  C  C   B LYS   A 19  ? 0.1698 0.1947 0.2400 0.0018  0.0264  0.0330  19  LYS   A C   
309  O  O   A LYS   A 19  ? 0.1382 0.1581 0.2933 -0.0044 0.0304  0.0381  19  LYS   A O   
310  O  O   B LYS   A 19  ? 0.1665 0.1927 0.2391 0.0022  0.0160  0.0337  19  LYS   A O   
311  C  CB  A LYS   A 19  ? 0.1898 0.1977 0.2841 -0.0058 0.0752  0.0348  19  LYS   A CB  
312  C  CB  B LYS   A 19  ? 0.1960 0.2051 0.2404 0.0089  0.0195  0.0307  19  LYS   A CB  
313  C  CG  A LYS   A 19  ? 0.2197 0.2169 0.2848 -0.0079 0.0748  0.0240  19  LYS   A CG  
314  C  CG  B LYS   A 19  ? 0.2109 0.2101 0.2501 0.0096  0.0101  0.0331  19  LYS   A CG  
315  C  CD  A LYS   A 19  ? 0.2487 0.2293 0.2697 -0.0129 0.0759  0.0267  19  LYS   A CD  
316  C  CD  B LYS   A 19  ? 0.2227 0.2128 0.2553 0.0099  0.0010  0.0402  19  LYS   A CD  
317  C  CE  A LYS   A 19  ? 0.2686 0.2452 0.2768 -0.0173 0.0713  0.0169  19  LYS   A CE  
318  C  CE  B LYS   A 19  ? 0.2255 0.2123 0.2572 0.0121  -0.0040 0.0480  19  LYS   A CE  
319  N  NZ  A LYS   A 19  ? 0.2805 0.2523 0.2720 -0.0207 0.0709  0.0049  19  LYS   A NZ  
320  N  NZ  B LYS   A 19  ? 0.2243 0.2070 0.2584 0.0147  -0.0028 0.0555  19  LYS   A NZ  
347  N  N   A ASN   A 20  ? 0.1639 0.1787 0.3377 0.0026  0.0540  0.0436  20  ASN   A N   
348  N  N   B ASN   A 20  ? 0.1672 0.1943 0.2582 -0.0059 0.0326  0.0312  20  ASN   A N   
349  C  CA  A ASN   A 20  ? 0.1848 0.2000 0.3498 0.0286  0.0545  0.0411  20  ASN   A CA  
350  C  CA  B ASN   A 20  ? 0.1680 0.1978 0.2663 -0.0033 0.0365  0.0255  20  ASN   A CA  
351  C  C   A ASN   A 20  ? 0.2013 0.2044 0.3438 0.0233  0.0604  0.0348  20  ASN   A C   
352  C  C   B ASN   A 20  ? 0.1760 0.1976 0.2712 -0.0156 0.0481  0.0171  20  ASN   A C   
353  O  O   A ASN   A 20  ? 0.2242 0.2179 0.3413 0.0051  0.0540  0.0352  20  ASN   A O   
354  O  O   B ASN   A 20  ? 0.1899 0.2041 0.2817 -0.0203 0.0460  0.0151  20  ASN   A O   
355  C  CB  A ASN   A 20  ? 0.1951 0.2170 0.3661 0.0423  0.0531  0.0537  20  ASN   A CB  
356  C  CB  B ASN   A 20  ? 0.1619 0.2020 0.2681 0.0026  0.0315  0.0314  20  ASN   A CB  
357  C  CG  A ASN   A 20  ? 0.2086 0.2288 0.3855 0.0597  0.0520  0.0598  20  ASN   A CG  
358  C  CG  B ASN   A 20  ? 0.1588 0.2043 0.2751 0.0120  0.0267  0.0358  20  ASN   A CG  
359  O  OD1 A ASN   A 20  ? 0.2341 0.2417 0.4089 0.0607  0.0553  0.0459  20  ASN   A OD1 
360  O  OD1 B ASN   A 20  ? 0.1618 0.2027 0.2828 0.0207  0.0244  0.0287  20  ASN   A OD1 
361  N  ND2 A ASN   A 20  ? 0.2187 0.2317 0.3998 0.0667  0.0372  0.0753  20  ASN   A ND2 
362  N  ND2 B ASN   A 20  ? 0.1667 0.2080 0.2877 0.0081  0.0229  0.0440  20  ASN   A ND2 
375  N  N   A ALA   A 21  ? 0.2008 0.2051 0.3451 0.0238  0.0501  0.0264  21  ALA   A N   
376  N  N   B ALA   A 21  ? 0.1736 0.1942 0.2700 -0.0241 0.0478  0.0077  21  ALA   A N   
377  C  CA  A ALA   A 21  ? 0.2078 0.2092 0.3332 0.0186  0.0459  0.0363  21  ALA   A CA  
378  C  CA  B ALA   A 21  ? 0.1796 0.1927 0.2654 -0.0303 0.0513  0.0077  21  ALA   A CA  
379  C  C   A ALA   A 21  ? 0.1975 0.2036 0.3223 0.0134  0.0464  0.0395  21  ALA   A C   
380  C  C   B ALA   A 21  ? 0.1699 0.1839 0.2553 -0.0335 0.0572  0.0007  21  ALA   A C   
381  O  O   A ALA   A 21  ? 0.1989 0.2084 0.3289 0.0137  0.0479  0.0384  21  ALA   A O   
382  O  O   B ALA   A 21  ? 0.1649 0.1803 0.2648 -0.0361 0.0534  -0.0130 21  ALA   A O   
383  C  CB  A ALA   A 21  ? 0.2286 0.2198 0.3399 0.0160  0.0402  0.0382  21  ALA   A CB  
384  C  CB  B ALA   A 21  ? 0.1945 0.2002 0.2704 -0.0296 0.0454  0.0097  21  ALA   A CB  
395  N  N   A ASP   A 22  ? 0.1926 0.1955 0.3176 0.0099  0.0477  0.0349  22  ASP   A N   
396  N  N   B ASP   A 22  ? 0.1709 0.1816 0.2498 -0.0287 0.0593  -0.0006 22  ASP   A N   
397  C  CA  A ASP   A 22  ? 0.1888 0.1912 0.3098 0.0072  0.0400  0.0341  22  ASP   A CA  
398  C  CA  B ASP   A 22  ? 0.1734 0.1816 0.2421 -0.0228 0.0577  0.0010  22  ASP   A CA  
399  C  C   A ASP   A 22  ? 0.1782 0.1919 0.2601 0.0012  0.0405  0.0323  22  ASP   A C   
400  C  C   B ASP   A 22  ? 0.1629 0.1781 0.2133 -0.0293 0.0621  -0.0020 22  ASP   A C   
401  O  O   A ASP   A 22  ? 0.1911 0.2003 0.2607 -0.0079 0.0391  0.0258  22  ASP   A O   
402  O  O   B ASP   A 22  ? 0.1642 0.1801 0.2201 -0.0339 0.0571  -0.0145 22  ASP   A O   
403  C  CB  A ASP   A 22  ? 0.2083 0.1963 0.3633 0.0064  0.0416  0.0246  22  ASP   A CB  
404  C  CB  B ASP   A 22  ? 0.1888 0.1885 0.2713 -0.0073 0.0566  0.0003  22  ASP   A CB  
405  C  CG  A ASP   A 22  ? 0.2215 0.1977 0.4088 0.0018  0.0311  0.0325  22  ASP   A CG  
406  C  CG  B ASP   A 22  ? 0.1973 0.1929 0.2957 0.0055  0.0548  0.0074  22  ASP   A CG  
407  O  OD1 A ASP   A 22  ? 0.2196 0.1884 0.4212 -0.0137 0.0104  0.0491  22  ASP   A OD1 
408  O  OD1 B ASP   A 22  ? 0.1962 0.1886 0.2988 0.0061  0.0519  0.0087  22  ASP   A OD1 
409  O  OD2 A ASP   A 22  ? 0.2372 0.2052 0.4398 0.0159  0.0452  0.0206  22  ASP   A OD2 
410  O  OD2 B ASP   A 22  ? 0.2048 0.2054 0.3110 0.0097  0.0548  0.0130  22  ASP   A OD2 
419  N  N   A ILE   A 23  ? 0.1758 0.1902 0.2427 0.0071  0.0425  0.0267  23  ILE   A N   
420  N  N   B ILE   A 23  ? 0.1634 0.1758 0.2010 -0.0238 0.0533  0.0024  23  ILE   A N   
421  C  CA  A ILE   A 23  ? 0.1713 0.1865 0.2295 0.0013  0.0405  0.0298  23  ILE   A CA  
422  C  CA  B ILE   A 23  ? 0.1633 0.1780 0.1848 -0.0278 0.0456  0.0090  23  ILE   A CA  
423  C  C   A ILE   A 23  ? 0.1704 0.2010 0.2190 0.0022  0.0490  0.0242  23  ILE   A C   
424  C  C   B ILE   A 23  ? 0.1722 0.1936 0.1856 -0.0346 0.0457  0.0017  23  ILE   A C   
425  O  O   A ILE   A 23  ? 0.1707 0.2136 0.2222 0.0053  0.0436  0.0231  23  ILE   A O   
426  O  O   B ILE   A 23  ? 0.1696 0.1974 0.1876 -0.0318 0.0477  0.0003  23  ILE   A O   
427  C  CB  A ILE   A 23  ? 0.1859 0.1869 0.2056 0.0065  0.0308  0.0194  23  ILE   A CB  
428  C  CB  B ILE   A 23  ? 0.1650 0.1721 0.1686 -0.0171 0.0318  0.0133  23  ILE   A CB  
429  C  CG1 A ILE   A 23  ? 0.1885 0.1864 0.1954 0.0060  0.0324  0.0101  23  ILE   A CG1 
430  C  CG1 B ILE   A 23  ? 0.1645 0.1702 0.1643 -0.0160 0.0216  0.0062  23  ILE   A CG1 
431  C  CG2 A ILE   A 23  ? 0.1881 0.1899 0.2058 0.0094  0.0293  0.0248  23  ILE   A CG2 
432  C  CG2 B ILE   A 23  ? 0.1658 0.1677 0.1620 -0.0124 0.0254  0.0205  23  ILE   A CG2 
433  C  CD1 A ILE   A 23  ? 0.1963 0.1901 0.1994 0.0106  0.0190  0.0108  23  ILE   A CD1 
434  C  CD1 B ILE   A 23  ? 0.1637 0.1727 0.1699 -0.0148 0.0115  0.0042  23  ILE   A CD1 
457  N  N   A VAL   A 24  ? 0.1823 0.2036 0.2193 -0.0026 0.0451  0.0126  24  VAL   A N   
458  N  N   B VAL   A 24  ? 0.1891 0.2059 0.1970 -0.0382 0.0356  -0.0036 24  VAL   A N   
459  C  CA  A VAL   A 24  ? 0.2003 0.2145 0.2330 -0.0154 0.0420  0.0085  24  VAL   A CA  
460  C  CA  B VAL   A 24  ? 0.2052 0.2189 0.2170 -0.0385 0.0288  -0.0022 24  VAL   A CA  
461  C  C   A VAL   A 24  ? 0.2097 0.2362 0.2396 -0.0262 0.0496  0.0110  24  VAL   A C   
462  C  C   B VAL   A 24  ? 0.2190 0.2384 0.2284 -0.0318 0.0340  -0.0023 24  VAL   A C   
463  O  O   A VAL   A 24  ? 0.2242 0.2405 0.2472 -0.0243 0.0528  0.0080  24  VAL   A O   
464  O  O   B VAL   A 24  ? 0.2251 0.2407 0.2406 -0.0311 0.0366  -0.0007 24  VAL   A O   
465  C  CB  A VAL   A 24  ? 0.2060 0.2145 0.2475 -0.0183 0.0400  0.0119  24  VAL   A CB  
466  C  CB  B VAL   A 24  ? 0.2066 0.2218 0.2322 -0.0426 0.0207  0.0034  24  VAL   A CB  
467  C  CG1 A VAL   A 24  ? 0.2185 0.2288 0.2525 -0.0130 0.0450  0.0062  24  VAL   A CG1 
468  C  CG1 B VAL   A 24  ? 0.2141 0.2268 0.2425 -0.0412 0.0167  0.0055  24  VAL   A CG1 
469  C  CG2 A VAL   A 24  ? 0.2171 0.2162 0.2494 -0.0113 0.0503  0.0186  24  VAL   A CG2 
470  C  CG2 B VAL   A 24  ? 0.2083 0.2222 0.2347 -0.0482 0.0175  0.0012  24  VAL   A CG2 
489  N  N   A GLU   A 25  ? 0.2167 0.2689 0.2535 -0.0349 0.0685  0.0158  25  GLU   A N   
490  N  N   B GLU   A 25  ? 0.2291 0.2621 0.2393 -0.0246 0.0426  -0.0018 25  GLU   A N   
491  C  CA  A GLU   A 25  ? 0.2322 0.3017 0.2730 -0.0331 0.0814  0.0154  25  GLU   A CA  
492  C  CA  B GLU   A 25  ? 0.2416 0.2863 0.2573 -0.0187 0.0442  0.0021  25  GLU   A CA  
493  C  C   A GLU   A 25  ? 0.2203 0.3029 0.2408 -0.0447 0.0844  0.0153  25  GLU   A C   
494  C  C   B GLU   A 25  ? 0.2387 0.2928 0.2436 -0.0208 0.0394  0.0025  25  GLU   A C   
495  O  O   A GLU   A 25  ? 0.2256 0.3170 0.2466 -0.0433 0.0898  0.0133  25  GLU   A O   
496  O  O   B GLU   A 25  ? 0.2397 0.2975 0.2486 -0.0190 0.0415  0.0009  25  GLU   A O   
497  C  CB  A GLU   A 25  ? 0.2617 0.3344 0.3210 -0.0209 0.0864  0.0176  25  GLU   A CB  
498  C  CB  B GLU   A 25  ? 0.2594 0.3038 0.2942 -0.0113 0.0469  0.0051  25  GLU   A CB  
499  C  CG  A GLU   A 25  ? 0.2986 0.3647 0.3959 -0.0165 0.0688  0.0179  25  GLU   A CG  
500  C  CG  B GLU   A 25  ? 0.2826 0.3205 0.3434 -0.0068 0.0421  0.0067  25  GLU   A CG  
501  C  CD  A GLU   A 25  ? 0.3293 0.3907 0.4637 -0.0122 0.0536  0.0164  25  GLU   A CD  
502  C  CD  B GLU   A 25  ? 0.3012 0.3341 0.3853 -0.0039 0.0370  0.0051  25  GLU   A CD  
503  O  OE1 A GLU   A 25  ? 0.3423 0.4012 0.4835 -0.0095 0.0426  0.0126  25  GLU   A OE1 
504  O  OE1 B GLU   A 25  ? 0.3107 0.3417 0.4041 -0.0021 0.0325  0.0059  25  GLU   A OE1 
505  O  OE2 A GLU   A 25  ? 0.3400 0.4013 0.4945 -0.0126 0.0482  0.0096  25  GLU   A OE2 
506  O  OE2 B GLU   A 25  ? 0.3070 0.3369 0.4017 -0.0047 0.0356  0.0000  25  GLU   A OE2 
519  N  N   A GLU   A 26  ? 0.2114 0.2861 0.2363 -0.0637 0.0835  0.0136  26  GLU   A N   
520  N  N   B GLU   A 26  ? 0.2382 0.2933 0.2339 -0.0259 0.0393  0.0023  26  GLU   A N   
521  C  CA  A GLU   A 26  ? 0.2237 0.2771 0.2431 -0.0787 0.0743  0.0106  26  GLU   A CA  
522  C  CA  B GLU   A 26  ? 0.2447 0.2961 0.2273 -0.0295 0.0343  0.0037  26  GLU   A CA  
523  C  C   A GLU   A 26  ? 0.2155 0.2682 0.2098 -0.0809 0.0643  0.0099  26  GLU   A C   
524  C  C   B GLU   A 26  ? 0.2481 0.2949 0.2132 -0.0258 0.0341  0.0025  26  GLU   A C   
525  O  O   A GLU   A 26  ? 0.2266 0.2691 0.2057 -0.0887 0.0549  0.0135  26  GLU   A O   
526  O  O   B GLU   A 26  ? 0.2484 0.2944 0.2103 -0.0315 0.0377  0.0045  26  GLU   A O   
527  C  CB  A GLU   A 26  ? 0.2497 0.2747 0.2992 -0.0925 0.0702  0.0171  26  GLU   A CB  
528  C  CB  B GLU   A 26  ? 0.2489 0.2990 0.2350 -0.0361 0.0240  0.0067  26  GLU   A CB  
529  C  CG  A GLU   A 26  ? 0.2696 0.2830 0.3656 -0.0989 0.0792  0.0059  26  GLU   A CG  
530  C  CG  B GLU   A 26  ? 0.2523 0.3023 0.2488 -0.0407 0.0183  0.0065  26  GLU   A CG  
531  C  CD  A GLU   A 26  ? 0.2771 0.2870 0.3972 -0.1048 0.1102  -0.0023 26  GLU   A CD  
532  C  CD  B GLU   A 26  ? 0.2504 0.3019 0.2515 -0.0462 0.0185  0.0102  26  GLU   A CD  
533  O  OE1 A GLU   A 26  ? 0.2707 0.2978 0.4127 -0.1028 0.1258  -0.0390 26  GLU   A OE1 
534  O  OE1 B GLU   A 26  ? 0.2549 0.3003 0.2507 -0.0491 0.0171  0.0153  26  GLU   A OE1 
535  O  OE2 A GLU   A 26  ? 0.2910 0.2949 0.4030 -0.0939 0.1232  0.0060  26  GLU   A OE2 
536  O  OE2 B GLU   A 26  ? 0.2440 0.3023 0.2475 -0.0501 0.0152  0.0059  26  GLU   A OE2 
549  N  N   A ALA   A 27  ? 0.1928 0.2550 0.1981 -0.0827 0.0628  0.0049  27  ALA   A N   
550  N  N   B ALA   A 27  ? 0.2502 0.2952 0.2086 -0.0179 0.0318  0.0025  27  ALA   A N   
551  C  CA  A ALA   A 27  ? 0.2003 0.2634 0.1855 -0.0779 0.0606  -0.0037 27  ALA   A CA  
552  C  CA  B ALA   A 27  ? 0.2613 0.3024 0.2056 -0.0113 0.0291  0.0018  27  ALA   A CA  
553  C  C   A ALA   A 27  ? 0.2330 0.2847 0.1963 -0.0881 0.0648  -0.0168 27  ALA   A C   
554  C  C   B ALA   A 27  ? 0.2809 0.3172 0.2212 -0.0087 0.0253  -0.0016 27  ALA   A C   
555  O  O   A ALA   A 27  ? 0.2401 0.2774 0.2060 -0.0924 0.0462  -0.0135 27  ALA   A O   
556  O  O   B ALA   A 27  ? 0.2790 0.3146 0.2200 -0.0075 0.0205  0.0010  27  ALA   A O   
557  C  CB  A ALA   A 27  ? 0.1880 0.2542 0.1940 -0.0746 0.0526  -0.0021 27  ALA   A CB  
558  C  CB  B ALA   A 27  ? 0.2579 0.2988 0.1991 -0.0109 0.0305  0.0018  27  ALA   A CB  
569  N  N   A LYS   A 28  ? 0.2756 0.3199 0.2277 -0.0814 0.0619  -0.0378 28  LYS   A N   
570  N  N   B LYS   A 28  ? 0.3056 0.3340 0.2499 -0.0057 0.0211  -0.0086 28  LYS   A N   
571  C  CA  A LYS   A 28  ? 0.3207 0.3617 0.2663 -0.0682 0.0650  -0.0553 28  LYS   A CA  
572  C  CA  B LYS   A 28  ? 0.3309 0.3532 0.2870 -0.0017 0.0176  -0.0190 28  LYS   A CA  
573  C  C   A LYS   A 28  ? 0.3443 0.3933 0.2686 -0.0699 0.0789  -0.0427 28  LYS   A C   
574  C  C   B LYS   A 28  ? 0.3443 0.3657 0.2953 -0.0048 0.0206  -0.0147 28  LYS   A C   
575  O  O   A LYS   A 28  ? 0.3551 0.4015 0.2932 -0.0651 0.0693  -0.0450 28  LYS   A O   
576  O  O   B LYS   A 28  ? 0.3490 0.3683 0.3013 -0.0035 0.0173  -0.0156 28  LYS   A O   
577  C  CB  A LYS   A 28  ? 0.3429 0.3768 0.3191 -0.0526 0.0574  -0.0692 28  LYS   A CB  
578  C  CB  B LYS   A 28  ? 0.3444 0.3621 0.3240 0.0044  0.0120  -0.0290 28  LYS   A CB  
579  C  CG  A LYS   A 28  ? 0.3636 0.3897 0.3740 -0.0403 0.0501  -0.0762 28  LYS   A CG  
580  C  CG  B LYS   A 28  ? 0.3574 0.3702 0.3637 0.0086  0.0076  -0.0349 28  LYS   A CG  
581  C  CD  A LYS   A 28  ? 0.3797 0.4047 0.4334 -0.0295 0.0421  -0.0817 28  LYS   A CD  
582  C  CD  B LYS   A 28  ? 0.3686 0.3795 0.4047 0.0117  0.0029  -0.0399 28  LYS   A CD  
583  C  CE  A LYS   A 28  ? 0.3902 0.4142 0.4800 -0.0224 0.0334  -0.0877 28  LYS   A CE  
584  C  CE  B LYS   A 28  ? 0.3771 0.3861 0.4375 0.0135  -0.0013 -0.0444 28  LYS   A CE  
585  N  NZ  A LYS   A 28  ? 0.3979 0.4200 0.5095 -0.0162 0.0303  -0.0911 28  LYS   A NZ  
586  N  NZ  B LYS   A 28  ? 0.3824 0.3900 0.4567 0.0158  -0.0033 -0.0474 28  LYS   A NZ  
613  N  N   A LYS   A 29  ? 0.3528 0.4156 0.2694 -0.0781 0.1015  -0.0198 29  LYS   A N   
614  N  N   B LYS   A 29  ? 0.3524 0.3757 0.3064 -0.0101 0.0270  -0.0066 29  LYS   A N   
615  C  CA  A LYS   A 29  ? 0.3667 0.4374 0.2909 -0.0827 0.1132  -0.0019 29  LYS   A CA  
616  C  CA  B LYS   A 29  ? 0.3611 0.3855 0.3235 -0.0143 0.0314  0.0003  29  LYS   A CA  
617  C  C   A LYS   A 29  ? 0.3664 0.4280 0.2747 -0.0956 0.0951  0.0119  29  LYS   A C   
618  C  C   B LYS   A 29  ? 0.3573 0.3791 0.3014 -0.0221 0.0262  0.0086  29  LYS   A C   
619  O  O   A LYS   A 29  ? 0.3783 0.4395 0.2883 -0.0864 0.0912  0.0084  29  LYS   A O   
620  O  O   B LYS   A 29  ? 0.3604 0.3835 0.3055 -0.0201 0.0259  0.0092  29  LYS   A O   
621  C  CB  A LYS   A 29  ? 0.3804 0.4670 0.3413 -0.0711 0.1282  -0.0011 29  LYS   A CB  
622  C  CB  B LYS   A 29  ? 0.3724 0.4004 0.3652 -0.0098 0.0379  -0.0010 29  LYS   A CB  
623  C  CG  A LYS   A 29  ? 0.3982 0.4933 0.4016 -0.0585 0.1318  -0.0020 29  LYS   A CG  
624  C  CG  B LYS   A 29  ? 0.3846 0.4140 0.4063 -0.0053 0.0417  -0.0027 29  LYS   A CG  
625  C  CD  A LYS   A 29  ? 0.4134 0.5154 0.4615 -0.0482 0.1290  -0.0040 29  LYS   A CD  
626  C  CD  B LYS   A 29  ? 0.3942 0.4249 0.4430 -0.0013 0.0429  -0.0036 29  LYS   A CD  
627  C  CE  A LYS   A 29  ? 0.4240 0.5299 0.5035 -0.0425 0.1261  -0.0046 29  LYS   A CE  
628  C  CE  B LYS   A 29  ? 0.4004 0.4324 0.4691 0.0010  0.0431  -0.0042 29  LYS   A CE  
629  N  NZ  A LYS   A 29  ? 0.4286 0.5377 0.5302 -0.0388 0.1238  -0.0071 29  LYS   A NZ  
630  N  NZ  B LYS   A 29  ? 0.4036 0.4361 0.4845 0.0025  0.0423  -0.0043 29  LYS   A NZ  
657  N  N   A VAL   A 30  ? 0.3513 0.4052 0.2366 -0.1174 0.0873  0.0292  30  VAL   A N   
658  N  N   B VAL   A 30  ? 0.3505 0.3685 0.2764 -0.0314 0.0223  0.0143  30  VAL   A N   
659  C  CA  A VAL   A 30  ? 0.3452 0.3829 0.2174 -0.1322 0.0559  0.0398  30  VAL   A CA  
660  C  CA  B VAL   A 30  ? 0.3446 0.3573 0.2569 -0.0392 0.0121  0.0193  30  VAL   A CA  
661  C  C   A VAL   A 30  ? 0.3436 0.3656 0.1777 -0.1338 0.0454  0.0446  30  VAL   A C   
662  C  C   B VAL   A 30  ? 0.3427 0.3516 0.2397 -0.0404 0.0047  0.0164  30  VAL   A C   
663  O  O   A VAL   A 30  ? 0.3536 0.3669 0.1775 -0.1272 0.0373  0.0472  30  VAL   A O   
664  O  O   B VAL   A 30  ? 0.3444 0.3509 0.2310 -0.0395 0.0008  0.0186  30  VAL   A O   
665  C  CB  A VAL   A 30  ? 0.3392 0.3756 0.2352 -0.1477 0.0376  0.0440  30  VAL   A CB  
666  C  CB  B VAL   A 30  ? 0.3405 0.3513 0.2584 -0.0459 0.0096  0.0249  30  VAL   A CB  
667  C  CG1 A VAL   A 30  ? 0.3446 0.3745 0.2430 -0.1474 0.0239  0.0451  30  VAL   A CG1 
668  C  CG1 B VAL   A 30  ? 0.3417 0.3497 0.2608 -0.0473 0.0076  0.0263  30  VAL   A CG1 
669  C  CG2 A VAL   A 30  ? 0.3344 0.3724 0.2508 -0.1578 0.0420  0.0499  30  VAL   A CG2 
670  C  CG2 B VAL   A 30  ? 0.3386 0.3494 0.2632 -0.0488 0.0106  0.0289  30  VAL   A CG2 
689  N  N   A LYS   A 31  ? 0.3346 0.3486 0.1830 -0.1358 0.0247  0.0378  31  LYS   A N   
690  N  N   B LYS   A 31  ? 0.3400 0.3469 0.2486 -0.0414 -0.0027 0.0122  31  LYS   A N   
691  C  CA  A LYS   A 31  ? 0.3411 0.3444 0.2123 -0.1182 -0.0017 0.0386  31  LYS   A CA  
692  C  CA  B LYS   A 31  ? 0.3391 0.3458 0.2692 -0.0388 -0.0112 0.0108  31  LYS   A CA  
693  C  C   A LYS   A 31  ? 0.3126 0.3211 0.1613 -0.1017 -0.0146 0.0683  31  LYS   A C   
694  C  C   B LYS   A 31  ? 0.3139 0.3286 0.2298 -0.0345 -0.0115 0.0240  31  LYS   A C   
695  O  O   A LYS   A 31  ? 0.3172 0.3286 0.1617 -0.0936 -0.0251 0.0827  31  LYS   A O   
696  O  O   B LYS   A 31  ? 0.3156 0.3318 0.2331 -0.0315 -0.0147 0.0270  31  LYS   A O   
697  C  CB  A LYS   A 31  ? 0.3794 0.3691 0.3189 -0.1063 -0.0181 0.0128  31  LYS   A CB  
698  C  CB  B LYS   A 31  ? 0.3629 0.3629 0.3386 -0.0385 -0.0193 -0.0006 31  LYS   A CB  
699  C  CG  A LYS   A 31  ? 0.4179 0.3933 0.4303 -0.0907 -0.0342 -0.0062 31  LYS   A CG  
700  C  CG  B LYS   A 31  ? 0.3858 0.3801 0.4103 -0.0370 -0.0271 -0.0096 31  LYS   A CG  
701  C  CD  A LYS   A 31  ? 0.4485 0.4110 0.5165 -0.0791 -0.0502 -0.0228 31  LYS   A CD  
702  C  CD  B LYS   A 31  ? 0.4040 0.3940 0.4697 -0.0357 -0.0350 -0.0182 31  LYS   A CD  
703  C  CE  A LYS   A 31  ? 0.4687 0.4233 0.5745 -0.0709 -0.0614 -0.0344 31  LYS   A CE  
704  C  CE  B LYS   A 31  ? 0.4166 0.4039 0.5114 -0.0353 -0.0403 -0.0249 31  LYS   A CE  
705  N  NZ  A LYS   A 31  ? 0.4809 0.4299 0.6048 -0.0649 -0.0668 -0.0394 31  LYS   A NZ  
706  N  NZ  B LYS   A 31  ? 0.4244 0.4089 0.5340 -0.0341 -0.0424 -0.0284 31  LYS   A NZ  
733  N  N   A PRO   A 32  ? 0.2766 0.2886 0.1502 -0.0999 -0.0116 0.0611  32  PRO   A N   
734  N  N   B PRO   A 32  ? 0.2875 0.3073 0.2005 -0.0344 -0.0062 0.0277  32  PRO   A N   
735  C  CA  A PRO   A 32  ? 0.2663 0.2731 0.1718 -0.0918 -0.0160 0.0672  32  PRO   A CA  
736  C  CA  B PRO   A 32  ? 0.2731 0.2945 0.1923 -0.0329 -0.0059 0.0350  32  PRO   A CA  
737  C  C   A PRO   A 32  ? 0.2629 0.2664 0.1749 -0.0753 -0.0180 0.0766  32  PRO   A C   
738  C  C   B PRO   A 32  ? 0.2606 0.2826 0.1826 -0.0300 -0.0092 0.0445  32  PRO   A C   
739  O  O   A PRO   A 32  ? 0.2564 0.2555 0.1810 -0.0805 -0.0283 0.0675  32  PRO   A O   
740  O  O   B PRO   A 32  ? 0.2563 0.2801 0.1826 -0.0282 -0.0151 0.0473  32  PRO   A O   
741  C  CB  A PRO   A 32  ? 0.2583 0.2766 0.1800 -0.0939 -0.0165 0.0598  32  PRO   A CB  
742  C  CB  B PRO   A 32  ? 0.2712 0.2976 0.1948 -0.0323 -0.0045 0.0302  32  PRO   A CB  
743  C  CG  A PRO   A 32  ? 0.2581 0.2825 0.1633 -0.0905 -0.0278 0.0453  32  PRO   A CG  
744  C  CG  B PRO   A 32  ? 0.2740 0.3013 0.1920 -0.0310 -0.0065 0.0237  32  PRO   A CG  
745  C  CD  A PRO   A 32  ? 0.2633 0.2850 0.1447 -0.0946 -0.0180 0.0507  32  PRO   A CD  
746  C  CD  B PRO   A 32  ? 0.2790 0.3040 0.1910 -0.0325 -0.0048 0.0243  32  PRO   A CD  
761  N  N   A THR   A 33  ? 0.2676 0.2656 0.1782 -0.0640 -0.0178 0.0820  33  THR   A N   
762  N  N   B THR   A 33  ? 0.2541 0.2727 0.1823 -0.0319 -0.0086 0.0473  33  THR   A N   
763  C  CA  A THR   A 33  ? 0.2685 0.2681 0.1771 -0.0478 -0.0341 0.0847  33  THR   A CA  
764  C  CA  B THR   A 33  ? 0.2479 0.2645 0.1821 -0.0317 -0.0150 0.0503  33  THR   A CA  
765  C  C   A THR   A 33  ? 0.2389 0.2505 0.1728 -0.0471 -0.0346 0.0674  33  THR   A C   
766  C  C   B THR   A 33  ? 0.2289 0.2467 0.1702 -0.0404 -0.0190 0.0491  33  THR   A C   
767  O  O   A THR   A 33  ? 0.2298 0.2440 0.1867 -0.0482 -0.0432 0.0635  33  THR   A O   
768  O  O   B THR   A 33  ? 0.2256 0.2398 0.1756 -0.0437 -0.0166 0.0443  33  THR   A O   
769  C  CB  A THR   A 33  ? 0.2975 0.2877 0.1970 -0.0386 -0.0354 0.0982  33  THR   A CB  
770  C  CB  B THR   A 33  ? 0.2612 0.2730 0.2026 -0.0255 -0.0109 0.0531  33  THR   A CB  
771  O  OG1 A THR   A 33  ? 0.3179 0.2997 0.2274 -0.0282 -0.0298 0.1036  33  THR   A OG1 
772  O  OG1 B THR   A 33  ? 0.2712 0.2793 0.2208 -0.0185 -0.0079 0.0557  33  THR   A OG1 
773  C  CG2 A THR   A 33  ? 0.3042 0.2963 0.2041 -0.0339 -0.0394 0.0961  33  THR   A CG2 
774  C  CG2 B THR   A 33  ? 0.2637 0.2764 0.2102 -0.0237 -0.0101 0.0508  33  THR   A CG2 
789  N  N   . VAL   A 34  ? 0.2106 0.2341 0.1639 -0.0481 -0.0227 0.0537  34  VAL   A N   
790  C  CA  . VAL   A 34  ? 0.1885 0.2060 0.1675 -0.0403 -0.0184 0.0392  34  VAL   A CA  
791  C  C   . VAL   A 34  ? 0.1793 0.1842 0.1724 -0.0359 -0.0059 0.0336  34  VAL   A C   
792  O  O   . VAL   A 34  ? 0.1794 0.1830 0.1903 -0.0422 -0.0068 0.0498  34  VAL   A O   
793  C  CB  . VAL   A 34  ? 0.1887 0.1987 0.1910 -0.0334 -0.0060 0.0320  34  VAL   A CB  
794  C  CG1 . VAL   A 34  ? 0.1972 0.1981 0.1846 -0.0287 0.0012  0.0223  34  VAL   A CG1 
795  C  CG2 . VAL   A 34  ? 0.1906 0.2078 0.2136 -0.0278 -0.0053 0.0355  34  VAL   A CG2 
806  N  N   . VAL   A 35  ? 0.1637 0.1681 0.1805 -0.0347 -0.0041 0.0350  35  VAL   A N   
807  C  CA  . VAL   A 35  ? 0.1526 0.1651 0.1712 -0.0256 -0.0011 0.0255  35  VAL   A CA  
808  C  C   . VAL   A 35  ? 0.1432 0.1521 0.1716 -0.0208 0.0079  0.0229  35  VAL   A C   
809  O  O   . VAL   A 35  ? 0.1383 0.1588 0.1923 -0.0248 0.0109  0.0226  35  VAL   A O   
810  C  CB  . VAL   A 35  ? 0.1585 0.1703 0.1819 -0.0158 0.0056  0.0151  35  VAL   A CB  
811  C  CG1 . VAL   A 35  ? 0.1698 0.1777 0.1875 -0.0058 -0.0035 0.0117  35  VAL   A CG1 
812  C  CG2 . VAL   A 35  ? 0.1633 0.1681 0.1972 -0.0072 0.0133  0.0098  35  VAL   A CG2 
822  N  N   . VAL   A 36  ? 0.1279 0.1460 0.1710 -0.0176 0.0106  0.0270  36  VAL   A N   
823  C  CA  . VAL   A 36  ? 0.1267 0.1361 0.1631 -0.0104 0.0113  0.0183  36  VAL   A CA  
824  C  C   . VAL   A 36  ? 0.1294 0.1347 0.1734 -0.0127 0.0074  0.0166  36  VAL   A C   
825  O  O   . VAL   A 36  ? 0.1337 0.1339 0.1962 -0.0083 0.0165  0.0228  36  VAL   A O   
826  C  CB  . VAL   A 36  ? 0.1307 0.1293 0.1683 -0.0126 0.0046  0.0283  36  VAL   A CB  
827  C  CG1 . VAL   A 36  ? 0.1401 0.1358 0.1818 -0.0158 0.0015  0.0086  36  VAL   A CG1 
828  C  CG2 . VAL   A 36  ? 0.1409 0.1341 0.1862 -0.0098 -0.0046 0.0306  36  VAL   A CG2 
838  N  N   . ASN   A 37  ? 0.1243 0.1272 0.1521 -0.0066 0.0101  0.0251  37  ASN   A N   
839  C  CA  . ASN   A 37  ? 0.1212 0.1242 0.1502 -0.0010 0.0021  0.0233  37  ASN   A CA  
840  C  C   . ASN   A 37  ? 0.1146 0.1302 0.1622 -0.0054 0.0116  0.0280  37  ASN   A C   
841  O  O   . ASN   A 37  ? 0.1246 0.1362 0.1645 0.0017  0.0090  0.0171  37  ASN   A O   
842  C  CB  . ASN   A 37  ? 0.1267 0.1272 0.1719 0.0007  0.0055  0.0249  37  ASN   A CB  
843  C  CG  . ASN   A 37  ? 0.1269 0.1278 0.1820 0.0004  0.0150  0.0205  37  ASN   A CG  
844  O  OD1 . ASN   A 37  ? 0.1285 0.1270 0.2066 -0.0018 0.0079  0.0238  37  ASN   A OD1 
845  N  ND2 . ASN   A 37  ? 0.1313 0.1265 0.1924 -0.0030 0.0026  0.0353  37  ASN   A ND2 
852  N  N   A ALA   A 38  ? 0.1170 0.1324 0.1719 -0.0033 0.0095  0.0135  38  ALA   A N   
853  N  N   B ALA   A 38  ? 0.1214 0.1365 0.1576 -0.0050 0.0063  0.0193  38  ALA   A N   
854  C  CA  A ALA   A 38  ? 0.1252 0.1346 0.1658 -0.0064 0.0048  0.0056  38  ALA   A CA  
855  C  CA  B ALA   A 38  ? 0.1324 0.1432 0.1539 -0.0086 -0.0000 0.0154  38  ALA   A CA  
856  C  C   A ALA   A 38  ? 0.1242 0.1313 0.1700 -0.0033 -0.0047 0.0059  38  ALA   A C   
857  C  C   B ALA   A 38  ? 0.1319 0.1392 0.1594 -0.0056 -0.0076 0.0124  38  ALA   A C   
858  O  O   A ALA   A 38  ? 0.1186 0.1256 0.1718 -0.0007 -0.0088 0.0117  38  ALA   A O   
859  O  O   B ALA   A 38  ? 0.1248 0.1309 0.1717 -0.0116 -0.0168 0.0045  38  ALA   A O   
860  C  CB  A ALA   A 38  ? 0.1214 0.1476 0.1809 -0.0163 -0.0067 0.0107  38  ALA   A CB  
861  C  CB  B ALA   A 38  ? 0.1381 0.1497 0.1535 -0.0143 -0.0039 0.0079  38  ALA   A CB  
872  N  N   A ALA   A 39  ? 0.1199 0.1288 0.1818 -0.0043 0.0028  0.0217  39  ALA   A N   
873  N  N   B ALA   A 39  ? 0.1359 0.1405 0.1596 -0.0005 -0.0039 0.0205  39  ALA   A N   
874  C  CA  A ALA   A 39  ? 0.1185 0.1189 0.1720 0.0001  0.0034  0.0088  39  ALA   A CA  
875  C  CA  B ALA   A 39  ? 0.1422 0.1437 0.1554 0.0040  -0.0029 0.0166  39  ALA   A CA  
876  C  C   A ALA   A 39  ? 0.1236 0.1176 0.1729 -0.0002 -0.0025 0.0070  39  ALA   A C   
877  C  C   B ALA   A 39  ? 0.1351 0.1372 0.1483 0.0009  0.0074  0.0188  39  ALA   A C   
878  O  O   A ALA   A 39  ? 0.1398 0.1270 0.1790 -0.0040 0.0008  0.0107  39  ALA   A O   
879  O  O   B ALA   A 39  ? 0.1327 0.1430 0.1456 -0.0076 0.0141  0.0195  39  ALA   A O   
880  C  CB  A ALA   A 39  ? 0.1134 0.1186 0.1847 0.0033  -0.0059 0.0008  39  ALA   A CB  
881  C  CB  B ALA   A 39  ? 0.1553 0.1500 0.1627 0.0111  -0.0053 0.0109  39  ALA   A CB  
892  N  N   A ASN   A 40  ? 0.1325 0.1198 0.1792 -0.0091 0.0114  0.0106  40  ASN   A N   
893  N  N   B ASN   A 40  ? 0.1389 0.1292 0.1480 0.0020  0.0227  0.0215  40  ASN   A N   
894  C  CA  A ASN   A 40  ? 0.1461 0.1236 0.1866 -0.0099 0.0022  0.0087  40  ASN   A CA  
895  C  CA  B ASN   A 40  ? 0.1454 0.1241 0.1509 0.0099  0.0205  0.0192  40  ASN   A CA  
896  C  C   A ASN   A 40  ? 0.1448 0.1163 0.1698 -0.0082 0.0124  0.0177  40  ASN   A C   
897  C  C   B ASN   A 40  ? 0.1468 0.1178 0.1419 0.0082  0.0329  0.0186  40  ASN   A C   
898  O  O   A ASN   A 40  ? 0.1380 0.1238 0.1877 -0.0099 0.0149  0.0222  40  ASN   A O   
899  O  O   B ASN   A 40  ? 0.1408 0.1181 0.1502 0.0024  0.0373  0.0185  40  ASN   A O   
900  C  CB  A ASN   A 40  ? 0.1629 0.1339 0.1968 -0.0052 -0.0058 0.0131  40  ASN   A CB  
901  C  CB  B ASN   A 40  ? 0.1510 0.1295 0.1618 0.0167  0.0218  0.0183  40  ASN   A CB  
902  C  CG  A ASN   A 40  ? 0.1654 0.1414 0.2110 -0.0045 -0.0099 0.0177  40  ASN   A CG  
903  C  CG  B ASN   A 40  ? 0.1493 0.1384 0.1741 0.0176  0.0245  0.0168  40  ASN   A CG  
904  O  OD1 A ASN   A 40  ? 0.1685 0.1369 0.2344 -0.0128 -0.0070 0.0152  40  ASN   A OD1 
905  O  OD1 B ASN   A 40  ? 0.1492 0.1389 0.1782 0.0150  0.0365  0.0145  40  ASN   A OD1 
906  N  ND2 A ASN   A 40  ? 0.1712 0.1555 0.2174 0.0029  -0.0130 0.0008  40  ASN   A ND2 
907  N  ND2 B ASN   A 40  ? 0.1523 0.1492 0.1918 0.0191  0.0180  0.0034  40  ASN   A ND2 
920  N  N   A VAL   A 41  ? 0.1480 0.1248 0.1815 -0.0037 0.0136  0.0156  41  VAL   A N   
921  N  N   B VAL   A 41  ? 0.1544 0.1206 0.1452 0.0059  0.0349  0.0165  41  VAL   A N   
922  C  CA  A VAL   A 41  ? 0.1507 0.1325 0.1896 -0.0030 0.0213  0.0163  41  VAL   A CA  
923  C  CA  B VAL   A 41  ? 0.1591 0.1238 0.1539 0.0015  0.0411  0.0144  41  VAL   A CA  
924  C  C   A VAL   A 41  ? 0.1511 0.1307 0.1741 -0.0008 0.0287  0.0181  41  VAL   A C   
925  C  C   B VAL   A 41  ? 0.1548 0.1233 0.1633 -0.0030 0.0380  0.0162  41  VAL   A C   
926  O  O   A VAL   A 41  ? 0.1505 0.1275 0.1850 0.0010  0.0252  0.0163  41  VAL   A O   
927  O  O   B VAL   A 41  ? 0.1577 0.1188 0.1786 -0.0076 0.0362  0.0126  41  VAL   A O   
928  C  CB  A VAL   A 41  ? 0.1609 0.1382 0.1903 -0.0038 0.0323  0.0112  41  VAL   A CB  
929  C  CB  B VAL   A 41  ? 0.1720 0.1278 0.1517 -0.0057 0.0476  0.0129  41  VAL   A CB  
930  C  CG1 A VAL   A 41  ? 0.1602 0.1438 0.1883 0.0082  0.0236  0.0129  41  VAL   A CG1 
931  C  CG1 B VAL   A 41  ? 0.1851 0.1336 0.1631 -0.0081 0.0510  0.0043  41  VAL   A CG1 
932  C  CG2 A VAL   A 41  ? 0.1825 0.1525 0.1937 -0.0116 0.0323  0.0044  41  VAL   A CG2 
933  C  CG2 B VAL   A 41  ? 0.1835 0.1327 0.1527 -0.0110 0.0463  0.0131  41  VAL   A CG2 
952  N  N   . TYR   A 42  ? 0.1450 0.1266 0.1827 -0.0025 0.0314  0.0250  42  TYR   A N   
953  C  CA  . TYR   A 42  ? 0.1430 0.1241 0.1807 -0.0069 0.0233  0.0279  42  TYR   A CA  
954  C  C   . TYR   A 42  ? 0.1333 0.1285 0.1793 -0.0051 0.0185  0.0284  42  TYR   A C   
955  O  O   . TYR   A 42  ? 0.1355 0.1278 0.2063 -0.0168 0.0186  0.0103  42  TYR   A O   
956  C  CB  . TYR   A 42  ? 0.1588 0.1376 0.1771 -0.0046 0.0293  0.0350  42  TYR   A CB  
957  C  CG  . TYR   A 42  ? 0.1799 0.1457 0.1716 -0.0047 0.0184  0.0365  42  TYR   A CG  
958  C  CD1 . TYR   A 42  ? 0.1874 0.1518 0.1841 -0.0089 0.0223  0.0337  42  TYR   A CD1 
959  C  CD2 . TYR   A 42  ? 0.1967 0.1671 0.1832 -0.0063 0.0147  0.0256  42  TYR   A CD2 
960  C  CE1 . TYR   A 42  ? 0.1963 0.1609 0.1833 -0.0098 0.0283  0.0262  42  TYR   A CE1 
961  C  CE2 . TYR   A 42  ? 0.2106 0.1796 0.1956 -0.0164 0.0174  0.0223  42  TYR   A CE2 
962  C  CZ  . TYR   A 42  ? 0.2191 0.1740 0.1838 -0.0187 0.0380  0.0212  42  TYR   A CZ  
963  O  OH  . TYR   A 42  ? 0.2412 0.1950 0.2198 -0.0303 0.0365  0.0131  42  TYR   A OH  
974  N  N   . LEU   A 43  ? 0.1319 0.1241 0.1737 -0.0060 0.0104  0.0150  43  LEU   A N   
975  C  CA  . LEU   A 43  ? 0.1269 0.1250 0.1778 -0.0082 0.0073  0.0118  43  LEU   A CA  
976  C  C   . LEU   A 43  ? 0.1307 0.1342 0.1712 -0.0099 0.0062  0.0129  43  LEU   A C   
977  O  O   . LEU   A 43  ? 0.1453 0.1373 0.1961 0.0010  -0.0049 0.0090  43  LEU   A O   
978  C  CB  . LEU   A 43  ? 0.1296 0.1236 0.1903 -0.0085 0.0045  0.0097  43  LEU   A CB  
979  C  CG  . LEU   A 43  ? 0.1340 0.1236 0.2002 -0.0051 0.0034  0.0120  43  LEU   A CG  
980  C  CD1 . LEU   A 43  ? 0.1407 0.1332 0.2193 0.0002  0.0002  0.0136  43  LEU   A CD1 
981  C  CD2 . LEU   A 43  ? 0.1529 0.1311 0.1907 -0.0022 0.0094  0.0266  43  LEU   A CD2 
993  N  N   A LYS   A 44  ? 0.1344 0.1236 0.1649 -0.0014 0.0061  0.0151  44  LYS   A N   
994  N  N   B LYS   A 44  ? 0.1459 0.1503 0.1661 -0.0081 0.0030  0.0112  44  LYS   A N   
995  C  CA  A LYS   A 44  ? 0.1454 0.1197 0.1757 0.0018  0.0144  0.0219  44  LYS   A CA  
996  C  CA  B LYS   A 44  ? 0.1637 0.1677 0.1772 -0.0095 0.0009  0.0105  44  LYS   A CA  
997  C  C   A LYS   A 44  ? 0.1305 0.1174 0.1700 0.0022  0.0067  0.0170  44  LYS   A C   
998  C  C   B LYS   A 44  ? 0.1606 0.1660 0.1614 -0.0080 -0.0004 0.0061  44  LYS   A C   
999  O  O   A LYS   A 44  ? 0.1374 0.1369 0.1760 -0.0032 0.0033  0.0057  44  LYS   A O   
1000 O  O   B LYS   A 44  ? 0.1650 0.1710 0.1553 -0.0108 -0.0013 0.0033  44  LYS   A O   
1001 C  CB  A LYS   A 44  ? 0.1757 0.1339 0.2151 0.0009  0.0313  0.0310  44  LYS   A CB  
1002 C  CB  B LYS   A 44  ? 0.1834 0.1890 0.2156 -0.0134 0.0034  0.0133  44  LYS   A CB  
1003 C  CG  A LYS   A 44  ? 0.2088 0.1712 0.2768 -0.0034 0.0583  0.0346  44  LYS   A CG  
1004 C  CG  B LYS   A 44  ? 0.2010 0.2083 0.2624 -0.0152 0.0099  0.0154  44  LYS   A CG  
1005 C  CD  A LYS   A 44  ? 0.2482 0.2283 0.3747 -0.0047 0.0481  0.0250  44  LYS   A CD  
1006 C  CD  B LYS   A 44  ? 0.2186 0.2296 0.3148 -0.0165 0.0030  0.0136  44  LYS   A CD  
1007 C  CE  A LYS   A 44  ? 0.2673 0.2598 0.4440 -0.0085 0.0390  0.0202  44  LYS   A CE  
1008 C  CE  B LYS   A 44  ? 0.2274 0.2413 0.3506 -0.0223 -0.0037 0.0124  44  LYS   A CE  
1009 N  NZ  A LYS   A 44  ? 0.2783 0.2799 0.4796 -0.0151 0.0341  0.0191  44  LYS   A NZ  
1010 N  NZ  B LYS   A 44  ? 0.2316 0.2397 0.3685 -0.0279 -0.0090 0.0133  44  LYS   A NZ  
1037 N  N   A HIS   A 45  ? 0.1190 0.1162 0.1784 -0.0024 -0.0015 0.0206  45  HIS   A N   
1038 N  N   B HIS   A 45  ? 0.1557 0.1631 0.1639 -0.0068 -0.0048 0.0072  45  HIS   A N   
1039 C  CA  A HIS   A 45  ? 0.1147 0.1149 0.1701 -0.0011 0.0046  0.0146  45  HIS   A CA  
1040 C  CA  B HIS   A 45  ? 0.1514 0.1559 0.1632 -0.0038 -0.0069 0.0022  45  HIS   A CA  
1041 C  C   A HIS   A 45  ? 0.1181 0.1291 0.1899 0.0029  0.0017  0.0255  45  HIS   A C   
1042 C  C   B HIS   A 45  ? 0.1568 0.1653 0.1790 0.0012  -0.0088 0.0041  45  HIS   A C   
1043 O  O   A HIS   A 45  ? 0.1209 0.1259 0.2099 0.0017  0.0026  0.0143  45  HIS   A O   
1044 O  O   B HIS   A 45  ? 0.1613 0.1670 0.1944 0.0041  -0.0116 -0.0017 45  HIS   A O   
1045 C  CB  A HIS   A 45  ? 0.1200 0.1189 0.1626 -0.0009 0.0055  0.0050  45  HIS   A CB  
1046 C  CB  B HIS   A 45  ? 0.1397 0.1451 0.1539 -0.0022 -0.0088 -0.0005 45  HIS   A CB  
1047 C  CG  A HIS   A 45  ? 0.1209 0.1169 0.1672 -0.0046 0.0062  0.0122  45  HIS   A CG  
1048 C  CG  B HIS   A 45  ? 0.1247 0.1366 0.1507 -0.0035 -0.0046 0.0056  45  HIS   A CG  
1049 N  ND1 A HIS   A 45  ? 0.1144 0.1191 0.1739 0.0001  0.0059  0.0117  45  HIS   A ND1 
1050 N  ND1 B HIS   A 45  ? 0.1171 0.1376 0.1588 -0.0007 -0.0119 0.0186  45  HIS   A ND1 
1051 C  CD2 A HIS   A 45  ? 0.1266 0.1229 0.1757 -0.0013 0.0004  0.0196  45  HIS   A CD2 
1052 C  CD2 B HIS   A 45  ? 0.1145 0.1238 0.1410 -0.0017 -0.0033 0.0009  45  HIS   A CD2 
1053 C  CE1 A HIS   A 45  ? 0.1242 0.1294 0.1727 -0.0081 0.0090  0.0252  45  HIS   A CE1 
1054 C  CE1 B HIS   A 45  ? 0.1105 0.1235 0.1387 -0.0058 -0.0062 0.0024  45  HIS   A CE1 
1055 N  NE2 A HIS   A 45  ? 0.1251 0.1279 0.1760 0.0025  0.0048  0.0207  45  HIS   A NE2 
1056 N  NE2 B HIS   A 45  ? 0.1091 0.1226 0.1299 -0.0069 -0.0043 0.0002  45  HIS   A NE2 
1071 N  N   A GLY   A 46  ? 0.1326 0.1499 0.2033 0.0142  -0.0085 0.0293  46  GLY   A N   
1072 N  N   B GLY   A 46  ? 0.1578 0.1666 0.1779 0.0042  -0.0093 0.0092  46  GLY   A N   
1073 C  CA  A GLY   A 46  ? 0.1382 0.1621 0.2075 0.0182  -0.0053 0.0367  46  GLY   A CA  
1074 C  CA  B GLY   A 46  ? 0.1515 0.1661 0.1614 0.0067  -0.0008 0.0132  46  GLY   A CA  
1075 C  C   A GLY   A 46  ? 0.1432 0.1604 0.2026 0.0274  -0.0137 0.0448  46  GLY   A C   
1076 C  C   B GLY   A 46  ? 0.1492 0.1563 0.1289 0.0109  0.0108  0.0247  46  GLY   A C   
1077 O  O   A GLY   A 46  ? 0.1498 0.1585 0.2009 0.0218  -0.0259 0.0410  46  GLY   A O   
1078 O  O   B GLY   A 46  ? 0.1556 0.1588 0.1273 0.0099  0.0167  0.0235  46  GLY   A O   
1085 N  N   A GLY   A 47  ? 0.1431 0.1656 0.1923 0.0268  -0.0047 0.0312  47  GLY   A N   
1086 N  N   B GLY   A 47  ? 0.1479 0.1523 0.1220 0.0110  0.0058  0.0209  47  GLY   A N   
1087 C  CA  A GLY   A 47  ? 0.1467 0.1709 0.1801 0.0223  -0.0121 0.0194  47  GLY   A CA  
1088 C  CA  B GLY   A 47  ? 0.1414 0.1528 0.1167 0.0083  -0.0022 0.0135  47  GLY   A CA  
1089 C  C   A GLY   A 47  ? 0.1424 0.1597 0.1709 0.0220  -0.0195 0.0164  47  GLY   A C   
1090 C  C   B GLY   A 47  ? 0.1337 0.1408 0.1052 0.0116  0.0007  0.0128  47  GLY   A C   
1091 O  O   A GLY   A 47  ? 0.1448 0.1543 0.1899 0.0258  -0.0134 0.0201  47  GLY   A O   
1092 O  O   B GLY   A 47  ? 0.1258 0.1364 0.1113 0.0180  0.0088  0.0199  47  GLY   A O   
1099 N  N   A GLY   A 48  ? 0.1404 0.1620 0.1629 0.0240  -0.0189 0.0175  48  GLY   A N   
1100 N  N   B GLY   A 48  ? 0.1334 0.1400 0.1057 0.0108  0.0023  0.0006  48  GLY   A N   
1101 C  CA  A GLY   A 48  ? 0.1447 0.1545 0.1773 0.0089  -0.0095 0.0104  48  GLY   A CA  
1102 C  CA  B GLY   A 48  ? 0.1356 0.1325 0.0988 0.0006  0.0020  -0.0060 48  GLY   A CA  
1103 C  C   A GLY   A 48  ? 0.1374 0.1460 0.1752 -0.0061 -0.0068 0.0137  48  GLY   A C   
1104 C  C   B GLY   A 48  ? 0.1369 0.1323 0.1033 -0.0073 0.0042  0.0003  48  GLY   A C   
1105 O  O   A GLY   A 48  ? 0.1471 0.1402 0.1719 0.0013  -0.0025 0.0198  48  GLY   A O   
1106 O  O   B GLY   A 48  ? 0.1440 0.1337 0.0986 -0.0059 0.0130  0.0065  48  GLY   A O   
1113 N  N   A VAL   A 49  ? 0.1311 0.1435 0.1871 -0.0044 -0.0134 0.0118  49  VAL   A N   
1114 N  N   B VAL   A 49  ? 0.1263 0.1305 0.1253 -0.0101 -0.0021 -0.0026 49  VAL   A N   
1115 C  CA  A VAL   A 49  ? 0.1435 0.1381 0.1869 -0.0051 -0.0037 0.0188  49  VAL   A CA  
1116 C  CA  B VAL   A 49  ? 0.1185 0.1330 0.1350 -0.0064 -0.0048 0.0045  49  VAL   A CA  
1117 C  C   A VAL   A 49  ? 0.1385 0.1268 0.1668 -0.0019 -0.0028 0.0215  49  VAL   A C   
1118 C  C   B VAL   A 49  ? 0.1211 0.1270 0.1226 -0.0004 -0.0019 -0.0043 49  VAL   A C   
1119 O  O   A VAL   A 49  ? 0.1448 0.1341 0.1684 -0.0117 -0.0056 0.0115  49  VAL   A O   
1120 O  O   B VAL   A 49  ? 0.1207 0.1290 0.1193 -0.0017 0.0057  0.0040  49  VAL   A O   
1121 C  CB  A VAL   A 49  ? 0.1531 0.1411 0.2187 -0.0076 -0.0127 0.0147  49  VAL   A CB  
1122 C  CB  B VAL   A 49  ? 0.1057 0.1258 0.1549 0.0009  -0.0187 0.0062  49  VAL   A CB  
1123 C  CG1 A VAL   A 49  ? 0.1660 0.1421 0.2299 0.0009  -0.0113 0.0231  49  VAL   A CG1 
1124 C  CG1 B VAL   A 49  ? 0.0908 0.1221 0.1629 0.0177  -0.0216 0.0152  49  VAL   A CG1 
1125 C  CG2 A VAL   A 49  ? 0.1550 0.1511 0.2601 -0.0251 -0.0100 0.0148  49  VAL   A CG2 
1126 C  CG2 B VAL   A 49  ? 0.1071 0.1258 0.1658 0.0033  -0.0116 0.0075  49  VAL   A CG2 
1145 N  N   A ALA   A 50  ? 0.1278 0.1230 0.1787 -0.0023 -0.0120 0.0211  50  ALA   A N   
1146 N  N   B ALA   A 50  ? 0.1217 0.1235 0.1189 0.0052  -0.0079 -0.0067 50  ALA   A N   
1147 C  CA  A ALA   A 50  ? 0.1191 0.1197 0.1820 -0.0142 -0.0102 0.0194  50  ALA   A CA  
1148 C  CA  B ALA   A 50  ? 0.1260 0.1210 0.1161 -0.0002 -0.0079 -0.0087 50  ALA   A CA  
1149 C  C   A ALA   A 50  ? 0.1176 0.1259 0.1814 -0.0112 -0.0096 0.0120  50  ALA   A C   
1150 C  C   B ALA   A 50  ? 0.1339 0.1234 0.1086 -0.0013 -0.0036 -0.0085 50  ALA   A C   
1151 O  O   A ALA   A 50  ? 0.1194 0.1253 0.1917 -0.0047 -0.0145 0.0039  50  ALA   A O   
1152 O  O   B ALA   A 50  ? 0.1398 0.1232 0.0989 0.0003  0.0090  -0.0058 50  ALA   A O   
1153 C  CB  A ALA   A 50  ? 0.1221 0.1283 0.1877 -0.0112 -0.0035 0.0133  50  ALA   A CB  
1154 C  CB  B ALA   A 50  ? 0.1303 0.1156 0.1165 0.0029  -0.0016 -0.0238 50  ALA   A CB  
1165 N  N   A GLY   A 51  ? 0.1218 0.1181 0.1798 0.0011  -0.0103 0.0093  51  GLY   A N   
1166 N  N   B GLY   A 51  ? 0.1373 0.1217 0.1200 0.0011  -0.0133 -0.0111 51  GLY   A N   
1167 C  CA  A GLY   A 51  ? 0.1363 0.1126 0.1905 0.0033  -0.0144 0.0059  51  GLY   A CA  
1168 C  CA  B GLY   A 51  ? 0.1462 0.1241 0.1195 0.0011  -0.0179 -0.0165 51  GLY   A CA  
1169 C  C   A GLY   A 51  ? 0.1179 0.1268 0.1887 0.0051  -0.0046 -0.0017 51  GLY   A C   
1170 C  C   B GLY   A 51  ? 0.1425 0.1349 0.1262 -0.0008 -0.0142 -0.0220 51  GLY   A C   
1171 O  O   A GLY   A 51  ? 0.1227 0.1390 0.2010 0.0031  0.0002  0.0014  51  GLY   A O   
1172 O  O   B GLY   A 51  ? 0.1442 0.1391 0.1272 -0.0042 -0.0092 -0.0240 51  GLY   A O   
1179 N  N   A ALA   A 52  ? 0.1138 0.1386 0.1789 0.0021  0.0010  -0.0024 52  ALA   A N   
1180 N  N   B ALA   A 52  ? 0.1429 0.1418 0.1329 -0.0039 -0.0021 -0.0264 52  ALA   A N   
1181 C  CA  A ALA   A 52  ? 0.1235 0.1543 0.1774 0.0030  0.0022  -0.0074 52  ALA   A CA  
1182 C  CA  B ALA   A 52  ? 0.1422 0.1508 0.1328 -0.0047 -0.0001 -0.0200 52  ALA   A CA  
1183 C  C   A ALA   A 52  ? 0.1233 0.1535 0.1632 -0.0069 0.0136  0.0042  52  ALA   A C   
1184 C  C   B ALA   A 52  ? 0.1391 0.1515 0.1122 -0.0106 0.0091  -0.0160 52  ALA   A C   
1185 O  O   A ALA   A 52  ? 0.1361 0.1635 0.1720 -0.0022 0.0124  -0.0007 52  ALA   A O   
1186 O  O   B ALA   A 52  ? 0.1464 0.1554 0.1098 -0.0110 0.0171  -0.0132 52  ALA   A O   
1187 C  CB  A ALA   A 52  ? 0.1265 0.1818 0.1912 -0.0047 0.0009  0.0040  52  ALA   A CB  
1188 C  CB  B ALA   A 52  ? 0.1427 0.1640 0.1503 -0.0061 -0.0029 -0.0103 52  ALA   A CB  
1199 N  N   A LEU   A 53  ? 0.1209 0.1449 0.1675 -0.0072 0.0086  0.0088  53  LEU   A N   
1200 N  N   B LEU   A 53  ? 0.1343 0.1485 0.1159 -0.0092 0.0030  -0.0109 53  LEU   A N   
1201 C  CA  A LEU   A 53  ? 0.1343 0.1529 0.1667 -0.0085 0.0088  0.0091  53  LEU   A CA  
1202 C  CA  B LEU   A 53  ? 0.1366 0.1510 0.1180 -0.0122 -0.0075 -0.0053 53  LEU   A CA  
1203 C  C   A LEU   A 53  ? 0.1356 0.1499 0.1482 0.0008  0.0058  0.0079  53  LEU   A C   
1204 C  C   B LEU   A 53  ? 0.1338 0.1496 0.1219 -0.0053 -0.0051 -0.0031 53  LEU   A C   
1205 O  O   A LEU   A 53  ? 0.1498 0.1559 0.1685 -0.0136 0.0059  0.0012  53  LEU   A O   
1206 O  O   B LEU   A 53  ? 0.1347 0.1508 0.1342 -0.0067 0.0015  -0.0052 53  LEU   A O   
1207 C  CB  A LEU   A 53  ? 0.1454 0.1482 0.1764 -0.0100 0.0103  0.0075  53  LEU   A CB  
1208 C  CB  B LEU   A 53  ? 0.1422 0.1537 0.1130 -0.0206 -0.0163 0.0042  53  LEU   A CB  
1209 C  CG  A LEU   A 53  ? 0.1692 0.1501 0.1854 -0.0095 0.0027  0.0040  53  LEU   A CG  
1210 C  CG  B LEU   A 53  ? 0.1571 0.1589 0.1174 -0.0258 -0.0182 0.0107  53  LEU   A CG  
1211 C  CD1 A LEU   A 53  ? 0.1718 0.1507 0.1848 0.0048  -0.0107 0.0077  53  LEU   A CD1 
1212 C  CD1 B LEU   A 53  ? 0.1582 0.1600 0.1252 -0.0290 -0.0242 0.0054  53  LEU   A CD1 
1213 C  CD2 A LEU   A 53  ? 0.1965 0.1647 0.2003 -0.0180 0.0104  0.0028  53  LEU   A CD2 
1214 C  CD2 B LEU   A 53  ? 0.1724 0.1679 0.1306 -0.0320 -0.0105 0.0192  53  LEU   A CD2 
1237 N  N   A ASN   A 54  ? 0.1252 0.1443 0.1564 -0.0038 -0.0119 0.0091  54  ASN   A N   
1238 N  N   B ASN   A 54  ? 0.1312 0.1485 0.1388 -0.0060 -0.0062 -0.0008 54  ASN   A N   
1239 C  CA  A ASN   A 54  ? 0.1165 0.1352 0.1704 -0.0035 -0.0065 0.0107  54  ASN   A CA  
1240 C  CA  B ASN   A 54  ? 0.1284 0.1456 0.1500 -0.0071 -0.0044 -0.0013 54  ASN   A CA  
1241 C  C   A ASN   A 54  ? 0.1279 0.1371 0.1807 -0.0112 0.0013  0.0051  54  ASN   A C   
1242 C  C   B ASN   A 54  ? 0.1320 0.1410 0.1573 -0.0087 0.0002  -0.0025 54  ASN   A C   
1243 O  O   A ASN   A 54  ? 0.1296 0.1462 0.1922 -0.0072 -0.0023 -0.0020 54  ASN   A O   
1244 O  O   B ASN   A 54  ? 0.1330 0.1406 0.1575 -0.0115 0.0014  -0.0039 54  ASN   A O   
1245 C  CB  A ASN   A 54  ? 0.1193 0.1313 0.1728 0.0004  -0.0141 0.0076  54  ASN   A CB  
1246 C  CB  B ASN   A 54  ? 0.1338 0.1486 0.1521 -0.0042 -0.0051 0.0002  54  ASN   A CB  
1247 C  CG  A ASN   A 54  ? 0.1173 0.1284 0.1877 0.0031  -0.0046 0.0016  54  ASN   A CG  
1248 C  CG  B ASN   A 54  ? 0.1338 0.1504 0.1576 -0.0026 -0.0026 -0.0035 54  ASN   A CG  
1249 O  OD1 A ASN   A 54  ? 0.1163 0.1312 0.1867 -0.0003 -0.0099 0.0143  54  ASN   A OD1 
1250 O  OD1 B ASN   A 54  ? 0.1321 0.1554 0.1604 -0.0090 -0.0117 -0.0028 54  ASN   A OD1 
1251 N  ND2 A ASN   A 54  ? 0.1167 0.1345 0.1996 -0.0055 -0.0103 0.0123  54  ASN   A ND2 
1252 N  ND2 B ASN   A 54  ? 0.1370 0.1499 0.1608 -0.0009 0.0037  0.0004  54  ASN   A ND2 
1265 N  N   . LYS   A 55  ? 0.1287 0.1370 0.1710 -0.0010 -0.0041 -0.0078 55  LYS   A N   
1266 C  CA  . LYS   A 55  ? 0.1350 0.1511 0.1847 0.0029  -0.0093 -0.0157 55  LYS   A CA  
1267 C  C   . LYS   A 55  ? 0.1344 0.1624 0.1794 -0.0032 -0.0069 -0.0173 55  LYS   A C   
1268 O  O   . LYS   A 55  ? 0.1444 0.1791 0.1910 0.0048  -0.0109 -0.0276 55  LYS   A O   
1269 C  CB  . LYS   A 55  ? 0.1387 0.1646 0.1993 0.0109  -0.0041 -0.0175 55  LYS   A CB  
1270 C  CG  . LYS   A 55  ? 0.1588 0.1910 0.2177 0.0266  -0.0218 -0.0301 55  LYS   A CG  
1271 C  CD  . LYS   A 55  ? 0.1809 0.2183 0.2315 0.0422  -0.0236 -0.0255 55  LYS   A CD  
1272 C  CE  . LYS   A 55  ? 0.2000 0.2519 0.2495 0.0552  -0.0290 -0.0211 55  LYS   A CE  
1273 N  NZ  . LYS   A 55  ? 0.2093 0.2669 0.2583 0.0595  -0.0300 -0.0191 55  LYS   A NZ  
1288 N  N   . ALA   A 56  ? 0.1393 0.1700 0.1813 -0.0079 0.0013  -0.0129 56  ALA   A N   
1289 C  CA  . ALA   A 56  ? 0.1546 0.1858 0.1732 -0.0105 0.0096  -0.0122 56  ALA   A CA  
1290 C  C   . ALA   A 56  ? 0.1561 0.1997 0.1540 -0.0082 0.0130  -0.0138 56  ALA   A C   
1291 O  O   . ALA   A 56  ? 0.1562 0.2292 0.1661 0.0023  0.0159  -0.0084 56  ALA   A O   
1292 C  CB  . ALA   A 56  ? 0.1576 0.2010 0.1903 -0.0219 0.0058  0.0020  56  ALA   A CB  
1298 N  N   . THR   A 57  ? 0.1411 0.1806 0.1588 -0.0095 0.0132  -0.0092 57  THR   A N   
1299 C  CA  . THR   A 57  ? 0.1474 0.1737 0.1608 -0.0093 0.0019  -0.0074 57  THR   A CA  
1300 C  C   . THR   A 57  ? 0.1462 0.1755 0.1679 -0.0053 0.0029  -0.0136 57  THR   A C   
1301 O  O   . THR   A 57  ? 0.1437 0.1808 0.1874 -0.0148 -0.0023 -0.0297 57  THR   A O   
1302 C  CB  . THR   A 57  ? 0.1432 0.1678 0.1496 -0.0125 0.0041  -0.0024 57  THR   A CB  
1303 O  OG1 . THR   A 57  ? 0.1358 0.1644 0.1631 -0.0069 -0.0002 -0.0072 57  THR   A OG1 
1304 C  CG2 . THR   A 57  ? 0.1486 0.1707 0.1444 -0.0087 -0.0016 0.0131  57  THR   A CG2 
1312 N  N   . ASN   A 58  ? 0.1463 0.1689 0.1901 -0.0060 0.0066  -0.0167 58  ASN   A N   
1313 C  CA  . ASN   A 58  ? 0.1675 0.1669 0.2085 -0.0095 0.0088  -0.0282 58  ASN   A CA  
1314 C  C   . ASN   A 58  ? 0.1459 0.1520 0.1975 -0.0003 0.0008  -0.0219 58  ASN   A C   
1315 O  O   . ASN   A 58  ? 0.1475 0.1618 0.2163 -0.0123 -0.0044 -0.0260 58  ASN   A O   
1316 C  CB  . ASN   A 58  ? 0.2102 0.1796 0.2373 -0.0133 0.0243  -0.0405 58  ASN   A CB  
1317 C  CG  . ASN   A 58  ? 0.2433 0.2037 0.2973 -0.0073 0.0286  -0.0186 58  ASN   A CG  
1318 O  OD1 . ASN   A 58  ? 0.2673 0.2047 0.3312 0.0258  0.0523  -0.0102 58  ASN   A OD1 
1319 N  ND2 . ASN   A 58  ? 0.2485 0.2107 0.3173 -0.0097 0.0208  -0.0205 58  ASN   A ND2 
1326 N  N   . ASN   A 59  ? 0.1297 0.1465 0.1876 -0.0022 -0.0101 -0.0090 59  ASN   A N   
1327 C  CA  . ASN   A 59  ? 0.1338 0.1389 0.1918 -0.0026 -0.0059 -0.0056 59  ASN   A CA  
1328 C  C   . ASN   A 59  ? 0.1340 0.1373 0.1732 -0.0060 -0.0013 -0.0004 59  ASN   A C   
1329 O  O   . ASN   A 59  ? 0.1371 0.1355 0.1802 -0.0049 -0.0017 0.0022  59  ASN   A O   
1330 C  CB  . ASN   A 59  ? 0.1381 0.1306 0.1923 0.0009  -0.0227 -0.0038 59  ASN   A CB  
1331 C  CG  . ASN   A 59  ? 0.1438 0.1359 0.1902 -0.0048 -0.0287 0.0030  59  ASN   A CG  
1332 O  OD1 . ASN   A 59  ? 0.1591 0.1455 0.1843 -0.0096 -0.0263 0.0036  59  ASN   A OD1 
1333 N  ND2 . ASN   A 59  ? 0.1519 0.1431 0.2024 -0.0152 -0.0167 0.0069  59  ASN   A ND2 
1340 N  N   . ALA   A 60  ? 0.1290 0.1449 0.1705 -0.0026 -0.0016 0.0054  60  ALA   A N   
1341 C  CA  . ALA   A 60  ? 0.1280 0.1463 0.1793 -0.0052 -0.0124 0.0005  60  ALA   A CA  
1342 C  C   . ALA   A 60  ? 0.1271 0.1413 0.1898 -0.0079 -0.0110 0.0064  60  ALA   A C   
1343 O  O   . ALA   A 60  ? 0.1224 0.1442 0.2074 -0.0027 -0.0038 0.0009  60  ALA   A O   
1344 C  CB  . ALA   A 60  ? 0.1384 0.1598 0.1826 0.0024  -0.0106 -0.0159 60  ALA   A CB  
1350 N  N   . MET   A 61  ? 0.1268 0.1325 0.1766 -0.0054 0.0032  0.0082  61  MET   A N   
1351 C  CA  . MET   A 61  ? 0.1271 0.1284 0.1848 -0.0071 0.0043  0.0083  61  MET   A CA  
1352 C  C   . MET   A 61  ? 0.1195 0.1287 0.1865 -0.0136 -0.0030 -0.0025 61  MET   A C   
1353 O  O   . MET   A 61  ? 0.1226 0.1312 0.1936 -0.0045 0.0061  0.0118  61  MET   A O   
1354 C  CB  . MET   A 61  ? 0.1358 0.1327 0.1803 -0.0066 0.0102  0.0053  61  MET   A CB  
1355 C  CG  . MET   A 61  ? 0.1337 0.1364 0.1989 -0.0035 -0.0029 0.0060  61  MET   A CG  
1356 S  SD  . MET   A 61  ? 0.1392 0.1444 0.2096 -0.0120 -0.0004 -0.0094 61  MET   A SD  
1357 C  CE  . MET   A 61  ? 0.1594 0.1589 0.2497 -0.0137 0.0104  -0.0086 61  MET   A CE  
1367 N  N   . GLN   A 62  ? 0.1274 0.1227 0.1807 -0.0069 -0.0014 0.0027  62  GLN   A N   
1368 C  CA  . GLN   A 62  ? 0.1271 0.1197 0.1892 -0.0055 0.0038  0.0070  62  GLN   A CA  
1369 C  C   . GLN   A 62  ? 0.1344 0.1128 0.1909 -0.0016 0.0039  0.0060  62  GLN   A C   
1370 O  O   . GLN   A 62  ? 0.1289 0.1282 0.1911 -0.0037 0.0033  0.0032  62  GLN   A O   
1371 C  CB  . GLN   A 62  ? 0.1265 0.1180 0.1904 -0.0033 0.0031  0.0103  62  GLN   A CB  
1372 C  CG  . GLN   A 62  ? 0.1293 0.1205 0.1925 -0.0069 -0.0008 0.0187  62  GLN   A CG  
1373 C  CD  . GLN   A 62  ? 0.1378 0.1256 0.1806 -0.0003 0.0041  0.0151  62  GLN   A CD  
1374 O  OE1 . GLN   A 62  ? 0.1382 0.1438 0.1947 -0.0038 -0.0045 0.0100  62  GLN   A OE1 
1375 N  NE2 . GLN   A 62  ? 0.1430 0.1307 0.1932 0.0018  0.0054  0.0024  62  GLN   A NE2 
1384 N  N   . VAL   A 63  ? 0.1302 0.1226 0.2060 -0.0037 0.0051  -0.0146 63  VAL   A N   
1385 C  CA  . VAL   A 63  ? 0.1270 0.1345 0.2157 -0.0129 -0.0062 -0.0065 63  VAL   A CA  
1386 C  C   . VAL   A 63  ? 0.1133 0.1324 0.2058 -0.0128 -0.0143 -0.0030 63  VAL   A C   
1387 O  O   . VAL   A 63  ? 0.1185 0.1362 0.2324 -0.0137 -0.0042 -0.0034 63  VAL   A O   
1388 C  CB  . VAL   A 63  ? 0.1418 0.1538 0.2498 -0.0204 -0.0079 -0.0285 63  VAL   A CB  
1389 C  CG1 . VAL   A 63  ? 0.1514 0.1741 0.2782 -0.0111 -0.0182 -0.0502 63  VAL   A CG1 
1390 C  CG2 . VAL   A 63  ? 0.1516 0.1460 0.2489 -0.0092 0.0081  -0.0285 63  VAL   A CG2 
1400 N  N   . GLU   A 64  ? 0.1251 0.1422 0.1867 -0.0009 -0.0068 -0.0013 64  GLU   A N   
1401 C  CA  . GLU   A 64  ? 0.1265 0.1401 0.1940 -0.0085 -0.0111 0.0039  64  GLU   A CA  
1402 C  C   . GLU   A 64  ? 0.1198 0.1363 0.1868 -0.0078 0.0040  0.0066  64  GLU   A C   
1403 O  O   . GLU   A 64  ? 0.1326 0.1378 0.1947 -0.0023 0.0002  0.0034  64  GLU   A O   
1404 C  CB  . GLU   A 64  ? 0.1378 0.1532 0.1925 -0.0046 0.0009  0.0041  64  GLU   A CB  
1405 C  CG  . GLU   A 64  ? 0.1405 0.1579 0.2031 -0.0096 0.0001  0.0006  64  GLU   A CG  
1406 C  CD  . GLU   A 64  ? 0.1547 0.1683 0.2151 -0.0162 0.0043  0.0018  64  GLU   A CD  
1407 O  OE1 . GLU   A 64  ? 0.1528 0.1762 0.2364 -0.0207 0.0082  0.0070  64  GLU   A OE1 
1408 O  OE2 . GLU   A 64  ? 0.1736 0.1669 0.2152 -0.0185 -0.0107 0.0161  64  GLU   A OE2 
1415 N  N   . SER   A 65  ? 0.1116 0.1334 0.1855 0.0023  -0.0053 0.0080  65  SER   A N   
1416 C  CA  . SER   A 65  ? 0.1228 0.1264 0.1827 -0.0003 -0.0044 -0.0003 65  SER   A CA  
1417 C  C   . SER   A 65  ? 0.1230 0.1341 0.1843 -0.0050 -0.0014 0.0100  65  SER   A C   
1418 O  O   . SER   A 65  ? 0.1316 0.1378 0.2065 -0.0021 0.0111  0.0047  65  SER   A O   
1419 C  CB  . SER   A 65  ? 0.1247 0.1275 0.1879 -0.0070 0.0010  0.0136  65  SER   A CB  
1420 O  OG  . SER   A 65  ? 0.1253 0.1384 0.1913 -0.0077 -0.0022 0.0175  65  SER   A OG  
1426 N  N   . ASP   A 66  ? 0.1280 0.1326 0.1895 -0.0029 0.0114  0.0160  66  ASP   A N   
1427 C  CA  . ASP   A 66  ? 0.1364 0.1436 0.2003 -0.0014 0.0069  0.0243  66  ASP   A CA  
1428 C  C   . ASP   A 66  ? 0.1350 0.1435 0.2056 -0.0047 0.0077  0.0219  66  ASP   A C   
1429 O  O   . ASP   A 66  ? 0.1410 0.1508 0.2164 -0.0024 0.0250  0.0282  66  ASP   A O   
1430 C  CB  . ASP   A 66  ? 0.1435 0.1518 0.2398 0.0103  0.0173  0.0366  66  ASP   A CB  
1431 C  CG  . ASP   A 66  ? 0.1692 0.1647 0.2625 0.0026  0.0028  0.0562  66  ASP   A CG  
1432 O  OD1 . ASP   A 66  ? 0.1731 0.1926 0.2504 -0.0076 -0.0018 0.0555  66  ASP   A OD1 
1433 O  OD2 . ASP   A 66  ? 0.1875 0.1856 0.3359 0.0287  -0.0150 0.0368  66  ASP   A OD2 
1438 N  N   . ASP   A 67  ? 0.1242 0.1414 0.2173 -0.0050 0.0051  0.0236  67  ASP   A N   
1439 C  CA  . ASP   A 67  ? 0.1277 0.1579 0.2228 0.0004  0.0054  0.0327  67  ASP   A CA  
1440 C  C   . ASP   A 67  ? 0.1322 0.1609 0.2273 0.0066  0.0118  0.0267  67  ASP   A C   
1441 O  O   . ASP   A 67  ? 0.1276 0.1693 0.2445 0.0040  0.0247  0.0356  67  ASP   A O   
1442 C  CB  . ASP   A 67  ? 0.1396 0.1714 0.2460 -0.0040 -0.0070 0.0395  67  ASP   A CB  
1443 C  CG  . ASP   A 67  ? 0.1336 0.1871 0.2805 -0.0061 -0.0172 0.0507  67  ASP   A CG  
1444 O  OD1 . ASP   A 67  ? 0.1369 0.2084 0.3525 -0.0162 -0.0267 0.0550  67  ASP   A OD1 
1445 O  OD2 . ASP   A 67  ? 0.1370 0.1928 0.2787 0.0007  -0.0109 0.0404  67  ASP   A OD2 
1450 N  N   . TYR   A 68  ? 0.1352 0.1446 0.2190 0.0048  0.0163  0.0372  68  TYR   A N   
1451 C  CA  . TYR   A 68  ? 0.1404 0.1444 0.2231 0.0017  0.0231  0.0325  68  TYR   A CA  
1452 C  C   . TYR   A 68  ? 0.1340 0.1416 0.2214 -0.0006 0.0241  0.0237  68  TYR   A C   
1453 O  O   . TYR   A 68  ? 0.1399 0.1526 0.2253 0.0108  0.0235  0.0241  68  TYR   A O   
1454 C  CB  . TYR   A 68  ? 0.1458 0.1401 0.2377 0.0111  0.0401  0.0355  68  TYR   A CB  
1455 C  CG  . TYR   A 68  ? 0.1524 0.1552 0.2662 0.0058  0.0468  0.0322  68  TYR   A CG  
1456 C  CD1 . TYR   A 68  ? 0.1622 0.1658 0.3030 -0.0227 0.0461  -0.0078 68  TYR   A CD1 
1457 C  CD2 . TYR   A 68  ? 0.1754 0.1583 0.3070 0.0133  0.0557  0.0459  68  TYR   A CD2 
1458 C  CE1 . TYR   A 68  ? 0.1741 0.1771 0.3345 -0.0239 0.0569  -0.0115 68  TYR   A CE1 
1459 C  CE2 . TYR   A 68  ? 0.1818 0.1681 0.3385 0.0041  0.0655  0.0180  68  TYR   A CE2 
1460 C  CZ  . TYR   A 68  ? 0.1741 0.1680 0.3528 -0.0223 0.0576  -0.0149 68  TYR   A CZ  
1461 O  OH  . TYR   A 68  ? 0.2013 0.1751 0.3857 -0.0181 0.0337  -0.0421 68  TYR   A OH  
1471 N  N   . ILE   A 69  ? 0.1271 0.1338 0.2124 -0.0013 0.0159  0.0198  69  ILE   A N   
1472 C  CA  . ILE   A 69  ? 0.1334 0.1402 0.2048 0.0077  0.0079  0.0058  69  ILE   A CA  
1473 C  C   . ILE   A 69  ? 0.1372 0.1381 0.2043 0.0052  0.0135  0.0153  69  ILE   A C   
1474 O  O   . ILE   A 69  ? 0.1446 0.1487 0.2108 0.0016  0.0178  0.0187  69  ILE   A O   
1475 C  CB  . ILE   A 69  ? 0.1428 0.1587 0.2014 0.0083  0.0144  0.0014  69  ILE   A CB  
1476 C  CG1 . ILE   A 69  ? 0.1421 0.1687 0.2212 0.0087  0.0110  -0.0130 69  ILE   A CG1 
1477 C  CG2 . ILE   A 69  ? 0.1638 0.1807 0.2101 0.0176  0.0021  -0.0177 69  ILE   A CG2 
1478 C  CD1 . ILE   A 69  ? 0.1484 0.1787 0.2457 -0.0053 0.0159  -0.0135 69  ILE   A CD1 
1490 N  N   . ALA   A 70  ? 0.1486 0.1383 0.2137 -0.0032 0.0169  0.0241  70  ALA   A N   
1491 C  CA  . ALA   A 70  ? 0.1523 0.1549 0.2343 -0.0136 0.0231  0.0288  70  ALA   A CA  
1492 C  C   . ALA   A 70  ? 0.1494 0.1729 0.2427 -0.0081 0.0233  0.0252  70  ALA   A C   
1493 O  O   . ALA   A 70  ? 0.1647 0.2107 0.2568 0.0132  0.0397  0.0470  70  ALA   A O   
1494 C  CB  . ALA   A 70  ? 0.1581 0.1505 0.2498 -0.0173 0.0204  0.0300  70  ALA   A CB  
1500 N  N   . THR   A 71  ? 0.1415 0.1713 0.2410 -0.0016 0.0161  0.0285  71  THR   A N   
1501 C  CA  . THR   A 71  ? 0.1511 0.1922 0.2713 0.0117  0.0209  0.0352  71  THR   A CA  
1502 C  C   . THR   A 71  ? 0.1365 0.1767 0.2874 0.0168  0.0233  0.0309  71  THR   A C   
1503 O  O   . THR   A 71  ? 0.1440 0.2038 0.3337 0.0176  0.0374  0.0039  71  THR   A O   
1504 C  CB  . THR   A 71  ? 0.1838 0.2255 0.3083 0.0169  -0.0138 0.0423  71  THR   A CB  
1505 O  OG1 . THR   A 71  ? 0.2131 0.2416 0.3278 0.0100  -0.0322 0.0435  71  THR   A OG1 
1506 C  CG2 . THR   A 71  ? 0.1938 0.2384 0.3316 0.0263  -0.0209 0.0593  71  THR   A CG2 
1514 N  N   . ASN   A 72  ? 0.1422 0.1627 0.2537 0.0175  0.0270  0.0347  72  ASN   A N   
1515 C  CA  . ASN   A 72  ? 0.1501 0.1610 0.2493 0.0196  0.0394  0.0316  72  ASN   A CA  
1516 C  C   . ASN   A 72  ? 0.1636 0.1557 0.2542 0.0150  0.0493  0.0274  72  ASN   A C   
1517 O  O   . ASN   A 72  ? 0.1798 0.1538 0.2766 0.0177  0.0450  0.0119  72  ASN   A O   
1518 C  CB  . ASN   A 72  ? 0.1783 0.1757 0.2459 0.0168  0.0391  0.0368  72  ASN   A CB  
1519 C  CG  . ASN   A 72  ? 0.2019 0.1883 0.2527 0.0279  0.0398  0.0377  72  ASN   A CG  
1520 O  OD1 . ASN   A 72  ? 0.2188 0.2198 0.2734 0.0329  0.0413  0.0364  72  ASN   A OD1 
1521 N  ND2 . ASN   A 72  ? 0.2180 0.1908 0.2648 0.0543  0.0228  0.0317  72  ASN   A ND2 
1528 N  N   . GLY   A 73  ? 0.1637 0.1488 0.2417 0.0055  0.0462  0.0190  73  GLY   A N   
1529 C  CA  . GLY   A 73  ? 0.1711 0.1521 0.2276 -0.0036 0.0495  0.0120  73  GLY   A CA  
1530 C  C   . GLY   A 73  ? 0.1724 0.1444 0.2116 0.0026  0.0518  0.0259  73  GLY   A C   
1531 O  O   . GLY   A 73  ? 0.1697 0.1503 0.2188 0.0133  0.0376  0.0305  73  GLY   A O   
1535 N  N   . PRO   A 74  ? 0.1797 0.1488 0.2140 -0.0124 0.0518  0.0128  74  PRO   A N   
1536 C  CA  . PRO   A 74  ? 0.1717 0.1464 0.2208 -0.0010 0.0503  0.0136  74  PRO   A CA  
1537 C  C   . PRO   A 74  ? 0.1645 0.1285 0.2263 0.0008  0.0305  0.0065  74  PRO   A C   
1538 O  O   . PRO   A 74  ? 0.1718 0.1384 0.2488 0.0036  0.0327  0.0031  74  PRO   A O   
1539 C  CB  . PRO   A 74  ? 0.1895 0.1770 0.2468 0.0033  0.0453  0.0227  74  PRO   A CB  
1540 C  CG  . PRO   A 74  ? 0.2164 0.2114 0.2829 -0.0146 0.0318  0.0137  74  PRO   A CG  
1541 C  CD  . PRO   A 74  ? 0.1962 0.1829 0.2345 -0.0227 0.0401  0.0067  74  PRO   A CD  
1549 N  N   . LEU   A 75  ? 0.1665 0.1188 0.2089 0.0008  0.0186  0.0070  75  LEU   A N   
1550 C  CA  . LEU   A 75  ? 0.1588 0.1291 0.1806 0.0039  0.0078  0.0160  75  LEU   A CA  
1551 C  C   . LEU   A 75  ? 0.1702 0.1390 0.1692 0.0087  0.0065  0.0180  75  LEU   A C   
1552 O  O   . LEU   A 75  ? 0.2072 0.1553 0.1762 0.0136  0.0062  0.0156  75  LEU   A O   
1553 C  CB  . LEU   A 75  ? 0.1622 0.1330 0.1828 -0.0027 0.0090  0.0255  75  LEU   A CB  
1554 C  CG  . LEU   A 75  ? 0.1849 0.1638 0.1969 -0.0363 0.0050  0.0156  75  LEU   A CG  
1555 C  CD1 . LEU   A 75  ? 0.1990 0.2175 0.2129 -0.0413 0.0059  -0.0007 75  LEU   A CD1 
1556 C  CD2 . LEU   A 75  ? 0.2132 0.2098 0.2387 -0.0162 0.0043  0.0181  75  LEU   A CD2 
1568 N  N   . LYS   A 76  ? 0.1683 0.1373 0.1949 -0.0037 0.0026  0.0090  76  LYS   A N   
1569 C  CA  . LYS   A 76  ? 0.1663 0.1533 0.2004 -0.0083 0.0030  -0.0000 76  LYS   A CA  
1570 C  C   . LYS   A 76  ? 0.1664 0.1392 0.1750 -0.0008 0.0020  0.0134  76  LYS   A C   
1571 O  O   . LYS   A 76  ? 0.1691 0.1335 0.1850 -0.0049 0.0164  0.0183  76  LYS   A O   
1572 C  CB  . LYS   A 76  ? 0.1687 0.1773 0.2310 0.0017  0.0041  -0.0209 76  LYS   A CB  
1573 C  CG  . LYS   A 76  ? 0.1752 0.1708 0.2763 0.0103  -0.0019 -0.0209 76  LYS   A CG  
1574 C  CD  . LYS   A 76  ? 0.1832 0.1784 0.3270 0.0138  -0.0067 -0.0197 76  LYS   A CD  
1575 C  CE  . LYS   A 76  ? 0.1950 0.1891 0.3767 0.0057  -0.0093 -0.0280 76  LYS   A CE  
1576 N  NZ  . LYS   A 76  ? 0.1942 0.1825 0.4161 -0.0064 -0.0158 -0.0330 76  LYS   A NZ  
1590 N  N   . VAL   A 77  ? 0.1786 0.1473 0.1725 -0.0051 0.0102  0.0142  77  VAL   A N   
1591 C  CA  . VAL   A 77  ? 0.1732 0.1462 0.1693 -0.0006 0.0069  0.0100  77  VAL   A CA  
1592 C  C   . VAL   A 77  ? 0.1661 0.1404 0.1857 0.0043  0.0089  0.0068  77  VAL   A C   
1593 O  O   . VAL   A 77  ? 0.1749 0.1477 0.1911 0.0112  0.0226  -0.0005 77  VAL   A O   
1594 C  CB  . VAL   A 77  ? 0.1898 0.1660 0.1749 -0.0007 0.0066  0.0129  77  VAL   A CB  
1595 C  CG1 . VAL   A 77  ? 0.1865 0.1766 0.1899 0.0084  0.0002  0.0046  77  VAL   A CG1 
1596 C  CG2 . VAL   A 77  ? 0.2079 0.1796 0.1987 -0.0041 -0.0031 0.0160  77  VAL   A CG2 
1606 N  N   . GLY   A 78  ? 0.1539 0.1410 0.1805 -0.0001 0.0159  0.0071  78  GLY   A N   
1607 C  CA  . GLY   A 78  ? 0.1594 0.1380 0.1906 -0.0060 0.0163  0.0114  78  GLY   A CA  
1608 C  C   . GLY   A 78  ? 0.1470 0.1361 0.2047 -0.0044 0.0177  0.0158  78  GLY   A C   
1609 O  O   . GLY   A 78  ? 0.1436 0.1403 0.2250 -0.0010 0.0153  0.0362  78  GLY   A O   
1613 N  N   . GLY   A 79  ? 0.1543 0.1319 0.1923 0.0027  0.0130  0.0203  79  GLY   A N   
1614 C  CA  . GLY   A 79  ? 0.1523 0.1355 0.1903 0.0005  0.0119  0.0210  79  GLY   A CA  
1615 C  C   . GLY   A 79  ? 0.1399 0.1267 0.1784 -0.0006 0.0096  0.0131  79  GLY   A C   
1616 O  O   . GLY   A 79  ? 0.1419 0.1372 0.2159 0.0146  0.0135  0.0126  79  GLY   A O   
1620 N  N   . SER   A 80  ? 0.1390 0.1477 0.2004 -0.0037 0.0121  0.0026  80  SER   A N   
1621 C  CA  . SER   A 80  ? 0.1364 0.1389 0.2073 -0.0034 0.0068  0.0121  80  SER   A CA  
1622 C  C   . SER   A 80  ? 0.1298 0.1368 0.2044 -0.0076 0.0009  0.0190  80  SER   A C   
1623 O  O   . SER   A 80  ? 0.1289 0.1647 0.2235 0.0077  0.0106  0.0020  80  SER   A O   
1624 C  CB  . SER   A 80  ? 0.1473 0.1357 0.2316 -0.0073 0.0090  0.0162  80  SER   A CB  
1625 O  OG  . SER   A 80  ? 0.1704 0.1388 0.2573 0.0026  0.0039  0.0278  80  SER   A OG  
1631 N  N   . CYS   A 81  ? 0.1277 0.1281 0.2115 -0.0053 -0.0024 0.0206  81  CYS   A N   
1632 C  CA  . CYS   A 81  ? 0.1272 0.1407 0.1994 -0.0051 -0.0070 0.0258  81  CYS   A CA  
1633 C  C   . CYS   A 81  ? 0.1258 0.1380 0.1963 -0.0069 -0.0048 0.0337  81  CYS   A C   
1634 O  O   . CYS   A 81  ? 0.1260 0.1710 0.2045 -0.0010 -0.0020 0.0417  81  CYS   A O   
1635 C  CB  . CYS   A 81  ? 0.1338 0.1519 0.2124 -0.0138 -0.0010 0.0352  81  CYS   A CB  
1636 S  SG  . CYS   A 81  ? 0.1486 0.1399 0.1974 -0.0138 0.0001  0.0208  81  CYS   A SG  
1642 N  N   . VAL   A 82  ? 0.1272 0.1484 0.2100 -0.0005 -0.0070 0.0350  82  VAL   A N   
1643 C  CA  . VAL   A 82  ? 0.1451 0.1494 0.2010 -0.0031 -0.0046 0.0342  82  VAL   A CA  
1644 C  C   . VAL   A 82  ? 0.1412 0.1529 0.2021 -0.0037 -0.0063 0.0307  82  VAL   A C   
1645 O  O   . VAL   A 82  ? 0.1351 0.1610 0.2265 -0.0029 -0.0024 0.0134  82  VAL   A O   
1646 C  CB  . VAL   A 82  ? 0.1759 0.1644 0.2091 0.0034  -0.0006 0.0431  82  VAL   A CB  
1647 C  CG1 . VAL   A 82  ? 0.1953 0.1742 0.2210 -0.0005 0.0043  0.0363  82  VAL   A CG1 
1648 C  CG2 . VAL   A 82  ? 0.1819 0.1686 0.2351 -0.0056 -0.0004 0.0458  82  VAL   A CG2 
1658 N  N   . LEU   A 83  ? 0.1390 0.1536 0.1898 -0.0093 -0.0091 0.0229  83  LEU   A N   
1659 C  CA  . LEU   A 83  ? 0.1414 0.1543 0.1836 -0.0158 -0.0111 0.0179  83  LEU   A CA  
1660 C  C   . LEU   A 83  ? 0.1473 0.1563 0.1756 -0.0152 -0.0102 0.0166  83  LEU   A C   
1661 O  O   . LEU   A 83  ? 0.1543 0.1644 0.1926 -0.0197 -0.0073 0.0388  83  LEU   A O   
1662 C  CB  . LEU   A 83  ? 0.1478 0.1582 0.1863 -0.0142 -0.0129 0.0172  83  LEU   A CB  
1663 C  CG  . LEU   A 83  ? 0.1599 0.1660 0.1963 -0.0128 0.0060  0.0136  83  LEU   A CG  
1664 C  CD1 . LEU   A 83  ? 0.1696 0.1655 0.1967 -0.0236 0.0006  0.0216  83  LEU   A CD1 
1665 C  CD2 . LEU   A 83  ? 0.1546 0.1767 0.2096 -0.0172 0.0116  0.0215  83  LEU   A CD2 
1677 N  N   . SER   A 84  ? 0.1663 0.1646 0.1752 -0.0174 -0.0146 0.0246  84  SER   A N   
1678 C  CA  . SER   A 84  ? 0.1782 0.1723 0.1577 -0.0181 -0.0099 0.0248  84  SER   A CA  
1679 C  C   . SER   A 84  ? 0.1792 0.1702 0.1542 -0.0283 0.0019  0.0221  84  SER   A C   
1680 O  O   . SER   A 84  ? 0.1695 0.1842 0.1534 -0.0175 -0.0035 0.0268  84  SER   A O   
1681 C  CB  . SER   A 84  ? 0.1902 0.1937 0.1763 -0.0202 -0.0131 0.0160  84  SER   A CB  
1682 O  OG  . SER   A 84  ? 0.1877 0.2162 0.1943 -0.0188 -0.0288 0.0011  84  SER   A OG  
1688 N  N   . GLY   A 85  ? 0.1908 0.1862 0.1636 -0.0269 0.0102  0.0268  85  GLY   A N   
1689 C  CA  . GLY   A 85  ? 0.1892 0.1919 0.1830 -0.0298 0.0124  0.0126  85  GLY   A CA  
1690 C  C   . GLY   A 85  ? 0.1831 0.2081 0.1629 -0.0266 -0.0039 0.0104  85  GLY   A C   
1691 O  O   . GLY   A 85  ? 0.1846 0.2243 0.1773 -0.0348 0.0051  -0.0054 85  GLY   A O   
1695 N  N   . HIS   A 86  ? 0.1848 0.1979 0.1587 -0.0200 -0.0056 0.0138  86  HIS   A N   
1696 C  CA  . HIS   A 86  ? 0.2069 0.2070 0.1552 -0.0219 -0.0075 0.0180  86  HIS   A CA  
1697 C  C   . HIS   A 86  ? 0.2327 0.2239 0.1443 -0.0229 -0.0123 0.0119  86  HIS   A C   
1698 O  O   . HIS   A 86  ? 0.2433 0.2451 0.1656 -0.0214 -0.0056 0.0105  86  HIS   A O   
1699 C  CB  . HIS   A 86  ? 0.2045 0.1998 0.1595 -0.0236 -0.0065 0.0164  86  HIS   A CB  
1700 C  CG  . HIS   A 86  ? 0.1973 0.1984 0.1698 -0.0115 0.0009  0.0211  86  HIS   A CG  
1701 N  ND1 . HIS   A 86  ? 0.2050 0.1971 0.2006 -0.0171 0.0012  0.0209  86  HIS   A ND1 
1702 C  CD2 . HIS   A 86  ? 0.1958 0.1999 0.1619 -0.0010 0.0032  0.0243  86  HIS   A CD2 
1703 C  CE1 . HIS   A 86  ? 0.2002 0.1981 0.2048 -0.0110 0.0141  0.0212  86  HIS   A CE1 
1704 N  NE2 . HIS   A 86  ? 0.1974 0.1933 0.1816 0.0036  0.0126  0.0337  86  HIS   A NE2 
1712 N  N   . ASN   A 87  ? 0.2458 0.2323 0.1509 -0.0140 0.0046  -0.0062 87  ASN   A N   
1713 C  CA  . ASN   A 87  ? 0.2694 0.2444 0.1572 -0.0140 0.0256  -0.0093 87  ASN   A CA  
1714 C  C   . ASN   A 87  ? 0.2676 0.2596 0.1780 -0.0245 0.0472  0.0017  87  ASN   A C   
1715 O  O   . ASN   A 87  ? 0.2939 0.2817 0.2173 -0.0376 0.0804  -0.0014 87  ASN   A O   
1716 C  CB  . ASN   A 87  ? 0.2863 0.2486 0.1664 -0.0018 0.0323  -0.0053 87  ASN   A CB  
1717 C  CG  . ASN   A 87  ? 0.2994 0.2537 0.1638 0.0086  0.0465  -0.0008 87  ASN   A CG  
1718 O  OD1 . ASN   A 87  ? 0.3169 0.2504 0.1686 0.0197  0.0409  0.0074  87  ASN   A OD1 
1719 N  ND2 . ASN   A 87  ? 0.3032 0.2743 0.1858 0.0118  0.0470  0.0019  87  ASN   A ND2 
1726 N  N   . LEU   A 88  ? 0.2393 0.2497 0.1749 -0.0287 0.0313  0.0119  88  LEU   A N   
1727 C  CA  . LEU   A 88  ? 0.2153 0.2433 0.1930 -0.0329 0.0375  0.0273  88  LEU   A CA  
1728 C  C   . LEU   A 88  ? 0.2017 0.2443 0.1952 -0.0345 0.0338  0.0367  88  LEU   A C   
1729 O  O   . LEU   A 88  ? 0.1950 0.2451 0.2322 -0.0348 0.0380  0.0458  88  LEU   A O   
1730 C  CB  . LEU   A 88  ? 0.2158 0.2496 0.2022 -0.0407 0.0112  0.0294  88  LEU   A CB  
1731 C  CG  . LEU   A 88  ? 0.2306 0.2614 0.2279 -0.0421 0.0023  0.0354  88  LEU   A CG  
1732 C  CD1 . LEU   A 88  ? 0.2395 0.2692 0.2300 -0.0474 -0.0087 0.0230  88  LEU   A CD1 
1733 C  CD2 . LEU   A 88  ? 0.2420 0.2706 0.2594 -0.0313 0.0057  0.0281  88  LEU   A CD2 
1745 N  N   . ALA   A 89  ? 0.2024 0.2379 0.1775 -0.0273 0.0122  0.0226  89  ALA   A N   
1746 C  CA  . ALA   A 89  ? 0.2022 0.2395 0.1631 -0.0173 0.0028  0.0353  89  ALA   A CA  
1747 C  C   . ALA   A 89  ? 0.2097 0.2436 0.1682 -0.0162 -0.0072 0.0343  89  ALA   A C   
1748 O  O   . ALA   A 89  ? 0.2040 0.2387 0.2089 -0.0288 -0.0088 0.0088  89  ALA   A O   
1749 C  CB  . ALA   A 89  ? 0.2001 0.2402 0.1609 -0.0158 -0.0007 0.0233  89  ALA   A CB  
1755 N  N   . LYS   A 90  ? 0.2223 0.2609 0.1699 -0.0250 -0.0131 0.0413  90  LYS   A N   
1756 C  CA  . LYS   A 90  ? 0.2447 0.2812 0.1695 -0.0250 -0.0236 0.0483  90  LYS   A CA  
1757 C  C   . LYS   A 90  ? 0.2203 0.2548 0.1571 -0.0297 -0.0228 0.0272  90  LYS   A C   
1758 O  O   . LYS   A 90  ? 0.2193 0.2656 0.1923 -0.0394 -0.0287 0.0173  90  LYS   A O   
1759 C  CB  . LYS   A 90  ? 0.2901 0.3308 0.2277 -0.0340 -0.0240 0.0750  90  LYS   A CB  
1760 C  CG  . LYS   A 90  ? 0.3563 0.3826 0.3370 -0.0400 -0.0168 0.0880  90  LYS   A CG  
1761 C  CD  . LYS   A 90  ? 0.4239 0.4399 0.4479 -0.0465 -0.0045 0.0946  90  LYS   A CD  
1762 C  CE  . LYS   A 90  ? 0.4682 0.4822 0.5380 -0.0505 0.0045  0.0943  90  LYS   A CE  
1763 N  NZ  . LYS   A 90  ? 0.5033 0.5033 0.5930 -0.0533 0.0103  0.0944  90  LYS   A NZ  
1777 N  N   . HIS   A 91  ? 0.2055 0.2194 0.1183 -0.0254 -0.0319 0.0326  91  HIS   A N   
1778 C  CA  . HIS   A 91  ? 0.1870 0.1960 0.1421 -0.0170 -0.0277 0.0314  91  HIS   A CA  
1779 C  C   . HIS   A 91  ? 0.1640 0.1799 0.1367 -0.0161 -0.0193 0.0296  91  HIS   A C   
1780 O  O   . HIS   A 91  ? 0.1572 0.1935 0.1794 -0.0225 -0.0055 0.0331  91  HIS   A O   
1781 C  CB  . HIS   A 91  ? 0.2035 0.2209 0.1958 0.0030  -0.0389 0.0295  91  HIS   A CB  
1782 C  CG  . HIS   A 91  ? 0.2448 0.2681 0.2536 0.0149  -0.0610 0.0144  91  HIS   A CG  
1783 N  ND1 . HIS   A 91  ? 0.2574 0.2949 0.2882 0.0211  -0.0685 -0.0025 91  HIS   A ND1 
1784 C  CD2 . HIS   A 91  ? 0.2728 0.2920 0.2729 0.0219  -0.0755 0.0184  91  HIS   A CD2 
1785 C  CE1 . HIS   A 91  ? 0.2728 0.3064 0.2973 0.0264  -0.0717 0.0059  91  HIS   A CE1 
1786 N  NE2 . HIS   A 91  ? 0.2834 0.3066 0.2918 0.0309  -0.0791 0.0131  91  HIS   A NE2 
1794 N  N   . CYS   A 92  ? 0.1552 0.1673 0.1515 -0.0187 -0.0137 0.0317  92  CYS   A N   
1795 C  CA  . CYS   A 92  ? 0.1439 0.1613 0.1610 -0.0108 0.0007  0.0292  92  CYS   A CA  
1796 C  C   . CYS   A 92  ? 0.1352 0.1474 0.1642 -0.0152 -0.0005 0.0292  92  CYS   A C   
1797 O  O   . CYS   A 92  ? 0.1387 0.1612 0.1874 -0.0178 -0.0010 0.0222  92  CYS   A O   
1798 C  CB  . CYS   A 92  ? 0.1494 0.1623 0.1775 -0.0056 -0.0046 0.0139  92  CYS   A CB  
1799 S  SG  . CYS   A 92  ? 0.1469 0.1468 0.1633 -0.0126 -0.0058 0.0191  92  CYS   A SG  
1805 N  N   . LEU   A 93  ? 0.1310 0.1364 0.1801 -0.0121 0.0087  0.0244  93  LEU   A N   
1806 C  CA  . LEU   A 93  ? 0.1241 0.1386 0.1706 -0.0103 0.0026  0.0273  93  LEU   A CA  
1807 C  C   . LEU   A 93  ? 0.1257 0.1287 0.1664 -0.0036 0.0033  0.0215  93  LEU   A C   
1808 O  O   . LEU   A 93  ? 0.1208 0.1379 0.1744 -0.0063 -0.0027 0.0272  93  LEU   A O   
1809 C  CB  . LEU   A 93  ? 0.1308 0.1366 0.1964 -0.0079 -0.0057 0.0295  93  LEU   A CB  
1810 C  CG  . LEU   A 93  ? 0.1375 0.1340 0.1964 -0.0053 0.0011  0.0295  93  LEU   A CG  
1811 C  CD1 . LEU   A 93  ? 0.1450 0.1369 0.2188 -0.0110 0.0080  0.0195  93  LEU   A CD1 
1812 C  CD2 . LEU   A 93  ? 0.1534 0.1356 0.2205 -0.0053 -0.0004 0.0262  93  LEU   A CD2 
1824 N  N   . HIS   A 94  ? 0.1261 0.1233 0.1721 -0.0053 0.0069  0.0283  94  HIS   A N   
1825 C  CA  . HIS   A 94  ? 0.1236 0.1254 0.1827 -0.0056 0.0021  0.0244  94  HIS   A CA  
1826 C  C   . HIS   A 94  ? 0.1202 0.1199 0.1807 -0.0061 -0.0011 0.0193  94  HIS   A C   
1827 O  O   . HIS   A 94  ? 0.1144 0.1410 0.2229 -0.0024 0.0029  -0.0062 94  HIS   A O   
1828 C  CB  . HIS   A 94  ? 0.1189 0.1236 0.1847 -0.0080 -0.0060 0.0227  94  HIS   A CB  
1829 C  CG  . HIS   A 94  ? 0.1262 0.1238 0.1776 -0.0103 -0.0041 0.0264  94  HIS   A CG  
1830 N  ND1 . HIS   A 94  ? 0.1233 0.1192 0.1880 -0.0061 -0.0003 0.0229  94  HIS   A ND1 
1831 C  CD2 . HIS   A 94  ? 0.1416 0.1350 0.1883 -0.0104 -0.0075 0.0093  94  HIS   A CD2 
1832 C  CE1 . HIS   A 94  ? 0.1335 0.1268 0.1775 -0.0082 -0.0187 0.0175  94  HIS   A CE1 
1833 N  NE2 . HIS   A 94  ? 0.1421 0.1323 0.1731 -0.0157 -0.0079 0.0085  94  HIS   A NE2 
1841 N  N   . VAL   A 95  ? 0.1157 0.1165 0.1657 -0.0042 0.0084  0.0168  95  VAL   A N   
1842 C  CA  . VAL   A 95  ? 0.1259 0.1199 0.1590 -0.0055 0.0126  0.0179  95  VAL   A CA  
1843 C  C   . VAL   A 95  ? 0.1249 0.1296 0.1515 -0.0184 0.0084  0.0200  95  VAL   A C   
1844 O  O   . VAL   A 95  ? 0.1252 0.1328 0.1838 0.0077  0.0046  0.0165  95  VAL   A O   
1845 C  CB  . VAL   A 95  ? 0.1317 0.1277 0.1821 -0.0110 0.0075  0.0175  95  VAL   A CB  
1846 C  CG1 . VAL   A 95  ? 0.1456 0.1308 0.1959 -0.0204 -0.0003 0.0090  95  VAL   A CG1 
1847 C  CG2 . VAL   A 95  ? 0.1356 0.1327 0.1759 -0.0129 0.0063  0.0258  95  VAL   A CG2 
1857 N  N   A VAL   A 96  ? 0.1307 0.1215 0.1427 -0.0060 0.0009  0.0149  96  VAL   A N   
1858 N  N   B VAL   A 96  ? 0.1299 0.1295 0.1339 -0.0114 0.0019  0.0175  96  VAL   A N   
1859 C  CA  A VAL   A 96  ? 0.1409 0.1236 0.1668 -0.0040 0.0070  0.0202  96  VAL   A CA  
1860 C  CA  B VAL   A 96  ? 0.1348 0.1341 0.1386 -0.0066 0.0054  0.0188  96  VAL   A CA  
1861 C  C   A VAL   A 96  ? 0.1421 0.1325 0.1838 -0.0049 0.0054  0.0208  96  VAL   A C   
1862 C  C   B VAL   A 96  ? 0.1372 0.1347 0.1553 -0.0042 0.0052  0.0192  96  VAL   A C   
1863 O  O   A VAL   A 96  ? 0.1457 0.1380 0.2132 -0.0071 0.0136  0.0047  96  VAL   A O   
1864 O  O   B VAL   A 96  ? 0.1411 0.1371 0.1640 -0.0032 0.0083  0.0124  96  VAL   A O   
1865 C  CB  A VAL   A 96  ? 0.1423 0.1212 0.1717 -0.0039 0.0119  0.0156  96  VAL   A CB  
1866 C  CB  B VAL   A 96  ? 0.1336 0.1365 0.1314 -0.0030 0.0124  0.0088  96  VAL   A CB  
1867 C  CG1 A VAL   A 96  ? 0.1536 0.1342 0.1670 -0.0013 0.0059  0.0084  96  VAL   A CG1 
1868 C  CG1 B VAL   A 96  ? 0.1327 0.1478 0.1260 -0.0011 0.0118  0.0034  96  VAL   A CG1 
1869 C  CG2 A VAL   A 96  ? 0.1333 0.1235 0.1833 -0.0057 0.0147  0.0046  96  VAL   A CG2 
1870 C  CG2 B VAL   A 96  ? 0.1330 0.1347 0.1270 -0.0057 0.0136  0.0085  96  VAL   A CG2 
1889 N  N   . GLY   A 97  ? 0.1357 0.1347 0.1723 -0.0045 0.0025  0.0186  97  GLY   A N   
1890 C  CA  . GLY   A 97  ? 0.1442 0.1464 0.1663 -0.0079 -0.0043 0.0157  97  GLY   A CA  
1891 C  C   . GLY   A 97  ? 0.1469 0.1610 0.1618 -0.0138 -0.0040 0.0130  97  GLY   A C   
1892 O  O   . GLY   A 97  ? 0.1594 0.1563 0.1791 -0.0114 -0.0039 0.0162  97  GLY   A O   
1897 N  N   . PRO   A 98  ? 0.1581 0.1692 0.1583 -0.0050 -0.0081 0.0197  98  PRO   A N   
1898 C  CA  . PRO   A 98  ? 0.1650 0.1945 0.1772 -0.0169 -0.0044 0.0141  98  PRO   A CA  
1899 C  C   . PRO   A 98  ? 0.1776 0.2023 0.1802 -0.0244 -0.0087 0.0321  98  PRO   A C   
1900 O  O   . PRO   A 98  ? 0.1678 0.1783 0.2025 -0.0151 -0.0099 0.0352  98  PRO   A O   
1901 C  CB  . PRO   A 98  ? 0.1755 0.2000 0.1797 -0.0077 -0.0077 0.0038  98  PRO   A CB  
1902 C  CG  . PRO   A 98  ? 0.1792 0.1888 0.1829 -0.0059 -0.0037 0.0005  98  PRO   A CG  
1903 C  CD  . PRO   A 98  ? 0.1653 0.1680 0.1678 -0.0023 -0.0073 0.0102  98  PRO   A CD  
1911 N  N   A ASN   A 99  ? 0.1853 0.2426 0.1647 -0.0264 -0.0184 0.0540  99  ASN   A N   
1912 N  N   B ASN   A 99  ? 0.2031 0.1904 0.1681 -0.0102 -0.0185 0.0473  99  ASN   A N   
1913 C  CA  A ASN   A 99  ? 0.2072 0.2721 0.1547 -0.0367 -0.0191 0.0653  99  ASN   A CA  
1914 C  CA  B ASN   A 99  ? 0.2329 0.1765 0.1645 -0.0013 -0.0220 0.0548  99  ASN   A CA  
1915 C  C   A ASN   A 99  ? 0.2244 0.3004 0.1468 -0.0462 -0.0199 0.0653  99  ASN   A C   
1916 C  C   B ASN   A 99  ? 0.2428 0.1657 0.1673 0.0117  -0.0197 0.0450  99  ASN   A C   
1917 O  O   A ASN   A 99  ? 0.2293 0.3185 0.1569 -0.0354 -0.0232 0.0665  99  ASN   A O   
1918 O  O   B ASN   A 99  ? 0.2427 0.1444 0.1641 0.0281  -0.0267 0.0302  99  ASN   A O   
1919 C  CB  A ASN   A 99  ? 0.2061 0.2712 0.1733 -0.0360 -0.0369 0.0723  99  ASN   A CB  
1920 C  CB  B ASN   A 99  ? 0.2486 0.1772 0.1713 -0.0062 -0.0324 0.0642  99  ASN   A CB  
1921 C  CG  A ASN   A 99  ? 0.2095 0.2736 0.1868 -0.0281 -0.0403 0.0725  99  ASN   A CG  
1922 C  CG  B ASN   A 99  ? 0.2605 0.1801 0.1645 -0.0105 -0.0381 0.0816  99  ASN   A CG  
1923 O  OD1 A ASN   A 99  ? 0.2200 0.2836 0.1824 -0.0224 -0.0421 0.0637  99  ASN   A OD1 
1924 O  OD1 B ASN   A 99  ? 0.2680 0.1894 0.1540 -0.0113 -0.0396 0.0859  99  ASN   A OD1 
1925 N  ND2 A ASN   A 99  ? 0.2103 0.2594 0.1954 -0.0212 -0.0287 0.0930  99  ASN   A ND2 
1926 N  ND2 B ASN   A 99  ? 0.2637 0.1767 0.1768 -0.0066 -0.0497 0.0744  99  ASN   A ND2 
1939 N  N   A VAL   A 100 ? 0.2389 0.3097 0.1452 -0.0612 -0.0377 0.0521  100 VAL   A N   
1940 N  N   B VAL   A 100 ? 0.2521 0.1863 0.1772 0.0086  -0.0160 0.0457  100 VAL   A N   
1941 C  CA  A VAL   A 100 ? 0.2628 0.3293 0.1728 -0.0598 -0.0402 0.0515  100 VAL   A CA  
1942 C  CA  B VAL   A 100 ? 0.2636 0.2010 0.1954 0.0078  -0.0196 0.0347  100 VAL   A CA  
1943 C  C   A VAL   A 100 ? 0.2730 0.3464 0.1977 -0.0634 -0.0433 0.0800  100 VAL   A C   
1944 C  C   B VAL   A 100 ? 0.2623 0.1995 0.1895 0.0189  -0.0271 0.0244  100 VAL   A C   
1945 O  O   A VAL   A 100 ? 0.2759 0.3544 0.2132 -0.0605 -0.0293 0.0798  100 VAL   A O   
1946 O  O   B VAL   A 100 ? 0.2668 0.2010 0.1936 0.0168  -0.0335 0.0135  100 VAL   A O   
1947 C  CB  A VAL   A 100 ? 0.2793 0.3319 0.1997 -0.0540 -0.0328 0.0275  100 VAL   A CB  
1948 C  CB  B VAL   A 100 ? 0.2762 0.2218 0.2315 0.0004  -0.0159 0.0280  100 VAL   A CB  
1949 C  CG1 A VAL   A 100 ? 0.2843 0.3377 0.2252 -0.0535 -0.0234 0.0196  100 VAL   A CG1 
1950 C  CG1 B VAL   A 100 ? 0.2783 0.2257 0.2487 0.0017  -0.0145 0.0234  100 VAL   A CG1 
1951 C  CG2 A VAL   A 100 ? 0.2855 0.3321 0.1939 -0.0538 -0.0277 0.0210  100 VAL   A CG2 
1952 C  CG2 B VAL   A 100 ? 0.2806 0.2295 0.2460 -0.0017 -0.0167 0.0289  100 VAL   A CG2 
1971 N  N   A ASN   A 101 ? 0.2850 0.3539 0.2239 -0.0707 -0.0466 0.1077  101 ASN   A N   
1972 N  N   B ASN   A 101 ? 0.2616 0.2017 0.1923 0.0250  -0.0280 0.0180  101 ASN   A N   
1973 C  CA  A ASN   A 101 ? 0.3107 0.3600 0.2476 -0.0700 -0.0477 0.1288  101 ASN   A CA  
1974 C  CA  B ASN   A 101 ? 0.2696 0.2150 0.2053 0.0313  -0.0248 0.0180  101 ASN   A CA  
1975 C  C   A ASN   A 101 ? 0.3395 0.3921 0.2806 -0.0677 -0.0213 0.1539  101 ASN   A C   
1976 C  C   B ASN   A 101 ? 0.2907 0.2374 0.2231 0.0291  -0.0155 0.0256  101 ASN   A C   
1977 O  O   A ASN   A 101 ? 0.3498 0.3970 0.3085 -0.0637 -0.0247 0.1527  101 ASN   A O   
1978 O  O   B ASN   A 101 ? 0.2943 0.2374 0.2237 0.0263  -0.0150 0.0309  101 ASN   A O   
1979 C  CB  A ASN   A 101 ? 0.3086 0.3304 0.2287 -0.0713 -0.0732 0.1203  101 ASN   A CB  
1980 C  CB  B ASN   A 101 ? 0.2562 0.2107 0.2115 0.0331  -0.0268 0.0108  101 ASN   A CB  
1981 C  CG  A ASN   A 101 ? 0.3077 0.3064 0.2247 -0.0697 -0.0925 0.0898  101 ASN   A CG  
1982 C  CG  B ASN   A 101 ? 0.2499 0.2199 0.2260 0.0275  -0.0322 0.0057  101 ASN   A CG  
1983 O  OD1 A ASN   A 101 ? 0.3023 0.3072 0.2466 -0.0539 -0.0936 0.0589  101 ASN   A OD1 
1984 O  OD1 B ASN   A 101 ? 0.2592 0.2332 0.2456 0.0170  -0.0338 0.0075  101 ASN   A OD1 
1985 N  ND2 A ASN   A 101 ? 0.3141 0.2938 0.2349 -0.0767 -0.0889 0.0839  101 ASN   A ND2 
1986 N  ND2 B ASN   A 101 ? 0.2435 0.2162 0.2331 0.0332  -0.0264 -0.0031 101 ASN   A ND2 
1999 N  N   A LYS   A 102 ? 0.3495 0.4192 0.3020 -0.0730 0.0008  0.1577  102 LYS   A N   
2000 N  N   B LYS   A 102 ? 0.3061 0.2571 0.2540 0.0295  -0.0032 0.0256  102 LYS   A N   
2001 C  CA  A LYS   A 102 ? 0.3656 0.4440 0.3112 -0.0714 0.0042  0.1462  102 LYS   A CA  
2002 C  CA  B LYS   A 102 ? 0.3245 0.2835 0.2792 0.0231  0.0079  0.0192  102 LYS   A CA  
2003 C  C   A LYS   A 102 ? 0.3728 0.4620 0.2967 -0.0576 0.0016  0.1365  102 LYS   A C   
2004 C  C   B LYS   A 102 ? 0.3283 0.2941 0.2753 0.0261  0.0122  0.0227  102 LYS   A C   
2005 O  O   A LYS   A 102 ? 0.3785 0.4733 0.2997 -0.0510 -0.0034 0.1336  102 LYS   A O   
2006 O  O   B LYS   A 102 ? 0.3320 0.2945 0.2750 0.0271  0.0171  0.0270  102 LYS   A O   
2007 C  CB  A LYS   A 102 ? 0.3770 0.4513 0.3481 -0.0803 0.0029  0.1289  102 LYS   A CB  
2008 C  CB  B LYS   A 102 ? 0.3377 0.2983 0.3146 0.0156  0.0093  0.0096  102 LYS   A CB  
2009 C  CG  A LYS   A 102 ? 0.3849 0.4550 0.3788 -0.0892 0.0019  0.1063  102 LYS   A CG  
2010 C  CG  B LYS   A 102 ? 0.3492 0.3125 0.3504 0.0087  0.0104  0.0003  102 LYS   A CG  
2011 C  CD  A LYS   A 102 ? 0.3940 0.4611 0.4112 -0.0928 -0.0009 0.0811  102 LYS   A CD  
2012 C  CD  B LYS   A 102 ? 0.3593 0.3261 0.3854 0.0016  0.0118  -0.0033 102 LYS   A CD  
2013 C  CE  A LYS   A 102 ? 0.4017 0.4650 0.4398 -0.0954 -0.0046 0.0632  102 LYS   A CE  
2014 C  CE  B LYS   A 102 ? 0.3663 0.3357 0.4117 -0.0030 0.0135  -0.0042 102 LYS   A CE  
2015 N  NZ  A LYS   A 102 ? 0.4059 0.4668 0.4538 -0.0984 -0.0034 0.0524  102 LYS   A NZ  
2016 N  NZ  B LYS   A 102 ? 0.3703 0.3415 0.4252 -0.0047 0.0133  -0.0059 102 LYS   A NZ  
2043 N  N   A GLY   A 103 ? 0.3713 0.4689 0.2971 -0.0474 -0.0033 0.1131  103 GLY   A N   
2044 N  N   B GLY   A 103 ? 0.3272 0.3058 0.2779 0.0312  0.0069  0.0164  103 GLY   A N   
2045 C  CA  A GLY   A 103 ? 0.3695 0.4699 0.2949 -0.0394 -0.0053 0.0938  103 GLY   A CA  
2046 C  CA  B GLY   A 103 ? 0.3244 0.3124 0.2840 0.0370  0.0012  0.0155  103 GLY   A CA  
2047 C  C   A GLY   A 103 ? 0.3615 0.4690 0.2877 -0.0342 -0.0036 0.0705  103 GLY   A C   
2048 C  C   B GLY   A 103 ? 0.3206 0.3171 0.2844 0.0415  -0.0040 0.0138  103 GLY   A C   
2049 O  O   A GLY   A 103 ? 0.3711 0.4765 0.3083 -0.0267 -0.0072 0.0632  103 GLY   A O   
2050 O  O   B GLY   A 103 ? 0.3236 0.3216 0.2976 0.0448  -0.0064 0.0123  103 GLY   A O   
2057 N  N   A GLU   A 104 ? 0.3381 0.4544 0.2414 -0.0406 0.0020  0.0572  104 GLU   A N   
2058 N  N   B GLU   A 104 ? 0.3110 0.3134 0.2609 0.0420  -0.0098 0.0236  104 GLU   A N   
2059 C  CA  A GLU   A 104 ? 0.3116 0.4345 0.2085 -0.0512 0.0059  0.0394  104 GLU   A CA  
2060 C  CA  B GLU   A 104 ? 0.3034 0.3109 0.2427 0.0369  -0.0125 0.0233  104 GLU   A CA  
2061 C  C   A GLU   A 104 ? 0.3153 0.4359 0.2057 -0.0493 0.0082  0.0080  104 GLU   A C   
2062 C  C   B GLU   A 104 ? 0.2964 0.3071 0.2329 0.0392  -0.0110 0.0139  104 GLU   A C   
2063 O  O   A GLU   A 104 ? 0.3125 0.4343 0.2002 -0.0533 0.0084  0.0004  104 GLU   A O   
2064 O  O   B GLU   A 104 ? 0.2912 0.3002 0.2220 0.0411  -0.0131 0.0129  104 GLU   A O   
2065 C  CB  A GLU   A 104 ? 0.2765 0.4126 0.1825 -0.0622 0.0081  0.0569  104 GLU   A CB  
2066 C  CB  B GLU   A 104 ? 0.3046 0.3140 0.2413 0.0303  -0.0138 0.0304  104 GLU   A CB  
2067 C  CG  A GLU   A 104 ? 0.2499 0.3946 0.1916 -0.0671 -0.0038 0.0683  104 GLU   A CG  
2068 C  CG  B GLU   A 104 ? 0.3081 0.3208 0.2478 0.0236  -0.0154 0.0338  104 GLU   A CG  
2069 C  CD  A GLU   A 104 ? 0.2211 0.3765 0.1867 -0.0707 -0.0101 0.0800  104 GLU   A CD  
2070 C  CD  B GLU   A 104 ? 0.3106 0.3273 0.2500 0.0196  -0.0188 0.0378  104 GLU   A CD  
2071 O  OE1 A GLU   A 104 ? 0.2046 0.3664 0.1656 -0.0713 -0.0153 0.0811  104 GLU   A OE1 
2072 O  OE1 B GLU   A 104 ? 0.3119 0.3305 0.2578 0.0213  -0.0174 0.0351  104 GLU   A OE1 
2073 O  OE2 A GLU   A 104 ? 0.2186 0.3736 0.2146 -0.0713 -0.0051 0.0883  104 GLU   A OE2 
2074 O  OE2 B GLU   A 104 ? 0.3129 0.3303 0.2496 0.0148  -0.0231 0.0433  104 GLU   A OE2 
2087 N  N   A ASP   A 105 ? 0.3192 0.4388 0.2273 -0.0438 0.0136  -0.0149 105 ASP   A N   
2088 N  N   B ASP   A 105 ? 0.2985 0.3106 0.2521 0.0383  -0.0083 0.0047  105 ASP   A N   
2089 C  CA  A ASP   A 105 ? 0.3189 0.4395 0.2642 -0.0334 0.0183  -0.0485 105 ASP   A CA  
2090 C  CA  B ASP   A 105 ? 0.3006 0.3140 0.2823 0.0377  -0.0040 -0.0129 105 ASP   A CA  
2091 C  C   A ASP   A 105 ? 0.2881 0.4161 0.2234 -0.0414 0.0081  -0.0635 105 ASP   A C   
2092 C  C   B ASP   A 105 ? 0.3059 0.3158 0.2742 0.0212  -0.0081 -0.0118 105 ASP   A C   
2093 O  O   A ASP   A 105 ? 0.2765 0.4099 0.1736 -0.0428 0.0096  -0.0736 105 ASP   A O   
2094 O  O   B ASP   A 105 ? 0.3019 0.3163 0.2581 0.0195  -0.0050 -0.0087 105 ASP   A O   
2095 C  CB  A ASP   A 105 ? 0.3445 0.4595 0.3415 -0.0193 0.0263  -0.0617 105 ASP   A CB  
2096 C  CB  B ASP   A 105 ? 0.2983 0.3156 0.3221 0.0500  0.0063  -0.0319 105 ASP   A CB  
2097 C  CG  A ASP   A 105 ? 0.3649 0.4757 0.4111 -0.0083 0.0299  -0.0721 105 ASP   A CG  
2098 C  CG  B ASP   A 105 ? 0.2975 0.3149 0.3581 0.0597  0.0147  -0.0498 105 ASP   A CG  
2099 O  OD1 A ASP   A 105 ? 0.3698 0.4817 0.4295 -0.0095 0.0288  -0.0786 105 ASP   A OD1 
2100 O  OD1 B ASP   A 105 ? 0.2971 0.3120 0.3643 0.0588  0.0153  -0.0580 105 ASP   A OD1 
2101 O  OD2 A ASP   A 105 ? 0.3761 0.4820 0.4456 -0.0030 0.0345  -0.0726 105 ASP   A OD2 
2102 O  OD2 B ASP   A 105 ? 0.2957 0.3147 0.3735 0.0674  0.0233  -0.0534 105 ASP   A OD2 
2111 N  N   A ILE   A 106 ? 0.2647 0.3964 0.2349 -0.0467 -0.0057 -0.0709 106 ILE   A N   
2112 N  N   B ILE   A 106 ? 0.3128 0.3195 0.2853 0.0089  -0.0156 -0.0100 106 ILE   A N   
2113 C  CA  A ILE   A 106 ? 0.2376 0.3774 0.2387 -0.0621 -0.0223 -0.0779 106 ILE   A CA  
2114 C  CA  B ILE   A 106 ? 0.3189 0.3216 0.2959 -0.0060 -0.0229 -0.0120 106 ILE   A CA  
2115 C  C   A ILE   A 106 ? 0.2225 0.3522 0.2475 -0.0848 -0.0158 -0.0918 106 ILE   A C   
2116 C  C   B ILE   A 106 ? 0.3265 0.3176 0.2970 -0.0103 -0.0172 -0.0039 106 ILE   A C   
2117 O  O   A ILE   A 106 ? 0.2016 0.3409 0.2509 -0.0861 0.0085  -0.0908 106 ILE   A O   
2118 O  O   B ILE   A 106 ? 0.3272 0.3177 0.2945 -0.0109 -0.0150 -0.0022 106 ILE   A O   
2119 C  CB  A ILE   A 106 ? 0.2393 0.3874 0.2616 -0.0470 -0.0364 -0.0543 106 ILE   A CB  
2120 C  CB  B ILE   A 106 ? 0.3189 0.3290 0.3069 -0.0151 -0.0346 -0.0217 106 ILE   A CB  
2121 C  CG1 A ILE   A 106 ? 0.2308 0.3904 0.2837 -0.0328 -0.0415 -0.0344 106 ILE   A CG1 
2122 C  CG1 B ILE   A 106 ? 0.3167 0.3300 0.3112 -0.0187 -0.0402 -0.0305 106 ILE   A CG1 
2123 C  CG2 A ILE   A 106 ? 0.2483 0.3917 0.2692 -0.0426 -0.0391 -0.0522 106 ILE   A CG2 
2124 C  CG2 B ILE   A 106 ? 0.3213 0.3325 0.3095 -0.0181 -0.0365 -0.0232 106 ILE   A CG2 
2125 C  CD1 A ILE   A 106 ? 0.2287 0.3897 0.2929 -0.0213 -0.0404 -0.0256 106 ILE   A CD1 
2126 C  CD1 B ILE   A 106 ? 0.3147 0.3304 0.3168 -0.0213 -0.0430 -0.0351 106 ILE   A CD1 
2149 N  N   A GLN   A 107 ? 0.2447 0.3409 0.2856 -0.0844 -0.0035 -0.0991 107 GLN   A N   
2150 N  N   B GLN   A 107 ? 0.3321 0.3116 0.3083 -0.0117 -0.0127 0.0024  107 GLN   A N   
2151 C  CA  A GLN   A 107 ? 0.2735 0.3323 0.3566 -0.0706 0.0105  -0.0918 107 GLN   A CA  
2152 C  CA  B GLN   A 107 ? 0.3377 0.3084 0.3338 -0.0139 -0.0089 0.0069  107 GLN   A CA  
2153 C  C   A GLN   A 107 ? 0.2362 0.2822 0.3316 -0.0611 0.0310  -0.0748 107 GLN   A C   
2154 C  C   B GLN   A 107 ? 0.3080 0.2724 0.2987 -0.0153 0.0047  0.0094  107 GLN   A C   
2155 O  O   A GLN   A 107 ? 0.2448 0.2805 0.3726 -0.0587 0.0453  -0.0732 107 GLN   A O   
2156 O  O   B GLN   A 107 ? 0.3114 0.2714 0.3053 -0.0202 0.0013  0.0094  107 GLN   A O   
2157 C  CB  A GLN   A 107 ? 0.3318 0.3713 0.4546 -0.0719 0.0012  -0.0953 107 GLN   A CB  
2158 C  CB  B GLN   A 107 ? 0.3687 0.3405 0.3945 -0.0168 -0.0203 0.0071  107 GLN   A CB  
2159 C  CG  A GLN   A 107 ? 0.3882 0.4091 0.5627 -0.0682 -0.0048 -0.0894 107 GLN   A CG  
2160 C  CG  B GLN   A 107 ? 0.3953 0.3694 0.4569 -0.0181 -0.0317 0.0110  107 GLN   A CG  
2161 C  CD  A GLN   A 107 ? 0.4323 0.4362 0.6573 -0.0645 -0.0093 -0.0798 107 GLN   A CD  
2162 C  CD  B GLN   A 107 ? 0.4156 0.3930 0.5110 -0.0188 -0.0406 0.0148  107 GLN   A CD  
2163 O  OE1 A GLN   A 107 ? 0.4455 0.4447 0.6923 -0.0632 -0.0109 -0.0759 107 GLN   A OE1 
2164 O  OE1 B GLN   A 107 ? 0.4227 0.4006 0.5291 -0.0187 -0.0441 0.0173  107 GLN   A OE1 
2165 N  NE2 A GLN   A 107 ? 0.4474 0.4455 0.6907 -0.0642 -0.0126 -0.0784 107 GLN   A NE2 
2166 N  NE2 B GLN   A 107 ? 0.4217 0.3997 0.5297 -0.0189 -0.0449 0.0156  107 GLN   A NE2 
2183 N  N   A LEU   A 108 ? 0.1976 0.2344 0.2763 -0.0541 0.0282  -0.0651 108 LEU   A N   
2184 N  N   B LEU   A 108 ? 0.2740 0.2397 0.2645 -0.0136 0.0160  0.0089  108 LEU   A N   
2185 C  CA  A LEU   A 108 ? 0.1834 0.1962 0.2459 -0.0272 0.0240  -0.0302 108 LEU   A CA  
2186 C  CA  B LEU   A 108 ? 0.2403 0.2095 0.2380 -0.0084 0.0227  0.0092  108 LEU   A CA  
2187 C  C   A LEU   A 108 ? 0.1712 0.1569 0.2295 -0.0128 0.0231  -0.0008 108 LEU   A C   
2188 C  C   B LEU   A 108 ? 0.2041 0.1762 0.2238 -0.0001 0.0244  0.0124  108 LEU   A C   
2189 O  O   A LEU   A 108 ? 0.1647 0.1481 0.2496 -0.0071 0.0263  0.0040  108 LEU   A O   
2190 O  O   B LEU   A 108 ? 0.2037 0.1753 0.2232 0.0087  0.0279  0.0105  108 LEU   A O   
2191 C  CB  A LEU   A 108 ? 0.1913 0.2058 0.2468 -0.0316 0.0292  -0.0336 108 LEU   A CB  
2192 C  CB  B LEU   A 108 ? 0.2439 0.2170 0.2347 -0.0142 0.0268  0.0034  108 LEU   A CB  
2193 C  CG  A LEU   A 108 ? 0.2071 0.2249 0.2699 -0.0230 0.0410  -0.0345 108 LEU   A CG  
2194 C  CG  B LEU   A 108 ? 0.2494 0.2266 0.2434 -0.0139 0.0315  -0.0019 108 LEU   A CG  
2195 C  CD1 A LEU   A 108 ? 0.2209 0.2291 0.2803 -0.0298 0.0437  -0.0397 108 LEU   A CD1 
2196 C  CD1 B LEU   A 108 ? 0.2536 0.2288 0.2475 -0.0165 0.0339  -0.0040 108 LEU   A CD1 
2197 C  CD2 A LEU   A 108 ? 0.2119 0.2429 0.2971 -0.0109 0.0469  -0.0279 108 LEU   A CD2 
2198 C  CD2 B LEU   A 108 ? 0.2514 0.2346 0.2560 -0.0107 0.0330  -0.0005 108 LEU   A CD2 
2221 N  N   . LEU   A 109 ? 0.1691 0.1543 0.2324 0.0028  0.0266  0.0159  109 LEU   A N   
2222 C  CA  . LEU   A 109 ? 0.1620 0.1440 0.2290 0.0041  0.0094  0.0196  109 LEU   A CA  
2223 C  C   . LEU   A 109 ? 0.1443 0.1385 0.2295 -0.0030 0.0071  0.0108  109 LEU   A C   
2224 O  O   . LEU   A 109 ? 0.1470 0.1294 0.2438 -0.0055 -0.0015 0.0118  109 LEU   A O   
2225 C  CB  . LEU   A 109 ? 0.1603 0.1534 0.2405 0.0066  0.0039  0.0296  109 LEU   A CB  
2226 C  CG  . LEU   A 109 ? 0.1561 0.1651 0.2521 0.0068  0.0132  0.0334  109 LEU   A CG  
2227 C  CD1 . LEU   A 109 ? 0.1606 0.1579 0.2664 -0.0051 0.0216  0.0184  109 LEU   A CD1 
2228 C  CD2 . LEU   A 109 ? 0.1544 0.1805 0.2671 0.0049  0.0077  0.0397  109 LEU   A CD2 
2241 N  N   . LYS   A 110 ? 0.1475 0.1379 0.2245 -0.0049 -0.0019 0.0100  110 LYS   A N   
2242 C  CA  . LYS   A 110 ? 0.1416 0.1322 0.2386 -0.0109 -0.0047 0.0155  110 LYS   A CA  
2243 C  C   . LYS   A 110 ? 0.1396 0.1273 0.2215 -0.0114 -0.0027 -0.0009 110 LYS   A C   
2244 O  O   . LYS   A 110 ? 0.1374 0.1291 0.2388 -0.0061 0.0052  -0.0041 110 LYS   A O   
2245 C  CB  . LYS   A 110 ? 0.1487 0.1367 0.2677 -0.0105 -0.0049 0.0009  110 LYS   A CB  
2246 C  CG  . LYS   A 110 ? 0.1505 0.1341 0.2763 -0.0074 -0.0083 0.0004  110 LYS   A CG  
2247 C  CD  . LYS   A 110 ? 0.1561 0.1427 0.2894 -0.0075 -0.0038 -0.0054 110 LYS   A CD  
2248 C  CE  . LYS   A 110 ? 0.1678 0.1468 0.2997 -0.0096 0.0081  -0.0087 110 LYS   A CE  
2249 N  NZ  . LYS   A 110 ? 0.1664 0.1483 0.3057 -0.0123 0.0153  0.0006  110 LYS   A NZ  
2263 N  N   . SER   A 111 ? 0.1408 0.1312 0.2295 -0.0061 -0.0036 0.0073  111 SER   A N   
2264 C  CA  . SER   A 111 ? 0.1363 0.1367 0.2291 -0.0036 0.0074  0.0063  111 SER   A CA  
2265 C  C   . SER   A 111 ? 0.1314 0.1293 0.2311 -0.0077 0.0076  0.0142  111 SER   A C   
2266 O  O   . SER   A 111 ? 0.1456 0.1214 0.2498 -0.0073 0.0120  0.0122  111 SER   A O   
2267 C  CB  . SER   A 111 ? 0.1567 0.1612 0.2307 -0.0033 0.0129  -0.0094 111 SER   A CB  
2268 O  OG  . SER   A 111 ? 0.2042 0.1766 0.2357 0.0037  0.0157  -0.0093 111 SER   A OG  
2274 N  N   . ALA   A 112 ? 0.1370 0.1242 0.2246 -0.0038 0.0109  0.0111  112 ALA   A N   
2275 C  CA  . ALA   A 112 ? 0.1418 0.1204 0.2191 -0.0049 0.0163  0.0029  112 ALA   A CA  
2276 C  C   . ALA   A 112 ? 0.1305 0.1198 0.2240 -0.0030 0.0084  0.0040  112 ALA   A C   
2277 O  O   . ALA   A 112 ? 0.1366 0.1210 0.2317 -0.0112 0.0151  0.0176  112 ALA   A O   
2278 C  CB  . ALA   A 112 ? 0.1508 0.1277 0.2195 -0.0025 0.0146  0.0091  112 ALA   A CB  
2284 N  N   . TYR   A 113 ? 0.1213 0.1249 0.2322 -0.0041 0.0126  0.0149  113 TYR   A N   
2285 C  CA  . TYR   A 113 ? 0.1243 0.1232 0.2234 -0.0050 0.0124  0.0209  113 TYR   A CA  
2286 C  C   . TYR   A 113 ? 0.1179 0.1222 0.2180 -0.0115 0.0100  0.0097  113 TYR   A C   
2287 O  O   . TYR   A 113 ? 0.1258 0.1278 0.2270 -0.0056 0.0204  0.0101  113 TYR   A O   
2288 C  CB  . TYR   A 113 ? 0.1216 0.1319 0.2331 -0.0026 -0.0001 0.0188  113 TYR   A CB  
2289 C  CG  . TYR   A 113 ? 0.1292 0.1349 0.2241 -0.0075 0.0153  0.0237  113 TYR   A CG  
2290 C  CD1 . TYR   A 113 ? 0.1317 0.1421 0.2204 0.0027  0.0116  0.0271  113 TYR   A CD1 
2291 C  CD2 . TYR   A 113 ? 0.1344 0.1465 0.2207 -0.0115 0.0100  0.0305  113 TYR   A CD2 
2292 C  CE1 . TYR   A 113 ? 0.1366 0.1564 0.2205 -0.0030 0.0083  0.0290  113 TYR   A CE1 
2293 C  CE2 . TYR   A 113 ? 0.1346 0.1531 0.2150 -0.0081 0.0080  0.0376  113 TYR   A CE2 
2294 C  CZ  . TYR   A 113 ? 0.1285 0.1500 0.2189 -0.0019 0.0137  0.0338  113 TYR   A CZ  
2295 O  OH  . TYR   A 113 ? 0.1325 0.1562 0.2341 0.0091  0.0064  0.0371  113 TYR   A OH  
2305 N  N   . GLU   A 114 ? 0.1218 0.1186 0.2234 -0.0038 0.0146  0.0196  114 GLU   A N   
2306 C  CA  . GLU   A 114 ? 0.1283 0.1178 0.2368 -0.0019 0.0075  0.0222  114 GLU   A CA  
2307 C  C   . GLU   A 114 ? 0.1221 0.1249 0.2234 -0.0044 0.0170  0.0181  114 GLU   A C   
2308 O  O   . GLU   A 114 ? 0.1393 0.1253 0.2265 0.0008  0.0088  0.0178  114 GLU   A O   
2309 C  CB  . GLU   A 114 ? 0.1294 0.1215 0.2391 -0.0070 0.0051  0.0227  114 GLU   A CB  
2310 C  CG  . GLU   A 114 ? 0.1315 0.1232 0.2612 -0.0009 0.0097  0.0068  114 GLU   A CG  
2311 C  CD  . GLU   A 114 ? 0.1459 0.1207 0.2715 0.0005  0.0010  0.0121  114 GLU   A CD  
2312 O  OE1 . GLU   A 114 ? 0.1451 0.1289 0.2760 -0.0113 0.0140  0.0006  114 GLU   A OE1 
2313 O  OE2 . GLU   A 114 ? 0.1667 0.1336 0.2764 -0.0075 0.0110  -0.0021 114 GLU   A OE2 
2320 N  N   . ASN   A 115 ? 0.1268 0.1266 0.2143 -0.0070 0.0166  0.0172  115 ASN   A N   
2321 C  CA  . ASN   A 115 ? 0.1286 0.1315 0.2286 -0.0096 0.0159  0.0202  115 ASN   A CA  
2322 C  C   . ASN   A 115 ? 0.1289 0.1259 0.2344 -0.0033 0.0169  0.0242  115 ASN   A C   
2323 O  O   . ASN   A 115 ? 0.1303 0.1378 0.2504 -0.0074 0.0211  0.0249  115 ASN   A O   
2324 C  CB  . ASN   A 115 ? 0.1388 0.1381 0.2193 -0.0120 0.0147  0.0132  115 ASN   A CB  
2325 C  CG  . ASN   A 115 ? 0.1382 0.1550 0.2161 -0.0178 0.0261  0.0098  115 ASN   A CG  
2326 O  OD1 . ASN   A 115 ? 0.1421 0.2470 0.2403 -0.0149 0.0295  0.0230  115 ASN   A OD1 
2327 N  ND2 . ASN   A 115 ? 0.1420 0.1368 0.2188 -0.0175 0.0246  0.0232  115 ASN   A ND2 
2334 N  N   . PHE   A 116 ? 0.1254 0.1271 0.2331 -0.0028 0.0141  0.0314  116 PHE   A N   
2335 C  CA  . PHE   A 116 ? 0.1278 0.1316 0.2267 -0.0023 0.0212  0.0234  116 PHE   A CA  
2336 C  C   . PHE   A 116 ? 0.1261 0.1399 0.2281 -0.0067 0.0160  0.0267  116 PHE   A C   
2337 O  O   . PHE   A 116 ? 0.1304 0.1498 0.2334 0.0026  0.0170  0.0382  116 PHE   A O   
2338 C  CB  . PHE   A 116 ? 0.1266 0.1273 0.2332 -0.0071 0.0243  0.0217  116 PHE   A CB  
2339 C  CG  . PHE   A 116 ? 0.1311 0.1290 0.2255 -0.0072 0.0145  0.0183  116 PHE   A CG  
2340 C  CD1 . PHE   A 116 ? 0.1329 0.1286 0.2270 -0.0062 0.0128  0.0179  116 PHE   A CD1 
2341 C  CD2 . PHE   A 116 ? 0.1332 0.1379 0.2207 -0.0094 0.0199  0.0222  116 PHE   A CD2 
2342 C  CE1 . PHE   A 116 ? 0.1357 0.1266 0.2335 -0.0186 0.0090  0.0138  116 PHE   A CE1 
2343 C  CE2 . PHE   A 116 ? 0.1319 0.1318 0.2267 -0.0075 0.0165  0.0142  116 PHE   A CE2 
2344 C  CZ  . PHE   A 116 ? 0.1317 0.1217 0.2276 -0.0052 0.0061  0.0139  116 PHE   A CZ  
2354 N  N   . ASN   A 117 ? 0.1278 0.1312 0.2381 -0.0086 0.0140  0.0282  117 ASN   A N   
2355 C  CA  . ASN   A 117 ? 0.1349 0.1325 0.2411 -0.0011 0.0153  0.0331  117 ASN   A CA  
2356 C  C   . ASN   A 117 ? 0.1391 0.1424 0.2552 -0.0044 0.0167  0.0333  117 ASN   A C   
2357 O  O   . ASN   A 117 ? 0.1394 0.1483 0.2743 -0.0064 0.0048  0.0392  117 ASN   A O   
2358 C  CB  . ASN   A 117 ? 0.1285 0.1360 0.2495 -0.0046 0.0101  0.0363  117 ASN   A CB  
2359 C  CG  . ASN   A 117 ? 0.1253 0.1390 0.2506 -0.0037 0.0159  0.0358  117 ASN   A CG  
2360 O  OD1 . ASN   A 117 ? 0.1304 0.1586 0.2635 -0.0143 0.0188  0.0280  117 ASN   A OD1 
2361 N  ND2 . ASN   A 117 ? 0.1247 0.1341 0.2400 -0.0016 0.0043  0.0327  117 ASN   A ND2 
2368 N  N   . GLN   A 118 ? 0.1272 0.1400 0.2554 -0.0046 0.0089  0.0329  118 GLN   A N   
2369 C  CA  . GLN   A 118 ? 0.1374 0.1531 0.2602 -0.0092 0.0068  0.0250  118 GLN   A CA  
2370 C  C   . GLN   A 118 ? 0.1446 0.1672 0.2507 -0.0162 0.0049  0.0397  118 GLN   A C   
2371 O  O   . GLN   A 118 ? 0.1431 0.1925 0.2750 -0.0046 -0.0038 0.0113  118 GLN   A O   
2372 C  CB  . GLN   A 118 ? 0.1354 0.1542 0.2681 -0.0058 0.0168  0.0228  118 GLN   A CB  
2373 C  CG  . GLN   A 118 ? 0.1360 0.1555 0.2682 -0.0037 0.0122  0.0309  118 GLN   A CG  
2374 C  CD  . GLN   A 118 ? 0.1290 0.1552 0.2820 -0.0046 0.0146  0.0342  118 GLN   A CD  
2375 O  OE1 . GLN   A 118 ? 0.1351 0.1699 0.2953 0.0087  0.0014  0.0246  118 GLN   A OE1 
2376 N  NE2 . GLN   A 118 ? 0.1330 0.1566 0.2844 0.0008  0.0107  0.0324  118 GLN   A NE2 
2385 N  N   . HIS   A 119 ? 0.1444 0.1587 0.2342 -0.0065 0.0055  0.0483  119 HIS   A N   
2386 C  CA  . HIS   A 119 ? 0.1531 0.1658 0.2367 -0.0091 0.0090  0.0512  119 HIS   A CA  
2387 C  C   . HIS   A 119 ? 0.1657 0.1798 0.2239 -0.0084 0.0100  0.0587  119 HIS   A C   
2388 O  O   . HIS   A 119 ? 0.1626 0.1791 0.2307 -0.0252 0.0044  0.0490  119 HIS   A O   
2389 C  CB  . HIS   A 119 ? 0.1540 0.1592 0.2531 -0.0060 0.0248  0.0473  119 HIS   A CB  
2390 C  CG  . HIS   A 119 ? 0.1558 0.1657 0.2857 0.0006  0.0188  0.0496  119 HIS   A CG  
2391 N  ND1 . HIS   A 119 ? 0.1686 0.1810 0.3311 -0.0101 0.0169  0.0323  119 HIS   A ND1 
2392 C  CD2 . HIS   A 119 ? 0.1686 0.1741 0.2963 0.0100  0.0388  0.0659  119 HIS   A CD2 
2393 C  CE1 . HIS   A 119 ? 0.1607 0.1790 0.3298 -0.0115 0.0312  0.0520  119 HIS   A CE1 
2394 N  NE2 . HIS   A 119 ? 0.1781 0.1776 0.3228 0.0033  0.0455  0.0713  119 HIS   A NE2 
2402 N  N   A GLU   A 120 ? 0.1703 0.2016 0.2256 -0.0051 0.0013  0.0819  120 GLU   A N   
2403 N  N   B GLU   A 120 ? 0.1818 0.2091 0.2329 -0.0080 0.0091  0.0653  120 GLU   A N   
2404 C  CA  A GLU   A 120 ? 0.1864 0.2238 0.2508 -0.0018 -0.0023 0.1148  120 GLU   A CA  
2405 C  CA  B GLU   A 120 ? 0.2019 0.2360 0.2583 -0.0099 0.0075  0.0762  120 GLU   A CA  
2406 C  C   A GLU   A 120 ? 0.1716 0.2152 0.2314 -0.0163 0.0015  0.1086  120 GLU   A C   
2407 C  C   B GLU   A 120 ? 0.1863 0.2291 0.2307 -0.0156 0.0064  0.0812  120 GLU   A C   
2408 O  O   A GLU   A 120 ? 0.1662 0.2041 0.2503 -0.0165 -0.0065 0.1106  120 GLU   A O   
2409 O  O   B GLU   A 120 ? 0.1881 0.2329 0.2348 -0.0146 0.0019  0.0744  120 GLU   A O   
2410 C  CB  A GLU   A 120 ? 0.2385 0.2615 0.3069 0.0168  0.0024  0.1438  120 GLU   A CB  
2411 C  CB  B GLU   A 120 ? 0.2435 0.2699 0.3208 -0.0053 0.0100  0.0785  120 GLU   A CB  
2412 C  CG  A GLU   A 120 ? 0.3009 0.3032 0.3997 0.0335  0.0032  0.1375  120 GLU   A CG  
2413 C  CG  B GLU   A 120 ? 0.2841 0.3011 0.3908 0.0011  0.0093  0.0717  120 GLU   A CG  
2414 C  CD  A GLU   A 120 ? 0.3534 0.3382 0.4860 0.0476  0.0124  0.1246  120 GLU   A CD  
2415 C  CD  B GLU   A 120 ? 0.3182 0.3279 0.4528 0.0076  0.0099  0.0624  120 GLU   A CD  
2416 O  OE1 A GLU   A 120 ? 0.3717 0.3573 0.5102 0.0481  0.0160  0.1171  120 GLU   A OE1 
2417 O  OE1 B GLU   A 120 ? 0.3300 0.3401 0.4700 0.0089  0.0114  0.0579  120 GLU   A OE1 
2418 O  OE2 A GLU   A 120 ? 0.3727 0.3489 0.5255 0.0487  0.0145  0.1196  120 GLU   A OE2 
2419 O  OE2 B GLU   A 120 ? 0.3303 0.3366 0.4791 0.0067  0.0097  0.0602  120 GLU   A OE2 
2432 N  N   . VAL   A 121 ? 0.1724 0.2170 0.2176 -0.0172 0.0068  0.0882  121 VAL   A N   
2433 C  CA  . VAL   A 121 ? 0.1799 0.2265 0.2048 -0.0156 0.0211  0.0769  121 VAL   A CA  
2434 C  C   . VAL   A 121 ? 0.1632 0.2067 0.2026 -0.0223 0.0144  0.0576  121 VAL   A C   
2435 O  O   . VAL   A 121 ? 0.1670 0.2071 0.2134 -0.0316 -0.0047 0.0500  121 VAL   A O   
2436 C  CB  . VAL   A 121 ? 0.2202 0.2651 0.2302 -0.0036 0.0261  0.0763  121 VAL   A CB  
2437 C  CG1 . VAL   A 121 ? 0.2211 0.2811 0.2235 0.0003  0.0308  0.0782  121 VAL   A CG1 
2438 C  CG2 . VAL   A 121 ? 0.2423 0.2804 0.2631 -0.0137 0.0240  0.0637  121 VAL   A CG2 
2449 N  N   . LEU   A 122 ? 0.1503 0.1735 0.1963 -0.0174 0.0094  0.0502  122 LEU   A N   
2450 C  CA  . LEU   A 122 ? 0.1547 0.1622 0.1959 -0.0213 0.0218  0.0449  122 LEU   A CA  
2451 C  C   . LEU   A 122 ? 0.1521 0.1630 0.2030 -0.0279 0.0102  0.0379  122 LEU   A C   
2452 O  O   . LEU   A 122 ? 0.1521 0.1694 0.2378 -0.0277 0.0119  0.0468  122 LEU   A O   
2453 C  CB  . LEU   A 122 ? 0.1697 0.1650 0.2236 -0.0150 0.0135  0.0539  122 LEU   A CB  
2454 C  CG  . LEU   A 122 ? 0.1719 0.1663 0.2240 -0.0108 0.0296  0.0422  122 LEU   A CG  
2455 C  CD1 . LEU   A 122 ? 0.1865 0.1633 0.2351 -0.0122 0.0309  0.0425  122 LEU   A CD1 
2456 C  CD2 . LEU   A 122 ? 0.1700 0.1587 0.2215 -0.0051 0.0386  0.0344  122 LEU   A CD2 
2468 N  N   A LEU   A 123 ? 0.1445 0.1556 0.1942 -0.0217 0.0087  0.0364  123 LEU   A N   
2469 N  N   B LEU   A 123 ? 0.1541 0.1614 0.1904 -0.0222 0.0072  0.0350  123 LEU   A N   
2470 C  CA  A LEU   A 123 ? 0.1390 0.1532 0.1841 -0.0222 0.0131  0.0397  123 LEU   A CA  
2471 C  CA  B LEU   A 123 ? 0.1553 0.1625 0.1830 -0.0179 0.0064  0.0327  123 LEU   A CA  
2472 C  C   A LEU   A 123 ? 0.1369 0.1458 0.1827 -0.0137 0.0114  0.0426  123 LEU   A C   
2473 C  C   B LEU   A 123 ? 0.1529 0.1520 0.1741 -0.0137 0.0103  0.0309  123 LEU   A C   
2474 O  O   A LEU   A 123 ? 0.1302 0.1434 0.1924 -0.0159 0.0072  0.0377  123 LEU   A O   
2475 O  O   B LEU   A 123 ? 0.1496 0.1485 0.1793 -0.0119 0.0137  0.0352  123 LEU   A O   
2476 C  CB  A LEU   A 123 ? 0.1520 0.1633 0.1877 -0.0238 0.0234  0.0404  123 LEU   A CB  
2477 C  CB  B LEU   A 123 ? 0.1641 0.1748 0.1904 -0.0161 0.0050  0.0305  123 LEU   A CB  
2478 C  CG  A LEU   A 123 ? 0.1585 0.1788 0.1973 -0.0229 0.0312  0.0234  123 LEU   A CG  
2479 C  CG  B LEU   A 123 ? 0.1696 0.1878 0.1940 -0.0141 0.0055  0.0259  123 LEU   A CG  
2480 C  CD1 A LEU   A 123 ? 0.1643 0.1920 0.2052 -0.0153 0.0306  0.0143  123 LEU   A CD1 
2481 C  CD1 B LEU   A 123 ? 0.1710 0.1937 0.1972 -0.0103 0.0040  0.0206  123 LEU   A CD1 
2482 C  CD2 A LEU   A 123 ? 0.1755 0.1829 0.2095 -0.0273 0.0215  0.0180  123 LEU   A CD2 
2483 C  CD2 B LEU   A 123 ? 0.1771 0.1938 0.2025 -0.0164 -0.0006 0.0247  123 LEU   A CD2 
2506 N  N   A ALA   A 124 ? 0.1364 0.1380 0.1785 -0.0092 0.0103  0.0353  124 ALA   A N   
2507 N  N   B ALA   A 124 ? 0.1502 0.1414 0.1636 -0.0132 0.0081  0.0176  124 ALA   A N   
2508 C  CA  A ALA   A 124 ? 0.1242 0.1295 0.1946 -0.0066 0.0039  0.0289  124 ALA   A CA  
2509 C  CA  B ALA   A 124 ? 0.1473 0.1370 0.1701 -0.0181 0.0101  0.0110  124 ALA   A CA  
2510 C  C   A ALA   A 124 ? 0.1204 0.1289 0.2012 -0.0107 0.0104  0.0305  124 ALA   A C   
2511 C  C   B ALA   A 124 ? 0.1376 0.1272 0.1685 -0.0118 0.0206  0.0128  124 ALA   A C   
2512 O  O   A ALA   A 124 ? 0.1212 0.1469 0.2180 -0.0091 0.0162  0.0394  124 ALA   A O   
2513 O  O   B ALA   A 124 ? 0.1356 0.1270 0.1817 -0.0018 0.0236  0.0214  124 ALA   A O   
2514 C  CB  A ALA   A 124 ? 0.1165 0.1287 0.2049 0.0004  -0.0013 0.0317  124 ALA   A CB  
2515 C  CB  B ALA   A 124 ? 0.1579 0.1379 0.1721 -0.0217 0.0112  0.0139  124 ALA   A CB  
2526 N  N   A PRO   A 125 ? 0.1218 0.1225 0.1972 -0.0057 0.0155  0.0377  125 PRO   A N   
2527 N  N   B PRO   A 125 ? 0.1289 0.1203 0.1624 -0.0028 0.0136  0.0093  125 PRO   A N   
2528 C  CA  A PRO   A 125 ? 0.1315 0.1304 0.2018 -0.0036 0.0059  0.0270  125 PRO   A CA  
2529 C  CA  B PRO   A 125 ? 0.1306 0.1253 0.1685 0.0003  0.0063  0.0142  125 PRO   A CA  
2530 C  C   A PRO   A 125 ? 0.1218 0.1533 0.1876 -0.0116 0.0105  0.0258  125 PRO   A C   
2531 C  C   B PRO   A 125 ? 0.1219 0.1321 0.1738 -0.0054 0.0049  0.0173  125 PRO   A C   
2532 O  O   A PRO   A 125 ? 0.1322 0.1521 0.1851 -0.0063 0.0138  0.0242  125 PRO   A O   
2533 O  O   B PRO   A 125 ? 0.1254 0.1274 0.1704 -0.0048 0.0004  0.0129  125 PRO   A O   
2534 C  CB  A PRO   A 125 ? 0.1528 0.1370 0.2029 -0.0117 0.0092  0.0393  125 PRO   A CB  
2535 C  CB  B PRO   A 125 ? 0.1429 0.1277 0.1618 -0.0038 0.0021  0.0091  125 PRO   A CB  
2536 C  CG  A PRO   A 125 ? 0.1532 0.1453 0.2200 -0.0141 0.0123  0.0386  125 PRO   A CG  
2537 C  CG  B PRO   A 125 ? 0.1398 0.1231 0.1619 -0.0132 0.0085  0.0079  125 PRO   A CG  
2538 C  CD  A PRO   A 125 ? 0.1321 0.1432 0.2077 -0.0053 0.0210  0.0405  125 PRO   A CD  
2539 C  CD  B PRO   A 125 ? 0.1240 0.1128 0.1461 -0.0138 0.0196  0.0093  125 PRO   A CD  
2554 N  N   A LEU   A 126 ? 0.1237 0.1669 0.2015 -0.0059 0.0068  0.0279  126 LEU   A N   
2555 N  N   B LEU   A 126 ? 0.1166 0.1428 0.1860 0.0018  0.0113  0.0149  126 LEU   A N   
2556 C  CA  A LEU   A 126 ? 0.1268 0.1592 0.2154 -0.0067 -0.0002 0.0381  126 LEU   A CA  
2557 C  CA  B LEU   A 126 ? 0.1188 0.1514 0.1856 -0.0031 0.0051  0.0227  126 LEU   A CA  
2558 C  C   A LEU   A 126 ? 0.1333 0.1532 0.2086 0.0001  -0.0009 0.0335  126 LEU   A C   
2559 C  C   B LEU   A 126 ? 0.1193 0.1511 0.1727 -0.0051 -0.0023 0.0257  126 LEU   A C   
2560 O  O   A LEU   A 126 ? 0.1378 0.1451 0.2336 0.0067  0.0065  0.0382  126 LEU   A O   
2561 O  O   B LEU   A 126 ? 0.1223 0.1498 0.1696 -0.0080 -0.0081 0.0287  126 LEU   A O   
2562 C  CB  A LEU   A 126 ? 0.1357 0.1632 0.2361 -0.0058 -0.0062 0.0375  126 LEU   A CB  
2563 C  CB  B LEU   A 126 ? 0.1226 0.1643 0.1905 -0.0107 0.0098  0.0126  126 LEU   A CB  
2564 C  CG  A LEU   A 126 ? 0.1397 0.1709 0.2523 -0.0002 0.0029  0.0286  126 LEU   A CG  
2565 C  CG  B LEU   A 126 ? 0.1136 0.1657 0.1958 -0.0052 0.0171  0.0074  126 LEU   A CG  
2566 C  CD1 A LEU   A 126 ? 0.1430 0.1785 0.2740 0.0087  0.0099  0.0251  126 LEU   A CD1 
2567 C  CD1 B LEU   A 126 ? 0.1183 0.1705 0.2069 -0.0064 0.0108  -0.0001 126 LEU   A CD1 
2568 C  CD2 A LEU   A 126 ? 0.1496 0.1637 0.2400 -0.0078 0.0120  0.0281  126 LEU   A CD2 
2569 C  CD2 B LEU   A 126 ? 0.1080 0.1634 0.1977 -0.0056 0.0172  0.0096  126 LEU   A CD2 
2592 N  N   A LEU   A 127 ? 0.1398 0.1537 0.1895 -0.0002 0.0088  0.0334  127 LEU   A N   
2593 N  N   B LEU   A 127 ? 0.1162 0.1504 0.1559 -0.0015 -0.0022 0.0338  127 LEU   A N   
2594 C  CA  A LEU   A 127 ? 0.1439 0.1519 0.1860 -0.0040 0.0019  0.0294  127 LEU   A CA  
2595 C  CA  B LEU   A 127 ? 0.1153 0.1545 0.1525 -0.0023 -0.0054 0.0293  127 LEU   A CA  
2596 C  C   A LEU   A 127 ? 0.1473 0.1408 0.1803 -0.0050 -0.0009 0.0283  127 LEU   A C   
2597 C  C   B LEU   A 127 ? 0.1213 0.1450 0.1657 -0.0024 -0.0076 0.0183  127 LEU   A C   
2598 O  O   A LEU   A 127 ? 0.1510 0.1431 0.1933 -0.0156 0.0034  0.0233  127 LEU   A O   
2599 O  O   B LEU   A 127 ? 0.1255 0.1429 0.1773 -0.0105 -0.0078 0.0246  127 LEU   A O   
2600 C  CB  A LEU   A 127 ? 0.1463 0.1491 0.1913 0.0042  0.0055  0.0239  127 LEU   A CB  
2601 C  CB  B LEU   A 127 ? 0.1111 0.1704 0.1458 -0.0003 -0.0079 0.0320  127 LEU   A CB  
2602 C  CG  A LEU   A 127 ? 0.1480 0.1423 0.2026 0.0049  -0.0075 0.0250  127 LEU   A CG  
2603 C  CG  B LEU   A 127 ? 0.1204 0.1864 0.1518 0.0067  -0.0086 0.0377  127 LEU   A CG  
2604 C  CD1 A LEU   A 127 ? 0.1493 0.1412 0.2143 -0.0047 -0.0046 0.0225  127 LEU   A CD1 
2605 C  CD1 B LEU   A 127 ? 0.1253 0.1913 0.1571 0.0139  -0.0034 0.0423  127 LEU   A CD1 
2606 C  CD2 A LEU   A 127 ? 0.1518 0.1395 0.2211 0.0139  -0.0189 0.0223  127 LEU   A CD2 
2607 C  CD2 B LEU   A 127 ? 0.1267 0.1947 0.1576 0.0017  -0.0136 0.0279  127 LEU   A CD2 
2630 N  N   A SER   A 128 ? 0.1478 0.1427 0.1722 -0.0125 -0.0035 0.0278  128 SER   A N   
2631 N  N   B SER   A 128 ? 0.1254 0.1411 0.1635 -0.0062 -0.0083 0.0062  128 SER   A N   
2632 C  CA  A SER   A 128 ? 0.1554 0.1419 0.1601 -0.0065 -0.0044 0.0188  128 SER   A CA  
2633 C  CA  B SER   A 128 ? 0.1301 0.1376 0.1501 -0.0093 -0.0041 0.0026  128 SER   A CA  
2634 C  C   A SER   A 128 ? 0.1614 0.1473 0.1518 -0.0003 0.0019  0.0331  128 SER   A C   
2635 C  C   B SER   A 128 ? 0.1321 0.1414 0.1489 -0.0077 -0.0138 0.0062  128 SER   A C   
2636 O  O   A SER   A 128 ? 0.1782 0.1587 0.1562 0.0022  0.0033  0.0224  128 SER   A O   
2637 O  O   B SER   A 128 ? 0.1373 0.1425 0.1488 -0.0057 -0.0036 0.0081  128 SER   A O   
2638 C  CB  A SER   A 128 ? 0.1531 0.1427 0.1633 -0.0090 -0.0098 0.0164  128 SER   A CB  
2639 C  CB  B SER   A 128 ? 0.1385 0.1389 0.1490 -0.0105 -0.0031 0.0129  128 SER   A CB  
2640 O  OG  A SER   A 128 ? 0.1504 0.1479 0.1814 -0.0055 -0.0076 0.0058  128 SER   A OG  
2641 O  OG  B SER   A 128 ? 0.1370 0.1417 0.1518 -0.0051 0.0091  0.0214  128 SER   A OG  
2652 N  N   A ALA   A 129 ? 0.1519 0.1589 0.1667 -0.0034 -0.0005 0.0365  129 ALA   A N   
2653 N  N   B ALA   A 129 ? 0.1291 0.1470 0.1531 -0.0007 -0.0153 0.0041  129 ALA   A N   
2654 C  CA  A ALA   A 129 ? 0.1463 0.1584 0.1859 0.0007  0.0039  0.0259  129 ALA   A CA  
2655 C  CA  B ALA   A 129 ? 0.1316 0.1494 0.1649 -0.0001 -0.0088 0.0003  129 ALA   A CA  
2656 C  C   A ALA   A 129 ? 0.1472 0.1479 0.2030 -0.0013 -0.0044 0.0152  129 ALA   A C   
2657 C  C   B ALA   A 129 ? 0.1436 0.1595 0.1803 0.0050  -0.0069 0.0102  129 ALA   A C   
2658 O  O   A ALA   A 129 ? 0.1495 0.1473 0.2155 -0.0023 -0.0042 0.0260  129 ALA   A O   
2659 O  O   B ALA   A 129 ? 0.1437 0.1628 0.1791 0.0006  -0.0087 0.0090  129 ALA   A O   
2660 C  CB  A ALA   A 129 ? 0.1524 0.1700 0.1905 0.0131  0.0017  0.0285  129 ALA   A CB  
2661 C  CB  B ALA   A 129 ? 0.1280 0.1489 0.1603 -0.0009 -0.0077 -0.0008 129 ALA   A CB  
2672 N  N   A GLY   A 130 ? 0.1574 0.1479 0.2300 -0.0012 -0.0054 0.0139  130 GLY   A N   
2673 N  N   B GLY   A 130 ? 0.1553 0.1609 0.1919 0.0142  0.0023  0.0245  130 GLY   A N   
2674 C  CA  A GLY   A 130 ? 0.1720 0.1517 0.2222 0.0026  -0.0153 0.0218  130 GLY   A CA  
2675 C  CA  B GLY   A 130 ? 0.1694 0.1618 0.1839 0.0165  0.0063  0.0275  130 GLY   A CA  
2676 C  C   A GLY   A 130 ? 0.1761 0.1554 0.2085 0.0059  -0.0255 0.0101  130 GLY   A C   
2677 C  C   B GLY   A 130 ? 0.1759 0.1621 0.1688 0.0126  0.0149  0.0145  130 GLY   A C   
2678 O  O   A GLY   A 130 ? 0.1745 0.1575 0.2237 0.0090  -0.0326 -0.0034 130 GLY   A O   
2679 O  O   B GLY   A 130 ? 0.1776 0.1605 0.1693 0.0082  0.0179  0.0047  130 GLY   A O   
2686 N  N   A ILE   A 131 ? 0.1788 0.1532 0.1937 -0.0092 -0.0198 0.0182  131 ILE   A N   
2687 N  N   B ILE   A 131 ? 0.1793 0.1627 0.1627 0.0093  0.0128  0.0071  131 ILE   A N   
2688 C  CA  A ILE   A 131 ? 0.1923 0.1460 0.1721 -0.0097 -0.0274 0.0151  131 ILE   A CA  
2689 C  CA  B ILE   A 131 ? 0.1910 0.1597 0.1609 0.0034  0.0075  -0.0021 131 ILE   A CA  
2690 C  C   A ILE   A 131 ? 0.1804 0.1504 0.1728 -0.0035 -0.0179 0.0122  131 ILE   A C   
2691 C  C   B ILE   A 131 ? 0.1889 0.1552 0.1550 0.0038  0.0080  -0.0048 131 ILE   A C   
2692 O  O   A ILE   A 131 ? 0.1858 0.1592 0.1720 0.0043  -0.0147 0.0163  131 ILE   A O   
2693 O  O   B ILE   A 131 ? 0.1843 0.1432 0.1522 0.0085  0.0013  -0.0074 131 ILE   A O   
2694 C  CB  A ILE   A 131 ? 0.2243 0.1583 0.1610 -0.0238 -0.0295 0.0079  131 ILE   A CB  
2695 C  CB  B ILE   A 131 ? 0.2022 0.1672 0.1721 -0.0038 0.0093  -0.0065 131 ILE   A CB  
2696 C  CG1 A ILE   A 131 ? 0.2339 0.1929 0.1669 -0.0399 -0.0266 0.0148  131 ILE   A CG1 
2697 C  CG1 B ILE   A 131 ? 0.2101 0.1835 0.1748 -0.0092 0.0032  -0.0072 131 ILE   A CG1 
2698 C  CG2 A ILE   A 131 ? 0.2422 0.1483 0.1669 -0.0159 -0.0200 0.0088  131 ILE   A CG2 
2699 C  CG2 B ILE   A 131 ? 0.2069 0.1634 0.1827 0.0009  0.0122  -0.0122 131 ILE   A CG2 
2700 C  CD1 A ILE   A 131 ? 0.2440 0.2027 0.1823 -0.0490 -0.0293 0.0042  131 ILE   A CD1 
2701 C  CD1 B ILE   A 131 ? 0.2156 0.1925 0.1791 -0.0142 -0.0003 -0.0029 131 ILE   A CD1 
2724 N  N   A PHE   A 132 ? 0.1676 0.1395 0.1757 0.0066  -0.0185 0.0220  132 PHE   A N   
2725 N  N   B PHE   A 132 ? 0.1874 0.1565 0.1535 0.0058  0.0136  0.0005  132 PHE   A N   
2726 C  CA  A PHE   A 132 ? 0.1712 0.1413 0.1867 -0.0005 -0.0220 0.0113  132 PHE   A CA  
2727 C  CA  B PHE   A 132 ? 0.1937 0.1635 0.1506 0.0047  0.0081  -0.0061 132 PHE   A CA  
2728 C  C   A PHE   A 132 ? 0.1808 0.1523 0.1994 -0.0059 -0.0282 0.0209  132 PHE   A C   
2729 C  C   B PHE   A 132 ? 0.2026 0.1710 0.1578 0.0058  -0.0035 -0.0027 132 PHE   A C   
2730 O  O   A PHE   A 132 ? 0.1981 0.1554 0.2171 -0.0022 -0.0323 0.0070  132 PHE   A O   
2731 O  O   B PHE   A 132 ? 0.2143 0.1744 0.1678 0.0117  -0.0042 -0.0029 132 PHE   A O   
2732 C  CB  A PHE   A 132 ? 0.1639 0.1374 0.1740 -0.0059 -0.0220 0.0226  132 PHE   A CB  
2733 C  CB  B PHE   A 132 ? 0.1895 0.1604 0.1434 0.0060  0.0075  -0.0184 132 PHE   A CB  
2734 C  CG  A PHE   A 132 ? 0.1654 0.1442 0.1616 0.0047  -0.0225 0.0205  132 PHE   A CG  
2735 C  CG  B PHE   A 132 ? 0.1846 0.1634 0.1414 0.0106  0.0052  -0.0204 132 PHE   A CG  
2736 C  CD1 A PHE   A 132 ? 0.1620 0.1628 0.1690 0.0133  -0.0176 0.0082  132 PHE   A CD1 
2737 C  CD1 B PHE   A 132 ? 0.1822 0.1716 0.1502 0.0145  0.0096  -0.0235 132 PHE   A CD1 
2738 C  CD2 A PHE   A 132 ? 0.1703 0.1557 0.1738 0.0123  -0.0294 0.0146  132 PHE   A CD2 
2739 C  CD2 B PHE   A 132 ? 0.1836 0.1627 0.1461 0.0150  0.0053  -0.0298 132 PHE   A CD2 
2740 C  CE1 A PHE   A 132 ? 0.1617 0.1744 0.1724 0.0091  -0.0263 0.0019  132 PHE   A CE1 
2741 C  CE1 B PHE   A 132 ? 0.1823 0.1774 0.1588 0.0144  0.0083  -0.0265 132 PHE   A CE1 
2742 C  CE2 A PHE   A 132 ? 0.1637 0.1693 0.1906 0.0131  -0.0306 0.0103  132 PHE   A CE2 
2743 C  CE2 B PHE   A 132 ? 0.1791 0.1717 0.1602 0.0214  0.0088  -0.0299 132 PHE   A CE2 
2744 C  CZ  A PHE   A 132 ? 0.1572 0.1678 0.1803 0.0045  -0.0456 0.0081  132 PHE   A CZ  
2745 C  CZ  B PHE   A 132 ? 0.1775 0.1727 0.1609 0.0163  0.0099  -0.0269 132 PHE   A CZ  
2764 N  N   A GLY   A 133 ? 0.1839 0.1663 0.1987 -0.0060 -0.0479 0.0195  133 GLY   A N   
2765 N  N   B GLY   A 133 ? 0.2012 0.1760 0.1572 0.0028  -0.0187 0.0002  133 GLY   A N   
2766 C  CA  A GLY   A 133 ? 0.1943 0.1749 0.2006 -0.0089 -0.0496 0.0069  133 GLY   A CA  
2767 C  CA  B GLY   A 133 ? 0.2029 0.1784 0.1657 0.0030  -0.0231 -0.0051 133 GLY   A CA  
2768 C  C   A GLY   A 133 ? 0.1894 0.1813 0.2091 -0.0077 -0.0499 0.0025  133 GLY   A C   
2769 C  C   B GLY   A 133 ? 0.1977 0.1793 0.1720 0.0068  -0.0210 -0.0142 133 GLY   A C   
2770 O  O   A GLY   A 133 ? 0.1983 0.1879 0.2094 -0.0094 -0.0473 -0.0146 133 GLY   A O   
2771 O  O   B GLY   A 133 ? 0.1977 0.1798 0.1677 0.0159  -0.0204 -0.0326 133 GLY   A O   
2778 N  N   A ALA   A 134 ? 0.1792 0.1689 0.2095 -0.0092 -0.0430 0.0029  134 ALA   A N   
2779 N  N   B ALA   A 134 ? 0.1941 0.1798 0.1804 0.0010  -0.0197 -0.0090 134 ALA   A N   
2780 C  CA  A ALA   A 134 ? 0.1734 0.1723 0.2288 -0.0090 -0.0359 0.0072  134 ALA   A CA  
2781 C  CA  B ALA   A 134 ? 0.1887 0.1791 0.1890 0.0003  -0.0182 -0.0032 134 ALA   A CA  
2782 C  C   A ALA   A 134 ? 0.1755 0.1843 0.2261 -0.0107 -0.0282 0.0062  134 ALA   A C   
2783 C  C   B ALA   A 134 ? 0.1873 0.1764 0.1880 0.0000  -0.0143 -0.0029 134 ALA   A C   
2784 O  O   A ALA   A 134 ? 0.1955 0.1928 0.2369 -0.0150 -0.0170 0.0136  134 ALA   A O   
2785 O  O   B ALA   A 134 ? 0.1927 0.1793 0.1967 0.0001  -0.0030 -0.0060 134 ALA   A O   
2786 C  CB  A ALA   A 134 ? 0.1771 0.1707 0.2588 -0.0040 -0.0427 0.0081  134 ALA   A CB  
2787 C  CB  B ALA   A 134 ? 0.1880 0.1799 0.2024 0.0014  -0.0234 -0.0016 134 ALA   A CB  
2798 N  N   A ASP   A 135 ? 0.1752 0.1846 0.2371 -0.0076 -0.0288 0.0110  135 ASP   A N   
2799 N  N   B ASP   A 135 ? 0.1878 0.1753 0.1915 -0.0016 -0.0172 0.0062  135 ASP   A N   
2800 C  CA  A ASP   A 135 ? 0.1780 0.1943 0.2490 -0.0159 -0.0334 0.0193  135 ASP   A CA  
2801 C  CA  B ASP   A 135 ? 0.1847 0.1743 0.2062 -0.0038 -0.0169 0.0091  135 ASP   A CA  
2802 C  C   A ASP   A 135 ? 0.1655 0.1874 0.2504 -0.0114 -0.0279 0.0337  135 ASP   A C   
2803 C  C   B ASP   A 135 ? 0.1771 0.1715 0.2041 0.0027  -0.0078 0.0174  135 ASP   A C   
2804 O  O   A ASP   A 135 ? 0.1544 0.1750 0.2623 -0.0078 -0.0203 0.0388  135 ASP   A O   
2805 O  O   B ASP   A 135 ? 0.1728 0.1660 0.2116 0.0027  -0.0058 0.0240  135 ASP   A O   
2806 C  CB  A ASP   A 135 ? 0.2026 0.2185 0.2855 -0.0298 -0.0412 0.0132  135 ASP   A CB  
2807 C  CB  B ASP   A 135 ? 0.1898 0.1824 0.2204 -0.0087 -0.0269 0.0013  135 ASP   A CB  
2808 C  CG  A ASP   A 135 ? 0.2219 0.2390 0.3250 -0.0457 -0.0409 0.0115  135 ASP   A CG  
2809 C  CG  B ASP   A 135 ? 0.1935 0.1948 0.2378 -0.0114 -0.0334 0.0012  135 ASP   A CG  
2810 O  OD1 A ASP   A 135 ? 0.2181 0.2471 0.3204 -0.0540 -0.0464 0.0206  135 ASP   A OD1 
2811 O  OD1 B ASP   A 135 ? 0.1927 0.1930 0.2464 -0.0036 -0.0351 0.0015  135 ASP   A OD1 
2812 O  OD2 A ASP   A 135 ? 0.2481 0.2555 0.3711 -0.0445 -0.0238 0.0058  135 ASP   A OD2 
2813 O  OD2 B ASP   A 135 ? 0.1974 0.2042 0.2524 -0.0185 -0.0389 0.0016  135 ASP   A OD2 
2822 N  N   A PRO   A 136 ? 0.1573 0.1906 0.2537 -0.0023 -0.0191 0.0439  136 PRO   A N   
2823 N  N   B PRO   A 136 ? 0.1775 0.1726 0.2012 0.0109  0.0015  0.0234  136 PRO   A N   
2824 C  CA  A PRO   A 136 ? 0.1542 0.1954 0.2703 -0.0021 -0.0109 0.0354  136 PRO   A CA  
2825 C  CA  B PRO   A 136 ? 0.1766 0.1832 0.2071 0.0085  0.0043  0.0222  136 PRO   A CA  
2826 C  C   A PRO   A 136 ? 0.1315 0.1923 0.2748 -0.0047 -0.0078 0.0391  136 PRO   A C   
2827 C  C   B PRO   A 136 ? 0.1705 0.1888 0.2080 0.0097  0.0041  0.0328  136 PRO   A C   
2828 O  O   A PRO   A 136 ? 0.1245 0.1961 0.2762 -0.0062 -0.0079 0.0398  136 PRO   A O   
2829 O  O   B PRO   A 136 ? 0.1673 0.1854 0.2016 0.0138  0.0111  0.0321  136 PRO   A O   
2830 C  CB  A PRO   A 136 ? 0.1765 0.1980 0.2812 0.0077  -0.0022 0.0408  136 PRO   A CB  
2831 C  CB  B PRO   A 136 ? 0.1860 0.1818 0.2127 0.0121  0.0074  0.0208  136 PRO   A CB  
2832 C  CG  A PRO   A 136 ? 0.1910 0.2042 0.2950 0.0168  -0.0007 0.0360  136 PRO   A CG  
2833 C  CG  B PRO   A 136 ? 0.1922 0.1813 0.2203 0.0176  0.0115  0.0211  136 PRO   A CG  
2834 C  CD  A PRO   A 136 ? 0.1769 0.1972 0.2735 0.0151  -0.0067 0.0481  136 PRO   A CD  
2835 C  CD  B PRO   A 136 ? 0.1858 0.1739 0.2086 0.0180  0.0125  0.0282  136 PRO   A CD  
2850 N  N   A ILE   A 137 ? 0.1299 0.1893 0.2859 -0.0056 -0.0113 0.0451  137 ILE   A N   
2851 N  N   B ILE   A 137 ? 0.1719 0.1928 0.2225 0.0052  -0.0055 0.0376  137 ILE   A N   
2852 C  CA  A ILE   A 137 ? 0.1318 0.1962 0.2856 -0.0202 -0.0226 0.0526  137 ILE   A CA  
2853 C  CA  B ILE   A 137 ? 0.1748 0.2033 0.2313 -0.0008 -0.0117 0.0378  137 ILE   A CA  
2854 C  C   A ILE   A 137 ? 0.1383 0.1917 0.2756 -0.0218 -0.0182 0.0496  137 ILE   A C   
2855 C  C   B ILE   A 137 ? 0.1715 0.2065 0.2321 -0.0034 -0.0066 0.0321  137 ILE   A C   
2856 O  O   A ILE   A 137 ? 0.1423 0.1844 0.2912 -0.0270 -0.0144 0.0356  137 ILE   A O   
2857 O  O   B ILE   A 137 ? 0.1725 0.2114 0.2393 -0.0024 -0.0061 0.0356  137 ILE   A O   
2858 C  CB  A ILE   A 137 ? 0.1459 0.2170 0.3093 -0.0256 -0.0365 0.0569  137 ILE   A CB  
2859 C  CB  B ILE   A 137 ? 0.1833 0.2087 0.2478 -0.0051 -0.0225 0.0403  137 ILE   A CB  
2860 C  CG1 A ILE   A 137 ? 0.1616 0.2439 0.3305 -0.0141 -0.0391 0.0623  137 ILE   A CG1 
2861 C  CG1 B ILE   A 137 ? 0.1915 0.2167 0.2575 0.0037  -0.0292 0.0496  137 ILE   A CG1 
2862 C  CG2 A ILE   A 137 ? 0.1597 0.2209 0.3103 -0.0331 -0.0486 0.0450  137 ILE   A CG2 
2863 C  CG2 B ILE   A 137 ? 0.1878 0.2071 0.2492 -0.0103 -0.0265 0.0369  137 ILE   A CG2 
2864 C  CD1 A ILE   A 137 ? 0.1879 0.2587 0.3495 -0.0077 -0.0271 0.0614  137 ILE   A CD1 
2865 C  CD1 B ILE   A 137 ? 0.1996 0.2189 0.2662 0.0071  -0.0286 0.0589  137 ILE   A CD1 
2888 N  N   A HIS   A 138 ? 0.1396 0.2073 0.2647 -0.0182 -0.0118 0.0394  138 HIS   A N   
2889 N  N   B HIS   A 138 ? 0.1668 0.2082 0.2305 -0.0075 -0.0003 0.0185  138 HIS   A N   
2890 C  CA  A HIS   A 138 ? 0.1485 0.2098 0.2533 -0.0135 -0.0092 0.0347  138 HIS   A CA  
2891 C  CA  B HIS   A 138 ? 0.1621 0.2014 0.2256 -0.0087 0.0017  0.0141  138 HIS   A CA  
2892 C  C   A HIS   A 138 ? 0.1435 0.1947 0.2488 -0.0091 -0.0127 0.0357  138 HIS   A C   
2893 C  C   B HIS   A 138 ? 0.1526 0.1921 0.2302 -0.0074 0.0001  0.0259  138 HIS   A C   
2894 O  O   A HIS   A 138 ? 0.1514 0.1928 0.2483 -0.0106 -0.0077 0.0335  138 HIS   A O   
2895 O  O   B HIS   A 138 ? 0.1586 0.1936 0.2281 -0.0077 0.0059  0.0257  138 HIS   A O   
2896 C  CB  A HIS   A 138 ? 0.1728 0.2238 0.2500 -0.0144 -0.0237 0.0278  138 HIS   A CB  
2897 C  CB  B HIS   A 138 ? 0.1665 0.2057 0.2215 -0.0097 -0.0020 -0.0063 138 HIS   A CB  
2898 C  CG  A HIS   A 138 ? 0.1955 0.2252 0.2588 -0.0235 -0.0209 0.0230  138 HIS   A CG  
2899 C  CG  B HIS   A 138 ? 0.1721 0.2079 0.2273 -0.0175 -0.0031 -0.0229 138 HIS   A CG  
2900 N  ND1 A HIS   A 138 ? 0.2099 0.2317 0.2735 -0.0293 -0.0141 0.0115  138 HIS   A ND1 
2901 N  ND1 B HIS   A 138 ? 0.1783 0.2111 0.2352 -0.0189 0.0007  -0.0299 138 HIS   A ND1 
2902 C  CD2 A HIS   A 138 ? 0.2014 0.2301 0.2657 -0.0197 -0.0197 0.0290  138 HIS   A CD2 
2903 C  CD2 B HIS   A 138 ? 0.1717 0.2081 0.2303 -0.0172 -0.0060 -0.0247 138 HIS   A CD2 
2904 C  CE1 A HIS   A 138 ? 0.2162 0.2371 0.2782 -0.0237 -0.0110 0.0186  138 HIS   A CE1 
2905 C  CE1 B HIS   A 138 ? 0.1783 0.2098 0.2356 -0.0183 0.0013  -0.0272 138 HIS   A CE1 
2906 N  NE2 A HIS   A 138 ? 0.2114 0.2356 0.2701 -0.0197 -0.0106 0.0246  138 HIS   A NE2 
2907 N  NE2 B HIS   A 138 ? 0.1751 0.2094 0.2326 -0.0165 -0.0002 -0.0275 138 HIS   A NE2 
2922 N  N   . SER   A 139 ? 0.1390 0.1812 0.2426 -0.0076 -0.0013 0.0379  139 SER   A N   
2923 C  CA  . SER   A 139 ? 0.1332 0.1741 0.2538 -0.0121 -0.0041 0.0456  139 SER   A CA  
2924 C  C   . SER   A 139 ? 0.1292 0.1607 0.2572 -0.0133 -0.0046 0.0353  139 SER   A C   
2925 O  O   . SER   A 139 ? 0.1255 0.1567 0.2721 -0.0126 -0.0000 0.0308  139 SER   A O   
2926 C  CB  . SER   A 139 ? 0.1313 0.1737 0.2435 -0.0133 -0.0024 0.0457  139 SER   A CB  
2927 O  OG  . SER   A 139 ? 0.1380 0.1738 0.2523 -0.0182 -0.0164 0.0512  139 SER   A OG  
2934 N  N   . LEU   A 140 ? 0.1244 0.1717 0.2476 -0.0107 0.0028  0.0469  140 LEU   A N   
2935 C  CA  . LEU   A 140 ? 0.1270 0.1662 0.2474 -0.0086 0.0007  0.0424  140 LEU   A CA  
2936 C  C   . LEU   A 140 ? 0.1204 0.1739 0.2529 -0.0103 0.0007  0.0393  140 LEU   A C   
2937 O  O   . LEU   A 140 ? 0.1258 0.1687 0.2725 -0.0084 0.0057  0.0389  140 LEU   A O   
2938 C  CB  . LEU   A 140 ? 0.1244 0.1762 0.2441 -0.0063 0.0065  0.0419  140 LEU   A CB  
2939 C  CG  . LEU   A 140 ? 0.1302 0.1917 0.2567 -0.0177 0.0061  0.0544  140 LEU   A CG  
2940 C  CD1 . LEU   A 140 ? 0.1323 0.1916 0.2713 -0.0131 0.0035  0.0530  140 LEU   A CD1 
2941 C  CD2 . LEU   A 140 ? 0.1345 0.2047 0.2600 -0.0149 0.0125  0.0562  140 LEU   A CD2 
2953 N  N   . ARG   A 141 ? 0.1315 0.1769 0.2510 -0.0095 -0.0083 0.0316  141 ARG   A N   
2954 C  CA  . ARG   A 141 ? 0.1485 0.1897 0.2668 -0.0200 -0.0113 0.0202  141 ARG   A CA  
2955 C  C   . ARG   A 141 ? 0.1413 0.1708 0.2639 -0.0165 -0.0027 0.0152  141 ARG   A C   
2956 O  O   . ARG   A 141 ? 0.1380 0.1660 0.2768 -0.0143 0.0054  0.0205  141 ARG   A O   
2957 C  CB  . ARG   A 141 ? 0.1671 0.2226 0.2815 -0.0201 -0.0234 -0.0019 141 ARG   A CB  
2958 C  CG  . ARG   A 141 ? 0.2086 0.2621 0.3083 -0.0325 -0.0127 -0.0121 141 ARG   A CG  
2959 C  CD  . ARG   A 141 ? 0.2435 0.2975 0.3413 -0.0477 -0.0076 -0.0121 141 ARG   A CD  
2960 N  NE  . ARG   A 141 ? 0.2380 0.3284 0.3614 -0.0554 -0.0198 -0.0111 141 ARG   A NE  
2961 C  CZ  . ARG   A 141 ? 0.2393 0.3490 0.3710 -0.0756 -0.0160 -0.0073 141 ARG   A CZ  
2962 N  NH1 . ARG   A 141 ? 0.2255 0.3511 0.3655 -0.0892 0.0024  -0.0198 141 ARG   A NH1 
2963 N  NH2 . ARG   A 141 ? 0.2479 0.3635 0.3867 -0.0676 -0.0307 -0.0031 141 ARG   A NH2 
2977 N  N   . VAL   A 142 ? 0.1321 0.1657 0.2574 -0.0134 -0.0033 0.0168  142 VAL   A N   
2978 C  CA  . VAL   A 142 ? 0.1403 0.1637 0.2552 -0.0134 0.0150  0.0179  142 VAL   A CA  
2979 C  C   . VAL   A 142 ? 0.1307 0.1537 0.2451 -0.0100 0.0011  0.0191  142 VAL   A C   
2980 O  O   . VAL   A 142 ? 0.1313 0.1534 0.2615 -0.0005 0.0052  0.0226  142 VAL   A O   
2981 C  CB  . VAL   A 142 ? 0.1500 0.1725 0.2459 -0.0102 0.0121  0.0223  142 VAL   A CB  
2982 C  CG1 . VAL   A 142 ? 0.1445 0.1606 0.2488 -0.0154 0.0114  0.0179  142 VAL   A CG1 
2983 C  CG2 . VAL   A 142 ? 0.1656 0.1843 0.2565 -0.0015 0.0139  0.0198  142 VAL   A CG2 
2993 N  N   . CYS   A 143 ? 0.1327 0.1513 0.2348 -0.0121 0.0049  0.0205  143 CYS   A N   
2994 C  CA  . CYS   A 143 ? 0.1316 0.1532 0.2456 -0.0121 0.0130  0.0364  143 CYS   A CA  
2995 C  C   . CYS   A 143 ? 0.1287 0.1474 0.2582 -0.0104 0.0049  0.0323  143 CYS   A C   
2996 O  O   . CYS   A 143 ? 0.1244 0.1515 0.2680 -0.0080 0.0103  0.0333  143 CYS   A O   
2997 C  CB  . CYS   A 143 ? 0.1400 0.1533 0.2539 -0.0035 0.0119  0.0418  143 CYS   A CB  
2998 S  SG  . CYS   A 143 ? 0.1544 0.1624 0.2506 0.0004  0.0118  0.0300  143 CYS   A SG  
3004 N  N   . VAL   A 144 ? 0.1255 0.1487 0.2805 -0.0100 0.0051  0.0414  144 VAL   A N   
3005 C  CA  . VAL   A 144 ? 0.1350 0.1664 0.3070 -0.0127 0.0168  0.0390  144 VAL   A CA  
3006 C  C   . VAL   A 144 ? 0.1359 0.1538 0.3016 -0.0187 -0.0062 0.0330  144 VAL   A C   
3007 O  O   . VAL   A 144 ? 0.1559 0.1601 0.3003 -0.0086 -0.0126 0.0410  144 VAL   A O   
3008 C  CB  . VAL   A 144 ? 0.1626 0.1855 0.3573 -0.0011 0.0344  0.0415  144 VAL   A CB  
3009 C  CG1 . VAL   A 144 ? 0.1704 0.2006 0.3902 -0.0167 0.0251  0.0364  144 VAL   A CG1 
3010 C  CG2 . VAL   A 144 ? 0.1503 0.1868 0.3592 -0.0012 0.0363  0.0513  144 VAL   A CG2 
3020 N  N   . ASP   A 145 ? 0.1408 0.1437 0.3109 -0.0211 -0.0080 0.0254  145 ASP   A N   
3021 C  CA  . ASP   A 145 ? 0.1574 0.1537 0.3025 -0.0176 -0.0131 0.0191  145 ASP   A CA  
3022 C  C   . ASP   A 145 ? 0.1510 0.1509 0.3056 -0.0117 -0.0081 0.0137  145 ASP   A C   
3023 O  O   . ASP   A 145 ? 0.1647 0.1606 0.3525 -0.0107 -0.0132 -0.0164 145 ASP   A O   
3024 C  CB  . ASP   A 145 ? 0.1665 0.1815 0.3134 -0.0219 -0.0200 0.0146  145 ASP   A CB  
3025 C  CG  . ASP   A 145 ? 0.1842 0.2213 0.3403 -0.0409 -0.0246 0.0189  145 ASP   A CG  
3026 O  OD1 . ASP   A 145 ? 0.1753 0.2394 0.3611 -0.0547 -0.0212 0.0234  145 ASP   A OD1 
3027 O  OD2 . ASP   A 145 ? 0.2110 0.2490 0.3566 -0.0494 -0.0403 0.0117  145 ASP   A OD2 
3032 N  N   . THR   A 146 ? 0.1376 0.1393 0.2787 -0.0114 0.0029  0.0113  146 THR   A N   
3033 C  CA  . THR   A 146 ? 0.1332 0.1380 0.2599 -0.0057 0.0043  0.0140  146 THR   A CA  
3034 C  C   . THR   A 146 ? 0.1351 0.1341 0.2621 0.0017  0.0103  0.0206  146 THR   A C   
3035 O  O   . THR   A 146 ? 0.1410 0.1481 0.2772 0.0096  0.0031  0.0140  146 THR   A O   
3036 C  CB  . THR   A 146 ? 0.1375 0.1478 0.2567 -0.0055 0.0074  0.0200  146 THR   A CB  
3037 O  OG1 . THR   A 146 ? 0.1403 0.1635 0.2611 -0.0025 0.0035  0.0160  146 THR   A OG1 
3038 C  CG2 . THR   A 146 ? 0.1330 0.1406 0.2623 -0.0101 0.0106  0.0186  146 THR   A CG2 
3046 N  N   . VAL   A 147 ? 0.1310 0.1403 0.2605 -0.0042 0.0101  0.0212  147 VAL   A N   
3047 C  CA  . VAL   A 147 ? 0.1352 0.1413 0.2627 -0.0103 0.0288  0.0277  147 VAL   A CA  
3048 C  C   . VAL   A 147 ? 0.1330 0.1421 0.2750 -0.0128 0.0229  0.0353  147 VAL   A C   
3049 O  O   . VAL   A 147 ? 0.1343 0.1485 0.2868 -0.0171 0.0126  0.0344  147 VAL   A O   
3050 C  CB  . VAL   A 147 ? 0.1484 0.1420 0.2499 -0.0146 0.0187  0.0322  147 VAL   A CB  
3051 C  CG1 . VAL   A 147 ? 0.1785 0.1497 0.2490 -0.0119 0.0194  0.0325  147 VAL   A CG1 
3052 C  CG2 . VAL   A 147 ? 0.1522 0.1419 0.2598 -0.0138 0.0165  0.0294  147 VAL   A CG2 
3062 N  N   . ARG   A 148 ? 0.1319 0.1462 0.2709 -0.0076 0.0173  0.0511  148 ARG   A N   
3063 C  CA  . ARG   A 148 ? 0.1420 0.1536 0.2695 -0.0131 0.0146  0.0575  148 ARG   A CA  
3064 C  C   . ARG   A 148 ? 0.1494 0.1554 0.2617 -0.0132 0.0159  0.0695  148 ARG   A C   
3065 O  O   . ARG   A 148 ? 0.1810 0.1652 0.2853 -0.0227 0.0264  0.0580  148 ARG   A O   
3066 C  CB  . ARG   A 148 ? 0.1510 0.1528 0.2914 -0.0085 0.0239  0.0426  148 ARG   A CB  
3067 C  CG  . ARG   A 148 ? 0.1652 0.1517 0.3127 -0.0102 0.0451  0.0365  148 ARG   A CG  
3068 C  CD  . ARG   A 148 ? 0.1857 0.1462 0.3250 -0.0081 0.0470  0.0555  148 ARG   A CD  
3069 N  NE  . ARG   A 148 ? 0.1793 0.1524 0.3209 0.0102  0.0488  0.0650  148 ARG   A NE  
3070 C  CZ  . ARG   A 148 ? 0.1740 0.1423 0.3000 0.0061  0.0427  0.0614  148 ARG   A CZ  
3071 N  NH1 . ARG   A 148 ? 0.1867 0.1399 0.3020 -0.0062 0.0428  0.0251  148 ARG   A NH1 
3072 N  NH2 . ARG   A 148 ? 0.1587 0.1608 0.3117 0.0113  0.0475  0.0571  148 ARG   A NH2 
3086 N  N   . THR   A 149 ? 0.1469 0.1617 0.2560 -0.0108 0.0105  0.0617  149 THR   A N   
3087 C  CA  . THR   A 149 ? 0.1545 0.1669 0.2483 -0.0079 0.0075  0.0612  149 THR   A CA  
3088 C  C   . THR   A 149 ? 0.1490 0.1688 0.2490 -0.0171 0.0099  0.0599  149 THR   A C   
3089 O  O   . THR   A 149 ? 0.1470 0.1701 0.2566 -0.0192 0.0129  0.0567  149 THR   A O   
3090 C  CB  . THR   A 149 ? 0.1524 0.1740 0.2608 -0.0112 0.0096  0.0491  149 THR   A CB  
3091 O  OG1 . THR   A 149 ? 0.1501 0.1569 0.2711 -0.0186 0.0097  0.0515  149 THR   A OG1 
3092 C  CG2 . THR   A 149 ? 0.1434 0.1902 0.2672 -0.0111 0.0014  0.0382  149 THR   A CG2 
3100 N  N   . ASN   A 150 ? 0.1541 0.1744 0.2532 -0.0097 0.0073  0.0752  150 ASN   A N   
3101 C  CA  . ASN   A 150 ? 0.1667 0.1841 0.2493 -0.0171 0.0121  0.0623  150 ASN   A CA  
3102 C  C   . ASN   A 150 ? 0.1452 0.1692 0.2466 -0.0232 0.0101  0.0544  150 ASN   A C   
3103 O  O   . ASN   A 150 ? 0.1515 0.1801 0.2768 -0.0175 -0.0021 0.0580  150 ASN   A O   
3104 C  CB  . ASN   A 150 ? 0.2073 0.2083 0.2723 -0.0256 0.0277  0.0754  150 ASN   A CB  
3105 C  CG  . ASN   A 150 ? 0.2660 0.2354 0.3239 -0.0241 0.0139  0.0792  150 ASN   A CG  
3106 O  OD1 . ASN   A 150 ? 0.2923 0.2377 0.3415 -0.0300 0.0194  0.0973  150 ASN   A OD1 
3107 N  ND2 . ASN   A 150 ? 0.2972 0.2571 0.3533 -0.0192 0.0078  0.0805  150 ASN   A ND2 
3114 N  N   . VAL   A 151 ? 0.1463 0.1532 0.2473 -0.0218 0.0141  0.0477  151 VAL   A N   
3115 C  CA  . VAL   A 151 ? 0.1567 0.1591 0.2473 -0.0219 0.0169  0.0474  151 VAL   A CA  
3116 C  C   . VAL   A 151 ? 0.1489 0.1542 0.2520 -0.0262 0.0157  0.0565  151 VAL   A C   
3117 O  O   . VAL   A 151 ? 0.1546 0.1609 0.2819 -0.0243 0.0177  0.0495  151 VAL   A O   
3118 C  CB  . VAL   A 151 ? 0.1841 0.1779 0.2437 -0.0087 0.0134  0.0384  151 VAL   A CB  
3119 C  CG1 . VAL   A 151 ? 0.1758 0.2033 0.2535 -0.0132 0.0068  0.0367  151 VAL   A CG1 
3120 C  CG2 . VAL   A 151 ? 0.1933 0.1666 0.2354 -0.0034 0.0227  0.0369  151 VAL   A CG2 
3130 N  N   . TYR   A 152 ? 0.1470 0.1565 0.2506 -0.0248 0.0109  0.0571  152 TYR   A N   
3131 C  CA  . TYR   A 152 ? 0.1466 0.1680 0.2170 -0.0199 0.0143  0.0526  152 TYR   A CA  
3132 C  C   . TYR   A 152 ? 0.1432 0.1618 0.2137 -0.0203 0.0216  0.0573  152 TYR   A C   
3133 O  O   . TYR   A 152 ? 0.1535 0.1525 0.2461 -0.0269 0.0218  0.0445  152 TYR   A O   
3134 C  CB  . TYR   A 152 ? 0.1592 0.1831 0.2211 -0.0206 0.0252  0.0635  152 TYR   A CB  
3135 C  CG  . TYR   A 152 ? 0.1734 0.2062 0.2128 -0.0222 0.0259  0.0587  152 TYR   A CG  
3136 C  CD1 . TYR   A 152 ? 0.1915 0.2275 0.2303 -0.0090 0.0394  0.0621  152 TYR   A CD1 
3137 C  CD2 . TYR   A 152 ? 0.1822 0.2124 0.2068 -0.0366 0.0254  0.0486  152 TYR   A CD2 
3138 C  CE1 . TYR   A 152 ? 0.2303 0.2396 0.2331 -0.0097 0.0259  0.0704  152 TYR   A CE1 
3139 C  CE2 . TYR   A 152 ? 0.2146 0.2277 0.2140 -0.0392 0.0246  0.0582  152 TYR   A CE2 
3140 C  CZ  . TYR   A 152 ? 0.2477 0.2346 0.2269 -0.0242 0.0211  0.0811  152 TYR   A CZ  
3141 O  OH  . TYR   A 152 ? 0.2854 0.2566 0.2661 -0.0190 0.0250  0.0975  152 TYR   A OH  
3151 N  N   . LEU   A 153 ? 0.1459 0.1584 0.2286 -0.0242 0.0162  0.0479  153 LEU   A N   
3152 C  CA  . LEU   A 153 ? 0.1377 0.1515 0.2410 -0.0152 0.0232  0.0481  153 LEU   A CA  
3153 C  C   . LEU   A 153 ? 0.1379 0.1563 0.2506 -0.0133 0.0254  0.0452  153 LEU   A C   
3154 O  O   . LEU   A 153 ? 0.1471 0.1688 0.2837 -0.0126 0.0375  0.0484  153 LEU   A O   
3155 C  CB  . LEU   A 153 ? 0.1264 0.1570 0.2422 -0.0145 0.0098  0.0377  153 LEU   A CB  
3156 C  CG  . LEU   A 153 ? 0.1396 0.1616 0.2380 -0.0143 0.0135  0.0363  153 LEU   A CG  
3157 C  CD1 . LEU   A 153 ? 0.1504 0.1716 0.2379 -0.0163 0.0059  0.0378  153 LEU   A CD1 
3158 C  CD2 . LEU   A 153 ? 0.1443 0.1638 0.2442 -0.0141 0.0192  0.0172  153 LEU   A CD2 
3170 N  N   A ALA   A 154 ? 0.1318 0.1508 0.2603 -0.0038 0.0280  0.0455  154 ALA   A N   
3171 N  N   B ALA   A 154 ? 0.1462 0.1605 0.2357 -0.0117 0.0250  0.0390  154 ALA   A N   
3172 C  CA  A ALA   A 154 ? 0.1440 0.1561 0.2726 -0.0040 0.0308  0.0480  154 ALA   A CA  
3173 C  CA  B ALA   A 154 ? 0.1623 0.1695 0.2278 -0.0113 0.0226  0.0358  154 ALA   A CA  
3174 C  C   A ALA   A 154 ? 0.1447 0.1584 0.2838 0.0044  0.0328  0.0588  154 ALA   A C   
3175 C  C   B ALA   A 154 ? 0.1748 0.1781 0.2276 -0.0089 0.0216  0.0419  154 ALA   A C   
3176 O  O   A ALA   A 154 ? 0.1528 0.1726 0.2856 0.0029  0.0323  0.0591  154 ALA   A O   
3177 O  O   B ALA   A 154 ? 0.1763 0.1842 0.2250 -0.0088 0.0205  0.0464  154 ALA   A O   
3178 C  CB  A ALA   A 154 ? 0.1516 0.1626 0.2739 0.0031  0.0319  0.0309  154 ALA   A CB  
3179 C  CB  B ALA   A 154 ? 0.1662 0.1724 0.2262 -0.0078 0.0218  0.0257  154 ALA   A CB  
3190 N  N   A VAL   A 155 ? 0.1457 0.1538 0.2935 0.0137  0.0316  0.0692  155 VAL   A N   
3191 N  N   B VAL   A 155 ? 0.1875 0.1813 0.2324 -0.0057 0.0201  0.0423  155 VAL   A N   
3192 C  CA  A VAL   A 155 ? 0.1522 0.1647 0.2926 0.0087  0.0287  0.0767  155 VAL   A CA  
3193 C  CA  B VAL   A 155 ? 0.2011 0.1900 0.2363 -0.0041 0.0152  0.0398  155 VAL   A CA  
3194 C  C   A VAL   A 155 ? 0.1608 0.1731 0.3216 0.0213  0.0294  0.0788  155 VAL   A C   
3195 C  C   B VAL   A 155 ? 0.2170 0.2017 0.2498 -0.0005 0.0196  0.0441  155 VAL   A C   
3196 O  O   A VAL   A 155 ? 0.1592 0.1789 0.3467 0.0305  0.0338  0.0692  155 VAL   A O   
3197 O  O   B VAL   A 155 ? 0.2175 0.2084 0.2550 -0.0003 0.0337  0.0495  155 VAL   A O   
3198 C  CB  A VAL   A 155 ? 0.1593 0.1760 0.2728 0.0101  0.0158  0.0698  155 VAL   A CB  
3199 C  CB  B VAL   A 155 ? 0.2010 0.1907 0.2258 -0.0024 0.0053  0.0347  155 VAL   A CB  
3200 C  CG1 A VAL   A 155 ? 0.1753 0.1879 0.2667 0.0170  0.0113  0.0660  155 VAL   A CG1 
3201 C  CG1 B VAL   A 155 ? 0.2021 0.1943 0.2197 0.0022  0.0045  0.0299  155 VAL   A CG1 
3202 C  CG2 A VAL   A 155 ? 0.1697 0.1873 0.2739 0.0174  -0.0060 0.0708  155 VAL   A CG2 
3203 C  CG2 B VAL   A 155 ? 0.2042 0.1925 0.2278 -0.0002 -0.0037 0.0334  155 VAL   A CG2 
3222 N  N   A PHE   A 156 ? 0.1781 0.1793 0.3269 0.0230  0.0352  0.0922  156 PHE   A N   
3223 N  N   B PHE   A 156 ? 0.2371 0.2103 0.2731 0.0016  0.0099  0.0387  156 PHE   A N   
3224 C  CA  A PHE   A 156 ? 0.2066 0.1817 0.3390 0.0310  0.0272  0.0947  156 PHE   A CA  
3225 C  CA  B PHE   A 156 ? 0.2606 0.2214 0.2953 0.0052  -0.0088 0.0337  156 PHE   A CA  
3226 C  C   A PHE   A 156 ? 0.2039 0.1887 0.3427 0.0407  0.0338  0.0984  156 PHE   A C   
3227 C  C   B PHE   A 156 ? 0.2692 0.2258 0.3177 -0.0015 -0.0201 0.0268  156 PHE   A C   
3228 O  O   A PHE   A 156 ? 0.2020 0.1943 0.3611 0.0415  0.0299  0.0728  156 PHE   A O   
3229 O  O   B PHE   A 156 ? 0.2740 0.2389 0.3383 -0.0033 -0.0220 0.0248  156 PHE   A O   
3230 C  CB  A PHE   A 156 ? 0.2339 0.1855 0.3462 0.0278  0.0160  0.1017  156 PHE   A CB  
3231 C  CB  B PHE   A 156 ? 0.2746 0.2311 0.2999 0.0154  -0.0123 0.0282  156 PHE   A CB  
3232 C  CG  A PHE   A 156 ? 0.2623 0.1934 0.3649 0.0386  0.0008  0.0902  156 PHE   A CG  
3233 C  CG  B PHE   A 156 ? 0.2873 0.2449 0.3043 0.0252  -0.0162 0.0191  156 PHE   A CG  
3234 C  CD1 A PHE   A 156 ? 0.2771 0.2058 0.3739 0.0442  -0.0015 0.0786  156 PHE   A CD1 
3235 C  CD1 B PHE   A 156 ? 0.2925 0.2514 0.3078 0.0317  -0.0232 0.0137  156 PHE   A CD1 
3236 C  CD2 A PHE   A 156 ? 0.2727 0.2032 0.3779 0.0546  -0.0040 0.0928  156 PHE   A CD2 
3237 C  CD2 B PHE   A 156 ? 0.2952 0.2537 0.3078 0.0254  -0.0167 0.0167  156 PHE   A CD2 
3238 C  CE1 A PHE   A 156 ? 0.2894 0.2124 0.3876 0.0492  -0.0026 0.0681  156 PHE   A CE1 
3239 C  CE1 B PHE   A 156 ? 0.2957 0.2552 0.3090 0.0319  -0.0247 0.0092  156 PHE   A CE1 
3240 C  CE2 A PHE   A 156 ? 0.2888 0.2137 0.3866 0.0599  -0.0036 0.0800  156 PHE   A CE2 
3241 C  CE2 B PHE   A 156 ? 0.2968 0.2578 0.3084 0.0264  -0.0208 0.0159  156 PHE   A CE2 
3242 C  CZ  A PHE   A 156 ? 0.2965 0.2135 0.3949 0.0598  -0.0053 0.0622  156 PHE   A CZ  
3243 C  CZ  B PHE   A 156 ? 0.2960 0.2556 0.3068 0.0270  -0.0224 0.0097  156 PHE   A CZ  
3262 N  N   A ASP   A 157 ? 0.2013 0.1957 0.3429 0.0450  0.0449  0.1176  157 ASP   A N   
3263 N  N   B ASP   A 157 ? 0.2703 0.2191 0.3113 -0.0072 -0.0251 0.0300  157 ASP   A N   
3264 C  CA  A ASP   A 157 ? 0.2128 0.2169 0.3577 0.0488  0.0353  0.1327  157 ASP   A CA  
3265 C  CA  B ASP   A 157 ? 0.2693 0.2131 0.2996 -0.0141 -0.0314 0.0258  157 ASP   A CA  
3266 C  C   A ASP   A 157 ? 0.1864 0.2319 0.3621 0.0563  0.0467  0.1398  157 ASP   A C   
3267 C  C   B ASP   A 157 ? 0.2545 0.2013 0.2774 -0.0271 -0.0271 0.0178  157 ASP   A C   
3268 O  O   A ASP   A 157 ? 0.1751 0.2265 0.3598 0.0483  0.0473  0.1428  157 ASP   A O   
3269 O  O   B ASP   A 157 ? 0.2501 0.1938 0.2753 -0.0266 -0.0287 0.0153  157 ASP   A O   
3270 C  CB  A ASP   A 157 ? 0.2404 0.2253 0.3787 0.0558  0.0171  0.1248  157 ASP   A CB  
3271 C  CB  B ASP   A 157 ? 0.2777 0.2174 0.3126 -0.0049 -0.0375 0.0332  157 ASP   A CB  
3272 C  CG  A ASP   A 157 ? 0.2742 0.2375 0.4217 0.0616  -0.0009 0.1095  157 ASP   A CG  
3273 C  CG  B ASP   A 157 ? 0.2877 0.2215 0.3320 0.0072  -0.0430 0.0335  157 ASP   A CG  
3274 O  OD1 A ASP   A 157 ? 0.3105 0.2463 0.4541 0.0511  -0.0192 0.0859  157 ASP   A OD1 
3275 O  OD1 B ASP   A 157 ? 0.2928 0.2225 0.3436 0.0131  -0.0433 0.0290  157 ASP   A OD1 
3276 O  OD2 A ASP   A 157 ? 0.2593 0.2371 0.4364 0.0633  0.0076  0.1206  157 ASP   A OD2 
3277 O  OD2 B ASP   A 157 ? 0.2880 0.2243 0.3389 0.0091  -0.0424 0.0371  157 ASP   A OD2 
3286 N  N   A LYS   A 158 ? 0.1968 0.2612 0.3816 0.0600  0.0581  0.1245  158 LYS   A N   
3287 N  N   B LYS   A 158 ? 0.2462 0.2027 0.2657 -0.0383 -0.0190 0.0135  158 LYS   A N   
3288 C  CA  A LYS   A 158 ? 0.2023 0.2904 0.3903 0.0690  0.0644  0.1133  158 LYS   A CA  
3289 C  CA  B LYS   A 158 ? 0.2416 0.2104 0.2598 -0.0463 -0.0032 0.0120  158 LYS   A CA  
3290 C  C   A LYS   A 158 ? 0.1861 0.2951 0.3695 0.0770  0.0435  0.1236  158 LYS   A C   
3291 C  C   B LYS   A 158 ? 0.2235 0.2002 0.2399 -0.0625 -0.0028 0.0115  158 LYS   A C   
3292 O  O   A LYS   A 158 ? 0.1832 0.2950 0.3606 0.0678  0.0519  0.1283  158 LYS   A O   
3293 O  O   B LYS   A 158 ? 0.2122 0.1866 0.2317 -0.0770 -0.0048 0.0166  158 LYS   A O   
3294 C  CB  A LYS   A 158 ? 0.2252 0.3093 0.4220 0.0716  0.0909  0.1055  158 LYS   A CB  
3295 C  CB  B LYS   A 158 ? 0.2546 0.2342 0.2835 -0.0343 0.0097  0.0153  158 LYS   A CB  
3296 C  CG  A LYS   A 158 ? 0.2442 0.3280 0.4587 0.0746  0.1105  0.1046  158 LYS   A CG  
3297 C  CG  B LYS   A 158 ? 0.2649 0.2541 0.3114 -0.0239 0.0244  0.0227  158 LYS   A CG  
3298 C  CD  A LYS   A 158 ? 0.2554 0.3410 0.4883 0.0707  0.1316  0.1179  158 LYS   A CD  
3299 C  CD  B LYS   A 158 ? 0.2730 0.2692 0.3422 -0.0174 0.0379  0.0312  158 LYS   A CD  
3300 C  CE  A LYS   A 158 ? 0.2623 0.3463 0.5046 0.0652  0.1509  0.1343  158 LYS   A CE  
3301 C  CE  B LYS   A 158 ? 0.2774 0.2787 0.3683 -0.0080 0.0469  0.0353  158 LYS   A CE  
3302 N  NZ  A LYS   A 158 ? 0.2651 0.3494 0.5175 0.0613  0.1582  0.1441  158 LYS   A NZ  
3303 N  NZ  B LYS   A 158 ? 0.2783 0.2835 0.3849 -0.0043 0.0536  0.0362  158 LYS   A NZ  
3330 N  N   A ASN   A 159 ? 0.1806 0.3016 0.3773 0.0754  0.0261  0.1228  159 ASN   A N   
3331 N  N   B ASN   A 159 ? 0.2217 0.2125 0.2432 -0.0585 -0.0030 0.0098  159 ASN   A N   
3332 C  CA  A ASN   A 159 ? 0.1809 0.3080 0.3792 0.0641  -0.0015 0.1361  159 ASN   A CA  
3333 C  CA  B ASN   A 159 ? 0.2231 0.2268 0.2602 -0.0476 -0.0032 0.0173  159 ASN   A CA  
3334 C  C   A ASN   A 159 ? 0.1653 0.3052 0.3428 0.0462  0.0023  0.1199  159 ASN   A C   
3335 C  C   B ASN   A 159 ? 0.2064 0.2182 0.2260 -0.0520 -0.0083 0.0135  159 ASN   A C   
3336 O  O   A ASN   A 159 ? 0.1464 0.3054 0.3292 0.0378  -0.0108 0.0962  159 ASN   A O   
3337 O  O   B ASN   A 159 ? 0.2082 0.2266 0.2159 -0.0546 -0.0140 0.0120  159 ASN   A O   
3338 C  CB  A ASN   A 159 ? 0.2037 0.3217 0.4419 0.0626  -0.0083 0.1510  159 ASN   A CB  
3339 C  CB  B ASN   A 159 ? 0.2435 0.2517 0.3203 -0.0346 0.0032  0.0264  159 ASN   A CB  
3340 C  CG  A ASN   A 159 ? 0.2318 0.3410 0.5164 0.0579  -0.0013 0.1480  159 ASN   A CG  
3341 C  CG  B ASN   A 159 ? 0.2633 0.2772 0.3805 -0.0245 0.0104  0.0310  159 ASN   A CG  
3342 O  OD1 A ASN   A 159 ? 0.2376 0.3572 0.5499 0.0526  0.0065  0.1424  159 ASN   A OD1 
3343 O  OD1 B ASN   A 159 ? 0.2671 0.2865 0.4034 -0.0212 0.0091  0.0303  159 ASN   A OD1 
3344 N  ND2 A ASN   A 159 ? 0.2440 0.3456 0.5431 0.0591  -0.0007 0.1441  159 ASN   A ND2 
3345 N  ND2 B ASN   A 159 ? 0.2715 0.2854 0.4025 -0.0215 0.0151  0.0329  159 ASN   A ND2 
3358 N  N   A LEU   A 160 ? 0.1611 0.2911 0.3223 0.0428  -0.0046 0.1272  160 LEU   A N   
3359 N  N   B LEU   A 160 ? 0.1921 0.2059 0.2179 -0.0514 -0.0093 0.0180  160 LEU   A N   
3360 C  CA  A LEU   A 160 ? 0.1579 0.2797 0.3002 0.0298  0.0145  0.1264  160 LEU   A CA  
3361 C  CA  B LEU   A 160 ? 0.1910 0.2077 0.2195 -0.0405 0.0046  0.0199  160 LEU   A CA  
3362 C  C   A LEU   A 160 ? 0.1463 0.2784 0.2952 0.0202  0.0304  0.1177  160 LEU   A C   
3363 C  C   B LEU   A 160 ? 0.1806 0.2013 0.2091 -0.0229 0.0058  0.0252  160 LEU   A C   
3364 O  O   A LEU   A 160 ? 0.1417 0.2903 0.3245 0.0115  0.0305  0.1035  160 LEU   A O   
3365 O  O   B LEU   A 160 ? 0.1803 0.1896 0.2136 -0.0239 0.0017  0.0202  160 LEU   A O   
3366 C  CB  A LEU   A 160 ? 0.1705 0.2752 0.2818 0.0222  0.0280  0.1222  160 LEU   A CB  
3367 C  CB  B LEU   A 160 ? 0.2062 0.2185 0.2403 -0.0392 0.0168  0.0113  160 LEU   A CB  
3368 C  CG  A LEU   A 160 ? 0.1817 0.2812 0.2727 0.0070  0.0393  0.1075  160 LEU   A CG  
3369 C  CG  B LEU   A 160 ? 0.2242 0.2390 0.2665 -0.0333 0.0260  0.0014  160 LEU   A CG  
3370 C  CD1 A LEU   A 160 ? 0.1948 0.2873 0.2740 0.0015  0.0434  0.0995  160 LEU   A CD1 
3371 C  CD1 B LEU   A 160 ? 0.2299 0.2436 0.2735 -0.0321 0.0306  -0.0052 160 LEU   A CD1 
3372 C  CD2 A LEU   A 160 ? 0.1899 0.2762 0.2652 0.0046  0.0438  0.1027  160 LEU   A CD2 
3373 C  CD2 B LEU   A 160 ? 0.2327 0.2455 0.2749 -0.0319 0.0307  0.0007  160 LEU   A CD2 
3396 N  N   A TYR   A 161 ? 0.1456 0.2668 0.2855 0.0252  0.0299  0.1165  161 TYR   A N   
3397 N  N   B TYR   A 161 ? 0.1741 0.2120 0.1988 -0.0075 0.0133  0.0400  161 TYR   A N   
3398 C  CA  A TYR   A 161 ? 0.1427 0.2653 0.2860 0.0211  0.0306  0.1059  161 TYR   A CA  
3399 C  CA  B TYR   A 161 ? 0.1710 0.2202 0.2020 0.0011  0.0172  0.0513  161 TYR   A CA  
3400 C  C   A TYR   A 161 ? 0.1339 0.2890 0.3025 0.0171  0.0261  0.1042  161 TYR   A C   
3401 C  C   B TYR   A 161 ? 0.1724 0.2308 0.2142 0.0010  0.0105  0.0505  161 TYR   A C   
3402 O  O   A TYR   A 161 ? 0.1304 0.2893 0.3027 0.0051  0.0156  0.0993  161 TYR   A O   
3403 O  O   B TYR   A 161 ? 0.1679 0.2273 0.2060 -0.0017 0.0071  0.0520  161 TYR   A O   
3404 C  CB  A TYR   A 161 ? 0.1615 0.2519 0.2934 0.0191  0.0205  0.0938  161 TYR   A CB  
3405 C  CB  B TYR   A 161 ? 0.1688 0.2210 0.2050 0.0113  0.0273  0.0586  161 TYR   A CB  
3406 C  CG  A TYR   A 161 ? 0.1655 0.2350 0.2979 0.0177  0.0125  0.0803  161 TYR   A CG  
3407 C  CG  B TYR   A 161 ? 0.1666 0.2252 0.2205 0.0194  0.0355  0.0636  161 TYR   A CG  
3408 C  CD1 A TYR   A 161 ? 0.1588 0.2188 0.3066 0.0068  0.0084  0.0685  161 TYR   A CD1 
3409 C  CD1 B TYR   A 161 ? 0.1627 0.2249 0.2332 0.0209  0.0355  0.0611  161 TYR   A CD1 
3410 C  CD2 A TYR   A 161 ? 0.1674 0.2307 0.2934 0.0216  0.0057  0.0771  161 TYR   A CD2 
3411 C  CD2 B TYR   A 161 ? 0.1666 0.2280 0.2258 0.0244  0.0391  0.0681  161 TYR   A CD2 
3412 C  CE1 A TYR   A 161 ? 0.1703 0.2073 0.3053 0.0038  0.0038  0.0681  161 TYR   A CE1 
3413 C  CE1 B TYR   A 161 ? 0.1656 0.2290 0.2353 0.0247  0.0347  0.0636  161 TYR   A CE1 
3414 C  CE2 A TYR   A 161 ? 0.1738 0.2188 0.3010 0.0143  0.0060  0.0759  161 TYR   A CE2 
3415 C  CE2 B TYR   A 161 ? 0.1686 0.2281 0.2320 0.0244  0.0395  0.0731  161 TYR   A CE2 
3416 C  CZ  A TYR   A 161 ? 0.1849 0.2045 0.3023 0.0030  0.0029  0.0775  161 TYR   A CZ  
3417 C  CZ  B TYR   A 161 ? 0.1751 0.2286 0.2396 0.0244  0.0370  0.0689  161 TYR   A CZ  
3418 O  OH  A TYR   A 161 ? 0.2005 0.1869 0.3112 -0.0002 -0.0010 0.0838  161 TYR   A OH  
3419 O  OH  B TYR   A 161 ? 0.1883 0.2302 0.2565 0.0229  0.0371  0.0683  161 TYR   A OH  
3438 N  N   A ASP   A 162 ? 0.1343 0.3139 0.3212 0.0226  0.0347  0.1175  162 ASP   A N   
3439 N  N   B ASP   A 162 ? 0.1808 0.2465 0.2407 0.0022  0.0097  0.0553  162 ASP   A N   
3440 C  CA  A ASP   A 162 ? 0.1304 0.3439 0.3281 0.0161  0.0330  0.1222  162 ASP   A CA  
3441 C  CA  B ASP   A 162 ? 0.1881 0.2674 0.2628 -0.0041 0.0086  0.0596  162 ASP   A CA  
3442 C  C   A ASP   A 162 ? 0.1230 0.3575 0.3181 0.0064  0.0281  0.1250  162 ASP   A C   
3443 C  C   B ASP   A 162 ? 0.1936 0.2831 0.2618 -0.0128 0.0094  0.0649  162 ASP   A C   
3444 O  O   A ASP   A 162 ? 0.1246 0.3634 0.3483 -0.0049 0.0281  0.1131  162 ASP   A O   
3445 O  O   B ASP   A 162 ? 0.1964 0.2828 0.2691 -0.0209 0.0090  0.0654  162 ASP   A O   
3446 C  CB  A ASP   A 162 ? 0.1411 0.3593 0.3446 0.0220  0.0413  0.1163  162 ASP   A CB  
3447 C  CB  B ASP   A 162 ? 0.1917 0.2765 0.2904 0.0013  0.0096  0.0536  162 ASP   A CB  
3448 C  CG  A ASP   A 162 ? 0.1570 0.3776 0.3637 0.0292  0.0482  0.1034  162 ASP   A CG  
3449 C  CG  B ASP   A 162 ? 0.1975 0.2861 0.3133 0.0071  0.0101  0.0463  162 ASP   A CG  
3450 O  OD1 A ASP   A 162 ? 0.1706 0.3870 0.3754 0.0236  0.0472  0.1009  162 ASP   A OD1 
3451 O  OD1 B ASP   A 162 ? 0.2030 0.2907 0.3257 0.0052  0.0119  0.0471  162 ASP   A OD1 
3452 O  OD2 A ASP   A 162 ? 0.1760 0.3853 0.3823 0.0409  0.0560  0.0873  162 ASP   A OD2 
3453 O  OD2 B ASP   A 162 ? 0.1986 0.2883 0.3227 0.0135  0.0062  0.0366  162 ASP   A OD2 
3462 N  N   A LYS   A 163 ? 0.1327 0.3740 0.3157 0.0057  0.0051  0.1310  163 LYS   A N   
3463 N  N   B LYS   A 163 ? 0.2005 0.2976 0.2678 -0.0151 0.0045  0.0625  163 LYS   A N   
3464 C  CA  A LYS   A 163 ? 0.1500 0.3865 0.3112 -0.0003 -0.0082 0.1241  163 LYS   A CA  
3465 C  CA  B LYS   A 163 ? 0.2106 0.3116 0.2767 -0.0147 0.0054  0.0571  163 LYS   A CA  
3466 C  C   A LYS   A 163 ? 0.1435 0.3735 0.3113 -0.0098 0.0070  0.1124  163 LYS   A C   
3467 C  C   B LYS   A 163 ? 0.1999 0.3069 0.2659 -0.0179 0.0117  0.0566  163 LYS   A C   
3468 O  O   A LYS   A 163 ? 0.1417 0.3895 0.3308 -0.0176 0.0120  0.1048  163 LYS   A O   
3469 O  O   B LYS   A 163 ? 0.2064 0.3165 0.2750 -0.0187 0.0116  0.0538  163 LYS   A O   
3470 C  CB  A LYS   A 163 ? 0.1916 0.4125 0.3454 0.0160  -0.0276 0.1220  163 LYS   A CB  
3471 C  CB  B LYS   A 163 ? 0.2334 0.3284 0.3081 -0.0096 -0.0012 0.0473  163 LYS   A CB  
3472 C  CG  A LYS   A 163 ? 0.2404 0.4363 0.3919 0.0217  -0.0255 0.1191  163 LYS   A CG  
3473 C  CG  B LYS   A 163 ? 0.2545 0.3439 0.3443 -0.0076 -0.0018 0.0400  163 LYS   A CG  
3474 C  CD  A LYS   A 163 ? 0.2954 0.4561 0.4515 0.0264  -0.0269 0.1118  163 LYS   A CD  
3475 C  CD  B LYS   A 163 ? 0.2720 0.3564 0.3809 -0.0052 0.0002  0.0340  163 LYS   A CD  
3476 C  CE  A LYS   A 163 ? 0.3362 0.4687 0.4997 0.0298  -0.0243 0.1066  163 LYS   A CE  
3477 C  CE  B LYS   A 163 ? 0.2868 0.3657 0.4112 -0.0045 0.0027  0.0298  163 LYS   A CE  
3478 N  NZ  A LYS   A 163 ? 0.3464 0.4762 0.5280 0.0310  -0.0237 0.1052  163 LYS   A NZ  
3479 N  NZ  B LYS   A 163 ? 0.2951 0.3702 0.4272 -0.0048 0.0044  0.0280  163 LYS   A NZ  
3506 N  N   A LEU   A 164 ? 0.1291 0.3402 0.3010 -0.0207 0.0080  0.1028  164 LEU   A N   
3507 N  N   B LEU   A 164 ? 0.1813 0.2935 0.2522 -0.0192 0.0149  0.0602  164 LEU   A N   
3508 C  CA  A LEU   A 164 ? 0.1392 0.3097 0.2915 -0.0285 0.0223  0.0954  164 LEU   A CA  
3509 C  CA  B LEU   A 164 ? 0.1692 0.2821 0.2443 -0.0162 0.0243  0.0661  164 LEU   A CA  
3510 C  C   A LEU   A 164 ? 0.1513 0.3028 0.2947 -0.0301 0.0274  0.0856  164 LEU   A C   
3511 C  C   B LEU   A 164 ? 0.1642 0.2878 0.2594 -0.0199 0.0281  0.0734  164 LEU   A C   
3512 O  O   A LEU   A 164 ? 0.1622 0.3094 0.3050 -0.0369 0.0340  0.0772  164 LEU   A O   
3513 O  O   B LEU   A 164 ? 0.1700 0.2914 0.2570 -0.0204 0.0360  0.0674  164 LEU   A O   
3514 C  CB  A LEU   A 164 ? 0.1491 0.2940 0.2864 -0.0299 0.0280  0.0951  164 LEU   A CB  
3515 C  CB  B LEU   A 164 ? 0.1640 0.2686 0.2292 -0.0085 0.0296  0.0660  164 LEU   A CB  
3516 C  CG  A LEU   A 164 ? 0.1577 0.2828 0.2831 -0.0243 0.0236  0.0888  164 LEU   A CG  
3517 C  CG  B LEU   A 164 ? 0.1588 0.2560 0.2164 -0.0006 0.0317  0.0648  164 LEU   A CG  
3518 C  CD1 A LEU   A 164 ? 0.1528 0.2789 0.2774 -0.0161 0.0171  0.0873  164 LEU   A CD1 
3519 C  CD1 B LEU   A 164 ? 0.1568 0.2515 0.2096 0.0057  0.0241  0.0673  164 LEU   A CD1 
3520 C  CD2 A LEU   A 164 ? 0.1702 0.2792 0.2791 -0.0251 0.0211  0.0829  164 LEU   A CD2 
3521 C  CD2 B LEU   A 164 ? 0.1562 0.2504 0.2070 0.0034  0.0393  0.0653  164 LEU   A CD2 
3544 N  N   . VAL   A 165 ? 0.1505 0.2899 0.2816 -0.0202 0.0253  0.0862  165 VAL   A N   
3545 C  CA  . VAL   A 165 ? 0.1641 0.2861 0.2714 -0.0249 0.0259  0.0958  165 VAL   A CA  
3546 C  C   . VAL   A 165 ? 0.1539 0.3073 0.2799 -0.0195 0.0243  0.0934  165 VAL   A C   
3547 O  O   . VAL   A 165 ? 0.1520 0.3035 0.2866 -0.0204 0.0205  0.0927  165 VAL   A O   
3548 C  CB  . VAL   A 165 ? 0.1872 0.2779 0.2771 -0.0230 0.0273  0.0851  165 VAL   A CB  
3549 C  CG1 . VAL   A 165 ? 0.1988 0.2826 0.2936 -0.0251 0.0298  0.0763  165 VAL   A CG1 
3550 C  CG2 . VAL   A 165 ? 0.1964 0.2748 0.2785 -0.0185 0.0252  0.0859  165 VAL   A CG2 
3561 N  N   A SER   A 166 ? 0.1421 0.3242 0.2953 -0.0154 0.0262  0.0985  166 SER   A N   
3562 N  N   B SER   A 166 ? 0.1706 0.3203 0.2811 -0.0138 0.0146  0.0824  166 SER   A N   
3563 C  CA  A SER   A 166 ? 0.1525 0.3522 0.3256 -0.0153 0.0201  0.0858  166 SER   A CA  
3564 C  CA  B SER   A 166 ? 0.1935 0.3388 0.2939 -0.0106 0.0030  0.0657  166 SER   A CA  
3565 C  C   A SER   A 166 ? 0.1514 0.3741 0.3263 -0.0285 0.0125  0.0749  166 SER   A C   
3566 C  C   B SER   A 166 ? 0.2042 0.3553 0.2963 -0.0117 -0.0045 0.0542  166 SER   A C   
3567 O  O   A SER   A 166 ? 0.1568 0.3822 0.3550 -0.0429 0.0157  0.0523  166 SER   A O   
3568 O  O   B SER   A 166 ? 0.2109 0.3589 0.3103 -0.0153 -0.0078 0.0435  166 SER   A O   
3569 C  CB  A SER   A 166 ? 0.1759 0.3650 0.3678 0.0013  0.0141  0.0727  166 SER   A CB  
3570 C  CB  B SER   A 166 ? 0.2090 0.3445 0.3119 -0.0046 -0.0017 0.0573  166 SER   A CB  
3571 O  OG  A SER   A 166 ? 0.2240 0.3762 0.4095 0.0035  0.0128  0.0721  166 SER   A OG  
3572 O  OG  B SER   A 166 ? 0.2317 0.3502 0.3319 -0.0024 -0.0046 0.0552  166 SER   A OG  
3583 N  N   A SER   A 167 ? 0.1570 0.3864 0.2951 -0.0131 0.0009  0.0770  167 SER   A N   
3584 N  N   B SER   A 167 ? 0.2079 0.3670 0.2854 -0.0030 -0.0088 0.0525  167 SER   A N   
3585 C  CA  A SER   A 167 ? 0.1922 0.4008 0.2917 -0.0027 -0.0063 0.0600  167 SER   A CA  
3586 C  CA  B SER   A 167 ? 0.2192 0.3800 0.2851 0.0045  -0.0109 0.0443  167 SER   A CA  
3587 C  C   A SER   A 167 ? 0.2072 0.4042 0.2944 0.0074  -0.0028 0.0443  167 SER   A C   
3588 C  C   B SER   A 167 ? 0.2196 0.3921 0.2890 0.0117  -0.0091 0.0386  167 SER   A C   
3589 O  O   A SER   A 167 ? 0.2168 0.4080 0.2987 0.0080  -0.0130 0.0360  167 SER   A O   
3590 O  O   B SER   A 167 ? 0.2247 0.3931 0.2891 0.0116  -0.0144 0.0347  167 SER   A O   
3591 C  CB  A SER   A 167 ? 0.2008 0.4107 0.2942 0.0024  0.0017  0.0604  167 SER   A CB  
3592 C  CB  B SER   A 167 ? 0.2251 0.3817 0.2861 0.0066  -0.0079 0.0424  167 SER   A CB  
3593 O  OG  A SER   A 167 ? 0.2103 0.4162 0.2972 0.0013  0.0154  0.0632  167 SER   A OG  
3594 O  OG  B SER   A 167 ? 0.2299 0.3827 0.2877 0.0069  -0.0023 0.0427  167 SER   A OG  
3605 N  N   . PHE   A 168 ? 0.2147 0.4041 0.2988 0.0206  -0.0092 0.0384  168 PHE   A N   
3606 C  CA  . PHE   A 168 ? 0.2482 0.4157 0.3318 0.0178  -0.0068 0.0292  168 PHE   A CA  
3607 C  C   . PHE   A 168 ? 0.3544 0.4754 0.4319 -0.0046 -0.0080 0.0170  168 PHE   A C   
3608 O  O   . PHE   A 168 ? 0.3475 0.4742 0.4305 -0.0110 0.0050  0.0235  168 PHE   A O   
3609 C  CB  . PHE   A 168 ? 0.2119 0.3719 0.2943 0.0133  -0.0043 0.0337  168 PHE   A CB  
3610 C  CG  . PHE   A 168 ? 0.1806 0.3324 0.2682 0.0016  -0.0012 0.0459  168 PHE   A CG  
3611 C  CD1 . PHE   A 168 ? 0.1725 0.3219 0.2629 -0.0020 -0.0013 0.0582  168 PHE   A CD1 
3612 C  CD2 . PHE   A 168 ? 0.1698 0.3147 0.2636 -0.0071 0.0141  0.0401  168 PHE   A CD2 
3613 C  CE1 . PHE   A 168 ? 0.1637 0.3133 0.2642 -0.0040 -0.0037 0.0569  168 PHE   A CE1 
3614 C  CE2 . PHE   A 168 ? 0.1738 0.3027 0.2767 -0.0138 0.0087  0.0518  168 PHE   A CE2 
3615 C  CZ  . PHE   A 168 ? 0.1680 0.3068 0.2722 -0.0136 0.0038  0.0562  168 PHE   A CZ  
3626 N  N   A LEU   A 169 ? 0.4176 0.5078 0.4978 -0.0183 -0.0198 0.0014  169 LEU   A N   
3627 N  N   B LEU   A 169 ? 0.4092 0.5036 0.4858 -0.0102 -0.0125 0.0095  169 LEU   A N   
3628 C  CA  A LEU   A 169 ? 0.4840 0.5401 0.5730 -0.0273 -0.0311 -0.0123 169 LEU   A CA  
3629 C  CA  B LEU   A 169 ? 0.4602 0.5294 0.5440 -0.0137 -0.0160 0.0022  169 LEU   A CA  
3630 C  C   A LEU   A 169 ? 0.5093 0.5501 0.6207 -0.0321 -0.0377 -0.0058 169 LEU   A C   
3631 C  C   B LEU   A 169 ? 0.4780 0.5377 0.5747 -0.0156 -0.0182 0.0071  169 LEU   A C   
3632 O  O   A LEU   A 169 ? 0.5187 0.5543 0.6378 -0.0347 -0.0383 -0.0035 169 LEU   A O   
3633 O  O   B LEU   A 169 ? 0.4832 0.5408 0.5857 -0.0166 -0.0183 0.0090  169 LEU   A O   
3634 C  CB  A LEU   A 169 ? 0.5174 0.5574 0.5910 -0.0324 -0.0344 -0.0317 169 LEU   A CB  
3635 C  CB  B LEU   A 169 ? 0.4877 0.5438 0.5644 -0.0159 -0.0168 -0.0097 169 LEU   A CB  
3636 C  CG  A LEU   A 169 ? 0.5449 0.5709 0.6051 -0.0369 -0.0353 -0.0503 169 LEU   A CG  
3637 C  CG  B LEU   A 169 ? 0.5090 0.5546 0.5810 -0.0178 -0.0165 -0.0211 169 LEU   A CG  
3638 C  CD1 A LEU   A 169 ? 0.5546 0.5756 0.6123 -0.0377 -0.0351 -0.0565 169 LEU   A CD1 
3639 C  CD1 B LEU   A 169 ? 0.5164 0.5581 0.5878 -0.0180 -0.0162 -0.0251 169 LEU   A CD1 
3640 C  CD2 A LEU   A 169 ? 0.5540 0.5754 0.6077 -0.0389 -0.0353 -0.0571 169 LEU   A CD2 
3641 C  CD2 B LEU   A 169 ? 0.5158 0.5583 0.5857 -0.0187 -0.0161 -0.0253 169 LEU   A CD2 
3642 O  OXT A LEU   A 169 ? 0.5121 0.5516 0.6340 -0.0333 -0.0395 -0.0040 169 LEU   A OXT 
3643 O  OXT B LEU   A 169 ? 0.4827 0.5400 0.5831 -0.0163 -0.0183 0.0086  169 LEU   A OXT 
3666 N  N   A SER   B 1   ? 0.3526 0.3240 0.3602 -0.1028 -0.0780 0.0070  1   SER   B N   
3667 N  N   B SER   B 1   ? 0.3287 0.3178 0.3346 -0.0648 -0.0519 0.0003  1   SER   B N   
3668 C  CA  A SER   B 1   ? 0.3408 0.3317 0.3675 -0.1100 -0.0920 0.0049  1   SER   B CA  
3669 C  CA  B SER   B 1   ? 0.3231 0.3218 0.3368 -0.0678 -0.0558 0.0018  1   SER   B CA  
3670 C  C   A SER   B 1   ? 0.3088 0.3354 0.3559 -0.1151 -0.1045 0.0248  1   SER   B C   
3671 C  C   B SER   B 1   ? 0.3099 0.3256 0.3303 -0.0669 -0.0627 0.0216  1   SER   B C   
3672 O  O   A SER   B 1   ? 0.3186 0.3416 0.3484 -0.1041 -0.1011 0.0270  1   SER   B O   
3673 O  O   B SER   B 1   ? 0.3152 0.3283 0.3263 -0.0625 -0.0597 0.0204  1   SER   B O   
3674 C  CB  A SER   B 1   ? 0.3599 0.3332 0.3887 -0.1065 -0.0820 -0.0125 1   SER   B CB  
3675 C  CB  B SER   B 1   ? 0.3283 0.3201 0.3477 -0.0694 -0.0484 -0.0140 1   SER   B CB  
3676 O  OG  A SER   B 1   ? 0.3790 0.3431 0.4249 -0.1008 -0.0672 -0.0172 1   SER   B OG  
3677 O  OG  B SER   B 1   ? 0.3340 0.3230 0.3650 -0.0713 -0.0444 -0.0228 1   SER   B OG  
3692 N  N   A MET   B 2   ? 0.2808 0.3338 0.3588 -0.1179 -0.0968 0.0647  2   MET   B N   
3693 N  N   B MET   B 2   ? 0.2940 0.3257 0.3295 -0.0676 -0.0665 0.0528  2   MET   B N   
3694 C  CA  A MET   B 2   ? 0.2665 0.3417 0.3712 -0.0958 -0.0929 0.0879  2   MET   B CA  
3695 C  CA  B MET   B 2   ? 0.2800 0.3284 0.3323 -0.0627 -0.0728 0.0796  2   MET   B CA  
3696 C  C   A MET   B 2   ? 0.2379 0.3286 0.3370 -0.0768 -0.0965 0.1140  2   MET   B C   
3697 C  C   B MET   B 2   ? 0.2501 0.3163 0.3135 -0.0682 -0.0789 0.1059  2   MET   B C   
3698 O  O   A MET   B 2   ? 0.2312 0.3453 0.3422 -0.0600 -0.1098 0.1167  2   MET   B O   
3699 O  O   B MET   B 2   ? 0.2513 0.3246 0.3137 -0.0616 -0.0813 0.1053  2   MET   B O   
3700 C  CB  A MET   B 2   ? 0.2923 0.3705 0.4502 -0.0761 -0.0687 0.0692  2   MET   B CB  
3701 C  CB  B MET   B 2   ? 0.2984 0.3456 0.3684 -0.0463 -0.0672 0.0738  2   MET   B CB  
3702 C  CG  A MET   B 2   ? 0.3191 0.3974 0.5258 -0.0520 -0.0425 0.0588  2   MET   B CG  
3703 C  CG  B MET   B 2   ? 0.3147 0.3608 0.3991 -0.0298 -0.0620 0.0732  2   MET   B CG  
3704 S  SD  A MET   B 2   ? 0.3490 0.4259 0.5968 -0.0283 -0.0207 0.0474  2   MET   B SD  
3705 S  SD  B MET   B 2   ? 0.3296 0.3759 0.4260 -0.0130 -0.0613 0.0710  2   MET   B SD  
3706 C  CE  A MET   B 2   ? 0.3503 0.4303 0.6071 -0.0285 -0.0128 0.0474  2   MET   B CE  
3707 C  CE  B MET   B 2   ? 0.3318 0.3787 0.4326 -0.0134 -0.0575 0.0686  2   MET   B CE  
3726 N  N   . VAL   B 3   ? 0.2180 0.2909 0.2996 -0.0826 -0.0792 0.1279  3   VAL   B N   
3727 C  CA  . VAL   B 3   ? 0.2117 0.2588 0.2915 -0.0718 -0.0734 0.1147  3   VAL   B CA  
3728 C  C   . VAL   B 3   ? 0.1961 0.2515 0.2542 -0.0647 -0.0719 0.1040  3   VAL   B C   
3729 O  O   . VAL   B 3   ? 0.1910 0.2716 0.2492 -0.0642 -0.0680 0.1041  3   VAL   B O   
3730 C  CB  . VAL   B 3   ? 0.2236 0.2474 0.3425 -0.0671 -0.0680 0.0943  3   VAL   B CB  
3731 C  CG1 . VAL   B 3   ? 0.2324 0.2374 0.3685 -0.0718 -0.0586 0.0977  3   VAL   B CG1 
3732 C  CG2 . VAL   B 3   ? 0.2212 0.2463 0.3563 -0.0611 -0.0565 0.1002  3   VAL   B CG2 
3743 N  N   . ASN   B 4   ? 0.1841 0.2208 0.2290 -0.0662 -0.0626 0.0863  4   ASN   B N   
3744 C  CA  . ASN   B 4   ? 0.1889 0.2265 0.1994 -0.0604 -0.0500 0.0508  4   ASN   B CA  
3745 C  C   . ASN   B 4   ? 0.1827 0.2423 0.1931 -0.0576 -0.0429 0.0433  4   ASN   B C   
3746 O  O   . ASN   B 4   ? 0.1783 0.2507 0.2090 -0.0565 -0.0314 0.0279  4   ASN   B O   
3747 C  CB  . ASN   B 4   ? 0.1956 0.2191 0.1744 -0.0617 -0.0475 0.0386  4   ASN   B CB  
3748 C  CG  . ASN   B 4   ? 0.2014 0.2003 0.1660 -0.0596 -0.0482 0.0352  4   ASN   B CG  
3749 O  OD1 . ASN   B 4   ? 0.2024 0.1861 0.1656 -0.0547 -0.0511 0.0353  4   ASN   B OD1 
3750 N  ND2 . ASN   B 4   ? 0.2227 0.2035 0.1890 -0.0437 -0.0392 0.0318  4   ASN   B ND2 
3757 N  N   . SER   B 5   ? 0.1892 0.2570 0.2066 -0.0574 -0.0422 0.0275  5   SER   B N   
3758 C  CA  . SER   B 5   ? 0.2159 0.2927 0.2306 -0.0548 -0.0232 0.0235  5   SER   B CA  
3759 C  C   . SER   B 5   ? 0.2507 0.3002 0.2526 -0.0784 0.0063  0.0250  5   SER   B C   
3760 O  O   . SER   B 5   ? 0.2728 0.2947 0.3142 -0.0654 0.0520  0.0299  5   SER   B O   
3761 C  CB  . SER   B 5   ? 0.2258 0.3134 0.2611 -0.0400 -0.0107 0.0347  5   SER   B CB  
3762 O  OG  . SER   B 5   ? 0.2587 0.3407 0.3194 -0.0255 -0.0140 0.0418  5   SER   B OG  
3768 N  N   A PHE   B 6   ? 0.2756 0.3233 0.2423 -0.0907 0.0195  0.0329  6   PHE   B N   
3769 N  N   B PHE   B 6   ? 0.2580 0.3031 0.2438 -0.0808 0.0118  0.0225  6   PHE   B N   
3770 C  CA  A PHE   B 6   ? 0.2988 0.3342 0.2219 -0.1059 0.0257  0.0231  6   PHE   B CA  
3771 C  CA  B PHE   B 6   ? 0.2654 0.2997 0.2351 -0.0844 0.0127  0.0118  6   PHE   B CA  
3772 C  C   A PHE   B 6   ? 0.3531 0.3663 0.2697 -0.1060 0.0545  0.0007  6   PHE   B C   
3773 C  C   B PHE   B 6   ? 0.2830 0.3046 0.2596 -0.0872 0.0226  -0.0034 6   PHE   B C   
3774 O  O   A PHE   B 6   ? 0.3674 0.3897 0.3026 -0.0976 0.0490  -0.0011 6   PHE   B O   
3775 O  O   B PHE   B 6   ? 0.2925 0.3153 0.2768 -0.0777 0.0220  -0.0014 6   PHE   B O   
3776 C  CB  A PHE   B 6   ? 0.2717 0.3138 0.1947 -0.1073 0.0013  0.0268  6   PHE   B CB  
3777 C  CB  B PHE   B 6   ? 0.2565 0.2911 0.2185 -0.0795 0.0025  0.0136  6   PHE   B CB  
3778 C  CG  A PHE   B 6   ? 0.2440 0.2881 0.1838 -0.1086 -0.0191 0.0316  6   PHE   B CG  
3779 C  CG  B PHE   B 6   ? 0.2466 0.2802 0.2093 -0.0755 -0.0066 0.0168  6   PHE   B CG  
3780 C  CD1 A PHE   B 6   ? 0.2422 0.2619 0.1643 -0.1093 -0.0334 0.0332  6   PHE   B CD1 
3781 C  CD1 B PHE   B 6   ? 0.2461 0.2707 0.2013 -0.0732 -0.0128 0.0182  6   PHE   B CD1 
3782 C  CD2 A PHE   B 6   ? 0.2258 0.2845 0.1814 -0.0981 -0.0242 0.0524  6   PHE   B CD2 
3783 C  CD2 B PHE   B 6   ? 0.2400 0.2779 0.2047 -0.0704 -0.0091 0.0261  6   PHE   B CD2 
3784 C  CE1 A PHE   B 6   ? 0.2408 0.2415 0.1735 -0.1012 -0.0375 0.0420  6   PHE   B CE1 
3785 C  CE1 B PHE   B 6   ? 0.2457 0.2634 0.2017 -0.0687 -0.0149 0.0202  6   PHE   B CE1 
3786 C  CE2 A PHE   B 6   ? 0.2302 0.2666 0.1978 -0.0878 -0.0204 0.0629  6   PHE   B CE2 
3787 C  CE2 B PHE   B 6   ? 0.2409 0.2720 0.2083 -0.0656 -0.0077 0.0311  6   PHE   B CE2 
3788 C  CZ  A PHE   B 6   ? 0.2340 0.2466 0.1853 -0.0914 -0.0359 0.0544  6   PHE   B CZ  
3789 C  CZ  B PHE   B 6   ? 0.2423 0.2641 0.2036 -0.0660 -0.0139 0.0253  6   PHE   B CZ  
3808 N  N   A SER   B 7   ? 0.3922 0.3626 0.3012 -0.1191 0.0893  -0.0222 7   SER   B N   
3809 N  N   B SER   B 7   ? 0.2912 0.2913 0.2747 -0.0999 0.0391  -0.0178 7   SER   B N   
3810 C  CA  A SER   B 7   ? 0.4291 0.3731 0.3550 -0.1162 0.1118  -0.0367 7   SER   B CA  
3811 C  CA  B SER   B 7   ? 0.3012 0.2912 0.3023 -0.1004 0.0466  -0.0259 7   SER   B CA  
3812 C  C   A SER   B 7   ? 0.4365 0.3632 0.3367 -0.1231 0.1257  -0.0518 7   SER   B C   
3813 C  C   B SER   B 7   ? 0.2945 0.2864 0.3020 -0.1040 0.0599  -0.0332 7   SER   B C   
3814 O  O   A SER   B 7   ? 0.4476 0.3647 0.3429 -0.1291 0.1250  -0.0542 7   SER   B O   
3815 O  O   B SER   B 7   ? 0.2982 0.2865 0.3105 -0.1099 0.0590  -0.0367 7   SER   B O   
3816 C  CB  A SER   B 7   ? 0.4454 0.3858 0.4155 -0.1125 0.1229  -0.0340 7   SER   B CB  
3817 C  CB  B SER   B 7   ? 0.3106 0.2918 0.3262 -0.1002 0.0455  -0.0225 7   SER   B CB  
3818 O  OG  A SER   B 7   ? 0.4551 0.3953 0.4600 -0.1098 0.1283  -0.0309 7   SER   B OG  
3819 O  OG  B SER   B 7   ? 0.3171 0.2929 0.3435 -0.0965 0.0450  -0.0191 7   SER   B OG  
3830 N  N   A GLY   B 8   ? 0.4342 0.3516 0.3283 -0.1163 0.1320  -0.0633 8   GLY   B N   
3831 N  N   B GLY   B 8   ? 0.2892 0.2840 0.2980 -0.0938 0.0652  -0.0373 8   GLY   B N   
3832 C  CA  A GLY   B 8   ? 0.4243 0.3324 0.3187 -0.1126 0.1316  -0.0703 8   GLY   B CA  
3833 C  CA  B GLY   B 8   ? 0.2837 0.2806 0.2933 -0.0819 0.0692  -0.0359 8   GLY   B CA  
3834 C  C   A GLY   B 8   ? 0.4103 0.3058 0.3078 -0.1132 0.1248  -0.0715 8   GLY   B C   
3835 C  C   B GLY   B 8   ? 0.2744 0.2735 0.2868 -0.0763 0.0706  -0.0355 8   GLY   B C   
3836 O  O   A GLY   B 8   ? 0.4209 0.3155 0.3332 -0.1049 0.1255  -0.0785 8   GLY   B O   
3837 O  O   B GLY   B 8   ? 0.2794 0.2755 0.3052 -0.0719 0.0705  -0.0389 8   GLY   B O   
3844 N  N   A TYR   B 9   ? 0.3925 0.2746 0.2777 -0.1123 0.0975  -0.0771 9   TYR   B N   
3845 N  N   B TYR   B 9   ? 0.2619 0.2663 0.2642 -0.0756 0.0584  -0.0394 9   TYR   B N   
3846 C  CA  A TYR   B 9   ? 0.3741 0.2418 0.2459 -0.1087 0.0719  -0.0649 9   TYR   B CA  
3847 C  CA  B TYR   B 9   ? 0.2518 0.2594 0.2385 -0.0755 0.0445  -0.0395 9   TYR   B CA  
3848 C  C   A TYR   B 9   ? 0.3620 0.2344 0.2368 -0.1108 0.0422  -0.0517 9   TYR   B C   
3849 C  C   B TYR   B 9   ? 0.2589 0.2646 0.2390 -0.0718 0.0284  -0.0380 9   TYR   B C   
3850 O  O   A TYR   B 9   ? 0.3647 0.2502 0.2612 -0.1103 0.0486  -0.0407 9   TYR   B O   
3851 O  O   B TYR   B 9   ? 0.2592 0.2719 0.2521 -0.0708 0.0325  -0.0372 9   TYR   B O   
3852 C  CB  A TYR   B 9   ? 0.3733 0.2182 0.2402 -0.1038 0.0659  -0.0616 9   TYR   B CB  
3853 C  CB  B TYR   B 9   ? 0.2400 0.2494 0.2205 -0.0775 0.0399  -0.0404 9   TYR   B CB  
3854 C  CG  A TYR   B 9   ? 0.3709 0.2001 0.2407 -0.1100 0.0591  -0.0618 9   TYR   B CG  
3855 C  CG  B TYR   B 9   ? 0.2279 0.2415 0.2106 -0.0844 0.0364  -0.0395 9   TYR   B CG  
3856 C  CD1 A TYR   B 9   ? 0.3730 0.1958 0.2469 -0.1190 0.0601  -0.0554 9   TYR   B CD1 
3857 C  CD1 B TYR   B 9   ? 0.2228 0.2382 0.2101 -0.0908 0.0364  -0.0382 9   TYR   B CD1 
3858 C  CD2 A TYR   B 9   ? 0.3651 0.1985 0.2276 -0.1038 0.0534  -0.0653 9   TYR   B CD2 
3859 C  CD2 B TYR   B 9   ? 0.2188 0.2385 0.1952 -0.0881 0.0357  -0.0416 9   TYR   B CD2 
3860 C  CE1 A TYR   B 9   ? 0.3714 0.2054 0.2430 -0.1135 0.0644  -0.0654 9   TYR   B CE1 
3861 C  CE1 B TYR   B 9   ? 0.2163 0.2380 0.2060 -0.0944 0.0376  -0.0375 9   TYR   B CE1 
3862 C  CE2 A TYR   B 9   ? 0.3668 0.1988 0.2312 -0.1012 0.0528  -0.0675 9   TYR   B CE2 
3863 C  CE2 B TYR   B 9   ? 0.2144 0.2376 0.1932 -0.0905 0.0314  -0.0429 9   TYR   B CE2 
3864 C  CZ  A TYR   B 9   ? 0.3698 0.2080 0.2417 -0.1039 0.0583  -0.0720 9   TYR   B CZ  
3865 C  CZ  B TYR   B 9   ? 0.2127 0.2395 0.1987 -0.0942 0.0294  -0.0416 9   TYR   B CZ  
3866 O  OH  A TYR   B 9   ? 0.3697 0.2143 0.2542 -0.1034 0.0618  -0.0783 9   TYR   B OH  
3867 O  OH  B TYR   B 9   ? 0.2094 0.2444 0.2083 -0.0963 0.0204  -0.0408 9   TYR   B OH  
3886 N  N   A LEU   B 10  ? 0.3497 0.2077 0.2249 -0.1143 0.0169  -0.0415 10  LEU   B N   
3887 N  N   B LEU   B 10  ? 0.2664 0.2632 0.2378 -0.0700 0.0139  -0.0332 10  LEU   B N   
3888 C  CA  A LEU   B 10  ? 0.3457 0.2027 0.2202 -0.1204 -0.0164 -0.0254 10  LEU   B CA  
3889 C  CA  B LEU   B 10  ? 0.2805 0.2682 0.2413 -0.0715 -0.0035 -0.0246 10  LEU   B CA  
3890 C  C   A LEU   B 10  ? 0.3331 0.2061 0.2147 -0.1101 -0.0347 -0.0107 10  LEU   B C   
3891 C  C   B LEU   B 10  ? 0.2812 0.2727 0.2424 -0.0684 -0.0156 -0.0226 10  LEU   B C   
3892 O  O   A LEU   B 10  ? 0.3197 0.2093 0.2098 -0.1015 -0.0345 -0.0000 10  LEU   B O   
3893 O  O   B LEU   B 10  ? 0.2704 0.2761 0.2327 -0.0654 -0.0152 -0.0226 10  LEU   B O   
3894 C  CB  A LEU   B 10  ? 0.3623 0.1974 0.2423 -0.1209 -0.0284 -0.0166 10  LEU   B CB  
3895 C  CB  B LEU   B 10  ? 0.2976 0.2704 0.2535 -0.0718 -0.0064 -0.0160 10  LEU   B CB  
3896 C  CG  A LEU   B 10  ? 0.3814 0.2053 0.2691 -0.1085 -0.0472 -0.0126 10  LEU   B CG  
3897 C  CG  B LEU   B 10  ? 0.3130 0.2742 0.2663 -0.0697 -0.0106 -0.0104 10  LEU   B CG  
3898 C  CD1 A LEU   B 10  ? 0.3954 0.2147 0.2823 -0.0969 -0.0467 -0.0163 10  LEU   B CD1 
3899 C  CD1 B LEU   B 10  ? 0.3206 0.2757 0.2729 -0.0662 -0.0099 -0.0118 10  LEU   B CD1 
3900 C  CD2 A LEU   B 10  ? 0.3847 0.2036 0.2900 -0.1103 -0.0440 0.0045  10  LEU   B CD2 
3901 C  CD2 B LEU   B 10  ? 0.3159 0.2757 0.2738 -0.0714 -0.0089 -0.0045 10  LEU   B CD2 
3924 N  N   A LYS   B 11  ? 0.3396 0.2272 0.2272 -0.0990 -0.0457 -0.0019 11  LYS   B N   
3925 N  N   B LYS   B 11  ? 0.2948 0.2773 0.2591 -0.0663 -0.0255 -0.0195 11  LYS   B N   
3926 C  CA  A LYS   B 11  ? 0.3516 0.2506 0.2774 -0.0842 -0.0440 -0.0066 11  LYS   B CA  
3927 C  CA  B LYS   B 11  ? 0.3123 0.2816 0.2899 -0.0630 -0.0302 -0.0193 11  LYS   B CA  
3928 C  C   A LYS   B 11  ? 0.3220 0.2296 0.2715 -0.0995 -0.0449 -0.0154 11  LYS   B C   
3929 C  C   B LYS   B 11  ? 0.2979 0.2554 0.2711 -0.0775 -0.0385 -0.0237 11  LYS   B C   
3930 O  O   A LYS   B 11  ? 0.3346 0.2316 0.2879 -0.1166 -0.0537 -0.0415 11  LYS   B O   
3931 O  O   B LYS   B 11  ? 0.2989 0.2648 0.2668 -0.0796 -0.0468 -0.0350 11  LYS   B O   
3932 C  CB  A LYS   B 11  ? 0.3870 0.2950 0.3480 -0.0620 -0.0432 -0.0166 11  LYS   B CB  
3933 C  CB  B LYS   B 11  ? 0.3412 0.3097 0.3457 -0.0486 -0.0274 -0.0198 11  LYS   B CB  
3934 C  CG  A LYS   B 11  ? 0.4158 0.3263 0.4214 -0.0439 -0.0435 -0.0241 11  LYS   B CG  
3935 C  CG  B LYS   B 11  ? 0.3653 0.3315 0.4038 -0.0372 -0.0259 -0.0207 11  LYS   B CG  
3936 C  CD  A LYS   B 11  ? 0.4377 0.3469 0.4833 -0.0292 -0.0414 -0.0272 11  LYS   B CD  
3937 C  CD  B LYS   B 11  ? 0.3837 0.3464 0.4531 -0.0283 -0.0240 -0.0201 11  LYS   B CD  
3938 C  CE  A LYS   B 11  ? 0.4527 0.3621 0.5293 -0.0204 -0.0402 -0.0300 11  LYS   B CE  
3939 C  CE  B LYS   B 11  ? 0.3960 0.3573 0.4891 -0.0232 -0.0231 -0.0194 11  LYS   B CE  
3940 N  NZ  A LYS   B 11  ? 0.4612 0.3708 0.5542 -0.0161 -0.0412 -0.0298 11  LYS   B NZ  
3941 N  NZ  B LYS   B 11  ? 0.4026 0.3632 0.5086 -0.0209 -0.0229 -0.0181 11  LYS   B NZ  
3968 N  N   . LEU   B 12  ? 0.2790 0.2202 0.2650 -0.0871 -0.0443 -0.0258 12  LEU   B N   
3969 C  CA  . LEU   B 12  ? 0.2484 0.1963 0.2687 -0.0708 -0.0245 -0.0248 12  LEU   B CA  
3970 C  C   . LEU   B 12  ? 0.2300 0.1966 0.2854 -0.0713 -0.0372 -0.0197 12  LEU   B C   
3971 O  O   . LEU   B 12  ? 0.2298 0.1954 0.3164 -0.0720 -0.0572 -0.0152 12  LEU   B O   
3972 C  CB  . LEU   B 12  ? 0.2468 0.1784 0.2637 -0.0499 -0.0154 -0.0240 12  LEU   B CB  
3973 C  CG  . LEU   B 12  ? 0.2508 0.1680 0.2642 -0.0482 -0.0109 -0.0137 12  LEU   B CG  
3974 C  CD1 . LEU   B 12  ? 0.2642 0.1656 0.2596 -0.0353 -0.0169 0.0087  12  LEU   B CD1 
3975 C  CD2 . LEU   B 12  ? 0.2523 0.1764 0.2688 -0.0488 -0.0085 -0.0260 12  LEU   B CD2 
3988 N  N   . THR   B 13  ? 0.2274 0.2048 0.2831 -0.0716 -0.0443 -0.0293 13  THR   B N   
3989 C  CA  . THR   B 13  ? 0.2265 0.2109 0.2784 -0.0803 -0.0690 -0.0177 13  THR   B CA  
3990 C  C   . THR   B 13  ? 0.2752 0.2351 0.3000 -0.0890 -0.0876 -0.0071 13  THR   B C   
3991 O  O   . THR   B 13  ? 0.2979 0.2374 0.3105 -0.0821 -0.0637 -0.0083 13  THR   B O   
3992 C  CB  . THR   B 13  ? 0.2099 0.2041 0.2866 -0.0647 -0.0616 -0.0120 13  THR   B CB  
3993 O  OG1 . THR   B 13  ? 0.2010 0.1913 0.2920 -0.0500 -0.0517 -0.0088 13  THR   B OG1 
3994 C  CG2 . THR   B 13  ? 0.2183 0.2098 0.2944 -0.0590 -0.0513 -0.0008 13  THR   B CG2 
4002 N  N   A ASP   B 14  ? 0.2911 0.2491 0.3125 -0.0977 -0.1176 0.0101  14  ASP   B N   
4003 N  N   B ASP   B 14  ? 0.2882 0.2472 0.3108 -0.0902 -0.0959 0.0046  14  ASP   B N   
4004 C  CA  A ASP   B 14  ? 0.3041 0.2659 0.3381 -0.0977 -0.1241 0.0216  14  ASP   B CA  
4005 C  CA  B ASP   B 14  ? 0.2984 0.2593 0.3282 -0.0877 -0.0959 0.0131  14  ASP   B CA  
4006 C  C   A ASP   B 14  ? 0.2925 0.2453 0.2974 -0.0984 -0.1068 0.0234  14  ASP   B C   
4007 C  C   B ASP   B 14  ? 0.2844 0.2401 0.2932 -0.0874 -0.0969 0.0184  14  ASP   B C   
4008 O  O   A ASP   B 14  ? 0.3184 0.2616 0.3054 -0.0983 -0.0915 0.0365  14  ASP   B O   
4009 O  O   B ASP   B 14  ? 0.2973 0.2453 0.2927 -0.0872 -0.0923 0.0252  14  ASP   B O   
4010 C  CB  A ASP   B 14  ? 0.3258 0.3078 0.4119 -0.0923 -0.1351 0.0222  14  ASP   B CB  
4011 C  CB  B ASP   B 14  ? 0.3194 0.2906 0.3829 -0.0836 -0.0911 0.0143  14  ASP   B CB  
4012 C  CG  A ASP   B 14  ? 0.3489 0.3411 0.4864 -0.0859 -0.1301 0.0117  14  ASP   B CG  
4013 C  CG  B ASP   B 14  ? 0.3380 0.3150 0.4332 -0.0790 -0.0837 0.0108  14  ASP   B CG  
4014 O  OD1 A ASP   B 14  ? 0.3608 0.3482 0.5065 -0.0873 -0.1276 0.0022  14  ASP   B OD1 
4015 O  OD1 B ASP   B 14  ? 0.3457 0.3231 0.4475 -0.0768 -0.0802 0.0076  14  ASP   B OD1 
4016 O  OD2 A ASP   B 14  ? 0.3542 0.3580 0.5214 -0.0836 -0.1246 0.0126  14  ASP   B OD2 
4017 O  OD2 B ASP   B 14  ? 0.3428 0.3237 0.4538 -0.0804 -0.0808 0.0111  14  ASP   B OD2 
4026 N  N   . ASN   B 15  ? 0.2598 0.2182 0.2748 -0.0784 -0.0999 0.0224  15  ASN   B N   
4027 C  CA  . ASN   B 15  ? 0.2140 0.1843 0.2547 -0.0549 -0.0759 0.0107  15  ASN   B CA  
4028 C  C   . ASN   B 15  ? 0.1909 0.1694 0.2471 -0.0406 -0.0562 0.0060  15  ASN   B C   
4029 O  O   . ASN   B 15  ? 0.1832 0.1549 0.2587 -0.0355 -0.0591 -0.0027 15  ASN   B O   
4030 C  CB  . ASN   B 15  ? 0.2034 0.1733 0.2723 -0.0303 -0.0669 0.0106  15  ASN   B CB  
4031 C  CG  . ASN   B 15  ? 0.1802 0.1726 0.2875 -0.0310 -0.0368 0.0176  15  ASN   B CG  
4032 O  OD1 . ASN   B 15  ? 0.1863 0.2048 0.3206 -0.0492 -0.0342 0.0157  15  ASN   B OD1 
4033 N  ND2 . ASN   B 15  ? 0.1814 0.1489 0.2776 -0.0179 -0.0083 -0.0052 15  ASN   B ND2 
4041 N  N   . VAL   B 16  ? 0.1836 0.1599 0.2481 -0.0453 -0.0624 0.0072  16  VAL   B N   
4042 C  CA  . VAL   B 16  ? 0.1838 0.1583 0.2410 -0.0383 -0.0434 -0.0187 16  VAL   B CA  
4043 C  C   . VAL   B 16  ? 0.1813 0.1729 0.2258 -0.0461 -0.0402 -0.0045 16  VAL   B C   
4044 O  O   . VAL   B 16  ? 0.1877 0.1810 0.2509 -0.0372 -0.0440 -0.0200 16  VAL   B O   
4045 C  CB  . VAL   B 16  ? 0.1844 0.1543 0.2465 -0.0239 -0.0325 -0.0139 16  VAL   B CB  
4046 C  CG1 . VAL   B 16  ? 0.1947 0.1546 0.2399 -0.0085 -0.0204 -0.0056 16  VAL   B CG1 
4047 C  CG2 . VAL   B 16  ? 0.1887 0.1528 0.2609 -0.0077 -0.0242 -0.0134 16  VAL   B CG2 
4057 N  N   . TYR   B 17  ? 0.1909 0.1872 0.2231 -0.0378 -0.0290 -0.0064 17  TYR   B N   
4058 C  CA  . TYR   B 17  ? 0.2014 0.2013 0.2222 -0.0515 -0.0445 0.0109  17  TYR   B CA  
4059 C  C   . TYR   B 17  ? 0.1940 0.1697 0.2259 -0.0487 -0.0243 -0.0020 17  TYR   B C   
4060 O  O   . TYR   B 17  ? 0.1917 0.1762 0.2300 -0.0452 -0.0327 -0.0308 17  TYR   B O   
4061 C  CB  . TYR   B 17  ? 0.2465 0.2638 0.2564 -0.0422 -0.0520 0.0406  17  TYR   B CB  
4062 C  CG  . TYR   B 17  ? 0.2888 0.3297 0.3052 -0.0322 -0.0706 0.0614  17  TYR   B CG  
4063 C  CD1 . TYR   B 17  ? 0.3107 0.3569 0.3371 -0.0318 -0.0809 0.0701  17  TYR   B CD1 
4064 C  CD2 . TYR   B 17  ? 0.3167 0.3627 0.3416 -0.0233 -0.0776 0.0664  17  TYR   B CD2 
4065 C  CE1 . TYR   B 17  ? 0.3327 0.3874 0.3624 -0.0219 -0.0904 0.0758  17  TYR   B CE1 
4066 C  CE2 . TYR   B 17  ? 0.3374 0.3903 0.3648 -0.0131 -0.0906 0.0786  17  TYR   B CE2 
4067 C  CZ  . TYR   B 17  ? 0.3472 0.4032 0.3791 -0.0114 -0.0972 0.0816  17  TYR   B CZ  
4068 O  OH  . TYR   B 17  ? 0.3623 0.4178 0.3934 -0.0041 -0.1069 0.0857  17  TYR   B OH  
4078 N  N   . ILE   B 18  ? 0.1954 0.1758 0.2126 -0.0400 -0.0155 -0.0096 18  ILE   B N   
4079 C  CA  . ILE   B 18  ? 0.1973 0.1654 0.2195 -0.0443 -0.0008 -0.0315 18  ILE   B CA  
4080 C  C   . ILE   B 18  ? 0.2052 0.1716 0.2218 -0.0519 -0.0084 -0.0416 18  ILE   B C   
4081 O  O   . ILE   B 18  ? 0.2173 0.1877 0.2225 -0.0483 -0.0021 -0.0434 18  ILE   B O   
4082 C  CB  . ILE   B 18  ? 0.2052 0.1635 0.2260 -0.0462 -0.0067 -0.0176 18  ILE   B CB  
4083 C  CG1 . ILE   B 18  ? 0.2081 0.1675 0.2397 -0.0486 0.0020  -0.0151 18  ILE   B CG1 
4084 C  CG2 . ILE   B 18  ? 0.2046 0.1747 0.2371 -0.0527 -0.0214 -0.0168 18  ILE   B CG2 
4085 C  CD1 . ILE   B 18  ? 0.2170 0.1958 0.2457 -0.0413 -0.0199 0.0131  18  ILE   B CD1 
4097 N  N   . LYS   B 19  ? 0.2126 0.1703 0.2304 -0.0242 0.0277  -0.0431 19  LYS   B N   
4098 C  CA  . LYS   B 19  ? 0.2222 0.1731 0.2616 -0.0361 0.0175  -0.0534 19  LYS   B CA  
4099 C  C   . LYS   B 19  ? 0.2002 0.1751 0.2714 -0.0300 0.0292  -0.0652 19  LYS   B C   
4100 O  O   . LYS   B 19  ? 0.2040 0.1838 0.2517 -0.0226 0.0324  -0.0571 19  LYS   B O   
4101 C  CB  . LYS   B 19  ? 0.2609 0.2023 0.2747 -0.0400 0.0436  -0.0517 19  LYS   B CB  
4102 C  CG  . LYS   B 19  ? 0.2942 0.2263 0.3106 -0.0561 0.0609  -0.0576 19  LYS   B CG  
4103 C  CD  . LYS   B 19  ? 0.3331 0.2571 0.3369 -0.0635 0.0830  -0.0520 19  LYS   B CD  
4104 C  CE  . LYS   B 19  ? 0.3670 0.2802 0.3649 -0.0669 0.0867  -0.0574 19  LYS   B CE  
4105 N  NZ  . LYS   B 19  ? 0.3826 0.2936 0.3752 -0.0700 0.0950  -0.0604 19  LYS   B NZ  
4119 N  N   . ASN   B 20  ? 0.2020 0.1877 0.2961 -0.0218 0.0356  -0.0685 20  ASN   B N   
4120 C  CA  . ASN   B 20  ? 0.2099 0.2000 0.3169 -0.0198 0.0408  -0.0884 20  ASN   B CA  
4121 C  C   . ASN   B 20  ? 0.2119 0.2248 0.3067 -0.0230 0.0524  -0.0893 20  ASN   B C   
4122 O  O   . ASN   B 20  ? 0.2340 0.2640 0.3223 -0.0364 0.0475  -0.0880 20  ASN   B O   
4123 C  CB  . ASN   B 20  ? 0.2382 0.2067 0.3582 0.0128  0.0321  -0.0938 20  ASN   B CB  
4124 C  CG  . ASN   B 20  ? 0.2691 0.2177 0.3826 0.0390  0.0262  -0.1034 20  ASN   B CG  
4125 O  OD1 . ASN   B 20  ? 0.2999 0.2421 0.4011 0.0516  0.0168  -0.1027 20  ASN   B OD1 
4126 N  ND2 . ASN   B 20  ? 0.2664 0.2209 0.3839 0.0366  0.0100  -0.1047 20  ASN   B ND2 
4133 N  N   A ALA   B 21  ? 0.2123 0.2094 0.3032 -0.0311 0.0531  -0.0829 21  ALA   B N   
4134 N  N   B ALA   B 21  ? 0.2143 0.2153 0.2923 -0.0277 0.0517  -0.0808 21  ALA   B N   
4135 C  CA  A ALA   B 21  ? 0.2230 0.2136 0.3054 -0.0351 0.0491  -0.0692 21  ALA   B CA  
4136 C  CA  B ALA   B 21  ? 0.2210 0.2143 0.2846 -0.0322 0.0486  -0.0694 21  ALA   B CA  
4137 C  C   A ALA   B 21  ? 0.2235 0.1960 0.2973 -0.0320 0.0496  -0.0543 21  ALA   B C   
4138 C  C   B ALA   B 21  ? 0.2208 0.1986 0.2795 -0.0311 0.0468  -0.0573 21  ALA   B C   
4139 O  O   A ALA   B 21  ? 0.2277 0.1823 0.3013 -0.0469 0.0461  -0.0550 21  ALA   B O   
4140 O  O   B ALA   B 21  ? 0.2239 0.1942 0.2749 -0.0378 0.0457  -0.0580 21  ALA   B O   
4141 C  CB  A ALA   B 21  ? 0.2321 0.2387 0.3177 -0.0452 0.0506  -0.0529 21  ALA   B CB  
4142 C  CB  B ALA   B 21  ? 0.2256 0.2285 0.2880 -0.0394 0.0492  -0.0610 21  ALA   B CB  
4153 N  N   . ASP   B 22  ? 0.2133 0.1824 0.2860 -0.0306 0.0399  -0.0487 22  ASP   B N   
4154 C  CA  . ASP   B 22  ? 0.2023 0.1728 0.2759 -0.0195 0.0225  -0.0319 22  ASP   B CA  
4155 C  C   . ASP   B 22  ? 0.1920 0.1650 0.2413 -0.0248 0.0185  -0.0201 22  ASP   B C   
4156 O  O   . ASP   B 22  ? 0.1942 0.1714 0.2398 -0.0193 0.0145  -0.0196 22  ASP   B O   
4157 C  CB  . ASP   B 22  ? 0.2097 0.1754 0.3127 -0.0048 0.0226  -0.0220 22  ASP   B CB  
4158 C  CG  . ASP   B 22  ? 0.2096 0.1969 0.3559 0.0088  0.0032  -0.0162 22  ASP   B CG  
4159 O  OD1 . ASP   B 22  ? 0.2198 0.1864 0.3551 0.0073  -0.0177 -0.0134 22  ASP   B OD1 
4160 O  OD2 . ASP   B 22  ? 0.2116 0.2249 0.4025 0.0128  -0.0135 -0.0292 22  ASP   B OD2 
4166 N  N   . ILE   B 23  ? 0.1881 0.1525 0.2224 -0.0166 0.0015  0.0101  23  ILE   B N   
4167 C  CA  . ILE   B 23  ? 0.1822 0.1484 0.2120 -0.0128 -0.0048 0.0050  23  ILE   B CA  
4168 C  C   . ILE   B 23  ? 0.1721 0.1514 0.1995 -0.0104 -0.0071 0.0020  23  ILE   B C   
4169 O  O   . ILE   B 23  ? 0.1631 0.1465 0.1931 -0.0118 -0.0120 0.0067  23  ILE   B O   
4170 C  CB  . ILE   B 23  ? 0.1783 0.1530 0.2114 -0.0199 -0.0039 0.0231  23  ILE   B CB  
4171 C  CG1 . ILE   B 23  ? 0.1730 0.1610 0.2267 -0.0128 -0.0009 0.0247  23  ILE   B CG1 
4172 C  CG2 . ILE   B 23  ? 0.1839 0.1737 0.2194 -0.0181 0.0019  0.0188  23  ILE   B CG2 
4173 C  CD1 . ILE   B 23  ? 0.1763 0.1749 0.2315 -0.0101 -0.0011 0.0273  23  ILE   B CD1 
4185 N  N   . VAL   B 24  ? 0.1731 0.1489 0.2035 -0.0079 -0.0070 -0.0027 24  VAL   B N   
4186 C  CA  . VAL   B 24  ? 0.1712 0.1541 0.2231 -0.0051 -0.0209 -0.0029 24  VAL   B CA  
4187 C  C   . VAL   B 24  ? 0.1679 0.1605 0.2218 -0.0121 -0.0189 0.0005  24  VAL   B C   
4188 O  O   . VAL   B 24  ? 0.1649 0.1734 0.2324 -0.0193 -0.0067 0.0068  24  VAL   B O   
4189 C  CB  . VAL   B 24  ? 0.1806 0.1656 0.2285 0.0033  -0.0210 0.0017  24  VAL   B CB  
4190 C  CG1 . VAL   B 24  ? 0.1725 0.1677 0.2578 -0.0127 -0.0174 0.0006  24  VAL   B CG1 
4191 C  CG2 . VAL   B 24  ? 0.1906 0.1952 0.2212 0.0095  -0.0172 -0.0048 24  VAL   B CG2 
4201 N  N   . GLU   B 25  ? 0.1889 0.1751 0.2248 -0.0124 -0.0052 0.0004  25  GLU   B N   
4202 C  CA  . GLU   B 25  ? 0.2017 0.2051 0.2502 -0.0029 0.0071  -0.0107 25  GLU   B CA  
4203 C  C   . GLU   B 25  ? 0.1933 0.2007 0.2042 -0.0163 0.0137  -0.0025 25  GLU   B C   
4204 O  O   . GLU   B 25  ? 0.1988 0.2196 0.2245 -0.0186 0.0197  0.0038  25  GLU   B O   
4205 C  CB  . GLU   B 25  ? 0.2437 0.2574 0.3453 0.0262  0.0233  -0.0124 25  GLU   B CB  
4206 C  CG  . GLU   B 25  ? 0.2856 0.3187 0.4550 0.0305  0.0245  -0.0148 25  GLU   B CG  
4207 C  CD  . GLU   B 25  ? 0.3303 0.3750 0.5466 0.0268  0.0235  -0.0183 25  GLU   B CD  
4208 O  OE1 . GLU   B 25  ? 0.3501 0.3964 0.5787 0.0304  0.0289  -0.0177 25  GLU   B OE1 
4209 O  OE2 . GLU   B 25  ? 0.3445 0.3934 0.5775 0.0271  0.0203  -0.0240 25  GLU   B OE2 
4216 N  N   A GLU   B 26  ? 0.1917 0.1903 0.1840 -0.0335 0.0073  -0.0008 26  GLU   B N   
4217 N  N   B GLU   B 26  ? 0.1917 0.1914 0.1953 -0.0290 0.0069  -0.0019 26  GLU   B N   
4218 C  CA  A GLU   B 26  ? 0.1963 0.2081 0.1954 -0.0399 -0.0075 0.0035  26  GLU   B CA  
4219 C  CA  B GLU   B 26  ? 0.1923 0.1931 0.2022 -0.0374 -0.0042 0.0007  26  GLU   B CA  
4220 C  C   A GLU   B 26  ? 0.1839 0.2036 0.1755 -0.0305 -0.0010 0.0092  26  GLU   B C   
4221 C  C   B GLU   B 26  ? 0.1831 0.1924 0.1805 -0.0310 0.0013  0.0083  26  GLU   B C   
4222 O  O   A GLU   B 26  ? 0.2009 0.2174 0.1888 -0.0285 0.0000  0.0129  26  GLU   B O   
4223 O  O   B GLU   B 26  ? 0.1920 0.2006 0.1830 -0.0295 0.0008  0.0099  26  GLU   B O   
4224 C  CB  A GLU   B 26  ? 0.2286 0.2283 0.2311 -0.0444 0.0082  0.0333  26  GLU   B CB  
4225 C  CB  B GLU   B 26  ? 0.2079 0.1942 0.2333 -0.0476 -0.0060 0.0085  26  GLU   B CB  
4226 C  CG  A GLU   B 26  ? 0.2725 0.2671 0.2984 -0.0422 0.0347  0.0307  26  GLU   B CG  
4227 C  CG  B GLU   B 26  ? 0.2286 0.2048 0.2783 -0.0559 -0.0038 -0.0024 26  GLU   B CG  
4228 C  CD  A GLU   B 26  ? 0.2961 0.2891 0.3314 -0.0556 0.0709  0.0285  26  GLU   B CD  
4229 C  CD  B GLU   B 26  ? 0.2314 0.2002 0.2936 -0.0765 -0.0059 -0.0227 26  GLU   B CD  
4230 O  OE1 A GLU   B 26  ? 0.3129 0.2864 0.3511 -0.0635 0.1127  0.0461  26  GLU   B OE1 
4231 O  OE1 B GLU   B 26  ? 0.2267 0.1928 0.3193 -0.1012 0.0031  -0.0448 26  GLU   B OE1 
4232 O  OE2 A GLU   B 26  ? 0.2963 0.3037 0.3594 -0.0597 0.0756  0.0289  26  GLU   B OE2 
4233 O  OE2 B GLU   B 26  ? 0.2359 0.1996 0.2995 -0.0718 -0.0038 -0.0119 26  GLU   B OE2 
4246 N  N   . ALA   B 27  ? 0.1702 0.1811 0.1779 -0.0271 0.0073  0.0167  27  ALA   B N   
4247 C  CA  . ALA   B 27  ? 0.1642 0.1762 0.1904 -0.0193 -0.0048 0.0314  27  ALA   B CA  
4248 C  C   . ALA   B 27  ? 0.1640 0.1914 0.2241 -0.0220 0.0026  0.0422  27  ALA   B C   
4249 O  O   . ALA   B 27  ? 0.1686 0.2005 0.2425 -0.0144 0.0006  0.0463  27  ALA   B O   
4250 C  CB  . ALA   B 27  ? 0.1754 0.1629 0.1981 -0.0147 -0.0016 0.0316  27  ALA   B CB  
4257 N  N   . LYS   B 28  ? 0.1593 0.2138 0.2613 -0.0291 0.0126  0.0628  28  LYS   B N   
4258 C  CA  . LYS   B 28  ? 0.1826 0.2569 0.2775 -0.0149 0.0444  0.0928  28  LYS   B CA  
4259 C  C   . LYS   B 28  ? 0.2093 0.2698 0.2577 -0.0052 0.0594  0.0860  28  LYS   B C   
4260 O  O   . LYS   B 28  ? 0.2337 0.2771 0.2657 -0.0019 0.0601  0.0760  28  LYS   B O   
4261 C  CB  . LYS   B 28  ? 0.2060 0.3006 0.3360 0.0033  0.0717  0.1138  28  LYS   B CB  
4262 C  CG  . LYS   B 28  ? 0.2383 0.3557 0.3919 0.0137  0.0872  0.1209  28  LYS   B CG  
4263 C  CD  . LYS   B 28  ? 0.2912 0.4177 0.4590 0.0201  0.1026  0.1266  28  LYS   B CD  
4264 C  CE  . LYS   B 28  ? 0.3314 0.4585 0.5111 0.0279  0.1050  0.1332  28  LYS   B CE  
4265 N  NZ  . LYS   B 28  ? 0.3729 0.4746 0.5401 0.0339  0.1020  0.1368  28  LYS   B NZ  
4279 N  N   . LYS   B 29  ? 0.2255 0.2888 0.2664 0.0107  0.0535  0.0701  29  LYS   B N   
4280 C  CA  . LYS   B 29  ? 0.2706 0.3214 0.2932 0.0069  0.0515  0.0624  29  LYS   B CA  
4281 C  C   . LYS   B 29  ? 0.2628 0.3155 0.2611 0.0001  0.0313  0.0629  29  LYS   B C   
4282 O  O   . LYS   B 29  ? 0.2830 0.3371 0.2740 0.0097  0.0368  0.0635  29  LYS   B O   
4283 C  CB  . LYS   B 29  ? 0.3319 0.3621 0.3812 0.0032  0.0528  0.0521  29  LYS   B CB  
4284 C  CG  . LYS   B 29  ? 0.3849 0.3981 0.4745 -0.0005 0.0508  0.0473  29  LYS   B CG  
4285 C  CD  . LYS   B 29  ? 0.4269 0.4255 0.5504 -0.0054 0.0566  0.0431  29  LYS   B CD  
4286 C  CE  . LYS   B 29  ? 0.4575 0.4431 0.6034 -0.0093 0.0635  0.0399  29  LYS   B CE  
4287 N  NZ  . LYS   B 29  ? 0.4746 0.4542 0.6333 -0.0117 0.0659  0.0361  29  LYS   B NZ  
4301 N  N   . VAL   B 30  ? 0.2286 0.2904 0.2476 -0.0205 0.0071  0.0562  30  VAL   B N   
4302 C  CA  . VAL   B 30  ? 0.2157 0.2725 0.2712 -0.0328 -0.0234 0.0615  30  VAL   B CA  
4303 C  C   . VAL   B 30  ? 0.1887 0.2553 0.2391 -0.0345 -0.0258 0.0718  30  VAL   B C   
4304 O  O   . VAL   B 30  ? 0.1937 0.2702 0.2490 -0.0314 -0.0185 0.0691  30  VAL   B O   
4305 C  CB  . VAL   B 30  ? 0.2247 0.2667 0.3299 -0.0488 -0.0462 0.0650  30  VAL   B CB  
4306 C  CG1 . VAL   B 30  ? 0.2362 0.2813 0.3465 -0.0427 -0.0338 0.0652  30  VAL   B CG1 
4307 C  CG2 . VAL   B 30  ? 0.2398 0.2647 0.3490 -0.0595 -0.0558 0.0486  30  VAL   B CG2 
4317 N  N   A LYS   B 31  ? 0.1811 0.2260 0.2507 -0.0459 -0.0265 0.0814  31  LYS   B N   
4318 N  N   B LYS   B 31  ? 0.1993 0.2428 0.2406 -0.0367 -0.0280 0.0663  31  LYS   B N   
4319 C  CA  A LYS   B 31  ? 0.1660 0.2268 0.2845 -0.0481 -0.0261 0.0844  31  LYS   B CA  
4320 C  CA  B LYS   B 31  ? 0.2060 0.2389 0.2556 -0.0364 -0.0298 0.0597  31  LYS   B CA  
4321 C  C   A LYS   B 31  ? 0.1638 0.1939 0.2494 -0.0456 -0.0396 0.0707  31  LYS   B C   
4322 C  C   B LYS   B 31  ? 0.1958 0.2038 0.2251 -0.0396 -0.0384 0.0542  31  LYS   B C   
4323 O  O   A LYS   B 31  ? 0.1607 0.1979 0.2613 -0.0377 -0.0350 0.0774  31  LYS   B O   
4324 O  O   B LYS   B 31  ? 0.1982 0.2047 0.2187 -0.0381 -0.0377 0.0541  31  LYS   B O   
4325 C  CB  A LYS   B 31  ? 0.1765 0.2708 0.3428 -0.0435 0.0075  0.1047  31  LYS   B CB  
4326 C  CB  B LYS   B 31  ? 0.2281 0.2707 0.3015 -0.0311 -0.0179 0.0592  31  LYS   B CB  
4327 C  CG  A LYS   B 31  ? 0.1968 0.3138 0.4004 -0.0471 0.0287  0.1117  31  LYS   B CG  
4328 C  CG  B LYS   B 31  ? 0.2490 0.2978 0.3479 -0.0301 -0.0085 0.0551  31  LYS   B CG  
4329 C  CD  A LYS   B 31  ? 0.2279 0.3598 0.4558 -0.0444 0.0299  0.1103  31  LYS   B CD  
4330 C  CD  B LYS   B 31  ? 0.2673 0.3229 0.3911 -0.0278 -0.0042 0.0507  31  LYS   B CD  
4331 C  CE  A LYS   B 31  ? 0.2489 0.3880 0.5018 -0.0420 0.0226  0.1032  31  LYS   B CE  
4332 C  CE  B LYS   B 31  ? 0.2799 0.3392 0.4247 -0.0255 -0.0030 0.0453  31  LYS   B CE  
4333 N  NZ  A LYS   B 31  ? 0.2615 0.4047 0.5240 -0.0324 0.0132  0.0938  31  LYS   B NZ  
4334 N  NZ  B LYS   B 31  ? 0.2884 0.3490 0.4404 -0.0205 -0.0047 0.0404  31  LYS   B NZ  
4361 N  N   . PRO   B 32  ? 0.1884 0.1700 0.2111 -0.0422 -0.0439 0.0509  32  PRO   B N   
4362 C  CA  . PRO   B 32  ? 0.1975 0.1610 0.1914 -0.0406 -0.0423 0.0255  32  PRO   B CA  
4363 C  C   . PRO   B 32  ? 0.1959 0.1576 0.1950 -0.0437 -0.0533 0.0331  32  PRO   B C   
4364 O  O   . PRO   B 32  ? 0.1999 0.1480 0.2318 -0.0360 -0.0712 0.0316  32  PRO   B O   
4365 C  CB  . PRO   B 32  ? 0.2107 0.1556 0.1873 -0.0481 -0.0300 0.0185  32  PRO   B CB  
4366 C  CG  . PRO   B 32  ? 0.2251 0.1481 0.1853 -0.0362 -0.0455 0.0219  32  PRO   B CG  
4367 C  CD  . PRO   B 32  ? 0.2118 0.1531 0.1990 -0.0299 -0.0537 0.0216  32  PRO   B CD  
4375 N  N   . THR   B 33  ? 0.1974 0.1456 0.1825 -0.0404 -0.0439 0.0255  33  THR   B N   
4376 C  CA  . THR   B 33  ? 0.2083 0.1471 0.1879 -0.0428 -0.0473 0.0309  33  THR   B CA  
4377 C  C   . THR   B 33  ? 0.2092 0.1373 0.1761 -0.0403 -0.0443 0.0202  33  THR   B C   
4378 O  O   . THR   B 33  ? 0.2252 0.1424 0.1921 -0.0505 -0.0437 0.0195  33  THR   B O   
4379 C  CB  . THR   B 33  ? 0.2216 0.1574 0.2036 -0.0370 -0.0510 0.0317  33  THR   B CB  
4380 O  OG1 . THR   B 33  ? 0.2082 0.1676 0.2093 -0.0349 -0.0556 0.0377  33  THR   B OG1 
4381 C  CG2 . THR   B 33  ? 0.2462 0.1640 0.2223 -0.0213 -0.0544 0.0237  33  THR   B CG2 
4389 N  N   . VAL   B 34  ? 0.1890 0.1419 0.1551 -0.0414 -0.0437 0.0245  34  VAL   B N   
4390 C  CA  . VAL   B 34  ? 0.1773 0.1395 0.1598 -0.0352 -0.0416 0.0104  34  VAL   B CA  
4391 C  C   . VAL   B 34  ? 0.1588 0.1349 0.1528 -0.0307 -0.0281 0.0113  34  VAL   B C   
4392 O  O   . VAL   B 34  ? 0.1775 0.1393 0.1643 -0.0293 -0.0402 0.0144  34  VAL   B O   
4393 C  CB  . VAL   B 34  ? 0.1880 0.1483 0.1856 -0.0135 -0.0237 0.0094  34  VAL   B CB  
4394 C  CG1 . VAL   B 34  ? 0.1844 0.1646 0.2058 -0.0143 -0.0079 0.0003  34  VAL   B CG1 
4395 C  CG2 . VAL   B 34  ? 0.1947 0.1563 0.1991 -0.0193 -0.0247 0.0123  34  VAL   B CG2 
4405 N  N   . VAL   B 35  ? 0.1503 0.1245 0.1412 -0.0308 -0.0163 0.0133  35  VAL   B N   
4406 C  CA  . VAL   B 35  ? 0.1469 0.1289 0.1466 -0.0237 -0.0116 0.0055  35  VAL   B CA  
4407 C  C   . VAL   B 35  ? 0.1368 0.1198 0.1484 -0.0172 -0.0149 0.0109  35  VAL   B C   
4408 O  O   . VAL   B 35  ? 0.1400 0.1275 0.1549 -0.0257 0.0000  -0.0022 35  VAL   B O   
4409 C  CB  . VAL   B 35  ? 0.1479 0.1455 0.1762 -0.0222 -0.0035 0.0001  35  VAL   B CB  
4410 C  CG1 . VAL   B 35  ? 0.1406 0.1470 0.2071 -0.0265 -0.0082 -0.0058 35  VAL   B CG1 
4411 C  CG2 . VAL   B 35  ? 0.1506 0.1437 0.1894 -0.0136 -0.0027 0.0074  35  VAL   B CG2 
4421 N  N   . VAL   B 36  ? 0.1342 0.1238 0.1514 -0.0204 -0.0124 0.0111  36  VAL   B N   
4422 C  CA  . VAL   B 36  ? 0.1337 0.1218 0.1464 -0.0151 -0.0059 0.0037  36  VAL   B CA  
4423 C  C   . VAL   B 36  ? 0.1270 0.1223 0.1252 -0.0093 -0.0059 -0.0025 36  VAL   B C   
4424 O  O   . VAL   B 36  ? 0.1366 0.1341 0.1635 -0.0114 -0.0108 -0.0006 36  VAL   B O   
4425 C  CB  . VAL   B 36  ? 0.1341 0.1303 0.1559 -0.0168 -0.0025 0.0057  36  VAL   B CB  
4426 C  CG1 . VAL   B 36  ? 0.1355 0.1380 0.1658 -0.0159 -0.0105 0.0077  36  VAL   B CG1 
4427 C  CG2 . VAL   B 36  ? 0.1347 0.1339 0.1724 -0.0179 -0.0187 0.0090  36  VAL   B CG2 
4437 N  N   . ASN   B 37  ? 0.1330 0.1256 0.1333 -0.0038 -0.0064 0.0036  37  ASN   B N   
4438 C  CA  . ASN   B 37  ? 0.1368 0.1283 0.1437 -0.0019 -0.0151 0.0069  37  ASN   B CA  
4439 C  C   . ASN   B 37  ? 0.1420 0.1293 0.1550 0.0030  -0.0056 0.0028  37  ASN   B C   
4440 O  O   . ASN   B 37  ? 0.1477 0.1393 0.1538 -0.0007 0.0061  0.0122  37  ASN   B O   
4441 C  CB  . ASN   B 37  ? 0.1321 0.1306 0.1437 -0.0016 -0.0070 0.0009  37  ASN   B CB  
4442 C  CG  . ASN   B 37  ? 0.1369 0.1338 0.1521 -0.0034 -0.0165 0.0011  37  ASN   B CG  
4443 O  OD1 . ASN   B 37  ? 0.1508 0.1342 0.1778 0.0132  -0.0202 -0.0014 37  ASN   B OD1 
4444 N  ND2 . ASN   B 37  ? 0.1475 0.1332 0.1619 -0.0019 -0.0187 0.0089  37  ASN   B ND2 
4451 N  N   . ALA   B 38  ? 0.1511 0.1224 0.1607 0.0046  -0.0061 0.0048  38  ALA   B N   
4452 C  CA  . ALA   B 38  ? 0.1586 0.1332 0.1642 -0.0042 0.0000  0.0141  38  ALA   B CA  
4453 C  C   . ALA   B 38  ? 0.1557 0.1279 0.1607 -0.0032 0.0020  0.0060  38  ALA   B C   
4454 O  O   . ALA   B 38  ? 0.1670 0.1401 0.1667 0.0065  -0.0010 0.0097  38  ALA   B O   
4455 C  CB  . ALA   B 38  ? 0.1834 0.1369 0.1773 -0.0104 0.0064  0.0089  38  ALA   B CB  
4461 N  N   . ALA   B 39  ? 0.1582 0.1275 0.1472 0.0053  -0.0056 0.0076  39  ALA   B N   
4462 C  CA  . ALA   B 39  ? 0.1581 0.1371 0.1460 0.0077  -0.0096 0.0072  39  ALA   B CA  
4463 C  C   . ALA   B 39  ? 0.1711 0.1427 0.1277 0.0085  -0.0056 0.0019  39  ALA   B C   
4464 O  O   . ALA   B 39  ? 0.1748 0.1483 0.1643 -0.0042 -0.0106 0.0128  39  ALA   B O   
4465 C  CB  . ALA   B 39  ? 0.1502 0.1385 0.1609 -0.0010 -0.0024 0.0071  39  ALA   B CB  
4471 N  N   . ASN   B 40  ? 0.1733 0.1621 0.1294 0.0036  -0.0018 -0.0038 40  ASN   B N   
4472 C  CA  . ASN   B 40  ? 0.1848 0.1642 0.1451 0.0089  -0.0112 -0.0032 40  ASN   B CA  
4473 C  C   . ASN   B 40  ? 0.1892 0.1589 0.1312 0.0102  -0.0114 0.0064  40  ASN   B C   
4474 O  O   . ASN   B 40  ? 0.1785 0.1555 0.1430 0.0102  -0.0131 0.0037  40  ASN   B O   
4475 C  CB  . ASN   B 40  ? 0.1904 0.1675 0.1677 0.0093  -0.0168 0.0151  40  ASN   B CB  
4476 C  CG  . ASN   B 40  ? 0.1953 0.1689 0.2000 0.0070  -0.0252 0.0169  40  ASN   B CG  
4477 O  OD1 . ASN   B 40  ? 0.1944 0.1632 0.2831 0.0063  -0.0360 0.0216  40  ASN   B OD1 
4478 N  ND2 . ASN   B 40  ? 0.2024 0.1666 0.1996 0.0102  -0.0208 0.0130  40  ASN   B ND2 
4485 N  N   . VAL   B 41  ? 0.1961 0.1633 0.1451 0.0167  0.0112  0.0068  41  VAL   B N   
4486 C  CA  . VAL   B 41  ? 0.2002 0.1778 0.1471 0.0097  0.0056  0.0006  41  VAL   B CA  
4487 C  C   . VAL   B 41  ? 0.1943 0.1776 0.1341 0.0177  -0.0008 -0.0021 41  VAL   B C   
4488 O  O   . VAL   B 41  ? 0.1905 0.1768 0.1577 0.0163  -0.0070 -0.0035 41  VAL   B O   
4489 C  CB  . VAL   B 41  ? 0.2176 0.1949 0.1766 -0.0021 0.0234  -0.0164 41  VAL   B CB  
4490 C  CG1 . VAL   B 41  ? 0.2160 0.1968 0.1899 -0.0072 0.0356  -0.0181 41  VAL   B CG1 
4491 C  CG2 . VAL   B 41  ? 0.2307 0.2223 0.1870 -0.0118 0.0194  -0.0067 41  VAL   B CG2 
4501 N  N   . TYR   B 42  ? 0.2096 0.1734 0.1386 0.0225  -0.0147 0.0024  42  TYR   B N   
4502 C  CA  . TYR   B 42  ? 0.2145 0.1768 0.1310 0.0210  -0.0253 -0.0110 42  TYR   B CA  
4503 C  C   . TYR   B 42  ? 0.1964 0.1638 0.1401 0.0259  -0.0228 -0.0046 42  TYR   B C   
4504 O  O   . TYR   B 42  ? 0.1899 0.1756 0.1862 0.0168  -0.0236 -0.0167 42  TYR   B O   
4505 C  CB  . TYR   B 42  ? 0.2365 0.2059 0.1480 0.0166  -0.0214 0.0013  42  TYR   B CB  
4506 C  CG  . TYR   B 42  ? 0.2344 0.2168 0.1464 0.0047  -0.0253 0.0100  42  TYR   B CG  
4507 C  CD1 . TYR   B 42  ? 0.2212 0.2134 0.1268 -0.0064 -0.0075 0.0113  42  TYR   B CD1 
4508 C  CD2 . TYR   B 42  ? 0.2388 0.2223 0.1738 0.0080  -0.0195 0.0132  42  TYR   B CD2 
4509 C  CE1 . TYR   B 42  ? 0.2243 0.2235 0.1372 -0.0035 -0.0130 0.0075  42  TYR   B CE1 
4510 C  CE2 . TYR   B 42  ? 0.2357 0.2344 0.1726 0.0063  0.0051  0.0268  42  TYR   B CE2 
4511 C  CZ  . TYR   B 42  ? 0.2362 0.2404 0.1636 0.0155  0.0091  0.0054  42  TYR   B CZ  
4512 O  OH  . TYR   B 42  ? 0.2598 0.2647 0.1987 0.0263  0.0062  0.0108  42  TYR   B OH  
4522 N  N   . LEU   B 43  ? 0.1823 0.1484 0.1377 0.0103  -0.0175 -0.0055 43  LEU   B N   
4523 C  CA  . LEU   B 43  ? 0.1790 0.1482 0.1361 0.0058  -0.0175 -0.0063 43  LEU   B CA  
4524 C  C   . LEU   B 43  ? 0.1820 0.1501 0.1505 0.0058  -0.0166 -0.0027 43  LEU   B C   
4525 O  O   . LEU   B 43  ? 0.1786 0.1561 0.1799 0.0039  -0.0207 0.0052  43  LEU   B O   
4526 C  CB  . LEU   B 43  ? 0.1684 0.1416 0.1586 0.0007  -0.0186 -0.0058 43  LEU   B CB  
4527 C  CG  . LEU   B 43  ? 0.1733 0.1434 0.1746 0.0002  -0.0233 -0.0069 43  LEU   B CG  
4528 C  CD1 . LEU   B 43  ? 0.1853 0.1498 0.2054 -0.0055 -0.0392 -0.0049 43  LEU   B CD1 
4529 C  CD2 . LEU   B 43  ? 0.1702 0.1466 0.1749 -0.0070 -0.0207 0.0001  43  LEU   B CD2 
4541 N  N   . LYS   B 44  ? 0.1781 0.1490 0.1503 0.0124  -0.0049 -0.0001 44  LYS   B N   
4542 C  CA  . LYS   B 44  ? 0.1900 0.1595 0.1619 0.0183  -0.0098 0.0033  44  LYS   B CA  
4543 C  C   . LYS   B 44  ? 0.1847 0.1552 0.1647 0.0194  -0.0165 -0.0031 44  LYS   B C   
4544 O  O   . LYS   B 44  ? 0.2012 0.1545 0.1874 0.0087  -0.0108 0.0029  44  LYS   B O   
4545 C  CB  . LYS   B 44  ? 0.2148 0.1887 0.1784 0.0229  -0.0297 0.0008  44  LYS   B CB  
4546 C  CG  . LYS   B 44  ? 0.2551 0.2180 0.2325 0.0094  -0.0535 0.0143  44  LYS   B CG  
4547 C  CD  . LYS   B 44  ? 0.2958 0.2460 0.3088 -0.0039 -0.0642 0.0165  44  LYS   B CD  
4548 C  CE  . LYS   B 44  ? 0.3304 0.2695 0.3675 -0.0046 -0.0689 0.0327  44  LYS   B CE  
4549 N  NZ  . LYS   B 44  ? 0.3363 0.2709 0.3919 -0.0046 -0.0750 0.0477  44  LYS   B NZ  
4563 N  N   . HIS   B 45  ? 0.1714 0.1605 0.1594 0.0059  -0.0135 0.0069  45  HIS   B N   
4564 C  CA  . HIS   B 45  ? 0.1743 0.1565 0.1741 0.0040  -0.0100 -0.0056 45  HIS   B CA  
4565 C  C   . HIS   B 45  ? 0.1970 0.1762 0.2109 0.0201  -0.0201 -0.0057 45  HIS   B C   
4566 O  O   . HIS   B 45  ? 0.2146 0.2090 0.2555 0.0467  0.0086  0.0013  45  HIS   B O   
4567 C  CB  . HIS   B 45  ? 0.1597 0.1599 0.1687 -0.0044 -0.0134 -0.0038 45  HIS   B CB  
4568 C  CG  . HIS   B 45  ? 0.1662 0.1550 0.1688 -0.0047 -0.0141 -0.0021 45  HIS   B CG  
4569 N  ND1 . HIS   B 45  ? 0.1737 0.1481 0.1669 0.0050  -0.0241 -0.0054 45  HIS   B ND1 
4570 C  CD2 . HIS   B 45  ? 0.1748 0.1533 0.1681 -0.0056 -0.0176 0.0012  45  HIS   B CD2 
4571 C  CE1 . HIS   B 45  ? 0.1808 0.1349 0.1509 0.0041  -0.0224 -0.0093 45  HIS   B CE1 
4572 N  NE2 . HIS   B 45  ? 0.1847 0.1451 0.1606 -0.0008 -0.0229 -0.0042 45  HIS   B NE2 
4580 N  N   A GLY   B 46  ? 0.2040 0.1673 0.2391 0.0235  -0.0350 0.0021  46  GLY   B N   
4581 N  N   B GLY   B 46  ? 0.2060 0.1804 0.2246 0.0195  -0.0307 0.0010  46  GLY   B N   
4582 C  CA  A GLY   B 46  ? 0.2187 0.1865 0.2720 0.0159  -0.0398 -0.0025 46  GLY   B CA  
4583 C  CA  B GLY   B 46  ? 0.2151 0.1935 0.2439 0.0142  -0.0355 0.0024  46  GLY   B CA  
4584 C  C   A GLY   B 46  ? 0.2165 0.2034 0.3110 0.0174  -0.0370 0.0002  46  GLY   B C   
4585 C  C   B GLY   B 46  ? 0.2166 0.2061 0.2721 0.0128  -0.0336 0.0068  46  GLY   B C   
4586 O  O   A GLY   B 46  ? 0.2178 0.2199 0.3889 0.0229  -0.0160 -0.0228 46  GLY   B O   
4587 O  O   B GLY   B 46  ? 0.2199 0.2149 0.2949 0.0157  -0.0257 0.0090  46  GLY   B O   
4594 N  N   . GLY   B 47  ? 0.2172 0.2134 0.2888 0.0000  -0.0256 0.0026  47  GLY   B N   
4595 C  CA  . GLY   B 47  ? 0.2047 0.1822 0.2567 -0.0062 -0.0217 0.0064  47  GLY   B CA  
4596 C  C   . GLY   B 47  ? 0.1928 0.1635 0.2241 -0.0038 -0.0077 0.0022  47  GLY   B C   
4597 O  O   . GLY   B 47  ? 0.2037 0.1540 0.2256 0.0019  -0.0141 0.0053  47  GLY   B O   
4602 N  N   . GLY   B 48  ? 0.1708 0.1532 0.2184 0.0023  -0.0174 0.0130  48  GLY   B N   
4603 C  CA  . GLY   B 48  ? 0.1657 0.1504 0.2189 -0.0054 -0.0101 0.0126  48  GLY   B CA  
4604 C  C   . GLY   B 48  ? 0.1567 0.1467 0.2111 -0.0015 -0.0066 0.0028  48  GLY   B C   
4605 O  O   . GLY   B 48  ? 0.1478 0.1448 0.2284 0.0060  -0.0169 0.0032  48  GLY   B O   
4609 N  N   . VAL   B 49  ? 0.1536 0.1475 0.1931 0.0100  -0.0038 -0.0050 49  VAL   B N   
4610 C  CA  . VAL   B 49  ? 0.1566 0.1557 0.1762 0.0058  -0.0147 -0.0072 49  VAL   B CA  
4611 C  C   . VAL   B 49  ? 0.1451 0.1489 0.1614 0.0095  -0.0087 -0.0001 49  VAL   B C   
4612 O  O   . VAL   B 49  ? 0.1564 0.1559 0.1745 0.0044  -0.0070 -0.0017 49  VAL   B O   
4613 C  CB  . VAL   B 49  ? 0.1591 0.1755 0.2014 -0.0001 -0.0193 -0.0105 49  VAL   B CB  
4614 C  CG1 . VAL   B 49  ? 0.1588 0.1859 0.2071 0.0078  -0.0384 -0.0002 49  VAL   B CG1 
4615 C  CG2 . VAL   B 49  ? 0.1817 0.1914 0.2159 -0.0096 -0.0330 -0.0167 49  VAL   B CG2 
4625 N  N   . ALA   B 50  ? 0.1444 0.1436 0.1718 0.0013  -0.0073 0.0073  50  ALA   B N   
4626 C  CA  . ALA   B 50  ? 0.1450 0.1327 0.1640 0.0039  -0.0087 0.0022  50  ALA   B CA  
4627 C  C   . ALA   B 50  ? 0.1528 0.1374 0.1715 0.0054  -0.0055 -0.0004 50  ALA   B C   
4628 O  O   . ALA   B 50  ? 0.1516 0.1380 0.1762 0.0037  -0.0041 -0.0059 50  ALA   B O   
4629 C  CB  . ALA   B 50  ? 0.1577 0.1335 0.1633 -0.0026 -0.0020 0.0153  50  ALA   B CB  
4635 N  N   . GLY   B 51  ? 0.1574 0.1443 0.1870 0.0122  -0.0163 0.0039  51  GLY   B N   
4636 C  CA  . GLY   B 51  ? 0.1596 0.1487 0.1971 0.0165  -0.0191 0.0095  51  GLY   B CA  
4637 C  C   . GLY   B 51  ? 0.1613 0.1531 0.1932 0.0208  -0.0077 0.0030  51  GLY   B C   
4638 O  O   . GLY   B 51  ? 0.1548 0.1651 0.2137 0.0090  -0.0123 -0.0056 51  GLY   B O   
4642 N  N   . ALA   B 52  ? 0.1550 0.1487 0.1834 0.0136  -0.0109 0.0002  52  ALA   B N   
4643 C  CA  . ALA   B 52  ? 0.1579 0.1525 0.1848 0.0127  -0.0079 -0.0028 52  ALA   B CA  
4644 C  C   . ALA   B 52  ? 0.1491 0.1527 0.1862 0.0098  -0.0061 -0.0067 52  ALA   B C   
4645 O  O   . ALA   B 52  ? 0.1409 0.1543 0.2127 0.0085  -0.0038 -0.0027 52  ALA   B O   
4646 C  CB  . ALA   B 52  ? 0.1726 0.1542 0.1939 0.0024  0.0024  -0.0046 52  ALA   B CB  
4652 N  N   . LEU   B 53  ? 0.1424 0.1468 0.1746 0.0116  -0.0036 0.0011  53  LEU   B N   
4653 C  CA  . LEU   B 53  ? 0.1408 0.1537 0.1729 0.0099  -0.0035 0.0001  53  LEU   B CA  
4654 C  C   . LEU   B 53  ? 0.1483 0.1448 0.1678 0.0058  0.0037  -0.0000 53  LEU   B C   
4655 O  O   . LEU   B 53  ? 0.1491 0.1546 0.1845 0.0024  0.0023  0.0077  53  LEU   B O   
4656 C  CB  . LEU   B 53  ? 0.1440 0.1634 0.1856 0.0109  -0.0063 0.0137  53  LEU   B CB  
4657 C  CG  . LEU   B 53  ? 0.1437 0.1732 0.1791 0.0060  -0.0060 0.0142  53  LEU   B CG  
4658 C  CD1 . LEU   B 53  ? 0.1579 0.1883 0.2010 0.0223  -0.0053 0.0006  53  LEU   B CD1 
4659 C  CD2 . LEU   B 53  ? 0.1556 0.2083 0.1977 -0.0024 -0.0143 -0.0077 53  LEU   B CD2 
4671 N  N   . ASN   B 54  ? 0.1471 0.1357 0.1666 0.0027  -0.0096 0.0031  54  ASN   B N   
4672 C  CA  . ASN   B 54  ? 0.1520 0.1477 0.1673 0.0022  -0.0074 -0.0053 54  ASN   B CA  
4673 C  C   . ASN   B 54  ? 0.1461 0.1516 0.1961 0.0031  -0.0076 -0.0082 54  ASN   B C   
4674 O  O   . ASN   B 54  ? 0.1437 0.1614 0.2160 -0.0007 0.0012  -0.0143 54  ASN   B O   
4675 C  CB  . ASN   B 54  ? 0.1565 0.1610 0.1857 0.0035  -0.0009 -0.0037 54  ASN   B CB  
4676 C  CG  . ASN   B 54  ? 0.1540 0.1705 0.1889 0.0061  -0.0087 -0.0009 54  ASN   B CG  
4677 O  OD1 . ASN   B 54  ? 0.1489 0.1667 0.2069 0.0037  -0.0165 -0.0154 54  ASN   B OD1 
4678 N  ND2 . ASN   B 54  ? 0.1657 0.1902 0.2160 0.0024  -0.0330 0.0078  54  ASN   B ND2 
4685 N  N   . LYS   B 55  ? 0.1453 0.1607 0.2126 0.0080  -0.0119 -0.0032 55  LYS   B N   
4686 C  CA  . LYS   B 55  ? 0.1479 0.1730 0.2312 0.0110  -0.0081 -0.0118 55  LYS   B CA  
4687 C  C   . LYS   B 55  ? 0.1459 0.1752 0.2300 0.0118  -0.0042 -0.0131 55  LYS   B C   
4688 O  O   . LYS   B 55  ? 0.1455 0.1908 0.2433 0.0125  -0.0009 -0.0167 55  LYS   B O   
4689 C  CB  . LYS   B 55  ? 0.1653 0.1870 0.2848 0.0194  0.0080  -0.0057 55  LYS   B CB  
4690 C  CG  . LYS   B 55  ? 0.2034 0.2197 0.3658 0.0307  0.0180  0.0112  55  LYS   B CG  
4691 C  CD  . LYS   B 55  ? 0.2427 0.2470 0.4379 0.0461  0.0347  0.0261  55  LYS   B CD  
4692 C  CE  . LYS   B 55  ? 0.2678 0.2646 0.5019 0.0516  0.0498  0.0330  55  LYS   B CE  
4693 N  NZ  . LYS   B 55  ? 0.2714 0.2777 0.5364 0.0529  0.0412  0.0420  55  LYS   B NZ  
4707 N  N   . ALA   B 56  ? 0.1436 0.1790 0.2155 0.0065  0.0073  -0.0140 56  ALA   B N   
4708 C  CA  . ALA   B 56  ? 0.1574 0.1941 0.2211 0.0031  0.0102  -0.0135 56  ALA   B CA  
4709 C  C   . ALA   B 56  ? 0.1590 0.1900 0.2099 -0.0013 0.0143  -0.0086 56  ALA   B C   
4710 O  O   . ALA   B 56  ? 0.1664 0.2007 0.2255 0.0018  0.0271  -0.0053 56  ALA   B O   
4711 C  CB  . ALA   B 56  ? 0.1731 0.2190 0.2285 -0.0098 -0.0009 -0.0186 56  ALA   B CB  
4717 N  N   . THR   B 57  ? 0.1471 0.1765 0.2137 -0.0028 0.0198  -0.0081 57  THR   B N   
4718 C  CA  . THR   B 57  ? 0.1591 0.1780 0.2080 -0.0004 0.0215  -0.0070 57  THR   B CA  
4719 C  C   . THR   B 57  ? 0.1606 0.1867 0.2226 -0.0019 0.0244  -0.0145 57  THR   B C   
4720 O  O   . THR   B 57  ? 0.1669 0.1839 0.2333 -0.0196 0.0155  -0.0162 57  THR   B O   
4721 C  CB  . THR   B 57  ? 0.1659 0.1637 0.1828 -0.0028 0.0183  0.0040  57  THR   B CB  
4722 O  OG1 . THR   B 57  ? 0.1634 0.1551 0.2126 -0.0023 0.0168  -0.0029 57  THR   B OG1 
4723 C  CG2 . THR   B 57  ? 0.1574 0.1670 0.1837 -0.0014 0.0200  0.0040  57  THR   B CG2 
4731 N  N   . ASN   B 58  ? 0.1491 0.2084 0.2459 -0.0139 0.0139  -0.0339 58  ASN   B N   
4732 C  CA  . ASN   B 58  ? 0.1733 0.2558 0.3001 -0.0297 0.0407  -0.0262 58  ASN   B CA  
4733 C  C   . ASN   B 58  ? 0.1501 0.2256 0.2593 -0.0193 0.0002  -0.0269 58  ASN   B C   
4734 O  O   . ASN   B 58  ? 0.1516 0.2336 0.2748 -0.0155 -0.0011 -0.0270 58  ASN   B O   
4735 C  CB  . ASN   B 58  ? 0.2774 0.3478 0.4327 -0.0436 0.0908  -0.0130 58  ASN   B CB  
4736 C  CG  . ASN   B 58  ? 0.3973 0.4304 0.5838 -0.0451 0.1186  0.0139  58  ASN   B CG  
4737 O  OD1 . ASN   B 58  ? 0.4203 0.4541 0.6434 -0.0450 0.1255  0.0225  58  ASN   B OD1 
4738 N  ND2 . ASN   B 58  ? 0.5127 0.5127 0.6333 -0.0479 0.1299  0.0219  58  ASN   B ND2 
4745 N  N   . ASN   B 59  ? 0.1470 0.2055 0.2362 -0.0117 -0.0052 -0.0151 59  ASN   B N   
4746 C  CA  . ASN   B 59  ? 0.1517 0.2090 0.2321 -0.0127 -0.0140 -0.0062 59  ASN   B CA  
4747 C  C   . ASN   B 59  ? 0.1456 0.1994 0.2068 -0.0123 -0.0201 -0.0148 59  ASN   B C   
4748 O  O   . ASN   B 59  ? 0.1473 0.2012 0.2140 -0.0125 -0.0072 -0.0104 59  ASN   B O   
4749 C  CB  . ASN   B 59  ? 0.1648 0.2245 0.2505 -0.0002 -0.0275 -0.0001 59  ASN   B CB  
4750 C  CG  . ASN   B 59  ? 0.1775 0.2353 0.2479 0.0076  -0.0436 0.0048  59  ASN   B CG  
4751 O  OD1 . ASN   B 59  ? 0.1764 0.2364 0.2597 0.0038  -0.0340 0.0191  59  ASN   B OD1 
4752 N  ND2 . ASN   B 59  ? 0.1829 0.2476 0.2560 0.0017  -0.0481 -0.0059 59  ASN   B ND2 
4759 N  N   . ALA   B 60  ? 0.1489 0.1852 0.2074 -0.0123 -0.0026 -0.0147 60  ALA   B N   
4760 C  CA  . ALA   B 60  ? 0.1586 0.1734 0.2044 -0.0192 -0.0029 -0.0076 60  ALA   B CA  
4761 C  C   . ALA   B 60  ? 0.1607 0.1589 0.1908 -0.0116 -0.0134 0.0028  60  ALA   B C   
4762 O  O   . ALA   B 60  ? 0.1692 0.1660 0.2139 -0.0152 -0.0041 -0.0130 60  ALA   B O   
4763 C  CB  . ALA   B 60  ? 0.1719 0.1764 0.2206 -0.0186 0.0061  -0.0075 60  ALA   B CB  
4769 N  N   . MET   B 61  ? 0.1512 0.1537 0.1830 -0.0112 -0.0074 0.0016  61  MET   B N   
4770 C  CA  . MET   B 61  ? 0.1463 0.1508 0.1744 -0.0070 -0.0136 0.0045  61  MET   B CA  
4771 C  C   . MET   B 61  ? 0.1472 0.1508 0.1779 -0.0123 -0.0154 0.0059  61  MET   B C   
4772 O  O   . MET   B 61  ? 0.1521 0.1462 0.1785 -0.0021 -0.0080 -0.0124 61  MET   B O   
4773 C  CB  . MET   B 61  ? 0.1381 0.1530 0.1877 0.0013  -0.0056 -0.0051 61  MET   B CB  
4774 C  CG  . MET   B 61  ? 0.1391 0.1547 0.1948 -0.0013 -0.0114 0.0038  61  MET   B CG  
4775 S  SD  . MET   B 61  ? 0.1473 0.1563 0.1901 -0.0056 -0.0084 -0.0110 61  MET   B SD  
4776 C  CE  . MET   B 61  ? 0.1544 0.1791 0.2248 -0.0009 0.0013  -0.0163 61  MET   B CE  
4786 N  N   . GLN   B 62  ? 0.1487 0.1595 0.1690 -0.0041 -0.0271 0.0009  62  GLN   B N   
4787 C  CA  . GLN   B 62  ? 0.1539 0.1599 0.1668 -0.0002 -0.0218 -0.0042 62  GLN   B CA  
4788 C  C   . GLN   B 62  ? 0.1499 0.1613 0.1854 -0.0014 -0.0231 -0.0142 62  GLN   B C   
4789 O  O   . GLN   B 62  ? 0.1650 0.1582 0.1867 0.0027  -0.0288 -0.0186 62  GLN   B O   
4790 C  CB  . GLN   B 62  ? 0.1625 0.1647 0.1734 0.0078  -0.0197 -0.0044 62  GLN   B CB  
4791 C  CG  . GLN   B 62  ? 0.1674 0.1676 0.1825 0.0085  -0.0299 -0.0087 62  GLN   B CG  
4792 C  CD  . GLN   B 62  ? 0.1639 0.1638 0.1800 0.0065  -0.0295 0.0025  62  GLN   B CD  
4793 O  OE1 . GLN   B 62  ? 0.1685 0.1608 0.1934 0.0046  -0.0376 -0.0102 62  GLN   B OE1 
4794 N  NE2 . GLN   B 62  ? 0.1668 0.1695 0.1902 0.0104  -0.0256 -0.0098 62  GLN   B NE2 
4803 N  N   . VAL   B 63  ? 0.1542 0.1658 0.1983 -0.0054 -0.0255 -0.0130 63  VAL   B N   
4804 C  CA  . VAL   B 63  ? 0.1665 0.1721 0.2098 -0.0105 -0.0271 -0.0096 63  VAL   B CA  
4805 C  C   . VAL   B 63  ? 0.1711 0.1592 0.1874 -0.0178 -0.0300 -0.0256 63  VAL   B C   
4806 O  O   . VAL   B 63  ? 0.1795 0.1613 0.2014 -0.0148 -0.0400 -0.0245 63  VAL   B O   
4807 C  CB  . VAL   B 63  ? 0.1639 0.1860 0.2365 -0.0160 -0.0260 -0.0175 63  VAL   B CB  
4808 C  CG1 . VAL   B 63  ? 0.1717 0.1954 0.2454 -0.0262 -0.0179 -0.0124 63  VAL   B CG1 
4809 C  CG2 . VAL   B 63  ? 0.1587 0.2023 0.2379 -0.0103 -0.0339 -0.0280 63  VAL   B CG2 
4819 N  N   . GLU   B 64  ? 0.1650 0.1532 0.1871 -0.0119 -0.0227 -0.0157 64  GLU   B N   
4820 C  CA  . GLU   B 64  ? 0.1605 0.1468 0.1873 -0.0128 -0.0258 -0.0050 64  GLU   B CA  
4821 C  C   . GLU   B 64  ? 0.1576 0.1469 0.1810 -0.0094 -0.0288 -0.0118 64  GLU   B C   
4822 O  O   . GLU   B 64  ? 0.1663 0.1597 0.1753 -0.0072 -0.0300 -0.0162 64  GLU   B O   
4823 C  CB  . GLU   B 64  ? 0.1619 0.1585 0.1777 -0.0159 -0.0174 -0.0006 64  GLU   B CB  
4824 C  CG  . GLU   B 64  ? 0.1695 0.1570 0.1822 -0.0195 -0.0226 -0.0082 64  GLU   B CG  
4825 C  CD  . GLU   B 64  ? 0.1767 0.1743 0.1934 -0.0339 -0.0291 -0.0030 64  GLU   B CD  
4826 O  OE1 . GLU   B 64  ? 0.1752 0.1966 0.2164 -0.0346 -0.0159 -0.0233 64  GLU   B OE1 
4827 O  OE2 . GLU   B 64  ? 0.1974 0.1850 0.1974 -0.0376 -0.0385 -0.0017 64  GLU   B OE2 
4834 N  N   . SER   B 65  ? 0.1628 0.1455 0.1613 -0.0075 -0.0163 -0.0146 65  SER   B N   
4835 C  CA  . SER   B 65  ? 0.1575 0.1458 0.1560 0.0016  -0.0197 -0.0084 65  SER   B CA  
4836 C  C   . SER   B 65  ? 0.1642 0.1484 0.1662 0.0044  -0.0185 -0.0073 65  SER   B C   
4837 O  O   . SER   B 65  ? 0.1695 0.1490 0.1695 0.0016  -0.0196 -0.0149 65  SER   B O   
4838 C  CB  . SER   B 65  ? 0.1608 0.1522 0.1603 -0.0068 -0.0142 -0.0114 65  SER   B CB  
4839 O  OG  . SER   B 65  ? 0.1658 0.1542 0.1692 -0.0030 -0.0180 -0.0261 65  SER   B OG  
4845 N  N   . ASP   B 66  ? 0.1702 0.1508 0.1639 0.0026  -0.0310 -0.0131 66  ASP   B N   
4846 C  CA  . ASP   B 66  ? 0.1772 0.1563 0.1623 0.0036  -0.0393 -0.0147 66  ASP   B CA  
4847 C  C   . ASP   B 66  ? 0.1787 0.1622 0.1711 -0.0078 -0.0271 -0.0147 66  ASP   B C   
4848 O  O   . ASP   B 66  ? 0.1843 0.1690 0.1759 0.0063  -0.0251 -0.0224 66  ASP   B O   
4849 C  CB  . ASP   B 66  ? 0.1958 0.1689 0.1882 0.0141  -0.0452 -0.0187 66  ASP   B CB  
4850 C  CG  . ASP   B 66  ? 0.2231 0.1841 0.2140 0.0238  -0.0492 -0.0023 66  ASP   B CG  
4851 O  OD1 . ASP   B 66  ? 0.2479 0.1778 0.2218 0.0127  -0.0438 -0.0006 66  ASP   B OD1 
4852 O  OD2 . ASP   B 66  ? 0.2377 0.2158 0.2697 0.0475  -0.0575 -0.0116 66  ASP   B OD2 
4857 N  N   . ASP   B 67  ? 0.1731 0.1556 0.1696 -0.0109 -0.0246 -0.0170 67  ASP   B N   
4858 C  CA  . ASP   B 67  ? 0.1881 0.1449 0.1776 -0.0084 -0.0256 -0.0073 67  ASP   B CA  
4859 C  C   . ASP   B 67  ? 0.1862 0.1461 0.1920 0.0047  -0.0238 -0.0139 67  ASP   B C   
4860 O  O   . ASP   B 67  ? 0.1890 0.1558 0.1993 0.0050  -0.0125 -0.0173 67  ASP   B O   
4861 C  CB  . ASP   B 67  ? 0.2043 0.1559 0.1981 -0.0116 -0.0364 -0.0077 67  ASP   B CB  
4862 C  CG  . ASP   B 67  ? 0.2399 0.1666 0.2173 -0.0088 -0.0601 -0.0070 67  ASP   B CG  
4863 O  OD1 . ASP   B 67  ? 0.2637 0.1729 0.2381 -0.0130 -0.0592 -0.0111 67  ASP   B OD1 
4864 O  OD2 . ASP   B 67  ? 0.2511 0.1734 0.2431 0.0133  -0.0631 -0.0002 67  ASP   B OD2 
4869 N  N   . TYR   B 68  ? 0.1784 0.1527 0.1861 -0.0031 -0.0327 -0.0178 68  TYR   B N   
4870 C  CA  . TYR   B 68  ? 0.1786 0.1637 0.1924 0.0096  -0.0331 -0.0258 68  TYR   B CA  
4871 C  C   . TYR   B 68  ? 0.1726 0.1552 0.1857 0.0050  -0.0293 -0.0313 68  TYR   B C   
4872 O  O   . TYR   B 68  ? 0.1753 0.1690 0.1943 0.0081  -0.0267 -0.0351 68  TYR   B O   
4873 C  CB  . TYR   B 68  ? 0.1812 0.1860 0.1959 0.0068  -0.0413 -0.0316 68  TYR   B CB  
4874 C  CG  . TYR   B 68  ? 0.1899 0.2013 0.2098 0.0141  -0.0320 -0.0498 68  TYR   B CG  
4875 C  CD1 . TYR   B 68  ? 0.1929 0.2069 0.2242 -0.0058 -0.0347 -0.0547 68  TYR   B CD1 
4876 C  CD2 . TYR   B 68  ? 0.1910 0.2233 0.2209 0.0202  -0.0483 -0.0493 68  TYR   B CD2 
4877 C  CE1 . TYR   B 68  ? 0.1943 0.2235 0.2407 -0.0037 -0.0255 -0.0528 68  TYR   B CE1 
4878 C  CE2 . TYR   B 68  ? 0.1950 0.2323 0.2385 0.0167  -0.0360 -0.0535 68  TYR   B CE2 
4879 C  CZ  . TYR   B 68  ? 0.1902 0.2293 0.2475 0.0055  -0.0284 -0.0562 68  TYR   B CZ  
4880 O  OH  . TYR   B 68  ? 0.1848 0.2441 0.2809 -0.0014 -0.0230 -0.0306 68  TYR   B OH  
4890 N  N   . ILE   B 69  ? 0.1715 0.1543 0.1859 0.0046  -0.0346 -0.0292 69  ILE   B N   
4891 C  CA  . ILE   B 69  ? 0.1768 0.1621 0.1914 0.0021  -0.0246 -0.0302 69  ILE   B CA  
4892 C  C   . ILE   B 69  ? 0.1763 0.1599 0.1860 0.0089  -0.0236 -0.0225 69  ILE   B C   
4893 O  O   . ILE   B 69  ? 0.1813 0.1699 0.1765 0.0077  -0.0227 -0.0285 69  ILE   B O   
4894 C  CB  . ILE   B 69  ? 0.1807 0.1639 0.2004 0.0023  -0.0019 -0.0284 69  ILE   B CB  
4895 C  CG1 . ILE   B 69  ? 0.1784 0.1684 0.2071 -0.0011 0.0033  -0.0296 69  ILE   B CG1 
4896 C  CG2 . ILE   B 69  ? 0.1884 0.1753 0.2211 0.0034  -0.0008 -0.0229 69  ILE   B CG2 
4897 C  CD1 . ILE   B 69  ? 0.1799 0.1848 0.2200 -0.0163 0.0007  -0.0292 69  ILE   B CD1 
4909 N  N   . ALA   B 70  ? 0.1731 0.1595 0.1887 0.0024  -0.0259 -0.0227 70  ALA   B N   
4910 C  CA  . ALA   B 70  ? 0.1743 0.1666 0.1739 -0.0038 -0.0320 -0.0208 70  ALA   B CA  
4911 C  C   . ALA   B 70  ? 0.1884 0.1673 0.1878 -0.0037 -0.0333 -0.0277 70  ALA   B C   
4912 O  O   . ALA   B 70  ? 0.1998 0.1641 0.2021 0.0030  -0.0342 -0.0265 70  ALA   B O   
4913 C  CB  . ALA   B 70  ? 0.1767 0.1833 0.1692 -0.0029 -0.0289 -0.0232 70  ALA   B CB  
4919 N  N   . THR   B 71  ? 0.1971 0.1644 0.1945 0.0046  -0.0445 -0.0287 71  THR   B N   
4920 C  CA  . THR   B 71  ? 0.2052 0.1710 0.2147 0.0128  -0.0554 -0.0310 71  THR   B CA  
4921 C  C   . THR   B 71  ? 0.1961 0.1700 0.2491 0.0277  -0.0534 -0.0463 71  THR   B C   
4922 O  O   . THR   B 71  ? 0.2084 0.1727 0.2862 0.0317  -0.0524 -0.0577 71  THR   B O   
4923 C  CB  . THR   B 71  ? 0.2296 0.1937 0.2349 0.0069  -0.0628 -0.0109 71  THR   B CB  
4924 O  OG1 . THR   B 71  ? 0.2465 0.2249 0.2744 -0.0169 -0.0591 0.0114  71  THR   B OG1 
4925 C  CG2 . THR   B 71  ? 0.2494 0.1884 0.2549 0.0074  -0.0440 -0.0133 71  THR   B CG2 
4933 N  N   . ASN   B 72  ? 0.1768 0.1738 0.2370 0.0198  -0.0522 -0.0599 72  ASN   B N   
4934 C  CA  . ASN   B 72  ? 0.1798 0.1849 0.2379 0.0216  -0.0364 -0.0586 72  ASN   B CA  
4935 C  C   . ASN   B 72  ? 0.1806 0.1913 0.2436 0.0089  -0.0185 -0.0555 72  ASN   B C   
4936 O  O   . ASN   B 72  ? 0.1799 0.2046 0.2683 0.0095  -0.0125 -0.0602 72  ASN   B O   
4937 C  CB  . ASN   B 72  ? 0.1870 0.1987 0.2474 0.0211  -0.0530 -0.0507 72  ASN   B CB  
4938 C  CG  . ASN   B 72  ? 0.2075 0.2157 0.2594 0.0351  -0.0572 -0.0352 72  ASN   B CG  
4939 O  OD1 . ASN   B 72  ? 0.2318 0.2351 0.2688 0.0213  -0.0429 -0.0346 72  ASN   B OD1 
4940 N  ND2 . ASN   B 72  ? 0.2192 0.2246 0.2917 0.0469  -0.0492 -0.0130 72  ASN   B ND2 
4947 N  N   . GLY   B 73  ? 0.1872 0.1927 0.2304 0.0052  -0.0243 -0.0610 73  GLY   B N   
4948 C  CA  . GLY   B 73  ? 0.1822 0.2027 0.2052 0.0011  -0.0128 -0.0496 73  GLY   B CA  
4949 C  C   . GLY   B 73  ? 0.1775 0.2002 0.1614 0.0078  -0.0164 -0.0284 73  GLY   B C   
4950 O  O   . GLY   B 73  ? 0.1723 0.1884 0.1721 0.0085  -0.0134 -0.0239 73  GLY   B O   
4954 N  N   . PRO   B 74  ? 0.1786 0.2059 0.1618 0.0068  -0.0250 -0.0195 74  PRO   B N   
4955 C  CA  . PRO   B 74  ? 0.1786 0.2068 0.1525 0.0104  -0.0159 -0.0128 74  PRO   B CA  
4956 C  C   . PRO   B 74  ? 0.1646 0.1884 0.1595 0.0091  -0.0078 -0.0107 74  PRO   B C   
4957 O  O   . PRO   B 74  ? 0.1744 0.1943 0.2047 0.0144  -0.0055 -0.0238 74  PRO   B O   
4958 C  CB  . PRO   B 74  ? 0.1946 0.2284 0.1585 0.0062  -0.0131 -0.0053 74  PRO   B CB  
4959 C  CG  . PRO   B 74  ? 0.2127 0.2378 0.1824 0.0048  -0.0121 -0.0009 74  PRO   B CG  
4960 C  CD  . PRO   B 74  ? 0.2058 0.2255 0.1751 0.0099  -0.0164 -0.0084 74  PRO   B CD  
4968 N  N   . LEU   B 75  ? 0.1624 0.1775 0.1542 0.0075  -0.0142 -0.0132 75  LEU   B N   
4969 C  CA  . LEU   B 75  ? 0.1647 0.1837 0.1547 0.0005  -0.0167 0.0076  75  LEU   B CA  
4970 C  C   . LEU   B 75  ? 0.1767 0.1933 0.1569 0.0002  -0.0089 0.0063  75  LEU   B C   
4971 O  O   . LEU   B 75  ? 0.1984 0.2065 0.1667 -0.0064 -0.0114 0.0129  75  LEU   B O   
4972 C  CB  . LEU   B 75  ? 0.1712 0.1871 0.1364 -0.0119 -0.0124 0.0120  75  LEU   B CB  
4973 C  CG  . LEU   B 75  ? 0.2083 0.2018 0.1583 -0.0351 -0.0049 0.0077  75  LEU   B CG  
4974 C  CD1 . LEU   B 75  ? 0.2435 0.2191 0.1795 -0.0378 0.0164  0.0038  75  LEU   B CD1 
4975 C  CD2 . LEU   B 75  ? 0.2461 0.2184 0.2150 -0.0280 0.0094  0.0134  75  LEU   B CD2 
4987 N  N   . LYS   B 76  ? 0.1745 0.2098 0.1936 -0.0018 0.0020  0.0133  76  LYS   B N   
4988 C  CA  . LYS   B 76  ? 0.1863 0.2154 0.2145 -0.0113 0.0153  0.0097  76  LYS   B CA  
4989 C  C   . LYS   B 76  ? 0.1844 0.2039 0.1922 -0.0057 0.0134  0.0306  76  LYS   B C   
4990 O  O   . LYS   B 76  ? 0.1916 0.1869 0.1952 -0.0104 0.0052  0.0242  76  LYS   B O   
4991 C  CB  . LYS   B 76  ? 0.1963 0.2174 0.2580 -0.0192 0.0308  -0.0105 76  LYS   B CB  
4992 C  CG  . LYS   B 76  ? 0.2077 0.2332 0.2959 -0.0121 0.0289  -0.0174 76  LYS   B CG  
4993 C  CD  . LYS   B 76  ? 0.2091 0.2367 0.3353 -0.0080 0.0278  -0.0296 76  LYS   B CD  
4994 C  CE  . LYS   B 76  ? 0.2104 0.2547 0.3865 -0.0046 0.0165  -0.0375 76  LYS   B CE  
4995 N  NZ  . LYS   B 76  ? 0.2133 0.2635 0.4094 -0.0064 0.0047  -0.0483 76  LYS   B NZ  
5009 N  N   . VAL   B 77  ? 0.1969 0.2161 0.1976 0.0007  0.0174  0.0380  77  VAL   B N   
5010 C  CA  . VAL   B 77  ? 0.1971 0.2100 0.2072 0.0065  0.0231  0.0635  77  VAL   B CA  
5011 C  C   . VAL   B 77  ? 0.1832 0.1885 0.2014 0.0063  0.0412  0.0408  77  VAL   B C   
5012 O  O   . VAL   B 77  ? 0.1876 0.1862 0.1991 0.0143  0.0379  0.0272  77  VAL   B O   
5013 C  CB  . VAL   B 77  ? 0.2141 0.2175 0.2449 0.0069  0.0346  0.0698  77  VAL   B CB  
5014 C  CG1 . VAL   B 77  ? 0.2218 0.2064 0.2568 0.0014  0.0383  0.0858  77  VAL   B CG1 
5015 C  CG2 . VAL   B 77  ? 0.2305 0.2368 0.2553 0.0032  0.0154  0.0728  77  VAL   B CG2 
5025 N  N   . GLY   B 78  ? 0.1761 0.1748 0.1985 0.0072  0.0231  0.0319  78  GLY   B N   
5026 C  CA  . GLY   B 78  ? 0.1774 0.1605 0.2034 0.0059  0.0296  0.0246  78  GLY   B CA  
5027 C  C   . GLY   B 78  ? 0.1647 0.1613 0.1949 0.0072  0.0232  0.0264  78  GLY   B C   
5028 O  O   . GLY   B 78  ? 0.1635 0.1603 0.2107 0.0147  0.0240  0.0234  78  GLY   B O   
5032 N  N   . GLY   B 79  ? 0.1538 0.1645 0.1911 0.0032  0.0189  0.0175  79  GLY   B N   
5033 C  CA  . GLY   B 79  ? 0.1541 0.1574 0.1822 0.0093  0.0128  0.0137  79  GLY   B CA  
5034 C  C   . GLY   B 79  ? 0.1448 0.1489 0.1830 0.0110  0.0106  0.0107  79  GLY   B C   
5035 O  O   . GLY   B 79  ? 0.1503 0.1484 0.1989 0.0068  0.0222  0.0241  79  GLY   B O   
5039 N  N   . SER   B 80  ? 0.1481 0.1391 0.1839 0.0013  0.0180  0.0106  80  SER   B N   
5040 C  CA  . SER   B 80  ? 0.1415 0.1439 0.1829 -0.0006 0.0091  0.0119  80  SER   B CA  
5041 C  C   . SER   B 80  ? 0.1440 0.1387 0.1785 0.0044  -0.0026 0.0040  80  SER   B C   
5042 O  O   . SER   B 80  ? 0.1518 0.1397 0.2121 0.0018  0.0116  0.0020  80  SER   B O   
5043 C  CB  . SER   B 80  ? 0.1492 0.1464 0.1824 -0.0024 0.0097  0.0080  80  SER   B CB  
5044 O  OG  . SER   B 80  ? 0.1508 0.1608 0.2015 -0.0046 -0.0075 0.0161  80  SER   B OG  
5050 N  N   . CYS   B 81  ? 0.1391 0.1292 0.1783 -0.0030 -0.0027 -0.0025 81  CYS   B N   
5051 C  CA  . CYS   B 81  ? 0.1445 0.1269 0.1777 0.0005  -0.0023 0.0014  81  CYS   B CA  
5052 C  C   . CYS   B 81  ? 0.1440 0.1258 0.1531 -0.0032 -0.0137 0.0044  81  CYS   B C   
5053 O  O   . CYS   B 81  ? 0.1613 0.1271 0.1798 0.0051  -0.0025 0.0046  81  CYS   B O   
5054 C  CB  . CYS   B 81  ? 0.1637 0.1414 0.1788 -0.0078 -0.0063 0.0018  81  CYS   B CB  
5055 S  SG  . CYS   B 81  ? 0.1651 0.1563 0.1624 -0.0039 -0.0227 -0.0034 81  CYS   B SG  
5061 N  N   . VAL   B 82  ? 0.1517 0.1254 0.1647 -0.0030 -0.0117 0.0079  82  VAL   B N   
5062 C  CA  . VAL   B 82  ? 0.1547 0.1253 0.1595 -0.0075 -0.0052 0.0111  82  VAL   B CA  
5063 C  C   . VAL   B 82  ? 0.1637 0.1221 0.1738 -0.0063 -0.0053 0.0048  82  VAL   B C   
5064 O  O   . VAL   B 82  ? 0.1718 0.1235 0.2038 -0.0060 -0.0001 -0.0096 82  VAL   B O   
5065 C  CB  . VAL   B 82  ? 0.1613 0.1511 0.1795 -0.0044 -0.0159 0.0176  82  VAL   B CB  
5066 C  CG1 . VAL   B 82  ? 0.1862 0.1738 0.1829 0.0015  -0.0187 0.0296  82  VAL   B CG1 
5067 C  CG2 . VAL   B 82  ? 0.1688 0.1706 0.2066 -0.0079 -0.0281 0.0194  82  VAL   B CG2 
5077 N  N   . LEU   B 83  ? 0.1460 0.1249 0.1731 -0.0094 -0.0183 -0.0050 83  LEU   B N   
5078 C  CA  . LEU   B 83  ? 0.1496 0.1347 0.1559 -0.0142 -0.0156 0.0001  83  LEU   B CA  
5079 C  C   . LEU   B 83  ? 0.1513 0.1308 0.1571 -0.0176 -0.0182 -0.0032 83  LEU   B C   
5080 O  O   . LEU   B 83  ? 0.1523 0.1397 0.1479 -0.0212 -0.0121 0.0029  83  LEU   B O   
5081 C  CB  . LEU   B 83  ? 0.1593 0.1459 0.1666 -0.0188 -0.0162 -0.0093 83  LEU   B CB  
5082 C  CG  . LEU   B 83  ? 0.1743 0.1648 0.1649 -0.0157 -0.0105 -0.0039 83  LEU   B CG  
5083 C  CD1 . LEU   B 83  ? 0.1868 0.1710 0.1702 -0.0154 -0.0136 -0.0049 83  LEU   B CD1 
5084 C  CD2 . LEU   B 83  ? 0.1984 0.1693 0.1734 -0.0055 -0.0166 -0.0112 83  LEU   B CD2 
5096 N  N   . SER   B 84  ? 0.1544 0.1427 0.1853 -0.0264 -0.0176 0.0017  84  SER   B N   
5097 C  CA  . SER   B 84  ? 0.1551 0.1651 0.1692 -0.0300 -0.0116 0.0186  84  SER   B CA  
5098 C  C   . SER   B 84  ? 0.1453 0.1808 0.1261 -0.0224 -0.0167 0.0218  84  SER   B C   
5099 O  O   . SER   B 84  ? 0.1555 0.1632 0.1395 -0.0204 -0.0090 0.0053  84  SER   B O   
5100 C  CB  . SER   B 84  ? 0.1730 0.1696 0.2146 -0.0310 0.0091  0.0148  84  SER   B CB  
5101 O  OG  . SER   B 84  ? 0.1720 0.1814 0.2414 -0.0388 0.0062  0.0164  84  SER   B OG  
5107 N  N   . GLY   B 85  ? 0.1460 0.2006 0.1419 -0.0251 -0.0175 0.0253  85  GLY   B N   
5108 C  CA  . GLY   B 85  ? 0.1557 0.1991 0.1676 -0.0329 -0.0004 -0.0037 85  GLY   B CA  
5109 C  C   . GLY   B 85  ? 0.1515 0.1846 0.1630 -0.0403 -0.0025 0.0052  85  GLY   B C   
5110 O  O   . GLY   B 85  ? 0.1618 0.1834 0.1760 -0.0510 0.0188  -0.0183 85  GLY   B O   
5114 N  N   . HIS   B 86  ? 0.1453 0.1712 0.1905 -0.0355 -0.0108 0.0100  86  HIS   B N   
5115 C  CA  . HIS   B 86  ? 0.1518 0.1727 0.1745 -0.0356 -0.0141 0.0170  86  HIS   B CA  
5116 C  C   . HIS   B 86  ? 0.1506 0.1849 0.1624 -0.0468 -0.0023 0.0208  86  HIS   B C   
5117 O  O   . HIS   B 86  ? 0.1652 0.1973 0.1795 -0.0327 0.0083  0.0226  86  HIS   B O   
5118 C  CB  . HIS   B 86  ? 0.1639 0.1806 0.1734 -0.0198 -0.0229 0.0113  86  HIS   B CB  
5119 C  CG  . HIS   B 86  ? 0.1596 0.1901 0.1747 -0.0098 -0.0222 0.0027  86  HIS   B CG  
5120 N  ND1 . HIS   B 86  ? 0.1744 0.2195 0.1963 -0.0268 -0.0196 -0.0119 86  HIS   B ND1 
5121 C  CD2 . HIS   B 86  ? 0.1644 0.1953 0.1873 -0.0086 -0.0170 -0.0011 86  HIS   B CD2 
5122 C  CE1 . HIS   B 86  ? 0.1792 0.2130 0.1843 -0.0126 -0.0075 -0.0267 86  HIS   B CE1 
5123 N  NE2 . HIS   B 86  ? 0.1754 0.2011 0.1808 -0.0011 -0.0043 -0.0057 86  HIS   B NE2 
5131 N  N   . ASN   B 87  ? 0.1562 0.1914 0.1843 -0.0355 0.0045  0.0099  87  ASN   B N   
5132 C  CA  . ASN   B 87  ? 0.1674 0.2098 0.1830 -0.0342 0.0269  0.0101  87  ASN   B CA  
5133 C  C   . ASN   B 87  ? 0.1840 0.1951 0.1761 -0.0330 0.0322  0.0091  87  ASN   B C   
5134 O  O   . ASN   B 87  ? 0.2129 0.2052 0.1941 -0.0244 0.0528  0.0085  87  ASN   B O   
5135 C  CB  . ASN   B 87  ? 0.1663 0.2410 0.2097 -0.0299 0.0374  0.0075  87  ASN   B CB  
5136 C  CG  . ASN   B 87  ? 0.1750 0.2570 0.2253 0.0040  0.0363  0.0280  87  ASN   B CG  
5137 O  OD1 . ASN   B 87  ? 0.1630 0.2425 0.2146 0.0094  0.0483  0.0342  87  ASN   B OD1 
5138 N  ND2 . ASN   B 87  ? 0.2131 0.2656 0.2461 0.0125  0.0422  0.0262  87  ASN   B ND2 
5145 N  N   . LEU   B 88  ? 0.1695 0.1772 0.1600 -0.0372 0.0142  0.0079  88  LEU   B N   
5146 C  CA  . LEU   B 88  ? 0.1870 0.1730 0.1598 -0.0368 0.0087  -0.0052 88  LEU   B CA  
5147 C  C   . LEU   B 88  ? 0.1871 0.1633 0.1704 -0.0458 -0.0001 -0.0055 88  LEU   B C   
5148 O  O   . LEU   B 88  ? 0.2152 0.1693 0.2012 -0.0273 -0.0240 -0.0181 88  LEU   B O   
5149 C  CB  . LEU   B 88  ? 0.2020 0.1792 0.1875 -0.0442 -0.0087 0.0009  88  LEU   B CB  
5150 C  CG  . LEU   B 88  ? 0.2355 0.2049 0.2026 -0.0414 -0.0213 0.0195  88  LEU   B CG  
5151 C  CD1 . LEU   B 88  ? 0.2465 0.2331 0.2160 -0.0570 -0.0131 0.0366  88  LEU   B CD1 
5152 C  CD2 . LEU   B 88  ? 0.2692 0.2290 0.2515 -0.0043 -0.0402 0.0044  88  LEU   B CD2 
5164 N  N   . ALA   B 89  ? 0.1645 0.1673 0.1633 -0.0456 0.0159  -0.0044 89  ALA   B N   
5165 C  CA  . ALA   B 89  ? 0.1613 0.1612 0.1503 -0.0419 0.0022  0.0096  89  ALA   B CA  
5166 C  C   . ALA   B 89  ? 0.1687 0.1641 0.1522 -0.0487 0.0147  0.0058  89  ALA   B C   
5167 O  O   . ALA   B 89  ? 0.1516 0.1664 0.1782 -0.0439 0.0125  -0.0193 89  ALA   B O   
5168 C  CB  . ALA   B 89  ? 0.1560 0.1584 0.1641 -0.0404 0.0022  0.0181  89  ALA   B CB  
5174 N  N   . LYS   B 90  ? 0.2029 0.1514 0.1604 -0.0520 -0.0108 0.0064  90  LYS   B N   
5175 C  CA  . LYS   B 90  ? 0.2078 0.1484 0.1482 -0.0506 -0.0162 0.0163  90  LYS   B CA  
5176 C  C   . LYS   B 90  ? 0.1905 0.1390 0.1579 -0.0417 -0.0126 0.0045  90  LYS   B C   
5177 O  O   . LYS   B 90  ? 0.1946 0.1519 0.1702 -0.0499 -0.0032 0.0079  90  LYS   B O   
5178 C  CB  . LYS   B 90  ? 0.2249 0.1580 0.1794 -0.0431 -0.0112 0.0196  90  LYS   B CB  
5179 C  CG  . LYS   B 90  ? 0.2192 0.1673 0.1893 -0.0294 0.0041  0.0124  90  LYS   B CG  
5180 C  CD  . LYS   B 90  ? 0.2339 0.1794 0.2292 -0.0117 0.0214  -0.0014 90  LYS   B CD  
5181 C  CE  . LYS   B 90  ? 0.2412 0.1957 0.2687 -0.0155 0.0297  -0.0102 90  LYS   B CE  
5182 N  NZ  . LYS   B 90  ? 0.2518 0.1865 0.2530 -0.0228 0.0448  -0.0198 90  LYS   B NZ  
5196 N  N   . HIS   B 91  ? 0.1680 0.1348 0.1455 -0.0311 -0.0123 0.0136  91  HIS   B N   
5197 C  CA  . HIS   B 91  ? 0.1558 0.1314 0.1567 -0.0248 -0.0189 0.0038  91  HIS   B CA  
5198 C  C   . HIS   B 91  ? 0.1473 0.1289 0.1397 -0.0265 -0.0082 0.0066  91  HIS   B C   
5199 O  O   . HIS   B 91  ? 0.1601 0.1374 0.1558 -0.0292 -0.0141 0.0019  91  HIS   B O   
5200 C  CB  . HIS   B 91  ? 0.1752 0.1382 0.1959 -0.0109 -0.0149 0.0097  91  HIS   B CB  
5201 C  CG  . HIS   B 91  ? 0.2136 0.1530 0.2547 -0.0014 0.0163  0.0289  91  HIS   B CG  
5202 N  ND1 . HIS   B 91  ? 0.2469 0.1601 0.2995 -0.0042 0.0286  0.0172  91  HIS   B ND1 
5203 C  CD2 . HIS   B 91  ? 0.2280 0.1851 0.2920 0.0169  -0.0012 0.0520  91  HIS   B CD2 
5204 C  CE1 . HIS   B 91  ? 0.2512 0.1763 0.3142 0.0103  0.0230  0.0183  91  HIS   B CE1 
5205 N  NE2 . HIS   B 91  ? 0.2453 0.1925 0.3209 0.0264  0.0109  0.0560  91  HIS   B NE2 
5213 N  N   . CYS   B 92  ? 0.1383 0.1338 0.1421 -0.0270 -0.0127 0.0022  92  CYS   B N   
5214 C  CA  . CYS   B 92  ? 0.1389 0.1343 0.1474 -0.0241 -0.0058 0.0017  92  CYS   B CA  
5215 C  C   . CYS   B 92  ? 0.1399 0.1225 0.1390 -0.0170 -0.0082 0.0091  92  CYS   B C   
5216 O  O   . CYS   B 92  ? 0.1491 0.1295 0.1653 -0.0170 -0.0034 0.0039  92  CYS   B O   
5217 C  CB  . CYS   B 92  ? 0.1420 0.1393 0.1582 -0.0132 -0.0085 0.0012  92  CYS   B CB  
5218 S  SG  . CYS   B 92  ? 0.1443 0.1400 0.1479 -0.0130 -0.0110 0.0071  92  CYS   B SG  
5224 N  N   . LEU   B 93  ? 0.1296 0.1268 0.1522 -0.0160 -0.0156 -0.0027 93  LEU   B N   
5225 C  CA  . LEU   B 93  ? 0.1309 0.1290 0.1419 -0.0087 -0.0146 0.0069  93  LEU   B CA  
5226 C  C   . LEU   B 93  ? 0.1292 0.1257 0.1298 -0.0065 -0.0160 0.0123  93  LEU   B C   
5227 O  O   . LEU   B 93  ? 0.1404 0.1256 0.1568 -0.0079 -0.0131 0.0030  93  LEU   B O   
5228 C  CB  . LEU   B 93  ? 0.1362 0.1294 0.1672 -0.0054 -0.0089 0.0108  93  LEU   B CB  
5229 C  CG  . LEU   B 93  ? 0.1345 0.1376 0.1827 -0.0058 -0.0081 0.0168  93  LEU   B CG  
5230 C  CD1 . LEU   B 93  ? 0.1431 0.1537 0.1882 0.0027  0.0010  0.0026  93  LEU   B CD1 
5231 C  CD2 . LEU   B 93  ? 0.1348 0.1377 0.1950 -0.0046 -0.0183 0.0084  93  LEU   B CD2 
5243 N  N   . HIS   B 94  ? 0.1325 0.1248 0.1284 -0.0085 -0.0141 0.0126  94  HIS   B N   
5244 C  CA  . HIS   B 94  ? 0.1377 0.1227 0.1436 -0.0043 -0.0090 0.0064  94  HIS   B CA  
5245 C  C   . HIS   B 94  ? 0.1334 0.1257 0.1700 -0.0037 -0.0100 0.0127  94  HIS   B C   
5246 O  O   . HIS   B 94  ? 0.1361 0.1318 0.2042 -0.0045 0.0103  -0.0007 94  HIS   B O   
5247 C  CB  . HIS   B 94  ? 0.1349 0.1311 0.1528 0.0001  -0.0122 0.0042  94  HIS   B CB  
5248 C  CG  . HIS   B 94  ? 0.1408 0.1278 0.1554 -0.0089 -0.0232 0.0047  94  HIS   B CG  
5249 N  ND1 . HIS   B 94  ? 0.1421 0.1334 0.1596 -0.0063 -0.0247 0.0046  94  HIS   B ND1 
5250 C  CD2 . HIS   B 94  ? 0.1397 0.1329 0.1540 -0.0043 -0.0169 0.0071  94  HIS   B CD2 
5251 C  CE1 . HIS   B 94  ? 0.1469 0.1324 0.1601 -0.0105 -0.0140 0.0021  94  HIS   B CE1 
5252 N  NE2 . HIS   B 94  ? 0.1394 0.1372 0.1612 -0.0147 -0.0101 0.0066  94  HIS   B NE2 
5260 N  N   . VAL   B 95  ? 0.1272 0.1198 0.1720 -0.0019 -0.0011 0.0082  95  VAL   B N   
5261 C  CA  . VAL   B 95  ? 0.1337 0.1295 0.1569 -0.0004 0.0014  0.0166  95  VAL   B CA  
5262 C  C   . VAL   B 95  ? 0.1438 0.1299 0.1520 -0.0003 0.0094  0.0149  95  VAL   B C   
5263 O  O   . VAL   B 95  ? 0.1478 0.1323 0.1824 0.0079  0.0062  0.0242  95  VAL   B O   
5264 C  CB  . VAL   B 95  ? 0.1392 0.1285 0.1655 -0.0033 -0.0091 0.0131  95  VAL   B CB  
5265 C  CG1 . VAL   B 95  ? 0.1467 0.1463 0.1980 -0.0093 0.0001  0.0152  95  VAL   B CG1 
5266 C  CG2 . VAL   B 95  ? 0.1416 0.1263 0.1665 0.0022  -0.0128 0.0096  95  VAL   B CG2 
5276 N  N   . VAL   B 96  ? 0.1539 0.1319 0.1596 0.0082  0.0095  0.0193  96  VAL   B N   
5277 C  CA  . VAL   B 96  ? 0.1651 0.1433 0.1516 0.0064  0.0058  0.0247  96  VAL   B CA  
5278 C  C   . VAL   B 96  ? 0.1732 0.1452 0.1729 0.0054  0.0175  0.0244  96  VAL   B C   
5279 O  O   . VAL   B 96  ? 0.1707 0.1529 0.1978 -0.0028 0.0248  0.0095  96  VAL   B O   
5280 C  CB  . VAL   B 96  ? 0.1683 0.1711 0.1545 0.0031  0.0131  0.0187  96  VAL   B CB  
5281 C  CG1 . VAL   B 96  ? 0.1693 0.1885 0.1697 0.0075  0.0163  0.0162  96  VAL   B CG1 
5282 C  CG2 . VAL   B 96  ? 0.1753 0.1722 0.1794 0.0050  0.0109  0.0113  96  VAL   B CG2 
5292 N  N   . GLY   B 97  ? 0.1825 0.1473 0.1726 0.0026  0.0035  0.0292  97  GLY   B N   
5293 C  CA  . GLY   B 97  ? 0.2045 0.1509 0.1787 0.0020  0.0163  0.0270  97  GLY   B CA  
5294 C  C   . GLY   B 97  ? 0.2316 0.1671 0.1936 0.0122  0.0274  0.0364  97  GLY   B C   
5295 O  O   . GLY   B 97  ? 0.2491 0.1678 0.2039 0.0102  0.0088  0.0236  97  GLY   B O   
5299 N  N   . PRO   B 98  ? 0.2507 0.1789 0.2082 0.0208  0.0595  0.0470  98  PRO   B N   
5300 C  CA  . PRO   B 98  ? 0.2677 0.2032 0.2063 0.0425  0.0746  0.0480  98  PRO   B CA  
5301 C  C   . PRO   B 98  ? 0.2832 0.2038 0.1829 0.0623  0.0843  0.0643  98  PRO   B C   
5302 O  O   . PRO   B 98  ? 0.2688 0.1979 0.1967 0.0483  0.0765  0.0664  98  PRO   B O   
5303 C  CB  . PRO   B 98  ? 0.2633 0.2135 0.2218 0.0359  0.0769  0.0517  98  PRO   B CB  
5304 C  CG  . PRO   B 98  ? 0.2573 0.1951 0.2367 0.0262  0.0693  0.0631  98  PRO   B CG  
5305 C  CD  . PRO   B 98  ? 0.2415 0.1764 0.2297 0.0326  0.0709  0.0616  98  PRO   B CD  
5313 N  N   . ASN   B 99  ? 0.2960 0.2275 0.2044 0.0863  0.0825  0.0591  99  ASN   B N   
5314 C  CA  . ASN   B 99  ? 0.3153 0.2441 0.2137 0.1029  0.0738  0.0798  99  ASN   B CA  
5315 C  C   . ASN   B 99  ? 0.3346 0.2838 0.2575 0.1094  0.0932  0.1049  99  ASN   B C   
5316 O  O   . ASN   B 99  ? 0.3475 0.2977 0.2704 0.1176  0.0828  0.1116  99  ASN   B O   
5317 C  CB  . ASN   B 99  ? 0.3252 0.2380 0.2141 0.0976  0.0573  0.0671  99  ASN   B CB  
5318 C  CG  . ASN   B 99  ? 0.3290 0.2383 0.2240 0.0910  0.0495  0.0558  99  ASN   B CG  
5319 O  OD1 . ASN   B 99  ? 0.3250 0.2376 0.2511 0.1004  0.0496  0.0572  99  ASN   B OD1 
5320 N  ND2 . ASN   B 99  ? 0.3317 0.2369 0.2326 0.0844  0.0334  0.0501  99  ASN   B ND2 
5327 N  N   . VAL   B 100 ? 0.3546 0.3029 0.3137 0.0873  0.0968  0.1318  100 VAL   B N   
5328 C  CA  . VAL   B 100 ? 0.3860 0.3305 0.3749 0.0674  0.0774  0.1534  100 VAL   B CA  
5329 C  C   . VAL   B 100 ? 0.4178 0.3496 0.3569 0.0635  0.0574  0.1646  100 VAL   B C   
5330 O  O   . VAL   B 100 ? 0.4236 0.3667 0.3671 0.0644  0.0723  0.1548  100 VAL   B O   
5331 C  CB  . VAL   B 100 ? 0.3906 0.3418 0.4479 0.0416  0.0737  0.1700  100 VAL   B CB  
5332 C  CG1 . VAL   B 100 ? 0.3957 0.3470 0.4725 0.0357  0.0700  0.1776  100 VAL   B CG1 
5333 C  CG2 . VAL   B 100 ? 0.3895 0.3460 0.4721 0.0299  0.0751  0.1765  100 VAL   B CG2 
5343 N  N   A ASN   B 101 ? 0.4337 0.3453 0.3485 0.0693  0.0332  0.1837  101 ASN   B N   
5344 N  N   B ASN   B 101 ? 0.4321 0.3666 0.3566 0.0540  0.0402  0.1387  101 ASN   B N   
5345 C  CA  A ASN   B 101 ? 0.4564 0.3498 0.3544 0.0669  0.0117  0.1887  101 ASN   B CA  
5346 C  CA  B ASN   B 101 ? 0.4486 0.3853 0.3643 0.0435  0.0249  0.1084  101 ASN   B CA  
5347 C  C   A ASN   B 101 ? 0.4971 0.3910 0.3747 0.0567  0.0052  0.1882  101 ASN   B C   
5348 C  C   B ASN   B 101 ? 0.4762 0.4148 0.3915 0.0385  0.0195  0.0930  101 ASN   B C   
5349 O  O   A ASN   B 101 ? 0.4982 0.3989 0.3912 0.0560  0.0084  0.1670  101 ASN   B O   
5350 O  O   B ASN   B 101 ? 0.4755 0.4163 0.3935 0.0387  0.0207  0.0862  101 ASN   B O   
5351 C  CB  A ASN   B 101 ? 0.4434 0.3247 0.3573 0.0638  0.0096  0.1683  101 ASN   B CB  
5352 C  CB  B ASN   B 101 ? 0.4393 0.3761 0.3524 0.0376  0.0185  0.0895  101 ASN   B CB  
5353 C  CG  A ASN   B 101 ? 0.4292 0.3008 0.3583 0.0647  0.0041  0.1591  101 ASN   B CG  
5354 C  CG  B ASN   B 101 ? 0.4312 0.3685 0.3435 0.0333  0.0131  0.0759  101 ASN   B CG  
5355 O  OD1 A ASN   B 101 ? 0.4271 0.3002 0.3737 0.0545  0.0165  0.1485  101 ASN   B OD1 
5356 O  OD1 B ASN   B 101 ? 0.4291 0.3670 0.3455 0.0311  0.0146  0.0713  101 ASN   B OD1 
5357 N  ND2 A ASN   B 101 ? 0.4210 0.2893 0.3576 0.0718  -0.0030 0.1473  101 ASN   B ND2 
5358 N  ND2 B ASN   B 101 ? 0.4275 0.3652 0.3372 0.0321  0.0098  0.0696  101 ASN   B ND2 
5371 N  N   A LYS   B 102 ? 0.5366 0.4320 0.4133 0.0443  0.0065  0.1783  102 LYS   B N   
5372 N  N   B LYS   B 102 ? 0.5046 0.4437 0.4262 0.0338  0.0158  0.0808  102 LYS   B N   
5373 C  CA  A LYS   B 102 ? 0.5738 0.4770 0.4557 0.0293  0.0132  0.1569  102 LYS   B CA  
5374 C  CA  B LYS   B 102 ? 0.5318 0.4731 0.4633 0.0288  0.0148  0.0688  102 LYS   B CA  
5375 C  C   A LYS   B 102 ? 0.5840 0.4892 0.4423 0.0327  0.0219  0.1734  102 LYS   B C   
5376 C  C   B LYS   B 102 ? 0.5444 0.4836 0.4652 0.0330  0.0235  0.0822  102 LYS   B C   
5377 O  O   A LYS   B 102 ? 0.5905 0.4916 0.4340 0.0317  0.0137  0.1796  102 LYS   B O   
5378 O  O   B LYS   B 102 ? 0.5476 0.4852 0.4613 0.0319  0.0187  0.0809  102 LYS   B O   
5379 C  CB  A LYS   B 102 ? 0.5967 0.5063 0.5191 0.0143  0.0193  0.1109  102 LYS   B CB  
5380 C  CB  B LYS   B 102 ? 0.5437 0.4895 0.5015 0.0216  0.0096  0.0433  102 LYS   B CB  
5381 C  CG  A LYS   B 102 ? 0.6156 0.5308 0.5805 0.0019  0.0263  0.0661  102 LYS   B CG  
5382 C  CG  B LYS   B 102 ? 0.5534 0.5030 0.5393 0.0157  0.0060  0.0207  102 LYS   B CG  
5383 C  CD  A LYS   B 102 ? 0.6318 0.5510 0.6363 -0.0079 0.0336  0.0295  102 LYS   B CD  
5384 C  CD  B LYS   B 102 ? 0.5621 0.5148 0.5748 0.0111  0.0043  0.0027  102 LYS   B CD  
5385 C  CE  A LYS   B 102 ? 0.6420 0.5644 0.6763 -0.0155 0.0402  0.0036  102 LYS   B CE  
5386 C  CE  B LYS   B 102 ? 0.5675 0.5226 0.6011 0.0077  0.0039  -0.0101 102 LYS   B CE  
5387 N  NZ  A LYS   B 102 ? 0.6478 0.5725 0.6982 -0.0191 0.0433  -0.0117 102 LYS   B NZ  
5388 N  NZ  B LYS   B 102 ? 0.5710 0.5276 0.6160 0.0060  0.0033  -0.0171 102 LYS   B NZ  
5415 N  N   A GLY   B 103 ? 0.5841 0.4956 0.4527 0.0379  0.0399  0.1748  103 GLY   B N   
5416 N  N   B GLY   B 103 ? 0.5524 0.4907 0.4771 0.0388  0.0389  0.0956  103 GLY   B N   
5417 C  CA  A GLY   B 103 ? 0.5805 0.5002 0.4707 0.0455  0.0584  0.1648  103 GLY   B CA  
5418 C  CA  B GLY   B 103 ? 0.5580 0.4961 0.4891 0.0457  0.0556  0.1070  103 GLY   B CA  
5419 C  C   A GLY   B 103 ? 0.5724 0.5014 0.4817 0.0522  0.0756  0.1488  103 GLY   B C   
5420 C  C   B GLY   B 103 ? 0.5607 0.4989 0.4946 0.0525  0.0722  0.1161  103 GLY   B C   
5421 O  O   A GLY   B 103 ? 0.5761 0.5052 0.4875 0.0507  0.0821  0.1557  103 GLY   B O   
5422 O  O   B GLY   B 103 ? 0.5638 0.5020 0.5054 0.0517  0.0758  0.1194  103 GLY   B O   
5429 N  N   . GLU   B 104 ? 0.5578 0.4959 0.4783 0.0605  0.0863  0.1180  104 GLU   B N   
5430 C  CA  . GLU   B 104 ? 0.5375 0.4848 0.4564 0.0792  0.1062  0.0877  104 GLU   B CA  
5431 C  C   . GLU   B 104 ? 0.5309 0.4824 0.4581 0.0575  0.1565  0.0892  104 GLU   B C   
5432 O  O   . GLU   B 104 ? 0.5304 0.4828 0.4717 0.0555  0.1638  0.0928  104 GLU   B O   
5433 C  CB  . GLU   B 104 ? 0.5256 0.4728 0.4346 0.1184  0.0706  0.0498  104 GLU   B CB  
5434 C  CG  . GLU   B 104 ? 0.5137 0.4638 0.4097 0.1541  0.0303  0.0113  104 GLU   B CG  
5435 C  CD  . GLU   B 104 ? 0.5023 0.4565 0.3817 0.1833  -0.0013 -0.0223 104 GLU   B CD  
5436 O  OE1 . GLU   B 104 ? 0.4927 0.4450 0.3470 0.2018  0.0029  -0.0445 104 GLU   B OE1 
5437 O  OE2 . GLU   B 104 ? 0.4986 0.4601 0.3763 0.1893  -0.0225 -0.0338 104 GLU   B OE2 
5445 N  N   . ASP   B 105 ? 0.5189 0.4764 0.4399 0.0400  0.1989  0.0844  105 ASP   B N   
5446 C  CA  . ASP   B 105 ? 0.5086 0.4676 0.4434 0.0235  0.2262  0.0671  105 ASP   B CA  
5447 C  C   . ASP   B 105 ? 0.4769 0.4267 0.4006 -0.0017 0.2190  0.0536  105 ASP   B C   
5448 O  O   . ASP   B 105 ? 0.4704 0.4215 0.3786 0.0069  0.2362  0.0552  105 ASP   B O   
5449 C  CB  . ASP   B 105 ? 0.5252 0.4945 0.5052 0.0352  0.2529  0.0563  105 ASP   B CB  
5450 C  CG  . ASP   B 105 ? 0.5343 0.5143 0.5656 0.0427  0.2819  0.0498  105 ASP   B CG  
5451 O  OD1 . ASP   B 105 ? 0.5334 0.5193 0.5709 0.0402  0.3057  0.0596  105 ASP   B OD1 
5452 O  OD2 . ASP   B 105 ? 0.5399 0.5230 0.6090 0.0501  0.2766  0.0387  105 ASP   B OD2 
5457 N  N   A ILE   B 106 ? 0.4626 0.3963 0.4003 -0.0192 0.2135  0.0533  106 ILE   B N   
5458 N  N   B ILE   B 106 ? 0.4669 0.4184 0.4002 -0.0113 0.1788  0.0407  106 ILE   B N   
5459 C  CA  A ILE   B 106 ? 0.4417 0.3651 0.4005 -0.0389 0.2172  0.0491  106 ILE   B CA  
5460 C  CA  B ILE   B 106 ? 0.4535 0.4085 0.4021 -0.0200 0.1437  0.0267  106 ILE   B CA  
5461 C  C   A ILE   B 106 ? 0.4066 0.3503 0.3895 -0.0402 0.2172  0.0414  106 ILE   B C   
5462 C  C   B ILE   B 106 ? 0.4309 0.3983 0.3994 -0.0179 0.1279  0.0190  106 ILE   B C   
5463 O  O   A ILE   B 106 ? 0.3977 0.3326 0.3863 -0.0453 0.2156  0.0446  106 ILE   B O   
5464 O  O   B ILE   B 106 ? 0.4308 0.3954 0.4003 -0.0191 0.1251  0.0174  106 ILE   B O   
5465 C  CB  A ILE   B 106 ? 0.4572 0.3529 0.4125 -0.0562 0.2143  0.0522  106 ILE   B CB  
5466 C  CB  B ILE   B 106 ? 0.4612 0.4092 0.4076 -0.0292 0.1270  0.0211  106 ILE   B CB  
5467 C  CG1 A ILE   B 106 ? 0.4653 0.3494 0.4138 -0.0591 0.2030  0.0439  106 ILE   B CG1 
5468 C  CG1 B ILE   B 106 ? 0.4650 0.4096 0.4055 -0.0325 0.1156  0.0163  106 ILE   B CG1 
5469 C  CG2 A ILE   B 106 ? 0.4616 0.3529 0.4301 -0.0629 0.2172  0.0563  106 ILE   B CG2 
5470 C  CG2 B ILE   B 106 ? 0.4636 0.4109 0.4161 -0.0317 0.1241  0.0200  106 ILE   B CG2 
5471 C  CD1 A ILE   B 106 ? 0.4702 0.3491 0.4088 -0.0580 0.1964  0.0414  106 ILE   B CD1 
5472 C  CD1 B ILE   B 106 ? 0.4670 0.4098 0.4029 -0.0337 0.1089  0.0138  106 ILE   B CD1 
5495 N  N   A GLN   B 107 ? 0.3810 0.3552 0.3977 -0.0408 0.2051  0.0385  107 GLN   B N   
5496 N  N   B GLN   B 107 ? 0.4074 0.3904 0.4017 -0.0160 0.1167  0.0158  107 GLN   B N   
5497 C  CA  A GLN   B 107 ? 0.3536 0.3601 0.4059 -0.0404 0.1776  0.0340  107 GLN   B CA  
5498 C  CA  B GLN   B 107 ? 0.3813 0.3800 0.4026 -0.0141 0.1047  0.0154  107 GLN   B CA  
5499 C  C   A GLN   B 107 ? 0.3134 0.3326 0.3671 -0.0300 0.1512  0.0204  107 GLN   B C   
5500 C  C   B GLN   B 107 ? 0.3357 0.3468 0.3619 -0.0111 0.1142  0.0144  107 GLN   B C   
5501 O  O   A GLN   B 107 ? 0.2964 0.3328 0.3848 -0.0238 0.1270  -0.0063 107 GLN   B O   
5502 O  O   B GLN   B 107 ? 0.3331 0.3481 0.3640 -0.0084 0.1024  0.0054  107 GLN   B O   
5503 C  CB  A GLN   B 107 ? 0.3818 0.3971 0.4737 -0.0396 0.1481  0.0352  107 GLN   B CB  
5504 C  CB  B GLN   B 107 ? 0.4018 0.4021 0.4512 -0.0135 0.0822  0.0155  107 GLN   B CB  
5505 C  CG  A GLN   B 107 ? 0.4112 0.4304 0.5383 -0.0345 0.1102  0.0346  107 GLN   B CG  
5506 C  CG  B GLN   B 107 ? 0.4201 0.4214 0.4969 -0.0116 0.0600  0.0159  107 GLN   B CG  
5507 C  CD  A GLN   B 107 ? 0.4334 0.4560 0.5881 -0.0327 0.0840  0.0377  107 GLN   B CD  
5508 C  CD  B GLN   B 107 ? 0.4342 0.4362 0.5340 -0.0104 0.0438  0.0170  107 GLN   B CD  
5509 O  OE1 A GLN   B 107 ? 0.4415 0.4662 0.6057 -0.0293 0.0785  0.0369  107 GLN   B OE1 
5510 O  OE1 B GLN   B 107 ? 0.4393 0.4421 0.5463 -0.0091 0.0402  0.0171  107 GLN   B OE1 
5511 N  NE2 A GLN   B 107 ? 0.4432 0.4639 0.6056 -0.0317 0.0719  0.0403  107 GLN   B NE2 
5512 N  NE2 B GLN   B 107 ? 0.4395 0.4408 0.5475 -0.0098 0.0371  0.0177  107 GLN   B NE2 
5529 N  N   . LEU   B 108 ? 0.2898 0.3120 0.3283 -0.0055 0.1343  0.0204  108 LEU   B N   
5530 C  CA  . LEU   B 108 ? 0.2533 0.2738 0.2803 0.0155  0.0991  0.0317  108 LEU   B CA  
5531 C  C   . LEU   B 108 ? 0.2008 0.2141 0.2707 0.0214  0.0593  0.0300  108 LEU   B C   
5532 O  O   . LEU   B 108 ? 0.1908 0.1957 0.2665 0.0246  0.0472  0.0266  108 LEU   B O   
5533 C  CB  . LEU   B 108 ? 0.2754 0.3002 0.2635 0.0211  0.0968  0.0469  108 LEU   B CB  
5534 C  CG  . LEU   B 108 ? 0.2913 0.3305 0.2812 0.0248  0.0895  0.0354  108 LEU   B CG  
5535 C  CD1 . LEU   B 108 ? 0.3067 0.3439 0.2846 0.0224  0.0850  0.0335  108 LEU   B CD1 
5536 C  CD2 . LEU   B 108 ? 0.2972 0.3411 0.2827 0.0300  0.0800  0.0247  108 LEU   B CD2 
5549 N  N   . LEU   B 109 ? 0.1809 0.1831 0.2730 0.0050  0.0428  0.0249  109 LEU   B N   
5550 C  CA  . LEU   B 109 ? 0.1612 0.1493 0.2785 -0.0010 0.0390  0.0317  109 LEU   B CA  
5551 C  C   . LEU   B 109 ? 0.1550 0.1346 0.2744 -0.0038 0.0351  0.0207  109 LEU   B C   
5552 O  O   . LEU   B 109 ? 0.1537 0.1320 0.2645 0.0021  0.0308  0.0348  109 LEU   B O   
5553 C  CB  . LEU   B 109 ? 0.1709 0.1455 0.2770 0.0028  0.0240  0.0457  109 LEU   B CB  
5554 C  CG  . LEU   B 109 ? 0.1661 0.1442 0.2653 0.0049  0.0193  0.0231  109 LEU   B CG  
5555 C  CD1 . LEU   B 109 ? 0.1614 0.1490 0.2528 0.0052  0.0138  0.0176  109 LEU   B CD1 
5556 C  CD2 . LEU   B 109 ? 0.1794 0.1440 0.2733 0.0060  0.0235  0.0247  109 LEU   B CD2 
5568 N  N   . LYS   B 110 ? 0.1516 0.1387 0.2692 -0.0079 0.0356  0.0181  110 LYS   B N   
5569 C  CA  . LYS   B 110 ? 0.1475 0.1374 0.2771 -0.0070 0.0290  0.0124  110 LYS   B CA  
5570 C  C   . LYS   B 110 ? 0.1420 0.1438 0.2669 -0.0059 0.0330  0.0168  110 LYS   B C   
5571 O  O   . LYS   B 110 ? 0.1368 0.1396 0.2699 -0.0090 0.0239  0.0061  110 LYS   B O   
5572 C  CB  . LYS   B 110 ? 0.1476 0.1356 0.3055 -0.0016 0.0276  0.0175  110 LYS   B CB  
5573 C  CG  . LYS   B 110 ? 0.1511 0.1391 0.3059 -0.0018 0.0182  0.0203  110 LYS   B CG  
5574 C  CD  . LYS   B 110 ? 0.1520 0.1418 0.3048 -0.0053 0.0142  0.0223  110 LYS   B CD  
5575 C  CE  . LYS   B 110 ? 0.1567 0.1561 0.3219 -0.0053 0.0131  0.0085  110 LYS   B CE  
5576 N  NZ  . LYS   B 110 ? 0.1576 0.1792 0.3154 0.0012  0.0139  0.0138  110 LYS   B NZ  
5590 N  N   . SER   B 111 ? 0.1461 0.1402 0.2716 -0.0058 0.0304  0.0182  111 SER   B N   
5591 C  CA  . SER   B 111 ? 0.1568 0.1409 0.2605 -0.0021 0.0205  0.0211  111 SER   B CA  
5592 C  C   . SER   B 111 ? 0.1486 0.1316 0.2512 -0.0015 0.0167  0.0060  111 SER   B C   
5593 O  O   . SER   B 111 ? 0.1437 0.1392 0.2676 -0.0025 0.0111  0.0063  111 SER   B O   
5594 C  CB  . SER   B 111 ? 0.1696 0.1602 0.2620 0.0045  0.0407  0.0297  111 SER   B CB  
5595 O  OG  . SER   B 111 ? 0.1898 0.1886 0.2664 0.0066  0.0386  0.0398  111 SER   B OG  
5601 N  N   . ALA   B 112 ? 0.1395 0.1378 0.2564 0.0022  0.0299  0.0118  112 ALA   B N   
5602 C  CA  . ALA   B 112 ? 0.1386 0.1434 0.2302 -0.0047 0.0199  0.0039  112 ALA   B CA  
5603 C  C   . ALA   B 112 ? 0.1313 0.1419 0.2251 -0.0047 0.0114  0.0001  112 ALA   B C   
5604 O  O   . ALA   B 112 ? 0.1350 0.1381 0.2352 -0.0102 0.0123  0.0002  112 ALA   B O   
5605 C  CB  . ALA   B 112 ? 0.1414 0.1428 0.2321 0.0016  0.0109  0.0140  112 ALA   B CB  
5611 N  N   . TYR   B 113 ? 0.1270 0.1270 0.2324 -0.0036 0.0158  0.0048  113 TYR   B N   
5612 C  CA  . TYR   B 113 ? 0.1256 0.1264 0.2368 -0.0052 0.0191  0.0018  113 TYR   B CA  
5613 C  C   . TYR   B 113 ? 0.1254 0.1179 0.2450 -0.0102 0.0147  0.0014  113 TYR   B C   
5614 O  O   . TYR   B 113 ? 0.1295 0.1245 0.2383 -0.0067 0.0036  0.0064  113 TYR   B O   
5615 C  CB  . TYR   B 113 ? 0.1307 0.1188 0.2493 -0.0077 0.0124  0.0103  113 TYR   B CB  
5616 C  CG  . TYR   B 113 ? 0.1284 0.1217 0.2514 -0.0054 0.0004  0.0114  113 TYR   B CG  
5617 C  CD1 . TYR   B 113 ? 0.1299 0.1344 0.2642 -0.0019 0.0116  0.0190  113 TYR   B CD1 
5618 C  CD2 . TYR   B 113 ? 0.1452 0.1176 0.2540 -0.0027 0.0033  0.0119  113 TYR   B CD2 
5619 C  CE1 . TYR   B 113 ? 0.1380 0.1332 0.2522 -0.0031 0.0098  0.0032  113 TYR   B CE1 
5620 C  CE2 . TYR   B 113 ? 0.1472 0.1183 0.2650 -0.0021 0.0045  0.0130  113 TYR   B CE2 
5621 C  CZ  . TYR   B 113 ? 0.1389 0.1259 0.2656 0.0061  0.0056  0.0064  113 TYR   B CZ  
5622 O  OH  . TYR   B 113 ? 0.1508 0.1228 0.3007 0.0098  0.0201  0.0090  113 TYR   B OH  
5632 N  N   . GLU   B 114 ? 0.1234 0.1141 0.2640 -0.0062 0.0152  0.0076  114 GLU   B N   
5633 C  CA  . GLU   B 114 ? 0.1258 0.1133 0.2639 -0.0004 0.0108  0.0043  114 GLU   B CA  
5634 C  C   . GLU   B 114 ? 0.1284 0.1131 0.2473 -0.0009 0.0090  0.0026  114 GLU   B C   
5635 O  O   . GLU   B 114 ? 0.1275 0.1201 0.2537 -0.0012 -0.0024 0.0130  114 GLU   B O   
5636 C  CB  . GLU   B 114 ? 0.1236 0.1235 0.2708 0.0003  0.0200  0.0129  114 GLU   B CB  
5637 C  CG  . GLU   B 114 ? 0.1272 0.1257 0.2783 -0.0053 0.0107  0.0166  114 GLU   B CG  
5638 C  CD  . GLU   B 114 ? 0.1296 0.1194 0.2754 -0.0105 0.0103  0.0126  114 GLU   B CD  
5639 O  OE1 . GLU   B 114 ? 0.1267 0.1413 0.2696 -0.0106 0.0203  0.0118  114 GLU   B OE1 
5640 O  OE2 . GLU   B 114 ? 0.1339 0.1445 0.2918 -0.0110 0.0103  0.0116  114 GLU   B OE2 
5647 N  N   . ASN   B 115 ? 0.1294 0.1141 0.2405 -0.0030 0.0006  0.0111  115 ASN   B N   
5648 C  CA  . ASN   B 115 ? 0.1282 0.1247 0.2220 -0.0121 0.0061  0.0103  115 ASN   B CA  
5649 C  C   . ASN   B 115 ? 0.1230 0.1195 0.2256 -0.0094 -0.0039 0.0020  115 ASN   B C   
5650 O  O   . ASN   B 115 ? 0.1346 0.1250 0.2286 -0.0118 0.0001  0.0059  115 ASN   B O   
5651 C  CB  . ASN   B 115 ? 0.1383 0.1360 0.2248 -0.0139 0.0044  -0.0003 115 ASN   B CB  
5652 C  CG  . ASN   B 115 ? 0.1512 0.1403 0.2291 -0.0034 0.0071  0.0002  115 ASN   B CG  
5653 O  OD1 . ASN   B 115 ? 0.1898 0.1544 0.2450 -0.0068 0.0135  -0.0030 115 ASN   B OD1 
5654 N  ND2 . ASN   B 115 ? 0.1438 0.1473 0.2337 -0.0057 0.0066  0.0139  115 ASN   B ND2 
5661 N  N   . PHE   B 116 ? 0.1293 0.1203 0.2156 -0.0069 0.0040  0.0022  116 PHE   B N   
5662 C  CA  . PHE   B 116 ? 0.1314 0.1248 0.2243 -0.0109 -0.0051 0.0102  116 PHE   B CA  
5663 C  C   . PHE   B 116 ? 0.1348 0.1118 0.2186 -0.0101 -0.0145 0.0023  116 PHE   B C   
5664 O  O   . PHE   B 116 ? 0.1349 0.1292 0.2233 -0.0063 -0.0154 0.0102  116 PHE   B O   
5665 C  CB  . PHE   B 116 ? 0.1236 0.1199 0.2134 -0.0072 -0.0103 0.0098  116 PHE   B CB  
5666 C  CG  . PHE   B 116 ? 0.1199 0.1249 0.2115 -0.0070 -0.0061 0.0063  116 PHE   B CG  
5667 C  CD1 . PHE   B 116 ? 0.1305 0.1272 0.2223 -0.0022 -0.0019 -0.0013 116 PHE   B CD1 
5668 C  CD2 . PHE   B 116 ? 0.1282 0.1319 0.2058 -0.0041 0.0011  0.0011  116 PHE   B CD2 
5669 C  CE1 . PHE   B 116 ? 0.1388 0.1293 0.2177 -0.0030 -0.0150 0.0037  116 PHE   B CE1 
5670 C  CE2 . PHE   B 116 ? 0.1302 0.1345 0.2021 -0.0021 -0.0008 0.0028  116 PHE   B CE2 
5671 C  CZ  . PHE   B 116 ? 0.1247 0.1335 0.2064 -0.0037 -0.0097 0.0126  116 PHE   B CZ  
5681 N  N   . ASN   B 117 ? 0.1320 0.1208 0.2334 -0.0027 -0.0183 0.0060  117 ASN   B N   
5682 C  CA  . ASN   B 117 ? 0.1378 0.1235 0.2406 -0.0011 -0.0138 0.0025  117 ASN   B CA  
5683 C  C   . ASN   B 117 ? 0.1390 0.1245 0.2530 -0.0031 -0.0143 0.0066  117 ASN   B C   
5684 O  O   . ASN   B 117 ? 0.1462 0.1305 0.2795 -0.0055 -0.0409 0.0139  117 ASN   B O   
5685 C  CB  . ASN   B 117 ? 0.1421 0.1181 0.2547 -0.0032 -0.0089 0.0021  117 ASN   B CB  
5686 C  CG  . ASN   B 117 ? 0.1359 0.1280 0.2610 0.0020  0.0012  0.0019  117 ASN   B CG  
5687 O  OD1 . ASN   B 117 ? 0.1499 0.1281 0.2712 -0.0161 -0.0023 0.0016  117 ASN   B OD1 
5688 N  ND2 . ASN   B 117 ? 0.1363 0.1287 0.2458 -0.0025 -0.0017 0.0024  117 ASN   B ND2 
5695 N  N   . GLN   B 118 ? 0.1383 0.1215 0.2440 -0.0078 -0.0249 0.0013  118 GLN   B N   
5696 C  CA  . GLN   B 118 ? 0.1429 0.1236 0.2557 -0.0013 -0.0157 0.0018  118 GLN   B CA  
5697 C  C   . GLN   B 118 ? 0.1472 0.1202 0.2575 -0.0005 -0.0225 0.0031  118 GLN   B C   
5698 O  O   . GLN   B 118 ? 0.1692 0.1237 0.2824 -0.0117 -0.0090 0.0085  118 GLN   B O   
5699 C  CB  . GLN   B 118 ? 0.1497 0.1278 0.2681 -0.0035 -0.0228 0.0104  118 GLN   B CB  
5700 C  CG  . GLN   B 118 ? 0.1581 0.1313 0.2649 0.0035  -0.0135 -0.0050 118 GLN   B CG  
5701 C  CD  . GLN   B 118 ? 0.1629 0.1277 0.2680 0.0032  -0.0148 -0.0093 118 GLN   B CD  
5702 O  OE1 . GLN   B 118 ? 0.1666 0.1251 0.2865 0.0014  -0.0046 0.0064  118 GLN   B OE1 
5703 N  NE2 . GLN   B 118 ? 0.1719 0.1298 0.2741 0.0046  -0.0169 0.0059  118 GLN   B NE2 
5712 N  N   . HIS   B 119 ? 0.1520 0.1265 0.2271 -0.0068 -0.0212 0.0139  119 HIS   B N   
5713 C  CA  . HIS   B 119 ? 0.1641 0.1391 0.2064 -0.0077 -0.0214 0.0123  119 HIS   B CA  
5714 C  C   . HIS   B 119 ? 0.1737 0.1437 0.1953 -0.0108 -0.0434 0.0157  119 HIS   B C   
5715 O  O   . HIS   B 119 ? 0.1772 0.1376 0.2211 -0.0370 -0.0347 0.0171  119 HIS   B O   
5716 C  CB  . HIS   B 119 ? 0.1636 0.1490 0.1964 -0.0023 -0.0207 0.0009  119 HIS   B CB  
5717 C  CG  . HIS   B 119 ? 0.1692 0.1706 0.2018 0.0055  -0.0428 -0.0092 119 HIS   B CG  
5718 N  ND1 . HIS   B 119 ? 0.1798 0.1894 0.2383 -0.0013 -0.0470 -0.0207 119 HIS   B ND1 
5719 C  CD2 . HIS   B 119 ? 0.1905 0.1956 0.2042 0.0349  -0.0527 -0.0113 119 HIS   B CD2 
5720 C  CE1 . HIS   B 119 ? 0.2018 0.2043 0.2395 0.0176  -0.0532 -0.0304 119 HIS   B CE1 
5721 N  NE2 . HIS   B 119 ? 0.2077 0.2178 0.2244 0.0319  -0.0495 -0.0333 119 HIS   B NE2 
5729 N  N   A GLU   B 120 ? 0.1908 0.1422 0.1925 -0.0206 -0.0573 0.0294  120 GLU   B N   
5730 N  N   B GLU   B 120 ? 0.1957 0.1617 0.2032 -0.0143 -0.0462 0.0220  120 GLU   B N   
5731 C  CA  A GLU   B 120 ? 0.2229 0.1610 0.2115 -0.0157 -0.0651 0.0524  120 GLU   B CA  
5732 C  CA  B GLU   B 120 ? 0.2217 0.1832 0.2259 -0.0135 -0.0478 0.0304  120 GLU   B CA  
5733 C  C   A GLU   B 120 ? 0.1984 0.1449 0.1873 -0.0249 -0.0535 0.0384  120 GLU   B C   
5734 C  C   B GLU   B 120 ? 0.2051 0.1645 0.1961 -0.0218 -0.0452 0.0303  120 GLU   B C   
5735 O  O   A GLU   B 120 ? 0.1839 0.1552 0.2089 -0.0238 -0.0461 0.0216  120 GLU   B O   
5736 O  O   B GLU   B 120 ? 0.2014 0.1716 0.1956 -0.0197 -0.0426 0.0247  120 GLU   B O   
5737 C  CB  A GLU   B 120 ? 0.2798 0.2043 0.2872 0.0005  -0.0816 0.0882  120 GLU   B CB  
5738 C  CB  B GLU   B 120 ? 0.2633 0.2233 0.2953 -0.0032 -0.0522 0.0383  120 GLU   B CB  
5739 C  CG  A GLU   B 120 ? 0.3282 0.2753 0.3903 0.0096  -0.0943 0.1065  120 GLU   B CG  
5740 C  CG  B GLU   B 120 ? 0.2980 0.2685 0.3710 0.0036  -0.0557 0.0466  120 GLU   B CG  
5741 C  CD  A GLU   B 120 ? 0.3610 0.3294 0.4899 0.0105  -0.0970 0.1159  120 GLU   B CD  
5742 C  CD  B GLU   B 120 ? 0.3267 0.3043 0.4396 0.0076  -0.0541 0.0526  120 GLU   B CD  
5743 O  OE1 A GLU   B 120 ? 0.3781 0.3459 0.5255 0.0057  -0.0892 0.1248  120 GLU   B OE1 
5744 O  OE1 B GLU   B 120 ? 0.3398 0.3168 0.4650 0.0085  -0.0523 0.0564  120 GLU   B OE1 
5745 O  OE2 A GLU   B 120 ? 0.3759 0.3532 0.5377 0.0089  -0.0957 0.1083  120 GLU   B OE2 
5746 O  OE2 B GLU   B 120 ? 0.3381 0.3143 0.4648 0.0069  -0.0550 0.0539  120 GLU   B OE2 
5759 N  N   . VAL   B 121 ? 0.1913 0.1469 0.1934 -0.0307 -0.0441 0.0328  121 VAL   B N   
5760 C  CA  . VAL   B 121 ? 0.1844 0.1581 0.1719 -0.0275 -0.0393 0.0313  121 VAL   B CA  
5761 C  C   . VAL   B 121 ? 0.1741 0.1470 0.1641 -0.0319 -0.0255 0.0217  121 VAL   B C   
5762 O  O   . VAL   B 121 ? 0.1806 0.1428 0.1881 -0.0378 -0.0311 0.0227  121 VAL   B O   
5763 C  CB  . VAL   B 121 ? 0.2085 0.1998 0.1879 -0.0280 -0.0455 0.0363  121 VAL   B CB  
5764 C  CG1 . VAL   B 121 ? 0.2105 0.2108 0.2227 -0.0425 -0.0361 0.0318  121 VAL   B CG1 
5765 C  CG2 . VAL   B 121 ? 0.2354 0.2314 0.1945 -0.0163 -0.0387 0.0272  121 VAL   B CG2 
5776 N  N   . LEU   B 122 ? 0.1621 0.1417 0.1660 -0.0264 -0.0358 0.0160  122 LEU   B N   
5777 C  CA  . LEU   B 122 ? 0.1497 0.1514 0.1566 -0.0233 -0.0275 0.0162  122 LEU   B CA  
5778 C  C   . LEU   B 122 ? 0.1486 0.1355 0.1685 -0.0327 -0.0142 0.0147  122 LEU   B C   
5779 O  O   . LEU   B 122 ? 0.1596 0.1409 0.1937 -0.0383 -0.0237 0.0117  122 LEU   B O   
5780 C  CB  . LEU   B 122 ? 0.1748 0.1626 0.1864 -0.0087 -0.0298 0.0136  122 LEU   B CB  
5781 C  CG  . LEU   B 122 ? 0.1594 0.1726 0.2003 -0.0207 -0.0160 0.0202  122 LEU   B CG  
5782 C  CD1 . LEU   B 122 ? 0.1643 0.1971 0.1939 -0.0279 -0.0202 0.0139  122 LEU   B CD1 
5783 C  CD2 . LEU   B 122 ? 0.1556 0.1723 0.1799 -0.0138 -0.0156 0.0112  122 LEU   B CD2 
5795 N  N   . LEU   B 123 ? 0.1482 0.1266 0.1686 -0.0234 -0.0225 0.0157  123 LEU   B N   
5796 C  CA  . LEU   B 123 ? 0.1553 0.1335 0.1586 -0.0298 -0.0221 0.0025  123 LEU   B CA  
5797 C  C   . LEU   B 123 ? 0.1469 0.1331 0.1538 -0.0338 -0.0208 0.0031  123 LEU   B C   
5798 O  O   . LEU   B 123 ? 0.1588 0.1335 0.1607 -0.0353 -0.0225 -0.0020 123 LEU   B O   
5799 C  CB  . LEU   B 123 ? 0.1662 0.1362 0.1724 -0.0254 -0.0179 -0.0024 123 LEU   B CB  
5800 C  CG  . LEU   B 123 ? 0.1592 0.1415 0.1807 -0.0250 -0.0100 0.0059  123 LEU   B CG  
5801 C  CD1 . LEU   B 123 ? 0.1675 0.1432 0.1946 -0.0226 -0.0010 -0.0077 123 LEU   B CD1 
5802 C  CD2 . LEU   B 123 ? 0.1661 0.1543 0.1870 -0.0237 -0.0057 0.0183  123 LEU   B CD2 
5814 N  N   . ALA   B 124 ? 0.1426 0.1282 0.1471 -0.0204 -0.0176 0.0001  124 ALA   B N   
5815 C  CA  . ALA   B 124 ? 0.1386 0.1272 0.1661 -0.0133 -0.0154 -0.0048 124 ALA   B CA  
5816 C  C   . ALA   B 124 ? 0.1348 0.1220 0.1589 -0.0187 -0.0145 0.0025  124 ALA   B C   
5817 O  O   . ALA   B 124 ? 0.1459 0.1246 0.1827 -0.0167 -0.0177 0.0007  124 ALA   B O   
5818 C  CB  . ALA   B 124 ? 0.1442 0.1337 0.1776 -0.0118 -0.0075 -0.0001 124 ALA   B CB  
5824 N  N   . PRO   B 125 ? 0.1470 0.1262 0.1600 -0.0185 -0.0156 0.0124  125 PRO   B N   
5825 C  CA  . PRO   B 125 ? 0.1488 0.1293 0.1796 -0.0161 -0.0164 0.0199  125 PRO   B CA  
5826 C  C   . PRO   B 125 ? 0.1446 0.1275 0.2053 -0.0151 -0.0103 0.0087  125 PRO   B C   
5827 O  O   . PRO   B 125 ? 0.1453 0.1281 0.2151 -0.0085 -0.0063 0.0164  125 PRO   B O   
5828 C  CB  . PRO   B 125 ? 0.1497 0.1519 0.1958 -0.0183 -0.0234 0.0299  125 PRO   B CB  
5829 C  CG  . PRO   B 125 ? 0.1583 0.1565 0.1770 -0.0233 -0.0300 0.0215  125 PRO   B CG  
5830 C  CD  . PRO   B 125 ? 0.1553 0.1419 0.1658 -0.0291 -0.0185 0.0095  125 PRO   B CD  
5838 N  N   . LEU   B 126 ? 0.1477 0.1244 0.2271 -0.0172 0.0069  0.0234  126 LEU   B N   
5839 C  CA  . LEU   B 126 ? 0.1578 0.1335 0.2249 -0.0104 0.0090  0.0163  126 LEU   B CA  
5840 C  C   . LEU   B 126 ? 0.1501 0.1515 0.2281 0.0037  0.0166  0.0200  126 LEU   B C   
5841 O  O   . LEU   B 126 ? 0.1779 0.1783 0.2597 0.0236  -0.0034 -0.0038 126 LEU   B O   
5842 C  CB  . LEU   B 126 ? 0.1743 0.1376 0.2436 -0.0142 0.0167  0.0148  126 LEU   B CB  
5843 C  CG  . LEU   B 126 ? 0.1951 0.1457 0.2531 -0.0220 0.0162  -0.0043 126 LEU   B CG  
5844 C  CD1 . LEU   B 126 ? 0.2103 0.1464 0.2961 -0.0155 0.0097  -0.0082 126 LEU   B CD1 
5845 C  CD2 . LEU   B 126 ? 0.2004 0.1592 0.2542 -0.0292 0.0203  0.0002  126 LEU   B CD2 
5857 N  N   . LEU   B 127 ? 0.1468 0.1321 0.2402 -0.0003 0.0209  0.0123  127 LEU   B N   
5858 C  CA  . LEU   B 127 ? 0.1520 0.1417 0.2462 -0.0059 0.0247  0.0213  127 LEU   B CA  
5859 C  C   . LEU   B 127 ? 0.1546 0.1315 0.2523 -0.0011 0.0177  0.0255  127 LEU   B C   
5860 O  O   . LEU   B 127 ? 0.1571 0.1346 0.2618 -0.0182 0.0146  0.0229  127 LEU   B O   
5861 C  CB  . LEU   B 127 ? 0.1646 0.1394 0.2568 -0.0072 0.0221  0.0245  127 LEU   B CB  
5862 C  CG  . LEU   B 127 ? 0.1777 0.1407 0.2735 -0.0031 0.0257  0.0236  127 LEU   B CG  
5863 C  CD1 . LEU   B 127 ? 0.1878 0.1377 0.2765 0.0015  0.0231  0.0162  127 LEU   B CD1 
5864 C  CD2 . LEU   B 127 ? 0.1813 0.1510 0.2850 -0.0212 0.0267  0.0335  127 LEU   B CD2 
5876 N  N   . SER   B 128 ? 0.1623 0.1320 0.2471 0.0014  0.0003  0.0215  128 SER   B N   
5877 C  CA  . SER   B 128 ? 0.1726 0.1399 0.2495 0.0060  -0.0124 0.0230  128 SER   B CA  
5878 C  C   . SER   B 128 ? 0.1845 0.1459 0.2916 0.0042  -0.0312 0.0172  128 SER   B C   
5879 O  O   . SER   B 128 ? 0.2023 0.1511 0.3233 -0.0017 -0.0318 0.0307  128 SER   B O   
5880 C  CB  . SER   B 128 ? 0.1789 0.1440 0.2490 0.0008  -0.0023 0.0424  128 SER   B CB  
5881 O  OG  . SER   B 128 ? 0.1783 0.1650 0.2477 0.0071  0.0077  0.0432  128 SER   B OG  
5887 N  N   . ALA   B 129 ? 0.1954 0.1547 0.3156 0.0241  -0.0140 0.0057  129 ALA   B N   
5888 C  CA  . ALA   B 129 ? 0.2082 0.1652 0.3359 0.0356  -0.0124 -0.0088 129 ALA   B CA  
5889 C  C   . ALA   B 129 ? 0.1944 0.1552 0.3220 0.0227  0.0004  0.0019  129 ALA   B C   
5890 O  O   . ALA   B 129 ? 0.1865 0.1585 0.3200 0.0147  -0.0098 -0.0062 129 ALA   B O   
5891 C  CB  . ALA   B 129 ? 0.2273 0.1854 0.3627 0.0396  0.0079  -0.0152 129 ALA   B CB  
5897 N  N   . GLY   B 130 ? 0.1943 0.1536 0.3164 0.0275  0.0028  -0.0036 130 GLY   B N   
5898 C  CA  . GLY   B 130 ? 0.1952 0.1617 0.3118 0.0256  0.0297  -0.0070 130 GLY   B CA  
5899 C  C   . GLY   B 130 ? 0.2033 0.1664 0.2961 0.0156  0.0252  0.0053  130 GLY   B C   
5900 O  O   . GLY   B 130 ? 0.2149 0.1782 0.3038 0.0200  0.0118  0.0117  130 GLY   B O   
5904 N  N   . ILE   B 131 ? 0.1993 0.1777 0.2974 0.0254  0.0238  0.0040  131 ILE   B N   
5905 C  CA  . ILE   B 131 ? 0.2204 0.2000 0.2923 0.0248  0.0175  0.0167  131 ILE   B CA  
5906 C  C   . ILE   B 131 ? 0.2281 0.1909 0.2634 0.0189  0.0161  0.0242  131 ILE   B C   
5907 O  O   . ILE   B 131 ? 0.2504 0.2082 0.2782 0.0169  0.0029  0.0254  131 ILE   B O   
5908 C  CB  . ILE   B 131 ? 0.2215 0.2275 0.3190 0.0203  0.0034  0.0257  131 ILE   B CB  
5909 C  CG1 . ILE   B 131 ? 0.2258 0.2431 0.3344 -0.0045 -0.0007 0.0276  131 ILE   B CG1 
5910 C  CG2 . ILE   B 131 ? 0.2171 0.2454 0.3383 0.0301  -0.0016 0.0204  131 ILE   B CG2 
5911 C  CD1 . ILE   B 131 ? 0.2290 0.2611 0.3559 -0.0205 -0.0120 0.0284  131 ILE   B CD1 
5923 N  N   . PHE   B 132 ? 0.2187 0.1749 0.2522 0.0124  0.0327  0.0244  132 PHE   B N   
5924 C  CA  . PHE   B 132 ? 0.2343 0.1763 0.2553 0.0072  0.0436  0.0213  132 PHE   B CA  
5925 C  C   . PHE   B 132 ? 0.2539 0.1909 0.2791 0.0083  0.0524  0.0173  132 PHE   B C   
5926 O  O   . PHE   B 132 ? 0.2702 0.2199 0.3041 0.0018  0.0690  0.0201  132 PHE   B O   
5927 C  CB  . PHE   B 132 ? 0.2166 0.1698 0.2315 0.0113  0.0440  0.0207  132 PHE   B CB  
5928 C  CG  . PHE   B 132 ? 0.2075 0.1700 0.2340 0.0152  0.0234  0.0259  132 PHE   B CG  
5929 C  CD1 . PHE   B 132 ? 0.2201 0.1796 0.2648 0.0090  0.0237  0.0240  132 PHE   B CD1 
5930 C  CD2 . PHE   B 132 ? 0.2020 0.1754 0.2305 0.0272  0.0192  0.0359  132 PHE   B CD2 
5931 C  CE1 . PHE   B 132 ? 0.2213 0.1830 0.2641 0.0037  0.0126  0.0260  132 PHE   B CE1 
5932 C  CE2 . PHE   B 132 ? 0.2115 0.1804 0.2324 0.0206  0.0080  0.0376  132 PHE   B CE2 
5933 C  CZ  . PHE   B 132 ? 0.2181 0.1841 0.2497 0.0112  0.0015  0.0438  132 PHE   B CZ  
5943 N  N   . GLY   B 133 ? 0.2498 0.1741 0.2752 0.0033  0.0439  0.0371  133 GLY   B N   
5944 C  CA  . GLY   B 133 ? 0.2663 0.1891 0.2907 -0.0186 0.0404  0.0417  133 GLY   B CA  
5945 C  C   . GLY   B 133 ? 0.2745 0.2020 0.3026 -0.0357 0.0426  0.0469  133 GLY   B C   
5946 O  O   . GLY   B 133 ? 0.2899 0.2130 0.3398 -0.0499 0.0359  0.0601  133 GLY   B O   
5950 N  N   . ALA   B 134 ? 0.2521 0.2028 0.2851 -0.0341 0.0426  0.0291  134 ALA   B N   
5951 C  CA  . ALA   B 134 ? 0.2484 0.1980 0.2863 -0.0287 0.0506  0.0162  134 ALA   B CA  
5952 C  C   . ALA   B 134 ? 0.2575 0.1809 0.2912 -0.0236 0.0433  0.0319  134 ALA   B C   
5953 O  O   . ALA   B 134 ? 0.2575 0.2005 0.3032 -0.0082 0.0255  0.0337  134 ALA   B O   
5954 C  CB  . ALA   B 134 ? 0.2425 0.2042 0.2931 -0.0253 0.0429  0.0095  134 ALA   B CB  
5960 N  N   . ASP   B 135 ? 0.2715 0.1726 0.3001 -0.0247 0.0262  0.0338  135 ASP   B N   
5961 C  CA  . ASP   B 135 ? 0.2868 0.1675 0.3178 -0.0238 0.0063  0.0410  135 ASP   B CA  
5962 C  C   . ASP   B 135 ? 0.2599 0.1539 0.3013 -0.0099 0.0048  0.0428  135 ASP   B C   
5963 O  O   . ASP   B 135 ? 0.2460 0.1506 0.3182 -0.0154 0.0064  0.0350  135 ASP   B O   
5964 C  CB  . ASP   B 135 ? 0.3184 0.1775 0.3481 -0.0393 0.0015  0.0399  135 ASP   B CB  
5965 C  CG  . ASP   B 135 ? 0.3448 0.1829 0.3930 -0.0543 -0.0027 0.0351  135 ASP   B CG  
5966 O  OD1 . ASP   B 135 ? 0.3536 0.1696 0.3938 -0.0360 -0.0075 0.0424  135 ASP   B OD1 
5967 O  OD2 . ASP   B 135 ? 0.3625 0.2159 0.4459 -0.0707 -0.0029 0.0180  135 ASP   B OD2 
5972 N  N   . PRO   B 136 ? 0.2454 0.1645 0.3027 0.0132  -0.0116 0.0341  136 PRO   B N   
5973 C  CA  . PRO   B 136 ? 0.2163 0.1577 0.3071 0.0187  -0.0102 0.0188  136 PRO   B CA  
5974 C  C   . PRO   B 136 ? 0.1914 0.1406 0.3229 0.0109  -0.0053 0.0138  136 PRO   B C   
5975 O  O   . PRO   B 136 ? 0.1731 0.1359 0.3195 0.0061  -0.0105 0.0177  136 PRO   B O   
5976 C  CB  . PRO   B 136 ? 0.2191 0.1822 0.3003 0.0340  -0.0205 0.0097  136 PRO   B CB  
5977 C  CG  . PRO   B 136 ? 0.2436 0.1899 0.3151 0.0369  -0.0146 0.0081  136 PRO   B CG  
5978 C  CD  . PRO   B 136 ? 0.2544 0.1833 0.3096 0.0378  -0.0130 0.0191  136 PRO   B CD  
5986 N  N   . ILE   B 137 ? 0.1990 0.1332 0.3393 0.0089  -0.0106 0.0100  137 ILE   B N   
5987 C  CA  . ILE   B 137 ? 0.2074 0.1264 0.3522 -0.0037 -0.0090 0.0020  137 ILE   B CA  
5988 C  C   . ILE   B 137 ? 0.1987 0.1305 0.3319 -0.0101 0.0048  0.0145  137 ILE   B C   
5989 O  O   . ILE   B 137 ? 0.1924 0.1370 0.3171 -0.0129 0.0057  0.0127  137 ILE   B O   
5990 C  CB  . ILE   B 137 ? 0.2359 0.1356 0.4034 -0.0036 -0.0037 0.0108  137 ILE   B CB  
5991 C  CG1 . ILE   B 137 ? 0.2540 0.1490 0.4493 0.0103  -0.0065 0.0056  137 ILE   B CG1 
5992 C  CG2 . ILE   B 137 ? 0.2419 0.1407 0.4112 -0.0338 -0.0006 0.0223  137 ILE   B CG2 
5993 C  CD1 . ILE   B 137 ? 0.2740 0.1809 0.4839 0.0231  -0.0163 0.0089  137 ILE   B CD1 
6005 N  N   . HIS   B 138 ? 0.2072 0.1328 0.3329 -0.0107 0.0102  0.0195  138 HIS   B N   
6006 C  CA  . HIS   B 138 ? 0.2149 0.1430 0.3200 -0.0124 0.0273  0.0210  138 HIS   B CA  
6007 C  C   . HIS   B 138 ? 0.1946 0.1395 0.3162 -0.0081 0.0247  0.0251  138 HIS   B C   
6008 O  O   . HIS   B 138 ? 0.1886 0.1439 0.3454 -0.0027 0.0327  0.0339  138 HIS   B O   
6009 C  CB  . HIS   B 138 ? 0.2469 0.1558 0.3213 -0.0229 0.0600  0.0223  138 HIS   B CB  
6010 C  CG  . HIS   B 138 ? 0.2814 0.1765 0.3306 -0.0283 0.0868  0.0342  138 HIS   B CG  
6011 N  ND1 . HIS   B 138 ? 0.2944 0.1960 0.3538 -0.0213 0.0978  0.0276  138 HIS   B ND1 
6012 C  CD2 . HIS   B 138 ? 0.3031 0.1872 0.3208 -0.0195 0.0929  0.0290  138 HIS   B CD2 
6013 C  CE1 . HIS   B 138 ? 0.3050 0.2049 0.3499 -0.0146 0.0998  0.0279  138 HIS   B CE1 
6014 N  NE2 . HIS   B 138 ? 0.3127 0.1889 0.3294 -0.0111 0.0991  0.0251  138 HIS   B NE2 
6022 N  N   . SER   B 139 ? 0.1865 0.1296 0.3049 -0.0019 0.0178  0.0161  139 SER   B N   
6023 C  CA  . SER   B 139 ? 0.1846 0.1217 0.2817 -0.0032 0.0225  0.0045  139 SER   B CA  
6024 C  C   . SER   B 139 ? 0.1603 0.1197 0.2794 -0.0018 0.0144  0.0051  139 SER   B C   
6025 O  O   . SER   B 139 ? 0.1603 0.1251 0.2744 -0.0008 0.0071  0.0108  139 SER   B O   
6026 C  CB  . SER   B 139 ? 0.2005 0.1219 0.2917 -0.0036 0.0035  0.0058  139 SER   B CB  
6027 O  OG  . SER   B 139 ? 0.1994 0.1246 0.3002 -0.0039 -0.0133 0.0187  139 SER   B OG  
6033 N  N   . LEU   B 140 ? 0.1664 0.1207 0.2778 -0.0061 0.0218  -0.0016 140 LEU   B N   
6034 C  CA  . LEU   B 140 ? 0.1597 0.1193 0.2740 -0.0054 0.0145  0.0005  140 LEU   B CA  
6035 C  C   . LEU   B 140 ? 0.1555 0.1210 0.2902 -0.0081 -0.0005 -0.0022 140 LEU   B C   
6036 O  O   . LEU   B 140 ? 0.1495 0.1342 0.2833 -0.0063 -0.0036 0.0061  140 LEU   B O   
6037 C  CB  . LEU   B 140 ? 0.1601 0.1180 0.2775 -0.0081 0.0165  0.0028  140 LEU   B CB  
6038 C  CG  . LEU   B 140 ? 0.1688 0.1193 0.2856 -0.0093 0.0050  0.0097  140 LEU   B CG  
6039 C  CD1 . LEU   B 140 ? 0.1740 0.1335 0.2984 -0.0158 0.0005  0.0009  140 LEU   B CD1 
6040 C  CD2 . LEU   B 140 ? 0.1868 0.1358 0.3000 -0.0058 -0.0008 -0.0005 140 LEU   B CD2 
6052 N  N   . ARG   B 141 ? 0.1463 0.1260 0.3096 -0.0094 0.0054  -0.0021 141 ARG   B N   
6053 C  CA  . ARG   B 141 ? 0.1443 0.1273 0.3420 -0.0168 0.0147  -0.0061 141 ARG   B CA  
6054 C  C   . ARG   B 141 ? 0.1375 0.1236 0.3406 -0.0146 0.0091  -0.0025 141 ARG   B C   
6055 O  O   . ARG   B 141 ? 0.1471 0.1267 0.3439 -0.0125 -0.0044 -0.0129 141 ARG   B O   
6056 C  CB  . ARG   B 141 ? 0.1654 0.1389 0.3636 -0.0259 0.0252  -0.0092 141 ARG   B CB  
6057 C  CG  . ARG   B 141 ? 0.2021 0.1663 0.3697 -0.0274 0.0266  -0.0008 141 ARG   B CG  
6058 C  CD  . ARG   B 141 ? 0.2435 0.1937 0.3616 -0.0215 0.0177  -0.0056 141 ARG   B CD  
6059 N  NE  . ARG   B 141 ? 0.2649 0.1885 0.3487 -0.0294 0.0225  -0.0163 141 ARG   B NE  
6060 C  CZ  . ARG   B 141 ? 0.2836 0.1770 0.3287 -0.0213 0.0205  -0.0292 141 ARG   B CZ  
6061 N  NH1 . ARG   B 141 ? 0.2907 0.1653 0.3185 -0.0210 0.0187  -0.0273 141 ARG   B NH1 
6062 N  NH2 . ARG   B 141 ? 0.3006 0.1909 0.3370 -0.0035 0.0067  -0.0174 141 ARG   B NH2 
6076 N  N   . VAL   B 142 ? 0.1524 0.1218 0.3342 -0.0118 0.0133  -0.0056 142 VAL   B N   
6077 C  CA  . VAL   B 142 ? 0.1448 0.1242 0.3091 -0.0073 0.0155  -0.0011 142 VAL   B CA  
6078 C  C   . VAL   B 142 ? 0.1373 0.1255 0.3069 -0.0038 0.0024  -0.0081 142 VAL   B C   
6079 O  O   . VAL   B 142 ? 0.1446 0.1258 0.3216 -0.0020 0.0191  -0.0016 142 VAL   B O   
6080 C  CB  . VAL   B 142 ? 0.1583 0.1391 0.3016 -0.0022 0.0198  0.0064  142 VAL   B CB  
6081 C  CG1 . VAL   B 142 ? 0.1560 0.1367 0.2929 -0.0012 0.0239  0.0023  142 VAL   B CG1 
6082 C  CG2 . VAL   B 142 ? 0.1779 0.1466 0.2960 0.0038  0.0240  0.0037  142 VAL   B CG2 
6092 N  N   . CYS   B 143 ? 0.1362 0.1254 0.2951 -0.0034 -0.0023 0.0052  143 CYS   B N   
6093 C  CA  . CYS   B 143 ? 0.1373 0.1241 0.2992 -0.0087 -0.0017 0.0085  143 CYS   B CA  
6094 C  C   . CYS   B 143 ? 0.1330 0.1256 0.3071 -0.0063 0.0021  0.0026  143 CYS   B C   
6095 O  O   . CYS   B 143 ? 0.1380 0.1290 0.3108 -0.0056 -0.0018 0.0055  143 CYS   B O   
6096 C  CB  . CYS   B 143 ? 0.1472 0.1325 0.2867 -0.0100 -0.0044 0.0034  143 CYS   B CB  
6097 S  SG  . CYS   B 143 ? 0.1460 0.1498 0.2809 -0.0082 0.0005  0.0088  143 CYS   B SG  
6103 N  N   . VAL   B 144 ? 0.1343 0.1263 0.3291 -0.0115 -0.0046 -0.0081 144 VAL   B N   
6104 C  CA  . VAL   B 144 ? 0.1446 0.1390 0.3440 -0.0191 -0.0173 -0.0123 144 VAL   B CA  
6105 C  C   . VAL   B 144 ? 0.1400 0.1386 0.3485 -0.0093 -0.0126 -0.0008 144 VAL   B C   
6106 O  O   . VAL   B 144 ? 0.1478 0.1644 0.3651 -0.0044 -0.0175 0.0186  144 VAL   B O   
6107 C  CB  . VAL   B 144 ? 0.1713 0.1510 0.3816 -0.0217 -0.0311 -0.0240 144 VAL   B CB  
6108 C  CG1 . VAL   B 144 ? 0.2001 0.1927 0.4021 -0.0142 -0.0298 -0.0184 144 VAL   B CG1 
6109 C  CG2 . VAL   B 144 ? 0.1895 0.1561 0.3725 -0.0074 -0.0409 -0.0382 144 VAL   B CG2 
6119 N  N   . ASP   B 145 ? 0.1420 0.1299 0.3534 -0.0110 -0.0105 -0.0063 145 ASP   B N   
6120 C  CA  . ASP   B 145 ? 0.1437 0.1343 0.3753 -0.0082 0.0022  0.0020  145 ASP   B CA  
6121 C  C   . ASP   B 145 ? 0.1410 0.1407 0.3624 -0.0110 -0.0034 0.0059  145 ASP   B C   
6122 O  O   . ASP   B 145 ? 0.1416 0.1531 0.4040 -0.0134 0.0011  -0.0077 145 ASP   B O   
6123 C  CB  . ASP   B 145 ? 0.1555 0.1470 0.4226 -0.0128 0.0100  0.0080  145 ASP   B CB  
6124 C  CG  . ASP   B 145 ? 0.1732 0.1480 0.4729 -0.0207 0.0194  0.0087  145 ASP   B CG  
6125 O  OD1 . ASP   B 145 ? 0.1746 0.1521 0.4747 -0.0243 -0.0188 -0.0042 145 ASP   B OD1 
6126 O  OD2 . ASP   B 145 ? 0.2046 0.1587 0.5184 -0.0353 0.0425  0.0189  145 ASP   B OD2 
6131 N  N   . THR   B 146 ? 0.1376 0.1249 0.3196 -0.0131 -0.0043 0.0088  146 THR   B N   
6132 C  CA  . THR   B 146 ? 0.1420 0.1244 0.3048 -0.0101 0.0009  0.0048  146 THR   B CA  
6133 C  C   . THR   B 146 ? 0.1396 0.1265 0.2905 -0.0062 -0.0060 0.0102  146 THR   B C   
6134 O  O   . THR   B 146 ? 0.1458 0.1211 0.2946 -0.0080 -0.0106 0.0120  146 THR   B O   
6135 C  CB  . THR   B 146 ? 0.1431 0.1297 0.3014 -0.0079 0.0120  0.0044  146 THR   B CB  
6136 O  OG1 . THR   B 146 ? 0.1464 0.1286 0.3134 -0.0070 0.0197  0.0163  146 THR   B OG1 
6137 C  CG2 . THR   B 146 ? 0.1524 0.1373 0.2875 -0.0060 0.0066  -0.0052 146 THR   B CG2 
6145 N  N   . VAL   B 147 ? 0.1410 0.1317 0.2684 -0.0049 0.0059  0.0117  147 VAL   B N   
6146 C  CA  . VAL   B 147 ? 0.1430 0.1243 0.2582 -0.0161 -0.0101 0.0109  147 VAL   B CA  
6147 C  C   . VAL   B 147 ? 0.1396 0.1255 0.2796 -0.0230 -0.0193 0.0039  147 VAL   B C   
6148 O  O   . VAL   B 147 ? 0.1549 0.1363 0.2953 -0.0240 -0.0308 0.0032  147 VAL   B O   
6149 C  CB  . VAL   B 147 ? 0.1469 0.1378 0.2330 -0.0120 -0.0159 0.0064  147 VAL   B CB  
6150 C  CG1 . VAL   B 147 ? 0.1482 0.1564 0.2112 -0.0132 -0.0181 0.0068  147 VAL   B CG1 
6151 C  CG2 . VAL   B 147 ? 0.1510 0.1363 0.2408 -0.0134 -0.0048 0.0022  147 VAL   B CG2 
6161 N  N   . ARG   B 148 ? 0.1413 0.1317 0.2712 -0.0139 -0.0343 -0.0046 148 ARG   B N   
6162 C  CA  . ARG   B 148 ? 0.1500 0.1406 0.2644 -0.0124 -0.0392 -0.0084 148 ARG   B CA  
6163 C  C   . ARG   B 148 ? 0.1580 0.1459 0.2407 -0.0147 -0.0414 0.0075  148 ARG   B C   
6164 O  O   . ARG   B 148 ? 0.1779 0.1771 0.2443 -0.0308 -0.0448 0.0123  148 ARG   B O   
6165 C  CB  . ARG   B 148 ? 0.1562 0.1475 0.2654 -0.0066 -0.0403 -0.0137 148 ARG   B CB  
6166 C  CG  . ARG   B 148 ? 0.1572 0.1633 0.2691 -0.0101 -0.0461 -0.0284 148 ARG   B CG  
6167 C  CD  . ARG   B 148 ? 0.1648 0.1840 0.2805 0.0062  -0.0400 -0.0323 148 ARG   B CD  
6168 N  NE  . ARG   B 148 ? 0.1674 0.1808 0.2811 0.0217  -0.0423 -0.0281 148 ARG   B NE  
6169 C  CZ  . ARG   B 148 ? 0.1582 0.1679 0.2702 0.0151  -0.0288 -0.0224 148 ARG   B CZ  
6170 N  NH1 . ARG   B 148 ? 0.1469 0.1718 0.2796 0.0082  -0.0124 -0.0211 148 ARG   B NH1 
6171 N  NH2 . ARG   B 148 ? 0.1725 0.1541 0.2714 0.0130  -0.0272 -0.0171 148 ARG   B NH2 
6185 N  N   . THR   B 149 ? 0.1624 0.1360 0.2524 -0.0207 -0.0443 0.0069  149 THR   B N   
6186 C  CA  . THR   B 149 ? 0.1656 0.1405 0.2446 -0.0264 -0.0444 0.0108  149 THR   B CA  
6187 C  C   . THR   B 149 ? 0.1703 0.1411 0.2320 -0.0262 -0.0441 0.0135  149 THR   B C   
6188 O  O   . THR   B 149 ? 0.1748 0.1403 0.2471 -0.0243 -0.0286 0.0168  149 THR   B O   
6189 C  CB  . THR   B 149 ? 0.1705 0.1403 0.2439 -0.0212 -0.0389 0.0043  149 THR   B CB  
6190 O  OG1 . THR   B 149 ? 0.1644 0.1485 0.2318 -0.0271 -0.0430 0.0120  149 THR   B OG1 
6191 C  CG2 . THR   B 149 ? 0.1843 0.1419 0.2597 -0.0108 -0.0326 0.0067  149 THR   B CG2 
6199 N  N   . ASN   B 150 ? 0.1711 0.1418 0.2214 -0.0227 -0.0424 0.0138  150 ASN   B N   
6200 C  CA  . ASN   B 150 ? 0.1845 0.1649 0.2083 -0.0262 -0.0420 0.0057  150 ASN   B CA  
6201 C  C   . ASN   B 150 ? 0.1662 0.1561 0.2094 -0.0223 -0.0350 0.0067  150 ASN   B C   
6202 O  O   . ASN   B 150 ? 0.1717 0.1514 0.2261 -0.0292 -0.0470 0.0044  150 ASN   B O   
6203 C  CB  . ASN   B 150 ? 0.2139 0.2001 0.2106 -0.0362 -0.0563 0.0150  150 ASN   B CB  
6204 C  CG  . ASN   B 150 ? 0.2418 0.2394 0.2448 -0.0323 -0.0606 0.0271  150 ASN   B CG  
6205 O  OD1 . ASN   B 150 ? 0.2482 0.2562 0.2535 -0.0402 -0.0709 0.0248  150 ASN   B OD1 
6206 N  ND2 . ASN   B 150 ? 0.2522 0.2592 0.2784 -0.0239 -0.0609 0.0649  150 ASN   B ND2 
6213 N  N   . VAL   B 151 ? 0.1592 0.1542 0.2048 -0.0289 -0.0450 0.0045  151 VAL   B N   
6214 C  CA  . VAL   B 151 ? 0.1630 0.1483 0.2065 -0.0335 -0.0321 0.0070  151 VAL   B CA  
6215 C  C   . VAL   B 151 ? 0.1651 0.1412 0.1960 -0.0403 -0.0318 0.0030  151 VAL   B C   
6216 O  O   . VAL   B 151 ? 0.1725 0.1532 0.2292 -0.0339 -0.0201 -0.0077 151 VAL   B O   
6217 C  CB  . VAL   B 151 ? 0.1868 0.1535 0.2178 -0.0163 -0.0269 0.0086  151 VAL   B CB  
6218 C  CG1 . VAL   B 151 ? 0.1863 0.1620 0.2428 -0.0209 -0.0210 -0.0017 151 VAL   B CG1 
6219 C  CG2 . VAL   B 151 ? 0.1935 0.1649 0.2080 -0.0070 -0.0224 0.0073  151 VAL   B CG2 
6229 N  N   . TYR   B 152 ? 0.1605 0.1360 0.1959 -0.0294 -0.0347 0.0020  152 TYR   B N   
6230 C  CA  . TYR   B 152 ? 0.1648 0.1577 0.1824 -0.0379 -0.0219 -0.0030 152 TYR   B CA  
6231 C  C   . TYR   B 152 ? 0.1617 0.1343 0.1839 -0.0270 -0.0179 -0.0098 152 TYR   B C   
6232 O  O   . TYR   B 152 ? 0.1703 0.1367 0.1945 -0.0286 -0.0186 0.0033  152 TYR   B O   
6233 C  CB  . TYR   B 152 ? 0.1841 0.1811 0.1760 -0.0429 -0.0201 0.0041  152 TYR   B CB  
6234 C  CG  . TYR   B 152 ? 0.2037 0.1927 0.1622 -0.0586 -0.0214 0.0018  152 TYR   B CG  
6235 C  CD1 . TYR   B 152 ? 0.2149 0.2036 0.1534 -0.0520 -0.0327 0.0136  152 TYR   B CD1 
6236 C  CD2 . TYR   B 152 ? 0.2245 0.2137 0.1633 -0.0595 -0.0178 -0.0010 152 TYR   B CD2 
6237 C  CE1 . TYR   B 152 ? 0.2336 0.2307 0.1712 -0.0461 -0.0390 0.0256  152 TYR   B CE1 
6238 C  CE2 . TYR   B 152 ? 0.2358 0.2393 0.1665 -0.0570 -0.0281 -0.0056 152 TYR   B CE2 
6239 C  CZ  . TYR   B 152 ? 0.2435 0.2529 0.1633 -0.0499 -0.0466 0.0241  152 TYR   B CZ  
6240 O  OH  . TYR   B 152 ? 0.2695 0.2916 0.2020 -0.0377 -0.0502 0.0279  152 TYR   B OH  
6250 N  N   . LEU   B 153 ? 0.1641 0.1318 0.1959 -0.0314 -0.0174 -0.0013 153 LEU   B N   
6251 C  CA  . LEU   B 153 ? 0.1627 0.1344 0.1892 -0.0248 -0.0117 -0.0091 153 LEU   B CA  
6252 C  C   . LEU   B 153 ? 0.1675 0.1326 0.1958 -0.0297 -0.0113 -0.0179 153 LEU   B C   
6253 O  O   . LEU   B 153 ? 0.1799 0.1593 0.1964 -0.0258 -0.0099 -0.0317 153 LEU   B O   
6254 C  CB  . LEU   B 153 ? 0.1656 0.1330 0.1968 -0.0275 -0.0063 -0.0098 153 LEU   B CB  
6255 C  CG  . LEU   B 153 ? 0.1579 0.1404 0.2208 -0.0274 -0.0040 -0.0045 153 LEU   B CG  
6256 C  CD1 . LEU   B 153 ? 0.1706 0.1509 0.2352 -0.0288 -0.0010 0.0106  153 LEU   B CD1 
6257 C  CD2 . LEU   B 153 ? 0.1547 0.1519 0.2330 -0.0285 0.0020  0.0055  153 LEU   B CD2 
6269 N  N   . ALA   B 154 ? 0.1545 0.1347 0.1997 -0.0109 -0.0086 -0.0132 154 ALA   B N   
6270 C  CA  . ALA   B 154 ? 0.1667 0.1454 0.2236 -0.0111 -0.0103 -0.0235 154 ALA   B CA  
6271 C  C   . ALA   B 154 ? 0.1825 0.1476 0.2216 -0.0032 -0.0270 -0.0302 154 ALA   B C   
6272 O  O   . ALA   B 154 ? 0.2204 0.1525 0.2431 0.0085  -0.0165 -0.0067 154 ALA   B O   
6273 C  CB  . ALA   B 154 ? 0.1661 0.1608 0.2452 -0.0051 -0.0048 -0.0276 154 ALA   B CB  
6279 N  N   . VAL   B 155 ? 0.1501 0.1418 0.2450 -0.0099 -0.0053 -0.0238 155 VAL   B N   
6280 C  CA  . VAL   B 155 ? 0.1520 0.1427 0.2711 -0.0048 -0.0086 -0.0144 155 VAL   B CA  
6281 C  C   . VAL   B 155 ? 0.1492 0.1454 0.2621 -0.0036 -0.0054 -0.0272 155 VAL   B C   
6282 O  O   . VAL   B 155 ? 0.1685 0.1656 0.2879 0.0024  -0.0009 -0.0496 155 VAL   B O   
6283 C  CB  . VAL   B 155 ? 0.1516 0.1569 0.2984 -0.0042 -0.0116 -0.0010 155 VAL   B CB  
6284 C  CG1 . VAL   B 155 ? 0.1536 0.1579 0.2956 -0.0095 -0.0143 -0.0001 155 VAL   B CG1 
6285 C  CG2 . VAL   B 155 ? 0.1477 0.1671 0.3234 -0.0039 -0.0226 0.0282  155 VAL   B CG2 
6295 N  N   . PHE   B 156 ? 0.1382 0.1525 0.2841 0.0037  -0.0073 -0.0223 156 PHE   B N   
6296 C  CA  . PHE   B 156 ? 0.1411 0.1581 0.3088 0.0053  -0.0067 -0.0255 156 PHE   B CA  
6297 C  C   . PHE   B 156 ? 0.1469 0.1735 0.3366 0.0157  -0.0072 -0.0407 156 PHE   B C   
6298 O  O   . PHE   B 156 ? 0.1726 0.1947 0.3569 0.0251  -0.0003 -0.0536 156 PHE   B O   
6299 C  CB  . PHE   B 156 ? 0.1479 0.1515 0.2961 0.0032  -0.0072 -0.0277 156 PHE   B CB  
6300 C  CG  . PHE   B 156 ? 0.1489 0.1645 0.3074 0.0016  -0.0050 -0.0093 156 PHE   B CG  
6301 C  CD1 . PHE   B 156 ? 0.1545 0.1895 0.3360 0.0056  0.0009  0.0186  156 PHE   B CD1 
6302 C  CD2 . PHE   B 156 ? 0.1603 0.1784 0.3023 0.0160  -0.0157 -0.0031 156 PHE   B CD2 
6303 C  CE1 . PHE   B 156 ? 0.1601 0.2033 0.3364 0.0096  -0.0001 0.0198  156 PHE   B CE1 
6304 C  CE2 . PHE   B 156 ? 0.1727 0.2004 0.3158 0.0181  -0.0113 0.0100  156 PHE   B CE2 
6305 C  CZ  . PHE   B 156 ? 0.1602 0.2042 0.3310 0.0221  -0.0096 0.0112  156 PHE   B CZ  
6315 N  N   A ASP   B 157 ? 0.1444 0.1541 0.3593 0.0167  -0.0238 -0.0260 157 ASP   B N   
6316 N  N   B ASP   B 157 ? 0.1666 0.1834 0.3112 0.0223  -0.0093 -0.0390 157 ASP   B N   
6317 C  CA  A ASP   B 157 ? 0.1609 0.1600 0.3784 0.0155  -0.0295 -0.0320 157 ASP   B CA  
6318 C  CA  B ASP   B 157 ? 0.1881 0.2008 0.2951 0.0270  -0.0075 -0.0435 157 ASP   B CA  
6319 C  C   A ASP   B 157 ? 0.1520 0.1536 0.3944 0.0089  -0.0267 -0.0507 157 ASP   B C   
6320 C  C   B ASP   B 157 ? 0.2035 0.2150 0.2883 0.0263  -0.0029 -0.0530 157 ASP   B C   
6321 O  O   A ASP   B 157 ? 0.1349 0.1445 0.3986 0.0010  -0.0255 -0.0322 157 ASP   B O   
6322 O  O   B ASP   B 157 ? 0.2005 0.2172 0.2855 0.0280  0.0054  -0.0487 157 ASP   B O   
6323 C  CB  A ASP   B 157 ? 0.2070 0.1786 0.3873 0.0088  -0.0469 -0.0141 157 ASP   B CB  
6324 C  CB  B ASP   B 157 ? 0.1980 0.2056 0.2948 0.0273  -0.0150 -0.0359 157 ASP   B CB  
6325 C  CG  A ASP   B 157 ? 0.2604 0.1969 0.4137 -0.0028 -0.0364 -0.0111 157 ASP   B CG  
6326 C  CG  B ASP   B 157 ? 0.2094 0.2106 0.3010 0.0257  -0.0181 -0.0335 157 ASP   B CG  
6327 O  OD1 A ASP   B 157 ? 0.2723 0.1975 0.4357 -0.0025 -0.0254 -0.0042 157 ASP   B OD1 
6328 O  OD1 B ASP   B 157 ? 0.2072 0.2082 0.3040 0.0290  -0.0263 -0.0299 157 ASP   B OD1 
6329 O  OD2 A ASP   B 157 ? 0.2922 0.2165 0.4318 -0.0017 -0.0275 -0.0100 157 ASP   B OD2 
6330 O  OD2 B ASP   B 157 ? 0.2245 0.2193 0.3149 0.0245  -0.0068 -0.0327 157 ASP   B OD2 
6339 N  N   A LYS   B 158 ? 0.1594 0.1854 0.4056 0.0115  -0.0135 -0.0787 158 LYS   B N   
6340 N  N   B LYS   B 158 ? 0.2188 0.2327 0.2951 0.0217  -0.0046 -0.0633 158 LYS   B N   
6341 C  CA  A LYS   B 158 ? 0.1762 0.2137 0.4134 0.0065  -0.0056 -0.1039 158 LYS   B CA  
6342 C  CA  B LYS   B 158 ? 0.2348 0.2474 0.3115 0.0177  -0.0063 -0.0733 158 LYS   B CA  
6343 C  C   A LYS   B 158 ? 0.1782 0.1948 0.4389 0.0062  -0.0205 -0.1001 158 LYS   B C   
6344 C  C   B LYS   B 158 ? 0.2323 0.2393 0.3215 0.0167  -0.0175 -0.0689 158 LYS   B C   
6345 O  O   A LYS   B 158 ? 0.1783 0.1872 0.4524 -0.0027 -0.0208 -0.1122 158 LYS   B O   
6346 O  O   B LYS   B 158 ? 0.2348 0.2412 0.3184 0.0158  -0.0178 -0.0713 158 LYS   B O   
6347 C  CB  A LYS   B 158 ? 0.2033 0.2681 0.4071 0.0116  0.0060  -0.1287 158 LYS   B CB  
6348 C  CB  B LYS   B 158 ? 0.2547 0.2694 0.3265 0.0179  -0.0001 -0.0855 158 LYS   B CB  
6349 C  CG  A LYS   B 158 ? 0.2409 0.3214 0.4043 0.0134  0.0105  -0.1406 158 LYS   B CG  
6350 C  CG  B LYS   B 158 ? 0.2754 0.2889 0.3431 0.0176  0.0045  -0.0935 158 LYS   B CG  
6351 C  CD  A LYS   B 158 ? 0.2640 0.3671 0.4081 0.0129  0.0109  -0.1356 158 LYS   B CD  
6352 C  CD  B LYS   B 158 ? 0.2913 0.3086 0.3610 0.0157  0.0074  -0.0925 158 LYS   B CD  
6353 C  CE  A LYS   B 158 ? 0.2830 0.4027 0.4167 0.0125  0.0053  -0.1258 158 LYS   B CE  
6354 C  CE  B LYS   B 158 ? 0.3031 0.3230 0.3770 0.0150  0.0072  -0.0885 158 LYS   B CE  
6355 N  NZ  A LYS   B 158 ? 0.2855 0.4238 0.4184 0.0093  0.0024  -0.1189 158 LYS   B NZ  
6356 N  NZ  B LYS   B 158 ? 0.3073 0.3308 0.3842 0.0126  0.0074  -0.0862 158 LYS   B NZ  
6383 N  N   A ASN   B 159 ? 0.1771 0.1769 0.4559 0.0154  -0.0307 -0.0814 159 ASN   B N   
6384 N  N   B ASN   B 159 ? 0.2248 0.2269 0.3404 0.0167  -0.0285 -0.0587 159 ASN   B N   
6385 C  CA  A ASN   B 159 ? 0.1932 0.1674 0.4619 0.0285  -0.0468 -0.0651 159 ASN   B CA  
6386 C  CA  B ASN   B 159 ? 0.2192 0.2131 0.3595 0.0185  -0.0393 -0.0527 159 ASN   B CA  
6387 C  C   A ASN   B 159 ? 0.1813 0.1571 0.4447 0.0184  -0.0587 -0.0458 159 ASN   B C   
6388 C  C   B ASN   B 159 ? 0.1974 0.1868 0.3845 0.0164  -0.0466 -0.0490 159 ASN   B C   
6389 O  O   A ASN   B 159 ? 0.1802 0.1504 0.4628 0.0037  -0.0645 -0.0277 159 ASN   B O   
6390 O  O   B ASN   B 159 ? 0.1962 0.1866 0.3852 0.0153  -0.0454 -0.0467 159 ASN   B O   
6391 C  CB  A ASN   B 159 ? 0.2207 0.1867 0.4835 0.0390  -0.0537 -0.0649 159 ASN   B CB  
6392 C  CB  B ASN   B 159 ? 0.2316 0.2255 0.3590 0.0218  -0.0435 -0.0494 159 ASN   B CB  
6393 C  CG  A ASN   B 159 ? 0.2529 0.2155 0.4978 0.0370  -0.0616 -0.0701 159 ASN   B CG  
6394 C  CG  B ASN   B 159 ? 0.2437 0.2384 0.3606 0.0252  -0.0489 -0.0479 159 ASN   B CG  
6395 O  OD1 A ASN   B 159 ? 0.2735 0.2238 0.5018 0.0427  -0.0593 -0.0770 159 ASN   B OD1 
6396 O  OD1 B ASN   B 159 ? 0.2498 0.2433 0.3607 0.0305  -0.0484 -0.0475 159 ASN   B OD1 
6397 N  ND2 A ASN   B 159 ? 0.2555 0.2305 0.5099 0.0327  -0.0652 -0.0634 159 ASN   B ND2 
6398 N  ND2 B ASN   B 159 ? 0.2459 0.2451 0.3666 0.0260  -0.0504 -0.0428 159 ASN   B ND2 
6411 N  N   . LEU   B 160 ? 0.1771 0.1645 0.4137 0.0149  -0.0521 -0.0412 160 LEU   B N   
6412 C  CA  . LEU   B 160 ? 0.1690 0.1641 0.3881 0.0107  -0.0455 -0.0174 160 LEU   B CA  
6413 C  C   . LEU   B 160 ? 0.1656 0.1505 0.3768 -0.0035 -0.0251 -0.0273 160 LEU   B C   
6414 O  O   . LEU   B 160 ? 0.1452 0.1556 0.3918 -0.0036 -0.0334 -0.0107 160 LEU   B O   
6415 C  CB  . LEU   B 160 ? 0.1625 0.1741 0.3686 0.0065  -0.0479 -0.0070 160 LEU   B CB  
6416 C  CG  . LEU   B 160 ? 0.1617 0.1845 0.3498 0.0064  -0.0416 -0.0016 160 LEU   B CG  
6417 C  CD1 . LEU   B 160 ? 0.1808 0.1972 0.3447 -0.0004 -0.0231 -0.0094 160 LEU   B CD1 
6418 C  CD2 . LEU   B 160 ? 0.1669 0.1898 0.3461 0.0222  -0.0322 -0.0051 160 LEU   B CD2 
6431 N  N   A TYR   B 161 ? 0.1676 0.1552 0.3745 -0.0120 -0.0021 -0.0475 161 TYR   B N   
6432 N  N   B TYR   B 161 ? 0.1735 0.1600 0.3519 -0.0077 -0.0087 -0.0387 161 TYR   B N   
6433 C  CA  A TYR   B 161 ? 0.1785 0.1513 0.3559 -0.0219 0.0166  -0.0505 161 TYR   B CA  
6434 C  CA  B TYR   B 161 ? 0.1847 0.1653 0.3254 -0.0121 0.0049  -0.0422 161 TYR   B CA  
6435 C  C   A TYR   B 161 ? 0.1793 0.1520 0.3541 -0.0186 0.0175  -0.0441 161 TYR   B C   
6436 C  C   B TYR   B 161 ? 0.1837 0.1602 0.3346 -0.0139 0.0083  -0.0450 161 TYR   B C   
6437 O  O   A TYR   B 161 ? 0.1721 0.1530 0.3550 -0.0261 0.0174  -0.0332 161 TYR   B O   
6438 O  O   B TYR   B 161 ? 0.1811 0.1625 0.3269 -0.0166 0.0087  -0.0399 161 TYR   B O   
6439 C  CB  A TYR   B 161 ? 0.1933 0.1623 0.3370 -0.0335 0.0280  -0.0615 161 TYR   B CB  
6440 C  CB  B TYR   B 161 ? 0.1985 0.1809 0.2961 -0.0140 0.0116  -0.0421 161 TYR   B CB  
6441 C  CG  A TYR   B 161 ? 0.2227 0.1642 0.3205 -0.0435 0.0364  -0.0647 161 TYR   B CG  
6442 C  CG  B TYR   B 161 ? 0.2186 0.1942 0.2744 -0.0179 0.0158  -0.0384 161 TYR   B CG  
6443 C  CD1 A TYR   B 161 ? 0.2289 0.1639 0.3095 -0.0547 0.0364  -0.0711 161 TYR   B CD1 
6444 C  CD1 B TYR   B 161 ? 0.2247 0.1993 0.2640 -0.0204 0.0193  -0.0388 161 TYR   B CD1 
6445 C  CD2 A TYR   B 161 ? 0.2459 0.1716 0.3093 -0.0407 0.0275  -0.0598 161 TYR   B CD2 
6446 C  CD2 B TYR   B 161 ? 0.2308 0.2015 0.2625 -0.0162 0.0124  -0.0340 161 TYR   B CD2 
6447 C  CE1 A TYR   B 161 ? 0.2502 0.1811 0.3127 -0.0545 0.0353  -0.0672 161 TYR   B CE1 
6448 C  CE1 B TYR   B 161 ? 0.2358 0.2090 0.2635 -0.0213 0.0196  -0.0350 161 TYR   B CE1 
6449 C  CE2 A TYR   B 161 ? 0.2642 0.1890 0.3141 -0.0449 0.0319  -0.0578 161 TYR   B CE2 
6450 C  CE2 B TYR   B 161 ? 0.2416 0.2107 0.2637 -0.0185 0.0153  -0.0317 161 TYR   B CE2 
6451 C  CZ  A TYR   B 161 ? 0.2679 0.1943 0.3161 -0.0566 0.0260  -0.0569 161 TYR   B CZ  
6452 C  CZ  B TYR   B 161 ? 0.2454 0.2148 0.2654 -0.0224 0.0142  -0.0304 161 TYR   B CZ  
6453 O  OH  A TYR   B 161 ? 0.2970 0.2243 0.3403 -0.0548 0.0309  -0.0486 161 TYR   B OH  
6454 O  OH  B TYR   B 161 ? 0.2614 0.2281 0.2789 -0.0236 0.0181  -0.0271 161 TYR   B OH  
6473 N  N   . ASP   B 162 ? 0.1833 0.1562 0.3640 -0.0156 0.0030  -0.0550 162 ASP   B N   
6474 C  CA  . ASP   B 162 ? 0.1893 0.1644 0.3814 -0.0062 -0.0030 -0.0541 162 ASP   B CA  
6475 C  C   . ASP   B 162 ? 0.1841 0.1565 0.3725 -0.0100 -0.0097 -0.0401 162 ASP   B C   
6476 O  O   . ASP   B 162 ? 0.1870 0.1623 0.3838 -0.0201 -0.0310 -0.0331 162 ASP   B O   
6477 C  CB  . ASP   B 162 ? 0.2068 0.1703 0.4097 -0.0047 -0.0103 -0.0801 162 ASP   B CB  
6478 C  CG  . ASP   B 162 ? 0.2141 0.1955 0.4358 0.0047  -0.0137 -0.0906 162 ASP   B CG  
6479 O  OD1 . ASP   B 162 ? 0.2103 0.2166 0.4383 -0.0077 -0.0012 -0.0795 162 ASP   B OD1 
6480 O  OD2 . ASP   B 162 ? 0.2272 0.2211 0.4594 0.0231  -0.0236 -0.0866 162 ASP   B OD2 
6486 N  N   . LYS   B 163 ? 0.1830 0.1442 0.3660 -0.0149 -0.0225 -0.0267 163 LYS   B N   
6487 C  CA  . LYS   B 163 ? 0.2004 0.1539 0.3722 -0.0239 -0.0185 -0.0173 163 LYS   B CA  
6488 C  C   . LYS   B 163 ? 0.1643 0.1502 0.3539 -0.0212 -0.0267 0.0034  163 LYS   B C   
6489 O  O   . LYS   B 163 ? 0.1602 0.1614 0.3668 -0.0265 -0.0277 0.0122  163 LYS   B O   
6490 C  CB  . LYS   B 163 ? 0.2669 0.2047 0.4158 -0.0304 -0.0254 -0.0088 163 LYS   B CB  
6491 C  CG  . LYS   B 163 ? 0.3561 0.3028 0.4830 -0.0320 -0.0190 -0.0071 163 LYS   B CG  
6492 C  CD  . LYS   B 163 ? 0.4330 0.3890 0.5523 -0.0421 -0.0225 -0.0112 163 LYS   B CD  
6493 C  CE  . LYS   B 163 ? 0.4926 0.4568 0.6038 -0.0485 -0.0246 -0.0122 163 LYS   B CE  
6494 N  NZ  . LYS   B 163 ? 0.5348 0.5047 0.6346 -0.0514 -0.0251 -0.0145 163 LYS   B NZ  
6508 N  N   . LEU   B 164 ? 0.1522 0.1398 0.3391 -0.0158 -0.0260 0.0044  164 LEU   B N   
6509 C  CA  . LEU   B 164 ? 0.1514 0.1434 0.3235 -0.0129 -0.0257 0.0099  164 LEU   B CA  
6510 C  C   . LEU   B 164 ? 0.1644 0.1428 0.3274 -0.0182 -0.0380 0.0028  164 LEU   B C   
6511 O  O   . LEU   B 164 ? 0.1605 0.1671 0.3423 -0.0208 -0.0361 0.0131  164 LEU   B O   
6512 C  CB  . LEU   B 164 ? 0.1494 0.1395 0.3049 -0.0070 -0.0174 0.0093  164 LEU   B CB  
6513 C  CG  . LEU   B 164 ? 0.1621 0.1538 0.2988 -0.0144 -0.0114 0.0061  164 LEU   B CG  
6514 C  CD1 . LEU   B 164 ? 0.1754 0.1504 0.2851 -0.0214 -0.0229 -0.0088 164 LEU   B CD1 
6515 C  CD2 . LEU   B 164 ? 0.1773 0.1932 0.3133 -0.0112 0.0014  -0.0034 164 LEU   B CD2 
6527 N  N   . VAL   B 165 ? 0.2030 0.1508 0.3449 -0.0287 -0.0492 0.0008  165 VAL   B N   
6528 C  CA  . VAL   B 165 ? 0.2538 0.1628 0.3481 -0.0403 -0.0724 -0.0031 165 VAL   B CA  
6529 C  C   . VAL   B 165 ? 0.2853 0.1747 0.3904 -0.0518 -0.1026 0.0029  165 VAL   B C   
6530 O  O   . VAL   B 165 ? 0.3039 0.1999 0.4030 -0.0588 -0.1083 0.0086  165 VAL   B O   
6531 C  CB  . VAL   B 165 ? 0.2781 0.1801 0.3321 -0.0270 -0.0497 -0.0149 165 VAL   B CB  
6532 C  CG1 . VAL   B 165 ? 0.2958 0.1918 0.3427 -0.0208 -0.0328 -0.0117 165 VAL   B CG1 
6533 C  CG2 . VAL   B 165 ? 0.2774 0.1828 0.3155 -0.0265 -0.0365 -0.0046 165 VAL   B CG2 
6543 N  N   . SER   B 166 ? 0.2993 0.1599 0.4364 -0.0535 -0.1166 -0.0153 166 SER   B N   
6544 C  CA  . SER   B 166 ? 0.2951 0.1710 0.4897 -0.0510 -0.1067 -0.0196 166 SER   B CA  
6545 C  C   . SER   B 166 ? 0.2720 0.1899 0.5045 -0.0574 -0.1027 0.0081  166 SER   B C   
6546 O  O   . SER   B 166 ? 0.2750 0.2079 0.5341 -0.0712 -0.1170 -0.0131 166 SER   B O   
6547 C  CB  . SER   B 166 ? 0.2943 0.1753 0.5226 -0.0407 -0.0991 -0.0225 166 SER   B CB  
6548 O  OG  . SER   B 166 ? 0.2792 0.1762 0.5455 -0.0308 -0.0990 -0.0070 166 SER   B OG  
6554 N  N   . SER   B 167 ? 0.2426 0.1787 0.4643 -0.0561 -0.1060 0.0362  167 SER   B N   
6555 C  CA  . SER   B 167 ? 0.2373 0.1804 0.4491 -0.0526 -0.0684 0.0430  167 SER   B CA  
6556 C  C   . SER   B 167 ? 0.2311 0.1925 0.4225 -0.0627 -0.0631 0.0661  167 SER   B C   
6557 O  O   . SER   B 167 ? 0.2241 0.2163 0.4252 -0.0693 -0.0631 0.0584  167 SER   B O   
6558 C  CB  . SER   B 167 ? 0.2207 0.1824 0.4545 -0.0441 -0.0364 0.0398  167 SER   B CB  
6559 O  OG  . SER   B 167 ? 0.2159 0.1956 0.4512 -0.0299 -0.0131 0.0376  167 SER   B OG  
6565 N  N   . PHE   B 168 ? 0.2363 0.1916 0.4085 -0.0552 -0.0498 0.0733  168 PHE   B N   
6566 C  CA  . PHE   B 168 ? 0.2275 0.1887 0.3743 -0.0642 -0.0407 0.0478  168 PHE   B CA  
6567 C  C   . PHE   B 168 ? 0.1913 0.1716 0.3207 -0.0472 -0.0304 0.0234  168 PHE   B C   
6568 O  O   . PHE   B 168 ? 0.2169 0.1650 0.3187 -0.0069 -0.0286 0.0095  168 PHE   B O   
6569 C  CB  . PHE   B 168 ? 0.2431 0.2004 0.3832 -0.0707 -0.0483 0.0511  168 PHE   B CB  
6570 C  CG  . PHE   B 168 ? 0.2679 0.1861 0.3640 -0.0785 -0.0443 0.0322  168 PHE   B CG  
6571 C  CD1 . PHE   B 168 ? 0.2888 0.1949 0.3681 -0.0783 -0.0414 0.0251  168 PHE   B CD1 
6572 C  CD2 . PHE   B 168 ? 0.2583 0.1787 0.3516 -0.0734 -0.0391 0.0443  168 PHE   B CD2 
6573 C  CE1 . PHE   B 168 ? 0.2970 0.1979 0.3526 -0.0664 -0.0283 0.0399  168 PHE   B CE1 
6574 C  CE2 . PHE   B 168 ? 0.2877 0.1898 0.3539 -0.0553 -0.0397 0.0324  168 PHE   B CE2 
6575 C  CZ  . PHE   B 168 ? 0.2941 0.1826 0.3476 -0.0472 -0.0371 0.0512  168 PHE   B CZ  
6585 N  N   . LEU   B 169 ? 0.2080 0.1831 0.3192 -0.0164 -0.0149 0.0035  169 LEU   B N   
6586 C  CA  . LEU   B 169 ? 0.2466 0.2081 0.3483 -0.0114 -0.0060 -0.0274 169 LEU   B CA  
6587 C  C   . LEU   B 169 ? 0.2801 0.2293 0.3968 0.0020  -0.0040 -0.0528 169 LEU   B C   
6588 O  O   . LEU   B 169 ? 0.3014 0.2512 0.4387 -0.0013 0.0003  -0.0682 169 LEU   B O   
6589 C  CB  . LEU   B 169 ? 0.2698 0.2403 0.3466 -0.0140 -0.0111 -0.0016 169 LEU   B CB  
6590 C  CG  . LEU   B 169 ? 0.3085 0.2723 0.3649 -0.0037 -0.0058 0.0013  169 LEU   B CG  
6591 C  CD1 . LEU   B 169 ? 0.3198 0.2861 0.3629 -0.0053 -0.0079 0.0123  169 LEU   B CD1 
6592 C  CD2 . LEU   B 169 ? 0.3114 0.2765 0.3661 0.0080  0.0080  -0.0047 169 LEU   B CD2 
6593 O  OXT . LEU   B 169 ? 0.2997 0.2433 0.4087 0.0286  0.0018  -0.0503 169 LEU   B OXT 
6605 N  N2  B A1BBL C .   ? 0.1419 0.2085 0.2270 -0.0225 0.0010  -0.0116 201 A1BBL A N2  
6606 C  C3  B A1BBL C .   ? 0.1392 0.2033 0.2266 -0.0143 -0.0033 -0.0096 201 A1BBL A C3  
6607 C  C6  B A1BBL C .   ? 0.1327 0.2072 0.2134 -0.0178 0.0015  -0.0077 201 A1BBL A C6  
6608 C  C9  B A1BBL C .   ? 0.1827 0.2207 0.2973 0.0032  -0.0217 -0.0183 201 A1BBL A C9  
6609 C  C12 B A1BBL C .   ? 0.1870 0.2189 0.2930 0.0035  -0.0261 -0.0219 201 A1BBL A C12 
6610 C  C1  B A1BBL C .   ? 0.1744 0.2140 0.2759 -0.0020 -0.0244 -0.0159 201 A1BBL A C1  
6611 C  C10 B A1BBL C .   ? 0.1945 0.2276 0.3169 0.0085  -0.0266 -0.0219 201 A1BBL A C10 
6612 C  C11 B A1BBL C .   ? 0.2011 0.2285 0.3121 0.0069  -0.0291 -0.0287 201 A1BBL A C11 
6613 C  C2  B A1BBL C .   ? 0.1442 0.2013 0.2562 0.0002  -0.0165 -0.0130 201 A1BBL A C2  
6614 C  C4  B A1BBL C .   ? 0.1474 0.2154 0.2226 -0.0190 0.0001  -0.0104 201 A1BBL A C4  
6615 C  C5  B A1BBL C .   ? 0.1329 0.2104 0.2102 -0.0168 -0.0003 -0.0061 201 A1BBL A C5  
6616 C  C7  B A1BBL C .   ? 0.1210 0.2084 0.2089 -0.0215 0.0099  -0.0032 201 A1BBL A C7  
6617 C  C8  B A1BBL C .   ? 0.1035 0.2043 0.2050 -0.0258 -0.0105 -0.0058 201 A1BBL A C8  
6618 N  N1  B A1BBL C .   ? 0.1396 0.1967 0.2391 -0.0035 -0.0117 -0.0066 201 A1BBL A N1  
6619 N  N3  B A1BBL C .   ? 0.1488 0.2152 0.2149 -0.0207 0.0092  -0.0035 201 A1BBL A N3  
6620 N  N4  B A1BBL C .   ? 0.1231 0.2119 0.2114 -0.0069 -0.0142 -0.0073 201 A1BBL A N4  
6621 O  O1  B A1BBL C .   ? 0.1912 0.2165 0.2627 -0.0012 -0.0365 -0.0170 201 A1BBL A O1  
6622 O  O2  B A1BBL C .   ? 0.2043 0.2326 0.3206 0.0127  -0.0382 -0.0303 201 A1BBL A O2  
6639 CL CL  B CL    D .   ? 0.2053 0.1621 0.2828 -0.0163 -0.0030 0.0223  202 CL    A CL  
6640 O  O   . HOH   E .   ? 0.7654 0.6612 0.4184 -0.1432 -0.0341 0.2468  301 HOH   A O   
6641 O  O   . HOH   E .   ? 0.4384 0.3254 0.6343 -0.0034 0.1849  0.0004  302 HOH   A O   
6642 O  O   . HOH   E .   ? 0.5022 0.2220 0.4904 -0.0418 -0.0493 0.0213  303 HOH   A O   
6643 O  O   . HOH   E .   ? 0.4512 0.7633 0.5389 -0.1242 0.1178  0.0365  304 HOH   A O   
6644 O  O   . HOH   E .   ? 0.2189 0.1802 0.2873 0.0266  -0.0498 -0.0012 305 HOH   A O   
6645 O  O   . HOH   E .   ? 0.6618 0.5102 0.3008 0.1980  -0.1182 0.0329  306 HOH   A O   
6646 O  O   . HOH   E .   ? 0.5424 0.6645 0.6218 -0.0971 -0.1067 -0.1130 307 HOH   A O   
6647 O  O   . HOH   E .   ? 0.2911 0.6194 0.3786 0.0094  -0.0116 0.1404  308 HOH   A O   
6648 O  O   . HOH   E .   ? 0.4973 0.6537 0.4026 0.2047  -0.0178 -0.0561 309 HOH   A O   
6649 O  O   . HOH   E .   ? 0.3610 0.3442 0.1840 -0.0495 0.0547  0.0298  310 HOH   A O   
6650 O  O   . HOH   E .   ? 0.2916 0.6338 0.6072 0.0920  0.0924  0.1890  311 HOH   A O   
6651 O  O   . HOH   E .   ? 0.2651 0.2507 0.3877 -0.0133 0.0836  0.0698  312 HOH   A O   
6652 O  O   . HOH   E .   ? 0.5953 0.3965 0.6168 -0.0758 0.1405  0.1434  313 HOH   A O   
6653 O  O   . HOH   E .   ? 0.5195 0.4097 0.3215 -0.1514 -0.1309 0.0425  314 HOH   A O   
6654 O  O   . HOH   E .   ? 0.4015 0.3744 0.3572 -0.1665 -0.0209 0.1057  315 HOH   A O   
6655 O  O   . HOH   E .   ? 0.6088 0.4681 0.6200 -0.1205 0.0744  0.1796  316 HOH   A O   
6656 O  O   . HOH   E .   ? 0.1823 0.4255 0.3842 0.0634  -0.0179 0.0353  317 HOH   A O   
6657 O  O   . HOH   E .   ? 0.2196 0.1816 0.3773 -0.0535 0.0205  -0.0239 318 HOH   A O   
6658 O  O   . HOH   E .   ? 0.3209 0.7017 0.5681 -0.0556 -0.0790 0.2808  319 HOH   A O   
6659 O  O   . HOH   E .   ? 0.3813 0.1919 0.2553 0.0138  0.0287  0.0155  320 HOH   A O   
6660 O  O   . HOH   E .   ? 0.7469 0.7124 0.5252 0.0093  -0.0512 -0.0721 321 HOH   A O   
6661 O  O   . HOH   E .   ? 0.1564 0.4469 0.3073 -0.0120 0.0274  0.0990  322 HOH   A O   
6662 O  O   . HOH   E .   ? 0.5964 0.6244 0.4189 -0.0584 0.0954  0.0890  323 HOH   A O   
6663 O  O   . HOH   E .   ? 0.2324 0.3371 0.4668 -0.0492 -0.0776 0.1463  324 HOH   A O   
6664 O  O   . HOH   E .   ? 0.1704 0.1806 0.2657 0.0131  -0.0326 0.0314  325 HOH   A O   
6665 O  O   . HOH   E .   ? 0.2873 0.4672 0.5574 -0.0318 0.1011  0.2307  326 HOH   A O   
6666 O  O   . HOH   E .   ? 0.6177 0.4740 0.5639 0.0610  -0.0926 -0.0205 327 HOH   A O   
6667 O  O   . HOH   E .   ? 0.5297 0.6741 0.4111 0.0579  -0.0478 0.2234  328 HOH   A O   
6668 O  O   . HOH   E .   ? 0.1665 0.1612 0.2853 -0.0235 0.0015  0.0166  329 HOH   A O   
6669 O  O   . HOH   E .   ? 0.3449 0.4658 0.2860 -0.0500 0.0333  0.0429  330 HOH   A O   
6670 O  O   . HOH   E .   ? 0.2641 0.4242 0.3721 0.1075  -0.0841 -0.0474 331 HOH   A O   
6671 O  O   . HOH   E .   ? 0.1592 0.2821 0.2602 0.0432  0.0303  0.0557  332 HOH   A O   
6672 O  O   . HOH   E .   ? 0.3407 0.3231 0.3677 -0.0847 0.0007  -0.0330 333 HOH   A O   
6673 O  O   . HOH   E .   ? 0.2313 0.2090 0.3240 0.0349  0.0144  0.0369  334 HOH   A O   
6674 O  O   . HOH   E .   ? 0.5273 0.6535 0.3895 -0.1090 0.1856  0.0791  335 HOH   A O   
6675 O  O   . HOH   E .   ? 0.2095 0.2538 0.4189 0.0185  0.0876  -0.0673 336 HOH   A O   
6676 O  O   . HOH   E .   ? 0.3027 0.3043 0.5561 -0.0511 -0.1408 0.1679  337 HOH   A O   
6677 O  O   . HOH   E .   ? 0.2132 0.1843 0.3200 -0.0029 -0.0720 -0.0151 338 HOH   A O   
6678 O  O   . HOH   E .   ? 0.2610 0.4133 0.4038 -0.0795 -0.0558 -0.0201 339 HOH   A O   
6679 O  O   . HOH   E .   ? 0.4750 0.3863 0.5413 -0.1719 -0.0368 0.2031  340 HOH   A O   
6680 O  O   . HOH   E .   ? 0.5193 0.1891 0.4893 0.0440  -0.0893 0.0405  341 HOH   A O   
6681 O  O   . HOH   E .   ? 0.4468 0.7238 0.5361 -0.0864 -0.1434 0.0985  342 HOH   A O   
6682 O  O   . HOH   E .   ? 0.1434 0.2101 0.2648 0.0000  -0.0136 0.0491  343 HOH   A O   
6683 O  O   A HOH   E .   ? 0.1961 0.3741 0.2184 0.0527  0.0011  0.0134  344 HOH   A O   
6684 O  O   . HOH   E .   ? 0.1547 0.1872 0.3315 0.0006  -0.0385 -0.0324 345 HOH   A O   
6685 O  O   . HOH   E .   ? 0.3671 0.3658 0.4578 -0.0373 0.1688  0.0526  346 HOH   A O   
6686 O  O   . HOH   E .   ? 0.5081 0.2199 0.6005 0.0752  -0.0090 -0.0073 347 HOH   A O   
6687 O  O   . HOH   E .   ? 0.6258 0.6366 0.4920 0.0345  0.2815  -0.0928 348 HOH   A O   
6688 O  O   . HOH   E .   ? 0.6606 0.9022 0.5877 -0.1048 0.0344  0.2829  349 HOH   A O   
6689 O  O   . HOH   E .   ? 0.8474 0.4433 0.5939 0.0048  -0.1289 0.0906  350 HOH   A O   
6690 O  O   . HOH   E .   ? 0.5792 0.6186 0.5828 0.1492  0.0716  0.0027  351 HOH   A O   
6691 O  O   . HOH   E .   ? 0.5263 0.3359 0.5110 0.1066  -0.0434 0.0194  352 HOH   A O   
6692 O  O   . HOH   E .   ? 0.3577 0.4553 0.4922 0.1850  0.0720  0.0446  353 HOH   A O   
6693 O  O   . HOH   E .   ? 0.1955 0.1966 0.4488 0.0237  0.0898  -0.0086 354 HOH   A O   
6694 O  O   . HOH   E .   ? 0.7080 0.3928 0.3059 0.0343  0.0450  0.1387  355 HOH   A O   
6695 O  O   . HOH   E .   ? 0.4921 0.5330 0.6393 0.1683  0.0945  -0.0310 356 HOH   A O   
6696 O  O   . HOH   E .   ? 0.2047 0.3877 0.4608 -0.0462 0.0345  -0.1135 357 HOH   A O   
6697 O  O   . HOH   E .   ? 0.1484 0.1955 0.3027 0.0044  0.0024  0.0204  358 HOH   A O   
6698 O  O   . HOH   E .   ? 0.3758 0.6597 0.4422 -0.0825 0.0033  0.1591  359 HOH   A O   
6699 O  O   . HOH   E .   ? 0.1338 0.1325 0.1962 -0.0033 0.0111  0.0134  360 HOH   A O   
6700 O  O   . HOH   E .   ? 0.1795 0.2427 0.2396 -0.0265 -0.0152 0.0832  361 HOH   A O   
6701 O  O   . HOH   E .   ? 0.1517 0.1666 0.2001 -0.0079 -0.0194 0.0005  362 HOH   A O   
6702 O  O   . HOH   E .   ? 0.3387 0.4397 0.2494 -0.1511 -0.0035 -0.0604 363 HOH   A O   
6703 O  O   . HOH   E .   ? 0.2895 0.3376 0.4386 -0.0436 -0.0676 -0.0684 364 HOH   A O   
6704 O  O   . HOH   E .   ? 0.1678 0.1373 0.2845 -0.0135 0.0176  -0.0027 365 HOH   A O   
6705 O  O   . HOH   E .   ? 0.4028 0.2283 0.2918 0.1136  0.0436  0.0212  366 HOH   A O   
6706 O  O   . HOH   E .   ? 0.1957 0.1877 0.2836 -0.0266 0.0088  0.0343  367 HOH   A O   
6707 O  O   . HOH   E .   ? 0.3509 0.7186 0.3704 0.1970  0.0347  -0.0519 368 HOH   A O   
6708 O  O   . HOH   E .   ? 0.2065 0.1812 0.2390 0.0018  0.0130  0.0215  369 HOH   A O   
6709 O  O   . HOH   E .   ? 0.2639 0.3478 0.3594 -0.0329 0.0964  -0.0259 370 HOH   A O   
6710 O  O   . HOH   E .   ? 0.2888 0.2128 0.2734 -0.0399 0.0353  -0.0058 371 HOH   A O   
6711 O  O   . HOH   E .   ? 0.2101 0.2348 0.2697 -0.0272 -0.0392 0.0497  372 HOH   A O   
6712 O  O   . HOH   E .   ? 0.1767 0.1431 0.2053 -0.0179 0.0196  0.0079  373 HOH   A O   
6713 O  O   . HOH   E .   ? 0.3383 0.2895 0.3198 -0.0673 -0.1252 0.0490  374 HOH   A O   
6714 O  O   . HOH   E .   ? 0.4725 0.2521 0.3658 -0.1589 0.1529  -0.0540 375 HOH   A O   
6715 O  O   . HOH   E .   ? 0.3475 0.2648 0.3606 -0.0084 -0.0324 0.1063  376 HOH   A O   
6716 O  O   . HOH   E .   ? 0.2652 0.4351 0.3642 -0.0230 0.0242  -0.0062 377 HOH   A O   
6717 O  O   . HOH   E .   ? 0.4158 0.2371 0.4700 -0.1069 0.0894  0.0479  378 HOH   A O   
6718 O  O   . HOH   E .   ? 0.1706 0.1788 0.2318 0.0093  -0.0271 0.0133  379 HOH   A O   
6719 O  O   . HOH   E .   ? 0.2529 0.2191 0.2139 -0.0624 0.0104  0.0373  380 HOH   A O   
6720 O  O   . HOH   E .   ? 0.2574 0.2570 0.4027 0.0046  -0.0211 0.0942  381 HOH   A O   
6721 O  O   . HOH   E .   ? 0.1732 0.1783 0.2878 -0.0179 0.0164  0.0446  382 HOH   A O   
6722 O  O   . HOH   E .   ? 0.2902 0.4843 0.3653 0.0791  0.0807  0.2331  383 HOH   A O   
6723 O  O   . HOH   E .   ? 0.2988 0.2506 0.5357 -0.0632 -0.0008 -0.0233 384 HOH   A O   
6724 O  O   . HOH   E .   ? 0.3018 0.3616 0.3967 -0.1326 0.0761  0.0035  385 HOH   A O   
6725 O  O   . HOH   E .   ? 0.6135 0.5629 0.7643 -0.1390 -0.0746 0.1011  386 HOH   A O   
6726 O  O   . HOH   E .   ? 0.1432 0.1745 0.2231 -0.0005 -0.0205 -0.0117 387 HOH   A O   
6727 O  O   . HOH   E .   ? 0.2705 0.4239 0.3893 -0.0246 0.1092  -0.1004 388 HOH   A O   
6728 O  O   . HOH   E .   ? 0.3219 0.3252 0.2145 0.0138  0.0518  0.0048  389 HOH   A O   
6729 O  O   . HOH   E .   ? 0.3742 0.5650 0.6386 0.0340  -0.0420 0.1901  390 HOH   A O   
6730 O  O   . HOH   E .   ? 0.1728 0.2850 0.3829 -0.0198 0.0684  0.0578  391 HOH   A O   
6731 O  O   . HOH   E .   ? 0.3154 0.3568 0.5367 0.1015  0.0875  0.0519  392 HOH   A O   
6732 O  O   . HOH   E .   ? 0.1426 0.1496 0.2234 -0.0025 -0.0169 0.0071  393 HOH   A O   
6733 O  O   . HOH   E .   ? 0.4734 0.4544 0.4447 0.1623  -0.1269 -0.1439 394 HOH   A O   
6734 O  O   . HOH   E .   ? 0.6611 0.7227 0.6278 -0.0987 0.0167  -0.0911 395 HOH   A O   
6735 O  O   . HOH   E .   ? 0.2221 0.2243 0.3755 0.0119  -0.0572 0.0363  396 HOH   A O   
6736 O  O   . HOH   E .   ? 0.2562 0.2933 0.3721 0.0107  -0.0262 -0.0722 397 HOH   A O   
6737 O  O   . HOH   E .   ? 0.1808 0.1889 0.4120 0.0357  0.0990  0.0885  398 HOH   A O   
6738 O  O   . HOH   E .   ? 0.2381 0.1847 0.3555 0.0116  -0.0351 0.0107  399 HOH   A O   
6739 O  O   A HOH   E .   ? 0.2950 0.2118 0.4315 -0.0179 0.1112  0.0163  400 HOH   A O   
6740 O  O   . HOH   E .   ? 0.3001 0.4102 0.4991 -0.0255 0.0842  0.0085  401 HOH   A O   
6741 O  O   . HOH   E .   ? 0.2160 0.1662 0.2149 -0.0007 0.0199  0.0278  402 HOH   A O   
6742 O  O   . HOH   E .   ? 0.2071 0.2322 0.3098 -0.0150 -0.0226 0.0859  403 HOH   A O   
6743 O  O   . HOH   E .   ? 0.5244 0.6347 0.6288 0.2548  0.1047  0.1091  404 HOH   A O   
6744 O  O   . HOH   E .   ? 0.2796 0.6318 0.2087 -0.0275 0.0534  -0.0129 405 HOH   A O   
6745 O  O   . HOH   E .   ? 0.1935 0.2978 0.4892 -0.0142 -0.0245 0.0323  406 HOH   A O   
6746 O  O   . HOH   E .   ? 0.2626 0.3503 0.7921 -0.0332 0.0395  -0.0463 407 HOH   A O   
6747 O  O   . HOH   E .   ? 0.2668 0.2307 0.2625 -0.0500 0.0034  0.0563  408 HOH   A O   
6748 O  O   . HOH   E .   ? 0.2308 0.3155 0.2753 -0.0224 -0.0523 0.0820  409 HOH   A O   
6749 O  O   . HOH   E .   ? 0.3941 0.4279 0.2547 -0.0734 -0.1026 0.0397  410 HOH   A O   
6750 O  O   . HOH   E .   ? 0.2704 0.2061 0.2929 0.0016  0.0210  0.0370  411 HOH   A O   
6751 O  O   . HOH   E .   ? 0.1971 0.1795 0.3380 0.0222  -0.0411 0.0198  412 HOH   A O   
6752 O  O   . HOH   E .   ? 0.3242 0.1326 0.2455 -0.0059 -0.0512 0.0145  413 HOH   A O   
6753 O  O   . HOH   E .   ? 0.1638 0.1764 0.3831 -0.0032 -0.0030 0.0270  414 HOH   A O   
6754 O  O   . HOH   E .   ? 0.5570 0.5572 0.2719 0.0190  0.0459  0.1089  415 HOH   A O   
6755 O  O   A HOH   E .   ? 0.3575 0.2242 0.2967 0.0710  0.1069  0.0852  416 HOH   A O   
6756 O  O   . HOH   E .   ? 0.4600 0.4247 0.6076 0.1502  0.1258  -0.1111 417 HOH   A O   
6757 O  O   . HOH   E .   ? 0.2453 0.4017 0.3009 0.1466  -0.0005 0.0410  418 HOH   A O   
6758 O  O   . HOH   E .   ? 0.1668 0.2297 0.3303 -0.0251 -0.0029 0.0604  419 HOH   A O   
6759 O  O   . HOH   E .   ? 0.5115 0.2636 0.3396 -0.1135 0.0301  0.0438  420 HOH   A O   
6760 O  O   . HOH   E .   ? 0.6238 0.4885 0.5127 -0.1394 0.0013  0.0952  421 HOH   A O   
6761 O  O   . HOH   E .   ? 0.2255 0.2652 0.3643 -0.0009 -0.0321 0.0123  422 HOH   A O   
6762 O  O   . HOH   E .   ? 0.4273 0.7042 0.3577 -0.0684 -0.0123 0.1791  423 HOH   A O   
6763 O  O   . HOH   E .   ? 0.5287 0.4865 0.3746 -0.0049 -0.1517 -0.0268 424 HOH   A O   
6764 O  O   . HOH   E .   ? 0.5489 0.6871 0.7238 -0.0655 -0.0624 -0.0263 425 HOH   A O   
6765 O  O   . HOH   E .   ? 0.6342 0.4280 0.5925 0.1735  -0.0837 0.1518  426 HOH   A O   
6766 O  O   . HOH   E .   ? 0.4072 0.2467 0.5870 -0.0954 -0.2394 0.1236  427 HOH   A O   
6767 O  O   . HOH   E .   ? 0.6152 0.7397 0.4439 0.0830  0.2567  -0.0782 428 HOH   A O   
6768 O  O   . HOH   E .   ? 0.6004 0.6968 0.7242 -0.1449 0.1029  -0.1265 429 HOH   A O   
6769 O  O   . HOH   E .   ? 0.1987 0.1688 0.2079 -0.0008 -0.0067 -0.0083 430 HOH   A O   
6770 O  O   . HOH   E .   ? 0.5118 0.3451 0.2706 -0.0836 0.0233  0.0109  431 HOH   A O   
6771 O  O   . HOH   E .   ? 0.1944 0.2250 0.4375 -0.0190 -0.0688 0.0565  432 HOH   A O   
6772 O  O   . HOH   E .   ? 0.2772 0.1822 0.3300 0.0233  0.0188  0.0156  433 HOH   A O   
6773 O  O   . HOH   E .   ? 0.3633 0.2980 0.2293 -0.0958 0.0141  0.0554  434 HOH   A O   
6774 O  O   . HOH   E .   ? 0.3879 0.3656 0.3398 0.2116  -0.0666 -0.0409 435 HOH   A O   
6775 O  O   . HOH   E .   ? 0.2745 0.3497 0.5233 0.0047  0.0761  -0.1155 436 HOH   A O   
6776 O  O   . HOH   E .   ? 0.5321 0.5007 0.5114 -0.0596 -0.1088 -0.1303 437 HOH   A O   
6777 O  O   . HOH   E .   ? 0.6765 0.8477 0.5181 0.2183  -0.1102 0.2520  438 HOH   A O   
6778 O  O   . HOH   E .   ? 0.4710 0.4708 0.7131 0.0156  -0.0622 -0.1379 439 HOH   A O   
6779 O  O   A HOH   E .   ? 0.2270 0.1508 0.2455 0.0169  -0.0772 -0.0110 440 HOH   A O   
6780 O  O   . HOH   E .   ? 0.6769 0.6728 0.7146 -0.0121 -0.0885 -0.0339 441 HOH   A O   
6781 O  O   . HOH   E .   ? 0.2243 0.2945 0.2761 0.0071  -0.0141 -0.0443 442 HOH   A O   
6782 O  O   . HOH   E .   ? 1.1265 1.0599 0.8904 -0.0324 -0.0449 -0.0509 443 HOH   A O   
6783 O  O   . HOH   E .   ? 0.2224 0.2041 0.3786 0.0089  0.0295  0.0346  444 HOH   A O   
6784 O  O   . HOH   E .   ? 0.6829 0.4688 0.7835 0.0126  -0.1206 0.1426  445 HOH   A O   
6785 O  O   A HOH   E .   ? 0.1536 0.1992 0.3018 0.0015  0.0109  0.0673  446 HOH   A O   
6786 O  O   . HOH   E .   ? 0.7271 0.6898 0.5436 -0.1044 0.1971  0.1379  447 HOH   A O   
6787 O  O   . HOH   E .   ? 0.4150 0.5713 0.4270 0.0144  0.1150  0.0671  448 HOH   A O   
6788 O  O   . HOH   E .   ? 0.5806 0.5154 0.4901 -0.0668 -0.0362 0.1406  449 HOH   A O   
6789 O  O   . HOH   E .   ? 0.3998 0.3354 0.4252 0.0412  0.0822  0.0192  450 HOH   A O   
6790 O  O   . HOH   E .   ? 0.3032 0.3675 0.3987 0.1157  -0.0321 0.0439  451 HOH   A O   
6791 O  O   . HOH   E .   ? 0.3986 0.5836 0.5124 -0.1462 0.1310  -0.0792 452 HOH   A O   
6792 O  O   . HOH   E .   ? 0.2697 0.2849 0.4043 -0.0457 0.0275  -0.0655 453 HOH   A O   
6793 O  O   . HOH   E .   ? 0.7609 0.8245 0.5139 -0.0349 -0.0854 -0.0286 454 HOH   A O   
6794 O  O   . HOH   E .   ? 0.3872 0.5413 0.5463 0.0484  -0.0361 0.1808  455 HOH   A O   
6795 O  O   . HOH   E .   ? 0.2834 0.4134 0.5678 0.0093  -0.0674 -0.0602 456 HOH   A O   
6796 O  O   . HOH   E .   ? 0.2878 0.2787 0.3439 -0.0873 0.0424  -0.0365 457 HOH   A O   
6797 O  O   . HOH   E .   ? 0.2769 0.4156 0.6288 0.0405  0.0037  -0.1656 458 HOH   A O   
6798 O  O   . HOH   E .   ? 0.6193 0.3955 0.7490 0.1078  -0.0157 0.2660  459 HOH   A O   
6799 O  O   . HOH   E .   ? 0.4316 0.4361 0.4080 -0.1389 0.0043  -0.0321 460 HOH   A O   
6800 O  O   . HOH   E .   ? 0.6327 0.4645 0.4747 0.0446  0.1273  0.0663  461 HOH   A O   
6801 O  O   . HOH   E .   ? 0.2618 0.1912 0.3028 0.0251  -0.0838 -0.0302 462 HOH   A O   
6802 O  O   . HOH   E .   ? 0.3790 0.6938 0.4364 -0.0859 -0.1031 0.2443  463 HOH   A O   
6803 O  O   . HOH   E .   ? 0.4508 0.5386 0.3886 0.0502  -0.1015 -0.0737 464 HOH   A O   
6804 O  O   . HOH   E .   ? 0.6006 0.5633 0.4517 0.1517  -0.0337 -0.0534 465 HOH   A O   
6805 O  O   . HOH   E .   ? 0.3406 0.2519 0.3871 0.0045  0.0877  0.0219  466 HOH   A O   
6806 O  O   . HOH   E .   ? 0.8088 0.6300 0.5952 -0.0090 0.1741  0.1968  467 HOH   A O   
6807 O  O   . HOH   E .   ? 0.2640 0.2664 0.2819 0.0292  -0.0148 -0.0050 468 HOH   A O   
6808 O  O   . HOH   E .   ? 0.6095 0.6738 0.7630 -0.1648 -0.1412 0.0625  469 HOH   A O   
6809 O  O   . HOH   E .   ? 0.4242 0.4624 0.5432 -0.1860 -0.0255 -0.0129 470 HOH   A O   
6810 O  O   . HOH   E .   ? 0.4479 0.4457 0.3490 -0.0047 -0.0467 -0.0376 471 HOH   A O   
6811 O  O   . HOH   E .   ? 0.4154 0.5386 0.2967 0.0235  -0.0100 0.0715  472 HOH   A O   
6812 O  O   . HOH   E .   ? 0.5761 0.4495 0.5042 -0.0432 -0.0547 -0.1143 473 HOH   A O   
6813 O  O   . HOH   E .   ? 0.6750 0.3886 0.5119 -0.0313 0.0709  0.0018  474 HOH   A O   
6814 O  O   . HOH   E .   ? 0.4415 0.4447 0.4526 0.0295  0.1911  0.0915  475 HOH   A O   
6815 O  O   . HOH   E .   ? 0.7545 0.3992 0.4109 -0.0355 -0.1407 0.0265  476 HOH   A O   
6816 O  O   . HOH   E .   ? 0.5742 0.2916 0.3381 -0.0589 -0.1215 0.0744  477 HOH   A O   
6817 O  O   . HOH   E .   ? 0.6879 0.5102 0.7138 -0.0963 0.0676  -0.0816 478 HOH   A O   
6818 O  O   . HOH   E .   ? 0.4800 0.4003 0.2815 -0.1155 0.1422  -0.0748 479 HOH   A O   
6819 O  O   . HOH   E .   ? 0.2704 0.2401 0.6106 -0.0021 -0.1148 0.0228  480 HOH   A O   
6820 O  O   . HOH   E .   ? 0.6053 0.6957 0.5878 0.0775  -0.1275 0.0486  481 HOH   A O   
6821 O  O   . HOH   E .   ? 0.7155 0.5174 0.5768 -0.1046 -0.0902 -0.1007 482 HOH   A O   
6822 O  O   . HOH   E .   ? 0.6733 0.5961 0.7295 0.1297  0.3006  -0.0923 483 HOH   A O   
6823 O  O   . HOH   E .   ? 0.2773 0.5432 0.3862 0.0980  0.0981  0.2504  484 HOH   A O   
6824 O  O   . HOH   E .   ? 0.5252 0.5535 0.4849 0.0151  -0.0386 -0.0657 485 HOH   A O   
6825 O  O   . HOH   E .   ? 0.3332 0.2344 0.7120 0.0091  0.0690  0.0775  486 HOH   A O   
6826 O  O   . HOH   E .   ? 0.7477 0.7990 0.5324 -0.0384 0.1906  0.2099  487 HOH   A O   
6827 O  O   . HOH   E .   ? 0.4267 0.3984 0.4824 -0.0774 0.0690  0.1065  488 HOH   A O   
6828 O  O   . HOH   E .   ? 0.4777 0.3249 0.4794 -0.0070 0.2309  0.0293  489 HOH   A O   
6829 O  O   . HOH   E .   ? 0.2961 0.2876 0.6288 0.0001  0.1579  -0.0493 490 HOH   A O   
6830 O  O   . HOH   E .   ? 0.2707 0.3853 0.3587 0.0772  -0.0647 0.0611  491 HOH   A O   
6831 O  O   . HOH   E .   ? 0.4145 0.9084 0.5946 -0.0365 -0.0583 0.1726  492 HOH   A O   
6832 O  O   . HOH   E .   ? 0.3336 0.3985 0.5047 0.0506  -0.0581 0.0373  493 HOH   A O   
6833 O  O   . HOH   E .   ? 0.5911 0.2688 0.4104 -0.0662 0.0740  0.0324  494 HOH   A O   
6834 O  O   . HOH   E .   ? 0.8100 0.8167 0.6687 0.1367  -0.1439 -0.0007 495 HOH   A O   
6835 O  O   . HOH   E .   ? 0.2989 0.4833 0.3525 -0.0283 -0.0367 -0.0568 496 HOH   A O   
6836 O  O   . HOH   E .   ? 0.5557 0.8132 0.5164 0.0782  -0.0549 0.1840  497 HOH   A O   
6837 O  O   . HOH   E .   ? 0.5723 0.2882 0.5333 -0.0750 -0.0941 0.1799  498 HOH   A O   
6838 O  O   . HOH   E .   ? 0.2883 0.6564 0.3421 0.0888  0.0492  0.0947  499 HOH   A O   
6839 O  O   . HOH   E .   ? 0.3225 0.2395 0.4390 0.0214  0.0324  0.0322  500 HOH   A O   
6840 O  O   . HOH   E .   ? 0.5581 0.7711 0.5706 0.3424  -0.0167 0.1599  501 HOH   A O   
6841 O  O   . HOH   E .   ? 0.6830 0.5576 0.4564 -0.0949 -0.0954 -0.1266 502 HOH   A O   
6842 O  O   . HOH   E .   ? 0.2923 0.7382 0.4399 0.0621  0.0484  -0.0691 503 HOH   A O   
6843 O  O   . HOH   E .   ? 0.4481 0.7149 0.4995 -0.0489 -0.0733 0.1015  504 HOH   A O   
6844 O  O   . HOH   E .   ? 0.5087 0.4950 0.4768 0.1357  0.0155  0.1267  505 HOH   A O   
6845 O  O   . HOH   E .   ? 0.2984 0.4622 0.5563 -0.0231 -0.0741 0.2771  506 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2191 0.2381 0.3166 0.0190  0.0620  0.0336  201 HOH   B O   
6847 O  O   . HOH   F .   ? 0.4921 0.3927 0.4195 -0.0078 -0.0088 -0.1498 202 HOH   B O   
6848 O  O   . HOH   F .   ? 0.3610 0.3313 0.6865 -0.0254 0.0407  -0.0590 203 HOH   B O   
6849 O  O   . HOH   F .   ? 0.3359 0.2401 0.5449 -0.0135 0.1879  0.0452  204 HOH   B O   
6850 O  O   . HOH   F .   ? 0.3293 0.5739 0.4390 -0.0229 0.1612  -0.1608 205 HOH   B O   
6851 O  O   . HOH   F .   ? 0.5044 0.6008 0.4877 0.3013  -0.1233 -0.0225 206 HOH   B O   
6852 O  O   . HOH   F .   ? 0.2916 0.7446 0.4496 0.1337  0.0549  0.2887  207 HOH   B O   
6853 O  O   . HOH   F .   ? 0.1671 0.2006 0.3593 -0.0215 -0.0104 0.0105  208 HOH   B O   
6854 O  O   . HOH   F .   ? 0.7596 0.4750 0.3997 -0.0772 0.0286  0.0547  209 HOH   B O   
6855 O  O   . HOH   F .   ? 0.7687 0.3753 0.4421 0.0748  0.1342  -0.0383 210 HOH   B O   
6856 O  O   . HOH   F .   ? 0.1911 0.2341 0.3095 -0.0036 0.0306  -0.0164 211 HOH   B O   
6857 O  O   . HOH   F .   ? 0.4166 0.5293 0.4361 0.2238  0.0340  0.0644  212 HOH   B O   
6858 O  O   . HOH   F .   ? 0.7270 0.7811 0.5457 0.3005  -0.0062 -0.0513 213 HOH   B O   
6859 O  O   . HOH   F .   ? 0.3134 0.5332 0.2950 -0.0175 -0.0217 -0.1293 214 HOH   B O   
6860 O  O   . HOH   F .   ? 0.3615 0.3145 0.4583 0.0672  -0.0607 -0.0047 215 HOH   B O   
6861 O  O   . HOH   F .   ? 0.2906 0.1919 0.5690 -0.0148 0.1592  0.0346  216 HOH   B O   
6862 O  O   . HOH   F .   ? 0.1833 0.2454 0.3420 -0.0190 0.0220  -0.0206 217 HOH   B O   
6863 O  O   . HOH   F .   ? 0.2827 0.2465 0.6464 0.0611  -0.1063 0.0404  218 HOH   B O   
6864 O  O   . HOH   F .   ? 0.4888 0.6593 0.2888 -0.1441 -0.1098 0.0035  219 HOH   B O   
6865 O  O   . HOH   F .   ? 0.3916 0.4398 0.5883 -0.1087 -0.0365 -0.1332 220 HOH   B O   
6866 O  O   . HOH   F .   ? 0.4438 0.4038 0.3490 -0.0069 -0.1391 0.0381  221 HOH   B O   
6867 O  O   . HOH   F .   ? 0.3985 0.5618 0.5739 0.2638  0.0279  -0.0705 222 HOH   B O   
6868 O  O   . HOH   F .   ? 0.4834 0.4589 0.4148 0.0551  0.1231  -0.1138 223 HOH   B O   
6869 O  O   . HOH   F .   ? 0.2269 0.2403 0.3869 -0.0351 0.0178  -0.0612 224 HOH   B O   
6870 O  O   . HOH   F .   ? 0.5573 0.4442 0.6306 0.0872  -0.0621 0.2795  225 HOH   B O   
6871 O  O   . HOH   F .   ? 0.2592 0.2668 0.3096 0.0232  0.0286  -0.0738 226 HOH   B O   
6872 O  O   . HOH   F .   ? 0.2362 0.1837 0.2695 -0.0314 0.0682  -0.0087 227 HOH   B O   
6873 O  O   . HOH   F .   ? 0.3769 0.1864 0.2212 0.0254  -0.0686 0.0004  228 HOH   B O   
6874 O  O   . HOH   F .   ? 0.5364 0.8363 0.4549 0.3085  0.0954  0.1293  229 HOH   B O   
6875 O  O   . HOH   F .   ? 0.6353 0.6481 0.3878 -0.0240 -0.0407 0.0849  230 HOH   B O   
6876 O  O   . HOH   F .   ? 0.2080 0.1376 0.3700 0.0152  -0.0524 -0.0074 231 HOH   B O   
6877 O  O   . HOH   F .   ? 0.5554 0.3288 0.4007 -0.2350 0.0233  0.0187  232 HOH   B O   
6878 O  O   . HOH   F .   ? 0.4018 0.3585 0.6368 -0.0113 -0.1617 -0.0658 233 HOH   B O   
6879 O  O   . HOH   F .   ? 0.4040 0.2403 0.4558 0.0570  -0.1075 -0.1201 234 HOH   B O   
6880 O  O   . HOH   F .   ? 0.5569 0.2125 0.3379 0.0183  -0.0668 0.0086  235 HOH   B O   
6881 O  O   . HOH   F .   ? 0.1535 0.1528 0.1726 -0.0119 -0.0051 0.0003  236 HOH   B O   
6882 O  O   . HOH   F .   ? 0.2603 0.3348 0.3481 -0.1003 0.0406  -0.0554 237 HOH   B O   
6883 O  O   . HOH   F .   ? 0.2773 0.4646 0.5865 0.1324  -0.0641 -0.0815 238 HOH   B O   
6884 O  O   . HOH   F .   ? 0.3959 0.2700 0.3908 0.0514  -0.0480 -0.0581 239 HOH   B O   
6885 O  O   . HOH   F .   ? 0.3490 0.3846 0.4336 0.1372  -0.0526 -0.0866 240 HOH   B O   
6886 O  O   . HOH   F .   ? 0.2223 0.4044 0.2406 -0.0259 -0.0085 0.0526  241 HOH   B O   
6887 O  O   . HOH   F .   ? 0.3668 0.2938 0.2401 0.0204  0.0472  0.0291  242 HOH   B O   
6888 O  O   . HOH   F .   ? 0.5055 0.3134 0.4132 -0.1648 -0.0490 0.0099  243 HOH   B O   
6889 O  O   . HOH   F .   ? 0.2929 0.4911 0.3106 -0.1190 -0.0277 -0.0733 244 HOH   B O   
6890 O  O   . HOH   F .   ? 0.3353 0.1945 0.6301 -0.0312 -0.1167 -0.0166 245 HOH   B O   
6891 O  O   . HOH   F .   ? 0.2952 0.3231 0.3510 -0.0712 0.0504  -0.0081 246 HOH   B O   
6892 O  O   . HOH   F .   ? 0.1547 0.1533 0.3231 -0.0117 0.0034  -0.0074 247 HOH   B O   
6893 O  O   . HOH   F .   ? 0.2822 0.2285 0.2937 0.0649  0.0572  -0.0203 248 HOH   B O   
6894 O  O   . HOH   F .   ? 0.2468 0.3420 0.2266 -0.0642 0.0192  0.0444  249 HOH   B O   
6895 O  O   . HOH   F .   ? 0.7509 0.5396 0.4165 0.1612  -0.0049 -0.1072 250 HOH   B O   
6896 O  O   . HOH   F .   ? 0.2160 0.1980 0.2398 -0.0328 -0.0362 0.0181  251 HOH   B O   
6897 O  O   . HOH   F .   ? 0.1609 0.1357 0.1926 0.0024  -0.0134 0.0104  252 HOH   B O   
6898 O  O   . HOH   F .   ? 0.1645 0.1743 0.3657 -0.0230 -0.0248 0.0196  253 HOH   B O   
6899 O  O   . HOH   F .   ? 0.3802 0.4479 0.2458 -0.0226 0.0847  -0.0033 254 HOH   B O   
6900 O  O   . HOH   F .   ? 0.2459 0.2218 0.2900 0.0861  -0.0792 -0.0558 255 HOH   B O   
6901 O  O   . HOH   F .   ? 0.3912 0.2370 0.2512 0.0693  -0.0429 -0.0291 256 HOH   B O   
6902 O  O   . HOH   F .   ? 0.2123 0.2026 0.4653 0.0056  -0.0505 -0.0532 257 HOH   B O   
6903 O  O   . HOH   F .   ? 0.3488 0.5082 0.3432 0.0166  -0.0986 0.0772  258 HOH   B O   
6904 O  O   . HOH   F .   ? 0.2696 0.3963 0.3147 -0.0799 -0.0627 -0.0363 259 HOH   B O   
6905 O  O   . HOH   F .   ? 0.3197 0.4657 0.6221 -0.0697 -0.0333 -0.1337 260 HOH   B O   
6906 O  O   . HOH   F .   ? 0.2273 0.1652 0.2284 -0.0369 -0.0445 0.0274  261 HOH   B O   
6907 O  O   . HOH   F .   ? 0.4355 0.4177 0.3151 0.0473  0.0198  -0.0640 262 HOH   B O   
6908 O  O   . HOH   F .   ? 0.1908 0.2804 0.3121 0.0410  0.0458  0.0941  263 HOH   B O   
6909 O  O   . HOH   F .   ? 0.4024 0.2844 0.2963 -0.0648 0.0201  -0.0553 264 HOH   B O   
6910 O  O   . HOH   F .   ? 0.2567 0.2276 0.2087 0.0101  -0.0029 -0.0016 265 HOH   B O   
6911 O  O   . HOH   F .   ? 0.4125 0.3877 0.5774 -0.1493 -0.0238 0.1129  266 HOH   B O   
6912 O  O   . HOH   F .   ? 0.3923 0.4313 0.4890 -0.0819 0.1060  -0.1071 267 HOH   B O   
6913 O  O   . HOH   F .   ? 0.4929 0.5289 0.5316 0.0291  -0.1513 0.0623  268 HOH   B O   
6914 O  O   . HOH   F .   ? 0.2025 0.5123 0.5364 -0.0118 0.0018  -0.1345 269 HOH   B O   
6915 O  O   . HOH   F .   ? 0.1412 0.1757 0.2585 -0.0036 0.0094  0.0186  270 HOH   B O   
6916 O  O   . HOH   F .   ? 0.2281 0.1606 0.2572 -0.0327 -0.0164 0.0111  271 HOH   B O   
6917 O  O   . HOH   F .   ? 0.1861 0.1481 0.4496 -0.0110 -0.0164 -0.0120 272 HOH   B O   
6918 O  O   . HOH   F .   ? 0.2812 0.4034 0.4174 0.0290  0.1519  0.0224  273 HOH   B O   
6919 O  O   . HOH   F .   ? 0.2565 0.2023 0.3002 -0.0531 0.0376  -0.0096 274 HOH   B O   
6920 O  O   . HOH   F .   ? 0.3317 0.2137 0.4955 0.0414  0.0328  0.0423  275 HOH   B O   
6921 O  O   . HOH   F .   ? 0.4479 0.3739 0.4047 -0.0668 0.0064  0.0229  276 HOH   B O   
6922 O  O   . HOH   F .   ? 0.2586 0.2759 0.2596 -0.0260 -0.0653 0.0330  277 HOH   B O   
6923 O  O   . HOH   F .   ? 0.1944 0.1890 0.1882 -0.0555 -0.0451 0.0144  278 HOH   B O   
6924 O  O   . HOH   F .   ? 0.2400 0.2750 0.2431 -0.0434 -0.0631 -0.0319 279 HOH   B O   
6925 O  O   . HOH   F .   ? 0.4406 0.2738 0.5090 -0.0340 -0.1176 -0.0370 280 HOH   B O   
6926 O  O   . HOH   F .   ? 0.2882 0.7886 0.2752 0.1492  -0.0450 -0.1196 281 HOH   B O   
6927 O  O   . HOH   F .   ? 0.2983 0.5501 0.2159 0.2005  -0.0166 -0.0118 282 HOH   B O   
6928 O  O   . HOH   F .   ? 0.3233 0.4830 0.4595 -0.1050 -0.1263 0.0887  283 HOH   B O   
6929 O  O   . HOH   F .   ? 0.3030 0.7551 0.7661 0.1340  -0.0825 -0.1256 284 HOH   B O   
6930 O  O   . HOH   F .   ? 0.1834 0.1552 0.2218 -0.0039 0.0137  0.0027  285 HOH   B O   
6931 O  O   . HOH   F .   ? 0.2426 0.3642 0.4033 -0.0616 0.0655  -0.1326 286 HOH   B O   
6932 O  O   . HOH   F .   ? 0.3576 0.3267 0.2883 -0.0705 0.0379  -0.1261 287 HOH   B O   
6933 O  O   . HOH   F .   ? 0.1726 0.1645 0.3764 -0.0120 -0.0006 -0.0005 288 HOH   B O   
6934 O  O   . HOH   F .   ? 0.3909 0.3153 0.4894 -0.0582 -0.0638 0.0928  289 HOH   B O   
6935 O  O   . HOH   F .   ? 0.4785 0.4116 0.3486 -0.1923 0.1262  -0.0237 290 HOH   B O   
6936 O  O   . HOH   F .   ? 0.2694 0.2794 0.3047 0.0052  -0.0806 0.0283  291 HOH   B O   
6937 O  O   . HOH   F .   ? 0.1735 0.2041 0.1844 -0.0101 -0.0110 0.0133  292 HOH   B O   
6938 O  O   . HOH   F .   ? 0.5177 0.4880 0.6363 0.0458  0.1090  -0.0596 293 HOH   B O   
6939 O  O   . HOH   F .   ? 0.1904 0.2188 0.3301 0.0220  -0.0010 0.0041  294 HOH   B O   
6940 O  O   . HOH   F .   ? 0.2222 0.2437 0.5058 -0.0569 0.0118  0.1235  295 HOH   B O   
6941 O  O   . HOH   F .   ? 0.4374 0.5699 0.2734 0.0351  0.1032  0.1443  296 HOH   B O   
6942 O  O   . HOH   F .   ? 0.3515 0.2508 0.2442 0.0039  -0.0772 0.0007  297 HOH   B O   
6943 O  O   . HOH   F .   ? 0.4342 0.2772 0.2576 -0.1605 0.0353  -0.0178 298 HOH   B O   
6944 O  O   . HOH   F .   ? 0.2106 0.3194 0.6595 0.0562  -0.0592 -0.1543 299 HOH   B O   
6945 O  O   . HOH   F .   ? 0.4127 0.3730 0.2481 0.0928  -0.0803 0.0503  300 HOH   B O   
6946 O  O   . HOH   F .   ? 0.1821 0.1739 0.2850 0.0123  0.0049  0.0155  301 HOH   B O   
6947 O  O   . HOH   F .   ? 0.2215 0.6174 0.5459 -0.0801 -0.0067 0.0496  302 HOH   B O   
6948 O  O   . HOH   F .   ? 0.1852 0.3901 0.5027 0.0429  -0.0250 -0.1501 303 HOH   B O   
6949 O  O   . HOH   F .   ? 0.8104 0.6898 0.3938 0.0407  -0.0566 0.1374  304 HOH   B O   
6950 O  O   . HOH   F .   ? 0.3109 0.3171 0.3414 -0.0308 0.1125  -0.0823 305 HOH   B O   
6951 O  O   . HOH   F .   ? 0.6131 0.4129 0.3314 0.2779  0.1386  0.0998  306 HOH   B O   
6952 O  O   . HOH   F .   ? 0.4177 0.2306 0.4389 -0.1158 -0.2147 0.1009  307 HOH   B O   
6953 O  O   . HOH   F .   ? 0.2320 0.1753 0.2868 -0.0350 -0.0211 -0.0093 308 HOH   B O   
6954 O  O   . HOH   F .   ? 0.5511 0.3814 0.2745 0.0099  -0.0378 -0.0328 309 HOH   B O   
6955 O  O   . HOH   F .   ? 0.2106 0.1613 0.3731 0.0431  -0.0802 -0.0009 310 HOH   B O   
6956 O  O   . HOH   F .   ? 0.6139 0.4064 0.3926 0.1000  0.1553  0.1751  311 HOH   B O   
6957 O  O   . HOH   F .   ? 0.2482 0.1924 0.2133 -0.0006 0.0196  0.0230  312 HOH   B O   
6958 O  O   . HOH   F .   ? 0.3338 0.1969 0.3575 0.0725  0.1030  0.0386  313 HOH   B O   
6959 O  O   . HOH   F .   ? 0.2144 0.2917 0.5317 -0.0140 -0.0847 -0.0169 314 HOH   B O   
6960 O  O   . HOH   F .   ? 0.3358 0.2476 0.2704 0.0400  -0.0296 0.0423  315 HOH   B O   
6961 O  O   . HOH   F .   ? 0.5834 0.4851 0.4950 0.2222  -0.0339 0.0816  316 HOH   B O   
6962 O  O   . HOH   F .   ? 0.7298 0.4887 0.5192 0.1851  0.1834  0.0274  317 HOH   B O   
6963 O  O   . HOH   F .   ? 0.2742 0.1587 0.3051 -0.0303 -0.0349 0.0381  318 HOH   B O   
6964 O  O   . HOH   F .   ? 0.4807 0.6852 0.3930 0.1077  -0.0702 0.0910  319 HOH   B O   
6965 O  O   . HOH   F .   ? 0.1706 0.2869 0.2529 -0.0202 -0.0174 0.0720  320 HOH   B O   
6966 O  O   . HOH   F .   ? 0.1698 0.1564 0.3702 0.0073  0.0032  0.0077  321 HOH   B O   
6967 O  O   . HOH   F .   ? 0.4097 0.2214 0.3054 0.1328  0.0947  0.0292  322 HOH   B O   
6968 O  O   . HOH   F .   ? 0.5295 0.4401 0.4386 -0.0254 0.1634  -0.1424 323 HOH   B O   
6969 O  O   . HOH   F .   ? 0.1681 0.1900 0.3292 -0.0316 -0.0082 0.0142  324 HOH   B O   
6970 O  O   . HOH   F .   ? 0.4599 0.4044 0.5726 0.0457  -0.0037 0.0406  325 HOH   B O   
6971 O  O   . HOH   F .   ? 0.3107 0.3288 0.5783 -0.0681 -0.1860 0.1847  326 HOH   B O   
6972 O  O   . HOH   F .   ? 0.1711 0.1730 0.3547 -0.0132 -0.0191 -0.0139 327 HOH   B O   
6973 O  O   . HOH   F .   ? 0.5175 0.3551 0.4246 -0.0832 0.0241  0.0749  328 HOH   B O   
6974 O  O   . HOH   F .   ? 0.1928 0.1998 0.2919 0.0237  0.0420  0.0206  329 HOH   B O   
6975 O  O   . HOH   F .   ? 0.2066 0.3231 0.3623 0.0623  -0.0393 -0.0884 330 HOH   B O   
6976 O  O   . HOH   F .   ? 0.2755 0.2029 0.5492 -0.0017 -0.0048 0.0580  331 HOH   B O   
6977 O  O   . HOH   F .   ? 0.5168 0.3183 0.3196 0.0927  0.0110  0.0467  332 HOH   B O   
6978 O  O   . HOH   F .   ? 0.5869 0.4869 0.6072 -0.1151 -0.1067 -0.1333 333 HOH   B O   
6979 O  O   . HOH   F .   ? 0.4871 0.3492 0.5766 0.1648  0.2360  0.2009  334 HOH   B O   
6980 O  O   . HOH   F .   ? 0.5092 0.4744 0.8555 -0.0693 -0.1337 0.2746  335 HOH   B O   
6981 O  O   . HOH   F .   ? 0.6605 0.5825 0.7216 0.1999  -0.0700 0.2732  336 HOH   B O   
6982 O  O   . HOH   F .   ? 0.3464 0.5947 0.7479 -0.0162 0.0207  -0.0329 337 HOH   B O   
6983 O  O   . HOH   F .   ? 0.1842 0.1525 0.2876 0.0053  -0.0103 0.0143  338 HOH   B O   
6984 O  O   . HOH   F .   ? 0.4388 0.7786 0.4100 -0.0986 -0.1143 0.2099  339 HOH   B O   
6985 O  O   . HOH   F .   ? 0.9036 0.2527 0.3796 0.0729  -0.1177 -0.0254 340 HOH   B O   
6986 O  O   . HOH   F .   ? 0.5031 0.3918 0.2481 0.1403  -0.1164 -0.0339 341 HOH   B O   
6987 O  O   . HOH   F .   ? 0.4265 0.5705 0.3910 -0.1180 -0.0832 -0.0539 342 HOH   B O   
6988 O  O   . HOH   F .   ? 0.2790 0.1890 0.3977 0.0270  -0.0758 -0.0354 343 HOH   B O   
6989 O  O   . HOH   F .   ? 0.4433 0.3419 0.3239 0.0310  -0.1126 -0.0593 344 HOH   B O   
6990 O  O   . HOH   F .   ? 0.5950 0.5730 0.5237 -0.1076 -0.0713 0.1537  345 HOH   B O   
6991 O  O   . HOH   F .   ? 0.5152 0.5575 0.3611 -0.0380 -0.1167 0.0242  346 HOH   B O   
6992 O  O   . HOH   F .   ? 0.2146 0.2128 0.5011 -0.0231 0.1069  -0.0484 347 HOH   B O   
6993 O  O   . HOH   F .   ? 0.3572 0.5026 0.5321 -0.1636 0.0147  -0.0457 348 HOH   B O   
6994 O  O   . HOH   F .   ? 0.4697 0.7039 0.5854 0.0364  -0.1115 -0.0061 349 HOH   B O   
6995 O  O   . HOH   F .   ? 0.4741 0.5561 0.6412 -0.1313 -0.0165 0.1336  350 HOH   B O   
6996 O  O   . HOH   F .   ? 0.3364 0.2376 0.4409 -0.0374 -0.0966 -0.0303 351 HOH   B O   
6997 O  O   . HOH   F .   ? 0.2509 0.6582 0.3298 0.1613  -0.0599 -0.1392 352 HOH   B O   
6998 O  O   . HOH   F .   ? 0.4241 0.6870 0.6793 0.0813  0.0609  -0.0498 353 HOH   B O   
6999 O  O   . HOH   F .   ? 0.2386 0.4353 0.5455 0.0043  -0.0119 0.0301  354 HOH   B O   
7000 O  O   . HOH   F .   ? 0.3982 0.2131 0.3266 -0.0817 0.0160  -0.0579 355 HOH   B O   
7001 O  O   . HOH   F .   ? 0.5096 0.5220 0.4347 0.1665  -0.1023 0.0811  356 HOH   B O   
7002 O  O   . HOH   F .   ? 0.4856 0.2589 0.5819 -0.0735 0.1387  0.0284  357 HOH   B O   
7003 O  O   . HOH   F .   ? 0.4025 0.2748 0.4266 -0.0896 -0.0310 -0.0704 358 HOH   B O   
7004 O  O   . HOH   F .   ? 0.5178 0.3708 0.4432 0.0103  0.1423  -0.0298 359 HOH   B O   
7005 O  O   . HOH   F .   ? 0.5056 0.4309 0.6102 0.0203  0.0722  0.1136  360 HOH   B O   
7006 O  O   . HOH   F .   ? 0.5896 0.3856 0.4837 -0.0274 -0.1363 -0.0770 361 HOH   B O   
7007 O  O   . HOH   F .   ? 0.3869 0.6929 0.3152 0.1761  0.0040  0.0538  362 HOH   B O   
7008 O  O   . HOH   F .   ? 0.6578 0.2629 0.4101 -0.0266 0.0461  0.0910  363 HOH   B O   
7009 O  O   . HOH   F .   ? 0.2222 0.3740 0.6994 -0.0726 -0.0612 -0.0617 364 HOH   B O   
7010 O  O   . HOH   F .   ? 0.5753 0.4433 0.5133 0.0044  0.0677  0.0246  365 HOH   B O   
7011 O  O   . HOH   F .   ? 0.5095 0.6648 0.4658 -0.0812 -0.0055 -0.1182 366 HOH   B O   
7012 O  O   . HOH   F .   ? 0.4874 0.2985 0.5411 0.0426  -0.1547 0.0031  367 HOH   B O   
7013 O  O   . HOH   F .   ? 0.6043 0.4929 0.4089 0.1277  0.0805  0.0825  368 HOH   B O   
7014 O  O   . HOH   F .   ? 0.5697 0.3002 0.5977 -0.1362 -0.0303 0.0281  369 HOH   B O   
7015 O  O   . HOH   F .   ? 0.4431 0.2716 0.3798 0.0503  -0.1417 -0.0096 370 HOH   B O   
7016 O  O   . HOH   F .   ? 0.3932 0.5597 0.5419 0.2230  0.0942  0.1641  371 HOH   B O   
7017 O  O   . HOH   F .   ? 0.7372 0.3742 0.2947 -0.0760 -0.1117 -0.0445 372 HOH   B O   
7018 O  O   . HOH   F .   ? 0.5675 0.6664 0.3903 0.2117  -0.1470 0.1103  373 HOH   B O   
7019 O  O   . HOH   F .   ? 0.8337 0.8485 0.6052 0.2897  -0.1328 0.0181  374 HOH   B O   
7020 O  O   . HOH   F .   ? 0.4210 0.4702 0.4550 -0.0312 -0.0499 -0.0249 375 HOH   B O   
7021 O  O   . HOH   F .   ? 0.4794 0.6990 0.5764 0.1534  0.0248  0.2548  376 HOH   B O   
7022 O  O   . HOH   F .   ? 0.2355 0.3565 0.5132 0.0314  -0.0515 -0.0771 377 HOH   B O   
7023 O  O   . HOH   F .   ? 0.3842 0.5772 0.6205 0.0504  -0.0091 0.0610  378 HOH   B O   
7024 O  O   . HOH   F .   ? 0.6772 0.3532 0.4620 -0.0998 -0.0169 0.0035  379 HOH   B O   
7025 O  O   . HOH   F .   ? 0.5272 0.7260 0.3734 -0.1416 0.0015  -0.1526 380 HOH   B O   
7026 O  O   . HOH   F .   ? 0.4164 0.6937 0.2416 -0.0967 0.0475  0.0266  381 HOH   B O   
7027 O  O   . HOH   F .   ? 0.4985 0.6918 0.6484 -0.0909 0.1781  0.0874  382 HOH   B O   
7028 O  O   . HOH   F .   ? 0.4547 0.9113 0.5194 0.1073  0.1327  0.0548  383 HOH   B O   
7029 O  O   . HOH   F .   ? 0.7739 0.3357 0.3982 0.0407  0.1766  -0.0579 384 HOH   B O   
7030 O  O   . HOH   F .   ? 0.8078 0.6568 0.5556 0.2157  0.0162  -0.0135 385 HOH   B O   
7031 O  O   . HOH   F .   ? 0.2810 0.2630 0.3447 -0.0009 0.0020  0.0298  386 HOH   B O   
7032 O  O   . HOH   F .   ? 0.4786 0.3456 0.5164 -0.1787 0.0107  0.0764  387 HOH   B O   
7033 O  O   . HOH   F .   ? 0.6476 0.4528 0.5469 -0.0831 0.1140  0.0119  388 HOH   B O   
7034 O  O   . HOH   F .   ? 0.5721 0.4087 0.3773 -0.0303 0.0861  -0.0242 389 HOH   B O   
7035 O  O   . HOH   F .   ? 0.2669 0.4466 0.4506 -0.0675 -0.1069 -0.0077 390 HOH   B O   
7036 O  O   . HOH   F .   ? 0.4674 0.2294 0.3429 0.1014  -0.0260 0.0119  391 HOH   B O   
7037 O  O   . HOH   F .   ? 0.4288 0.2290 0.4488 -0.0743 -0.0223 0.0554  392 HOH   B O   
7038 O  O   . HOH   F .   ? 0.5747 0.5466 0.5373 0.1269  0.0169  0.0209  393 HOH   B O   
7039 O  O   . HOH   F .   ? 0.2762 0.5256 0.6810 -0.1713 -0.0733 -0.0383 394 HOH   B O   
7040 O  O   . HOH   F .   ? 0.3174 0.4528 0.4111 0.0163  0.0259  -0.0908 395 HOH   B O   
7041 O  O   . HOH   F .   ? 0.2102 0.2808 0.6127 -0.0640 -0.0579 0.0064  396 HOH   B O   
7042 O  O   . HOH   F .   ? 0.4735 0.6098 0.5196 0.0953  0.0609  -0.1029 397 HOH   B O   
7043 O  O   . HOH   F .   ? 0.5032 0.4822 0.4522 0.1206  0.1409  0.1192  398 HOH   B O   
7044 O  O   . HOH   F .   ? 0.5343 0.5643 0.5307 -0.0104 -0.1319 0.2479  399 HOH   B O   
7045 O  O   . HOH   F .   ? 0.5840 0.4167 0.3259 -0.2273 -0.0700 0.0925  400 HOH   B O   
7046 O  O   . HOH   F .   ? 0.6192 0.4978 0.3683 0.1184  -0.0804 -0.0531 401 HOH   B O   
# 
