data_7HEN
# 
_entry.id   7HEN 
# 
_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   7HEN         pdb_00007hen 10.2210/pdb7hen/pdb 
WWPDB D_1001407377 ?            ?                   
# 
_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                        7HEN 
_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 '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 218.255   1   ?                      ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                      35.453    1   ?                      ? ? ? 
4 water       nat water                                                               18.015    436 ?                      ? ? ? 
# 
_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 '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1A92 
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 
A1A92 non-polymer         . '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C11 H14 N4 O'   218.255 
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 A1A92 1   201  201  A1A92 LA1 A . 
D 3 CL    1   202  1    CL    CL  A . 
E 4 HOH   1   1301 1301 HOH   HOH A . 
E 4 HOH   2   1302 292  HOH   HOH A . 
E 4 HOH   3   1303 109  HOH   HOH A . 
E 4 HOH   4   1304 209  HOH   HOH A . 
E 4 HOH   5   1305 625  HOH   HOH A . 
E 4 HOH   6   1306 964  HOH   HOH A . 
E 4 HOH   7   1307 132  HOH   HOH A . 
E 4 HOH   8   1308 196  HOH   HOH A . 
E 4 HOH   9   1309 1295 HOH   HOH A . 
E 4 HOH   10  1310 18   HOH   HOH A . 
E 4 HOH   11  1311 661  HOH   HOH A . 
E 4 HOH   12  1312 26   HOH   HOH A . 
E 4 HOH   13  1313 1283 HOH   HOH A . 
E 4 HOH   14  1314 136  HOH   HOH A . 
E 4 HOH   15  1315 192  HOH   HOH A . 
E 4 HOH   16  1316 409  HOH   HOH A . 
E 4 HOH   17  1317 153  HOH   HOH A . 
E 4 HOH   18  1318 247  HOH   HOH A . 
E 4 HOH   19  1319 124  HOH   HOH A . 
E 4 HOH   20  1320 76   HOH   HOH A . 
E 4 HOH   21  1321 229  HOH   HOH A . 
E 4 HOH   22  1322 199  HOH   HOH A . 
E 4 HOH   23  1323 236  HOH   HOH A . 
E 4 HOH   24  1324 9    HOH   HOH A . 
E 4 HOH   25  1325 1300 HOH   HOH A . 
E 4 HOH   26  1326 140  HOH   HOH A . 
E 4 HOH   27  1327 26   HOH   HOH A . 
E 4 HOH   28  1328 151  HOH   HOH A . 
E 4 HOH   29  1329 164  HOH   HOH A . 
E 4 HOH   30  1330 36   HOH   HOH A . 
E 4 HOH   31  1331 225  HOH   HOH A . 
E 4 HOH   32  1332 1    HOH   HOH A . 
E 4 HOH   33  1333 630  HOH   HOH A . 
E 4 HOH   34  1334 337  HOH   HOH A . 
E 4 HOH   35  1335 461  HOH   HOH A . 
E 4 HOH   36  1336 17   HOH   HOH A . 
E 4 HOH   37  1337 165  HOH   HOH A . 
E 4 HOH   38  1338 42   HOH   HOH A . 
E 4 HOH   39  1339 93   HOH   HOH A . 
E 4 HOH   40  1340 381  HOH   HOH A . 
E 4 HOH   41  1341 320  HOH   HOH A . 
E 4 HOH   42  1342 396  HOH   HOH A . 
E 4 HOH   43  1343 241  HOH   HOH A . 
E 4 HOH   44  1344 7    HOH   HOH A . 
E 4 HOH   45  1345 162  HOH   HOH A . 
E 4 HOH   46  1346 1275 HOH   HOH A . 
E 4 HOH   47  1347 1290 HOH   HOH A . 
E 4 HOH   48  1348 57   HOH   HOH A . 
E 4 HOH   49  1349 102  HOH   HOH A . 
E 4 HOH   50  1350 105  HOH   HOH A . 
E 4 HOH   51  1351 25   HOH   HOH A . 
E 4 HOH   52  1352 469  HOH   HOH A . 
E 4 HOH   53  1353 169  HOH   HOH A . 
E 4 HOH   54  1354 1309 HOH   HOH A . 
E 4 HOH   55  1355 66   HOH   HOH A . 
E 4 HOH   56  1356 92   HOH   HOH A . 
E 4 HOH   57  1357 2    HOH   HOH A . 
E 4 HOH   58  1358 493  HOH   HOH A . 
E 4 HOH   59  1359 68   HOH   HOH A . 
E 4 HOH   60  1360 354  HOH   HOH A . 
E 4 HOH   61  1361 33   HOH   HOH A . 
E 4 HOH   62  1362 5    HOH   HOH A . 
E 4 HOH   63  1363 159  HOH   HOH A . 
E 4 HOH   64  1364 19   HOH   HOH A . 
E 4 HOH   65  1365 139  HOH   HOH A . 
E 4 HOH   66  1366 45   HOH   HOH A . 
E 4 HOH   67  1367 56   HOH   HOH A . 
E 4 HOH   68  1368 1094 HOH   HOH A . 
E 4 HOH   69  1369 393  HOH   HOH A . 
E 4 HOH   70  1370 21   HOH   HOH A . 
E 4 HOH   71  1371 39   HOH   HOH A . 
E 4 HOH   72  1372 10   HOH   HOH A . 
E 4 HOH   73  1373 46   HOH   HOH A . 
E 4 HOH   74  1374 186  HOH   HOH A . 
E 4 HOH   75  1375 218  HOH   HOH A . 
E 4 HOH   76  1376 662  HOH   HOH A . 
E 4 HOH   77  1377 86   HOH   HOH A . 
E 4 HOH   78  1378 134  HOH   HOH A . 
E 4 HOH   79  1379 49   HOH   HOH A . 
E 4 HOH   80  1380 138  HOH   HOH A . 
E 4 HOH   81  1381 18   HOH   HOH A . 
E 4 HOH   82  1382 405  HOH   HOH A . 
E 4 HOH   83  1383 78   HOH   HOH A . 
E 4 HOH   84  1384 366  HOH   HOH A . 
E 4 HOH   85  1385 939  HOH   HOH A . 
E 4 HOH   86  1386 12   HOH   HOH A . 
E 4 HOH   87  1387 11   HOH   HOH A . 
E 4 HOH   88  1388 24   HOH   HOH A . 
E 4 HOH   89  1389 122  HOH   HOH A . 
E 4 HOH   90  1390 5    HOH   HOH A . 
E 4 HOH   91  1391 155  HOH   HOH A . 
E 4 HOH   92  1392 85   HOH   HOH A . 
E 4 HOH   93  1393 148  HOH   HOH A . 
E 4 HOH   94  1394 83   HOH   HOH A . 
E 4 HOH   95  1395 35   HOH   HOH A . 
E 4 HOH   96  1396 27   HOH   HOH A . 
E 4 HOH   97  1397 58   HOH   HOH A . 
E 4 HOH   98  1398 1308 HOH   HOH A . 
E 4 HOH   99  1399 154  HOH   HOH A . 
E 4 HOH   100 1400 212  HOH   HOH A . 
E 4 HOH   101 1401 195  HOH   HOH A . 
E 4 HOH   102 1402 74   HOH   HOH A . 
E 4 HOH   103 1403 1310 HOH   HOH A . 
E 4 HOH   104 1404 121  HOH   HOH A . 
E 4 HOH   105 1405 582  HOH   HOH A . 
E 4 HOH   106 1406 1296 HOH   HOH A . 
E 4 HOH   107 1407 6    HOH   HOH A . 
E 4 HOH   108 1408 4    HOH   HOH A . 
E 4 HOH   109 1409 296  HOH   HOH A . 
E 4 HOH   110 1410 1286 HOH   HOH A . 
E 4 HOH   111 1411 67   HOH   HOH A . 
E 4 HOH   112 1412 116  HOH   HOH A . 
E 4 HOH   113 1413 351  HOH   HOH A . 
E 4 HOH   114 1414 12   HOH   HOH A . 
E 4 HOH   115 1415 34   HOH   HOH A . 
E 4 HOH   116 1416 3    HOH   HOH A . 
E 4 HOH   117 1417 51   HOH   HOH A . 
E 4 HOH   118 1418 123  HOH   HOH A . 
E 4 HOH   119 1419 303  HOH   HOH A . 
E 4 HOH   120 1420 2    HOH   HOH A . 
E 4 HOH   121 1421 281  HOH   HOH A . 
E 4 HOH   122 1422 53   HOH   HOH A . 
E 4 HOH   123 1423 278  HOH   HOH A . 
E 4 HOH   124 1424 156  HOH   HOH A . 
E 4 HOH   125 1425 1315 HOH   HOH A . 
E 4 HOH   126 1426 1289 HOH   HOH A . 
E 4 HOH   127 1427 25   HOH   HOH A . 
E 4 HOH   128 1428 1068 HOH   HOH A . 
E 4 HOH   129 1429 1313 HOH   HOH A . 
E 4 HOH   130 1430 70   HOH   HOH A . 
E 4 HOH   131 1431 125  HOH   HOH A . 
E 4 HOH   132 1432 397  HOH   HOH A . 
E 4 HOH   133 1433 96   HOH   HOH A . 
E 4 HOH   134 1434 21   HOH   HOH A . 
E 4 HOH   135 1435 7    HOH   HOH A . 
E 4 HOH   136 1436 8    HOH   HOH A . 
E 4 HOH   137 1437 95   HOH   HOH A . 
E 4 HOH   138 1438 333  HOH   HOH A . 
E 4 HOH   139 1439 4    HOH   HOH A . 
E 4 HOH   140 1440 27   HOH   HOH A . 
E 4 HOH   141 1441 115  HOH   HOH A . 
E 4 HOH   142 1442 71   HOH   HOH A . 
E 4 HOH   143 1443 16   HOH   HOH A . 
E 4 HOH   144 1444 40   HOH   HOH A . 
E 4 HOH   145 1445 1279 HOH   HOH A . 
E 4 HOH   146 1446 1222 HOH   HOH A . 
E 4 HOH   147 1447 1189 HOH   HOH A . 
E 4 HOH   148 1448 80   HOH   HOH A . 
E 4 HOH   149 1449 188  HOH   HOH A . 
E 4 HOH   150 1450 944  HOH   HOH A . 
E 4 HOH   151 1451 73   HOH   HOH A . 
E 4 HOH   152 1452 94   HOH   HOH A . 
E 4 HOH   153 1453 952  HOH   HOH A . 
E 4 HOH   154 1454 1238 HOH   HOH A . 
E 4 HOH   155 1455 97   HOH   HOH A . 
E 4 HOH   156 1456 1134 HOH   HOH A . 
E 4 HOH   157 1457 576  HOH   HOH A . 
E 4 HOH   158 1458 104  HOH   HOH A . 
E 4 HOH   159 1459 330  HOH   HOH A . 
E 4 HOH   160 1460 79   HOH   HOH A . 
E 4 HOH   161 1461 13   HOH   HOH A . 
E 4 HOH   162 1462 1119 HOH   HOH A . 
E 4 HOH   163 1463 509  HOH   HOH A . 
E 4 HOH   164 1464 163  HOH   HOH A . 
E 4 HOH   165 1465 726  HOH   HOH A . 
E 4 HOH   166 1466 107  HOH   HOH A . 
E 4 HOH   167 1467 756  HOH   HOH A . 
E 4 HOH   168 1468 408  HOH   HOH A . 
E 4 HOH   169 1469 361  HOH   HOH A . 
E 4 HOH   170 1470 319  HOH   HOH A . 
E 4 HOH   171 1471 6    HOH   HOH A . 
E 4 HOH   172 1472 14   HOH   HOH A . 
E 4 HOH   173 1473 1276 HOH   HOH A . 
E 4 HOH   174 1474 801  HOH   HOH A . 
E 4 HOH   175 1475 126  HOH   HOH A . 
E 4 HOH   176 1476 556  HOH   HOH A . 
E 4 HOH   177 1477 280  HOH   HOH A . 
E 4 HOH   178 1478 63   HOH   HOH A . 
E 4 HOH   179 1479 1307 HOH   HOH A . 
E 4 HOH   180 1480 250  HOH   HOH A . 
E 4 HOH   181 1481 135  HOH   HOH A . 
E 4 HOH   182 1482 15   HOH   HOH A . 
E 4 HOH   183 1483 1306 HOH   HOH A . 
E 4 HOH   184 1484 342  HOH   HOH A . 
E 4 HOH   185 1485 370  HOH   HOH A . 
E 4 HOH   186 1486 1287 HOH   HOH A . 
E 4 HOH   187 1487 674  HOH   HOH A . 
E 4 HOH   188 1488 202  HOH   HOH A . 
E 4 HOH   189 1489 19   HOH   HOH A . 
E 4 HOH   190 1490 521  HOH   HOH A . 
E 4 HOH   191 1491 919  HOH   HOH A . 
E 4 HOH   192 1492 20   HOH   HOH A . 
E 4 HOH   193 1493 695  HOH   HOH A . 
E 4 HOH   194 1494 224  HOH   HOH A . 
E 4 HOH   195 1495 267  HOH   HOH A . 
E 4 HOH   196 1496 318  HOH   HOH A . 
E 4 HOH   197 1497 309  HOH   HOH A . 
E 4 HOH   198 1498 331  HOH   HOH A . 
E 4 HOH   199 1499 1299 HOH   HOH A . 
E 4 HOH   200 1500 315  HOH   HOH A . 
E 4 HOH   201 1501 1314 HOH   HOH A . 
E 4 HOH   202 1502 711  HOH   HOH A . 
E 4 HOH   203 1503 263  HOH   HOH A . 
E 4 HOH   204 1504 152  HOH   HOH A . 
E 4 HOH   205 1505 805  HOH   HOH A . 
E 4 HOH   206 1506 941  HOH   HOH A . 
E 4 HOH   207 1507 326  HOH   HOH A . 
E 4 HOH   208 1508 981  HOH   HOH A . 
E 4 HOH   209 1509 208  HOH   HOH A . 
E 4 HOH   210 1510 16   HOH   HOH A . 
E 4 HOH   211 1511 350  HOH   HOH A . 
E 4 HOH   212 1512 1071 HOH   HOH A . 
E 4 HOH   213 1513 180  HOH   HOH A . 
E 4 HOH   214 1514 371  HOH   HOH A . 
E 4 HOH   215 1515 356  HOH   HOH A . 
E 4 HOH   216 1516 363  HOH   HOH A . 
E 4 HOH   217 1517 24   HOH   HOH A . 
E 4 HOH   218 1518 313  HOH   HOH A . 
E 4 HOH   219 1519 3    HOH   HOH A . 
E 4 HOH   220 1520 17   HOH   HOH A . 
E 4 HOH   221 1521 22   HOH   HOH A . 
E 4 HOH   222 1522 28   HOH   HOH A . 
E 4 HOH   223 1523 29   HOH   HOH A . 
E 4 HOH   224 1524 30   HOH   HOH A . 
E 4 HOH   225 1525 185  HOH   HOH A . 
E 4 HOH   226 1526 1284 HOH   HOH A . 
E 4 HOH   227 1527 429  HOH   HOH A . 
E 4 HOH   228 1528 772  HOH   HOH A . 
E 4 HOH   229 1529 376  HOH   HOH A . 
E 4 HOH   230 1530 346  HOH   HOH A . 
E 4 HOH   231 1531 1074 HOH   HOH A . 
E 4 HOH   232 1532 1292 HOH   HOH A . 
E 4 HOH   233 1533 23   HOH   HOH A . 
E 4 HOH   234 1534 1078 HOH   HOH A . 
F 4 HOH   1   201  64   HOH   HOH B . 
F 4 HOH   2   202  398  HOH   HOH B . 
F 4 HOH   3   203  240  HOH   HOH B . 
F 4 HOH   4   204  364  HOH   HOH B . 
F 4 HOH   5   205  900  HOH   HOH B . 
F 4 HOH   6   206  531  HOH   HOH B . 
F 4 HOH   7   207  549  HOH   HOH B . 
F 4 HOH   8   208  1249 HOH   HOH B . 
F 4 HOH   9   209  358  HOH   HOH B . 
F 4 HOH   10  210  654  HOH   HOH B . 
F 4 HOH   11  211  758  HOH   HOH B . 
F 4 HOH   12  212  120  HOH   HOH B . 
F 4 HOH   13  213  264  HOH   HOH B . 
F 4 HOH   14  214  444  HOH   HOH B . 
F 4 HOH   15  215  166  HOH   HOH B . 
F 4 HOH   16  216  232  HOH   HOH B . 
F 4 HOH   17  217  743  HOH   HOH B . 
F 4 HOH   18  218  282  HOH   HOH B . 
F 4 HOH   19  219  332  HOH   HOH B . 
F 4 HOH   20  220  50   HOH   HOH B . 
F 4 HOH   21  221  276  HOH   HOH B . 
F 4 HOH   22  222  452  HOH   HOH B . 
F 4 HOH   23  223  15   HOH   HOH B . 
F 4 HOH   24  224  343  HOH   HOH B . 
F 4 HOH   25  225  353  HOH   HOH B . 
F 4 HOH   26  226  54   HOH   HOH B . 
F 4 HOH   27  227  81   HOH   HOH B . 
F 4 HOH   28  228  131  HOH   HOH B . 
F 4 HOH   29  229  75   HOH   HOH B . 
F 4 HOH   30  230  1312 HOH   HOH B . 
F 4 HOH   31  231  325  HOH   HOH B . 
F 4 HOH   32  232  82   HOH   HOH B . 
F 4 HOH   33  233  127  HOH   HOH B . 
F 4 HOH   34  234  110  HOH   HOH B . 
F 4 HOH   35  235  60   HOH   HOH B . 
F 4 HOH   36  236  128  HOH   HOH B . 
F 4 HOH   37  237  181  HOH   HOH B . 
F 4 HOH   38  238  205  HOH   HOH B . 
F 4 HOH   39  239  72   HOH   HOH B . 
F 4 HOH   40  240  133  HOH   HOH B . 
F 4 HOH   41  241  723  HOH   HOH B . 
F 4 HOH   42  242  172  HOH   HOH B . 
F 4 HOH   43  243  1    HOH   HOH B . 
F 4 HOH   44  244  52   HOH   HOH B . 
F 4 HOH   45  245  9    HOH   HOH B . 
F 4 HOH   46  246  129  HOH   HOH B . 
F 4 HOH   47  247  41   HOH   HOH B . 
F 4 HOH   48  248  30   HOH   HOH B . 
F 4 HOH   49  249  69   HOH   HOH B . 
F 4 HOH   50  250  252  HOH   HOH B . 
F 4 HOH   51  251  272  HOH   HOH B . 
F 4 HOH   52  252  31   HOH   HOH B . 
F 4 HOH   53  253  300  HOH   HOH B . 
F 4 HOH   54  254  14   HOH   HOH B . 
F 4 HOH   55  255  103  HOH   HOH B . 
F 4 HOH   56  256  150  HOH   HOH B . 
F 4 HOH   57  257  1278 HOH   HOH B . 
F 4 HOH   58  258  391  HOH   HOH B . 
F 4 HOH   59  259  62   HOH   HOH B . 
F 4 HOH   60  260  1140 HOH   HOH B . 
F 4 HOH   61  261  61   HOH   HOH B . 
F 4 HOH   62  262  302  HOH   HOH B . 
F 4 HOH   63  263  47   HOH   HOH B . 
F 4 HOH   64  264  271  HOH   HOH B . 
F 4 HOH   65  265  20   HOH   HOH B . 
F 4 HOH   66  266  144  HOH   HOH B . 
F 4 HOH   67  267  10   HOH   HOH B . 
F 4 HOH   68  268  59   HOH   HOH B . 
F 4 HOH   69  269  231  HOH   HOH B . 
F 4 HOH   70  270  143  HOH   HOH B . 
F 4 HOH   71  271  114  HOH   HOH B . 
F 4 HOH   72  272  221  HOH   HOH B . 
F 4 HOH   73  273  117  HOH   HOH B . 
F 4 HOH   74  274  243  HOH   HOH B . 
F 4 HOH   75  275  84   HOH   HOH B . 
F 4 HOH   76  276  1277 HOH   HOH B . 
F 4 HOH   77  277  175  HOH   HOH B . 
F 4 HOH   78  278  11   HOH   HOH B . 
F 4 HOH   79  279  1305 HOH   HOH B . 
F 4 HOH   80  280  287  HOH   HOH B . 
F 4 HOH   81  281  88   HOH   HOH B . 
F 4 HOH   82  282  347  HOH   HOH B . 
F 4 HOH   83  283  77   HOH   HOH B . 
F 4 HOH   84  284  147  HOH   HOH B . 
F 4 HOH   85  285  1285 HOH   HOH B . 
F 4 HOH   86  286  22   HOH   HOH B . 
F 4 HOH   87  287  137  HOH   HOH B . 
F 4 HOH   88  288  242  HOH   HOH B . 
F 4 HOH   89  289  43   HOH   HOH B . 
F 4 HOH   90  290  1106 HOH   HOH B . 
F 4 HOH   91  291  387  HOH   HOH B . 
F 4 HOH   92  292  89   HOH   HOH B . 
F 4 HOH   93  293  235  HOH   HOH B . 
F 4 HOH   94  294  1066 HOH   HOH B . 
F 4 HOH   95  295  106  HOH   HOH B . 
F 4 HOH   96  296  13   HOH   HOH B . 
F 4 HOH   97  297  341  HOH   HOH B . 
F 4 HOH   98  298  416  HOH   HOH B . 
F 4 HOH   99  299  99   HOH   HOH B . 
F 4 HOH   100 300  316  HOH   HOH B . 
F 4 HOH   101 301  299  HOH   HOH B . 
F 4 HOH   102 302  216  HOH   HOH B . 
F 4 HOH   103 303  160  HOH   HOH B . 
F 4 HOH   104 304  445  HOH   HOH B . 
F 4 HOH   105 305  38   HOH   HOH B . 
F 4 HOH   106 306  297  HOH   HOH B . 
F 4 HOH   107 307  1126 HOH   HOH B . 
F 4 HOH   108 308  112  HOH   HOH B . 
F 4 HOH   109 309  101  HOH   HOH B . 
F 4 HOH   110 310  142  HOH   HOH B . 
F 4 HOH   111 311  170  HOH   HOH B . 
F 4 HOH   112 312  48   HOH   HOH B . 
F 4 HOH   113 313  37   HOH   HOH B . 
F 4 HOH   114 314  32   HOH   HOH B . 
F 4 HOH   115 315  311  HOH   HOH B . 
F 4 HOH   116 316  91   HOH   HOH B . 
F 4 HOH   117 317  118  HOH   HOH B . 
F 4 HOH   118 318  23   HOH   HOH B . 
F 4 HOH   119 319  220  HOH   HOH B . 
F 4 HOH   120 320  635  HOH   HOH B . 
F 4 HOH   121 321  215  HOH   HOH B . 
F 4 HOH   122 322  1274 HOH   HOH B . 
F 4 HOH   123 323  177  HOH   HOH B . 
F 4 HOH   124 324  44   HOH   HOH B . 
F 4 HOH   125 325  28   HOH   HOH B . 
F 4 HOH   126 326  197  HOH   HOH B . 
F 4 HOH   127 327  704  HOH   HOH B . 
F 4 HOH   128 328  55   HOH   HOH B . 
F 4 HOH   129 329  182  HOH   HOH B . 
F 4 HOH   130 330  100  HOH   HOH B . 
F 4 HOH   131 331  141  HOH   HOH B . 
F 4 HOH   132 332  717  HOH   HOH B . 
F 4 HOH   133 333  29   HOH   HOH B . 
F 4 HOH   134 334  1291 HOH   HOH B . 
F 4 HOH   135 335  334  HOH   HOH B . 
F 4 HOH   136 336  1294 HOH   HOH B . 
F 4 HOH   137 337  339  HOH   HOH B . 
F 4 HOH   138 338  98   HOH   HOH B . 
F 4 HOH   139 339  161  HOH   HOH B . 
F 4 HOH   140 340  65   HOH   HOH B . 
F 4 HOH   141 341  207  HOH   HOH B . 
F 4 HOH   142 342  362  HOH   HOH B . 
F 4 HOH   143 343  1293 HOH   HOH B . 
F 4 HOH   144 344  234  HOH   HOH B . 
F 4 HOH   145 345  619  HOH   HOH B . 
F 4 HOH   146 346  463  HOH   HOH B . 
F 4 HOH   147 347  90   HOH   HOH B . 
F 4 HOH   148 348  178  HOH   HOH B . 
F 4 HOH   149 349  1280 HOH   HOH B . 
F 4 HOH   150 350  203  HOH   HOH B . 
F 4 HOH   151 351  191  HOH   HOH B . 
F 4 HOH   152 352  1304 HOH   HOH B . 
F 4 HOH   153 353  304  HOH   HOH B . 
F 4 HOH   154 354  335  HOH   HOH B . 
F 4 HOH   155 355  960  HOH   HOH B . 
F 4 HOH   156 356  1046 HOH   HOH B . 
F 4 HOH   157 357  623  HOH   HOH B . 
F 4 HOH   158 358  87   HOH   HOH B . 
F 4 HOH   159 359  541  HOH   HOH B . 
F 4 HOH   160 360  290  HOH   HOH B . 
F 4 HOH   161 361  389  HOH   HOH B . 
F 4 HOH   162 362  1077 HOH   HOH B . 
F 4 HOH   163 363  718  HOH   HOH B . 
F 4 HOH   164 364  479  HOH   HOH B . 
F 4 HOH   165 365  1072 HOH   HOH B . 
F 4 HOH   166 366  283  HOH   HOH B . 
F 4 HOH   167 367  898  HOH   HOH B . 
F 4 HOH   168 368  373  HOH   HOH B . 
F 4 HOH   169 369  615  HOH   HOH B . 
F 4 HOH   170 370  1316 HOH   HOH B . 
F 4 HOH   171 371  667  HOH   HOH B . 
F 4 HOH   172 372  291  HOH   HOH B . 
F 4 HOH   173 373  310  HOH   HOH B . 
F 4 HOH   174 374  340  HOH   HOH B . 
F 4 HOH   175 375  190  HOH   HOH B . 
F 4 HOH   176 376  418  HOH   HOH B . 
F 4 HOH   177 377  1303 HOH   HOH B . 
F 4 HOH   178 378  431  HOH   HOH B . 
F 4 HOH   179 379  1173 HOH   HOH B . 
F 4 HOH   180 380  149  HOH   HOH B . 
F 4 HOH   181 381  183  HOH   HOH B . 
F 4 HOH   182 382  1000 HOH   HOH B . 
F 4 HOH   183 383  1163 HOH   HOH B . 
F 4 HOH   184 384  1311 HOH   HOH B . 
F 4 HOH   185 385  176  HOH   HOH B . 
F 4 HOH   186 386  424  HOH   HOH B . 
F 4 HOH   187 387  491  HOH   HOH B . 
F 4 HOH   188 388  1298 HOH   HOH B . 
F 4 HOH   189 389  265  HOH   HOH B . 
F 4 HOH   190 390  470  HOH   HOH B . 
F 4 HOH   191 391  248  HOH   HOH B . 
F 4 HOH   192 392  184  HOH   HOH B . 
F 4 HOH   193 393  360  HOH   HOH B . 
F 4 HOH   194 394  410  HOH   HOH B . 
F 4 HOH   195 395  355  HOH   HOH B . 
F 4 HOH   196 396  274  HOH   HOH B . 
F 4 HOH   197 397  566  HOH   HOH B . 
F 4 HOH   198 398  314  HOH   HOH B . 
F 4 HOH   199 399  157  HOH   HOH B . 
F 4 HOH   200 400  792  HOH   HOH B . 
F 4 HOH   201 401  321  HOH   HOH B . 
F 4 HOH   202 402  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           7HEN 
_cell.length_a           88.829 
_cell.length_b           88.829 
_cell.length_c           39.575 
_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                         7HEN 
_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          7HEN 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.83 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_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                     7HEN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            0.980 
_reflns.number_obs                   175068 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.100 
_reflns.pdbx_Rmerge_I_obs            0.042 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.100 
_reflns.B_iso_Wilson_estimate        11.390 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.046 
_reflns.pdbx_Rpim_I_all              0.018 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1080783 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.980 1.000  ? 26616 7675 ? 1.297 ? ? ? 3.500 ? 0.700  ? ? ? ? ? ? 88.400 1.519 0.769 0.445 
1 2 5.370 44.410 ? 8052  1166 ? 0.023 ? ? ? 6.900 ? 60.500 ? ? ? ? ? ? 99.700 0.025 0.010 0.999 
# 
_refine.entry_id                                 7HEN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9800 
_refine.ls_d_res_low                             36.1500 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.0200 
_refine.ls_number_reflns_obs                     174945 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1441 
_refine.ls_R_factor_R_work                       0.1436 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1552 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  8419 
_refine.ls_number_reflns_R_work                  166526 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.0432 
_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                            0.1400 
_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                                70.870 
_refine.B_iso_min                                5.150 
_refine.pdbx_overall_phase_error                 17.3200 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9800 
_refine_hist.d_res_low                        36.1500 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.number_atoms_solvent             436 
_refine_hist.number_atoms_total               3009 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           13.84 
_refine_hist.pdbx_B_iso_mean_solvent          29.77 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9800 0.9900  30 86.0000  4791 . 0.4749 0.4285 . 235 0.0000 5026 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 93.0000  5164 . 0.4062 0.4004 . 252 0.0000 5416 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 96.0000  5351 . 0.3601 0.3489 . 270 0.0000 5621 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 98.0000  5482 . 0.3076 0.3312 . 248 0.0000 5730 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5565 . 0.2796 0.2653 . 306 0.0000 5871 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5552 . 0.2211 0.2219 . 291 0.0000 5843 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5576 . 0.1926 0.2147 . 323 0.0000 5899 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5552 . 0.1700 0.1956 . 255 0.0000 5807 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 5608 . 0.1539 0.1662 . 285 0.0000 5893 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5572 . 0.1454 0.1630 . 296 0.0000 5868 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5608 . 0.1421 0.1561 . 239 0.0000 5847 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5598 . 0.1348 0.1609 . 277 0.0000 5875 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5570 . 0.1354 0.1583 . 281 0.0000 5851 . 'X-RAY DIFFRACTION' 
1.1800 1.2100  30 100.0000 5548 . 0.1365 0.1725 . 319 0.0000 5867 . 'X-RAY DIFFRACTION' 
1.2100 1.2400  30 100.0000 5640 . 0.1260 0.1482 . 244 0.0000 5884 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 5574 . 0.1236 0.1405 . 277 0.0000 5851 . 'X-RAY DIFFRACTION' 
1.2600 1.3000  30 100.0000 5575 . 0.1223 0.1435 . 286 0.0000 5861 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5557 . 0.1196 0.1311 . 305 0.0000 5862 . 'X-RAY DIFFRACTION' 
1.3300 1.3700  30 100.0000 5635 . 0.1182 0.1436 . 296 0.0000 5931 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5614 . 0.1156 0.1466 . 254 0.0000 5868 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5581 . 0.1205 0.1271 . 300 0.0000 5881 . 'X-RAY DIFFRACTION' 
1.4600 1.5200  30 100.0000 5607 . 0.1180 0.1362 . 263 0.0000 5870 . 'X-RAY DIFFRACTION' 
1.5200 1.5900  30 100.0000 5581 . 0.1159 0.1206 . 305 0.0000 5886 . 'X-RAY DIFFRACTION' 
1.5900 1.6800  30 100.0000 5612 . 0.1190 0.1308 . 280 0.0000 5892 . 'X-RAY DIFFRACTION' 
1.6800 1.7800  30 100.0000 5640 . 0.1261 0.1446 . 260 0.0000 5900 . 'X-RAY DIFFRACTION' 
1.7800 1.9200  30 100.0000 5606 . 0.1328 0.1376 . 308 0.0000 5914 . 'X-RAY DIFFRACTION' 
1.9200 2.1100  30 100.0000 5643 . 0.1369 0.1375 . 282 0.0000 5925 . 'X-RAY DIFFRACTION' 
2.1100 2.4200  30 100.0000 5624 . 0.1377 0.1395 . 311 0.0000 5935 . 'X-RAY DIFFRACTION' 
2.4200 3.0500  30 100.0000 5693 . 0.1474 0.1632 . 290 0.0000 5983 . 'X-RAY DIFFRACTION' 
3.0500 36.1500 30 100.0000 5807 . 0.1482 0.1627 . 281 0.0000 6088 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEN 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003685' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEN 
_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 7HEN A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEN 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 7HEN SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEN MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEN SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEN MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.30  -132.50 
2 1 SER A 128 ? B 72.42  -6.48   
3 1 ALA A 129 ? B -87.63 -152.97 
4 1 HIS B 86  ? ? 57.00  -128.20 
# 
_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 1530 ? 5.83 . 
2 1 O ? A HOH 1531 ? 5.93 . 
3 1 O ? A HOH 1532 ? 6.01 . 
4 1 O B A HOH 1533 ? 6.15 . 
5 1 O ? A HOH 1534 ? 7.51 . 
6 1 O ? B HOH 402  ? 6.42 . 
# 
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 
A1A92 N2   N  Y N 1   
A1A92 C3   C  N N 2   
A1A92 C6   C  Y N 3   
A1A92 C9   C  Y N 4   
A1A92 C1   C  N N 5   
A1A92 C10  C  Y N 6   
A1A92 C11  C  Y N 7   
A1A92 C2   C  N S 8   
A1A92 C4   C  N N 9   
A1A92 C5   C  N N 10  
A1A92 C7   C  Y N 11  
A1A92 C8   C  Y N 12  
A1A92 N1   N  N N 13  
A1A92 N3   N  Y N 14  
A1A92 N4   N  Y N 15  
A1A92 O1   O  N N 16  
A1A92 H5   H  N N 17  
A1A92 H6   H  N N 18  
A1A92 H3   H  N N 19  
A1A92 H4   H  N N 20  
A1A92 H12  H  N N 21  
A1A92 H13  H  N N 22  
A1A92 H1   H  N N 23  
A1A92 H7   H  N N 24  
A1A92 H8   H  N N 25  
A1A92 H10  H  N N 26  
A1A92 H9   H  N N 27  
A1A92 H11  H  N N 28  
A1A92 H14  H  N N 29  
A1A92 H2   H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CL    CL   CL N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
GLN   N    N  N N 119 
GLN   CA   C  N S 120 
GLN   C    C  N N 121 
GLN   O    O  N N 122 
GLN   CB   C  N N 123 
GLN   CG   C  N N 124 
GLN   CD   C  N N 125 
GLN   OE1  O  N N 126 
GLN   NE2  N  N N 127 
GLN   OXT  O  N N 128 
GLN   H    H  N N 129 
GLN   H2   H  N N 130 
GLN   HA   H  N N 131 
GLN   HB2  H  N N 132 
GLN   HB3  H  N N 133 
GLN   HG2  H  N N 134 
GLN   HG3  H  N N 135 
GLN   HE21 H  N N 136 
GLN   HE22 H  N N 137 
GLN   HXT  H  N N 138 
GLU   N    N  N N 139 
GLU   CA   C  N S 140 
GLU   C    C  N N 141 
GLU   O    O  N N 142 
GLU   CB   C  N N 143 
GLU   CG   C  N N 144 
GLU   CD   C  N N 145 
GLU   OE1  O  N N 146 
GLU   OE2  O  N N 147 
GLU   OXT  O  N N 148 
GLU   H    H  N N 149 
GLU   H2   H  N N 150 
GLU   HA   H  N N 151 
GLU   HB2  H  N N 152 
GLU   HB3  H  N N 153 
GLU   HG2  H  N N 154 
GLU   HG3  H  N N 155 
GLU   HE2  H  N N 156 
GLU   HXT  H  N N 157 
GLY   N    N  N N 158 
GLY   CA   C  N N 159 
GLY   C    C  N N 160 
GLY   O    O  N N 161 
GLY   OXT  O  N N 162 
GLY   H    H  N N 163 
GLY   H2   H  N N 164 
GLY   HA2  H  N N 165 
GLY   HA3  H  N N 166 
GLY   HXT  H  N N 167 
HIS   N    N  N N 168 
HIS   CA   C  N S 169 
HIS   C    C  N N 170 
HIS   O    O  N N 171 
HIS   CB   C  N N 172 
HIS   CG   C  Y N 173 
HIS   ND1  N  Y N 174 
HIS   CD2  C  Y N 175 
HIS   CE1  C  Y N 176 
HIS   NE2  N  Y N 177 
HIS   OXT  O  N N 178 
HIS   H    H  N N 179 
HIS   H2   H  N N 180 
HIS   HA   H  N N 181 
HIS   HB2  H  N N 182 
HIS   HB3  H  N N 183 
HIS   HD1  H  N N 184 
HIS   HD2  H  N N 185 
HIS   HE1  H  N N 186 
HIS   HE2  H  N N 187 
HIS   HXT  H  N N 188 
HOH   O    O  N N 189 
HOH   H1   H  N N 190 
HOH   H2   H  N N 191 
ILE   N    N  N N 192 
ILE   CA   C  N S 193 
ILE   C    C  N N 194 
ILE   O    O  N N 195 
ILE   CB   C  N S 196 
ILE   CG1  C  N N 197 
ILE   CG2  C  N N 198 
ILE   CD1  C  N N 199 
ILE   OXT  O  N N 200 
ILE   H    H  N N 201 
ILE   H2   H  N N 202 
ILE   HA   H  N N 203 
ILE   HB   H  N N 204 
ILE   HG12 H  N N 205 
ILE   HG13 H  N N 206 
ILE   HG21 H  N N 207 
ILE   HG22 H  N N 208 
ILE   HG23 H  N N 209 
ILE   HD11 H  N N 210 
ILE   HD12 H  N N 211 
ILE   HD13 H  N N 212 
ILE   HXT  H  N N 213 
LEU   N    N  N N 214 
LEU   CA   C  N S 215 
LEU   C    C  N N 216 
LEU   O    O  N N 217 
LEU   CB   C  N N 218 
LEU   CG   C  N N 219 
LEU   CD1  C  N N 220 
LEU   CD2  C  N N 221 
LEU   OXT  O  N N 222 
LEU   H    H  N N 223 
LEU   H2   H  N N 224 
LEU   HA   H  N N 225 
LEU   HB2  H  N N 226 
LEU   HB3  H  N N 227 
LEU   HG   H  N N 228 
LEU   HD11 H  N N 229 
LEU   HD12 H  N N 230 
LEU   HD13 H  N N 231 
LEU   HD21 H  N N 232 
LEU   HD22 H  N N 233 
LEU   HD23 H  N N 234 
LEU   HXT  H  N N 235 
LYS   N    N  N N 236 
LYS   CA   C  N S 237 
LYS   C    C  N N 238 
LYS   O    O  N N 239 
LYS   CB   C  N N 240 
LYS   CG   C  N N 241 
LYS   CD   C  N N 242 
LYS   CE   C  N N 243 
LYS   NZ   N  N N 244 
LYS   OXT  O  N N 245 
LYS   H    H  N N 246 
LYS   H2   H  N N 247 
LYS   HA   H  N N 248 
LYS   HB2  H  N N 249 
LYS   HB3  H  N N 250 
LYS   HG2  H  N N 251 
LYS   HG3  H  N N 252 
LYS   HD2  H  N N 253 
LYS   HD3  H  N N 254 
LYS   HE2  H  N N 255 
LYS   HE3  H  N N 256 
LYS   HZ1  H  N N 257 
LYS   HZ2  H  N N 258 
LYS   HZ3  H  N N 259 
LYS   HXT  H  N N 260 
MET   N    N  N N 261 
MET   CA   C  N S 262 
MET   C    C  N N 263 
MET   O    O  N N 264 
MET   CB   C  N N 265 
MET   CG   C  N N 266 
MET   SD   S  N N 267 
MET   CE   C  N N 268 
MET   OXT  O  N N 269 
MET   H    H  N N 270 
MET   H2   H  N N 271 
MET   HA   H  N N 272 
MET   HB2  H  N N 273 
MET   HB3  H  N N 274 
MET   HG2  H  N N 275 
MET   HG3  H  N N 276 
MET   HE1  H  N N 277 
MET   HE2  H  N N 278 
MET   HE3  H  N N 279 
MET   HXT  H  N N 280 
PHE   N    N  N N 281 
PHE   CA   C  N S 282 
PHE   C    C  N N 283 
PHE   O    O  N N 284 
PHE   CB   C  N N 285 
PHE   CG   C  Y N 286 
PHE   CD1  C  Y N 287 
PHE   CD2  C  Y N 288 
PHE   CE1  C  Y N 289 
PHE   CE2  C  Y N 290 
PHE   CZ   C  Y N 291 
PHE   OXT  O  N N 292 
PHE   H    H  N N 293 
PHE   H2   H  N N 294 
PHE   HA   H  N N 295 
PHE   HB2  H  N N 296 
PHE   HB3  H  N N 297 
PHE   HD1  H  N N 298 
PHE   HD2  H  N N 299 
PHE   HE1  H  N N 300 
PHE   HE2  H  N N 301 
PHE   HZ   H  N N 302 
PHE   HXT  H  N N 303 
PRO   N    N  N N 304 
PRO   CA   C  N S 305 
PRO   C    C  N N 306 
PRO   O    O  N N 307 
PRO   CB   C  N N 308 
PRO   CG   C  N N 309 
PRO   CD   C  N N 310 
PRO   OXT  O  N N 311 
PRO   H    H  N N 312 
PRO   HA   H  N N 313 
PRO   HB2  H  N N 314 
PRO   HB3  H  N N 315 
PRO   HG2  H  N N 316 
PRO   HG3  H  N N 317 
PRO   HD2  H  N N 318 
PRO   HD3  H  N N 319 
PRO   HXT  H  N N 320 
SER   N    N  N N 321 
SER   CA   C  N S 322 
SER   C    C  N N 323 
SER   O    O  N N 324 
SER   CB   C  N N 325 
SER   OG   O  N N 326 
SER   OXT  O  N N 327 
SER   H    H  N N 328 
SER   H2   H  N N 329 
SER   HA   H  N N 330 
SER   HB2  H  N N 331 
SER   HB3  H  N N 332 
SER   HG   H  N N 333 
SER   HXT  H  N N 334 
THR   N    N  N N 335 
THR   CA   C  N S 336 
THR   C    C  N N 337 
THR   O    O  N N 338 
THR   CB   C  N R 339 
THR   OG1  O  N N 340 
THR   CG2  C  N N 341 
THR   OXT  O  N N 342 
THR   H    H  N N 343 
THR   H2   H  N N 344 
THR   HA   H  N N 345 
THR   HB   H  N N 346 
THR   HG1  H  N N 347 
THR   HG21 H  N N 348 
THR   HG22 H  N N 349 
THR   HG23 H  N N 350 
THR   HXT  H  N N 351 
TYR   N    N  N N 352 
TYR   CA   C  N S 353 
TYR   C    C  N N 354 
TYR   O    O  N N 355 
TYR   CB   C  N N 356 
TYR   CG   C  Y N 357 
TYR   CD1  C  Y N 358 
TYR   CD2  C  Y N 359 
TYR   CE1  C  Y N 360 
TYR   CE2  C  Y N 361 
TYR   CZ   C  Y N 362 
TYR   OH   O  N N 363 
TYR   OXT  O  N N 364 
TYR   H    H  N N 365 
TYR   H2   H  N N 366 
TYR   HA   H  N N 367 
TYR   HB2  H  N N 368 
TYR   HB3  H  N N 369 
TYR   HD1  H  N N 370 
TYR   HD2  H  N N 371 
TYR   HE1  H  N N 372 
TYR   HE2  H  N N 373 
TYR   HH   H  N N 374 
TYR   HXT  H  N N 375 
VAL   N    N  N N 376 
VAL   CA   C  N S 377 
VAL   C    C  N N 378 
VAL   O    O  N N 379 
VAL   CB   C  N N 380 
VAL   CG1  C  N N 381 
VAL   CG2  C  N N 382 
VAL   OXT  O  N N 383 
VAL   H    H  N N 384 
VAL   H2   H  N N 385 
VAL   HA   H  N N 386 
VAL   HB   H  N N 387 
VAL   HG11 H  N N 388 
VAL   HG12 H  N N 389 
VAL   HG13 H  N N 390 
VAL   HG21 H  N N 391 
VAL   HG22 H  N N 392 
VAL   HG23 H  N N 393 
VAL   HXT  H  N N 394 
# 
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 
A1A92 C4  C3   sing N N 1   
A1A92 C4  C5   sing N N 2   
A1A92 O1  C1   sing N N 3   
A1A92 C3  C2   sing N N 4   
A1A92 C1  C2   sing N N 5   
A1A92 C2  N1   sing N N 6   
A1A92 C5  N1   sing N N 7   
A1A92 N1  C6   sing N N 8   
A1A92 C6  N2   doub Y N 9   
A1A92 C6  C9   sing Y N 10  
A1A92 C10 C9   sing Y N 11  
A1A92 C10 C11  doub Y N 12  
A1A92 N2  C7   sing Y N 13  
A1A92 C9  C8   doub Y N 14  
A1A92 C11 N4   sing Y N 15  
A1A92 C7  N3   doub Y N 16  
A1A92 C8  N3   sing Y N 17  
A1A92 C8  N4   sing Y N 18  
A1A92 C3  H5   sing N N 19  
A1A92 C3  H6   sing N N 20  
A1A92 C1  H3   sing N N 21  
A1A92 C1  H4   sing N N 22  
A1A92 C10 H12  sing N N 23  
A1A92 C11 H13  sing N N 24  
A1A92 C2  H1   sing N N 25  
A1A92 C4  H7   sing N N 26  
A1A92 C4  H8   sing N N 27  
A1A92 C5  H10  sing N N 28  
A1A92 C5  H9   sing N N 29  
A1A92 C7  H11  sing N N 30  
A1A92 N4  H14  sing N N 31  
A1A92 O1  H2   sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TYR   N   CA   sing N N 338 
TYR   N   H    sing N N 339 
TYR   N   H2   sing N N 340 
TYR   CA  C    sing N N 341 
TYR   CA  CB   sing N N 342 
TYR   CA  HA   sing N N 343 
TYR   C   O    doub N N 344 
TYR   C   OXT  sing N N 345 
TYR   CB  CG   sing N N 346 
TYR   CB  HB2  sing N N 347 
TYR   CB  HB3  sing N N 348 
TYR   CG  CD1  doub Y N 349 
TYR   CG  CD2  sing Y N 350 
TYR   CD1 CE1  sing Y N 351 
TYR   CD1 HD1  sing N N 352 
TYR   CD2 CE2  doub Y N 353 
TYR   CD2 HD2  sing N N 354 
TYR   CE1 CZ   doub Y N 355 
TYR   CE1 HE1  sing N N 356 
TYR   CE2 CZ   sing Y N 357 
TYR   CE2 HE2  sing N N 358 
TYR   CZ  OH   sing N N 359 
TYR   OH  HH   sing N N 360 
TYR   OXT HXT  sing N N 361 
VAL   N   CA   sing N N 362 
VAL   N   H    sing N N 363 
VAL   N   H2   sing N N 364 
VAL   CA  C    sing N N 365 
VAL   CA  CB   sing N N 366 
VAL   CA  HA   sing N N 367 
VAL   C   O    doub N N 368 
VAL   C   OXT  sing N N 369 
VAL   CB  CG1  sing N N 370 
VAL   CB  CG2  sing N N 371 
VAL   CB  HB   sing N N 372 
VAL   CG1 HG11 sing N N 373 
VAL   CG1 HG12 sing N N 374 
VAL   CG1 HG13 sing N N 375 
VAL   CG2 HG21 sing N N 376 
VAL   CG2 HG22 sing N N 377 
VAL   CG2 HG23 sing N N 378 
VAL   OXT HXT  sing N N 379 
# 
_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                    7HEN 
_atom_sites.fract_transf_matrix[1][1]   0.011258 
_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]   0.011258 
_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]   0.025268 
_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   ? 19.733 -16.319 22.222  0.30 48.83 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.632 -16.176 22.384  0.70 51.66 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.754 -15.253 22.389  0.30 48.51 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.697 -15.077 22.592  0.70 51.30 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.399 -13.897 22.121  0.30 46.72 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.363 -13.748 22.253  0.70 49.30 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.498 -13.618 22.600  0.30 47.10 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.491 -13.487 22.673  0.70 49.75 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.112 -15.298 23.792  0.30 49.65 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.138 -15.082 24.031  0.70 52.57 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.084 -14.185 23.945  0.30 49.97 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.127 -13.959 24.217  0.70 52.90 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.472 -16.656 24.043  0.30 49.95 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.507 -16.429 24.347  0.70 52.91 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.045 -15.374 21.742  0.30 58.24 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.947 -15.186 21.994  0.70 61.59 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.800 -15.164 24.461  0.30 59.60 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.864 -14.937 24.658  0.70 63.11 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.571 -14.340 24.753  0.30 59.99 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.669 -14.084 25.063  0.70 63.50 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.544 -13.333 24.005  0.30 59.99 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.593 -13.108 24.217  0.70 63.50 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.495 -14.191 23.174  0.30 59.99 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.487 -13.988 23.488  0.70 63.50 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.020 -16.638 24.901  0.30 59.97 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.095 -16.387 25.224  0.70 63.52 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.834 -16.839 23.336  0.30 59.97 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.836 -16.627 23.675  0.70 63.52 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.164 -17.336 24.049  0.30 59.97 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.196 -17.112 24.338  0.70 63.52 ?  3    VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.711 -13.061 21.345  0.30 44.30 ?  4    ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.665 -12.914 21.483  0.70 46.57 ?  4    ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.147 -11.698 21.070  0.30 41.66 ?  4    ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.149 -11.586 21.127  0.70 43.58 ?  4    ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.985 -10.742 21.326  0.30 38.97 ?  4    ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 18.055 -10.557 21.389  0.70 41.07 ?  4    ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.881 -11.156 21.691  0.30 39.09 ?  4    ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.934 -10.892 21.785  0.70 41.09 ?  4    ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.709 -11.556 19.648  0.30 41.49 ?  4    ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.657 -11.527 19.679  0.70 42.89 ?  4    ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.722 -11.980 18.580  0.30 41.22 ?  4    ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.603 -11.919 18.668  0.70 42.07 ?  4    ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.570 -11.549 18.573  0.30 41.19 ?  4    ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.478 -11.419 18.697  0.70 41.89 ?  4    ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.174 -12.834 17.667  0.30 41.16 ?  4    ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.965 -12.819 17.760  0.70 41.83 ?  4    ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.970 -13.269 20.961  0.30 53.18 ?  4    ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.892 -13.102 21.151  0.70 55.90 ?  4    ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.860 -11.474 21.685  0.30 50.01 ?  4    ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.896 -11.371 21.700  0.70 52.32 ?  4    ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.939 -10.625 19.491  0.30 49.81 ?  4    ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.939 -10.619 19.482  0.70 51.49 ?  4    ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.500 -12.109 19.564  0.30 49.81 ?  4    ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.405 -12.134 19.584  0.70 51.49 ?  4    ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.657 -13.106 17.037  0.30 49.41 ?  4    ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.406 -13.076 17.160  0.70 50.22 ?  4    ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.987 -13.116 17.707  0.30 49.41 ?  4    ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.761 -13.146 17.774  0.70 50.22 ?  4    ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.240 -9.449  21.129  0.30 35.91 ?  5    SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.391 -9.291  21.153  0.70 38.26 ?  5    SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.299 -8.400  21.500  0.30 32.72 ?  5    SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.548 -8.168  21.540  0.70 35.26 ?  5    SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.425 -7.933  20.339  0.30 29.35 ?  5    SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.604 -7.704  20.435  0.70 31.70 ?  5    SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.692 -6.950  20.488  0.30 29.35 ?  5    SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.904 -6.702  20.621  0.70 31.74 ?  5    SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.043 -7.212  22.118  0.30 33.03 ?  5    SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.420 -6.999  22.014  0.70 36.30 ?  5    SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 18.993 -6.674  21.214  0.30 33.10 ?  5    SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.570 -6.857  21.198  0.70 36.67 ?  5    SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.964 -9.154  20.770  0.30 43.12 ?  5    SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.119 -9.056  20.756  0.70 45.94 ?  5    SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.708 -8.749  22.181  0.30 39.29 ?  5    SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 17.007 -8.442  22.295  0.70 42.34 ?  5    SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.400 -6.521  22.345  0.30 39.67 ?  5    SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.906 -6.179  21.965  0.70 43.58 ?  5    SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.501 -7.510  22.921  0.30 39.67 ?  5    SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.694 -7.162  22.933  0.70 43.58 ?  5    SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.394 -6.026  21.571  0.30 39.74 ?  5    SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 20.048 -6.224  21.479  0.70 44.03 ?  5    SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.478 -8.609  19.194  0.30 25.71 ?  6    PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.565 -8.392  19.297  0.70 27.38 ?  6    PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.613 -8.248  18.077  0.30 22.23 ?  6    PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.603 -8.052  18.257  0.70 23.63 ?  6    PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.166 -8.599  18.407  0.30 20.96 ?  6    PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 14.204 -8.456  18.698  0.70 24.19 ?  6    PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.865 -9.730  18.798  0.30 20.83 ?  6    PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 14.014 -9.502  19.323  0.70 25.18 ?  6    PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 16.056 -8.984  16.814  0.30 20.35 ?  6    PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.952 -8.771  16.956  0.70 20.13 ?  6    PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.329 -8.449  16.211  0.30 19.01 ?  6    PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 17.225 -8.288  16.318  0.70 17.70 ?  6    PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.321 -7.280  15.466  0.30 18.36 ?  6    PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.267 -7.071  15.659  0.70 16.64 ?  6    PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.529 -9.122  16.375  0.30 18.76 ?  6    PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.373 -9.059  16.368  0.70 17.80 ?  6    PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.486 -6.789  14.904  0.30 18.11 ?  6    PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.435 -6.627  15.070  0.70 16.71 ?  6    PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.697 -8.634  15.815  0.30 18.54 ?  6    PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.540 -8.621  15.781  0.70 17.69 ?  6    PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.674 -7.466  15.078  0.30 18.22 ?  6    PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.573 -7.404  15.131  0.70 17.17 ?  6    PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 17.002 -9.274  19.041  0.30 30.88 ?  6    PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 17.083 -9.051  19.105  0.70 32.88 ?  6    PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.671 -7.295  17.918  0.30 26.69 ?  6    PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.615 -7.098  18.105  0.70 28.38 ?  6    PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.201 -9.918  17.033  0.30 24.45 ?  6    PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 16.048 -9.720  17.142  0.70 24.18 ?  6    PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.356 -8.907  16.149  0.30 24.45 ?  6    PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 15.228 -8.633  16.325  0.70 24.18 ?  6    PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.523 -6.819  15.346  0.30 22.05 ?  6    PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.500 -6.543  15.621  0.70 19.99 ?  6    PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.551 -9.910  16.870  0.30 22.54 ?  6    PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.353 -9.880  16.809  0.70 21.39 ?  6    PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.468 -6.001  14.409  0.30 21.75 ?  6    PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.455 -5.803  14.634  0.70 20.07 ?  6    PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.498 -9.093  15.933  0.30 22.27 ?  6    PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.306 -9.145  15.825  0.70 21.26 ?  6    PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.459 -7.136  14.701  0.30 21.89 ?  6    PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.360 -7.105  14.736  0.70 20.62 ?  6    PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.266 -7.631  18.236  0.30 20.00 ?  7    SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 13.216 -7.627  18.368  0.70 23.83 ?  7    SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.893 -7.736  18.711  0.30 19.47 ?  7    SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 11.861 -7.841  18.856  0.70 24.02 ?  7    SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.904 -7.518  17.572  0.30 18.36 ?  7    SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.848 -7.554  17.756  0.70 22.23 ?  7    SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.114 -6.662  16.707  0.30 18.30 ?  7    SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 11.033 -6.642  16.946  0.70 22.73 ?  7    SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.633 -6.701  19.815  0.30 19.88 ?  7    SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.573 -6.957  20.076  0.70 26.07 ?  7    SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.268 -6.676  20.189  0.30 20.16 ?  7    SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.437 -7.431  20.777  0.70 27.46 ?  7    SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.434 -6.890  17.833  0.30 24.02 ?  7    SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 13.307 -6.941  17.861  0.70 28.63 ?  7    SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.743 -8.621  19.079  0.30 23.39 ?  7    SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.757 -8.766  19.126  0.70 28.85 ?  7    SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.172 -6.929  20.591  0.30 23.88 ?  7    SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.345 -6.972  20.669  0.70 31.31 ?  7    SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.877 -5.824  19.489  0.30 23.88 ?  7    SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 11.405 -6.049  19.779  0.70 31.31 ?  7    SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 10.146 -6.116  20.804  0.30 24.22 ?  7    SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 10.575 -8.214  21.053  0.70 32.98 ?  7    SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.829  -8.305  17.575  0.30 17.69 ?  8    GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.779  -8.347  17.731  0.70 20.94 ?  8    GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.719  -8.078  16.670  0.30 16.95 ?  8    GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.690  -8.125  16.805  0.70 19.82 ?  8    GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.920  -8.553  15.250  0.30 16.01 ?  8    GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.882  -8.689  15.418  0.70 18.27 ?  8    GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.240  -8.059  14.344  0.30 16.24 ?  8    GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 8.056  -8.413  14.539  0.70 18.62 ?  8    GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.724  -8.982  18.095  0.30 21.26 ?  8    GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.669  -9.024  18.246  0.70 25.15 ?  8    GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.929  -8.511  17.035  0.30 20.36 ?  8    GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.889  -8.529  17.163  0.70 23.81 ?  8    GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.542  -7.127  16.628  0.30 20.36 ?  8    GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.537  -7.170  16.726  0.70 23.81 ?  8    GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.835  -9.490  15.020  0.30 14.61 ?  9    TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.931  -9.473  15.186  0.70 16.44 ?  9    TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.094 -10.004 13.684  0.30 13.53 ?  9    TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.186 -10.000 13.854  0.70 15.00 ?  9    TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.222  -11.219 13.389  0.30 13.59 ?  9    TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.337  -11.233 13.575  0.70 14.65 ?  9    TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.842  -11.977 14.286  0.30 14.24 ?  9    TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 9.086  -12.062 14.458  0.70 15.91 ?  9    TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.566 -10.397 13.537  0.30 13.17 ?  9    TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.667 -10.354 13.684  0.70 14.78 ?  9    TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.515 -9.223  13.418  0.30 13.09 ?  9    TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.539 -9.137  13.461  0.70 14.49 ?  9    TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.853 -8.463  14.529  0.30 13.46 ?  9    TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.841 -8.279  14.506  0.70 15.43 ?  9    TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 13.077 -8.877  12.194  0.30 12.91 ?  9    TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 13.034 -8.829  12.197  0.70 13.76 ?  9    TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.715 -7.387  14.427  0.30 13.64 ?  9    TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.619 -7.150  14.307  0.70 15.40 ?  9    TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.941 -7.802  12.082  0.30 13.20 ?  9    TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.817 -7.706  11.987  0.70 13.87 ?  9    TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.256 -7.062  13.202  0.30 13.90 ?  9    TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 14.099 -6.870  13.043  0.70 14.73 ?  9    TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 15.115 -5.995  13.098  0.30 14.75 ?  9    TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.864 -5.754  12.822  0.70 15.37 ?  9    TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.326 -9.846  15.627  0.30 17.56 ?  9    TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.503 -9.717  15.781  0.70 19.75 ?  9    TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.893  -9.321  13.027  0.30 16.26 ?  9    TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.968  -9.316  13.197  0.70 18.02 ?  9    TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.836 -10.916 14.310  0.30 15.83 ?  9    TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.981 -10.808 14.479  0.70 17.76 ?  9    TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.659 -10.927 12.733  0.30 15.83 ?  9    TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.759 -10.934 12.910  0.70 17.76 ?  9    TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.485 -8.676  15.355  0.30 16.18 ?  9    TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.509 -8.465  15.356  0.70 18.54 ?  9    TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.866 -9.374  11.436  0.30 15.52 ?  9    TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.841 -9.390  11.480  0.70 16.53 ?  9    TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.927 -6.884  15.180  0.30 16.39 ?  9    TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.812 -6.585  15.020  0.70 18.50 ?  9    TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.309 -7.581  11.255  0.30 15.86 ?  9    TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 14.144 -7.515  11.136  0.70 16.66 ?  9    TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.214 -5.634  13.850  0.30 17.73 ?  9    TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 14.979 -5.334  13.540  0.70 18.46 ?  9    TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.907  -11.391 12.109  0.30 13.42 ?  10   LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.922  -11.352 12.320  0.70 13.69 ?  10   LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.311  -12.620 11.610  0.30 13.52 ?  10   LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.328  -12.576 11.809  0.70 13.98 ?  10   LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.428  -13.557 11.170  0.30 13.00 ?  10   LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.457  -13.500 11.370  0.70 13.01 ?  10   LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.387 -13.133 10.520  0.30 13.28 ?  10   LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.396 -13.064 10.701  0.70 13.10 ?  10   LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.404  -12.313 10.419  0.30 14.38 ?  10   LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.450  -12.224 10.608  0.70 15.11 ?  10   LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.685  -13.516 9.807   0.30 15.77 ?  10   LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.744  -13.370 9.886   0.70 17.93 ?  10   LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.549  -13.984 10.704  0.30 16.60 ?  10   LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.689  -13.984 10.776  0.70 19.67 ?  10   LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 6.179  -13.192 8.414   0.30 16.59 ?  10   LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 6.135  -12.882 8.579   0.70 19.58 ?  10   LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 9.027  -10.798 11.497  0.30 16.13 ?  10   LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.995  -10.726 11.729  0.70 16.45 ?  10   LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.787  -13.050 12.307  0.30 16.24 ?  10   LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.788  -13.000 12.499  0.70 16.80 ?  10   LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.724  -11.683 10.705  0.30 17.28 ?  10   LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.763  -11.608 10.904  0.70 18.15 ?  10   LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.944  -11.911 9.720   0.30 17.28 ?  10   LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 8.012  -11.780 9.952   0.70 18.15 ?  10   LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.314  -14.249 9.723   0.30 18.95 ?  10   LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.395  -14.057 9.675   0.70 21.54 ?  10   LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.166  -14.793 10.331  0.30 19.94 ?  10   LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 5.339  -14.780 10.348  0.70 23.63 ?  10   LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.901  -14.164 11.591  0.30 19.94 ?  10   LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 6.087  -14.212 11.630  0.70 23.63 ?  10   LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.877  -13.288 10.752  0.30 19.94 ?  10   LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 4.980  -13.338 10.908  0.70 23.63 ?  10   LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.724  -13.970 8.058   0.30 19.93 ?  10   LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 5.692  -13.628 8.146   0.70 23.52 ?  10   LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.565  -12.444 8.470   0.30 19.93 ?  10   LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.494  -12.183 8.775   0.70 23.52 ?  10   LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.934  -12.961 7.852   0.30 19.93 ?  10   LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 6.842  -12.540 8.013   0.70 23.52 ?  10   LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.292  -14.834 11.516  0.30 12.50 ?  11   LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.374  -14.768 11.755  0.70 13.49 ?  11   LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.336 -15.821 11.269  0.30 12.20 ?  11   LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.353 -15.758 11.334  0.70 13.55 ?  11   LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 10.044 -16.510 9.941   0.30 11.63 ?  11   LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.961  -16.276 9.956   0.70 13.06 ?  11   LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 9.109  -17.307 9.845   0.30 11.35 ?  11   LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.831  -16.733 9.764   0.70 14.23 ?  11   LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.380 -16.826 12.418  0.30 12.24 ?  11   LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.369 -16.902 12.354  0.70 13.38 ?  11   LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.351 -17.972 12.207  0.30 12.38 ?  11   LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.468 -17.950 12.190  0.70 13.34 ?  11   LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.439 -18.855 13.438  0.30 12.90 ?  11   LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.565 -18.813 13.455  0.70 13.68 ?  11   LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.418 -20.001 13.231  0.30 13.03 ?  11   LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.609 -19.927 13.350  0.70 13.66 ?  11   LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.789 -19.511 12.919  0.30 13.17 ?  11   LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.973 -19.384 13.144  0.70 13.74 ?  11   LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.584  -15.161 11.892  0.30 15.03 ?  11   LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.745  -15.080 12.261  0.70 16.21 ?  11   LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 11.193 -15.377 11.208  0.30 14.66 ?  11   LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.229 -15.354 11.284  0.70 16.28 ?  11   LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.644 -16.358 13.227  0.30 14.71 ?  11   LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.464 -16.512 13.238  0.70 16.08 ?  11   LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.494  -17.204 12.536  0.30 14.71 ?  11   LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.515  -17.362 12.301  0.70 16.08 ?  11   LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 11.048 -18.517 11.464  0.30 14.89 ?  11   LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 11.260 -18.525 11.436  0.70 16.03 ?  11   LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.232 -17.612 12.023  0.30 14.89 ?  11   LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.321 -17.506 12.052  0.70 16.03 ?  11   LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.743 -18.325 14.191  0.30 15.51 ?  11   LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.803 -18.246 14.205  0.70 16.44 ?  11   LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.564 -19.232 13.625  0.30 15.51 ?  11   LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.701 -19.228 13.617  0.70 16.44 ?  11   LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.464 -20.531 14.041  0.30 15.66 ?  11   LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.611 -20.441 14.173  0.70 16.42 ?  11   LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 12.115 -20.546 12.489  0.30 15.66 ?  11   LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 12.394 -20.498 12.598  0.70 16.42 ?  11   LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.349 -20.198 12.850  0.30 15.82 ?  11   LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.558 -20.050 13.070  0.70 16.51 ?  11   LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.785 -19.064 12.148  0.30 15.82 ?  11   LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.996 -18.896 12.399  0.70 16.51 ?  11   LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 14.074 -18.969 13.565  0.30 15.82 ?  11   LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 14.204 -18.870 13.832  0.70 16.51 ?  11   LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.849 -16.214 8.919   0.30 11.18 ?  12   LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.879 -16.204 8.992   0.70 12.71 ?  12   LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.609 -16.794 7.601   0.30 11.51 ?  12   LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.627 -16.771 7.669   0.70 13.13 ?  12   LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.214 -18.187 7.469   0.30 11.76 ?  12   LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 11.201 -18.170 7.507   0.70 12.78 ?  12   LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.603 -19.076 6.866   0.30 11.65 ?  12   LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.559 -19.035 6.904   0.70 13.10 ?  12   LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.157 -15.872 6.512   0.30 11.79 ?  12   LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.209 -15.879 6.570   0.70 13.98 ?  12   LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.508 -14.487 6.439   0.30 12.88 ?  12   LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.529 -14.540 6.301   0.70 15.61 ?  12   LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.184 -13.621 5.388   0.30 13.51 ?  12   LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 11.265 -13.805 5.192   0.70 16.49 ?  12   LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 9.021  -14.609 6.152   0.30 13.53 ?  12   LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 9.068  -14.735 5.935   0.70 16.62 ?  12   LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.523 -15.686 8.963   0.30 13.44 ?  12   LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.654 -15.845 9.085   0.70 15.28 ?  12   LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.654  -16.877 7.466   0.30 13.84 ?  12   LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.669  -16.826 7.531   0.70 15.77 ?  12   LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 12.106 -15.741 6.669   0.30 14.17 ?  12   LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 12.131 -15.680 6.801   0.70 16.80 ?  12   LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 11.028 -16.301 5.652   0.30 14.17 ?  12   LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 11.189 -16.374 5.739   0.70 16.80 ?  12   LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.609 -14.043 7.295   0.30 15.48 ?  12   LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.570 -13.995 7.101   0.70 18.76 ?  12   LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.754 -12.751 5.368   0.30 16.23 ?  12   LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.827 -12.956 5.029   0.70 19.81 ?  12   LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.122 -13.520 5.620   0.30 16.23 ?  12   LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 12.184 -13.655 5.468   0.70 19.81 ?  12   LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.102 -14.051 4.523   0.30 16.23 ?  12   LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 11.248 -14.347 4.387   0.70 19.81 ?  12   LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.665  -13.733 5.937   0.30 16.26 ?  12   LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.707  -13.895 5.613   0.70 19.97 ?  12   LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.894  -15.211 5.402   0.30 16.26 ?  12   LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 9.003  -15.410 5.241   0.70 19.97 ?  12   LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.577  -14.964 6.938   0.30 16.26 ?  12   LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.580  -15.024 6.722   0.70 19.97 ?  12   LEU   A HD23 1 
ATOM   319  N  N    . THR   A 1 13  ? 12.417 -18.388 8.002   1.00 12.25 ?  13   THR   A N    1 
ATOM   320  C  CA   . THR   A 1 13  ? 13.109 -19.668 7.909   1.00 12.30 ?  13   THR   A CA   1 
ATOM   321  C  C    . THR   A 1 13  ? 13.886 -19.884 9.200   1.00 12.64 ?  13   THR   A C    1 
ATOM   322  O  O    . THR   A 1 13  ? 13.788 -19.103 10.150  1.00 12.49 ?  13   THR   A O    1 
ATOM   323  C  CB   . THR   A 1 13  ? 14.085 -19.707 6.725   1.00 12.97 ?  13   THR   A CB   1 
ATOM   324  O  OG1  . THR   A 1 13  ? 15.144 -18.779 6.970   1.00 12.94 ?  13   THR   A OG1  1 
ATOM   325  C  CG2  . THR   A 1 13  ? 13.421 -19.383 5.396   1.00 14.32 ?  13   THR   A CG2  1 
ATOM   326  H  H    A THR   A 1 13  ? 12.864 -17.782 8.416   0.30 14.73 ?  13   THR   A H    1 
ATOM   327  H  H    B THR   A 1 13  ? 12.878 -17.785 8.405   0.70 14.73 ?  13   THR   A H    1 
ATOM   328  H  HA   . THR   A 1 13  ? 12.467 -20.385 7.804   1.00 14.79 ?  13   THR   A HA   1 
ATOM   329  H  HB   . THR   A 1 13  ? 14.463 -20.596 6.655   1.00 15.59 ?  13   THR   A HB   1 
ATOM   330  H  HG1  . THR   A 1 13  ? 15.845 -19.192 7.187   1.00 15.55 ?  13   THR   A HG1  1 
ATOM   331  H  HG21 . THR   A 1 13  ? 14.069 -19.491 4.672   1.00 17.21 ?  13   THR   A HG21 1 
ATOM   332  H  HG22 . THR   A 1 13  ? 12.683 -19.989 5.240   1.00 17.21 ?  13   THR   A HG22 1 
ATOM   333  H  HG23 . THR   A 1 13  ? 13.100 -18.474 5.393   1.00 17.21 ?  13   THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.711 -20.931 9.214   0.30 12.55 ?  14   ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.686 -20.949 9.222   0.70 12.90 ?  14   ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.533 -21.207 10.385  0.30 12.73 ?  14   ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.537 -21.214 10.374  0.70 13.54 ?  14   ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.414 -20.022 10.763  0.30 12.17 ?  14   ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.351 -19.982 10.771  0.70 12.94 ?  14   ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.737 -19.849 11.943  0.30 12.47 ?  14   ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.537 -19.715 11.963  0.70 14.40 ?  14   ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.414 -22.427 10.129  0.30 14.27 ?  14   ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.467 -22.386 10.056  0.70 16.13 ?  14   ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.426 -22.648 11.235  0.30 16.60 ?  14   ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.250 -22.848 11.263  0.70 20.46 ?  14   ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 17.014 -23.052 12.344  0.30 17.35 ?  14   ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.609 -23.294 12.237  0.70 21.93 ?  14   ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.630 -22.405 10.998  0.30 17.96 -1 14   ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.493 -22.784 11.238  0.70 22.92 -1 14   ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.812 -21.485 8.565   0.30 15.09 ?  14   ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.757 -21.519 8.581   0.70 15.50 ?  14   ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.955 -21.402 11.137  0.30 15.30 ?  14   ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.981 -21.467 11.125  0.70 16.27 ?  14   ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.843 -23.214 10.047  0.30 17.15 ?  14   ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.926 -23.148 9.764   0.70 19.39 ?  14   ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.912 -22.297 9.309   0.30 17.15 ?  14   ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 17.076 -22.132 9.349   0.70 19.39 ?  14   ASP   A HB3  1 
ATOM   358  N  N    . ASN   A 1 15  ? 16.828 -19.207 9.787   1.00 12.06 ?  15   ASN   A N    1 
ATOM   359  C  CA   . ASN   A 1 15  ? 17.812 -18.158 10.041  1.00 12.49 ?  15   ASN   A CA   1 
ATOM   360  C  C    . ASN   A 1 15  ? 17.437 -16.769 9.542   1.00 12.57 ?  15   ASN   A C    1 
ATOM   361  O  O    . ASN   A 1 15  ? 18.206 -15.832 9.783   1.00 13.83 ?  15   ASN   A O    1 
ATOM   362  C  CB   . ASN   A 1 15  ? 19.181 -18.547 9.448   1.00 12.14 ?  15   ASN   A CB   1 
ATOM   363  C  CG   . ASN   A 1 15  ? 19.162 -18.624 7.943   1.00 12.49 ?  15   ASN   A CG   1 
ATOM   364  O  OD1  . ASN   A 1 15  ? 18.456 -19.455 7.363   1.00 13.33 ?  15   ASN   A OD1  1 
ATOM   365  N  ND2  . ASN   A 1 15  ? 19.939 -17.756 7.292   1.00 12.59 ?  15   ASN   A ND2  1 
ATOM   366  H  H    A ASN   A 1 15  ? 16.553 -19.244 8.977   0.30 14.50 ?  15   ASN   A H    1 
ATOM   367  H  H    B ASN   A 1 15  ? 16.587 -19.268 8.968   0.70 14.50 ?  15   ASN   A H    1 
ATOM   368  H  HA   . ASN   A 1 15  ? 17.942 -18.086 11.000  1.00 15.01 ?  15   ASN   A HA   1 
ATOM   369  H  HB2  . ASN   A 1 15  ? 19.840 -17.876 9.709   1.00 14.60 ?  15   ASN   A HB2  1 
ATOM   370  H  HB3  . ASN   A 1 15  ? 19.446 -19.414 9.787   1.00 14.60 ?  15   ASN   A HB3  1 
ATOM   371  H  HD21 . ASN   A 1 15  ? 19.958 -17.755 6.431   1.00 15.13 ?  15   ASN   A HD21 1 
ATOM   372  H  HD22 . ASN   A 1 15  ? 20.417 -17.184 7.728   1.00 15.13 ?  15   ASN   A HD22 1 
ATOM   373  N  N    . VAL   A 1 16  ? 16.299 -16.599 8.870   1.00 12.09 ?  16   VAL   A N    1 
ATOM   374  C  CA   . VAL   A 1 16  ? 15.895 -15.317 8.301   1.00 12.05 ?  16   VAL   A CA   1 
ATOM   375  C  C    . VAL   A 1 16  ? 14.628 -14.826 8.986   1.00 11.60 ?  16   VAL   A C    1 
ATOM   376  O  O    . VAL   A 1 16  ? 13.631 -15.556 9.082   1.00 12.40 ?  16   VAL   A O    1 
ATOM   377  C  CB   . VAL   A 1 16  ? 15.710 -15.384 6.775   1.00 12.67 ?  16   VAL   A CB   1 
ATOM   378  C  CG1  . VAL   A 1 16  ? 15.269 -14.028 6.221   1.00 13.19 ?  16   VAL   A CG1  1 
ATOM   379  C  CG2  . VAL   A 1 16  ? 16.997 -15.836 6.102   1.00 13.73 ?  16   VAL   A CG2  1 
ATOM   380  H  H    . VAL   A 1 16  ? 15.729 -17.230 8.741   1.00 14.53 ?  16   VAL   A H    1 
ATOM   381  H  HA   . VAL   A 1 16  ? 16.594 -14.668 8.480   1.00 14.49 ?  16   VAL   A HA   1 
ATOM   382  H  HB   . VAL   A 1 16  ? 15.023 -16.035 6.572   1.00 15.23 ?  16   VAL   A HB   1 
ATOM   383  H  HG11 . VAL   A 1 16  ? 15.344 -14.049 5.253   1.00 15.86 ?  16   VAL   A HG11 1 
ATOM   384  H  HG12 . VAL   A 1 16  ? 14.347 -13.867 6.475   1.00 15.86 ?  16   VAL   A HG12 1 
ATOM   385  H  HG13 . VAL   A 1 16  ? 15.841 -13.336 6.582   1.00 15.86 ?  16   VAL   A HG13 1 
ATOM   386  H  HG21 . VAL   A 1 16  ? 16.873 -15.823 5.141   1.00 16.50 ?  16   VAL   A HG21 1 
ATOM   387  H  HG22 . VAL   A 1 16  ? 17.715 -15.222 6.346   1.00 16.50 ?  16   VAL   A HG22 1 
ATOM   388  H  HG23 . VAL   A 1 16  ? 17.219 -16.730 6.399   1.00 16.50 ?  16   VAL   A HG23 1 
ATOM   389  N  N    A TYR   A 1 17  ? 14.666 -13.567 9.415   0.30 11.38 ?  17   TYR   A N    1 
ATOM   390  N  N    B TYR   A 1 17  ? 14.670 -13.569 9.435   0.70 11.39 ?  17   TYR   A N    1 
ATOM   391  C  CA   A TYR   A 1 17  ? 13.559 -12.887 10.062  0.30 11.23 ?  17   TYR   A CA   1 
ATOM   392  C  CA   B TYR   A 1 17  ? 13.601 -12.894 10.155  0.70 11.43 ?  17   TYR   A CA   1 
ATOM   393  C  C    A TYR   A 1 17  ? 13.287 -11.586 9.315   0.30 10.92 ?  17   TYR   A C    1 
ATOM   394  C  C    B TYR   A 1 17  ? 13.314 -11.566 9.463   0.70 11.57 ?  17   TYR   A C    1 
ATOM   395  O  O    A TYR   A 1 17  ? 14.149 -11.078 8.594   0.30 10.88 ?  17   TYR   A O    1 
ATOM   396  O  O    B TYR   A 1 17  ? 14.217 -10.969 8.877   0.70 11.77 ?  17   TYR   A O    1 
ATOM   397  C  CB   A TYR   A 1 17  ? 13.911 -12.600 11.526  0.30 11.69 ?  17   TYR   A CB   1 
ATOM   398  C  CB   B TYR   A 1 17  ? 14.055 -12.620 11.596  0.70 12.01 ?  17   TYR   A CB   1 
ATOM   399  C  CG   A TYR   A 1 17  ? 14.114 -13.858 12.342  0.30 12.20 ?  17   TYR   A CG   1 
ATOM   400  C  CG   B TYR   A 1 17  ? 14.277 -13.873 12.416  0.70 12.75 ?  17   TYR   A CG   1 
ATOM   401  C  CD1  A TYR   A 1 17  ? 15.300 -14.586 12.274  0.30 12.61 ?  17   TYR   A CD1  1 
ATOM   402  C  CD1  B TYR   A 1 17  ? 15.469 -14.590 12.343  0.70 13.74 ?  17   TYR   A CD1  1 
ATOM   403  C  CD2  A TYR   A 1 17  ? 13.108 -14.335 13.169  0.30 12.29 ?  17   TYR   A CD2  1 
ATOM   404  C  CD2  B TYR   A 1 17  ? 13.283 -14.359 13.255  0.70 13.09 ?  17   TYR   A CD2  1 
ATOM   405  C  CE1  A TYR   A 1 17  ? 15.472 -15.754 13.014  0.30 12.90 ?  17   TYR   A CE1  1 
ATOM   406  C  CE1  B TYR   A 1 17  ? 15.661 -15.756 13.088  0.70 14.84 ?  17   TYR   A CE1  1 
ATOM   407  C  CE2  A TYR   A 1 17  ? 13.274 -15.495 13.912  0.30 12.78 ?  17   TYR   A CE2  1 
ATOM   408  C  CE2  B TYR   A 1 17  ? 13.470 -15.519 14.006  0.70 13.99 ?  17   TYR   A CE2  1 
ATOM   409  C  CZ   A TYR   A 1 17  ? 14.454 -16.199 13.833  0.30 12.98 ?  17   TYR   A CZ   1 
ATOM   410  C  CZ   B TYR   A 1 17  ? 14.658 -16.211 13.920  0.70 14.82 ?  17   TYR   A CZ   1 
ATOM   411  O  OH   A TYR   A 1 17  ? 14.609 -17.348 14.576  0.30 13.48 ?  17   TYR   A OH   1 
ATOM   412  O  OH   B TYR   A 1 17  ? 14.841 -17.357 14.666  0.70 15.90 ?  17   TYR   A OH   1 
ATOM   413  H  H    A TYR   A 1 17  ? 15.361 -13.062 9.329   0.30 13.68 ?  17   TYR   A H    1 
ATOM   414  H  H    B TYR   A 1 17  ? 15.354 -13.054 9.309   0.70 13.70 ?  17   TYR   A H    1 
ATOM   415  H  HA   A TYR   A 1 17  ? 12.769 -13.452 10.028  0.30 13.51 ?  17   TYR   A HA   1 
ATOM   416  H  HA   B TYR   A 1 17  ? 12.799 -13.440 10.159  0.70 13.74 ?  17   TYR   A HA   1 
ATOM   417  H  HB2  A TYR   A 1 17  ? 14.730 -12.087 11.559  0.30 14.05 ?  17   TYR   A HB2  1 
ATOM   418  H  HB2  B TYR   A 1 17  ? 14.892 -12.136 11.575  0.70 14.44 ?  17   TYR   A HB2  1 
ATOM   419  H  HB3  A TYR   A 1 17  ? 13.187 -12.100 11.927  0.30 14.05 ?  17   TYR   A HB3  1 
ATOM   420  H  HB3  B TYR   A 1 17  ? 13.377 -12.097 12.043  0.70 14.44 ?  17   TYR   A HB3  1 
ATOM   421  H  HD1  A TYR   A 1 17  ? 15.987 -14.291 11.722  0.30 15.16 ?  17   TYR   A HD1  1 
ATOM   422  H  HD1  B TYR   A 1 17  ? 16.149 -14.293 11.784  0.70 16.51 ?  17   TYR   A HD1  1 
ATOM   423  H  HD2  A TYR   A 1 17  ? 12.304 -13.875 13.228  0.30 14.77 ?  17   TYR   A HD2  1 
ATOM   424  H  HD2  B TYR   A 1 17  ? 12.475 -13.908 13.321  0.70 15.74 ?  17   TYR   A HD2  1 
ATOM   425  H  HE1  A TYR   A 1 17  ? 16.276 -16.227 12.961  0.30 15.51 ?  17   TYR   A HE1  1 
ATOM   426  H  HE1  B TYR   A 1 17  ? 16.468 -16.221 13.032  0.70 17.84 ?  17   TYR   A HE1  1 
ATOM   427  H  HE2  A TYR   A 1 17  ? 12.590 -15.802 14.463  0.30 15.36 ?  17   TYR   A HE2  1 
ATOM   428  H  HE2  B TYR   A 1 17  ? 12.791 -15.830 14.565  0.70 16.82 ?  17   TYR   A HE2  1 
ATOM   429  H  HH   A TYR   A 1 17  ? 13.872 -17.575 14.908  0.30 16.20 ?  17   TYR   A HH   1 
ATOM   430  H  HH   B TYR   A 1 17  ? 15.613 -17.661 14.543  0.70 19.10 ?  17   TYR   A HH   1 
ATOM   431  N  N    A ILE   A 1 18  ? 12.081 -11.040 9.488   0.30 11.10 ?  18   ILE   A N    1 
ATOM   432  N  N    B ILE   A 1 18  ? 12.062 -11.088 9.531   0.70 12.26 ?  18   ILE   A N    1 
ATOM   433  C  CA   A ILE   A 1 18  ? 11.665 -9.854  8.742   0.30 11.51 ?  18   ILE   A CA   1 
ATOM   434  C  CA   B ILE   A 1 18  ? 11.668 -9.896  8.779   0.70 13.01 ?  18   ILE   A CA   1 
ATOM   435  C  C    A ILE   A 1 18  ? 10.715 -9.024  9.598   0.30 11.64 ?  18   ILE   A C    1 
ATOM   436  C  C    B ILE   A 1 18  ? 10.683 -9.043  9.569   0.70 13.68 ?  18   ILE   A C    1 
ATOM   437  O  O    A ILE   A 1 18  ? 9.929  -9.561  10.384  0.30 11.71 ?  18   ILE   A O    1 
ATOM   438  O  O    B ILE   A 1 18  ? 9.850  -9.556  10.323  0.70 14.07 ?  18   ILE   A O    1 
ATOM   439  C  CB   A ILE   A 1 18  ? 11.059 -10.239 7.368   0.30 12.28 ?  18   ILE   A CB   1 
ATOM   440  C  CB   B ILE   A 1 18  ? 11.113 -10.300 7.392   0.70 13.55 ?  18   ILE   A CB   1 
ATOM   441  C  CG1  A ILE   A 1 18  ? 10.977 -9.019  6.446   0.30 13.11 ?  18   ILE   A CG1  1 
ATOM   442  C  CG1  B ILE   A 1 18  ? 11.015 -9.105  6.444   0.70 14.01 ?  18   ILE   A CG1  1 
ATOM   443  C  CG2  A ILE   A 1 18  ? 9.698  -10.908 7.539   0.30 12.47 ?  18   ILE   A CG2  1 
ATOM   444  C  CG2  B ILE   A 1 18  ? 9.787  -11.053 7.533   0.70 13.77 ?  18   ILE   A CG2  1 
ATOM   445  C  CD1  A ILE   A 1 18  ? 10.672 -9.369  5.003   0.30 14.71 ?  18   ILE   A CD1  1 
ATOM   446  C  CD1  B ILE   A 1 18  ? 10.838 -9.537  5.009   0.70 15.91 ?  18   ILE   A CD1  1 
ATOM   447  H  H    A ILE   A 1 18  ? 11.494 -11.341 10.037  0.30 13.35 ?  18   ILE   A H    1 
ATOM   448  H  H    B ILE   A 1 18  ? 11.427 -11.449 9.995   0.70 14.74 ?  18   ILE   A H    1 
ATOM   449  H  HA   A ILE   A 1 18  ? 12.451 -9.315  8.569   0.30 13.84 ?  18   ILE   A HA   1 
ATOM   450  H  HA   B ILE   A 1 18  ? 12.465 -9.363  8.631   0.70 15.63 ?  18   ILE   A HA   1 
ATOM   451  H  HB   A ILE   A 1 18  ? 11.650 -10.883 6.951   0.30 14.76 ?  18   ILE   A HB   1 
ATOM   452  H  HB   B ILE   A 1 18  ? 11.749 -10.916 7.004   0.70 16.29 ?  18   ILE   A HB   1 
ATOM   453  H  HG12 A ILE   A 1 18  ? 10.276 -8.431  6.762   0.30 15.75 ?  18   ILE   A HG12 1 
ATOM   454  H  HG12 B ILE   A 1 18  ? 10.255 -8.560  6.689   0.70 16.84 ?  18   ILE   A HG12 1 
ATOM   455  H  HG13 A ILE   A 1 18  ? 11.830 -8.557  6.463   0.30 15.75 ?  18   ILE   A HG13 1 
ATOM   456  H  HG13 B ILE   A 1 18  ? 11.833 -8.585  6.498   0.70 16.84 ?  18   ILE   A HG13 1 
ATOM   457  H  HG21 A ILE   A 1 18  ? 9.420  -11.276 6.684   0.30 14.99 ?  18   ILE   A HG21 1 
ATOM   458  H  HG21 B ILE   A 1 18  ? 9.545  -11.417 6.667   0.70 16.55 ?  18   ILE   A HG21 1 
ATOM   459  H  HG22 A ILE   A 1 18  ? 9.779  -11.617 8.193   0.30 14.99 ?  18   ILE   A HG22 1 
ATOM   460  H  HG22 B ILE   A 1 18  ? 9.903  -11.771 8.173   0.70 16.55 ?  18   ILE   A HG22 1 
ATOM   461  H  HG23 A ILE   A 1 18  ? 9.055  -10.249 7.839   0.30 14.99 ?  18   ILE   A HG23 1 
ATOM   462  H  HG23 B ILE   A 1 18  ? 9.106  -10.438 7.839   0.70 16.55 ?  18   ILE   A HG23 1 
ATOM   463  H  HD11 A ILE   A 1 18  ? 10.689 -8.557  4.471   0.30 17.67 ?  18   ILE   A HD11 1 
ATOM   464  H  HD11 B ILE   A 1 18  ? 10.861 -8.751  4.437   0.70 19.12 ?  18   ILE   A HD11 1 
ATOM   465  H  HD12 A ILE   A 1 18  ? 11.345 -9.989  4.679   0.30 17.67 ?  18   ILE   A HD12 1 
ATOM   466  H  HD12 B ILE   A 1 18  ? 11.556 -10.140 4.767   0.70 19.12 ?  18   ILE   A HD12 1 
ATOM   467  H  HD13 A ILE   A 1 18  ? 9.795  -9.779  4.955   0.30 17.67 ?  18   ILE   A HD13 1 
ATOM   468  H  HD13 B ILE   A 1 18  ? 9.982  -9.984  4.917   0.70 19.12 ?  18   ILE   A HD13 1 
ATOM   469  N  N    A LYS   A 1 19  ? 10.790 -7.701  9.432   0.30 12.10 ?  19   LYS   A N    1 
ATOM   470  N  N    B LYS   A 1 19  ? 10.772 -7.725  9.370   0.70 14.07 ?  19   LYS   A N    1 
ATOM   471  C  CA   A LYS   A 1 19  ? 10.008 -6.761  10.224  0.30 13.16 ?  19   LYS   A CA   1 
ATOM   472  C  CA   B LYS   A 1 19  ? 9.915  -6.769  10.061  0.70 15.21 ?  19   LYS   A CA   1 
ATOM   473  C  C    A LYS   A 1 19  ? 9.812  -5.481  9.424   0.30 13.50 ?  19   LYS   A C    1 
ATOM   474  C  C    B LYS   A 1 19  ? 9.713  -5.542  9.179   0.70 14.88 ?  19   LYS   A C    1 
ATOM   475  O  O    A LYS   A 1 19  ? 10.722 -5.042  8.718   0.30 13.45 ?  19   LYS   A O    1 
ATOM   476  O  O    B LYS   A 1 19  ? 10.611 -5.149  8.430   0.70 14.36 ?  19   LYS   A O    1 
ATOM   477  C  CB   A LYS   A 1 19  ? 10.749 -6.434  11.526  0.30 13.84 ?  19   LYS   A CB   1 
ATOM   478  C  CB   B LYS   A 1 19  ? 10.584 -6.352  11.375  0.70 16.24 ?  19   LYS   A CB   1 
ATOM   479  C  CG   A LYS   A 1 19  ? 10.068 -5.435  12.451  0.30 14.63 ?  19   LYS   A CG   1 
ATOM   480  C  CG   B LYS   A 1 19  ? 9.777  -5.445  12.281  0.70 17.54 ?  19   LYS   A CG   1 
ATOM   481  C  CD   A LYS   A 1 19  ? 10.988 -5.123  13.624  0.30 14.89 ?  19   LYS   A CD   1 
ATOM   482  C  CD   B LYS   A 1 19  ? 10.601 -5.134  13.518  0.70 18.57 ?  19   LYS   A CD   1 
ATOM   483  C  CE   A LYS   A 1 19  ? 10.335 -4.223  14.655  0.30 15.41 ?  19   LYS   A CE   1 
ATOM   484  C  CE   B LYS   A 1 19  ? 9.901  -4.167  14.453  0.70 19.46 ?  19   LYS   A CE   1 
ATOM   485  N  NZ   A LYS   A 1 19  ? 11.230 -4.046  15.834  0.30 15.71 ?  19   LYS   A NZ   1 
ATOM   486  N  NZ   B LYS   A 1 19  ? 10.764 -3.837  15.619  0.70 20.02 ?  19   LYS   A NZ   1 
ATOM   487  H  H    A LYS   A 1 19  ? 11.301 -7.319  8.854   0.30 14.54 ?  19   LYS   A H    1 
ATOM   488  H  H    B LYS   A 1 19  ? 11.340 -7.357  8.835   0.70 16.91 ?  19   LYS   A H    1 
ATOM   489  H  HA   A LYS   A 1 19  ? 9.140  -7.140  10.437  0.30 15.82 ?  19   LYS   A HA   1 
ATOM   490  H  HA   B LYS   A 1 19  ? 9.056  -7.185  10.256  0.70 18.28 ?  19   LYS   A HA   1 
ATOM   491  H  HB2  A LYS   A 1 19  ? 10.858 -7.257  12.027  0.30 16.63 ?  19   LYS   A HB2  1 
ATOM   492  H  HB2  B LYS   A 1 19  ? 10.786 -7.156  11.881  0.70 19.51 ?  19   LYS   A HB2  1 
ATOM   493  H  HB3  A LYS   A 1 19  ? 11.620 -6.074  11.301  0.30 16.63 ?  19   LYS   A HB3  1 
ATOM   494  H  HB3  B LYS   A 1 19  ? 11.406 -5.892  11.159  0.70 19.51 ?  19   LYS   A HB3  1 
ATOM   495  H  HG2  A LYS   A 1 19  ? 9.889  -4.610  11.974  0.30 17.58 ?  19   LYS   A HG2  1 
ATOM   496  H  HG2  B LYS   A 1 19  ? 9.579  -4.613  11.823  0.70 21.07 ?  19   LYS   A HG2  1 
ATOM   497  H  HG3  A LYS   A 1 19  ? 9.245  -5.816  12.796  0.30 17.58 ?  19   LYS   A HG3  1 
ATOM   498  H  HG3  B LYS   A 1 19  ? 8.960  -5.890  12.555  0.70 21.07 ?  19   LYS   A HG3  1 
ATOM   499  H  HD2  A LYS   A 1 19  ? 11.233 -5.952  14.063  0.30 17.89 ?  19   LYS   A HD2  1 
ATOM   500  H  HD2  B LYS   A 1 19  ? 10.766 -5.958  14.004  0.70 22.31 ?  19   LYS   A HD2  1 
ATOM   501  H  HD3  A LYS   A 1 19  ? 11.781 -4.674  13.293  0.30 17.89 ?  19   LYS   A HD3  1 
ATOM   502  H  HD3  B LYS   A 1 19  ? 11.444 -4.736  13.246  0.70 22.31 ?  19   LYS   A HD3  1 
ATOM   503  H  HE2  A LYS   A 1 19  ? 10.165 -3.352  14.262  0.30 18.51 ?  19   LYS   A HE2  1 
ATOM   504  H  HE2  B LYS   A 1 19  ? 9.706  -3.345  13.975  0.70 23.38 ?  19   LYS   A HE2  1 
ATOM   505  H  HE3  A LYS   A 1 19  ? 9.505  -4.625  14.956  0.30 18.51 ?  19   LYS   A HE3  1 
ATOM   506  H  HE3  B LYS   A 1 19  ? 9.085  -4.572  14.781  0.70 23.38 ?  19   LYS   A HE3  1 
ATOM   507  H  HZ1  A LYS   A 1 19  ? 10.836 -3.523  16.437  0.30 18.88 ?  19   LYS   A HZ1  1 
ATOM   508  H  HZ1  B LYS   A 1 19  ? 10.343 -3.270  16.159  0.70 24.05 ?  19   LYS   A HZ1  1 
ATOM   509  H  HZ2  A LYS   A 1 19  ? 11.404 -4.835  16.204  0.30 18.88 ?  19   LYS   A HZ2  1 
ATOM   510  H  HZ2  B LYS   A 1 19  ? 10.960 -4.578  16.073  0.70 24.05 ?  19   LYS   A HZ2  1 
ATOM   511  H  HZ3  A LYS   A 1 19  ? 11.994 -3.669  15.580  0.30 18.88 ?  19   LYS   A HZ3  1 
ATOM   512  H  HZ3  B LYS   A 1 19  ? 11.523 -3.462  15.340  0.70 24.05 ?  19   LYS   A HZ3  1 
ATOM   513  N  N    A ASN   A 1 20  ? 8.626  -4.884  9.536   0.30 14.24 ?  20   ASN   A N    1 
ATOM   514  N  N    B ASN   A 1 20  ? 8.526  -4.940  9.263   0.70 15.78 ?  20   ASN   A N    1 
ATOM   515  C  CA   A ASN   A 1 20  ? 8.390  -3.563  8.962   0.30 14.80 ?  20   ASN   A CA   1 
ATOM   516  C  CA   B ASN   A 1 20  ? 8.289  -3.635  8.641   0.70 16.71 ?  20   ASN   A CA   1 
ATOM   517  C  C    A ASN   A 1 20  ? 8.984  -2.539  9.918   0.30 14.70 ?  20   ASN   A C    1 
ATOM   518  C  C    B ASN   A 1 20  ? 8.901  -2.586  9.562   0.70 16.98 ?  20   ASN   A C    1 
ATOM   519  O  O    A ASN   A 1 20  ? 8.474  -2.346  11.027  0.30 15.04 ?  20   ASN   A O    1 
ATOM   520  O  O    B ASN   A 1 20  ? 8.336  -2.258  10.608  0.70 18.41 ?  20   ASN   A O    1 
ATOM   521  C  CB   A ASN   A 1 20  ? 6.897  -3.328  8.740   0.30 15.91 ?  20   ASN   A CB   1 
ATOM   522  C  CB   B ASN   A 1 20  ? 6.795  -3.398  8.420   0.70 17.65 ?  20   ASN   A CB   1 
ATOM   523  C  CG   A ASN   A 1 20  ? 6.575  -1.888  8.364   0.30 17.14 ?  20   ASN   A CG   1 
ATOM   524  C  CG   B ASN   A 1 20  ? 6.472  -1.969  7.981   0.70 19.13 ?  20   ASN   A CG   1 
ATOM   525  O  OD1  A ASN   A 1 20  ? 5.637  -1.293  8.897   0.30 18.26 ?  20   ASN   A OD1  1 
ATOM   526  O  OD1  B ASN   A 1 20  ? 5.515  -1.357  8.474   0.70 21.41 ?  20   ASN   A OD1  1 
ATOM   527  N  ND2  A ASN   A 1 20  ? 7.358  -1.321  7.449   0.30 17.52 ?  20   ASN   A ND2  1 
ATOM   528  N  ND2  B ASN   A 1 20  ? 7.261  -1.438  7.046   0.70 19.92 ?  20   ASN   A ND2  1 
ATOM   529  H  H    A ASN   A 1 20  ? 7.947  -5.216  9.945   0.30 17.11 ?  20   ASN   A H    1 
ATOM   530  H  H    B ASN   A 1 20  ? 7.837  -5.275  9.667   0.70 18.96 ?  20   ASN   A H    1 
ATOM   531  H  HA   A ASN   A 1 20  ? 8.843  -3.494  8.109   0.30 17.78 ?  20   ASN   A HA   1 
ATOM   532  H  HA   B ASN   A 1 20  ? 8.741  -3.604  7.782   0.70 20.08 ?  20   ASN   A HA   1 
ATOM   533  H  HB2  A ASN   A 1 20  ? 6.592  -3.903  8.018   0.30 19.11 ?  20   ASN   A HB2  1 
ATOM   534  H  HB2  B ASN   A 1 20  ? 6.481  -3.999  7.727   0.70 21.20 ?  20   ASN   A HB2  1 
ATOM   535  H  HB3  A ASN   A 1 20  ? 6.417  -3.539  9.554   0.30 19.11 ?  20   ASN   A HB3  1 
ATOM   536  H  HB3  B ASN   A 1 20  ? 6.326  -3.577  9.250   0.70 21.20 ?  20   ASN   A HB3  1 
ATOM   537  H  HD21 A ASN   A 1 20  ? 7.212  -0.510  7.200   0.30 21.05 ?  20   ASN   A HD21 1 
ATOM   538  H  HD21 B ASN   A 1 20  ? 7.121  -0.636  6.776   0.70 23.93 ?  20   ASN   A HD21 1 
ATOM   539  H  HD22 A ASN   A 1 20  ? 8.007  -1.765  7.102   0.30 21.05 ?  20   ASN   A HD22 1 
ATOM   540  H  HD22 B ASN   A 1 20  ? 7.909  -1.899  6.715   0.70 23.93 ?  20   ASN   A HD22 1 
ATOM   541  N  N    A ALA   A 1 21  ? 10.080 -1.903  9.511   0.30 14.58 ?  21   ALA   A N    1 
ATOM   542  N  N    B ALA   A 1 21  ? 10.073 -2.071  9.187   0.70 15.94 ?  21   ALA   A N    1 
ATOM   543  C  CA   A ALA   A 1 21  ? 10.758 -0.992  10.420  0.30 14.60 ?  21   ALA   A CA   1 
ATOM   544  C  CA   B ALA   A 1 21  ? 10.793 -1.142  10.046  0.70 15.66 ?  21   ALA   A CA   1 
ATOM   545  C  C    A ALA   A 1 21  ? 11.761 -0.149  9.653   0.30 14.30 ?  21   ALA   A C    1 
ATOM   546  C  C    B ALA   A 1 21  ? 11.787 -0.348  9.214   0.70 14.54 ?  21   ALA   A C    1 
ATOM   547  O  O    A ALA   A 1 21  ? 12.267 -0.557  8.603   0.30 14.45 ?  21   ALA   A O    1 
ATOM   548  O  O    B ALA   A 1 21  ? 12.225 -0.796  8.152   0.70 14.64 ?  21   ALA   A O    1 
ATOM   549  C  CB   A ALA   A 1 21  ? 11.470 -1.763  11.534  0.30 15.44 ?  21   ALA   A CB   1 
ATOM   550  C  CB   B ALA   A 1 21  ? 11.537 -1.879  11.166  0.70 16.74 ?  21   ALA   A CB   1 
ATOM   551  H  H    A ALA   A 1 21  ? 10.445 -1.983  8.736   0.30 17.52 ?  21   ALA   A H    1 
ATOM   552  H  H    B ALA   A 1 21  ? 10.461 -2.245  8.439   0.70 19.15 ?  21   ALA   A H    1 
ATOM   553  H  HA   A ALA   A 1 21  ? 10.109 -0.396  10.823  0.30 17.54 ?  21   ALA   A HA   1 
ATOM   554  H  HA   B ALA   A 1 21  ? 10.159 -0.527  10.448  0.70 18.82 ?  21   ALA   A HA   1 
ATOM   555  H  HB1  A ALA   A 1 21  ? 11.853 -1.127  12.153  0.30 18.55 ?  21   ALA   A HB1  1 
ATOM   556  H  HB1  B ALA   A 1 21  ? 11.983 -1.226  11.725  0.70 20.11 ?  21   ALA   A HB1  1 
ATOM   557  H  HB2  A ALA   A 1 21  ? 10.819 -2.321  11.987  0.30 18.55 ?  21   ALA   A HB2  1 
ATOM   558  H  HB2  B ALA   A 1 21  ? 10.893 -2.382  11.696  0.70 20.11 ?  21   ALA   A HB2  1 
ATOM   559  H  HB3  A ALA   A 1 21  ? 12.163 -2.314  11.140  0.30 18.55 ?  21   ALA   A HB3  1 
ATOM   560  H  HB3  B ALA   A 1 21  ? 12.182 -2.483  10.773  0.70 20.11 ?  21   ALA   A HB3  1 
ATOM   561  N  N    A ASP   A 1 22  ? 12.028 1.036   10.197  0.30 14.27 ?  22   ASP   A N    1 
ATOM   562  N  N    B ASP   A 1 22  ? 12.113 0.844   9.714   0.70 14.48 ?  22   ASP   A N    1 
ATOM   563  C  CA   A ASP   A 1 22  ? 13.074 1.917   9.700   0.30 14.40 ?  22   ASP   A CA   1 
ATOM   564  C  CA   B ASP   A 1 22  ? 13.209 1.658   9.199   0.70 13.77 ?  22   ASP   A CA   1 
ATOM   565  C  C    A ASP   A 1 22  ? 14.411 1.420   10.234  0.30 13.83 ?  22   ASP   A C    1 
ATOM   566  C  C    B ASP   A 1 22  ? 14.501 1.156   9.833   0.70 12.62 ?  22   ASP   A C    1 
ATOM   567  O  O    A ASP   A 1 22  ? 14.631 1.404   11.450  0.30 14.15 ?  22   ASP   A O    1 
ATOM   568  O  O    B ASP   A 1 22  ? 14.629 1.154   11.061  0.70 12.96 ?  22   ASP   A O    1 
ATOM   569  C  CB   A ASP   A 1 22  ? 12.802 3.334   10.197  0.30 15.30 ?  22   ASP   A CB   1 
ATOM   570  C  CB   B ASP   A 1 22  ? 12.955 3.110   9.604   0.70 15.07 ?  22   ASP   A CB   1 
ATOM   571  C  CG   A ASP   A 1 22  ? 13.796 4.349   9.659   0.30 15.73 ?  22   ASP   A CG   1 
ATOM   572  C  CG   B ASP   A 1 22  ? 13.972 4.091   9.029   0.70 15.95 ?  22   ASP   A CG   1 
ATOM   573  O  OD1  A ASP   A 1 22  ? 14.827 3.951   9.081   0.30 15.71 ?  22   ASP   A OD1  1 
ATOM   574  O  OD1  B ASP   A 1 22  ? 15.115 3.690   8.709   0.70 14.78 ?  22   ASP   A OD1  1 
ATOM   575  O  OD2  A ASP   A 1 22  ? 13.540 5.559   9.818   0.30 16.15 -1 22   ASP   A OD2  1 
ATOM   576  O  OD2  B ASP   A 1 22  ? 13.615 5.283   8.908   0.70 18.66 -1 22   ASP   A OD2  1 
ATOM   577  H  H    A ASP   A 1 22  ? 11.603 1.360   10.869  0.30 17.15 ?  22   ASP   A H    1 
ATOM   578  H  H    B ASP   A 1 22  ? 11.689 1.210   10.367  0.70 17.40 ?  22   ASP   A H    1 
ATOM   579  H  HA   A ASP   A 1 22  ? 13.092 1.915   8.728   0.30 17.30 ?  22   ASP   A HA   1 
ATOM   580  H  HA   B ASP   A 1 22  ? 13.262 1.580   8.234   0.70 16.55 ?  22   ASP   A HA   1 
ATOM   581  H  HB2  A ASP   A 1 22  ? 11.914 3.605   9.916   0.30 18.39 ?  22   ASP   A HB2  1 
ATOM   582  H  HB2  B ASP   A 1 22  ? 12.081 3.370   9.288   0.70 18.11 ?  22   ASP   A HB2  1 
ATOM   583  H  HB3  A ASP   A 1 22  ? 12.855 3.342   11.169  0.30 18.39 ?  22   ASP   A HB3  1 
ATOM   584  H  HB3  B ASP   A 1 22  ? 12.989 3.165   10.574  0.70 18.11 ?  22   ASP   A HB3  1 
ATOM   585  N  N    A ILE   A 1 23  ? 15.302 1.015   9.327   0.30 13.23 ?  23   ILE   A N    1 
ATOM   586  N  N    B ILE   A 1 23  ? 15.452 0.713   9.003   0.70 12.48 ?  23   ILE   A N    1 
ATOM   587  C  CA   A ILE   A 1 23  ? 16.567 0.414   9.743   0.30 12.51 ?  23   ILE   A CA   1 
ATOM   588  C  CA   B ILE   A 1 23  ? 16.700 0.149   9.520   0.70 12.37 ?  23   ILE   A CA   1 
ATOM   589  C  C    A ILE   A 1 23  ? 17.379 1.370   10.606  0.30 12.56 ?  23   ILE   A C    1 
ATOM   590  C  C    B ILE   A 1 23  ? 17.403 1.126   10.452  0.70 12.47 ?  23   ILE   A C    1 
ATOM   591  O  O    A ILE   A 1 23  ? 18.150 0.934   11.470  0.30 12.94 ?  23   ILE   A O    1 
ATOM   592  O  O    B ILE   A 1 23  ? 18.072 0.711   11.407  0.70 12.62 ?  23   ILE   A O    1 
ATOM   593  C  CB   A ILE   A 1 23  ? 17.352 -0.084  8.513   0.30 12.01 ?  23   ILE   A CB   1 
ATOM   594  C  CB   B ILE   A 1 23  ? 17.621 -0.346  8.376   0.70 12.15 ?  23   ILE   A CB   1 
ATOM   595  C  CG1  A ILE   A 1 23  ? 18.543 -0.941  8.951   0.30 12.69 ?  23   ILE   A CG1  1 
ATOM   596  C  CG1  B ILE   A 1 23  ? 18.683 -1.311  8.926   0.70 12.68 ?  23   ILE   A CG1  1 
ATOM   597  C  CG2  A ILE   A 1 23  ? 17.794 1.087   7.643   0.30 11.53 ?  23   ILE   A CG2  1 
ATOM   598  C  CG2  B ILE   A 1 23  ? 18.272 0.820   7.633   0.70 12.21 ?  23   ILE   A CG2  1 
ATOM   599  C  CD1  A ILE   A 1 23  ? 19.168 -1.723  7.818   0.30 12.94 ?  23   ILE   A CD1  1 
ATOM   600  C  CD1  B ILE   A 1 23  ? 19.604 -1.901  7.867   0.70 12.77 ?  23   ILE   A CD1  1 
ATOM   601  H  H    A ILE   A 1 23  ? 15.195 1.073   8.478   0.30 15.90 ?  23   ILE   A H    1 
ATOM   602  H  H    B ILE   A 1 23  ? 15.398 0.721   8.154   0.70 14.99 ?  23   ILE   A H    1 
ATOM   603  H  HA   A ILE   A 1 23  ? 16.368 -0.361  10.287  0.30 15.04 ?  23   ILE   A HA   1 
ATOM   604  H  HA   B ILE   A 1 23  ? 16.476 -0.633  10.046  0.70 14.87 ?  23   ILE   A HA   1 
ATOM   605  H  HB   A ILE   A 1 23  ? 16.761 -0.641  7.987   0.30 14.43 ?  23   ILE   A HB   1 
ATOM   606  H  HB   B ILE   A 1 23  ? 17.080 -0.838  7.739   0.70 14.60 ?  23   ILE   A HB   1 
ATOM   607  H  HG12 A ILE   A 1 23  ? 19.226 -0.363  9.326   0.30 15.25 ?  23   ILE   A HG12 1 
ATOM   608  H  HG12 B ILE   A 1 23  ? 19.237 -0.838  9.565   0.70 15.23 ?  23   ILE   A HG12 1 
ATOM   609  H  HG13 A ILE   A 1 23  ? 18.243 -1.576  9.620   0.30 15.25 ?  23   ILE   A HG13 1 
ATOM   610  H  HG13 B ILE   A 1 23  ? 18.235 -2.051  9.366   0.70 15.23 ?  23   ILE   A HG13 1 
ATOM   611  H  HG21 A ILE   A 1 23  ? 18.163 0.742   6.814   0.30 13.86 ?  23   ILE   A HG21 1 
ATOM   612  H  HG21 B ILE   A 1 23  ? 18.669 0.491   6.806   0.70 14.68 ?  23   ILE   A HG21 1 
ATOM   613  H  HG22 A ILE   A 1 23  ? 17.025 1.647   7.452   0.30 13.86 ?  23   ILE   A HG22 1 
ATOM   614  H  HG22 B ILE   A 1 23  ? 17.596 1.482   7.429   0.70 14.68 ?  23   ILE   A HG22 1 
ATOM   615  H  HG23 A ILE   A 1 23  ? 18.467 1.600   8.116   0.30 13.86 ?  23   ILE   A HG23 1 
ATOM   616  H  HG23 B ILE   A 1 23  ? 18.963 1.212   8.191   0.70 14.68 ?  23   ILE   A HG23 1 
ATOM   617  H  HD11 A ILE   A 1 23  ? 19.881 -2.275  8.172   0.30 15.55 ?  23   ILE   A HD11 1 
ATOM   618  H  HD11 B ILE   A 1 23  ? 20.172 -2.572  8.279   0.70 15.35 ?  23   ILE   A HD11 1 
ATOM   619  H  HD12 A ILE   A 1 23  ? 18.488 -2.280  7.408   0.30 15.55 ?  23   ILE   A HD12 1 
ATOM   620  H  HD12 B ILE   A 1 23  ? 19.067 -2.306  7.170   0.70 15.35 ?  23   ILE   A HD12 1 
ATOM   621  H  HD13 A ILE   A 1 23  ? 19.523 -1.100  7.164   0.30 15.55 ?  23   ILE   A HD13 1 
ATOM   622  H  HD13 B ILE   A 1 23  ? 20.152 -1.192  7.493   0.70 15.35 ?  23   ILE   A HD13 1 
ATOM   623  N  N    A VAL   A 1 24  ? 17.231 2.679   10.391  0.30 12.76 ?  24   VAL   A N    1 
ATOM   624  N  N    B VAL   A 1 24  ? 17.268 2.431   10.198  0.70 13.21 ?  24   VAL   A N    1 
ATOM   625  C  CA   A VAL   A 1 24  ? 17.914 3.653   11.239  0.30 13.34 ?  24   VAL   A CA   1 
ATOM   626  C  CA   B VAL   A 1 24  ? 17.913 3.430   11.046  0.70 14.37 ?  24   VAL   A CA   1 
ATOM   627  C  C    A VAL   A 1 24  ? 17.407 3.554   12.671  0.30 14.03 ?  24   VAL   A C    1 
ATOM   628  C  C    B VAL   A 1 24  ? 17.330 3.392   12.451  0.70 15.18 ?  24   VAL   A C    1 
ATOM   629  O  O    A VAL   A 1 24  ? 18.190 3.440   13.622  0.30 13.95 ?  24   VAL   A O    1 
ATOM   630  O  O    B VAL   A 1 24  ? 18.064 3.449   13.446  0.70 15.41 ?  24   VAL   A O    1 
ATOM   631  C  CB   A VAL   A 1 24  ? 17.743 5.073   10.672  0.30 13.44 ?  24   VAL   A CB   1 
ATOM   632  C  CB   B VAL   A 1 24  ? 17.784 4.826   10.411  0.70 15.41 ?  24   VAL   A CB   1 
ATOM   633  C  CG1  A VAL   A 1 24  ? 18.220 6.109   11.683  0.30 13.83 ?  24   VAL   A CG1  1 
ATOM   634  C  CG1  B VAL   A 1 24  ? 18.386 5.881   11.325  0.70 17.42 ?  24   VAL   A CG1  1 
ATOM   635  C  CG2  A VAL   A 1 24  ? 18.496 5.213   9.359   0.30 13.55 ?  24   VAL   A CG2  1 
ATOM   636  C  CG2  B VAL   A 1 24  ? 18.446 4.847   9.042   0.70 15.93 ?  24   VAL   A CG2  1 
ATOM   637  H  H    A VAL   A 1 24  ? 16.751 3.025   9.768   0.30 15.33 ?  24   VAL   A H    1 
ATOM   638  H  H    B VAL   A 1 24  ? 16.805 2.756   9.550   0.70 15.88 ?  24   VAL   A H    1 
ATOM   639  H  HA   A VAL   A 1 24  ? 18.860 3.453   11.249  0.30 16.04 ?  24   VAL   A HA   1 
ATOM   640  H  HA   B VAL   A 1 24  ? 18.853 3.221   11.115  0.70 17.27 ?  24   VAL   A HA   1 
ATOM   641  H  HB   A VAL   A 1 24  ? 16.803 5.237   10.498  0.30 16.15 ?  24   VAL   A HB   1 
ATOM   642  H  HB   B VAL   A 1 24  ? 16.843 5.034   10.291  0.70 18.52 ?  24   VAL   A HB   1 
ATOM   643  H  HG11 A VAL   A 1 24  ? 18.377 6.947   11.221  0.30 16.63 ?  24   VAL   A HG11 1 
ATOM   644  H  HG11 B VAL   A 1 24  ? 18.501 6.701   10.822  0.70 20.93 ?  24   VAL   A HG11 1 
ATOM   645  H  HG12 A VAL   A 1 24  ? 17.539 6.228   12.361  0.30 16.63 ?  24   VAL   A HG12 1 
ATOM   646  H  HG12 B VAL   A 1 24  ? 17.785 6.034   12.072  0.70 20.93 ?  24   VAL   A HG12 1 
ATOM   647  H  HG13 A VAL   A 1 24  ? 19.045 5.796   12.087  0.30 16.63 ?  24   VAL   A HG13 1 
ATOM   648  H  HG13 B VAL   A 1 24  ? 19.243 5.566   11.647  0.70 20.93 ?  24   VAL   A HG13 1 
ATOM   649  H  HG21 A VAL   A 1 24  ? 18.262 6.060   8.950   0.30 16.28 ?  24   VAL   A HG21 1 
ATOM   650  H  HG21 B VAL   A 1 24  ? 18.393 5.743   8.680   0.70 19.14 ?  24   VAL   A HG21 1 
ATOM   651  H  HG22 A VAL   A 1 24  ? 19.449 5.183   9.538   0.30 16.28 ?  24   VAL   A HG22 1 
ATOM   652  H  HG22 B VAL   A 1 24  ? 19.375 4.583   9.140   0.70 19.14 ?  24   VAL   A HG22 1 
ATOM   653  H  HG23 A VAL   A 1 24  ? 18.245 4.482   8.772   0.30 16.28 ?  24   VAL   A HG23 1 
ATOM   654  H  HG23 B VAL   A 1 24  ? 17.986 4.224   8.458   0.70 19.14 ?  24   VAL   A HG23 1 
ATOM   655  N  N    A GLU   A 1 25  ? 16.084 3.603   12.846  0.30 14.91 ?  25   GLU   A N    1 
ATOM   656  N  N    B GLU   A 1 25  ? 16.003 3.300   12.555  0.70 16.07 ?  25   GLU   A N    1 
ATOM   657  C  CA   A GLU   A 1 25  ? 15.514 3.518   14.186  0.30 16.35 ?  25   GLU   A CA   1 
ATOM   658  C  CA   B GLU   A 1 25  ? 15.367 3.222   13.866  0.70 17.20 ?  25   GLU   A CA   1 
ATOM   659  C  C    A GLU   A 1 25  ? 15.716 2.138   14.792  0.30 15.57 ?  25   GLU   A C    1 
ATOM   660  C  C    B GLU   A 1 25  ? 15.678 1.899   14.555  0.70 16.51 ?  25   GLU   A C    1 
ATOM   661  O  O    A GLU   A 1 25  ? 15.905 2.021   16.008  0.30 15.70 ?  25   GLU   A O    1 
ATOM   662  O  O    B GLU   A 1 25  ? 15.922 1.868   15.767  0.70 17.03 ?  25   GLU   A O    1 
ATOM   663  C  CB   A GLU   A 1 25  ? 14.030 3.886   14.152  0.30 18.70 ?  25   GLU   A CB   1 
ATOM   664  C  CB   B GLU   A 1 25  ? 13.858 3.446   13.734  0.70 19.39 ?  25   GLU   A CB   1 
ATOM   665  C  CG   A GLU   A 1 25  ? 13.779 5.330   13.746  0.30 20.93 ?  25   GLU   A CG   1 
ATOM   666  C  CG   B GLU   A 1 25  ? 13.493 4.858   13.297  0.70 23.09 ?  25   GLU   A CG   1 
ATOM   667  C  CD   A GLU   A 1 25  ? 14.572 6.327   14.581  0.30 22.72 ?  25   GLU   A CD   1 
ATOM   668  C  CD   B GLU   A 1 25  ? 14.099 5.912   14.194  0.70 26.25 ?  25   GLU   A CD   1 
ATOM   669  O  OE1  A GLU   A 1 25  ? 14.661 6.142   15.814  0.30 23.37 ?  25   GLU   A OE1  1 
ATOM   670  O  OE1  B GLU   A 1 25  ? 14.099 5.709   15.429  0.70 27.61 ?  25   GLU   A OE1  1 
ATOM   671  O  OE2  A GLU   A 1 25  ? 15.123 7.286   14.000  0.30 23.39 -1 25   GLU   A OE2  1 
ATOM   672  O  OE2  B GLU   A 1 25  ? 14.583 6.932   13.665  0.70 27.33 -1 25   GLU   A OE2  1 
ATOM   673  H  H    A GLU   A 1 25  ? 15.506 3.680   12.215  0.30 17.91 ?  25   GLU   A H    1 
ATOM   674  H  H    B GLU   A 1 25  ? 15.453 3.281   11.891  0.70 19.31 ?  25   GLU   A H    1 
ATOM   675  H  HA   A GLU   A 1 25  ? 15.968 4.152   14.760  0.30 19.64 ?  25   GLU   A HA   1 
ATOM   676  H  HA   B GLU   A 1 25  ? 15.724 3.924   14.427  0.70 20.67 ?  25   GLU   A HA   1 
ATOM   677  H  HB2  A GLU   A 1 25  ? 13.576 3.312   13.512  0.30 22.46 ?  25   GLU   A HB2  1 
ATOM   678  H  HB2  B GLU   A 1 25  ? 13.499 2.836   13.072  0.70 23.29 ?  25   GLU   A HB2  1 
ATOM   679  H  HB3  A GLU   A 1 25  ? 13.650 3.754   15.036  0.30 22.46 ?  25   GLU   A HB3  1 
ATOM   680  H  HB3  B GLU   A 1 25  ? 13.434 3.287   14.593  0.70 23.29 ?  25   GLU   A HB3  1 
ATOM   681  H  HG2  A GLU   A 1 25  ? 14.047 5.444   12.823  0.30 25.15 ?  25   GLU   A HG2  1 
ATOM   682  H  HG2  B GLU   A 1 25  ? 13.818 5.008   12.397  0.70 27.73 ?  25   GLU   A HG2  1 
ATOM   683  H  HG3  A GLU   A 1 25  ? 12.834 5.523   13.849  0.30 25.15 ?  25   GLU   A HG3  1 
ATOM   684  H  HG3  B GLU   A 1 25  ? 12.531 4.969   13.331  0.70 27.73 ?  25   GLU   A HG3  1 
ATOM   685  N  N    A GLU   A 1 26  ? 15.677 1.087   13.970  0.30 15.15 ?  26   GLU   A N    1 
ATOM   686  N  N    B GLU   A 1 26  ? 15.682 0.796   13.801  0.70 16.46 ?  26   GLU   A N    1 
ATOM   687  C  CA   A GLU   A 1 26  ? 15.999 -0.249  14.463  0.30 15.03 ?  26   GLU   A CA   1 
ATOM   688  C  CA   B GLU   A 1 26  ? 16.047 -0.492  14.386  0.70 16.40 ?  26   GLU   A CA   1 
ATOM   689  C  C    A GLU   A 1 26  ? 17.422 -0.294  15.004  0.30 14.31 ?  26   GLU   A C    1 
ATOM   690  C  C    B GLU   A 1 26  ? 17.465 -0.457  14.936  0.70 14.92 ?  26   GLU   A C    1 
ATOM   691  O  O    A GLU   A 1 26  ? 17.658 -0.732  16.135  0.30 14.34 ?  26   GLU   A O    1 
ATOM   692  O  O    B GLU   A 1 26  ? 17.737 -0.993  16.016  0.70 15.41 ?  26   GLU   A O    1 
ATOM   693  C  CB   A GLU   A 1 26  ? 15.823 -1.280  13.345  0.30 15.89 ?  26   GLU   A CB   1 
ATOM   694  C  CB   B GLU   A 1 26  ? 15.934 -1.601  13.339  0.70 18.16 ?  26   GLU   A CB   1 
ATOM   695  C  CG   A GLU   A 1 26  ? 14.420 -1.821  13.187  0.30 17.40 ?  26   GLU   A CG   1 
ATOM   696  C  CG   B GLU   A 1 26  ? 14.531 -2.076  13.055  0.70 19.98 ?  26   GLU   A CG   1 
ATOM   697  C  CD   A GLU   A 1 26  ? 14.012 -2.715  14.349  0.30 18.14 ?  26   GLU   A CD   1 
ATOM   698  C  CD   B GLU   A 1 26  ? 13.884 -2.729  14.257  0.70 20.94 ?  26   GLU   A CD   1 
ATOM   699  O  OE1  A GLU   A 1 26  ? 14.311 -3.933  14.323  0.30 18.79 ?  26   GLU   A OE1  1 
ATOM   700  O  OE1  B GLU   A 1 26  ? 14.461 -3.701  14.801  0.70 20.69 ?  26   GLU   A OE1  1 
ATOM   701  O  OE2  A GLU   A 1 26  ? 13.408 -2.191  15.300  0.30 17.86 -1 26   GLU   A OE2  1 
ATOM   702  O  OE2  B GLU   A 1 26  ? 12.805 -2.257  14.658  0.70 20.79 -1 26   GLU   A OE2  1 
ATOM   703  H  H    A GLU   A 1 26  ? 15.473 1.126   13.136  0.30 18.20 ?  26   GLU   A H    1 
ATOM   704  H  H    B GLU   A 1 26  ? 15.480 0.768   12.966  0.70 19.78 ?  26   GLU   A H    1 
ATOM   705  H  HA   A GLU   A 1 26  ? 15.393 -0.476  15.183  0.30 18.06 ?  26   GLU   A HA   1 
ATOM   706  H  HA   B GLU   A 1 26  ? 15.446 -0.696  15.115  0.70 19.70 ?  26   GLU   A HA   1 
ATOM   707  H  HB2  A GLU   A 1 26  ? 16.075 -0.870  12.502  0.30 19.09 ?  26   GLU   A HB2  1 
ATOM   708  H  HB2  B GLU   A 1 26  ? 16.308 -1.276  12.503  0.70 21.81 ?  26   GLU   A HB2  1 
ATOM   709  H  HB3  A GLU   A 1 26  ? 16.404 -2.034  13.526  0.30 19.09 ?  26   GLU   A HB3  1 
ATOM   710  H  HB3  B GLU   A 1 26  ? 16.448 -2.367  13.644  0.70 21.81 ?  26   GLU   A HB3  1 
ATOM   711  H  HG2  A GLU   A 1 26  ? 13.810 -1.066  13.118  0.30 20.91 ?  26   GLU   A HG2  1 
ATOM   712  H  HG2  B GLU   A 1 26  ? 13.993 -1.316  12.782  0.70 24.00 ?  26   GLU   A HG2  1 
ATOM   713  H  HG3  A GLU   A 1 26  ? 14.376 -2.354  12.380  0.30 20.91 ?  26   GLU   A HG3  1 
ATOM   714  H  HG3  B GLU   A 1 26  ? 14.556 -2.738  12.351  0.70 24.00 ?  26   GLU   A HG3  1 
ATOM   715  N  N    . ALA   A 1 27  ? 18.388 0.165   14.204  1.00 14.00 ?  27   ALA   A N    1 
ATOM   716  C  CA   . ALA   A 1 27  ? 19.775 0.176   14.654  1.00 13.86 ?  27   ALA   A CA   1 
ATOM   717  C  C    . ALA   A 1 27  ? 19.938 0.999   15.928  1.00 15.55 ?  27   ALA   A C    1 
ATOM   718  O  O    . ALA   A 1 27  ? 20.610 0.569   16.872  1.00 15.48 ?  27   ALA   A O    1 
ATOM   719  C  CB   . ALA   A 1 27  ? 20.687 0.693   13.540  1.00 13.09 ?  27   ALA   A CB   1 
ATOM   720  H  H    A ALA   A 1 27  ? 18.264 0.479   13.413  0.30 16.82 ?  27   ALA   A H    1 
ATOM   721  H  H    B ALA   A 1 27  ? 18.240 0.580   13.466  0.70 16.82 ?  27   ALA   A H    1 
ATOM   722  H  HA   . ALA   A 1 27  ? 20.041 -0.733  14.852  1.00 16.65 ?  27   ALA   A HA   1 
ATOM   723  H  HB1  . ALA   A 1 27  ? 21.606 0.690   13.857  1.00 15.73 ?  27   ALA   A HB1  1 
ATOM   724  H  HB2  . ALA   A 1 27  ? 20.607 0.109   12.767  1.00 15.73 ?  27   ALA   A HB2  1 
ATOM   725  H  HB3  . ALA   A 1 27  ? 20.423 1.594   13.302  1.00 15.73 ?  27   ALA   A HB3  1 
ATOM   726  N  N    A LYS   A 1 28  ? 19.320 2.179   15.993  0.30 18.27 ?  28   LYS   A N    1 
ATOM   727  N  N    B LYS   A 1 28  ? 19.317 2.181   15.972  0.70 16.74 ?  28   LYS   A N    1 
ATOM   728  C  CA   A LYS   A 1 28  ? 19.483 3.003   17.187  0.30 21.49 ?  28   LYS   A CA   1 
ATOM   729  C  CA   B LYS   A 1 28  ? 19.411 3.024   17.159  0.70 19.45 ?  28   LYS   A CA   1 
ATOM   730  C  C    A LYS   A 1 28  ? 18.906 2.347   18.434  0.30 22.76 ?  28   LYS   A C    1 
ATOM   731  C  C    B LYS   A 1 28  ? 18.848 2.315   18.383  0.70 20.26 ?  28   LYS   A C    1 
ATOM   732  O  O    A LYS   A 1 28  ? 19.326 2.686   19.546  0.30 23.26 ?  28   LYS   A O    1 
ATOM   733  O  O    B LYS   A 1 28  ? 19.421 2.399   19.475  0.70 21.67 ?  28   LYS   A O    1 
ATOM   734  C  CB   A LYS   A 1 28  ? 18.871 4.388   16.985  0.30 23.55 ?  28   LYS   A CB   1 
ATOM   735  C  CB   B LYS   A 1 28  ? 18.696 4.357   16.919  0.70 21.90 ?  28   LYS   A CB   1 
ATOM   736  C  CG   A LYS   A 1 28  ? 19.759 5.318   16.178  0.30 25.55 ?  28   LYS   A CG   1 
ATOM   737  C  CG   B LYS   A 1 28  ? 19.429 5.272   15.954  0.70 24.84 ?  28   LYS   A CG   1 
ATOM   738  C  CD   A LYS   A 1 28  ? 19.262 6.750   16.212  0.30 27.34 ?  28   LYS   A CD   1 
ATOM   739  C  CD   B LYS   A 1 28  ? 18.939 6.709   16.033  0.70 28.06 ?  28   LYS   A CD   1 
ATOM   740  C  CE   A LYS   A 1 28  ? 17.933 6.895   15.498  0.30 28.53 ?  28   LYS   A CE   1 
ATOM   741  C  CE   B LYS   A 1 28  ? 17.638 6.901   15.281  0.70 30.38 ?  28   LYS   A CE   1 
ATOM   742  N  NZ   A LYS   A 1 28  ? 17.508 8.319   15.421  0.30 29.29 ?  28   LYS   A NZ   1 
ATOM   743  N  NZ   B LYS   A 1 28  ? 17.285 8.343   15.161  0.70 31.61 ?  28   LYS   A NZ   1 
ATOM   744  H  H    A LYS   A 1 28  ? 18.819 2.513   15.384  0.30 21.95 ?  28   LYS   A H    1 
ATOM   745  H  H    B LYS   A 1 28  ? 18.841 2.508   15.340  0.70 20.11 ?  28   LYS   A H    1 
ATOM   746  H  HA   A LYS   A 1 28  ? 20.433 3.128   17.339  0.30 25.81 ?  28   LYS   A HA   1 
ATOM   747  H  HA   B LYS   A 1 28  ? 20.341 3.217   17.341  0.70 23.36 ?  28   LYS   A HA   1 
ATOM   748  H  HB2  A LYS   A 1 28  ? 18.029 4.290   16.516  0.30 28.29 ?  28   LYS   A HB2  1 
ATOM   749  H  HB2  B LYS   A 1 28  ? 17.819 4.183   16.547  0.70 26.31 ?  28   LYS   A HB2  1 
ATOM   750  H  HB3  A LYS   A 1 28  ? 18.721 4.794   17.855  0.30 28.29 ?  28   LYS   A HB3  1 
ATOM   751  H  HB3  B LYS   A 1 28  ? 18.611 4.827   17.762  0.70 26.31 ?  28   LYS   A HB3  1 
ATOM   752  H  HG2  A LYS   A 1 28  ? 20.657 5.299   16.546  0.30 30.68 ?  28   LYS   A HG2  1 
ATOM   753  H  HG2  B LYS   A 1 28  ? 20.375 5.265   16.165  0.70 29.83 ?  28   LYS   A HG2  1 
ATOM   754  H  HG3  A LYS   A 1 28  ? 19.770 5.022   15.255  0.30 30.68 ?  28   LYS   A HG3  1 
ATOM   755  H  HG3  B LYS   A 1 28  ? 19.287 4.957   15.047  0.70 29.83 ?  28   LYS   A HG3  1 
ATOM   756  H  HD2  A LYS   A 1 28  ? 19.144 7.026   17.135  0.30 32.83 ?  28   LYS   A HD2  1 
ATOM   757  H  HD2  B LYS   A 1 28  ? 18.790 6.947   16.963  0.70 33.69 ?  28   LYS   A HD2  1 
ATOM   758  H  HD3  A LYS   A 1 28  ? 19.909 7.323   15.772  0.30 32.83 ?  28   LYS   A HD3  1 
ATOM   759  H  HD3  B LYS   A 1 28  ? 19.605 7.296   15.642  0.70 33.69 ?  28   LYS   A HD3  1 
ATOM   760  H  HE2  A LYS   A 1 28  ? 18.018 6.552   14.594  0.30 34.26 ?  28   LYS   A HE2  1 
ATOM   761  H  HE2  B LYS   A 1 28  ? 17.729 6.535   14.387  0.70 36.47 ?  28   LYS   A HE2  1 
ATOM   762  H  HE3  A LYS   A 1 28  ? 17.253 6.401   15.982  0.30 34.26 ?  28   LYS   A HE3  1 
ATOM   763  H  HE3  B LYS   A 1 28  ? 16.924 6.451   15.758  0.70 36.47 ?  28   LYS   A HE3  1 
ATOM   764  H  HZ1  A LYS   A 1 28  ? 16.728 8.381   14.998  0.30 35.18 ?  28   LYS   A HZ1  1 
ATOM   765  H  HZ1  B LYS   A 1 28  ? 16.520 8.434   14.716  0.70 37.96 ?  28   LYS   A HZ1  1 
ATOM   766  H  HZ2  A LYS   A 1 28  ? 17.422 8.655   16.241  0.30 35.18 ?  28   LYS   A HZ2  1 
ATOM   767  H  HZ2  B LYS   A 1 28  ? 17.194 8.703   15.970  0.70 37.96 ?  28   LYS   A HZ2  1 
ATOM   768  H  HZ3  A LYS   A 1 28  ? 18.117 8.794   14.977  0.30 35.18 ?  28   LYS   A HZ3  1 
ATOM   769  H  HZ3  B LYS   A 1 28  ? 17.928 8.778   14.723  0.70 37.96 ?  28   LYS   A HZ3  1 
ATOM   770  N  N    A LYS   A 1 29  ? 17.958 1.422   18.282  0.30 23.78 ?  29   LYS   A N    1 
ATOM   771  N  N    B LYS   A 1 29  ? 17.735 1.599   18.217  0.70 20.76 ?  29   LYS   A N    1 
ATOM   772  C  CA   A LYS   A 1 29  ? 17.378 0.729   19.429  0.30 25.10 ?  29   LYS   A CA   1 
ATOM   773  C  CA   B LYS   A 1 29  ? 17.114 0.916   19.347  0.70 21.97 ?  29   LYS   A CA   1 
ATOM   774  C  C    A LYS   A 1 29  ? 18.189 -0.503  19.829  0.30 23.78 ?  29   LYS   A C    1 
ATOM   775  C  C    B LYS   A 1 29  ? 17.928 -0.300  19.772  0.70 20.47 ?  29   LYS   A C    1 
ATOM   776  O  O    A LYS   A 1 29  ? 18.482 -0.700  21.012  0.30 24.09 ?  29   LYS   A O    1 
ATOM   777  O  O    B LYS   A 1 29  ? 18.184 -0.504  20.965  0.70 21.52 ?  29   LYS   A O    1 
ATOM   778  C  CB   A LYS   A 1 29  ? 15.934 0.323   19.113  0.30 27.51 ?  29   LYS   A CB   1 
ATOM   779  C  CB   B LYS   A 1 29  ? 15.691 0.495   18.977  0.70 25.17 ?  29   LYS   A CB   1 
ATOM   780  C  CG   A LYS   A 1 29  ? 15.216 -0.402  20.246  0.30 29.82 ?  29   LYS   A CG   1 
ATOM   781  C  CG   B LYS   A 1 29  ? 14.947 -0.225  20.094  0.70 28.70 ?  29   LYS   A CG   1 
ATOM   782  C  CD   A LYS   A 1 29  ? 14.839 0.546   21.372  0.30 31.96 ?  29   LYS   A CD   1 
ATOM   783  C  CD   B LYS   A 1 29  ? 14.665 0.707   21.261  0.70 32.09 ?  29   LYS   A CD   1 
ATOM   784  C  CE   A LYS   A 1 29  ? 13.956 -0.144  22.401  0.30 33.35 ?  29   LYS   A CE   1 
ATOM   785  C  CE   B LYS   A 1 29  ? 13.905 0.002   22.372  0.70 34.18 ?  29   LYS   A CE   1 
ATOM   786  N  NZ   A LYS   A 1 29  ? 13.464 0.804   23.439  0.30 34.20 ?  29   LYS   A NZ   1 
ATOM   787  N  NZ   B LYS   A 1 29  ? 13.559 0.939   23.475  0.70 35.59 ?  29   LYS   A NZ   1 
ATOM   788  H  H    A LYS   A 1 29  ? 17.623 1.188   17.522  0.30 28.56 ?  29   LYS   A H    1 
ATOM   789  H  H    B LYS   A 1 29  ? 17.323 1.496   17.470  0.70 24.93 ?  29   LYS   A H    1 
ATOM   790  H  HA   A LYS   A 1 29  ? 17.357 1.336   20.184  0.30 30.14 ?  29   LYS   A HA   1 
ATOM   791  H  HA   B LYS   A 1 29  ? 17.061 1.523   20.102  0.70 26.39 ?  29   LYS   A HA   1 
ATOM   792  H  HB2  A LYS   A 1 29  ? 15.425 1.124   18.910  0.30 33.03 ?  29   LYS   A HB2  1 
ATOM   793  H  HB2  B LYS   A 1 29  ? 15.177 1.286   18.749  0.70 30.23 ?  29   LYS   A HB2  1 
ATOM   794  H  HB3  A LYS   A 1 29  ? 15.938 -0.265  18.343  0.30 33.03 ?  29   LYS   A HB3  1 
ATOM   795  H  HB3  B LYS   A 1 29  ? 15.727 -0.104  18.216  0.70 30.23 ?  29   LYS   A HB3  1 
ATOM   796  H  HG2  A LYS   A 1 29  ? 14.402 -0.797  19.900  0.30 35.80 ?  29   LYS   A HG2  1 
ATOM   797  H  HG2  B LYS   A 1 29  ? 14.097 -0.548  19.756  0.70 34.46 ?  29   LYS   A HG2  1 
ATOM   798  H  HG3  A LYS   A 1 29  ? 15.790 -1.095  20.611  0.30 35.80 ?  29   LYS   A HG3  1 
ATOM   799  H  HG3  B LYS   A 1 29  ? 15.478 -0.970  20.419  0.70 34.46 ?  29   LYS   A HG3  1 
ATOM   800  H  HD2  A LYS   A 1 29  ? 15.644 0.853   21.819  0.30 38.38 ?  29   LYS   A HD2  1 
ATOM   801  H  HD2  B LYS   A 1 29  ? 15.505 1.028   21.626  0.70 38.53 ?  29   LYS   A HD2  1 
ATOM   802  H  HD3  A LYS   A 1 29  ? 14.350 1.300   21.007  0.30 38.38 ?  29   LYS   A HD3  1 
ATOM   803  H  HD3  B LYS   A 1 29  ? 14.128 1.453   20.950  0.70 38.53 ?  29   LYS   A HD3  1 
ATOM   804  H  HE2  A LYS   A 1 29  ? 13.185 -0.528  21.953  0.30 40.04 ?  29   LYS   A HE2  1 
ATOM   805  H  HE2  B LYS   A 1 29  ? 13.082 -0.366  22.013  0.70 41.05 ?  29   LYS   A HE2  1 
ATOM   806  H  HE3  A LYS   A 1 29  ? 14.466 -0.840  22.844  0.30 40.04 ?  29   LYS   A HE3  1 
ATOM   807  H  HE3  B LYS   A 1 29  ? 14.458 -0.708  22.737  0.70 41.05 ?  29   LYS   A HE3  1 
ATOM   808  H  HZ1  A LYS   A 1 29  ? 12.950 0.373   24.025  0.30 41.07 ?  29   LYS   A HZ1  1 
ATOM   809  H  HZ1  B LYS   A 1 29  ? 13.115 0.506   24.113  0.70 42.73 ?  29   LYS   A HZ1  1 
ATOM   810  H  HZ2  A LYS   A 1 29  ? 14.152 1.168   23.870  0.30 41.07 ?  29   LYS   A HZ2  1 
ATOM   811  H  HZ2  B LYS   A 1 29  ? 14.301 1.287   23.822  0.70 42.73 ?  29   LYS   A HZ2  1 
ATOM   812  H  HZ3  A LYS   A 1 29  ? 12.986 1.451   23.058  0.30 41.07 ?  29   LYS   A HZ3  1 
ATOM   813  H  HZ3  B LYS   A 1 29  ? 13.048 1.598   23.163  0.70 42.73 ?  29   LYS   A HZ3  1 
ATOM   814  N  N    A VAL   A 1 30  ? 18.553 -1.338  18.856  0.30 22.48 ?  30   VAL   A N    1 
ATOM   815  N  N    B VAL   A 1 30  ? 18.331 -1.126  18.810  0.70 19.24 ?  30   VAL   A N    1 
ATOM   816  C  CA   A VAL   A 1 30  ? 19.193 -2.614  19.163  0.30 21.36 ?  30   VAL   A CA   1 
ATOM   817  C  CA   B VAL   A 1 30  ? 18.977 -2.393  19.129  0.70 18.29 ?  30   VAL   A CA   1 
ATOM   818  C  C    A VAL   A 1 30  ? 20.697 -2.457  19.374  0.30 20.14 ?  30   VAL   A C    1 
ATOM   819  C  C    B VAL   A 1 30  ? 20.480 -2.233  19.355  0.70 17.66 ?  30   VAL   A C    1 
ATOM   820  O  O    A VAL   A 1 30  ? 21.292 -3.170  20.191  0.30 20.24 ?  30   VAL   A O    1 
ATOM   821  O  O    B VAL   A 1 30  ? 21.063 -2.943  20.180  0.70 18.59 ?  30   VAL   A O    1 
ATOM   822  C  CB   A VAL   A 1 30  ? 18.885 -3.627  18.046  0.30 21.68 ?  30   VAL   A CB   1 
ATOM   823  C  CB   B VAL   A 1 30  ? 18.685 -3.413  18.013  0.70 19.03 ?  30   VAL   A CB   1 
ATOM   824  C  CG1  A VAL   A 1 30  ? 19.645 -4.928  18.268  0.30 21.81 ?  30   VAL   A CG1  1 
ATOM   825  C  CG1  B VAL   A 1 30  ? 19.455 -4.700  18.249  0.70 19.61 ?  30   VAL   A CG1  1 
ATOM   826  C  CG2  A VAL   A 1 30  ? 17.388 -3.887  17.962  0.30 21.93 ?  30   VAL   A CG2  1 
ATOM   827  C  CG2  B VAL   A 1 30  ? 17.189 -3.694  17.917  0.70 19.76 ?  30   VAL   A CG2  1 
ATOM   828  H  H    A VAL   A 1 30  ? 18.435 -1.191  18.018  0.30 27.00 ?  30   VAL   A H    1 
ATOM   829  H  H    B VAL   A 1 30  ? 18.235 -0.978  17.965  0.70 23.11 ?  30   VAL   A H    1 
ATOM   830  H  HA   A VAL   A 1 30  ? 18.808 -2.960  19.984  0.30 25.66 ?  30   VAL   A HA   1 
ATOM   831  H  HA   B VAL   A 1 30  ? 18.575 -2.742  19.944  0.70 21.97 ?  30   VAL   A HA   1 
ATOM   832  H  HB   A VAL   A 1 30  ? 19.174 -3.255  17.197  0.30 26.04 ?  30   VAL   A HB   1 
ATOM   833  H  HB   B VAL   A 1 30  ? 18.972 -3.045  17.162  0.70 22.86 ?  30   VAL   A HB   1 
ATOM   834  H  HG11 A VAL   A 1 30  ? 19.270 -5.612  17.690  0.30 26.20 ?  30   VAL   A HG11 1 
ATOM   835  H  HG11 B VAL   A 1 30  ? 19.085 -5.398  17.683  0.70 23.56 ?  30   VAL   A HG11 1 
ATOM   836  H  HG12 A VAL   A 1 30  ? 20.581 -4.793  18.051  0.30 26.20 ?  30   VAL   A HG12 1 
ATOM   837  H  HG12 B VAL   A 1 30  ? 20.387 -4.558  18.030  0.70 23.56 ?  30   VAL   A HG12 1 
ATOM   838  H  HG13 A VAL   A 1 30  ? 19.552 -5.194  19.195  0.30 26.20 ?  30   VAL   A HG13 1 
ATOM   839  H  HG13 B VAL   A 1 30  ? 19.364 -4.953  19.181  0.70 23.56 ?  30   VAL   A HG13 1 
ATOM   840  H  HG21 A VAL   A 1 30  ? 17.222 -4.556  17.280  0.30 26.34 ?  30   VAL   A HG21 1 
ATOM   841  H  HG21 B VAL   A 1 30  ? 17.036 -4.366  17.231  0.70 23.73 ?  30   VAL   A HG21 1 
ATOM   842  H  HG22 A VAL   A 1 30  ? 17.075 -4.207  18.823  0.30 26.34 ?  30   VAL   A HG22 1 
ATOM   843  H  HG22 B VAL   A 1 30  ? 16.875 -4.022  18.774  0.70 23.73 ?  30   VAL   A HG22 1 
ATOM   844  H  HG23 A VAL   A 1 30  ? 16.936 -3.060  17.731  0.30 26.34 ?  30   VAL   A HG23 1 
ATOM   845  H  HG23 B VAL   A 1 30  ? 16.727 -2.875  17.684  0.70 23.73 ?  30   VAL   A HG23 1 
ATOM   846  N  N    A LYS   A 1 31  ? 21.330 -1.539  18.653  0.30 19.19 ?  31   LYS   A N    1 
ATOM   847  N  N    B LYS   A 1 31  ? 21.115 -1.310  18.645  0.70 16.94 ?  31   LYS   A N    1 
ATOM   848  C  CA   A LYS   A 1 31  ? 22.782 -1.426  18.607  0.30 19.07 ?  31   LYS   A CA   1 
ATOM   849  C  CA   B LYS   A 1 31  ? 22.568 -1.197  18.608  0.70 17.46 ?  31   LYS   A CA   1 
ATOM   850  C  C    A LYS   A 1 31  ? 23.414 -2.780  18.267  0.30 16.60 ?  31   LYS   A C    1 
ATOM   851  C  C    B LYS   A 1 31  ? 23.207 -2.561  18.325  0.70 15.95 ?  31   LYS   A C    1 
ATOM   852  O  O    A LYS   A 1 31  ? 24.184 -3.331  19.058  0.30 16.36 ?  31   LYS   A O    1 
ATOM   853  O  O    B LYS   A 1 31  ? 23.972 -3.080  19.145  0.70 17.56 ?  31   LYS   A O    1 
ATOM   854  C  CB   A LYS   A 1 31  ? 23.352 -0.866  19.904  0.30 21.83 ?  31   LYS   A CB   1 
ATOM   855  C  CB   B LYS   A 1 31  ? 23.124 -0.579  19.883  0.70 21.25 ?  31   LYS   A CB   1 
ATOM   856  C  CG   A LYS   A 1 31  ? 22.651 0.391   20.402  0.30 24.79 ?  31   LYS   A CG   1 
ATOM   857  C  CG   B LYS   A 1 31  ? 22.447 0.724   20.283  0.70 26.03 ?  31   LYS   A CG   1 
ATOM   858  C  CD   A LYS   A 1 31  ? 23.649 1.420   20.913  0.30 27.15 ?  31   LYS   A CD   1 
ATOM   859  C  CD   B LYS   A 1 31  ? 23.430 1.675   20.945  0.70 29.78 ?  31   LYS   A CD   1 
ATOM   860  C  CE   A LYS   A 1 31  ? 22.981 2.463   21.798  0.30 28.59 ?  31   LYS   A CE   1 
ATOM   861  C  CE   B LYS   A 1 31  ? 22.716 2.736   21.767  0.70 32.33 ?  31   LYS   A CE   1 
ATOM   862  N  NZ   A LYS   A 1 31  ? 21.839 3.142   21.127  0.30 29.48 ?  31   LYS   A NZ   1 
ATOM   863  N  NZ   B LYS   A 1 31  ? 21.659 3.442   20.996  0.70 34.03 ?  31   LYS   A NZ   1 
ATOM   864  H  H    A LYS   A 1 31  ? 20.923 -0.961  18.169  0.30 23.06 ?  31   LYS   A H    1 
ATOM   865  H  H    B LYS   A 1 31  ? 20.701 -0.719  18.166  0.70 20.35 ?  31   LYS   A H    1 
ATOM   866  H  HA   A LYS   A 1 31  ? 23.009 -0.809  17.901  0.30 22.91 ?  31   LYS   A HA   1 
ATOM   867  H  HA   B LYS   A 1 31  ? 22.791 -0.606  17.879  0.70 20.98 ?  31   LYS   A HA   1 
ATOM   868  H  HB2  A LYS   A 1 31  ? 23.280 -1.539  20.595  0.30 26.22 ?  31   LYS   A HB2  1 
ATOM   869  H  HB2  B LYS   A 1 31  ? 23.009 -1.205  20.608  0.70 25.52 ?  31   LYS   A HB2  1 
ATOM   870  H  HB3  A LYS   A 1 31  ? 24.286 -0.643  19.758  0.30 26.22 ?  31   LYS   A HB3  1 
ATOM   871  H  HB3  B LYS   A 1 31  ? 24.065 -0.394  19.746  0.70 25.52 ?  31   LYS   A HB3  1 
ATOM   872  H  HG2  A LYS   A 1 31  ? 22.150 0.790   19.673  0.30 29.78 ?  31   LYS   A HG2  1 
ATOM   873  H  HG2  B LYS   A 1 31  ? 22.087 1.158   19.494  0.70 31.26 ?  31   LYS   A HG2  1 
ATOM   874  H  HG3  A LYS   A 1 31  ? 22.055 0.158   21.131  0.30 29.78 ?  31   LYS   A HG3  1 
ATOM   875  H  HG3  B LYS   A 1 31  ? 21.737 0.534   20.917  0.70 31.26 ?  31   LYS   A HG3  1 
ATOM   876  H  HD2  A LYS   A 1 31  ? 24.331 0.972   21.436  0.30 32.60 ?  31   LYS   A HD2  1 
ATOM   877  H  HD2  B LYS   A 1 31  ? 24.015 1.173   21.535  0.70 35.76 ?  31   LYS   A HD2  1 
ATOM   878  H  HD3  A LYS   A 1 31  ? 24.052 1.878   20.158  0.30 32.60 ?  31   LYS   A HD3  1 
ATOM   879  H  HD3  B LYS   A 1 31  ? 23.953 2.122   20.259  0.70 35.76 ?  31   LYS   A HD3  1 
ATOM   880  H  HE2  A LYS   A 1 31  ? 22.644 2.029   22.598  0.30 34.33 ?  31   LYS   A HE2  1 
ATOM   881  H  HE2  B LYS   A 1 31  ? 22.298 2.311   22.532  0.70 38.82 ?  31   LYS   A HE2  1 
ATOM   882  H  HE3  A LYS   A 1 31  ? 23.634 3.140   22.037  0.30 34.33 ?  31   LYS   A HE3  1 
ATOM   883  H  HE3  B LYS   A 1 31  ? 23.362 3.394   22.065  0.70 38.82 ?  31   LYS   A HE3  1 
ATOM   884  H  HZ1  A LYS   A 1 31  ? 21.488 3.754   21.670  0.30 35.40 ?  31   LYS   A HZ1  1 
ATOM   885  H  HZ1  B LYS   A 1 31  ? 21.291 4.078   21.498  0.70 40.87 ?  31   LYS   A HZ1  1 
ATOM   886  H  HZ2  A LYS   A 1 31  ? 22.118 3.542   20.382  0.30 35.40 ?  31   LYS   A HZ2  1 
ATOM   887  H  HZ2  B LYS   A 1 31  ? 22.011 3.815   20.269  0.70 40.87 ?  31   LYS   A HZ2  1 
ATOM   888  H  HZ3  A LYS   A 1 31  ? 21.211 2.547   20.918  0.30 35.40 ?  31   LYS   A HZ3  1 
ATOM   889  H  HZ3  B LYS   A 1 31  ? 21.026 2.867   20.748  0.70 40.87 ?  31   LYS   A HZ3  1 
ATOM   890  N  N    A PRO   A 1 32  ? 23.110 -3.332  17.095  0.30 15.35 ?  32   PRO   A N    1 
ATOM   891  N  N    B PRO   A 1 32  ? 22.918 -3.151  17.169  0.70 14.12 ?  32   PRO   A N    1 
ATOM   892  C  CA   A PRO   A 1 32  ? 23.592 -4.674  16.762  0.30 15.02 ?  32   PRO   A CA   1 
ATOM   893  C  CA   B PRO   A 1 32  ? 23.413 -4.496  16.865  0.70 14.55 ?  32   PRO   A CA   1 
ATOM   894  C  C    A PRO   A 1 32  ? 25.094 -4.693  16.536  0.30 14.36 ?  32   PRO   A C    1 
ATOM   895  C  C    B PRO   A 1 32  ? 24.919 -4.503  16.663  0.70 14.76 ?  32   PRO   A C    1 
ATOM   896  O  O    A PRO   A 1 32  ? 25.730 -3.672  16.263  0.30 13.89 ?  32   PRO   A O    1 
ATOM   897  O  O    B PRO   A 1 32  ? 25.570 -3.469  16.502  0.70 15.40 ?  32   PRO   A O    1 
ATOM   898  C  CB   A PRO   A 1 32  ? 22.850 -4.996  15.461  0.30 15.41 ?  32   PRO   A CB   1 
ATOM   899  C  CB   B PRO   A 1 32  ? 22.692 -4.830  15.556  0.70 14.72 ?  32   PRO   A CB   1 
ATOM   900  C  CG   A PRO   A 1 32  ? 22.645 -3.662  14.826  0.30 15.25 ?  32   PRO   A CG   1 
ATOM   901  C  CG   B PRO   A 1 32  ? 22.520 -3.496  14.894  0.70 13.43 ?  32   PRO   A CG   1 
ATOM   902  C  CD   A PRO   A 1 32  ? 22.386 -2.714  15.970  0.30 15.13 ?  32   PRO   A CD   1 
ATOM   903  C  CD   B PRO   A 1 32  ? 22.192 -2.562  16.030  0.70 13.28 ?  32   PRO   A CD   1 
ATOM   904  H  HA   A PRO   A 1 32  ? 23.344 -5.313  17.451  0.30 18.05 ?  32   PRO   A HA   1 
ATOM   905  H  HA   B PRO   A 1 32  ? 23.151 -5.123  17.557  0.70 17.48 ?  32   PRO   A HA   1 
ATOM   906  H  HB2  A PRO   A 1 32  ? 23.401 -5.566  14.900  0.30 18.51 ?  32   PRO   A HB2  1 
ATOM   907  H  HB2  B PRO   A 1 32  ? 23.245 -5.418  15.016  0.70 17.69 ?  32   PRO   A HB2  1 
ATOM   908  H  HB3  A PRO   A 1 32  ? 22.001 -5.422  15.658  0.30 18.51 ?  32   PRO   A HB3  1 
ATOM   909  H  HB3  B PRO   A 1 32  ? 21.830 -5.239  15.741  0.70 17.69 ?  32   PRO   A HB3  1 
ATOM   910  H  HG2  A PRO   A 1 32  ? 23.445 -3.408  14.340  0.30 18.33 ?  32   PRO   A HG2  1 
ATOM   911  H  HG2  B PRO   A 1 32  ? 23.345 -3.240  14.456  0.70 16.14 ?  32   PRO   A HG2  1 
ATOM   912  H  HG3  A PRO   A 1 32  ? 21.881 -3.702  14.228  0.30 18.33 ?  32   PRO   A HG3  1 
ATOM   913  H  HG3  B PRO   A 1 32  ? 21.790 -3.543  14.252  0.70 16.14 ?  32   PRO   A HG3  1 
ATOM   914  H  HD2  A PRO   A 1 32  ? 22.753 -1.839  15.764  0.30 18.18 ?  32   PRO   A HD2  1 
ATOM   915  H  HD2  B PRO   A 1 32  ? 22.520 -1.671  15.823  0.70 15.96 ?  32   PRO   A HD2  1 
ATOM   916  H  HD3  A PRO   A 1 32  ? 21.435 -2.666  16.154  0.30 18.18 ?  32   PRO   A HD3  1 
ATOM   917  H  HD3  B PRO   A 1 32  ? 21.232 -2.556  16.184  0.70 15.96 ?  32   PRO   A HD3  1 
ATOM   918  N  N    A THR   A 1 33  ? 25.658 -5.897  16.635  0.30 14.22 ?  33   THR   A N    1 
ATOM   919  N  N    B THR   A 1 33  ? 25.471 -5.716  16.643  0.70 14.65 ?  33   THR   A N    1 
ATOM   920  C  CA   A THR   A 1 33  ? 27.062 -6.071  16.293  0.30 14.49 ?  33   THR   A CA   1 
ATOM   921  C  CA   B THR   A 1 33  ? 26.889 -5.869  16.348  0.70 14.77 ?  33   THR   A CA   1 
ATOM   922  C  C    A THR   A 1 33  ? 27.335 -5.625  14.864  0.30 13.55 ?  33   THR   A C    1 
ATOM   923  C  C    B THR   A 1 33  ? 27.208 -5.423  14.923  0.70 13.69 ?  33   THR   A C    1 
ATOM   924  O  O    A THR   A 1 33  ? 28.415 -5.094  14.577  0.30 13.38 ?  33   THR   A O    1 
ATOM   925  O  O    B THR   A 1 33  ? 28.213 -4.738  14.689  0.70 13.78 ?  33   THR   A O    1 
ATOM   926  C  CB   A THR   A 1 33  ? 27.465 -7.535  16.481  0.30 15.96 ?  33   THR   A CB   1 
ATOM   927  C  CB   B THR   A 1 33  ? 27.300 -7.323  16.570  0.70 16.69 ?  33   THR   A CB   1 
ATOM   928  O  OG1  A THR   A 1 33  ? 27.210 -7.937  17.832  0.30 17.03 ?  33   THR   A OG1  1 
ATOM   929  O  OG1  B THR   A 1 33  ? 26.979 -7.705  17.912  0.70 18.11 ?  33   THR   A OG1  1 
ATOM   930  C  CG2  A THR   A 1 33  ? 28.942 -7.732  16.179  0.30 16.27 ?  33   THR   A CG2  1 
ATOM   931  C  CG2  B THR   A 1 33  ? 28.793 -7.505  16.336  0.70 17.44 ?  33   THR   A CG2  1 
ATOM   932  H  H    A THR   A 1 33  ? 25.254 -6.612  16.881  0.30 17.09 ?  33   THR   A H    1 
ATOM   933  H  H    B THR   A 1 33  ? 25.046 -6.448  16.794  0.70 17.61 ?  33   THR   A H    1 
ATOM   934  H  HA   A THR   A 1 33  ? 27.603 -5.528  16.889  0.30 17.41 ?  33   THR   A HA   1 
ATOM   935  H  HA   B THR   A 1 33  ? 27.397 -5.314  16.960  0.70 17.75 ?  33   THR   A HA   1 
ATOM   936  H  HB   A THR   A 1 33  ? 26.948 -8.090  15.875  0.30 19.18 ?  33   THR   A HB   1 
ATOM   937  H  HB   B THR   A 1 33  ? 26.818 -7.894  15.950  0.70 20.06 ?  33   THR   A HB   1 
ATOM   938  H  HG1  A THR   A 1 33  ? 27.644 -7.450  18.362  0.30 20.46 ?  33   THR   A HG1  1 
ATOM   939  H  HG1  B THR   A 1 33  ? 27.391 -7.216  18.459  0.70 21.76 ?  33   THR   A HG1  1 
ATOM   940  H  HG21 A THR   A 1 33  ? 29.217 -8.620  16.456  0.30 19.55 ?  33   THR   A HG21 1 
ATOM   941  H  HG21 B THR   A 1 33  ? 29.069 -8.385  16.634  0.70 20.95 ?  33   THR   A HG21 1 
ATOM   942  H  HG22 A THR   A 1 33  ? 29.106 -7.634  15.229  0.30 19.55 ?  33   THR   A HG22 1 
ATOM   943  H  HG22 B THR   A 1 33  ? 28.995 -7.414  15.392  0.70 20.95 ?  33   THR   A HG22 1 
ATOM   944  H  HG23 A THR   A 1 33  ? 29.468 -7.076  16.662  0.30 19.55 ?  33   THR   A HG23 1 
ATOM   945  H  HG23 B THR   A 1 33  ? 29.288 -6.834  16.832  0.70 20.95 ?  33   THR   A HG23 1 
ATOM   946  N  N    . VAL   A 1 34  ? 26.373 -5.820  13.959  1.00 12.60 ?  34   VAL   A N    1 
ATOM   947  C  CA   . VAL   A 1 34  ? 26.552 -5.480  12.549  1.00 11.82 ?  34   VAL   A CA   1 
ATOM   948  C  C    . VAL   A 1 34  ? 25.251 -4.934  11.977  1.00 11.06 ?  34   VAL   A C    1 
ATOM   949  O  O    . VAL   A 1 34  ? 24.217 -5.612  12.018  1.00 11.71 ?  34   VAL   A O    1 
ATOM   950  C  CB   . VAL   A 1 34  ? 27.013 -6.690  11.707  1.00 12.66 ?  34   VAL   A CB   1 
ATOM   951  C  CG1  . VAL   A 1 34  ? 27.211 -6.285  10.257  1.00 12.81 ?  34   VAL   A CG1  1 
ATOM   952  C  CG2  . VAL   A 1 34  ? 28.288 -7.317  12.267  1.00 14.03 ?  34   VAL   A CG2  1 
ATOM   953  H  H    A VAL   A 1 34  ? 25.607 -6.169  14.141  0.30 15.14 ?  34   VAL   A H    1 
ATOM   954  H  H    B VAL   A 1 34  ? 25.681 -6.312  14.104  0.70 15.14 ?  34   VAL   A H    1 
ATOM   955  H  HA   . VAL   A 1 34  ? 27.225 -4.787  12.471  1.00 14.20 ?  34   VAL   A HA   1 
ATOM   956  H  HB   . VAL   A 1 34  ? 26.316 -7.366  11.731  1.00 15.22 ?  34   VAL   A HB   1 
ATOM   957  H  HG11 . VAL   A 1 34  ? 27.695 -6.989  9.797   1.00 15.39 ?  34   VAL   A HG11 1 
ATOM   958  H  HG12 . VAL   A 1 34  ? 26.349 -6.148  9.840   1.00 15.39 ?  34   VAL   A HG12 1 
ATOM   959  H  HG13 . VAL   A 1 34  ? 27.729 -5.461  10.229  1.00 15.39 ?  34   VAL   A HG13 1 
ATOM   960  H  HG21 . VAL   A 1 34  ? 28.575 -8.030  11.669  1.00 16.86 ?  34   VAL   A HG21 1 
ATOM   961  H  HG22 . VAL   A 1 34  ? 28.976 -6.639  12.325  1.00 16.86 ?  34   VAL   A HG22 1 
ATOM   962  H  HG23 . VAL   A 1 34  ? 28.103 -7.682  13.145  1.00 16.86 ?  34   VAL   A HG23 1 
ATOM   963  N  N    . VAL   A 1 35  ? 25.316 -3.732  11.397  1.00 10.51 ?  35   VAL   A N    1 
ATOM   964  C  CA   . VAL   A 1 35  ? 24.276 -3.224  10.513  1.00 10.15 ?  35   VAL   A CA   1 
ATOM   965  C  C    . VAL   A 1 35  ? 24.825 -3.223  9.093   1.00 9.53  ?  35   VAL   A C    1 
ATOM   966  O  O    . VAL   A 1 35  ? 25.968 -2.815  8.862   1.00 10.38 ?  35   VAL   A O    1 
ATOM   967  C  CB   . VAL   A 1 35  ? 23.745 -1.834  10.931  1.00 10.87 ?  35   VAL   A CB   1 
ATOM   968  C  CG1  . VAL   A 1 35  ? 24.806 -0.737  10.787  1.00 11.45 ?  35   VAL   A CG1  1 
ATOM   969  C  CG2  . VAL   A 1 35  ? 22.495 -1.482  10.134  1.00 11.49 ?  35   VAL   A CG2  1 
ATOM   970  H  H    . VAL   A 1 35  ? 25.971 -3.185  11.501  1.00 12.64 ?  35   VAL   A H    1 
ATOM   971  H  HA   . VAL   A 1 35  ? 23.523 -3.836  10.536  1.00 12.20 ?  35   VAL   A HA   1 
ATOM   972  H  HB   . VAL   A 1 35  ? 23.490 -1.867  11.863  1.00 13.07 ?  35   VAL   A HB   1 
ATOM   973  H  HG11 . VAL   A 1 35  ? 24.463 0.090   11.168  1.00 13.76 ?  35   VAL   A HG11 1 
ATOM   974  H  HG12 . VAL   A 1 35  ? 25.608 -1.008  11.261  1.00 13.76 ?  35   VAL   A HG12 1 
ATOM   975  H  HG13 . VAL   A 1 35  ? 25.007 -0.604  9.847   1.00 13.76 ?  35   VAL   A HG13 1 
ATOM   976  H  HG21 . VAL   A 1 35  ? 22.148 -0.631  10.443  1.00 13.82 ?  35   VAL   A HG21 1 
ATOM   977  H  HG22 . VAL   A 1 35  ? 22.725 -1.420  9.191   1.00 13.82 ?  35   VAL   A HG22 1 
ATOM   978  H  HG23 . VAL   A 1 35  ? 21.831 -2.177  10.265  1.00 13.82 ?  35   VAL   A HG23 1 
ATOM   979  N  N    . VAL   A 1 36  ? 24.015 -3.688  8.147   1.00 9.26  ?  36   VAL   A N    1 
ATOM   980  C  CA   . VAL   A 1 36  ? 24.384 -3.697  6.739   1.00 8.85  ?  36   VAL   A CA   1 
ATOM   981  C  C    . VAL   A 1 36  ? 23.922 -2.405  6.076   1.00 9.08  ?  36   VAL   A C    1 
ATOM   982  O  O    . VAL   A 1 36  ? 22.763 -1.995  6.228   1.00 9.84  ?  36   VAL   A O    1 
ATOM   983  C  CB   . VAL   A 1 36  ? 23.777 -4.915  6.024   1.00 9.00  ?  36   VAL   A CB   1 
ATOM   984  C  CG1  . VAL   A 1 36  ? 24.041 -4.845  4.534   1.00 9.94  ?  36   VAL   A CG1  1 
ATOM   985  C  CG2  . VAL   A 1 36  ? 24.325 -6.199  6.601   1.00 9.86  ?  36   VAL   A CG2  1 
ATOM   986  H  H    . VAL   A 1 36  ? 23.224 -4.008  8.301   1.00 11.13 ?  36   VAL   A H    1 
ATOM   987  H  HA   . VAL   A 1 36  ? 25.352 -3.757  6.670   1.00 10.64 ?  36   VAL   A HA   1 
ATOM   988  H  HB   . VAL   A 1 36  ? 22.818 -4.908  6.156   1.00 10.82 ?  36   VAL   A HB   1 
ATOM   989  H  HG11 . VAL   A 1 36  ? 23.893 -5.721  4.146   1.00 11.95 ?  36   VAL   A HG11 1 
ATOM   990  H  HG12 . VAL   A 1 36  ? 23.441 -4.199  4.129   1.00 11.95 ?  36   VAL   A HG12 1 
ATOM   991  H  HG13 . VAL   A 1 36  ? 24.965 -4.575  4.388   1.00 11.95 ?  36   VAL   A HG13 1 
ATOM   992  H  HG21 . VAL   A 1 36  ? 23.935 -6.954  6.125   1.00 11.86 ?  36   VAL   A HG21 1 
ATOM   993  H  HG22 . VAL   A 1 36  ? 25.289 -6.212  6.501   1.00 11.86 ?  36   VAL   A HG22 1 
ATOM   994  H  HG23 . VAL   A 1 36  ? 24.090 -6.255  7.543   1.00 11.86 ?  36   VAL   A HG23 1 
ATOM   995  N  N    . ASN   A 1 37  ? 24.828 -1.773  5.327   1.00 8.79  ?  37   ASN   A N    1 
ATOM   996  C  CA   . ASN   A 1 37  ? 24.492 -0.667  4.448   1.00 8.88  ?  37   ASN   A CA   1 
ATOM   997  C  C    . ASN   A 1 37  ? 24.365 -1.150  3.013   1.00 8.84  ?  37   ASN   A C    1 
ATOM   998  O  O    . ASN   A 1 37  ? 25.162 -1.975  2.543   1.00 9.31  ?  37   ASN   A O    1 
ATOM   999  C  CB   . ASN   A 1 37  ? 25.562 0.420   4.524   1.00 9.04  ?  37   ASN   A CB   1 
ATOM   1000 C  CG   . ASN   A 1 37  ? 25.222 1.622   3.672   1.00 9.44  ?  37   ASN   A CG   1 
ATOM   1001 O  OD1  . ASN   A 1 37  ? 24.045 1.940   3.468   1.00 10.13 ?  37   ASN   A OD1  1 
ATOM   1002 N  ND2  . ASN   A 1 37  ? 26.246 2.286   3.155   1.00 9.52  ?  37   ASN   A ND2  1 
ATOM   1003 H  H    . ASN   A 1 37  ? 25.670 -1.976  5.318   1.00 10.57 ?  37   ASN   A H    1 
ATOM   1004 H  HA   . ASN   A 1 37  ? 23.650 -0.283  4.725   1.00 10.68 ?  37   ASN   A HA   1 
ATOM   1005 H  HB2  . ASN   A 1 37  ? 25.646 0.720   5.443   1.00 10.87 ?  37   ASN   A HB2  1 
ATOM   1006 H  HB3  . ASN   A 1 37  ? 26.409 0.057   4.215   1.00 10.87 ?  37   ASN   A HB3  1 
ATOM   1007 H  HD21 . ASN   A 1 37  ? 26.106 2.973   2.655   1.00 11.44 ?  37   ASN   A HD21 1 
ATOM   1008 H  HD22 . ASN   A 1 37  ? 27.049 2.033   3.307   1.00 11.44 ?  37   ASN   A HD22 1 
ATOM   1009 N  N    A ALA   A 1 38  ? 23.333 -0.637  2.339   0.30 8.91  ?  38   ALA   A N    1 
ATOM   1010 N  N    B ALA   A 1 38  ? 23.345 -0.646  2.317   0.70 9.43  ?  38   ALA   A N    1 
ATOM   1011 C  CA   A ALA   A 1 38  ? 23.142 -0.766  0.897   0.30 8.98  ?  38   ALA   A CA   1 
ATOM   1012 C  CA   B ALA   A 1 38  ? 23.176 -0.876  0.881   0.70 10.01 ?  38   ALA   A CA   1 
ATOM   1013 C  C    A ALA   A 1 38  ? 24.052 0.254   0.219   0.30 9.24  ?  38   ALA   A C    1 
ATOM   1014 C  C    B ALA   A 1 38  ? 24.013 0.159   0.126   0.70 9.44  ?  38   ALA   A C    1 
ATOM   1015 O  O    A ALA   A 1 38  ? 23.656 1.377   -0.106  0.30 9.12  ?  38   ALA   A O    1 
ATOM   1016 O  O    B ALA   A 1 38  ? 23.530 1.196   -0.341  0.70 9.69  ?  38   ALA   A O    1 
ATOM   1017 C  CB   A ALA   A 1 38  ? 21.680 -0.522  0.541   0.30 9.32  ?  38   ALA   A CB   1 
ATOM   1018 C  CB   B ALA   A 1 38  ? 21.703 -0.827  0.499   0.70 11.45 ?  38   ALA   A CB   1 
ATOM   1019 H  H    A ALA   A 1 38  ? 22.706 -0.184  2.720   0.30 10.72 ?  38   ALA   A H    1 
ATOM   1020 H  H    B ALA   A 1 38  ? 22.728 -0.155  2.666   0.70 11.34 ?  38   ALA   A H    1 
ATOM   1021 H  HA   A ALA   A 1 38  ? 23.392 -1.654  0.610   0.30 10.80 ?  38   ALA   A HA   1 
ATOM   1022 H  HA   B ALA   A 1 38  ? 23.513 -1.761  0.666   0.70 12.03 ?  38   ALA   A HA   1 
ATOM   1023 H  HB1  A ALA   A 1 38  ? 21.573 -0.596  -0.419  0.30 11.20 ?  38   ALA   A HB1  1 
ATOM   1024 H  HB1  B ALA   A 1 38  ? 21.623 -0.987  -0.454  0.70 13.76 ?  38   ALA   A HB1  1 
ATOM   1025 H  HB2  A ALA   A 1 38  ? 21.130 -1.185  0.989   0.30 11.20 ?  38   ALA   A HB2  1 
ATOM   1026 H  HB2  B ALA   A 1 38  ? 21.223 -1.513  0.991   0.70 13.76 ?  38   ALA   A HB2  1 
ATOM   1027 H  HB3  A ALA   A 1 38  ? 21.426 0.369   0.834   0.30 11.20 ?  38   ALA   A HB3  1 
ATOM   1028 H  HB3  B ALA   A 1 38  ? 21.349 0.048   0.720   0.70 13.76 ?  38   ALA   A HB3  1 
ATOM   1029 N  N    . ALA   A 1 39  ? 25.305 -0.144  0.018   1.00 9.96  ?  39   ALA   A N    1 
ATOM   1030 C  CA   . ALA   A 1 39  ? 26.325 0.769   -0.477  1.00 9.66  ?  39   ALA   A CA   1 
ATOM   1031 C  C    . ALA   A 1 39  ? 26.465 0.705   -1.994  1.00 9.50  ?  39   ALA   A C    1 
ATOM   1032 O  O    . ALA   A 1 39  ? 26.032 -0.243  -2.651  1.00 10.08 ?  39   ALA   A O    1 
ATOM   1033 C  CB   . ALA   A 1 39  ? 27.668 0.420   0.173   1.00 10.48 ?  39   ALA   A CB   1 
ATOM   1034 H  H    A ALA   A 1 39  ? 25.589 -0.945  0.170   0.30 11.98 ?  39   ALA   A H    1 
ATOM   1035 H  H    B ALA   A 1 39  ? 25.626 -0.914  0.241   0.70 11.98 ?  39   ALA   A H    1 
ATOM   1036 H  HA   . ALA   A 1 39  ? 26.086 1.675   -0.227  1.00 11.62 ?  39   ALA   A HA   1 
ATOM   1037 H  HB1  . ALA   A 1 39  ? 28.341 1.034   -0.156  1.00 12.60 ?  39   ALA   A HB1  1 
ATOM   1038 H  HB2  . ALA   A 1 39  ? 27.580 0.515   1.139   1.00 12.60 ?  39   ALA   A HB2  1 
ATOM   1039 H  HB3  . ALA   A 1 39  ? 27.901 -0.489  -0.050  1.00 12.60 ?  39   ALA   A HB3  1 
ATOM   1040 N  N    . ASN   A 1 40  ? 27.112 1.733   -2.548  1.00 9.97  ?  40   ASN   A N    1 
ATOM   1041 C  CA   . ASN   A 1 40  ? 27.642 1.693   -3.906  1.00 10.44 ?  40   ASN   A CA   1 
ATOM   1042 C  C    . ASN   A 1 40  ? 29.168 1.582   -3.855  1.00 10.02 ?  40   ASN   A C    1 
ATOM   1043 O  O    . ASN   A 1 40  ? 29.776 1.699   -2.793  1.00 9.88  ?  40   ASN   A O    1 
ATOM   1044 C  CB   . ASN   A 1 40  ? 27.159 2.883   -4.754  1.00 10.82 ?  40   ASN   A CB   1 
ATOM   1045 C  CG   . ASN   A 1 40  ? 27.515 4.222   -4.157  1.00 11.53 ?  40   ASN   A CG   1 
ATOM   1046 O  OD1  . ASN   A 1 40  ? 28.692 4.518   -3.929  1.00 12.62 ?  40   ASN   A OD1  1 
ATOM   1047 N  ND2  . ASN   A 1 40  ? 26.504 5.052   -3.919  1.00 12.77 ?  40   ASN   A ND2  1 
ATOM   1048 H  H    . ASN   A 1 40  ? 27.266 2.477   -2.147  1.00 11.98 ?  40   ASN   A H    1 
ATOM   1049 H  HA   . ASN   A 1 40  ? 27.312 0.888   -4.337  1.00 12.56 ?  40   ASN   A HA   1 
ATOM   1050 H  HB2  . ASN   A 1 40  ? 27.563 2.825   -5.636  1.00 13.01 ?  40   ASN   A HB2  1 
ATOM   1051 H  HB3  . ASN   A 1 40  ? 26.193 2.835   -4.835  1.00 13.01 ?  40   ASN   A HB3  1 
ATOM   1052 H  HD21 . ASN   A 1 40  ? 26.658 5.834   -3.591  1.00 15.35 ?  40   ASN   A HD21 1 
ATOM   1053 H  HD22 . ASN   A 1 40  ? 25.699 4.814   -4.101  1.00 15.35 ?  40   ASN   A HD22 1 
ATOM   1054 N  N    . VAL   A 1 41  ? 29.786 1.343   -5.015  1.00 10.41 ?  41   VAL   A N    1 
ATOM   1055 C  CA   . VAL   A 1 41  ? 31.215 1.038   -5.040  1.00 10.81 ?  41   VAL   A CA   1 
ATOM   1056 C  C    . VAL   A 1 41  ? 32.069 2.196   -4.556  1.00 10.42 ?  41   VAL   A C    1 
ATOM   1057 O  O    . VAL   A 1 41  ? 33.214 1.982   -4.138  1.00 11.38 ?  41   VAL   A O    1 
ATOM   1058 C  CB   . VAL   A 1 41  ? 31.701 0.567   -6.430  1.00 11.99 ?  41   VAL   A CB   1 
ATOM   1059 C  CG1  . VAL   A 1 41  ? 31.019 -0.732  -6.836  1.00 12.82 ?  41   VAL   A CG1  1 
ATOM   1060 C  CG2  . VAL   A 1 41  ? 31.534 1.645   -7.490  1.00 12.80 ?  41   VAL   A CG2  1 
ATOM   1061 H  H    . VAL   A 1 41  ? 29.403 1.340   -5.786  1.00 12.52 ?  41   VAL   A H    1 
ATOM   1062 H  HA   . VAL   A 1 41  ? 31.372 0.299   -4.429  1.00 13.00 ?  41   VAL   A HA   1 
ATOM   1063 H  HB   . VAL   A 1 41  ? 32.648 0.376   -6.368  1.00 14.41 ?  41   VAL   A HB   1 
ATOM   1064 H  HG11 . VAL   A 1 41  ? 31.361 -1.016  -7.700  1.00 15.41 ?  41   VAL   A HG11 1 
ATOM   1065 H  HG12 . VAL   A 1 41  ? 31.209 -1.413  -6.169  1.00 15.41 ?  41   VAL   A HG12 1 
ATOM   1066 H  HG13 . VAL   A 1 41  ? 30.061 -0.587  -6.893  1.00 15.41 ?  41   VAL   A HG13 1 
ATOM   1067 H  HG21 . VAL   A 1 41  ? 31.767 1.272   -8.357  1.00 15.38 ?  41   VAL   A HG21 1 
ATOM   1068 H  HG22 . VAL   A 1 41  ? 30.612 1.942   -7.496  1.00 15.38 ?  41   VAL   A HG22 1 
ATOM   1069 H  HG23 . VAL   A 1 41  ? 32.123 2.386   -7.281  1.00 15.38 ?  41   VAL   A HG23 1 
ATOM   1070 N  N    . TYR   A 1 42  ? 31.561 3.425   -4.630  1.00 10.54 ?  42   TYR   A N    1 
ATOM   1071 C  CA   . TYR   A 1 42  ? 32.290 4.616   -4.216  1.00 10.57 ?  42   TYR   A CA   1 
ATOM   1072 C  C    . TYR   A 1 42  ? 32.033 4.986   -2.764  1.00 10.11 ?  42   TYR   A C    1 
ATOM   1073 O  O    . TYR   A 1 42  ? 32.601 5.972   -2.275  1.00 11.11 ?  42   TYR   A O    1 
ATOM   1074 C  CB   . TYR   A 1 42  ? 31.927 5.800   -5.135  1.00 11.46 ?  42   TYR   A CB   1 
ATOM   1075 C  CG   . TYR   A 1 42  ? 32.109 5.498   -6.610  1.00 11.94 ?  42   TYR   A CG   1 
ATOM   1076 C  CD1  . TYR   A 1 42  ? 33.372 5.312   -7.147  1.00 12.71 ?  42   TYR   A CD1  1 
ATOM   1077 C  CD2  . TYR   A 1 42  ? 31.020 5.364   -7.455  1.00 13.36 ?  42   TYR   A CD2  1 
ATOM   1078 C  CE1  . TYR   A 1 42  ? 33.544 5.012   -8.486  1.00 13.30 ?  42   TYR   A CE1  1 
ATOM   1079 C  CE2  . TYR   A 1 42  ? 31.187 5.077   -8.799  1.00 14.41 ?  42   TYR   A CE2  1 
ATOM   1080 C  CZ   . TYR   A 1 42  ? 32.452 4.900   -9.311  1.00 14.19 ?  42   TYR   A CZ   1 
ATOM   1081 O  OH   . TYR   A 1 42  ? 32.615 4.607   -10.645 1.00 15.88 ?  42   TYR   A OH   1 
ATOM   1082 H  H    . TYR   A 1 42  ? 30.776 3.596   -4.936  1.00 12.67 ?  42   TYR   A H    1 
ATOM   1083 H  HA   . TYR   A 1 42  ? 33.238 4.456   -4.313  1.00 12.71 ?  42   TYR   A HA   1 
ATOM   1084 H  HB2  . TYR   A 1 42  ? 30.996 6.038   -4.991  1.00 13.77 ?  42   TYR   A HB2  1 
ATOM   1085 H  HB3  . TYR   A 1 42  ? 32.495 6.557   -4.913  1.00 13.77 ?  42   TYR   A HB3  1 
ATOM   1086 H  HD1  . TYR   A 1 42  ? 34.117 5.380   -6.594  1.00 15.27 ?  42   TYR   A HD1  1 
ATOM   1087 H  HD2  . TYR   A 1 42  ? 30.164 5.490   -7.114  1.00 16.06 ?  42   TYR   A HD2  1 
ATOM   1088 H  HE1  . TYR   A 1 42  ? 34.400 4.889   -8.830  1.00 15.98 ?  42   TYR   A HE1  1 
ATOM   1089 H  HE2  . TYR   A 1 42  ? 30.443 5.000   -9.354  1.00 17.32 ?  42   TYR   A HE2  1 
ATOM   1090 H  HH   . TYR   A 1 42  ? 33.435 4.515   -10.818 1.00 19.07 ?  42   TYR   A HH   1 
ATOM   1091 N  N    . LEU   A 1 43  ? 31.188 4.221   -2.072  1.00 9.94  ?  43   LEU   A N    1 
ATOM   1092 C  CA   . LEU   A 1 43  ? 30.748 4.562   -0.723  1.00 9.59  ?  43   LEU   A CA   1 
ATOM   1093 C  C    . LEU   A 1 43  ? 30.257 6.005   -0.628  1.00 9.79  ?  43   LEU   A C    1 
ATOM   1094 O  O    . LEU   A 1 43  ? 30.503 6.704   0.356   1.00 10.65 ?  43   LEU   A O    1 
ATOM   1095 C  CB   . LEU   A 1 43  ? 31.805 4.258   0.334   1.00 9.93  ?  43   LEU   A CB   1 
ATOM   1096 C  CG   . LEU   A 1 43  ? 32.301 2.810   0.421   1.00 10.31 ?  43   LEU   A CG   1 
ATOM   1097 C  CD1  . LEU   A 1 43  ? 33.360 2.702   1.500   1.00 11.52 ?  43   LEU   A CD1  1 
ATOM   1098 C  CD2  . LEU   A 1 43  ? 31.165 1.828   0.677   1.00 10.70 ?  43   LEU   A CD2  1 
ATOM   1099 H  H    . LEU   A 1 43  ? 30.837 3.485   -2.369  1.00 11.96 ?  43   LEU   A H    1 
ATOM   1100 H  HA   . LEU   A 1 43  ? 29.984 3.998   -0.513  1.00 11.54 ?  43   LEU   A HA   1 
ATOM   1101 H  HB2  . LEU   A 1 43  ? 32.577 4.811   0.163   1.00 11.93 ?  43   LEU   A HB2  1 
ATOM   1102 H  HB3  . LEU   A 1 43  ? 31.434 4.475   1.204   1.00 11.93 ?  43   LEU   A HB3  1 
ATOM   1103 H  HG   . LEU   A 1 43  ? 32.714 2.565   -0.424  1.00 12.39 ?  43   LEU   A HG   1 
ATOM   1104 H  HD11 . LEU   A 1 43  ? 33.674 1.784   1.549   1.00 13.84 ?  43   LEU   A HD11 1 
ATOM   1105 H  HD12 . LEU   A 1 43  ? 34.099 3.290   1.275   1.00 13.84 ?  43   LEU   A HD12 1 
ATOM   1106 H  HD13 . LEU   A 1 43  ? 32.974 2.965   2.349   1.00 13.84 ?  43   LEU   A HD13 1 
ATOM   1107 H  HD21 . LEU   A 1 43  ? 31.536 0.942   0.819   1.00 12.86 ?  43   LEU   A HD21 1 
ATOM   1108 H  HD22 . LEU   A 1 43  ? 30.677 2.111   1.467   1.00 12.86 ?  43   LEU   A HD22 1 
ATOM   1109 H  HD23 . LEU   A 1 43  ? 30.575 1.820   -0.091  1.00 12.86 ?  43   LEU   A HD23 1 
ATOM   1110 N  N    A LYS   A 1 44  ? 29.533 6.448   -1.654  0.30 11.09 ?  44   LYS   A N    1 
ATOM   1111 N  N    B LYS   A 1 44  ? 29.529 6.442   -1.660  0.70 9.68  ?  44   LYS   A N    1 
ATOM   1112 C  CA   A LYS   A 1 44  ? 28.896 7.764   -1.643  0.30 12.53 ?  44   LYS   A CA   1 
ATOM   1113 C  CA   B LYS   A 1 44  ? 28.871 7.750   -1.675  0.70 9.82  ?  44   LYS   A CA   1 
ATOM   1114 C  C    A LYS   A 1 44  ? 27.473 7.580   -1.133  0.30 11.71 ?  44   LYS   A C    1 
ATOM   1115 C  C    B LYS   A 1 44  ? 27.450 7.553   -1.168  0.70 9.14  ?  44   LYS   A C    1 
ATOM   1116 O  O    A LYS   A 1 44  ? 26.585 7.132   -1.864  0.30 12.01 ?  44   LYS   A O    1 
ATOM   1117 O  O    B LYS   A 1 44  ? 26.581 7.040   -1.881  0.70 10.32 ?  44   LYS   A O    1 
ATOM   1118 C  CB   A LYS   A 1 44  ? 28.943 8.398   -3.029  0.30 15.15 ?  44   LYS   A CB   1 
ATOM   1119 C  CB   B LYS   A 1 44  ? 28.897 8.351   -3.074  0.70 11.98 ?  44   LYS   A CB   1 
ATOM   1120 C  CG   A LYS   A 1 44  ? 30.341 8.806   -3.473  0.30 17.86 ?  44   LYS   A CG   1 
ATOM   1121 C  CG   B LYS   A 1 44  ? 30.255 8.867   -3.505  0.70 14.94 ?  44   LYS   A CG   1 
ATOM   1122 C  CD   A LYS   A 1 44  ? 31.011 9.715   -2.449  0.30 20.84 ?  44   LYS   A CD   1 
ATOM   1123 C  CD   B LYS   A 1 44  ? 30.873 9.781   -2.453  0.70 20.70 ?  44   LYS   A CD   1 
ATOM   1124 C  CE   A LYS   A 1 44  ? 32.358 10.209  -2.934  0.30 22.66 ?  44   LYS   A CE   1 
ATOM   1125 C  CE   B LYS   A 1 44  ? 32.151 10.416  -2.951  0.70 23.69 ?  44   LYS   A CE   1 
ATOM   1126 N  NZ   A LYS   A 1 44  ? 33.075 10.970  -1.876  0.30 23.60 ?  44   LYS   A NZ   1 
ATOM   1127 N  NZ   B LYS   A 1 44  ? 33.058 10.760  -1.824  0.70 25.23 ?  44   LYS   A NZ   1 
ATOM   1128 H  H    A LYS   A 1 44  ? 29.398 6.002   -2.375  0.30 13.33 ?  44   LYS   A H    1 
ATOM   1129 H  H    B LYS   A 1 44  ? 29.409 5.991   -2.380  0.70 11.64 ?  44   LYS   A H    1 
ATOM   1130 H  HA   A LYS   A 1 44  ? 29.354 8.340   -1.013  0.30 15.07 ?  44   LYS   A HA   1 
ATOM   1131 H  HA   B LYS   A 1 44  ? 29.315 8.343   -1.049  0.70 11.80 ?  44   LYS   A HA   1 
ATOM   1132 H  HB2  A LYS   A 1 44  ? 28.602 7.760   -3.676  0.30 18.21 ?  44   LYS   A HB2  1 
ATOM   1133 H  HB2  B LYS   A 1 44  ? 28.622 7.669   -3.708  0.70 14.40 ?  44   LYS   A HB2  1 
ATOM   1134 H  HB3  A LYS   A 1 44  ? 28.389 9.194   -3.028  0.30 18.21 ?  44   LYS   A HB3  1 
ATOM   1135 H  HB3  B LYS   A 1 44  ? 28.273 9.094   -3.102  0.70 14.40 ?  44   LYS   A HB3  1 
ATOM   1136 H  HG2  A LYS   A 1 44  ? 30.888 8.012   -3.581  0.30 21.45 ?  44   LYS   A HG2  1 
ATOM   1137 H  HG2  B LYS   A 1 44  ? 30.852 8.117   -3.648  0.70 17.95 ?  44   LYS   A HG2  1 
ATOM   1138 H  HG3  A LYS   A 1 44  ? 30.281 9.289   -4.314  0.30 21.45 ?  44   LYS   A HG3  1 
ATOM   1139 H  HG3  B LYS   A 1 44  ? 30.156 9.378   -4.326  0.70 17.95 ?  44   LYS   A HG3  1 
ATOM   1140 H  HD2  A LYS   A 1 44  ? 30.437 10.480  -2.279  0.30 25.03 ?  44   LYS   A HD2  1 
ATOM   1141 H  HD2  B LYS   A 1 44  ? 30.238 10.476  -2.223  0.70 24.86 ?  44   LYS   A HD2  1 
ATOM   1142 H  HD3  A LYS   A 1 44  ? 31.159 9.218   -1.628  0.30 25.03 ?  44   LYS   A HD3  1 
ATOM   1143 H  HD3  B LYS   A 1 44  ? 31.093 9.252   -1.666  0.70 24.86 ?  44   LYS   A HD3  1 
ATOM   1144 H  HE2  A LYS   A 1 44  ? 32.904 9.448   -3.185  0.30 27.22 ?  44   LYS   A HE2  1 
ATOM   1145 H  HE2  B LYS   A 1 44  ? 32.613 9.789   -3.532  0.70 28.45 ?  44   LYS   A HE2  1 
ATOM   1146 H  HE3  A LYS   A 1 44  ? 32.226 10.795  -3.694  0.30 27.22 ?  44   LYS   A HE3  1 
ATOM   1147 H  HE3  B LYS   A 1 44  ? 31.936 11.226  -3.432  0.70 28.45 ?  44   LYS   A HE3  1 
ATOM   1148 H  HZ1  A LYS   A 1 44  ? 33.865 11.242  -2.180  0.30 28.34 ?  44   LYS   A HZ1  1 
ATOM   1149 H  HZ1  B LYS   A 1 44  ? 33.802 11.134  -2.138  0.70 30.30 ?  44   LYS   A HZ1  1 
ATOM   1150 H  HZ2  A LYS   A 1 44  ? 32.596 11.682  -1.636  0.30 28.34 ?  44   LYS   A HZ2  1 
ATOM   1151 H  HZ2  B LYS   A 1 44  ? 32.655 11.336  -1.276  0.70 30.30 ?  44   LYS   A HZ2  1 
ATOM   1152 H  HZ3  A LYS   A 1 44  ? 33.201 10.453  -1.162  0.30 28.34 ?  44   LYS   A HZ3  1 
ATOM   1153 H  HZ3  B LYS   A 1 44  ? 33.271 10.028  -1.367  0.70 30.30 ?  44   LYS   A HZ3  1 
ATOM   1154 N  N    A HIS   A 1 45  ? 27.262 7.921   0.137   0.30 11.31 ?  45   HIS   A N    1 
ATOM   1155 N  N    B HIS   A 1 45  ? 27.224 7.931   0.085   0.70 8.82  ?  45   HIS   A N    1 
ATOM   1156 C  CA   A HIS   A 1 45  ? 26.008 7.622   0.828   0.30 11.15 ?  45   HIS   A CA   1 
ATOM   1157 C  CA   B HIS   A 1 45  ? 25.992 7.574   0.787   0.70 8.80  ?  45   HIS   A CA   1 
ATOM   1158 C  C    A HIS   A 1 45  ? 25.043 8.800   0.676   0.30 11.30 ?  45   HIS   A C    1 
ATOM   1159 C  C    B HIS   A 1 45  ? 24.938 8.669   0.609   0.70 9.39  ?  45   HIS   A C    1 
ATOM   1160 O  O    A HIS   A 1 45  ? 24.748 9.540   1.615   0.30 12.10 ?  45   HIS   A O    1 
ATOM   1161 O  O    B HIS   A 1 45  ? 24.615 9.420   1.525   0.70 11.09 ?  45   HIS   A O    1 
ATOM   1162 C  CB   A HIS   A 1 45  ? 26.288 7.307   2.291   0.30 11.10 ?  45   HIS   A CB   1 
ATOM   1163 C  CB   B HIS   A 1 45  ? 26.295 7.346   2.259   0.70 9.03  ?  45   HIS   A CB   1 
ATOM   1164 C  CG   A HIS   A 1 45  ? 27.423 6.353   2.497   0.30 10.75 ?  45   HIS   A CG   1 
ATOM   1165 C  CG   B HIS   A 1 45  ? 27.409 6.382   2.500   0.70 8.80  ?  45   HIS   A CG   1 
ATOM   1166 N  ND1  A HIS   A 1 45  ? 27.414 5.064   2.009   0.30 10.82 ?  45   HIS   A ND1  1 
ATOM   1167 N  ND1  B HIS   A 1 45  ? 27.410 5.096   2.003   0.70 9.26  ?  45   HIS   A ND1  1 
ATOM   1168 C  CD2  A HIS   A 1 45  ? 28.605 6.507   3.139   0.30 10.89 ?  45   HIS   A CD2  1 
ATOM   1169 C  CD2  B HIS   A 1 45  ? 28.569 6.535   3.181   0.70 9.18  ?  45   HIS   A CD2  1 
ATOM   1170 C  CE1  A HIS   A 1 45  ? 28.544 4.466   2.345   0.30 10.77 ?  45   HIS   A CE1  1 
ATOM   1171 C  CE1  B HIS   A 1 45  ? 28.531 4.502   2.378   0.70 8.77  ?  45   HIS   A CE1  1 
ATOM   1172 N  NE2  A HIS   A 1 45  ? 29.284 5.319   3.032   0.30 10.92 ?  45   HIS   A NE2  1 
ATOM   1173 N  NE2  B HIS   A 1 45  ? 29.251 5.352   3.093   0.70 9.05  ?  45   HIS   A NE2  1 
ATOM   1174 H  H    A HIS   A 1 45  ? 27.834 8.337   0.626   0.30 13.60 ?  45   HIS   A H    1 
ATOM   1175 H  H    B HIS   A 1 45  ? 27.760 8.405   0.555   0.70 10.61 ?  45   HIS   A H    1 
ATOM   1176 H  HA   A HIS   A 1 45  ? 25.602 6.839   0.425   0.30 13.40 ?  45   HIS   A HA   1 
ATOM   1177 H  HA   B HIS   A 1 45  ? 25.635 6.746   0.422   0.70 10.59 ?  45   HIS   A HA   1 
ATOM   1178 H  HB2  A HIS   A 1 45  ? 26.506 8.132   2.752   0.30 13.35 ?  45   HIS   A HB2  1 
ATOM   1179 H  HB2  B HIS   A 1 45  ? 26.534 8.195   2.663   0.70 10.86 ?  45   HIS   A HB2  1 
ATOM   1180 H  HB3  A HIS   A 1 45  ? 25.494 6.911   2.683   0.30 13.35 ?  45   HIS   A HB3  1 
ATOM   1181 H  HB3  B HIS   A 1 45  ? 25.497 6.994   2.694   0.70 10.86 ?  45   HIS   A HB3  1 
ATOM   1182 H  HD2  A HIS   A 1 45  ? 28.904 7.274   3.572   0.30 13.09 ?  45   HIS   A HD2  1 
ATOM   1183 H  HD2  B HIS   A 1 45  ? 28.856 7.306   3.623   0.70 11.04 ?  45   HIS   A HD2  1 
ATOM   1184 H  HE1  A HIS   A 1 45  ? 28.778 3.590   2.137   0.30 12.94 ?  45   HIS   A HE1  1 
ATOM   1185 H  HE1  B HIS   A 1 45  ? 28.766 3.625   2.183   0.70 10.55 ?  45   HIS   A HE1  1 
ATOM   1186 H  HE2  A HIS   A 1 45  ? 30.066 5.156   3.358   0.30 13.12 ?  45   HIS   A HE2  1 
ATOM   1187 H  HE2  B HIS   A 1 45  ? 30.018 5.185   3.444   0.70 10.88 ?  45   HIS   A HE2  1 
ATOM   1188 N  N    A GLY   A 1 46  ? 24.543 8.959   -0.547  0.30 10.88 ?  46   GLY   A N    1 
ATOM   1189 N  N    B GLY   A 1 46  ? 24.373 8.731   -0.593  0.70 10.21 ?  46   GLY   A N    1 
ATOM   1190 C  CA   A GLY   A 1 46  ? 23.755 10.128  -0.885  0.30 10.51 ?  46   GLY   A CA   1 
ATOM   1191 C  CA   B GLY   A 1 46  ? 23.555 9.877   -0.950  0.70 11.02 ?  46   GLY   A CA   1 
ATOM   1192 C  C    A GLY   A 1 46  ? 22.253 9.975   -0.724  0.30 10.34 ?  46   GLY   A C    1 
ATOM   1193 C  C    B GLY   A 1 46  ? 22.085 9.786   -0.582  0.70 11.16 ?  46   GLY   A C    1 
ATOM   1194 O  O    A GLY   A 1 46  ? 21.549 10.961  -0.485  0.30 10.41 ?  46   GLY   A O    1 
ATOM   1195 O  O    B GLY   A 1 46  ? 21.468 10.796  -0.224  0.70 12.70 ?  46   GLY   A O    1 
ATOM   1196 H  H    A GLY   A 1 46  ? 24.653 8.404   -1.195  0.30 13.08 ?  46   GLY   A H    1 
ATOM   1197 H  H    B GLY   A 1 46  ? 24.432 8.125   -1.201  0.70 12.27 ?  46   GLY   A H    1 
ATOM   1198 H  HA2  A GLY   A 1 46  ? 24.058 10.872  -0.335  0.30 12.64 ?  46   GLY   A HA2  1 
ATOM   1199 H  HA2  B GLY   A 1 46  ? 23.910 10.662  -0.510  0.70 13.25 ?  46   GLY   A HA2  1 
ATOM   1200 H  HA3  A GLY   A 1 46  ? 23.924 10.357  -1.811  0.30 12.64 ?  46   GLY   A HA3  1 
ATOM   1201 H  HA3  B GLY   A 1 46  ? 23.618 10.015  -1.907  0.70 13.25 ?  46   GLY   A HA3  1 
ATOM   1202 N  N    A GLY   A 1 47  ? 21.743 8.758   -0.881  0.30 9.98  ?  47   GLY   A N    1 
ATOM   1203 N  N    B GLY   A 1 47  ? 21.503 8.596   -0.684  0.70 10.98 ?  47   GLY   A N    1 
ATOM   1204 C  CA   A GLY   A 1 47  ? 20.312 8.529   -0.836  0.30 10.08 ?  47   GLY   A CA   1 
ATOM   1205 C  CA   B GLY   A 1 47  ? 20.068 8.434   -0.542  0.70 11.06 ?  47   GLY   A CA   1 
ATOM   1206 C  C    A GLY   A 1 47  ? 20.003 7.095   -0.463  0.30 10.20 ?  47   GLY   A C    1 
ATOM   1207 C  C    B GLY   A 1 47  ? 19.714 7.010   -0.178  0.70 10.22 ?  47   GLY   A C    1 
ATOM   1208 O  O    A GLY   A 1 47  ? 20.899 6.281   -0.231  0.30 10.85 ?  47   GLY   A O    1 
ATOM   1209 O  O    B GLY   A 1 47  ? 20.583 6.151   -0.013  0.70 10.14 ?  47   GLY   A O    1 
ATOM   1210 H  H    A GLY   A 1 47  ? 22.211 8.055   -1.021  0.30 12.01 ?  47   GLY   A H    1 
ATOM   1211 H  H    B GLY   A 1 47  ? 21.925 7.861   -0.816  0.70 13.19 ?  47   GLY   A H    1 
ATOM   1212 H  HA2  A GLY   A 1 47  ? 19.907 9.128   -0.186  0.30 12.11 ?  47   GLY   A HA2  1 
ATOM   1213 H  HA2  B GLY   A 1 47  ? 19.733 9.023   0.152   0.70 13.30 ?  47   GLY   A HA2  1 
ATOM   1214 H  HA3  A GLY   A 1 47  ? 19.935 8.719   -1.710  0.30 12.11 ?  47   GLY   A HA3  1 
ATOM   1215 H  HA3  B GLY   A 1 47  ? 19.626 8.658   -1.378  0.70 13.30 ?  47   GLY   A HA3  1 
ATOM   1216 N  N    A GLY   A 1 48  ? 18.710 6.788   -0.417  0.30 10.06 ?  48   GLY   A N    1 
ATOM   1217 N  N    B GLY   A 1 48  ? 18.411 6.758   -0.063  0.70 10.50 ?  48   GLY   A N    1 
ATOM   1218 C  CA   A GLY   A 1 48  ? 18.287 5.451   -0.045  0.30 10.15 ?  48   GLY   A CA   1 
ATOM   1219 C  CA   B GLY   A 1 48  ? 17.966 5.436   0.335   0.70 10.76 ?  48   GLY   A CA   1 
ATOM   1220 C  C    A GLY   A 1 48  ? 18.672 5.117   1.387   0.30 9.75  ?  48   GLY   A C    1 
ATOM   1221 C  C    B GLY   A 1 48  ? 18.530 5.038   1.688   0.70 10.27 ?  48   GLY   A C    1 
ATOM   1222 O  O    A GLY   A 1 48  ? 18.800 5.994   2.249   0.30 9.85  ?  48   GLY   A O    1 
ATOM   1223 O  O    B GLY   A 1 48  ? 18.722 5.866   2.589   0.70 10.81 ?  48   GLY   A O    1 
ATOM   1224 H  H    A GLY   A 1 48  ? 18.073 7.331   -0.602  0.30 12.09 ?  48   GLY   A H    1 
ATOM   1225 H  H    B GLY   A 1 48  ? 17.772 7.325   -0.205  0.70 12.63 ?  48   GLY   A H    1 
ATOM   1226 H  HA2  A GLY   A 1 48  ? 17.326 5.381   -0.135  0.30 12.21 ?  48   GLY   A HA2  1 
ATOM   1227 H  HA2  B GLY   A 1 48  ? 16.994 5.412   0.379   0.70 12.94 ?  48   GLY   A HA2  1 
ATOM   1228 H  HA3  A GLY   A 1 48  ? 18.702 4.802   -0.637  0.30 12.21 ?  48   GLY   A HA3  1 
ATOM   1229 H  HA3  B GLY   A 1 48  ? 18.257 4.782   -0.321  0.70 12.94 ?  48   GLY   A HA3  1 
ATOM   1230 N  N    A VAL   A 1 49  ? 18.862 3.820   1.646   0.30 10.26 ?  49   VAL   A N    1 
ATOM   1231 N  N    B VAL   A 1 49  ? 18.792 3.737   1.836   0.70 10.27 ?  49   VAL   A N    1 
ATOM   1232 C  CA   A VAL   A 1 49  ? 19.279 3.383   2.978   0.30 10.25 ?  49   VAL   A CA   1 
ATOM   1233 C  CA   B VAL   A 1 49  ? 19.389 3.216   3.066   0.70 10.25 ?  49   VAL   A CA   1 
ATOM   1234 C  C    A VAL   A 1 49  ? 20.612 4.014   3.362   0.30 9.68  ?  49   VAL   A C    1 
ATOM   1235 C  C    B VAL   A 1 49  ? 20.659 3.979   3.413   0.70 9.55  ?  49   VAL   A C    1 
ATOM   1236 O  O    A VAL   A 1 49  ? 20.824 4.397   4.519   0.30 9.80  ?  49   VAL   A O    1 
ATOM   1237 O  O    B VAL   A 1 49  ? 20.854 4.415   4.553   0.70 9.86  ?  49   VAL   A O    1 
ATOM   1238 C  CB   A VAL   A 1 49  ? 19.338 1.844   3.049   0.30 11.27 ?  49   VAL   A CB   1 
ATOM   1239 C  CB   B VAL   A 1 49  ? 19.675 1.709   2.922   0.70 10.75 ?  49   VAL   A CB   1 
ATOM   1240 C  CG1  A VAL   A 1 49  ? 20.024 1.390   4.338   0.30 11.63 ?  49   VAL   A CG1  1 
ATOM   1241 C  CG1  B VAL   A 1 49  ? 20.527 1.219   4.090   0.70 10.38 ?  49   VAL   A CG1  1 
ATOM   1242 C  CG2  A VAL   A 1 49  ? 17.943 1.247   2.950   0.30 12.12 ?  49   VAL   A CG2  1 
ATOM   1243 C  CG2  B VAL   A 1 49  ? 18.375 0.915   2.820   0.70 11.69 ?  49   VAL   A CG2  1 
ATOM   1244 H  H    A VAL   A 1 49  ? 18.752 3.185   1.077   0.30 12.33 ?  49   VAL   A H    1 
ATOM   1245 H  H    B VAL   A 1 49  ? 18.629 3.140   1.242   0.70 12.35 ?  49   VAL   A H    1 
ATOM   1246 H  HA   A VAL   A 1 49  ? 18.618 3.677   3.622   0.30 12.32 ?  49   VAL   A HA   1 
ATOM   1247 H  HA   B VAL   A 1 49  ? 18.762 3.331   3.797   0.70 12.33 ?  49   VAL   A HA   1 
ATOM   1248 H  HB   A VAL   A 1 49  ? 19.861 1.512   2.302   0.30 13.55 ?  49   VAL   A HB   1 
ATOM   1249 H  HB   B VAL   A 1 49  ? 20.174 1.561   2.104   0.70 12.92 ?  49   VAL   A HB   1 
ATOM   1250 H  HG11 A VAL   A 1 49  ? 19.813 0.457   4.497   0.30 13.98 ?  49   VAL   A HG11 1 
ATOM   1251 H  HG11 B VAL   A 1 49  ? 20.450 0.253   4.153   0.70 12.48 ?  49   VAL   A HG11 1 
ATOM   1252 H  HG12 A VAL   A 1 49  ? 20.984 1.498   4.247   0.30 13.98 ?  49   VAL   A HG12 1 
ATOM   1253 H  HG12 B VAL   A 1 49  ? 21.455 1.462   3.933   0.70 12.48 ?  49   VAL   A HG12 1 
ATOM   1254 H  HG13 A VAL   A 1 49  ? 19.699 1.930   5.077   0.30 13.98 ?  49   VAL   A HG13 1 
ATOM   1255 H  HG13 B VAL   A 1 49  ? 20.210 1.628   4.909   0.70 12.48 ?  49   VAL   A HG13 1 
ATOM   1256 H  HG21 A VAL   A 1 49  ? 18.010 0.280   2.994   0.30 14.57 ?  49   VAL   A HG21 1 
ATOM   1257 H  HG21 B VAL   A 1 49  ? 18.583 -0.020  2.677   0.70 14.06 ?  49   VAL   A HG21 1 
ATOM   1258 H  HG22 A VAL   A 1 49  ? 17.408 1.575   3.690   0.30 14.57 ?  49   VAL   A HG22 1 
ATOM   1259 H  HG22 B VAL   A 1 49  ? 17.876 1.021   3.647   0.70 14.06 ?  49   VAL   A HG22 1 
ATOM   1260 H  HG23 A VAL   A 1 49  ? 17.546 1.515   2.108   0.30 14.57 ?  49   VAL   A HG23 1 
ATOM   1261 H  HG23 B VAL   A 1 49  ? 17.852 1.256   2.075   0.70 14.06 ?  49   VAL   A HG23 1 
ATOM   1262 N  N    A ALA   A 1 50  ? 21.542 4.104   2.408   0.30 9.45  ?  50   ALA   A N    1 
ATOM   1263 N  N    B ALA   A 1 50  ? 21.567 4.101   2.444   0.70 9.26  ?  50   ALA   A N    1 
ATOM   1264 C  CA   A ALA   A 1 50  ? 22.863 4.648   2.712   0.30 9.44  ?  50   ALA   A CA   1 
ATOM   1265 C  CA   B ALA   A 1 50  ? 22.881 4.662   2.735   0.70 9.33  ?  50   ALA   A CA   1 
ATOM   1266 C  C    A ALA   A 1 50  ? 22.778 6.103   3.150   0.30 9.44  ?  50   ALA   A C    1 
ATOM   1267 C  C    B ALA   A 1 50  ? 22.775 6.114   3.168   0.70 9.27  ?  50   ALA   A C    1 
ATOM   1268 O  O    A ALA   A 1 50  ? 23.429 6.508   4.121   0.30 9.60  ?  50   ALA   A O    1 
ATOM   1269 O  O    B ALA   A 1 50  ? 23.407 6.533   4.146   0.70 9.61  ?  50   ALA   A O    1 
ATOM   1270 C  CB   A ALA   A 1 50  ? 23.774 4.505   1.493   0.30 9.45  ?  50   ALA   A CB   1 
ATOM   1271 C  CB   B ALA   A 1 50  ? 23.784 4.534   1.513   0.70 9.34  ?  50   ALA   A CB   1 
ATOM   1272 H  H    A ALA   A 1 50  ? 21.436 3.860   1.591   0.30 11.36 ?  50   ALA   A H    1 
ATOM   1273 H  H    B ALA   A 1 50  ? 21.444 3.877   1.620   0.70 11.14 ?  50   ALA   A H    1 
ATOM   1274 H  HA   A ALA   A 1 50  ? 23.254 4.145   3.441   0.30 11.35 ?  50   ALA   A HA   1 
ATOM   1275 H  HA   B ALA   A 1 50  ? 23.281 4.166   3.463   0.70 11.23 ?  50   ALA   A HA   1 
ATOM   1276 H  HB1  A ALA   A 1 50  ? 24.648 4.870   1.705   0.30 11.36 ?  50   ALA   A HB1  1 
ATOM   1277 H  HB1  B ALA   A 1 50  ? 24.653 4.913   1.725   0.70 11.24 ?  50   ALA   A HB1  1 
ATOM   1278 H  HB2  A ALA   A 1 50  ? 23.855 3.566   1.265   0.30 11.36 ?  50   ALA   A HB2  1 
ATOM   1279 H  HB2  B ALA   A 1 50  ? 23.876 3.598   1.287   0.70 11.24 ?  50   ALA   A HB2  1 
ATOM   1280 H  HB3  A ALA   A 1 50  ? 23.386 4.993   0.748   0.30 11.36 ?  50   ALA   A HB3  1 
ATOM   1281 H  HB3  B ALA   A 1 50  ? 23.385 5.019   0.773   0.70 11.24 ?  50   ALA   A HB3  1 
ATOM   1282 N  N    . GLY   A 1 51  ? 21.990 6.910   2.440   1.00 9.57  ?  51   GLY   A N    1 
ATOM   1283 C  CA   . GLY   A 1 51  ? 21.839 8.299   2.822   1.00 9.75  ?  51   GLY   A CA   1 
ATOM   1284 C  C    . GLY   A 1 51  ? 21.223 8.445   4.198   1.00 10.03 ?  51   GLY   A C    1 
ATOM   1285 O  O    . GLY   A 1 51  ? 21.607 9.333   4.968   1.00 10.46 ?  51   GLY   A O    1 
ATOM   1286 H  H    A GLY   A 1 51  ? 21.541 6.679   1.745   0.30 11.51 ?  51   GLY   A H    1 
ATOM   1287 H  H    B GLY   A 1 51  ? 21.552 6.676   1.739   0.70 11.51 ?  51   GLY   A H    1 
ATOM   1288 H  HA2  . GLY   A 1 51  ? 22.704 8.737   2.827   1.00 11.72 ?  51   GLY   A HA2  1 
ATOM   1289 H  HA3  . GLY   A 1 51  ? 21.266 8.756   2.183   1.00 11.72 ?  51   GLY   A HA3  1 
ATOM   1290 N  N    A ALA   A 1 52  ? 20.262 7.575   4.528   0.30 10.10 ?  52   ALA   A N    1 
ATOM   1291 N  N    B ALA   A 1 52  ? 20.259 7.578   4.524   0.70 9.85  ?  52   ALA   A N    1 
ATOM   1292 C  CA   A ALA   A 1 52  ? 19.614 7.637   5.834   0.30 10.51 ?  52   ALA   A CA   1 
ATOM   1293 C  CA   B ALA   A 1 52  ? 19.603 7.638   5.825   0.70 10.49 ?  52   ALA   A CA   1 
ATOM   1294 C  C    A ALA   A 1 52  ? 20.559 7.201   6.948   0.30 10.34 ?  52   ALA   A C    1 
ATOM   1295 C  C    B ALA   A 1 52  ? 20.549 7.221   6.951   0.70 9.76  ?  52   ALA   A C    1 
ATOM   1296 O  O    A ALA   A 1 52  ? 20.618 7.841   8.004   0.30 10.69 ?  52   ALA   A O    1 
ATOM   1297 O  O    B ALA   A 1 52  ? 20.617 7.882   7.993   0.70 10.68 ?  52   ALA   A O    1 
ATOM   1298 C  CB   A ALA   A 1 52  ? 18.348 6.779   5.828   0.30 11.13 ?  52   ALA   A CB   1 
ATOM   1299 C  CB   B ALA   A 1 52  ? 18.345 6.768   5.803   0.70 11.66 ?  52   ALA   A CB   1 
ATOM   1300 H  H    A ALA   A 1 52  ? 19.976 6.943   4.018   0.30 12.14 ?  52   ALA   A H    1 
ATOM   1301 H  H    B ALA   A 1 52  ? 19.982 6.941   4.014   0.70 11.84 ?  52   ALA   A H    1 
ATOM   1302 H  HA   A ALA   A 1 52  ? 19.350 8.550   6.009   0.30 12.63 ?  52   ALA   A HA   1 
ATOM   1303 H  HA   B ALA   A 1 52  ? 19.328 8.549   5.991   0.70 12.61 ?  52   ALA   A HA   1 
ATOM   1304 H  HB1  A ALA   A 1 52  ? 17.927 6.831   6.702   0.30 13.38 ?  52   ALA   A HB1  1 
ATOM   1305 H  HB1  B ALA   A 1 52  ? 17.909 6.823   6.668   0.70 14.01 ?  52   ALA   A HB1  1 
ATOM   1306 H  HB2  A ALA   A 1 52  ? 17.741 7.115   5.150   0.30 13.38 ?  52   ALA   A HB2  1 
ATOM   1307 H  HB2  B ALA   A 1 52  ? 17.748 7.095   5.111   0.70 14.01 ?  52   ALA   A HB2  1 
ATOM   1308 H  HB3  A ALA   A 1 52  ? 18.587 5.859   5.632   0.30 13.38 ?  52   ALA   A HB3  1 
ATOM   1309 H  HB3  B ALA   A 1 52  ? 18.596 5.850   5.616   0.70 14.01 ?  52   ALA   A HB3  1 
ATOM   1310 N  N    A LEU   A 1 53  ? 21.302 6.110   6.740   0.30 10.32 ?  53   LEU   A N    1 
ATOM   1311 N  N    B LEU   A 1 53  ? 21.285 6.120   6.766   0.70 9.47  ?  53   LEU   A N    1 
ATOM   1312 C  CA   A LEU   A 1 53  ? 22.262 5.679   7.753   0.30 10.65 ?  53   LEU   A CA   1 
ATOM   1313 C  CA   B LEU   A 1 53  ? 22.260 5.715   7.779   0.70 9.79  ?  53   LEU   A CA   1 
ATOM   1314 C  C    A LEU   A 1 53  ? 23.336 6.737   7.966   0.30 10.62 ?  53   LEU   A C    1 
ATOM   1315 C  C    B LEU   A 1 53  ? 23.301 6.808   7.981   0.70 9.31  ?  53   LEU   A C    1 
ATOM   1316 O  O    A LEU   A 1 53  ? 23.730 7.016   9.104   0.30 10.91 ?  53   LEU   A O    1 
ATOM   1317 O  O    B LEU   A 1 53  ? 23.614 7.188   9.114   0.70 10.17 ?  53   LEU   A O    1 
ATOM   1318 C  CB   A LEU   A 1 53  ? 22.895 4.343   7.356   0.30 11.01 ?  53   LEU   A CB   1 
ATOM   1319 C  CB   B LEU   A 1 53  ? 22.944 4.401   7.384   0.70 10.28 ?  53   LEU   A CB   1 
ATOM   1320 C  CG   A LEU   A 1 53  ? 21.986 3.111   7.399   0.30 11.25 ?  53   LEU   A CG   1 
ATOM   1321 C  CG   B LEU   A 1 53  ? 22.142 3.099   7.475   0.70 10.85 ?  53   LEU   A CG   1 
ATOM   1322 C  CD1  A LEU   A 1 53  ? 22.710 1.897   6.838   0.30 11.54 ?  53   LEU   A CD1  1 
ATOM   1323 C  CD1  B LEU   A 1 53  ? 22.922 1.964   6.829   0.70 11.75 ?  53   LEU   A CD1  1 
ATOM   1324 C  CD2  A LEU   A 1 53  ? 21.506 2.831   8.814   0.30 11.73 ?  53   LEU   A CD2  1 
ATOM   1325 C  CD2  B LEU   A 1 53  ? 21.825 2.738   8.913   0.70 11.88 ?  53   LEU   A CD2  1 
ATOM   1326 H  H    A LEU   A 1 53  ? 21.269 5.614   6.038   0.30 12.41 ?  53   LEU   A H    1 
ATOM   1327 H  H    B LEU   A 1 53  ? 21.232 5.597   6.083   0.70 11.39 ?  53   LEU   A H    1 
ATOM   1328 H  HA   A LEU   A 1 53  ? 21.798 5.551   8.594   0.30 12.80 ?  53   LEU   A HA   1 
ATOM   1329 H  HA   B LEU   A 1 53  ? 21.800 5.574   8.621   0.70 11.77 ?  53   LEU   A HA   1 
ATOM   1330 H  HB2  A LEU   A 1 53  ? 23.225 4.418   6.447   0.30 13.23 ?  53   LEU   A HB2  1 
ATOM   1331 H  HB2  B LEU   A 1 53  ? 23.238 4.481   6.464   0.70 12.36 ?  53   LEU   A HB2  1 
ATOM   1332 H  HB3  A LEU   A 1 53  ? 23.638 4.166   7.953   0.30 13.23 ?  53   LEU   A HB3  1 
ATOM   1333 H  HB3  B LEU   A 1 53  ? 23.720 4.286   7.955   0.70 12.36 ?  53   LEU   A HB3  1 
ATOM   1334 H  HG   A LEU   A 1 53  ? 21.206 3.274   6.845   0.30 13.52 ?  53   LEU   A HG   1 
ATOM   1335 H  HG   B LEU   A 1 53  ? 21.305 3.203   6.993   0.70 13.04 ?  53   LEU   A HG   1 
ATOM   1336 H  HD11 A LEU   A 1 53  ? 22.117 1.131   6.874   0.30 13.87 ?  53   LEU   A HD11 1 
ATOM   1337 H  HD11 B LEU   A 1 53  ? 22.402 1.147   6.898   0.70 14.12 ?  53   LEU   A HD11 1 
ATOM   1338 H  HD12 A LEU   A 1 53  ? 22.962 2.077   5.919   0.30 13.87 ?  53   LEU   A HD12 1 
ATOM   1339 H  HD12 B LEU   A 1 53  ? 23.078 2.179   5.897   0.70 14.12 ?  53   LEU   A HD12 1 
ATOM   1340 H  HD13 A LEU   A 1 53  ? 23.502 1.728   7.372   0.30 13.87 ?  53   LEU   A HD13 1 
ATOM   1341 H  HD13 B LEU   A 1 53  ? 23.766 1.860   7.294   0.70 14.12 ?  53   LEU   A HD13 1 
ATOM   1342 H  HD21 A LEU   A 1 53  ? 21.009 1.997   8.820   0.30 14.10 ?  53   LEU   A HD21 1 
ATOM   1343 H  HD21 B LEU   A 1 53  ? 21.287 1.929   8.925   0.70 14.28 ?  53   LEU   A HD21 1 
ATOM   1344 H  HD22 A LEU   A 1 53  ? 22.277 2.759   9.399   0.30 14.10 ?  53   LEU   A HD22 1 
ATOM   1345 H  HD22 B LEU   A 1 53  ? 22.652 2.592   9.393   0.70 14.28 ?  53   LEU   A HD22 1 
ATOM   1346 H  HD23 A LEU   A 1 53  ? 20.935 3.557   9.106   0.30 14.10 ?  53   LEU   A HD23 1 
ATOM   1347 H  HD23 B LEU   A 1 53  ? 21.329 3.467   9.320   0.70 14.28 ?  53   LEU   A HD23 1 
ATOM   1348 N  N    A ASN   A 1 54  ? 23.814 7.347   6.882   0.30 10.48 ?  54   ASN   A N    1 
ATOM   1349 N  N    B ASN   A 1 54  ? 23.846 7.332   6.886   0.70 9.24  ?  54   ASN   A N    1 
ATOM   1350 C  CA   A ASN   A 1 54  ? 24.877 8.336   7.015   0.30 10.49 ?  54   ASN   A CA   1 
ATOM   1351 C  CA   B ASN   A 1 54  ? 24.888 8.338   7.027   0.70 9.38  ?  54   ASN   A CA   1 
ATOM   1352 C  C    A ASN   A 1 54  ? 24.379 9.590   7.723   0.30 10.32 ?  54   ASN   A C    1 
ATOM   1353 C  C    B ASN   A 1 54  ? 24.366 9.571   7.756   0.70 9.73  ?  54   ASN   A C    1 
ATOM   1354 O  O    A ASN   A 1 54  ? 25.090 10.166  8.555   0.30 10.59 ?  54   ASN   A O    1 
ATOM   1355 O  O    B ASN   A 1 54  ? 25.043 10.114  8.640   0.70 10.20 ?  54   ASN   A O    1 
ATOM   1356 C  CB   A ASN   A 1 54  ? 25.449 8.677   5.644   0.30 10.62 ?  54   ASN   A CB   1 
ATOM   1357 C  CB   B ASN   A 1 54  ? 25.461 8.716   5.672   0.70 9.04  ?  54   ASN   A CB   1 
ATOM   1358 C  CG   A ASN   A 1 54  ? 26.513 9.745   5.718   0.30 11.02 ?  54   ASN   A CG   1 
ATOM   1359 C  CG   B ASN   A 1 54  ? 26.457 9.834   5.790   0.70 9.07  ?  54   ASN   A CG   1 
ATOM   1360 O  OD1  A ASN   A 1 54  ? 27.559 9.550   6.339   0.30 11.65 ?  54   ASN   A OD1  1 
ATOM   1361 O  OD1  B ASN   A 1 54  ? 27.457 9.706   6.509   0.70 9.02  ?  54   ASN   A OD1  1 
ATOM   1362 N  ND2  A ASN   A 1 54  ? 26.254 10.887  5.095   0.30 11.28 ?  54   ASN   A ND2  1 
ATOM   1363 N  ND2  B ASN   A 1 54  ? 26.188 10.953  5.133   0.70 9.94  ?  54   ASN   A ND2  1 
ATOM   1364 H  H    A ASN   A 1 54  ? 23.535 7.215   6.079   0.30 12.60 ?  54   ASN   A H    1 
ATOM   1365 H  H    B ASN   A 1 54  ? 23.625 7.132   6.077   0.70 11.11 ?  54   ASN   A H    1 
ATOM   1366 H  HA   A ASN   A 1 54  ? 25.587 7.956   7.552   0.30 12.61 ?  54   ASN   A HA   1 
ATOM   1367 H  HA   B ASN   A 1 54  ? 25.599 7.964   7.561   0.70 11.28 ?  54   ASN   A HA   1 
ATOM   1368 H  HB2  A ASN   A 1 54  ? 25.851 7.879   5.263   0.30 12.77 ?  54   ASN   A HB2  1 
ATOM   1369 H  HB2  B ASN   A 1 54  ? 25.918 7.939   5.297   0.70 10.87 ?  54   ASN   A HB2  1 
ATOM   1370 H  HB3  A ASN   A 1 54  ? 24.737 8.997   5.071   0.30 12.77 ?  54   ASN   A HB3  1 
ATOM   1371 H  HB3  B ASN   A 1 54  ? 24.748 8.997   5.085   0.70 10.87 ?  54   ASN   A HB3  1 
ATOM   1372 H  HD21 A ASN   A 1 54  ? 26.830 11.524  5.111   0.30 13.56 ?  54   ASN   A HD21 1 
ATOM   1373 H  HD21 B ASN   A 1 54  ? 26.730 11.620  5.180   0.70 11.95 ?  54   ASN   A HD21 1 
ATOM   1374 H  HD22 A ASN   A 1 54  ? 25.513 10.986  4.671   0.30 13.56 ?  54   ASN   A HD22 1 
ATOM   1375 H  HD22 B ASN   A 1 54  ? 25.481 11.007  4.650   0.70 11.95 ?  54   ASN   A HD22 1 
ATOM   1376 N  N    . LYS   A 1 55  ? 23.159 10.029  7.406   1.00 10.20 ?  55   LYS   A N    1 
ATOM   1377 C  CA   . LYS   A 1 55  ? 22.587 11.189  8.082   1.00 10.62 ?  55   LYS   A CA   1 
ATOM   1378 C  C    . LYS   A 1 55  ? 22.481 10.947  9.582   1.00 10.81 ?  55   LYS   A C    1 
ATOM   1379 O  O    . LYS   A 1 55  ? 22.760 11.845  10.387  1.00 11.36 ?  55   LYS   A O    1 
ATOM   1380 C  CB   . LYS   A 1 55  ? 21.221 11.512  7.472   1.00 11.78 ?  55   LYS   A CB   1 
ATOM   1381 C  CG   . LYS   A 1 55  ? 20.483 12.680  8.117   1.00 12.95 ?  55   LYS   A CG   1 
ATOM   1382 C  CD   . LYS   A 1 55  ? 19.158 12.952  7.401   1.00 14.35 ?  55   LYS   A CD   1 
ATOM   1383 C  CE   . LYS   A 1 55  ? 18.349 14.040  8.088   1.00 16.13 ?  55   LYS   A CE   1 
ATOM   1384 N  NZ   . LYS   A 1 55  ? 17.040 14.265  7.413   1.00 16.80 ?  55   LYS   A NZ   1 
ATOM   1385 H  H    A LYS   A 1 55  ? 22.646 9.677   6.809   0.30 12.27 ?  55   LYS   A H    1 
ATOM   1386 H  H    B LYS   A 1 55  ? 22.656 9.688   6.795   0.70 12.27 ?  55   LYS   A H    1 
ATOM   1387 H  HA   . LYS   A 1 55  ? 23.166 11.955  7.942   1.00 12.77 ?  55   LYS   A HA   1 
ATOM   1388 H  HB2  . LYS   A 1 55  ? 21.345 11.732  6.536   1.00 14.16 ?  55   LYS   A HB2  1 
ATOM   1389 H  HB3  . LYS   A 1 55  ? 20.654 10.730  7.552   1.00 14.16 ?  55   LYS   A HB3  1 
ATOM   1390 H  HG2  . LYS   A 1 55  ? 20.286 12.466  9.046   1.00 15.57 ?  55   LYS   A HG2  1 
ATOM   1391 H  HG3  . LYS   A 1 55  ? 21.029 13.478  8.065   1.00 15.57 ?  55   LYS   A HG3  1 
ATOM   1392 H  HD2  . LYS   A 1 55  ? 19.344 13.237  6.493   1.00 17.24 ?  55   LYS   A HD2  1 
ATOM   1393 H  HD3  . LYS   A 1 55  ? 18.630 12.136  7.393   1.00 17.24 ?  55   LYS   A HD3  1 
ATOM   1394 H  HE2  . LYS   A 1 55  ? 18.174 13.773  9.006   1.00 19.39 ?  55   LYS   A HE2  1 
ATOM   1395 H  HE3  . LYS   A 1 55  ? 18.849 14.868  8.069   1.00 19.39 ?  55   LYS   A HE3  1 
ATOM   1396 H  HZ1  . LYS   A 1 55  ? 16.501 14.734  7.944   1.00 20.19 ?  55   LYS   A HZ1  1 
ATOM   1397 H  HZ2  . LYS   A 1 55  ? 17.162 14.717  6.656   1.00 20.19 ?  55   LYS   A HZ2  1 
ATOM   1398 H  HZ3  . LYS   A 1 55  ? 16.653 13.485  7.226   1.00 20.19 ?  55   LYS   A HZ3  1 
ATOM   1399 N  N    . ALA   A 1 56  ? 22.100 9.733   9.979   1.00 11.11 ?  56   ALA   A N    1 
ATOM   1400 C  CA   . ALA   A 1 56  ? 21.973 9.405   11.394  1.00 11.60 ?  56   ALA   A CA   1 
ATOM   1401 C  C    . ALA   A 1 56  ? 23.311 9.435   12.124  1.00 11.49 ?  56   ALA   A C    1 
ATOM   1402 O  O    . ALA   A 1 56  ? 23.326 9.618   13.343  1.00 13.20 ?  56   ALA   A O    1 
ATOM   1403 C  CB   . ALA   A 1 56  ? 21.282 8.042   11.560  1.00 12.88 ?  56   ALA   A CB   1 
ATOM   1404 H  H    . ALA   A 1 56  ? 21.903 9.092   9.446   1.00 13.36 ?  56   ALA   A H    1 
ATOM   1405 H  HA   . ALA   A 1 56  ? 21.410 10.063  11.815  1.00 13.95 ?  56   ALA   A HA   1 
ATOM   1406 H  HB1  . ALA   A 1 56  ? 21.210 7.836   12.508  1.00 15.48 ?  56   ALA   A HB1  1 
ATOM   1407 H  HB2  . ALA   A 1 56  ? 20.397 8.086   11.166  1.00 15.48 ?  56   ALA   A HB2  1 
ATOM   1408 H  HB3  . ALA   A 1 56  ? 21.808 7.358   11.116  1.00 15.48 ?  56   ALA   A HB3  1 
ATOM   1409 N  N    . THR   A 1 57  ? 24.429 9.264   11.408  1.00 10.63 ?  57   THR   A N    1 
ATOM   1410 C  CA   . THR   A 1 57  ? 25.770 9.393   11.985  1.00 10.96 ?  57   THR   A CA   1 
ATOM   1411 C  C    . THR   A 1 57  ? 26.318 10.813  11.913  1.00 11.24 ?  57   THR   A C    1 
ATOM   1412 O  O    . THR   A 1 57  ? 27.502 11.026  12.216  1.00 11.80 ?  57   THR   A O    1 
ATOM   1413 C  CB   . THR   A 1 57  ? 26.789 8.447   11.316  1.00 10.97 ?  57   THR   A CB   1 
ATOM   1414 O  OG1  . THR   A 1 57  ? 27.183 8.947   10.021  1.00 10.50 ?  57   THR   A OG1  1 
ATOM   1415 C  CG2  . THR   A 1 57  ? 26.259 7.019   11.209  1.00 11.09 ?  57   THR   A CG2  1 
ATOM   1416 H  H    . THR   A 1 57  ? 24.436 9.052   10.566  1.00 12.78 ?  57   THR   A H    1 
ATOM   1417 H  HA   . THR   A 1 57  ? 25.720 9.140   12.922  1.00 13.17 ?  57   THR   A HA   1 
ATOM   1418 H  HB   . THR   A 1 57  ? 27.581 8.405   11.885  1.00 13.19 ?  57   THR   A HB   1 
ATOM   1419 H  HG1  . THR   A 1 57  ? 26.511 9.008   9.531   1.00 12.63 ?  57   THR   A HG1  1 
ATOM   1420 H  HG21 . THR   A 1 57  ? 26.903 6.454   10.748  1.00 13.33 ?  57   THR   A HG21 1 
ATOM   1421 H  HG22 . THR   A 1 57  ? 26.101 6.648   12.094  1.00 13.33 ?  57   THR   A HG22 1 
ATOM   1422 H  HG23 . THR   A 1 57  ? 25.427 7.005   10.714  1.00 13.33 ?  57   THR   A HG23 1 
ATOM   1423 N  N    . ASN   A 1 58  ? 25.501 11.784  11.507  1.00 11.63 ?  58   ASN   A N    1 
ATOM   1424 C  CA   . ASN   A 1 58  ? 25.958 13.167  11.408  1.00 12.75 ?  58   ASN   A CA   1 
ATOM   1425 C  C    . ASN   A 1 58  ? 27.105 13.300  10.401  1.00 11.84 ?  58   ASN   A C    1 
ATOM   1426 O  O    . ASN   A 1 58  ? 28.000 14.134  10.562  1.00 12.35 ?  58   ASN   A O    1 
ATOM   1427 C  CB   . ASN   A 1 58  ? 26.334 13.709  12.799  1.00 15.82 ?  58   ASN   A CB   1 
ATOM   1428 C  CG   . ASN   A 1 58  ? 26.692 15.179  12.796  1.00 20.01 ?  58   ASN   A CG   1 
ATOM   1429 O  OD1  . ASN   A 1 58  ? 26.069 15.982  12.109  1.00 21.52 ?  58   ASN   A OD1  1 
ATOM   1430 N  ND2  . ASN   A 1 58  ? 27.699 15.543  13.584  1.00 21.68 ?  58   ASN   A ND2  1 
ATOM   1431 H  H    . ASN   A 1 58  ? 24.678 11.660  11.277  1.00 13.98 ?  58   ASN   A H    1 
ATOM   1432 H  HA   . ASN   A 1 58  ? 25.221 13.699  11.080  1.00 15.32 ?  58   ASN   A HA   1 
ATOM   1433 H  HB2  . ASN   A 1 58  ? 25.576 13.579  13.401  1.00 19.00 ?  58   ASN   A HB2  1 
ATOM   1434 H  HB3  . ASN   A 1 58  ? 27.099 13.219  13.137  1.00 19.00 ?  58   ASN   A HB3  1 
ATOM   1435 H  HD21 . ASN   A 1 58  ? 27.929 16.371  13.621  1.00 26.04 ?  58   ASN   A HD21 1 
ATOM   1436 H  HD22 . ASN   A 1 58  ? 28.104 14.958  14.058  1.00 26.04 ?  58   ASN   A HD22 1 
ATOM   1437 N  N    . ASN   A 1 59  ? 27.088 12.482  9.347   1.00 10.57 ?  59   ASN   A N    1 
ATOM   1438 C  CA   . ASN   A 1 59  ? 28.075 12.460  8.262   1.00 10.48 ?  59   ASN   A CA   1 
ATOM   1439 C  C    . ASN   A 1 59  ? 29.392 11.782  8.650   1.00 9.94  ?  59   ASN   A C    1 
ATOM   1440 O  O    . ASN   A 1 59  ? 30.311 11.745  7.820   1.00 10.57 ?  59   ASN   A O    1 
ATOM   1441 C  CB   . ASN   A 1 59  ? 28.362 13.850  7.665   1.00 10.74 ?  59   ASN   A CB   1 
ATOM   1442 C  CG   . ASN   A 1 59  ? 28.720 13.790  6.197   1.00 10.60 ?  59   ASN   A CG   1 
ATOM   1443 O  OD1  . ASN   A 1 59  ? 28.026 13.159  5.402   1.00 11.02 ?  59   ASN   A OD1  1 
ATOM   1444 N  ND2  . ASN   A 1 59  ? 29.802 14.458  5.821   1.00 11.53 ?  59   ASN   A ND2  1 
ATOM   1445 H  H    . ASN   A 1 59  ? 26.473 11.894  9.229   1.00 12.70 ?  59   ASN   A H    1 
ATOM   1446 H  HA   . ASN   A 1 59  ? 27.698 11.935  7.546   1.00 12.60 ?  59   ASN   A HA   1 
ATOM   1447 H  HB2  . ASN   A 1 59  ? 27.573 14.411  7.750   1.00 12.92 ?  59   ASN   A HB2  1 
ATOM   1448 H  HB3  . ASN   A 1 59  ? 29.109 14.259  8.128   1.00 12.92 ?  59   ASN   A HB3  1 
ATOM   1449 H  HD21 . ASN   A 1 59  ? 30.045 14.463  4.994   1.00 13.86 ?  59   ASN   A HD21 1 
ATOM   1450 H  HD22 . ASN   A 1 59  ? 30.263 14.895  6.403   1.00 13.86 ?  59   ASN   A HD22 1 
ATOM   1451 N  N    . ALA   A 1 60  ? 29.520 11.234  9.858   1.00 10.08 ?  60   ALA   A N    1 
ATOM   1452 C  CA   . ALA   A 1 60  ? 30.759 10.551  10.212  1.00 10.65 ?  60   ALA   A CA   1 
ATOM   1453 C  C    . ALA   A 1 60  ? 30.985 9.319   9.344   1.00 10.44 ?  60   ALA   A C    1 
ATOM   1454 O  O    . ALA   A 1 60  ? 32.130 9.004   8.998   1.00 10.95 ?  60   ALA   A O    1 
ATOM   1455 C  CB   . ALA   A 1 60  ? 30.758 10.193  11.696  1.00 11.18 ?  60   ALA   A CB   1 
ATOM   1456 H  H    . ALA   A 1 60  ? 28.920 11.243  10.472  1.00 12.11 ?  60   ALA   A H    1 
ATOM   1457 H  HA   . ALA   A 1 60  ? 31.500 11.158  10.057  1.00 12.81 ?  60   ALA   A HA   1 
ATOM   1458 H  HB1  . ALA   A 1 60  ? 31.588 9.743   11.912  1.00 13.43 ?  60   ALA   A HB1  1 
ATOM   1459 H  HB2  . ALA   A 1 60  ? 30.680 11.011  12.217  1.00 13.43 ?  60   ALA   A HB2  1 
ATOM   1460 H  HB3  . ALA   A 1 60  ? 30.005 9.612   11.881  1.00 13.43 ?  60   ALA   A HB3  1 
ATOM   1461 N  N    . MET   A 1 61  ? 29.914 8.624   8.961   1.00 9.92  ?  61   MET   A N    1 
ATOM   1462 C  CA   . MET   A 1 61  ? 30.061 7.490   8.054   1.00 9.86  ?  61   MET   A CA   1 
ATOM   1463 C  C    . MET   A 1 61  ? 30.692 7.920   6.731   1.00 9.47  ?  61   MET   A C    1 
ATOM   1464 O  O    . MET   A 1 61  ? 31.584 7.240   6.209   1.00 10.00 ?  61   MET   A O    1 
ATOM   1465 C  CB   . MET   A 1 61  ? 28.699 6.826   7.832   1.00 9.75  ?  61   MET   A CB   1 
ATOM   1466 C  CG   . MET   A 1 61  ? 28.707 5.663   6.851   1.00 10.46 ?  61   MET   A CG   1 
ATOM   1467 S  SD   . MET   A 1 61  ? 27.086 4.904   6.653   1.00 11.18 ?  61   MET   A SD   1 
ATOM   1468 C  CE   . MET   A 1 61  ? 26.966 3.989   8.194   1.00 12.55 ?  61   MET   A CE   1 
ATOM   1469 H  H    . MET   A 1 61  ? 29.105 8.780   9.207   1.00 11.93 ?  61   MET   A H    1 
ATOM   1470 H  HA   . MET   A 1 61  ? 30.639 6.831   8.471   1.00 11.86 ?  61   MET   A HA   1 
ATOM   1471 H  HB2  . MET   A 1 61  ? 28.378 6.487   8.680   1.00 11.73 ?  61   MET   A HB2  1 
ATOM   1472 H  HB3  . MET   A 1 61  ? 28.081 7.490   7.491   1.00 11.73 ?  61   MET   A HB3  1 
ATOM   1473 H  HG2  . MET   A 1 61  ? 28.986 5.978   5.976   1.00 12.58 ?  61   MET   A HG2  1 
ATOM   1474 H  HG3  . MET   A 1 61  ? 29.313 4.978   7.167   1.00 12.58 ?  61   MET   A HG3  1 
ATOM   1475 H  HE1  . MET   A 1 61  ? 26.125 3.505   8.210   1.00 15.08 ?  61   MET   A HE1  1 
ATOM   1476 H  HE2  . MET   A 1 61  ? 27.708 3.370   8.249   1.00 15.08 ?  61   MET   A HE2  1 
ATOM   1477 H  HE3  . MET   A 1 61  ? 27.000 4.614   8.939   1.00 15.08 ?  61   MET   A HE3  1 
ATOM   1478 N  N    . GLN   A 1 62  ? 30.240 9.042   6.171   1.00 9.71  ?  62   GLN   A N    1 
ATOM   1479 C  CA   . GLN   A 1 62  ? 30.800 9.515   4.907   1.00 9.91  ?  62   GLN   A CA   1 
ATOM   1480 C  C    . GLN   A 1 62  ? 32.269 9.906   5.050   1.00 9.71  ?  62   GLN   A C    1 
ATOM   1481 O  O    . GLN   A 1 62  ? 33.083 9.599   4.171   1.00 10.34 ?  62   GLN   A O    1 
ATOM   1482 C  CB   . GLN   A 1 62  ? 29.989 10.697  4.370   1.00 10.03 ?  62   GLN   A CB   1 
ATOM   1483 C  CG   . GLN   A 1 62  ? 30.358 11.060  2.942   1.00 9.91  ?  62   GLN   A CG   1 
ATOM   1484 C  CD   . GLN   A 1 62  ? 30.027 9.925   1.997   1.00 10.19 ?  62   GLN   A CD   1 
ATOM   1485 O  OE1  . GLN   A 1 62  ? 28.851 9.607   1.796   1.00 10.74 ?  62   GLN   A OE1  1 
ATOM   1486 N  NE2  . GLN   A 1 62  ? 31.050 9.258   1.465   1.00 10.88 ?  62   GLN   A NE2  1 
ATOM   1487 H  H    . GLN   A 1 62  ? 29.621 9.539   6.498   1.00 11.68 ?  62   GLN   A H    1 
ATOM   1488 H  HA   . GLN   A 1 62  ? 30.750 8.794   4.260   1.00 11.92 ?  62   GLN   A HA   1 
ATOM   1489 H  HB2  . GLN   A 1 62  ? 29.051 10.471  4.392   1.00 12.06 ?  62   GLN   A HB2  1 
ATOM   1490 H  HB3  . GLN   A 1 62  ? 30.162 11.473  4.926   1.00 12.06 ?  62   GLN   A HB3  1 
ATOM   1491 H  HG2  . GLN   A 1 62  ? 29.845 11.836  2.669   1.00 11.91 ?  62   GLN   A HG2  1 
ATOM   1492 H  HG3  . GLN   A 1 62  ? 31.306 11.240  2.883   1.00 11.91 ?  62   GLN   A HG3  1 
ATOM   1493 H  HE21 . GLN   A 1 62  ? 31.859 9.495   1.642   1.00 13.08 ?  62   GLN   A HE21 1 
ATOM   1494 H  HE22 . GLN   A 1 62  ? 30.906 8.598   0.930   1.00 13.08 ?  62   GLN   A HE22 1 
ATOM   1495 N  N    . VAL   A 1 63  ? 32.624 10.598  6.136   1.00 10.45 ?  63   VAL   A N    1 
ATOM   1496 C  CA   . VAL   A 1 63  ? 34.014 10.995  6.350   1.00 11.29 ?  63   VAL   A CA   1 
ATOM   1497 C  C    . VAL   A 1 63  ? 34.915 9.762   6.410   1.00 10.71 ?  63   VAL   A C    1 
ATOM   1498 O  O    . VAL   A 1 63  ? 35.971 9.702   5.761   1.00 11.19 ?  63   VAL   A O    1 
ATOM   1499 C  CB   . VAL   A 1 63  ? 34.122 11.872  7.611   1.00 12.85 ?  63   VAL   A CB   1 
ATOM   1500 C  CG1  . VAL   A 1 63  ? 35.566 12.116  7.976   1.00 14.44 ?  63   VAL   A CG1  1 
ATOM   1501 C  CG2  . VAL   A 1 63  ? 33.398 13.197  7.389   1.00 13.58 ?  63   VAL   A CG2  1 
ATOM   1502 H  H    . VAL   A 1 63  ? 32.080 10.839  6.758   1.00 12.56 ?  63   VAL   A H    1 
ATOM   1503 H  HA   . VAL   A 1 63  ? 34.297 11.531  5.596   1.00 13.57 ?  63   VAL   A HA   1 
ATOM   1504 H  HB   . VAL   A 1 63  ? 33.692 11.417  8.354   1.00 15.44 ?  63   VAL   A HB   1 
ATOM   1505 H  HG11 . VAL   A 1 63  ? 35.605 12.853  8.603   1.00 17.35 ?  63   VAL   A HG11 1 
ATOM   1506 H  HG12 . VAL   A 1 63  ? 35.927 11.315  8.379   1.00 17.35 ?  63   VAL   A HG12 1 
ATOM   1507 H  HG13 . VAL   A 1 63  ? 36.054 12.339  7.170   1.00 17.35 ?  63   VAL   A HG13 1 
ATOM   1508 H  HG21 . VAL   A 1 63  ? 33.480 13.738  8.191   1.00 16.32 ?  63   VAL   A HG21 1 
ATOM   1509 H  HG22 . VAL   A 1 63  ? 33.807 13.656  6.639   1.00 16.32 ?  63   VAL   A HG22 1 
ATOM   1510 H  HG23 . VAL   A 1 63  ? 32.464 13.023  7.203   1.00 16.32 ?  63   VAL   A HG23 1 
ATOM   1511 N  N    . GLU   A 1 64  ? 34.501 8.752   7.179   1.00 10.74 ?  64   GLU   A N    1 
ATOM   1512 C  CA   . GLU   A 1 64  ? 35.269 7.517   7.274   1.00 10.52 ?  64   GLU   A CA   1 
ATOM   1513 C  C    . GLU   A 1 64  ? 35.358 6.827   5.918   1.00 10.28 ?  64   GLU   A C    1 
ATOM   1514 O  O    . GLU   A 1 64  ? 36.411 6.287   5.543   1.00 10.86 ?  64   GLU   A O    1 
ATOM   1515 C  CB   . GLU   A 1 64  ? 34.585 6.603   8.291   1.00 11.09 ?  64   GLU   A CB   1 
ATOM   1516 C  CG   . GLU   A 1 64  ? 35.244 5.256   8.446   1.00 11.58 ?  64   GLU   A CG   1 
ATOM   1517 C  CD   . GLU   A 1 64  ? 34.374 4.258   9.182   1.00 12.12 ?  64   GLU   A CD   1 
ATOM   1518 O  OE1  . GLU   A 1 64  ? 33.133 4.354   9.050   1.00 13.19 ?  64   GLU   A OE1  1 
ATOM   1519 O  OE2  . GLU   A 1 64  ? 34.938 3.370   9.872   1.00 12.45 -1 64   GLU   A OE2  1 
ATOM   1520 H  H    . GLU   A 1 64  ? 33.772 8.754   7.641   1.00 12.92 ?  64   GLU   A H    1 
ATOM   1521 H  HA   . GLU   A 1 64  ? 36.164 7.717   7.590   1.00 12.64 ?  64   GLU   A HA   1 
ATOM   1522 H  HB2  . GLU   A 1 64  ? 34.594 7.038   9.162   1.00 13.34 ?  64   GLU   A HB2  1 
ATOM   1523 H  HB3  . GLU   A 1 64  ? 33.667 6.459   8.011   1.00 13.34 ?  64   GLU   A HB3  1 
ATOM   1524 H  HG2  . GLU   A 1 64  ? 35.438 4.886   7.570   1.00 13.92 ?  64   GLU   A HG2  1 
ATOM   1525 H  HG3  . GLU   A 1 64  ? 36.064 5.366   8.948   1.00 13.92 ?  64   GLU   A HG3  1 
ATOM   1526 N  N    . SER   A 1 65  ? 34.240 6.808   5.186   1.00 10.12 ?  65   SER   A N    1 
ATOM   1527 C  CA   . SER   A 1 65  ? 34.191 6.147   3.888   1.00 10.00 ?  65   SER   A CA   1 
ATOM   1528 C  C    . SER   A 1 65  ? 35.103 6.822   2.874   1.00 10.26 ?  65   SER   A C    1 
ATOM   1529 O  O    . SER   A 1 65  ? 35.747 6.144   2.064   1.00 11.06 ?  65   SER   A O    1 
ATOM   1530 C  CB   . SER   A 1 65  ? 32.759 6.142   3.358   1.00 10.00 ?  65   SER   A CB   1 
ATOM   1531 O  OG   . SER   A 1 65  ? 31.907 5.335   4.152   1.00 10.45 ?  65   SER   A OG   1 
ATOM   1532 H  H    . SER   A 1 65  ? 33.497 7.174   5.427   1.00 12.17 ?  65   SER   A H    1 
ATOM   1533 H  HA   . SER   A 1 65  ? 34.481 5.230   3.991   1.00 12.03 ?  65   SER   A HA   1 
ATOM   1534 H  HB2  . SER   A 1 65  ? 32.422 7.050   3.362   1.00 12.02 ?  65   SER   A HB2  1 
ATOM   1535 H  HB3  . SER   A 1 65  ? 32.769 5.796   2.454   1.00 12.02 ?  65   SER   A HB3  1 
ATOM   1536 H  HG   . SER   A 1 65  ? 31.901 5.621   4.946   1.00 12.56 ?  65   SER   A HG   1 
ATOM   1537 N  N    . ASP   A 1 66  ? 35.181 8.157   2.897   1.00 10.39 ?  66   ASP   A N    1 
ATOM   1538 C  CA   . ASP   A 1 66  ? 36.035 8.856   1.943   1.00 11.23 ?  66   ASP   A CA   1 
ATOM   1539 C  C    . ASP   A 1 66  ? 37.503 8.509   2.179   1.00 11.29 ?  66   ASP   A C    1 
ATOM   1540 O  O    . ASP   A 1 66  ? 38.274 8.336   1.226   1.00 12.23 ?  66   ASP   A O    1 
ATOM   1541 C  CB   . ASP   A 1 66  ? 35.813 10.362  2.049   1.00 12.51 ?  66   ASP   A CB   1 
ATOM   1542 C  CG   . ASP   A 1 66  ? 34.469 10.816  1.463   1.00 14.06 ?  66   ASP   A CG   1 
ATOM   1543 O  OD1  . ASP   A 1 66  ? 33.756 10.023  0.819   1.00 13.96 ?  66   ASP   A OD1  1 
ATOM   1544 O  OD2  . ASP   A 1 66  ? 34.154 12.012  1.620   1.00 16.86 -1 66   ASP   A OD2  1 
ATOM   1545 H  H    . ASP   A 1 66  ? 34.745 8.672   3.434   1.00 12.50 ?  66   ASP   A H    1 
ATOM   1546 H  HA   . ASP   A 1 66  ? 35.799 8.580   1.042   1.00 13.50 ?  66   ASP   A HA   1 
ATOM   1547 H  HB2  . ASP   A 1 66  ? 35.838 10.617  2.983   1.00 15.04 ?  66   ASP   A HB2  1 
ATOM   1548 H  HB3  . ASP   A 1 66  ? 36.527 10.816  1.565   1.00 15.04 ?  66   ASP   A HB3  1 
ATOM   1549 N  N    . ASP   A 1 67  ? 37.902 8.377   3.443   1.00 11.53 ?  67   ASP   A N    1 
ATOM   1550 C  CA   . ASP   A 1 67  ? 39.259 7.929   3.738   1.00 12.33 ?  67   ASP   A CA   1 
ATOM   1551 C  C    . ASP   A 1 67  ? 39.481 6.496   3.264   1.00 12.34 ?  67   ASP   A C    1 
ATOM   1552 O  O    . ASP   A 1 67  ? 40.543 6.178   2.720   1.00 13.05 ?  67   ASP   A O    1 
ATOM   1553 C  CB   . ASP   A 1 67  ? 39.537 8.058   5.234   1.00 13.59 ?  67   ASP   A CB   1 
ATOM   1554 C  CG   . ASP   A 1 67  ? 40.835 7.399   5.645   1.00 14.90 ?  67   ASP   A CG   1 
ATOM   1555 O  OD1  . ASP   A 1 67  ? 41.907 8.026   5.490   1.00 17.79 ?  67   ASP   A OD1  1 
ATOM   1556 O  OD2  . ASP   A 1 67  ? 40.787 6.241   6.120   1.00 14.26 -1 67   ASP   A OD2  1 
ATOM   1557 H  H    . ASP   A 1 67  ? 37.413 8.540   4.129   1.00 13.86 ?  67   ASP   A H    1 
ATOM   1558 H  HA   . ASP   A 1 67  ? 39.884 8.500   3.266   1.00 14.82 ?  67   ASP   A HA   1 
ATOM   1559 H  HB2  . ASP   A 1 67  ? 39.589 8.995   5.462   1.00 16.33 ?  67   ASP   A HB2  1 
ATOM   1560 H  HB3  . ASP   A 1 67  ? 38.811 7.633   5.723   1.00 16.33 ?  67   ASP   A HB3  1 
ATOM   1561 N  N    A TYR   A 1 68  ? 38.481 5.628   3.435   0.30 11.56 ?  68   TYR   A N    1 
ATOM   1562 N  N    B TYR   A 1 68  ? 38.488 5.614   3.461   0.70 11.78 ?  68   TYR   A N    1 
ATOM   1563 C  CA   A TYR   A 1 68  ? 38.624 4.249   2.981   0.30 11.16 ?  68   TYR   A CA   1 
ATOM   1564 C  CA   B TYR   A 1 68  ? 38.603 4.234   2.980   0.70 12.15 ?  68   TYR   A CA   1 
ATOM   1565 C  C    A TYR   A 1 68  ? 38.841 4.182   1.473   0.30 11.09 ?  68   TYR   A C    1 
ATOM   1566 C  C    B TYR   A 1 68  ? 38.857 4.198   1.476   0.70 11.82 ?  68   TYR   A C    1 
ATOM   1567 O  O    A TYR   A 1 68  ? 39.703 3.433   0.995   0.30 11.23 ?  68   TYR   A O    1 
ATOM   1568 O  O    B TYR   A 1 68  ? 39.748 3.479   1.002   0.70 12.31 ?  68   TYR   A O    1 
ATOM   1569 C  CB   A TYR   A 1 68  ? 37.403 3.420   3.394   0.30 10.98 ?  68   TYR   A CB   1 
ATOM   1570 C  CB   B TYR   A 1 68  ? 37.346 3.407   3.334   0.70 12.75 ?  68   TYR   A CB   1 
ATOM   1571 C  CG   A TYR   A 1 68  ? 37.483 2.004   2.884   0.30 11.34 ?  68   TYR   A CG   1 
ATOM   1572 C  CG   B TYR   A 1 68  ? 37.365 2.039   2.661   0.70 13.46 ?  68   TYR   A CG   1 
ATOM   1573 C  CD1  A TYR   A 1 68  ? 37.007 1.679   1.622   0.30 11.69 ?  68   TYR   A CD1  1 
ATOM   1574 C  CD1  B TYR   A 1 68  ? 36.926 1.891   1.345   0.70 13.66 ?  68   TYR   A CD1  1 
ATOM   1575 C  CD2  A TYR   A 1 68  ? 38.088 1.007   3.635   0.30 12.42 ?  68   TYR   A CD2  1 
ATOM   1576 C  CD2  B TYR   A 1 68  ? 37.887 0.926   3.306   0.70 14.57 ?  68   TYR   A CD2  1 
ATOM   1577 C  CE1  A TYR   A 1 68  ? 37.109 0.400   1.128   0.30 13.12 ?  68   TYR   A CE1  1 
ATOM   1578 C  CE1  B TYR   A 1 68  ? 36.995 0.683   0.700   0.70 13.78 ?  68   TYR   A CE1  1 
ATOM   1579 C  CE2  A TYR   A 1 68  ? 38.189 -0.283  3.150   0.30 13.21 ?  68   TYR   A CE2  1 
ATOM   1580 C  CE2  B TYR   A 1 68  ? 37.945 -0.305  2.667   0.70 13.71 ?  68   TYR   A CE2  1 
ATOM   1581 C  CZ   A TYR   A 1 68  ? 37.698 -0.577  1.897   0.30 13.93 ?  68   TYR   A CZ   1 
ATOM   1582 C  CZ   B TYR   A 1 68  ? 37.503 -0.407  1.366   0.70 13.53 ?  68   TYR   A CZ   1 
ATOM   1583 O  OH   A TYR   A 1 68  ? 37.808 -1.852  1.397   0.30 15.81 ?  68   TYR   A OH   1 
ATOM   1584 O  OH   B TYR   A 1 68  ? 37.590 -1.617  0.735   0.70 14.60 ?  68   TYR   A OH   1 
ATOM   1585 H  H    A TYR   A 1 68  ? 37.721 5.813   3.797   0.30 13.89 ?  68   TYR   A H    1 
ATOM   1586 H  H    B TYR   A 1 68  ? 37.744 5.794   3.861   0.70 14.16 ?  68   TYR   A H    1 
ATOM   1587 H  HA   A TYR   A 1 68  ? 39.400 3.864   3.408   0.30 13.42 ?  68   TYR   A HA   1 
ATOM   1588 H  HA   B TYR   A 1 68  ? 39.358 3.821   3.417   0.70 14.60 ?  68   TYR   A HA   1 
ATOM   1589 H  HB2  A TYR   A 1 68  ? 37.353 3.390   4.361   0.30 13.20 ?  68   TYR   A HB2  1 
ATOM   1590 H  HB2  B TYR   A 1 68  ? 37.310 3.275   4.293   0.70 15.33 ?  68   TYR   A HB2  1 
ATOM   1591 H  HB3  A TYR   A 1 68  ? 36.601 3.829   3.029   0.30 13.20 ?  68   TYR   A HB3  1 
ATOM   1592 H  HB3  B TYR   A 1 68  ? 36.553 3.886   3.033   0.70 15.33 ?  68   TYR   A HB3  1 
ATOM   1593 H  HD1  A TYR   A 1 68  ? 36.610 2.341   1.098   0.30 14.05 ?  68   TYR   A HD1  1 
ATOM   1594 H  HD1  B TYR   A 1 68  ? 36.586 2.627   0.889   0.70 16.41 ?  68   TYR   A HD1  1 
ATOM   1595 H  HD2  A TYR   A 1 68  ? 38.428 1.210   4.475   0.30 14.92 ?  68   TYR   A HD2  1 
ATOM   1596 H  HD2  B TYR   A 1 68  ? 38.200 1.009   4.174   0.70 17.50 ?  68   TYR   A HD2  1 
ATOM   1597 H  HE1  A TYR   A 1 68  ? 36.773 0.200   0.282   0.30 15.77 ?  68   TYR   A HE1  1 
ATOM   1598 H  HE1  B TYR   A 1 68  ? 36.684 0.589   -0.175  0.70 16.56 ?  68   TYR   A HE1  1 
ATOM   1599 H  HE2  A TYR   A 1 68  ? 38.593 -0.946  3.657   0.30 15.88 ?  68   TYR   A HE2  1 
ATOM   1600 H  HE2  B TYR   A 1 68  ? 38.298 -1.047  3.103   0.70 16.48 ?  68   TYR   A HE2  1 
ATOM   1601 H  HH   A TYR   A 1 68  ? 38.174 -2.352  1.954   0.30 19.00 ?  68   TYR   A HH   1 
ATOM   1602 H  HH   B TYR   A 1 68  ? 37.911 -2.206  1.263   0.70 17.55 ?  68   TYR   A HH   1 
ATOM   1603 N  N    . ILE   A 1 69  ? 38.069 4.957   0.706   1.00 10.89 ?  69   ILE   A N    1 
ATOM   1604 C  CA   . ILE   A 1 69  ? 38.207 4.944   -0.748  1.00 11.21 ?  69   ILE   A CA   1 
ATOM   1605 C  C    . ILE   A 1 69  ? 39.536 5.554   -1.172  1.00 11.35 ?  69   ILE   A C    1 
ATOM   1606 O  O    . ILE   A 1 69  ? 40.186 5.068   -2.104  1.00 11.66 ?  69   ILE   A O    1 
ATOM   1607 C  CB   . ILE   A 1 69  ? 37.014 5.660   -1.412  1.00 12.25 ?  69   ILE   A CB   1 
ATOM   1608 C  CG1  . ILE   A 1 69  ? 35.700 4.928   -1.129  1.00 12.50 ?  69   ILE   A CG1  1 
ATOM   1609 C  CG2  . ILE   A 1 69  ? 37.250 5.843   -2.915  1.00 13.78 ?  69   ILE   A CG2  1 
ATOM   1610 C  CD1  . ILE   A 1 69  ? 35.533 3.627   -1.877  1.00 13.26 ?  69   ILE   A CD1  1 
ATOM   1611 H  H    A ILE   A 1 69  ? 37.462 5.491   1.002   0.30 13.09 ?  69   ILE   A H    1 
ATOM   1612 H  H    B ILE   A 1 69  ? 37.452 5.482   1.000   0.70 13.09 ?  69   ILE   A H    1 
ATOM   1613 H  HA   . ILE   A 1 69  ? 38.202 4.023   -1.051  1.00 13.47 ?  69   ILE   A HA   1 
ATOM   1614 H  HB   . ILE   A 1 69  ? 36.946 6.541   -1.019  1.00 14.72 ?  69   ILE   A HB   1 
ATOM   1615 H  HG12 . ILE   A 1 69  ? 35.656 4.731   -0.175  1.00 15.02 ?  69   ILE   A HG12 1 
ATOM   1616 H  HG13 . ILE   A 1 69  ? 34.963 5.509   -1.370  1.00 15.02 ?  69   ILE   A HG13 1 
ATOM   1617 H  HG21 . ILE   A 1 69  ? 36.400 6.050   -3.343  1.00 16.56 ?  69   ILE   A HG21 1 
ATOM   1618 H  HG22 . ILE   A 1 69  ? 37.870 6.575   -3.052  1.00 16.56 ?  69   ILE   A HG22 1 
ATOM   1619 H  HG23 . ILE   A 1 69  ? 37.610 5.024   -3.283  1.00 16.56 ?  69   ILE   A HG23 1 
ATOM   1620 H  HD11 . ILE   A 1 69  ? 34.726 3.191   -1.566  1.00 15.94 ?  69   ILE   A HD11 1 
ATOM   1621 H  HD12 . ILE   A 1 69  ? 35.464 3.816   -2.824  1.00 15.94 ?  69   ILE   A HD12 1 
ATOM   1622 H  HD13 . ILE   A 1 69  ? 36.302 3.062   -1.704  1.00 15.94 ?  69   ILE   A HD13 1 
ATOM   1623 N  N    . ALA   A 1 70  ? 39.951 6.640   -0.519  1.00 11.64 ?  70   ALA   A N    1 
ATOM   1624 C  CA   . ALA   A 1 70  ? 41.228 7.251   -0.869  1.00 12.27 ?  70   ALA   A CA   1 
ATOM   1625 C  C    . ALA   A 1 70  ? 42.380 6.266   -0.698  1.00 12.98 ?  70   ALA   A C    1 
ATOM   1626 O  O    . ALA   A 1 70  ? 43.350 6.301   -1.465  1.00 14.72 ?  70   ALA   A O    1 
ATOM   1627 C  CB   . ALA   A 1 70  ? 41.448 8.505   -0.025  1.00 13.01 ?  70   ALA   A CB   1 
ATOM   1628 H  H    . ALA   A 1 70  ? 39.509 7.040   0.101   1.00 14.00 ?  70   ALA   A H    1 
ATOM   1629 H  HA   . ALA   A 1 70  ? 41.201 7.526   -1.798  1.00 14.75 ?  70   ALA   A HA   1 
ATOM   1630 H  HB1  . ALA   A 1 70  ? 42.302 8.900   -0.265  1.00 15.63 ?  70   ALA   A HB1  1 
ATOM   1631 H  HB2  . ALA   A 1 70  ? 40.733 9.139   -0.201  1.00 15.63 ?  70   ALA   A HB2  1 
ATOM   1632 H  HB3  . ALA   A 1 70  ? 41.448 8.261   0.913   1.00 15.63 ?  70   ALA   A HB3  1 
ATOM   1633 N  N    . THR   A 1 71  ? 42.274 5.356   0.269   1.00 12.47 ?  71   THR   A N    1 
ATOM   1634 C  CA   . THR   A 1 71  ? 43.329 4.380   0.519   1.00 13.40 ?  71   THR   A CA   1 
ATOM   1635 C  C    . THR   A 1 71  ? 43.214 3.163   -0.385  1.00 13.85 ?  71   THR   A C    1 
ATOM   1636 O  O    . THR   A 1 71  ? 44.225 2.667   -0.897  1.00 16.08 ?  71   THR   A O    1 
ATOM   1637 C  CB   . THR   A 1 71  ? 43.266 3.939   1.977   1.00 15.36 ?  71   THR   A CB   1 
ATOM   1638 O  OG1  . THR   A 1 71  ? 43.530 5.066   2.817   1.00 16.92 ?  71   THR   A OG1  1 
ATOM   1639 C  CG2  . THR   A 1 71  ? 44.266 2.820   2.266   1.00 16.87 ?  71   THR   A CG2  1 
ATOM   1640 H  H    . THR   A 1 71  ? 41.588 5.270   0.784   1.00 14.99 ?  71   THR   A H    1 
ATOM   1641 H  HA   . THR   A 1 71  ? 44.188 4.792   0.356   1.00 16.10 ?  71   THR   A HA   1 
ATOM   1642 H  HB   . THR   A 1 71  ? 42.375 3.604   2.165   1.00 18.46 ?  71   THR   A HB   1 
ATOM   1643 H  HG1  . THR   A 1 71  ? 43.498 4.830   3.622   1.00 20.32 ?  71   THR   A HG1  1 
ATOM   1644 H  HG21 . THR   A 1 71  ? 44.399 2.744   3.222   1.00 20.27 ?  71   THR   A HG21 1 
ATOM   1645 H  HG22 . THR   A 1 71  ? 43.930 1.978   1.925   1.00 20.27 ?  71   THR   A HG22 1 
ATOM   1646 H  HG23 . THR   A 1 71  ? 45.115 3.021   1.843   1.00 20.27 ?  71   THR   A HG23 1 
ATOM   1647 N  N    . ASN   A 1 72  ? 41.995 2.653   -0.574  1.00 12.85 ?  72   ASN   A N    1 
ATOM   1648 C  CA   . ASN   A 1 72  ? 41.782 1.330   -1.145  1.00 13.10 ?  72   ASN   A CA   1 
ATOM   1649 C  C    . ASN   A 1 72  ? 41.156 1.326   -2.529  1.00 13.15 ?  72   ASN   A C    1 
ATOM   1650 O  O    . ASN   A 1 72  ? 41.155 0.271   -3.179  1.00 14.66 ?  72   ASN   A O    1 
ATOM   1651 C  CB   . ASN   A 1 72  ? 40.900 0.498   -0.206  1.00 14.03 ?  72   ASN   A CB   1 
ATOM   1652 C  CG   . ASN   A 1 72  ? 41.512 0.343   1.164   1.00 14.84 ?  72   ASN   A CG   1 
ATOM   1653 O  OD1  . ASN   A 1 72  ? 41.043 0.930   2.140   1.00 16.72 ?  72   ASN   A OD1  1 
ATOM   1654 N  ND2  . ASN   A 1 72  ? 42.580 -0.420  1.241   1.00 15.70 ?  72   ASN   A ND2  1 
ATOM   1655 H  H    . ASN   A 1 72  ? 41.258 3.061   -0.370  1.00 15.44 ?  72   ASN   A H    1 
ATOM   1656 H  HA   . ASN   A 1 72  ? 42.636 0.885   -1.214  1.00 15.74 ?  72   ASN   A HA   1 
ATOM   1657 H  HB2  . ASN   A 1 72  ? 40.039 0.930   -0.104  1.00 16.86 ?  72   ASN   A HB2  1 
ATOM   1658 H  HB3  . ASN   A 1 72  ? 40.785 -0.391  -0.582  1.00 16.86 ?  72   ASN   A HB3  1 
ATOM   1659 H  HD21 . ASN   A 1 72  ? 42.974 -0.535  1.999   1.00 18.86 ?  72   ASN   A HD21 1 
ATOM   1660 H  HD22 . ASN   A 1 72  ? 42.890 -0.804  0.536   1.00 18.86 ?  72   ASN   A HD22 1 
ATOM   1661 N  N    . GLY   A 1 73  ? 40.603 2.445   -2.983  1.00 12.58 ?  73   GLY   A N    1 
ATOM   1662 C  CA   . GLY   A 1 73  ? 39.854 2.470   -4.216  1.00 12.36 ?  73   GLY   A CA   1 
ATOM   1663 C  C    . GLY   A 1 73  ? 38.466 1.879   -4.045  1.00 12.02 ?  73   GLY   A C    1 
ATOM   1664 O  O    . GLY   A 1 73  ? 38.087 1.415   -2.962  1.00 12.64 ?  73   GLY   A O    1 
ATOM   1665 H  H    . GLY   A 1 73  ? 40.643 3.216   -2.586  1.00 15.12 ?  73   GLY   A H    1 
ATOM   1666 H  HA2  . GLY   A 1 73  ? 39.769 3.388   -4.525  1.00 14.86 ?  73   GLY   A HA2  1 
ATOM   1667 H  HA3  . GLY   A 1 73  ? 40.326 1.960   -4.889  1.00 14.86 ?  73   GLY   A HA3  1 
ATOM   1668 N  N    . PRO   A 1 74  ? 37.683 1.888   -5.124  1.00 12.76 ?  74   PRO   A N    1 
ATOM   1669 C  CA   . PRO   A 1 74  ? 36.290 1.443   -5.033  1.00 12.69 ?  74   PRO   A CA   1 
ATOM   1670 C  C    . PRO   A 1 74  ? 36.155 -0.040  -4.715  1.00 11.95 ?  74   PRO   A C    1 
ATOM   1671 O  O    . PRO   A 1 74  ? 37.028 -0.865  -5.009  1.00 13.09 ?  74   PRO   A O    1 
ATOM   1672 C  CB   . PRO   A 1 74  ? 35.731 1.741   -6.429  1.00 14.37 ?  74   PRO   A CB   1 
ATOM   1673 C  CG   . PRO   A 1 74  ? 36.655 2.767   -7.015  1.00 17.04 ?  74   PRO   A CG   1 
ATOM   1674 C  CD   . PRO   A 1 74  ? 38.003 2.420   -6.460  1.00 14.82 ?  74   PRO   A CD   1 
ATOM   1675 H  HA   . PRO   A 1 74  ? 35.808 1.962   -4.367  1.00 15.25 ?  74   PRO   A HA   1 
ATOM   1676 H  HB2  . PRO   A 1 74  ? 35.728 0.931   -6.958  1.00 17.27 ?  74   PRO   A HB2  1 
ATOM   1677 H  HB3  . PRO   A 1 74  ? 34.828 2.098   -6.345  1.00 17.27 ?  74   PRO   A HB3  1 
ATOM   1678 H  HG2  . PRO   A 1 74  ? 36.651 2.696   -7.980  1.00 20.48 ?  74   PRO   A HG2  1 
ATOM   1679 H  HG3  . PRO   A 1 74  ? 36.384 3.653   -6.730  1.00 20.48 ?  74   PRO   A HG3  1 
ATOM   1680 H  HD2  . PRO   A 1 74  ? 38.432 1.734   -7.001  1.00 17.81 ?  74   PRO   A HD2  1 
ATOM   1681 H  HD3  . PRO   A 1 74  ? 38.556 3.215   -6.396  1.00 17.81 ?  74   PRO   A HD3  1 
ATOM   1682 N  N    . LEU   A 1 75  ? 35.021 -0.372  -4.110  1.00 11.42 ?  75   LEU   A N    1 
ATOM   1683 C  CA   . LEU   A 1 75  ? 34.640 -1.764  -3.948  1.00 10.97 ?  75   LEU   A CA   1 
ATOM   1684 C  C    . LEU   A 1 75  ? 34.258 -2.363  -5.302  1.00 11.26 ?  75   LEU   A C    1 
ATOM   1685 O  O    . LEU   A 1 75  ? 34.071 -1.659  -6.300  1.00 12.79 ?  75   LEU   A O    1 
ATOM   1686 C  CB   . LEU   A 1 75  ? 33.454 -1.888  -2.993  1.00 10.99 ?  75   LEU   A CB   1 
ATOM   1687 C  CG   . LEU   A 1 75  ? 33.670 -1.478  -1.540  1.00 12.37 ?  75   LEU   A CG   1 
ATOM   1688 C  CD1  . LEU   A 1 75  ? 32.381 -1.644  -0.746  1.00 14.53 ?  75   LEU   A CD1  1 
ATOM   1689 C  CD2  . LEU   A 1 75  ? 34.787 -2.238  -0.886  1.00 15.80 ?  75   LEU   A CD2  1 
ATOM   1690 H  H    . LEU   A 1 75  ? 34.453 0.193   -3.792  1.00 13.73 ?  75   LEU   A H    1 
ATOM   1691 H  HA   . LEU   A 1 75  ? 35.388 -2.263  -3.588  1.00 13.19 ?  75   LEU   A HA   1 
ATOM   1692 H  HB2  . LEU   A 1 75  ? 32.733 -1.339  -3.339  1.00 13.22 ?  75   LEU   A HB2  1 
ATOM   1693 H  HB3  . LEU   A 1 75  ? 33.172 -2.816  -2.988  1.00 13.22 ?  75   LEU   A HB3  1 
ATOM   1694 H  HG   . LEU   A 1 75  ? 33.914 -0.536  -1.515  1.00 14.87 ?  75   LEU   A HG   1 
ATOM   1695 H  HD11 . LEU   A 1 75  ? 32.539 -1.375  0.173   1.00 17.46 ?  75   LEU   A HD11 1 
ATOM   1696 H  HD12 . LEU   A 1 75  ? 31.698 -1.081  -1.143  1.00 17.46 ?  75   LEU   A HD12 1 
ATOM   1697 H  HD13 . LEU   A 1 75  ? 32.110 -2.572  -0.781  1.00 17.46 ?  75   LEU   A HD13 1 
ATOM   1698 H  HD21 . LEU   A 1 75  ? 34.843 -1.987  0.049   1.00 18.98 ?  75   LEU   A HD21 1 
ATOM   1699 H  HD22 . LEU   A 1 75  ? 34.613 -3.189  -0.964  1.00 18.98 ?  75   LEU   A HD22 1 
ATOM   1700 H  HD23 . LEU   A 1 75  ? 35.627 -2.022  -1.331  1.00 18.98 ?  75   LEU   A HD23 1 
ATOM   1701 N  N    . LYS   A 1 76  ? 34.143 -3.689  -5.321  1.00 11.59 ?  76   LYS   A N    1 
ATOM   1702 C  CA   . LYS   A 1 76  ? 33.555 -4.420  -6.435  1.00 12.12 ?  76   LYS   A CA   1 
ATOM   1703 C  C    . LYS   A 1 76  ? 32.042 -4.503  -6.255  1.00 10.91 ?  76   LYS   A C    1 
ATOM   1704 O  O    . LYS   A 1 76  ? 31.544 -4.604  -5.134  1.00 11.07 ?  76   LYS   A O    1 
ATOM   1705 C  CB   . LYS   A 1 76  ? 34.105 -5.853  -6.468  1.00 13.43 ?  76   LYS   A CB   1 
ATOM   1706 C  CG   . LYS   A 1 76  ? 35.610 -5.953  -6.687  1.00 14.82 ?  76   LYS   A CG   1 
ATOM   1707 C  CD   . LYS   A 1 76  ? 36.139 -7.347  -6.435  1.00 15.97 ?  76   LYS   A CD   1 
ATOM   1708 C  CE   . LYS   A 1 76  ? 37.628 -7.422  -6.699  1.00 18.38 ?  76   LYS   A CE   1 
ATOM   1709 N  NZ   . LYS   A 1 76  ? 38.155 -8.787  -6.531  1.00 19.61 ?  76   LYS   A NZ   1 
ATOM   1710 H  H    . LYS   A 1 76  ? 34.405 -4.199  -4.677  1.00 13.93 ?  76   LYS   A H    1 
ATOM   1711 H  HA   . LYS   A 1 76  ? 33.760 -3.976  -7.273  1.00 14.57 ?  76   LYS   A HA   1 
ATOM   1712 H  HB2  . LYS   A 1 76  ? 33.906 -6.280  -5.625  1.00 16.13 ?  76   LYS   A HB2  1 
ATOM   1713 H  HB3  . LYS   A 1 76  ? 33.675 -6.329  -7.193  1.00 16.13 ?  76   LYS   A HB3  1 
ATOM   1714 H  HG2  . LYS   A 1 76  ? 35.816 -5.711  -7.606  1.00 17.80 ?  76   LYS   A HG2  1 
ATOM   1715 H  HG3  . LYS   A 1 76  ? 36.063 -5.344  -6.079  1.00 17.80 ?  76   LYS   A HG3  1 
ATOM   1716 H  HD2  . LYS   A 1 76  ? 35.976 -7.588  -5.510  1.00 19.18 ?  76   LYS   A HD2  1 
ATOM   1717 H  HD3  . LYS   A 1 76  ? 35.687 -7.970  -7.029  1.00 19.18 ?  76   LYS   A HD3  1 
ATOM   1718 H  HE2  . LYS   A 1 76  ? 37.800 -7.140  -7.611  1.00 22.08 ?  76   LYS   A HE2  1 
ATOM   1719 H  HE3  . LYS   A 1 76  ? 38.087 -6.843  -6.075  1.00 22.08 ?  76   LYS   A HE3  1 
ATOM   1720 H  HZ1  . LYS   A 1 76  ? 39.028 -8.805  -6.696  1.00 23.56 ?  76   LYS   A HZ1  1 
ATOM   1721 H  HZ2  . LYS   A 1 76  ? 38.009 -9.078  -5.702  1.00 23.56 ?  76   LYS   A HZ2  1 
ATOM   1722 H  HZ3  . LYS   A 1 76  ? 37.747 -9.348  -7.101  1.00 23.56 ?  76   LYS   A HZ3  1 
ATOM   1723 N  N    . VAL   A 1 77  ? 31.307 -4.492  -7.371  1.00 11.50 ?  77   VAL   A N    1 
ATOM   1724 C  CA   . VAL   A 1 77  ? 29.900 -4.874  -7.302  1.00 11.58 ?  77   VAL   A CA   1 
ATOM   1725 C  C    . VAL   A 1 77  ? 29.834 -6.322  -6.844  1.00 11.18 ?  77   VAL   A C    1 
ATOM   1726 O  O    . VAL   A 1 77  ? 30.500 -7.194  -7.414  1.00 11.63 ?  77   VAL   A O    1 
ATOM   1727 C  CB   . VAL   A 1 77  ? 29.206 -4.673  -8.658  1.00 12.76 ?  77   VAL   A CB   1 
ATOM   1728 C  CG1  . VAL   A 1 77  ? 27.740 -5.094  -8.575  1.00 13.72 ?  77   VAL   A CG1  1 
ATOM   1729 C  CG2  . VAL   A 1 77  ? 29.324 -3.224  -9.109  1.00 13.46 ?  77   VAL   A CG2  1 
ATOM   1730 H  H    . VAL   A 1 77  ? 31.595 -4.282  -8.153  1.00 13.82 ?  77   VAL   A H    1 
ATOM   1731 H  HA   . VAL   A 1 77  ? 29.453 -4.324  -6.641  1.00 13.92 ?  77   VAL   A HA   1 
ATOM   1732 H  HB   . VAL   A 1 77  ? 29.646 -5.228  -9.322  1.00 15.34 ?  77   VAL   A HB   1 
ATOM   1733 H  HG11 . VAL   A 1 77  ? 27.292 -4.827  -9.393  1.00 16.49 ?  77   VAL   A HG11 1 
ATOM   1734 H  HG12 . VAL   A 1 77  ? 27.689 -6.053  -8.467  1.00 16.49 ?  77   VAL   A HG12 1 
ATOM   1735 H  HG13 . VAL   A 1 77  ? 27.329 -4.649  -7.816  1.00 16.49 ?  77   VAL   A HG13 1 
ATOM   1736 H  HG21 . VAL   A 1 77  ? 28.821 -3.109  -9.926  1.00 16.17 ?  77   VAL   A HG21 1 
ATOM   1737 H  HG22 . VAL   A 1 77  ? 28.967 -2.651  -8.412  1.00 16.17 ?  77   VAL   A HG22 1 
ATOM   1738 H  HG23 . VAL   A 1 77  ? 30.260 -3.015  -9.260  1.00 16.17 ?  77   VAL   A HG23 1 
ATOM   1739 N  N    . GLY   A 1 78  ? 29.048 -6.585  -5.795  1.00 10.73 ?  78   GLY   A N    1 
ATOM   1740 C  CA   . GLY   A 1 78  ? 29.030 -7.871  -5.135  1.00 10.78 ?  78   GLY   A CA   1 
ATOM   1741 C  C    . GLY   A 1 78  ? 29.935 -7.955  -3.926  1.00 10.45 ?  78   GLY   A C    1 
ATOM   1742 O  O    . GLY   A 1 78  ? 29.871 -8.953  -3.187  1.00 11.05 ?  78   GLY   A O    1 
ATOM   1743 H  H    . GLY   A 1 78  ? 28.500 -6.016  -5.456  1.00 12.90 ?  78   GLY   A H    1 
ATOM   1744 H  HA2  . GLY   A 1 78  ? 28.124 -8.067  -4.852  1.00 12.96 ?  78   GLY   A HA2  1 
ATOM   1745 H  HA3  . GLY   A 1 78  ? 29.302 -8.556  -5.769  1.00 12.96 ?  78   GLY   A HA3  1 
ATOM   1746 N  N    . GLY   A 1 79  ? 30.781 -6.944  -3.710  1.00 10.51 ?  79   GLY   A N    1 
ATOM   1747 C  CA   . GLY   A 1 79  ? 31.737 -6.945  -2.627  1.00 10.76 ?  79   GLY   A CA   1 
ATOM   1748 C  C    . GLY   A 1 79  ? 31.275 -6.150  -1.417  1.00 10.14 ?  79   GLY   A C    1 
ATOM   1749 O  O    . GLY   A 1 79  ? 30.155 -5.651  -1.344  1.00 10.60 ?  79   GLY   A O    1 
ATOM   1750 H  H    . GLY   A 1 79  ? 30.825 -6.235  -4.197  1.00 12.64 ?  79   GLY   A H    1 
ATOM   1751 H  HA2  . GLY   A 1 79  ? 31.897 -7.866  -2.345  1.00 12.94 ?  79   GLY   A HA2  1 
ATOM   1752 H  HA3  . GLY   A 1 79  ? 32.577 -6.577  -2.935  1.00 12.94 ?  79   GLY   A HA3  1 
ATOM   1753 N  N    . SER   A 1 80  ? 32.177 -6.053  -0.442  1.00 10.91 ?  80   SER   A N    1 
ATOM   1754 C  CA   . SER   A 1 80  ? 31.859 -5.429  0.833   1.00 10.30 ?  80   SER   A CA   1 
ATOM   1755 C  C    . SER   A 1 80  ? 33.123 -4.969  1.538   1.00 10.26 ?  80   SER   A C    1 
ATOM   1756 O  O    . SER   A 1 80  ? 34.242 -5.383  1.208   1.00 11.67 ?  80   SER   A O    1 
ATOM   1757 C  CB   . SER   A 1 80  ? 31.103 -6.394  1.756   1.00 10.97 ?  80   SER   A CB   1 
ATOM   1758 O  OG   . SER   A 1 80  ? 31.936 -7.431  2.247   1.00 12.70 ?  80   SER   A OG   1 
ATOM   1759 H  H    . SER   A 1 80  ? 32.989 -6.328  -0.500  1.00 13.11 ?  80   SER   A H    1 
ATOM   1760 H  HA   . SER   A 1 80  ? 31.301 -4.655  0.664   1.00 12.38 ?  80   SER   A HA   1 
ATOM   1761 H  HB2  . SER   A 1 80  ? 30.748 -5.890  2.507   1.00 13.19 ?  80   SER   A HB2  1 
ATOM   1762 H  HB3  . SER   A 1 80  ? 30.369 -6.790  1.256   1.00 13.19 ?  80   SER   A HB3  1 
ATOM   1763 H  HG   . SER   A 1 80  ? 32.250 -7.870  1.603   1.00 15.26 ?  80   SER   A HG   1 
ATOM   1764 N  N    . CYS   A 1 81  ? 32.919 -4.120  2.542   1.00 9.84  ?  81   CYS   A N    1 
ATOM   1765 C  CA   . CYS   A 1 81  ? 33.965 -3.817  3.507   1.00 10.30 ?  81   CYS   A CA   1 
ATOM   1766 C  C    . CYS   A 1 81  ? 33.322 -3.588  4.867   1.00 9.94  ?  81   CYS   A C    1 
ATOM   1767 O  O    . CYS   A 1 81  ? 32.157 -3.191  4.961   1.00 10.99 ?  81   CYS   A O    1 
ATOM   1768 C  CB   . CYS   A 1 81  ? 34.832 -2.624  3.080   1.00 11.03 ?  81   CYS   A CB   1 
ATOM   1769 S  SG   . CYS   A 1 81  ? 33.922 -1.051  3.094   1.00 10.95 ?  81   CYS   A SG   1 
ATOM   1770 H  H    . CYS   A 1 81  ? 32.176 -3.702  2.688   1.00 11.83 ?  81   CYS   A H    1 
ATOM   1771 H  HA   . CYS   A 1 81  ? 34.544 -4.586  3.585   1.00 12.38 ?  81   CYS   A HA   1 
ATOM   1772 H  HB2  . CYS   A 1 81  ? 35.585 -2.546  3.690   1.00 13.26 ?  81   CYS   A HB2  1 
ATOM   1773 H  HB3  . CYS   A 1 81  ? 35.157 -2.778  2.177   1.00 13.26 ?  81   CYS   A HB3  1 
ATOM   1774 H  HG   . CYS   A 1 81  ? 34.664 -0.168  2.752   1.00 13.16 ?  81   CYS   A HG   1 
ATOM   1775 N  N    . VAL   A 1 82  ? 34.093 -3.843  5.919   1.00 10.42 ?  82   VAL   A N    1 
ATOM   1776 C  CA   . VAL   A 1 82  ? 33.672 -3.603  7.292   1.00 10.74 ?  82   VAL   A CA   1 
ATOM   1777 C  C    . VAL   A 1 82  ? 34.265 -2.285  7.756   1.00 10.90 ?  82   VAL   A C    1 
ATOM   1778 O  O    . VAL   A 1 82  ? 35.487 -2.106  7.738   1.00 12.00 ?  82   VAL   A O    1 
ATOM   1779 C  CB   . VAL   A 1 82  ? 34.108 -4.741  8.227   1.00 12.42 ?  82   VAL   A CB   1 
ATOM   1780 C  CG1  . VAL   A 1 82  ? 33.654 -4.450  9.654   1.00 14.15 ?  82   VAL   A CG1  1 
ATOM   1781 C  CG2  . VAL   A 1 82  ? 33.568 -6.076  7.749   1.00 13.61 ?  82   VAL   A CG2  1 
ATOM   1782 H  H    . VAL   A 1 82  ? 34.893 -4.170  5.865   1.00 12.52 ?  82   VAL   A H    1 
ATOM   1783 H  HA   . VAL   A 1 82  ? 32.705 -3.532  7.327   1.00 12.92 ?  82   VAL   A HA   1 
ATOM   1784 H  HB   . VAL   A 1 82  ? 35.075 -4.791  8.233   1.00 14.92 ?  82   VAL   A HB   1 
ATOM   1785 H  HG11 . VAL   A 1 82  ? 33.749 -5.256  10.187  1.00 17.01 ?  82   VAL   A HG11 1 
ATOM   1786 H  HG12 . VAL   A 1 82  ? 34.200 -3.742  10.029  1.00 17.01 ?  82   VAL   A HG12 1 
ATOM   1787 H  HG13 . VAL   A 1 82  ? 32.720 -4.177  9.642   1.00 17.01 ?  82   VAL   A HG13 1 
ATOM   1788 H  HG21 . VAL   A 1 82  ? 33.820 -6.763  8.385   1.00 16.36 ?  82   VAL   A HG21 1 
ATOM   1789 H  HG22 . VAL   A 1 82  ? 32.604 -6.021  7.682   1.00 16.36 ?  82   VAL   A HG22 1 
ATOM   1790 H  HG23 . VAL   A 1 82  ? 33.951 -6.274  6.880   1.00 16.36 ?  82   VAL   A HG23 1 
ATOM   1791 N  N    . LEU   A 1 83  ? 33.403 -1.367  8.175   1.00 10.42 ?  83   LEU   A N    1 
ATOM   1792 C  CA   . LEU   A 1 83  ? 33.803 -0.091  8.747   1.00 10.49 ?  83   LEU   A CA   1 
ATOM   1793 C  C    . LEU   A 1 83  ? 33.090 0.081   10.082  1.00 10.47 ?  83   LEU   A C    1 
ATOM   1794 O  O    . LEU   A 1 83  ? 32.379 -0.813  10.548  1.00 11.14 ?  83   LEU   A O    1 
ATOM   1795 C  CB   . LEU   A 1 83  ? 33.542 1.062   7.767   1.00 11.12 ?  83   LEU   A CB   1 
ATOM   1796 C  CG   . LEU   A 1 83  ? 34.439 1.057   6.521   1.00 11.94 ?  83   LEU   A CG   1 
ATOM   1797 C  CD1  . LEU   A 1 83  ? 33.989 2.103   5.519   1.00 12.09 ?  83   LEU   A CD1  1 
ATOM   1798 C  CD2  . LEU   A 1 83  ? 35.911 1.262   6.882   1.00 12.77 ?  83   LEU   A CD2  1 
ATOM   1799 H  H    . LEU   A 1 83  ? 32.553 -1.462  8.127   1.00 12.53 ?  83   LEU   A H    1 
ATOM   1800 H  HA   . LEU   A 1 83  ? 34.752 -0.105  8.930   1.00 12.62 ?  83   LEU   A HA   1 
ATOM   1801 H  HB2  . LEU   A 1 83  ? 32.619 1.012   7.464   1.00 13.37 ?  83   LEU   A HB2  1 
ATOM   1802 H  HB3  . LEU   A 1 83  ? 33.682 1.905   8.227   1.00 13.37 ?  83   LEU   A HB3  1 
ATOM   1803 H  HG   . LEU   A 1 83  ? 34.361 0.190   6.097   1.00 14.35 ?  83   LEU   A HG   1 
ATOM   1804 H  HD11 . LEU   A 1 83  ? 34.572 2.061   4.746   1.00 14.54 ?  83   LEU   A HD11 1 
ATOM   1805 H  HD12 . LEU   A 1 83  ? 33.075 1.908   5.255   1.00 14.54 ?  83   LEU   A HD12 1 
ATOM   1806 H  HD13 . LEU   A 1 83  ? 34.039 2.975   5.931   1.00 14.54 ?  83   LEU   A HD13 1 
ATOM   1807 H  HD21 . LEU   A 1 83  ? 36.418 1.403   6.066   1.00 15.35 ?  83   LEU   A HD21 1 
ATOM   1808 H  HD22 . LEU   A 1 83  ? 35.991 2.041   7.457   1.00 15.35 ?  83   LEU   A HD22 1 
ATOM   1809 H  HD23 . LEU   A 1 83  ? 36.239 0.476   7.344   1.00 15.35 ?  83   LEU   A HD23 1 
ATOM   1810 N  N    . SER   A 1 84  ? 33.286 1.235   10.712  1.00 11.43 ?  84   SER   A N    1 
ATOM   1811 C  CA   . SER   A 1 84  ? 32.640 1.482   11.990  1.00 11.61 ?  84   SER   A CA   1 
ATOM   1812 C  C    . SER   A 1 84  ? 31.124 1.563   11.837  1.00 11.37 ?  84   SER   A C    1 
ATOM   1813 O  O    . SER   A 1 84  ? 30.601 2.021   10.822  1.00 11.35 ?  84   SER   A O    1 
ATOM   1814 C  CB   . SER   A 1 84  ? 33.135 2.800   12.572  1.00 12.70 ?  84   SER   A CB   1 
ATOM   1815 O  OG   . SER   A 1 84  ? 32.503 3.082   13.806  1.00 13.68 ?  84   SER   A OG   1 
ATOM   1816 H  H    . SER   A 1 84  ? 33.777 1.880   10.422  1.00 13.74 ?  84   SER   A H    1 
ATOM   1817 H  HA   . SER   A 1 84  ? 32.856 0.766   12.605  1.00 13.95 ?  84   SER   A HA   1 
ATOM   1818 H  HB2  . SER   A 1 84  ? 34.095 2.743   12.709  1.00 15.26 ?  84   SER   A HB2  1 
ATOM   1819 H  HB3  . SER   A 1 84  ? 32.933 3.516   11.950  1.00 15.26 ?  84   SER   A HB3  1 
ATOM   1820 H  HG   . SER   A 1 84  ? 32.796 3.806   14.118  1.00 16.44 ?  84   SER   A HG   1 
ATOM   1821 N  N    . GLY   A 1 85  ? 30.410 1.137   12.879  1.00 12.13 ?  85   GLY   A N    1 
ATOM   1822 C  CA   . GLY   A 1 85  ? 28.988 1.382   12.963  1.00 12.54 ?  85   GLY   A CA   1 
ATOM   1823 C  C    . GLY   A 1 85  ? 28.619 2.691   13.624  1.00 12.30 ?  85   GLY   A C    1 
ATOM   1824 O  O    . GLY   A 1 85  ? 27.427 2.999   13.749  1.00 12.95 ?  85   GLY   A O    1 
ATOM   1825 H  H    . GLY   A 1 85  ? 30.736 0.703   13.549  1.00 14.57 ?  85   GLY   A H    1 
ATOM   1826 H  HA2  . GLY   A 1 85  ? 28.616 1.379   12.065  1.00 15.07 ?  85   GLY   A HA2  1 
ATOM   1827 H  HA3  . GLY   A 1 85  ? 28.572 0.668   13.463  1.00 15.07 ?  85   GLY   A HA3  1 
ATOM   1828 N  N    . HIS   A 1 86  ? 29.606 3.470   14.058  1.00 12.32 ?  86   HIS   A N    1 
ATOM   1829 C  CA   . HIS   A 1 86  ? 29.379 4.807   14.624  1.00 12.91 ?  86   HIS   A CA   1 
ATOM   1830 C  C    . HIS   A 1 86  ? 28.394 4.685   15.780  1.00 13.75 ?  86   HIS   A C    1 
ATOM   1831 O  O    . HIS   A 1 86  ? 28.581 3.810   16.641  1.00 14.63 ?  86   HIS   A O    1 
ATOM   1832 C  CB   . HIS   A 1 86  ? 28.999 5.784   13.517  1.00 12.95 ?  86   HIS   A CB   1 
ATOM   1833 C  CG   . HIS   A 1 86  ? 30.055 5.887   12.478  1.00 12.56 ?  86   HIS   A CG   1 
ATOM   1834 N  ND1  . HIS   A 1 86  ? 31.155 6.709   12.618  1.00 13.75 ?  86   HIS   A ND1  1 
ATOM   1835 C  CD2  . HIS   A 1 86  ? 30.235 5.201   11.328  1.00 12.30 ?  86   HIS   A CD2  1 
ATOM   1836 C  CE1  . HIS   A 1 86  ? 31.950 6.543   11.577  1.00 13.21 ?  86   HIS   A CE1  1 
ATOM   1837 N  NE2  . HIS   A 1 86  ? 31.419 5.630   10.784  1.00 12.47 ?  86   HIS   A NE2  1 
ATOM   1838 H  H    . HIS   A 1 86  ? 30.436 3.247   14.043  1.00 14.81 ?  86   HIS   A H    1 
ATOM   1839 H  HA   . HIS   A 1 86  ? 30.213 5.120   14.997  1.00 15.52 ?  86   HIS   A HA   1 
ATOM   1840 H  HB2  . HIS   A 1 86  ? 28.182 5.485   13.087  1.00 15.57 ?  86   HIS   A HB2  1 
ATOM   1841 H  HB3  . HIS   A 1 86  ? 28.871 6.667   13.897  1.00 15.57 ?  86   HIS   A HB3  1 
ATOM   1842 H  HD2  . HIS   A 1 86  ? 29.668 4.553   10.966  1.00 14.79 ?  86   HIS   A HD2  1 
ATOM   1843 H  HE1  . HIS   A 1 86  ? 32.750 6.992   11.423  1.00 15.88 ?  86   HIS   A HE1  1 
ATOM   1844 H  HE2  . HIS   A 1 86  ? 31.755 5.360   10.032  1.00 14.99 ?  86   HIS   A HE2  1 
ATOM   1845 N  N    . ASN   A 1 87  ? 27.370 5.528   15.842  1.00 14.25 ?  87   ASN   A N    1 
ATOM   1846 C  CA   . ASN   A 1 87  ? 26.375 5.516   16.899  1.00 15.06 ?  87   ASN   A CA   1 
ATOM   1847 C  C    . ASN   A 1 87  ? 25.250 4.523   16.649  1.00 16.12 ?  87   ASN   A C    1 
ATOM   1848 O  O    . ASN   A 1 87  ? 24.316 4.469   17.453  1.00 19.05 ?  87   ASN   A O    1 
ATOM   1849 C  CB   . ASN   A 1 87  ? 25.782 6.925   17.062  1.00 16.20 ?  87   ASN   A CB   1 
ATOM   1850 C  CG   . ASN   A 1 87  ? 25.253 7.504   15.752  1.00 17.23 ?  87   ASN   A CG   1 
ATOM   1851 O  OD1  . ASN   A 1 87  ? 25.879 7.380   14.705  1.00 17.83 ?  87   ASN   A OD1  1 
ATOM   1852 N  ND2  . ASN   A 1 87  ? 24.101 8.155   15.817  1.00 18.66 ?  87   ASN   A ND2  1 
ATOM   1853 H  H    . ASN   A 1 87  ? 27.226 6.138   15.258  1.00 17.12 ?  87   ASN   A H    1 
ATOM   1854 H  HA   . ASN   A 1 87  ? 26.797 5.269   17.736  1.00 18.10 ?  87   ASN   A HA   1 
ATOM   1855 H  HB2  . ASN   A 1 87  ? 25.045 6.887   17.695  1.00 19.46 ?  87   ASN   A HB2  1 
ATOM   1856 H  HB3  . ASN   A 1 87  ? 26.472 7.518   17.395  1.00 19.46 ?  87   ASN   A HB3  1 
ATOM   1857 H  HD21 . ASN   A 1 87  ? 23.764 8.496   15.103  1.00 22.42 ?  87   ASN   A HD21 1 
ATOM   1858 H  HD22 . ASN   A 1 87  ? 23.689 8.230   16.567  1.00 22.42 ?  87   ASN   A HD22 1 
ATOM   1859 N  N    A LEU   A 1 88  ? 25.314 3.742   15.571  0.30 15.34 ?  88   LEU   A N    1 
ATOM   1860 N  N    B LEU   A 1 88  ? 25.324 3.723   15.588  0.70 14.97 ?  88   LEU   A N    1 
ATOM   1861 C  CA   A LEU   A 1 88  ? 24.223 2.853   15.181  0.30 14.96 ?  88   LEU   A CA   1 
ATOM   1862 C  CA   B LEU   A 1 88  ? 24.221 2.854   15.201  0.70 14.54 ?  88   LEU   A CA   1 
ATOM   1863 C  C    A LEU   A 1 88  ? 24.464 1.391   15.532  0.30 14.42 ?  88   LEU   A C    1 
ATOM   1864 C  C    B LEU   A 1 88  ? 24.462 1.378   15.473  0.70 14.11 ?  88   LEU   A C    1 
ATOM   1865 O  O    A LEU   A 1 88  ? 23.501 0.664   15.796  0.30 14.91 ?  88   LEU   A O    1 
ATOM   1866 O  O    B LEU   A 1 88  ? 23.490 0.627   15.606  0.70 15.21 ?  88   LEU   A O    1 
ATOM   1867 C  CB   A LEU   A 1 88  ? 23.978 2.957   13.671  0.30 15.29 ?  88   LEU   A CB   1 
ATOM   1868 C  CB   B LEU   A 1 88  ? 23.930 3.028   13.706  0.70 14.98 ?  88   LEU   A CB   1 
ATOM   1869 C  CG   A LEU   A 1 88  ? 23.735 4.360   13.116  0.30 16.06 ?  88   LEU   A CG   1 
ATOM   1870 C  CG   B LEU   A 1 88  ? 23.612 4.458   13.265  0.70 16.17 ?  88   LEU   A CG   1 
ATOM   1871 C  CD1  A LEU   A 1 88  ? 23.620 4.307   11.603  0.30 16.20 ?  88   LEU   A CD1  1 
ATOM   1872 C  CD1  B LEU   A 1 88  ? 23.372 4.521   11.765  0.70 16.54 ?  88   LEU   A CD1  1 
ATOM   1873 C  CD2  A LEU   A 1 88  ? 22.488 4.982   13.731  0.30 16.99 ?  88   LEU   A CD2  1 
ATOM   1874 C  CD2  B LEU   A 1 88  ? 22.410 5.015   14.025  0.70 17.40 ?  88   LEU   A CD2  1 
ATOM   1875 H  H    A LEU   A 1 88  ? 25.990 3.715   15.042  0.30 18.43 ?  88   LEU   A H    1 
ATOM   1876 H  H    B LEU   A 1 88  ? 26.017 3.660   15.083  0.70 17.99 ?  88   LEU   A H    1 
ATOM   1877 H  HA   A LEU   A 1 88  ? 23.415 3.132   15.628  0.30 17.98 ?  88   LEU   A HA   1 
ATOM   1878 H  HA   B LEU   A 1 88  ? 23.430 3.119   15.692  0.70 17.47 ?  88   LEU   A HA   1 
ATOM   1879 H  HB2  A LEU   A 1 88  ? 24.747 2.598   13.205  0.30 18.38 ?  88   LEU   A HB2  1 
ATOM   1880 H  HB2  B LEU   A 1 88  ? 24.701 2.732   13.205  0.70 18.01 ?  88   LEU   A HB2  1 
ATOM   1881 H  HB3  A LEU   A 1 88  ? 23.193 2.429   13.452  0.30 18.38 ?  88   LEU   A HB3  1 
ATOM   1882 H  HB3  B LEU   A 1 88  ? 23.162 2.479   13.482  0.70 18.01 ?  88   LEU   A HB3  1 
ATOM   1883 H  HG   A LEU   A 1 88  ? 24.493 4.924   13.336  0.30 19.29 ?  88   LEU   A HG   1 
ATOM   1884 H  HG   B LEU   A 1 88  ? 24.375 5.023   13.462  0.70 19.43 ?  88   LEU   A HG   1 
ATOM   1885 H  HD11 A LEU   A 1 88  ? 23.494 5.207   11.262  0.30 19.46 ?  88   LEU   A HD11 1 
ATOM   1886 H  HD11 B LEU   A 1 88  ? 23.177 5.438   11.511  0.70 19.87 ?  88   LEU   A HD11 1 
ATOM   1887 H  HD12 A LEU   A 1 88  ? 24.432 3.925   11.236  0.30 19.46 ?  88   LEU   A HD12 1 
ATOM   1888 H  HD12 B LEU   A 1 88  ? 24.166 4.212   11.301  0.70 19.87 ?  88   LEU   A HD12 1 
ATOM   1889 H  HD13 A LEU   A 1 88  ? 22.858 3.755   11.364  0.30 19.46 ?  88   LEU   A HD13 1 
ATOM   1890 H  HD13 B LEU   A 1 88  ? 22.617 3.952   11.540  0.70 19.87 ?  88   LEU   A HD13 1 
ATOM   1891 H  HD21 A LEU   A 1 88  ? 22.321 5.840   13.311  0.30 20.41 ?  88   LEU   A HD21 1 
ATOM   1892 H  HD21 B LEU   A 1 88  ? 22.155 5.861   13.627  0.70 20.90 ?  88   LEU   A HD21 1 
ATOM   1893 H  HD22 A LEU   A 1 88  ? 21.735 4.389   13.585  0.30 20.41 ?  88   LEU   A HD22 1 
ATOM   1894 H  HD22 B LEU   A 1 88  ? 21.681 4.382   13.961  0.70 20.90 ?  88   LEU   A HD22 1 
ATOM   1895 H  HD23 A LEU   A 1 88  ? 22.634 5.103   14.683  0.30 20.41 ?  88   LEU   A HD23 1 
ATOM   1896 H  HD23 B LEU   A 1 88  ? 22.661 5.145   14.952  0.70 20.90 ?  88   LEU   A HD23 1 
ATOM   1897 N  N    . ALA   A 1 89  ? 25.717 0.948   15.547  1.00 13.83 ?  89   ALA   A N    1 
ATOM   1898 C  CA   . ALA   A 1 89  ? 26.061 -0.460  15.670  1.00 13.40 ?  89   ALA   A CA   1 
ATOM   1899 C  C    . ALA   A 1 89  ? 27.548 -0.508  15.973  1.00 14.07 ?  89   ALA   A C    1 
ATOM   1900 O  O    . ALA   A 1 89  ? 28.246 0.499   15.861  1.00 14.72 ?  89   ALA   A O    1 
ATOM   1901 C  CB   . ALA   A 1 89  ? 25.791 -1.182  14.352  1.00 13.02 ?  89   ALA   A CB   1 
ATOM   1902 H  H    A ALA   A 1 89  ? 26.403 1.465   15.490  0.30 16.62 ?  89   ALA   A H    1 
ATOM   1903 H  H    B ALA   A 1 89  ? 26.402 1.469   15.508  0.70 16.62 ?  89   ALA   A H    1 
ATOM   1904 H  HA   . ALA   A 1 89  ? 25.561 -0.875  16.389  1.00 16.11 ?  89   ALA   A HA   1 
ATOM   1905 H  HB1  . ALA   A 1 89  ? 26.050 -2.113  14.442  1.00 15.65 ?  89   ALA   A HB1  1 
ATOM   1906 H  HB2  . ALA   A 1 89  ? 24.844 -1.122  14.143  1.00 15.65 ?  89   ALA   A HB2  1 
ATOM   1907 H  HB3  . ALA   A 1 89  ? 26.311 -0.763  13.648  1.00 15.65 ?  89   ALA   A HB3  1 
ATOM   1908 N  N    A LYS   A 1 90  ? 28.038 -1.694  16.330  0.30 14.81 ?  90   LYS   A N    1 
ATOM   1909 N  N    B LYS   A 1 90  ? 28.033 -1.682  16.362  0.70 14.04 ?  90   LYS   A N    1 
ATOM   1910 C  CA   A LYS   A 1 90  ? 29.480 -1.848  16.509  0.30 15.77 ?  90   LYS   A CA   1 
ATOM   1911 C  CA   B LYS   A 1 90  ? 29.478 -1.822  16.500  0.70 14.06 ?  90   LYS   A CA   1 
ATOM   1912 C  C    A LYS   A 1 90  ? 30.214 -1.712  15.179  0.30 14.57 ?  90   LYS   A C    1 
ATOM   1913 C  C    B LYS   A 1 90  ? 30.161 -1.629  15.149  0.70 13.72 ?  90   LYS   A C    1 
ATOM   1914 O  O    A LYS   A 1 90  ? 31.235 -1.016  15.088  0.30 15.46 ?  90   LYS   A O    1 
ATOM   1915 O  O    B LYS   A 1 90  ? 31.063 -0.787  15.003  0.70 14.75 ?  90   LYS   A O    1 
ATOM   1916 C  CB   A LYS   A 1 90  ? 29.797 -3.189  17.172  0.30 18.61 ?  90   LYS   A CB   1 
ATOM   1917 C  CB   B LYS   A 1 90  ? 29.834 -3.174  17.122  0.70 16.70 ?  90   LYS   A CB   1 
ATOM   1918 C  CG   A LYS   A 1 90  ? 31.279 -3.388  17.471  0.30 21.66 ?  90   LYS   A CG   1 
ATOM   1919 C  CG   B LYS   A 1 90  ? 31.313 -3.303  17.458  0.70 20.80 ?  90   LYS   A CG   1 
ATOM   1920 C  CD   A LYS   A 1 90  ? 31.504 -4.623  18.329  0.30 24.24 ?  90   LYS   A CD   1 
ATOM   1921 C  CD   B LYS   A 1 90  ? 31.573 -4.494  18.365  0.70 24.47 ?  90   LYS   A CD   1 
ATOM   1922 C  CE   A LYS   A 1 90  ? 32.927 -4.695  18.866  0.30 26.15 ?  90   LYS   A CE   1 
ATOM   1923 C  CE   B LYS   A 1 90  ? 32.991 -4.483  18.915  0.70 27.48 ?  90   LYS   A CE   1 
ATOM   1924 N  NZ   A LYS   A 1 90  ? 33.929 -5.013  17.814  0.30 27.39 ?  90   LYS   A NZ   1 
ATOM   1925 N  NZ   B LYS   A 1 90  ? 34.014 -4.675  17.853  0.70 29.54 ?  90   LYS   A NZ   1 
ATOM   1926 H  H    A LYS   A 1 90  ? 27.570 -2.399  16.480  0.30 17.80 ?  90   LYS   A H    1 
ATOM   1927 H  H    B LYS   A 1 90  ? 27.567 -2.379  16.554  0.70 16.87 ?  90   LYS   A H    1 
ATOM   1928 H  HA   A LYS   A 1 90  ? 29.798 -1.145  17.092  0.30 18.95 ?  90   LYS   A HA   1 
ATOM   1929 H  HA   B LYS   A 1 90  ? 29.802 -1.131  17.094  0.70 16.90 ?  90   LYS   A HA   1 
ATOM   1930 H  HB2  A LYS   A 1 90  ? 29.314 -3.242  18.012  0.30 22.36 ?  90   LYS   A HB2  1 
ATOM   1931 H  HB2  B LYS   A 1 90  ? 29.328 -3.285  17.946  0.70 20.06 ?  90   LYS   A HB2  1 
ATOM   1932 H  HB3  A LYS   A 1 90  ? 29.513 -3.905  16.583  0.30 22.36 ?  90   LYS   A HB3  1 
ATOM   1933 H  HB3  B LYS   A 1 90  ? 29.604 -3.881  16.500  0.70 20.06 ?  90   LYS   A HB3  1 
ATOM   1934 H  HG2  A LYS   A 1 90  ? 31.764 -3.502  16.637  0.30 26.02 ?  90   LYS   A HG2  1 
ATOM   1935 H  HG2  B LYS   A 1 90  ? 31.818 -3.428  16.639  0.70 24.99 ?  90   LYS   A HG2  1 
ATOM   1936 H  HG3  A LYS   A 1 90  ? 31.617 -2.615  17.952  0.30 26.02 ?  90   LYS   A HG3  1 
ATOM   1937 H  HG3  B LYS   A 1 90  ? 31.610 -2.501  17.916  0.70 24.99 ?  90   LYS   A HG3  1 
ATOM   1938 H  HD2  A LYS   A 1 90  ? 30.897 -4.600  19.085  0.30 29.11 ?  90   LYS   A HD2  1 
ATOM   1939 H  HD2  B LYS   A 1 90  ? 30.956 -4.466  19.115  0.70 29.39 ?  90   LYS   A HD2  1 
ATOM   1940 H  HD3  A LYS   A 1 90  ? 31.342 -5.416  17.794  0.30 29.11 ?  90   LYS   A HD3  1 
ATOM   1941 H  HD3  B LYS   A 1 90  ? 31.449 -5.314  17.861  0.70 29.39 ?  90   LYS   A HD3  1 
ATOM   1942 H  HE2  A LYS   A 1 90  ? 33.162 -3.837  19.254  0.30 31.40 ?  90   LYS   A HE2  1 
ATOM   1943 H  HE2  B LYS   A 1 90  ? 33.158 -3.628  19.343  0.70 33.00 ?  90   LYS   A HE2  1 
ATOM   1944 H  HE3  A LYS   A 1 90  ? 32.974 -5.388  19.543  0.30 31.40 ?  90   LYS   A HE3  1 
ATOM   1945 H  HE3  B LYS   A 1 90  ? 33.087 -5.202  19.560  0.70 33.00 ?  90   LYS   A HE3  1 
ATOM   1946 H  HZ1  A LYS   A 1 90  ? 34.739 -5.087  18.178  0.30 32.90 ?  90   LYS   A HZ1  1 
ATOM   1947 H  HZ1  B LYS   A 1 90  ? 34.829 -4.669  18.211  0.70 35.47 ?  90   LYS   A HZ1  1 
ATOM   1948 H  HZ2  A LYS   A 1 90  ? 33.720 -5.781  17.416  0.30 32.90 ?  90   LYS   A HZ2  1 
ATOM   1949 H  HZ2  B LYS   A 1 90  ? 33.884 -5.456  17.444  0.70 35.47 ?  90   LYS   A HZ2  1 
ATOM   1950 H  HZ3  A LYS   A 1 90  ? 33.945 -4.366  17.204  0.30 32.90 ?  90   LYS   A HZ3  1 
ATOM   1951 H  HZ3  B LYS   A 1 90  ? 33.956 -4.022  17.253  0.70 35.47 ?  90   LYS   A HZ3  1 
ATOM   1952 N  N    . HIS   A 1 91  ? 29.704 -2.369  14.139  1.00 12.55 ?  91   HIS   A N    1 
ATOM   1953 C  CA   . HIS   A 1 91  ? 30.285 -2.343  12.810  1.00 11.88 ?  91   HIS   A CA   1 
ATOM   1954 C  C    . HIS   A 1 91  ? 29.198 -2.079  11.784  1.00 10.85 ?  91   HIS   A C    1 
ATOM   1955 O  O    . HIS   A 1 91  ? 28.033 -2.451  11.977  1.00 11.52 ?  91   HIS   A O    1 
ATOM   1956 C  CB   . HIS   A 1 91  ? 30.892 -3.707  12.460  1.00 14.17 ?  91   HIS   A CB   1 
ATOM   1957 C  CG   . HIS   A 1 91  ? 31.873 -4.214  13.466  1.00 18.00 ?  91   HIS   A CG   1 
ATOM   1958 N  ND1  . HIS   A 1 91  ? 33.142 -3.696  13.593  1.00 20.49 ?  91   HIS   A ND1  1 
ATOM   1959 C  CD2  . HIS   A 1 91  ? 31.776 -5.203  14.385  1.00 19.90 ?  91   HIS   A CD2  1 
ATOM   1960 C  CE1  . HIS   A 1 91  ? 33.786 -4.342  14.550  1.00 21.61 ?  91   HIS   A CE1  1 
ATOM   1961 N  NE2  . HIS   A 1 91  ? 32.977 -5.261  15.048  1.00 21.55 ?  91   HIS   A NE2  1 
ATOM   1962 H  H    A HIS   A 1 91  ? 28.993 -2.865  14.188  0.30 15.09 ?  91   HIS   A H    1 
ATOM   1963 H  H    B HIS   A 1 91  ? 29.030 -2.913  14.205  0.70 15.09 ?  91   HIS   A H    1 
ATOM   1964 H  HA   . HIS   A 1 91  ? 30.968 -1.666  12.748  1.00 14.28 ?  91   HIS   A HA   1 
ATOM   1965 H  HB2  . HIS   A 1 91  ? 30.175 -4.362  12.393  1.00 17.03 ?  91   HIS   A HB2  1 
ATOM   1966 H  HB3  . HIS   A 1 91  ? 31.347 -3.636  11.608  1.00 17.03 ?  91   HIS   A HB3  1 
ATOM   1967 H  HD1  . HIS   A 1 91  ? 33.466 -3.052  13.118  1.00 24.61 ?  91   HIS   A HD1  1 
ATOM   1968 H  HD2  . HIS   A 1 91  ? 31.038 -5.743  14.541  1.00 23.91 ?  91   HIS   A HD2  1 
ATOM   1969 H  HE1  . HIS   A 1 91  ? 34.661 -4.171  14.824  1.00 25.96 ?  91   HIS   A HE1  1 
ATOM   1970 N  N    . CYS   A 1 92  ? 29.600 -1.479  10.668  1.00 10.54 ?  92   CYS   A N    1 
ATOM   1971 C  CA   . CYS   A 1 92  ? 28.761 -1.411  9.481   1.00 10.32 ?  92   CYS   A CA   1 
ATOM   1972 C  C    . CYS   A 1 92  ? 29.410 -2.231  8.376   1.00 9.68  ?  92   CYS   A C    1 
ATOM   1973 O  O    . CYS   A 1 92  ? 30.565 -1.980  8.001   1.00 10.74 ?  92   CYS   A O    1 
ATOM   1974 C  CB   . CYS   A 1 92  ? 28.541 0.028   9.018   1.00 10.82 ?  92   CYS   A CB   1 
ATOM   1975 S  SG   . CYS   A 1 92  ? 27.519 0.121   7.506   1.00 10.26 ?  92   CYS   A SG   1 
ATOM   1976 H  H    . CYS   A 1 92  ? 30.368 -1.096  10.577  1.00 12.67 ?  92   CYS   A H    1 
ATOM   1977 H  HA   . CYS   A 1 92  ? 27.896 -1.797  9.684   1.00 12.41 ?  92   CYS   A HA   1 
ATOM   1978 H  HB2  . CYS   A 1 92  ? 28.081 0.524   9.719   1.00 13.01 ?  92   CYS   A HB2  1 
ATOM   1979 H  HB3  . CYS   A 1 92  ? 29.394 0.440   8.826   1.00 13.01 ?  92   CYS   A HB3  1 
ATOM   1980 H  HG   . CYS   A 1 92  ? 27.369 1.271   7.206   1.00 12.33 ?  92   CYS   A HG   1 
ATOM   1981 N  N    . LEU   A 1 93  ? 28.673 -3.220  7.878   1.00 9.63  ?  93   LEU   A N    1 
ATOM   1982 C  CA   . LEU   A 1 93  ? 29.084 -3.983  6.704   1.00 9.54  ?  93   LEU   A CA   1 
ATOM   1983 C  C    . LEU   A 1 93  ? 28.491 -3.299  5.477   1.00 9.07  ?  93   LEU   A C    1 
ATOM   1984 O  O    . LEU   A 1 93  ? 27.276 -3.370  5.251   1.00 9.40  ?  93   LEU   A O    1 
ATOM   1985 C  CB   . LEU   A 1 93  ? 28.612 -5.433  6.813   1.00 9.82  ?  93   LEU   A CB   1 
ATOM   1986 C  CG   . LEU   A 1 93  ? 29.010 -6.329  5.640   1.00 10.15 ?  93   LEU   A CG   1 
ATOM   1987 C  CD1  . LEU   A 1 93  ? 30.515 -6.561  5.621   1.00 11.09 ?  93   LEU   A CD1  1 
ATOM   1988 C  CD2  . LEU   A 1 93  ? 28.258 -7.662  5.681   1.00 10.85 ?  93   LEU   A CD2  1 
ATOM   1989 H  H    . LEU   A 1 93  ? 27.913 -3.469  8.212   1.00 11.58 ?  93   LEU   A H    1 
ATOM   1990 H  HA   . LEU   A 1 93  ? 30.047 -3.969  6.639   1.00 11.48 ?  93   LEU   A HA   1 
ATOM   1991 H  HB2  . LEU   A 1 93  ? 28.989 -5.820  7.621   1.00 11.81 ?  93   LEU   A HB2  1 
ATOM   1992 H  HB3  . LEU   A 1 93  ? 27.645 -5.441  6.872   1.00 11.81 ?  93   LEU   A HB3  1 
ATOM   1993 H  HG   . LEU   A 1 93  ? 28.775 -5.885  4.815   1.00 12.20 ?  93   LEU   A HG   1 
ATOM   1994 H  HD11 . LEU   A 1 93  ? 30.739 -7.176  4.906   1.00 13.33 ?  93   LEU   A HD11 1 
ATOM   1995 H  HD12 . LEU   A 1 93  ? 30.971 -5.711  5.475   1.00 13.33 ?  93   LEU   A HD12 1 
ATOM   1996 H  HD13 . LEU   A 1 93  ? 30.797 -6.934  6.475   1.00 13.33 ?  93   LEU   A HD13 1 
ATOM   1997 H  HD21 . LEU   A 1 93  ? 28.540 -8.207  4.926   1.00 13.04 ?  93   LEU   A HD21 1 
ATOM   1998 H  HD22 . LEU   A 1 93  ? 28.472 -8.122  6.512   1.00 13.04 ?  93   LEU   A HD22 1 
ATOM   1999 H  HD23 . LEU   A 1 93  ? 27.308 -7.493  5.632   1.00 13.04 ?  93   LEU   A HD23 1 
ATOM   2000 N  N    . HIS   A 1 94  ? 29.335 -2.604  4.715   1.00 9.03  ?  94   HIS   A N    1 
ATOM   2001 C  CA   . HIS   A 1 94  ? 28.907 -1.941  3.490   1.00 8.78  ?  94   HIS   A CA   1 
ATOM   2002 C  C    . HIS   A 1 94  ? 28.924 -2.974  2.376   1.00 8.82  ?  94   HIS   A C    1 
ATOM   2003 O  O    . HIS   A 1 94  ? 29.998 -3.485  2.038   1.00 10.40 ?  94   HIS   A O    1 
ATOM   2004 C  CB   . HIS   A 1 94  ? 29.853 -0.785  3.160   1.00 9.39  ?  94   HIS   A CB   1 
ATOM   2005 C  CG   . HIS   A 1 94  ? 29.830 0.312   4.170   1.00 9.38  ?  94   HIS   A CG   1 
ATOM   2006 N  ND1  . HIS   A 1 94  ? 28.950 1.374   4.108   1.00 9.60  ?  94   HIS   A ND1  1 
ATOM   2007 C  CD2  . HIS   A 1 94  ? 30.572 0.488   5.286   1.00 10.01 ?  94   HIS   A CD2  1 
ATOM   2008 C  CE1  . HIS   A 1 94  ? 29.163 2.157   5.152   1.00 9.55  ?  94   HIS   A CE1  1 
ATOM   2009 N  NE2  . HIS   A 1 94  ? 30.140 1.643   5.881   1.00 9.84  ?  94   HIS   A NE2  1 
ATOM   2010 H  H    . HIS   A 1 94  ? 30.171 -2.499  4.898   1.00 10.86 ?  94   HIS   A H    1 
ATOM   2011 H  HA   . HIS   A 1 94  ? 28.003 -1.602  3.597   1.00 10.56 ?  94   HIS   A HA   1 
ATOM   2012 H  HB2  . HIS   A 1 94  ? 30.755 -1.128  3.112   1.00 11.29 ?  94   HIS   A HB2  1 
ATOM   2013 H  HB3  . HIS   A 1 94  ? 29.590 -0.407  2.309   1.00 11.29 ?  94   HIS   A HB3  1 
ATOM   2014 H  HD2  . HIS   A 1 94  ? 31.254 -0.062  5.597   1.00 12.04 ?  94   HIS   A HD2  1 
ATOM   2015 H  HE1  . HIS   A 1 94  ? 28.699 2.943   5.337   1.00 11.48 ?  94   HIS   A HE1  1 
ATOM   2016 H  HE2  . HIS   A 1 94  ? 30.459 1.997   6.601   1.00 11.83 ?  94   HIS   A HE2  1 
ATOM   2017 N  N    . VAL   A 1 95  ? 27.758 -3.293  1.813   1.00 8.58  ?  95   VAL   A N    1 
ATOM   2018 C  CA   . VAL   A 1 95  ? 27.636 -4.333  0.796   1.00 8.80  ?  95   VAL   A CA   1 
ATOM   2019 C  C    . VAL   A 1 95  ? 27.088 -3.707  -0.473  1.00 8.74  ?  95   VAL   A C    1 
ATOM   2020 O  O    . VAL   A 1 95  ? 26.070 -3.000  -0.427  1.00 9.63  ?  95   VAL   A O    1 
ATOM   2021 C  CB   . VAL   A 1 95  ? 26.715 -5.481  1.254   1.00 9.72  ?  95   VAL   A CB   1 
ATOM   2022 C  CG1  . VAL   A 1 95  ? 26.627 -6.541  0.161   1.00 10.36 ?  95   VAL   A CG1  1 
ATOM   2023 C  CG2  . VAL   A 1 95  ? 27.212 -6.077  2.560   1.00 9.95  ?  95   VAL   A CG2  1 
ATOM   2024 H  H    . VAL   A 1 95  ? 27.009 -2.914  2.012   1.00 10.32 ?  95   VAL   A H    1 
ATOM   2025 H  HA   . VAL   A 1 95  ? 28.511 -4.705  0.607   1.00 10.59 ?  95   VAL   A HA   1 
ATOM   2026 H  HB   . VAL   A 1 95  ? 25.826 -5.135  1.406   1.00 11.69 ?  95   VAL   A HB   1 
ATOM   2027 H  HG11 . VAL   A 1 95  ? 26.243 -7.352  0.534   1.00 12.46 ?  95   VAL   A HG11 1 
ATOM   2028 H  HG12 . VAL   A 1 95  ? 26.065 -6.213  -0.558  1.00 12.46 ?  95   VAL   A HG12 1 
ATOM   2029 H  HG13 . VAL   A 1 95  ? 27.520 -6.728  -0.175  1.00 12.46 ?  95   VAL   A HG13 1 
ATOM   2030 H  HG21 . VAL   A 1 95  ? 26.659 -6.843  2.786   1.00 11.96 ?  95   VAL   A HG21 1 
ATOM   2031 H  HG22 . VAL   A 1 95  ? 28.133 -6.355  2.451   1.00 11.96 ?  95   VAL   A HG22 1 
ATOM   2032 H  HG23 . VAL   A 1 95  ? 27.146 -5.406  3.255   1.00 11.96 ?  95   VAL   A HG23 1 
ATOM   2033 N  N    . VAL   A 1 96  ? 27.721 -4.003  -1.607  1.00 8.73  ?  96   VAL   A N    1 
ATOM   2034 C  CA   . VAL   A 1 96  ? 27.310 -3.459  -2.895  1.00 9.70  ?  96   VAL   A CA   1 
ATOM   2035 C  C    . VAL   A 1 96  ? 26.530 -4.517  -3.667  1.00 9.98  ?  96   VAL   A C    1 
ATOM   2036 O  O    . VAL   A 1 96  ? 27.111 -5.463  -4.209  1.00 10.89 ?  96   VAL   A O    1 
ATOM   2037 C  CB   . VAL   A 1 96  ? 28.504 -2.971  -3.717  1.00 10.10 ?  96   VAL   A CB   1 
ATOM   2038 C  CG1  . VAL   A 1 96  ? 28.012 -2.344  -5.009  1.00 10.14 ?  96   VAL   A CG1  1 
ATOM   2039 C  CG2  . VAL   A 1 96  ? 29.348 -1.981  -2.921  1.00 10.50 ?  96   VAL   A CG2  1 
ATOM   2040 H  H    . VAL   A 1 96  ? 28.411 -4.522  -1.654  1.00 10.50 ?  96   VAL   A H    1 
ATOM   2041 H  HA   . VAL   A 1 96  ? 26.721 -2.702  -2.742  1.00 11.66 ?  96   VAL   A HA   1 
ATOM   2042 H  HB   . VAL   A 1 96  ? 29.062 -3.723  -3.943  1.00 12.15 ?  96   VAL   A HB   1 
ATOM   2043 H  HG11 . VAL   A 1 96  ? 28.750 -1.865  -5.425  1.00 12.20 ?  96   VAL   A HG11 1 
ATOM   2044 H  HG12 . VAL   A 1 96  ? 27.697 -3.041  -5.601  1.00 12.20 ?  96   VAL   A HG12 1 
ATOM   2045 H  HG13 . VAL   A 1 96  ? 27.293 -1.723  -4.809  1.00 12.20 ?  96   VAL   A HG13 1 
ATOM   2046 H  HG21 . VAL   A 1 96  ? 30.053 -1.635  -3.488  1.00 12.62 ?  96   VAL   A HG21 1 
ATOM   2047 H  HG22 . VAL   A 1 96  ? 28.782 -1.251  -2.616  1.00 12.62 ?  96   VAL   A HG22 1 
ATOM   2048 H  HG23 . VAL   A 1 96  ? 29.733 -2.438  -2.155  1.00 12.62 ?  96   VAL   A HG23 1 
ATOM   2049 N  N    A GLY   A 1 97  ? 25.208 -4.369  -3.683  0.30 10.19 ?  97   GLY   A N    1 
ATOM   2050 N  N    B GLY   A 1 97  ? 25.210 -4.361  -3.751  0.70 10.11 ?  97   GLY   A N    1 
ATOM   2051 C  CA   A GLY   A 1 97  ? 24.372 -5.127  -4.574  0.30 10.55 ?  97   GLY   A CA   1 
ATOM   2052 C  CA   B GLY   A 1 97  ? 24.433 -5.150  -4.676  0.70 10.87 ?  97   GLY   A CA   1 
ATOM   2053 C  C    A GLY   A 1 97  ? 24.298 -4.429  -5.915  0.30 10.42 ?  97   GLY   A C    1 
ATOM   2054 C  C    B GLY   A 1 97  ? 24.498 -4.554  -6.072  0.70 10.91 ?  97   GLY   A C    1 
ATOM   2055 O  O    A GLY   A 1 97  ? 24.553 -3.225  -6.026  0.30 10.28 ?  97   GLY   A O    1 
ATOM   2056 O  O    B GLY   A 1 97  ? 24.806 -3.367  -6.246  0.70 11.44 ?  97   GLY   A O    1 
ATOM   2057 H  H    A GLY   A 1 97  ? 24.773 -3.823  -3.177  0.30 12.26 ?  97   GLY   A H    1 
ATOM   2058 H  H    B GLY   A 1 97  ? 24.747 -3.804  -3.282  0.70 12.15 ?  97   GLY   A H    1 
ATOM   2059 H  HA2  A GLY   A 1 97  ? 24.748 -6.011  -4.700  0.30 12.69 ?  97   GLY   A HA2  1 
ATOM   2060 H  HA2  B GLY   A 1 97  ? 24.783 -6.057  -4.698  0.70 13.07 ?  97   GLY   A HA2  1 
ATOM   2061 H  HA3  A GLY   A 1 97  ? 23.479 -5.214  -4.199  0.30 12.69 ?  97   GLY   A HA3  1 
ATOM   2062 H  HA3  B GLY   A 1 97  ? 23.507 -5.184  -4.387  0.70 13.07 ?  97   GLY   A HA3  1 
ATOM   2063 N  N    A PRO   A 1 98  ? 23.944 -5.166  -6.964  0.30 9.57  ?  98   PRO   A N    1 
ATOM   2064 N  N    B PRO   A 1 98  ? 24.206 -5.356  -7.098  0.70 11.46 ?  98   PRO   A N    1 
ATOM   2065 C  CA   A PRO   A 1 98  ? 23.856 -4.549  -8.291  0.30 9.47  ?  98   PRO   A CA   1 
ATOM   2066 C  CA   B PRO   A 1 98  ? 24.158 -4.809  -8.459  0.70 12.41 ?  98   PRO   A CA   1 
ATOM   2067 C  C    A PRO   A 1 98  ? 22.746 -3.510  -8.340  0.30 9.18  ?  98   PRO   A C    1 
ATOM   2068 C  C    B PRO   A 1 98  ? 23.048 -3.779  -8.603  0.70 12.49 ?  98   PRO   A C    1 
ATOM   2069 O  O    A PRO   A 1 98  ? 21.679 -3.686  -7.751  0.30 8.80  ?  98   PRO   A O    1 
ATOM   2070 O  O    B PRO   A 1 98  ? 21.962 -3.910  -8.031  0.70 13.34 ?  98   PRO   A O    1 
ATOM   2071 C  CB   A PRO   A 1 98  ? 23.557 -5.736  -9.211  0.30 9.35  ?  98   PRO   A CB   1 
ATOM   2072 C  CB   B PRO   A 1 98  ? 23.896 -6.043  -9.331  0.70 12.84 ?  98   PRO   A CB   1 
ATOM   2073 C  CG   A PRO   A 1 98  ? 22.905 -6.752  -8.320  0.30 9.42  ?  98   PRO   A CG   1 
ATOM   2074 C  CG   B PRO   A 1 98  ? 23.265 -7.041  -8.407  0.70 13.30 ?  98   PRO   A CG   1 
ATOM   2075 C  CD   A PRO   A 1 98  ? 23.580 -6.593  -6.985  0.30 9.31  ?  98   PRO   A CD   1 
ATOM   2076 C  CD   B PRO   A 1 98  ? 23.953 -6.807  -7.083  0.70 11.93 ?  98   PRO   A CD   1 
ATOM   2077 H  HA   A PRO   A 1 98  ? 24.700 -4.142  -8.535  0.30 11.39 ?  98   PRO   A HA   1 
ATOM   2078 H  HA   B PRO   A 1 98  ? 25.013 -4.415  -8.696  0.70 14.91 ?  98   PRO   A HA   1 
ATOM   2079 H  HB2  A PRO   A 1 98  ? 22.952 -5.461  -9.915  0.30 11.24 ?  98   PRO   A HB2  1 
ATOM   2080 H  HB2  B PRO   A 1 98  ? 23.289 -5.809  -10.051 0.70 15.43 ?  98   PRO   A HB2  1 
ATOM   2081 H  HB3  A PRO   A 1 98  ? 24.385 -6.082  -9.578  0.30 11.24 ?  98   PRO   A HB3  1 
ATOM   2082 H  HB3  B PRO   A 1 98  ? 24.734 -6.382  -9.683  0.70 15.43 ?  98   PRO   A HB3  1 
ATOM   2083 H  HG2  A PRO   A 1 98  ? 21.957 -6.567  -8.245  0.30 11.33 ?  98   PRO   A HG2  1 
ATOM   2084 H  HG2  B PRO   A 1 98  ? 22.311 -6.872  -8.331  0.70 15.99 ?  98   PRO   A HG2  1 
ATOM   2085 H  HG3  A PRO   A 1 98  ? 23.055 -7.644  -8.671  0.30 11.33 ?  98   PRO   A HG3  1 
ATOM   2086 H  HG3  B PRO   A 1 98  ? 23.428 -7.944  -8.728  0.70 15.99 ?  98   PRO   A HG3  1 
ATOM   2087 H  HD2  A PRO   A 1 98  ? 22.964 -6.801  -6.261  0.30 11.20 ?  98   PRO   A HD2  1 
ATOM   2088 H  HD2  B PRO   A 1 98  ? 23.370 -7.050  -6.346  0.70 14.34 ?  98   PRO   A HD2  1 
ATOM   2089 H  HD3  A PRO   A 1 98  ? 24.380 -7.142  -6.935  0.30 11.20 ?  98   PRO   A HD3  1 
ATOM   2090 H  HD3  B PRO   A 1 98  ? 24.793 -7.301  -7.045  0.70 14.34 ?  98   PRO   A HD3  1 
ATOM   2091 N  N    A ASN   A 1 99  ? 23.017 -2.410  -9.040  0.30 10.13 ?  99   ASN   A N    1 
ATOM   2092 N  N    B ASN   A 1 99  ? 23.335 -2.744  -9.378  0.70 13.11 ?  99   ASN   A N    1 
ATOM   2093 C  CA   A ASN   A 1 99  ? 22.043 -1.343  -9.251  0.30 11.54 ?  99   ASN   A CA   1 
ATOM   2094 C  CA   B ASN   A 1 99  ? 22.372 -1.701  -9.698  0.70 13.93 ?  99   ASN   A CA   1 
ATOM   2095 C  C    A ASN   A 1 99  ? 21.470 -1.497  -10.656 0.30 13.15 ?  99   ASN   A C    1 
ATOM   2096 C  C    B ASN   A 1 99  ? 21.807 -1.999  -11.082 0.70 14.39 ?  99   ASN   A C    1 
ATOM   2097 O  O    A ASN   A 1 99  ? 22.143 -1.190  -11.647 0.30 13.79 ?  99   ASN   A O    1 
ATOM   2098 O  O    B ASN   A 1 99  ? 22.498 -1.840  -12.093 0.70 14.68 ?  99   ASN   A O    1 
ATOM   2099 C  CB   A ASN   A 1 99  ? 22.695 0.027   -9.078  0.30 11.59 ?  99   ASN   A CB   1 
ATOM   2100 C  CB   B ASN   A 1 99  ? 23.049 -0.336  -9.662  0.70 15.24 ?  99   ASN   A CB   1 
ATOM   2101 C  CG   A ASN   A 1 99  ? 21.679 1.166   -9.035  0.30 11.90 ?  99   ASN   A CG   1 
ATOM   2102 C  CG   B ASN   A 1 99  ? 22.077 0.793   -9.892  0.70 16.37 ?  99   ASN   A CG   1 
ATOM   2103 O  OD1  A ASN   A 1 99  ? 20.653 1.128   -9.717  0.30 12.06 ?  99   ASN   A OD1  1 
ATOM   2104 O  OD1  B ASN   A 1 99  ? 21.142 0.666   -10.674 0.70 16.60 ?  99   ASN   A OD1  1 
ATOM   2105 N  ND2  A ASN   A 1 99  ? 21.970 2.188   -8.235  0.30 11.91 ?  99   ASN   A ND2  1 
ATOM   2106 N  ND2  B ASN   A 1 99  ? 22.288 1.907   -9.204  0.70 17.34 ?  99   ASN   A ND2  1 
ATOM   2107 H  H    A ASN   A 1 99  ? 23.782 -2.253  -9.396  0.30 12.18 ?  99   ASN   A H    1 
ATOM   2108 H  H    B ASN   A 1 99  ? 24.110 -2.617  -9.734  0.70 15.76 ?  99   ASN   A H    1 
ATOM   2109 H  HA   A ASN   A 1 99  ? 21.319 -1.430  -8.608  0.30 13.87 ?  99   ASN   A HA   1 
ATOM   2110 H  HA   B ASN   A 1 99  ? 21.648 -1.713  -9.051  0.70 16.75 ?  99   ASN   A HA   1 
ATOM   2111 H  HB2  A ASN   A 1 99  ? 23.196 0.038   -8.251  0.30 13.93 ?  99   ASN   A HB2  1 
ATOM   2112 H  HB2  B ASN   A 1 99  ? 23.463 -0.209  -8.794  0.70 18.31 ?  99   ASN   A HB2  1 
ATOM   2113 H  HB3  A ASN   A 1 99  ? 23.289 0.186   -9.830  0.30 13.93 ?  99   ASN   A HB3  1 
ATOM   2114 H  HB3  B ASN   A 1 99  ? 23.724 -0.301  -10.359 0.70 18.31 ?  99   ASN   A HB3  1 
ATOM   2115 H  HD21 A ASN   A 1 99  ? 21.429 2.855   -8.174  0.30 14.32 ?  99   ASN   A HD21 1 
ATOM   2116 H  HD21 B ASN   A 1 99  ? 21.760 2.576   -9.298  0.70 20.83 ?  99   ASN   A HD21 1 
ATOM   2117 H  HD22 A ASN   A 1 99  ? 22.697 2.181   -7.777  0.30 14.32 ?  99   ASN   A HD22 1 
ATOM   2118 H  HD22 B ASN   A 1 99  ? 22.955 1.955   -8.661  0.70 20.83 ?  99   ASN   A HD22 1 
ATOM   2119 N  N    A VAL   A 1 100 ? 20.223 -1.975  -10.735 0.30 14.54 ?  100  VAL   A N    1 
ATOM   2120 N  N    B VAL   A 1 100 ? 20.548 -2.439  -11.116 0.70 16.04 ?  100  VAL   A N    1 
ATOM   2121 C  CA   A VAL   A 1 100 ? 19.592 -2.217  -12.031 0.30 15.82 ?  100  VAL   A CA   1 
ATOM   2122 C  CA   B VAL   A 1 100 ? 19.913 -2.827  -12.372 0.70 18.23 ?  100  VAL   A CA   1 
ATOM   2123 C  C    A VAL   A 1 100 ? 19.522 -0.931  -12.843 0.30 16.20 ?  100  VAL   A C    1 
ATOM   2124 C  C    B VAL   A 1 100 ? 19.728 -1.626  -13.285 0.70 18.32 ?  100  VAL   A C    1 
ATOM   2125 O  O    A VAL   A 1 100 ? 19.649 -0.951  -14.073 0.30 15.75 ?  100  VAL   A O    1 
ATOM   2126 O  O    B VAL   A 1 100 ? 19.699 -1.772  -14.514 0.70 19.13 ?  100  VAL   A O    1 
ATOM   2127 C  CB   A VAL   A 1 100 ? 18.205 -2.874  -11.840 0.30 16.90 ?  100  VAL   A CB   1 
ATOM   2128 C  CB   B VAL   A 1 100 ? 18.581 -3.545  -12.083 0.70 20.67 ?  100  VAL   A CB   1 
ATOM   2129 C  CG1  A VAL   A 1 100 ? 17.512 -3.083  -13.179 0.30 17.41 ?  100  VAL   A CG1  1 
ATOM   2130 C  CG1  B VAL   A 1 100 ? 17.810 -3.804  -13.373 0.70 21.54 ?  100  VAL   A CG1  1 
ATOM   2131 C  CG2  A VAL   A 1 100 ? 18.341 -4.203  -11.105 0.30 17.29 ?  100  VAL   A CG2  1 
ATOM   2132 C  CG2  B VAL   A 1 100 ? 18.838 -4.842  -11.342 0.70 21.57 ?  100  VAL   A CG2  1 
ATOM   2133 H  H    A VAL   A 1 100 ? 19.725 -2.164  -10.054 0.30 17.47 ?  100  VAL   A H    1 
ATOM   2134 H  H    B VAL   A 1 100 ? 20.045 -2.525  -10.423 0.70 19.27 ?  100  VAL   A H    1 
ATOM   2135 H  HA   A VAL   A 1 100 ? 20.136 -2.852  -12.523 0.30 19.00 ?  100  VAL   A HA   1 
ATOM   2136 H  HA   B VAL   A 1 100 ? 20.490 -3.458  -12.827 0.70 21.90 ?  100  VAL   A HA   1 
ATOM   2137 H  HB   A VAL   A 1 100 ? 17.646 -2.296  -11.299 0.30 20.31 ?  100  VAL   A HB   1 
ATOM   2138 H  HB   B VAL   A 1 100 ? 18.033 -2.976  -11.518 0.70 24.83 ?  100  VAL   A HB   1 
ATOM   2139 H  HG11 A VAL   A 1 100 ? 16.740 -3.660  -13.051 0.30 20.92 ?  100  VAL   A HG11 1 
ATOM   2140 H  HG11 B VAL   A 1 100 ? 17.098 -4.437  -13.190 0.70 25.88 ?  100  VAL   A HG11 1 
ATOM   2141 H  HG12 A VAL   A 1 100 ? 17.226 -2.225  -13.525 0.30 20.92 ?  100  VAL   A HG12 1 
ATOM   2142 H  HG12 B VAL   A 1 100 ? 17.432 -2.969  -13.694 0.70 25.88 ?  100  VAL   A HG12 1 
ATOM   2143 H  HG13 A VAL   A 1 100 ? 18.134 -3.501  -13.795 0.30 20.92 ?  100  VAL   A HG13 1 
ATOM   2144 H  HG13 B VAL   A 1 100 ? 18.416 -4.171  -14.035 0.70 25.88 ?  100  VAL   A HG13 1 
ATOM   2145 H  HG21 A VAL   A 1 100 ? 17.469 -4.628  -11.050 0.30 20.78 ?  100  VAL   A HG21 1 
ATOM   2146 H  HG21 B VAL   A 1 100 ? 17.991 -5.283  -11.178 0.70 25.91 ?  100  VAL   A HG21 1 
ATOM   2147 H  HG22 A VAL   A 1 100 ? 18.954 -4.775  -11.595 0.30 20.78 ?  100  VAL   A HG22 1 
ATOM   2148 H  HG22 B VAL   A 1 100 ? 19.407 -5.408  -11.887 0.70 25.91 ?  100  VAL   A HG22 1 
ATOM   2149 H  HG23 A VAL   A 1 100 ? 18.683 -4.040  -10.212 0.30 20.78 ?  100  VAL   A HG23 1 
ATOM   2150 H  HG23 B VAL   A 1 100 ? 19.277 -4.643  -10.501 0.70 25.91 ?  100  VAL   A HG23 1 
ATOM   2151 N  N    A ASN   A 1 101 ? 19.334 0.206   -12.177 0.30 16.96 ?  101  ASN   A N    1 
ATOM   2152 N  N    B ASN   A 1 101 ? 19.578 -0.428  -12.715 0.70 18.29 ?  101  ASN   A N    1 
ATOM   2153 C  CA   A ASN   A 1 101 ? 19.283 1.484   -12.875 0.30 17.87 ?  101  ASN   A CA   1 
ATOM   2154 C  CA   B ASN   A 1 101 ? 19.480 0.773   -13.536 0.70 19.16 ?  101  ASN   A CA   1 
ATOM   2155 C  C    A ASN   A 1 101 ? 20.640 1.910   -13.427 0.30 18.85 ?  101  ASN   A C    1 
ATOM   2156 C  C    B ASN   A 1 101 ? 20.771 1.056   -14.292 0.70 20.31 ?  101  ASN   A C    1 
ATOM   2157 O  O    A ASN   A 1 101 ? 20.715 2.935   -14.118 0.30 19.51 ?  101  ASN   A O    1 
ATOM   2158 O  O    B ASN   A 1 101 ? 20.733 1.753   -15.312 0.70 21.18 ?  101  ASN   A O    1 
ATOM   2159 C  CB   A ASN   A 1 101 ? 18.708 2.554   -11.947 0.30 17.32 ?  101  ASN   A CB   1 
ATOM   2160 C  CB   B ASN   A 1 101 ? 19.106 1.978   -12.668 0.70 19.14 ?  101  ASN   A CB   1 
ATOM   2161 C  CG   A ASN   A 1 101 ? 17.351 2.165   -11.384 0.30 16.74 ?  101  ASN   A CG   1 
ATOM   2162 C  CG   B ASN   A 1 101 ? 17.804 1.773   -11.910 0.70 20.07 ?  101  ASN   A CG   1 
ATOM   2163 O  OD1  A ASN   A 1 101 ? 16.495 1.639   -12.098 0.30 16.68 ?  101  ASN   A OD1  1 
ATOM   2164 O  OD1  B ASN   A 1 101 ? 16.835 1.229   -12.445 0.70 21.33 ?  101  ASN   A OD1  1 
ATOM   2165 N  ND2  A ASN   A 1 101 ? 17.153 2.410   -10.093 0.30 16.62 ?  101  ASN   A ND2  1 
ATOM   2166 N  ND2  B ASN   A 1 101 ? 17.779 2.199   -10.654 0.70 20.58 ?  101  ASN   A ND2  1 
ATOM   2167 H  H    A ASN   A 1 101 ? 19.235 0.257   -11.327 0.30 20.37 ?  101  ASN   A H    1 
ATOM   2168 H  H    B ASN   A 1 101 ? 19.524 -0.288  -11.867 0.70 21.98 ?  101  ASN   A H    1 
ATOM   2169 H  HA   A ASN   A 1 101 ? 18.677 1.391   -13.627 0.30 21.46 ?  101  ASN   A HA   1 
ATOM   2170 H  HA   B ASN   A 1 101 ? 18.781 0.650   -14.190 0.70 23.02 ?  101  ASN   A HA   1 
ATOM   2171 H  HB2  A ASN   A 1 101 ? 19.317 2.688   -11.206 0.30 20.80 ?  101  ASN   A HB2  1 
ATOM   2172 H  HB2  B ASN   A 1 101 ? 19.809 2.140   -12.021 0.70 22.99 ?  101  ASN   A HB2  1 
ATOM   2173 H  HB3  A ASN   A 1 101 ? 18.601 3.376   -12.448 0.30 20.80 ?  101  ASN   A HB3  1 
ATOM   2174 H  HB3  B ASN   A 1 101 ? 19.000 2.757   -13.240 0.70 22.99 ?  101  ASN   A HB3  1 
ATOM   2175 H  HD21 A ASN   A 1 101 ? 16.402 2.204   -9.727  0.30 19.97 ?  101  ASN   A HD21 1 
ATOM   2176 H  HD21 B ASN   A 1 101 ? 17.064 2.107   -10.185 0.70 24.72 ?  101  ASN   A HD21 1 
ATOM   2177 H  HD22 A ASN   A 1 101 ? 17.773 2.777   -9.625  0.30 19.97 ?  101  ASN   A HD22 1 
ATOM   2178 H  HD22 B ASN   A 1 101 ? 18.474 2.571   -10.312 0.70 24.72 ?  101  ASN   A HD22 1 
ATOM   2179 N  N    A LYS   A 1 102 ? 21.704 1.158   -13.140 0.30 19.36 ?  102  LYS   A N    1 
ATOM   2180 N  N    B LYS   A 1 102 ? 21.902 0.531   -13.819 0.70 21.94 ?  102  LYS   A N    1 
ATOM   2181 C  CA   A LYS   A 1 102 ? 22.998 1.336   -13.786 0.30 20.21 ?  102  LYS   A CA   1 
ATOM   2182 C  CA   B LYS   A 1 102 ? 23.198 0.694   -14.466 0.70 23.20 ?  102  LYS   A CA   1 
ATOM   2183 C  C    A LYS   A 1 102 ? 23.286 0.259   -14.820 0.30 20.50 ?  102  LYS   A C    1 
ATOM   2184 C  C    B LYS   A 1 102 ? 23.564 -0.486  -15.360 0.70 22.91 ?  102  LYS   A C    1 
ATOM   2185 O  O    A LYS   A 1 102 ? 24.353 0.288   -15.444 0.30 20.66 ?  102  LYS   A O    1 
ATOM   2186 O  O    B LYS   A 1 102 ? 24.691 -0.543  -15.863 0.70 23.58 ?  102  LYS   A O    1 
ATOM   2187 C  CB   A LYS   A 1 102 ? 24.119 1.352   -12.740 0.30 20.82 ?  102  LYS   A CB   1 
ATOM   2188 C  CB   B LYS   A 1 102 ? 24.297 0.890   -13.415 0.70 26.01 ?  102  LYS   A CB   1 
ATOM   2189 C  CG   A LYS   A 1 102 ? 24.053 2.517   -11.771 0.30 21.06 ?  102  LYS   A CG   1 
ATOM   2190 C  CG   B LYS   A 1 102 ? 24.231 2.202   -12.655 0.70 28.92 ?  102  LYS   A CG   1 
ATOM   2191 C  CD   A LYS   A 1 102 ? 25.184 2.447   -10.755 0.30 21.37 ?  102  LYS   A CD   1 
ATOM   2192 C  CD   B LYS   A 1 102 ? 25.357 2.290   -11.631 0.70 31.86 ?  102  LYS   A CD   1 
ATOM   2193 C  CE   A LYS   A 1 102 ? 25.181 3.653   -9.832  0.30 21.77 ?  102  LYS   A CE   1 
ATOM   2194 C  CE   B LYS   A 1 102 ? 25.644 3.731   -11.243 0.70 34.11 ?  102  LYS   A CE   1 
ATOM   2195 N  NZ   A LYS   A 1 102 ? 26.233 3.548   -8.781  0.30 21.88 ?  102  LYS   A NZ   1 
ATOM   2196 N  NZ   B LYS   A 1 102 ? 24.409 4.458   -10.845 0.70 35.48 ?  102  LYS   A NZ   1 
ATOM   2197 H  H    A LYS   A 1 102 ? 21.700 0.523   -12.558 0.30 23.26 ?  102  LYS   A H    1 
ATOM   2198 H  H    B LYS   A 1 102 ? 21.943 0.058   -13.099 0.70 26.35 ?  102  LYS   A H    1 
ATOM   2199 H  HA   A LYS   A 1 102 ? 23.009 2.183   -14.246 0.30 24.27 ?  102  LYS   A HA   1 
ATOM   2200 H  HA   B LYS   A 1 102 ? 23.178 1.490   -15.013 0.70 27.87 ?  102  LYS   A HA   1 
ATOM   2201 H  HB2  A LYS   A 1 102 ? 24.073 0.535   -12.219 0.30 25.01 ?  102  LYS   A HB2  1 
ATOM   2202 H  HB2  B LYS   A 1 102 ? 24.239 0.175   -12.762 0.70 31.24 ?  102  LYS   A HB2  1 
ATOM   2203 H  HB3  A LYS   A 1 102 ? 24.972 1.400   -13.198 0.30 25.01 ?  102  LYS   A HB3  1 
ATOM   2204 H  HB3  B LYS   A 1 102 ? 25.162 0.857   -13.856 0.70 31.24 ?  102  LYS   A HB3  1 
ATOM   2205 H  HG2  A LYS   A 1 102 ? 24.134 3.350   -12.263 0.30 25.30 ?  102  LYS   A HG2  1 
ATOM   2206 H  HG2  B LYS   A 1 102 ? 24.325 2.943   -13.275 0.70 34.73 ?  102  LYS   A HG2  1 
ATOM   2207 H  HG3  A LYS   A 1 102 ? 23.209 2.491   -11.292 0.30 25.30 ?  102  LYS   A HG3  1 
ATOM   2208 H  HG3  B LYS   A 1 102 ? 23.385 2.262   -12.183 0.70 34.73 ?  102  LYS   A HG3  1 
ATOM   2209 H  HD2  A LYS   A 1 102 ? 25.078 1.649   -10.214 0.30 25.67 ?  102  LYS   A HD2  1 
ATOM   2210 H  HD2  B LYS   A 1 102 ? 25.102 1.805   -10.830 0.70 38.26 ?  102  LYS   A HD2  1 
ATOM   2211 H  HD3  A LYS   A 1 102 ? 26.033 2.424   -11.224 0.30 25.67 ?  102  LYS   A HD3  1 
ATOM   2212 H  HD3  B LYS   A 1 102 ? 26.166 1.910   -12.009 0.70 38.26 ?  102  LYS   A HD3  1 
ATOM   2213 H  HE2  A LYS   A 1 102 ? 25.352 4.453   -10.354 0.30 26.14 ?  102  LYS   A HE2  1 
ATOM   2214 H  HE2  B LYS   A 1 102 ? 26.258 3.742   -10.490 0.70 40.95 ?  102  LYS   A HE2  1 
ATOM   2215 H  HE3  A LYS   A 1 102 ? 24.318 3.717   -9.394  0.30 26.14 ?  102  LYS   A HE3  1 
ATOM   2216 H  HE3  B LYS   A 1 102 ? 26.038 4.193   -12.000 0.70 40.95 ?  102  LYS   A HE3  1 
ATOM   2217 H  HZ1  A LYS   A 1 102 ? 26.209 4.266   -8.255  0.30 26.28 ?  102  LYS   A HZ1  1 
ATOM   2218 H  HZ1  B LYS   A 1 102 ? 24.616 5.278   -10.568 0.70 42.60 ?  102  LYS   A HZ1  1 
ATOM   2219 H  HZ2  A LYS   A 1 102 ? 26.094 2.822   -8.285  0.30 26.28 ?  102  LYS   A HZ2  1 
ATOM   2220 H  HZ2  B LYS   A 1 102 ? 23.855 4.518   -11.538 0.70 42.60 ?  102  LYS   A HZ2  1 
ATOM   2221 H  HZ3  A LYS   A 1 102 ? 27.036 3.492   -9.159  0.30 26.28 ?  102  LYS   A HZ3  1 
ATOM   2222 H  HZ3  B LYS   A 1 102 ? 24.002 4.024   -10.184 0.70 42.60 ?  102  LYS   A HZ3  1 
ATOM   2223 N  N    A GLY   A 1 103 ? 22.368 -0.685  -15.021 0.30 21.09 ?  103  GLY   A N    1 
ATOM   2224 N  N    B GLY   A 1 103 ? 22.652 -1.433  -15.560 0.70 21.89 ?  103  GLY   A N    1 
ATOM   2225 C  CA   A GLY   A 1 103 ? 22.599 -1.778  -15.943 0.30 21.80 ?  103  GLY   A CA   1 
ATOM   2226 C  CA   B GLY   A 1 103 ? 22.953 -2.596  -16.370 0.70 21.97 ?  103  GLY   A CA   1 
ATOM   2227 C  C    A GLY   A 1 103 ? 23.497 -2.866  -15.407 0.30 22.27 ?  103  GLY   A C    1 
ATOM   2228 C  C    B GLY   A 1 103 ? 23.759 -3.671  -15.677 0.70 20.92 ?  103  GLY   A C    1 
ATOM   2229 O  O    A GLY   A 1 103 ? 24.105 -3.596  -16.196 0.30 22.71 ?  103  GLY   A O    1 
ATOM   2230 O  O    B GLY   A 1 103 ? 24.210 -4.611  -16.343 0.70 21.98 ?  103  GLY   A O    1 
ATOM   2231 H  H    A GLY   A 1 103 ? 21.603 -0.714  -14.633 0.30 25.33 ?  103  GLY   A H    1 
ATOM   2232 H  H    B GLY   A 1 103 ? 21.853 -1.415  -15.241 0.70 26.30 ?  103  GLY   A H    1 
ATOM   2233 H  HA2  A GLY   A 1 103 ? 21.743 -2.168  -16.195 0.30 26.18 ?  103  GLY   A HA2  1 
ATOM   2234 H  HA2  B GLY   A 1 103 ? 22.124 -2.998  -16.661 0.70 26.38 ?  103  GLY   A HA2  1 
ATOM   2235 H  HA3  A GLY   A 1 103 ? 23.020 -1.437  -16.744 0.30 26.18 ?  103  GLY   A HA3  1 
ATOM   2236 H  HA3  B GLY   A 1 103 ? 23.439 -2.303  -17.160 0.70 26.38 ?  103  GLY   A HA3  1 
ATOM   2237 N  N    A GLU   A 1 104 ? 23.615 -2.989  -14.088 0.30 22.12 ?  104  GLU   A N    1 
ATOM   2238 N  N    B GLU   A 1 104 ? 23.946 -3.575  -14.366 0.70 18.65 ?  104  GLU   A N    1 
ATOM   2239 C  CA   A GLU   A 1 104 ? 24.496 -3.982  -13.495 0.30 22.07 ?  104  GLU   A CA   1 
ATOM   2240 C  CA   B GLU   A 1 104 ? 24.780 -4.531  -13.654 0.70 16.58 ?  104  GLU   A CA   1 
ATOM   2241 C  C    A GLU   A 1 104 ? 23.809 -5.340  -13.400 0.30 22.32 ?  104  GLU   A C    1 
ATOM   2242 C  C    B GLU   A 1 104 ? 24.052 -5.864  -13.489 0.70 16.64 ?  104  GLU   A C    1 
ATOM   2243 O  O    A GLU   A 1 104 ? 22.591 -5.439  -13.222 0.30 22.33 ?  104  GLU   A O    1 
ATOM   2244 O  O    B GLU   A 1 104 ? 22.825 -5.921  -13.360 0.70 17.76 ?  104  GLU   A O    1 
ATOM   2245 C  CB   A GLU   A 1 104 ? 24.977 -3.508  -12.123 0.30 22.02 ?  104  GLU   A CB   1 
ATOM   2246 C  CB   B GLU   A 1 104 ? 25.227 -3.943  -12.312 0.70 15.40 ?  104  GLU   A CB   1 
ATOM   2247 C  CG   A GLU   A 1 104 ? 25.939 -2.328  -12.225 0.30 22.17 ?  104  GLU   A CG   1 
ATOM   2248 C  CG   B GLU   A 1 104 ? 26.103 -2.699  -12.505 0.70 15.68 ?  104  GLU   A CG   1 
ATOM   2249 C  CD   A GLU   A 1 104 ? 26.207 -1.648  -10.892 0.30 22.28 ?  104  GLU   A CD   1 
ATOM   2250 C  CD   B GLU   A 1 104 ? 26.435 -1.929  -11.230 0.70 15.18 ?  104  GLU   A CD   1 
ATOM   2251 O  OE1  A GLU   A 1 104 ? 25.563 -2.013  -9.888  0.30 22.10 ?  104  GLU   A OE1  1 
ATOM   2252 O  OE1  B GLU   A 1 104 ? 25.912 -2.252  -10.144 0.70 15.19 ?  104  GLU   A OE1  1 
ATOM   2253 O  OE2  A GLU   A 1 104 ? 27.061 -0.737  -10.853 0.30 22.79 -1 104  GLU   A OE2  1 
ATOM   2254 O  OE2  B GLU   A 1 104 ? 27.233 -0.970  -11.337 0.70 15.99 -1 104  GLU   A OE2  1 
ATOM   2255 H  H    A GLU   A 1 104 ? 23.204 -2.498  -13.515 0.30 26.57 ?  104  GLU   A H    1 
ATOM   2256 H  H    B GLU   A 1 104 ? 23.598 -2.964  -13.874 0.70 22.41 ?  104  GLU   A H    1 
ATOM   2257 H  HA   A GLU   A 1 104 ? 25.271 -4.089  -14.060 0.30 26.51 ?  104  GLU   A HA   1 
ATOM   2258 H  HA   B GLU   A 1 104 ? 25.579 -4.692  -14.181 0.70 19.92 ?  104  GLU   A HA   1 
ATOM   2259 H  HB2  A GLU   A 1 104 ? 24.211 -3.229  -11.595 0.30 26.45 ?  104  GLU   A HB2  1 
ATOM   2260 H  HB2  B GLU   A 1 104 ? 24.449 -3.689  -11.798 0.70 18.51 ?  104  GLU   A HB2  1 
ATOM   2261 H  HB3  A GLU   A 1 104 ? 25.439 -4.237  -11.677 0.30 26.45 ?  104  GLU   A HB3  1 
ATOM   2262 H  HB3  B GLU   A 1 104 ? 25.749 -4.607  -11.835 0.70 18.51 ?  104  GLU   A HB3  1 
ATOM   2263 H  HG2  A GLU   A 1 104 ? 26.785 -2.646  -12.584 0.30 26.63 ?  104  GLU   A HG2  1 
ATOM   2264 H  HG2  B GLU   A 1 104 ? 26.943 -2.968  -12.911 0.70 18.84 ?  104  GLU   A HG2  1 
ATOM   2265 H  HG3  A GLU   A 1 104 ? 25.559 -1.668  -12.828 0.30 26.63 ?  104  GLU   A HG3  1 
ATOM   2266 H  HG3  B GLU   A 1 104 ? 25.642 -2.081  -13.096 0.70 18.84 ?  104  GLU   A HG3  1 
ATOM   2267 N  N    A ASP   A 1 105 ? 24.618 -6.391  -13.520 0.30 22.77 ?  105  ASP   A N    1 
ATOM   2268 N  N    B ASP   A 1 105 ? 24.836 -6.943  -13.507 0.70 16.93 ?  105  ASP   A N    1 
ATOM   2269 C  CA   A ASP   A 1 105 ? 24.111 -7.754  -13.610 0.30 23.34 ?  105  ASP   A CA   1 
ATOM   2270 C  CA   B ASP   A 1 105 ? 24.317 -8.307  -13.580 0.70 17.73 ?  105  ASP   A CA   1 
ATOM   2271 C  C    A ASP   A 1 105 ? 23.410 -8.141  -12.315 0.30 22.74 ?  105  ASP   A C    1 
ATOM   2272 C  C    B ASP   A 1 105 ? 23.598 -8.686  -12.289 0.70 15.90 ?  105  ASP   A C    1 
ATOM   2273 O  O    A ASP   A 1 105 ? 24.006 -8.080  -11.235 0.30 22.37 ?  105  ASP   A O    1 
ATOM   2274 O  O    B ASP   A 1 105 ? 24.213 -8.727  -11.222 0.70 14.54 ?  105  ASP   A O    1 
ATOM   2275 C  CB   A ASP   A 1 105 ? 25.281 -8.699  -13.885 0.30 24.56 ?  105  ASP   A CB   1 
ATOM   2276 C  CB   B ASP   A 1 105 ? 25.498 -9.247  -13.823 0.70 20.61 ?  105  ASP   A CB   1 
ATOM   2277 C  CG   A ASP   A 1 105 ? 24.829 -10.105 -14.203 0.30 25.66 ?  105  ASP   A CG   1 
ATOM   2278 C  CG   B ASP   A 1 105 ? 25.093 -10.701 -13.932 0.70 23.33 ?  105  ASP   A CG   1 
ATOM   2279 O  OD1  A ASP   A 1 105 ? 23.606 -10.321 -14.327 0.30 25.87 ?  105  ASP   A OD1  1 
ATOM   2280 O  OD1  B ASP   A 1 105 ? 23.881 -10.992 -13.985 0.70 23.74 ?  105  ASP   A OD1  1 
ATOM   2281 O  OD2  A ASP   A 1 105 ? 25.697 -10.993 -14.336 0.30 26.44 -1 105  ASP   A OD2  1 
ATOM   2282 O  OD2  B ASP   A 1 105 ? 26.009 -11.557 -13.965 0.70 25.21 -1 105  ASP   A OD2  1 
ATOM   2283 H  H    A ASP   A 1 105 ? 25.474 -6.343  -13.539 0.30 27.34 ?  105  ASP   A H    1 
ATOM   2284 H  H    B ASP   A 1 105 ? 25.696 -6.904  -13.478 0.70 20.35 ?  105  ASP   A H    1 
ATOM   2285 H  HA   A ASP   A 1 105 ? 23.481 -7.833  -14.343 0.30 28.04 ?  105  ASP   A HA   1 
ATOM   2286 H  HA   B ASP   A 1 105 ? 23.694 -8.383  -14.314 0.70 21.30 ?  105  ASP   A HA   1 
ATOM   2287 H  HB2  A ASP   A 1 105 ? 25.783 -8.375  -14.652 0.30 29.50 ?  105  ASP   A HB2  1 
ATOM   2288 H  HB2  B ASP   A 1 105 ? 25.936 -8.991  -14.648 0.70 24.76 ?  105  ASP   A HB2  1 
ATOM   2289 H  HB3  A ASP   A 1 105 ? 25.861 -8.730  -13.106 0.30 29.50 ?  105  ASP   A HB3  1 
ATOM   2290 H  HB3  B ASP   A 1 105 ? 26.117 -9.176  -13.081 0.70 24.76 ?  105  ASP   A HB3  1 
ATOM   2291 N  N    A ILE   A 1 106 ? 22.139 -8.538  -12.423 0.30 22.53 ?  106  ILE   A N    1 
ATOM   2292 N  N    B ILE   A 1 106 ? 22.299 -8.985  -12.385 0.70 16.36 ?  106  ILE   A N    1 
ATOM   2293 C  CA   A ILE   A 1 106 ? 21.388 -8.948  -11.243 0.30 22.13 ?  106  ILE   A CA   1 
ATOM   2294 C  CA   B ILE   A 1 106 ? 21.526 -9.361  -11.205 0.70 16.63 ?  106  ILE   A CA   1 
ATOM   2295 C  C    A ILE   A 1 106 ? 21.928 -10.242 -10.649 0.30 21.67 ?  106  ILE   A C    1 
ATOM   2296 C  C    B ILE   A 1 106 ? 22.070 -10.619 -10.549 0.70 15.71 ?  106  ILE   A C    1 
ATOM   2297 O  O    A ILE   A 1 106 ? 21.690 -10.520 -9.468  0.30 21.19 ?  106  ILE   A O    1 
ATOM   2298 O  O    B ILE   A 1 106 ? 21.843 -10.830 -9.354  0.70 15.68 ?  106  ILE   A O    1 
ATOM   2299 C  CB   A ILE   A 1 106 ? 19.881 -9.047  -11.558 0.30 22.36 ?  106  ILE   A CB   1 
ATOM   2300 C  CB   B ILE   A 1 106 ? 20.026 -9.496  -11.554 0.70 19.21 ?  106  ILE   A CB   1 
ATOM   2301 C  CG1  A ILE   A 1 106 ? 19.058 -9.097  -10.268 0.30 22.37 ?  106  ILE   A CG1  1 
ATOM   2302 C  CG1  B ILE   A 1 106 ? 19.167 -9.558  -10.288 0.70 20.24 ?  106  ILE   A CG1  1 
ATOM   2303 C  CG2  A ILE   A 1 106 ? 19.589 -10.273 -12.410 0.30 22.41 ?  106  ILE   A CG2  1 
ATOM   2304 C  CG2  B ILE   A 1 106 ? 19.777 -10.740 -12.384 0.70 19.92 ?  106  ILE   A CG2  1 
ATOM   2305 C  CD1  A ILE   A 1 106 ? 19.264 -7.899  -9.364  0.30 22.41 ?  106  ILE   A CD1  1 
ATOM   2306 C  CD1  B ILE   A 1 106 ? 19.210 -8.298  -9.449  0.70 20.86 ?  106  ILE   A CD1  1 
ATOM   2307 H  H    A ILE   A 1 106 ? 21.693 -8.567  -13.155 0.30 27.06 ?  106  ILE   A H    1 
ATOM   2308 H  H    B ILE   A 1 106 ? 21.851 -8.970  -13.113 0.70 19.66 ?  106  ILE   A H    1 
ATOM   2309 H  HA   A ILE   A 1 106 ? 21.504 -8.266  -10.572 0.30 26.58 ?  106  ILE   A HA   1 
ATOM   2310 H  HA   B ILE   A 1 106 ? 21.610 -8.655  -10.552 0.70 19.98 ?  106  ILE   A HA   1 
ATOM   2311 H  HB   A ILE   A 1 106 ? 19.620 -8.260  -12.058 0.30 26.86 ?  106  ILE   A HB   1 
ATOM   2312 H  HB   B ILE   A 1 106 ? 19.759 -8.720  -12.070 0.70 23.07 ?  106  ILE   A HB   1 
ATOM   2313 H  HG12 A ILE   A 1 106 ? 18.115 -9.133  -10.500 0.30 26.86 ?  106  ILE   A HG12 1 
ATOM   2314 H  HG12 B ILE   A 1 106 ? 18.244 -9.705  -10.545 0.70 24.31 ?  106  ILE   A HG12 1 
ATOM   2315 H  HG13 A ILE   A 1 106 ? 19.301 -9.893  -9.769  0.30 26.86 ?  106  ILE   A HG13 1 
ATOM   2316 H  HG13 B ILE   A 1 106 ? 19.473 -10.292 -9.734  0.70 24.31 ?  106  ILE   A HG13 1 
ATOM   2317 H  HG21 A ILE   A 1 106 ? 18.697 -10.193 -12.782 0.30 26.91 ?  106  ILE   A HG21 1 
ATOM   2318 H  HG21 B ILE   A 1 106 ? 18.893 -10.682 -12.776 0.70 23.92 ?  106  ILE   A HG21 1 
ATOM   2319 H  HG22 A ILE   A 1 106 ? 20.243 -10.322 -13.124 0.30 26.91 ?  106  ILE   A HG22 1 
ATOM   2320 H  HG22 B ILE   A 1 106 ? 20.448 -10.789 -13.079 0.70 23.92 ?  106  ILE   A HG22 1 
ATOM   2321 H  HG23 A ILE   A 1 106 ? 19.646 -11.067 -11.855 0.30 26.91 ?  106  ILE   A HG23 1 
ATOM   2322 H  HG23 B ILE   A 1 106 ? 19.835 -11.519 -11.809 0.70 23.92 ?  106  ILE   A HG23 1 
ATOM   2323 H  HD11 A ILE   A 1 106 ? 18.518 -7.837  -8.750  0.30 26.91 ?  106  ILE   A HD11 1 
ATOM   2324 H  HD11 B ILE   A 1 106 ? 18.490 -8.326  -8.801  0.70 25.06 ?  106  ILE   A HD11 1 
ATOM   2325 H  HD12 A ILE   A 1 106 ? 20.091 -8.015  -8.870  0.30 26.91 ?  106  ILE   A HD12 1 
ATOM   2326 H  HD12 B ILE   A 1 106 ? 20.065 -8.252  -8.990  0.70 25.06 ?  106  ILE   A HD12 1 
ATOM   2327 H  HD13 A ILE   A 1 106 ? 19.311 -7.099  -9.909  0.30 26.91 ?  106  ILE   A HD13 1 
ATOM   2328 H  HD13 B ILE   A 1 106 ? 19.104 -7.529  -10.030 0.70 25.06 ?  106  ILE   A HD13 1 
ATOM   2329 N  N    A GLN   A 1 107 ? 22.659 -11.040 -11.434 0.30 22.06 ?  107  GLN   A N    1 
ATOM   2330 N  N    B GLN   A 1 107 ? 22.797 -11.460 -11.300 0.70 15.97 ?  107  GLN   A N    1 
ATOM   2331 C  CA   A GLN   A 1 107 ? 23.240 -12.277 -10.922 0.30 22.67 ?  107  GLN   A CA   1 
ATOM   2332 C  CA   B GLN   A 1 107 ? 23.434 -12.629 -10.700 0.70 18.45 ?  107  GLN   A CA   1 
ATOM   2333 C  C    A GLN   A 1 107 ? 24.230 -12.024 -9.793  0.30 20.50 ?  107  GLN   A C    1 
ATOM   2334 C  C    B GLN   A 1 107 ? 24.385 -12.233 -9.579  0.70 15.98 ?  107  GLN   A C    1 
ATOM   2335 O  O    A GLN   A 1 107 ? 24.463 -12.921 -8.977  0.30 21.20 ?  107  GLN   A O    1 
ATOM   2336 O  O    B GLN   A 1 107 ? 24.616 -13.014 -8.647  0.70 17.10 ?  107  GLN   A O    1 
ATOM   2337 C  CB   A GLN   A 1 107 ? 23.935 -13.042 -12.054 0.30 25.62 ?  107  GLN   A CB   1 
ATOM   2338 C  CB   B GLN   A 1 107 ? 24.178 -13.433 -11.772 0.70 24.01 ?  107  GLN   A CB   1 
ATOM   2339 C  CG   A GLN   A 1 107 ? 23.057 -13.289 -13.271 0.30 28.41 ?  107  GLN   A CG   1 
ATOM   2340 C  CG   B GLN   A 1 107 ? 23.267 -14.023 -12.835 0.70 29.44 ?  107  GLN   A CG   1 
ATOM   2341 C  CD   A GLN   A 1 107 ? 21.804 -14.073 -12.938 0.30 30.71 ?  107  GLN   A CD   1 
ATOM   2342 C  CD   B GLN   A 1 107 ? 22.269 -15.008 -12.255 0.70 34.29 ?  107  GLN   A CD   1 
ATOM   2343 O  OE1  A GLN   A 1 107 ? 21.864 -15.120 -12.293 0.30 31.62 ?  107  GLN   A OE1  1 
ATOM   2344 O  OE1  B GLN   A 1 107 ? 22.617 -15.842 -11.418 0.70 35.90 ?  107  GLN   A OE1  1 
ATOM   2345 N  NE2  A GLN   A 1 107 ? 20.657 -13.565 -13.372 0.30 31.44 ?  107  GLN   A NE2  1 
ATOM   2346 N  NE2  B GLN   A 1 107 ? 21.018 -14.909 -12.688 0.70 35.70 ?  107  GLN   A NE2  1 
ATOM   2347 H  H    A GLN   A 1 107 ? 22.833 -10.886 -12.258 0.30 26.49 ?  107  GLN   A H    1 
ATOM   2348 H  H    B GLN   A 1 107 ? 22.939 -11.373 -12.147 0.70 19.19 ?  107  GLN   A H    1 
ATOM   2349 H  HA   A GLN   A 1 107 ? 22.536 -12.843 -10.573 0.30 27.23 ?  107  GLN   A HA   1 
ATOM   2350 H  HA   B GLN   A 1 107 ? 22.755 -13.202 -10.327 0.70 22.17 ?  107  GLN   A HA   1 
ATOM   2351 H  HB2  A GLN   A 1 107 ? 24.709 -12.536 -12.348 0.30 30.76 ?  107  GLN   A HB2  1 
ATOM   2352 H  HB2  B GLN   A 1 107 ? 24.818 -12.858 -12.221 0.70 28.84 ?  107  GLN   A HB2  1 
ATOM   2353 H  HB3  A GLN   A 1 107 ? 24.221 -13.909 -11.720 0.30 30.76 ?  107  GLN   A HB3  1 
ATOM   2354 H  HB3  B GLN   A 1 107 ? 24.646 -14.173 -11.348 0.70 28.84 ?  107  GLN   A HB3  1 
ATOM   2355 H  HG2  A GLN   A 1 107 ? 22.785 -12.438 -13.647 0.30 34.12 ?  107  GLN   A HG2  1 
ATOM   2356 H  HG2  B GLN   A 1 107 ? 22.773 -13.304 -13.260 0.70 35.36 ?  107  GLN   A HG2  1 
ATOM   2357 H  HG3  A GLN   A 1 107 ? 23.562 -13.794 -13.929 0.30 34.12 ?  107  GLN   A HG3  1 
ATOM   2358 H  HG3  B GLN   A 1 107 ? 23.806 -14.491 -13.494 0.70 35.36 ?  107  GLN   A HG3  1 
ATOM   2359 H  HE21 A GLN   A 1 107 ? 20.654 -12.830 -13.818 0.30 37.75 ?  107  GLN   A HE21 1 
ATOM   2360 H  HE21 B GLN   A 1 107 ? 20.811 -14.312 -13.270 0.70 42.86 ?  107  GLN   A HE21 1 
ATOM   2361 H  HE22 A GLN   A 1 107 ? 19.919 -13.973 -13.208 0.30 37.75 ?  107  GLN   A HE22 1 
ATOM   2362 H  HE22 B GLN   A 1 107 ? 20.417 -15.445 -12.386 0.70 42.86 ?  107  GLN   A HE22 1 
ATOM   2363 N  N    A LEU   A 1 108 ? 24.813 -10.824 -9.725  0.30 17.77 ?  108  LEU   A N    1 
ATOM   2364 N  N    B LEU   A 1 108 ? 24.930 -11.016 -9.641  0.70 14.08 ?  108  LEU   A N    1 
ATOM   2365 C  CA   A LEU   A 1 108 ? 25.761 -10.492 -8.667  0.30 15.77 ?  108  LEU   A CA   1 
ATOM   2366 C  CA   B LEU   A 1 108 ? 25.818 -10.525 -8.598  0.70 13.58 ?  108  LEU   A CA   1 
ATOM   2367 C  C    A LEU   A 1 108 ? 25.093 -10.321 -7.309  0.30 13.79 ?  108  LEU   A C    1 
ATOM   2368 C  C    B LEU   A 1 108 ? 25.096 -10.304 -7.275  0.70 12.35 ?  108  LEU   A C    1 
ATOM   2369 O  O    A LEU   A 1 108 ? 25.798 -10.183 -6.304  0.30 14.00 ?  108  LEU   A O    1 
ATOM   2370 O  O    B LEU   A 1 108 ? 25.767 -10.123 -6.253  0.70 13.13 ?  108  LEU   A O    1 
ATOM   2371 C  CB   A LEU   A 1 108 ? 26.532 -9.223  -9.042  0.30 15.63 ?  108  LEU   A CB   1 
ATOM   2372 C  CB   B LEU   A 1 108 ? 26.524 -9.246  -9.058  0.70 13.82 ?  108  LEU   A CB   1 
ATOM   2373 C  CG   A LEU   A 1 108 ? 27.498 -9.380  -10.218 0.30 16.16 ?  108  LEU   A CG   1 
ATOM   2374 C  CG   B LEU   A 1 108 ? 27.538 -9.458  -10.184 0.70 15.51 ?  108  LEU   A CG   1 
ATOM   2375 C  CD1  A LEU   A 1 108 ? 27.927 -8.028  -10.762 0.30 16.52 ?  108  LEU   A CD1  1 
ATOM   2376 C  CD1  B LEU   A 1 108 ? 28.038 -8.139  -10.736 0.70 16.32 ?  108  LEU   A CD1  1 
ATOM   2377 C  CD2  A LEU   A 1 108 ? 28.714 -10.190 -9.796  0.30 16.82 ?  108  LEU   A CD2  1 
ATOM   2378 C  CD2  B LEU   A 1 108 ? 28.711 -10.296 -9.695  0.70 17.25 ?  108  LEU   A CD2  1 
ATOM   2379 H  H    A LEU   A 1 108 ? 24.672 -10.190 -10.281 0.30 21.35 ?  108  LEU   A H    1 
ATOM   2380 H  H    B LEU   A 1 108 ? 24.805 -10.464 -10.285 0.70 16.92 ?  108  LEU   A H    1 
ATOM   2381 H  HA   A LEU   A 1 108 ? 26.403 -11.213 -8.585  0.30 18.94 ?  108  LEU   A HA   1 
ATOM   2382 H  HA   B LEU   A 1 108 ? 26.500 -11.196 -8.440  0.70 16.32 ?  108  LEU   A HA   1 
ATOM   2383 H  HB2  A LEU   A 1 108 ? 25.893 -8.533  -9.280  0.30 18.77 ?  108  LEU   A HB2  1 
ATOM   2384 H  HB2  B LEU   A 1 108 ? 25.856 -8.621  -9.377  0.70 16.60 ?  108  LEU   A HB2  1 
ATOM   2385 H  HB3  A LEU   A 1 108 ? 27.050 -8.937  -8.274  0.30 18.77 ?  108  LEU   A HB3  1 
ATOM   2386 H  HB3  B LEU   A 1 108 ? 26.998 -8.867  -8.305  0.70 16.60 ?  108  LEU   A HB3  1 
ATOM   2387 H  HG   A LEU   A 1 108 ? 27.052 -9.861  -10.933 0.30 19.41 ?  108  LEU   A HG   1 
ATOM   2388 H  HG   B LEU   A 1 108 ? 27.109 -9.941  -10.910 0.70 18.64 ?  108  LEU   A HG   1 
ATOM   2389 H  HD11 A LEU   A 1 108 ? 28.502 -8.166  -11.533 0.30 19.85 ?  108  LEU   A HD11 1 
ATOM   2390 H  HD11 B LEU   A 1 108 ? 28.663 -8.314  -11.459 0.70 19.61 ?  108  LEU   A HD11 1 
ATOM   2391 H  HD12 A LEU   A 1 108 ? 27.139 -7.528  -11.023 0.30 19.85 ?  108  LEU   A HD12 1 
ATOM   2392 H  HD12 B LEU   A 1 108 ? 27.284 -7.629  -11.071 0.70 19.61 ?  108  LEU   A HD12 1 
ATOM   2393 H  HD13 A LEU   A 1 108 ? 28.411 -7.549  -10.072 0.30 19.85 ?  108  LEU   A HD13 1 
ATOM   2394 H  HD13 B LEU   A 1 108 ? 28.482 -7.647  -10.028 0.70 19.61 ?  108  LEU   A HD13 1 
ATOM   2395 H  HD21 A LEU   A 1 108 ? 29.350 -10.208 -10.527 0.30 20.21 ?  108  LEU   A HD21 1 
ATOM   2396 H  HD21 B LEU   A 1 108 ? 29.424 -10.251 -10.349 0.70 20.72 ?  108  LEU   A HD21 1 
ATOM   2397 H  HD22 A LEU   A 1 108 ? 29.115 -9.773  -9.018  0.30 20.21 ?  108  LEU   A HD22 1 
ATOM   2398 H  HD22 B LEU   A 1 108 ? 29.016 -9.940  -8.846  0.70 20.72 ?  108  LEU   A HD22 1 
ATOM   2399 H  HD23 A LEU   A 1 108 ? 28.432 -11.093 -9.580  0.30 20.21 ?  108  LEU   A HD23 1 
ATOM   2400 H  HD23 B LEU   A 1 108 ? 28.418 -11.213 -9.584  0.70 20.72 ?  108  LEU   A HD23 1 
ATOM   2401 N  N    . LEU   A 1 109 ? 23.759 -10.343 -7.257  1.00 12.46 ?  109  LEU   A N    1 
ATOM   2402 C  CA   . LEU   A 1 109 ? 23.052 -10.215 -5.989  1.00 11.64 ?  109  LEU   A CA   1 
ATOM   2403 C  C    . LEU   A 1 109 ? 23.386 -11.372 -5.053  1.00 10.77 ?  109  LEU   A C    1 
ATOM   2404 O  O    . LEU   A 1 109 ? 23.518 -11.184 -3.839  1.00 11.21 ?  109  LEU   A O    1 
ATOM   2405 C  CB   . LEU   A 1 109 ? 21.547 -10.125 -6.246  1.00 12.43 ?  109  LEU   A CB   1 
ATOM   2406 C  CG   . LEU   A 1 109 ? 20.662 -9.848  -5.033  1.00 12.65 ?  109  LEU   A CG   1 
ATOM   2407 C  CD1  . LEU   A 1 109 ? 21.138 -8.612  -4.301  1.00 13.06 ?  109  LEU   A CD1  1 
ATOM   2408 C  CD2  . LEU   A 1 109 ? 19.206 -9.682  -5.453  1.00 13.50 ?  109  LEU   A CD2  1 
ATOM   2409 H  H    A LEU   A 1 109 ? 23.246 -10.434 -7.939  0.30 14.98 ?  109  LEU   A H    1 
ATOM   2410 H  H    B LEU   A 1 109 ? 23.256 -10.440 -7.946  0.70 14.98 ?  109  LEU   A H    1 
ATOM   2411 H  HA   . LEU   A 1 109 ? 23.337 -9.395  -5.560  1.00 13.99 ?  109  LEU   A HA   1 
ATOM   2412 H  HB2  . LEU   A 1 109 ? 21.392 -9.408  -6.880  1.00 14.94 ?  109  LEU   A HB2  1 
ATOM   2413 H  HB3  . LEU   A 1 109 ? 21.252 -10.963 -6.627  1.00 14.94 ?  109  LEU   A HB3  1 
ATOM   2414 H  HG   . LEU   A 1 109 ? 20.711 -10.595 -4.420  1.00 15.20 ?  109  LEU   A HG   1 
ATOM   2415 H  HD11 . LEU   A 1 109 ? 20.459 -8.322  -3.678  1.00 15.69 ?  109  LEU   A HD11 1 
ATOM   2416 H  HD12 . LEU   A 1 109 ? 21.960 -8.820  -3.826  1.00 15.69 ?  109  LEU   A HD12 1 
ATOM   2417 H  HD13 . LEU   A 1 109 ? 21.310 -7.906  -4.952  1.00 15.69 ?  109  LEU   A HD13 1 
ATOM   2418 H  HD21 . LEU   A 1 109 ? 18.680 -9.423  -4.676  1.00 16.23 ?  109  LEU   A HD21 1 
ATOM   2419 H  HD22 . LEU   A 1 109 ? 19.149 -8.989  -6.130  1.00 16.23 ?  109  LEU   A HD22 1 
ATOM   2420 H  HD23 . LEU   A 1 109 ? 18.880 -10.521 -5.808  1.00 16.23 ?  109  LEU   A HD23 1 
ATOM   2421 N  N    . LYS   A 1 110 ? 23.535 -12.583 -5.594  1.00 10.91 ?  110  LYS   A N    1 
ATOM   2422 C  CA   . LYS   A 1 110 ? 23.915 -13.708 -4.743  1.00 11.20 ?  110  LYS   A CA   1 
ATOM   2423 C  C    . LYS   A 1 110 ? 25.296 -13.484 -4.134  1.00 10.36 ?  110  LYS   A C    1 
ATOM   2424 O  O    . LYS   A 1 110 ? 25.487 -13.679 -2.931  1.00 10.55 ?  110  LYS   A O    1 
ATOM   2425 C  CB   . LYS   A 1 110 ? 23.853 -15.025 -5.517  1.00 11.96 ?  110  LYS   A CB   1 
ATOM   2426 C  CG   . LYS   A 1 110 ? 24.038 -16.233 -4.611  1.00 11.92 ?  110  LYS   A CG   1 
ATOM   2427 C  CD   . LYS   A 1 110 ? 23.795 -17.551 -5.334  1.00 12.50 ?  110  LYS   A CD   1 
ATOM   2428 C  CE   . LYS   A 1 110 ? 23.875 -18.750 -4.395  1.00 13.13 ?  110  LYS   A CE   1 
ATOM   2429 N  NZ   . LYS   A 1 110 ? 22.697 -18.866 -3.497  1.00 13.21 ?  110  LYS   A NZ   1 
ATOM   2430 H  H    . LYS   A 1 110 ? 23.434 -12.774 -6.423  1.00 13.11 ?  110  LYS   A H    1 
ATOM   2431 H  HA   . LYS   A 1 110 ? 23.277 -13.768 -4.012  1.00 13.46 ?  110  LYS   A HA   1 
ATOM   2432 H  HB2  . LYS   A 1 110 ? 22.990 -15.103 -5.949  1.00 14.38 ?  110  LYS   A HB2  1 
ATOM   2433 H  HB3  . LYS   A 1 110 ? 24.562 -15.039 -6.178  1.00 14.38 ?  110  LYS   A HB3  1 
ATOM   2434 H  HG2  . LYS   A 1 110 ? 24.943 -16.240 -4.265  1.00 14.33 ?  110  LYS   A HG2  1 
ATOM   2435 H  HG3  . LYS   A 1 110 ? 23.404 -16.174 -3.874  1.00 14.33 ?  110  LYS   A HG3  1 
ATOM   2436 H  HD2  . LYS   A 1 110 ? 22.911 -17.535 -5.729  1.00 15.03 ?  110  LYS   A HD2  1 
ATOM   2437 H  HD3  . LYS   A 1 110 ? 24.470 -17.658 -6.020  1.00 15.03 ?  110  LYS   A HD3  1 
ATOM   2438 H  HE2  . LYS   A 1 110 ? 23.933 -19.560 -4.923  1.00 15.77 ?  110  LYS   A HE2  1 
ATOM   2439 H  HE3  . LYS   A 1 110 ? 24.666 -18.662 -3.836  1.00 15.77 ?  110  LYS   A HE3  1 
ATOM   2440 H  HZ1  . LYS   A 1 110 ? 22.782 -19.576 -2.970  1.00 15.88 ?  110  LYS   A HZ1  1 
ATOM   2441 H  HZ2  . LYS   A 1 110 ? 22.623 -18.136 -2.994  1.00 15.88 ?  110  LYS   A HZ2  1 
ATOM   2442 H  HZ3  . LYS   A 1 110 ? 21.954 -18.955 -3.984  1.00 15.88 ?  110  LYS   A HZ3  1 
ATOM   2443 N  N    . SER   A 1 111 ? 26.256 -13.030 -4.943  1.00 10.45 ?  111  SER   A N    1 
ATOM   2444 C  CA   . SER   A 1 111 ? 27.584 -12.720 -4.422  1.00 10.78 ?  111  SER   A CA   1 
ATOM   2445 C  C    . SER   A 1 111 ? 27.510 -11.673 -3.312  1.00 10.25 ?  111  SER   A C    1 
ATOM   2446 O  O    . SER   A 1 111 ? 28.213 -11.773 -2.298  1.00 10.97 ?  111  SER   A O    1 
ATOM   2447 C  CB   . SER   A 1 111 ? 28.482 -12.237 -5.562  1.00 12.35 ?  111  SER   A CB   1 
ATOM   2448 O  OG   . SER   A 1 111 ? 28.543 -13.204 -6.599  1.00 14.14 ?  111  SER   A OG   1 
ATOM   2449 H  H    . SER   A 1 111 ? 26.156 -12.887 -5.785  1.00 12.57 ?  111  SER   A H    1 
ATOM   2450 H  HA   . SER   A 1 111 ? 27.972 -13.530 -4.053  1.00 12.96 ?  111  SER   A HA   1 
ATOM   2451 H  HB2  . SER   A 1 111 ? 28.116 -11.417 -5.927  1.00 14.84 ?  111  SER   A HB2  1 
ATOM   2452 H  HB3  . SER   A 1 111 ? 29.373 -12.076 -5.214  1.00 14.84 ?  111  SER   A HB3  1 
ATOM   2453 H  HG   . SER   A 1 111 ? 29.059 -12.928 -7.214  1.00 16.99 ?  111  SER   A HG   1 
ATOM   2454 N  N    . ALA   A 1 112 ? 26.666 -10.653 -3.492  1.00 10.15 ?  112  ALA   A N    1 
ATOM   2455 C  CA   . ALA   A 1 112 ? 26.506 -9.620  -2.471  1.00 10.13 ?  112  ALA   A CA   1 
ATOM   2456 C  C    . ALA   A 1 112 ? 26.033 -10.228 -1.152  1.00 9.85  ?  112  ALA   A C    1 
ATOM   2457 O  O    . ALA   A 1 112 ? 26.582 -9.942  -0.082  1.00 10.36 ?  112  ALA   A O    1 
ATOM   2458 C  CB   . ALA   A 1 112 ? 25.531 -8.548  -2.966  1.00 10.85 ?  112  ALA   A CB   1 
ATOM   2459 H  H    . ALA   A 1 112 ? 26.190 -10.529 -4.199  1.00 12.21 ?  112  ALA   A H    1 
ATOM   2460 H  HA   . ALA   A 1 112 ? 27.361 -9.190  -2.314  1.00 12.18 ?  112  ALA   A HA   1 
ATOM   2461 H  HB1  . ALA   A 1 112 ? 25.454 -7.853  -2.287  1.00 13.05 ?  112  ALA   A HB1  1 
ATOM   2462 H  HB2  . ALA   A 1 112 ? 25.869 -8.163  -3.789  1.00 13.05 ?  112  ALA   A HB2  1 
ATOM   2463 H  HB3  . ALA   A 1 112 ? 24.663 -8.952  -3.121  1.00 13.05 ?  112  ALA   A HB3  1 
ATOM   2464 N  N    . TYR   A 1 113 ? 24.991 -11.063 -1.205  1.00 10.05 ?  113  TYR   A N    1 
ATOM   2465 C  CA   . TYR   A 1 113 ? 24.473 -11.672 0.019   1.00 9.94  ?  113  TYR   A CA   1 
ATOM   2466 C  C    . TYR   A 1 113 ? 25.476 -12.628 0.665   1.00 9.44  ?  113  TYR   A C    1 
ATOM   2467 O  O    . TYR   A 1 113 ? 25.439 -12.816 1.884   1.00 10.13 ?  113  TYR   A O    1 
ATOM   2468 C  CB   . TYR   A 1 113 ? 23.150 -12.391 -0.254  1.00 10.22 ?  113  TYR   A CB   1 
ATOM   2469 C  CG   . TYR   A 1 113 ? 21.935 -11.491 -0.201  1.00 10.62 ?  113  TYR   A CG   1 
ATOM   2470 C  CD1  . TYR   A 1 113 ? 21.567 -10.855 0.979   1.00 10.95 ?  113  TYR   A CD1  1 
ATOM   2471 C  CD2  . TYR   A 1 113 ? 21.137 -11.298 -1.324  1.00 10.69 ?  113  TYR   A CD2  1 
ATOM   2472 C  CE1  . TYR   A 1 113 ? 20.442 -10.056 1.039   1.00 11.30 ?  113  TYR   A CE1  1 
ATOM   2473 C  CE2  . TYR   A 1 113 ? 20.001 -10.498 -1.274  1.00 11.32 ?  113  TYR   A CE2  1 
ATOM   2474 C  CZ   . TYR   A 1 113 ? 19.659 -9.881  -0.092  1.00 11.19 ?  113  TYR   A CZ   1 
ATOM   2475 O  OH   . TYR   A 1 113 ? 18.534 -9.088  -0.027  1.00 12.38 ?  113  TYR   A OH   1 
ATOM   2476 H  H    . TYR   A 1 113 ? 24.579 -11.291 -1.924  1.00 12.09 ?  113  TYR   A H    1 
ATOM   2477 H  HA   . TYR   A 1 113 ? 24.298 -10.962 0.658   1.00 11.95 ?  113  TYR   A HA   1 
ATOM   2478 H  HB2  . TYR   A 1 113 ? 23.186 -12.782 -1.141  1.00 12.28 ?  113  TYR   A HB2  1 
ATOM   2479 H  HB3  . TYR   A 1 113 ? 23.033 -13.087 0.409   1.00 12.28 ?  113  TYR   A HB3  1 
ATOM   2480 H  HD1  . TYR   A 1 113 ? 22.090 -10.984 1.744   1.00 13.16 ?  113  TYR   A HD1  1 
ATOM   2481 H  HD2  . TYR   A 1 113 ? 21.358 -11.722 -2.120  1.00 12.85 ?  113  TYR   A HD2  1 
ATOM   2482 H  HE1  . TYR   A 1 113 ? 20.213 -9.645  1.840   1.00 13.58 ?  113  TYR   A HE1  1 
ATOM   2483 H  HE2  . TYR   A 1 113 ? 19.472 -10.379 -2.030  1.00 13.61 ?  113  TYR   A HE2  1 
ATOM   2484 H  HH   . TYR   A 1 113 ? 18.155 -9.073  -0.783  1.00 14.88 ?  113  TYR   A HH   1 
ATOM   2485 N  N    . GLU   A 1 114 ? 26.381 -13.234 -0.116  1.00 9.65  ?  114  GLU   A N    1 
ATOM   2486 C  CA   . GLU   A 1 114 ? 27.374 -14.130 0.475   1.00 10.15 ?  114  GLU   A CA   1 
ATOM   2487 C  C    . GLU   A 1 114 ? 28.225 -13.420 1.525   1.00 10.18 ?  114  GLU   A C    1 
ATOM   2488 O  O    . GLU   A 1 114 ? 28.710 -14.061 2.467   1.00 10.42 ?  114  GLU   A O    1 
ATOM   2489 C  CB   . GLU   A 1 114 ? 28.248 -14.762 -0.617  1.00 10.23 ?  114  GLU   A CB   1 
ATOM   2490 C  CG   . GLU   A 1 114 ? 27.498 -15.825 -1.403  1.00 10.47 ?  114  GLU   A CG   1 
ATOM   2491 C  CD   . GLU   A 1 114 ? 28.210 -16.346 -2.647  1.00 10.81 ?  114  GLU   A CD   1 
ATOM   2492 O  OE1  . GLU   A 1 114 ? 29.167 -15.718 -3.144  1.00 11.39 ?  114  GLU   A OE1  1 
ATOM   2493 O  OE2  . GLU   A 1 114 ? 27.767 -17.405 -3.149  1.00 12.18 -1 114  GLU   A OE2  1 
ATOM   2494 H  H    . GLU   A 1 114 ? 26.433 -13.145 -0.977  1.00 11.61 ?  114  GLU   A H    1 
ATOM   2495 H  HA   . GLU   A 1 114 ? 26.903 -14.852 0.916   1.00 12.21 ?  114  GLU   A HA   1 
ATOM   2496 H  HB2  . GLU   A 1 114 ? 28.534 -14.071 -1.239  1.00 12.30 ?  114  GLU   A HB2  1 
ATOM   2497 H  HB3  . GLU   A 1 114 ? 29.021 -15.178 -0.204  1.00 12.30 ?  114  GLU   A HB3  1 
ATOM   2498 H  HG2  . GLU   A 1 114 ? 27.346 -16.586 -0.823  1.00 12.59 ?  114  GLU   A HG2  1 
ATOM   2499 H  HG3  . GLU   A 1 114 ? 26.649 -15.458 -1.689  1.00 12.59 ?  114  GLU   A HG3  1 
ATOM   2500 N  N    . ASN   A 1 115 ? 28.404 -12.099 1.397   1.00 9.85  ?  115  ASN   A N    1 
ATOM   2501 C  CA   . ASN   A 1 115 ? 29.177 -11.373 2.397   1.00 10.24 ?  115  ASN   A CA   1 
ATOM   2502 C  C    . ASN   A 1 115 ? 28.562 -11.506 3.787   1.00 9.82  ?  115  ASN   A C    1 
ATOM   2503 O  O    . ASN   A 1 115 ? 29.276 -11.425 4.795   1.00 10.35 ?  115  ASN   A O    1 
ATOM   2504 C  CB   . ASN   A 1 115 ? 29.273 -9.898  2.013   1.00 10.58 ?  115  ASN   A CB   1 
ATOM   2505 C  CG   . ASN   A 1 115 ? 30.081 -9.674  0.757   1.00 11.38 ?  115  ASN   A CG   1 
ATOM   2506 O  OD1  . ASN   A 1 115 ? 31.300 -9.758  0.784   1.00 14.48 ?  115  ASN   A OD1  1 
ATOM   2507 N  ND2  . ASN   A 1 115 ? 29.415 -9.381  -0.344  1.00 10.61 ?  115  ASN   A ND2  1 
ATOM   2508 H  H    . ASN   A 1 115 ? 28.082 -11.611 0.763   1.00 11.84 ?  115  ASN   A H    1 
ATOM   2509 H  HA   . ASN   A 1 115 ? 30.073 -11.739 2.429   1.00 12.32 ?  115  ASN   A HA   1 
ATOM   2510 H  HB2  . ASN   A 1 115 ? 28.377 -9.551  1.873   1.00 12.72 ?  115  ASN   A HB2  1 
ATOM   2511 H  HB3  . ASN   A 1 115 ? 29.699 -9.414  2.743   1.00 12.72 ?  115  ASN   A HB3  1 
ATOM   2512 H  HD21 . ASN   A 1 115 ? 29.838 -9.240  -1.080  1.00 12.75 ?  115  ASN   A HD21 1 
ATOM   2513 H  HD22 . ASN   A 1 115 ? 28.554 -9.340  -0.331  1.00 12.75 ?  115  ASN   A HD22 1 
ATOM   2514 N  N    . PHE   A 1 116 ? 27.235 -11.675 3.868   1.00 9.74  ?  116  PHE   A N    1 
ATOM   2515 C  CA   . PHE   A 1 116 ? 26.582 -11.771 5.170   1.00 9.86  ?  116  PHE   A CA   1 
ATOM   2516 C  C    . PHE   A 1 116 ? 27.054 -13.001 5.946   1.00 10.04 ?  116  PHE   A C    1 
ATOM   2517 O  O    . PHE   A 1 116 ? 26.981 -13.016 7.174   1.00 10.79 ?  116  PHE   A O    1 
ATOM   2518 C  CB   . PHE   A 1 116 ? 25.052 -11.898 5.034   1.00 10.17 ?  116  PHE   A CB   1 
ATOM   2519 C  CG   . PHE   A 1 116 ? 24.290 -10.656 4.556   1.00 9.94  ?  116  PHE   A CG   1 
ATOM   2520 C  CD1  . PHE   A 1 116 ? 24.855 -9.641  3.794   1.00 10.27 ?  116  PHE   A CD1  1 
ATOM   2521 C  CD2  . PHE   A 1 116 ? 22.938 -10.552 4.881   1.00 10.77 ?  116  PHE   A CD2  1 
ATOM   2522 C  CE1  . PHE   A 1 116 ? 24.082 -8.566  3.369   1.00 10.41 ?  116  PHE   A CE1  1 
ATOM   2523 C  CE2  . PHE   A 1 116 ? 22.167 -9.483  4.466   1.00 10.82 ?  116  PHE   A CE2  1 
ATOM   2524 C  CZ   . PHE   A 1 116 ? 22.734 -8.491  3.705   1.00 10.70 ?  116  PHE   A CZ   1 
ATOM   2525 H  H    . PHE   A 1 116 ? 26.704 -11.733 3.192   1.00 11.71 ?  116  PHE   A H    1 
ATOM   2526 H  HA   . PHE   A 1 116 ? 26.782 -10.978 5.692   1.00 11.86 ?  116  PHE   A HA   1 
ATOM   2527 H  HB2  . PHE   A 1 116 ? 24.867 -12.613 4.405   1.00 12.22 ?  116  PHE   A HB2  1 
ATOM   2528 H  HB3  . PHE   A 1 116 ? 24.696 -12.142 5.905   1.00 12.22 ?  116  PHE   A HB3  1 
ATOM   2529 H  HD1  . PHE   A 1 116 ? 25.746 -9.696  3.555   1.00 12.35 ?  116  PHE   A HD1  1 
ATOM   2530 H  HD2  . PHE   A 1 116 ? 22.538 -11.231 5.388   1.00 12.95 ?  116  PHE   A HD2  1 
ATOM   2531 H  HE1  . PHE   A 1 116 ? 24.471 -7.896  2.860   1.00 12.52 ?  116  PHE   A HE1  1 
ATOM   2532 H  HE2  . PHE   A 1 116 ? 21.267 -9.442  4.698   1.00 13.00 ?  116  PHE   A HE2  1 
ATOM   2533 H  HZ   . PHE   A 1 116 ? 22.220 -7.766  3.432   1.00 12.86 ?  116  PHE   A HZ   1 
ATOM   2534 N  N    . ASN   A 1 117 ? 27.501 -14.050 5.247   1.00 10.21 ?  117  ASN   A N    1 
ATOM   2535 C  CA   . ASN   A 1 117 ? 27.879 -15.293 5.910   1.00 10.39 ?  117  ASN   A CA   1 
ATOM   2536 C  C    . ASN   A 1 117 ? 29.149 -15.172 6.735   1.00 10.99 ?  117  ASN   A C    1 
ATOM   2537 O  O    . ASN   A 1 117 ? 29.448 -16.093 7.504   1.00 11.82 ?  117  ASN   A O    1 
ATOM   2538 C  CB   . ASN   A 1 117 ? 27.993 -16.414 4.885   1.00 10.55 ?  117  ASN   A CB   1 
ATOM   2539 C  CG   . ASN   A 1 117 ? 26.640 -16.804 4.346   1.00 10.59 ?  117  ASN   A CG   1 
ATOM   2540 O  OD1  . ASN   A 1 117 ? 25.662 -16.831 5.098   1.00 11.40 ?  117  ASN   A OD1  1 
ATOM   2541 N  ND2  . ASN   A 1 117 ? 26.555 -17.064 3.054   1.00 10.74 ?  117  ASN   A ND2  1 
ATOM   2542 H  H    . ASN   A 1 117 ? 27.588 -14.061 4.388   1.00 12.27 ?  117  ASN   A H    1 
ATOM   2543 H  HA   . ASN   A 1 117 ? 27.161 -15.527 6.517   1.00 12.50 ?  117  ASN   A HA   1 
ATOM   2544 H  HB2  . ASN   A 1 117 ? 28.545 -16.120 4.143   1.00 12.69 ?  117  ASN   A HB2  1 
ATOM   2545 H  HB3  . ASN   A 1 117 ? 28.386 -17.193 5.309   1.00 12.69 ?  117  ASN   A HB3  1 
ATOM   2546 H  HD21 . ASN   A 1 117 ? 25.800 -17.283 2.710   1.00 12.91 ?  117  ASN   A HD21 1 
ATOM   2547 H  HD22 . ASN   A 1 117 ? 27.258 -17.017 2.560   1.00 12.91 ?  117  ASN   A HD22 1 
ATOM   2548 N  N    . GLN   A 1 118 ? 29.874 -14.060 6.621   1.00 10.85 ?  118  GLN   A N    1 
ATOM   2549 C  CA   . GLN   A 1 118 ? 31.047 -13.825 7.449   1.00 11.45 ?  118  GLN   A CA   1 
ATOM   2550 C  C    . GLN   A 1 118 ? 30.701 -13.246 8.817   1.00 11.40 ?  118  GLN   A C    1 
ATOM   2551 O  O    . GLN   A 1 118 ? 31.615 -12.951 9.596   1.00 12.88 ?  118  GLN   A O    1 
ATOM   2552 C  CB   . GLN   A 1 118 ? 32.041 -12.925 6.710   1.00 12.01 ?  118  GLN   A CB   1 
ATOM   2553 C  CG   . GLN   A 1 118 ? 32.496 -13.512 5.385   1.00 11.72 ?  118  GLN   A CG   1 
ATOM   2554 C  CD   . GLN   A 1 118 ? 33.337 -14.763 5.556   1.00 11.86 ?  118  GLN   A CD   1 
ATOM   2555 O  OE1  . GLN   A 1 118 ? 34.196 -14.830 6.441   1.00 12.79 ?  118  GLN   A OE1  1 
ATOM   2556 N  NE2  . GLN   A 1 118 ? 33.097 -15.764 4.708   1.00 12.09 ?  118  GLN   A NE2  1 
ATOM   2557 H  H    . GLN   A 1 118 ? 29.691 -13.410 6.077   1.00 13.05 ?  118  GLN   A H    1 
ATOM   2558 H  HA   . GLN   A 1 118 ? 31.473 -14.681 7.599   1.00 13.76 ?  118  GLN   A HA   1 
ATOM   2559 H  HB2  . GLN   A 1 118 ? 31.625 -12.071 6.538   1.00 14.44 ?  118  GLN   A HB2  1 
ATOM   2560 H  HB3  . GLN   A 1 118 ? 32.825 -12.810 7.272   1.00 14.44 ?  118  GLN   A HB3  1 
ATOM   2561 H  HG2  . GLN   A 1 118 ? 31.718 -13.740 4.850   1.00 14.09 ?  118  GLN   A HG2  1 
ATOM   2562 H  HG3  . GLN   A 1 118 ? 33.035 -12.853 4.917   1.00 14.09 ?  118  GLN   A HG3  1 
ATOM   2563 H  HE21 . GLN   A 1 118 ? 32.484 -15.682 4.103   1.00 14.53 ?  118  GLN   A HE21 1 
ATOM   2564 H  HE22 . GLN   A 1 118 ? 33.544 -16.495 4.762   1.00 14.53 ?  118  GLN   A HE22 1 
ATOM   2565 N  N    . HIS   A 1 119 ? 29.411 -13.099 9.130   1.00 11.10 ?  119  HIS   A N    1 
ATOM   2566 C  CA   . HIS   A 1 119 ? 28.956 -12.490 10.375  1.00 11.77 ?  119  HIS   A CA   1 
ATOM   2567 C  C    . HIS   A 1 119 ? 27.821 -13.321 10.945  1.00 12.06 ?  119  HIS   A C    1 
ATOM   2568 O  O    . HIS   A 1 119 ? 26.878 -13.663 10.226  1.00 12.41 ?  119  HIS   A O    1 
ATOM   2569 C  CB   . HIS   A 1 119 ? 28.492 -11.058 10.113  1.00 12.02 ?  119  HIS   A CB   1 
ATOM   2570 C  CG   . HIS   A 1 119 ? 29.570 -10.238 9.508   1.00 13.40 ?  119  HIS   A CG   1 
ATOM   2571 N  ND1  . HIS   A 1 119 ? 30.540 -9.631  10.270  1.00 15.69 ?  119  HIS   A ND1  1 
ATOM   2572 C  CD2  . HIS   A 1 119 ? 29.912 -10.033 8.217   1.00 14.77 ?  119  HIS   A CD2  1 
ATOM   2573 C  CE1  . HIS   A 1 119 ? 31.411 -9.042  9.471   1.00 16.36 ?  119  HIS   A CE1  1 
ATOM   2574 N  NE2  . HIS   A 1 119 ? 31.060 -9.280  8.220   1.00 16.21 ?  119  HIS   A NE2  1 
ATOM   2575 H  H    . HIS   A 1 119 ? 28.759 -13.359 8.625   1.00 13.34 ?  119  HIS   A H    1 
ATOM   2576 H  HA   . HIS   A 1 119 ? 29.683 -12.476 11.018  1.00 14.14 ?  119  HIS   A HA   1 
ATOM   2577 H  HB2  . HIS   A 1 119 ? 27.739 -11.079 9.504   1.00 14.45 ?  119  HIS   A HB2  1 
ATOM   2578 H  HB3  . HIS   A 1 119 ? 28.233 -10.655 10.956  1.00 14.45 ?  119  HIS   A HB3  1 
ATOM   2579 H  HD1  . HIS   A 1 119 ? 30.570 -9.628  11.128  1.00 18.85 ?  119  HIS   A HD1  1 
ATOM   2580 H  HD2  . HIS   A 1 119 ? 29.452 -10.340 7.467   1.00 17.75 ?  119  HIS   A HD2  1 
ATOM   2581 H  HE1  . HIS   A 1 119 ? 32.144 -8.539  9.740   1.00 19.66 ?  119  HIS   A HE1  1 
ATOM   2582 N  N    A GLU   A 1 120 ? 27.905 -13.635 12.239  0.30 13.61 ?  120  GLU   A N    1 
ATOM   2583 N  N    B GLU   A 1 120 ? 27.912 -13.626 12.240  0.70 12.04 ?  120  GLU   A N    1 
ATOM   2584 C  CA   A GLU   A 1 120 ? 26.953 -14.577 12.828  0.30 15.70 ?  120  GLU   A CA   1 
ATOM   2585 C  CA   B GLU   A 1 120 ? 26.971 -14.564 12.849  0.70 13.76 ?  120  GLU   A CA   1 
ATOM   2586 C  C    A GLU   A 1 120 ? 25.538 -14.006 12.882  0.30 14.17 ?  120  GLU   A C    1 
ATOM   2587 C  C    B GLU   A 1 120 ? 25.551 -14.013 12.915  0.70 12.80 ?  120  GLU   A C    1 
ATOM   2588 O  O    A GLU   A 1 120 ? 24.561 -14.747 12.717  0.30 14.32 ?  120  GLU   A O    1 
ATOM   2589 O  O    B GLU   A 1 120 ? 24.586 -14.786 12.818  0.70 12.85 ?  120  GLU   A O    1 
ATOM   2590 C  CB   A GLU   A 1 120 ? 27.421 -15.011 14.218  0.30 19.47 ?  120  GLU   A CB   1 
ATOM   2591 C  CB   B GLU   A 1 120 ? 27.443 -14.945 14.252  0.70 17.38 ?  120  GLU   A CB   1 
ATOM   2592 C  CG   A GLU   A 1 120 ? 28.579 -15.995 14.197  0.30 23.62 ?  120  GLU   A CG   1 
ATOM   2593 C  CG   B GLU   A 1 120 ? 28.649 -15.864 14.266  0.70 23.50 ?  120  GLU   A CG   1 
ATOM   2594 C  CD   A GLU   A 1 120 ? 28.751 -16.720 15.517  0.30 27.67 ?  120  GLU   A CD   1 
ATOM   2595 C  CD   B GLU   A 1 120 ? 28.818 -16.577 15.587  0.70 29.98 ?  120  GLU   A CD   1 
ATOM   2596 O  OE1  A GLU   A 1 120 ? 28.441 -16.125 16.571  0.30 28.60 ?  120  GLU   A OE1  1 
ATOM   2597 O  OE1  B GLU   A 1 120 ? 28.269 -16.093 16.600  0.70 31.53 ?  120  GLU   A OE1  1 
ATOM   2598 O  OE2  A GLU   A 1 120 ? 29.188 -17.890 15.498  0.30 29.14 -1 120  GLU   A OE2  1 
ATOM   2599 O  OE2  B GLU   A 1 120 ? 29.495 -17.627 15.608  0.70 33.09 -1 120  GLU   A OE2  1 
ATOM   2600 H  H    A GLU   A 1 120 ? 28.495 -13.327 12.786  0.30 16.35 ?  120  GLU   A H    1 
ATOM   2601 H  H    B GLU   A 1 120 ? 28.505 -13.317 12.782  0.70 14.47 ?  120  GLU   A H    1 
ATOM   2602 H  HA   A GLU   A 1 120 ? 26.928 -15.370 12.274  0.30 18.86 ?  120  GLU   A HA   1 
ATOM   2603 H  HA   B GLU   A 1 120 ? 26.949 -15.376 12.322  0.70 16.54 ?  120  GLU   A HA   1 
ATOM   2604 H  HB2  A GLU   A 1 120 ? 27.709 -14.229 14.714  0.30 23.39 ?  120  GLU   A HB2  1 
ATOM   2605 H  HB2  B GLU   A 1 120 ? 27.684 -14.141 14.740  0.70 20.88 ?  120  GLU   A HB2  1 
ATOM   2606 H  HB3  A GLU   A 1 120 ? 26.682 -15.438 14.679  0.30 23.39 ?  120  GLU   A HB3  1 
ATOM   2607 H  HB3  B GLU   A 1 120 ? 26.722 -15.403 14.719  0.70 20.88 ?  120  GLU   A HB3  1 
ATOM   2608 H  HG2  A GLU   A 1 120 ? 28.420 -16.660 13.510  0.30 28.36 ?  120  GLU   A HG2  1 
ATOM   2609 H  HG2  B GLU   A 1 120 ? 28.550 -16.534 13.573  0.70 28.23 ?  120  GLU   A HG2  1 
ATOM   2610 H  HG3  A GLU   A 1 120 ? 29.401 -15.515 14.012  0.30 28.36 ?  120  GLU   A HG3  1 
ATOM   2611 H  HG3  B GLU   A 1 120 ? 29.452 -15.343 14.117  0.70 28.23 ?  120  GLU   A HG3  1 
ATOM   2612 N  N    . VAL   A 1 121 ? 25.404 -12.703 13.120  1.00 12.88 ?  121  VAL   A N    1 
ATOM   2613 C  CA   . VAL   A 1 121 ? 24.104 -12.049 13.244  1.00 12.75 ?  121  VAL   A CA   1 
ATOM   2614 C  C    . VAL   A 1 121 ? 24.208 -10.662 12.615  1.00 11.79 ?  121  VAL   A C    1 
ATOM   2615 O  O    . VAL   A 1 121 ? 25.175 -9.929  12.860  1.00 12.48 ?  121  VAL   A O    1 
ATOM   2616 C  CB   . VAL   A 1 121 ? 23.667 -11.910 14.723  1.00 16.21 ?  121  VAL   A CB   1 
ATOM   2617 C  CG1  . VAL   A 1 121 ? 22.282 -11.284 14.811  1.00 16.72 ?  121  VAL   A CG1  1 
ATOM   2618 C  CG2  . VAL   A 1 121 ? 23.679 -13.237 15.465  1.00 19.06 ?  121  VAL   A CG2  1 
ATOM   2619 H  H    A VAL   A 1 121 ? 26.069 -12.164 13.211  0.30 15.48 ?  121  VAL   A H    1 
ATOM   2620 H  H    B VAL   A 1 121 ? 26.067 -12.158 13.191  0.70 15.48 ?  121  VAL   A H    1 
ATOM   2621 H  HA   . VAL   A 1 121 ? 23.435 -12.567 12.770  1.00 15.33 ?  121  VAL   A HA   1 
ATOM   2622 H  HB   . VAL   A 1 121 ? 24.283 -11.317 15.175  1.00 19.48 ?  121  VAL   A HB   1 
ATOM   2623 H  HG11 . VAL   A 1 121 ? 21.962 -11.348 15.726  1.00 20.09 ?  121  VAL   A HG11 1 
ATOM   2624 H  HG12 . VAL   A 1 121 ? 22.335 -10.351 14.548  1.00 20.09 ?  121  VAL   A HG12 1 
ATOM   2625 H  HG13 . VAL   A 1 121 ? 21.678 -11.761 14.219  1.00 20.09 ?  121  VAL   A HG13 1 
ATOM   2626 H  HG21 . VAL   A 1 121 ? 23.340 -13.095 16.371  1.00 22.90 ?  121  VAL   A HG21 1 
ATOM   2627 H  HG22 . VAL   A 1 121 ? 23.105 -13.868 15.002  1.00 22.90 ?  121  VAL   A HG22 1 
ATOM   2628 H  HG23 . VAL   A 1 121 ? 24.583 -13.573 15.505  1.00 22.90 ?  121  VAL   A HG23 1 
ATOM   2629 N  N    . LEU   A 1 122 ? 23.194 -10.282 11.833  1.00 11.21 ?  122  LEU   A N    1 
ATOM   2630 C  CA   . LEU   A 1 122 ? 23.189 -8.983  11.170  1.00 11.23 ?  122  LEU   A CA   1 
ATOM   2631 C  C    . LEU   A 1 122 ? 21.790 -8.400  11.120  1.00 10.80 ?  122  LEU   A C    1 
ATOM   2632 O  O    . LEU   A 1 122 ? 20.806 -9.128  10.983  1.00 11.90 ?  122  LEU   A O    1 
ATOM   2633 C  CB   . LEU   A 1 122 ? 23.618 -9.062  9.700   1.00 12.71 ?  122  LEU   A CB   1 
ATOM   2634 C  CG   . LEU   A 1 122 ? 24.830 -9.902  9.325   1.00 12.90 ?  122  LEU   A CG   1 
ATOM   2635 C  CD1  . LEU   A 1 122 ? 24.435 -11.352 9.111   1.00 13.41 ?  122  LEU   A CD1  1 
ATOM   2636 C  CD2  . LEU   A 1 122 ? 25.483 -9.335  8.079   1.00 12.35 ?  122  LEU   A CD2  1 
ATOM   2637 H  H    . LEU   A 1 122 ? 22.496 -10.760 11.669  1.00 13.48 ?  122  LEU   A H    1 
ATOM   2638 H  HA   . LEU   A 1 122 ? 23.773 -8.366  11.638  1.00 13.50 ?  122  LEU   A HA   1 
ATOM   2639 H  HB2  . LEU   A 1 122 ? 22.880 -9.418  9.191   1.00 15.27 ?  122  LEU   A HB2  1 
ATOM   2640 H  HB3  . LEU   A 1 122 ? 23.811 -8.163  9.397   1.00 15.27 ?  122  LEU   A HB3  1 
ATOM   2641 H  HG   . LEU   A 1 122 ? 25.491 -9.871  10.039  1.00 15.50 ?  122  LEU   A HG   1 
ATOM   2642 H  HD11 . LEU   A 1 122 ? 25.207 -11.858 8.814   1.00 16.12 ?  122  LEU   A HD11 1 
ATOM   2643 H  HD12 . LEU   A 1 122 ? 24.109 -11.716 9.951   1.00 16.12 ?  122  LEU   A HD12 1 
ATOM   2644 H  HD13 . LEU   A 1 122 ? 23.735 -11.394 8.441   1.00 16.12 ?  122  LEU   A HD13 1 
ATOM   2645 H  HD21 . LEU   A 1 122 ? 26.228 -9.902  7.817   1.00 14.84 ?  122  LEU   A HD21 1 
ATOM   2646 H  HD22 . LEU   A 1 122 ? 24.827 -9.305  7.365   1.00 14.84 ?  122  LEU   A HD22 1 
ATOM   2647 H  HD23 . LEU   A 1 122 ? 25.806 -8.438  8.268   1.00 14.84 ?  122  LEU   A HD23 1 
ATOM   2648 N  N    A LEU   A 1 123 ? 21.722 -7.073  11.213  0.30 10.47 ?  123  LEU   A N    1 
ATOM   2649 N  N    B LEU   A 1 123 ? 21.729 -7.072  11.225  0.70 10.57 ?  123  LEU   A N    1 
ATOM   2650 C  CA   A LEU   A 1 123 ? 20.565 -6.298  10.784  0.30 10.18 ?  123  LEU   A CA   1 
ATOM   2651 C  CA   B LEU   A 1 123 ? 20.552 -6.282  10.884  0.70 10.16 ?  123  LEU   A CA   1 
ATOM   2652 C  C    A LEU   A 1 123 ? 20.843 -5.823  9.367   0.30 9.75  ?  123  LEU   A C    1 
ATOM   2653 C  C    B LEU   A 1 123 ? 20.773 -5.720  9.486   0.70 9.67  ?  123  LEU   A C    1 
ATOM   2654 O  O    A LEU   A 1 123 ? 21.938 -5.326  9.088   0.30 9.32  ?  123  LEU   A O    1 
ATOM   2655 O  O    B LEU   A 1 123 ? 21.791 -5.064  9.246   0.70 10.22 ?  123  LEU   A O    1 
ATOM   2656 C  CB   A LEU   A 1 123 ? 20.384 -5.085  11.694  0.30 10.64 ?  123  LEU   A CB   1 
ATOM   2657 C  CB   B LEU   A 1 123 ? 20.403 -5.127  11.877  0.70 10.72 ?  123  LEU   A CB   1 
ATOM   2658 C  CG   A LEU   A 1 123 ? 19.307 -4.055  11.355  0.30 11.31 ?  123  LEU   A CG   1 
ATOM   2659 C  CG   B LEU   A 1 123 ? 19.379 -4.055  11.504  0.70 11.71 ?  123  LEU   A CG   1 
ATOM   2660 C  CD1  A LEU   A 1 123 ? 17.920 -4.677  11.387  0.30 11.39 ?  123  LEU   A CD1  1 
ATOM   2661 C  CD1  B LEU   A 1 123 ? 17.969 -4.632  11.498  0.70 12.47 ?  123  LEU   A CD1  1 
ATOM   2662 C  CD2  A LEU   A 1 123 ? 19.397 -2.890  12.330  0.30 11.85 ?  123  LEU   A CD2  1 
ATOM   2663 C  CD2  B LEU   A 1 123 ? 19.477 -2.870  12.450  0.70 12.52 ?  123  LEU   A CD2  1 
ATOM   2664 H  H    A LEU   A 1 123 ? 22.359 -6.583  11.531  0.30 12.59 ?  123  LEU   A H    1 
ATOM   2665 H  H    B LEU   A 1 123 ? 22.392 -6.582  11.490  0.70 12.71 ?  123  LEU   A H    1 
ATOM   2666 H  HA   A LEU   A 1 123 ? 19.766 -6.853  10.800  0.30 12.24 ?  123  LEU   A HA   1 
ATOM   2667 H  HA   B LEU   A 1 123 ? 19.754 -6.830  10.898  0.70 12.21 ?  123  LEU   A HA   1 
ATOM   2668 H  HB2  A LEU   A 1 123 ? 20.185 -5.412  12.579  0.30 12.80 ?  123  LEU   A HB2  1 
ATOM   2669 H  HB2  B LEU   A 1 123 ? 20.134 -5.497  12.735  0.70 12.89 ?  123  LEU   A HB2  1 
ATOM   2670 H  HB3  A LEU   A 1 123 ? 21.226 -4.609  11.709  0.30 12.80 ?  123  LEU   A HB3  1 
ATOM   2671 H  HB3  B LEU   A 1 123 ? 21.261 -4.688  11.969  0.70 12.89 ?  123  LEU   A HB3  1 
ATOM   2672 H  HG   A LEU   A 1 123 ? 19.460 -3.708  10.461  0.30 13.60 ?  123  LEU   A HG   1 
ATOM   2673 H  HG   B LEU   A 1 123 ? 19.564 -3.725  10.610  0.70 14.07 ?  123  LEU   A HG   1 
ATOM   2674 H  HD11 A LEU   A 1 123 ? 17.262 -3.990  11.196  0.30 13.69 ?  123  LEU   A HD11 1 
ATOM   2675 H  HD11 B LEU   A 1 123 ? 17.341 -3.924  11.291  0.70 14.99 ?  123  LEU   A HD11 1 
ATOM   2676 H  HD12 A LEU   A 1 123 ? 17.874 -5.377  10.719  0.30 13.69 ?  123  LEU   A HD12 1 
ATOM   2677 H  HD12 B LEU   A 1 123 ? 17.918 -5.329  10.825  0.70 14.99 ?  123  LEU   A HD12 1 
ATOM   2678 H  HD13 A LEU   A 1 123 ? 17.764 -5.048  12.270  0.30 13.69 ?  123  LEU   A HD13 1 
ATOM   2679 H  HD13 B LEU   A 1 123 ? 17.779 -5.001  12.373  0.70 14.99 ?  123  LEU   A HD13 1 
ATOM   2680 H  HD21 A LEU   A 1 123 ? 18.711 -2.242  12.114  0.30 14.24 ?  123  LEU   A HD21 1 
ATOM   2681 H  HD21 B LEU   A 1 123 ? 18.819 -2.208  12.192  0.70 15.04 ?  123  LEU   A HD21 1 
ATOM   2682 H  HD22 A LEU   A 1 123 ? 19.265 -3.227  13.232  0.30 14.24 ?  123  LEU   A HD22 1 
ATOM   2683 H  HD22 B LEU   A 1 123 ? 19.305 -3.179  13.353  0.70 15.04 ?  123  LEU   A HD22 1 
ATOM   2684 H  HD23 A LEU   A 1 123 ? 20.275 -2.485  12.255  0.30 14.24 ?  123  LEU   A HD23 1 
ATOM   2685 H  HD23 B LEU   A 1 123 ? 20.369 -2.498  12.389  0.70 15.04 ?  123  LEU   A HD23 1 
ATOM   2686 N  N    A ALA   A 1 124 ? 19.868 -5.966  8.472   0.30 10.09 ?  124  ALA   A N    1 
ATOM   2687 N  N    B ALA   A 1 124 ? 19.837 -5.953  8.569   0.70 9.63  ?  124  ALA   A N    1 
ATOM   2688 C  CA   A ALA   A 1 124 ? 20.171 -5.761  7.065   0.30 10.51 ?  124  ALA   A CA   1 
ATOM   2689 C  CA   B ALA   A 1 124 ? 20.082 -5.624  7.174   0.70 9.19  ?  124  ALA   A CA   1 
ATOM   2690 C  C    A ALA   A 1 124 ? 18.930 -5.337  6.295   0.30 10.06 ?  124  ALA   A C    1 
ATOM   2691 C  C    B ALA   A 1 124 ? 18.834 -5.138  6.455   0.70 9.25  ?  124  ALA   A C    1 
ATOM   2692 O  O    A ALA   A 1 124 ? 17.810 -5.721  6.656   0.30 10.07 ?  124  ALA   A O    1 
ATOM   2693 O  O    B ALA   A 1 124 ? 17.707 -5.476  6.835   0.70 9.78  ?  124  ALA   A O    1 
ATOM   2694 C  CB   A ALA   A 1 124 ? 20.772 -7.033  6.444   0.30 10.88 ?  124  ALA   A CB   1 
ATOM   2695 C  CB   B ALA   A 1 124 ? 20.630 -6.836  6.408   0.70 9.36  ?  124  ALA   A CB   1 
ATOM   2696 H  H    A ALA   A 1 124 ? 19.049 -6.161  8.648   0.30 12.13 ?  124  ALA   A H    1 
ATOM   2697 H  H    B ALA   A 1 124 ? 19.067 -6.302  8.722   0.70 11.58 ?  124  ALA   A H    1 
ATOM   2698 H  HA   A ALA   A 1 124 ? 20.835 -5.062  6.995   0.30 12.64 ?  124  ALA   A HA   1 
ATOM   2699 H  HA   B ALA   A 1 124 ? 20.754 -4.924  7.138   0.70 11.06 ?  124  ALA   A HA   1 
ATOM   2700 H  HB1  A ALA   A 1 124 ? 20.971 -6.874  5.509   0.30 13.09 ?  124  ALA   A HB1  1 
ATOM   2701 H  HB1  B ALA   A 1 124 ? 20.775 -6.591  5.480   0.70 11.26 ?  124  ALA   A HB1  1 
ATOM   2702 H  HB2  A ALA   A 1 124 ? 21.593 -7.262  6.919   0.30 13.09 ?  124  ALA   A HB2  1 
ATOM   2703 H  HB2  B ALA   A 1 124 ? 21.469 -7.114  6.810   0.70 11.26 ?  124  ALA   A HB2  1 
ATOM   2704 H  HB3  A ALA   A 1 124 ? 20.136 -7.761  6.528   0.30 13.09 ?  124  ALA   A HB3  1 
ATOM   2705 H  HB3  B ALA   A 1 124 ? 19.985 -7.559  6.460   0.70 11.26 ?  124  ALA   A HB3  1 
ATOM   2706 N  N    A PRO   A 1 125 ? 19.097 -4.548  5.239   0.30 9.62  ?  125  PRO   A N    1 
ATOM   2707 N  N    B PRO   A 1 125 ? 19.015 -4.366  5.387   0.70 9.40  ?  125  PRO   A N    1 
ATOM   2708 C  CA   A PRO   A 1 125 ? 18.002 -4.272  4.311   0.30 9.45  ?  125  PRO   A CA   1 
ATOM   2709 C  CA   B PRO   A 1 125 ? 17.941 -4.119  4.428   0.70 10.30 ?  125  PRO   A CA   1 
ATOM   2710 C  C    A PRO   A 1 125 ? 18.028 -5.293  3.181   0.30 9.24  ?  125  PRO   A C    1 
ATOM   2711 C  C    B PRO   A 1 125 ? 17.988 -5.215  3.369   0.70 10.45 ?  125  PRO   A C    1 
ATOM   2712 O  O    A PRO   A 1 125 ? 18.979 -6.060  3.022   0.30 9.55  ?  125  PRO   A O    1 
ATOM   2713 O  O    B PRO   A 1 125 ? 18.931 -6.005  3.302   0.70 10.67 ?  125  PRO   A O    1 
ATOM   2714 C  CB   A PRO   A 1 125 ? 18.394 -2.898  3.761   0.30 9.54  ?  125  PRO   A CB   1 
ATOM   2715 C  CB   B PRO   A 1 125 ? 18.386 -2.790  3.805   0.70 10.47 ?  125  PRO   A CB   1 
ATOM   2716 C  CG   A PRO   A 1 125 ? 19.898 -2.993  3.671   0.30 10.00 ?  125  PRO   A CG   1 
ATOM   2717 C  CG   B PRO   A 1 125 ? 19.902 -2.985  3.685   0.70 11.15 ?  125  PRO   A CG   1 
ATOM   2718 C  CD   A PRO   A 1 125 ? 20.322 -3.822  4.864   0.30 9.86  ?  125  PRO   A CD   1 
ATOM   2719 C  CD   B PRO   A 1 125 ? 20.291 -3.783  4.924   0.70 10.52 ?  125  PRO   A CD   1 
ATOM   2720 H  HA   A PRO   A 1 125 ? 17.135 -4.249  4.754   0.30 11.36 ?  125  PRO   A HA   1 
ATOM   2721 H  HA   B PRO   A 1 125 ? 17.065 -4.051  4.846   0.70 12.39 ?  125  PRO   A HA   1 
ATOM   2722 H  HB2  A PRO   A 1 125 ? 17.995 -2.767  2.886   0.30 11.47 ?  125  PRO   A HB2  1 
ATOM   2723 H  HB2  B PRO   A 1 125 ? 17.965 -2.669  2.937   0.70 12.59 ?  125  PRO   A HB2  1 
ATOM   2724 H  HB3  A PRO   A 1 125 ? 18.120 -2.205  4.380   0.30 11.47 ?  125  PRO   A HB3  1 
ATOM   2725 H  HB3  B PRO   A 1 125 ? 18.165 -2.050  4.402   0.70 12.59 ?  125  PRO   A HB3  1 
ATOM   2726 H  HG2  A PRO   A 1 125 ? 20.145 -3.431  2.842   0.30 12.02 ?  125  PRO   A HG2  1 
ATOM   2727 H  HG2  B PRO   A 1 125 ? 20.102 -3.479  2.874   0.70 13.40 ?  125  PRO   A HG2  1 
ATOM   2728 H  HG3  A PRO   A 1 125 ? 20.279 -2.104  3.717   0.30 12.02 ?  125  PRO   A HG3  1 
ATOM   2729 H  HG3  B PRO   A 1 125 ? 20.342 -2.118  3.675   0.70 13.40 ?  125  PRO   A HG3  1 
ATOM   2730 H  HD2  A PRO   A 1 125 ? 21.020 -4.447  4.615   0.30 11.86 ?  125  PRO   A HD2  1 
ATOM   2731 H  HD2  B PRO   A 1 125 ? 20.920 -4.482  4.685   0.70 12.65 ?  125  PRO   A HD2  1 
ATOM   2732 H  HD3  A PRO   A 1 125 ? 20.600 -3.249  5.595   0.30 11.86 ?  125  PRO   A HD3  1 
ATOM   2733 H  HD3  B PRO   A 1 125 ? 20.661 -3.190  5.599   0.70 12.65 ?  125  PRO   A HD3  1 
ATOM   2734 N  N    A LEU   A 1 126 ? 16.969 -5.276  2.381   0.30 9.33  ?  126  LEU   A N    1 
ATOM   2735 N  N    B LEU   A 1 126 ? 16.961 -5.244  2.525   0.70 11.33 ?  126  LEU   A N    1 
ATOM   2736 C  CA   A LEU   A 1 126 ? 16.957 -6.078  1.164   0.30 9.56  ?  126  LEU   A CA   1 
ATOM   2737 C  CA   B LEU   A 1 126 ? 17.108 -5.990  1.284   0.70 12.33 ?  126  LEU   A CA   1 
ATOM   2738 C  C    A LEU   A 1 126 ? 17.894 -5.449  0.144   0.30 8.92  ?  126  LEU   A C    1 
ATOM   2739 C  C    B LEU   A 1 126 ? 18.167 -5.308  0.422   0.70 13.62 ?  126  LEU   A C    1 
ATOM   2740 O  O    A LEU   A 1 126 ? 17.656 -4.330  -0.331  0.30 8.38  ?  126  LEU   A O    1 
ATOM   2741 O  O    B LEU   A 1 126 ? 18.388 -4.098  0.523   0.70 15.51 ?  126  LEU   A O    1 
ATOM   2742 C  CB   A LEU   A 1 126 ? 15.537 -6.211  0.623   0.30 10.76 ?  126  LEU   A CB   1 
ATOM   2743 C  CB   B LEU   A 1 126 ? 15.780 -6.077  0.532   0.70 13.41 ?  126  LEU   A CB   1 
ATOM   2744 C  CG   A LEU   A 1 126 ? 14.703 -7.232  1.403   0.30 11.49 ?  126  LEU   A CG   1 
ATOM   2745 C  CG   B LEU   A 1 126 ? 14.675 -6.933  1.154   0.70 14.31 ?  126  LEU   A CG   1 
ATOM   2746 C  CD1  A LEU   A 1 126 ? 13.256 -7.173  0.972   0.30 11.81 ?  126  LEU   A CD1  1 
ATOM   2747 C  CD1  B LEU   A 1 126 ? 13.387 -6.753  0.375   0.70 15.02 ?  126  LEU   A CD1  1 
ATOM   2748 C  CD2  A LEU   A 1 126 ? 15.262 -8.645  1.233   0.30 12.01 ?  126  LEU   A CD2  1 
ATOM   2749 C  CD2  B LEU   A 1 126 ? 15.055 -8.410  1.191   0.70 14.67 ?  126  LEU   A CD2  1 
ATOM   2750 H  H    A LEU   A 1 126 ? 16.255 -4.819  2.516   0.30 11.22 ?  126  LEU   A H    1 
ATOM   2751 H  H    B LEU   A 1 126 ? 16.201 -4.851  2.637   0.70 13.62 ?  126  LEU   A H    1 
ATOM   2752 H  HA   A LEU   A 1 126 ? 17.293 -6.963  1.364   0.30 11.50 ?  126  LEU   A HA   1 
ATOM   2753 H  HA   B LEU   A 1 126 ? 17.403 -6.888  1.486   0.70 14.83 ?  126  LEU   A HA   1 
ATOM   2754 H  HB2  A LEU   A 1 126 ? 15.093 -5.351  0.682   0.30 12.93 ?  126  LEU   A HB2  1 
ATOM   2755 H  HB2  B LEU   A 1 126 ? 15.422 -5.182  0.439   0.70 16.12 ?  126  LEU   A HB2  1 
ATOM   2756 H  HB3  A LEU   A 1 126 ? 15.578 -6.500  -0.304  0.30 12.93 ?  126  LEU   A HB3  1 
ATOM   2757 H  HB3  B LEU   A 1 126 ? 15.954 -6.444  -0.349  0.70 16.12 ?  126  LEU   A HB3  1 
ATOM   2758 H  HG   A LEU   A 1 126 ? 14.743 -7.011  2.345   0.30 13.81 ?  126  LEU   A HG   1 
ATOM   2759 H  HG   B LEU   A 1 126 ? 14.517 -6.641  2.065   0.70 17.20 ?  126  LEU   A HG   1 
ATOM   2760 H  HD11 A LEU   A 1 126 ? 12.748 -7.818  1.488   0.30 14.19 ?  126  LEU   A HD11 1 
ATOM   2761 H  HD11 B LEU   A 1 126 ? 12.692 -7.301  0.776   0.70 18.04 ?  126  LEU   A HD11 1 
ATOM   2762 H  HD12 A LEU   A 1 126 ? 12.917 -6.279  1.134   0.30 14.19 ?  126  LEU   A HD12 1 
ATOM   2763 H  HD12 B LEU   A 1 126 ? 13.126 -5.817  0.407   0.70 18.04 ?  126  LEU   A HD12 1 
ATOM   2764 H  HD13 A LEU   A 1 126 ? 13.199 -7.384  0.028   0.30 14.19 ?  126  LEU   A HD13 1 
ATOM   2765 H  HD13 B LEU   A 1 126 ? 13.531 -7.024  -0.545  0.70 18.04 ?  126  LEU   A HD13 1 
ATOM   2766 H  HD21 A LEU   A 1 126 ? 14.585 -9.286  1.494   0.30 14.43 ?  126  LEU   A HD21 1 
ATOM   2767 H  HD21 B LEU   A 1 126 ? 14.306 -8.925  1.530   0.70 17.62 ?  126  LEU   A HD21 1 
ATOM   2768 H  HD22 A LEU   A 1 126 ? 15.505 -8.779  0.303   0.30 14.43 ?  126  LEU   A HD22 1 
ATOM   2769 H  HD22 B LEU   A 1 126 ? 15.275 -8.703  0.291   0.70 17.62 ?  126  LEU   A HD22 1 
ATOM   2770 H  HD23 A LEU   A 1 126 ? 16.048 -8.746  1.795   0.30 14.43 ?  126  LEU   A HD23 1 
ATOM   2771 H  HD23 B LEU   A 1 126 ? 15.825 -8.524  1.771   0.70 17.62 ?  126  LEU   A HD23 1 
ATOM   2772 N  N    A LEU   A 1 127 ? 18.974 -6.168  -0.167  0.30 8.89  ?  127  LEU   A N    1 
ATOM   2773 N  N    B LEU   A 1 127 ? 18.853 -6.094  -0.407  0.70 12.37 ?  127  LEU   A N    1 
ATOM   2774 C  CA   A LEU   A 1 127 ? 19.963 -5.691  -1.120  0.30 9.26  ?  127  LEU   A CA   1 
ATOM   2775 C  CA   B LEU   A 1 127 ? 19.873 -5.557  -1.295  0.70 12.31 ?  127  LEU   A CA   1 
ATOM   2776 C  C    A LEU   A 1 127 ? 19.324 -5.461  -2.479  0.30 8.88  ?  127  LEU   A C    1 
ATOM   2777 C  C    B LEU   A 1 127 ? 19.363 -5.492  -2.731  0.70 12.06 ?  127  LEU   A C    1 
ATOM   2778 O  O    A LEU   A 1 127 ? 18.469 -6.230  -2.928  0.30 9.43  ?  127  LEU   A O    1 
ATOM   2779 O  O    B LEU   A 1 127 ? 18.546 -6.307  -3.169  0.70 12.12 ?  127  LEU   A O    1 
ATOM   2780 C  CB   A LEU   A 1 127 ? 21.090 -6.715  -1.265  0.30 9.29  ?  127  LEU   A CB   1 
ATOM   2781 C  CB   B LEU   A 1 127 ? 21.162 -6.386  -1.230  0.70 13.17 ?  127  LEU   A CB   1 
ATOM   2782 C  CG   A LEU   A 1 127 ? 21.921 -6.972  -0.006  0.30 8.96  ?  127  LEU   A CG   1 
ATOM   2783 C  CG   B LEU   A 1 127 ? 21.935 -6.374  0.096   0.70 14.11 ?  127  LEU   A CG   1 
ATOM   2784 C  CD1  A LEU   A 1 127 ? 23.032 -7.967  -0.301  0.30 9.11  ?  127  LEU   A CD1  1 
ATOM   2785 C  CD1  B LEU   A 1 127 ? 23.124 -7.311  0.015   0.70 14.55 ?  127  LEU   A CD1  1 
ATOM   2786 C  CD2  A LEU   A 1 127 ? 22.491 -5.675  0.548   0.30 8.93  ?  127  LEU   A CD2  1 
ATOM   2787 C  CD2  B LEU   A 1 127 ? 22.399 -4.969  0.465   0.70 15.17 ?  127  LEU   A CD2  1 
ATOM   2788 H  H    A LEU   A 1 127 ? 19.153 -6.942  0.171   0.30 10.69 ?  127  LEU   A H    1 
ATOM   2789 H  H    B LEU   A 1 127 ? 18.741 -6.952  -0.472  0.70 14.87 ?  127  LEU   A H    1 
ATOM   2790 H  HA   A LEU   A 1 127 ? 20.339 -4.858  -0.805  0.30 11.13 ?  127  LEU   A HA   1 
ATOM   2791 H  HA   B LEU   A 1 127 ? 20.096 -4.661  -1.009  0.70 14.79 ?  127  LEU   A HA   1 
ATOM   2792 H  HB2  A LEU   A 1 127 ? 20.700 -7.565  -1.535  0.30 11.17 ?  127  LEU   A HB2  1 
ATOM   2793 H  HB2  B LEU   A 1 127 ? 20.944 -7.314  -1.416  0.70 15.83 ?  127  LEU   A HB2  1 
ATOM   2794 H  HB3  A LEU   A 1 127 ? 21.695 -6.407  -1.957  0.30 11.17 ?  127  LEU   A HB3  1 
ATOM   2795 H  HB3  B LEU   A 1 127 ? 21.770 -6.060  -1.910  0.70 15.83 ?  127  LEU   A HB3  1 
ATOM   2796 H  HG   A LEU   A 1 127 ? 21.348 -7.364  0.672   0.30 10.78 ?  127  LEU   A HG   1 
ATOM   2797 H  HG   B LEU   A 1 127 ? 21.358 -6.694  0.808   0.70 16.96 ?  127  LEU   A HG   1 
ATOM   2798 H  HD11 A LEU   A 1 127 ? 23.502 -8.171  0.524   0.30 10.96 ?  127  LEU   A HD11 1 
ATOM   2799 H  HD11 B LEU   A 1 127 ? 23.614 -7.277  0.855   0.70 17.48 ?  127  LEU   A HD11 1 
ATOM   2800 H  HD12 A LEU   A 1 127 ? 22.645 -8.778  -0.668  0.30 10.96 ?  127  LEU   A HD12 1 
ATOM   2801 H  HD12 B LEU   A 1 127 ? 22.808 -8.213  -0.145  0.70 17.48 ?  127  LEU   A HD12 1 
ATOM   2802 H  HD13 A LEU   A 1 127 ? 23.644 -7.575  -0.942  0.30 10.96 ?  127  LEU   A HD13 1 
ATOM   2803 H  HD13 B LEU   A 1 127 ? 23.701 -7.027  -0.711  0.70 17.48 ?  127  LEU   A HD13 1 
ATOM   2804 H  HD21 A LEU   A 1 127 ? 23.151 -5.888  1.226   0.30 10.74 ?  127  LEU   A HD21 1 
ATOM   2805 H  HD21 B LEU   A 1 127 ? 22.974 -5.017  1.246   0.70 18.22 ?  127  LEU   A HD21 1 
ATOM   2806 H  HD22 A LEU   A 1 127 ? 22.909 -5.183  -0.177  0.30 10.74 ?  127  LEU   A HD22 1 
ATOM   2807 H  HD22 B LEU   A 1 127 ? 22.894 -4.596  -0.284  0.70 18.22 ?  127  LEU   A HD22 1 
ATOM   2808 H  HD23 A LEU   A 1 127 ? 21.773 -5.155  0.933   0.30 10.74 ?  127  LEU   A HD23 1 
ATOM   2809 H  HD23 B LEU   A 1 127 ? 21.625 -4.421  0.656   0.70 18.22 ?  127  LEU   A HD23 1 
ATOM   2810 N  N    A SER   A 1 128 ? 19.755 -4.387  -3.130  0.30 8.90  ?  128  SER   A N    1 
ATOM   2811 N  N    B SER   A 1 128 ? 19.855 -4.483  -3.446  0.70 12.31 ?  128  SER   A N    1 
ATOM   2812 C  CA   A SER   A 1 128 ? 19.337 -3.990  -4.468  0.30 9.20  ?  128  SER   A CA   1 
ATOM   2813 C  CA   B SER   A 1 128 ? 19.589 -4.232  -4.860  0.70 12.58 ?  128  SER   A CA   1 
ATOM   2814 C  C    A SER   A 1 128 ? 17.874 -3.570  -4.547  0.30 9.91  ?  128  SER   A C    1 
ATOM   2815 C  C    B SER   A 1 128 ? 18.184 -3.721  -5.156  0.70 13.04 ?  128  SER   A C    1 
ATOM   2816 O  O    A SER   A 1 128 ? 17.369 -3.334  -5.649  0.30 10.48 ?  128  SER   A O    1 
ATOM   2817 O  O    B SER   A 1 128 ? 17.896 -3.360  -6.299  0.70 13.77 ?  128  SER   A O    1 
ATOM   2818 C  CB   A SER   A 1 128 ? 19.668 -5.044  -5.530  0.30 9.15  ?  128  SER   A CB   1 
ATOM   2819 C  CB   B SER   A 1 128 ? 19.947 -5.428  -5.748  0.70 12.98 ?  128  SER   A CB   1 
ATOM   2820 O  OG   A SER   A 1 128 ? 21.069 -5.237  -5.628  0.30 9.24  ?  128  SER   A OG   1 
ATOM   2821 O  OG   B SER   A 1 128 ? 21.351 -5.587  -5.819  0.70 12.91 ?  128  SER   A OG   1 
ATOM   2822 H  H    A SER   A 1 128 ? 20.335 -3.843  -2.793  0.30 10.71 ?  128  SER   A H    1 
ATOM   2823 H  H    B SER   A 1 128 ? 20.394 -3.903  -3.108  0.70 14.80 ?  128  SER   A H    1 
ATOM   2824 H  HA   A SER   A 1 128 ? 19.858 -3.213  -4.694  0.30 11.06 ?  128  SER   A HA   1 
ATOM   2825 H  HA   B SER   A 1 128 ? 20.183 -3.522  -5.125  0.70 15.12 ?  128  SER   A HA   1 
ATOM   2826 H  HB2  A SER   A 1 128 ? 19.245 -5.882  -5.290  0.30 11.01 ?  128  SER   A HB2  1 
ATOM   2827 H  HB2  B SER   A 1 128 ? 19.553 -6.234  -5.387  0.70 15.60 ?  128  SER   A HB2  1 
ATOM   2828 H  HB3  A SER   A 1 128 ? 19.344 -4.737  -6.389  0.30 11.01 ?  128  SER   A HB3  1 
ATOM   2829 H  HB3  B SER   A 1 128 ? 19.605 -5.264  -6.646  0.70 15.60 ?  128  SER   A HB3  1 
ATOM   2830 H  HG   A SER   A 1 128 ? 21.446 -4.505  -5.795  0.30 11.11 ?  128  SER   A HG   1 
ATOM   2831 H  HG   B SER   A 1 128 ? 21.700 -4.884  -6.128  0.70 15.51 ?  128  SER   A HG   1 
ATOM   2832 N  N    A ALA   A 1 129 ? 17.185 -3.449  -3.414  0.30 9.97  ?  129  ALA   A N    1 
ATOM   2833 N  N    B ALA   A 1 129 ? 17.307 -3.678  -4.153  0.70 13.22 ?  129  ALA   A N    1 
ATOM   2834 C  CA   A ALA   A 1 129 ? 15.821 -2.951  -3.406  0.30 9.55  ?  129  ALA   A CA   1 
ATOM   2835 C  CA   B ALA   A 1 129 ? 16.001 -3.061  -4.353  0.70 14.00 ?  129  ALA   A CA   1 
ATOM   2836 C  C    A ALA   A 1 129 ? 15.826 -1.424  -3.423  0.30 9.79  ?  129  ALA   A C    1 
ATOM   2837 C  C    B ALA   A 1 129 ? 16.111 -1.568  -4.062  0.70 14.13 ?  129  ALA   A C    1 
ATOM   2838 O  O    A ALA   A 1 129 ? 16.871 -0.778  -3.532  0.30 9.56  ?  129  ALA   A O    1 
ATOM   2839 O  O    B ALA   A 1 129 ? 17.188 -0.987  -4.227  0.70 13.93 ?  129  ALA   A O    1 
ATOM   2840 C  CB   A ALA   A 1 129 ? 15.064 -3.494  -2.197  0.30 9.63  ?  129  ALA   A CB   1 
ATOM   2841 C  CB   B ALA   A 1 129 ? 14.941 -3.752  -3.496  0.70 15.54 ?  129  ALA   A CB   1 
ATOM   2842 H  H    A ALA   A 1 129 ? 17.486 -3.654  -2.636  0.30 11.98 ?  129  ALA   A H    1 
ATOM   2843 H  H    B ALA   A 1 129 ? 17.441 -4.002  -3.360  0.70 15.88 ?  129  ALA   A H    1 
ATOM   2844 H  HA   A ALA   A 1 129 ? 15.368 -3.251  -4.206  0.30 11.49 ?  129  ALA   A HA   1 
ATOM   2845 H  HA   B ALA   A 1 129 ? 15.751 -3.164  -5.279  0.70 16.82 ?  129  ALA   A HA   1 
ATOM   2846 H  HB1  A ALA   A 1 129 ? 14.152 -3.163  -2.221  0.30 11.58 ?  129  ALA   A HB1  1 
ATOM   2847 H  HB1  B ALA   A 1 129 ? 14.076 -3.355  -3.695  0.70 18.68 ?  129  ALA   A HB1  1 
ATOM   2848 H  HB2  A ALA   A 1 129 ? 15.066 -4.462  -2.237  0.30 11.58 ?  129  ALA   A HB2  1 
ATOM   2849 H  HB2  B ALA   A 1 129 ? 14.927 -4.694  -3.716  0.70 18.68 ?  129  ALA   A HB2  1 
ATOM   2850 H  HB3  A ALA   A 1 129 ? 15.505 -3.194  -1.387  0.30 11.58 ?  129  ALA   A HB3  1 
ATOM   2851 H  HB3  B ALA   A 1 129 ? 15.157 -3.629  -2.562  0.70 18.68 ?  129  ALA   A HB3  1 
ATOM   2852 N  N    A GLY   A 1 130 ? 14.638 -0.840  -3.322  0.30 10.48 ?  130  GLY   A N    1 
ATOM   2853 N  N    B GLY   A 1 130 ? 15.022 -0.926  -3.651  0.70 14.65 ?  130  GLY   A N    1 
ATOM   2854 C  CA   A GLY   A 1 130 ? 14.538 0.608   -3.284  0.30 11.62 ?  130  GLY   A CA   1 
ATOM   2855 C  CA   B GLY   A 1 130 ? 15.111 0.504   -3.421  0.70 15.20 ?  130  GLY   A CA   1 
ATOM   2856 C  C    A GLY   A 1 130 ? 15.118 1.218   -4.544  0.30 11.84 ?  130  GLY   A C    1 
ATOM   2857 C  C    B GLY   A 1 130 ? 15.594 1.205   -4.670  0.70 14.95 ?  130  GLY   A C    1 
ATOM   2858 O  O    A GLY   A 1 130 ? 14.858 0.761   -5.662  0.30 11.49 ?  130  GLY   A O    1 
ATOM   2859 O  O    B GLY   A 1 130 ? 15.200 0.863   -5.791  0.70 15.06 ?  130  GLY   A O    1 
ATOM   2860 H  H    A GLY   A 1 130 ? 13.887 -1.257  -3.281  0.30 12.61 ?  130  GLY   A H    1 
ATOM   2861 H  H    B GLY   A 1 130 ? 14.251 -1.279  -3.515  0.70 17.61 ?  130  GLY   A H    1 
ATOM   2862 H  HA2  A GLY   A 1 130 ? 13.607 0.869   -3.194  0.30 13.97 ?  130  GLY   A HA2  1 
ATOM   2863 H  HA2  B GLY   A 1 130 ? 14.237 0.854   -3.181  0.70 18.27 ?  130  GLY   A HA2  1 
ATOM   2864 H  HA3  A GLY   A 1 130 ? 15.031 0.951   -2.522  0.30 13.97 ?  130  GLY   A HA3  1 
ATOM   2865 H  HA3  B GLY   A 1 130 ? 15.733 0.681   -2.705  0.70 18.27 ?  130  GLY   A HA3  1 
ATOM   2866 N  N    A ILE   A 1 131 ? 15.936 2.259   -4.363  0.30 12.38 ?  131  ILE   A N    1 
ATOM   2867 N  N    B ILE   A 1 131 ? 16.484 2.184   -4.484  0.70 14.78 ?  131  ILE   A N    1 
ATOM   2868 C  CA   A ILE   A 1 131 ? 16.471 3.011   -5.494  0.30 12.18 ?  131  ILE   A CA   1 
ATOM   2869 C  CA   B ILE   A 1 131 ? 16.947 2.991   -5.608  0.70 14.24 ?  131  ILE   A CA   1 
ATOM   2870 C  C    A ILE   A 1 131 ? 17.496 2.233   -6.305  0.30 12.20 ?  131  ILE   A C    1 
ATOM   2871 C  C    B ILE   A 1 131 ? 17.869 2.232   -6.550  0.70 14.31 ?  131  ILE   A C    1 
ATOM   2872 O  O    A ILE   A 1 131 ? 17.946 2.732   -7.343  0.30 12.43 ?  131  ILE   A O    1 
ATOM   2873 O  O    B ILE   A 1 131 ? 18.238 2.776   -7.598  0.70 15.27 ?  131  ILE   A O    1 
ATOM   2874 C  CB   A ILE   A 1 131 ? 17.044 4.374   -5.053  0.30 12.95 ?  131  ILE   A CB   1 
ATOM   2875 C  CB   B ILE   A 1 131 ? 17.561 4.337   -5.154  0.70 15.33 ?  131  ILE   A CB   1 
ATOM   2876 C  CG1  A ILE   A 1 131 ? 18.291 4.193   -4.181  0.30 14.11 ?  131  ILE   A CG1  1 
ATOM   2877 C  CG1  B ILE   A 1 131 ? 18.861 4.134   -4.369  0.70 16.34 ?  131  ILE   A CG1  1 
ATOM   2878 C  CG2  A ILE   A 1 131 ? 15.980 5.179   -4.317  0.30 12.74 ?  131  ILE   A CG2  1 
ATOM   2879 C  CG2  B ILE   A 1 131 ? 16.567 5.114   -4.305  0.70 15.83 ?  131  ILE   A CG2  1 
ATOM   2880 C  CD1  A ILE   A 1 131 ? 18.949 5.502   -3.783  0.30 15.04 ?  131  ILE   A CD1  1 
ATOM   2881 C  CD1  B ILE   A 1 131 ? 19.517 5.440   -3.927  0.70 17.67 ?  131  ILE   A CD1  1 
ATOM   2882 H  H    A ILE   A 1 131 ? 16.185 2.549   -3.598  0.30 14.88 ?  131  ILE   A H    1 
ATOM   2883 H  H    B ILE   A 1 131 ? 16.830 2.398   -3.725  0.70 17.76 ?  131  ILE   A H    1 
ATOM   2884 H  HA   A ILE   A 1 131 ? 15.732 3.202   -6.090  0.30 14.64 ?  131  ILE   A HA   1 
ATOM   2885 H  HA   B ILE   A 1 131 ? 16.172 3.218   -6.133  0.70 17.11 ?  131  ILE   A HA   1 
ATOM   2886 H  HB   A ILE   A 1 131 ? 17.297 4.865   -5.851  0.30 15.56 ?  131  ILE   A HB   1 
ATOM   2887 H  HB   B ILE   A 1 131 ? 17.764 4.864   -5.948  0.70 18.43 ?  131  ILE   A HB   1 
ATOM   2888 H  HG12 A ILE   A 1 131 ? 18.038 3.725   -3.371  0.30 16.96 ?  131  ILE   A HG12 1 
ATOM   2889 H  HG12 B ILE   A 1 131 ? 18.666 3.616   -3.573  0.70 19.64 ?  131  ILE   A HG12 1 
ATOM   2890 H  HG13 A ILE   A 1 131 ? 18.946 3.671   -4.672  0.30 16.96 ?  131  ILE   A HG13 1 
ATOM   2891 H  HG13 B ILE   A 1 131 ? 19.497 3.659   -4.925  0.70 19.64 ?  131  ILE   A HG13 1 
ATOM   2892 H  HG21 A ILE   A 1 131 ? 16.309 6.079   -4.167  0.30 15.32 ?  131  ILE   A HG21 1 
ATOM   2893 H  HG21 B ILE   A 1 131 ? 16.881 6.025   -4.202  0.70 19.03 ?  131  ILE   A HG21 1 
ATOM   2894 H  HG22 A ILE   A 1 131 ? 15.176 5.209   -4.860  0.30 15.32 ?  131  ILE   A HG22 1 
ATOM   2895 H  HG22 B ILE   A 1 131 ? 15.706 5.108   -4.749  0.70 19.03 ?  131  ILE   A HG22 1 
ATOM   2896 H  HG23 A ILE   A 1 131 ? 15.788 4.749   -3.469  0.30 15.32 ?  131  ILE   A HG23 1 
ATOM   2897 H  HG23 B ILE   A 1 131 ? 16.497 4.685   -3.439  0.70 19.03 ?  131  ILE   A HG23 1 
ATOM   2898 H  HD11 A ILE   A 1 131 ? 19.800 5.310   -3.359  0.30 18.07 ?  131  ILE   A HD11 1 
ATOM   2899 H  HD11 B ILE   A 1 131 ? 20.431 5.262   -3.659  0.70 21.22 ?  131  ILE   A HD11 1 
ATOM   2900 H  HD12 A ILE   A 1 131 ? 19.090 6.039   -4.579  0.30 18.07 ?  131  ILE   A HD12 1 
ATOM   2901 H  HD12 B ILE   A 1 131 ? 19.505 6.067   -4.668  0.70 21.22 ?  131  ILE   A HD12 1 
ATOM   2902 H  HD13 A ILE   A 1 131 ? 18.369 5.973   -3.165  0.30 18.07 ?  131  ILE   A HD13 1 
ATOM   2903 H  HD13 B ILE   A 1 131 ? 19.017 5.808   -3.180  0.70 21.22 ?  131  ILE   A HD13 1 
ATOM   2904 N  N    A PHE   A 1 132 ? 17.889 1.035   -5.856  0.30 12.10 ?  132  PHE   A N    1 
ATOM   2905 N  N    B PHE   A 1 132 ? 18.244 0.991   -6.211  0.70 13.73 ?  132  PHE   A N    1 
ATOM   2906 C  CA   A PHE   A 1 132 ? 18.742 0.155   -6.649  0.30 12.13 ?  132  PHE   A CA   1 
ATOM   2907 C  CA   B PHE   A 1 132 ? 19.103 0.167   -7.059  0.70 14.45 ?  132  PHE   A CA   1 
ATOM   2908 C  C    A PHE   A 1 132 ? 17.973 -0.603  -7.731  0.30 11.97 ?  132  PHE   A C    1 
ATOM   2909 C  C    B PHE   A 1 132 ? 18.331 -0.584  -8.147  0.70 15.29 ?  132  PHE   A C    1 
ATOM   2910 O  O    A PHE   A 1 132 ? 18.596 -1.236  -8.590  0.30 12.27 ?  132  PHE   A O    1 
ATOM   2911 O  O    B PHE   A 1 132 ? 18.958 -1.175  -9.035  0.70 16.89 ?  132  PHE   A O    1 
ATOM   2912 C  CB   A PHE   A 1 132 ? 19.486 -0.825  -5.733  0.30 12.27 ?  132  PHE   A CB   1 
ATOM   2913 C  CB   B PHE   A 1 132 ? 19.908 -0.829  -6.206  0.70 13.30 ?  132  PHE   A CB   1 
ATOM   2914 C  CG   A PHE   A 1 132 ? 20.716 -0.245  -5.073  0.30 11.72 ?  132  PHE   A CG   1 
ATOM   2915 C  CG   B PHE   A 1 132 ? 21.120 -0.229  -5.512  0.70 13.14 ?  132  PHE   A CG   1 
ATOM   2916 C  CD1  A PHE   A 1 132 ? 20.614 0.783   -4.147  0.30 11.64 ?  132  PHE   A CD1  1 
ATOM   2917 C  CD1  B PHE   A 1 132 ? 21.006 0.872   -4.673  0.70 13.99 ?  132  PHE   A CD1  1 
ATOM   2918 C  CD2  A PHE   A 1 132 ? 21.974 -0.759  -5.355  0.30 11.63 ?  132  PHE   A CD2  1 
ATOM   2919 C  CD2  B PHE   A 1 132 ? 22.371 -0.810  -5.672  0.70 13.99 ?  132  PHE   A CD2  1 
ATOM   2920 C  CE1  A PHE   A 1 132 ? 21.746 1.304   -3.536  0.30 11.08 ?  132  PHE   A CE1  1 
ATOM   2921 C  CE1  B PHE   A 1 132 ? 22.120 1.398   -4.035  0.70 14.51 ?  132  PHE   A CE1  1 
ATOM   2922 C  CE2  A PHE   A 1 132 ? 23.107 -0.245  -4.746  0.30 11.31 ?  132  PHE   A CE2  1 
ATOM   2923 C  CE2  B PHE   A 1 132 ? 23.486 -0.290  -5.036  0.70 14.89 ?  132  PHE   A CE2  1 
ATOM   2924 C  CZ   A PHE   A 1 132 ? 22.992 0.786   -3.834  0.30 10.83 ?  132  PHE   A CZ   1 
ATOM   2925 C  CZ   B PHE   A 1 132 ? 23.360 0.811   -4.212  0.70 14.99 ?  132  PHE   A CZ   1 
ATOM   2926 H  H    A PHE   A 1 132 ? 17.682 0.716   -5.080  0.30 14.54 ?  132  PHE   A H    1 
ATOM   2927 H  H    B PHE   A 1 132 ? 18.022 0.605   -5.474  0.70 16.50 ?  132  PHE   A H    1 
ATOM   2928 H  HA   A PHE   A 1 132 ? 19.409 0.698   -7.090  0.30 14.58 ?  132  PHE   A HA   1 
ATOM   2929 H  HA   B PHE   A 1 132 ? 19.748 0.745   -7.496  0.70 17.36 ?  132  PHE   A HA   1 
ATOM   2930 H  HB2  A PHE   A 1 132 ? 18.886 -1.110  -5.026  0.30 14.75 ?  132  PHE   A HB2  1 
ATOM   2931 H  HB2  B PHE   A 1 132 ? 19.334 -1.195  -5.519  0.70 15.99 ?  132  PHE   A HB2  1 
ATOM   2932 H  HB3  A PHE   A 1 132 ? 19.768 -1.589  -6.257  0.30 14.75 ?  132  PHE   A HB3  1 
ATOM   2933 H  HB3  B PHE   A 1 132 ? 20.230 -1.546  -6.779  0.70 15.99 ?  132  PHE   A HB3  1 
ATOM   2934 H  HD1  A PHE   A 1 132 ? 19.778 1.137   -3.940  0.30 13.99 ?  132  PHE   A HD1  1 
ATOM   2935 H  HD1  B PHE   A 1 132 ? 20.175 1.267   -4.549  0.70 16.81 ?  132  PHE   A HD1  1 
ATOM   2936 H  HD2  A PHE   A 1 132 ? 22.057 -1.453  -5.967  0.30 13.99 ?  132  PHE   A HD2  1 
ATOM   2937 H  HD2  B PHE   A 1 132 ? 22.466 -1.553  -6.224  0.70 16.81 ?  132  PHE   A HD2  1 
ATOM   2938 H  HE1  A PHE   A 1 132 ? 21.669 1.999   -2.920  0.30 13.32 ?  132  PHE   A HE1  1 
ATOM   2939 H  HE1  B PHE   A 1 132 ? 22.034 2.141   -3.481  0.70 17.44 ?  132  PHE   A HE1  1 
ATOM   2940 H  HE2  A PHE   A 1 132 ? 23.944 -0.595  -4.950  0.30 13.59 ?  132  PHE   A HE2  1 
ATOM   2941 H  HE2  B PHE   A 1 132 ? 24.322 -0.686  -5.161  0.70 17.90 ?  132  PHE   A HE2  1 
ATOM   2942 H  HZ   A PHE   A 1 132 ? 23.753 1.133   -3.426  0.30 13.02 ?  132  PHE   A HZ   1 
ATOM   2943 H  HZ   B PHE   A 1 132 ? 24.111 1.166   -3.786  0.70 18.02 ?  132  PHE   A HZ   1 
ATOM   2944 N  N    A GLY   A 1 133 ? 16.642 -0.580  -7.698  0.30 12.14 ?  133  GLY   A N    1 
ATOM   2945 N  N    B GLY   A 1 133 ? 16.998 -0.608  -8.092  0.70 15.12 ?  133  GLY   A N    1 
ATOM   2946 C  CA   A GLY   A 1 133 ? 15.843 -0.978  -8.841  0.30 13.07 ?  133  GLY   A CA   1 
ATOM   2947 C  CA   B GLY   A 1 133 ? 16.196 -0.982  -9.237  0.70 15.88 ?  133  GLY   A CA   1 
ATOM   2948 C  C    A GLY   A 1 133 ? 15.630 -2.461  -9.059  0.30 13.94 ?  133  GLY   A C    1 
ATOM   2949 C  C    B GLY   A 1 133 ? 15.664 -2.403  -9.275  0.70 16.02 ?  133  GLY   A C    1 
ATOM   2950 O  O    A GLY   A 1 133 ? 15.162 -2.838  -10.140 0.30 14.55 ?  133  GLY   A O    1 
ATOM   2951 O  O    B GLY   A 1 133 ? 14.772 -2.676  -10.088 0.70 16.98 ?  133  GLY   A O    1 
ATOM   2952 H  H    A GLY   A 1 133 ? 16.179 -0.334  -7.017  0.30 14.59 ?  133  GLY   A H    1 
ATOM   2953 H  H    B GLY   A 1 133 ? 16.547 -0.412  -7.389  0.70 18.16 ?  133  GLY   A H    1 
ATOM   2954 H  HA2  A GLY   A 1 133 ? 14.973 -0.558  -8.767  0.30 15.71 ?  133  GLY   A HA2  1 
ATOM   2955 H  HA2  B GLY   A 1 133 ? 15.434 -0.393  -9.275  0.70 19.08 ?  133  GLY   A HA2  1 
ATOM   2956 H  HA3  A GLY   A 1 133 ? 16.267 -0.640  -9.644  0.30 15.71 ?  133  GLY   A HA3  1 
ATOM   2957 H  HA3  B GLY   A 1 133 ? 16.726 -0.837  -10.039 0.70 19.08 ?  133  GLY   A HA3  1 
ATOM   2958 N  N    A ALA   A 1 134 ? 15.954 -3.319  -8.094  0.30 14.04 ?  134  ALA   A N    1 
ATOM   2959 N  N    B ALA   A 1 134 ? 16.165 -3.317  -8.442  0.70 15.17 ?  134  ALA   A N    1 
ATOM   2960 C  CA   A ALA   A 1 134 ? 15.677 -4.740  -8.254  0.30 14.51 ?  134  ALA   A CA   1 
ATOM   2961 C  CA   B ALA   A 1 134 ? 15.753 -4.707  -8.573  0.70 15.44 ?  134  ALA   A CA   1 
ATOM   2962 C  C    A ALA   A 1 134 ? 14.332 -5.109  -7.635  0.30 15.06 ?  134  ALA   A C    1 
ATOM   2963 C  C    B ALA   A 1 134 ? 14.422 -4.961  -7.863  0.70 15.90 ?  134  ALA   A C    1 
ATOM   2964 O  O    A ALA   A 1 134 ? 13.770 -4.378  -6.816  0.30 15.44 ?  134  ALA   A O    1 
ATOM   2965 O  O    B ALA   A 1 134 ? 13.934 -4.146  -7.075  0.70 16.39 ?  134  ALA   A O    1 
ATOM   2966 C  CB   A ALA   A 1 134 ? 16.778 -5.595  -7.627  0.30 14.63 ?  134  ALA   A CB   1 
ATOM   2967 C  CB   B ALA   A 1 134 ? 16.833 -5.653  -8.047  0.70 16.06 ?  134  ALA   A CB   1 
ATOM   2968 H  H    A ALA   A 1 134 ? 16.341 -3.106  -7.353  0.30 16.88 ?  134  ALA   A H    1 
ATOM   2969 H  H    B ALA   A 1 134 ? 16.731 -3.157  -7.809  0.70 18.23 ?  134  ALA   A H    1 
ATOM   2970 H  HA   A ALA   A 1 134 ? 15.642 -4.949  -9.200  0.30 17.43 ?  134  ALA   A HA   1 
ATOM   2971 H  HA   B ALA   A 1 134 ? 15.630 -4.901  -9.512  0.70 18.55 ?  134  ALA   A HA   1 
ATOM   2972 H  HB1  A ALA   A 1 134 ? 16.574 -6.532  -7.785  0.30 17.58 ?  134  ALA   A HB1  1 
ATOM   2973 H  HB1  B ALA   A 1 134 ? 16.536 -6.569  -8.175  0.70 19.30 ?  134  ALA   A HB1  1 
ATOM   2974 H  HB2  A ALA   A 1 134 ? 17.626 -5.369  -8.037  0.30 17.58 ?  134  ALA   A HB2  1 
ATOM   2975 H  HB2  B ALA   A 1 134 ? 17.655 -5.503  -8.542  0.70 19.30 ?  134  ALA   A HB2  1 
ATOM   2976 H  HB3  A ALA   A 1 134 ? 16.811 -5.421  -6.675  0.30 17.58 ?  134  ALA   A HB3  1 
ATOM   2977 H  HB3  B ALA   A 1 134 ? 16.978 -5.481  -7.105  0.70 19.30 ?  134  ALA   A HB3  1 
ATOM   2978 N  N    A ASP   A 1 135 ? 13.822 -6.265  -8.042  0.30 15.39 ?  135  ASP   A N    1 
ATOM   2979 N  N    B ASP   A 1 135 ? 13.839 -6.122  -8.157  0.70 16.78 ?  135  ASP   A N    1 
ATOM   2980 C  CA   A ASP   A 1 135 ? 12.577 -6.795  -7.493  0.30 15.77 ?  135  ASP   A CA   1 
ATOM   2981 C  CA   B ASP   A 1 135 ? 12.566 -6.521  -7.563  0.70 17.92 ?  135  ASP   A CA   1 
ATOM   2982 C  C    A ASP   A 1 135 ? 12.804 -7.215  -6.047  0.30 15.87 ?  135  ASP   A C    1 
ATOM   2983 C  C    B ASP   A 1 135 ? 12.804 -7.027  -6.145  0.70 17.14 ?  135  ASP   A C    1 
ATOM   2984 O  O    A ASP   A 1 135 ? 13.587 -8.141  -5.799  0.30 15.71 ?  135  ASP   A O    1 
ATOM   2985 O  O    B ASP   A 1 135 ? 13.535 -8.009  -5.966  0.70 16.61 ?  135  ASP   A O    1 
ATOM   2986 C  CB   A ASP   A 1 135 ? 12.150 -8.003  -8.321  0.30 16.22 ?  135  ASP   A CB   1 
ATOM   2987 C  CB   B ASP   A 1 135 ? 11.937 -7.630  -8.397  0.70 19.90 ?  135  ASP   A CB   1 
ATOM   2988 C  CG   A ASP   A 1 135 ? 10.884 -8.662  -7.805  0.30 16.92 ?  135  ASP   A CG   1 
ATOM   2989 C  CG   B ASP   A 1 135 ? 10.545 -8.034  -7.905  0.70 22.30 ?  135  ASP   A CG   1 
ATOM   2990 O  OD1  A ASP   A 1 135 ? 10.236 -8.109  -6.893  0.30 16.98 ?  135  ASP   A OD1  1 
ATOM   2991 O  OD1  B ASP   A 1 135 ? 10.125 -7.578  -6.818  0.70 23.49 ?  135  ASP   A OD1  1 
ATOM   2992 O  OD2  A ASP   A 1 135 ? 10.549 -9.754  -8.309  0.30 18.09 -1 135  ASP   A OD2  1 
ATOM   2993 O  OD2  B ASP   A 1 135 ? 9.866  -8.811  -8.611  0.70 23.68 -1 135  ASP   A OD2  1 
ATOM   2994 H  H    A ASP   A 1 135 ? 14.179 -6.765  -8.641  0.30 18.50 ?  135  ASP   A H    1 
ATOM   2995 H  H    B ASP   A 1 135 ? 14.169 -6.700  -8.699  0.70 20.16 ?  135  ASP   A H    1 
ATOM   2996 H  HA   A ASP   A 1 135 ? 11.886 -6.117  -7.541  0.30 18.95 ?  135  ASP   A HA   1 
ATOM   2997 H  HA   B ASP   A 1 135 ? 11.969 -5.759  -7.552  0.70 21.52 ?  135  ASP   A HA   1 
ATOM   2998 H  HB2  A ASP   A 1 135 ? 12.015 -7.723  -9.239  0.30 19.48 ?  135  ASP   A HB2  1 
ATOM   2999 H  HB2  B ASP   A 1 135 ? 11.882 -7.329  -9.319  0.70 23.91 ?  135  ASP   A HB2  1 
ATOM   3000 H  HB3  A ASP   A 1 135 ? 12.837 -8.679  -8.274  0.30 19.48 ?  135  ASP   A HB3  1 
ATOM   3001 H  HB3  B ASP   A 1 135 ? 12.497 -8.419  -8.339  0.70 23.91 ?  135  ASP   A HB3  1 
ATOM   3002 N  N    A PRO   A 1 136 ? 12.154 -6.578  -5.069  0.30 16.09 ?  136  PRO   A N    1 
ATOM   3003 N  N    B PRO   A 1 136 ? 12.216 -6.403  -5.122  0.70 16.80 ?  136  PRO   A N    1 
ATOM   3004 C  CA   A PRO   A 1 136 ? 12.389 -6.969  -3.669  0.30 15.81 ?  136  PRO   A CA   1 
ATOM   3005 C  CA   B PRO   A 1 136 ? 12.458 -6.867  -3.743  0.70 16.60 ?  136  PRO   A CA   1 
ATOM   3006 C  C    A PRO   A 1 136 ? 11.953 -8.387  -3.348  0.30 15.14 ?  136  PRO   A C    1 
ATOM   3007 C  C    B PRO   A 1 136 ? 11.995 -8.290  -3.463  0.70 15.92 ?  136  PRO   A C    1 
ATOM   3008 O  O    A PRO   A 1 136 ? 12.544 -9.019  -2.463  0.30 14.63 ?  136  PRO   A O    1 
ATOM   3009 O  O    B PRO   A 1 136 ? 12.568 -8.952  -2.587  0.70 15.04 ?  136  PRO   A O    1 
ATOM   3010 C  CB   A PRO   A 1 136 ? 11.592 -5.925  -2.873  0.30 16.40 ?  136  PRO   A CB   1 
ATOM   3011 C  CB   B PRO   A 1 136 ? 11.703 -5.838  -2.888  0.70 17.63 ?  136  PRO   A CB   1 
ATOM   3012 C  CG   A PRO   A 1 136 ? 10.543 -5.447  -3.822  0.30 16.84 ?  136  PRO   A CG   1 
ATOM   3013 C  CG   B PRO   A 1 136 ? 10.737 -5.179  -3.828  0.70 18.45 ?  136  PRO   A CG   1 
ATOM   3014 C  CD   A PRO   A 1 136 ? 11.164 -5.494  -5.186  0.30 16.52 ?  136  PRO   A CD   1 
ATOM   3015 C  CD   B PRO   A 1 136 ? 11.368 -5.199  -5.167  0.70 17.51 ?  136  PRO   A CD   1 
ATOM   3016 H  HA   A PRO   A 1 136 ? 13.331 -6.877  -3.451  0.30 19.00 ?  136  PRO   A HA   1 
ATOM   3017 H  HA   B PRO   A 1 136 ? 13.407 -6.804  -3.535  0.70 19.94 ?  136  PRO   A HA   1 
ATOM   3018 H  HB2  A PRO   A 1 136 ? 11.190 -6.341  -2.094  0.30 19.70 ?  136  PRO   A HB2  1 
ATOM   3019 H  HB2  B PRO   A 1 136 ? 11.230 -6.294  -2.174  0.70 21.18 ?  136  PRO   A HB2  1 
ATOM   3020 H  HB3  A PRO   A 1 136 ? 12.178 -5.197  -2.610  0.30 19.70 ?  136  PRO   A HB3  1 
ATOM   3021 H  HB3  B PRO   A 1 136 ? 12.328 -5.191  -2.527  0.70 21.18 ?  136  PRO   A HB3  1 
ATOM   3022 H  HG2  A PRO   A 1 136 ? 9.776  -6.037  -3.779  0.30 20.23 ?  136  PRO   A HG2  1 
ATOM   3023 H  HG2  B PRO   A 1 136 ? 9.909  -5.681  -3.844  0.70 22.16 ?  136  PRO   A HG2  1 
ATOM   3024 H  HG3  A PRO   A 1 136 ? 10.293 -4.539  -3.597  0.30 20.23 ?  136  PRO   A HG3  1 
ATOM   3025 H  HG3  B PRO   A 1 136 ? 10.582 -4.269  -3.547  0.70 22.16 ?  136  PRO   A HG3  1 
ATOM   3026 H  HD2  A PRO   A 1 136 ? 10.497 -5.720  -5.854  0.30 19.85 ?  136  PRO   A HD2  1 
ATOM   3027 H  HD2  B PRO   A 1 136 ? 10.691 -5.295  -5.857  0.70 21.04 ?  136  PRO   A HD2  1 
ATOM   3028 H  HD3  A PRO   A 1 136 ? 11.605 -4.655  -5.392  0.30 19.85 ?  136  PRO   A HD3  1 
ATOM   3029 H  HD3  B PRO   A 1 136 ? 11.910 -4.408  -5.306  0.70 21.04 ?  136  PRO   A HD3  1 
ATOM   3030 N  N    A ILE   A 1 137 ? 10.928 -8.907  -4.028  0.30 15.17 ?  137  ILE   A N    1 
ATOM   3031 N  N    B ILE   A 1 137 ? 10.963 -8.778  -4.154  0.70 16.35 ?  137  ILE   A N    1 
ATOM   3032 C  CA   A ILE   A 1 137 ? 10.561 -10.309 -3.846  0.30 14.99 ?  137  ILE   A CA   1 
ATOM   3033 C  CA   B ILE   A 1 137 ? 10.548 -10.169 -3.971  0.70 16.39 ?  137  ILE   A CA   1 
ATOM   3034 C  C    A ILE   A 1 137 ? 11.716 -11.210 -4.262  0.30 14.58 ?  137  ILE   A C    1 
ATOM   3035 C  C    B ILE   A 1 137 ? 11.690 -11.113 -4.331  0.70 15.85 ?  137  ILE   A C    1 
ATOM   3036 O  O    A ILE   A 1 137 ? 12.052 -12.180 -3.569  0.30 14.08 ?  137  ILE   A O    1 
ATOM   3037 O  O    B ILE   A 1 137 ? 11.983 -12.077 -3.610  0.70 15.48 ?  137  ILE   A O    1 
ATOM   3038 C  CB   A ILE   A 1 137 ? 9.267  -10.633 -4.616  0.30 15.74 ?  137  ILE   A CB   1 
ATOM   3039 C  CB   B ILE   A 1 137 ? 9.284  -10.466 -4.795  0.70 18.34 ?  137  ILE   A CB   1 
ATOM   3040 C  CG1  A ILE   A 1 137 ? 8.086  -9.834  -4.052  0.30 16.55 ?  137  ILE   A CG1  1 
ATOM   3041 C  CG1  B ILE   A 1 137 ? 8.150  -9.505  -4.413  0.70 20.08 ?  137  ILE   A CG1  1 
ATOM   3042 C  CG2  A ILE   A 1 137 ? 8.971  -12.131 -4.569  0.30 16.12 ?  137  ILE   A CG2  1 
ATOM   3043 C  CG2  B ILE   A 1 137 ? 8.865  -11.915 -4.599  0.70 19.05 ?  137  ILE   A CG2  1 
ATOM   3044 C  CD1  A ILE   A 1 137 ? 6.789  -10.044 -4.806  0.30 17.04 ?  137  ILE   A CD1  1 
ATOM   3045 C  CD1  B ILE   A 1 137 ? 6.935  -9.600  -5.306  0.70 21.56 ?  137  ILE   A CD1  1 
ATOM   3046 H  H    A ILE   A 1 137 ? 10.443 -8.480  -4.592  0.30 18.23 ?  137  ILE   A H    1 
ATOM   3047 H  H    B ILE   A 1 137 ? 10.491 -8.329  -4.714  0.70 19.64 ?  137  ILE   A H    1 
ATOM   3048 H  HA   A ILE   A 1 137 ? 10.392 -10.472 -2.907  0.30 18.02 ?  137  ILE   A HA   1 
ATOM   3049 H  HA   B ILE   A 1 137 ? 10.333 -10.311 -3.038  0.70 19.70 ?  137  ILE   A HA   1 
ATOM   3050 H  HB   A ILE   A 1 137 ? 9.386  -10.375 -5.541  0.30 18.91 ?  137  ILE   A HB   1 
ATOM   3051 H  HB   B ILE   A 1 137 ? 9.494  -10.334 -5.732  0.70 22.03 ?  137  ILE   A HB   1 
ATOM   3052 H  HG12 A ILE   A 1 137 ? 7.938  -10.094 -3.129  0.30 19.89 ?  137  ILE   A HG12 1 
ATOM   3053 H  HG12 B ILE   A 1 137 ? 7.873  -9.701  -3.506  0.70 24.13 ?  137  ILE   A HG12 1 
ATOM   3054 H  HG13 A ILE   A 1 137 ? 8.300  -8.885  -4.093  0.30 19.89 ?  137  ILE   A HG13 1 
ATOM   3055 H  HG13 B ILE   A 1 137 ? 8.479  -8.593  -4.464  0.70 24.13 ?  137  ILE   A HG13 1 
ATOM   3056 H  HG21 A ILE   A 1 137 ? 8.196  -12.323 -5.118  0.30 19.37 ?  137  ILE   A HG21 1 
ATOM   3057 H  HG21 B ILE   A 1 137 ? 8.006  -12.058 -5.027  0.70 22.89 ?  137  ILE   A HG21 1 
ATOM   3058 H  HG22 A ILE   A 1 137 ? 9.726  -12.622 -4.916  0.30 19.37 ?  137  ILE   A HG22 1 
ATOM   3059 H  HG22 B ILE   A 1 137 ? 9.529  -12.496 -4.999  0.70 22.89 ?  137  ILE   A HG22 1 
ATOM   3060 H  HG23 A ILE   A 1 137 ? 8.798  -12.387 -3.651  0.30 19.37 ?  137  ILE   A HG23 1 
ATOM   3061 H  HG23 B ILE   A 1 137 ? 8.792  -12.096 -3.649  0.70 22.89 ?  137  ILE   A HG23 1 
ATOM   3062 H  HD11 A ILE   A 1 137 ? 6.074  -9.676  -4.274  0.30 20.48 ?  137  ILE   A HD11 1 
ATOM   3063 H  HD11 B ILE   A 1 137 ? 6.352  -8.847  -5.125  0.70 25.90 ?  137  ILE   A HD11 1 
ATOM   3064 H  HD12 A ILE   A 1 137 ? 6.843  -9.589  -5.663  0.30 20.48 ?  137  ILE   A HD12 1 
ATOM   3065 H  HD12 B ILE   A 1 137 ? 7.221  -9.583  -6.233  0.70 25.90 ?  137  ILE   A HD12 1 
ATOM   3066 H  HD13 A ILE   A 1 137 ? 6.631  -10.989 -4.942  0.30 20.48 ?  137  ILE   A HD13 1 
ATOM   3067 H  HD13 B ILE   A 1 137 ? 6.470  -10.431 -5.120  0.70 25.90 ?  137  ILE   A HD13 1 
ATOM   3068 N  N    A HIS   A 1 138 ? 12.338 -10.908 -5.404  0.30 14.63 ?  138  HIS   A N    1 
ATOM   3069 N  N    B HIS   A 1 138 ? 12.345 -10.853 -5.464  0.70 15.61 ?  138  HIS   A N    1 
ATOM   3070 C  CA   A HIS   A 1 138 ? 13.503 -11.673 -5.833  0.30 14.68 ?  138  HIS   A CA   1 
ATOM   3071 C  CA   B HIS   A 1 138 ? 13.505 -11.647 -5.854  0.70 15.41 ?  138  HIS   A CA   1 
ATOM   3072 C  C    A HIS   A 1 138 ? 14.659 -11.508 -4.855  0.30 14.00 ?  138  HIS   A C    1 
ATOM   3073 C  C    B HIS   A 1 138 ? 14.637 -11.507 -4.843  0.70 14.21 ?  138  HIS   A C    1 
ATOM   3074 O  O    A HIS   A 1 138 ? 15.353 -12.481 -4.531  0.30 14.17 ?  138  HIS   A O    1 
ATOM   3075 O  O    B HIS   A 1 138 ? 15.290 -12.495 -4.484  0.70 14.57 ?  138  HIS   A O    1 
ATOM   3076 C  CB   A HIS   A 1 138 ? 13.920 -11.246 -7.241  0.30 15.38 ?  138  HIS   A CB   1 
ATOM   3077 C  CB   B HIS   A 1 138 ? 13.958 -11.223 -7.250  0.70 16.37 ?  138  HIS   A CB   1 
ATOM   3078 C  CG   A HIS   A 1 138 ? 15.207 -11.859 -7.698  0.30 15.98 ?  138  HIS   A CG   1 
ATOM   3079 C  CG   B HIS   A 1 138 ? 15.229 -11.873 -7.697  0.70 17.30 ?  138  HIS   A CG   1 
ATOM   3080 N  ND1  A HIS   A 1 138 ? 15.343 -13.208 -7.946  0.30 16.51 ?  138  HIS   A ND1  1 
ATOM   3081 N  ND1  B HIS   A 1 138 ? 15.319 -13.220 -7.980  0.70 18.24 ?  138  HIS   A ND1  1 
ATOM   3082 C  CD2  A HIS   A 1 138 ? 16.418 -11.307 -7.946  0.30 16.12 ?  138  HIS   A CD2  1 
ATOM   3083 C  CD2  B HIS   A 1 138 ? 16.462 -11.359 -7.914  0.70 17.46 ?  138  HIS   A CD2  1 
ATOM   3084 C  CE1  A HIS   A 1 138 ? 16.582 -13.460 -8.330  0.30 16.61 ?  138  HIS   A CE1  1 
ATOM   3085 C  CE1  B HIS   A 1 138 ? 16.554 -13.507 -8.350  0.70 18.39 ?  138  HIS   A CE1  1 
ATOM   3086 N  NE2  A HIS   A 1 138 ? 17.254 -12.323 -8.338  0.30 16.44 ?  138  HIS   A NE2  1 
ATOM   3087 N  NE2  B HIS   A 1 138 ? 17.267 -12.396 -8.317  0.70 17.93 ?  138  HIS   A NE2  1 
ATOM   3088 H  H    A HIS   A 1 138 ? 12.108 -10.271 -5.939  0.30 17.58 ?  138  HIS   A H    1 
ATOM   3089 H  H    B HIS   A 1 138 ? 12.138 -10.224 -6.020  0.70 18.75 ?  138  HIS   A H    1 
ATOM   3090 H  HA   A HIS   A 1 138 ? 13.269 -12.612 -5.867  0.30 17.64 ?  138  HIS   A HA   1 
ATOM   3091 H  HA   B HIS   A 1 138 ? 13.248 -12.579 -5.893  0.70 18.52 ?  138  HIS   A HA   1 
ATOM   3092 H  HB2  A HIS   A 1 138 ? 13.225 -11.507 -7.869  0.30 18.48 ?  138  HIS   A HB2  1 
ATOM   3093 H  HB2  B HIS   A 1 138 ? 13.263 -11.458 -7.890  0.70 19.66 ?  138  HIS   A HB2  1 
ATOM   3094 H  HB3  A HIS   A 1 138 ? 14.031 -10.283 -7.257  0.30 18.48 ?  138  HIS   A HB3  1 
ATOM   3095 H  HB3  B HIS   A 1 138 ? 14.097 -10.263 -7.260  0.70 19.66 ?  138  HIS   A HB3  1 
ATOM   3096 H  HD2  A HIS   A 1 138 ? 16.640 -10.408 -7.866  0.30 19.37 ?  138  HIS   A HD2  1 
ATOM   3097 H  HD2  B HIS   A 1 138 ? 16.714 -10.471 -7.807  0.70 20.97 ?  138  HIS   A HD2  1 
ATOM   3098 H  HE1  A HIS   A 1 138 ? 16.922 -14.295 -8.557  0.30 19.96 ?  138  HIS   A HE1  1 
ATOM   3099 H  HE1  B HIS   A 1 138 ? 16.868 -14.347 -8.593  0.70 22.10 ?  138  HIS   A HE1  1 
ATOM   3100 H  HE2  A HIS   A 1 138 ? 18.082 -12.233 -8.553  0.30 19.75 ?  138  HIS   A HE2  1 
ATOM   3101 H  HE2  B HIS   A 1 138 ? 18.100 -12.330 -8.517  0.70 21.55 ?  138  HIS   A HE2  1 
ATOM   3102 N  N    . SER   A 1 139 ? 14.885 -10.285 -4.370  1.00 13.43 ?  139  SER   A N    1 
ATOM   3103 C  CA   . SER   A 1 139 ? 15.967 -10.070 -3.419  1.00 12.90 ?  139  SER   A CA   1 
ATOM   3104 C  C    . SER   A 1 139 ? 15.764 -10.896 -2.154  1.00 12.61 ?  139  SER   A C    1 
ATOM   3105 O  O    . SER   A 1 139 ? 16.720 -11.479 -1.627  1.00 12.56 ?  139  SER   A O    1 
ATOM   3106 C  CB   . SER   A 1 139 ? 16.095 -8.585  -3.088  1.00 13.28 ?  139  SER   A CB   1 
ATOM   3107 O  OG   . SER   A 1 139 ? 17.183 -8.401  -2.210  1.00 13.46 ?  139  SER   A OG   1 
ATOM   3108 H  H    A SER   A 1 139 ? 14.435 -9.579  -4.573  0.30 16.14 ?  139  SER   A H    1 
ATOM   3109 H  H    B SER   A 1 139 ? 14.444 -9.575  -4.580  0.70 16.14 ?  139  SER   A H    1 
ATOM   3110 H  HA   . SER   A 1 139 ? 16.801 -10.349 -3.825  1.00 15.50 ?  139  SER   A HA   1 
ATOM   3111 H  HB2  . SER   A 1 139 ? 16.250 -8.079  -3.903  1.00 15.96 ?  139  SER   A HB2  1 
ATOM   3112 H  HB3  . SER   A 1 139 ? 15.281 -8.277  -2.654  1.00 15.96 ?  139  SER   A HB3  1 
ATOM   3113 H  HG   . SER   A 1 139 ? 17.272 -7.586  -2.017  1.00 16.18 ?  139  SER   A HG   1 
ATOM   3114 N  N    A LEU   A 1 140 ? 14.533 -10.941 -1.639  0.30 12.31 ?  140  LEU   A N    1 
ATOM   3115 N  N    B LEU   A 1 140 ? 14.523 -10.975 -1.663  0.70 12.53 ?  140  LEU   A N    1 
ATOM   3116 C  CA   A LEU   A 1 140 ? 14.263 -11.780 -0.477  0.30 12.00 ?  140  LEU   A CA   1 
ATOM   3117 C  CA   B LEU   A 1 140 ? 14.256 -11.772 -0.471  0.70 11.99 ?  140  LEU   A CA   1 
ATOM   3118 C  C    A LEU   A 1 140 ? 14.520 -13.247 -0.798  0.30 11.85 ?  140  LEU   A C    1 
ATOM   3119 C  C    B LEU   A 1 140 ? 14.547 -13.249 -0.718  0.70 11.74 ?  140  LEU   A C    1 
ATOM   3120 O  O    A LEU   A 1 140 ? 15.077 -13.985 0.026   0.30 12.01 ?  140  LEU   A O    1 
ATOM   3121 O  O    B LEU   A 1 140 ? 15.119 -13.932 0.143   0.70 12.43 ?  140  LEU   A O    1 
ATOM   3122 C  CB   A LEU   A 1 140 ? 12.825 -11.574 0.000   0.30 12.29 ?  140  LEU   A CB   1 
ATOM   3123 C  CB   B LEU   A 1 140 ? 12.811 -11.573 -0.014  0.70 12.60 ?  140  LEU   A CB   1 
ATOM   3124 C  CG   A LEU   A 1 140 ? 12.384 -12.489 1.145   0.30 12.64 ?  140  LEU   A CG   1 
ATOM   3125 C  CG   B LEU   A 1 140 ? 12.385 -12.417 1.190   0.70 13.14 ?  140  LEU   A CG   1 
ATOM   3126 C  CD1  A LEU   A 1 140 ? 13.292 -12.325 2.353   0.30 12.90 ?  140  LEU   A CD1  1 
ATOM   3127 C  CD1  B LEU   A 1 140 ? 13.278 -12.147 2.389   0.70 13.45 ?  140  LEU   A CD1  1 
ATOM   3128 C  CD2  A LEU   A 1 140 ? 10.933 -12.221 1.524   0.30 13.17 ?  140  LEU   A CD2  1 
ATOM   3129 C  CD2  B LEU   A 1 140 ? 10.925 -12.146 1.547   0.70 14.17 ?  140  LEU   A CD2  1 
ATOM   3130 H  H    A LEU   A 1 140 ? 13.855 -10.504 -1.938  0.30 14.80 ?  140  LEU   A H    1 
ATOM   3131 H  H    B LEU   A 1 140 ? 13.835 -10.580 -1.997  0.70 15.06 ?  140  LEU   A H    1 
ATOM   3132 H  HA   A LEU   A 1 140 ? 14.858 -11.522 0.242   0.30 14.43 ?  140  LEU   A HA   1 
ATOM   3133 H  HA   B LEU   A 1 140 ? 14.836 -11.471 0.242   0.70 14.42 ?  140  LEU   A HA   1 
ATOM   3134 H  HB2  A LEU   A 1 140 ? 12.729 -10.659 0.308   0.30 14.77 ?  140  LEU   A HB2  1 
ATOM   3135 H  HB2  B LEU   A 1 140 ? 12.686 -10.646 0.229   0.70 15.15 ?  140  LEU   A HB2  1 
ATOM   3136 H  HB3  A LEU   A 1 140 ? 12.225 -11.731 -0.745  0.30 14.77 ?  140  LEU   A HB3  1 
ATOM   3137 H  HB3  B LEU   A 1 140 ? 12.219 -11.803 -0.748  0.70 15.15 ?  140  LEU   A HB3  1 
ATOM   3138 H  HG   A LEU   A 1 140 ? 12.442 -13.413 0.853   0.30 15.19 ?  140  LEU   A HG   1 
ATOM   3139 H  HG   B LEU   A 1 140 ? 12.459 -13.361 0.967   0.70 15.79 ?  140  LEU   A HG   1 
ATOM   3140 H  HD11 A LEU   A 1 140 ? 12.918 -12.822 3.097   0.30 15.50 ?  140  LEU   A HD11 1 
ATOM   3141 H  HD11 B LEU   A 1 140 ? 12.907 -12.598 3.164   0.70 16.16 ?  140  LEU   A HD11 1 
ATOM   3142 H  HD12 A LEU   A 1 140 ? 14.172 -12.671 2.135   0.30 15.50 ?  140  LEU   A HD12 1 
ATOM   3143 H  HD12 B LEU   A 1 140 ? 14.165 -12.490 2.201   0.70 16.16 ?  140  LEU   A HD12 1 
ATOM   3144 H  HD13 A LEU   A 1 140 ? 13.350 -11.384 2.578   0.30 15.50 ?  140  LEU   A HD13 1 
ATOM   3145 H  HD13 B LEU   A 1 140 ? 13.312 -11.193 2.543   0.70 16.16 ?  140  LEU   A HD13 1 
ATOM   3146 H  HD21 A LEU   A 1 140 ? 10.681 -12.817 2.249   0.30 15.82 ?  140  LEU   A HD21 1 
ATOM   3147 H  HD21 B LEU   A 1 140 ? 10.673 -12.705 2.303   0.70 17.02 ?  140  LEU   A HD21 1 
ATOM   3148 H  HD22 A LEU   A 1 140 ? 10.846 -11.299 1.810   0.30 15.82 ?  140  LEU   A HD22 1 
ATOM   3149 H  HD22 B LEU   A 1 140 ? 10.826 -11.212 1.782   0.70 17.02 ?  140  LEU   A HD22 1 
ATOM   3150 H  HD23 A LEU   A 1 140 ? 10.369 -12.384 0.752   0.30 15.82 ?  140  LEU   A HD23 1 
ATOM   3151 H  HD23 B LEU   A 1 140 ? 10.366 -12.358 0.783   0.70 17.02 ?  140  LEU   A HD23 1 
ATOM   3152 N  N    A ARG   A 1 141 ? 14.124 -13.688 -1.994  0.30 12.12 ?  141  ARG   A N    1 
ATOM   3153 N  N    B ARG   A 1 141 ? 14.158 -13.765 -1.889  0.70 12.48 ?  141  ARG   A N    1 
ATOM   3154 C  CA   A ARG   A 1 141 ? 14.361 -15.071 -2.395  0.30 12.60 ?  141  ARG   A CA   1 
ATOM   3155 C  CA   B ARG   A 1 141 ? 14.411 -15.173 -2.183  0.70 13.59 ?  141  ARG   A CA   1 
ATOM   3156 C  C    A ARG   A 1 141 ? 15.850 -15.400 -2.371  0.30 12.15 ?  141  ARG   A C    1 
ATOM   3157 C  C    B ARG   A 1 141 ? 15.907 -15.455 -2.240  0.70 12.79 ?  141  ARG   A C    1 
ATOM   3158 O  O    A ARG   A 1 141 ? 16.259 -16.435 -1.834  0.30 11.96 ?  141  ARG   A O    1 
ATOM   3159 O  O    B ARG   A 1 141 ? 16.382 -16.440 -1.664  0.70 12.84 ?  141  ARG   A O    1 
ATOM   3160 C  CB   A ARG   A 1 141 ? 13.774 -15.311 -3.786  0.30 13.49 ?  141  ARG   A CB   1 
ATOM   3161 C  CB   B ARG   A 1 141 ? 13.721 -15.586 -3.484  0.70 14.91 ?  141  ARG   A CB   1 
ATOM   3162 C  CG   A ARG   A 1 141 ? 13.756 -16.769 -4.221  0.30 14.53 ?  141  ARG   A CG   1 
ATOM   3163 C  CG   B ARG   A 1 141 ? 13.857 -17.078 -3.807  0.70 16.42 ?  141  ARG   A CG   1 
ATOM   3164 C  CD   A ARG   A 1 141 ? 12.736 -17.569 -3.431  0.30 14.72 ?  141  ARG   A CD   1 
ATOM   3165 C  CD   B ARG   A 1 141 ? 13.238 -17.962 -2.729  0.70 17.13 ?  141  ARG   A CD   1 
ATOM   3166 N  NE   A ARG   A 1 141 ? 13.351 -18.384 -2.390  0.30 15.01 ?  141  ARG   A NE   1 
ATOM   3167 N  NE   B ARG   A 1 141 ? 11.819 -17.680 -2.555  0.70 17.85 ?  141  ARG   A NE   1 
ATOM   3168 C  CZ   A ARG   A 1 141 ? 12.673 -18.973 -1.414  0.30 15.39 ?  141  ARG   A CZ   1 
ATOM   3169 C  CZ   B ARG   A 1 141 ? 11.055 -18.203 -1.606  0.70 18.26 ?  141  ARG   A CZ   1 
ATOM   3170 N  NH1  A ARG   A 1 141 ? 11.366 -18.813 -1.286  0.30 16.00 ?  141  ARG   A NH1  1 
ATOM   3171 N  NH1  B ARG   A 1 141 ? 11.541 -19.052 -0.715  0.70 18.63 ?  141  ARG   A NH1  1 
ATOM   3172 N  NH2  A ARG   A 1 141 ? 13.322 -19.738 -0.542  0.30 15.52 ?  141  ARG   A NH2  1 
ATOM   3173 N  NH2  B ARG   A 1 141 ? 9.770  -17.861 -1.547  0.70 18.68 ?  141  ARG   A NH2  1 
ATOM   3174 H  H    A ARG   A 1 141 ? 13.717 -13.210 -2.583  0.30 14.56 ?  141  ARG   A H    1 
ATOM   3175 H  H    B ARG   A 1 141 ? 13.758 -13.332 -2.515  0.70 15.00 ?  141  ARG   A H    1 
ATOM   3176 H  HA   A ARG   A 1 141 ? 13.914 -15.661 -1.770  0.30 15.14 ?  141  ARG   A HA   1 
ATOM   3177 H  HA   B ARG   A 1 141 ? 14.045 -15.706 -1.466  0.70 16.33 ?  141  ARG   A HA   1 
ATOM   3178 H  HB2  A ARG   A 1 141 ? 12.860 -14.989 -3.797  0.30 16.21 ?  141  ARG   A HB2  1 
ATOM   3179 H  HB2  B ARG   A 1 141 ? 12.776 -15.384 -3.413  0.70 17.91 ?  141  ARG   A HB2  1 
ATOM   3180 H  HB3  A ARG   A 1 141 ? 14.301 -14.821 -4.433  0.30 16.21 ?  141  ARG   A HB3  1 
ATOM   3181 H  HB3  B ARG   A 1 141 ? 14.111 -15.087 -4.220  0.70 17.91 ?  141  ARG   A HB3  1 
ATOM   3182 H  HG2  A ARG   A 1 141 ? 13.522 -16.822 -5.160  0.30 17.46 ?  141  ARG   A HG2  1 
ATOM   3183 H  HG2  B ARG   A 1 141 ? 13.406 -17.263 -4.646  0.70 19.73 ?  141  ARG   A HG2  1 
ATOM   3184 H  HG3  A ARG   A 1 141 ? 14.632 -17.163 -4.072  0.30 17.46 ?  141  ARG   A HG3  1 
ATOM   3185 H  HG3  B ARG   A 1 141 ? 14.800 -17.306 -3.883  0.70 19.73 ?  141  ARG   A HG3  1 
ATOM   3186 H  HD2  A ARG   A 1 141 ? 12.118 -16.959 -3.000  0.30 17.68 ?  141  ARG   A HD2  1 
ATOM   3187 H  HD2  B ARG   A 1 141 ? 13.332 -18.890 -2.989  0.70 20.58 ?  141  ARG   A HD2  1 
ATOM   3188 H  HD3  A ARG   A 1 141 ? 12.256 -18.156 -4.036  0.30 17.68 ?  141  ARG   A HD3  1 
ATOM   3189 H  HD3  B ARG   A 1 141 ? 13.685 -17.806 -1.883  0.70 20.58 ?  141  ARG   A HD3  1 
ATOM   3190 H  HE   A ARG   A 1 141 ? 14.186 -18.577 -2.470  0.30 18.03 ?  141  ARG   A HE   1 
ATOM   3191 H  HE   B ARG   A 1 141 ? 11.446 -17.143 -3.115  0.70 21.45 ?  141  ARG   A HE   1 
ATOM   3192 H  HH11 A ARG   A 1 141 ? 10.933 -18.329 -1.848  0.30 19.22 ?  141  ARG   A HH11 1 
ATOM   3193 H  HH11 B ARG   A 1 141 ? 12.366 -19.286 -0.748  0.70 22.38 ?  141  ARG   A HH11 1 
ATOM   3194 H  HH12 A ARG   A 1 141 ? 10.948 -19.204 -0.644  0.30 19.22 ?  141  ARG   A HH12 1 
ATOM   3195 H  HH12 B ARG   A 1 141 ? 11.024 -19.385 -0.113  0.70 22.38 ?  141  ARG   A HH12 1 
ATOM   3196 H  HH21 A ARG   A 1 141 ? 14.174 -19.846 -0.614  0.30 18.65 ?  141  ARG   A HH21 1 
ATOM   3197 H  HH21 B ARG   A 1 141 ? 9.444  -17.312 -2.123  0.70 22.44 ?  141  ARG   A HH21 1 
ATOM   3198 H  HH22 A ARG   A 1 141 ? 12.896 -20.118 0.101   0.30 18.65 ?  141  ARG   A HH22 1 
ATOM   3199 H  HH22 B ARG   A 1 141 ? 9.262  -18.197 -0.939  0.70 22.44 ?  141  ARG   A HH22 1 
ATOM   3200 N  N    A VAL   A 1 142 ? 16.678 -14.526 -2.950  0.30 11.94 ?  142  VAL   A N    1 
ATOM   3201 N  N    B VAL   A 1 142 ? 16.670 -14.596 -2.924  0.70 12.49 ?  142  VAL   A N    1 
ATOM   3202 C  CA   A VAL   A 1 142 ? 18.117 -14.780 -2.968  0.30 11.64 ?  142  VAL   A CA   1 
ATOM   3203 C  CA   B VAL   A 1 142 ? 18.121 -14.772 -2.962  0.70 12.34 ?  142  VAL   A CA   1 
ATOM   3204 C  C    A VAL   A 1 142 ? 18.689 -14.744 -1.556  0.30 11.48 ?  142  VAL   A C    1 
ATOM   3205 C  C    B VAL   A 1 142 ? 18.690 -14.744 -1.553  0.70 11.91 ?  142  VAL   A C    1 
ATOM   3206 O  O    A VAL   A 1 142 ? 19.554 -15.554 -1.204  0.30 11.50 ?  142  VAL   A O    1 
ATOM   3207 O  O    B VAL   A 1 142 ? 19.554 -15.555 -1.200  0.70 12.21 ?  142  VAL   A O    1 
ATOM   3208 C  CB   A VAL   A 1 142 ? 18.839 -13.805 -3.919  0.30 11.61 ?  142  VAL   A CB   1 
ATOM   3209 C  CB   B VAL   A 1 142 ? 18.791 -13.724 -3.875  0.70 12.71 ?  142  VAL   A CB   1 
ATOM   3210 C  CG1  A VAL   A 1 142 ? 20.345 -14.029 -3.870  0.30 11.58 ?  142  VAL   A CG1  1 
ATOM   3211 C  CG1  B VAL   A 1 142 ? 20.302 -13.926 -3.887  0.70 12.68 ?  142  VAL   A CG1  1 
ATOM   3212 C  CG2  A VAL   A 1 142 ? 18.333 -13.976 -5.343  0.30 12.34 ?  142  VAL   A CG2  1 
ATOM   3213 C  CG2  B VAL   A 1 142 ? 18.252 -13.816 -5.288  0.70 14.36 ?  142  VAL   A CG2  1 
ATOM   3214 H  H    A VAL   A 1 142 ? 16.437 -13.795 -3.336  0.30 14.36 ?  142  VAL   A H    1 
ATOM   3215 H  H    B VAL   A 1 142 ? 16.384 -13.913 -3.363  0.70 15.01 ?  142  VAL   A H    1 
ATOM   3216 H  HA   A VAL   A 1 142 ? 18.263 -15.672 -3.316  0.30 13.99 ?  142  VAL   A HA   1 
ATOM   3217 H  HA   B VAL   A 1 142 ? 18.321 -15.641 -3.340  0.70 14.83 ?  142  VAL   A HA   1 
ATOM   3218 H  HB   A VAL   A 1 142 ? 18.663 -12.891 -3.642  0.30 13.96 ?  142  VAL   A HB   1 
ATOM   3219 H  HB   B VAL   A 1 142 ? 18.613 -12.830 -3.536  0.70 15.28 ?  142  VAL   A HB   1 
ATOM   3220 H  HG11 A VAL   A 1 142 ? 20.759 -13.564 -4.616  0.30 13.92 ?  142  VAL   A HG11 1 
ATOM   3221 H  HG11 B VAL   A 1 142 ? 20.688 -13.402 -4.608  0.70 15.24 ?  142  VAL   A HG11 1 
ATOM   3222 H  HG12 A VAL   A 1 142 ? 20.694 -13.682 -3.034  0.30 13.92 ?  142  VAL   A HG12 1 
ATOM   3223 H  HG12 B VAL   A 1 142 ? 20.672 -13.636 -3.038  0.70 15.24 ?  142  VAL   A HG12 1 
ATOM   3224 H  HG13 A VAL   A 1 142 ? 20.525 -14.980 -3.937  0.30 13.92 ?  142  VAL   A HG13 1 
ATOM   3225 H  HG13 B VAL   A 1 142 ? 20.492 -14.867 -4.027  0.70 15.24 ?  142  VAL   A HG13 1 
ATOM   3226 H  HG21 A VAL   A 1 142 ? 18.822 -13.375 -5.928  0.30 14.83 ?  142  VAL   A HG21 1 
ATOM   3227 H  HG21 B VAL   A 1 142 ? 18.712 -13.167 -5.845  0.70 17.26 ?  142  VAL   A HG21 1 
ATOM   3228 H  HG22 A VAL   A 1 142 ? 18.477 -14.895 -5.619  0.30 14.83 ?  142  VAL   A HG22 1 
ATOM   3229 H  HG22 B VAL   A 1 142 ? 18.412 -14.711 -5.624  0.70 17.26 ?  142  VAL   A HG22 1 
ATOM   3230 H  HG23 A VAL   A 1 142 ? 17.387 -13.766 -5.368  0.30 14.83 ?  142  VAL   A HG23 1 
ATOM   3231 H  HG23 B VAL   A 1 142 ? 17.304 -13.628 -5.275  0.70 17.26 ?  142  VAL   A HG23 1 
ATOM   3232 N  N    . CYS   A 1 143 ? 18.228 -13.804 -0.727  1.00 11.45 ?  143  CYS   A N    1 
ATOM   3233 C  CA   . CYS   A 1 143 ? 18.684 -13.745 0.659   1.00 11.61 ?  143  CYS   A CA   1 
ATOM   3234 C  C    . CYS   A 1 143 ? 18.460 -15.081 1.363   1.00 11.61 ?  143  CYS   A C    1 
ATOM   3235 O  O    . CYS   A 1 143 ? 19.380 -15.660 1.949   1.00 11.42 ?  143  CYS   A O    1 
ATOM   3236 C  CB   . CYS   A 1 143 ? 17.952 -12.620 1.389   1.00 12.36 ?  143  CYS   A CB   1 
ATOM   3237 S  SG   . CYS   A 1 143 ? 18.438 -12.429 3.119   1.00 12.60 ?  143  CYS   A SG   1 
ATOM   3238 H  H    A CYS   A 1 143 ? 17.657 -13.204 -0.941  0.30 13.76 ?  143  CYS   A H    1 
ATOM   3239 H  H    B CYS   A 1 143 ? 17.654 -13.207 -0.940  0.70 13.76 ?  143  CYS   A H    1 
ATOM   3240 H  HA   . CYS   A 1 143 ? 19.636 -13.557 0.674   1.00 13.96 ?  143  CYS   A HA   1 
ATOM   3241 H  HB2  . CYS   A 1 143 ? 18.128 -11.786 0.929   1.00 14.86 ?  143  CYS   A HB2  1 
ATOM   3242 H  HB3  . CYS   A 1 143 ? 17.003 -12.809 1.370   1.00 14.86 ?  143  CYS   A HB3  1 
ATOM   3243 H  HG   . CYS   A 1 143 ? 17.886 -11.467 3.573   1.00 15.15 ?  143  CYS   A HG   1 
ATOM   3244 N  N    . VAL   A 1 144 ? 17.229 -15.582 1.319   1.00 11.83 ?  144  VAL   A N    1 
ATOM   3245 C  CA   . VAL   A 1 144 ? 16.891 -16.815 2.019   1.00 12.95 ?  144  VAL   A CA   1 
ATOM   3246 C  C    . VAL   A 1 144 ? 17.714 -17.986 1.499   1.00 12.37 ?  144  VAL   A C    1 
ATOM   3247 O  O    . VAL   A 1 144 ? 18.086 -18.884 2.264   1.00 13.38 ?  144  VAL   A O    1 
ATOM   3248 C  CB   . VAL   A 1 144 ? 15.375 -17.059 1.893   1.00 15.71 ?  144  VAL   A CB   1 
ATOM   3249 C  CG1  . VAL   A 1 144 ? 15.014 -18.492 2.212   1.00 17.44 ?  144  VAL   A CG1  1 
ATOM   3250 C  CG2  . VAL   A 1 144 ? 14.623 -16.073 2.784   1.00 15.75 ?  144  VAL   A CG2  1 
ATOM   3251 H  H    . VAL   A 1 144 ? 16.573 -15.223 0.891   1.00 14.22 ?  144  VAL   A H    1 
ATOM   3252 H  HA   . VAL   A 1 144 ? 17.087 -16.710 2.958   1.00 15.56 ?  144  VAL   A HA   1 
ATOM   3253 H  HB   . VAL   A 1 144 ? 15.102 -16.885 0.975   1.00 18.87 ?  144  VAL   A HB   1 
ATOM   3254 H  HG11 . VAL   A 1 144 ? 14.058 -18.544 2.390   1.00 20.95 ?  144  VAL   A HG11 1 
ATOM   3255 H  HG12 . VAL   A 1 144 ? 15.235 -19.054 1.454   1.00 20.95 ?  144  VAL   A HG12 1 
ATOM   3256 H  HG13 . VAL   A 1 144 ? 15.507 -18.775 2.996   1.00 20.95 ?  144  VAL   A HG13 1 
ATOM   3257 H  HG21 . VAL   A 1 144 ? 13.667 -16.229 2.700   1.00 18.93 ?  144  VAL   A HG21 1 
ATOM   3258 H  HG22 . VAL   A 1 144 ? 14.898 -16.201 3.704   1.00 18.93 ?  144  VAL   A HG22 1 
ATOM   3259 H  HG23 . VAL   A 1 144 ? 14.831 -15.166 2.500   1.00 18.93 ?  144  VAL   A HG23 1 
ATOM   3260 N  N    . ASP   A 1 145 ? 17.984 -18.015 0.195   1.00 12.54 ?  145  ASP   A N    1 
ATOM   3261 C  CA   . ASP   A 1 145 ? 18.699 -19.121 -0.436  1.00 13.36 ?  145  ASP   A CA   1 
ATOM   3262 C  C    . ASP   A 1 145 ? 20.220 -18.968 -0.393  1.00 13.02 ?  145  ASP   A C    1 
ATOM   3263 O  O    . ASP   A 1 145 ? 20.930 -19.856 -0.880  1.00 15.18 ?  145  ASP   A O    1 
ATOM   3264 C  CB   . ASP   A 1 145 ? 18.253 -19.265 -1.893  1.00 14.59 ?  145  ASP   A CB   1 
ATOM   3265 C  CG   . ASP   A 1 145 ? 16.826 -19.764 -2.028  1.00 16.45 ?  145  ASP   A CG   1 
ATOM   3266 O  OD1  . ASP   A 1 145 ? 16.262 -20.295 -1.043  1.00 17.44 ?  145  ASP   A OD1  1 
ATOM   3267 O  OD2  . ASP   A 1 145 ? 16.278 -19.619 -3.137  1.00 18.36 -1 145  ASP   A OD2  1 
ATOM   3268 H  H    . ASP   A 1 145 ? 17.748 -17.395 -0.356  1.00 15.07 ?  145  ASP   A H    1 
ATOM   3269 H  HA   . ASP   A 1 145 ? 18.472 -19.938 0.025   1.00 16.05 ?  145  ASP   A HA   1 
ATOM   3270 H  HB2  . ASP   A 1 145 ? 18.313 -18.399 -2.331  1.00 17.53 ?  145  ASP   A HB2  1 
ATOM   3271 H  HB3  . ASP   A 1 145 ? 18.837 -19.899 -2.338  1.00 17.53 ?  145  ASP   A HB3  1 
ATOM   3272 N  N    . THR   A 1 146 ? 20.739 -17.880 0.175   1.00 11.57 ?  146  THR   A N    1 
ATOM   3273 C  CA   . THR   A 1 146 ? 22.175 -17.614 0.196   1.00 11.13 ?  146  THR   A CA   1 
ATOM   3274 C  C    . THR   A 1 146 ? 22.721 -17.427 1.601   1.00 11.09 ?  146  THR   A C    1 
ATOM   3275 O  O    . THR   A 1 146 ? 23.802 -17.951 1.917   1.00 12.15 ?  146  THR   A O    1 
ATOM   3276 C  CB   . THR   A 1 146 ? 22.482 -16.359 -0.646  1.00 11.32 ?  146  THR   A CB   1 
ATOM   3277 O  OG1  . THR   A 1 146 ? 21.963 -16.528 -1.966  1.00 11.89 ?  146  THR   A OG1  1 
ATOM   3278 C  CG2  . THR   A 1 146 ? 23.983 -16.105 -0.735  1.00 11.93 ?  146  THR   A CG2  1 
ATOM   3279 H  H    . THR   A 1 146 ? 20.272 -17.264 0.559   1.00 13.91 ?  146  THR   A H    1 
ATOM   3280 H  HA   . THR   A 1 146 ? 22.644 -18.355 -0.205  1.00 13.38 ?  146  THR   A HA   1 
ATOM   3281 H  HB   . THR   A 1 146 ? 22.070 -15.583 -0.232  1.00 13.61 ?  146  THR   A HB   1 
ATOM   3282 H  HG1  . THR   A 1 146 ? 21.128 -16.617 -1.930  1.00 14.30 ?  146  THR   A HG1  1 
ATOM   3283 H  HG21 . THR   A 1 146 ? 24.162 -15.424 -1.402  1.00 14.34 ?  146  THR   A HG21 1 
ATOM   3284 H  HG22 . THR   A 1 146 ? 24.321 -15.798 0.123   1.00 14.34 ?  146  THR   A HG22 1 
ATOM   3285 H  HG23 . THR   A 1 146 ? 24.442 -16.919 -0.983  1.00 14.34 ?  146  THR   A HG23 1 
ATOM   3286 N  N    . VAL   A 1 147 ? 22.043 -16.644 2.434   1.00 11.10 ?  147  VAL   A N    1 
ATOM   3287 C  CA   . VAL   A 1 147 ? 22.524 -16.345 3.776   1.00 10.86 ?  147  VAL   A CA   1 
ATOM   3288 C  C    . VAL   A 1 147 ? 22.203 -17.520 4.687   1.00 11.52 ?  147  VAL   A C    1 
ATOM   3289 O  O    . VAL   A 1 147 ? 21.060 -18.004 4.722   1.00 12.08 ?  147  VAL   A O    1 
ATOM   3290 C  CB   . VAL   A 1 147 ? 21.892 -15.044 4.295   1.00 11.34 ?  147  VAL   A CB   1 
ATOM   3291 C  CG1  . VAL   A 1 147 ? 22.417 -14.723 5.666   1.00 12.50 ?  147  VAL   A CG1  1 
ATOM   3292 C  CG2  . VAL   A 1 147 ? 22.134 -13.890 3.325   1.00 11.21 ?  147  VAL   A CG2  1 
ATOM   3293 H  H    . VAL   A 1 147 ? 21.287 -16.277 2.246   1.00 13.35 ?  147  VAL   A H    1 
ATOM   3294 H  HA   . VAL   A 1 147 ? 23.487 -16.227 3.751   1.00 13.05 ?  147  VAL   A HA   1 
ATOM   3295 H  HB   . VAL   A 1 147 ? 20.934 -15.172 4.372   1.00 13.63 ?  147  VAL   A HB   1 
ATOM   3296 H  HG11 . VAL   A 1 147 ? 22.149 -13.822 5.904   1.00 15.03 ?  147  VAL   A HG11 1 
ATOM   3297 H  HG12 . VAL   A 1 147 ? 22.045 -15.354 6.305   1.00 15.03 ?  147  VAL   A HG12 1 
ATOM   3298 H  HG13 . VAL   A 1 147 ? 23.384 -14.790 5.659   1.00 15.03 ?  147  VAL   A HG13 1 
ATOM   3299 H  HG21 . VAL   A 1 147 ? 21.786 -13.072 3.721   1.00 13.48 ?  147  VAL   A HG21 1 
ATOM   3300 H  HG22 . VAL   A 1 147 ? 23.080 -13.806 3.163   1.00 13.48 ?  147  VAL   A HG22 1 
ATOM   3301 H  HG23 . VAL   A 1 147 ? 21.664 -14.076 2.495   1.00 13.48 ?  147  VAL   A HG23 1 
ATOM   3302 N  N    . ARG   A 1 148 ? 23.225 -17.986 5.412   1.00 11.57 ?  148  ARG   A N    1 
ATOM   3303 C  CA   . ARG   A 1 148 ? 23.090 -19.066 6.376   1.00 11.76 ?  148  ARG   A CA   1 
ATOM   3304 C  C    . ARG   A 1 148 ? 23.224 -18.593 7.813   1.00 12.00 ?  148  ARG   A C    1 
ATOM   3305 O  O    . ARG   A 1 148 ? 22.812 -19.314 8.729   1.00 13.46 ?  148  ARG   A O    1 
ATOM   3306 C  CB   . ARG   A 1 148 ? 24.120 -20.173 6.096   1.00 12.68 ?  148  ARG   A CB   1 
ATOM   3307 C  CG   . ARG   A 1 148 ? 23.961 -20.793 4.725   1.00 13.60 ?  148  ARG   A CG   1 
ATOM   3308 C  CD   . ARG   A 1 148 ? 25.038 -21.838 4.420   1.00 14.48 ?  148  ARG   A CD   1 
ATOM   3309 N  NE   . ARG   A 1 148 ? 26.380 -21.268 4.427   1.00 14.55 ?  148  ARG   A NE   1 
ATOM   3310 C  CZ   . ARG   A 1 148 ? 26.882 -20.529 3.447   1.00 13.86 ?  148  ARG   A CZ   1 
ATOM   3311 N  NH1  . ARG   A 1 148 ? 26.193 -20.282 2.346   1.00 14.21 ?  148  ARG   A NH1  1 
ATOM   3312 N  NH2  . ARG   A 1 148 ? 28.105 -20.014 3.580   1.00 14.13 ?  148  ARG   A NH2  1 
ATOM   3313 H  H    . ARG   A 1 148 ? 24.030 -17.681 5.347   1.00 13.90 ?  148  ARG   A H    1 
ATOM   3314 H  HA   . ARG   A 1 148 ? 22.212 -19.456 6.280   1.00 14.13 ?  148  ARG   A HA   1 
ATOM   3315 H  HB2  . ARG   A 1 148 ? 25.012 -19.805 6.155   1.00 15.23 ?  148  ARG   A HB2  1 
ATOM   3316 H  HB3  . ARG   A 1 148 ? 24.007 -20.881 6.753   1.00 15.23 ?  148  ARG   A HB3  1 
ATOM   3317 H  HG2  . ARG   A 1 148 ? 23.093 -21.223 4.676   1.00 16.34 ?  148  ARG   A HG2  1 
ATOM   3318 H  HG3  . ARG   A 1 148 ? 24.022 -20.090 4.059   1.00 16.34 ?  148  ARG   A HG3  1 
ATOM   3319 H  HD2  . ARG   A 1 148 ? 25.002 -22.534 5.094   1.00 17.41 ?  148  ARG   A HD2  1 
ATOM   3320 H  HD3  . ARG   A 1 148 ? 24.869 -22.216 3.542   1.00 17.41 ?  148  ARG   A HD3  1 
ATOM   3321 H  HE   . ARG   A 1 148 ? 26.878 -21.421 5.107   1.00 17.48 ?  148  ARG   A HE   1 
ATOM   3322 H  HH11 . ARG   A 1 148 ? 25.401 -20.599 2.248   1.00 17.08 ?  148  ARG   A HH11 1 
ATOM   3323 H  HH12 . ARG   A 1 148 ? 26.538 -19.797 1.720   1.00 17.08 ?  148  ARG   A HH12 1 
ATOM   3324 H  HH21 . ARG   A 1 148 ? 28.565 -20.169 4.289   1.00 16.98 ?  148  ARG   A HH21 1 
ATOM   3325 H  HH22 . ARG   A 1 148 ? 28.446 -19.535 2.946   1.00 16.98 ?  148  ARG   A HH22 1 
ATOM   3326 N  N    . THR   A 1 149 ? 23.779 -17.407 8.027   1.00 11.99 ?  149  THR   A N    1 
ATOM   3327 C  CA   . THR   A 1 149 ? 23.856 -16.821 9.350   1.00 12.20 ?  149  THR   A CA   1 
ATOM   3328 C  C    . THR   A 1 149 ? 22.529 -16.129 9.661   1.00 11.52 ?  149  THR   A C    1 
ATOM   3329 O  O    . THR   A 1 149 ? 21.592 -16.130 8.851   1.00 12.38 ?  149  THR   A O    1 
ATOM   3330 C  CB   . THR   A 1 149 ? 25.055 -15.882 9.404   1.00 12.38 ?  149  THR   A CB   1 
ATOM   3331 O  OG1  . THR   A 1 149 ? 24.914 -14.941 8.337   1.00 12.71 ?  149  THR   A OG1  1 
ATOM   3332 C  CG2  . THR   A 1 149 ? 26.362 -16.671 9.250   1.00 13.46 ?  149  THR   A CG2  1 
ATOM   3333 H  H    . THR   A 1 149 ? 24.129 -16.917 7.412   1.00 14.41 ?  149  THR   A H    1 
ATOM   3334 H  HA   . THR   A 1 149 ? 23.993 -17.526 10.003  1.00 14.67 ?  149  THR   A HA   1 
ATOM   3335 H  HB   . THR   A 1 149 ? 25.063 -15.417 10.255  1.00 14.88 ?  149  THR   A HB   1 
ATOM   3336 H  HG1  . THR   A 1 149 ? 25.557 -14.402 8.339   1.00 15.27 ?  149  THR   A HG1  1 
ATOM   3337 H  HG21 . THR   A 1 149 ? 27.122 -16.071 9.314   1.00 16.18 ?  149  THR   A HG21 1 
ATOM   3338 H  HG22 . THR   A 1 149 ? 26.432 -17.342 9.948   1.00 16.18 ?  149  THR   A HG22 1 
ATOM   3339 H  HG23 . THR   A 1 149 ? 26.385 -17.115 8.386   1.00 16.18 ?  149  THR   A HG23 1 
ATOM   3340 N  N    . ASN   A 1 150 ? 22.409 -15.584 10.865  1.00 11.93 ?  150  ASN   A N    1 
ATOM   3341 C  CA   . ASN   A 1 150 ? 21.126 -15.077 11.349  1.00 12.57 ?  150  ASN   A CA   1 
ATOM   3342 C  C    . ASN   A 1 150 ? 20.940 -13.638 10.892  1.00 11.87 ?  150  ASN   A C    1 
ATOM   3343 O  O    . ASN   A 1 150 ? 21.675 -12.742 11.320  1.00 13.40 ?  150  ASN   A O    1 
ATOM   3344 C  CB   . ASN   A 1 150 ? 21.055 -15.202 12.864  1.00 14.71 ?  150  ASN   A CB   1 
ATOM   3345 C  CG   . ASN   A 1 150 ? 20.964 -16.640 13.310  1.00 18.61 ?  150  ASN   A CG   1 
ATOM   3346 O  OD1  . ASN   A 1 150 ? 20.397 -17.476 12.610  1.00 20.08 ?  150  ASN   A OD1  1 
ATOM   3347 N  ND2  . ASN   A 1 150 ? 21.546 -16.945 14.464  1.00 20.66 ?  150  ASN   A ND2  1 
ATOM   3348 H  H    . ASN   A 1 150 ? 23.059 -15.495 11.426  1.00 14.34 ?  150  ASN   A H    1 
ATOM   3349 H  HA   . ASN   A 1 150 ? 20.412 -15.611 10.970  1.00 15.11 ?  150  ASN   A HA   1 
ATOM   3350 H  HB2  . ASN   A 1 150 ? 21.852 -14.817 13.258  1.00 17.68 ?  150  ASN   A HB2  1 
ATOM   3351 H  HB3  . ASN   A 1 150 ? 20.265 -14.740 13.187  1.00 17.68 ?  150  ASN   A HB3  1 
ATOM   3352 H  HD21 . ASN   A 1 150 ? 21.527 -17.755 14.765  1.00 24.82 ?  150  ASN   A HD21 1 
ATOM   3353 H  HD22 . ASN   A 1 150 ? 21.944 -16.334 14.924  1.00 24.82 ?  150  ASN   A HD22 1 
ATOM   3354 N  N    . VAL   A 1 151 ? 19.950 -13.412 10.032  1.00 11.54 ?  151  VAL   A N    1 
ATOM   3355 C  CA   . VAL   A 1 151 ? 19.731 -12.104 9.433   1.00 11.37 ?  151  VAL   A CA   1 
ATOM   3356 C  C    . VAL   A 1 151 ? 18.336 -11.601 9.782   1.00 11.43 ?  151  VAL   A C    1 
ATOM   3357 O  O    . VAL   A 1 151 ? 17.333 -12.318 9.632   1.00 12.57 ?  151  VAL   A O    1 
ATOM   3358 C  CB   . VAL   A 1 151 ? 20.028 -12.093 7.918   1.00 12.44 ?  151  VAL   A CB   1 
ATOM   3359 C  CG1  . VAL   A 1 151 ? 19.187 -13.091 7.161   1.00 13.78 ?  151  VAL   A CG1  1 
ATOM   3360 C  CG2  . VAL   A 1 151 ? 19.859 -10.688 7.349   1.00 12.96 ?  151  VAL   A CG2  1 
ATOM   3361 H  H    . VAL   A 1 151 ? 19.392 -14.012 9.775   1.00 13.88 ?  151  VAL   A H    1 
ATOM   3362 H  HA   . VAL   A 1 151 ? 20.364 -11.485 9.833   1.00 13.67 ?  151  VAL   A HA   1 
ATOM   3363 H  HB   . VAL   A 1 151 ? 20.959 -12.343 7.782   1.00 14.95 ?  151  VAL   A HB   1 
ATOM   3364 H  HG11 . VAL   A 1 151 ? 19.407 -13.050 6.217   1.00 16.56 ?  151  VAL   A HG11 1 
ATOM   3365 H  HG12 . VAL   A 1 151 ? 19.369 -13.984 7.502   1.00 16.56 ?  151  VAL   A HG12 1 
ATOM   3366 H  HG13 . VAL   A 1 151 ? 18.248 -12.878 7.289   1.00 16.56 ?  151  VAL   A HG13 1 
ATOM   3367 H  HG21 . VAL   A 1 151 ? 20.181 -10.677 6.430   1.00 15.58 ?  151  VAL   A HG21 1 
ATOM   3368 H  HG22 . VAL   A 1 151 ? 18.922 -10.447 7.370   1.00 15.58 ?  151  VAL   A HG22 1 
ATOM   3369 H  HG23 . VAL   A 1 151 ? 20.377 -10.065 7.883   1.00 15.58 ?  151  VAL   A HG23 1 
ATOM   3370 N  N    . TYR   A 1 152 ? 18.306 -10.359 10.263  1.00 11.22 ?  152  TYR   A N    1 
ATOM   3371 C  CA   . TYR   A 1 152 ? 17.104 -9.635  10.642  1.00 10.88 ?  152  TYR   A CA   1 
ATOM   3372 C  C    . TYR   A 1 152 ? 16.903 -8.541  9.608   1.00 10.55 ?  152  TYR   A C    1 
ATOM   3373 O  O    . TYR   A 1 152 ? 17.669 -7.569  9.563   1.00 11.30 ?  152  TYR   A O    1 
ATOM   3374 C  CB   . TYR   A 1 152 ? 17.283 -9.087  12.055  1.00 11.47 ?  152  TYR   A CB   1 
ATOM   3375 C  CG   . TYR   A 1 152 ? 17.227 -10.206 13.068  1.00 12.61 ?  152  TYR   A CG   1 
ATOM   3376 C  CD1  . TYR   A 1 152 ? 18.352 -10.967 13.361  1.00 13.97 ?  152  TYR   A CD1  1 
ATOM   3377 C  CD2  . TYR   A 1 152 ? 16.039 -10.538 13.694  1.00 12.88 ?  152  TYR   A CD2  1 
ATOM   3378 C  CE1  . TYR   A 1 152 ? 18.298 -12.019 14.259  1.00 15.43 ?  152  TYR   A CE1  1 
ATOM   3379 C  CE2  . TYR   A 1 152 ? 15.970 -11.591 14.593  1.00 14.18 ?  152  TYR   A CE2  1 
ATOM   3380 C  CZ   . TYR   A 1 152 ? 17.106 -12.323 14.874  1.00 15.53 ?  152  TYR   A CZ   1 
ATOM   3381 O  OH   . TYR   A 1 152 ? 17.045 -13.372 15.766  1.00 18.16 ?  152  TYR   A OH   1 
ATOM   3382 H  H    . TYR   A 1 152 ? 19.023 -9.883  10.366  1.00 13.48 ?  152  TYR   A H    1 
ATOM   3383 H  HA   . TYR   A 1 152 ? 16.344 -10.239 10.625  1.00 13.08 ?  152  TYR   A HA   1 
ATOM   3384 H  HB2  . TYR   A 1 152 ? 18.154 -8.662  12.121  1.00 13.79 ?  152  TYR   A HB2  1 
ATOM   3385 H  HB3  . TYR   A 1 152 ? 16.580 -8.459  12.247  1.00 13.79 ?  152  TYR   A HB3  1 
ATOM   3386 H  HD1  . TYR   A 1 152 ? 19.159 -10.770 12.940  1.00 16.78 ?  152  TYR   A HD1  1 
ATOM   3387 H  HD2  . TYR   A 1 152 ? 15.271 -10.048 13.497  1.00 15.49 ?  152  TYR   A HD2  1 
ATOM   3388 H  HE1  . TYR   A 1 152 ? 19.061 -12.512 14.448  1.00 18.54 ?  152  TYR   A HE1  1 
ATOM   3389 H  HE2  . TYR   A 1 152 ? 15.162 -11.792 15.008  1.00 17.04 ?  152  TYR   A HE2  1 
ATOM   3390 H  HH   . TYR   A 1 152 ? 16.258 -13.437 16.072  1.00 21.82 ?  152  TYR   A HH   1 
ATOM   3391 N  N    A LEU   A 1 153 ? 15.905 -8.740  8.749   0.30 10.55 ?  153  LEU   A N    1 
ATOM   3392 N  N    B LEU   A 1 153 ? 15.878 -8.695  8.779   0.70 11.25 ?  153  LEU   A N    1 
ATOM   3393 C  CA   A LEU   A 1 153 ? 15.633 -7.851  7.632   0.30 10.45 ?  153  LEU   A CA   1 
ATOM   3394 C  CA   B LEU   A 1 153 ? 15.616 -7.786  7.673   0.70 11.48 ?  153  LEU   A CA   1 
ATOM   3395 C  C    A LEU   A 1 153 ? 14.653 -6.769  8.059   0.30 10.60 ?  153  LEU   A C    1 
ATOM   3396 C  C    B LEU   A 1 153 ? 14.597 -6.728  8.069   0.70 12.01 ?  153  LEU   A C    1 
ATOM   3397 O  O    A LEU   A 1 153 ? 13.582 -7.064  8.601   0.30 11.37 ?  153  LEU   A O    1 
ATOM   3398 O  O    B LEU   A 1 153 ? 13.476 -7.051  8.482   0.70 13.32 ?  153  LEU   A O    1 
ATOM   3399 C  CB   A LEU   A 1 153 ? 15.048 -8.638  6.459   0.30 10.42 ?  153  LEU   A CB   1 
ATOM   3400 C  CB   B LEU   A 1 153 ? 15.077 -8.557  6.470   0.70 11.79 ?  153  LEU   A CB   1 
ATOM   3401 C  CG   A LEU   A 1 153 ? 16.007 -9.583  5.732   0.30 10.67 ?  153  LEU   A CG   1 
ATOM   3402 C  CG   B LEU   A 1 153 ? 16.025 -9.583  5.860   0.70 12.04 ?  153  LEU   A CG   1 
ATOM   3403 C  CD1  A LEU   A 1 153 ? 15.237 -10.513 4.807   0.30 11.01 ?  153  LEU   A CD1  1 
ATOM   3404 C  CD1  B LEU   A 1 153 ? 15.264 -10.434 4.854   0.70 12.64 ?  153  LEU   A CD1  1 
ATOM   3405 C  CD2  A LEU   A 1 153 ? 17.044 -8.786  4.951   0.30 10.98 ?  153  LEU   A CD2  1 
ATOM   3406 C  CD2  B LEU   A 1 153 ? 17.223 -8.887  5.212   0.70 12.49 ?  153  LEU   A CD2  1 
ATOM   3407 H  H    A LEU   A 1 153 ? 15.354 -9.406  8.796   0.30 12.68 ?  153  LEU   A H    1 
ATOM   3408 H  H    B LEU   A 1 153 ? 15.299 -9.340  8.838   0.70 13.52 ?  153  LEU   A H    1 
ATOM   3409 H  HA   A LEU   A 1 153 ? 16.457 -7.436  7.348   0.30 12.57 ?  153  LEU   A HA   1 
ATOM   3410 H  HA   B LEU   A 1 153 ? 16.445 -7.345  7.425   0.70 13.80 ?  153  LEU   A HA   1 
ATOM   3411 H  HB2  A LEU   A 1 153 ? 14.311 -9.172  6.787   0.30 12.53 ?  153  LEU   A HB2  1 
ATOM   3412 H  HB2  B LEU   A 1 153 ? 14.278 -9.022  6.746   0.70 14.17 ?  153  LEU   A HB2  1 
ATOM   3413 H  HB3  A LEU   A 1 153 ? 14.720 -8.002  5.803   0.30 12.53 ?  153  LEU   A HB3  1 
ATOM   3414 H  HB3  B LEU   A 1 153 ? 14.860 -7.911  5.779   0.70 14.17 ?  153  LEU   A HB3  1 
ATOM   3415 H  HG   A LEU   A 1 153 ? 16.475 -10.128 6.385   0.30 12.82 ?  153  LEU   A HG   1 
ATOM   3416 H  HG   B LEU   A 1 153 ? 16.362 -10.162 6.563   0.70 14.47 ?  153  LEU   A HG   1 
ATOM   3417 H  HD11 A LEU   A 1 153 ? 15.851 -11.163 4.429   0.30 13.24 ?  153  LEU   A HD11 1 
ATOM   3418 H  HD11 B LEU   A 1 153 ? 15.856 -11.124 4.515   0.70 15.19 ?  153  LEU   A HD11 1 
ATOM   3419 H  HD12 A LEU   A 1 153 ? 14.550 -10.966 5.317   0.30 13.24 ?  153  LEU   A HD12 1 
ATOM   3420 H  HD12 B LEU   A 1 153 ? 14.503 -10.837 5.296   0.70 15.19 ?  153  LEU   A HD12 1 
ATOM   3421 H  HD13 A LEU   A 1 153 ? 14.835 -9.988  4.097   0.30 13.24 ?  153  LEU   A HD13 1 
ATOM   3422 H  HD13 B LEU   A 1 153 ? 14.965 -9.867  4.126   0.70 15.19 ?  153  LEU   A HD13 1 
ATOM   3423 H  HD21 A LEU   A 1 153 ? 17.602 -9.400  4.450   0.30 13.20 ?  153  LEU   A HD21 1 
ATOM   3424 H  HD21 B LEU   A 1 153 ? 17.780 -9.552  4.785   0.70 15.02 ?  153  LEU   A HD21 1 
ATOM   3425 H  HD22 A LEU   A 1 153 ? 16.585 -8.184  4.345   0.30 13.20 ?  153  LEU   A HD22 1 
ATOM   3426 H  HD22 B LEU   A 1 153 ? 16.898 -8.251  4.555   0.70 15.02 ?  153  LEU   A HD22 1 
ATOM   3427 H  HD23 A LEU   A 1 153 ? 17.586 -8.280  5.575   0.30 13.20 ?  153  LEU   A HD23 1 
ATOM   3428 H  HD23 B LEU   A 1 153 ? 17.729 -8.421  5.898   0.70 15.02 ?  153  LEU   A HD23 1 
ATOM   3429 N  N    A ALA   A 1 154 ? 15.021 -5.521  7.800   0.30 10.64 ?  154  ALA   A N    1 
ATOM   3430 N  N    B ALA   A 1 154 ? 14.978 -5.466  7.896   0.70 11.87 ?  154  ALA   A N    1 
ATOM   3431 C  CA   A ALA   A 1 154 ? 14.173 -4.370  8.068   0.30 11.15 ?  154  ALA   A CA   1 
ATOM   3432 C  CA   B ALA   A 1 154 ? 14.094 -4.325  8.100   0.70 12.83 ?  154  ALA   A CA   1 
ATOM   3433 C  C    A ALA   A 1 154 ? 13.648 -3.845  6.743   0.30 11.49 ?  154  ALA   A C    1 
ATOM   3434 C  C    B ALA   A 1 154 ? 13.614 -3.831  6.740   0.70 12.93 ?  154  ALA   A C    1 
ATOM   3435 O  O    A ALA   A 1 154 ? 14.435 -3.495  5.856   0.30 11.72 ?  154  ALA   A O    1 
ATOM   3436 O  O    B ALA   A 1 154 ? 14.425 -3.384  5.920   0.70 13.35 ?  154  ALA   A O    1 
ATOM   3437 C  CB   A ALA   A 1 154 ? 14.954 -3.273  8.788   0.30 11.24 ?  154  ALA   A CB   1 
ATOM   3438 C  CB   B ALA   A 1 154 ? 14.829 -3.202  8.831   0.70 13.18 ?  154  ALA   A CB   1 
ATOM   3439 H  H    A ALA   A 1 154 ? 15.780 -5.312  7.452   0.30 12.79 ?  154  ALA   A H    1 
ATOM   3440 H  H    B ALA   A 1 154 ? 15.769 -5.237  7.646   0.70 14.27 ?  154  ALA   A H    1 
ATOM   3441 H  HA   A ALA   A 1 154 ? 13.419 -4.634  8.615   0.30 13.41 ?  154  ALA   A HA   1 
ATOM   3442 H  HA   B ALA   A 1 154 ? 13.323 -4.590  8.628   0.70 15.42 ?  154  ALA   A HA   1 
ATOM   3443 H  HB1  A ALA   A 1 154 ? 14.362 -2.522  8.948   0.30 13.51 ?  154  ALA   A HB1  1 
ATOM   3444 H  HB1  B ALA   A 1 154 ? 14.225 -2.454  8.955   0.70 15.84 ?  154  ALA   A HB1  1 
ATOM   3445 H  HB2  A ALA   A 1 154 ? 15.282 -3.625  9.627   0.30 13.51 ?  154  ALA   A HB2  1 
ATOM   3446 H  HB2  B ALA   A 1 154 ? 15.132 -3.530  9.692   0.70 15.84 ?  154  ALA   A HB2  1 
ATOM   3447 H  HB3  A ALA   A 1 154 ? 15.696 -2.997  8.228   0.30 13.51 ?  154  ALA   A HB3  1 
ATOM   3448 H  HB3  B ALA   A 1 154 ? 15.592 -2.925  8.297   0.70 15.84 ?  154  ALA   A HB3  1 
ATOM   3449 N  N    A VAL   A 1 155 ? 12.327 -3.796  6.611   0.30 11.99 ?  155  VAL   A N    1 
ATOM   3450 N  N    B VAL   A 1 155 ? 12.305 -3.915  6.507   0.70 13.64 ?  155  VAL   A N    1 
ATOM   3451 C  CA   A VAL   A 1 155 ? 11.662 -3.296  5.414   0.30 12.75 ?  155  VAL   A CA   1 
ATOM   3452 C  CA   B VAL   A 1 155 ? 11.672 -3.530  5.246   0.70 14.34 ?  155  VAL   A CA   1 
ATOM   3453 C  C    A VAL   A 1 155 ? 10.939 -2.014  5.794   0.30 13.66 ?  155  VAL   A C    1 
ATOM   3454 C  C    B VAL   A 1 155 ? 10.942 -2.215  5.468   0.70 14.81 ?  155  VAL   A C    1 
ATOM   3455 O  O    A VAL   A 1 155 ? 10.011 -2.033  6.614   0.30 14.13 ?  155  VAL   A O    1 
ATOM   3456 O  O    B VAL   A 1 155 ? 9.980  -2.159  6.246   0.70 15.28 ?  155  VAL   A O    1 
ATOM   3457 C  CB   A VAL   A 1 155 ? 10.703 -4.338  4.820   0.30 13.16 ?  155  VAL   A CB   1 
ATOM   3458 C  CB   B VAL   A 1 155 ? 10.696 -4.612  4.755   0.70 14.94 ?  155  VAL   A CB   1 
ATOM   3459 C  CG1  A VAL   A 1 155 ? 9.958  -3.760  3.629   0.30 13.54 ?  155  VAL   A CG1  1 
ATOM   3460 C  CG1  B VAL   A 1 155 ? 9.910  -4.124  3.543   0.70 15.54 ?  155  VAL   A CG1  1 
ATOM   3461 C  CG2  A VAL   A 1 155 ? 11.481 -5.579  4.403   0.30 13.61 ?  155  VAL   A CG2  1 
ATOM   3462 C  CG2  B VAL   A 1 155 ? 11.443 -5.894  4.420   0.70 15.71 ?  155  VAL   A CG2  1 
ATOM   3463 H  H    A VAL   A 1 155 ? 11.777 -4.049  7.222   0.30 14.41 ?  155  VAL   A H    1 
ATOM   3464 H  H    B VAL   A 1 155 ? 11.743 -4.206  7.085   0.70 16.39 ?  155  VAL   A H    1 
ATOM   3465 H  HA   A VAL   A 1 155 ? 12.324 -3.080  4.742   0.30 15.32 ?  155  VAL   A HA   1 
ATOM   3466 H  HA   B VAL   A 1 155 ? 12.349 -3.405  4.563   0.70 17.24 ?  155  VAL   A HA   1 
ATOM   3467 H  HB   A VAL   A 1 155 ? 10.051 -4.599  5.491   0.30 15.82 ?  155  VAL   A HB   1 
ATOM   3468 H  HB   B VAL   A 1 155 ? 10.059 -4.817  5.462   0.70 17.96 ?  155  VAL   A HB   1 
ATOM   3469 H  HG11 A VAL   A 1 155 ? 9.516  -4.482  3.154   0.30 16.27 ?  155  VAL   A HG11 1 
ATOM   3470 H  HG11 B VAL   A 1 155 ? 9.501  -4.885  3.100   0.70 18.68 ?  155  VAL   A HG11 1 
ATOM   3471 H  HG12 A VAL   A 1 155 ? 9.301  -3.121  3.944   0.30 16.27 ?  155  VAL   A HG12 1 
ATOM   3472 H  HG12 B VAL   A 1 155 ? 9.219  -3.508  3.837   0.70 18.68 ?  155  VAL   A HG12 1 
ATOM   3473 H  HG13 A VAL   A 1 155 ? 10.596 -3.323  3.043   0.30 16.27 ?  155  VAL   A HG13 1 
ATOM   3474 H  HG13 B VAL   A 1 155 ? 10.516 -3.676  2.934   0.70 18.68 ?  155  VAL   A HG13 1 
ATOM   3475 H  HG21 A VAL   A 1 155 ? 10.871 -6.216  3.999   0.30 16.35 ?  155  VAL   A HG21 1 
ATOM   3476 H  HG21 B VAL   A 1 155 ? 10.820 -6.535  4.040   0.70 18.88 ?  155  VAL   A HG21 1 
ATOM   3477 H  HG22 A VAL   A 1 155 ? 12.162 -5.323  3.760   0.30 16.35 ?  155  VAL   A HG22 1 
ATOM   3478 H  HG22 B VAL   A 1 155 ? 12.140 -5.693  3.777   0.70 18.88 ?  155  VAL   A HG22 1 
ATOM   3479 H  HG23 A VAL   A 1 155 ? 11.898 -5.971  5.186   0.30 16.35 ?  155  VAL   A HG23 1 
ATOM   3480 H  HG23 B VAL   A 1 155 ? 11.833 -6.255  5.231   0.70 18.88 ?  155  VAL   A HG23 1 
ATOM   3481 N  N    A PHE   A 1 156 ? 11.370 -0.899  5.201   0.30 13.80 ?  156  PHE   A N    1 
ATOM   3482 N  N    B PHE   A 1 156 ? 11.367 -1.175  4.742   0.70 15.26 ?  156  PHE   A N    1 
ATOM   3483 C  CA   A PHE   A 1 156 ? 10.840 0.405   5.588   0.30 14.77 ?  156  PHE   A CA   1 
ATOM   3484 C  CA   B PHE   A 1 156 ? 10.897 0.187   4.996   0.70 15.80 ?  156  PHE   A CA   1 
ATOM   3485 C  C    A PHE   A 1 156 ? 9.375  0.558   5.195   0.30 14.75 ?  156  PHE   A C    1 
ATOM   3486 C  C    B PHE   A 1 156 ? 9.428  0.370   4.621   0.70 16.92 ?  156  PHE   A C    1 
ATOM   3487 O  O    A PHE   A 1 156 ? 8.571  1.077   5.977   0.30 15.25 ?  156  PHE   A O    1 
ATOM   3488 O  O    B PHE   A 1 156 ? 8.674  1.012   5.362   0.70 18.91 ?  156  PHE   A O    1 
ATOM   3489 C  CB   A PHE   A 1 156 ? 11.690 1.514   4.961   0.30 15.64 ?  156  PHE   A CB   1 
ATOM   3490 C  CB   B PHE   A 1 156 ? 11.803 1.155   4.222   0.70 15.14 ?  156  PHE   A CB   1 
ATOM   3491 C  CG   A PHE   A 1 156 ? 11.183 2.902   5.248   0.30 16.80 ?  156  PHE   A CG   1 
ATOM   3492 C  CG   B PHE   A 1 156 ? 11.521 2.629   4.452   0.70 15.76 ?  156  PHE   A CG   1 
ATOM   3493 C  CD1  A PHE   A 1 156 ? 11.157 3.385   6.544   0.30 17.35 ?  156  PHE   A CD1  1 
ATOM   3494 C  CD1  B PHE   A 1 156 ? 11.866 3.255   5.647   0.70 16.83 ?  156  PHE   A CD1  1 
ATOM   3495 C  CD2  A PHE   A 1 156 ? 10.743 3.725   4.222   0.30 17.58 ?  156  PHE   A CD2  1 
ATOM   3496 C  CD2  B PHE   A 1 156 ? 10.992 3.403   3.436   0.70 16.64 ?  156  PHE   A CD2  1 
ATOM   3497 C  CE1  A PHE   A 1 156 ? 10.694 4.657   6.816   0.30 17.94 ?  156  PHE   A CE1  1 
ATOM   3498 C  CE1  B PHE   A 1 156 ? 11.629 4.618   5.835   0.70 17.59 ?  156  PHE   A CE1  1 
ATOM   3499 C  CE2  A PHE   A 1 156 ? 10.279 5.002   4.488   0.30 18.00 ?  156  PHE   A CE2  1 
ATOM   3500 C  CE2  B PHE   A 1 156 ? 10.757 4.756   3.614   0.70 17.20 ?  156  PHE   A CE2  1 
ATOM   3501 C  CZ   A PHE   A 1 156 ? 10.257 5.469   5.786   0.30 18.10 ?  156  PHE   A CZ   1 
ATOM   3502 C  CZ   B PHE   A 1 156 ? 11.079 5.366   4.817   0.70 17.83 ?  156  PHE   A CZ   1 
ATOM   3503 H  H    A PHE   A 1 156 ? 11.964 -0.873  4.580   0.30 16.59 ?  156  PHE   A H    1 
ATOM   3504 H  H    B PHE   A 1 156 ? 11.927 -1.240  4.089   0.70 18.33 ?  156  PHE   A H    1 
ATOM   3505 H  HA   A PHE   A 1 156 ? 10.901 0.498   6.549   0.30 17.75 ?  156  PHE   A HA   1 
ATOM   3506 H  HA   B PHE   A 1 156 ? 10.994 0.378   5.937   0.70 18.99 ?  156  PHE   A HA   1 
ATOM   3507 H  HB2  A PHE   A 1 156 ? 12.596 1.452   5.310   0.30 18.79 ?  156  PHE   A HB2  1 
ATOM   3508 H  HB2  B PHE   A 1 156 ? 12.718 0.991   4.493   0.70 18.19 ?  156  PHE   A HB2  1 
ATOM   3509 H  HB3  A PHE   A 1 156 ? 11.703 1.396   3.998   0.30 18.79 ?  156  PHE   A HB3  1 
ATOM   3510 H  HB3  B PHE   A 1 156 ? 11.710 0.984   3.271   0.70 18.19 ?  156  PHE   A HB3  1 
ATOM   3511 H  HD1  A PHE   A 1 156 ? 11.451 2.842   7.242   0.30 20.85 ?  156  PHE   A HD1  1 
ATOM   3512 H  HD1  B PHE   A 1 156 ? 12.238 2.746   6.339   0.70 20.22 ?  156  PHE   A HD1  1 
ATOM   3513 H  HD2  A PHE   A 1 156 ? 10.761 3.413   3.344   0.30 21.12 ?  156  PHE   A HD2  1 
ATOM   3514 H  HD2  B PHE   A 1 156 ? 10.768 3.005   2.629   0.70 19.99 ?  156  PHE   A HD2  1 
ATOM   3515 H  HE1  A PHE   A 1 156 ? 10.679 4.969   7.693   0.30 21.55 ?  156  PHE   A HE1  1 
ATOM   3516 H  HE1  B PHE   A 1 156 ? 11.852 5.011   6.648   0.70 21.13 ?  156  PHE   A HE1  1 
ATOM   3517 H  HE2  A PHE   A 1 156 ? 9.988  5.544   3.792   0.30 21.63 ?  156  PHE   A HE2  1 
ATOM   3518 H  HE2  B PHE   A 1 156 ? 10.381 5.258   2.929   0.70 20.66 ?  156  PHE   A HE2  1 
ATOM   3519 H  HZ   A PHE   A 1 156 ? 9.946  6.325   5.969   0.30 21.74 ?  156  PHE   A HZ   1 
ATOM   3520 H  HZ   B PHE   A 1 156 ? 10.918 6.272   4.942   0.70 21.42 ?  156  PHE   A HZ   1 
ATOM   3521 N  N    A ASP   A 1 157 ? 9.010  0.110   3.995   0.30 14.55 ?  157  ASP   A N    1 
ATOM   3522 N  N    B ASP   A 1 157 ? 9.001  -0.188  3.491   0.70 18.03 ?  157  ASP   A N    1 
ATOM   3523 C  CA   A ASP   A 1 157 ? 7.675  0.341   3.451   0.30 15.35 ?  157  ASP   A CA   1 
ATOM   3524 C  CA   B ASP   A 1 157 ? 7.668  0.071   2.951   0.70 18.92 ?  157  ASP   A CA   1 
ATOM   3525 C  C    A ASP   A 1 157 ? 6.701  -0.703  3.989   0.30 15.55 ?  157  ASP   A C    1 
ATOM   3526 C  C    B ASP   A 1 157 ? 6.671  -0.992  3.416   0.70 18.29 ?  157  ASP   A C    1 
ATOM   3527 O  O    A ASP   A 1 157 ? 6.918  -1.906  3.818   0.30 15.17 ?  157  ASP   A O    1 
ATOM   3528 O  O    B ASP   A 1 157 ? 6.869  -2.185  3.171   0.70 17.01 ?  157  ASP   A O    1 
ATOM   3529 C  CB   A ASP   A 1 157 ? 7.742  0.258   1.928   0.30 16.02 ?  157  ASP   A CB   1 
ATOM   3530 C  CB   B ASP   A 1 157 ? 7.730  0.103   1.426   0.70 20.29 ?  157  ASP   A CB   1 
ATOM   3531 C  CG   A ASP   A 1 157 ? 6.509  0.811   1.254   0.30 16.94 ?  157  ASP   A CG   1 
ATOM   3532 C  CG   B ASP   A 1 157 ? 6.414  0.534   0.802   0.70 21.88 ?  157  ASP   A CG   1 
ATOM   3533 O  OD1  A ASP   A 1 157 ? 5.485  0.097   1.208   0.30 17.17 ?  157  ASP   A OD1  1 
ATOM   3534 O  OD1  B ASP   A 1 157 ? 5.794  -0.285  0.099   0.70 21.55 ?  157  ASP   A OD1  1 
ATOM   3535 O  OD2  A ASP   A 1 157 ? 6.572  1.964   0.773   0.30 17.19 -1 157  ASP   A OD2  1 
ATOM   3536 O  OD2  B ASP   A 1 157 ? 5.984  1.685   1.038   0.70 23.55 -1 157  ASP   A OD2  1 
ATOM   3537 H  H    A ASP   A 1 157 ? 9.527  -0.335  3.469   0.30 17.48 ?  157  ASP   A H    1 
ATOM   3538 H  H    B ASP   A 1 157 ? 9.468  -0.735  3.016   0.70 21.66 ?  157  ASP   A H    1 
ATOM   3539 H  HA   A ASP   A 1 157 ? 7.362  1.225   3.701   0.30 18.44 ?  157  ASP   A HA   1 
ATOM   3540 H  HA   B ASP   A 1 157 ? 7.360  0.936   3.260   0.70 22.73 ?  157  ASP   A HA   1 
ATOM   3541 H  HB2  A ASP   A 1 157 ? 8.492  0.772   1.612   0.30 19.25 ?  157  ASP   A HB2  1 
ATOM   3542 H  HB2  B ASP   A 1 157 ? 8.432  0.715   1.153   0.70 24.37 ?  157  ASP   A HB2  1 
ATOM   3543 H  HB3  A ASP   A 1 157 ? 7.844  -0.672  1.670   0.30 19.25 ?  157  ASP   A HB3  1 
ATOM   3544 H  HB3  B ASP   A 1 157 ? 7.934  -0.794  1.103   0.70 24.37 ?  157  ASP   A HB3  1 
ATOM   3545 N  N    A LYS   A 1 158 ? 5.611  -0.246  4.613   0.30 16.53 ?  158  LYS   A N    1 
ATOM   3546 N  N    B LYS   A 1 158 ? 5.576  -0.551  4.049   0.70 19.28 ?  158  LYS   A N    1 
ATOM   3547 C  CA   A LYS   A 1 158 ? 4.648  -1.181  5.191   0.30 17.28 ?  158  LYS   A CA   1 
ATOM   3548 C  CA   B LYS   A 1 158 ? 4.589  -1.480  4.610   0.70 20.32 ?  158  LYS   A CA   1 
ATOM   3549 C  C    A LYS   A 1 158 ? 3.924  -1.977  4.112   0.30 17.44 ?  158  LYS   A C    1 
ATOM   3550 C  C    B LYS   A 1 158 ? 3.908  -2.306  3.518   0.70 19.39 ?  158  LYS   A C    1 
ATOM   3551 O  O    A LYS   A 1 158 ? 3.752  -3.195  4.246   0.30 17.63 ?  158  LYS   A O    1 
ATOM   3552 O  O    B LYS   A 1 158 ? 3.731  -3.523  3.656   0.70 18.79 ?  158  LYS   A O    1 
ATOM   3553 C  CB   A LYS   A 1 158 ? 3.654  -0.439  6.087   0.30 17.90 ?  158  LYS   A CB   1 
ATOM   3554 C  CB   B LYS   A 1 158 ? 3.556  -0.693  5.427   0.70 22.36 ?  158  LYS   A CB   1 
ATOM   3555 C  CG   A LYS   A 1 158 ? 2.454  -1.275  6.537   0.30 18.95 ?  158  LYS   A CG   1 
ATOM   3556 C  CG   B LYS   A 1 158 ? 2.332  -1.491  5.885   0.70 24.54 ?  158  LYS   A CG   1 
ATOM   3557 C  CD   A LYS   A 1 158 ? 2.861  -2.521  7.321   0.30 19.87 ?  158  LYS   A CD   1 
ATOM   3558 C  CD   B LYS   A 1 158 ? 2.680  -2.600  6.876   0.70 26.47 ?  158  LYS   A CD   1 
ATOM   3559 C  CE   A LYS   A 1 158 ? 1.633  -3.265  7.834   0.30 20.59 ?  158  LYS   A CE   1 
ATOM   3560 C  CE   B LYS   A 1 158 ? 1.417  -3.282  7.402   0.70 27.44 ?  158  LYS   A CE   1 
ATOM   3561 N  NZ   A LYS   A 1 158 ? 1.968  -4.591  8.423   0.30 20.93 ?  158  LYS   A NZ   1 
ATOM   3562 N  NZ   B LYS   A 1 158 ? 1.711  -4.469  8.253   0.70 27.74 ?  158  LYS   A NZ   1 
ATOM   3563 H  H    A LYS   A 1 158 ? 5.407  0.585   4.702   0.30 19.85 ?  158  LYS   A H    1 
ATOM   3564 H  H    B LYS   A 1 158 ? 5.384  0.278   4.166   0.70 23.16 ?  158  LYS   A H    1 
ATOM   3565 H  HA   A LYS   A 1 158 ? 5.128  -1.811  5.746   0.30 20.76 ?  158  LYS   A HA   1 
ATOM   3566 H  HA   B LYS   A 1 158 ? 5.039  -2.090  5.216   0.70 24.41 ?  158  LYS   A HA   1 
ATOM   3567 H  HB2  A LYS   A 1 158 ? 4.120  -0.143  6.886   0.30 21.50 ?  158  LYS   A HB2  1 
ATOM   3568 H  HB2  B LYS   A 1 158 ? 3.988  -0.345  6.225   0.70 26.86 ?  158  LYS   A HB2  1 
ATOM   3569 H  HB3  A LYS   A 1 158 ? 3.313  0.330   5.605   0.30 21.50 ?  158  LYS   A HB3  1 
ATOM   3570 H  HB3  B LYS   A 1 158 ? 3.235  0.049   4.888   0.70 26.86 ?  158  LYS   A HB3  1 
ATOM   3571 H  HG2  A LYS   A 1 158 ? 1.896  -0.731  7.113   0.30 22.76 ?  158  LYS   A HG2  1 
ATOM   3572 H  HG2  B LYS   A 1 158 ? 1.713  -0.885  6.324   0.70 29.47 ?  158  LYS   A HG2  1 
ATOM   3573 H  HG3  A LYS   A 1 158 ? 1.944  -1.556  5.760   0.30 22.76 ?  158  LYS   A HG3  1 
ATOM   3574 H  HG3  B LYS   A 1 158 ? 1.899  -1.894  5.116   0.70 29.47 ?  158  LYS   A HG3  1 
ATOM   3575 H  HD2  A LYS   A 1 158 ? 3.360  -3.116  6.742   0.30 23.87 ?  158  LYS   A HD2  1 
ATOM   3576 H  HD2  B LYS   A 1 158 ? 3.229  -3.264  6.432   0.70 31.78 ?  158  LYS   A HD2  1 
ATOM   3577 H  HD3  A LYS   A 1 158 ? 3.402  -2.256  8.082   0.30 23.87 ?  158  LYS   A HD3  1 
ATOM   3578 H  HD3  B LYS   A 1 158 ? 3.159  -2.214  7.628   0.70 31.78 ?  158  LYS   A HD3  1 
ATOM   3579 H  HE2  A LYS   A 1 158 ? 1.199  -2.728  8.517   0.30 24.74 ?  158  LYS   A HE2  1 
ATOM   3580 H  HE2  B LYS   A 1 158 ? 0.916  -2.644  7.935   0.70 32.96 ?  158  LYS   A HE2  1 
ATOM   3581 H  HE3  A LYS   A 1 158 ? 1.023  -3.409  7.095   0.30 24.74 ?  158  LYS   A HE3  1 
ATOM   3582 H  HE3  B LYS   A 1 158 ? 0.883  -3.574  6.647   0.70 32.96 ?  158  LYS   A HE3  1 
ATOM   3583 H  HZ1  A LYS   A 1 158 ? 1.227  -4.990  8.711   0.30 25.14 ?  158  LYS   A HZ1  1 
ATOM   3584 H  HZ1  B LYS   A 1 158 ? 0.951  -4.835  8.536   0.70 33.31 ?  158  LYS   A HZ1  1 
ATOM   3585 H  HZ2  A LYS   A 1 158 ? 2.355  -5.105  7.809   0.30 25.14 ?  158  LYS   A HZ2  1 
ATOM   3586 H  HZ2  B LYS   A 1 158 ? 2.166  -5.074  7.785   0.70 33.31 ?  158  LYS   A HZ2  1 
ATOM   3587 H  HZ3  A LYS   A 1 158 ? 2.526  -4.487  9.108   0.30 25.14 ?  158  LYS   A HZ3  1 
ATOM   3588 H  HZ3  B LYS   A 1 158 ? 2.195  -4.225  8.959   0.70 33.31 ?  158  LYS   A HZ3  1 
ATOM   3589 N  N    A ASN   A 1 159 ? 3.487  -1.313  3.039   0.30 17.83 ?  159  ASN   A N    1 
ATOM   3590 N  N    B ASN   A 1 159 ? 3.497  -1.647  2.435   0.70 20.17 ?  159  ASN   A N    1 
ATOM   3591 C  CA   A ASN   A 1 159 ? 2.837  -2.033  1.948   0.30 17.96 ?  159  ASN   A CA   1 
ATOM   3592 C  CA   B ASN   A 1 159 ? 2.911  -2.336  1.289   0.70 21.57 ?  159  ASN   A CA   1 
ATOM   3593 C  C    A ASN   A 1 159 ? 3.765  -3.091  1.368   0.30 17.43 ?  159  ASN   A C    1 
ATOM   3594 C  C    B ASN   A 1 159 ? 3.805  -3.486  0.832   0.70 19.88 ?  159  ASN   A C    1 
ATOM   3595 O  O    A ASN   A 1 159 ? 3.346  -4.226  1.116   0.30 17.63 ?  159  ASN   A O    1 
ATOM   3596 O  O    B ASN   A 1 159 ? 3.349  -4.620  0.631   0.70 20.32 ?  159  ASN   A O    1 
ATOM   3597 C  CB   A ASN   A 1 159 ? 2.381  -1.051  0.864   0.30 18.58 ?  159  ASN   A CB   1 
ATOM   3598 C  CB   B ASN   A 1 159 ? 2.745  -1.299  0.175   0.70 24.60 ?  159  ASN   A CB   1 
ATOM   3599 C  CG   A ASN   A 1 159 ? 1.195  -0.219  1.298   0.30 19.29 ?  159  ASN   A CG   1 
ATOM   3600 C  CG   B ASN   A 1 159 ? 1.956  -1.813  -1.004  0.70 27.47 ?  159  ASN   A CG   1 
ATOM   3601 O  OD1  A ASN   A 1 159 ? 0.336  -0.698  2.033   0.30 19.78 ?  159  ASN   A OD1  1 
ATOM   3602 O  OD1  B ASN   A 1 159 ? 0.778  -1.491  -1.165  0.70 28.89 ?  159  ASN   A OD1  1 
ATOM   3603 N  ND2  A ASN   A 1 159 ? 1.141  1.032   0.846   0.30 19.76 ?  159  ASN   A ND2  1 
ATOM   3604 N  ND2  B ASN   A 1 159 ? 2.608  -2.591  -1.854  0.70 28.13 ?  159  ASN   A ND2  1 
ATOM   3605 H  H    A ASN   A 1 159 ? 3.559  -0.467  2.915   0.30 21.42 ?  159  ASN   A H    1 
ATOM   3606 H  H    B ASN   A 1 159 ? 3.541  -0.794  2.347   0.70 24.23 ?  159  ASN   A H    1 
ATOM   3607 H  HA   A ASN   A 1 159 ? 2.048  -2.484  2.286   0.30 21.58 ?  159  ASN   A HA   1 
ATOM   3608 H  HA   B ASN   A 1 159 ? 2.038  -2.685  1.525   0.70 25.91 ?  159  ASN   A HA   1 
ATOM   3609 H  HB2  A ASN   A 1 159 ? 3.105  -0.444  0.654   0.30 22.32 ?  159  ASN   A HB2  1 
ATOM   3610 H  HB2  B ASN   A 1 159 ? 2.287  -0.521  0.534   0.70 29.55 ?  159  ASN   A HB2  1 
ATOM   3611 H  HB3  A ASN   A 1 159 ? 2.120  -1.545  0.069   0.30 22.32 ?  159  ASN   A HB3  1 
ATOM   3612 H  HB3  B ASN   A 1 159 ? 3.628  -1.037  -0.141  0.70 29.55 ?  159  ASN   A HB3  1 
ATOM   3613 H  HD21 A ASN   A 1 159 ? 0.485  1.545   1.064   0.30 23.74 ?  159  ASN   A HD21 1 
ATOM   3614 H  HD21 B ASN   A 1 159 ? 2.204  -2.900  -2.544  0.70 33.78 ?  159  ASN   A HD21 1 
ATOM   3615 H  HD22 A ASN   A 1 159 ? 1.765  1.331   0.337   0.30 23.74 ?  159  ASN   A HD22 1 
ATOM   3616 H  HD22 B ASN   A 1 159 ? 3.433  -2.790  -1.711  0.70 33.78 ?  159  ASN   A HD22 1 
ATOM   3617 N  N    A LEU   A 1 160 ? 5.034  -2.743  1.161   0.30 16.55 ?  160  LEU   A N    1 
ATOM   3618 N  N    B LEU   A 1 160 ? 5.098  -3.203  0.677   0.70 18.61 ?  160  LEU   A N    1 
ATOM   3619 C  CA   A LEU   A 1 160 ? 5.978  -3.721  0.633   0.30 15.69 ?  160  LEU   A CA   1 
ATOM   3620 C  CA   B LEU   A 1 160 ? 6.046  -4.213  0.220   0.70 17.93 ?  160  LEU   A CA   1 
ATOM   3621 C  C    A LEU   A 1 160 ? 6.192  -4.860  1.620   0.30 14.68 ?  160  LEU   A C    1 
ATOM   3622 C  C    B LEU   A 1 160 ? 6.205  -5.327  1.245   0.70 17.23 ?  160  LEU   A C    1 
ATOM   3623 O  O    A LEU   A 1 160 ? 6.271  -6.027  1.221   0.30 14.70 ?  160  LEU   A O    1 
ATOM   3624 O  O    B LEU   A 1 160 ? 6.204  -6.510  0.888   0.70 17.59 ?  160  LEU   A O    1 
ATOM   3625 C  CB   A LEU   A 1 160 ? 7.305  -3.046  0.295   0.30 15.66 ?  160  LEU   A CB   1 
ATOM   3626 C  CB   B LEU   A 1 160 ? 7.392  -3.555  -0.073  0.70 18.00 ?  160  LEU   A CB   1 
ATOM   3627 C  CG   A LEU   A 1 160 ? 8.391  -4.002  -0.197  0.30 15.90 ?  160  LEU   A CG   1 
ATOM   3628 C  CG   B LEU   A 1 160 ? 8.522  -4.533  -0.378  0.70 18.54 ?  160  LEU   A CG   1 
ATOM   3629 C  CD1  A LEU   A 1 160 ? 7.925  -4.739  -1.443  0.30 16.00 ?  160  LEU   A CD1  1 
ATOM   3630 C  CD1  B LEU   A 1 160 ? 8.157  -5.372  -1.588  0.70 19.15 ?  160  LEU   A CD1  1 
ATOM   3631 C  CD2  A LEU   A 1 160 ? 9.684  -3.254  -0.459  0.30 16.02 ?  160  LEU   A CD2  1 
ATOM   3632 C  CD2  B LEU   A 1 160 ? 9.817  -3.775  -0.592  0.70 18.72 ?  160  LEU   A CD2  1 
ATOM   3633 H  H    A LEU   A 1 160 ? 5.365  -1.968  1.323   0.30 19.88 ?  160  LEU   A H    1 
ATOM   3634 H  H    B LEU   A 1 160 ? 5.452  -2.438  0.839   0.70 22.35 ?  160  LEU   A H    1 
ATOM   3635 H  HA   A LEU   A 1 160 ? 5.614  -4.095  -0.184  0.30 18.85 ?  160  LEU   A HA   1 
ATOM   3636 H  HA   B LEU   A 1 160 ? 5.714  -4.605  -0.602  0.70 21.54 ?  160  LEU   A HA   1 
ATOM   3637 H  HB2  A LEU   A 1 160 ? 7.155  -2.376  -0.396  0.30 18.82 ?  160  LEU   A HB2  1 
ATOM   3638 H  HB2  B LEU   A 1 160 ? 7.289  -2.974  -0.844  0.70 21.63 ?  160  LEU   A HB2  1 
ATOM   3639 H  HB3  A LEU   A 1 160 ? 7.640  -2.625  1.096   0.30 18.82 ?  160  LEU   A HB3  1 
ATOM   3640 H  HB3  B LEU   A 1 160 ? 7.654  -3.031  0.698   0.70 21.63 ?  160  LEU   A HB3  1 
ATOM   3641 H  HG   A LEU   A 1 160 ? 8.567  -4.660  0.493   0.30 19.11 ?  160  LEU   A HG   1 
ATOM   3642 H  HG   B LEU   A 1 160 ? 8.649  -5.129  0.378   0.70 22.28 ?  160  LEU   A HG   1 
ATOM   3643 H  HD11 A LEU   A 1 160 ? 8.674  -5.232  -1.811  0.30 19.22 ?  160  LEU   A HD11 1 
ATOM   3644 H  HD11 B LEU   A 1 160 ? 8.916  -5.917  -1.829  0.70 23.01 ?  160  LEU   A HD11 1 
ATOM   3645 H  HD12 A LEU   A 1 160 ? 7.213  -5.353  -1.202  0.30 19.22 ?  160  LEU   A HD12 1 
ATOM   3646 H  HD12 B LEU   A 1 160 ? 7.400  -5.940  -1.363  0.70 23.01 ?  160  LEU   A HD12 1 
ATOM   3647 H  HD13 A LEU   A 1 160 ? 7.603  -4.093  -2.090  0.30 19.22 ?  160  LEU   A HD13 1 
ATOM   3648 H  HD13 B LEU   A 1 160 ? 7.919  -4.781  -2.319  0.70 23.01 ?  160  LEU   A HD13 1 
ATOM   3649 H  HD21 A LEU   A 1 160 ? 10.355 -3.886  -0.764  0.30 19.25 ?  160  LEU   A HD21 1 
ATOM   3650 H  HD21 B LEU   A 1 160 ? 10.528 -4.409  -0.762  0.70 22.48 ?  160  LEU   A HD21 1 
ATOM   3651 H  HD22 A LEU   A 1 160 ? 9.527  -2.582  -1.139  0.30 19.25 ?  160  LEU   A HD22 1 
ATOM   3652 H  HD22 B LEU   A 1 160 ? 9.710  -3.181  -1.351  0.70 22.48 ?  160  LEU   A HD22 1 
ATOM   3653 H  HD23 A LEU   A 1 160 ? 9.977  -2.832  0.364   0.30 19.25 ?  160  LEU   A HD23 1 
ATOM   3654 H  HD23 B LEU   A 1 160 ? 10.014 -3.259  0.206   0.70 22.48 ?  160  LEU   A HD23 1 
ATOM   3655 N  N    A TYR   A 1 161 ? 6.284  -4.544  2.912   0.30 14.59 ?  161  TYR   A N    1 
ATOM   3656 N  N    B TYR   A 1 161 ? 6.347  -4.972  2.523   0.70 16.76 ?  161  TYR   A N    1 
ATOM   3657 C  CA   A TYR   A 1 161 ? 6.425  -5.597  3.910   0.30 14.38 ?  161  TYR   A CA   1 
ATOM   3658 C  CA   B TYR   A 1 161 ? 6.462  -5.980  3.575   0.70 16.81 ?  161  TYR   A CA   1 
ATOM   3659 C  C    A TYR   A 1 161 ? 5.280  -6.599  3.815   0.30 14.88 ?  161  TYR   A C    1 
ATOM   3660 C  C    B TYR   A 1 161 ? 5.307  -6.970  3.522   0.70 16.91 ?  161  TYR   A C    1 
ATOM   3661 O  O    A TYR   A 1 161 ? 5.498  -7.814  3.844   0.30 14.72 ?  161  TYR   A O    1 
ATOM   3662 O  O    B TYR   A 1 161 ? 5.514  -8.186  3.565   0.70 16.66 ?  161  TYR   A O    1 
ATOM   3663 C  CB   A TYR   A 1 161 ? 6.499  -5.008  5.317   0.30 14.44 ?  161  TYR   A CB   1 
ATOM   3664 C  CB   B TYR   A 1 161 ? 6.532  -5.293  4.942   0.70 17.40 ?  161  TYR   A CB   1 
ATOM   3665 C  CG   A TYR   A 1 161 ? 6.452  -6.100  6.350   0.30 14.14 ?  161  TYR   A CG   1 
ATOM   3666 C  CG   B TYR   A 1 161 ? 6.395  -6.217  6.145   0.70 18.16 ?  161  TYR   A CG   1 
ATOM   3667 C  CD1  A TYR   A 1 161 ? 7.596  -6.807  6.681   0.30 13.97 ?  161  TYR   A CD1  1 
ATOM   3668 C  CD1  B TYR   A 1 161 ? 7.498  -6.880  6.675   0.70 18.68 ?  161  TYR   A CD1  1 
ATOM   3669 C  CD2  A TYR   A 1 161 ? 5.257  -6.458  6.959   0.30 14.08 ?  161  TYR   A CD2  1 
ATOM   3670 C  CD2  B TYR   A 1 161 ? 5.165  -6.402  6.767   0.70 18.87 ?  161  TYR   A CD2  1 
ATOM   3671 C  CE1  A TYR   A 1 161 ? 7.560  -7.828  7.602   0.30 13.94 ?  161  TYR   A CE1  1 
ATOM   3672 C  CE1  B TYR   A 1 161 ? 7.370  -7.725  7.780   0.70 19.24 ?  161  TYR   A CE1  1 
ATOM   3673 C  CE2  A TYR   A 1 161 ? 5.211  -7.476  7.884   0.30 13.98 ?  161  TYR   A CE2  1 
ATOM   3674 C  CE2  B TYR   A 1 161 ? 5.030  -7.236  7.870   0.70 19.24 ?  161  TYR   A CE2  1 
ATOM   3675 C  CZ   A TYR   A 1 161 ? 6.368  -8.158  8.203   0.30 13.85 ?  161  TYR   A CZ   1 
ATOM   3676 C  CZ   B TYR   A 1 161 ? 6.132  -7.894  8.373   0.70 19.69 ?  161  TYR   A CZ   1 
ATOM   3677 O  OH   A TYR   A 1 161 ? 6.331  -9.173  9.126   0.30 13.59 ?  161  TYR   A OH   1 
ATOM   3678 O  OH   B TYR   A 1 161 ? 5.988  -8.724  9.471   0.70 20.68 ?  161  TYR   A OH   1 
ATOM   3679 H  H    A TYR   A 1 161 ? 6.262  -3.747  3.229   0.30 17.53 ?  161  TYR   A H    1 
ATOM   3680 H  H    B TYR   A 1 161 ? 6.359  -4.168  2.806   0.70 20.14 ?  161  TYR   A H    1 
ATOM   3681 H  HA   A TYR   A 1 161 ? 7.252  -6.075  3.748   0.30 17.28 ?  161  TYR   A HA   1 
ATOM   3682 H  HA   B TYR   A 1 161 ? 7.279  -6.483  3.445   0.70 20.20 ?  161  TYR   A HA   1 
ATOM   3683 H  HB2  A TYR   A 1 161 ? 7.333  -4.521  5.422   0.30 17.36 ?  161  TYR   A HB2  1 
ATOM   3684 H  HB2  B TYR   A 1 161 ? 7.386  -4.851  5.013   0.70 20.90 ?  161  TYR   A HB2  1 
ATOM   3685 H  HB3  A TYR   A 1 161 ? 5.743  -4.415  5.462   0.30 17.36 ?  161  TYR   A HB3  1 
ATOM   3686 H  HB3  B TYR   A 1 161 ? 5.815  -4.644  4.994   0.70 20.90 ?  161  TYR   A HB3  1 
ATOM   3687 H  HD1  A TYR   A 1 161 ? 8.404  -6.583  6.275   0.30 16.79 ?  161  TYR   A HD1  1 
ATOM   3688 H  HD1  B TYR   A 1 161 ? 8.331  -6.773  6.278   0.70 22.44 ?  161  TYR   A HD1  1 
ATOM   3689 H  HD2  A TYR   A 1 161 ? 4.475  -5.998  6.742   0.30 16.93 ?  161  TYR   A HD2  1 
ATOM   3690 H  HD2  B TYR   A 1 161 ? 4.412  -5.971  6.436   0.70 22.67 ?  161  TYR   A HD2  1 
ATOM   3691 H  HE1  A TYR   A 1 161 ? 8.337  -8.287  7.819   0.30 16.75 ?  161  TYR   A HE1  1 
ATOM   3692 H  HE1  B TYR   A 1 161 ? 8.118  -8.164  8.124   0.70 23.11 ?  161  TYR   A HE1  1 
ATOM   3693 H  HE2  A TYR   A 1 161 ? 4.403  -7.702  8.288   0.30 16.80 ?  161  TYR   A HE2  1 
ATOM   3694 H  HE2  B TYR   A 1 161 ? 4.196  -7.354  8.272   0.70 23.11 ?  161  TYR   A HE2  1 
ATOM   3695 H  HH   A TYR   A 1 161 ? 5.540  -9.267  9.402   0.30 16.33 ?  161  TYR   A HH   1 
ATOM   3696 H  HH   B TYR   A 1 161 ? 5.183  -8.724  9.730   0.70 24.84 ?  161  TYR   A HH   1 
ATOM   3697 N  N    A ASP   A 1 162 ? 4.046  -6.105  3.701   0.30 15.57 ?  162  ASP   A N    1 
ATOM   3698 N  N    B ASP   A 1 162 ? 4.077  -6.463  3.418   0.70 17.87 ?  162  ASP   A N    1 
ATOM   3699 C  CA   A ASP   A 1 162 ? 2.902  -7.008  3.622   0.30 16.23 ?  162  ASP   A CA   1 
ATOM   3700 C  CA   B ASP   A 1 162 ? 2.918  -7.349  3.375   0.70 18.66 ?  162  ASP   A CA   1 
ATOM   3701 C  C    A ASP   A 1 162 ? 2.944  -7.846  2.350   0.30 16.89 ?  162  ASP   A C    1 
ATOM   3702 C  C    B ASP   A 1 162 ? 2.974  -8.276  2.166   0.70 19.06 ?  162  ASP   A C    1 
ATOM   3703 O  O    A ASP   A 1 162 ? 2.589  -9.030  2.371   0.30 17.15 ?  162  ASP   A O    1 
ATOM   3704 O  O    B ASP   A 1 162 ? 2.613  -9.454  2.263   0.70 19.48 ?  162  ASP   A O    1 
ATOM   3705 C  CB   A ASP   A 1 162 ? 1.595  -6.218  3.705   0.30 16.73 ?  162  ASP   A CB   1 
ATOM   3706 C  CB   B ASP   A 1 162 ? 1.621  -6.535  3.370   0.70 20.49 ?  162  ASP   A CB   1 
ATOM   3707 C  CG   A ASP   A 1 162 ? 1.288  -5.732  5.109   0.30 17.11 ?  162  ASP   A CG   1 
ATOM   3708 C  CG   B ASP   A 1 162 ? 1.365  -5.813  4.679   0.70 22.25 ?  162  ASP   A CG   1 
ATOM   3709 O  OD1  A ASP   A 1 162 ? 2.046  -6.063  6.043   0.30 17.43 ?  162  ASP   A OD1  1 
ATOM   3710 O  OD1  B ASP   A 1 162 ? 1.927  -6.215  5.716   0.70 22.69 ?  162  ASP   A OD1  1 
ATOM   3711 O  OD2  A ASP   A 1 162 ? 0.274  -5.019  5.277   0.30 16.89 -1 162  ASP   A OD2  1 
ATOM   3712 O  OD2  B ASP   A 1 162 ? 0.566  -4.848  4.669   0.70 23.24 -1 162  ASP   A OD2  1 
ATOM   3713 H  H    A ASP   A 1 162 ? 3.850  -5.272  3.662   0.30 18.71 ?  162  ASP   A H    1 
ATOM   3714 H  H    B ASP   A 1 162 ? 3.884  -5.634  3.370   0.70 21.46 ?  162  ASP   A H    1 
ATOM   3715 H  HA   A ASP   A 1 162 ? 2.928  -7.619  4.373   0.30 19.50 ?  162  ASP   A HA   1 
ATOM   3716 H  HA   B ASP   A 1 162 ? 2.906  -7.913  4.163   0.70 22.41 ?  162  ASP   A HA   1 
ATOM   3717 H  HB2  A ASP   A 1 162 ? 1.653  -5.448  3.120   0.30 20.10 ?  162  ASP   A HB2  1 
ATOM   3718 H  HB2  B ASP   A 1 162 ? 1.665  -5.858  2.684   0.70 24.61 ?  162  ASP   A HB2  1 
ATOM   3719 H  HB3  A ASP   A 1 162 ? 0.860  -6.790  3.431   0.30 20.10 ?  162  ASP   A HB3  1 
ATOM   3720 H  HB3  B ASP   A 1 162 ? 0.863  -7.125  3.211   0.70 24.61 ?  162  ASP   A HB3  1 
ATOM   3721 N  N    A LYS   A 1 163 ? 3.373  -7.254  1.232   0.30 17.47 ?  163  LYS   A N    1 
ATOM   3722 N  N    B LYS   A 1 163 ? 3.432  -7.766  1.020   0.70 19.51 ?  163  LYS   A N    1 
ATOM   3723 C  CA   A LYS   A 1 163 ? 3.475  -8.019  -0.007  0.30 17.94 ?  163  LYS   A CA   1 
ATOM   3724 C  CA   B LYS   A 1 163 ? 3.544  -8.598  -0.174  0.70 20.67 ?  163  LYS   A CA   1 
ATOM   3725 C  C    A LYS   A 1 163 ? 4.569  -9.077  0.086   0.30 17.19 ?  163  LYS   A C    1 
ATOM   3726 C  C    B LYS   A 1 163 ? 4.643  -9.646  -0.022  0.70 18.61 ?  163  LYS   A C    1 
ATOM   3727 O  O    A LYS   A 1 163 ? 4.416  -10.181 -0.448  0.30 17.52 ?  163  LYS   A O    1 
ATOM   3728 O  O    B LYS   A 1 163 ? 4.467  -10.802 -0.426  0.70 19.02 ?  163  LYS   A O    1 
ATOM   3729 C  CB   A LYS   A 1 163 ? 3.727  -7.083  -1.191  0.30 19.60 ?  163  LYS   A CB   1 
ATOM   3730 C  CB   B LYS   A 1 163 ? 3.800  -7.710  -1.392  0.70 24.85 ?  163  LYS   A CB   1 
ATOM   3731 C  CG   A LYS   A 1 163 ? 3.780  -7.793  -2.540  0.30 21.19 ?  163  LYS   A CG   1 
ATOM   3732 C  CG   B LYS   A 1 163 ? 3.840  -8.455  -2.709  0.70 29.11 ?  163  LYS   A CG   1 
ATOM   3733 C  CD   A LYS   A 1 163 ? 4.221  -6.857  -3.654  0.30 22.63 ?  163  LYS   A CD   1 
ATOM   3734 C  CD   B LYS   A 1 163 ? 3.551  -7.515  -3.865  0.70 33.23 ?  163  LYS   A CD   1 
ATOM   3735 C  CE   A LYS   A 1 163 ? 4.161  -7.540  -5.012  0.30 23.80 ?  163  LYS   A CE   1 
ATOM   3736 C  CE   B LYS   A 1 163 ? 3.350  -8.278  -5.161  0.70 36.69 ?  163  LYS   A CE   1 
ATOM   3737 N  NZ   A LYS   A 1 163 ? 4.766  -6.703  -6.082  0.30 24.49 ?  163  LYS   A NZ   1 
ATOM   3738 N  NZ   B LYS   A 1 163 ? 2.034  -7.970  -5.787  0.70 38.62 ?  163  LYS   A NZ   1 
ATOM   3739 H  H    A LYS   A 1 163 ? 3.603  -6.429  1.167   0.30 20.99 ?  163  LYS   A H    1 
ATOM   3740 H  H    B LYS   A 1 163 ? 3.687  -6.954  0.912   0.70 23.43 ?  163  LYS   A H    1 
ATOM   3741 H  HA   A LYS   A 1 163 ? 2.634  -8.474  -0.167  0.30 21.55 ?  163  LYS   A HA   1 
ATOM   3742 H  HA   B LYS   A 1 163 ? 2.705  -9.062  -0.320  0.70 24.83 ?  163  LYS   A HA   1 
ATOM   3743 H  HB2  A LYS   A 1 163 ? 3.009  -6.429  -1.233  0.30 23.54 ?  163  LYS   A HB2  1 
ATOM   3744 H  HB2  B LYS   A 1 163 ? 3.089  -7.051  -1.450  0.70 29.85 ?  163  LYS   A HB2  1 
ATOM   3745 H  HB3  A LYS   A 1 163 ? 4.574  -6.632  -1.063  0.30 23.54 ?  163  LYS   A HB3  1 
ATOM   3746 H  HB3  B LYS   A 1 163 ? 4.651  -7.263  -1.281  0.70 29.85 ?  163  LYS   A HB3  1 
ATOM   3747 H  HG2  A LYS   A 1 163 ? 4.414  -8.525  -2.497  0.30 25.45 ?  163  LYS   A HG2  1 
ATOM   3748 H  HG2  B LYS   A 1 163 ? 4.724  -8.835  -2.838  0.70 34.95 ?  163  LYS   A HG2  1 
ATOM   3749 H  HG3  A LYS   A 1 163 ? 2.896  -8.129  -2.759  0.30 25.45 ?  163  LYS   A HG3  1 
ATOM   3750 H  HG3  B LYS   A 1 163 ? 3.168  -9.154  -2.706  0.70 34.95 ?  163  LYS   A HG3  1 
ATOM   3751 H  HD2  A LYS   A 1 163 ? 3.631  -6.087  -3.677  0.30 27.18 ?  163  LYS   A HD2  1 
ATOM   3752 H  HD2  B LYS   A 1 163 ? 2.740  -7.016  -3.676  0.70 39.91 ?  163  LYS   A HD2  1 
ATOM   3753 H  HD3  A LYS   A 1 163 ? 5.135  -6.577  -3.494  0.30 27.18 ?  163  LYS   A HD3  1 
ATOM   3754 H  HD3  B LYS   A 1 163 ? 4.299  -6.908  -3.978  0.70 39.91 ?  163  LYS   A HD3  1 
ATOM   3755 H  HE2  A LYS   A 1 163 ? 4.639  -8.381  -4.975  0.30 28.59 ?  163  LYS   A HE2  1 
ATOM   3756 H  HE2  B LYS   A 1 163 ? 4.049  -8.031  -5.785  0.70 44.05 ?  163  LYS   A HE2  1 
ATOM   3757 H  HE3  A LYS   A 1 163 ? 3.234  -7.701  -5.244  0.30 28.59 ?  163  LYS   A HE3  1 
ATOM   3758 H  HE3  B LYS   A 1 163 ? 3.385  -9.230  -4.979  0.70 44.05 ?  163  LYS   A HE3  1 
ATOM   3759 H  HZ1  A LYS   A 1 163 ? 4.719  -7.127  -6.863  0.30 29.41 ?  163  LYS   A HZ1  1 
ATOM   3760 H  HZ1  B LYS   A 1 163 ? 1.943  -8.430  -6.543  0.70 46.37 ?  163  LYS   A HZ1  1 
ATOM   3761 H  HZ2  A LYS   A 1 163 ? 4.329  -5.930  -6.145  0.30 29.41 ?  163  LYS   A HZ2  1 
ATOM   3762 H  HZ2  B LYS   A 1 163 ? 1.374  -8.192  -5.231  0.70 46.37 ?  163  LYS   A HZ2  1 
ATOM   3763 H  HZ3  A LYS   A 1 163 ? 5.620  -6.538  -5.893  0.30 29.41 ?  163  LYS   A HZ3  1 
ATOM   3764 H  HZ3  B LYS   A 1 163 ? 1.980  -7.100  -5.968  0.70 46.37 ?  163  LYS   A HZ3  1 
ATOM   3765 N  N    A LEU   A 1 164 ? 5.683  -8.755  0.751   0.30 16.27 ?  164  LEU   A N    1 
ATOM   3766 N  N    B LEU   A 1 164 ? 5.790  -9.260  0.546   0.70 17.44 ?  164  LEU   A N    1 
ATOM   3767 C  CA   A LEU   A 1 164 ? 6.772  -9.719  0.890   0.30 15.87 ?  164  LEU   A CA   1 
ATOM   3768 C  CA   B LEU   A 1 164 ? 6.877  -10.214 0.758   0.70 16.68 ?  164  LEU   A CA   1 
ATOM   3769 C  C    A LEU   A 1 164 ? 6.339  -10.925 1.712   0.30 16.08 ?  164  LEU   A C    1 
ATOM   3770 C  C    B LEU   A 1 164 ? 6.437  -11.353 1.667   0.70 16.42 ?  164  LEU   A C    1 
ATOM   3771 O  O    A LEU   A 1 164 ? 6.648  -12.069 1.362   0.30 16.41 ?  164  LEU   A O    1 
ATOM   3772 O  O    B LEU   A 1 164 ? 6.766  -12.518 1.418   0.70 17.19 ?  164  LEU   A O    1 
ATOM   3773 C  CB   A LEU   A 1 164 ? 7.981  -9.045  1.542   0.30 15.56 ?  164  LEU   A CB   1 
ATOM   3774 C  CB   B LEU   A 1 164 ? 8.089  -9.508  1.369   0.70 16.49 ?  164  LEU   A CB   1 
ATOM   3775 C  CG   A LEU   A 1 164 ? 8.725  -8.021  0.682   0.30 15.81 ?  164  LEU   A CG   1 
ATOM   3776 C  CG   B LEU   A 1 164 ? 8.824  -8.483  0.508   0.70 16.64 ?  164  LEU   A CG   1 
ATOM   3777 C  CD1  A LEU   A 1 164 ? 9.661  -7.165  1.528   0.30 15.88 ?  164  LEU   A CD1  1 
ATOM   3778 C  CD1  B LEU   A 1 164 ? 9.779  -7.644  1.346   0.70 16.78 ?  164  LEU   A CD1  1 
ATOM   3779 C  CD2  A LEU   A 1 164 ? 9.492  -8.714  -0.439  0.30 15.80 ?  164  LEU   A CD2  1 
ATOM   3780 C  CD2  B LEU   A 1 164 ? 9.569  -9.188  -0.605  0.70 17.12 ?  164  LEU   A CD2  1 
ATOM   3781 H  H    A LEU   A 1 164 ? 5.829  -7.995  1.121   0.30 19.55 ?  164  LEU   A H    1 
ATOM   3782 H  H    B LEU   A 1 164 ? 5.961  -8.471  0.814   0.70 20.95 ?  164  LEU   A H    1 
ATOM   3783 H  HA   A LEU   A 1 164 ? 7.037  -10.031 0.010   0.30 19.07 ?  164  LEU   A HA   1 
ATOM   3784 H  HA   B LEU   A 1 164 ? 7.139  -10.605 -0.092  0.70 20.04 ?  164  LEU   A HA   1 
ATOM   3785 H  HB2  A LEU   A 1 164 ? 7.679  -8.585  2.340   0.30 18.70 ?  164  LEU   A HB2  1 
ATOM   3786 H  HB2  B LEU   A 1 164 ? 7.793  -9.059  2.170   0.70 19.82 ?  164  LEU   A HB2  1 
ATOM   3787 H  HB3  A LEU   A 1 164 ? 8.618  -9.734  1.788   0.30 18.70 ?  164  LEU   A HB3  1 
ATOM   3788 H  HB3  B LEU   A 1 164 ? 8.736  -10.195 1.611   0.70 19.82 ?  164  LEU   A HB3  1 
ATOM   3789 H  HG   A LEU   A 1 164 ? 8.077  -7.431  0.271   0.30 19.00 ?  164  LEU   A HG   1 
ATOM   3790 H  HG   B LEU   A 1 164 ? 8.173  -7.888  0.108   0.70 19.99 ?  164  LEU   A HG   1 
ATOM   3791 H  HD11 A LEU   A 1 164 ? 10.116 -6.530  0.951   0.30 19.09 ?  164  LEU   A HD11 1 
ATOM   3792 H  HD11 B LEU   A 1 164 ? 10.226 -7.005  0.769   0.70 20.16 ?  164  LEU   A HD11 1 
ATOM   3793 H  HD12 A LEU   A 1 164 ? 9.138  -6.690  2.193   0.30 19.09 ?  164  LEU   A HD12 1 
ATOM   3794 H  HD12 B LEU   A 1 164 ? 9.276  -7.176  2.031   0.70 20.16 ?  164  LEU   A HD12 1 
ATOM   3795 H  HD13 A LEU   A 1 164 ? 10.309 -7.739  1.964   0.30 19.09 ?  164  LEU   A HD13 1 
ATOM   3796 H  HD13 B LEU   A 1 164 ? 10.435 -8.229  1.760   0.70 20.16 ?  164  LEU   A HD13 1 
ATOM   3797 H  HD21 A LEU   A 1 164 ? 10.007 -8.052  -0.926  0.30 18.99 ?  164  LEU   A HD21 1 
ATOM   3798 H  HD21 B LEU   A 1 164 ? 10.059 -8.529  -1.118  0.70 20.57 ?  164  LEU   A HD21 1 
ATOM   3799 H  HD22 A LEU   A 1 164 ? 10.086 -9.378  -0.054  0.30 18.99 ?  164  LEU   A HD22 1 
ATOM   3800 H  HD22 B LEU   A 1 164 ? 10.181 -9.832  -0.216  0.70 20.57 ?  164  LEU   A HD22 1 
ATOM   3801 H  HD23 A LEU   A 1 164 ? 8.859  -9.145  -1.036  0.30 18.99 ?  164  LEU   A HD23 1 
ATOM   3802 H  HD23 B LEU   A 1 164 ? 8.927  -9.642  -1.174  0.70 20.57 ?  164  LEU   A HD23 1 
ATOM   3803 N  N    A VAL   A 1 165 ? 5.627  -10.687 2.813   0.30 16.15 ?  165  VAL   A N    1 
ATOM   3804 N  N    B VAL   A 1 165 ? 5.697  -11.034 2.730   0.70 16.60 ?  165  VAL   A N    1 
ATOM   3805 C  CA   A VAL   A 1 165 ? 5.186  -11.785 3.667   0.30 16.28 ?  165  VAL   A CA   1 
ATOM   3806 C  CA   B VAL   A 1 165 ? 5.218  -12.063 3.649   0.70 16.53 ?  165  VAL   A CA   1 
ATOM   3807 C  C    A VAL   A 1 165 ? 4.126  -12.622 2.960   0.30 16.08 ?  165  VAL   A C    1 
ATOM   3808 C  C    B VAL   A 1 165 ? 4.205  -12.968 2.957   0.70 16.04 ?  165  VAL   A C    1 
ATOM   3809 O  O    A VAL   A 1 165 ? 4.231  -13.851 2.882   0.30 16.33 ?  165  VAL   A O    1 
ATOM   3810 O  O    B VAL   A 1 165 ? 4.292  -14.200 3.031   0.70 16.14 ?  165  VAL   A O    1 
ATOM   3811 C  CB   A VAL   A 1 165 ? 4.688  -11.239 5.018   0.30 16.94 ?  165  VAL   A CB   1 
ATOM   3812 C  CB   B VAL   A 1 165 ? 4.618  -11.408 4.908   0.70 18.15 ?  165  VAL   A CB   1 
ATOM   3813 C  CG1  A VAL   A 1 165 ? 3.942  -12.317 5.787   0.30 17.20 ?  165  VAL   A CG1  1 
ATOM   3814 C  CG1  B VAL   A 1 165 ? 3.878  -12.438 5.761   0.70 18.56 ?  165  VAL   A CG1  1 
ATOM   3815 C  CG2  A VAL   A 1 165 ? 5.857  -10.699 5.832   0.30 17.30 ?  165  VAL   A CG2  1 
ATOM   3816 C  CG2  B VAL   A 1 165 ? 5.699  -10.706 5.710   0.70 18.68 ?  165  VAL   A CG2  1 
ATOM   3817 H  H    A VAL   A 1 165 ? 5.388  -9.907  3.081   0.30 19.40 ?  165  VAL   A H    1 
ATOM   3818 H  H    B VAL   A 1 165 ? 5.458  -10.243 2.941   0.70 19.95 ?  165  VAL   A H    1 
ATOM   3819 H  HA   A VAL   A 1 165 ? 5.943  -12.360 3.848   0.30 19.56 ?  165  VAL   A HA   1 
ATOM   3820 H  HA   B VAL   A 1 165 ? 5.958  -12.620 3.929   0.70 19.85 ?  165  VAL   A HA   1 
ATOM   3821 H  HB   A VAL   A 1 165 ? 4.074  -10.505 4.858   0.30 20.36 ?  165  VAL   A HB   1 
ATOM   3822 H  HB   B VAL   A 1 165 ? 3.970  -10.742 4.632   0.70 21.80 ?  165  VAL   A HB   1 
ATOM   3823 H  HG11 A VAL   A 1 165 ? 3.882  -12.054 6.717   0.30 20.67 ?  165  VAL   A HG11 1 
ATOM   3824 H  HG11 B VAL   A 1 165 ? 3.751  -12.073 6.651   0.70 22.30 ?  165  VAL   A HG11 1 
ATOM   3825 H  HG12 A VAL   A 1 165 ? 3.051  -12.413 5.413   0.30 20.67 ?  165  VAL   A HG12 1 
ATOM   3826 H  HG12 B VAL   A 1 165 ? 3.014  -12.625 5.358   0.70 22.30 ?  165  VAL   A HG12 1 
ATOM   3827 H  HG13 A VAL   A 1 165 ? 4.429  -13.151 5.709   0.30 20.67 ?  165  VAL   A HG13 1 
ATOM   3828 H  HG13 B VAL   A 1 165 ? 4.406  -13.248 5.809   0.70 22.30 ?  165  VAL   A HG13 1 
ATOM   3829 H  HG21 A VAL   A 1 165 ? 5.531  -10.389 6.691   0.30 20.78 ?  165  VAL   A HG21 1 
ATOM   3830 H  HG21 B VAL   A 1 165 ? 5.298  -10.289 6.488   0.70 22.44 ?  165  VAL   A HG21 1 
ATOM   3831 H  HG22 A VAL   A 1 165 ? 6.508  -11.407 5.961   0.30 20.78 ?  165  VAL   A HG22 1 
ATOM   3832 H  HG22 B VAL   A 1 165 ? 6.362  -11.357 5.987   0.70 22.44 ?  165  VAL   A HG22 1 
ATOM   3833 H  HG23 A VAL   A 1 165 ? 6.265  -9.961  5.349   0.30 20.78 ?  165  VAL   A HG23 1 
ATOM   3834 H  HG23 B VAL   A 1 165 ? 6.115  -10.029 5.150   0.70 22.44 ?  165  VAL   A HG23 1 
ATOM   3835 N  N    A SER   A 1 166 ? 3.093  -11.969 2.425   0.30 16.30 ?  166  SER   A N    1 
ATOM   3836 N  N    B SER   A 1 166 ? 3.229  -12.371 2.270   0.70 16.78 ?  166  SER   A N    1 
ATOM   3837 C  CA   A SER   A 1 166 ? 1.983  -12.695 1.815   0.30 16.91 ?  166  SER   A CA   1 
ATOM   3838 C  CA   B SER   A 1 166 ? 2.105  -13.148 1.759   0.70 17.96 ?  166  SER   A CA   1 
ATOM   3839 C  C    A SER   A 1 166 ? 2.392  -13.472 0.570   0.30 16.62 ?  166  SER   A C    1 
ATOM   3840 C  C    B SER   A 1 166 ? 2.536  -14.129 0.682   0.70 18.03 ?  166  SER   A C    1 
ATOM   3841 O  O    A SER   A 1 166 ? 1.681  -14.407 0.184   0.30 16.89 ?  166  SER   A O    1 
ATOM   3842 O  O    B SER   A 1 166 ? 1.958  -15.215 0.574   0.70 18.44 ?  166  SER   A O    1 
ATOM   3843 C  CB   A SER   A 1 166 ? 0.855  -11.729 1.453   0.30 18.09 ?  166  SER   A CB   1 
ATOM   3844 C  CB   B SER   A 1 166 ? 1.028  -12.216 1.206   0.70 20.26 ?  166  SER   A CB   1 
ATOM   3845 O  OG   A SER   A 1 166 ? 0.284  -11.138 2.610   0.30 19.31 ?  166  SER   A OG   1 
ATOM   3846 O  OG   B SER   A 1 166 ? 0.742  -11.185 2.127   0.70 23.48 ?  166  SER   A OG   1 
ATOM   3847 H  H    A SER   A 1 166 ? 3.007  -11.117 2.413   0.30 19.58 ?  166  SER   A H    1 
ATOM   3848 H  H    B SER   A 1 166 ? 3.196  -11.547 2.081   0.70 20.16 ?  166  SER   A H    1 
ATOM   3849 H  HA   A SER   A 1 166 ? 1.633  -13.333 2.458   0.30 20.32 ?  166  SER   A HA   1 
ATOM   3850 H  HA   B SER   A 1 166 ? 1.706  -13.666 2.479   0.70 21.58 ?  166  SER   A HA   1 
ATOM   3851 H  HB2  A SER   A 1 166 ? 1.216  -11.028 0.886   0.30 21.73 ?  166  SER   A HB2  1 
ATOM   3852 H  HB2  B SER   A 1 166 ? 1.342  -11.826 0.375   0.70 24.34 ?  166  SER   A HB2  1 
ATOM   3853 H  HB3  A SER   A 1 166 ? 0.166  -12.216 0.977   0.30 21.73 ?  166  SER   A HB3  1 
ATOM   3854 H  HB3  B SER   A 1 166 ? 0.214  -12.726 1.039   0.70 24.34 ?  166  SER   A HB3  1 
ATOM   3855 H  HG   A SER   A 1 166 ? 0.877  -10.712 3.028   0.30 23.19 ?  166  SER   A HG   1 
ATOM   3856 H  HG   B SER   A 1 166 ? 1.420  -10.706 2.244   0.70 28.20 ?  166  SER   A HG   1 
ATOM   3857 N  N    A SER   A 1 167 ? 3.502  -13.110 -0.073  0.30 16.33 ?  167  SER   A N    1 
ATOM   3858 N  N    B SER   A 1 167 ? 3.538  -13.773 -0.115  0.70 17.96 ?  167  SER   A N    1 
ATOM   3859 C  CA   A SER   A 1 167 ? 3.954  -13.791 -1.279  0.30 16.33 ?  167  SER   A CA   1 
ATOM   3860 C  CA   B SER   A 1 167 ? 3.964  -14.585 -1.242  0.70 18.46 ?  167  SER   A CA   1 
ATOM   3861 C  C    A SER   A 1 167 ? 5.148  -14.704 -1.042  0.30 16.49 ?  167  SER   A C    1 
ATOM   3862 C  C    B SER   A 1 167 ? 5.100  -15.537 -0.897  0.70 18.35 ?  167  SER   A C    1 
ATOM   3863 O  O    A SER   A 1 167 ? 5.677  -15.263 -2.009  0.30 16.70 ?  167  SER   A O    1 
ATOM   3864 O  O    B SER   A 1 167 ? 5.673  -16.143 -1.805  0.70 19.10 ?  167  SER   A O    1 
ATOM   3865 C  CB   A SER   A 1 167 ? 4.309  -12.775 -2.372  0.30 16.28 ?  167  SER   A CB   1 
ATOM   3866 C  CB   B SER   A 1 167 ? 4.372  -13.681 -2.411  0.70 19.25 ?  167  SER   A CB   1 
ATOM   3867 O  OG   A SER   A 1 167 ? 5.376  -11.938 -1.962  0.30 16.45 ?  167  SER   A OG   1 
ATOM   3868 O  OG   B SER   A 1 167 ? 5.504  -12.890 -2.078  0.70 19.62 ?  167  SER   A OG   1 
ATOM   3869 H  H    A SER   A 1 167 ? 4.013  -12.465 0.170   0.30 19.62 ?  167  SER   A H    1 
ATOM   3870 H  H    B SER   A 1 167 ? 3.989  -13.050 -0.020  0.70 21.57 ?  167  SER   A H    1 
ATOM   3871 H  HA   A SER   A 1 167 ? 3.231  -14.341 -1.619  0.30 19.62 ?  167  SER   A HA   1 
ATOM   3872 H  HA   B SER   A 1 167 ? 3.223  -15.128 -1.539  0.70 22.18 ?  167  SER   A HA   1 
ATOM   3873 H  HB2  A SER   A 1 167 ? 4.575  -13.257 -3.174  0.30 19.56 ?  167  SER   A HB2  1 
ATOM   3874 H  HB2  B SER   A 1 167 ? 4.584  -14.233 -3.181  0.70 23.12 ?  167  SER   A HB2  1 
ATOM   3875 H  HB3  A SER   A 1 167 ? 3.530  -12.230 -2.558  0.30 19.56 ?  167  SER   A HB3  1 
ATOM   3876 H  HB3  B SER   A 1 167 ? 3.625  -13.094 -2.627  0.70 23.12 ?  167  SER   A HB3  1 
ATOM   3877 H  HG   A SER   A 1 167 ? 5.163  -11.529 -1.261  0.30 19.76 ?  167  SER   A HG   1 
ATOM   3878 H  HG   B SER   A 1 167 ? 5.325  -12.402 -1.421  0.70 23.57 ?  167  SER   A HG   1 
ATOM   3879 N  N    A PHE   A 1 168 ? 5.591  -14.871 0.203   0.30 16.59 ?  168  PHE   A N    1 
ATOM   3880 N  N    B PHE   A 1 168 ? 5.409  -15.728 0.389   0.70 18.22 ?  168  PHE   A N    1 
ATOM   3881 C  CA   A PHE   A 1 168 ? 6.778  -15.670 0.471   0.30 17.34 ?  168  PHE   A CA   1 
ATOM   3882 C  CA   B PHE   A 1 168 ? 6.673  -16.372 0.733   0.70 18.05 ?  168  PHE   A CA   1 
ATOM   3883 C  C    A PHE   A 1 168 ? 6.450  -17.153 0.377   0.30 18.89 ?  168  PHE   A C    1 
ATOM   3884 C  C    B PHE   A 1 168 ? 6.642  -17.893 0.580   0.70 19.88 ?  168  PHE   A C    1 
ATOM   3885 O  O    A PHE   A 1 168 ? 5.447  -17.614 0.931   0.30 19.29 ?  168  PHE   A O    1 
ATOM   3886 O  O    B PHE   A 1 168 ? 7.561  -18.470 -0.012  0.70 19.81 ?  168  PHE   A O    1 
ATOM   3887 C  CB   A PHE   A 1 168 ? 7.352  -15.354 1.851   0.30 16.42 ?  168  PHE   A CB   1 
ATOM   3888 C  CB   B PHE   A 1 168 ? 7.146  -15.992 2.134   0.70 17.88 ?  168  PHE   A CB   1 
ATOM   3889 C  CG   A PHE   A 1 168 ? 8.595  -16.137 2.176   0.30 15.57 ?  168  PHE   A CG   1 
ATOM   3890 C  CG   B PHE   A 1 168 ? 8.500  -16.553 2.463   0.70 17.42 ?  168  PHE   A CG   1 
ATOM   3891 C  CD1  A PHE   A 1 168 ? 9.800  -15.822 1.572   0.30 15.25 ?  168  PHE   A CD1  1 
ATOM   3892 C  CD1  B PHE   A 1 168 ? 9.630  -16.061 1.837   0.70 17.51 ?  168  PHE   A CD1  1 
ATOM   3893 C  CD2  A PHE   A 1 168 ? 8.557  -17.195 3.071   0.30 15.09 ?  168  PHE   A CD2  1 
ATOM   3894 C  CD2  B PHE   A 1 168 ? 8.640  -17.593 3.362   0.70 16.89 ?  168  PHE   A CD2  1 
ATOM   3895 C  CE1  A PHE   A 1 168 ? 10.943 -16.541 1.856   0.30 14.81 ?  168  PHE   A CE1  1 
ATOM   3896 C  CE1  B PHE   A 1 168 ? 10.874 -16.580 2.114   0.70 17.45 ?  168  PHE   A CE1  1 
ATOM   3897 C  CE2  A PHE   A 1 168 ? 9.703  -17.918 3.359   0.30 14.74 ?  168  PHE   A CE2  1 
ATOM   3898 C  CE2  B PHE   A 1 168 ? 9.890  -18.116 3.645   0.70 16.96 ?  168  PHE   A CE2  1 
ATOM   3899 C  CZ   A PHE   A 1 168 ? 10.896 -17.588 2.751   0.30 14.56 ?  168  PHE   A CZ   1 
ATOM   3900 C  CZ   B PHE   A 1 168 ? 11.006 -17.608 3.017   0.70 17.42 ?  168  PHE   A CZ   1 
ATOM   3901 H  H    A PHE   A 1 168 ? 5.221  -14.537 0.904   0.30 19.93 ?  168  PHE   A H    1 
ATOM   3902 H  H    B PHE   A 1 168 ? 4.918  -15.506 1.055   0.70 21.89 ?  168  PHE   A H    1 
ATOM   3903 H  HA   A PHE   A 1 168 ? 7.453  -15.470 -0.192  0.30 20.83 ?  168  PHE   A HA   1 
ATOM   3904 H  HA   B PHE   A 1 168 ? 7.347  -16.048 0.116   0.70 21.69 ?  168  PHE   A HA   1 
ATOM   3905 H  HB2  A PHE   A 1 168 ? 7.574  -14.410 1.886   0.30 19.73 ?  168  PHE   A HB2  1 
ATOM   3906 H  HB2  B PHE   A 1 168 ? 7.201  -15.027 2.196   0.70 21.48 ?  168  PHE   A HB2  1 
ATOM   3907 H  HB3  A PHE   A 1 168 ? 6.683  -15.559 2.524   0.30 19.73 ?  168  PHE   A HB3  1 
ATOM   3908 H  HB3  B PHE   A 1 168 ? 6.517  -16.336 2.785   0.70 21.48 ?  168  PHE   A HB3  1 
ATOM   3909 H  HD1  A PHE   A 1 168 ? 9.838  -15.115 0.968   0.30 18.33 ?  168  PHE   A HD1  1 
ATOM   3910 H  HD1  B PHE   A 1 168 ? 9.551  -15.365 1.224   0.70 21.03 ?  168  PHE   A HD1  1 
ATOM   3911 H  HD2  A PHE   A 1 168 ? 7.754  -17.421 3.483   0.30 18.13 ?  168  PHE   A HD2  1 
ATOM   3912 H  HD2  B PHE   A 1 168 ? 7.887  -17.942 3.783   0.70 20.30 ?  168  PHE   A HD2  1 
ATOM   3913 H  HE1  A PHE   A 1 168 ? 11.748 -16.315 1.447   0.30 17.80 ?  168  PHE   A HE1  1 
ATOM   3914 H  HE1  B PHE   A 1 168 ? 11.629 -16.232 1.691   0.70 20.96 ?  168  PHE   A HE1  1 
ATOM   3915 H  HE2  A PHE   A 1 168 ? 9.668  -18.625 3.963   0.30 17.71 ?  168  PHE   A HE2  1 
ATOM   3916 H  HE2  B PHE   A 1 168 ? 9.973  -18.815 4.254   0.70 20.38 ?  168  PHE   A HE2  1 
ATOM   3917 H  HZ   A PHE   A 1 168 ? 11.668 -18.072 2.945   0.30 17.50 ?  168  PHE   A HZ   1 
ATOM   3918 H  HZ   B PHE   A 1 168 ? 11.848 -17.959 3.208   0.70 20.93 ?  168  PHE   A HZ   1 
ATOM   3919 N  N    A LEU   A 1 169 ? 7.302  -17.897 -0.321  0.30 19.76 ?  169  LEU   A N    1 
ATOM   3920 N  N    B LEU   A 1 169 ? 5.649  -18.569 1.150   0.70 22.10 ?  169  LEU   A N    1 
ATOM   3921 C  CA   A LEU   A 1 169 ? 7.126  -19.337 -0.465  0.30 20.59 ?  169  LEU   A CA   1 
ATOM   3922 C  CA   B LEU   A 1 169 ? 5.663  -20.037 1.141   0.70 25.04 ?  169  LEU   A CA   1 
ATOM   3923 C  C    A LEU   A 1 169 ? 7.999  -20.089 0.538   0.30 20.57 ?  169  LEU   A C    1 
ATOM   3924 C  C    B LEU   A 1 169 ? 4.934  -20.646 -0.054  0.70 27.16 ?  169  LEU   A C    1 
ATOM   3925 O  O    A LEU   A 1 169 ? 7.503  -20.531 1.575   0.30 20.91 ?  169  LEU   A O    1 
ATOM   3926 O  O    B LEU   A 1 169 ? 5.387  -21.650 -0.610  0.70 28.49 ?  169  LEU   A O    1 
ATOM   3927 C  CB   A LEU   A 1 169 ? 7.443  -19.768 -1.901  0.30 21.16 ?  169  LEU   A CB   1 
ATOM   3928 C  CB   B LEU   A 1 169 ? 5.090  -20.601 2.445   0.70 26.09 ?  169  LEU   A CB   1 
ATOM   3929 C  CG   A LEU   A 1 169 ? 7.127  -21.218 -2.277  0.30 21.62 ?  169  LEU   A CG   1 
ATOM   3930 C  CG   B LEU   A 1 169 ? 4.986  -22.130 2.531   0.70 27.19 ?  169  LEU   A CG   1 
ATOM   3931 C  CD1  A LEU   A 1 169 ? 5.691  -21.566 -1.923  0.30 21.88 ?  169  LEU   A CD1  1 
ATOM   3932 C  CD1  B LEU   A 1 169 ? 6.317  -22.812 2.236   0.70 28.35 ?  169  LEU   A CD1  1 
ATOM   3933 C  CD2  A LEU   A 1 169 ? 7.380  -21.447 -3.761  0.30 21.51 ?  169  LEU   A CD2  1 
ATOM   3934 C  CD2  B LEU   A 1 169 ? 4.457  -22.557 3.897   0.70 27.28 ?  169  LEU   A CD2  1 
ATOM   3935 O  OXT  A LEU   A 1 169 ? 9.205  -20.270 0.358   0.30 20.08 -1 169  LEU   A OXT  1 
ATOM   3936 O  OXT  B LEU   A 1 169 ? 3.888  -20.165 -0.486  0.70 27.41 -1 169  LEU   A OXT  1 
ATOM   3937 H  H    A LEU   A 1 169 ? 7.995  -17.589 -0.729  0.30 23.74 ?  169  LEU   A H    1 
ATOM   3938 H  H    B LEU   A 1 169 ? 4.979  -18.213 1.551   0.70 26.54 ?  169  LEU   A H    1 
ATOM   3939 H  HA   A LEU   A 1 169 ? 6.207  -19.565 -0.274  0.30 24.73 ?  169  LEU   A HA   1 
ATOM   3940 H  HA   B LEU   A 1 169 ? 6.585  -20.325 1.085   0.70 30.08 ?  169  LEU   A HA   1 
ATOM   3941 H  HB2  A LEU   A 1 169 ? 6.935  -19.203 -2.505  0.30 25.42 ?  169  LEU   A HB2  1 
ATOM   3942 H  HB2  B LEU   A 1 169 ? 5.658  -20.311 3.174   0.70 31.33 ?  169  LEU   A HB2  1 
ATOM   3943 H  HB3  A LEU   A 1 169 ? 8.390  -19.635 -2.059  0.30 25.42 ?  169  LEU   A HB3  1 
ATOM   3944 H  HB3  B LEU   A 1 169 ? 4.198  -20.245 2.567   0.70 31.33 ?  169  LEU   A HB3  1 
ATOM   3945 H  HG   A LEU   A 1 169 ? 7.712  -21.811 -1.780  0.30 25.97 ?  169  LEU   A HG   1 
ATOM   3946 H  HG   B LEU   A 1 169 ? 4.347  -22.435 1.870   0.70 32.65 ?  169  LEU   A HG   1 
ATOM   3947 H  HD11 A LEU   A 1 169 ? 5.459  -22.411 -2.339  0.30 26.28 ?  169  LEU   A HD11 1 
ATOM   3948 H  HD11 B LEU   A 1 169 ? 6.172  -23.769 2.192   0.70 34.05 ?  169  LEU   A HD11 1 
ATOM   3949 H  HD12 A LEU   A 1 169 ? 5.612  -21.640 -0.959  0.30 26.28 ?  169  LEU   A HD12 1 
ATOM   3950 H  HD12 B LEU   A 1 169 ? 6.662  -22.494 1.388   0.70 34.05 ?  169  LEU   A HD12 1 
ATOM   3951 H  HD13 A LEU   A 1 169 ? 5.107  -20.865 -2.252  0.30 26.28 ?  169  LEU   A HD13 1 
ATOM   3952 H  HD13 B LEU   A 1 169 ? 6.940  -22.610 2.947   0.70 34.05 ?  169  LEU   A HD13 1 
ATOM   3953 H  HD21 A LEU   A 1 169 ? 7.178  -22.372 -3.978  0.30 25.83 ?  169  LEU   A HD21 1 
ATOM   3954 H  HD21 B LEU   A 1 169 ? 4.399  -23.525 3.923   0.70 32.76 ?  169  LEU   A HD21 1 
ATOM   3955 H  HD22 A LEU   A 1 169 ? 6.806  -20.856 -4.274  0.30 25.83 ?  169  LEU   A HD22 1 
ATOM   3956 H  HD22 B LEU   A 1 169 ? 5.067  -22.243 4.583   0.70 32.76 ?  169  LEU   A HD22 1 
ATOM   3957 H  HD23 A LEU   A 1 169 ? 8.310  -21.257 -3.957  0.30 25.83 ?  169  LEU   A HD23 1 
ATOM   3958 H  HD23 B LEU   A 1 169 ? 3.580  -22.168 4.031   0.70 32.76 ?  169  LEU   A HD23 1 
ATOM   3959 N  N    A SER   B 1 1   ? 50.797 -9.157  -23.655 0.30 29.84 ?  1    SER   B N    1 
ATOM   3960 N  N    B SER   B 1 1   ? 50.811 -9.252  -23.755 0.70 29.45 ?  1    SER   B N    1 
ATOM   3961 C  CA   A SER   B 1 1   ? 51.362 -10.250 -22.838 0.30 29.60 ?  1    SER   B CA   1 
ATOM   3962 C  CA   B SER   B 1 1   ? 51.296 -10.264 -22.798 0.70 29.10 ?  1    SER   B CA   1 
ATOM   3963 C  C    A SER   B 1 1   ? 50.321 -11.333 -22.612 0.30 28.56 ?  1    SER   B C    1 
ATOM   3964 C  C    B SER   B 1 1   ? 50.219 -11.304 -22.531 0.70 27.13 ?  1    SER   B C    1 
ATOM   3965 O  O    A SER   B 1 1   ? 49.142 -11.159 -22.926 0.30 28.37 ?  1    SER   B O    1 
ATOM   3966 O  O    B SER   B 1 1   ? 49.044 -11.135 -22.886 0.70 26.26 ?  1    SER   B O    1 
ATOM   3967 C  CB   A SER   B 1 1   ? 51.860 -9.714  -21.499 0.30 29.89 ?  1    SER   B CB   1 
ATOM   3968 C  CB   B SER   B 1 1   ? 51.732 -9.613  -21.489 0.70 29.82 ?  1    SER   B CB   1 
ATOM   3969 O  OG   A SER   B 1 1   ? 50.776 -9.327  -20.676 0.30 30.75 ?  1    SER   B OG   1 
ATOM   3970 O  OG   B SER   B 1 1   ? 50.649 -9.539  -20.581 0.70 31.54 ?  1    SER   B OG   1 
ATOM   3971 H  H1   A SER   B 1 1   ? 50.494 -9.494  -24.418 0.30 35.83 ?  1    SER   B H1   1 
ATOM   3972 H  H1   B SER   B 1 1   ? 51.509 -8.824  -24.096 0.70 35.37 ?  1    SER   B H1   1 
ATOM   3973 H  H2   A SER   B 1 1   ? 50.134 -8.774  -23.208 0.30 35.83 ?  1    SER   B H2   1 
ATOM   3974 H  H2   B SER   B 1 1   ? 50.361 -9.661  -24.402 0.70 35.37 ?  1    SER   B H2   1 
ATOM   3975 H  H3   A SER   B 1 1   ? 51.436 -8.564  -23.819 0.30 35.83 ?  1    SER   B H3   1 
ATOM   3976 H  H3   B SER   B 1 1   ? 50.282 -8.684  -23.330 0.70 35.37 ?  1    SER   B H3   1 
ATOM   3977 H  HA   A SER   B 1 1   ? 52.106 -10.636 -23.314 0.30 35.55 ?  1    SER   B HA   1 
ATOM   3978 H  HA   B SER   B 1 1   ? 52.059 -10.710 -23.187 0.70 34.94 ?  1    SER   B HA   1 
ATOM   3979 H  HB2  A SER   B 1 1   ? 52.370 -10.411 -21.060 0.30 35.89 ?  1    SER   B HB2  1 
ATOM   3980 H  HB2  B SER   B 1 1   ? 52.446 -10.144 -21.102 0.70 35.81 ?  1    SER   B HB2  1 
ATOM   3981 H  HB3  A SER   B 1 1   ? 52.421 -8.940  -21.658 0.30 35.89 ?  1    SER   B HB3  1 
ATOM   3982 H  HB3  B SER   B 1 1   ? 52.050 -8.714  -21.671 0.70 35.81 ?  1    SER   B HB3  1 
ATOM   3983 H  HG   A SER   B 1 1   ? 51.045 -8.798  -20.083 0.30 36.93 ?  1    SER   B HG   1 
ATOM   3984 H  HG   B SER   B 1 1   ? 50.768 -8.898  -20.051 0.70 37.87 ?  1    SER   B HG   1 
ATOM   3985 N  N    A MET   B 1 2   ? 50.770 -12.450 -22.053 0.30 27.44 ?  2    MET   B N    1 
ATOM   3986 N  N    B MET   B 1 2   ? 50.641 -12.383 -21.886 0.70 25.80 ?  2    MET   B N    1 
ATOM   3987 C  CA   A MET   B 1 2   ? 49.946 -13.633 -21.867 0.30 26.67 ?  2    MET   B CA   1 
ATOM   3988 C  CA   B MET   B 1 2   ? 49.840 -13.590 -21.727 0.70 25.23 ?  2    MET   B CA   1 
ATOM   3989 C  C    A MET   B 1 2   ? 49.720 -13.829 -20.375 0.30 23.99 ?  2    MET   B C    1 
ATOM   3990 C  C    B MET   B 1 2   ? 49.603 -13.785 -20.236 0.70 22.80 ?  2    MET   B C    1 
ATOM   3991 O  O    A MET   B 1 2   ? 50.676 -14.031 -19.619 0.30 23.64 ?  2    MET   B O    1 
ATOM   3992 O  O    B MET   B 1 2   ? 50.525 -14.149 -19.500 0.70 23.35 ?  2    MET   B O    1 
ATOM   3993 C  CB   A MET   B 1 2   ? 50.640 -14.847 -22.478 0.30 28.84 ?  2    MET   B CB   1 
ATOM   3994 C  CB   B MET   B 1 2   ? 50.603 -14.760 -22.322 0.70 28.27 ?  2    MET   B CB   1 
ATOM   3995 C  CG   A MET   B 1 2   ? 49.758 -16.074 -22.628 0.30 30.89 ?  2    MET   B CG   1 
ATOM   3996 C  CG   B MET   B 1 2   ? 49.762 -15.957 -22.742 0.70 31.06 ?  2    MET   B CG   1 
ATOM   3997 S  SD   A MET   B 1 2   ? 50.567 -17.376 -23.575 0.30 32.97 ?  2    MET   B SD   1 
ATOM   3998 S  SD   B MET   B 1 2   ? 50.686 -17.011 -23.872 0.70 33.72 ?  2    MET   B SD   1 
ATOM   3999 C  CE   A MET   B 1 2   ? 51.160 -16.415 -24.966 0.30 33.13 ?  2    MET   B CE   1 
ATOM   4000 C  CE   B MET   B 1 2   ? 51.483 -15.772 -24.873 0.70 34.29 ?  2    MET   B CE   1 
ATOM   4001 H  H    A MET   B 1 2   ? 51.572 -12.548 -21.760 0.30 32.95 ?  2    MET   B H    1 
ATOM   4002 H  H    B MET   B 1 2   ? 51.416 -12.451 -21.517 0.70 30.99 ?  2    MET   B H    1 
ATOM   4003 H  HA   A MET   B 1 2   ? 49.093 -13.520 -22.314 0.30 32.03 ?  2    MET   B HA   1 
ATOM   4004 H  HA   B MET   B 1 2   ? 48.998 -13.505 -22.202 0.70 30.30 ?  2    MET   B HA   1 
ATOM   4005 H  HB2  A MET   B 1 2   ? 50.953 -14.580 -23.355 0.30 34.63 ?  2    MET   B HB2  1 
ATOM   4006 H  HB2  B MET   B 1 2   ? 51.068 -14.390 -23.081 0.70 33.95 ?  2    MET   B HB2  1 
ATOM   4007 H  HB3  A MET   B 1 2   ? 51.393 -15.100 -21.926 0.30 34.63 ?  2    MET   B HB3  1 
ATOM   4008 H  HB3  B MET   B 1 2   ? 51.248 -15.095 -21.690 0.70 33.95 ?  2    MET   B HB3  1 
ATOM   4009 H  HG2  A MET   B 1 2   ? 49.550 -16.420 -21.746 0.30 37.09 ?  2    MET   B HG2  1 
ATOM   4010 H  HG2  B MET   B 1 2   ? 49.527 -16.480 -21.954 0.70 37.30 ?  2    MET   B HG2  1 
ATOM   4011 H  HG3  A MET   B 1 2   ? 48.945 -15.832 -23.095 0.30 37.09 ?  2    MET   B HG3  1 
ATOM   4012 H  HG3  B MET   B 1 2   ? 48.963 -15.665 -23.199 0.70 37.30 ?  2    MET   B HG3  1 
ATOM   4013 H  HE1  A MET   B 1 2   ? 51.326 -17.008 -25.706 0.30 39.78 ?  2    MET   B HE1  1 
ATOM   4014 H  HE1  B MET   B 1 2   ? 51.709 -16.177 -25.700 0.70 41.17 ?  2    MET   B HE1  1 
ATOM   4015 H  HE2  A MET   B 1 2   ? 50.479 -15.762 -25.204 0.30 39.78 ?  2    MET   B HE2  1 
ATOM   4016 H  HE2  B MET   B 1 2   ? 50.863 -15.036 -25.023 0.70 41.17 ?  2    MET   B HE2  1 
ATOM   4017 H  HE3  A MET   B 1 2   ? 51.980 -15.953 -24.717 0.30 39.78 ?  2    MET   B HE3  1 
ATOM   4018 H  HE3  B MET   B 1 2   ? 52.286 -15.448 -24.419 0.70 41.17 ?  2    MET   B HE3  1 
ATOM   4019 N  N    A VAL   B 1 3   ? 48.459 -13.732 -19.955 0.30 21.74 ?  3    VAL   B N    1 
ATOM   4020 N  N    B VAL   B 1 3   ? 48.382 -13.504 -19.791 0.70 20.57 ?  3    VAL   B N    1 
ATOM   4021 C  CA   A VAL   B 1 3   ? 48.055 -13.971 -18.578 0.30 19.90 ?  3    VAL   B CA   1 
ATOM   4022 C  CA   B VAL   B 1 3   ? 47.947 -13.795 -18.432 0.70 19.94 ?  3    VAL   B CA   1 
ATOM   4023 C  C    A VAL   B 1 3   ? 46.827 -14.870 -18.599 0.30 17.87 ?  3    VAL   B C    1 
ATOM   4024 C  C    B VAL   B 1 3   ? 46.719 -14.692 -18.495 0.70 18.42 ?  3    VAL   B C    1 
ATOM   4025 O  O    A VAL   B 1 3   ? 46.148 -15.009 -19.618 0.30 17.29 ?  3    VAL   B O    1 
ATOM   4026 O  O    B VAL   B 1 3   ? 45.951 -14.674 -19.461 0.70 18.86 ?  3    VAL   B O    1 
ATOM   4027 C  CB   A VAL   B 1 3   ? 47.763 -12.656 -17.821 0.30 20.51 ?  3    VAL   B CB   1 
ATOM   4028 C  CB   B VAL   B 1 3   ? 47.669 -12.516 -17.606 0.70 21.47 ?  3    VAL   B CB   1 
ATOM   4029 C  CG1  A VAL   B 1 3   ? 49.017 -11.791 -17.745 0.30 20.94 ?  3    VAL   B CG1  1 
ATOM   4030 C  CG1  B VAL   B 1 3   ? 48.930 -11.663 -17.492 0.70 22.33 ?  3    VAL   B CG1  1 
ATOM   4031 C  CG2  A VAL   B 1 3   ? 46.625 -11.899 -18.489 0.30 20.59 ?  3    VAL   B CG2  1 
ATOM   4032 C  CG2  B VAL   B 1 3   ? 46.522 -11.717 -18.212 0.70 21.48 ?  3    VAL   B CG2  1 
ATOM   4033 H  H    A VAL   B 1 3   ? 47.804 -13.510 -20.467 0.30 26.11 ?  3    VAL   B H    1 
ATOM   4034 H  H    B VAL   B 1 3   ? 47.779 -13.118 -20.270 0.70 24.71 ?  3    VAL   B H    1 
ATOM   4035 H  HA   A VAL   B 1 3   ? 48.764 -14.437 -18.110 0.30 23.91 ?  3    VAL   B HA   1 
ATOM   4036 H  HA   B VAL   B 1 3   ? 48.644 -14.286 -17.977 0.70 23.95 ?  3    VAL   B HA   1 
ATOM   4037 H  HB   A VAL   B 1 3   ? 47.492 -12.866 -16.913 0.30 24.63 ?  3    VAL   B HB   1 
ATOM   4038 H  HB   B VAL   B 1 3   ? 47.410 -12.772 -16.707 0.70 25.78 ?  3    VAL   B HB   1 
ATOM   4039 H  HG11 A VAL   B 1 3   ? 48.814 -10.981 -17.249 0.30 25.15 ?  3    VAL   B HG11 1 
ATOM   4040 H  HG11 B VAL   B 1 3   ? 48.734 -10.877 -16.956 0.70 26.83 ?  3    VAL   B HG11 1 
ATOM   4041 H  HG12 A VAL   B 1 3   ? 49.717 -12.287 -17.292 0.30 25.15 ?  3    VAL   B HG12 1 
ATOM   4042 H  HG12 B VAL   B 1 3   ? 49.627 -12.186 -17.067 0.70 26.83 ?  3    VAL   B HG12 1 
ATOM   4043 H  HG13 A VAL   B 1 3   ? 49.301 -11.565 -18.644 0.30 25.15 ?  3    VAL   B HG13 1 
ATOM   4044 H  HG13 B VAL   B 1 3   ? 49.211 -11.395 -18.380 0.70 26.83 ?  3    VAL   B HG13 1 
ATOM   4045 H  HG21 A VAL   B 1 3   ? 46.560 -11.017 -18.094 0.30 24.73 ?  3    VAL   B HG21 1 
ATOM   4046 H  HG21 B VAL   B 1 3   ? 46.475 -10.851 -17.778 0.70 25.80 ?  3    VAL   B HG21 1 
ATOM   4047 H  HG22 A VAL   B 1 3   ? 46.811 -11.823 -19.438 0.30 24.73 ?  3    VAL   B HG22 1 
ATOM   4048 H  HG22 B VAL   B 1 3   ? 46.683 -11.605 -19.161 0.70 25.80 ?  3    VAL   B HG22 1 
ATOM   4049 H  HG23 A VAL   B 1 3   ? 45.798 -12.385 -18.351 0.30 24.73 ?  3    VAL   B HG23 1 
ATOM   4050 H  HG23 B VAL   B 1 3   ? 45.693 -12.202 -18.071 0.70 25.80 ?  3    VAL   B HG23 1 
ATOM   4051 N  N    . ASN   B 1 4   ? 46.554 -15.501 -17.457 1.00 16.39 ?  4    ASN   B N    1 
ATOM   4052 C  CA   . ASN   B 1 4   ? 45.414 -16.412 -17.345 1.00 14.95 ?  4    ASN   B CA   1 
ATOM   4053 C  C    . ASN   B 1 4   ? 45.364 -17.377 -18.530 1.00 15.30 ?  4    ASN   B C    1 
ATOM   4054 O  O    . ASN   B 1 4   ? 44.305 -17.631 -19.100 1.00 16.22 ?  4    ASN   B O    1 
ATOM   4055 C  CB   . ASN   B 1 4   ? 44.092 -15.654 -17.195 1.00 14.20 ?  4    ASN   B CB   1 
ATOM   4056 C  CG   . ASN   B 1 4   ? 44.032 -14.845 -15.919 1.00 13.49 ?  4    ASN   B CG   1 
ATOM   4057 O  OD1  . ASN   B 1 4   ? 44.317 -15.353 -14.838 1.00 13.35 ?  4    ASN   B OD1  1 
ATOM   4058 N  ND2  . ASN   B 1 4   ? 43.680 -13.569 -16.041 1.00 14.35 ?  4    ASN   B ND2  1 
ATOM   4059 H  H    A ASN   B 1 4   ? 47.018 -15.426 -16.739 0.30 19.69 ?  4    ASN   B H    1 
ATOM   4060 H  H    B ASN   B 1 4   ? 47.108 -15.558 -16.804 0.70 19.69 ?  4    ASN   B H    1 
ATOM   4061 H  HA   . ASN   B 1 4   ? 45.536 -16.943 -16.541 1.00 17.96 ?  4    ASN   B HA   1 
ATOM   4062 H  HB2  . ASN   B 1 4   ? 43.987 -15.048 -17.942 1.00 17.06 ?  4    ASN   B HB2  1 
ATOM   4063 H  HB3  . ASN   B 1 4   ? 43.363 -16.295 -17.179 1.00 17.06 ?  4    ASN   B HB3  1 
ATOM   4064 H  HD21 . ASN   B 1 4   ? 43.631 -13.064 -15.343 1.00 17.24 ?  4    ASN   B HD21 1 
ATOM   4065 H  HD22 . ASN   B 1 4   ? 43.491 -13.244 -16.815 1.00 17.24 ?  4    ASN   B HD22 1 
ATOM   4066 N  N    . SER   B 1 5   ? 46.524 -17.911 -18.912 1.00 16.41 ?  5    SER   B N    1 
ATOM   4067 C  CA   . SER   B 1 5   ? 46.622 -18.825 -20.052 1.00 18.55 ?  5    SER   B CA   1 
ATOM   4068 C  C    . SER   B 1 5   ? 46.603 -20.260 -19.536 1.00 19.78 ?  5    SER   B C    1 
ATOM   4069 O  O    . SER   B 1 5   ? 47.614 -20.955 -19.485 1.00 22.25 ?  5    SER   B O    1 
ATOM   4070 C  CB   . SER   B 1 5   ? 47.883 -18.536 -20.864 1.00 19.85 ?  5    SER   B CB   1 
ATOM   4071 O  OG   . SER   B 1 5   ? 49.053 -18.725 -20.084 1.00 22.25 ?  5    SER   B OG   1 
ATOM   4072 H  H    . SER   B 1 5   ? 47.278 -17.761 -18.523 1.00 19.72 ?  5    SER   B H    1 
ATOM   4073 H  HA   . SER   B 1 5   ? 45.854 -18.702 -20.631 1.00 22.28 ?  5    SER   B HA   1 
ATOM   4074 H  HB2  . SER   B 1 5   ? 47.910 -19.136 -21.629 1.00 23.85 ?  5    SER   B HB2  1 
ATOM   4075 H  HB3  . SER   B 1 5   ? 47.844 -17.617 -21.170 1.00 23.85 ?  5    SER   B HB3  1 
ATOM   4076 H  HG   . SER   B 1 5   ? 49.100 -19.527 -19.836 1.00 26.72 ?  5    SER   B HG   1 
ATOM   4077 N  N    . PHE   B 1 6   ? 45.415 -20.683 -19.123 1.00 19.74 ?  6    PHE   B N    1 
ATOM   4078 C  CA   . PHE   B 1 6   ? 45.223 -22.024 -18.594 1.00 19.25 ?  6    PHE   B CA   1 
ATOM   4079 C  C    . PHE   B 1 6   ? 45.165 -23.014 -19.749 1.00 22.71 ?  6    PHE   B C    1 
ATOM   4080 O  O    . PHE   B 1 6   ? 44.509 -22.753 -20.762 1.00 25.02 ?  6    PHE   B O    1 
ATOM   4081 C  CB   . PHE   B 1 6   ? 43.928 -22.072 -17.786 1.00 17.26 ?  6    PHE   B CB   1 
ATOM   4082 C  CG   . PHE   B 1 6   ? 43.948 -21.209 -16.553 1.00 15.78 ?  6    PHE   B CG   1 
ATOM   4083 C  CD1  . PHE   B 1 6   ? 44.461 -21.699 -15.368 1.00 14.64 ?  6    PHE   B CD1  1 
ATOM   4084 C  CD2  . PHE   B 1 6   ? 43.455 -19.912 -16.578 1.00 15.44 ?  6    PHE   B CD2  1 
ATOM   4085 C  CE1  . PHE   B 1 6   ? 44.479 -20.919 -14.225 1.00 14.24 ?  6    PHE   B CE1  1 
ATOM   4086 C  CE2  . PHE   B 1 6   ? 43.477 -19.122 -15.441 1.00 15.40 ?  6    PHE   B CE2  1 
ATOM   4087 C  CZ   . PHE   B 1 6   ? 43.995 -19.620 -14.267 1.00 14.41 ?  6    PHE   B CZ   1 
ATOM   4088 H  H    . PHE   B 1 6   ? 44.692 -20.216 -19.151 1.00 23.71 ?  6    PHE   B H    1 
ATOM   4089 H  HA   . PHE   B 1 6   ? 45.963 -22.262 -18.015 1.00 23.12 ?  6    PHE   B HA   1 
ATOM   4090 H  HB2  . PHE   B 1 6   ? 43.196 -21.769 -18.346 1.00 20.74 ?  6    PHE   B HB2  1 
ATOM   4091 H  HB3  . PHE   B 1 6   ? 43.767 -22.987 -17.503 1.00 20.74 ?  6    PHE   B HB3  1 
ATOM   4092 H  HD1  . PHE   B 1 6   ? 44.798 -22.567 -15.337 1.00 17.59 ?  6    PHE   B HD1  1 
ATOM   4093 H  HD2  . PHE   B 1 6   ? 43.105 -19.570 -17.369 1.00 18.55 ?  6    PHE   B HD2  1 
ATOM   4094 H  HE1  . PHE   B 1 6   ? 44.836 -21.257 -13.434 1.00 17.11 ?  6    PHE   B HE1  1 
ATOM   4095 H  HE2  . PHE   B 1 6   ? 43.140 -18.254 -15.470 1.00 18.50 ?  6    PHE   B HE2  1 
ATOM   4096 H  HZ   . PHE   B 1 6   ? 44.006 -19.096 -13.501 1.00 17.32 ?  6    PHE   B HZ   1 
ATOM   4097 N  N    . SER   B 1 7   ? 45.872 -24.136 -19.605 1.00 23.94 ?  7    SER   B N    1 
ATOM   4098 C  CA   . SER   B 1 7   ? 45.961 -25.133 -20.661 1.00 26.44 ?  7    SER   B CA   1 
ATOM   4099 C  C    . SER   B 1 7   ? 45.889 -26.533 -20.069 1.00 25.64 ?  7    SER   B C    1 
ATOM   4100 O  O    . SER   B 1 7   ? 46.462 -26.804 -19.010 1.00 26.85 ?  7    SER   B O    1 
ATOM   4101 C  CB   . SER   B 1 7   ? 47.266 -24.976 -21.457 1.00 29.71 ?  7    SER   B CB   1 
ATOM   4102 O  OG   . SER   B 1 7   ? 47.296 -25.859 -22.564 1.00 32.39 ?  7    SER   B OG   1 
ATOM   4103 H  H    . SER   B 1 7   ? 46.326 -24.336 -18.898 1.00 28.76 ?  7    SER   B H    1 
ATOM   4104 H  HA   . SER   B 1 7   ? 45.219 -25.024 -21.272 1.00 31.76 ?  7    SER   B HA   1 
ATOM   4105 H  HB2  . SER   B 1 7   ? 47.332 -24.061 -21.778 1.00 35.67 ?  7    SER   B HB2  1 
ATOM   4106 H  HB3  . SER   B 1 7   ? 48.018 -25.175 -20.878 1.00 35.67 ?  7    SER   B HB3  1 
ATOM   4107 H  HG   . SER   B 1 7   ? 48.011 -25.758 -22.995 1.00 38.89 ?  7    SER   B HG   1 
ATOM   4108 N  N    . GLY   B 1 8   ? 45.183 -27.420 -20.767 1.00 25.58 ?  8    GLY   B N    1 
ATOM   4109 C  CA   . GLY   B 1 8   ? 45.133 -28.814 -20.383 1.00 24.54 ?  8    GLY   B CA   1 
ATOM   4110 C  C    . GLY   B 1 8   ? 44.173 -29.141 -19.268 1.00 22.92 ?  8    GLY   B C    1 
ATOM   4111 O  O    . GLY   B 1 8   ? 44.301 -30.206 -18.650 1.00 24.14 ?  8    GLY   B O    1 
ATOM   4112 H  H    . GLY   B 1 8   ? 44.730 -27.229 -21.470 1.00 30.72 ?  8    GLY   B H    1 
ATOM   4113 H  HA2  . GLY   B 1 8   ? 44.877 -29.340 -21.154 1.00 29.48 ?  8    GLY   B HA2  1 
ATOM   4114 H  HA3  . GLY   B 1 8   ? 46.015 -29.096 -20.103 1.00 29.48 ?  8    GLY   B HA3  1 
ATOM   4115 N  N    . TYR   B 1 9   ? 43.195 -28.278 -19.003 1.00 20.92 ?  9    TYR   B N    1 
ATOM   4116 C  CA   . TYR   B 1 9   ? 42.229 -28.540 -17.949 1.00 18.69 ?  9    TYR   B CA   1 
ATOM   4117 C  C    . TYR   B 1 9   ? 41.042 -29.326 -18.477 1.00 18.00 ?  9    TYR   B C    1 
ATOM   4118 O  O    . TYR   B 1 9   ? 40.626 -29.178 -19.629 1.00 20.06 ?  9    TYR   B O    1 
ATOM   4119 C  CB   . TYR   B 1 9   ? 41.730 -27.243 -17.311 1.00 18.18 ?  9    TYR   B CB   1 
ATOM   4120 C  CG   . TYR   B 1 9   ? 42.753 -26.624 -16.390 1.00 17.75 ?  9    TYR   B CG   1 
ATOM   4121 C  CD1  . TYR   B 1 9   ? 43.853 -25.957 -16.904 1.00 18.26 ?  9    TYR   B CD1  1 
ATOM   4122 C  CD2  . TYR   B 1 9   ? 42.637 -26.732 -15.014 1.00 17.04 ?  9    TYR   B CD2  1 
ATOM   4123 C  CE1  . TYR   B 1 9   ? 44.806 -25.403 -16.073 1.00 18.48 ?  9    TYR   B CE1  1 
ATOM   4124 C  CE2  . TYR   B 1 9   ? 43.580 -26.179 -14.171 1.00 17.51 ?  9    TYR   B CE2  1 
ATOM   4125 C  CZ   . TYR   B 1 9   ? 44.668 -25.516 -14.707 1.00 18.39 ?  9    TYR   B CZ   1 
ATOM   4126 O  OH   . TYR   B 1 9   ? 45.616 -24.969 -13.877 1.00 19.44 ?  9    TYR   B OH   1 
ATOM   4127 H  H    . TYR   B 1 9   ? 43.049 -27.547 -19.436 1.00 25.12 ?  9    TYR   B H    1 
ATOM   4128 H  HA   . TYR   B 1 9   ? 42.645 -29.068 -17.256 1.00 22.46 ?  9    TYR   B HA   1 
ATOM   4129 H  HB2  . TYR   B 1 9   ? 41.512 -26.597 -18.005 1.00 21.84 ?  9    TYR   B HB2  1 
ATOM   4130 H  HB3  . TYR   B 1 9   ? 40.941 -27.444 -16.786 1.00 21.84 ?  9    TYR   B HB3  1 
ATOM   4131 H  HD1  . TYR   B 1 9   ? 43.949 -25.877 -17.828 1.00 21.94 ?  9    TYR   B HD1  1 
ATOM   4132 H  HD2  . TYR   B 1 9   ? 41.901 -27.183 -14.654 1.00 20.47 ?  9    TYR   B HD2  1 
ATOM   4133 H  HE1  . TYR   B 1 9   ? 45.533 -24.955 -16.432 1.00 22.20 ?  9    TYR   B HE1  1 
ATOM   4134 H  HE2  . TYR   B 1 9   ? 43.478 -26.265 -13.251 1.00 21.04 ?  9    TYR   B HE2  1 
ATOM   4135 H  HH   . TYR   B 1 9   ? 46.202 -24.594 -14.336 1.00 23.35 ?  9    TYR   B HH   1 
ATOM   4136 N  N    . LEU   B 1 10  ? 40.508 -30.177 -17.610 1.00 16.01 ?  10   LEU   B N    1 
ATOM   4137 C  CA   . LEU   B 1 10  ? 39.302 -30.934 -17.884 1.00 15.74 ?  10   LEU   B CA   1 
ATOM   4138 C  C    . LEU   B 1 10  ? 38.115 -30.167 -17.317 1.00 15.40 ?  10   LEU   B C    1 
ATOM   4139 O  O    . LEU   B 1 10  ? 38.134 -29.751 -16.156 1.00 15.26 ?  10   LEU   B O    1 
ATOM   4140 C  CB   . LEU   B 1 10  ? 39.410 -32.304 -17.218 1.00 16.79 ?  10   LEU   B CB   1 
ATOM   4141 C  CG   . LEU   B 1 10  ? 38.261 -33.252 -17.549 1.00 18.35 ?  10   LEU   B CG   1 
ATOM   4142 C  CD1  . LEU   B 1 10  ? 38.414 -33.798 -18.964 1.00 19.45 ?  10   LEU   B CD1  1 
ATOM   4143 C  CD2  . LEU   B 1 10  ? 38.154 -34.379 -16.536 1.00 19.29 ?  10   LEU   B CD2  1 
ATOM   4144 H  H    . LEU   B 1 10  ? 40.833 -30.330 -16.825 1.00 19.23 ?  10   LEU   B H    1 
ATOM   4145 H  HA   . LEU   B 1 10  ? 39.185 -31.052 -18.837 1.00 18.91 ?  10   LEU   B HA   1 
ATOM   4146 H  HB2  . LEU   B 1 10  ? 40.236 -32.730 -17.507 1.00 20.18 ?  10   LEU   B HB2  1 
ATOM   4147 H  HB3  . LEU   B 1 10  ? 39.427 -32.187 -16.254 1.00 20.18 ?  10   LEU   B HB3  1 
ATOM   4148 H  HG   . LEU   B 1 10  ? 37.429 -32.755 -17.518 1.00 22.05 ?  10   LEU   B HG   1 
ATOM   4149 H  HD11 . LEU   B 1 10  ? 37.695 -34.424 -19.139 1.00 23.37 ?  10   LEU   B HD11 1 
ATOM   4150 H  HD12 . LEU   B 1 10  ? 38.371 -33.060 -19.592 1.00 23.37 ?  10   LEU   B HD12 1 
ATOM   4151 H  HD13 . LEU   B 1 10  ? 39.270 -34.247 -19.037 1.00 23.37 ?  10   LEU   B HD13 1 
ATOM   4152 H  HD21 . LEU   B 1 10  ? 37.414 -34.953 -16.785 1.00 23.17 ?  10   LEU   B HD21 1 
ATOM   4153 H  HD22 . LEU   B 1 10  ? 38.981 -34.879 -16.534 1.00 23.17 ?  10   LEU   B HD22 1 
ATOM   4154 H  HD23 . LEU   B 1 10  ? 37.993 -33.994 -15.659 1.00 23.17 ?  10   LEU   B HD23 1 
ATOM   4155 N  N    . LYS   B 1 11  ? 37.084 -29.997 -18.132 1.00 16.58 ?  11   LYS   B N    1 
ATOM   4156 C  CA   . LYS   B 1 11  ? 35.894 -29.268 -17.719 1.00 18.68 ?  11   LYS   B CA   1 
ATOM   4157 C  C    . LYS   B 1 11  ? 35.003 -30.186 -16.890 1.00 17.94 ?  11   LYS   B C    1 
ATOM   4158 O  O    . LYS   B 1 11  ? 34.604 -31.257 -17.356 1.00 19.96 ?  11   LYS   B O    1 
ATOM   4159 C  CB   . LYS   B 1 11  ? 35.163 -28.778 -18.968 1.00 22.96 ?  11   LYS   B CB   1 
ATOM   4160 C  CG   . LYS   B 1 11  ? 34.003 -27.836 -18.714 1.00 26.73 ?  11   LYS   B CG   1 
ATOM   4161 C  CD   . LYS   B 1 11  ? 33.276 -27.520 -20.018 1.00 30.01 ?  11   LYS   B CD   1 
ATOM   4162 C  CE   . LYS   B 1 11  ? 32.247 -26.417 -19.840 1.00 32.49 ?  11   LYS   B CE   1 
ATOM   4163 N  NZ   . LYS   B 1 11  ? 32.886 -25.095 -19.603 1.00 33.92 ?  11   LYS   B NZ   1 
ATOM   4164 H  H    . LYS   B 1 11  ? 37.042 -30.311 -18.933 1.00 19.92 ?  11   LYS   B H    1 
ATOM   4165 H  HA   . LYS   B 1 11  ? 36.147 -28.506 -17.180 1.00 22.44 ?  11   LYS   B HA   1 
ATOM   4166 H  HB2  . LYS   B 1 11  ? 35.801 -28.310 -19.532 1.00 27.58 ?  11   LYS   B HB2  1 
ATOM   4167 H  HB3  . LYS   B 1 11  ? 34.815 -29.548 -19.445 1.00 27.58 ?  11   LYS   B HB3  1 
ATOM   4168 H  HG2  . LYS   B 1 11  ? 33.374 -28.254 -18.107 1.00 32.10 ?  11   LYS   B HG2  1 
ATOM   4169 H  HG3  . LYS   B 1 11  ? 34.336 -27.006 -18.340 1.00 32.10 ?  11   LYS   B HG3  1 
ATOM   4170 H  HD2  . LYS   B 1 11  ? 33.923 -27.228 -20.681 1.00 36.03 ?  11   LYS   B HD2  1 
ATOM   4171 H  HD3  . LYS   B 1 11  ? 32.818 -28.317 -20.329 1.00 36.03 ?  11   LYS   B HD3  1 
ATOM   4172 H  HE2  . LYS   B 1 11  ? 31.706 -26.353 -20.643 1.00 39.01 ?  11   LYS   B HE2  1 
ATOM   4173 H  HE3  . LYS   B 1 11  ? 31.688 -26.629 -19.076 1.00 39.01 ?  11   LYS   B HE3  1 
ATOM   4174 H  HZ1  . LYS   B 1 11  ? 32.261 -24.467 -19.518 1.00 40.73 ?  11   LYS   B HZ1  1 
ATOM   4175 H  HZ2  . LYS   B 1 11  ? 33.373 -25.121 -18.859 1.00 40.73 ?  11   LYS   B HZ2  1 
ATOM   4176 H  HZ3  . LYS   B 1 11  ? 33.415 -24.886 -20.288 1.00 40.73 ?  11   LYS   B HZ3  1 
ATOM   4177 N  N    . LEU   B 1 12  ? 34.694 -29.776 -15.661 1.00 16.52 ?  12   LEU   B N    1 
ATOM   4178 C  CA   . LEU   B 1 12  ? 33.731 -30.479 -14.819 1.00 16.15 ?  12   LEU   B CA   1 
ATOM   4179 C  C    . LEU   B 1 12  ? 32.341 -29.871 -14.913 1.00 15.91 ?  12   LEU   B C    1 
ATOM   4180 O  O    . LEU   B 1 12  ? 31.354 -30.587 -15.089 1.00 16.86 ?  12   LEU   B O    1 
ATOM   4181 C  CB   . LEU   B 1 12  ? 34.190 -30.489 -13.357 1.00 15.49 ?  12   LEU   B CB   1 
ATOM   4182 C  CG   . LEU   B 1 12  ? 35.530 -31.174 -13.093 1.00 15.64 ?  12   LEU   B CG   1 
ATOM   4183 C  CD1  . LEU   B 1 12  ? 35.880 -31.156 -11.613 1.00 15.92 ?  12   LEU   B CD1  1 
ATOM   4184 C  CD2  . LEU   B 1 12  ? 35.518 -32.602 -13.626 1.00 16.20 ?  12   LEU   B CD2  1 
ATOM   4185 H  H    . LEU   B 1 12  ? 35.033 -29.082 -15.290 1.00 19.85 ?  12   LEU   B H    1 
ATOM   4186 H  HA   . LEU   B 1 12  ? 33.663 -31.399 -15.119 1.00 19.41 ?  12   LEU   B HA   1 
ATOM   4187 H  HB2  . LEU   B 1 12  ? 34.262 -29.572 -13.053 1.00 18.61 ?  12   LEU   B HB2  1 
ATOM   4188 H  HB3  . LEU   B 1 12  ? 33.517 -30.952 -12.829 1.00 18.61 ?  12   LEU   B HB3  1 
ATOM   4189 H  HG   . LEU   B 1 12  ? 36.223 -30.686 -13.565 1.00 18.80 ?  12   LEU   B HG   1 
ATOM   4190 H  HD11 . LEU   B 1 12  ? 36.740 -31.594 -11.487 1.00 19.12 ?  12   LEU   B HD11 1 
ATOM   4191 H  HD12 . LEU   B 1 12  ? 35.931 -30.238 -11.307 1.00 19.12 ?  12   LEU   B HD12 1 
ATOM   4192 H  HD13 . LEU   B 1 12  ? 35.194 -31.633 -11.118 1.00 19.12 ?  12   LEU   B HD13 1 
ATOM   4193 H  HD21 . LEU   B 1 12  ? 36.297 -33.070 -13.292 1.00 19.47 ?  12   LEU   B HD21 1 
ATOM   4194 H  HD22 . LEU   B 1 12  ? 34.709 -33.044 -13.326 1.00 19.47 ?  12   LEU   B HD22 1 
ATOM   4195 H  HD23 . LEU   B 1 12  ? 35.538 -32.576 -14.597 1.00 19.47 ?  12   LEU   B HD23 1 
ATOM   4196 N  N    . THR   B 1 13  ? 32.252 -28.554 -14.795 1.00 15.68 ?  13   THR   B N    1 
ATOM   4197 C  CA   . THR   B 1 13  ? 31.027 -27.804 -14.991 1.00 15.56 ?  13   THR   B CA   1 
ATOM   4198 C  C    . THR   B 1 13  ? 31.363 -26.602 -15.865 1.00 17.41 ?  13   THR   B C    1 
ATOM   4199 O  O    . THR   B 1 13  ? 32.509 -26.410 -16.288 1.00 18.53 ?  13   THR   B O    1 
ATOM   4200 C  CB   . THR   B 1 13  ? 30.433 -27.336 -13.657 1.00 15.68 ?  13   THR   B CB   1 
ATOM   4201 O  OG1  . THR   B 1 13  ? 31.274 -26.311 -13.106 1.00 15.58 ?  13   THR   B OG1  1 
ATOM   4202 C  CG2  . THR   B 1 13  ? 30.316 -28.489 -12.670 1.00 16.75 ?  13   THR   B CG2  1 
ATOM   4203 H  H    . THR   B 1 13  ? 32.919 -28.054 -14.587 1.00 18.84 ?  13   THR   B H    1 
ATOM   4204 H  HA   . THR   B 1 13  ? 30.369 -28.356 -15.443 1.00 18.70 ?  13   THR   B HA   1 
ATOM   4205 H  HB   . THR   B 1 13  ? 29.543 -26.973 -13.811 1.00 18.84 ?  13   THR   B HB   1 
ATOM   4206 H  HG1  . THR   B 1 13  ? 30.973 -25.551 -13.318 1.00 18.72 ?  13   THR   B HG1  1 
ATOM   4207 H  HG21 . THR   B 1 13  ? 29.818 -28.206 -11.887 1.00 20.12 ?  13   THR   B HG21 1 
ATOM   4208 H  HG22 . THR   B 1 13  ? 29.854 -29.233 -13.085 1.00 20.12 ?  13   THR   B HG22 1 
ATOM   4209 H  HG23 . THR   B 1 13  ? 31.199 -28.780 -12.395 1.00 20.12 ?  13   THR   B HG23 1 
ATOM   4210 N  N    A ASP   B 1 14  ? 30.353 -25.767 -16.120 0.30 18.48 ?  14   ASP   B N    1 
ATOM   4211 N  N    B ASP   B 1 14  ? 30.354 -25.771 -16.129 0.70 18.44 ?  14   ASP   B N    1 
ATOM   4212 C  CA   A ASP   B 1 14  ? 30.559 -24.609 -16.980 0.30 19.59 ?  14   ASP   B CA   1 
ATOM   4213 C  CA   B ASP   B 1 14  ? 30.571 -24.614 -16.987 0.70 19.62 ?  14   ASP   B CA   1 
ATOM   4214 C  C    A ASP   B 1 14  ? 31.622 -23.665 -16.437 0.30 18.03 ?  14   ASP   B C    1 
ATOM   4215 C  C    B ASP   B 1 14  ? 31.627 -23.665 -16.438 0.70 18.17 ?  14   ASP   B C    1 
ATOM   4216 O  O    A ASP   B 1 14  ? 32.213 -22.909 -17.216 0.30 18.98 ?  14   ASP   B O    1 
ATOM   4217 O  O    B ASP   B 1 14  ? 32.217 -22.907 -17.214 0.70 19.95 ?  14   ASP   B O    1 
ATOM   4218 C  CB   A ASP   B 1 14  ? 29.245 -23.849 -17.168 0.30 22.50 ?  14   ASP   B CB   1 
ATOM   4219 C  CB   B ASP   B 1 14  ? 29.260 -23.860 -17.205 0.70 23.28 ?  14   ASP   B CB   1 
ATOM   4220 C  CG   A ASP   B 1 14  ? 28.268 -24.577 -18.068 0.30 25.06 ?  14   ASP   B CG   1 
ATOM   4221 C  CG   B ASP   B 1 14  ? 28.347 -24.558 -18.189 0.70 26.91 ?  14   ASP   B CG   1 
ATOM   4222 O  OD1  A ASP   B 1 14  ? 28.614 -25.661 -18.589 0.30 25.62 ?  14   ASP   B OD1  1 
ATOM   4223 O  OD1  B ASP   B 1 14  ? 28.861 -25.288 -19.064 0.70 27.74 ?  14   ASP   B OD1  1 
ATOM   4224 O  OD2  A ASP   B 1 14  ? 27.146 -24.060 -18.253 0.30 26.11 -1 14   ASP   B OD2  1 
ATOM   4225 O  OD2  B ASP   B 1 14  ? 27.115 -24.382 -18.090 0.70 28.39 -1 14   ASP   B OD2  1 
ATOM   4226 H  H    A ASP   B 1 14  ? 29.559 -25.840 -15.800 0.30 22.20 ?  14   ASP   B H    1 
ATOM   4227 H  H    B ASP   B 1 14  ? 29.557 -25.847 -15.819 0.70 22.16 ?  14   ASP   B H    1 
ATOM   4228 H  HA   A ASP   B 1 14  ? 30.855 -24.913 -17.850 0.30 23.53 ?  14   ASP   B HA   1 
ATOM   4229 H  HA   B ASP   B 1 14  ? 30.882 -24.922 -17.851 0.70 23.57 ?  14   ASP   B HA   1 
ATOM   4230 H  HB2  A ASP   B 1 14  ? 28.815 -23.742 -16.308 0.30 27.03 ?  14   ASP   B HB2  1 
ATOM   4231 H  HB2  B ASP   B 1 14  ? 28.786 -23.797 -16.363 0.70 27.96 ?  14   ASP   B HB2  1 
ATOM   4232 H  HB3  A ASP   B 1 14  ? 29.435 -22.980 -17.557 0.30 27.03 ?  14   ASP   B HB3  1 
ATOM   4233 H  HB3  B ASP   B 1 14  ? 29.457 -22.971 -17.544 0.70 27.96 ?  14   ASP   B HB3  1 
ATOM   4234 N  N    . ASN   B 1 15  ? 31.879 -23.688 -15.125 1.00 15.95 ?  15   ASN   B N    1 
ATOM   4235 C  CA   . ASN   B 1 15  ? 32.844 -22.776 -14.517 1.00 14.02 ?  15   ASN   B CA   1 
ATOM   4236 C  C    . ASN   B 1 15  ? 33.937 -23.437 -13.685 1.00 12.94 ?  15   ASN   B C    1 
ATOM   4237 O  O    . ASN   B 1 15  ? 34.787 -22.715 -13.151 1.00 13.18 ?  15   ASN   B O    1 
ATOM   4238 C  CB   . ASN   B 1 15  ? 32.135 -21.724 -13.648 1.00 14.13 ?  15   ASN   B CB   1 
ATOM   4239 C  CG   . ASN   B 1 15  ? 31.506 -22.327 -12.413 1.00 14.01 ?  15   ASN   B CG   1 
ATOM   4240 O  OD1  . ASN   B 1 15  ? 30.559 -23.118 -12.505 1.00 15.89 ?  15   ASN   B OD1  1 
ATOM   4241 N  ND2  . ASN   B 1 15  ? 32.036 -21.990 -11.253 1.00 13.42 ?  15   ASN   B ND2  1 
ATOM   4242 H  H    A ASN   B 1 15  ? 31.491 -24.214 -14.566 0.30 19.16 ?  15   ASN   B H    1 
ATOM   4243 H  H    B ASN   B 1 15  ? 31.491 -24.215 -14.567 0.70 19.16 ?  15   ASN   B H    1 
ATOM   4244 H  HA   . ASN   B 1 15  ? 33.291 -22.289 -15.219 1.00 16.85 ?  15   ASN   B HA   1 
ATOM   4245 H  HB2  . ASN   B 1 15  ? 32.782 -21.054 -13.367 1.00 16.98 ?  15   ASN   B HB2  1 
ATOM   4246 H  HB3  . ASN   B 1 15  ? 31.431 -21.300 -14.167 1.00 16.98 ?  15   ASN   B HB3  1 
ATOM   4247 H  HD21 . ASN   B 1 15  ? 31.714 -22.304 -10.518 1.00 16.13 ?  15   ASN   B HD21 1 
ATOM   4248 H  HD22 . ASN   B 1 15  ? 32.701 -21.437 -11.219 1.00 16.13 ?  15   ASN   B HD22 1 
ATOM   4249 N  N    . VAL   B 1 16  ? 33.953 -24.761 -13.552 1.00 13.10 ?  16   VAL   B N    1 
ATOM   4250 C  CA   . VAL   B 1 16  ? 34.950 -25.454 -12.744 1.00 12.69 ?  16   VAL   B CA   1 
ATOM   4251 C  C    . VAL   B 1 16  ? 35.743 -26.396 -13.637 1.00 12.96 ?  16   VAL   B C    1 
ATOM   4252 O  O    . VAL   B 1 16  ? 35.166 -27.268 -14.305 1.00 13.87 ?  16   VAL   B O    1 
ATOM   4253 C  CB   . VAL   B 1 16  ? 34.326 -26.217 -11.561 1.00 13.22 ?  16   VAL   B CB   1 
ATOM   4254 C  CG1  . VAL   B 1 16  ? 35.414 -26.933 -10.759 1.00 13.36 ?  16   VAL   B CG1  1 
ATOM   4255 C  CG2  . VAL   B 1 16  ? 33.526 -25.267 -10.679 1.00 13.65 ?  16   VAL   B CG2  1 
ATOM   4256 H  H    . VAL   B 1 16  ? 33.379 -25.290 -13.919 1.00 15.74 ?  16   VAL   B H    1 
ATOM   4257 H  HA   . VAL   B 1 16  ? 35.567 -24.801 -12.373 1.00 15.25 ?  16   VAL   B HA   1 
ATOM   4258 H  HB   . VAL   B 1 16  ? 33.717 -26.889 -11.900 1.00 15.88 ?  16   VAL   B HB   1 
ATOM   4259 H  HG11 . VAL   B 1 16  ? 35.040 -27.227 -9.912  1.00 16.06 ?  16   VAL   B HG11 1 
ATOM   4260 H  HG12 . VAL   B 1 16  ? 35.735 -27.692 -11.261 1.00 16.06 ?  16   VAL   B HG12 1 
ATOM   4261 H  HG13 . VAL   B 1 16  ? 36.143 -26.309 -10.591 1.00 16.06 ?  16   VAL   B HG13 1 
ATOM   4262 H  HG21 . VAL   B 1 16  ? 33.196 -25.750 -9.907  1.00 16.40 ?  16   VAL   B HG21 1 
ATOM   4263 H  HG22 . VAL   B 1 16  ? 34.103 -24.540 -10.392 1.00 16.40 ?  16   VAL   B HG22 1 
ATOM   4264 H  HG23 . VAL   B 1 16  ? 32.782 -24.912 -11.192 1.00 16.40 ?  16   VAL   B HG23 1 
ATOM   4265 N  N    . TYR   B 1 17  ? 37.071 -26.233 -13.605 1.00 13.06 ?  17   TYR   B N    1 
ATOM   4266 C  CA   . TYR   B 1 17  ? 38.022 -26.976 -14.417 1.00 13.54 ?  17   TYR   B CA   1 
ATOM   4267 C  C    . TYR   B 1 17  ? 39.073 -27.588 -13.501 1.00 12.62 ?  17   TYR   B C    1 
ATOM   4268 O  O    . TYR   B 1 17  ? 39.341 -27.062 -12.416 1.00 12.92 ?  17   TYR   B O    1 
ATOM   4269 C  CB   . TYR   B 1 17  ? 38.733 -26.037 -15.399 1.00 15.75 ?  17   TYR   B CB   1 
ATOM   4270 C  CG   . TYR   B 1 17  ? 37.810 -25.273 -16.312 1.00 18.46 ?  17   TYR   B CG   1 
ATOM   4271 C  CD1  . TYR   B 1 17  ? 37.225 -24.079 -15.908 1.00 19.97 ?  17   TYR   B CD1  1 
ATOM   4272 C  CD2  . TYR   B 1 17  ? 37.525 -25.746 -17.583 1.00 20.42 ?  17   TYR   B CD2  1 
ATOM   4273 C  CE1  . TYR   B 1 17  ? 36.381 -23.377 -16.747 1.00 21.74 ?  17   TYR   B CE1  1 
ATOM   4274 C  CE2  . TYR   B 1 17  ? 36.683 -25.053 -18.430 1.00 22.20 ?  17   TYR   B CE2  1 
ATOM   4275 C  CZ   . TYR   B 1 17  ? 36.111 -23.870 -18.006 1.00 22.94 ?  17   TYR   B CZ   1 
ATOM   4276 O  OH   . TYR   B 1 17  ? 35.272 -23.178 -18.848 1.00 24.55 ?  17   TYR   B OH   1 
ATOM   4277 H  H    . TYR   B 1 17  ? 37.465 -25.660 -13.087 1.00 15.70 ?  17   TYR   B H    1 
ATOM   4278 H  HA   . TYR   B 1 17  ? 37.566 -27.681 -14.908 1.00 16.27 ?  17   TYR   B HA   1 
ATOM   4279 H  HB2  . TYR   B 1 17  ? 39.258 -25.397 -14.897 1.00 18.93 ?  17   TYR   B HB2  1 
ATOM   4280 H  HB3  . TYR   B 1 17  ? 39.315 -26.570 -15.960 1.00 18.93 ?  17   TYR   B HB3  1 
ATOM   4281 H  HD1  . TYR   B 1 17  ? 37.409 -23.745 -15.060 1.00 23.99 ?  17   TYR   B HD1  1 
ATOM   4282 H  HD2  . TYR   B 1 17  ? 37.903 -26.544 -17.874 1.00 24.53 ?  17   TYR   B HD2  1 
ATOM   4283 H  HE1  . TYR   B 1 17  ? 35.997 -22.577 -16.466 1.00 26.11 ?  17   TYR   B HE1  1 
ATOM   4284 H  HE2  . TYR   B 1 17  ? 36.494 -25.383 -19.281 1.00 26.67 ?  17   TYR   B HE2  1 
ATOM   4285 H  HH   . TYR   B 1 17  ? 35.191 -23.583 -19.579 1.00 29.49 ?  17   TYR   B HH   1 
ATOM   4286 N  N    . ILE   B 1 18  ? 39.686 -28.693 -13.936 1.00 12.56 ?  18   ILE   B N    1 
ATOM   4287 C  CA   . ILE   B 1 18  ? 40.612 -29.423 -13.076 1.00 12.59 ?  18   ILE   B CA   1 
ATOM   4288 C  C    . ILE   B 1 18  ? 41.775 -29.980 -13.893 1.00 12.79 ?  18   ILE   B C    1 
ATOM   4289 O  O    . ILE   B 1 18  ? 41.616 -30.382 -15.050 1.00 14.05 ?  18   ILE   B O    1 
ATOM   4290 C  CB   . ILE   B 1 18  ? 39.855 -30.525 -12.289 1.00 13.26 ?  18   ILE   B CB   1 
ATOM   4291 C  CG1  . ILE   B 1 18  ? 40.698 -31.071 -11.134 1.00 14.09 ?  18   ILE   B CG1  1 
ATOM   4292 C  CG2  . ILE   B 1 18  ? 39.353 -31.633 -13.224 1.00 13.91 ?  18   ILE   B CG2  1 
ATOM   4293 C  CD1  . ILE   B 1 18  ? 39.869 -31.863 -10.131 1.00 15.62 ?  18   ILE   B CD1  1 
ATOM   4294 H  H    . ILE   B 1 18  ? 39.592 -29.031 -14.722 1.00 15.09 ?  18   ILE   B H    1 
ATOM   4295 H  HA   . ILE   B 1 18  ? 40.976 -28.812 -12.418 1.00 15.14 ?  18   ILE   B HA   1 
ATOM   4296 H  HB   . ILE   B 1 18  ? 39.070 -30.117 -11.896 1.00 15.93 ?  18   ILE   B HB   1 
ATOM   4297 H  HG12 . ILE   B 1 18  ? 41.383 -31.654 -11.486 1.00 16.93 ?  18   ILE   B HG12 1 
ATOM   4298 H  HG13 . ILE   B 1 18  ? 41.101 -30.324 -10.662 1.00 16.93 ?  18   ILE   B HG13 1 
ATOM   4299 H  HG21 . ILE   B 1 18  ? 38.760 -32.221 -12.728 1.00 16.72 ?  18   ILE   B HG21 1 
ATOM   4300 H  HG22 . ILE   B 1 18  ? 38.870 -31.225 -13.960 1.00 16.72 ?  18   ILE   B HG22 1 
ATOM   4301 H  HG23 . ILE   B 1 18  ? 40.110 -32.134 -13.560 1.00 16.72 ?  18   ILE   B HG23 1 
ATOM   4302 H  HD11 . ILE   B 1 18  ? 40.439 -32.142 -9.399  1.00 18.77 ?  18   ILE   B HD11 1 
ATOM   4303 H  HD12 . ILE   B 1 18  ? 39.151 -31.301 -9.796  1.00 18.77 ?  18   ILE   B HD12 1 
ATOM   4304 H  HD13 . ILE   B 1 18  ? 39.496 -32.642 -10.575 1.00 18.77 ?  18   ILE   B HD13 1 
ATOM   4305 N  N    . LYS   B 1 19  ? 42.957 -30.010 -13.271 1.00 13.42 ?  19   LYS   B N    1 
ATOM   4306 C  CA   . LYS   B 1 19  ? 44.164 -30.493 -13.928 1.00 14.12 ?  19   LYS   B CA   1 
ATOM   4307 C  C    . LYS   B 1 19  ? 45.063 -31.167 -12.903 1.00 14.46 ?  19   LYS   B C    1 
ATOM   4308 O  O    . LYS   B 1 19  ? 45.148 -30.725 -11.756 1.00 14.16 ?  19   LYS   B O    1 
ATOM   4309 C  CB   . LYS   B 1 19  ? 44.926 -29.323 -14.566 1.00 15.24 ?  19   LYS   B CB   1 
ATOM   4310 C  CG   . LYS   B 1 19  ? 46.136 -29.724 -15.396 1.00 17.13 ?  19   LYS   B CG   1 
ATOM   4311 C  CD   . LYS   B 1 19  ? 46.871 -28.487 -15.898 1.00 18.94 ?  19   LYS   B CD   1 
ATOM   4312 C  CE   . LYS   B 1 19  ? 48.017 -28.845 -16.825 1.00 21.15 ?  19   LYS   B CE   1 
ATOM   4313 N  NZ   . LYS   B 1 19  ? 48.723 -27.637 -17.322 1.00 22.13 ?  19   LYS   B NZ   1 
ATOM   4314 H  H    . LYS   B 1 19  ? 43.080 -29.750 -12.458 1.00 16.13 ?  19   LYS   B H    1 
ATOM   4315 H  HA   . LYS   B 1 19  ? 43.926 -31.135 -14.617 1.00 16.97 ?  19   LYS   B HA   1 
ATOM   4316 H  HB2  . LYS   B 1 19  ? 44.315 -28.843 -15.147 1.00 18.31 ?  19   LYS   B HB2  1 
ATOM   4317 H  HB3  . LYS   B 1 19  ? 45.229 -28.734 -13.855 1.00 18.31 ?  19   LYS   B HB3  1 
ATOM   4318 H  HG2  . LYS   B 1 19  ? 46.741 -30.246 -14.848 1.00 20.58 ?  19   LYS   B HG2  1 
ATOM   4319 H  HG3  . LYS   B 1 19  ? 45.837 -30.242 -16.161 1.00 20.58 ?  19   LYS   B HG3  1 
ATOM   4320 H  HD2  . LYS   B 1 19  ? 46.248 -27.923 -16.384 1.00 22.76 ?  19   LYS   B HD2  1 
ATOM   4321 H  HD3  . LYS   B 1 19  ? 47.233 -28.004 -15.137 1.00 22.76 ?  19   LYS   B HD3  1 
ATOM   4322 H  HE2  . LYS   B 1 19  ? 48.653 -29.395 -16.343 1.00 25.40 ?  19   LYS   B HE2  1 
ATOM   4323 H  HE3  . LYS   B 1 19  ? 47.665 -29.330 -17.588 1.00 25.40 ?  19   LYS   B HE3  1 
ATOM   4324 H  HZ1  . LYS   B 1 19  ? 49.361 -27.873 -17.896 1.00 26.58 ?  19   LYS   B HZ1  1 
ATOM   4325 H  HZ2  . LYS   B 1 19  ? 48.149 -27.096 -17.736 1.00 26.58 ?  19   LYS   B HZ2  1 
ATOM   4326 H  HZ3  . LYS   B 1 19  ? 49.093 -27.198 -16.643 1.00 26.58 ?  19   LYS   B HZ3  1 
ATOM   4327 N  N    . ASN   B 1 20  ? 45.748 -32.226 -13.330 1.00 14.81 ?  20   ASN   B N    1 
ATOM   4328 C  CA   . ASN   B 1 20  ? 46.793 -32.844 -12.519 1.00 15.58 ?  20   ASN   B CA   1 
ATOM   4329 C  C    . ASN   B 1 20  ? 48.065 -32.020 -12.702 1.00 16.18 ?  20   ASN   B C    1 
ATOM   4330 O  O    . ASN   B 1 20  ? 48.714 -32.094 -13.753 1.00 18.15 ?  20   ASN   B O    1 
ATOM   4331 C  CB   . ASN   B 1 20  ? 46.982 -34.293 -12.963 1.00 17.55 ?  20   ASN   B CB   1 
ATOM   4332 C  CG   . ASN   B 1 20  ? 48.150 -34.983 -12.287 1.00 19.16 ?  20   ASN   B CG   1 
ATOM   4333 O  OD1  . ASN   B 1 20  ? 48.850 -35.780 -12.917 1.00 21.29 ?  20   ASN   B OD1  1 
ATOM   4334 N  ND2  . ASN   B 1 20  ? 48.358 -34.705 -11.004 1.00 18.74 ?  20   ASN   B ND2  1 
ATOM   4335 H  H    . ASN   B 1 20  ? 45.624 -32.604 -14.089 1.00 17.79 ?  20   ASN   B H    1 
ATOM   4336 H  HA   . ASN   B 1 20  ? 46.521 -32.834 -11.584 1.00 18.72 ?  20   ASN   B HA   1 
ATOM   4337 H  HB2  . ASN   B 1 20  ? 46.180 -34.799 -12.752 1.00 21.09 ?  20   ASN   B HB2  1 
ATOM   4338 H  HB3  . ASN   B 1 20  ? 47.138 -34.307 -13.920 1.00 21.09 ?  20   ASN   B HB3  1 
ATOM   4339 H  HD21 . ASN   B 1 20  ? 49.012 -35.068 -10.581 1.00 22.51 ?  20   ASN   B HD21 1 
ATOM   4340 H  HD22 . ASN   B 1 20  ? 47.837 -34.155 -10.590 1.00 22.51 ?  20   ASN   B HD22 1 
ATOM   4341 N  N    . ALA   B 1 21  ? 48.420 -31.224 -11.693 1.00 15.48 ?  21   ALA   B N    1 
ATOM   4342 C  CA   . ALA   B 1 21  ? 49.520 -30.285 -11.846 1.00 16.28 ?  21   ALA   B CA   1 
ATOM   4343 C  C    . ALA   B 1 21  ? 49.985 -29.804 -10.480 1.00 15.72 ?  21   ALA   B C    1 
ATOM   4344 O  O    . ALA   B 1 21  ? 49.238 -29.838 -9.495  1.00 15.26 ?  21   ALA   B O    1 
ATOM   4345 C  CB   . ALA   B 1 21  ? 49.104 -29.098 -12.716 1.00 17.80 ?  21   ALA   B CB   1 
ATOM   4346 H  H    . ALA   B 1 21  ? 48.039 -31.219 -10.912 1.00 18.60 ?  21   ALA   B H    1 
ATOM   4347 H  HA   . ALA   B 1 21  ? 50.258 -30.740 -12.275 1.00 19.56 ?  21   ALA   B HA   1 
ATOM   4348 H  HB1  . ALA   B 1 21  ? 49.879 -28.544 -12.864 1.00 21.39 ?  21   ALA   B HB1  1 
ATOM   4349 H  HB2  . ALA   B 1 21  ? 48.765 -29.436 -13.559 1.00 21.39 ?  21   ALA   B HB2  1 
ATOM   4350 H  HB3  . ALA   B 1 21  ? 48.410 -28.600 -12.257 1.00 21.39 ?  21   ALA   B HB3  1 
ATOM   4351 N  N    . ASP   B 1 22  ? 51.246 -29.367 -10.453 1.00 15.07 ?  22   ASP   B N    1 
ATOM   4352 C  CA   . ASP   B 1 22  ? 51.857 -28.666 -9.327  1.00 14.10 ?  22   ASP   B CA   1 
ATOM   4353 C  C    . ASP   B 1 22  ? 51.445 -27.197 -9.412  1.00 12.98 ?  22   ASP   B C    1 
ATOM   4354 O  O    . ASP   B 1 22  ? 51.755 -26.520 -10.398 1.00 13.38 ?  22   ASP   B O    1 
ATOM   4355 C  CB   . ASP   B 1 22  ? 53.376 -28.834 -9.484  1.00 15.70 ?  22   ASP   B CB   1 
ATOM   4356 C  CG   . ASP   B 1 22  ? 54.201 -28.097 -8.436  1.00 17.40 ?  22   ASP   B CG   1 
ATOM   4357 O  OD1  . ASP   B 1 22  ? 53.841 -26.979 -8.040  1.00 17.65 ?  22   ASP   B OD1  1 
ATOM   4358 O  OD2  . ASP   B 1 22  ? 55.260 -28.641 -8.037  1.00 20.02 -1 22   ASP   B OD2  1 
ATOM   4359 H  H    . ASP   B 1 22  ? 51.793 -29.475 -11.112 1.00 18.10 ?  22   ASP   B H    1 
ATOM   4360 H  HA   . ASP   B 1 22  ? 51.570 -29.051 -8.482  1.00 16.94 ?  22   ASP   B HA   1 
ATOM   4361 H  HB2  . ASP   B 1 22  ? 53.601 -29.773 -9.423  1.00 18.87 ?  22   ASP   B HB2  1 
ATOM   4362 H  HB3  . ASP   B 1 22  ? 53.640 -28.486 -10.351 1.00 18.87 ?  22   ASP   B HB3  1 
ATOM   4363 N  N    . ILE   B 1 23  ? 50.737 -26.705 -8.388  1.00 12.75 ?  23   ILE   B N    1 
ATOM   4364 C  CA   . ILE   B 1 23  ? 50.145 -25.366 -8.453  1.00 12.23 ?  23   ILE   B CA   1 
ATOM   4365 C  C    . ILE   B 1 23  ? 51.200 -24.272 -8.595  1.00 12.17 ?  23   ILE   B C    1 
ATOM   4366 O  O    . ILE   B 1 23  ? 50.931 -23.231 -9.201  1.00 11.71 ?  23   ILE   B O    1 
ATOM   4367 C  CB   . ILE   B 1 23  ? 49.204 -25.123 -7.253  1.00 12.11 ?  23   ILE   B CB   1 
ATOM   4368 C  CG1  . ILE   B 1 23  ? 48.387 -23.846 -7.442  1.00 12.96 ?  23   ILE   B CG1  1 
ATOM   4369 C  CG2  . ILE   B 1 23  ? 49.977 -25.110 -5.945  1.00 13.15 ?  23   ILE   B CG2  1 
ATOM   4370 C  CD1  . ILE   B 1 23  ? 47.251 -23.698 -6.445  1.00 13.94 ?  23   ILE   B CD1  1 
ATOM   4371 H  H    . ILE   B 1 23  ? 50.585 -27.130 -7.655  1.00 15.32 ?  23   ILE   B H    1 
ATOM   4372 H  HA   . ILE   B 1 23  ? 49.596 -25.328 -9.248  1.00 14.70 ?  23   ILE   B HA   1 
ATOM   4373 H  HB   . ILE   B 1 23  ? 48.579 -25.864 -7.218  1.00 14.56 ?  23   ILE   B HB   1 
ATOM   4374 H  HG12 . ILE   B 1 23  ? 48.981 -23.078 -7.338  1.00 15.58 ?  23   ILE   B HG12 1 
ATOM   4375 H  HG13 . ILE   B 1 23  ? 48.010 -23.842 -8.336  1.00 15.58 ?  23   ILE   B HG13 1 
ATOM   4376 H  HG21 . ILE   B 1 23  ? 49.347 -25.090 -5.209  1.00 15.81 ?  23   ILE   B HG21 1 
ATOM   4377 H  HG22 . ILE   B 1 23  ? 50.518 -25.915 -5.893  1.00 15.81 ?  23   ILE   B HG22 1 
ATOM   4378 H  HG23 . ILE   B 1 23  ? 50.545 -24.328 -5.922  1.00 15.81 ?  23   ILE   B HG23 1 
ATOM   4379 H  HD11 . ILE   B 1 23  ? 46.736 -22.909 -6.669  1.00 16.75 ?  23   ILE   B HD11 1 
ATOM   4380 H  HD12 . ILE   B 1 23  ? 46.690 -24.487 -6.495  1.00 16.75 ?  23   ILE   B HD12 1 
ATOM   4381 H  HD13 . ILE   B 1 23  ? 47.623 -23.612 -5.554  1.00 16.75 ?  23   ILE   B HD13 1 
ATOM   4382 N  N    . VAL   B 1 24  ? 52.398 -24.475 -8.038  1.00 12.15 ?  24   VAL   B N    1 
ATOM   4383 C  CA   . VAL   B 1 24  ? 53.474 -23.494 -8.202  1.00 12.86 ?  24   VAL   B CA   1 
ATOM   4384 C  C    . VAL   B 1 24  ? 53.933 -23.445 -9.653  1.00 12.82 ?  24   VAL   B C    1 
ATOM   4385 O  O    . VAL   B 1 24  ? 54.068 -22.369 -10.247 1.00 13.23 ?  24   VAL   B O    1 
ATOM   4386 C  CB   . VAL   B 1 24  ? 54.648 -23.811 -7.255  1.00 13.82 ?  24   VAL   B CB   1 
ATOM   4387 C  CG1  . VAL   B 1 24  ? 55.862 -22.930 -7.574  1.00 14.28 ?  24   VAL   B CG1  1 
ATOM   4388 C  CG2  . VAL   B 1 24  ? 54.222 -23.646 -5.816  1.00 14.98 ?  24   VAL   B CG2  1 
ATOM   4389 H  H    . VAL   B 1 24  ? 52.614 -25.165 -7.574  1.00 14.61 ?  24   VAL   B H    1 
ATOM   4390 H  HA   . VAL   B 1 24  ? 53.133 -22.617 -7.969  1.00 15.45 ?  24   VAL   B HA   1 
ATOM   4391 H  HB   . VAL   B 1 24  ? 54.908 -24.737 -7.378  1.00 16.61 ?  24   VAL   B HB   1 
ATOM   4392 H  HG11 . VAL   B 1 24  ? 56.448 -22.917 -6.802  1.00 17.16 ?  24   VAL   B HG11 1 
ATOM   4393 H  HG12 . VAL   B 1 24  ? 56.327 -23.306 -8.336  1.00 17.16 ?  24   VAL   B HG12 1 
ATOM   4394 H  HG13 . VAL   B 1 24  ? 55.556 -22.033 -7.774  1.00 17.16 ?  24   VAL   B HG13 1 
ATOM   4395 H  HG21 . VAL   B 1 24  ? 54.948 -23.919 -5.237  1.00 18.01 ?  24   VAL   B HG21 1 
ATOM   4396 H  HG22 . VAL   B 1 24  ? 54.001 -22.715 -5.657  1.00 18.01 ?  24   VAL   B HG22 1 
ATOM   4397 H  HG23 . VAL   B 1 24  ? 53.440 -24.203 -5.650  1.00 18.01 ?  24   VAL   B HG23 1 
ATOM   4398 N  N    . GLU   B 1 25  ? 54.199 -24.615 -10.239 1.00 13.77 ?  25   GLU   B N    1 
ATOM   4399 C  CA   . GLU   B 1 25  ? 54.585 -24.659 -11.643 1.00 15.58 ?  25   GLU   B CA   1 
ATOM   4400 C  C    . GLU   B 1 25  ? 53.476 -24.107 -12.530 1.00 14.23 ?  25   GLU   B C    1 
ATOM   4401 O  O    . GLU   B 1 25  ? 53.746 -23.383 -13.498 1.00 14.98 ?  25   GLU   B O    1 
ATOM   4402 C  CB   . GLU   B 1 25  ? 54.965 -26.086 -12.033 1.00 20.48 ?  25   GLU   B CB   1 
ATOM   4403 C  CG   . GLU   B 1 25  ? 56.273 -26.543 -11.396 1.00 27.65 ?  25   GLU   B CG   1 
ATOM   4404 C  CD   . GLU   B 1 25  ? 57.391 -25.518 -11.514 1.00 33.63 ?  25   GLU   B CD   1 
ATOM   4405 O  OE1  . GLU   B 1 25  ? 57.707 -25.099 -12.648 1.00 36.34 ?  25   GLU   B OE1  1 
ATOM   4406 O  OE2  . GLU   B 1 25  ? 57.941 -25.118 -10.464 1.00 36.24 -1 25   GLU   B OE2  1 
ATOM   4407 H  H    . GLU   B 1 25  ? 54.164 -25.380 -9.848  1.00 16.55 ?  25   GLU   B H    1 
ATOM   4408 H  HA   . GLU   B 1 25  ? 55.349 -24.083 -11.774 1.00 18.72 ?  25   GLU   B HA   1 
ATOM   4409 H  HB2  . GLU   B 1 25  ? 54.265 -26.695 -11.738 1.00 24.60 ?  25   GLU   B HB2  1 
ATOM   4410 H  HB3  . GLU   B 1 25  ? 55.063 -26.139 -12.996 1.00 24.60 ?  25   GLU   B HB3  1 
ATOM   4411 H  HG2  . GLU   B 1 25  ? 56.131 -26.695 -10.454 1.00 33.20 ?  25   GLU   B HG2  1 
ATOM   4412 H  HG3  . GLU   B 1 25  ? 56.571 -27.353 -11.834 1.00 33.20 ?  25   GLU   B HG3  1 
ATOM   4413 N  N    . GLU   B 1 26  ? 52.222 -24.418 -12.199 1.00 13.58 ?  26   GLU   B N    1 
ATOM   4414 C  CA   . GLU   B 1 26  ? 51.099 -23.885 -12.964 1.00 14.07 ?  26   GLU   B CA   1 
ATOM   4415 C  C    . GLU   B 1 26  ? 51.051 -22.366 -12.879 1.00 13.15 ?  26   GLU   B C    1 
ATOM   4416 O  O    . GLU   B 1 26  ? 50.855 -21.686 -13.891 1.00 14.36 ?  26   GLU   B O    1 
ATOM   4417 C  CB   . GLU   B 1 26  ? 49.786 -24.477 -12.453 1.00 15.94 ?  26   GLU   B CB   1 
ATOM   4418 C  CG   . GLU   B 1 26  ? 49.363 -25.762 -13.131 1.00 19.64 ?  26   GLU   B CG   1 
ATOM   4419 C  CD   . GLU   B 1 26  ? 49.108 -25.613 -14.627 1.00 20.94 ?  26   GLU   B CD   1 
ATOM   4420 O  OE1  . GLU   B 1 26  ? 48.130 -24.955 -15.042 1.00 20.89 ?  26   GLU   B OE1  1 
ATOM   4421 O  OE2  . GLU   B 1 26  ? 49.892 -26.189 -15.389 1.00 23.55 -1 26   GLU   B OE2  1 
ATOM   4422 H  H    . GLU   B 1 26  ? 51.996 -24.926 -11.537 1.00 16.32 ?  26   GLU   B H    1 
ATOM   4423 H  HA   . GLU   B 1 26  ? 51.205 -24.129 -13.892 1.00 16.91 ?  26   GLU   B HA   1 
ATOM   4424 H  HB2  . GLU   B 1 26  ? 49.877 -24.664 -11.503 1.00 19.16 ?  26   GLU   B HB2  1 
ATOM   4425 H  HB3  . GLU   B 1 26  ? 49.079 -23.824 -12.585 1.00 19.16 ?  26   GLU   B HB3  1 
ATOM   4426 H  HG2  . GLU   B 1 26  ? 50.070 -26.406 -13.022 1.00 23.59 ?  26   GLU   B HG2  1 
ATOM   4427 H  HG3  . GLU   B 1 26  ? 48.545 -26.075 -12.721 1.00 23.59 ?  26   GLU   B HG3  1 
ATOM   4428 N  N    . ALA   B 1 27  ? 51.196 -21.817 -11.670 1.00 12.21 ?  27   ALA   B N    1 
ATOM   4429 C  CA   . ALA   B 1 27  ? 51.157 -20.368 -11.514 1.00 12.83 ?  27   ALA   B CA   1 
ATOM   4430 C  C    . ALA   B 1 27  ? 52.228 -19.702 -12.366 1.00 13.95 ?  27   ALA   B C    1 
ATOM   4431 O  O    . ALA   B 1 27  ? 51.965 -18.702 -13.046 1.00 14.54 ?  27   ALA   B O    1 
ATOM   4432 C  CB   . ALA   B 1 27  ? 51.319 -19.996 -10.040 1.00 12.96 ?  27   ALA   B CB   1 
ATOM   4433 H  H    . ALA   B 1 27  ? 51.314 -22.254 -10.935 1.00 14.67 ?  27   ALA   B H    1 
ATOM   4434 H  HA   . ALA   B 1 27  ? 50.297 -20.039 -11.807 1.00 15.42 ?  27   ALA   B HA   1 
ATOM   4435 H  HB1  . ALA   B 1 27  ? 51.287 -19.029 -9.949  1.00 15.58 ?  27   ALA   B HB1  1 
ATOM   4436 H  HB2  . ALA   B 1 27  ? 50.592 -20.395 -9.531  1.00 15.58 ?  27   ALA   B HB2  1 
ATOM   4437 H  HB3  . ALA   B 1 27  ? 52.169 -20.329 -9.715  1.00 15.58 ?  27   ALA   B HB3  1 
ATOM   4438 N  N    . LYS   B 1 28  ? 53.439 -20.258 -12.366 1.00 15.25 ?  28   LYS   B N    1 
ATOM   4439 C  CA   . LYS   B 1 28  ? 54.518 -19.638 -13.129 1.00 17.33 ?  28   LYS   B CA   1 
ATOM   4440 C  C    . LYS   B 1 28  ? 54.266 -19.713 -14.631 1.00 17.92 ?  28   LYS   B C    1 
ATOM   4441 O  O    . LYS   B 1 28  ? 54.668 -18.804 -15.368 1.00 18.78 ?  28   LYS   B O    1 
ATOM   4442 C  CB   . LYS   B 1 28  ? 55.873 -20.238 -12.736 1.00 20.96 ?  28   LYS   B CB   1 
ATOM   4443 C  CG   . LYS   B 1 28  ? 56.271 -19.900 -11.302 1.00 24.59 ?  28   LYS   B CG   1 
ATOM   4444 C  CD   . LYS   B 1 28  ? 57.696 -20.316 -10.966 1.00 29.46 ?  28   LYS   B CD   1 
ATOM   4445 C  CE   . LYS   B 1 28  ? 57.788 -21.789 -10.639 1.00 34.16 ?  28   LYS   B CE   1 
ATOM   4446 N  NZ   . LYS   B 1 28  ? 59.137 -22.148 -10.113 1.00 36.68 ?  28   LYS   B NZ   1 
ATOM   4447 H  H    . LYS   B 1 28  ? 53.662 -20.972 -11.941 1.00 18.32 ?  28   LYS   B H    1 
ATOM   4448 H  HA   . LYS   B 1 28  ? 54.551 -18.698 -12.898 1.00 20.81 ?  28   LYS   B HA   1 
ATOM   4449 H  HB2  . LYS   B 1 28  ? 55.833 -21.201 -12.815 1.00 25.18 ?  28   LYS   B HB2  1 
ATOM   4450 H  HB3  . LYS   B 1 28  ? 56.561 -19.883 -13.325 1.00 25.18 ?  28   LYS   B HB3  1 
ATOM   4451 H  HG2  . LYS   B 1 28  ? 56.200 -18.939 -11.174 1.00 29.53 ?  28   LYS   B HG2  1 
ATOM   4452 H  HG3  . LYS   B 1 28  ? 55.671 -20.359 -10.695 1.00 29.53 ?  28   LYS   B HG3  1 
ATOM   4453 H  HD2  . LYS   B 1 28  ? 58.268 -20.137 -11.728 1.00 35.38 ?  28   LYS   B HD2  1 
ATOM   4454 H  HD3  . LYS   B 1 28  ? 58.000 -19.812 -10.194 1.00 35.38 ?  28   LYS   B HD3  1 
ATOM   4455 H  HE2  . LYS   B 1 28  ? 57.129 -22.007 -9.961  1.00 41.02 ?  28   LYS   B HE2  1 
ATOM   4456 H  HE3  . LYS   B 1 28  ? 57.626 -22.307 -11.442 1.00 41.02 ?  28   LYS   B HE3  1 
ATOM   4457 H  HZ1  . LYS   B 1 28  ? 59.169 -23.017 -9.927  1.00 44.05 ?  28   LYS   B HZ1  1 
ATOM   4458 H  HZ2  . LYS   B 1 28  ? 59.759 -21.957 -10.720 1.00 44.05 ?  28   LYS   B HZ2  1 
ATOM   4459 H  HZ3  . LYS   B 1 28  ? 59.306 -21.686 -9.371  1.00 44.05 ?  28   LYS   B HZ3  1 
ATOM   4460 N  N    . LYS   B 1 29  ? 53.577 -20.756 -15.098 1.00 18.94 ?  29   LYS   B N    1 
ATOM   4461 C  CA   . LYS   B 1 29  ? 53.289 -20.888 -16.525 1.00 21.60 ?  29   LYS   B CA   1 
ATOM   4462 C  C    . LYS   B 1 29  ? 52.051 -20.100 -16.943 1.00 20.35 ?  29   LYS   B C    1 
ATOM   4463 O  O    . LYS   B 1 29  ? 52.062 -19.439 -17.987 1.00 21.60 ?  29   LYS   B O    1 
ATOM   4464 C  CB   . LYS   B 1 29  ? 53.121 -22.363 -16.891 1.00 26.44 ?  29   LYS   B CB   1 
ATOM   4465 C  CG   . LYS   B 1 29  ? 52.868 -22.610 -18.371 1.00 31.24 ?  29   LYS   B CG   1 
ATOM   4466 C  CD   . LYS   B 1 29  ? 53.110 -24.065 -18.752 1.00 35.38 ?  29   LYS   B CD   1 
ATOM   4467 C  CE   . LYS   B 1 29  ? 52.085 -24.995 -18.124 1.00 38.56 ?  29   LYS   B CE   1 
ATOM   4468 N  NZ   . LYS   B 1 29  ? 52.339 -26.418 -18.489 1.00 40.69 ?  29   LYS   B NZ   1 
ATOM   4469 H  H    . LYS   B 1 29  ? 53.266 -21.394 -14.612 1.00 22.75 ?  29   LYS   B H    1 
ATOM   4470 H  HA   . LYS   B 1 29  ? 54.037 -20.539 -17.027 1.00 25.94 ?  29   LYS   B HA   1 
ATOM   4471 H  HB2  . LYS   B 1 29  ? 53.933 -22.835 -16.648 1.00 31.75 ?  29   LYS   B HB2  1 
ATOM   4472 H  HB3  . LYS   B 1 29  ? 52.370 -22.725 -16.398 1.00 31.75 ?  29   LYS   B HB3  1 
ATOM   4473 H  HG2  . LYS   B 1 29  ? 51.946 -22.393 -18.578 1.00 37.51 ?  29   LYS   B HG2  1 
ATOM   4474 H  HG3  . LYS   B 1 29  ? 53.468 -22.056 -18.896 1.00 37.51 ?  29   LYS   B HG3  1 
ATOM   4475 H  HD2  . LYS   B 1 29  ? 53.051 -24.158 -19.716 1.00 42.48 ?  29   LYS   B HD2  1 
ATOM   4476 H  HD3  . LYS   B 1 29  ? 53.990 -24.334 -18.444 1.00 42.48 ?  29   LYS   B HD3  1 
ATOM   4477 H  HE2  . LYS   B 1 29  ? 52.129 -24.918 -17.158 1.00 46.30 ?  29   LYS   B HE2  1 
ATOM   4478 H  HE3  . LYS   B 1 29  ? 51.199 -24.754 -18.439 1.00 46.30 ?  29   LYS   B HE3  1 
ATOM   4479 H  HZ1  . LYS   B 1 29  ? 51.728 -26.943 -18.111 1.00 48.85 ?  29   LYS   B HZ1  1 
ATOM   4480 H  HZ2  . LYS   B 1 29  ? 52.299 -26.517 -19.373 1.00 48.85 ?  29   LYS   B HZ2  1 
ATOM   4481 H  HZ3  . LYS   B 1 29  ? 53.146 -26.664 -18.206 1.00 48.85 ?  29   LYS   B HZ3  1 
ATOM   4482 N  N    . VAL   B 1 30  ? 50.980 -20.171 -16.147 1.00 18.72 ?  30   VAL   B N    1 
ATOM   4483 C  CA   . VAL   B 1 30  ? 49.685 -19.593 -16.516 1.00 19.47 ?  30   VAL   B CA   1 
ATOM   4484 C  C    . VAL   B 1 30  ? 49.677 -18.079 -16.358 1.00 18.66 ?  30   VAL   B C    1 
ATOM   4485 O  O    . VAL   B 1 30  ? 48.938 -17.372 -17.064 1.00 19.49 ?  30   VAL   B O    1 
ATOM   4486 C  CB   . VAL   B 1 30  ? 48.585 -20.231 -15.643 1.00 20.67 ?  30   VAL   B CB   1 
ATOM   4487 C  CG1  . VAL   B 1 30  ? 47.286 -19.431 -15.711 1.00 21.22 ?  30   VAL   B CG1  1 
ATOM   4488 C  CG2  . VAL   B 1 30  ? 48.360 -21.687 -16.040 1.00 21.77 ?  30   VAL   B CG2  1 
ATOM   4489 H  H    . VAL   B 1 30  ? 50.973 -20.571 -15.375 1.00 22.48 ?  30   VAL   B H    1 
ATOM   4490 H  HA   . VAL   B 1 30  ? 49.492 -19.821 -17.439 1.00 23.39 ?  30   VAL   B HA   1 
ATOM   4491 H  HB   . VAL   B 1 30  ? 48.877 -20.235 -14.718 1.00 24.83 ?  30   VAL   B HB   1 
ATOM   4492 H  HG11 . VAL   B 1 30  ? 46.548 -20.019 -15.483 1.00 25.49 ?  30   VAL   B HG11 1 
ATOM   4493 H  HG12 . VAL   B 1 30  ? 47.327 -18.701 -15.077 1.00 25.49 ?  30   VAL   B HG12 1 
ATOM   4494 H  HG13 . VAL   B 1 30  ? 47.164 -19.098 -16.609 1.00 25.49 ?  30   VAL   B HG13 1 
ATOM   4495 H  HG21 . VAL   B 1 30  ? 47.670 -22.071 -15.471 1.00 26.14 ?  30   VAL   B HG21 1 
ATOM   4496 H  HG22 . VAL   B 1 30  ? 48.075 -21.721 -16.967 1.00 26.14 ?  30   VAL   B HG22 1 
ATOM   4497 H  HG23 . VAL   B 1 30  ? 49.188 -22.177 -15.930 1.00 26.14 ?  30   VAL   B HG23 1 
ATOM   4498 N  N    . LYS   B 1 31  ? 50.455 -17.574 -15.416 1.00 18.14 ?  31   LYS   B N    1 
ATOM   4499 C  CA   . LYS   B 1 31  ? 50.471 -16.165 -15.055 1.00 18.74 ?  31   LYS   B CA   1 
ATOM   4500 C  C    . LYS   B 1 31  ? 49.067 -15.701 -14.667 1.00 16.31 ?  31   LYS   B C    1 
ATOM   4501 O  O    . LYS   B 1 31  ? 48.524 -14.777 -15.286 1.00 17.48 ?  31   LYS   B O    1 
ATOM   4502 C  CB   . LYS   B 1 31  ? 51.097 -15.346 -16.194 1.00 21.84 ?  31   LYS   B CB   1 
ATOM   4503 C  CG   . LYS   B 1 31  ? 52.509 -15.810 -16.555 1.00 24.99 ?  31   LYS   B CG   1 
ATOM   4504 C  CD   . LYS   B 1 31  ? 53.093 -15.029 -17.719 1.00 28.67 ?  31   LYS   B CD   1 
ATOM   4505 C  CE   . LYS   B 1 31  ? 54.588 -15.262 -17.854 1.00 31.69 ?  31   LYS   B CE   1 
ATOM   4506 N  NZ   . LYS   B 1 31  ? 55.310 -14.820 -16.630 1.00 33.66 ?  31   LYS   B NZ   1 
ATOM   4507 H  H    . LYS   B 1 31  ? 51.001 -18.059 -14.964 1.00 21.79 ?  31   LYS   B H    1 
ATOM   4508 H  HA   . LYS   B 1 31  ? 51.030 -16.075 -14.282 1.00 22.51 ?  31   LYS   B HA   1 
ATOM   4509 H  HB2  . LYS   B 1 31  ? 50.546 -15.425 -16.991 1.00 26.24 ?  31   LYS   B HB2  1 
ATOM   4510 H  HB3  . LYS   B 1 31  ? 51.149 -14.421 -15.917 1.00 26.24 ?  31   LYS   B HB3  1 
ATOM   4511 H  HG2  . LYS   B 1 31  ? 53.080 -15.694 -15.780 1.00 30.01 ?  31   LYS   B HG2  1 
ATOM   4512 H  HG3  . LYS   B 1 31  ? 52.478 -16.751 -16.804 1.00 30.01 ?  31   LYS   B HG3  1 
ATOM   4513 H  HD2  . LYS   B 1 31  ? 52.664 -15.316 -18.540 1.00 34.42 ?  31   LYS   B HD2  1 
ATOM   4514 H  HD3  . LYS   B 1 31  ? 52.943 -14.085 -17.572 1.00 34.42 ?  31   LYS   B HD3  1 
ATOM   4515 H  HE2  . LYS   B 1 31  ? 54.762 -16.209 -17.984 1.00 38.05 ?  31   LYS   B HE2  1 
ATOM   4516 H  HE3  . LYS   B 1 31  ? 54.929 -14.753 -18.608 1.00 38.05 ?  31   LYS   B HE3  1 
ATOM   4517 H  HZ1  . LYS   B 1 31  ? 56.188 -14.829 -16.773 1.00 40.41 ?  31   LYS   B HZ1  1 
ATOM   4518 H  HZ2  . LYS   B 1 31  ? 55.060 -13.993 -16.414 1.00 40.41 ?  31   LYS   B HZ2  1 
ATOM   4519 H  HZ3  . LYS   B 1 31  ? 55.122 -15.365 -15.952 1.00 40.41 ?  31   LYS   B HZ3  1 
ATOM   4520 N  N    . PRO   B 1 32  ? 48.457 -16.301 -13.639 1.00 13.69 ?  32   PRO   B N    1 
ATOM   4521 C  CA   . PRO   B 1 32  ? 47.078 -15.945 -13.285 1.00 12.78 ?  32   PRO   B CA   1 
ATOM   4522 C  C    . PRO   B 1 32  ? 46.991 -14.602 -12.576 1.00 13.04 ?  32   PRO   B C    1 
ATOM   4523 O  O    . PRO   B 1 32  ? 47.907 -14.180 -11.864 1.00 14.18 ?  32   PRO   B O    1 
ATOM   4524 C  CB   . PRO   B 1 32  ? 46.678 -17.067 -12.319 1.00 13.08 ?  32   PRO   B CB   1 
ATOM   4525 C  CG   . PRO   B 1 32  ? 47.969 -17.390 -11.626 1.00 13.40 ?  32   PRO   B CG   1 
ATOM   4526 C  CD   . PRO   B 1 32  ? 49.024 -17.288 -12.698 1.00 13.73 ?  32   PRO   B CD   1 
ATOM   4527 H  HA   . PRO   B 1 32  ? 46.499 -15.960 -14.072 1.00 15.36 ?  32   PRO   B HA   1 
ATOM   4528 H  HB2  . PRO   B 1 32  ? 46.013 -16.743 -11.692 1.00 15.71 ?  32   PRO   B HB2  1 
ATOM   4529 H  HB3  . PRO   B 1 32  ? 46.347 -17.836 -12.813 1.00 15.71 ?  32   PRO   B HB3  1 
ATOM   4530 H  HG2  . PRO   B 1 32  ? 48.134 -16.738 -10.922 1.00 16.10 ?  32   PRO   B HG2  1 
ATOM   4531 H  HG3  . PRO   B 1 32  ? 47.935 -18.286 -11.261 1.00 16.10 ?  32   PRO   B HG3  1 
ATOM   4532 H  HD2  . PRO   B 1 32  ? 49.852 -16.957 -12.327 1.00 16.50 ?  32   PRO   B HD2  1 
ATOM   4533 H  HD3  . PRO   B 1 32  ? 49.139 -18.144 -13.134 1.00 16.50 ?  32   PRO   B HD3  1 
ATOM   4534 N  N    . THR   B 1 33  ? 45.840 -13.946 -12.747 1.00 12.16 ?  33   THR   B N    1 
ATOM   4535 C  CA   . THR   B 1 33  ? 45.547 -12.771 -11.934 1.00 12.55 ?  33   THR   B CA   1 
ATOM   4536 C  C    . THR   B 1 33  ? 45.502 -13.126 -10.453 1.00 12.32 ?  33   THR   B C    1 
ATOM   4537 O  O    . THR   B 1 33  ? 45.970 -12.348 -9.610  1.00 13.50 ?  33   THR   B O    1 
ATOM   4538 C  CB   . THR   B 1 33  ? 44.224 -12.141 -12.381 1.00 13.29 ?  33   THR   B CB   1 
ATOM   4539 O  OG1  . THR   B 1 33  ? 44.274 -11.879 -13.785 1.00 13.59 ?  33   THR   B OG1  1 
ATOM   4540 C  CG2  . THR   B 1 33  ? 43.968 -10.843 -11.639 1.00 14.55 ?  33   THR   B CG2  1 
ATOM   4541 H  H    . THR   B 1 33  ? 45.215 -14.165 -13.308 1.00 14.62 ?  33   THR   B H    1 
ATOM   4542 H  HA   . THR   B 1 33  ? 46.244 -12.120 -12.068 1.00 15.08 ?  33   THR   B HA   1 
ATOM   4543 H  HB   . THR   B 1 33  ? 43.491 -12.753 -12.192 1.00 15.97 ?  33   THR   B HB   1 
ATOM   4544 H  HG1  . THR   B 1 33  ? 43.551 -11.527 -14.043 1.00 16.34 ?  33   THR   B HG1  1 
ATOM   4545 H  HG21 . THR   B 1 33  ? 43.207 -10.385 -12.024 1.00 17.48 ?  33   THR   B HG21 1 
ATOM   4546 H  HG22 . THR   B 1 33  ? 43.789 -11.023 -10.703 1.00 17.48 ?  33   THR   B HG22 1 
ATOM   4547 H  HG23 . THR   B 1 33  ? 44.748 -10.268 -11.706 1.00 17.48 ?  33   THR   B HG23 1 
ATOM   4548 N  N    . VAL   B 1 34  ? 44.950 -14.296 -10.113 1.00 11.50 ?  34   VAL   B N    1 
ATOM   4549 C  CA   . VAL   B 1 34  ? 44.763 -14.698 -8.721  1.00 11.04 ?  34   VAL   B CA   1 
ATOM   4550 C  C    . VAL   B 1 34  ? 45.195 -16.145 -8.558  1.00 10.14 ?  34   VAL   B C    1 
ATOM   4551 O  O    . VAL   B 1 34  ? 44.671 -17.029 -9.245  1.00 10.90 ?  34   VAL   B O    1 
ATOM   4552 C  CB   . VAL   B 1 34  ? 43.294 -14.559 -8.264  1.00 12.26 ?  34   VAL   B CB   1 
ATOM   4553 C  CG1  . VAL   B 1 34  ? 43.146 -15.004 -6.813  1.00 12.54 ?  34   VAL   B CG1  1 
ATOM   4554 C  CG2  . VAL   B 1 34  ? 42.791 -13.137 -8.458  1.00 13.55 ?  34   VAL   B CG2  1 
ATOM   4555 H  H    . VAL   B 1 34  ? 44.686 -14.889 -10.677 1.00 13.83 ?  34   VAL   B H    1 
ATOM   4556 H  HA   . VAL   B 1 34  ? 45.316 -14.146 -8.141  1.00 13.27 ?  34   VAL   B HA   1 
ATOM   4557 H  HB   . VAL   B 1 34  ? 42.742 -15.144 -8.810  1.00 14.74 ?  34   VAL   B HB   1 
ATOM   4558 H  HG11 . VAL   B 1 34  ? 42.293 -14.687 -6.473  1.00 15.07 ?  34   VAL   B HG11 1 
ATOM   4559 H  HG12 . VAL   B 1 34  ? 43.178 -15.971 -6.770  1.00 15.07 ?  34   VAL   B HG12 1 
ATOM   4560 H  HG13 . VAL   B 1 34  ? 43.869 -14.622 -6.292  1.00 15.07 ?  34   VAL   B HG13 1 
ATOM   4561 H  HG21 . VAL   B 1 34  ? 41.876 -13.079 -8.140  1.00 16.29 ?  34   VAL   B HG21 1 
ATOM   4562 H  HG22 . VAL   B 1 34  ? 43.356 -12.531 -7.957  1.00 16.29 ?  34   VAL   B HG22 1 
ATOM   4563 H  HG23 . VAL   B 1 34  ? 42.825 -12.916 -9.404  1.00 16.29 ?  34   VAL   B HG23 1 
ATOM   4564 N  N    . VAL   B 1 35  ? 46.106 -16.397 -7.618  1.00 9.81  ?  35   VAL   B N    1 
ATOM   4565 C  CA   . VAL   B 1 35  ? 46.341 -17.742 -7.105  1.00 9.62  ?  35   VAL   B CA   1 
ATOM   4566 C  C    . VAL   B 1 35  ? 45.805 -17.805 -5.684  1.00 9.21  ?  35   VAL   B C    1 
ATOM   4567 O  O    . VAL   B 1 35  ? 46.028 -16.884 -4.892  1.00 10.00 ?  35   VAL   B O    1 
ATOM   4568 C  CB   . VAL   B 1 35  ? 47.823 -18.160 -7.191  1.00 10.23 ?  35   VAL   B CB   1 
ATOM   4569 C  CG1  . VAL   B 1 35  ? 48.724 -17.316 -6.286  1.00 11.07 ?  35   VAL   B CG1  1 
ATOM   4570 C  CG2  . VAL   B 1 35  ? 47.972 -19.647 -6.865  1.00 11.14 ?  35   VAL   B CG2  1 
ATOM   4571 H  H    . VAL   B 1 35  ? 46.606 -15.795 -7.256  1.00 11.80 ?  35   VAL   B H    1 
ATOM   4572 H  HA   . VAL   B 1 35  ? 45.828 -18.369 -7.631  1.00 11.57 ?  35   VAL   B HA   1 
ATOM   4573 H  HB   . VAL   B 1 35  ? 48.125 -18.041 -8.105  1.00 12.31 ?  35   VAL   B HB   1 
ATOM   4574 H  HG11 . VAL   B 1 35  ? 49.648 -17.548 -6.464  1.00 13.31 ?  35   VAL   B HG11 1 
ATOM   4575 H  HG12 . VAL   B 1 35  ? 48.566 -16.385 -6.478  1.00 13.31 ?  35   VAL   B HG12 1 
ATOM   4576 H  HG13 . VAL   B 1 35  ? 48.506 -17.512 -5.360  1.00 13.31 ?  35   VAL   B HG13 1 
ATOM   4577 H  HG21 . VAL   B 1 35  ? 48.894 -19.917 -6.984  1.00 13.39 ?  35   VAL   B HG21 1 
ATOM   4578 H  HG22 . VAL   B 1 35  ? 47.699 -19.804 -5.943  1.00 13.39 ?  35   VAL   B HG22 1 
ATOM   4579 H  HG23 . VAL   B 1 35  ? 47.399 -20.167 -7.460  1.00 13.39 ?  35   VAL   B HG23 1 
ATOM   4580 N  N    . VAL   B 1 36  ? 45.083 -18.877 -5.371  1.00 9.42  ?  36   VAL   B N    1 
ATOM   4581 C  CA   . VAL   B 1 36  ? 44.537 -19.086 -4.038  1.00 9.18  ?  36   VAL   B CA   1 
ATOM   4582 C  C    . VAL   B 1 36  ? 45.546 -19.842 -3.184  1.00 8.75  ?  36   VAL   B C    1 
ATOM   4583 O  O    . VAL   B 1 36  ? 46.093 -20.875 -3.601  1.00 9.94  ?  36   VAL   B O    1 
ATOM   4584 C  CB   . VAL   B 1 36  ? 43.203 -19.847 -4.113  1.00 9.48  ?  36   VAL   B CB   1 
ATOM   4585 C  CG1  . VAL   B 1 36  ? 42.706 -20.206 -2.723  1.00 10.34 ?  36   VAL   B CG1  1 
ATOM   4586 C  CG2  . VAL   B 1 36  ? 42.171 -19.023 -4.854  1.00 10.31 ?  36   VAL   B CG2  1 
ATOM   4587 H  H    . VAL   B 1 36  ? 44.907 -19.514 -5.919  1.00 11.33 ?  36   VAL   B H    1 
ATOM   4588 H  HA   . VAL   B 1 36  ? 44.371 -18.231 -3.617  1.00 11.04 ?  36   VAL   B HA   1 
ATOM   4589 H  HB   . VAL   B 1 36  ? 43.336 -20.675 -4.601  1.00 11.41 ?  36   VAL   B HB   1 
ATOM   4590 H  HG11 . VAL   B 1 36  ? 41.766 -20.437 -2.772  1.00 12.44 ?  36   VAL   B HG11 1 
ATOM   4591 H  HG12 . VAL   B 1 36  ? 43.214 -20.959 -2.383  1.00 12.44 ?  36   VAL   B HG12 1 
ATOM   4592 H  HG13 . VAL   B 1 36  ? 42.823 -19.437 -2.138  1.00 12.44 ?  36   VAL   B HG13 1 
ATOM   4593 H  HG21 . VAL   B 1 36  ? 41.334 -19.511 -4.875  1.00 12.40 ?  36   VAL   B HG21 1 
ATOM   4594 H  HG22 . VAL   B 1 36  ? 42.055 -18.179 -4.395  1.00 12.40 ?  36   VAL   B HG22 1 
ATOM   4595 H  HG23 . VAL   B 1 36  ? 42.487 -18.869 -5.760  1.00 12.40 ?  36   VAL   B HG23 1 
ATOM   4596 N  N    . ASN   B 1 37  ? 45.763 -19.348 -1.967  1.00 9.21  ?  37   ASN   B N    1 
ATOM   4597 C  CA   . ASN   B 1 37  ? 46.518 -20.073 -0.958  1.00 9.33  ?  37   ASN   B CA   1 
ATOM   4598 C  C    . ASN   B 1 37  ? 45.567 -20.747 0.021   1.00 9.41  ?  37   ASN   B C    1 
ATOM   4599 O  O    . ASN   B 1 37  ? 44.553 -20.167 0.426   1.00 10.22 ?  37   ASN   B O    1 
ATOM   4600 C  CB   . ASN   B 1 37  ? 47.442 -19.128 -0.196  1.00 9.65  ?  37   ASN   B CB   1 
ATOM   4601 C  CG   . ASN   B 1 37  ? 48.302 -19.843 0.815   1.00 9.92  ?  37   ASN   B CG   1 
ATOM   4602 O  OD1  . ASN   B 1 37  ? 48.636 -21.019 0.647   1.00 10.48 ?  37   ASN   B OD1  1 
ATOM   4603 N  ND2  . ASN   B 1 37  ? 48.653 -19.142 1.887   1.00 10.15 ?  37   ASN   B ND2  1 
ATOM   4604 H  H    . ASN   B 1 37  ? 45.484 -18.579 -1.696  1.00 11.08 ?  37   ASN   B H    1 
ATOM   4605 H  HA   . ASN   B 1 37  ? 47.059 -20.758 -1.377  1.00 11.22 ?  37   ASN   B HA   1 
ATOM   4606 H  HB2  . ASN   B 1 37  ? 48.034 -18.689 -0.822  1.00 11.60 ?  37   ASN   B HB2  1 
ATOM   4607 H  HB3  . ASN   B 1 37  ? 46.911 -18.472 0.281   1.00 11.60 ?  37   ASN   B HB3  1 
ATOM   4608 H  HD21 . ASN   B 1 37  ? 49.147 -19.504 2.494   1.00 12.21 ?  37   ASN   B HD21 1 
ATOM   4609 H  HD22 . ASN   B 1 37  ? 48.401 -18.332 1.973   1.00 12.21 ?  37   ASN   B HD22 1 
ATOM   4610 N  N    . ALA   B 1 38  ? 45.919 -21.980 0.401   1.00 9.79  ?  38   ALA   B N    1 
ATOM   4611 C  CA   . ALA   B 1 38  ? 45.267 -22.724 1.480   1.00 10.41 ?  38   ALA   B CA   1 
ATOM   4612 C  C    . ALA   B 1 38  ? 45.855 -22.241 2.806   1.00 9.82  ?  38   ALA   B C    1 
ATOM   4613 O  O    . ALA   B 1 38  ? 46.758 -22.853 3.392   1.00 10.88 ?  38   ALA   B O    1 
ATOM   4614 C  CB   . ALA   B 1 38  ? 45.484 -24.220 1.288   1.00 11.34 ?  38   ALA   B CB   1 
ATOM   4615 H  H    . ALA   B 1 38  ? 46.569 -22.419 0.042   1.00 11.77 ?  38   ALA   B H    1 
ATOM   4616 H  HA   . ALA   B 1 38  ? 44.315 -22.539 1.477   1.00 12.51 ?  38   ALA   B HA   1 
ATOM   4617 H  HB1  . ALA   B 1 38  ? 45.038 -24.695 2.014   1.00 13.64 ?  38   ALA   B HB1  1 
ATOM   4618 H  HB2  . ALA   B 1 38  ? 45.098 -24.484 0.440   1.00 13.64 ?  38   ALA   B HB2  1 
ATOM   4619 H  HB3  . ALA   B 1 38  ? 46.430 -24.407 1.303   1.00 13.64 ?  38   ALA   B HB3  1 
ATOM   4620 N  N    . ALA   B 1 39  ? 45.337 -21.104 3.269   1.00 9.99  ?  39   ALA   B N    1 
ATOM   4621 C  CA   . ALA   B 1 39  ? 45.889 -20.370 4.397   1.00 10.48 ?  39   ALA   B CA   1 
ATOM   4622 C  C    . ALA   B 1 39  ? 45.276 -20.817 5.724   1.00 10.04 ?  39   ALA   B C    1 
ATOM   4623 O  O    . ALA   B 1 39  ? 44.248 -21.495 5.776   1.00 10.92 ?  39   ALA   B O    1 
ATOM   4624 C  CB   . ALA   B 1 39  ? 45.640 -18.871 4.203   1.00 11.26 ?  39   ALA   B CB   1 
ATOM   4625 H  H    . ALA   B 1 39  ? 44.637 -20.729 2.932   1.00 12.01 ?  39   ALA   B H    1 
ATOM   4626 H  HA   . ALA   B 1 39  ? 46.844 -20.513 4.437   1.00 12.60 ?  39   ALA   B HA   1 
ATOM   4627 H  HB1  . ALA   B 1 39  ? 46.014 -18.386 4.957   1.00 13.53 ?  39   ALA   B HB1  1 
ATOM   4628 H  HB2  . ALA   B 1 39  ? 46.071 -18.580 3.381   1.00 13.53 ?  39   ALA   B HB2  1 
ATOM   4629 H  HB3  . ALA   B 1 39  ? 44.686 -18.709 4.148   1.00 13.53 ?  39   ALA   B HB3  1 
ATOM   4630 N  N    . ASN   B 1 40  ? 45.917 -20.393 6.810   1.00 10.90 ?  40   ASN   B N    1 
ATOM   4631 C  CA   . ASN   B 1 40  ? 45.361 -20.445 8.152   1.00 11.60 ?  40   ASN   B CA   1 
ATOM   4632 C  C    . ASN   B 1 40  ? 45.178 -19.019 8.674   1.00 11.30 ?  40   ASN   B C    1 
ATOM   4633 O  O    . ASN   B 1 40  ? 45.588 -18.039 8.042   1.00 11.40 ?  40   ASN   B O    1 
ATOM   4634 C  CB   . ASN   B 1 40  ? 46.221 -21.316 9.084   1.00 12.39 ?  40   ASN   B CB   1 
ATOM   4635 C  CG   . ASN   B 1 40  ? 47.675 -20.915 9.090   1.00 13.62 ?  40   ASN   B CG   1 
ATOM   4636 O  OD1  . ASN   B 1 40  ? 47.999 -19.734 9.130   1.00 15.65 ?  40   ASN   B OD1  1 
ATOM   4637 N  ND2  . ASN   B 1 40  ? 48.567 -21.900 9.059   1.00 13.89 ?  40   ASN   B ND2  1 
ATOM   4638 H  H    . ASN   B 1 40  ? 46.712 -20.061 6.786   1.00 13.11 ?  40   ASN   B H    1 
ATOM   4639 H  HA   . ASN   B 1 40  ? 44.482 -20.847 8.107   1.00 13.95 ?  40   ASN   B HA   1 
ATOM   4640 H  HB2  . ASN   B 1 40  ? 45.885 -21.231 9.991   1.00 14.89 ?  40   ASN   B HB2  1 
ATOM   4641 H  HB3  . ASN   B 1 40  ? 46.159 -22.238 8.793   1.00 14.89 ?  40   ASN   B HB3  1 
ATOM   4642 H  HD21 . ASN   B 1 40  ? 49.409 -21.725 9.059   1.00 16.70 ?  40   ASN   B HD21 1 
ATOM   4643 H  HD22 . ASN   B 1 40  ? 48.302 -22.720 9.036   1.00 16.70 ?  40   ASN   B HD22 1 
ATOM   4644 N  N    . VAL   B 1 41  ? 44.516 -18.894 9.830   1.00 11.76 ?  41   VAL   B N    1 
ATOM   4645 C  CA   . VAL   B 1 41  ? 44.064 -17.574 10.282  1.00 12.39 ?  41   VAL   B CA   1 
ATOM   4646 C  C    . VAL   B 1 41  ? 45.218 -16.619 10.572  1.00 12.23 ?  41   VAL   B C    1 
ATOM   4647 O  O    . VAL   B 1 41  ? 45.040 -15.396 10.492  1.00 12.19 ?  41   VAL   B O    1 
ATOM   4648 C  CB   . VAL   B 1 41  ? 43.090 -17.652 11.479  1.00 13.86 ?  41   VAL   B CB   1 
ATOM   4649 C  CG1  . VAL   B 1 41  ? 41.783 -18.322 11.081  1.00 14.26 ?  41   VAL   B CG1  1 
ATOM   4650 C  CG2  . VAL   B 1 41  ? 43.733 -18.348 12.664  1.00 14.68 ?  41   VAL   B CG2  1 
ATOM   4651 H  H    . VAL   B 1 41  ? 44.319 -19.542 10.355  1.00 14.13 ?  41   VAL   B H    1 
ATOM   4652 H  HA   . VAL   B 1 41  ? 43.561 -17.179 9.555   1.00 14.89 ?  41   VAL   B HA   1 
ATOM   4653 H  HB   . VAL   B 1 41  ? 42.875 -16.747 11.758  1.00 16.65 ?  41   VAL   B HB   1 
ATOM   4654 H  HG11 . VAL   B 1 41  ? 41.188 -18.334 11.849  1.00 17.13 ?  41   VAL   B HG11 1 
ATOM   4655 H  HG12 . VAL   B 1 41  ? 41.377 -17.818 10.358  1.00 17.13 ?  41   VAL   B HG12 1 
ATOM   4656 H  HG13 . VAL   B 1 41  ? 41.969 -19.227 10.792  1.00 17.13 ?  41   VAL   B HG13 1 
ATOM   4657 H  HG21 . VAL   B 1 41  ? 43.099 -18.369 13.398  1.00 17.64 ?  41   VAL   B HG21 1 
ATOM   4658 H  HG22 . VAL   B 1 41  ? 43.967 -19.255 12.407  1.00 17.64 ?  41   VAL   B HG22 1 
ATOM   4659 H  HG23 . VAL   B 1 41  ? 44.527 -17.861 12.925  1.00 17.64 ?  41   VAL   B HG23 1 
ATOM   4660 N  N    . TYR   B 1 42  ? 46.386 -17.134 10.956  1.00 12.55 ?  42   TYR   B N    1 
ATOM   4661 C  CA   . TYR   B 1 42  ? 47.543 -16.287 11.228  1.00 12.94 ?  42   TYR   B CA   1 
ATOM   4662 C  C    . TYR   B 1 42  ? 48.505 -16.208 10.046  1.00 12.12 ?  42   TYR   B C    1 
ATOM   4663 O  O    . TYR   B 1 42  ? 49.593 -15.635 10.180  1.00 13.23 ?  42   TYR   B O    1 
ATOM   4664 C  CB   . TYR   B 1 42  ? 48.243 -16.694 12.532  1.00 14.89 ?  42   TYR   B CB   1 
ATOM   4665 C  CG   . TYR   B 1 42  ? 47.643 -16.012 13.763  1.00 15.21 ?  42   TYR   B CG   1 
ATOM   4666 C  CD1  . TYR   B 1 42  ? 47.863 -14.656 14.005  1.00 14.23 ?  42   TYR   B CD1  1 
ATOM   4667 C  CD2  . TYR   B 1 42  ? 46.860 -16.710 14.667  1.00 17.13 ?  42   TYR   B CD2  1 
ATOM   4668 C  CE1  . TYR   B 1 42  ? 47.325 -14.020 15.106  1.00 15.49 ?  42   TYR   B CE1  1 
ATOM   4669 C  CE2  . TYR   B 1 42  ? 46.313 -16.081 15.778  1.00 17.49 ?  42   TYR   B CE2  1 
ATOM   4670 C  CZ   . TYR   B 1 42  ? 46.550 -14.733 15.991  1.00 17.84 ?  42   TYR   B CZ   1 
ATOM   4671 O  OH   . TYR   B 1 42  ? 46.016 -14.101 17.096  1.00 21.27 ?  42   TYR   B OH   1 
ATOM   4672 H  H    . TYR   B 1 42  ? 46.533 -17.978 11.057  1.00 15.08 ?  42   TYR   B H    1 
ATOM   4673 H  HA   . TYR   B 1 42  ? 47.213 -15.388 11.362  1.00 15.55 ?  42   TYR   B HA   1 
ATOM   4674 H  HB2  . TYR   B 1 42  ? 48.159 -17.649 12.649  1.00 17.89 ?  42   TYR   B HB2  1 
ATOM   4675 H  HB3  . TYR   B 1 42  ? 49.177 -16.443 12.473  1.00 17.89 ?  42   TYR   B HB3  1 
ATOM   4676 H  HD1  . TYR   B 1 42  ? 48.390 -14.169 13.402  1.00 17.10 ?  42   TYR   B HD1  1 
ATOM   4677 H  HD2  . TYR   B 1 42  ? 46.694 -17.615 14.523  1.00 20.58 ?  42   TYR   B HD2  1 
ATOM   4678 H  HE1  . TYR   B 1 42  ? 47.494 -13.117 15.248  1.00 18.62 ?  42   TYR   B HE1  1 
ATOM   4679 H  HE2  . TYR   B 1 42  ? 45.792 -16.563 16.376  1.00 21.01 ?  42   TYR   B HE2  1 
ATOM   4680 H  HH   . TYR   B 1 42  ? 46.248 -13.297 17.100  1.00 25.55 ?  42   TYR   B HH   1 
ATOM   4681 N  N    . LEU   B 1 43  ? 48.108 -16.725 8.883   1.00 11.25 ?  43   LEU   B N    1 
ATOM   4682 C  CA   . LEU   B 1 43  ? 48.923 -16.658 7.673   1.00 11.40 ?  43   LEU   B CA   1 
ATOM   4683 C  C    . LEU   B 1 43  ? 50.338 -17.165 7.930   1.00 11.43 ?  43   LEU   B C    1 
ATOM   4684 O  O    . LEU   B 1 43  ? 51.318 -16.567 7.488   1.00 12.08 ?  43   LEU   B O    1 
ATOM   4685 C  CB   . LEU   B 1 43  ? 48.939 -15.254 7.061   1.00 11.28 ?  43   LEU   B CB   1 
ATOM   4686 C  CG   . LEU   B 1 43  ? 47.580 -14.647 6.689   1.00 11.39 ?  43   LEU   B CG   1 
ATOM   4687 C  CD1  . LEU   B 1 43  ? 47.788 -13.253 6.116   1.00 13.26 ?  43   LEU   B CD1  1 
ATOM   4688 C  CD2  . LEU   B 1 43  ? 46.809 -15.532 5.717   1.00 11.47 ?  43   LEU   B CD2  1 
ATOM   4689 H  H    . LEU   B 1 43  ? 47.359 -17.133 8.769   1.00 13.52 ?  43   LEU   B H    1 
ATOM   4690 H  HA   . LEU   B 1 43  ? 48.527 -17.249 7.013   1.00 13.71 ?  43   LEU   B HA   1 
ATOM   4691 H  HB2  . LEU   B 1 43  ? 49.357 -14.652 7.694   1.00 13.56 ?  43   LEU   B HB2  1 
ATOM   4692 H  HB3  . LEU   B 1 43  ? 49.469 -15.287 6.249   1.00 13.56 ?  43   LEU   B HB3  1 
ATOM   4693 H  HG   . LEU   B 1 43  ? 47.047 -14.559 7.490   1.00 13.70 ?  43   LEU   B HG   1 
ATOM   4694 H  HD11 . LEU   B 1 43  ? 46.924 -12.871 5.881   1.00 15.93 ?  43   LEU   B HD11 1 
ATOM   4695 H  HD12 . LEU   B 1 43  ? 48.218 -12.695 6.786   1.00 15.93 ?  43   LEU   B HD12 1 
ATOM   4696 H  HD13 . LEU   B 1 43  ? 48.347 -13.307 5.326   1.00 15.93 ?  43   LEU   B HD13 1 
ATOM   4697 H  HD21 . LEU   B 1 43  ? 45.997 -15.072 5.442   1.00 13.79 ?  43   LEU   B HD21 1 
ATOM   4698 H  HD22 . LEU   B 1 43  ? 47.361 -15.716 4.941   1.00 13.79 ?  43   LEU   B HD22 1 
ATOM   4699 H  HD23 . LEU   B 1 43  ? 46.576 -16.365 6.160   1.00 13.79 ?  43   LEU   B HD23 1 
ATOM   4700 N  N    . LYS   B 1 44  ? 50.440 -18.290 8.639   1.00 11.47 ?  44   LYS   B N    1 
ATOM   4701 C  CA   . LYS   B 1 44  ? 51.709 -18.965 8.876   1.00 12.15 ?  44   LYS   B CA   1 
ATOM   4702 C  C    . LYS   B 1 44  ? 51.823 -20.079 7.846   1.00 11.63 ?  44   LYS   B C    1 
ATOM   4703 O  O    . LYS   B 1 44  ? 51.128 -21.097 7.938   1.00 12.86 ?  44   LYS   B O    1 
ATOM   4704 C  CB   . LYS   B 1 44  ? 51.770 -19.484 10.310  1.00 13.67 ?  44   LYS   B CB   1 
ATOM   4705 C  CG   . LYS   B 1 44  ? 51.952 -18.374 11.338  1.00 16.53 ?  44   LYS   B CG   1 
ATOM   4706 C  CD   . LYS   B 1 44  ? 53.162 -17.517 10.971  1.00 19.76 ?  44   LYS   B CD   1 
ATOM   4707 C  CE   . LYS   B 1 44  ? 53.614 -16.621 12.096  1.00 22.15 ?  44   LYS   B CE   1 
ATOM   4708 N  NZ   . LYS   B 1 44  ? 54.803 -15.813 11.722  1.00 22.92 ?  44   LYS   B NZ   1 
ATOM   4709 H  H    . LYS   B 1 44  ? 49.767 -18.677 9.010   1.00 13.78 ?  44   LYS   B H    1 
ATOM   4710 H  HA   . LYS   B 1 44  ? 52.437 -18.350 8.716   1.00 14.61 ?  44   LYS   B HA   1 
ATOM   4711 H  HB2  . LYS   B 1 44  ? 50.935 -19.944 10.515  1.00 16.42 ?  44   LYS   B HB2  1 
ATOM   4712 H  HB3  . LYS   B 1 44  ? 52.512 -20.099 10.394  1.00 16.42 ?  44   LYS   B HB3  1 
ATOM   4713 H  HG2  . LYS   B 1 44  ? 51.165 -17.812 11.356  1.00 19.87 ?  44   LYS   B HG2  1 
ATOM   4714 H  HG3  . LYS   B 1 44  ? 52.109 -18.769 12.214  1.00 19.87 ?  44   LYS   B HG3  1 
ATOM   4715 H  HD2  . LYS   B 1 44  ? 53.897 -18.105 10.719  1.00 23.73 ?  44   LYS   B HD2  1 
ATOM   4716 H  HD3  . LYS   B 1 44  ? 52.923 -16.949 10.221  1.00 23.73 ?  44   LYS   B HD3  1 
ATOM   4717 H  HE2  . LYS   B 1 44  ? 52.903 -16.000 12.287  1.00 26.60 ?  44   LYS   B HE2  1 
ATOM   4718 H  HE3  . LYS   B 1 44  ? 53.829 -17.158 12.877  1.00 26.60 ?  44   LYS   B HE3  1 
ATOM   4719 H  HZ1  . LYS   B 1 44  ? 55.044 -15.295 12.404  1.00 27.53 ?  44   LYS   B HZ1  1 
ATOM   4720 H  HZ2  . LYS   B 1 44  ? 55.481 -16.345 11.507  1.00 27.53 ?  44   LYS   B HZ2  1 
ATOM   4721 H  HZ3  . LYS   B 1 44  ? 54.609 -15.295 11.022  1.00 27.53 ?  44   LYS   B HZ3  1 
ATOM   4722 N  N    . HIS   B 1 45  ? 52.669 -19.860 6.843   1.00 11.19 ?  45   HIS   B N    1 
ATOM   4723 C  CA   . HIS   B 1 45  ? 52.685 -20.690 5.640   1.00 11.51 ?  45   HIS   B CA   1 
ATOM   4724 C  C    . HIS   B 1 45  ? 53.696 -21.824 5.795   1.00 13.77 ?  45   HIS   B C    1 
ATOM   4725 O  O    . HIS   B 1 45  ? 54.765 -21.839 5.191   1.00 16.24 ?  45   HIS   B O    1 
ATOM   4726 C  CB   . HIS   B 1 45  ? 53.007 -19.833 4.428   1.00 11.61 ?  45   HIS   B CB   1 
ATOM   4727 C  CG   . HIS   B 1 45  ? 52.141 -18.625 4.321   1.00 11.41 ?  45   HIS   B CG   1 
ATOM   4728 N  ND1  . HIS   B 1 45  ? 50.765 -18.699 4.285   1.00 11.61 ?  45   HIS   B ND1  1 
ATOM   4729 C  CD2  . HIS   B 1 45  ? 52.460 -17.312 4.255   1.00 12.17 ?  45   HIS   B CD2  1 
ATOM   4730 C  CE1  . HIS   B 1 45  ? 50.280 -17.474 4.186   1.00 11.24 ?  45   HIS   B CE1  1 
ATOM   4731 N  NE2  . HIS   B 1 45  ? 51.284 -16.614 4.165   1.00 11.65 ?  45   HIS   B NE2  1 
ATOM   4732 H  H    . HIS   B 1 45  ? 53.240 -19.218 6.828   1.00 13.46 ?  45   HIS   B H    1 
ATOM   4733 H  HA   . HIS   B 1 45  ? 51.806 -21.083 5.506   1.00 13.83 ?  45   HIS   B HA   1 
ATOM   4734 H  HB2  . HIS   B 1 45  ? 53.929 -19.542 4.480   1.00 13.95 ?  45   HIS   B HB2  1 
ATOM   4735 H  HB3  . HIS   B 1 45  ? 52.877 -20.367 3.621   1.00 13.95 ?  45   HIS   B HB3  1 
ATOM   4736 H  HD2  . HIS   B 1 45  ? 53.321 -16.949 4.261   1.00 14.62 ?  45   HIS   B HD2  1 
ATOM   4737 H  HE1  . HIS   B 1 45  ? 49.380 -17.250 4.138   1.00 13.51 ?  45   HIS   B HE1  1 
ATOM   4738 H  HE2  . HIS   B 1 45  ? 51.214 -15.757 4.115   1.00 14.01 ?  45   HIS   B HE2  1 
ATOM   4739 N  N    A GLY   B 1 46  ? 53.318 -22.804 6.611   0.30 14.79 ?  46   GLY   B N    1 
ATOM   4740 N  N    B GLY   B 1 46  ? 53.325 -22.799 6.619   0.70 14.50 ?  46   GLY   B N    1 
ATOM   4741 C  CA   A GLY   B 1 46  ? 54.238 -23.862 6.984   0.30 16.24 ?  46   GLY   B CA   1 
ATOM   4742 C  CA   B GLY   B 1 46  ? 54.244 -23.865 6.968   0.70 16.32 ?  46   GLY   B CA   1 
ATOM   4743 C  C    A GLY   B 1 46  ? 54.278 -25.068 6.066   0.30 17.79 ?  46   GLY   B C    1 
ATOM   4744 C  C    B GLY   B 1 46  ? 54.275 -25.047 6.018   0.70 18.39 ?  46   GLY   B C    1 
ATOM   4745 O  O    A GLY   B 1 46  ? 55.352 -25.456 5.593   0.30 19.36 ?  46   GLY   B O    1 
ATOM   4746 O  O    B GLY   B 1 46  ? 55.330 -25.400 5.478   0.70 21.19 ?  46   GLY   B O    1 
ATOM   4747 H  H    A GLY   B 1 46  ? 52.534 -22.869 6.968   0.30 17.77 ?  46   GLY   B H    1 
ATOM   4748 H  H    B GLY   B 1 46  ? 52.551 -22.847 7.002   0.70 17.42 ?  46   GLY   B H    1 
ATOM   4749 H  HA2  A GLY   B 1 46  ? 55.132 -23.491 7.022   0.30 19.52 ?  46   GLY   B HA2  1 
ATOM   4750 H  HA2  B GLY   B 1 46  ? 55.138 -23.498 7.021   0.70 19.61 ?  46   GLY   B HA2  1 
ATOM   4751 H  HA3  A GLY   B 1 46  ? 54.006 -24.169 7.874   0.30 19.52 ?  46   GLY   B HA3  1 
ATOM   4752 H  HA3  B GLY   B 1 46  ? 54.005 -24.201 7.847   0.70 19.61 ?  46   GLY   B HA3  1 
ATOM   4753 N  N    . GLY   B 1 47  ? 53.124 -25.685 5.812   1.00 17.89 ?  47   GLY   B N    1 
ATOM   4754 C  CA   . GLY   B 1 47  ? 53.061 -26.948 5.108   1.00 15.49 ?  47   GLY   B CA   1 
ATOM   4755 C  C    . GLY   B 1 47  ? 52.170 -26.910 3.882   1.00 13.34 ?  47   GLY   B C    1 
ATOM   4756 O  O    . GLY   B 1 47  ? 51.540 -25.898 3.571   1.00 13.65 ?  47   GLY   B O    1 
ATOM   4757 H  H    A GLY   B 1 47  ? 52.351 -25.382 6.049   0.30 21.49 ?  47   GLY   B H    1 
ATOM   4758 H  H    B GLY   B 1 47  ? 52.356 -25.409 6.095   0.70 21.49 ?  47   GLY   B H    1 
ATOM   4759 H  HA2  . GLY   B 1 47  ? 53.951 -27.210 4.823   1.00 18.61 ?  47   GLY   B HA2  1 
ATOM   4760 H  HA3  . GLY   B 1 47  ? 52.724 -27.633 5.708   1.00 18.61 ?  47   GLY   B HA3  1 
ATOM   4761 N  N    . GLY   B 1 48  ? 52.114 -28.054 3.199   1.00 12.35 ?  48   GLY   B N    1 
ATOM   4762 C  CA   . GLY   B 1 48  ? 51.202 -28.190 2.082   1.00 12.34 ?  48   GLY   B CA   1 
ATOM   4763 C  C    . GLY   B 1 48  ? 51.339 -27.070 1.075   1.00 11.67 ?  48   GLY   B C    1 
ATOM   4764 O  O    . GLY   B 1 48  ? 52.442 -26.610 0.756   1.00 12.08 ?  48   GLY   B O    1 
ATOM   4765 H  H    . GLY   B 1 48  ? 52.596 -28.744 3.354   1.00 14.84 ?  48   GLY   B H    1 
ATOM   4766 H  HA2  . GLY   B 1 48  ? 51.367 -29.034 1.629   1.00 14.84 ?  48   GLY   B HA2  1 
ATOM   4767 H  HA3  . GLY   B 1 48  ? 50.287 -28.196 2.408   1.00 14.84 ?  48   GLY   B HA3  1 
ATOM   4768 N  N    . VAL   B 1 49  ? 50.192 -26.630 0.552   1.00 11.56 ?  49   VAL   B N    1 
ATOM   4769 C  CA   . VAL   B 1 49  ? 50.176 -25.596 -0.481  1.00 11.66 ?  49   VAL   B CA   1 
ATOM   4770 C  C    . VAL   B 1 49  ? 50.842 -24.313 0.014   1.00 10.81 ?  49   VAL   B C    1 
ATOM   4771 O  O    . VAL   B 1 49  ? 51.635 -23.692 -0.705  1.00 11.70 ?  49   VAL   B O    1 
ATOM   4772 C  CB   . VAL   B 1 49  ? 48.735 -25.345 -0.968  1.00 12.72 ?  49   VAL   B CB   1 
ATOM   4773 C  CG1  . VAL   B 1 49  ? 48.660 -24.086 -1.826  1.00 13.00 ?  49   VAL   B CG1  1 
ATOM   4774 C  CG2  . VAL   B 1 49  ? 48.209 -26.555 -1.733  1.00 13.69 ?  49   VAL   B CG2  1 
ATOM   4775 H  H    . VAL   B 1 49  ? 49.408 -26.903 0.781   1.00 13.90 ?  49   VAL   B H    1 
ATOM   4776 H  HA   . VAL   B 1 49  ? 50.684 -25.910 -1.243  1.00 14.02 ?  49   VAL   B HA   1 
ATOM   4777 H  HB   . VAL   B 1 49  ? 48.160 -25.212 -0.200  1.00 15.29 ?  49   VAL   B HB   1 
ATOM   4778 H  HG11 . VAL   B 1 49  ? 47.831 -24.096 -2.334  1.00 15.62 ?  49   VAL   B HG11 1 
ATOM   4779 H  HG12 . VAL   B 1 49  ? 48.680 -23.304 -1.251  1.00 15.62 ?  49   VAL   B HG12 1 
ATOM   4780 H  HG13 . VAL   B 1 49  ? 49.415 -24.069 -2.435  1.00 15.62 ?  49   VAL   B HG13 1 
ATOM   4781 H  HG21 . VAL   B 1 49  ? 47.304 -26.378 -2.031  1.00 16.46 ?  49   VAL   B HG21 1 
ATOM   4782 H  HG22 . VAL   B 1 49  ? 48.783 -26.717 -2.503  1.00 16.46 ?  49   VAL   B HG22 1 
ATOM   4783 H  HG23 . VAL   B 1 49  ? 48.221 -27.328 -1.148  1.00 16.46 ?  49   VAL   B HG23 1 
ATOM   4784 N  N    . ALA   B 1 50  ? 50.507 -23.877 1.230   1.00 10.78 ?  50   ALA   B N    1 
ATOM   4785 C  CA   . ALA   B 1 50  ? 51.025 -22.598 1.713   1.00 10.60 ?  50   ALA   B CA   1 
ATOM   4786 C  C    . ALA   B 1 50  ? 52.545 -22.626 1.815   1.00 10.67 ?  50   ALA   B C    1 
ATOM   4787 O  O    . ALA   B 1 50  ? 53.227 -21.656 1.448   1.00 10.82 ?  50   ALA   B O    1 
ATOM   4788 C  CB   . ALA   B 1 50  ? 50.400 -22.245 3.062   1.00 10.86 ?  50   ALA   B CB   1 
ATOM   4789 H  H    . ALA   B 1 50  ? 49.996 -24.292 1.784   1.00 12.96 ?  50   ALA   B H    1 
ATOM   4790 H  HA   . ALA   B 1 50  ? 50.794 -21.904 1.086   1.00 12.74 ?  50   ALA   B HA   1 
ATOM   4791 H  HB1  . ALA   B 1 50  ? 50.758 -21.393 3.366   1.00 13.06 ?  50   ALA   B HB1  1 
ATOM   4792 H  HB2  . ALA   B 1 50  ? 49.438 -22.175 2.955   1.00 13.06 ?  50   ALA   B HB2  1 
ATOM   4793 H  HB3  . ALA   B 1 50  ? 50.612 -22.937 3.707   1.00 13.06 ?  50   ALA   B HB3  1 
ATOM   4794 N  N    . GLY   B 1 51  ? 53.097 -23.727 2.316   1.00 11.38 ?  51   GLY   B N    1 
ATOM   4795 C  CA   . GLY   B 1 51  ? 54.541 -23.835 2.389   1.00 12.43 ?  51   GLY   B CA   1 
ATOM   4796 C  C    . GLY   B 1 51  ? 55.192 -23.781 1.022   1.00 12.10 ?  51   GLY   B C    1 
ATOM   4797 O  O    . GLY   B 1 51  ? 56.233 -23.146 0.844   1.00 12.70 ?  51   GLY   B O    1 
ATOM   4798 H  H    . GLY   B 1 51  ? 52.667 -24.417 2.610   1.00 13.68 ?  51   GLY   B H    1 
ATOM   4799 H  HA2  . GLY   B 1 51  ? 54.891 -23.107 2.927   1.00 14.94 ?  51   GLY   B HA2  1 
ATOM   4800 H  HA3  . GLY   B 1 51  ? 54.784 -24.674 2.816   1.00 14.94 ?  51   GLY   B HA3  1 
ATOM   4801 N  N    . ALA   B 1 52  ? 54.581 -24.437 0.035   1.00 11.60 ?  52   ALA   B N    1 
ATOM   4802 C  CA   . ALA   B 1 52  ? 55.147 -24.443 -1.308  1.00 11.78 ?  52   ALA   B CA   1 
ATOM   4803 C  C    . ALA   B 1 52  ? 55.064 -23.065 -1.956  1.00 11.52 ?  52   ALA   B C    1 
ATOM   4804 O  O    . ALA   B 1 52  ? 56.031 -22.610 -2.584  1.00 11.84 ?  52   ALA   B O    1 
ATOM   4805 C  CB   . ALA   B 1 52  ? 54.440 -25.482 -2.168  1.00 12.70 ?  52   ALA   B CB   1 
ATOM   4806 H  H    . ALA   B 1 52  ? 53.843 -24.870 0.116   1.00 13.94 ?  52   ALA   B H    1 
ATOM   4807 H  HA   . ALA   B 1 52  ? 56.084 -24.688 -1.247  1.00 14.16 ?  52   ALA   B HA   1 
ATOM   4808 H  HB1  . ALA   B 1 52  ? 54.834 -25.472 -3.055  1.00 15.26 ?  52   ALA   B HB1  1 
ATOM   4809 H  HB2  . ALA   B 1 52  ? 54.558 -26.355 -1.763  1.00 15.26 ?  52   ALA   B HB2  1 
ATOM   4810 H  HB3  . ALA   B 1 52  ? 53.500 -25.261 -2.218  1.00 15.26 ?  52   ALA   B HB3  1 
ATOM   4811 N  N    . LEU   B 1 53  ? 53.919 -22.386 -1.832  1.00 11.03 ?  53   LEU   B N    1 
ATOM   4812 C  CA   . LEU   B 1 53  ? 53.810 -21.045 -2.397  1.00 11.27 ?  53   LEU   B CA   1 
ATOM   4813 C  C    . LEU   B 1 53  ? 54.822 -20.109 -1.749  1.00 11.15 ?  53   LEU   B C    1 
ATOM   4814 O  O    . LEU   B 1 53  ? 55.517 -19.350 -2.436  1.00 11.88 ?  53   LEU   B O    1 
ATOM   4815 C  CB   . LEU   B 1 53  ? 52.387 -20.507 -2.215  1.00 11.48 ?  53   LEU   B CB   1 
ATOM   4816 C  CG   . LEU   B 1 53  ? 51.257 -21.214 -2.970  1.00 11.87 ?  53   LEU   B CG   1 
ATOM   4817 C  CD1  . LEU   B 1 53  ? 49.907 -20.606 -2.605  1.00 13.37 ?  53   LEU   B CD1  1 
ATOM   4818 C  CD2  . LEU   B 1 53  ? 51.463 -21.158 -4.476  1.00 13.35 ?  53   LEU   B CD2  1 
ATOM   4819 H  H    . LEU   B 1 53  ? 53.218 -22.670 -1.427  1.00 13.26 ?  53   LEU   B H    1 
ATOM   4820 H  HA   . LEU   B 1 53  ? 54.004 -21.089 -3.349  1.00 13.55 ?  53   LEU   B HA   1 
ATOM   4821 H  HB2  . LEU   B 1 53  ? 52.171 -20.563 -1.272  1.00 13.80 ?  53   LEU   B HB2  1 
ATOM   4822 H  HB3  . LEU   B 1 53  ? 52.380 -19.586 -2.494  1.00 13.80 ?  53   LEU   B HB3  1 
ATOM   4823 H  HG   . LEU   B 1 53  ? 51.231 -22.148 -2.709  1.00 14.27 ?  53   LEU   B HG   1 
ATOM   4824 H  HD11 . LEU   B 1 53  ? 49.204 -21.071 -3.095  1.00 16.07 ?  53   LEU   B HD11 1 
ATOM   4825 H  HD12 . LEU   B 1 53  ? 49.758 -20.709 -1.650  1.00 16.07 ?  53   LEU   B HD12 1 
ATOM   4826 H  HD13 . LEU   B 1 53  ? 49.904 -19.667 -2.840  1.00 16.07 ?  53   LEU   B HD13 1 
ATOM   4827 H  HD21 . LEU   B 1 53  ? 50.734 -21.617 -4.918  1.00 16.05 ?  53   LEU   B HD21 1 
ATOM   4828 H  HD22 . LEU   B 1 53  ? 51.485 -20.228 -4.757  1.00 16.05 ?  53   LEU   B HD22 1 
ATOM   4829 H  HD23 . LEU   B 1 53  ? 52.305 -21.588 -4.696  1.00 16.05 ?  53   LEU   B HD23 1 
ATOM   4830 N  N    . ASN   B 1 54  ? 54.910 -20.136 -0.420  1.00 10.78 ?  54   ASN   B N    1 
ATOM   4831 C  CA   . ASN   B 1 54  ? 55.830 -19.229 0.253   1.00 11.35 ?  54   ASN   B CA   1 
ATOM   4832 C  C    . ASN   B 1 54  ? 57.272 -19.506 -0.150  1.00 11.76 ?  54   ASN   B C    1 
ATOM   4833 O  O    . ASN   B 1 54  ? 58.048 -18.570 -0.386  1.00 12.14 ?  54   ASN   B O    1 
ATOM   4834 C  CB   . ASN   B 1 54  ? 55.671 -19.309 1.764   1.00 11.78 ?  54   ASN   B CB   1 
ATOM   4835 C  CG   . ASN   B 1 54  ? 56.640 -18.388 2.479   1.00 12.13 ?  54   ASN   B CG   1 
ATOM   4836 O  OD1  . ASN   B 1 54  ? 56.654 -17.183 2.228   1.00 12.41 ?  54   ASN   B OD1  1 
ATOM   4837 N  ND2  . ASN   B 1 54  ? 57.476 -18.948 3.345   1.00 13.79 ?  54   ASN   B ND2  1 
ATOM   4838 H  H    . ASN   B 1 54  ? 54.462 -20.657 0.096   1.00 12.96 ?  54   ASN   B H    1 
ATOM   4839 H  HA   . ASN   B 1 54  ? 55.616 -18.320 -0.020  1.00 13.64 ?  54   ASN   B HA   1 
ATOM   4840 H  HB2  . ASN   B 1 54  ? 54.767 -19.040 2.005   1.00 14.16 ?  54   ASN   B HB2  1 
ATOM   4841 H  HB3  . ASN   B 1 54  ? 55.840 -20.214 2.057   1.00 14.16 ?  54   ASN   B HB3  1 
ATOM   4842 H  HD21 . ASN   B 1 54  ? 58.045 -18.461 3.768   1.00 16.57 ?  54   ASN   B HD21 1 
ATOM   4843 H  HD22 . ASN   B 1 54  ? 57.444 -19.795 3.488   1.00 16.57 ?  54   ASN   B HD22 1 
ATOM   4844 N  N    . LYS   B 1 55  ? 57.656 -20.783 -0.218  1.00 12.62 ?  55   LYS   B N    1 
ATOM   4845 C  CA   . LYS   B 1 55  ? 59.010 -21.127 -0.640  1.00 13.55 ?  55   LYS   B CA   1 
ATOM   4846 C  C    . LYS   B 1 55  ? 59.307 -20.579 -2.031  1.00 13.43 ?  55   LYS   B C    1 
ATOM   4847 O  O    . LYS   B 1 55  ? 60.408 -20.073 -2.285  1.00 13.88 ?  55   LYS   B O    1 
ATOM   4848 C  CB   . LYS   B 1 55  ? 59.185 -22.646 -0.598  1.00 14.97 ?  55   LYS   B CB   1 
ATOM   4849 C  CG   . LYS   B 1 55  ? 60.557 -23.127 -1.024  1.00 18.82 ?  55   LYS   B CG   1 
ATOM   4850 C  CD   . LYS   B 1 55  ? 60.718 -24.627 -0.824  1.00 22.10 ?  55   LYS   B CD   1 
ATOM   4851 C  CE   . LYS   B 1 55  ? 60.725 -25.009 0.655   1.00 24.98 ?  55   LYS   B CE   1 
ATOM   4852 N  NZ   . LYS   B 1 55  ? 61.126 -26.420 0.876   1.00 26.37 ?  55   LYS   B NZ   1 
ATOM   4853 H  H    . LYS   B 1 55  ? 57.155 -21.452 -0.030  1.00 15.17 ?  55   LYS   B H    1 
ATOM   4854 H  HA   . LYS   B 1 55  ? 59.643 -20.733 -0.025  1.00 16.29 ?  55   LYS   B HA   1 
ATOM   4855 H  HB2  . LYS   B 1 55  ? 59.032 -22.944 0.312   1.00 17.99 ?  55   LYS   B HB2  1 
ATOM   4856 H  HB3  . LYS   B 1 55  ? 58.533 -23.053 -1.190  1.00 17.99 ?  55   LYS   B HB3  1 
ATOM   4857 H  HG2  . LYS   B 1 55  ? 60.686 -22.932 -1.967  1.00 22.61 ?  55   LYS   B HG2  1 
ATOM   4858 H  HG3  . LYS   B 1 55  ? 61.232 -22.674 -0.495  1.00 22.61 ?  55   LYS   B HG3  1 
ATOM   4859 H  HD2  . LYS   B 1 55  ? 59.979 -25.088 -1.251  1.00 26.55 ?  55   LYS   B HD2  1 
ATOM   4860 H  HD3  . LYS   B 1 55  ? 61.560 -24.914 -1.212  1.00 26.55 ?  55   LYS   B HD3  1 
ATOM   4861 H  HE2  . LYS   B 1 55  ? 61.352 -24.431 1.124   1.00 30.00 ?  55   LYS   B HE2  1 
ATOM   4862 H  HE3  . LYS   B 1 55  ? 59.831 -24.885 1.016   1.00 30.00 ?  55   LYS   B HE3  1 
ATOM   4863 H  HZ1  . LYS   B 1 55  ? 61.104 -26.608 1.745   1.00 31.67 ?  55   LYS   B HZ1  1 
ATOM   4864 H  HZ2  . LYS   B 1 55  ? 60.567 -26.963 0.447   1.00 31.67 ?  55   LYS   B HZ2  1 
ATOM   4865 H  HZ3  . LYS   B 1 55  ? 61.950 -26.551 0.571   1.00 31.67 ?  55   LYS   B HZ3  1 
ATOM   4866 N  N    . ALA   B 1 56  ? 58.330 -20.647 -2.942  1.00 12.99 ?  56   ALA   B N    1 
ATOM   4867 C  CA   . ALA   B 1 56  ? 58.550 -20.146 -4.294  1.00 13.67 ?  56   ALA   B CA   1 
ATOM   4868 C  C    . ALA   B 1 56  ? 58.830 -18.648 -4.293  1.00 13.45 ?  56   ALA   B C    1 
ATOM   4869 O  O    . ALA   B 1 56  ? 59.564 -18.150 -5.158  1.00 14.17 ?  56   ALA   B O    1 
ATOM   4870 C  CB   . ALA   B 1 56  ? 57.343 -20.472 -5.175  1.00 14.57 ?  56   ALA   B CB   1 
ATOM   4871 H  H    . ALA   B 1 56  ? 57.543 -20.967 -2.802  1.00 15.61 ?  56   ALA   B H    1 
ATOM   4872 H  HA   . ALA   B 1 56  ? 59.323 -20.587 -4.672  1.00 16.43 ?  56   ALA   B HA   1 
ATOM   4873 H  HB1  . ALA   B 1 56  ? 57.506 -20.139 -6.073  1.00 17.51 ?  56   ALA   B HB1  1 
ATOM   4874 H  HB2  . ALA   B 1 56  ? 57.222 -21.435 -5.199  1.00 17.51 ?  56   ALA   B HB2  1 
ATOM   4875 H  HB3  . ALA   B 1 56  ? 56.553 -20.050 -4.804  1.00 17.51 ?  56   ALA   B HB3  1 
ATOM   4876 N  N    . THR   B 1 57  ? 58.253 -17.914 -3.336  1.00 13.05 ?  57   THR   B N    1 
ATOM   4877 C  CA   . THR   B 1 57  ? 58.499 -16.480 -3.198  1.00 13.04 ?  57   THR   B CA   1 
ATOM   4878 C  C    . THR   B 1 57  ? 59.754 -16.164 -2.389  1.00 14.08 ?  57   THR   B C    1 
ATOM   4879 O  O    . THR   B 1 57  ? 59.993 -14.993 -2.079  1.00 14.26 ?  57   THR   B O    1 
ATOM   4880 C  CB   . THR   B 1 57  ? 57.300 -15.759 -2.558  1.00 12.44 ?  57   THR   B CB   1 
ATOM   4881 O  OG1  . THR   B 1 57  ? 57.275 -15.977 -1.140  1.00 12.51 ?  57   THR   B OG1  1 
ATOM   4882 C  CG2  . THR   B 1 57  ? 55.984 -16.196 -3.189  1.00 12.80 ?  57   THR   B CG2  1 
ATOM   4883 H  H    . THR   B 1 57  ? 57.700 -18.229 -2.752  1.00 15.69 ?  57   THR   B H    1 
ATOM   4884 H  HA   . THR   B 1 57  ? 58.616 -16.106 -4.087  1.00 15.67 ?  57   THR   B HA   1 
ATOM   4885 H  HB   . THR   B 1 57  ? 57.390 -14.808 -2.723  1.00 14.95 ?  57   THR   B HB   1 
ATOM   4886 H  HG1  . THR   B 1 57  ? 57.214 -16.801 -0.977  1.00 15.03 ?  57   THR   B HG1  1 
ATOM   4887 H  HG21 . THR   B 1 57  ? 55.267 -15.612 -2.908  1.00 15.38 ?  57   THR   B HG21 1 
ATOM   4888 H  HG22 . THR   B 1 57  ? 56.054 -16.171 -4.157  1.00 15.38 ?  57   THR   B HG22 1 
ATOM   4889 H  HG23 . THR   B 1 57  ? 55.773 -17.105 -2.918  1.00 15.38 ?  57   THR   B HG23 1 
ATOM   4890 N  N    . ASN   B 1 58  ? 60.553 -17.166 -2.034  1.00 14.77 ?  58   ASN   B N    1 
ATOM   4891 C  CA   . ASN   B 1 58  ? 61.752 -16.950 -1.226  1.00 17.07 ?  58   ASN   B CA   1 
ATOM   4892 C  C    . ASN   B 1 58  ? 61.416 -16.245 0.089   1.00 14.82 ?  58   ASN   B C    1 
ATOM   4893 O  O    . ASN   B 1 58  ? 62.156 -15.379 0.561   1.00 15.26 ?  58   ASN   B O    1 
ATOM   4894 C  CB   . ASN   B 1 58  ? 62.834 -16.194 -2.003  1.00 24.81 ?  58   ASN   B CB   1 
ATOM   4895 C  CG   . ASN   B 1 58  ? 64.203 -16.320 -1.363  1.00 34.61 ?  58   ASN   B CG   1 
ATOM   4896 O  OD1  . ASN   B 1 58  ? 64.533 -17.350 -0.773  1.00 38.14 ?  58   ASN   B OD1  1 
ATOM   4897 N  ND2  . ASN   B 1 58  ? 65.007 -15.268 -1.470  1.00 37.53 ?  58   ASN   B ND2  1 
ATOM   4898 H  H    . ASN   B 1 58  ? 60.419 -17.989 -2.247  1.00 17.75 ?  58   ASN   B H    1 
ATOM   4899 H  HA   . ASN   B 1 58  ? 62.120 -17.819 -1.006  1.00 20.51 ?  58   ASN   B HA   1 
ATOM   4900 H  HB2  . ASN   B 1 58  ? 62.889 -16.552 -2.906  1.00 29.79 ?  58   ASN   B HB2  1 
ATOM   4901 H  HB3  . ASN   B 1 58  ? 62.605 -15.252 -2.036  1.00 29.79 ?  58   ASN   B HB3  1 
ATOM   4902 H  HD21 . ASN   B 1 58  ? 65.794 -15.291 -1.123  1.00 45.06 ?  58   ASN   B HD21 1 
ATOM   4903 H  HD22 . ASN   B 1 58  ? 64.741 -14.565 -1.887  1.00 45.06 ?  58   ASN   B HD22 1 
ATOM   4904 N  N    . ASN   B 1 59  ? 60.286 -16.622 0.685   1.00 13.70 ?  59   ASN   B N    1 
ATOM   4905 C  CA   . ASN   B 1 59  ? 59.819 -16.167 1.992   1.00 13.79 ?  59   ASN   B CA   1 
ATOM   4906 C  C    . ASN   B 1 59  ? 59.224 -14.758 1.942   1.00 13.33 ?  59   ASN   B C    1 
ATOM   4907 O  O    . ASN   B 1 59  ? 58.785 -14.256 2.985   1.00 13.18 ?  59   ASN   B O    1 
ATOM   4908 C  CB   . ASN   B 1 59  ? 60.892 -16.253 3.094   1.00 14.80 ?  59   ASN   B CB   1 
ATOM   4909 C  CG   . ASN   B 1 59  ? 60.299 -16.404 4.475   1.00 15.87 ?  59   ASN   B CG   1 
ATOM   4910 O  OD1  . ASN   B 1 59  ? 59.469 -17.279 4.710   1.00 16.31 ?  59   ASN   B OD1  1 
ATOM   4911 N  ND2  . ASN   B 1 59  ? 60.724 -15.554 5.401   1.00 16.62 ?  59   ASN   B ND2  1 
ATOM   4912 H  H    . ASN   B 1 59  ? 59.743 -17.188 0.330   1.00 16.46 ?  59   ASN   B H    1 
ATOM   4913 H  HA   . ASN   B 1 59  ? 59.104 -16.765 2.266   1.00 16.58 ?  59   ASN   B HA   1 
ATOM   4914 H  HB2  . ASN   B 1 59  ? 61.456 -17.028 2.938   1.00 17.79 ?  59   ASN   B HB2  1 
ATOM   4915 H  HB3  . ASN   B 1 59  ? 61.422 -15.447 3.093   1.00 17.79 ?  59   ASN   B HB3  1 
ATOM   4916 H  HD21 . ASN   B 1 59  ? 60.407 -15.590 6.204   1.00 19.97 ?  59   ASN   B HD21 1 
ATOM   4917 H  HD22 . ASN   B 1 59  ? 61.298 -14.949 5.196   1.00 19.97 ?  59   ASN   B HD22 1 
ATOM   4918 N  N    . ALA   B 1 60  ? 59.164 -14.112 0.774   1.00 12.94 ?  60   ALA   B N    1 
ATOM   4919 C  CA   . ALA   B 1 60  ? 58.568 -12.780 0.704   1.00 13.22 ?  60   ALA   B CA   1 
ATOM   4920 C  C    . ALA   B 1 60  ? 57.100 -12.803 1.108   1.00 12.20 ?  60   ALA   B C    1 
ATOM   4921 O  O    . ALA   B 1 60  ? 56.597 -11.850 1.716   1.00 12.89 ?  60   ALA   B O    1 
ATOM   4922 C  CB   . ALA   B 1 60  ? 58.720 -12.210 -0.704  1.00 14.37 ?  60   ALA   B CB   1 
ATOM   4923 H  H    . ALA   B 1 60  ? 59.460 -14.423 0.029   1.00 15.55 ?  60   ALA   B H    1 
ATOM   4924 H  HA   . ALA   B 1 60  ? 59.040 -12.197 1.318   1.00 15.89 ?  60   ALA   B HA   1 
ATOM   4925 H  HB1  . ALA   B 1 60  ? 58.320 -11.330 -0.729  1.00 17.27 ?  60   ALA   B HB1  1 
ATOM   4926 H  HB2  . ALA   B 1 60  ? 59.664 -12.155 -0.922  1.00 17.27 ?  60   ALA   B HB2  1 
ATOM   4927 H  HB3  . ALA   B 1 60  ? 58.271 -12.799 -1.331  1.00 17.27 ?  60   ALA   B HB3  1 
ATOM   4928 N  N    . MET   B 1 61  ? 56.387 -13.875 0.755   1.00 11.75 ?  61   MET   B N    1 
ATOM   4929 C  CA   . MET   B 1 61  ? 54.990 -14.002 1.152   1.00 11.46 ?  61   MET   B CA   1 
ATOM   4930 C  C    . MET   B 1 61  ? 54.852 -14.016 2.673   1.00 11.28 ?  61   MET   B C    1 
ATOM   4931 O  O    . MET   B 1 61  ? 53.961 -13.363 3.228   1.00 11.41 ?  61   MET   B O    1 
ATOM   4932 C  CB   . MET   B 1 61  ? 54.398 -15.267 0.521   1.00 11.34 ?  61   MET   B CB   1 
ATOM   4933 C  CG   . MET   B 1 61  ? 52.965 -15.569 0.951   1.00 11.13 ?  61   MET   B CG   1 
ATOM   4934 S  SD   . MET   B 1 61  ? 52.319 -17.059 0.172   1.00 11.99 ?  61   MET   B SD   1 
ATOM   4935 C  CE   . MET   B 1 61  ? 52.087 -16.469 -1.498  1.00 13.32 ?  61   MET   B CE   1 
ATOM   4936 H  H    . MET   B 1 61  ? 56.687 -14.536 0.283   1.00 14.13 ?  61   MET   B H    1 
ATOM   4937 H  HA   . MET   B 1 61  ? 54.498 -13.244 0.796   1.00 13.78 ?  61   MET   B HA   1 
ATOM   4938 H  HB2  . MET   B 1 61  ? 54.399 -15.167 -0.446  1.00 13.64 ?  61   MET   B HB2  1 
ATOM   4939 H  HB3  . MET   B 1 61  ? 54.949 -16.027 0.767   1.00 13.64 ?  61   MET   B HB3  1 
ATOM   4940 H  HG2  . MET   B 1 61  ? 52.944 -15.705 1.913   1.00 13.38 ?  61   MET   B HG2  1 
ATOM   4941 H  HG3  . MET   B 1 61  ? 52.396 -14.828 0.705   1.00 13.38 ?  61   MET   B HG3  1 
ATOM   4942 H  HE1  . MET   B 1 61  ? 51.681 -17.169 -2.027  1.00 16.00 ?  61   MET   B HE1  1 
ATOM   4943 H  HE2  . MET   B 1 61  ? 51.517 -15.687 -1.478  1.00 16.00 ?  61   MET   B HE2  1 
ATOM   4944 H  HE3  . MET   B 1 61  ? 52.956 -16.234 -1.870  1.00 16.00 ?  61   MET   B HE3  1 
ATOM   4945 N  N    . GLN   B 1 62  ? 55.732 -14.739 3.371   1.00 11.36 ?  62   GLN   B N    1 
ATOM   4946 C  CA   . GLN   B 1 62  ? 55.633 -14.798 4.827   1.00 11.60 ?  62   GLN   B CA   1 
ATOM   4947 C  C    . GLN   B 1 62  ? 55.919 -13.443 5.462   1.00 11.82 ?  62   GLN   B C    1 
ATOM   4948 O  O    . GLN   B 1 62  ? 55.238 -13.040 6.412   1.00 12.29 ?  62   GLN   B O    1 
ATOM   4949 C  CB   . GLN   B 1 62  ? 56.579 -15.857 5.391   1.00 11.88 ?  62   GLN   B CB   1 
ATOM   4950 C  CG   . GLN   B 1 62  ? 56.350 -16.131 6.869   1.00 12.28 ?  62   GLN   B CG   1 
ATOM   4951 C  CD   . GLN   B 1 62  ? 54.974 -16.711 7.114   1.00 11.86 ?  62   GLN   B CD   1 
ATOM   4952 O  OE1  . GLN   B 1 62  ? 54.712 -17.855 6.751   1.00 12.38 ?  62   GLN   B OE1  1 
ATOM   4953 N  NE2  . GLN   B 1 62  ? 54.063 -15.912 7.669   1.00 12.37 ?  62   GLN   B NE2  1 
ATOM   4954 H  H    . GLN   B 1 62  ? 56.366 -15.206 3.023   1.00 13.66 ?  62   GLN   B H    1 
ATOM   4955 H  HA   . GLN   B 1 62  ? 54.727 -15.053 5.061   1.00 13.94 ?  62   GLN   B HA   1 
ATOM   4956 H  HB2  . GLN   B 1 62  ? 56.454 -16.688 4.903   1.00 14.28 ?  62   GLN   B HB2  1 
ATOM   4957 H  HB3  . GLN   B 1 62  ? 57.494 -15.548 5.280   1.00 14.28 ?  62   GLN   B HB3  1 
ATOM   4958 H  HG2  . GLN   B 1 62  ? 57.007 -16.778 7.173   1.00 14.76 ?  62   GLN   B HG2  1 
ATOM   4959 H  HG3  . GLN   B 1 62  ? 56.427 -15.309 7.365   1.00 14.76 ?  62   GLN   B HG3  1 
ATOM   4960 H  HE21 . GLN   B 1 62  ? 54.274 -15.112 7.893   1.00 14.87 ?  62   GLN   B HE21 1 
ATOM   4961 H  HE22 . GLN   B 1 62  ? 53.265 -16.204 7.816   1.00 14.87 ?  62   GLN   B HE22 1 
ATOM   4962 N  N    . VAL   B 1 63  ? 56.930 -12.724 4.967   1.00 12.61 ?  63   VAL   B N    1 
ATOM   4963 C  CA   . VAL   B 1 63  ? 57.235 -11.409 5.526   1.00 13.37 ?  63   VAL   B CA   1 
ATOM   4964 C  C    . VAL   B 1 63  ? 56.044 -10.474 5.347   1.00 12.52 ?  63   VAL   B C    1 
ATOM   4965 O  O    . VAL   B 1 63  ? 55.633 -9.763  6.274   1.00 13.05 ?  63   VAL   B O    1 
ATOM   4966 C  CB   . VAL   B 1 63  ? 58.519 -10.842 4.895   1.00 14.46 ?  63   VAL   B CB   1 
ATOM   4967 C  CG1  . VAL   B 1 63  ? 58.736 -9.400  5.337   1.00 15.45 ?  63   VAL   B CG1  1 
ATOM   4968 C  CG2  . VAL   B 1 63  ? 59.714 -11.708 5.269   1.00 15.28 ?  63   VAL   B CG2  1 
ATOM   4969 H  H    . VAL   B 1 63  ? 57.446 -12.978 4.317   1.00 15.16 ?  63   VAL   B H    1 
ATOM   4970 H  HA   . VAL   B 1 63  ? 57.395 -11.512 6.473   1.00 16.06 ?  63   VAL   B HA   1 
ATOM   4971 H  HB   . VAL   B 1 63  ? 58.438 -10.855 3.930   1.00 17.38 ?  63   VAL   B HB   1 
ATOM   4972 H  HG11 . VAL   B 1 63  ? 59.651 -9.147  5.151   1.00 18.56 ?  63   VAL   B HG11 1 
ATOM   4973 H  HG12 . VAL   B 1 63  ? 58.126 -8.827  4.848   1.00 18.56 ?  63   VAL   B HG12 1 
ATOM   4974 H  HG13 . VAL   B 1 63  ? 58.561 -9.335  6.290   1.00 18.56 ?  63   VAL   B HG13 1 
ATOM   4975 H  HG21 . VAL   B 1 63  ? 60.519 -11.325 4.882   1.00 18.37 ?  63   VAL   B HG21 1 
ATOM   4976 H  HG22 . VAL   B 1 63  ? 59.798 -11.734 6.237   1.00 18.37 ?  63   VAL   B HG22 1 
ATOM   4977 H  HG23 . VAL   B 1 63  ? 59.580 -12.606 4.927   1.00 18.37 ?  63   VAL   B HG23 1 
ATOM   4978 N  N    . GLU   B 1 64  ? 55.473 -10.462 4.143   1.00 12.17 ?  64   GLU   B N    1 
ATOM   4979 C  CA   . GLU   B 1 64  ? 54.302 -9.630  3.874   1.00 11.86 ?  64   GLU   B CA   1 
ATOM   4980 C  C    . GLU   B 1 64  ? 53.121 -10.032 4.753   1.00 11.71 ?  64   GLU   B C    1 
ATOM   4981 O  O    . GLU   B 1 64  ? 52.376 -9.173  5.251   1.00 12.26 ?  64   GLU   B O    1 
ATOM   4982 C  CB   . GLU   B 1 64  ? 53.932 -9.770  2.398   1.00 12.11 ?  64   GLU   B CB   1 
ATOM   4983 C  CG   . GLU   B 1 64  ? 52.647 -9.064  1.987   1.00 12.14 ?  64   GLU   B CG   1 
ATOM   4984 C  CD   . GLU   B 1 64  ? 52.122 -9.545  0.641   1.00 12.89 ?  64   GLU   B CD   1 
ATOM   4985 O  OE1  . GLU   B 1 64  ? 52.313 -10.743 0.312   1.00 13.76 ?  64   GLU   B OE1  1 
ATOM   4986 O  OE2  . GLU   B 1 64  ? 51.498 -8.724  -0.080  1.00 13.76 -1 64   GLU   B OE2  1 
ATOM   4987 H  H    . GLU   B 1 64  ? 55.745 -10.926 3.466   1.00 14.62 ?  64   GLU   B H    1 
ATOM   4988 H  HA   . GLU   B 1 64  ? 54.516 -8.705  4.049   1.00 14.26 ?  64   GLU   B HA   1 
ATOM   4989 H  HB2  . GLU   B 1 64  ? 54.649 -9.389  1.857   1.00 14.56 ?  64   GLU   B HB2  1 
ATOM   4990 H  HB3  . GLU   B 1 64  ? 53.834 -10.709 2.184   1.00 14.56 ?  64   GLU   B HB3  1 
ATOM   4991 H  HG2  . GLU   B 1 64  ? 51.952 -9.235  2.649   1.00 14.60 ?  64   GLU   B HG2  1 
ATOM   4992 H  HG3  . GLU   B 1 64  ? 52.811 -8.113  1.925   1.00 14.60 ?  64   GLU   B HG3  1 
ATOM   4993 N  N    . SER   B 1 65  ? 52.935 -11.340 4.943   1.00 11.38 ?  65   SER   B N    1 
ATOM   4994 C  CA   . SER   B 1 65  ? 51.822 -11.848 5.738   1.00 11.51 ?  65   SER   B CA   1 
ATOM   4995 C  C    . SER   B 1 65  ? 51.953 -11.454 7.203   1.00 11.42 ?  65   SER   B C    1 
ATOM   4996 O  O    . SER   B 1 65  ? 50.956 -11.089 7.845   1.00 11.84 ?  65   SER   B O    1 
ATOM   4997 C  CB   . SER   B 1 65  ? 51.740 -13.369 5.603   1.00 12.03 ?  65   SER   B CB   1 
ATOM   4998 O  OG   . SER   B 1 65  ? 51.401 -13.761 4.281   1.00 11.83 ?  65   SER   B OG   1 
ATOM   4999 H  H    . SER   B 1 65  ? 53.445 -11.961 4.622   1.00 13.68 ?  65   SER   B H    1 
ATOM   5000 H  HA   . SER   B 1 65  ? 50.995 -11.475 5.396   1.00 13.84 ?  65   SER   B HA   1 
ATOM   5001 H  HB2  . SER   B 1 65  ? 52.599 -13.754 5.835   1.00 14.46 ?  65   SER   B HB2  1 
ATOM   5002 H  HB3  . SER   B 1 65  ? 51.057 -13.699 6.211   1.00 14.46 ?  65   SER   B HB3  1 
ATOM   5003 H  HG   . SER   B 1 65  ? 51.987 -13.472 3.742   1.00 14.22 ?  65   SER   B HG   1 
ATOM   5004 N  N    . ASP   B 1 66  ? 53.164 -11.544 7.761   1.00 11.85 ?  66   ASP   B N    1 
ATOM   5005 C  CA   . ASP   B 1 66  ? 53.355 -11.155 9.155   1.00 12.34 ?  66   ASP   B CA   1 
ATOM   5006 C  C    . ASP   B 1 66  ? 53.036 -9.679  9.357   1.00 12.34 ?  66   ASP   B C    1 
ATOM   5007 O  O    . ASP   B 1 66  ? 52.460 -9.291  10.379  1.00 12.87 ?  66   ASP   B O    1 
ATOM   5008 C  CB   . ASP   B 1 66  ? 54.791 -11.454 9.599   1.00 13.45 ?  66   ASP   B CB   1 
ATOM   5009 C  CG   . ASP   B 1 66  ? 55.074 -12.944 9.754   1.00 15.08 ?  66   ASP   B CG   1 
ATOM   5010 O  OD1  . ASP   B 1 66  ? 54.125 -13.761 9.670   1.00 15.90 ?  66   ASP   B OD1  1 
ATOM   5011 O  OD2  . ASP   B 1 66  ? 56.260 -13.292 9.978   1.00 17.74 -1 66   ASP   B OD2  1 
ATOM   5012 H  H    . ASP   B 1 66  ? 53.869 -11.837 7.367   1.00 14.24 ?  66   ASP   B H    1 
ATOM   5013 H  HA   . ASP   B 1 66  ? 52.758 -11.669 9.720   1.00 14.84 ?  66   ASP   B HA   1 
ATOM   5014 H  HB2  . ASP   B 1 66  ? 55.407 -11.103 8.935   1.00 16.16 ?  66   ASP   B HB2  1 
ATOM   5015 H  HB3  . ASP   B 1 66  ? 54.955 -11.026 10.457  1.00 16.16 ?  66   ASP   B HB3  1 
ATOM   5016 N  N    . ASP   B 1 67  ? 53.404 -8.836  8.392   1.00 11.91 ?  67   ASP   B N    1 
ATOM   5017 C  CA   . ASP   B 1 67  ? 53.057 -7.423  8.481   1.00 12.58 ?  67   ASP   B CA   1 
ATOM   5018 C  C    . ASP   B 1 67  ? 51.545 -7.218  8.404   1.00 12.96 ?  67   ASP   B C    1 
ATOM   5019 O  O    . ASP   B 1 67  ? 50.985 -6.408  9.156   1.00 13.82 ?  67   ASP   B O    1 
ATOM   5020 C  CB   . ASP   B 1 67  ? 53.777 -6.651  7.381   1.00 13.63 ?  67   ASP   B CB   1 
ATOM   5021 C  CG   . ASP   B 1 67  ? 53.351 -5.208  7.333   1.00 14.98 ?  67   ASP   B CG   1 
ATOM   5022 O  OD1  . ASP   B 1 67  ? 53.854 -4.396  8.144   1.00 16.16 ?  67   ASP   B OD1  1 
ATOM   5023 O  OD2  . ASP   B 1 67  ? 52.477 -4.902  6.502   1.00 16.35 -1 67   ASP   B OD2  1 
ATOM   5024 H  H    . ASP   B 1 67  ? 53.850 -9.056  7.692   1.00 14.32 ?  67   ASP   B H    1 
ATOM   5025 H  HA   . ASP   B 1 67  ? 53.364 -7.078  9.336   1.00 15.12 ?  67   ASP   B HA   1 
ATOM   5026 H  HB2  . ASP   B 1 67  ? 54.733 -6.679  7.542   1.00 16.38 ?  67   ASP   B HB2  1 
ATOM   5027 H  HB3  . ASP   B 1 67  ? 53.575 -7.064  6.522   1.00 16.38 ?  67   ASP   B HB3  1 
ATOM   5028 N  N    . TYR   B 1 68  ? 50.867 -7.951  7.515   1.00 12.40 ?  68   TYR   B N    1 
ATOM   5029 C  CA   . TYR   B 1 68  ? 49.410 -7.878  7.441   1.00 13.08 ?  68   TYR   B CA   1 
ATOM   5030 C  C    . TYR   B 1 68  ? 48.776 -8.222  8.786   1.00 12.52 ?  68   TYR   B C    1 
ATOM   5031 O  O    . TYR   B 1 68  ? 47.842 -7.547  9.239   1.00 13.24 ?  68   TYR   B O    1 
ATOM   5032 C  CB   . TYR   B 1 68  ? 48.879 -8.822  6.353   1.00 13.78 ?  68   TYR   B CB   1 
ATOM   5033 C  CG   . TYR   B 1 68  ? 47.366 -8.970  6.408   1.00 14.67 ?  68   TYR   B CG   1 
ATOM   5034 C  CD1  . TYR   B 1 68  ? 46.772 -9.921  7.231   1.00 15.14 ?  68   TYR   B CD1  1 
ATOM   5035 C  CD2  . TYR   B 1 68  ? 46.537 -8.135  5.676   1.00 15.54 ?  68   TYR   B CD2  1 
ATOM   5036 C  CE1  . TYR   B 1 68  ? 45.403 -10.042 7.320   1.00 16.14 ?  68   TYR   B CE1  1 
ATOM   5037 C  CE2  . TYR   B 1 68  ? 45.150 -8.257  5.753   1.00 15.69 ?  68   TYR   B CE2  1 
ATOM   5038 C  CZ   . TYR   B 1 68  ? 44.604 -9.209  6.580   1.00 16.02 ?  68   TYR   B CZ   1 
ATOM   5039 O  OH   . TYR   B 1 68  ? 43.236 -9.324  6.676   1.00 17.06 ?  68   TYR   B OH   1 
ATOM   5040 H  H    . TYR   B 1 68  ? 51.227 -8.500  6.953   1.00 14.90 ?  68   TYR   B H    1 
ATOM   5041 H  HA   . TYR   B 1 68  ? 49.155 -6.976  7.213   1.00 15.72 ?  68   TYR   B HA   1 
ATOM   5042 H  HB2  . TYR   B 1 68  ? 49.114 -8.464  5.486   1.00 16.56 ?  68   TYR   B HB2  1 
ATOM   5043 H  HB3  . TYR   B 1 68  ? 49.274 -9.699  6.474   1.00 16.56 ?  68   TYR   B HB3  1 
ATOM   5044 H  HD1  . TYR   B 1 68  ? 47.310 -10.491 7.737   1.00 18.19 ?  68   TYR   B HD1  1 
ATOM   5045 H  HD2  . TYR   B 1 68  ? 46.912 -7.486  5.132   1.00 18.68 ?  68   TYR   B HD2  1 
ATOM   5046 H  HE1  . TYR   B 1 68  ? 45.021 -10.697 7.863   1.00 19.39 ?  68   TYR   B HE1  1 
ATOM   5047 H  HE2  . TYR   B 1 68  ? 44.596 -7.695  5.260   1.00 18.85 ?  68   TYR   B HE2  1 
ATOM   5048 H  HH   . TYR   B 1 68  ? 42.852 -8.775  6.160   1.00 20.50 ?  68   TYR   B HH   1 
ATOM   5049 N  N    . ILE   B 1 69  ? 49.257 -9.291  9.428   1.00 12.47 ?  69   ILE   B N    1 
ATOM   5050 C  CA   . ILE   B 1 69  ? 48.703 -9.718  10.709  1.00 12.65 ?  69   ILE   B CA   1 
ATOM   5051 C  C    . ILE   B 1 69  ? 48.953 -8.672  11.789  1.00 12.76 ?  69   ILE   B C    1 
ATOM   5052 O  O    . ILE   B 1 69  ? 48.080 -8.398  12.620  1.00 12.95 ?  69   ILE   B O    1 
ATOM   5053 C  CB   . ILE   B 1 69  ? 49.279 -11.090 11.103  1.00 13.71 ?  69   ILE   B CB   1 
ATOM   5054 C  CG1  . ILE   B 1 69  ? 48.759 -12.190 10.169  1.00 14.39 ?  69   ILE   B CG1  1 
ATOM   5055 C  CG2  . ILE   B 1 69  ? 48.985 -11.408 12.564  1.00 14.76 ?  69   ILE   B CG2  1 
ATOM   5056 C  CD1  . ILE   B 1 69  ? 47.279 -12.497 10.317  1.00 14.83 ?  69   ILE   B CD1  1 
ATOM   5057 H  H    . ILE   B 1 69  ? 49.912 -9.775  9.148   1.00 14.99 ?  69   ILE   B H    1 
ATOM   5058 H  HA   . ILE   B 1 69  ? 47.748 -9.815  10.613  1.00 15.21 ?  69   ILE   B HA   1 
ATOM   5059 H  HB   . ILE   B 1 69  ? 50.246 -11.047 11.000  1.00 16.47 ?  69   ILE   B HB   1 
ATOM   5060 H  HG12 . ILE   B 1 69  ? 48.915 -11.913 9.251   1.00 17.29 ?  69   ILE   B HG12 1 
ATOM   5061 H  HG13 . ILE   B 1 69  ? 49.253 -13.007 10.348  1.00 17.29 ?  69   ILE   B HG13 1 
ATOM   5062 H  HG21 . ILE   B 1 69  ? 49.121 -12.358 12.707  1.00 17.74 ?  69   ILE   B HG21 1 
ATOM   5063 H  HG22 . ILE   B 1 69  ? 49.588 -10.901 13.128  1.00 17.74 ?  69   ILE   B HG22 1 
ATOM   5064 H  HG23 . ILE   B 1 69  ? 48.065 -11.173 12.756  1.00 17.74 ?  69   ILE   B HG23 1 
ATOM   5065 H  HD11 . ILE   B 1 69  ? 47.050 -13.215 9.709   1.00 17.82 ?  69   ILE   B HD11 1 
ATOM   5066 H  HD12 . ILE   B 1 69  ? 47.104 -12.771 11.231  1.00 17.82 ?  69   ILE   B HD12 1 
ATOM   5067 H  HD13 . ILE   B 1 69  ? 46.768 -11.704 10.103  1.00 17.82 ?  69   ILE   B HD13 1 
ATOM   5068 N  N    . ALA   B 1 70  ? 50.146 -8.081  11.815  1.00 12.64 ?  70   ALA   B N    1 
ATOM   5069 C  CA   . ALA   B 1 70  ? 50.418 -7.039  12.800  1.00 12.71 ?  70   ALA   B CA   1 
ATOM   5070 C  C    . ALA   B 1 70  ? 49.420 -5.894  12.679  1.00 13.07 ?  70   ALA   B C    1 
ATOM   5071 O  O    . ALA   B 1 70  ? 48.978 -5.342  13.689  1.00 13.56 ?  70   ALA   B O    1 
ATOM   5072 C  CB   . ALA   B 1 70  ? 51.850 -6.524  12.649  1.00 13.11 ?  70   ALA   B CB   1 
ATOM   5073 H  H    . ALA   B 1 70  ? 50.798 -8.265  11.292  1.00 15.20 ?  70   ALA   B H    1 
ATOM   5074 H  HA   . ALA   B 1 70  ? 50.334 -7.416  13.693  1.00 15.28 ?  70   ALA   B HA   1 
ATOM   5075 H  HB1  . ALA   B 1 70  ? 52.024 -5.857  13.335  1.00 15.75 ?  70   ALA   B HB1  1 
ATOM   5076 H  HB2  . ALA   B 1 70  ? 52.469 -7.266  12.753  1.00 15.75 ?  70   ALA   B HB2  1 
ATOM   5077 H  HB3  . ALA   B 1 70  ? 51.955 -6.129  11.771  1.00 15.75 ?  70   ALA   B HB3  1 
ATOM   5078 N  N    . THR   B 1 71  ? 49.055 -5.526  11.453  1.00 13.36 ?  71   THR   B N    1 
ATOM   5079 C  CA   . THR   B 1 71  ? 48.156 -4.396  11.239  1.00 14.09 ?  71   THR   B CA   1 
ATOM   5080 C  C    . THR   B 1 71  ? 46.688 -4.764  11.448  1.00 14.75 ?  71   THR   B C    1 
ATOM   5081 O  O    . THR   B 1 71  ? 45.913 -3.947  11.964  1.00 16.23 ?  71   THR   B O    1 
ATOM   5082 C  CB   . THR   B 1 71  ? 48.374 -3.838  9.833   1.00 15.95 ?  71   THR   B CB   1 
ATOM   5083 O  OG1  . THR   B 1 71  ? 49.701 -3.305  9.731   1.00 17.81 ?  71   THR   B OG1  1 
ATOM   5084 C  CG2  . THR   B 1 71  ? 47.359 -2.749  9.518   1.00 17.24 ?  71   THR   B CG2  1 
ATOM   5085 H  H    . THR   B 1 71  ? 49.316 -5.921  10.736  1.00 16.05 ?  71   THR   B H    1 
ATOM   5086 H  HA   . THR   B 1 71  ? 48.381 -3.701  11.874  1.00 16.93 ?  71   THR   B HA   1 
ATOM   5087 H  HB   . THR   B 1 71  ? 48.271 -4.548  9.181   1.00 19.16 ?  71   THR   B HB   1 
ATOM   5088 H  HG1  . THR   B 1 71  ? 49.820 -2.978  8.962   1.00 21.40 ?  71   THR   B HG1  1 
ATOM   5089 H  HG21 . THR   B 1 71  ? 47.662 -2.224  8.761   1.00 20.71 ?  71   THR   B HG21 1 
ATOM   5090 H  HG22 . THR   B 1 71  ? 46.500 -3.142  9.306   1.00 20.71 ?  71   THR   B HG22 1 
ATOM   5091 H  HG23 . THR   B 1 71  ? 47.258 -2.160  10.285  1.00 20.71 ?  71   THR   B HG23 1 
ATOM   5092 N  N    . ASN   B 1 72  ? 46.288 -5.979  11.057  1.00 14.34 ?  72   ASN   B N    1 
ATOM   5093 C  CA   . ASN   B 1 72  ? 44.882 -6.335  10.940  1.00 15.36 ?  72   ASN   B CA   1 
ATOM   5094 C  C    . ASN   B 1 72  ? 44.417 -7.438  11.880  1.00 15.37 ?  72   ASN   B C    1 
ATOM   5095 O  O    . ASN   B 1 72  ? 43.203 -7.596  12.051  1.00 16.55 ?  72   ASN   B O    1 
ATOM   5096 C  CB   . ASN   B 1 72  ? 44.560 -6.753  9.496   1.00 16.03 ?  72   ASN   B CB   1 
ATOM   5097 C  CG   . ASN   B 1 72  ? 44.851 -5.654  8.497   1.00 17.20 ?  72   ASN   B CG   1 
ATOM   5098 O  OD1  . ASN   B 1 72  ? 45.877 -5.664  7.815   1.00 18.34 ?  72   ASN   B OD1  1 
ATOM   5099 N  ND2  . ASN   B 1 72  ? 43.961 -4.687  8.421   1.00 18.50 ?  72   ASN   B ND2  1 
ATOM   5100 H  H    . ASN   B 1 72  ? 46.829 -6.623  10.850  1.00 17.23 ?  72   ASN   B H    1 
ATOM   5101 H  HA   . ASN   B 1 72  ? 44.357 -5.547  11.136  1.00 18.45 ?  72   ASN   B HA   1 
ATOM   5102 H  HB2  . ASN   B 1 72  ? 45.100 -7.523  9.260   1.00 19.26 ?  72   ASN   B HB2  1 
ATOM   5103 H  HB3  . ASN   B 1 72  ? 43.619 -6.971  9.434   1.00 19.26 ?  72   ASN   B HB3  1 
ATOM   5104 H  HD21 . ASN   B 1 72  ? 44.074 -4.036  7.867   1.00 22.22 ?  72   ASN   B HD21 1 
ATOM   5105 H  HD22 . ASN   B 1 72  ? 43.250 -4.713  8.908   1.00 22.22 ?  72   ASN   B HD22 1 
ATOM   5106 N  N    . GLY   B 1 73  ? 45.319 -8.195  12.492  1.00 14.71 ?  73   GLY   B N    1 
ATOM   5107 C  CA   . GLY   B 1 73  ? 44.916 -9.327  13.287  1.00 14.34 ?  73   GLY   B CA   1 
ATOM   5108 C  C    . GLY   B 1 73  ? 44.567 -10.517 12.418  1.00 13.05 ?  73   GLY   B C    1 
ATOM   5109 O  O    . GLY   B 1 73  ? 44.563 -10.438 11.187  1.00 13.23 ?  73   GLY   B O    1 
ATOM   5110 H  H    . GLY   B 1 73  ? 46.171 -8.070  12.455  1.00 17.68 ?  73   GLY   B H    1 
ATOM   5111 H  HA2  . GLY   B 1 73  ? 45.637 -9.574  13.890  1.00 17.23 ?  73   GLY   B HA2  1 
ATOM   5112 H  HA3  . GLY   B 1 73  ? 44.139 -9.090  13.821  1.00 17.23 ?  73   GLY   B HA3  1 
ATOM   5113 N  N    . PRO   B 1 74  ? 44.265 -11.645 13.056  1.00 13.46 ?  74   PRO   B N    1 
ATOM   5114 C  CA   . PRO   B 1 74  ? 44.016 -12.879 12.307  1.00 12.84 ?  74   PRO   B CA   1 
ATOM   5115 C  C    . PRO   B 1 74  ? 42.714 -12.828 11.518  1.00 12.33 ?  74   PRO   B C    1 
ATOM   5116 O  O    . PRO   B 1 74  ? 41.771 -12.094 11.838  1.00 13.91 ?  74   PRO   B O    1 
ATOM   5117 C  CB   . PRO   B 1 74  ? 43.950 -13.945 13.407  1.00 13.62 ?  74   PRO   B CB   1 
ATOM   5118 C  CG   . PRO   B 1 74  ? 43.490 -13.201 14.617  1.00 15.42 ?  74   PRO   B CG   1 
ATOM   5119 C  CD   . PRO   B 1 74  ? 44.144 -11.849 14.509  1.00 14.89 ?  74   PRO   B CD   1 
ATOM   5120 H  HA   . PRO   B 1 74  ? 44.763 -13.069 11.711  1.00 15.44 ?  74   PRO   B HA   1 
ATOM   5121 H  HB2  . PRO   B 1 74  ? 43.312 -14.633 13.157  1.00 16.36 ?  74   PRO   B HB2  1 
ATOM   5122 H  HB3  . PRO   B 1 74  ? 44.831 -14.328 13.550  1.00 16.36 ?  74   PRO   B HB3  1 
ATOM   5123 H  HG2  . PRO   B 1 74  ? 42.522 -13.120 14.602  1.00 18.52 ?  74   PRO   B HG2  1 
ATOM   5124 H  HG3  . PRO   B 1 74  ? 43.782 -13.664 15.417  1.00 18.52 ?  74   PRO   B HG3  1 
ATOM   5125 H  HD2  . PRO   B 1 74  ? 43.572 -11.169 14.905  1.00 17.89 ?  74   PRO   B HD2  1 
ATOM   5126 H  HD3  . PRO   B 1 74  ? 45.018 -11.863 14.925  1.00 17.89 ?  74   PRO   B HD3  1 
ATOM   5127 N  N    . LEU   B 1 75  ? 42.686 -13.643 10.468  1.00 11.72 ?  75   LEU   B N    1 
ATOM   5128 C  CA   . LEU   B 1 75  ? 41.473 -13.855 9.701   1.00 11.96 ?  75   LEU   B CA   1 
ATOM   5129 C  C    . LEU   B 1 75  ? 40.496 -14.716 10.501  1.00 12.60 ?  75   LEU   B C    1 
ATOM   5130 O  O    . LEU   B 1 75  ? 40.842 -15.293 11.534  1.00 13.51 ?  75   LEU   B O    1 
ATOM   5131 C  CB   . LEU   B 1 75  ? 41.797 -14.565 8.387   1.00 11.98 ?  75   LEU   B CB   1 
ATOM   5132 C  CG   . LEU   B 1 75  ? 42.636 -13.811 7.351   1.00 14.08 ?  75   LEU   B CG   1 
ATOM   5133 C  CD1  . LEU   B 1 75  ? 42.899 -14.682 6.122   1.00 15.68 ?  75   LEU   B CD1  1 
ATOM   5134 C  CD2  . LEU   B 1 75  ? 41.991 -12.515 6.946   1.00 17.57 ?  75   LEU   B CD2  1 
ATOM   5135 H  H    . LEU   B 1 75  ? 43.362 -14.096 10.180  1.00 14.09 ?  75   LEU   B H    1 
ATOM   5136 H  HA   . LEU   B 1 75  ? 41.054 -13.006 9.503   1.00 14.37 ?  75   LEU   B HA   1 
ATOM   5137 H  HB2  . LEU   B 1 75  ? 42.279 -15.385 8.596   1.00 14.41 ?  75   LEU   B HB2  1 
ATOM   5138 H  HB3  . LEU   B 1 75  ? 40.959 -14.800 7.954   1.00 14.41 ?  75   LEU   B HB3  1 
ATOM   5139 H  HG   . LEU   B 1 75  ? 43.496 -13.602 7.743   1.00 16.92 ?  75   LEU   B HG   1 
ATOM   5140 H  HD11 . LEU   B 1 75  ? 43.438 -14.178 5.485   1.00 18.84 ?  75   LEU   B HD11 1 
ATOM   5141 H  HD12 . LEU   B 1 75  ? 43.383 -15.480 6.393   1.00 18.84 ?  75   LEU   B HD12 1 
ATOM   5142 H  HD13 . LEU   B 1 75  ? 42.056 -14.929 5.715   1.00 18.84 ?  75   LEU   B HD13 1 
ATOM   5143 H  HD21 . LEU   B 1 75  ? 42.512 -12.112 6.238   1.00 21.10 ?  75   LEU   B HD21 1 
ATOM   5144 H  HD22 . LEU   B 1 75  ? 41.090 -12.697 6.636   1.00 21.10 ?  75   LEU   B HD22 1 
ATOM   5145 H  HD23 . LEU   B 1 75  ? 41.964 -11.928 7.717   1.00 21.10 ?  75   LEU   B HD23 1 
ATOM   5146 N  N    . LYS   B 1 76  ? 39.258 -14.798 10.005  1.00 13.71 ?  76   LYS   B N    1 
ATOM   5147 C  CA   . LYS   B 1 76  ? 38.275 -15.769 10.470  1.00 14.60 ?  76   LYS   B CA   1 
ATOM   5148 C  C    . LYS   B 1 76  ? 38.378 -17.042 9.631   1.00 13.23 ?  76   LYS   B C    1 
ATOM   5149 O  O    . LYS   B 1 76  ? 38.640 -16.983 8.432   1.00 12.74 ?  76   LYS   B O    1 
ATOM   5150 C  CB   . LYS   B 1 76  ? 36.854 -15.209 10.286  1.00 17.66 ?  76   LYS   B CB   1 
ATOM   5151 C  CG   . LYS   B 1 76  ? 36.576 -13.819 10.885  1.00 19.71 ?  76   LYS   B CG   1 
ATOM   5152 C  CD   . LYS   B 1 76  ? 35.166 -13.306 10.543  1.00 21.14 ?  76   LYS   B CD   1 
ATOM   5153 C  CE   . LYS   B 1 76  ? 34.911 -11.935 11.155  1.00 23.19 ?  76   LYS   B CE   1 
ATOM   5154 N  NZ   . LYS   B 1 76  ? 33.601 -11.357 10.754  1.00 23.53 ?  76   LYS   B NZ   1 
ATOM   5155 H  H    . LYS   B 1 76  ? 38.965 -14.295 9.373   1.00 16.48 ?  76   LYS   B H    1 
ATOM   5156 H  HA   . LYS   B 1 76  ? 38.423 -15.989 11.402  1.00 17.54 ?  76   LYS   B HA   1 
ATOM   5157 H  HB2  . LYS   B 1 76  ? 36.673 -15.153 9.334   1.00 21.22 ?  76   LYS   B HB2  1 
ATOM   5158 H  HB3  . LYS   B 1 76  ? 36.230 -15.827 10.695  1.00 21.22 ?  76   LYS   B HB3  1 
ATOM   5159 H  HG2  . LYS   B 1 76  ? 36.658 -13.868 11.850  1.00 23.67 ?  76   LYS   B HG2  1 
ATOM   5160 H  HG3  . LYS   B 1 76  ? 37.225 -13.186 10.529  1.00 23.67 ?  76   LYS   B HG3  1 
ATOM   5161 H  HD2  . LYS   B 1 76  ? 35.079 -13.233 9.578   1.00 25.40 ?  76   LYS   B HD2  1 
ATOM   5162 H  HD3  . LYS   B 1 76  ? 34.509 -13.927 10.893  1.00 25.40 ?  76   LYS   B HD3  1 
ATOM   5163 H  HE2  . LYS   B 1 76  ? 34.922 -12.017 12.121  1.00 27.85 ?  76   LYS   B HE2  1 
ATOM   5164 H  HE3  . LYS   B 1 76  ? 35.610 -11.328 10.865  1.00 27.85 ?  76   LYS   B HE3  1 
ATOM   5165 H  HZ1  . LYS   B 1 76  ? 33.491 -10.558 11.132  1.00 28.27 ?  76   LYS   B HZ1  1 
ATOM   5166 H  HZ2  . LYS   B 1 76  ? 33.565 -11.263 9.869   1.00 28.27 ?  76   LYS   B HZ2  1 
ATOM   5167 H  HZ3  . LYS   B 1 76  ? 32.938 -11.892 11.013  1.00 28.27 ?  76   LYS   B HZ3  1 
ATOM   5168 N  N    . VAL   B 1 77  ? 38.135 -18.201 10.257  1.00 13.74 ?  77   VAL   B N    1 
ATOM   5169 C  CA   . VAL   B 1 77  ? 37.922 -19.412 9.468   1.00 13.61 ?  77   VAL   B CA   1 
ATOM   5170 C  C    . VAL   B 1 77  ? 36.725 -19.177 8.557   1.00 12.62 ?  77   VAL   B C    1 
ATOM   5171 O  O    . VAL   B 1 77  ? 35.663 -18.722 9.003   1.00 12.95 ?  77   VAL   B O    1 
ATOM   5172 C  CB   . VAL   B 1 77  ? 37.731 -20.640 10.372  1.00 15.00 ?  77   VAL   B CB   1 
ATOM   5173 C  CG1  . VAL   B 1 77  ? 37.439 -21.871 9.519   1.00 15.63 ?  77   VAL   B CG1  1 
ATOM   5174 C  CG2  . VAL   B 1 77  ? 38.971 -20.873 11.237  1.00 16.24 ?  77   VAL   B CG2  1 
ATOM   5175 H  H    . VAL   B 1 77  ? 38.100 -18.307 11.102  1.00 16.51 ?  77   VAL   B H    1 
ATOM   5176 H  HA   . VAL   B 1 77  ? 38.701 -19.569 8.906   1.00 16.36 ?  77   VAL   B HA   1 
ATOM   5177 H  HB   . VAL   B 1 77  ? 36.973 -20.487 10.957  1.00 18.02 ?  77   VAL   B HB   1 
ATOM   5178 H  HG11 . VAL   B 1 77  ? 37.503 -22.659 10.078  1.00 18.78 ?  77   VAL   B HG11 1 
ATOM   5179 H  HG12 . VAL   B 1 77  ? 36.543 -21.798 9.151   1.00 18.78 ?  77   VAL   B HG12 1 
ATOM   5180 H  HG13 . VAL   B 1 77  ? 38.089 -21.919 8.802   1.00 18.78 ?  77   VAL   B HG13 1 
ATOM   5181 H  HG21 . VAL   B 1 77  ? 38.832 -21.670 11.772  1.00 19.51 ?  77   VAL   B HG21 1 
ATOM   5182 H  HG22 . VAL   B 1 77  ? 39.740 -20.990 10.660  1.00 19.51 ?  77   VAL   B HG22 1 
ATOM   5183 H  HG23 . VAL   B 1 77  ? 39.101 -20.105 11.814  1.00 19.51 ?  77   VAL   B HG23 1 
ATOM   5184 N  N    . GLY   B 1 78  ? 36.901 -19.463 7.267   1.00 12.11 ?  78   GLY   B N    1 
ATOM   5185 C  CA   . GLY   B 1 78  ? 35.924 -19.129 6.258   1.00 12.02 ?  78   GLY   B CA   1 
ATOM   5186 C  C    . GLY   B 1 78  ? 36.166 -17.808 5.563   1.00 11.50 ?  78   GLY   B C    1 
ATOM   5187 O  O    . GLY   B 1 78  ? 35.482 -17.519 4.576   1.00 11.91 ?  78   GLY   B O    1 
ATOM   5188 H  H    . GLY   B 1 78  ? 37.600 -19.860 6.949   1.00 14.56 ?  78   GLY   B H    1 
ATOM   5189 H  HA2  . GLY   B 1 78  ? 35.914 -19.823 5.582   1.00 14.44 ?  78   GLY   B HA2  1 
ATOM   5190 H  HA3  . GLY   B 1 78  ? 35.046 -19.095 6.668   1.00 14.44 ?  78   GLY   B HA3  1 
ATOM   5191 N  N    . GLY   B 1 79  ? 37.112 -16.999 6.050   1.00 11.33 ?  79   GLY   B N    1 
ATOM   5192 C  CA   . GLY   B 1 79  ? 37.414 -15.706 5.472   1.00 11.33 ?  79   GLY   B CA   1 
ATOM   5193 C  C    . GLY   B 1 79  ? 38.652 -15.722 4.588   1.00 10.80 ?  79   GLY   B C    1 
ATOM   5194 O  O    . GLY   B 1 79  ? 39.265 -16.756 4.340   1.00 11.53 ?  79   GLY   B O    1 
ATOM   5195 H  H    . GLY   B 1 79  ? 37.604 -17.189 6.726   1.00 13.62 ?  79   GLY   B H    1 
ATOM   5196 H  HA2  . GLY   B 1 79  ? 36.660 -15.406 4.935   1.00 13.62 ?  79   GLY   B HA2  1 
ATOM   5197 H  HA3  . GLY   B 1 79  ? 37.557 -15.062 6.181   1.00 13.62 ?  79   GLY   B HA3  1 
ATOM   5198 N  N    . SER   B 1 80  ? 39.014 -14.529 4.110   1.00 10.89 ?  80   SER   B N    1 
ATOM   5199 C  CA   . SER   B 1 80  ? 40.127 -14.395 3.180   1.00 10.75 ?  80   SER   B CA   1 
ATOM   5200 C  C    . SER   B 1 80  ? 40.707 -12.987 3.235   1.00 10.58 ?  80   SER   B C    1 
ATOM   5201 O  O    . SER   B 1 80  ? 40.091 -12.054 3.754   1.00 11.82 ?  80   SER   B O    1 
ATOM   5202 C  CB   . SER   B 1 80  ? 39.695 -14.684 1.741   1.00 10.88 ?  80   SER   B CB   1 
ATOM   5203 O  OG   . SER   B 1 80  ? 38.855 -13.667 1.225   1.00 12.04 ?  80   SER   B OG   1 
ATOM   5204 H  H    . SER   B 1 80  ? 38.639 -13.785 4.320   1.00 13.09 ?  80   SER   B H    1 
ATOM   5205 H  HA   . SER   B 1 80  ? 40.819 -15.025 3.431   1.00 12.92 ?  80   SER   B HA   1 
ATOM   5206 H  HB2  . SER   B 1 80  ? 40.481 -14.745 1.178   1.00 13.08 ?  80   SER   B HB2  1 
ATOM   5207 H  HB3  . SER   B 1 80  ? 39.209 -15.526 1.720   1.00 13.08 ?  80   SER   B HB3  1 
ATOM   5208 H  HG   . SER   B 1 80  ? 38.157 -13.599 1.702   1.00 14.47 ?  80   SER   B HG   1 
ATOM   5209 N  N    . CYS   B 1 81  ? 41.895 -12.837 2.648   1.00 10.49 ?  81   CYS   B N    1 
ATOM   5210 C  CA   . CYS   B 1 81  ? 42.440 -11.522 2.338   1.00 11.06 ?  81   CYS   B CA   1 
ATOM   5211 C  C    . CYS   B 1 81  ? 43.214 -11.604 1.031   1.00 10.09 ?  81   CYS   B C    1 
ATOM   5212 O  O    . CYS   B 1 81  ? 43.730 -12.667 0.657   1.00 11.20 ?  81   CYS   B O    1 
ATOM   5213 C  CB   . CYS   B 1 81  ? 43.330 -10.972 3.464   1.00 11.56 ?  81   CYS   B CB   1 
ATOM   5214 S  SG   . CYS   B 1 81  ? 44.855 -11.910 3.705   1.00 11.81 ?  81   CYS   B SG   1 
ATOM   5215 H  H    . CYS   B 1 81  ? 42.407 -13.490 2.411   1.00 12.61 ?  81   CYS   B H    1 
ATOM   5216 H  HA   . CYS   B 1 81  ? 41.708 -10.900 2.211   1.00 13.29 ?  81   CYS   B HA   1 
ATOM   5217 H  HB2  . CYS   B 1 81  ? 43.575 -10.058 3.255   1.00 13.89 ?  81   CYS   B HB2  1 
ATOM   5218 H  HB3  . CYS   B 1 81  ? 42.829 -10.993 4.298   1.00 13.89 ?  81   CYS   B HB3  1 
ATOM   5219 H  HG   . CYS   B 1 81  ? 45.484 -11.420 4.605   1.00 14.20 ?  81   CYS   B HG   1 
ATOM   5220 N  N    . VAL   B 1 82  ? 43.312 -10.460 0.357   1.00 10.69 ?  82   VAL   B N    1 
ATOM   5221 C  CA   . VAL   B 1 82  ? 44.074 -10.329 -0.880  1.00 10.84 ?  82   VAL   B CA   1 
ATOM   5222 C  C    . VAL   B 1 82  ? 45.417 -9.691  -0.559  1.00 10.67 ?  82   VAL   B C    1 
ATOM   5223 O  O    . VAL   B 1 82  ? 45.471 -8.579  -0.015  1.00 11.90 ?  82   VAL   B O    1 
ATOM   5224 C  CB   . VAL   B 1 82  ? 43.324 -9.482  -1.920  1.00 11.92 ?  82   VAL   B CB   1 
ATOM   5225 C  CG1  . VAL   B 1 82  ? 44.175 -9.319  -3.177  1.00 13.43 ?  82   VAL   B CG1  1 
ATOM   5226 C  CG2  . VAL   B 1 82  ? 41.972 -10.086 -2.255  1.00 12.83 ?  82   VAL   B CG2  1 
ATOM   5227 H  H    . VAL   B 1 82  ? 42.926 -9.724  0.600   1.00 12.85 ?  82   VAL   B H    1 
ATOM   5228 H  HA   . VAL   B 1 82  ? 44.227 -11.205 -1.258  1.00 13.03 ?  82   VAL   B HA   1 
ATOM   5229 H  HB   . VAL   B 1 82  ? 43.166 -8.596  -1.553  1.00 14.32 ?  82   VAL   B HB   1 
ATOM   5230 H  HG11 . VAL   B 1 82  ? 43.614 -8.999  -3.902  1.00 16.14 ?  82   VAL   B HG11 1 
ATOM   5231 H  HG12 . VAL   B 1 82  ? 44.881 -8.671  -3.004  1.00 16.14 ?  82   VAL   B HG12 1 
ATOM   5232 H  HG13 . VAL   B 1 82  ? 44.562 -10.174 -3.413  1.00 16.14 ?  82   VAL   B HG13 1 
ATOM   5233 H  HG21 . VAL   B 1 82  ? 41.538 -9.544  -2.936  1.00 15.41 ?  82   VAL   B HG21 1 
ATOM   5234 H  HG22 . VAL   B 1 82  ? 42.101 -10.988 -2.590  1.00 15.41 ?  82   VAL   B HG22 1 
ATOM   5235 H  HG23 . VAL   B 1 82  ? 41.423 -10.107 -1.455  1.00 15.41 ?  82   VAL   B HG23 1 
ATOM   5236 N  N    . LEU   B 1 83  ? 46.495 -10.375 -0.931  1.00 10.61 ?  83   LEU   B N    1 
ATOM   5237 C  CA   . LEU   B 1 83  ? 47.851 -9.859  -0.811  1.00 10.55 ?  83   LEU   B CA   1 
ATOM   5238 C  C    . LEU   B 1 83  ? 48.553 -10.004 -2.160  1.00 10.69 ?  83   LEU   B C    1 
ATOM   5239 O  O    . LEU   B 1 83  ? 47.946 -10.412 -3.153  1.00 10.64 ?  83   LEU   B O    1 
ATOM   5240 C  CB   . LEU   B 1 83  ? 48.599 -10.535 0.343   1.00 11.14 ?  83   LEU   B CB   1 
ATOM   5241 C  CG   . LEU   B 1 83  ? 48.089 -10.182 1.750   1.00 12.57 ?  83   LEU   B CG   1 
ATOM   5242 C  CD1  . LEU   B 1 83  ? 48.738 -11.050 2.815   1.00 12.74 ?  83   LEU   B CD1  1 
ATOM   5243 C  CD2  . LEU   B 1 83  ? 48.293 -8.703  2.064   1.00 13.84 ?  83   LEU   B CD2  1 
ATOM   5244 H  H    . LEU   B 1 83  ? 46.455 -11.172 -1.267  1.00 12.75 ?  83   LEU   B H    1 
ATOM   5245 H  HA   . LEU   B 1 83  ? 47.792 -8.913  -0.617  1.00 12.68 ?  83   LEU   B HA   1 
ATOM   5246 H  HB2  . LEU   B 1 83  ? 48.527 -11.492 0.237   1.00 13.39 ?  83   LEU   B HB2  1 
ATOM   5247 H  HB3  . LEU   B 1 83  ? 49.530 -10.267 0.292   1.00 13.39 ?  83   LEU   B HB3  1 
ATOM   5248 H  HG   . LEU   B 1 83  ? 47.137 -10.349 1.779   1.00 15.11 ?  83   LEU   B HG   1 
ATOM   5249 H  HD11 . LEU   B 1 83  ? 48.386 -10.801 3.685   1.00 15.31 ?  83   LEU   B HD11 1 
ATOM   5250 H  HD12 . LEU   B 1 83  ? 48.529 -11.981 2.631   1.00 15.31 ?  83   LEU   B HD12 1 
ATOM   5251 H  HD13 . LEU   B 1 83  ? 49.697 -10.917 2.795   1.00 15.31 ?  83   LEU   B HD13 1 
ATOM   5252 H  HD21 . LEU   B 1 83  ? 48.093 -8.550  3.002   1.00 16.63 ?  83   LEU   B HD21 1 
ATOM   5253 H  HD22 . LEU   B 1 83  ? 49.214 -8.463  1.880   1.00 16.63 ?  83   LEU   B HD22 1 
ATOM   5254 H  HD23 . LEU   B 1 83  ? 47.696 -8.175  1.510   1.00 16.63 ?  83   LEU   B HD23 1 
ATOM   5255 N  N    . SER   B 1 84  ? 49.831 -9.632  -2.212  1.00 11.46 ?  84   SER   B N    1 
ATOM   5256 C  CA   . SER   B 1 84  ? 50.565 -9.736  -3.466  1.00 11.67 ?  84   SER   B CA   1 
ATOM   5257 C  C    . SER   B 1 84  ? 50.726 -11.192 -3.890  1.00 10.85 ?  84   SER   B C    1 
ATOM   5258 O  O    . SER   B 1 84  ? 50.834 -12.095 -3.063  1.00 10.81 ?  84   SER   B O    1 
ATOM   5259 C  CB   . SER   B 1 84  ? 51.954 -9.125  -3.313  1.00 13.43 ?  84   SER   B CB   1 
ATOM   5260 O  OG   . SER   B 1 84  ? 52.709 -9.350  -4.486  1.00 15.46 ?  84   SER   B OG   1 
ATOM   5261 H  H    . SER   B 1 84  ? 50.282 -9.314  -1.550  1.00 13.78 ?  84   SER   B H    1 
ATOM   5262 H  HA   . SER   B 1 84  ? 50.088 -9.263  -4.163  1.00 14.03 ?  84   SER   B HA   1 
ATOM   5263 H  HB2  . SER   B 1 84  ? 51.864 -8.166  -3.164  1.00 16.13 ?  84   SER   B HB2  1 
ATOM   5264 H  HB3  . SER   B 1 84  ? 52.407 -9.535  -2.563  1.00 16.13 ?  84   SER   B HB3  1 
ATOM   5265 H  HG   . SER   B 1 84  ? 53.477 -8.997  -4.411  1.00 18.58 ?  84   SER   B HG   1 
ATOM   5266 N  N    . GLY   B 1 85  ? 50.782 -11.409 -5.197  1.00 12.12 ?  85   GLY   B N    1 
ATOM   5267 C  CA   . GLY   B 1 85  ? 51.138 -12.699 -5.737  1.00 12.58 ?  85   GLY   B CA   1 
ATOM   5268 C  C    . GLY   B 1 85  ? 52.609 -12.888 -6.041  1.00 11.89 ?  85   GLY   B C    1 
ATOM   5269 O  O    . GLY   B 1 85  ? 52.989 -13.964 -6.511  1.00 12.50 ?  85   GLY   B O    1 
ATOM   5270 H  H    . GLY   B 1 85  ? 50.616 -10.819 -5.797  1.00 14.57 ?  85   GLY   B H    1 
ATOM   5271 H  HA2  . GLY   B 1 85  ? 50.877 -13.392 -5.107  1.00 15.12 ?  85   GLY   B HA2  1 
ATOM   5272 H  HA3  . GLY   B 1 85  ? 50.648 -12.848 -6.559  1.00 15.12 ?  85   GLY   B HA3  1 
ATOM   5273 N  N    . HIS   B 1 86  ? 53.453 -11.887 -5.807  1.00 11.93 ?  86   HIS   B N    1 
ATOM   5274 C  CA   . HIS   B 1 86  ? 54.913 -12.055 -5.902  1.00 11.88 ?  86   HIS   B CA   1 
ATOM   5275 C  C    . HIS   B 1 86  ? 55.283 -12.559 -7.295  1.00 12.16 ?  86   HIS   B C    1 
ATOM   5276 O  O    . HIS   B 1 86  ? 54.892 -11.938 -8.297  1.00 12.90 ?  86   HIS   B O    1 
ATOM   5277 C  CB   . HIS   B 1 86  ? 55.412 -12.903 -4.734  1.00 12.39 ?  86   HIS   B CB   1 
ATOM   5278 C  CG   . HIS   B 1 86  ? 55.100 -12.302 -3.404  1.00 12.34 ?  86   HIS   B CG   1 
ATOM   5279 N  ND1  . HIS   B 1 86  ? 55.923 -11.380 -2.794  1.00 13.77 ?  86   HIS   B ND1  1 
ATOM   5280 C  CD2  . HIS   B 1 86  ? 54.033 -12.463 -2.584  1.00 12.88 ?  86   HIS   B CD2  1 
ATOM   5281 C  CE1  . HIS   B 1 86  ? 55.371 -11.000 -1.655  1.00 13.58 ?  86   HIS   B CE1  1 
ATOM   5282 N  NE2  . HIS   B 1 86  ? 54.223 -11.637 -1.506  1.00 12.94 ?  86   HIS   B NE2  1 
ATOM   5283 H  H    . HIS   B 1 86  ? 53.214 -11.091 -5.602  1.00 14.34 ?  86   HIS   B H    1 
ATOM   5284 H  HA   . HIS   B 1 86  ? 55.324 -11.183 -5.803  1.00 14.28 ?  86   HIS   B HA   1 
ATOM   5285 H  HB2  . HIS   B 1 86  ? 54.997 -13.779 -4.777  1.00 14.89 ?  86   HIS   B HB2  1 
ATOM   5286 H  HB3  . HIS   B 1 86  ? 56.380 -12.999 -4.800  1.00 14.89 ?  86   HIS   B HB3  1 
ATOM   5287 H  HD2  . HIS   B 1 86  ? 53.303 -13.022 -2.737  1.00 15.48 ?  86   HIS   B HD2  1 
ATOM   5288 H  HE1  . HIS   B 1 86  ? 55.739 -10.399 -1.052  1.00 16.32 ?  86   HIS   B HE1  1 
ATOM   5289 H  HE2  . HIS   B 1 86  ? 53.694 -11.569 -0.835  1.00 15.56 ?  86   HIS   B HE2  1 
ATOM   5290 N  N    . ASN   B 1 87  ? 56.056 -13.640 -7.410  1.00 12.52 ?  87   ASN   B N    1 
ATOM   5291 C  CA   . ASN   B 1 87  ? 56.453 -14.217 -8.686  1.00 12.99 ?  87   ASN   B CA   1 
ATOM   5292 C  C    . ASN   B 1 87  ? 55.473 -15.260 -9.192  1.00 12.56 ?  87   ASN   B C    1 
ATOM   5293 O  O    . ASN   B 1 87  ? 55.795 -15.970 -10.151 1.00 14.19 ?  87   ASN   B O    1 
ATOM   5294 C  CB   . ASN   B 1 87  ? 57.849 -14.850 -8.574  1.00 14.68 ?  87   ASN   B CB   1 
ATOM   5295 C  CG   . ASN   B 1 87  ? 57.919 -15.937 -7.511  1.00 15.92 ?  87   ASN   B CG   1 
ATOM   5296 O  OD1  . ASN   B 1 87  ? 57.269 -15.846 -6.471  1.00 15.09 ?  87   ASN   B OD1  1 
ATOM   5297 N  ND2  . ASN   B 1 87  ? 58.699 -16.989 -7.782  1.00 18.32 ?  87   ASN   B ND2  1 
ATOM   5298 H  H    . ASN   B 1 87  ? 56.372 -14.071 -6.740  1.00 15.05 ?  87   ASN   B H    1 
ATOM   5299 H  HA   . ASN   B 1 87  ? 56.505 -13.512 -9.350  1.00 15.62 ?  87   ASN   B HA   1 
ATOM   5300 H  HB2  . ASN   B 1 87  ? 58.087 -15.251 -9.429  1.00 17.64 ?  87   ASN   B HB2  1 
ATOM   5301 H  HB3  . ASN   B 1 87  ? 58.492 -14.165 -8.342  1.00 17.64 ?  87   ASN   B HB3  1 
ATOM   5302 H  HD21 . ASN   B 1 87  ? 58.777 -17.629 -7.212  1.00 22.01 ?  87   ASN   B HD21 1 
ATOM   5303 H  HD22 . ASN   B 1 87  ? 59.139 -17.023 -8.524  1.00 22.01 ?  87   ASN   B HD22 1 
ATOM   5304 N  N    . LEU   B 1 88  ? 54.293 -15.360 -8.577  1.00 11.81 ?  88   LEU   B N    1 
ATOM   5305 C  CA   . LEU   B 1 88  ? 53.317 -16.392 -8.899  1.00 12.13 ?  88   LEU   B CA   1 
ATOM   5306 C  C    . LEU   B 1 88  ? 52.079 -15.876 -9.617  1.00 11.82 ?  88   LEU   B C    1 
ATOM   5307 O  O    . LEU   B 1 88  ? 51.477 -16.623 -10.397 1.00 13.31 ?  88   LEU   B O    1 
ATOM   5308 C  CB   . LEU   B 1 88  ? 52.852 -17.073 -7.609  1.00 13.22 ?  88   LEU   B CB   1 
ATOM   5309 C  CG   . LEU   B 1 88  ? 53.967 -17.719 -6.801  1.00 15.38 ?  88   LEU   B CG   1 
ATOM   5310 C  CD1  . LEU   B 1 88  ? 53.467 -18.047 -5.404  1.00 16.93 ?  88   LEU   B CD1  1 
ATOM   5311 C  CD2  . LEU   B 1 88  ? 54.442 -18.969 -7.509  1.00 18.80 ?  88   LEU   B CD2  1 
ATOM   5312 H  H    . LEU   B 1 88  ? 54.041 -14.836 -7.938  1.00 14.19 ?  88   LEU   B H    1 
ATOM   5313 H  HA   . LEU   B 1 88  ? 53.735 -17.060 -9.456  1.00 14.58 ?  88   LEU   B HA   1 
ATOM   5314 H  HB2  . LEU   B 1 88  ? 52.421 -16.413 -7.040  1.00 15.89 ?  88   LEU   B HB2  1 
ATOM   5315 H  HB3  . LEU   B 1 88  ? 52.214 -17.769 -7.837  1.00 15.89 ?  88   LEU   B HB3  1 
ATOM   5316 H  HG   . LEU   B 1 88  ? 54.712 -17.102 -6.724  1.00 18.48 ?  88   LEU   B HG   1 
ATOM   5317 H  HD11 . LEU   B 1 88  ? 54.099 -18.641 -4.975  1.00 20.34 ?  88   LEU   B HD11 1 
ATOM   5318 H  HD12 . LEU   B 1 88  ? 53.387 -17.223 -4.897  1.00 20.34 ?  88   LEU   B HD12 1 
ATOM   5319 H  HD13 . LEU   B 1 88  ? 52.600 -18.475 -5.476  1.00 20.34 ?  88   LEU   B HD13 1 
ATOM   5320 H  HD21 . LEU   B 1 88  ? 55.110 -19.407 -6.957  1.00 22.58 ?  88   LEU   B HD21 1 
ATOM   5321 H  HD22 . LEU   B 1 88  ? 53.687 -19.561 -7.646  1.00 22.58 ?  88   LEU   B HD22 1 
ATOM   5322 H  HD23 . LEU   B 1 88  ? 54.831 -18.722 -8.362  1.00 22.58 ?  88   LEU   B HD23 1 
ATOM   5323 N  N    . ALA   B 1 89  ? 51.671 -14.640 -9.354  1.00 11.21 ?  89   ALA   B N    1 
ATOM   5324 C  CA   . ALA   B 1 89  ? 50.371 -14.153 -9.795  1.00 10.99 ?  89   ALA   B CA   1 
ATOM   5325 C  C    . ALA   B 1 89  ? 50.341 -12.660 -9.518  1.00 11.18 ?  89   ALA   B C    1 
ATOM   5326 O  O    . ALA   B 1 89  ? 51.189 -12.139 -8.794  1.00 12.23 ?  89   ALA   B O    1 
ATOM   5327 C  CB   . ALA   B 1 89  ? 49.250 -14.844 -9.025  1.00 11.15 ?  89   ALA   B CB   1 
ATOM   5328 H  H    . ALA   B 1 89  ? 52.131 -14.054 -8.915  1.00 13.47 ?  89   ALA   B H    1 
ATOM   5329 H  HA   . ALA   B 1 89  ? 50.256 -14.308 -10.749 1.00 13.22 ?  89   ALA   B HA   1 
ATOM   5330 H  HB1  . ALA   B 1 89  ? 48.398 -14.516 -9.347  1.00 13.40 ?  89   ALA   B HB1  1 
ATOM   5331 H  HB2  . ALA   B 1 89  ? 49.315 -15.802 -9.172  1.00 13.40 ?  89   ALA   B HB2  1 
ATOM   5332 H  HB3  . ALA   B 1 89  ? 49.352 -14.647 -8.083  1.00 13.40 ?  89   ALA   B HB3  1 
ATOM   5333 N  N    . LYS   B 1 90  ? 49.344 -11.970 -10.071 1.00 12.05 ?  90   LYS   B N    1 
ATOM   5334 C  CA   . LYS   B 1 90  ? 49.145 -10.586 -9.659  1.00 12.68 ?  90   LYS   B CA   1 
ATOM   5335 C  C    . LYS   B 1 90  ? 48.837 -10.519 -8.167  1.00 12.29 ?  90   LYS   B C    1 
ATOM   5336 O  O    . LYS   B 1 90  ? 49.479 -9.770  -7.417  1.00 13.37 ?  90   LYS   B O    1 
ATOM   5337 C  CB   . LYS   B 1 90  ? 48.050 -9.927  -10.501 1.00 14.01 ?  90   LYS   B CB   1 
ATOM   5338 C  CG   . LYS   B 1 90  ? 47.772 -8.482  -10.131 1.00 14.99 ?  90   LYS   B CG   1 
ATOM   5339 C  CD   . LYS   B 1 90  ? 48.990 -7.589  -10.221 1.00 17.78 ?  90   LYS   B CD   1 
ATOM   5340 C  CE   . LYS   B 1 90  ? 48.555 -6.158  -10.001 1.00 19.80 ?  90   LYS   B CE   1 
ATOM   5341 N  NZ   . LYS   B 1 90  ? 49.699 -5.225  -9.872  1.00 20.19 ?  90   LYS   B NZ   1 
ATOM   5342 H  H    . LYS   B 1 90  ? 48.790 -12.273 -10.656 1.00 14.49 ?  90   LYS   B H    1 
ATOM   5343 H  HA   . LYS   B 1 90  ? 49.966 -10.102 -9.812  1.00 15.24 ?  90   LYS   B HA   1 
ATOM   5344 H  HB2  . LYS   B 1 90  ? 48.319 -9.947  -11.434 1.00 16.84 ?  90   LYS   B HB2  1 
ATOM   5345 H  HB3  . LYS   B 1 90  ? 47.223 -10.426 -10.391 1.00 16.84 ?  90   LYS   B HB3  1 
ATOM   5346 H  HG2  . LYS   B 1 90  ? 47.099 -8.126  -10.733 1.00 18.01 ?  90   LYS   B HG2  1 
ATOM   5347 H  HG3  . LYS   B 1 90  ? 47.442 -8.446  -9.217  1.00 18.01 ?  90   LYS   B HG3  1 
ATOM   5348 H  HD2  . LYS   B 1 90  ? 49.629 -7.832  -9.530  1.00 21.36 ?  90   LYS   B HD2  1 
ATOM   5349 H  HD3  . LYS   B 1 90  ? 49.391 -7.667  -11.101 1.00 21.36 ?  90   LYS   B HD3  1 
ATOM   5350 H  HE2  . LYS   B 1 90  ? 48.022 -5.867  -10.758 1.00 23.79 ?  90   LYS   B HE2  1 
ATOM   5351 H  HE3  . LYS   B 1 90  ? 48.036 -6.101  -9.186  1.00 23.79 ?  90   LYS   B HE3  1 
ATOM   5352 H  HZ1  . LYS   B 1 90  ? 49.406 -4.390  -9.747  1.00 24.25 ?  90   LYS   B HZ1  1 
ATOM   5353 H  HZ2  . LYS   B 1 90  ? 50.210 -5.455  -9.180  1.00 24.25 ?  90   LYS   B HZ2  1 
ATOM   5354 H  HZ3  . LYS   B 1 90  ? 50.197 -5.241  -10.613 1.00 24.25 ?  90   LYS   B HZ3  1 
ATOM   5355 N  N    . HIS   B 1 91  ? 47.886 -11.341 -7.715  1.00 10.78 ?  91   HIS   B N    1 
ATOM   5356 C  CA   . HIS   B 1 91  ? 47.424 -11.367 -6.339  1.00 11.00 ?  91   HIS   B CA   1 
ATOM   5357 C  C    . HIS   B 1 91  ? 47.425 -12.794 -5.822  1.00 9.98  ?  91   HIS   B C    1 
ATOM   5358 O  O    . HIS   B 1 91  ? 47.194 -13.747 -6.575  1.00 10.60 ?  91   HIS   B O    1 
ATOM   5359 C  CB   . HIS   B 1 91  ? 45.971 -10.887 -6.216  1.00 12.50 ?  91   HIS   B CB   1 
ATOM   5360 C  CG   . HIS   B 1 91  ? 45.758 -9.482  -6.651  1.00 15.91 ?  91   HIS   B CG   1 
ATOM   5361 N  ND1  . HIS   B 1 91  ? 46.374 -8.411  -6.042  1.00 18.69 ?  91   HIS   B ND1  1 
ATOM   5362 C  CD2  . HIS   B 1 91  ? 44.964 -8.964  -7.613  1.00 18.03 ?  91   HIS   B CD2  1 
ATOM   5363 C  CE1  . HIS   B 1 91  ? 45.986 -7.290  -6.627  1.00 19.49 ?  91   HIS   B CE1  1 
ATOM   5364 N  NE2  . HIS   B 1 91  ? 45.125 -7.599  -7.581  1.00 19.61 ?  91   HIS   B NE2  1 
ATOM   5365 H  H    . HIS   B 1 91  ? 47.474 -11.911 -8.215  1.00 12.96 ?  91   HIS   B H    1 
ATOM   5366 H  HA   . HIS   B 1 91  ? 47.996 -10.813 -5.778  1.00 13.23 ?  91   HIS   B HA   1 
ATOM   5367 H  HB2  . HIS   B 1 91  ? 45.411 -11.455 -6.766  1.00 15.03 ?  91   HIS   B HB2  1 
ATOM   5368 H  HB3  . HIS   B 1 91  ? 45.699 -10.957 -5.287  1.00 15.03 ?  91   HIS   B HB3  1 
ATOM   5369 H  HD1  . HIS   B 1 91  ? 46.932 -8.459  -5.388  1.00 22.46 ?  91   HIS   B HD1  1 
ATOM   5370 H  HD2  . HIS   B 1 91  ? 44.419 -9.433  -8.196  1.00 21.66 ?  91   HIS   B HD2  1 
ATOM   5371 H  HE1  . HIS   B 1 91  ? 46.267 -6.428  -6.395  1.00 23.41 ?  91   HIS   B HE1  1 
ATOM   5372 N  N    . CYS   B 1 92  ? 47.626 -12.929 -4.520  1.00 9.83  ?  92   CYS   B N    1 
ATOM   5373 C  CA   . CYS   B 1 92  ? 47.326 -14.165 -3.808  1.00 9.77  ?  92   CYS   B CA   1 
ATOM   5374 C  C    . CYS   B 1 92  ? 46.103 -13.934 -2.928  1.00 9.35  ?  92   CYS   B C    1 
ATOM   5375 O  O    . CYS   B 1 92  ? 46.106 -13.037 -2.071  1.00 10.48 ?  92   CYS   B O    1 
ATOM   5376 C  CB   . CYS   B 1 92  ? 48.511 -14.620 -2.960  1.00 10.28 ?  92   CYS   B CB   1 
ATOM   5377 S  SG   . CYS   B 1 92  ? 48.153 -16.159 -2.065  1.00 10.38 ?  92   CYS   B SG   1 
ATOM   5378 H  H    . CYS   B 1 92  ? 47.957 -12.310 -4.014  1.00 11.82 ?  92   CYS   B H    1 
ATOM   5379 H  HA   . CYS   B 1 92  ? 47.131 -14.863 -4.453  1.00 11.75 ?  92   CYS   B HA   1 
ATOM   5380 H  HB2  . CYS   B 1 92  ? 49.277 -14.776 -3.534  1.00 12.37 ?  92   CYS   B HB2  1 
ATOM   5381 H  HB3  . CYS   B 1 92  ? 48.717 -13.931 -2.309  1.00 12.37 ?  92   CYS   B HB3  1 
ATOM   5382 H  HG   . CYS   B 1 92  ? 49.125 -16.474 -1.434  1.00 12.48 ?  92   CYS   B HG   1 
ATOM   5383 N  N    . LEU   B 1 93  ? 45.066 -14.744 -3.143  1.00 9.49  ?  93   LEU   B N    1 
ATOM   5384 C  CA   . LEU   B 1 93  ? 43.893 -14.761 -2.279  1.00 9.46  ?  93   LEU   B CA   1 
ATOM   5385 C  C    . LEU   B 1 93  ? 44.125 -15.828 -1.219  1.00 9.06  ?  93   LEU   B C    1 
ATOM   5386 O  O    . LEU   B 1 93  ? 44.082 -17.028 -1.515  1.00 9.68  ?  93   LEU   B O    1 
ATOM   5387 C  CB   . LEU   B 1 93  ? 42.631 -15.045 -3.087  1.00 9.64  ?  93   LEU   B CB   1 
ATOM   5388 C  CG   . LEU   B 1 93  ? 41.332 -15.068 -2.280  1.00 10.36 ?  93   LEU   B CG   1 
ATOM   5389 C  CD1  . LEU   B 1 93  ? 40.966 -13.676 -1.776  1.00 10.94 ?  93   LEU   B CD1  1 
ATOM   5390 C  CD2  . LEU   B 1 93  ? 40.208 -15.654 -3.115  1.00 11.29 ?  93   LEU   B CD2  1 
ATOM   5391 H  H    . LEU   B 1 93  ? 45.022 -15.309 -3.801  1.00 11.42 ?  93   LEU   B H    1 
ATOM   5392 H  HA   . LEU   B 1 93  ? 43.801 -13.901 -1.846  1.00 11.38 ?  93   LEU   B HA   1 
ATOM   5393 H  HB2  . LEU   B 1 93  ? 42.540 -14.355 -3.766  1.00 11.59 ?  93   LEU   B HB2  1 
ATOM   5394 H  HB3  . LEU   B 1 93  ? 42.724 -15.908 -3.513  1.00 11.59 ?  93   LEU   B HB3  1 
ATOM   5395 H  HG   . LEU   B 1 93  ? 41.455 -15.634 -1.505  1.00 12.46 ?  93   LEU   B HG   1 
ATOM   5396 H  HD11 . LEU   B 1 93  ? 40.117 -13.721 -1.307  1.00 13.16 ?  93   LEU   B HD11 1 
ATOM   5397 H  HD12 . LEU   B 1 93  ? 41.658 -13.358 -1.175  1.00 13.16 ?  93   LEU   B HD12 1 
ATOM   5398 H  HD13 . LEU   B 1 93  ? 40.887 -13.071 -2.535  1.00 13.16 ?  93   LEU   B HD13 1 
ATOM   5399 H  HD21 . LEU   B 1 93  ? 39.391 -15.646 -2.596  1.00 13.57 ?  93   LEU   B HD21 1 
ATOM   5400 H  HD22 . LEU   B 1 93  ? 40.099 -15.122 -3.918  1.00 13.57 ?  93   LEU   B HD22 1 
ATOM   5401 H  HD23 . LEU   B 1 93  ? 40.441 -16.568 -3.354  1.00 13.57 ?  93   LEU   B HD23 1 
ATOM   5402 N  N    . HIS   B 1 94  ? 44.392 -15.391 0.007   1.00 9.28  ?  94   HIS   B N    1 
ATOM   5403 C  CA   . HIS   B 1 94  ? 44.615 -16.294 1.130   1.00 9.34  ?  94   HIS   B CA   1 
ATOM   5404 C  C    . HIS   B 1 94  ? 43.257 -16.645 1.716   1.00 9.51  ?  94   HIS   B C    1 
ATOM   5405 O  O    . HIS   B 1 94  ? 42.590 -15.770 2.274   1.00 10.86 ?  94   HIS   B O    1 
ATOM   5406 C  CB   . HIS   B 1 94  ? 45.489 -15.614 2.182   1.00 9.78  ?  94   HIS   B CB   1 
ATOM   5407 C  CG   . HIS   B 1 94  ? 46.871 -15.312 1.705   1.00 9.53  ?  94   HIS   B CG   1 
ATOM   5408 N  ND1  . HIS   B 1 94  ? 47.900 -16.226 1.793   1.00 9.95  ?  94   HIS   B ND1  1 
ATOM   5409 C  CD2  . HIS   B 1 94  ? 47.376 -14.206 1.104   1.00 10.21 ?  94   HIS   B CD2  1 
ATOM   5410 C  CE1  . HIS   B 1 94  ? 48.989 -15.676 1.286   1.00 10.13 ?  94   HIS   B CE1  1 
ATOM   5411 N  NE2  . HIS   B 1 94  ? 48.700 -14.456 0.856   1.00 10.23 ?  94   HIS   B NE2  1 
ATOM   5412 H  H    . HIS   B 1 94  ? 44.444 -14.554 0.221   1.00 11.16 ?  94   HIS   B H    1 
ATOM   5413 H  HA   . HIS   B 1 94  ? 45.051 -17.102 0.825   1.00 11.23 ?  94   HIS   B HA   1 
ATOM   5414 H  HB2  . HIS   B 1 94  ? 45.074 -14.776 2.442   1.00 11.76 ?  94   HIS   B HB2  1 
ATOM   5415 H  HB3  . HIS   B 1 94  ? 45.563 -16.197 2.953   1.00 11.76 ?  94   HIS   B HB3  1 
ATOM   5416 H  HD2  . HIS   B 1 94  ? 46.921 -13.423 0.905   1.00 12.28 ?  94   HIS   B HD2  1 
ATOM   5417 H  HE1  . HIS   B 1 94  ? 49.822 -16.093 1.236   1.00 12.18 ?  94   HIS   B HE1  1 
ATOM   5418 H  HE2  . HIS   B 1 94  ? 49.260 -13.918 0.490   1.00 12.30 ?  94   HIS   B HE2  1 
ATOM   5419 N  N    . VAL   B 1 95  ? 42.823 -17.900 1.560   1.00 9.48  ?  95   VAL   B N    1 
ATOM   5420 C  CA   . VAL   B 1 95  ? 41.497 -18.338 1.993   1.00 9.74  ?  95   VAL   B CA   1 
ATOM   5421 C  C    . VAL   B 1 95  ? 41.661 -19.380 3.083   1.00 9.82  ?  95   VAL   B C    1 
ATOM   5422 O  O    . VAL   B 1 95  ? 42.430 -20.335 2.918   1.00 10.37 ?  95   VAL   B O    1 
ATOM   5423 C  CB   . VAL   B 1 95  ? 40.675 -18.937 0.837   1.00 9.92  ?  95   VAL   B CB   1 
ATOM   5424 C  CG1  . VAL   B 1 95  ? 39.302 -19.386 1.330   1.00 10.74 ?  95   VAL   B CG1  1 
ATOM   5425 C  CG2  . VAL   B 1 95  ? 40.530 -17.961 -0.299  1.00 9.93  ?  95   VAL   B CG2  1 
ATOM   5426 H  H    . VAL   B 1 95  ? 43.288 -18.527 1.197   1.00 11.40 ?  95   VAL   B H    1 
ATOM   5427 H  HA   . VAL   B 1 95  ? 41.007 -17.583 2.360   1.00 11.71 ?  95   VAL   B HA   1 
ATOM   5428 H  HB   . VAL   B 1 95  ? 41.132 -19.718 0.500   1.00 11.93 ?  95   VAL   B HB   1 
ATOM   5429 H  HG11 . VAL   B 1 95  ? 38.731 -19.564 0.564   1.00 12.91 ?  95   VAL   B HG11 1 
ATOM   5430 H  HG12 . VAL   B 1 95  ? 39.397 -20.191 1.861   1.00 12.91 ?  95   VAL   B HG12 1 
ATOM   5431 H  HG13 . VAL   B 1 95  ? 38.908 -18.678 1.869   1.00 12.91 ?  95   VAL   B HG13 1 
ATOM   5432 H  HG21 . VAL   B 1 95  ? 39.963 -18.359 -0.981  1.00 11.94 ?  95   VAL   B HG21 1 
ATOM   5433 H  HG22 . VAL   B 1 95  ? 40.120 -17.148 0.035   1.00 11.94 ?  95   VAL   B HG22 1 
ATOM   5434 H  HG23 . VAL   B 1 95  ? 41.404 -17.773 -0.661  1.00 11.94 ?  95   VAL   B HG23 1 
ATOM   5435 N  N    . VAL   B 1 96  ? 40.933 -19.211 4.180   1.00 10.34 ?  96   VAL   B N    1 
ATOM   5436 C  CA   . VAL   B 1 96  ? 41.014 -20.130 5.313   1.00 10.53 ?  96   VAL   B CA   1 
ATOM   5437 C  C    . VAL   B 1 96  ? 39.825 -21.089 5.262   1.00 10.94 ?  96   VAL   B C    1 
ATOM   5438 O  O    . VAL   B 1 96  ? 38.704 -20.728 5.635   1.00 11.61 ?  96   VAL   B O    1 
ATOM   5439 C  CB   . VAL   B 1 96  ? 41.069 -19.385 6.650   1.00 11.33 ?  96   VAL   B CB   1 
ATOM   5440 C  CG1  . VAL   B 1 96  ? 41.230 -20.379 7.788   1.00 11.94 ?  96   VAL   B CG1  1 
ATOM   5441 C  CG2  . VAL   B 1 96  ? 42.199 -18.361 6.665   1.00 12.22 ?  96   VAL   B CG2  1 
ATOM   5442 H  H    . VAL   B 1 96  ? 40.369 -18.569 4.297   1.00 12.43 ?  96   VAL   B H    1 
ATOM   5443 H  HA   . VAL   B 1 96  ? 41.828 -20.654 5.234   1.00 12.66 ?  96   VAL   B HA   1 
ATOM   5444 H  HB   . VAL   B 1 96  ? 40.234 -18.914 6.784   1.00 13.62 ?  96   VAL   B HB   1 
ATOM   5445 H  HG11 . VAL   B 1 96  ? 41.427 -19.895 8.608   1.00 14.35 ?  96   VAL   B HG11 1 
ATOM   5446 H  HG12 . VAL   B 1 96  ? 40.405 -20.880 7.897   1.00 14.35 ?  96   VAL   B HG12 1 
ATOM   5447 H  HG13 . VAL   B 1 96  ? 41.960 -20.985 7.584   1.00 14.35 ?  96   VAL   B HG13 1 
ATOM   5448 H  HG21 . VAL   B 1 96  ? 42.246 -17.952 7.547   1.00 14.69 ?  96   VAL   B HG21 1 
ATOM   5449 H  HG22 . VAL   B 1 96  ? 43.037 -18.805 6.465   1.00 14.69 ?  96   VAL   B HG22 1 
ATOM   5450 H  HG23 . VAL   B 1 96  ? 42.018 -17.679 5.998   1.00 14.69 ?  96   VAL   B HG23 1 
ATOM   5451 N  N    . GLY   B 1 97  ? 40.060 -22.326 4.827   1.00 11.06 ?  97   GLY   B N    1 
ATOM   5452 C  CA   . GLY   B 1 97  ? 39.081 -23.376 4.992   1.00 11.38 ?  97   GLY   B CA   1 
ATOM   5453 C  C    . GLY   B 1 97  ? 39.207 -23.988 6.370   1.00 12.31 ?  97   GLY   B C    1 
ATOM   5454 O  O    . GLY   B 1 97  ? 40.249 -23.873 7.025   1.00 12.76 ?  97   GLY   B O    1 
ATOM   5455 H  H    . GLY   B 1 97  ? 40.787 -22.570 4.429   1.00 13.30 ?  97   GLY   B H    1 
ATOM   5456 H  HA2  . GLY   B 1 97  ? 38.191 -23.006 4.878   1.00 13.68 ?  97   GLY   B HA2  1 
ATOM   5457 H  HA3  . GLY   B 1 97  ? 39.222 -24.063 4.319   1.00 13.68 ?  97   GLY   B HA3  1 
ATOM   5458 N  N    . PRO   B 1 98  ? 38.156 -24.662 6.837   1.00 13.07 ?  98   PRO   B N    1 
ATOM   5459 C  CA   . PRO   B 1 98  ? 38.244 -25.355 8.126   1.00 14.06 ?  98   PRO   B CA   1 
ATOM   5460 C  C    . PRO   B 1 98  ? 39.269 -26.478 8.080   1.00 13.50 ?  98   PRO   B C    1 
ATOM   5461 O  O    . PRO   B 1 98  ? 39.372 -27.212 7.098   1.00 13.81 ?  98   PRO   B O    1 
ATOM   5462 C  CB   . PRO   B 1 98  ? 36.826 -25.901 8.325   1.00 14.70 ?  98   PRO   B CB   1 
ATOM   5463 C  CG   . PRO   B 1 98  ? 36.275 -26.030 6.954   1.00 14.35 ?  98   PRO   B CG   1 
ATOM   5464 C  CD   . PRO   B 1 98  ? 36.842 -24.859 6.200   1.00 13.33 ?  98   PRO   B CD   1 
ATOM   5465 H  HA   . PRO   B 1 98  ? 38.464 -24.732 8.834   1.00 16.90 ?  98   PRO   B HA   1 
ATOM   5466 H  HB2  . PRO   B 1 98  ? 36.869 -26.767 8.760   1.00 17.66 ?  98   PRO   B HB2  1 
ATOM   5467 H  HB3  . PRO   B 1 98  ? 36.303 -25.276 8.847   1.00 17.66 ?  98   PRO   B HB3  1 
ATOM   5468 H  HG2  . PRO   B 1 98  ? 36.571 -26.867 6.559   1.00 17.24 ?  98   PRO   B HG2  1 
ATOM   5469 H  HG3  . PRO   B 1 98  ? 35.310 -25.984 6.982   1.00 17.24 ?  98   PRO   B HG3  1 
ATOM   5470 H  HD2  . PRO   B 1 98  ? 36.948 -25.077 5.256   1.00 16.02 ?  98   PRO   B HD2  1 
ATOM   5471 H  HD3  . PRO   B 1 98  ? 36.289 -24.071 6.320   1.00 16.02 ?  98   PRO   B HD3  1 
ATOM   5472 N  N    . ASN   B 1 99  ? 40.013 -26.616 9.168   1.00 14.57 ?  99   ASN   B N    1 
ATOM   5473 C  CA   . ASN   B 1 99  ? 40.982 -27.695 9.330   1.00 15.24 ?  99   ASN   B CA   1 
ATOM   5474 C  C    . ASN   B 1 99  ? 40.343 -28.777 10.199  1.00 17.16 ?  99   ASN   B C    1 
ATOM   5475 O  O    . ASN   B 1 99  ? 40.252 -28.635 11.420  1.00 18.06 ?  99   ASN   B O    1 
ATOM   5476 C  CB   . ASN   B 1 99  ? 42.260 -27.139 9.946   1.00 15.71 ?  99   ASN   B CB   1 
ATOM   5477 C  CG   . ASN   B 1 99  ? 43.392 -28.143 9.943   1.00 16.74 ?  99   ASN   B CG   1 
ATOM   5478 O  OD1  . ASN   B 1 99  ? 43.170 -29.334 10.120  1.00 17.40 ?  99   ASN   B OD1  1 
ATOM   5479 N  ND2  . ASN   B 1 99  ? 44.612 -27.668 9.738   1.00 17.05 ?  99   ASN   B ND2  1 
ATOM   5480 H  H    . ASN   B 1 99  ? 39.974 -26.084 9.842   1.00 17.51 ?  99   ASN   B H    1 
ATOM   5481 H  HA   . ASN   B 1 99  ? 41.195 -28.078 8.464   1.00 18.31 ?  99   ASN   B HA   1 
ATOM   5482 H  HB2  . ASN   B 1 99  ? 42.544 -26.367 9.446   1.00 18.88 ?  99   ASN   B HB2  1 
ATOM   5483 H  HB3  . ASN   B 1 99  ? 42.079 -26.895 10.870  1.00 18.88 ?  99   ASN   B HB3  1 
ATOM   5484 H  HD21 . ASN   B 1 99  ? 45.286 -28.202 9.725   1.00 20.48 ?  99   ASN   B HD21 1 
ATOM   5485 H  HD22 . ASN   B 1 99  ? 44.725 -26.826 9.620   1.00 20.48 ?  99   ASN   B HD22 1 
ATOM   5486 N  N    A VAL   B 1 100 ? 39.887 -29.857 9.558   0.30 19.38 ?  100  VAL   B N    1 
ATOM   5487 N  N    B VAL   B 1 100 ? 39.894 -29.857 9.553   0.70 19.25 ?  100  VAL   B N    1 
ATOM   5488 C  CA   A VAL   B 1 100 ? 39.275 -30.959 10.298  0.30 21.67 ?  100  VAL   B CA   1 
ATOM   5489 C  CA   B VAL   B 1 100 ? 39.277 -30.969 10.273  0.70 21.75 ?  100  VAL   B CA   1 
ATOM   5490 C  C    A VAL   B 1 100 ? 40.283 -31.614 11.232  0.30 22.19 ?  100  VAL   B C    1 
ATOM   5491 C  C    B VAL   B 1 100 ? 40.275 -31.642 11.208  0.70 21.88 ?  100  VAL   B C    1 
ATOM   5492 O  O    A VAL   B 1 100 ? 39.917 -32.099 12.310  0.30 22.67 ?  100  VAL   B O    1 
ATOM   5493 O  O    B VAL   B 1 100 ? 39.892 -32.179 12.254  0.70 22.68 ?  100  VAL   B O    1 
ATOM   5494 C  CB   A VAL   B 1 100 ? 38.631 -31.972 9.330   0.30 23.53 ?  100  VAL   B CB   1 
ATOM   5495 C  CB   B VAL   B 1 100 ? 38.658 -31.967 9.274   0.70 24.48 ?  100  VAL   B CB   1 
ATOM   5496 C  CG1  A VAL   B 1 100 ? 38.145 -33.205 10.082  0.30 24.20 ?  100  VAL   B CG1  1 
ATOM   5497 C  CG1  B VAL   B 1 100 ? 38.194 -33.228 9.987   0.70 25.57 ?  100  VAL   B CG1  1 
ATOM   5498 C  CG2  A VAL   B 1 100 ? 37.481 -31.324 8.577   0.30 24.15 ?  100  VAL   B CG2  1 
ATOM   5499 C  CG2  B VAL   B 1 100 ? 37.502 -31.317 8.530   0.70 25.25 ?  100  VAL   B CG2  1 
ATOM   5500 H  H    A VAL   B 1 100 ? 39.914 -29.969 8.705   0.30 23.28 ?  100  VAL   B H    1 
ATOM   5501 H  H    B VAL   B 1 100 ? 39.927 -29.962 8.699   0.70 23.12 ?  100  VAL   B H    1 
ATOM   5502 H  HA   A VAL   B 1 100 ? 38.562 -30.597 10.847  0.30 26.03 ?  100  VAL   B HA   1 
ATOM   5503 H  HA   B VAL   B 1 100 ? 38.553 -30.618 10.816  0.70 26.12 ?  100  VAL   B HA   1 
ATOM   5504 H  HB   A VAL   B 1 100 ? 39.292 -32.260 8.684   0.30 28.27 ?  100  VAL   B HB   1 
ATOM   5505 H  HB   B VAL   B 1 100 ? 39.330 -32.224 8.625   0.70 29.40 ?  100  VAL   B HB   1 
ATOM   5506 H  HG11 A VAL   B 1 100 ? 37.559 -33.717 9.500   0.30 29.07 ?  100  VAL   B HG11 1 
ATOM   5507 H  HG11 B VAL   B 1 100 ? 37.614 -33.730 9.391   0.70 30.71 ?  100  VAL   B HG11 1 
ATOM   5508 H  HG12 A VAL   B 1 100 ? 38.908 -33.747 10.336  0.30 29.07 ?  100  VAL   B HG12 1 
ATOM   5509 H  HG12 B VAL   B 1 100 ? 38.966 -33.767 10.223  0.70 30.71 ?  100  VAL   B HG12 1 
ATOM   5510 H  HG13 A VAL   B 1 100 ? 37.658 -32.924 10.872  0.30 29.07 ?  100  VAL   B HG13 1 
ATOM   5511 H  HG13 B VAL   B 1 100 ? 37.705 -32.979 10.787  0.70 30.71 ?  100  VAL   B HG13 1 
ATOM   5512 H  HG21 A VAL   B 1 100 ? 37.081 -31.981 7.987   0.30 29.00 ?  100  VAL   B HG21 1 
ATOM   5513 H  HG21 B VAL   B 1 100 ? 37.117 -31.966 7.920   0.70 30.32 ?  100  VAL   B HG21 1 
ATOM   5514 H  HG22 A VAL   B 1 100 ? 36.822 -31.010 9.217   0.30 29.00 ?  100  VAL   B HG22 1 
ATOM   5515 H  HG22 B VAL   B 1 100 ? 36.834 -31.032 9.173   0.70 30.32 ?  100  VAL   B HG22 1 
ATOM   5516 H  HG23 A VAL   B 1 100 ? 37.824 -30.580 8.061   0.30 29.00 ?  100  VAL   B HG23 1 
ATOM   5517 H  HG23 B VAL   B 1 100 ? 37.836 -30.555 8.036   0.70 30.32 ?  100  VAL   B HG23 1 
ATOM   5518 N  N    . ASN   B 1 101 ? 41.560 -31.648 10.842  1.00 22.59 ?  101  ASN   B N    1 
ATOM   5519 C  CA   . ASN   B 1 101 ? 42.589 -32.181 11.734  1.00 25.10 ?  101  ASN   B CA   1 
ATOM   5520 C  C    . ASN   B 1 101 ? 42.740 -31.346 13.002  1.00 28.03 ?  101  ASN   B C    1 
ATOM   5521 O  O    . ASN   B 1 101 ? 43.327 -31.827 13.980  1.00 28.90 ?  101  ASN   B O    1 
ATOM   5522 C  CB   . ASN   B 1 101 ? 43.927 -32.312 11.000  1.00 25.06 ?  101  ASN   B CB   1 
ATOM   5523 C  CG   . ASN   B 1 101 ? 43.924 -33.444 9.986   1.00 24.42 ?  101  ASN   B CG   1 
ATOM   5524 O  OD1  . ASN   B 1 101 ? 43.237 -34.447 10.168  1.00 25.29 ?  101  ASN   B OD1  1 
ATOM   5525 N  ND2  . ASN   B 1 101 ? 44.687 -33.283 8.911   1.00 23.95 ?  101  ASN   B ND2  1 
ATOM   5526 H  H    A ASN   B 1 101 ? 41.847 -31.380 10.076  0.30 27.13 ?  101  ASN   B H    1 
ATOM   5527 H  H    B ASN   B 1 101 ? 41.854 -31.363 10.085  0.70 27.13 ?  101  ASN   B H    1 
ATOM   5528 H  HA   . ASN   B 1 101 ? 42.324 -33.065 12.010  1.00 30.15 ?  101  ASN   B HA   1 
ATOM   5529 H  HB2  . ASN   B 1 101 ? 44.121 -31.488 10.526  1.00 30.09 ?  101  ASN   B HB2  1 
ATOM   5530 H  HB3  . ASN   B 1 101 ? 44.628 -32.493 11.647  1.00 30.09 ?  101  ASN   B HB3  1 
ATOM   5531 H  HD21 . ASN   B 1 101 ? 44.719 -33.898 8.310   1.00 28.77 ?  101  ASN   B HD21 1 
ATOM   5532 H  HD22 . ASN   B 1 101 ? 45.155 -32.567 8.817   1.00 28.77 ?  101  ASN   B HD22 1 
ATOM   5533 N  N    A LYS   B 1 102 ? 42.224 -30.116 13.005  0.30 29.95 ?  102  LYS   B N    1 
ATOM   5534 N  N    B LYS   B 1 102 ? 42.228 -30.114 13.006  0.70 29.60 ?  102  LYS   B N    1 
ATOM   5535 C  CA   A LYS   B 1 102 ? 42.198 -29.265 14.188  0.30 31.76 ?  102  LYS   B CA   1 
ATOM   5536 C  CA   B LYS   B 1 102 ? 42.199 -29.268 14.192  0.70 31.60 ?  102  LYS   B CA   1 
ATOM   5537 C  C    A LYS   B 1 102 ? 40.830 -29.247 14.859  0.30 31.14 ?  102  LYS   B C    1 
ATOM   5538 C  C    B LYS   B 1 102 ? 40.820 -29.225 14.839  0.70 30.87 ?  102  LYS   B C    1 
ATOM   5539 O  O    A LYS   B 1 102 ? 40.630 -28.490 15.815  0.30 31.57 ?  102  LYS   B O    1 
ATOM   5540 O  O    B LYS   B 1 102 ? 40.599 -28.418 15.747  0.70 31.51 ?  102  LYS   B O    1 
ATOM   5541 C  CB   A LYS   B 1 102 ? 42.603 -27.833 13.826  0.30 34.19 ?  102  LYS   B CB   1 
ATOM   5542 C  CB   B LYS   B 1 102 ? 42.629 -27.842 13.845  0.70 34.48 ?  102  LYS   B CB   1 
ATOM   5543 C  CG   A LYS   B 1 102 ? 44.065 -27.647 13.456  0.30 36.25 ?  102  LYS   B CG   1 
ATOM   5544 C  CG   B LYS   B 1 102 ? 44.089 -27.680 13.468  0.70 37.09 ?  102  LYS   B CG   1 
ATOM   5545 C  CD   A LYS   B 1 102 ? 44.340 -26.186 13.120  0.30 38.13 ?  102  LYS   B CD   1 
ATOM   5546 C  CD   B LYS   B 1 102 ? 44.360 -26.250 13.030  0.70 39.68 ?  102  LYS   B CD   1 
ATOM   5547 C  CE   A LYS   B 1 102 ? 45.805 -25.935 12.803  0.30 39.47 ?  102  LYS   B CE   1 
ATOM   5548 C  CE   B LYS   B 1 102 ? 45.839 -25.994 12.808  0.70 41.62 ?  102  LYS   B CE   1 
ATOM   5549 N  NZ   A LYS   B 1 102 ? 46.055 -24.508 12.442  0.30 40.17 ?  102  LYS   B NZ   1 
ATOM   5550 N  NZ   B LYS   B 1 102 ? 46.077 -24.597 12.343  0.70 42.68 ?  102  LYS   B NZ   1 
ATOM   5551 H  H    A LYS   B 1 102 ? 41.868 -29.743 12.315  0.30 35.96 ?  102  LYS   B H    1 
ATOM   5552 H  H    B LYS   B 1 102 ? 41.878 -29.738 12.315  0.70 35.54 ?  102  LYS   B H    1 
ATOM   5553 H  HA   A LYS   B 1 102 ? 42.840 -29.599 14.831  0.30 38.14 ?  102  LYS   B HA   1 
ATOM   5554 H  HA   B LYS   B 1 102 ? 42.832 -29.614 14.840  0.70 37.94 ?  102  LYS   B HA   1 
ATOM   5555 H  HB2  A LYS   B 1 102 ? 42.072 -27.543 13.068  0.30 41.05 ?  102  LYS   B HB2  1 
ATOM   5556 H  HB2  B LYS   B 1 102 ? 42.098 -27.532 13.096  0.70 41.40 ?  102  LYS   B HB2  1 
ATOM   5557 H  HB3  A LYS   B 1 102 ? 42.422 -27.259 14.587  0.30 41.05 ?  102  LYS   B HB3  1 
ATOM   5558 H  HB3  B LYS   B 1 102 ? 42.464 -27.273 14.615  0.70 41.40 ?  102  LYS   B HB3  1 
ATOM   5559 H  HG2  A LYS   B 1 102 ? 44.626 -27.901 14.207  0.30 43.53 ?  102  LYS   B HG2  1 
ATOM   5560 H  HG2  B LYS   B 1 102 ? 44.648 -27.876 14.236  0.70 44.53 ?  102  LYS   B HG2  1 
ATOM   5561 H  HG3  A LYS   B 1 102 ? 44.275 -28.187 12.678  0.30 43.53 ?  102  LYS   B HG3  1 
ATOM   5562 H  HG3  B LYS   B 1 102 ? 44.302 -28.273 12.731  0.70 44.53 ?  102  LYS   B HG3  1 
ATOM   5563 H  HD2  A LYS   B 1 102 ? 43.815 -25.935 12.343  0.30 45.78 ?  102  LYS   B HD2  1 
ATOM   5564 H  HD2  B LYS   B 1 102 ? 43.896 -26.079 12.195  0.70 47.64 ?  102  LYS   B HD2  1 
ATOM   5565 H  HD3  A LYS   B 1 102 ? 44.095 -25.634 13.880  0.30 45.78 ?  102  LYS   B HD3  1 
ATOM   5566 H  HD3  B LYS   B 1 102 ? 44.047 -25.640 13.716  0.70 47.64 ?  102  LYS   B HD3  1 
ATOM   5567 H  HE2  A LYS   B 1 102 ? 46.342 -26.148 13.582  0.30 47.39 ?  102  LYS   B HE2  1 
ATOM   5568 H  HE2  B LYS   B 1 102 ? 46.316 -26.123 13.643  0.70 49.97 ?  102  LYS   B HE2  1 
ATOM   5569 H  HE3  A LYS   B 1 102 ? 46.069 -26.488 12.052  0.30 47.39 ?  102  LYS   B HE3  1 
ATOM   5570 H  HE3  B LYS   B 1 102 ? 46.173 -26.603 12.131  0.70 49.97 ?  102  LYS   B HE3  1 
ATOM   5571 H  HZ1  A LYS   B 1 102 ? 46.918 -24.387 12.261  0.30 48.22 ?  102  LYS   B HZ1  1 
ATOM   5572 H  HZ1  B LYS   B 1 102 ? 46.947 -24.463 12.218  0.70 51.24 ?  102  LYS   B HZ1  1 
ATOM   5573 H  HZ2  A LYS   B 1 102 ? 45.576 -24.287 11.725  0.30 48.22 ?  102  LYS   B HZ2  1 
ATOM   5574 H  HZ2  B LYS   B 1 102 ? 45.648 -24.456 11.576  0.70 51.24 ?  102  LYS   B HZ2  1 
ATOM   5575 H  HZ3  A LYS   B 1 102 ? 45.824 -23.978 13.119  0.30 48.22 ?  102  LYS   B HZ3  1 
ATOM   5576 H  HZ3  B LYS   B 1 102 ? 45.778 -24.020 12.951  0.70 51.24 ?  102  LYS   B HZ3  1 
ATOM   5577 N  N    . GLY   B 1 103 ? 39.883 -30.049 14.376  1.00 30.08 ?  103  GLY   B N    1 
ATOM   5578 C  CA   . GLY   B 1 103 ? 38.552 -30.082 14.948  1.00 29.24 ?  103  GLY   B CA   1 
ATOM   5579 C  C    . GLY   B 1 103 ? 37.622 -28.986 14.481  1.00 27.69 ?  103  GLY   B C    1 
ATOM   5580 O  O    . GLY   B 1 103 ? 36.532 -28.838 15.047  1.00 28.29 ?  103  GLY   B O    1 
ATOM   5581 H  H    A GLY   B 1 103 ? 39.993 -30.586 13.715  0.30 36.12 ?  103  GLY   B H    1 
ATOM   5582 H  H    B GLY   B 1 103 ? 39.995 -30.592 13.721  0.70 36.12 ?  103  GLY   B H    1 
ATOM   5583 H  HA2  . GLY   B 1 103 ? 38.142 -30.934 14.733  1.00 35.11 ?  103  GLY   B HA2  1 
ATOM   5584 H  HA3  . GLY   B 1 103 ? 38.624 -30.020 15.913  1.00 35.11 ?  103  GLY   B HA3  1 
ATOM   5585 N  N    A GLU   B 1 104 ? 38.024 -28.199 13.487  0.30 27.67 ?  104  GLU   B N    1 
ATOM   5586 N  N    B GLU   B 1 104 ? 37.996 -28.229 13.454  0.70 25.64 ?  104  GLU   B N    1 
ATOM   5587 C  CA   A GLU   B 1 104 ? 37.201 -27.092 13.027  0.30 27.30 ?  104  GLU   B CA   1 
ATOM   5588 C  CA   B GLU   B 1 104 ? 37.151 -27.146 12.974  0.70 23.53 ?  104  GLU   B CA   1 
ATOM   5589 C  C    A GLU   B 1 104 ? 36.021 -27.608 12.208  0.30 27.75 ?  104  GLU   B C    1 
ATOM   5590 C  C    B GLU   B 1 104 ? 35.986 -27.691 12.150  0.70 24.52 ?  104  GLU   B C    1 
ATOM   5591 O  O    A GLU   B 1 104 ? 36.074 -28.683 11.603  0.30 28.06 ?  104  GLU   B O    1 
ATOM   5592 O  O    B GLU   B 1 104 ? 36.060 -28.776 11.566  0.70 25.68 ?  104  GLU   B O    1 
ATOM   5593 C  CB   A GLU   B 1 104 ? 38.049 -26.113 12.215  0.30 26.68 ?  104  GLU   B CB   1 
ATOM   5594 C  CB   B GLU   B 1 104 ? 37.991 -26.141 12.184  0.70 21.87 ?  104  GLU   B CB   1 
ATOM   5595 C  CG   A GLU   B 1 104 ? 39.166 -25.476 13.037  0.30 26.15 ?  104  GLU   B CG   1 
ATOM   5596 C  CG   B GLU   B 1 104 ? 39.067 -25.505 13.056  0.70 20.49 ?  104  GLU   B CG   1 
ATOM   5597 C  CD   A GLU   B 1 104 ? 40.075 -24.581 12.219  0.30 25.88 ?  104  GLU   B CD   1 
ATOM   5598 C  CD   B GLU   B 1 104 ? 40.054 -24.640 12.302  0.70 19.45 ?  104  GLU   B CD   1 
ATOM   5599 O  OE1  A GLU   B 1 104 ? 40.030 -24.652 10.973  0.30 25.49 ?  104  GLU   B OE1  1 
ATOM   5600 O  OE1  B GLU   B 1 104 ? 40.094 -24.666 11.053  0.70 17.89 ?  104  GLU   B OE1  1 
ATOM   5601 O  OE2  A GLU   B 1 104 ? 40.840 -23.804 12.828  0.30 26.18 -1 104  GLU   B OE2  1 
ATOM   5602 O  OE2  B GLU   B 1 104 ? 40.807 -23.924 12.990  0.70 20.13 -1 104  GLU   B OE2  1 
ATOM   5603 H  H    A GLU   B 1 104 ? 38.772 -28.282 13.071  0.30 33.23 ?  104  GLU   B H    1 
ATOM   5604 H  H    B GLU   B 1 104 ? 38.737 -28.317 13.026  0.70 30.79 ?  104  GLU   B H    1 
ATOM   5605 H  HA   A GLU   B 1 104 ? 36.851 -26.616 13.795  0.30 32.78 ?  104  GLU   B HA   1 
ATOM   5606 H  HA   B GLU   B 1 104 ? 36.781 -26.679 13.738  0.70 28.26 ?  104  GLU   B HA   1 
ATOM   5607 H  HB2  A GLU   B 1 104 ? 38.459 -26.583 11.472  0.30 32.04 ?  104  GLU   B HB2  1 
ATOM   5608 H  HB2  B GLU   B 1 104 ? 38.428 -26.593 11.447  0.70 26.26 ?  104  GLU   B HB2  1 
ATOM   5609 H  HB3  A GLU   B 1 104 ? 37.482 -25.399 11.882  0.30 32.04 ?  104  GLU   B HB3  1 
ATOM   5610 H  HB3  B GLU   B 1 104 ? 37.416 -25.433 11.852  0.70 26.26 ?  104  GLU   B HB3  1 
ATOM   5611 H  HG2  A GLU   B 1 104 ? 38.773 -24.937 13.742  0.30 31.40 ?  104  GLU   B HG2  1 
ATOM   5612 H  HG2  B GLU   B 1 104 ? 38.643 -24.944 13.726  0.70 24.61 ?  104  GLU   B HG2  1 
ATOM   5613 H  HG3  A GLU   B 1 104 ? 39.713 -26.177 13.427  0.30 31.40 ?  104  GLU   B HG3  1 
ATOM   5614 H  HG3  B GLU   B 1 104 ? 39.578 -26.203 13.493  0.70 24.61 ?  104  GLU   B HG3  1 
ATOM   5615 N  N    A ASP   B 1 105 ? 34.944 -26.827 12.201  0.30 27.88 ?  105  ASP   B N    1 
ATOM   5616 N  N    B ASP   B 1 105 ? 34.897 -26.924 12.122  0.70 24.46 ?  105  ASP   B N    1 
ATOM   5617 C  CA   A ASP   B 1 105 ? 33.677 -27.281 11.642  0.30 28.25 ?  105  ASP   B CA   1 
ATOM   5618 C  CA   B ASP   B 1 105 ? 33.627 -27.398 11.584  0.70 25.10 ?  105  ASP   B CA   1 
ATOM   5619 C  C    A ASP   B 1 105 ? 33.757 -27.341 10.121  0.30 27.16 ?  105  ASP   B C    1 
ATOM   5620 C  C    B ASP   B 1 105 ? 33.671 -27.419 10.061  0.70 23.21 ?  105  ASP   B C    1 
ATOM   5621 O  O    A ASP   B 1 105 ? 33.977 -26.320 9.460   0.30 26.84 ?  105  ASP   B O    1 
ATOM   5622 O  O    B ASP   B 1 105 ? 33.813 -26.371 9.421   0.70 22.24 ?  105  ASP   B O    1 
ATOM   5623 C  CB   A ASP   B 1 105 ? 32.560 -26.338 12.081  0.30 29.63 ?  105  ASP   B CB   1 
ATOM   5624 C  CB   B ASP   B 1 105 ? 32.491 -26.501 12.073  0.70 28.06 ?  105  ASP   B CB   1 
ATOM   5625 C  CG   A ASP   B 1 105 ? 31.185 -26.827 11.670  0.30 30.92 ?  105  ASP   B CG   1 
ATOM   5626 C  CG   B ASP   B 1 105 ? 31.116 -27.059 11.737  0.70 30.58 ?  105  ASP   B CG   1 
ATOM   5627 O  OD1  A ASP   B 1 105 ? 31.084 -27.951 11.134  0.30 31.27 ?  105  ASP   B OD1  1 
ATOM   5628 O  OD1  B ASP   B 1 105 ? 31.035 -28.053 10.984  0.70 30.91 ?  105  ASP   B OD1  1 
ATOM   5629 O  OD2  A ASP   B 1 105 ? 30.204 -26.082 11.878  0.30 31.47 -1 105  ASP   B OD2  1 
ATOM   5630 O  OD2  B ASP   B 1 105 ? 30.111 -26.511 12.239  0.70 31.90 -1 105  ASP   B OD2  1 
ATOM   5631 H  H    A ASP   B 1 105 ? 34.925 -26.026 12.515  0.30 33.48 ?  105  ASP   B H    1 
ATOM   5632 H  H    B ASP   B 1 105 ? 34.875 -26.114 12.408  0.70 29.38 ?  105  ASP   B H    1 
ATOM   5633 H  HA   A ASP   B 1 105 ? 33.479 -28.171 11.975  0.30 33.93 ?  105  ASP   B HA   1 
ATOM   5634 H  HA   B ASP   B 1 105 ? 33.461 -28.299 11.896  0.70 30.14 ?  105  ASP   B HA   1 
ATOM   5635 H  HB2  A ASP   B 1 105 ? 32.583 -26.250 13.049  0.30 35.58 ?  105  ASP   B HB2  1 
ATOM   5636 H  HB2  B ASP   B 1 105 ? 32.554 -26.411 13.037  0.70 33.70 ?  105  ASP   B HB2  1 
ATOM   5637 H  HB3  A ASP   B 1 105 ? 32.694 -25.473 11.667  0.30 35.58 ?  105  ASP   B HB3  1 
ATOM   5638 H  HB3  B ASP   B 1 105 ? 32.579 -25.626 11.656  0.70 33.70 ?  105  ASP   B HB3  1 
ATOM   5639 N  N    A ILE   B 1 106 ? 33.567 -28.542 9.567   0.30 26.49 ?  106  ILE   B N    1 
ATOM   5640 N  N    B ILE   B 1 106 ? 33.527 -28.616 9.483   0.70 23.15 ?  106  ILE   B N    1 
ATOM   5641 C  CA   A ILE   B 1 106 ? 33.580 -28.731 8.121   0.30 25.79 ?  106  ILE   B CA   1 
ATOM   5642 C  CA   B ILE   B 1 106 ? 33.520 -28.773 8.032   0.70 22.50 ?  106  ILE   B CA   1 
ATOM   5643 C  C    A ILE   B 1 106 ? 32.486 -27.924 7.434   0.30 25.11 ?  106  ILE   B C    1 
ATOM   5644 C  C    B ILE   B 1 106 ? 32.429 -27.931 7.379   0.70 21.38 ?  106  ILE   B C    1 
ATOM   5645 O  O    A ILE   B 1 106 ? 32.588 -27.638 6.236   0.30 25.00 ?  106  ILE   B O    1 
ATOM   5646 O  O    B ILE   B 1 106 ? 32.531 -27.595 6.195   0.70 20.60 ?  106  ILE   B O    1 
ATOM   5647 C  CB   A ILE   B 1 106 ? 33.474 -30.238 7.792   0.30 25.85 ?  106  ILE   B CB   1 
ATOM   5648 C  CB   B ILE   B 1 106 ? 33.397 -30.273 7.675   0.70 23.33 ?  106  ILE   B CB   1 
ATOM   5649 C  CG1  A ILE   B 1 106 ? 33.715 -30.492 6.301   0.30 25.67 ?  106  ILE   B CG1  1 
ATOM   5650 C  CG1  B ILE   B 1 106 ? 33.707 -30.511 6.196   0.70 23.75 ?  106  ILE   B CG1  1 
ATOM   5651 C  CG2  A ILE   B 1 106 ? 32.114 -30.783 8.209   0.30 26.18 ?  106  ILE   B CG2  1 
ATOM   5652 C  CG2  B ILE   B 1 106 ? 32.005 -30.796 8.015   0.70 24.29 ?  106  ILE   B CG2  1 
ATOM   5653 C  CD1  A ILE   B 1 106 ? 35.071 -30.027 5.816   0.30 25.50 ?  106  ILE   B CD1  1 
ATOM   5654 C  CD1  B ILE   B 1 106 ? 35.084 -30.043 5.785   0.70 23.84 ?  106  ILE   B CD1  1 
ATOM   5655 H  H    A ILE   B 1 106 ? 33.438 -29.263 10.012  0.30 31.81 ?  106  ILE   B H    1 
ATOM   5656 H  H    B ILE   B 1 106 ? 33.442 -29.350 9.915   0.70 27.81 ?  106  ILE   B H    1 
ATOM   5657 H  HA   A ILE   B 1 106 ? 34.430 -28.414 7.784   0.30 30.97 ?  106  ILE   B HA   1 
ATOM   5658 H  HA   B ILE   B 1 106 ? 34.368 -28.458 7.693   0.70 27.02 ?  106  ILE   B HA   1 
ATOM   5659 H  HB   A ILE   B 1 106 ? 34.156 -30.709 8.294   0.30 31.04 ?  106  ILE   B HB   1 
ATOM   5660 H  HB   B ILE   B 1 106 ? 34.043 -30.770 8.205   0.70 28.02 ?  106  ILE   B HB   1 
ATOM   5661 H  HG12 A ILE   B 1 106 ? 33.656 -31.448 6.135   0.30 30.83 ?  106  ILE   B HG12 1 
ATOM   5662 H  HG12 B ILE   B 1 106 ? 33.654 -31.465 6.013   0.70 28.53 ?  106  ILE   B HG12 1 
ATOM   5663 H  HG13 A ILE   B 1 106 ? 33.039 -30.028 5.786   0.30 30.83 ?  106  ILE   B HG13 1 
ATOM   5664 H  HG13 B ILE   B 1 106 ? 33.057 -30.038 5.657   0.70 28.53 ?  106  ILE   B HG13 1 
ATOM   5665 H  HG21 A ILE   B 1 106 ? 32.122 -31.749 8.121   0.30 31.44 ?  106  ILE   B HG21 1 
ATOM   5666 H  HG21 B ILE   B 1 106 ? 32.011 -31.765 7.970   0.70 29.17 ?  106  ILE   B HG21 1 
ATOM   5667 H  HG22 A ILE   B 1 106 ? 31.945 -30.537 9.132   0.30 31.44 ?  106  ILE   B HG22 1 
ATOM   5668 H  HG22 B ILE   B 1 106 ? 31.773 -30.508 8.911   0.70 29.17 ?  106  ILE   B HG22 1 
ATOM   5669 H  HG23 A ILE   B 1 106 ? 31.430 -30.405 7.635   0.30 31.44 ?  106  ILE   B HG23 1 
ATOM   5670 H  HG23 B ILE   B 1 106 ? 31.369 -30.439 7.377   0.70 29.17 ?  106  ILE   B HG23 1 
ATOM   5671 H  HD11 A ILE   B 1 106 ? 35.251 -30.429 4.953   0.30 30.62 ?  106  ILE   B HD11 1 
ATOM   5672 H  HD11 B ILE   B 1 106 ? 35.328 -30.471 4.951   0.70 28.64 ?  106  ILE   B HD11 1 
ATOM   5673 H  HD12 A ILE   B 1 106 ? 35.064 -29.061 5.735   0.30 30.62 ?  106  ILE   B HD12 1 
ATOM   5674 H  HD12 B ILE   B 1 106 ? 35.070 -29.079 5.669   0.70 28.64 ?  106  ILE   B HD12 1 
ATOM   5675 H  HD13 A ILE   B 1 106 ? 35.747 -30.302 6.456   0.30 30.62 ?  106  ILE   B HD13 1 
ATOM   5676 H  HD13 B ILE   B 1 106 ? 35.721 -30.284 6.478   0.70 28.64 ?  106  ILE   B HD13 1 
ATOM   5677 N  N    A GLN   B 1 107 ? 31.435 -27.544 8.165   0.30 24.96 ?  107  GLN   B N    1 
ATOM   5678 N  N    B GLN   B 1 107 ? 31.392 -27.560 8.129   0.70 22.25 ?  107  GLN   B N    1 
ATOM   5679 C  CA   A GLN   B 1 107 ? 30.355 -26.761 7.574   0.30 24.74 ?  107  GLN   B CA   1 
ATOM   5680 C  CA   B GLN   B 1 107 ? 30.320 -26.746 7.567   0.70 22.95 ?  107  GLN   B CA   1 
ATOM   5681 C  C    A GLN   B 1 107 ? 30.840 -25.414 7.056   0.30 22.06 ?  107  GLN   B C    1 
ATOM   5682 C  C    B GLN   B 1 107 ? 30.814 -25.389 7.078   0.70 20.98 ?  107  GLN   B C    1 
ATOM   5683 O  O    A GLN   B 1 107 ? 30.212 -24.845 6.157   0.30 22.36 ?  107  GLN   B O    1 
ATOM   5684 O  O    B GLN   B 1 107 ? 30.173 -24.793 6.208   0.70 21.94 ?  107  GLN   B O    1 
ATOM   5685 C  CB   A GLN   B 1 107 ? 29.241 -26.559 8.607   0.30 27.37 ?  107  GLN   B CB   1 
ATOM   5686 C  CB   B GLN   B 1 107 ? 29.211 -26.566 8.604   0.70 26.72 ?  107  GLN   B CB   1 
ATOM   5687 C  CG   A GLN   B 1 107 ? 27.924 -26.040 8.039   0.30 29.77 ?  107  GLN   B CG   1 
ATOM   5688 C  CG   B GLN   B 1 107 ? 27.867 -26.133 8.031   0.70 30.68 ?  107  GLN   B CG   1 
ATOM   5689 C  CD   A GLN   B 1 107 ? 27.878 -24.527 7.930   0.30 31.62 ?  107  GLN   B CD   1 
ATOM   5690 C  CD   B GLN   B 1 107 ? 27.730 -24.625 7.921   0.70 33.74 ?  107  GLN   B CD   1 
ATOM   5691 O  OE1  A GLN   B 1 107 ? 28.715 -23.824 8.500   0.30 32.34 ?  107  GLN   B OE1  1 
ATOM   5692 O  OE1  B GLN   B 1 107 ? 28.557 -23.872 8.438   0.70 34.96 ?  107  GLN   B OE1  1 
ATOM   5693 N  NE2  A GLN   B 1 107 ? 26.894 -24.016 7.197   0.30 32.26 ?  107  GLN   B NE2  1 
ATOM   5694 N  NE2  B GLN   B 1 107 ? 26.676 -24.176 7.247   0.70 34.77 ?  107  GLN   B NE2  1 
ATOM   5695 H  H    A GLN   B 1 107 ? 31.330 -27.721 8.998   0.30 29.98 ?  107  GLN   B H    1 
ATOM   5696 H  H    B GLN   B 1 107 ? 31.295 -27.752 8.953   0.70 26.73 ?  107  GLN   B H    1 
ATOM   5697 H  HA   A GLN   B 1 107 ? 29.980 -27.256 6.828   0.30 29.71 ?  107  GLN   B HA   1 
ATOM   5698 H  HA   B GLN   B 1 107 ? 29.942 -27.214 6.806   0.70 27.56 ?  107  GLN   B HA   1 
ATOM   5699 H  HB2  A GLN   B 1 107 ? 29.058 -27.410 9.030   0.30 32.87 ?  107  GLN   B HB2  1 
ATOM   5700 H  HB2  B GLN   B 1 107 ? 29.077 -27.411 9.054   0.70 32.09 ?  107  GLN   B HB2  1 
ATOM   5701 H  HB3  A GLN   B 1 107 ? 29.546 -25.923 9.272   0.30 32.87 ?  107  GLN   B HB3  1 
ATOM   5702 H  HB3  B GLN   B 1 107 ? 29.492 -25.895 9.244   0.70 32.09 ?  107  GLN   B HB3  1 
ATOM   5703 H  HG2  A GLN   B 1 107 ? 27.794 -26.406 7.151   0.30 35.75 ?  107  GLN   B HG2  1 
ATOM   5704 H  HG2  B GLN   B 1 107 ? 27.763 -26.508 7.143   0.70 36.84 ?  107  GLN   B HG2  1 
ATOM   5705 H  HG3  A GLN   B 1 107 ? 27.197 -26.323 8.620   0.30 35.75 ?  107  GLN   B HG3  1 
ATOM   5706 H  HG3  B GLN   B 1 107 ? 27.159 -26.460 8.611   0.70 36.84 ?  107  GLN   B HG3  1 
ATOM   5707 H  HE21 A GLN   B 1 107 ? 26.328 -24.538 6.812   0.30 38.73 ?  107  GLN   B HE21 1 
ATOM   5708 H  HE21 B GLN   B 1 107 ? 26.119 -24.731 6.897   0.70 41.75 ?  107  GLN   B HE21 1 
ATOM   5709 H  HE22 A GLN   B 1 107 ? 26.821 -23.164 7.107   0.30 38.73 ?  107  GLN   B HE22 1 
ATOM   5710 H  HE22 B GLN   B 1 107 ? 26.551 -23.330 7.160   0.70 41.75 ?  107  GLN   B HE22 1 
ATOM   5711 N  N    . LEU   B 1 108 ? 31.948 -24.897 7.593   1.00 19.53 ?  108  LEU   B N    1 
ATOM   5712 C  CA   . LEU   B 1 108 ? 32.500 -23.603 7.183   1.00 16.96 ?  108  LEU   B CA   1 
ATOM   5713 C  C    . LEU   B 1 108 ? 33.149 -23.631 5.808   1.00 15.28 ?  108  LEU   B C    1 
ATOM   5714 O  O    . LEU   B 1 108 ? 33.576 -22.578 5.316   1.00 14.73 ?  108  LEU   B O    1 
ATOM   5715 C  CB   . LEU   B 1 108 ? 33.512 -23.122 8.223   1.00 17.22 ?  108  LEU   B CB   1 
ATOM   5716 C  CG   . LEU   B 1 108 ? 32.899 -22.605 9.523   1.00 18.70 ?  108  LEU   B CG   1 
ATOM   5717 C  CD1  . LEU   B 1 108 ? 33.903 -22.630 10.661  1.00 18.79 ?  108  LEU   B CD1  1 
ATOM   5718 C  CD2  . LEU   B 1 108 ? 32.378 -21.192 9.313   1.00 19.72 ?  108  LEU   B CD2  1 
ATOM   5719 H  H    A LEU   B 1 108 ? 32.398 -25.284 8.212   0.30 23.46 ?  108  LEU   B H    1 
ATOM   5720 H  H    B LEU   B 1 108 ? 32.413 -25.301 8.190   0.70 23.46 ?  108  LEU   B H    1 
ATOM   5721 H  HA   . LEU   B 1 108 ? 31.779 -22.957 7.153   1.00 20.38 ?  108  LEU   B HA   1 
ATOM   5722 H  HB2  . LEU   B 1 108 ? 34.096 -23.861 8.453   1.00 20.69 ?  108  LEU   B HB2  1 
ATOM   5723 H  HB3  . LEU   B 1 108 ? 34.033 -22.401 7.839   1.00 20.69 ?  108  LEU   B HB3  1 
ATOM   5724 H  HG   . LEU   B 1 108 ? 32.147 -23.166 9.772   1.00 22.46 ?  108  LEU   B HG   1 
ATOM   5725 H  HD11 . LEU   B 1 108 ? 33.470 -22.319 11.474  1.00 22.57 ?  108  LEU   B HD11 1 
ATOM   5726 H  HD12 . LEU   B 1 108 ? 34.221 -23.537 10.783  1.00 22.57 ?  108  LEU   B HD12 1 
ATOM   5727 H  HD13 . LEU   B 1 108 ? 34.645 -22.044 10.441  1.00 22.57 ?  108  LEU   B HD13 1 
ATOM   5728 H  HD21 . LEU   B 1 108 ? 32.004 -20.863 10.146  1.00 23.69 ?  108  LEU   B HD21 1 
ATOM   5729 H  HD22 . LEU   B 1 108 ? 33.112 -20.622 9.034   1.00 23.69 ?  108  LEU   B HD22 1 
ATOM   5730 H  HD23 . LEU   B 1 108 ? 31.692 -21.205 8.627   1.00 23.69 ?  108  LEU   B HD23 1 
ATOM   5731 N  N    . LEU   B 1 109 ? 33.226 -24.801 5.180   1.00 14.01 ?  109  LEU   B N    1 
ATOM   5732 C  CA   . LEU   B 1 109 ? 33.855 -24.908 3.872   1.00 13.34 ?  109  LEU   B CA   1 
ATOM   5733 C  C    . LEU   B 1 109 ? 33.090 -24.118 2.818   1.00 12.48 ?  109  LEU   B C    1 
ATOM   5734 O  O    . LEU   B 1 109 ? 33.700 -23.524 1.923   1.00 12.31 ?  109  LEU   B O    1 
ATOM   5735 C  CB   . LEU   B 1 109 ? 33.965 -26.383 3.488   1.00 13.35 ?  109  LEU   B CB   1 
ATOM   5736 C  CG   . LEU   B 1 109 ? 34.752 -26.720 2.228   1.00 13.15 ?  109  LEU   B CG   1 
ATOM   5737 C  CD1  . LEU   B 1 109 ? 36.134 -26.065 2.246   1.00 13.11 ?  109  LEU   B CD1  1 
ATOM   5738 C  CD2  . LEU   B 1 109 ? 34.869 -28.232 2.062   1.00 13.98 ?  109  LEU   B CD2  1 
ATOM   5739 H  H    . LEU   B 1 109 ? 32.930 -25.542 5.488   1.00 16.84 ?  109  LEU   B H    1 
ATOM   5740 H  HA   . LEU   B 1 109 ? 34.753 -24.542 3.923   1.00 16.04 ?  109  LEU   B HA   1 
ATOM   5741 H  HB2  . LEU   B 1 109 ? 34.384 -26.853 4.221   1.00 16.04 ?  109  LEU   B HB2  1 
ATOM   5742 H  HB3  . LEU   B 1 109 ? 33.065 -26.725 3.360   1.00 16.04 ?  109  LEU   B HB3  1 
ATOM   5743 H  HG   . LEU   B 1 109 ? 34.274 -26.382 1.456   1.00 15.81 ?  109  LEU   B HG   1 
ATOM   5744 H  HD11 . LEU   B 1 109 ? 36.669 -26.432 1.525   1.00 15.76 ?  109  LEU   B HD11 1 
ATOM   5745 H  HD12 . LEU   B 1 109 ? 36.031 -25.109 2.128   1.00 15.76 ?  109  LEU   B HD12 1 
ATOM   5746 H  HD13 . LEU   B 1 109 ? 36.560 -26.251 3.099   1.00 15.76 ?  109  LEU   B HD13 1 
ATOM   5747 H  HD21 . LEU   B 1 109 ? 35.446 -28.426 1.303   1.00 16.80 ?  109  LEU   B HD21 1 
ATOM   5748 H  HD22 . LEU   B 1 109 ? 35.248 -28.614 2.868   1.00 16.80 ?  109  LEU   B HD22 1 
ATOM   5749 H  HD23 . LEU   B 1 109 ? 33.986 -28.605 1.903   1.00 16.80 ?  109  LEU   B HD23 1 
ATOM   5750 N  N    . LYS   B 1 110 ? 31.757 -24.083 2.905   1.00 12.33 ?  110  LYS   B N    1 
ATOM   5751 C  CA   . LYS   B 1 110 ? 30.998 -23.324 1.917   1.00 12.37 ?  110  LYS   B CA   1 
ATOM   5752 C  C    . LYS   B 1 110 ? 31.332 -21.839 2.006   1.00 11.91 ?  110  LYS   B C    1 
ATOM   5753 O  O    . LYS   B 1 110 ? 31.583 -21.189 0.987   1.00 11.76 ?  110  LYS   B O    1 
ATOM   5754 C  CB   . LYS   B 1 110 ? 29.493 -23.572 2.063   1.00 12.85 ?  110  LYS   B CB   1 
ATOM   5755 C  CG   . LYS   B 1 110 ? 28.686 -22.964 0.907   1.00 13.06 ?  110  LYS   B CG   1 
ATOM   5756 C  CD   . LYS   B 1 110 ? 27.213 -23.380 0.934   1.00 13.14 ?  110  LYS   B CD   1 
ATOM   5757 C  CE   . LYS   B 1 110 ? 26.451 -22.842 -0.279  1.00 14.21 ?  110  LYS   B CE   1 
ATOM   5758 N  NZ   . LYS   B 1 110 ? 26.781 -23.568 -1.536  1.00 14.21 ?  110  LYS   B NZ   1 
ATOM   5759 H  H    . LYS   B 1 110 ? 31.289 -24.482 3.504   1.00 14.82 ?  110  LYS   B H    1 
ATOM   5760 H  HA   . LYS   B 1 110 ? 31.259 -23.626 1.032   1.00 14.87 ?  110  LYS   B HA   1 
ATOM   5761 H  HB2  . LYS   B 1 110 ? 29.331 -24.530 2.075   1.00 15.44 ?  110  LYS   B HB2  1 
ATOM   5762 H  HB3  . LYS   B 1 110 ? 29.184 -23.173 2.889   1.00 15.44 ?  110  LYS   B HB3  1 
ATOM   5763 H  HG2  . LYS   B 1 110 ? 28.725 -22.001 0.964   1.00 15.70 ?  110  LYS   B HG2  1 
ATOM   5764 H  HG3  . LYS   B 1 110 ? 29.063 -23.266 0.065   1.00 15.70 ?  110  LYS   B HG3  1 
ATOM   5765 H  HD2  . LYS   B 1 110 ? 27.148 -24.350 0.924   1.00 15.80 ?  110  LYS   B HD2  1 
ATOM   5766 H  HD3  . LYS   B 1 110 ? 26.792 -23.027 1.735   1.00 15.80 ?  110  LYS   B HD3  1 
ATOM   5767 H  HE2  . LYS   B 1 110 ? 25.498 -22.929 -0.125  1.00 17.07 ?  110  LYS   B HE2  1 
ATOM   5768 H  HE3  . LYS   B 1 110 ? 26.682 -21.907 -0.409  1.00 17.07 ?  110  LYS   B HE3  1 
ATOM   5769 H  HZ1  . LYS   B 1 110 ? 26.322 -23.228 -2.217  1.00 17.08 ?  110  LYS   B HZ1  1 
ATOM   5770 H  HZ2  . LYS   B 1 110 ? 27.651 -23.500 -1.709  1.00 17.08 ?  110  LYS   B HZ2  1 
ATOM   5771 H  HZ3  . LYS   B 1 110 ? 26.572 -24.432 -1.451  1.00 17.08 ?  110  LYS   B HZ3  1 
ATOM   5772 N  N    . SER   B 1 111 ? 31.356 -21.287 3.225   1.00 12.15 ?  111  SER   B N    1 
ATOM   5773 C  CA   . SER   B 1 111 ? 31.747 -19.890 3.401   1.00 12.07 ?  111  SER   B CA   1 
ATOM   5774 C  C    . SER   B 1 111 ? 33.128 -19.627 2.814   1.00 11.44 ?  111  SER   B C    1 
ATOM   5775 O  O    . SER   B 1 111 ? 33.354 -18.595 2.165   1.00 11.85 ?  111  SER   B O    1 
ATOM   5776 C  CB   . SER   B 1 111 ? 31.734 -19.528 4.886   1.00 13.20 ?  111  SER   B CB   1 
ATOM   5777 O  OG   . SER   B 1 111 ? 30.421 -19.533 5.405   1.00 14.96 ?  111  SER   B OG   1 
ATOM   5778 H  H    . SER   B 1 111 ? 31.163 -21.701 3.955   1.00 14.60 ?  111  SER   B H    1 
ATOM   5779 H  HA   . SER   B 1 111 ? 31.113 -19.322 2.945   1.00 14.51 ?  111  SER   B HA   1 
ATOM   5780 H  HB2  . SER   B 1 111 ? 32.261 -20.179 5.377   1.00 15.86 ?  111  SER   B HB2  1 
ATOM   5781 H  HB3  . SER   B 1 111 ? 32.114 -18.644 5.000   1.00 15.86 ?  111  SER   B HB3  1 
ATOM   5782 H  HG   . SER   B 1 111 ? 30.433 -19.325 6.226   1.00 17.98 ?  111  SER   B HG   1 
ATOM   5783 N  N    . ALA   B 1 112 ? 34.064 -20.552 3.028   1.00 11.63 ?  112  ALA   B N    1 
ATOM   5784 C  CA   . ALA   B 1 112 ? 35.408 -20.375 2.489   1.00 11.31 ?  112  ALA   B CA   1 
ATOM   5785 C  C    . ALA   B 1 112 ? 35.378 -20.277 0.966   1.00 10.77 ?  112  ALA   B C    1 
ATOM   5786 O  O    . ALA   B 1 112 ? 36.002 -19.385 0.376   1.00 11.13 ?  112  ALA   B O    1 
ATOM   5787 C  CB   . ALA   B 1 112 ? 36.314 -21.514 2.964   1.00 12.04 ?  112  ALA   B CB   1 
ATOM   5788 H  H    . ALA   B 1 112 ? 33.951 -21.281 3.476   1.00 13.98 ?  112  ALA   B H    1 
ATOM   5789 H  HA   . ALA   B 1 112 ? 35.775 -19.543 2.833   1.00 13.60 ?  112  ALA   B HA   1 
ATOM   5790 H  HB1  . ALA   B 1 112 ? 37.209 -21.378 2.606   1.00 14.47 ?  112  ALA   B HB1  1 
ATOM   5791 H  HB2  . ALA   B 1 112 ? 36.351 -21.504 3.937   1.00 14.47 ?  112  ALA   B HB2  1 
ATOM   5792 H  HB3  . ALA   B 1 112 ? 35.958 -22.356 2.656   1.00 14.47 ?  112  ALA   B HB3  1 
ATOM   5793 N  N    . TYR   B 1 113 ? 34.648 -21.183 0.307   1.00 10.67 ?  113  TYR   B N    1 
ATOM   5794 C  CA   . TYR   B 1 113 ? 34.562 -21.136 -1.149  1.00 10.59 ?  113  TYR   B CA   1 
ATOM   5795 C  C    . TYR   B 1 113 ? 33.856 -19.882 -1.662  1.00 10.27 ?  113  TYR   B C    1 
ATOM   5796 O  O    . TYR   B 1 113 ? 34.137 -19.445 -2.783  1.00 10.52 ?  113  TYR   B O    1 
ATOM   5797 C  CB   . TYR   B 1 113 ? 33.896 -22.395 -1.703  1.00 10.84 ?  113  TYR   B CB   1 
ATOM   5798 C  CG   . TYR   B 1 113 ? 34.856 -23.541 -1.963  1.00 11.07 ?  113  TYR   B CG   1 
ATOM   5799 C  CD1  . TYR   B 1 113 ? 35.853 -23.437 -2.928  1.00 11.44 ?  113  TYR   B CD1  1 
ATOM   5800 C  CD2  . TYR   B 1 113 ? 34.758 -24.730 -1.262  1.00 11.23 ?  113  TYR   B CD2  1 
ATOM   5801 C  CE1  . TYR   B 1 113 ? 36.726 -24.466 -3.177  1.00 11.48 ?  113  TYR   B CE1  1 
ATOM   5802 C  CE2  . TYR   B 1 113 ? 35.635 -25.779 -1.505  1.00 11.38 ?  113  TYR   B CE2  1 
ATOM   5803 C  CZ   . TYR   B 1 113 ? 36.609 -25.643 -2.474  1.00 11.96 ?  113  TYR   B CZ   1 
ATOM   5804 O  OH   . TYR   B 1 113 ? 37.492 -26.655 -2.752  1.00 12.62 ?  113  TYR   B OH   1 
ATOM   5805 H  H    . TYR   B 1 113 ? 34.194 -21.812 0.682   1.00 12.83 ?  113  TYR   B H    1 
ATOM   5806 H  HA   . TYR   B 1 113 ? 35.463 -21.115 -1.491  1.00 12.73 ?  113  TYR   B HA   1 
ATOM   5807 H  HB2  . TYR   B 1 113 ? 33.231 -22.709 -1.067  1.00 13.04 ?  113  TYR   B HB2  1 
ATOM   5808 H  HB3  . TYR   B 1 113 ? 33.463 -22.175 -2.543  1.00 13.04 ?  113  TYR   B HB3  1 
ATOM   5809 H  HD1  . TYR   B 1 113 ? 35.935 -22.641 -3.411  1.00 13.75 ?  113  TYR   B HD1  1 
ATOM   5810 H  HD2  . TYR   B 1 113 ? 34.093 -24.829 -0.620  1.00 13.50 ?  113  TYR   B HD2  1 
ATOM   5811 H  HE1  . TYR   B 1 113 ? 37.382 -24.371 -3.831  1.00 13.80 ?  113  TYR   B HE1  1 
ATOM   5812 H  HE2  . TYR   B 1 113 ? 35.547 -26.578 -1.036  1.00 13.68 ?  113  TYR   B HE2  1 
ATOM   5813 H  HH   . TYR   B 1 113 ? 37.316 -27.327 -2.276  1.00 15.17 ?  113  TYR   B HH   1 
ATOM   5814 N  N    . GLU   B 1 114 ? 32.938 -19.299 -0.884  1.00 10.45 ?  114  GLU   B N    1 
ATOM   5815 C  CA   . GLU   B 1 114 ? 32.258 -18.088 -1.340  1.00 10.35 ?  114  GLU   B CA   1 
ATOM   5816 C  C    . GLU   B 1 114 ? 33.243 -16.965 -1.635  1.00 10.13 ?  114  GLU   B C    1 
ATOM   5817 O  O    . GLU   B 1 114 ? 32.970 -16.102 -2.475  1.00 10.66 ?  114  GLU   B O    1 
ATOM   5818 C  CB   . GLU   B 1 114 ? 31.198 -17.665 -0.317  1.00 10.50 ?  114  GLU   B CB   1 
ATOM   5819 C  CG   . GLU   B 1 114 ? 29.976 -18.578 -0.390  1.00 11.15 ?  114  GLU   B CG   1 
ATOM   5820 C  CD   . GLU   B 1 114 ? 28.952 -18.400 0.720   1.00 11.27 ?  114  GLU   B CD   1 
ATOM   5821 O  OE1  . GLU   B 1 114 ? 29.243 -17.781 1.765   1.00 11.47 ?  114  GLU   B OE1  1 
ATOM   5822 O  OE2  . GLU   B 1 114 ? 27.831 -18.938 0.558   1.00 12.43 -1 114  GLU   B OE2  1 
ATOM   5823 H  H    . GLU   B 1 114 ? 32.688 -19.587 -0.111  1.00 12.56 ?  114  GLU   B H    1 
ATOM   5824 H  HA   . GLU   B 1 114 ? 31.794 -18.289 -2.164  1.00 12.44 ?  114  GLU   B HA   1 
ATOM   5825 H  HB2  . GLU   B 1 114 ? 31.572 -17.722 0.580   1.00 12.62 ?  114  GLU   B HB2  1 
ATOM   5826 H  HB3  . GLU   B 1 114 ? 30.913 -16.758 -0.504  1.00 12.62 ?  114  GLU   B HB3  1 
ATOM   5827 H  HG2  . GLU   B 1 114 ? 29.525 -18.416 -1.228  1.00 13.40 ?  114  GLU   B HG2  1 
ATOM   5828 H  HG3  . GLU   B 1 114 ? 30.286 -19.499 -0.358  1.00 13.40 ?  114  GLU   B HG3  1 
ATOM   5829 N  N    . ASN   B 1 115 ? 34.408 -16.962 -0.983  1.00 10.25 ?  115  ASN   B N    1 
ATOM   5830 C  CA   . ASN   B 1 115 ? 35.402 -15.932 -1.274  1.00 10.28 ?  115  ASN   B CA   1 
ATOM   5831 C  C    . ASN   B 1 115 ? 35.816 -15.952 -2.739  1.00 10.17 ?  115  ASN   B C    1 
ATOM   5832 O  O    . ASN   B 1 115 ? 36.196 -14.909 -3.291  1.00 10.62 ?  115  ASN   B O    1 
ATOM   5833 C  CB   . ASN   B 1 115 ? 36.639 -16.121 -0.390  1.00 10.90 ?  115  ASN   B CB   1 
ATOM   5834 C  CG   . ASN   B 1 115 ? 36.373 -15.852 1.071   1.00 11.20 ?  115  ASN   B CG   1 
ATOM   5835 O  OD1  . ASN   B 1 115 ? 36.379 -14.705 1.507   1.00 12.90 ?  115  ASN   B OD1  1 
ATOM   5836 N  ND2  . ASN   B 1 115 ? 36.196 -16.912 1.853   1.00 11.37 ?  115  ASN   B ND2  1 
ATOM   5837 H  H    . ASN   B 1 115 ? 34.634 -17.525 -0.366  1.00 12.32 ?  115  ASN   B H    1 
ATOM   5838 H  HA   . ASN   B 1 115 ? 35.023 -15.060 -1.075  1.00 12.36 ?  115  ASN   B HA   1 
ATOM   5839 H  HB2  . ASN   B 1 115 ? 36.950 -17.035 -0.471  1.00 13.11 ?  115  ASN   B HB2  1 
ATOM   5840 H  HB3  . ASN   B 1 115 ? 37.331 -15.508 -0.684  1.00 13.11 ?  115  ASN   B HB3  1 
ATOM   5841 H  HD21 . ASN   B 1 115 ? 36.052 -16.806 2.699   1.00 13.66 ?  115  ASN   B HD21 1 
ATOM   5842 H  HD22 . ASN   B 1 115 ? 36.208 -17.701 1.519   1.00 13.66 ?  115  ASN   B HD22 1 
ATOM   5843 N  N    . PHE   B 1 116 ? 35.788 -17.129 -3.379  1.00 9.96  ?  116  PHE   B N    1 
ATOM   5844 C  CA   . PHE   B 1 116 ? 36.213 -17.225 -4.773  1.00 10.08 ?  116  PHE   B CA   1 
ATOM   5845 C  C    . PHE   B 1 116 ? 35.312 -16.395 -5.685  1.00 10.04 ?  116  PHE   B C    1 
ATOM   5846 O  O    . PHE   B 1 116 ? 35.742 -15.968 -6.760  1.00 10.59 ?  116  PHE   B O    1 
ATOM   5847 C  CB   . PHE   B 1 116 ? 36.181 -18.675 -5.299  1.00 9.84  ?  116  PHE   B CB   1 
ATOM   5848 C  CG   . PHE   B 1 116 ? 37.246 -19.628 -4.751  1.00 9.71  ?  116  PHE   B CG   1 
ATOM   5849 C  CD1  . PHE   B 1 116 ? 37.900 -19.442 -3.541  1.00 10.74 ?  116  PHE   B CD1  1 
ATOM   5850 C  CD2  . PHE   B 1 116 ? 37.550 -20.759 -5.493  1.00 10.10 ?  116  PHE   B CD2  1 
ATOM   5851 C  CE1  . PHE   B 1 116 ? 38.833 -20.378 -3.091  1.00 10.91 ?  116  PHE   B CE1  1 
ATOM   5852 C  CE2  . PHE   B 1 116 ? 38.474 -21.696 -5.051  1.00 10.23 ?  116  PHE   B CE2  1 
ATOM   5853 C  CZ   . PHE   B 1 116 ? 39.112 -21.509 -3.852  1.00 10.37 ?  116  PHE   B CZ   1 
ATOM   5854 H  H    . PHE   B 1 116 ? 35.527 -17.880 -3.029  1.00 11.97 ?  116  PHE   B H    1 
ATOM   5855 H  HA   . PHE   B 1 116 ? 37.116 -16.893 -4.853  1.00 12.12 ?  116  PHE   B HA   1 
ATOM   5856 H  HB2  . PHE   B 1 116 ? 35.311 -19.053 -5.086  1.00 11.83 ?  116  PHE   B HB2  1 
ATOM   5857 H  HB3  . PHE   B 1 116 ? 36.286 -18.645 -6.262  1.00 11.83 ?  116  PHE   B HB3  1 
ATOM   5858 H  HD1  . PHE   B 1 116 ? 37.701 -18.692 -3.018  1.00 12.91 ?  116  PHE   B HD1  1 
ATOM   5859 H  HD2  . PHE   B 1 116 ? 37.110 -20.902 -6.300  1.00 12.15 ?  116  PHE   B HD2  1 
ATOM   5860 H  HE1  . PHE   B 1 116 ? 39.268 -20.241 -2.280  1.00 13.11 ?  116  PHE   B HE1  1 
ATOM   5861 H  HE2  . PHE   B 1 116 ? 38.668 -22.442 -5.567  1.00 12.29 ?  116  PHE   B HE2  1 
ATOM   5862 H  HZ   . PHE   B 1 116 ? 39.749 -22.118 -3.557  1.00 12.47 ?  116  PHE   B HZ   1 
ATOM   5863 N  N    . ASN   B 1 117 ? 34.046 -16.190 -5.300  1.00 10.52 ?  117  ASN   B N    1 
ATOM   5864 C  CA   . ASN   B 1 117 ? 33.099 -15.487 -6.162  1.00 10.66 ?  117  ASN   B CA   1 
ATOM   5865 C  C    . ASN   B 1 117 ? 33.412 -14.006 -6.306  1.00 10.84 ?  117  ASN   B C    1 
ATOM   5866 O  O    . ASN   B 1 117 ? 32.813 -13.346 -7.159  1.00 11.89 ?  117  ASN   B O    1 
ATOM   5867 C  CB   . ASN   B 1 117 ? 31.679 -15.705 -5.663  1.00 10.63 ?  117  ASN   B CB   1 
ATOM   5868 C  CG   . ASN   B 1 117 ? 31.217 -17.116 -5.920  1.00 11.18 ?  117  ASN   B CG   1 
ATOM   5869 O  OD1  . ASN   B 1 117 ? 31.575 -17.707 -6.943  1.00 11.84 ?  117  ASN   B OD1  1 
ATOM   5870 N  ND2  . ASN   B 1 117 ? 30.478 -17.687 -4.982  1.00 11.24 ?  117  ASN   B ND2  1 
ATOM   5871 H  H    . ASN   B 1 117 ? 33.716 -16.451 -4.541  1.00 12.65 ?  117  ASN   B H    1 
ATOM   5872 H  HA   . ASN   B 1 117 ? 33.152 -15.881 -7.039  1.00 12.81 ?  117  ASN   B HA   1 
ATOM   5873 H  HB2  . ASN   B 1 117 ? 31.640 -15.543 -4.705  1.00 12.78 ?  117  ASN   B HB2  1 
ATOM   5874 H  HB3  . ASN   B 1 117 ? 31.081 -15.095 -6.127  1.00 12.78 ?  117  ASN   B HB3  1 
ATOM   5875 H  HD21 . ASN   B 1 117 ? 30.194 -18.488 -5.086  1.00 13.52 ?  117  ASN   B HD21 1 
ATOM   5876 H  HD22 . ASN   B 1 117 ? 30.258 -17.239 -4.277  1.00 13.52 ?  117  ASN   B HD22 1 
ATOM   5877 N  N    . GLN   B 1 118 ? 34.346 -13.484 -5.521  1.00 10.47 ?  118  GLN   B N    1 
ATOM   5878 C  CA   . GLN   B 1 118 ? 34.778 -12.097 -5.655  1.00 11.04 ?  118  GLN   B CA   1 
ATOM   5879 C  C    . GLN   B 1 118 ? 35.847 -11.906 -6.727  1.00 11.12 ?  118  GLN   B C    1 
ATOM   5880 O  O    . GLN   B 1 118 ? 36.333 -10.778 -6.897  1.00 12.64 ?  118  GLN   B O    1 
ATOM   5881 C  CB   . GLN   B 1 118 ? 35.258 -11.576 -4.298  1.00 11.55 ?  118  GLN   B CB   1 
ATOM   5882 C  CG   . GLN   B 1 118 ? 34.173 -11.606 -3.230  1.00 11.75 ?  118  GLN   B CG   1 
ATOM   5883 C  CD   . GLN   B 1 118 ? 33.008 -10.698 -3.566  1.00 11.64 ?  118  GLN   B CD   1 
ATOM   5884 O  OE1  . GLN   B 1 118 ? 33.202 -9.556  -3.991  1.00 12.35 ?  118  GLN   B OE1  1 
ATOM   5885 N  NE2  . GLN   B 1 118 ? 31.792 -11.195 -3.382  1.00 12.17 ?  118  GLN   B NE2  1 
ATOM   5886 H  H    . GLN   B 1 118 ? 34.755 -13.914 -4.893  1.00 12.59 ?  118  GLN   B H    1 
ATOM   5887 H  HA   . GLN   B 1 118 ? 34.015 -11.566 -5.918  1.00 13.27 ?  118  GLN   B HA   1 
ATOM   5888 H  HB2  . GLN   B 1 118 ? 35.996 -12.119 -3.987  1.00 13.88 ?  118  GLN   B HB2  1 
ATOM   5889 H  HB3  . GLN   B 1 118 ? 35.544 -10.652 -4.395  1.00 13.88 ?  118  GLN   B HB3  1 
ATOM   5890 H  HG2  . GLN   B 1 118 ? 33.836 -12.516 -3.148  1.00 14.13 ?  118  GLN   B HG2  1 
ATOM   5891 H  HG3  . GLN   B 1 118 ? 34.549 -11.317 -2.384  1.00 14.13 ?  118  GLN   B HG3  1 
ATOM   5892 H  HE21 . GLN   B 1 118 ? 31.697 -11.995 -3.080  1.00 14.62 ?  118  GLN   B HE21 1 
ATOM   5893 H  HE22 . GLN   B 1 118 ? 31.107 -10.715 -3.560  1.00 14.62 ?  118  GLN   B HE22 1 
ATOM   5894 N  N    . HIS   B 1 119 ? 36.202 -12.962 -7.466  1.00 10.66 ?  119  HIS   B N    1 
ATOM   5895 C  CA   . HIS   B 1 119 ? 37.245 -12.911 -8.483  1.00 11.24 ?  119  HIS   B CA   1 
ATOM   5896 C  C    . HIS   B 1 119 ? 36.762 -13.640 -9.726  1.00 11.27 ?  119  HIS   B C    1 
ATOM   5897 O  O    . HIS   B 1 119 ? 36.253 -14.758 -9.630  1.00 11.91 ?  119  HIS   B O    1 
ATOM   5898 C  CB   . HIS   B 1 119 ? 38.525 -13.543 -7.932  1.00 11.85 ?  119  HIS   B CB   1 
ATOM   5899 C  CG   . HIS   B 1 119 ? 39.004 -12.855 -6.700  1.00 12.89 ?  119  HIS   B CG   1 
ATOM   5900 N  ND1  . HIS   B 1 119 ? 39.802 -11.732 -6.742  1.00 14.76 ?  119  HIS   B ND1  1 
ATOM   5901 C  CD2  . HIS   B 1 119 ? 38.717 -13.070 -5.396  1.00 13.70 ?  119  HIS   B CD2  1 
ATOM   5902 C  CE1  . HIS   B 1 119 ? 40.014 -11.307 -5.509  1.00 15.26 ?  119  HIS   B CE1  1 
ATOM   5903 N  NE2  . HIS   B 1 119 ? 39.362 -12.098 -4.675  1.00 15.34 ?  119  HIS   B NE2  1 
ATOM   5904 H  H    . HIS   B 1 119 ? 35.836 -13.742 -7.396  1.00 12.81 ?  119  HIS   B H    1 
ATOM   5905 H  HA   . HIS   B 1 119 ? 37.431 -11.982 -8.709  1.00 13.51 ?  119  HIS   B HA   1 
ATOM   5906 H  HB2  . HIS   B 1 119 ? 38.355 -14.470 -7.714  1.00 14.24 ?  119  HIS   B HB2  1 
ATOM   5907 H  HB3  . HIS   B 1 119 ? 39.225 -13.478 -8.603  1.00 14.24 ?  119  HIS   B HB3  1 
ATOM   5908 H  HD2  . HIS   B 1 119 ? 38.193 -13.757 -5.049  1.00 16.46 ?  119  HIS   B HD2  1 
ATOM   5909 H  HE1  . HIS   B 1 119 ? 40.544 -10.582 -5.261  1.00 18.33 ?  119  HIS   B HE1  1 
ATOM   5910 H  HE2  . HIS   B 1 119 ? 39.370 -12.035 -3.812  1.00 18.43 ?  119  HIS   B HE2  1 
ATOM   5911 N  N    . GLU   B 1 120 ? 36.915 -13.017 -10.894 1.00 11.68 ?  120  GLU   B N    1 
ATOM   5912 C  CA   . GLU   B 1 120 ? 36.315 -13.595 -12.094 1.00 12.92 ?  120  GLU   B CA   1 
ATOM   5913 C  C    . GLU   B 1 120 ? 36.991 -14.893 -12.517 1.00 11.91 ?  120  GLU   B C    1 
ATOM   5914 O  O    . GLU   B 1 120 ? 36.329 -15.765 -13.096 1.00 12.11 ?  120  GLU   B O    1 
ATOM   5915 C  CB   . GLU   B 1 120 ? 36.315 -12.580 -13.234 1.00 16.97 ?  120  GLU   B CB   1 
ATOM   5916 C  CG   . GLU   B 1 120 ? 35.360 -11.425 -12.990 1.00 23.05 ?  120  GLU   B CG   1 
ATOM   5917 C  CD   . GLU   B 1 120 ? 35.103 -10.586 -14.223 1.00 29.15 ?  120  GLU   B CD   1 
ATOM   5918 O  OE1  . GLU   B 1 120 ? 36.071 -10.279 -14.949 1.00 31.78 ?  120  GLU   B OE1  1 
ATOM   5919 O  OE2  . GLU   B 1 120 ? 33.928 -10.233 -14.459 1.00 31.64 -1 120  GLU   B OE2  1 
ATOM   5920 H  H    . GLU   B 1 120 ? 37.346 -12.278 -11.017 1.00 14.05 ?  120  GLU   B H    1 
ATOM   5921 H  HA   . GLU   B 1 120 ? 35.393 -13.807 -11.895 1.00 15.53 ?  120  GLU   B HA   1 
ATOM   5922 H  HB2  . GLU   B 1 120 ? 37.207 -12.216 -13.335 1.00 20.38 ?  120  GLU   B HB2  1 
ATOM   5923 H  HB3  . GLU   B 1 120 ? 36.044 -13.028 -14.052 1.00 20.38 ?  120  GLU   B HB3  1 
ATOM   5924 H  HG2  . GLU   B 1 120 ? 34.506 -11.778 -12.695 1.00 27.68 ?  120  GLU   B HG2  1 
ATOM   5925 H  HG3  . GLU   B 1 120 ? 35.733 -10.844 -12.313 1.00 27.68 ?  120  GLU   B HG3  1 
ATOM   5926 N  N    . VAL   B 1 121 ? 38.290 -15.042 -12.249 1.00 11.56 ?  121  VAL   B N    1 
ATOM   5927 C  CA   . VAL   B 1 121 ? 39.034 -16.247 -12.608 1.00 11.26 ?  121  VAL   B CA   1 
ATOM   5928 C  C    . VAL   B 1 121 ? 40.152 -16.458 -11.593 1.00 10.84 ?  121  VAL   B C    1 
ATOM   5929 O  O    . VAL   B 1 121 ? 40.833 -15.505 -11.192 1.00 11.61 ?  121  VAL   B O    1 
ATOM   5930 C  CB   . VAL   B 1 121 ? 39.537 -16.194 -14.069 1.00 13.37 ?  121  VAL   B CB   1 
ATOM   5931 C  CG1  . VAL   B 1 121 ? 40.386 -14.955 -14.324 1.00 14.66 ?  121  VAL   B CG1  1 
ATOM   5932 C  CG2  . VAL   B 1 121 ? 40.292 -17.466 -14.419 1.00 14.84 ?  121  VAL   B CG2  1 
ATOM   5933 H  H    . VAL   B 1 121 ? 38.768 -14.446 -11.852 1.00 13.89 ?  121  VAL   B H    1 
ATOM   5934 H  HA   . VAL   B 1 121 ? 38.427 -17.000 -12.538 1.00 13.53 ?  121  VAL   B HA   1 
ATOM   5935 H  HB   . VAL   B 1 121 ? 38.762 -16.145 -14.654 1.00 16.07 ?  121  VAL   B HB   1 
ATOM   5936 H  HG11 . VAL   B 1 121 ? 40.695 -14.969 -15.244 1.00 17.62 ?  121  VAL   B HG11 1 
ATOM   5937 H  HG12 . VAL   B 1 121 ? 39.845 -14.162 -14.172 1.00 17.62 ?  121  VAL   B HG12 1 
ATOM   5938 H  HG13 . VAL   B 1 121 ? 41.143 -14.959 -13.720 1.00 17.62 ?  121  VAL   B HG13 1 
ATOM   5939 H  HG21 . VAL   B 1 121 ? 40.475 -17.469 -15.372 1.00 17.83 ?  121  VAL   B HG21 1 
ATOM   5940 H  HG22 . VAL   B 1 121 ? 41.127 -17.485 -13.924 1.00 17.83 ?  121  VAL   B HG22 1 
ATOM   5941 H  HG23 . VAL   B 1 121 ? 39.749 -18.234 -14.184 1.00 17.83 ?  121  VAL   B HG23 1 
ATOM   5942 N  N    . LEU   B 1 122 ? 40.337 -17.716 -11.178 1.00 10.43 ?  122  LEU   B N    1 
ATOM   5943 C  CA   . LEU   B 1 122 ? 41.310 -18.065 -10.147 1.00 10.11 ?  122  LEU   B CA   1 
ATOM   5944 C  C    . LEU   B 1 122 ? 41.971 -19.396 -10.467 1.00 9.92  ?  122  LEU   B C    1 
ATOM   5945 O  O    . LEU   B 1 122 ? 41.315 -20.324 -10.961 1.00 11.29 ?  122  LEU   B O    1 
ATOM   5946 C  CB   . LEU   B 1 122 ? 40.649 -18.308 -8.777  1.00 11.87 ?  122  LEU   B CB   1 
ATOM   5947 C  CG   . LEU   B 1 122 ? 39.625 -17.286 -8.284  1.00 12.11 ?  122  LEU   B CG   1 
ATOM   5948 C  CD1  . LEU   B 1 122 ? 38.230 -17.646 -8.755  1.00 12.90 ?  122  LEU   B CD1  1 
ATOM   5949 C  CD2  . LEU   B 1 122 ? 39.684 -17.192 -6.780  1.00 11.73 ?  122  LEU   B CD2  1 
ATOM   5950 H  H    . LEU   B 1 122 ? 39.909 -18.398 -11.481 1.00 12.53 ?  122  LEU   B H    1 
ATOM   5951 H  HA   . LEU   B 1 122 ? 41.986 -17.368 -10.060 1.00 12.16 ?  122  LEU   B HA   1 
ATOM   5952 H  HB2  . LEU   B 1 122 ? 40.194 -19.161 -8.816  1.00 14.27 ?  122  LEU   B HB2  1 
ATOM   5953 H  HB3  . LEU   B 1 122 ? 41.347 -18.346 -8.109  1.00 14.27 ?  122  LEU   B HB3  1 
ATOM   5954 H  HG   . LEU   B 1 122 ? 39.846 -16.414 -8.648  1.00 14.56 ?  122  LEU   B HG   1 
ATOM   5955 H  HD11 . LEU   B 1 122 ? 37.601 -16.991 -8.410  1.00 15.51 ?  122  LEU   B HD11 1 
ATOM   5956 H  HD12 . LEU   B 1 122 ? 38.209 -17.641 -9.725  1.00 15.51 ?  122  LEU   B HD12 1 
ATOM   5957 H  HD13 . LEU   B 1 122 ? 38.001 -18.528 -8.424  1.00 15.51 ?  122  LEU   B HD13 1 
ATOM   5958 H  HD21 . LEU   B 1 122 ? 39.001 -16.579 -6.472  1.00 14.10 ?  122  LEU   B HD21 1 
ATOM   5959 H  HD22 . LEU   B 1 122 ? 39.536 -18.073 -6.402  1.00 14.10 ?  122  LEU   B HD22 1 
ATOM   5960 H  HD23 . LEU   B 1 122 ? 40.563 -16.866 -6.519  1.00 14.10 ?  122  LEU   B HD23 1 
ATOM   5961 N  N    . LEU   B 1 123 ? 43.261 -19.497 -10.107 1.00 9.79  ?  123  LEU   B N    1 
ATOM   5962 C  CA   . LEU   B 1 123 ? 43.976 -20.769 -9.989  1.00 10.14 ?  123  LEU   B CA   1 
ATOM   5963 C  C    . LEU   B 1 123 ? 43.942 -21.172 -8.519  1.00 9.70  ?  123  LEU   B C    1 
ATOM   5964 O  O    . LEU   B 1 123 ? 44.299 -20.349 -7.665  1.00 10.29 ?  123  LEU   B O    1 
ATOM   5965 C  CB   . LEU   B 1 123 ? 45.428 -20.592 -10.449 1.00 10.63 ?  123  LEU   B CB   1 
ATOM   5966 C  CG   . LEU   B 1 123 ? 46.369 -21.776 -10.206 1.00 10.99 ?  123  LEU   B CG   1 
ATOM   5967 C  CD1  . LEU   B 1 123 ? 45.936 -23.025 -10.977 1.00 11.38 ?  123  LEU   B CD1  1 
ATOM   5968 C  CD2  . LEU   B 1 123 ? 47.786 -21.387 -10.576 1.00 12.02 ?  123  LEU   B CD2  1 
ATOM   5969 H  H    . LEU   B 1 123 ? 43.755 -18.815 -9.905  1.00 11.78 ?  123  LEU   B H    1 
ATOM   5970 H  HA   . LEU   B 1 123 ? 43.540 -21.450 -10.522 1.00 12.20 ?  123  LEU   B HA   1 
ATOM   5971 H  HB2  . LEU   B 1 123 ? 45.423 -20.422 -11.402 1.00 12.78 ?  123  LEU   B HB2  1 
ATOM   5972 H  HB3  . LEU   B 1 123 ? 45.804 -19.832 -9.985  1.00 12.78 ?  123  LEU   B HB3  1 
ATOM   5973 H  HG   . LEU   B 1 123 ? 46.361 -22.002 -9.262  1.00 13.21 ?  123  LEU   B HG   1 
ATOM   5974 H  HD11 . LEU   B 1 123 ? 46.567 -23.740 -10.803 1.00 13.67 ?  123  LEU   B HD11 1 
ATOM   5975 H  HD12 . LEU   B 1 123 ? 45.048 -23.290 -10.679 1.00 13.67 ?  123  LEU   B HD12 1 
ATOM   5976 H  HD13 . LEU   B 1 123 ? 45.917 -22.820 -11.924 1.00 13.67 ?  123  LEU   B HD13 1 
ATOM   5977 H  HD21 . LEU   B 1 123 ? 48.373 -22.143 -10.424 1.00 14.45 ?  123  LEU   B HD21 1 
ATOM   5978 H  HD22 . LEU   B 1 123 ? 47.807 -21.135 -11.515 1.00 14.45 ?  123  LEU   B HD22 1 
ATOM   5979 H  HD23 . LEU   B 1 123 ? 48.058 -20.637 -10.027 1.00 14.45 ?  123  LEU   B HD23 1 
ATOM   5980 N  N    . ALA   B 1 124 ? 43.511 -22.403 -8.213  1.00 9.90  ?  124  ALA   B N    1 
ATOM   5981 C  CA   . ALA   B 1 124 ? 43.248 -22.721 -6.816  1.00 9.98  ?  124  ALA   B CA   1 
ATOM   5982 C  C    . ALA   B 1 124 ? 43.534 -24.179 -6.499  1.00 9.91  ?  124  ALA   B C    1 
ATOM   5983 O  O    . ALA   B 1 124 ? 43.389 -25.056 -7.364  1.00 10.54 ?  124  ALA   B O    1 
ATOM   5984 C  CB   . ALA   B 1 124 ? 41.794 -22.417 -6.443  1.00 10.16 ?  124  ALA   B CB   1 
ATOM   5985 H  H    . ALA   B 1 124 ? 43.352 -23.038 -8.779  1.00 11.90 ?  124  ALA   B H    1 
ATOM   5986 H  HA   . ALA   B 1 124 ? 43.824 -22.173 -6.271  1.00 12.00 ?  124  ALA   B HA   1 
ATOM   5987 H  HB1  . ALA   B 1 124 ? 41.650 -22.640 -5.511  1.00 12.22 ?  124  ALA   B HB1  1 
ATOM   5988 H  HB2  . ALA   B 1 124 ? 41.624 -21.471 -6.587  1.00 12.22 ?  124  ALA   B HB2  1 
ATOM   5989 H  HB3  . ALA   B 1 124 ? 41.202 -22.945 -7.004  1.00 12.22 ?  124  ALA   B HB3  1 
ATOM   5990 N  N    . PRO   B 1 125 ? 43.826 -24.479 -5.235  1.00 10.23 ?  125  PRO   B N    1 
ATOM   5991 C  CA   . PRO   B 1 125 ? 43.761 -25.846 -4.718  1.00 10.78 ?  125  PRO   B CA   1 
ATOM   5992 C  C    . PRO   B 1 125 ? 42.359 -26.121 -4.172  1.00 10.58 ?  125  PRO   B C    1 
ATOM   5993 O  O    . PRO   B 1 125 ? 41.560 -25.205 -3.963  1.00 11.22 ?  125  PRO   B O    1 
ATOM   5994 C  CB   . PRO   B 1 125 ? 44.751 -25.776 -3.548  1.00 11.94 ?  125  PRO   B CB   1 
ATOM   5995 C  CG   . PRO   B 1 125 ? 44.498 -24.390 -2.969  1.00 11.81 ?  125  PRO   B CG   1 
ATOM   5996 C  CD   . PRO   B 1 125 ? 44.162 -23.515 -4.169  1.00 10.95 ?  125  PRO   B CD   1 
ATOM   5997 H  HA   . PRO   B 1 125 ? 44.033 -26.511 -5.370  1.00 12.96 ?  125  PRO   B HA   1 
ATOM   5998 H  HB2  . PRO   B 1 125 ? 44.549 -26.469 -2.893  1.00 14.35 ?  125  PRO   B HB2  1 
ATOM   5999 H  HB3  . PRO   B 1 125 ? 45.662 -25.860 -3.870  1.00 14.35 ?  125  PRO   B HB3  1 
ATOM   6000 H  HG2  . PRO   B 1 125 ? 43.749 -24.418 -2.350  1.00 14.20 ?  125  PRO   B HG2  1 
ATOM   6001 H  HG3  . PRO   B 1 125 ? 45.297 -24.066 -2.517  1.00 14.20 ?  125  PRO   B HG3  1 
ATOM   6002 H  HD2  . PRO   B 1 125 ? 43.407 -22.942 -3.976  1.00 13.17 ?  125  PRO   B HD2  1 
ATOM   6003 H  HD3  . PRO   B 1 125 ? 44.944 -22.987 -4.427  1.00 13.17 ?  125  PRO   B HD3  1 
ATOM   6004 N  N    . LEU   B 1 126 ? 42.086 -27.400 -3.895  1.00 11.32 ?  126  LEU   B N    1 
ATOM   6005 C  CA   . LEU   B 1 126 ? 40.867 -27.769 -3.179  1.00 11.93 ?  126  LEU   B CA   1 
ATOM   6006 C  C    . LEU   B 1 126 ? 40.978 -27.366 -1.716  1.00 12.16 ?  126  LEU   B C    1 
ATOM   6007 O  O    . LEU   B 1 126 ? 41.871 -27.823 -0.993  1.00 13.70 ?  126  LEU   B O    1 
ATOM   6008 C  CB   . LEU   B 1 126 ? 40.611 -29.266 -3.294  1.00 13.08 ?  126  LEU   B CB   1 
ATOM   6009 C  CG   . LEU   B 1 126 ? 40.082 -29.745 -4.643  1.00 13.99 ?  126  LEU   B CG   1 
ATOM   6010 C  CD1  . LEU   B 1 126 ? 40.111 -31.258 -4.695  1.00 15.89 ?  126  LEU   B CD1  1 
ATOM   6011 C  CD2  . LEU   B 1 126 ? 38.672 -29.226 -4.903  1.00 14.45 ?  126  LEU   B CD2  1 
ATOM   6012 H  H    . LEU   B 1 126 ? 42.593 -28.069 -4.102  1.00 13.61 ?  126  LEU   B H    1 
ATOM   6013 H  HA   . LEU   B 1 126 ? 40.118 -27.292 -3.572  1.00 14.34 ?  126  LEU   B HA   1 
ATOM   6014 H  HB2  . LEU   B 1 126 ? 41.442 -29.727 -3.125  1.00 15.72 ?  126  LEU   B HB2  1 
ATOM   6015 H  HB3  . LEU   B 1 126 ? 39.956 -29.509 -2.625  1.00 15.72 ?  126  LEU   B HB3  1 
ATOM   6016 H  HG   . LEU   B 1 126 ? 40.663 -29.408 -5.349  1.00 16.82 ?  126  LEU   B HG   1 
ATOM   6017 H  HD11 . LEU   B 1 126 ? 39.770 -31.553 -5.552  1.00 19.09 ?  126  LEU   B HD11 1 
ATOM   6018 H  HD12 . LEU   B 1 126 ? 41.021 -31.564 -4.573  1.00 19.09 ?  126  LEU   B HD12 1 
ATOM   6019 H  HD13 . LEU   B 1 126 ? 39.548 -31.605 -3.980  1.00 19.09 ?  126  LEU   B HD13 1 
ATOM   6020 H  HD21 . LEU   B 1 126 ? 38.322 -29.651 -5.699  1.00 17.37 ?  126  LEU   B HD21 1 
ATOM   6021 H  HD22 . LEU   B 1 126 ? 38.116 -29.433 -4.139  1.00 17.37 ?  126  LEU   B HD22 1 
ATOM   6022 H  HD23 . LEU   B 1 126 ? 38.708 -28.262 -5.034  1.00 17.37 ?  126  LEU   B HD23 1 
ATOM   6023 N  N    . LEU   B 1 127 ? 40.049 -26.534 -1.265  1.00 11.71 ?  127  LEU   B N    1 
ATOM   6024 C  CA   . LEU   B 1 127 ? 40.101 -26.051 0.100   1.00 12.01 ?  127  LEU   B CA   1 
ATOM   6025 C  C    . LEU   B 1 127 ? 39.827 -27.175 1.091   1.00 11.81 ?  127  LEU   B C    1 
ATOM   6026 O  O    . LEU   B 1 127 ? 39.005 -28.069 0.865   1.00 12.06 ?  127  LEU   B O    1 
ATOM   6027 C  CB   . LEU   B 1 127 ? 39.088 -24.926 0.313   1.00 12.33 ?  127  LEU   B CB   1 
ATOM   6028 C  CG   . LEU   B 1 127 ? 39.270 -23.656 -0.515  1.00 13.09 ?  127  LEU   B CG   1 
ATOM   6029 C  CD1  . LEU   B 1 127 ? 38.143 -22.680 -0.196  1.00 13.10 ?  127  LEU   B CD1  1 
ATOM   6030 C  CD2  . LEU   B 1 127 ? 40.637 -23.019 -0.267  1.00 13.83 ?  127  LEU   B CD2  1 
ATOM   6031 H  H    . LEU   B 1 127 ? 39.381 -26.234 -1.729  1.00 14.07 ?  127  LEU   B H    1 
ATOM   6032 H  HA   . LEU   B 1 127 ? 40.985 -25.693 0.274   1.00 14.44 ?  127  LEU   B HA   1 
ATOM   6033 H  HB2  . LEU   B 1 127 ? 38.203 -25.270 0.108   1.00 14.82 ?  127  LEU   B HB2  1 
ATOM   6034 H  HB3  . LEU   B 1 127 ? 39.117 -24.662 1.245   1.00 14.82 ?  127  LEU   B HB3  1 
ATOM   6035 H  HG   . LEU   B 1 127 ? 39.207 -23.875 -1.455  1.00 15.73 ?  127  LEU   B HG   1 
ATOM   6036 H  HD11 . LEU   B 1 127 ? 38.269 -21.868 -0.717  1.00 15.74 ?  127  LEU   B HD11 1 
ATOM   6037 H  HD12 . LEU   B 1 127 ? 37.294 -23.088 -0.421  1.00 15.74 ?  127  LEU   B HD12 1 
ATOM   6038 H  HD13 . LEU   B 1 127 ? 38.167 -22.466 0.752   1.00 15.74 ?  127  LEU   B HD13 1 
ATOM   6039 H  HD21 . LEU   B 1 127 ? 40.678 -22.163 -0.720  1.00 16.62 ?  127  LEU   B HD21 1 
ATOM   6040 H  HD22 . LEU   B 1 127 ? 40.758 -22.891 0.690   1.00 16.62 ?  127  LEU   B HD22 1 
ATOM   6041 H  HD23 . LEU   B 1 127 ? 41.326 -23.609 -0.608  1.00 16.62 ?  127  LEU   B HD23 1 
ATOM   6042 N  N    . SER   B 1 128 ? 40.510 -27.086 2.224   1.00 11.81 ?  128  SER   B N    1 
ATOM   6043 C  CA   . SER   B 1 128 ? 40.406 -28.003 3.348   1.00 12.29 ?  128  SER   B CA   1 
ATOM   6044 C  C    . SER   B 1 128 ? 40.899 -29.412 3.023   1.00 13.34 ?  128  SER   B C    1 
ATOM   6045 O  O    . SER   B 1 128 ? 40.813 -30.293 3.879   1.00 14.98 ?  128  SER   B O    1 
ATOM   6046 C  CB   . SER   B 1 128 ? 39.006 -28.011 3.983   1.00 12.76 ?  128  SER   B CB   1 
ATOM   6047 O  OG   . SER   B 1 128 ? 38.696 -26.737 4.545   1.00 13.45 ?  128  SER   B OG   1 
ATOM   6048 H  H    . SER   B 1 128 ? 41.071 -26.449 2.372   1.00 14.20 ?  128  SER   B H    1 
ATOM   6049 H  HA   . SER   B 1 128 ? 40.997 -27.664 4.028   1.00 14.78 ?  128  SER   B HA   1 
ATOM   6050 H  HB2  . SER   B 1 128 ? 38.342 -28.234 3.312   1.00 15.34 ?  128  SER   B HB2  1 
ATOM   6051 H  HB3  . SER   B 1 128 ? 38.987 -28.679 4.696   1.00 15.34 ?  128  SER   B HB3  1 
ATOM   6052 H  HG   . SER   B 1 128 ? 39.270 -26.534 5.126   1.00 16.16 ?  128  SER   B HG   1 
ATOM   6053 N  N    . ALA   B 1 129 ? 41.458 -29.640 1.831   1.00 14.01 ?  129  ALA   B N    1 
ATOM   6054 C  CA   . ALA   B 1 129 ? 42.001 -30.939 1.466   1.00 15.09 ?  129  ALA   B CA   1 
ATOM   6055 C  C    . ALA   B 1 129 ? 43.390 -31.123 2.068   1.00 14.53 ?  129  ALA   B C    1 
ATOM   6056 O  O    . ALA   B 1 129 ? 43.947 -30.226 2.715   1.00 14.25 ?  129  ALA   B O    1 
ATOM   6057 C  CB   . ALA   B 1 129 ? 42.055 -31.086 -0.053  1.00 17.10 ?  129  ALA   B CB   1 
ATOM   6058 H  H    . ALA   B 1 129 ? 41.526 -29.049 1.205   1.00 16.84 ?  129  ALA   B H    1 
ATOM   6059 H  HA   . ALA   B 1 129 ? 41.423 -31.633 1.816   1.00 18.13 ?  129  ALA   B HA   1 
ATOM   6060 H  HB1  . ALA   B 1 129 ? 42.413 -31.962 -0.273  1.00 20.54 ?  129  ALA   B HB1  1 
ATOM   6061 H  HB2  . ALA   B 1 129 ? 41.158 -30.997 -0.412  1.00 20.54 ?  129  ALA   B HB2  1 
ATOM   6062 H  HB3  . ALA   B 1 129 ? 42.628 -30.394 -0.419  1.00 20.54 ?  129  ALA   B HB3  1 
ATOM   6063 N  N    . GLY   B 1 130 ? 43.952 -32.307 1.845   1.00 14.54 ?  130  GLY   B N    1 
ATOM   6064 C  CA   . GLY   B 1 130 ? 45.342 -32.541 2.189   1.00 15.00 ?  130  GLY   B CA   1 
ATOM   6065 C  C    . GLY   B 1 130 ? 45.563 -32.443 3.679   1.00 15.16 ?  130  GLY   B C    1 
ATOM   6066 O  O    . GLY   B 1 130 ? 44.872 -33.089 4.480   1.00 16.00 ?  130  GLY   B O    1 
ATOM   6067 H  H    . GLY   B 1 130 ? 43.555 -32.981 1.489   1.00 17.47 ?  130  GLY   B H    1 
ATOM   6068 H  HA2  . GLY   B 1 130 ? 45.607 -33.429 1.894   1.00 18.02 ?  130  GLY   B HA2  1 
ATOM   6069 H  HA3  . GLY   B 1 130 ? 45.907 -31.888 1.748   1.00 18.02 ?  130  GLY   B HA3  1 
ATOM   6070 N  N    . ILE   B 1 131 ? 46.533 -31.606 4.064   1.00 15.52 ?  131  ILE   B N    1 
ATOM   6071 C  CA   . ILE   B 1 131 ? 46.901 -31.475 5.467   1.00 16.29 ?  131  ILE   B CA   1 
ATOM   6072 C  C    . ILE   B 1 131 ? 45.787 -30.885 6.314   1.00 15.50 ?  131  ILE   B C    1 
ATOM   6073 O  O    . ILE   B 1 131 ? 45.869 -30.957 7.543   1.00 16.40 ?  131  ILE   B O    1 
ATOM   6074 C  CB   . ILE   B 1 131 ? 48.221 -30.693 5.663   1.00 18.38 ?  131  ILE   B CB   1 
ATOM   6075 C  CG1  . ILE   B 1 131 ? 48.050 -29.220 5.268   1.00 19.55 ?  131  ILE   B CG1  1 
ATOM   6076 C  CG2  . ILE   B 1 131 ? 49.353 -31.338 4.867   1.00 19.67 ?  131  ILE   B CG2  1 
ATOM   6077 C  CD1  . ILE   B 1 131 ? 49.252 -28.343 5.601   1.00 20.67 ?  131  ILE   B CD1  1 
ATOM   6078 H  H    . ILE   B 1 131 ? 46.987 -31.105 3.531   1.00 18.65 ?  131  ILE   B H    1 
ATOM   6079 H  HA   . ILE   B 1 131 ? 47.058 -32.365 5.811   1.00 19.57 ?  131  ILE   B HA   1 
ATOM   6080 H  HB   . ILE   B 1 131 ? 48.454 -30.726 6.603   1.00 22.08 ?  131  ILE   B HB   1 
ATOM   6081 H  HG12 . ILE   B 1 131 ? 47.899 -29.170 4.311   1.00 23.48 ?  131  ILE   B HG12 1 
ATOM   6082 H  HG13 . ILE   B 1 131 ? 47.283 -28.848 5.737   1.00 23.48 ?  131  ILE   B HG13 1 
ATOM   6083 H  HG21 . ILE   B 1 131 ? 50.191 -30.919 5.118   1.00 23.63 ?  131  ILE   B HG21 1 
ATOM   6084 H  HG22 . ILE   B 1 131 ? 49.378 -32.282 5.069   1.00 23.63 ?  131  ILE   B HG22 1 
ATOM   6085 H  HG23 . ILE   B 1 131 ? 49.185 -31.202 3.920   1.00 23.63 ?  131  ILE   B HG23 1 
ATOM   6086 H  HD11 . ILE   B 1 131 ? 49.028 -27.419 5.404   1.00 24.82 ?  131  ILE   B HD11 1 
ATOM   6087 H  HD12 . ILE   B 1 131 ? 49.458 -28.440 6.543   1.00 24.82 ?  131  ILE   B HD12 1 
ATOM   6088 H  HD13 . ILE   B 1 131 ? 50.004 -28.625 5.063   1.00 24.82 ?  131  ILE   B HD13 1 
ATOM   6089 N  N    . PHE   B 1 132 ? 44.750 -30.309 5.695   1.00 14.37 ?  132  PHE   B N    1 
ATOM   6090 C  CA   . PHE   B 1 132 ? 43.600 -29.799 6.436   1.00 14.49 ?  132  PHE   B CA   1 
ATOM   6091 C  C    . PHE   B 1 132 ? 42.571 -30.883 6.760   1.00 15.54 ?  132  PHE   B C    1 
ATOM   6092 O  O    . PHE   B 1 132 ? 41.662 -30.624 7.556   1.00 17.28 ?  132  PHE   B O    1 
ATOM   6093 C  CB   . PHE   B 1 132 ? 42.924 -28.656 5.664   1.00 13.63 ?  132  PHE   B CB   1 
ATOM   6094 C  CG   . PHE   B 1 132 ? 43.628 -27.314 5.775   1.00 13.16 ?  132  PHE   B CG   1 
ATOM   6095 C  CD1  . PHE   B 1 132 ? 44.923 -27.133 5.310   1.00 14.91 ?  132  PHE   B CD1  1 
ATOM   6096 C  CD2  . PHE   B 1 132 ? 42.952 -26.218 6.297   1.00 12.79 ?  132  PHE   B CD2  1 
ATOM   6097 C  CE1  . PHE   B 1 132 ? 45.540 -25.892 5.408   1.00 15.39 ?  132  PHE   B CE1  1 
ATOM   6098 C  CE2  . PHE   B 1 132 ? 43.560 -24.980 6.390   1.00 13.37 ?  132  PHE   B CE2  1 
ATOM   6099 C  CZ   . PHE   B 1 132 ? 44.851 -24.816 5.945   1.00 14.46 ?  132  PHE   B CZ   1 
ATOM   6100 H  H    . PHE   B 1 132 ? 44.691 -30.207 4.845   1.00 17.27 ?  132  PHE   B H    1 
ATOM   6101 H  HA   . PHE   B 1 132 ? 43.916 -29.435 7.277   1.00 17.41 ?  132  PHE   B HA   1 
ATOM   6102 H  HB2  . PHE   B 1 132 ? 42.900 -28.895 4.727   1.00 16.38 ?  132  PHE   B HB2  1 
ATOM   6103 H  HB3  . PHE   B 1 132 ? 42.021 -28.549 6.002   1.00 16.38 ?  132  PHE   B HB3  1 
ATOM   6104 H  HD1  . PHE   B 1 132 ? 45.388 -27.860 4.956   1.00 17.92 ?  132  PHE   B HD1  1 
ATOM   6105 H  HD2  . PHE   B 1 132 ? 42.075 -26.328 6.606   1.00 15.37 ?  132  PHE   B HD2  1 
ATOM   6106 H  HE1  . PHE   B 1 132 ? 46.412 -25.785 5.108   1.00 18.49 ?  132  PHE   B HE1  1 
ATOM   6107 H  HE2  . PHE   B 1 132 ? 43.095 -24.261 6.757   1.00 16.07 ?  132  PHE   B HE2  1 
ATOM   6108 H  HZ   . PHE   B 1 132 ? 45.263 -23.984 6.011   1.00 17.37 ?  132  PHE   B HZ   1 
ATOM   6109 N  N    . GLY   B 1 133 ? 42.671 -32.076 6.158   1.00 15.37 ?  133  GLY   B N    1 
ATOM   6110 C  CA   . GLY   B 1 133 ? 41.961 -33.245 6.648   1.00 16.37 ?  133  GLY   B CA   1 
ATOM   6111 C  C    . GLY   B 1 133 ? 40.571 -33.512 6.101   1.00 16.89 ?  133  GLY   B C    1 
ATOM   6112 O  O    . GLY   B 1 133 ? 39.988 -34.543 6.453   1.00 19.15 ?  133  GLY   B O    1 
ATOM   6113 H  H    . GLY   B 1 133 ? 43.153 -32.221 5.462   1.00 18.46 ?  133  GLY   B H    1 
ATOM   6114 H  HA2  . GLY   B 1 133 ? 42.498 -34.026 6.455   1.00 19.67 ?  133  GLY   B HA2  1 
ATOM   6115 H  HA3  . GLY   B 1 133 ? 41.886 -33.170 7.612   1.00 19.67 ?  133  GLY   B HA3  1 
ATOM   6116 N  N    . ALA   B 1 134 ? 40.009 -32.639 5.270   1.00 16.26 ?  134  ALA   B N    1 
ATOM   6117 C  CA   . ALA   B 1 134 ? 38.685 -32.913 4.729   1.00 16.25 ?  134  ALA   B CA   1 
ATOM   6118 C  C    . ALA   B 1 134 ? 38.773 -33.909 3.573   1.00 15.84 ?  134  ALA   B C    1 
ATOM   6119 O  O    . ALA   B 1 134 ? 39.829 -34.098 2.962   1.00 16.51 ?  134  ALA   B O    1 
ATOM   6120 C  CB   . ALA   B 1 134 ? 38.012 -31.622 4.261   1.00 16.59 ?  134  ALA   B CB   1 
ATOM   6121 H  H    . ALA   B 1 134 ? 40.363 -31.897 5.008   1.00 19.54 ?  134  ALA   B H    1 
ATOM   6122 H  HA   . ALA   B 1 134 ? 38.132 -33.305 5.425   1.00 19.52 ?  134  ALA   B HA   1 
ATOM   6123 H  HB1  . ALA   B 1 134 ? 37.125 -31.833 3.926   1.00 19.93 ?  134  ALA   B HB1  1 
ATOM   6124 H  HB2  . ALA   B 1 134 ? 37.943 -31.012 5.013   1.00 19.93 ?  134  ALA   B HB2  1 
ATOM   6125 H  HB3  . ALA   B 1 134 ? 38.545 -31.224 3.558   1.00 19.93 ?  134  ALA   B HB3  1 
ATOM   6126 N  N    . ASP   B 1 135 ? 37.641 -34.545 3.280   1.00 16.04 ?  135  ASP   B N    1 
ATOM   6127 C  CA   . ASP   B 1 135 ? 37.541 -35.439 2.132   1.00 16.70 ?  135  ASP   B CA   1 
ATOM   6128 C  C    . ASP   B 1 135 ? 37.639 -34.598 0.865   1.00 15.52 ?  135  ASP   B C    1 
ATOM   6129 O  O    . ASP   B 1 135 ? 36.789 -33.723 0.648   1.00 15.63 ?  135  ASP   B O    1 
ATOM   6130 C  CB   . ASP   B 1 135 ? 36.196 -36.172 2.194   1.00 18.30 ?  135  ASP   B CB   1 
ATOM   6131 C  CG   . ASP   B 1 135 ? 35.989 -37.147 1.046   1.00 20.18 ?  135  ASP   B CG   1 
ATOM   6132 O  OD1  . ASP   B 1 135 ? 36.853 -37.206 0.146   1.00 19.62 ?  135  ASP   B OD1  1 
ATOM   6133 O  OD2  . ASP   B 1 135 ? 34.963 -37.871 1.056   1.00 22.87 -1 135  ASP   B OD2  1 
ATOM   6134 H  H    . ASP   B 1 135 ? 36.912 -34.470 3.731   1.00 19.27 ?  135  ASP   B H    1 
ATOM   6135 H  HA   . ASP   B 1 135 ? 38.259 -36.091 2.159   1.00 20.06 ?  135  ASP   B HA   1 
ATOM   6136 H  HB2  . ASP   B 1 135 ? 36.155 -36.673 3.021   1.00 21.98 ?  135  ASP   B HB2  1 
ATOM   6137 H  HB3  . ASP   B 1 135 ? 35.485 -35.515 2.164   1.00 21.98 ?  135  ASP   B HB3  1 
ATOM   6138 N  N    . PRO   B 1 136 ? 38.652 -34.800 0.016   1.00 15.61 ?  136  PRO   B N    1 
ATOM   6139 C  CA   . PRO   B 1 136 ? 38.743 -33.977 -1.201  1.00 15.38 ?  136  PRO   B CA   1 
ATOM   6140 C  C    . PRO   B 1 136 ? 37.552 -34.133 -2.126  1.00 14.43 ?  136  PRO   B C    1 
ATOM   6141 O  O    . PRO   B 1 136 ? 37.225 -33.183 -2.848  1.00 13.67 ?  136  PRO   B O    1 
ATOM   6142 C  CB   . PRO   B 1 136 ? 40.053 -34.441 -1.851  1.00 16.66 ?  136  PRO   B CB   1 
ATOM   6143 C  CG   . PRO   B 1 136 ? 40.276 -35.820 -1.305  1.00 17.68 ?  136  PRO   B CG   1 
ATOM   6144 C  CD   . PRO   B 1 136 ? 39.742 -35.786 0.096   1.00 16.98 ?  136  PRO   B CD   1 
ATOM   6145 H  HA   . PRO   B 1 136 ? 38.826 -33.040 -0.963  1.00 18.48 ?  136  PRO   B HA   1 
ATOM   6146 H  HB2  . PRO   B 1 136 ? 39.955 -34.463 -2.818  1.00 20.02 ?  136  PRO   B HB2  1 
ATOM   6147 H  HB3  . PRO   B 1 136 ? 40.775 -33.846 -1.595  1.00 20.02 ?  136  PRO   B HB3  1 
ATOM   6148 H  HG2  . PRO   B 1 136 ? 39.791 -36.467 -1.841  1.00 21.24 ?  136  PRO   B HG2  1 
ATOM   6149 H  HG3  . PRO   B 1 136 ? 41.226 -36.020 -1.304  1.00 21.24 ?  136  PRO   B HG3  1 
ATOM   6150 H  HD2  . PRO   B 1 136 ? 39.395 -36.654 0.349   1.00 20.40 ?  136  PRO   B HD2  1 
ATOM   6151 H  HD3  . PRO   B 1 136 ? 40.422 -35.476 0.716   1.00 20.40 ?  136  PRO   B HD3  1 
ATOM   6152 N  N    . ILE   B 1 137 ? 36.894 -35.296 -2.129  1.00 14.58 ?  137  ILE   B N    1 
ATOM   6153 C  CA   . ILE   B 1 137 ? 35.675 -35.462 -2.917  1.00 15.23 ?  137  ILE   B CA   1 
ATOM   6154 C  C    . ILE   B 1 137 ? 34.602 -34.491 -2.441  1.00 14.46 ?  137  ILE   B C    1 
ATOM   6155 O  O    . ILE   B 1 137 ? 33.885 -33.881 -3.246  1.00 14.64 ?  137  ILE   B O    1 
ATOM   6156 C  CB   . ILE   B 1 137 ? 35.205 -36.930 -2.860  1.00 17.54 ?  137  ILE   B CB   1 
ATOM   6157 C  CG1  . ILE   B 1 137 ? 36.191 -37.829 -3.610  1.00 19.79 ?  137  ILE   B CG1  1 
ATOM   6158 C  CG2  . ILE   B 1 137 ? 33.809 -37.076 -3.444  1.00 18.02 ?  137  ILE   B CG2  1 
ATOM   6159 C  CD1  . ILE   B 1 137 ? 35.893 -39.313 -3.492  1.00 22.07 ?  137  ILE   B CD1  1 
ATOM   6160 H  H    . ILE   B 1 137 ? 37.131 -35.994 -1.694  1.00 17.52 ?  137  ILE   B H    1 
ATOM   6161 H  HA   . ILE   B 1 137 ? 35.868 -35.253 -3.846  1.00 18.29 ?  137  ILE   B HA   1 
ATOM   6162 H  HB   . ILE   B 1 137 ? 35.178 -37.208 -1.935  1.00 21.07 ?  137  ILE   B HB   1 
ATOM   6163 H  HG12 . ILE   B 1 137 ? 36.170 -37.601 -4.553  1.00 23.77 ?  137  ILE   B HG12 1 
ATOM   6164 H  HG13 . ILE   B 1 137 ? 37.080 -37.680 -3.256  1.00 23.77 ?  137  ILE   B HG13 1 
ATOM   6165 H  HG21 . ILE   B 1 137 ? 33.595 -38.019 -3.535  1.00 21.65 ?  137  ILE   B HG21 1 
ATOM   6166 H  HG22 . ILE   B 1 137 ? 33.169 -36.658 -2.850  1.00 21.65 ?  137  ILE   B HG22 1 
ATOM   6167 H  HG23 . ILE   B 1 137 ? 33.784 -36.650 -4.315  1.00 21.65 ?  137  ILE   B HG23 1 
ATOM   6168 H  HD11 . ILE   B 1 137 ? 36.668 -39.811 -3.789  1.00 26.51 ?  137  ILE   B HD11 1 
ATOM   6169 H  HD12 . ILE   B 1 137 ? 35.698 -39.521 -2.565  1.00 26.51 ?  137  ILE   B HD12 1 
ATOM   6170 H  HD13 . ILE   B 1 137 ? 35.127 -39.529 -4.047  1.00 26.51 ?  137  ILE   B HD13 1 
ATOM   6171 N  N    . HIS   B 1 138 ? 34.468 -34.341 -1.125  1.00 14.48 ?  138  HIS   B N    1 
ATOM   6172 C  CA   . HIS   B 1 138 ? 33.524 -33.370 -0.588  1.00 14.95 ?  138  HIS   B CA   1 
ATOM   6173 C  C    . HIS   B 1 138 ? 33.948 -31.942 -0.904  1.00 14.15 ?  138  HIS   B C    1 
ATOM   6174 O  O    . HIS   B 1 138 ? 33.102 -31.098 -1.221  1.00 14.39 ?  138  HIS   B O    1 
ATOM   6175 C  CB   . HIS   B 1 138 ? 33.391 -33.557 0.917   1.00 16.51 ?  138  HIS   B CB   1 
ATOM   6176 C  CG   . HIS   B 1 138 ? 32.458 -32.579 1.553   1.00 17.38 ?  138  HIS   B CG   1 
ATOM   6177 N  ND1  . HIS   B 1 138 ? 31.119 -32.515 1.236   1.00 19.07 ?  138  HIS   B ND1  1 
ATOM   6178 C  CD2  . HIS   B 1 138 ? 32.674 -31.607 2.470   1.00 17.83 ?  138  HIS   B CD2  1 
ATOM   6179 C  CE1  . HIS   B 1 138 ? 30.547 -31.554 1.938   1.00 19.14 ?  138  HIS   B CE1  1 
ATOM   6180 N  NE2  . HIS   B 1 138 ? 31.468 -30.987 2.696   1.00 18.41 ?  138  HIS   B NE2  1 
ATOM   6181 H  H    . HIS   B 1 138 ? 34.910 -34.783 -0.537  1.00 17.40 ?  138  HIS   B H    1 
ATOM   6182 H  HA   . HIS   B 1 138 ? 32.657 -33.522 -0.992  1.00 17.97 ?  138  HIS   B HA   1 
ATOM   6183 H  HB2  . HIS   B 1 138 ? 33.049 -34.449 1.091   1.00 19.84 ?  138  HIS   B HB2  1 
ATOM   6184 H  HB3  . HIS   B 1 138 ? 34.261 -33.450 1.326   1.00 19.84 ?  138  HIS   B HB3  1 
ATOM   6185 H  HD1  . HIS   B 1 138 ? 30.716 -33.029 0.671   1.00 22.91 ?  138  HIS   B HD1  1 
ATOM   6186 H  HD2  . HIS   B 1 138 ? 33.480 -31.400 2.877   1.00 21.42 ?  138  HIS   B HD2  1 
ATOM   6187 H  HE1  . HIS   B 1 138 ? 29.642 -31.325 1.908   1.00 22.99 ?  138  HIS   B HE1  1 
ATOM   6188 N  N    . SER   B 1 139 ? 35.244 -31.644 -0.822  1.00 14.04 ?  139  SER   B N    1 
ATOM   6189 C  CA   . SER   B 1 139 ? 35.687 -30.297 -1.147  1.00 13.25 ?  139  SER   B CA   1 
ATOM   6190 C  C    . SER   B 1 139 ? 35.347 -29.943 -2.587  1.00 12.53 ?  139  SER   B C    1 
ATOM   6191 O  O    . SER   B 1 139 ? 34.904 -28.826 -2.867  1.00 12.64 ?  139  SER   B O    1 
ATOM   6192 C  CB   . SER   B 1 139 ? 37.181 -30.159 -0.885  1.00 13.73 ?  139  SER   B CB   1 
ATOM   6193 O  OG   . SER   B 1 139 ? 37.585 -28.829 -1.141  1.00 13.64 ?  139  SER   B OG   1 
ATOM   6194 H  H    . SER   B 1 139 ? 35.869 -32.188 -0.599  1.00 16.87 ?  139  SER   B H    1 
ATOM   6195 H  HA   . SER   B 1 139 ? 35.224 -29.669 -0.576  1.00 15.92 ?  139  SER   B HA   1 
ATOM   6196 H  HB2  . SER   B 1 139 ? 37.365 -30.378 0.040   1.00 16.50 ?  139  SER   B HB2  1 
ATOM   6197 H  HB3  . SER   B 1 139 ? 37.670 -30.751 -1.476  1.00 16.50 ?  139  SER   B HB3  1 
ATOM   6198 H  HG   . SER   B 1 139 ? 38.410 -28.736 -0.987  1.00 16.39 ?  139  SER   B HG   1 
ATOM   6199 N  N    . LEU   B 1 140 ? 35.529 -30.888 -3.513  1.00 12.78 ?  140  LEU   B N    1 
ATOM   6200 C  CA   . LEU   B 1 140 ? 35.166 -30.635 -4.902  1.00 12.80 ?  140  LEU   B CA   1 
ATOM   6201 C  C    . LEU   B 1 140 ? 33.663 -30.399 -5.033  1.00 12.75 ?  140  LEU   B C    1 
ATOM   6202 O  O    . LEU   B 1 140 ? 33.226 -29.501 -5.759  1.00 12.78 ?  140  LEU   B O    1 
ATOM   6203 C  CB   . LEU   B 1 140 ? 35.637 -31.795 -5.781  1.00 12.73 ?  140  LEU   B CB   1 
ATOM   6204 C  CG   . LEU   B 1 140 ? 35.275 -31.680 -7.253  1.00 12.57 ?  140  LEU   B CG   1 
ATOM   6205 C  CD1  . LEU   B 1 140 ? 35.844 -30.410 -7.855  1.00 13.69 ?  140  LEU   B CD1  1 
ATOM   6206 C  CD2  . LEU   B 1 140 ? 35.747 -32.909 -8.014  1.00 13.52 ?  140  LEU   B CD2  1 
ATOM   6207 H  H    . LEU   B 1 140 ? 35.849 -31.666 -3.368  1.00 15.35 ?  140  LEU   B H    1 
ATOM   6208 H  HA   . LEU   B 1 140 ? 35.621 -29.829 -5.206  1.00 15.38 ?  140  LEU   B HA   1 
ATOM   6209 H  HB2  . LEU   B 1 140 ? 36.604 -31.853 -5.724  1.00 15.30 ?  140  LEU   B HB2  1 
ATOM   6210 H  HB3  . LEU   B 1 140 ? 35.240 -32.612 -5.451  1.00 15.30 ?  140  LEU   B HB3  1 
ATOM   6211 H  HG   . LEU   B 1 140 ? 34.312 -31.630 -7.337  1.00 15.10 ?  140  LEU   B HG   1 
ATOM   6212 H  HD11 . LEU   B 1 140 ? 35.721 -30.432 -8.817  1.00 16.45 ?  140  LEU   B HD11 1 
ATOM   6213 H  HD12 . LEU   B 1 140 ? 35.375 -29.642 -7.483  1.00 16.45 ?  140  LEU   B HD12 1 
ATOM   6214 H  HD13 . LEU   B 1 140 ? 36.788 -30.352 -7.644  1.00 16.45 ?  140  LEU   B HD13 1 
ATOM   6215 H  HD21 . LEU   B 1 140 ? 35.499 -32.806 -8.948  1.00 16.25 ?  140  LEU   B HD21 1 
ATOM   6216 H  HD22 . LEU   B 1 140 ? 36.704 -32.981 -7.928  1.00 16.25 ?  140  LEU   B HD22 1 
ATOM   6217 H  HD23 . LEU   B 1 140 ? 35.309 -33.686 -7.639  1.00 16.25 ?  140  LEU   B HD23 1 
ATOM   6218 N  N    . ARG   B 1 141 ? 32.859 -31.192 -4.321  1.00 13.00 ?  141  ARG   B N    1 
ATOM   6219 C  CA   . ARG   B 1 141 ? 31.408 -31.012 -4.307  1.00 14.12 ?  141  ARG   B CA   1 
ATOM   6220 C  C    . ARG   B 1 141 ? 31.031 -29.603 -3.870  1.00 13.16 ?  141  ARG   B C    1 
ATOM   6221 O  O    . ARG   B 1 141 ? 30.231 -28.921 -4.527  1.00 13.52 ?  141  ARG   B O    1 
ATOM   6222 C  CB   . ARG   B 1 141 ? 30.814 -32.047 -3.343  1.00 15.51 ?  141  ARG   B CB   1 
ATOM   6223 C  CG   . ARG   B 1 141 ? 29.349 -31.914 -3.015  1.00 18.14 ?  141  ARG   B CG   1 
ATOM   6224 C  CD   . ARG   B 1 141 ? 28.547 -32.546 -4.077  1.00 19.82 ?  141  ARG   B CD   1 
ATOM   6225 N  NE   . ARG   B 1 141 ? 28.286 -31.635 -5.179  1.00 20.20 ?  141  ARG   B NE   1 
ATOM   6226 C  CZ   . ARG   B 1 141 ? 28.270 -31.982 -6.458  1.00 19.60 ?  141  ARG   B CZ   1 
ATOM   6227 N  NH1  . ARG   B 1 141 ? 28.708 -33.165 -6.862  1.00 19.72 ?  141  ARG   B NH1  1 
ATOM   6228 N  NH2  . ARG   B 1 141 ? 27.801 -31.117 -7.355  1.00 21.11 ?  141  ARG   B NH2  1 
ATOM   6229 H  H    . ARG   B 1 141 ? 33.138 -31.839 -3.831  1.00 15.62 ?  141  ARG   B H    1 
ATOM   6230 H  HA   . ARG   B 1 141 ? 31.053 -31.169 -5.191  1.00 16.97 ?  141  ARG   B HA   1 
ATOM   6231 H  HB2  . ARG   B 1 141 ? 30.958 -32.930 -3.724  1.00 18.64 ?  141  ARG   B HB2  1 
ATOM   6232 H  HB3  . ARG   B 1 141 ? 31.303 -31.990 -2.506  1.00 18.64 ?  141  ARG   B HB3  1 
ATOM   6233 H  HG2  . ARG   B 1 141 ? 29.175 -32.356 -2.176  1.00 21.79 ?  141  ARG   B HG2  1 
ATOM   6234 H  HG3  . ARG   B 1 141 ? 29.108 -30.970 -2.953  1.00 21.79 ?  141  ARG   B HG3  1 
ATOM   6235 H  HD2  . ARG   B 1 141 ? 29.022 -33.323 -4.416  1.00 23.81 ?  141  ARG   B HD2  1 
ATOM   6236 H  HD3  . ARG   B 1 141 ? 27.703 -32.820 -3.701  1.00 23.81 ?  141  ARG   B HD3  1 
ATOM   6237 H  HE   . ARG   B 1 141 ? 28.119 -30.811 -4.984  1.00 24.26 ?  141  ARG   B HE   1 
ATOM   6238 H  HH11 . ARG   B 1 141 ? 29.001 -33.738 -6.293  1.00 23.68 ?  141  ARG   B HH11 1 
ATOM   6239 H  HH12 . ARG   B 1 141 ? 28.694 -33.362 -7.696  1.00 23.68 ?  141  ARG   B HH12 1 
ATOM   6240 H  HH21 . ARG   B 1 141 ? 27.521 -30.340 -7.104  1.00 25.35 ?  141  ARG   B HH21 1 
ATOM   6241 H  HH22 . ARG   B 1 141 ? 27.802 -31.317 -8.192  1.00 25.35 ?  141  ARG   B HH22 1 
ATOM   6242 N  N    . VAL   B 1 142 ? 31.576 -29.163 -2.736  1.00 12.89 ?  142  VAL   B N    1 
ATOM   6243 C  CA   . VAL   B 1 142 ? 31.247 -27.831 -2.245  1.00 12.59 ?  142  VAL   B CA   1 
ATOM   6244 C  C    . VAL   B 1 142 ? 31.726 -26.768 -3.228  1.00 12.58 ?  142  VAL   B C    1 
ATOM   6245 O  O    . VAL   B 1 142 ? 31.028 -25.781 -3.483  1.00 13.13 ?  142  VAL   B O    1 
ATOM   6246 C  CB   . VAL   B 1 142 ? 31.792 -27.612 -0.821  1.00 13.43 ?  142  VAL   B CB   1 
ATOM   6247 C  CG1  . VAL   B 1 142 ? 31.475 -26.191 -0.346  1.00 13.56 ?  142  VAL   B CG1  1 
ATOM   6248 C  CG2  . VAL   B 1 142 ? 31.204 -28.632 0.138   1.00 14.46 ?  142  VAL   B CG2  1 
ATOM   6249 H  H    . VAL   B 1 142 ? 32.129 -29.603 -2.245  1.00 15.50 ?  142  VAL   B H    1 
ATOM   6250 H  HA   . VAL   B 1 142 ? 30.287 -27.755 -2.195  1.00 15.13 ?  142  VAL   B HA   1 
ATOM   6251 H  HB   . VAL   B 1 142 ? 32.753 -27.723 -0.820  1.00 16.14 ?  142  VAL   B HB   1 
ATOM   6252 H  HG11 . VAL   B 1 142 ? 31.647 -26.131 0.606   1.00 16.30 ?  142  VAL   B HG11 1 
ATOM   6253 H  HG12 . VAL   B 1 142 ? 32.043 -25.565 -0.824  1.00 16.30 ?  142  VAL   B HG12 1 
ATOM   6254 H  HG13 . VAL   B 1 142 ? 30.543 -25.998 -0.527  1.00 16.30 ?  142  VAL   B HG13 1 
ATOM   6255 H  HG21 . VAL   B 1 142 ? 31.527 -28.446 1.034   1.00 17.38 ?  142  VAL   B HG21 1 
ATOM   6256 H  HG22 . VAL   B 1 142 ? 30.234 -28.558 0.118   1.00 17.38 ?  142  VAL   B HG22 1 
ATOM   6257 H  HG23 . VAL   B 1 142 ? 31.474 -29.518 -0.137  1.00 17.38 ?  142  VAL   B HG23 1 
ATOM   6258 N  N    . CYS   B 1 143 ? 32.905 -26.972 -3.822  1.00 12.11 ?  143  CYS   B N    1 
ATOM   6259 C  CA   . CYS   B 1 143 ? 33.403 -26.032 -4.823  1.00 12.05 ?  143  CYS   B CA   1 
ATOM   6260 C  C    . CYS   B 1 143 ? 32.404 -25.880 -5.966  1.00 12.22 ?  143  CYS   B C    1 
ATOM   6261 O  O    . CYS   B 1 143 ? 31.993 -24.767 -6.312  1.00 12.57 ?  143  CYS   B O    1 
ATOM   6262 C  CB   . CYS   B 1 143 ? 34.757 -26.517 -5.352  1.00 12.37 ?  143  CYS   B CB   1 
ATOM   6263 S  SG   . CYS   B 1 143 ? 35.511 -25.414 -6.566  1.00 12.72 ?  143  CYS   B SG   1 
ATOM   6264 H  H    . CYS   B 1 143 ? 33.428 -27.634 -3.663  1.00 14.56 ?  143  CYS   B H    1 
ATOM   6265 H  HA   . CYS   B 1 143 ? 33.530 -25.162 -4.414  1.00 14.49 ?  143  CYS   B HA   1 
ATOM   6266 H  HB2  . CYS   B 1 143 ? 35.374 -26.600 -4.611  1.00 14.87 ?  143  CYS   B HB2  1 
ATOM   6267 H  HB3  . CYS   B 1 143 ? 34.634 -27.378 -5.773  1.00 14.87 ?  143  CYS   B HB3  1 
ATOM   6268 H  HG   . CYS   B 1 143 ? 36.579 -25.853 -6.891  1.00 15.28 ?  143  CYS   B HG   1 
ATOM   6269 N  N    . VAL   B 1 144 ? 32.000 -26.999 -6.567  1.00 12.61 ?  144  VAL   B N    1 
ATOM   6270 C  CA   . VAL   B 1 144 ? 31.088 -26.937 -7.704  1.00 13.57 ?  144  VAL   B CA   1 
ATOM   6271 C  C    . VAL   B 1 144 ? 29.748 -26.324 -7.322  1.00 13.55 ?  144  VAL   B C    1 
ATOM   6272 O  O    . VAL   B 1 144 ? 29.128 -25.617 -8.128  1.00 15.08 ?  144  VAL   B O    1 
ATOM   6273 C  CB   . VAL   B 1 144 ? 30.932 -28.346 -8.284  1.00 16.28 ?  144  VAL   B CB   1 
ATOM   6274 C  CG1  . VAL   B 1 144 ? 29.659 -28.474 -9.120  1.00 19.01 ?  144  VAL   B CG1  1 
ATOM   6275 C  CG2  . VAL   B 1 144 ? 32.181 -28.741 -9.072  1.00 16.96 ?  144  VAL   B CG2  1 
ATOM   6276 H  H    . VAL   B 1 144 ? 32.238 -27.798 -6.341  1.00 15.15 ?  144  VAL   B H    1 
ATOM   6277 H  HA   . VAL   B 1 144 ? 31.481 -26.384 -8.394  1.00 16.30 ?  144  VAL   B HA   1 
ATOM   6278 H  HB   . VAL   B 1 144 ? 30.851 -28.977 -7.550  1.00 19.56 ?  144  VAL   B HB   1 
ATOM   6279 H  HG11 . VAL   B 1 144 ? 29.732 -29.266 -9.683  1.00 22.84 ?  144  VAL   B HG11 1 
ATOM   6280 H  HG12 . VAL   B 1 144 ? 28.898 -28.568 -8.528  1.00 22.84 ?  144  VAL   B HG12 1 
ATOM   6281 H  HG13 . VAL   B 1 144 ? 29.563 -27.688 -9.674  1.00 22.84 ?  144  VAL   B HG13 1 
ATOM   6282 H  HG21 . VAL   B 1 144 ? 32.063 -29.639 -9.426  1.00 20.38 ?  144  VAL   B HG21 1 
ATOM   6283 H  HG22 . VAL   B 1 144 ? 32.302 -28.115 -9.803  1.00 20.38 ?  144  VAL   B HG22 1 
ATOM   6284 H  HG23 . VAL   B 1 144 ? 32.946 -28.717 -8.481  1.00 20.38 ?  144  VAL   B HG23 1 
ATOM   6285 N  N    . ASP   B 1 145 ? 29.283 -26.568 -6.100  1.00 13.52 ?  145  ASP   B N    1 
ATOM   6286 C  CA   . ASP   B 1 145 ? 27.975 -26.102 -5.657  1.00 14.39 ?  145  ASP   B CA   1 
ATOM   6287 C  C    . ASP   B 1 145 ? 28.003 -24.682 -5.112  1.00 13.84 ?  145  ASP   B C    1 
ATOM   6288 O  O    . ASP   B 1 145 ? 26.945 -24.144 -4.773  1.00 15.95 ?  145  ASP   B O    1 
ATOM   6289 C  CB   . ASP   B 1 145 ? 27.407 -27.035 -4.578  1.00 16.00 ?  145  ASP   B CB   1 
ATOM   6290 C  CG   . ASP   B 1 145 ? 27.020 -28.401 -5.109  1.00 17.92 ?  145  ASP   B CG   1 
ATOM   6291 O  OD1  . ASP   B 1 145 ? 26.895 -28.573 -6.340  1.00 17.96 ?  145  ASP   B OD1  1 
ATOM   6292 O  OD2  . ASP   B 1 145 ? 26.830 -29.303 -4.270  1.00 19.96 -1 145  ASP   B OD2  1 
ATOM   6293 H  H    . ASP   B 1 145 ? 29.725 -26.993 -5.501  1.00 16.25 ?  145  ASP   B H    1 
ATOM   6294 H  HA   . ASP   B 1 145 ? 27.375 -26.101 -6.412  1.00 17.29 ?  145  ASP   B HA   1 
ATOM   6295 H  HB2  . ASP   B 1 145 ? 28.073 -27.160 -3.891  1.00 19.22 ?  145  ASP   B HB2  1 
ATOM   6296 H  HB3  . ASP   B 1 145 ? 26.612 -26.622 -4.205  1.00 19.22 ?  145  ASP   B HB3  1 
ATOM   6297 N  N    . THR   B 1 146 ? 29.176 -24.065 -5.008  1.00 12.35 ?  146  THR   B N    1 
ATOM   6298 C  CA   . THR   B 1 146 ? 29.312 -22.745 -4.400  1.00 12.06 ?  146  THR   B CA   1 
ATOM   6299 C  C    . THR   B 1 146 ? 29.946 -21.716 -5.316  1.00 11.78 ?  146  THR   B C    1 
ATOM   6300 O  O    . THR   B 1 146 ? 29.488 -20.557 -5.363  1.00 12.14 ?  146  THR   B O    1 
ATOM   6301 C  CB   . THR   B 1 146 ? 30.139 -22.855 -3.112  1.00 12.57 ?  146  THR   B CB   1 
ATOM   6302 O  OG1  . THR   B 1 146 ? 29.565 -23.851 -2.257  1.00 12.46 ?  146  THR   B OG1  1 
ATOM   6303 C  CG2  . THR   B 1 146 ? 30.216 -21.509 -2.389  1.00 12.71 ?  146  THR   B CG2  1 
ATOM   6304 H  H    . THR   B 1 146 ? 29.929 -24.391 -5.290  1.00 14.84 ?  146  THR   B H    1 
ATOM   6305 H  HA   . THR   B 1 146 ? 28.440 -22.419 -4.158  1.00 14.50 ?  146  THR   B HA   1 
ATOM   6306 H  HB   . THR   B 1 146 ? 31.047 -23.115 -3.339  1.00 15.11 ?  146  THR   B HB   1 
ATOM   6307 H  HG1  . THR   B 1 146 ? 29.604 -24.608 -2.638  1.00 14.98 ?  146  THR   B HG1  1 
ATOM   6308 H  HG21 . THR   B 1 146 ? 30.567 -21.634 -1.495  1.00 15.28 ?  146  THR   B HG21 1 
ATOM   6309 H  HG22 . THR   B 1 146 ? 30.801 -20.903 -2.874  1.00 15.28 ?  146  THR   B HG22 1 
ATOM   6310 H  HG23 . THR   B 1 146 ? 29.332 -21.116 -2.330  1.00 15.28 ?  146  THR   B HG23 1 
ATOM   6311 N  N    . VAL   B 1 147 ? 31.014 -22.091 -6.013  1.00 11.56 ?  147  VAL   B N    1 
ATOM   6312 C  CA   . VAL   B 1 147 ? 31.738 -21.147 -6.849  1.00 11.64 ?  147  VAL   B CA   1 
ATOM   6313 C  C    . VAL   B 1 147 ? 31.007 -21.008 -8.173  1.00 11.83 ?  147  VAL   B C    1 
ATOM   6314 O  O    . VAL   B 1 147 ? 30.634 -22.010 -8.800  1.00 12.17 ?  147  VAL   B O    1 
ATOM   6315 C  CB   . VAL   B 1 147 ? 33.190 -21.603 -7.054  1.00 11.44 ?  147  VAL   B CB   1 
ATOM   6316 C  CG1  . VAL   B 1 147 ? 33.944 -20.573 -7.871  1.00 12.10 ?  147  VAL   B CG1  1 
ATOM   6317 C  CG2  . VAL   B 1 147 ? 33.875 -21.818 -5.719  1.00 11.68 ?  147  VAL   B CG2  1 
ATOM   6318 H  H    . VAL   B 1 147 ? 31.341 -22.888 -6.020  1.00 13.90 ?  147  VAL   B H    1 
ATOM   6319 H  HA   . VAL   B 1 147 ? 31.754 -20.279 -6.416  1.00 13.99 ?  147  VAL   B HA   1 
ATOM   6320 H  HB   . VAL   B 1 147 ? 33.202 -22.440 -7.545  1.00 13.75 ?  147  VAL   B HB   1 
ATOM   6321 H  HG11 . VAL   B 1 147 ? 34.890 -20.791 -7.859  1.00 14.55 ?  147  VAL   B HG11 1 
ATOM   6322 H  HG12 . VAL   B 1 147 ? 33.615 -20.584 -8.783  1.00 14.55 ?  147  VAL   B HG12 1 
ATOM   6323 H  HG13 . VAL   B 1 147 ? 33.804 -19.696 -7.478  1.00 14.55 ?  147  VAL   B HG13 1 
ATOM   6324 H  HG21 . VAL   B 1 147 ? 34.812 -22.012 -5.871  1.00 14.04 ?  147  VAL   B HG21 1 
ATOM   6325 H  HG22 . VAL   B 1 147 ? 33.784 -21.013 -5.187  1.00 14.04 ?  147  VAL   B HG22 1 
ATOM   6326 H  HG23 . VAL   B 1 147 ? 33.451 -22.564 -5.267  1.00 14.04 ?  147  VAL   B HG23 1 
ATOM   6327 N  N    . ARG   B 1 148 ? 30.797 -19.757 -8.594  1.00 11.85 ?  148  ARG   B N    1 
ATOM   6328 C  CA   . ARG   B 1 148 ? 30.167 -19.433 -9.865  1.00 11.78 ?  148  ARG   B CA   1 
ATOM   6329 C  C    . ARG   B 1 148 ? 31.124 -18.760 -10.837 1.00 11.71 ?  148  ARG   B C    1 
ATOM   6330 O  O    . ARG   B 1 148 ? 30.840 -18.739 -12.038 1.00 13.31 ?  148  ARG   B O    1 
ATOM   6331 C  CB   . ARG   B 1 148 ? 28.932 -18.545 -9.637  1.00 12.23 ?  148  ARG   B CB   1 
ATOM   6332 C  CG   . ARG   B 1 148 ? 27.860 -19.264 -8.839  1.00 13.17 ?  148  ARG   B CG   1 
ATOM   6333 C  CD   . ARG   B 1 148 ? 26.656 -18.389 -8.520  1.00 14.18 ?  148  ARG   B CD   1 
ATOM   6334 N  NE   . ARG   B 1 148 ? 27.022 -17.184 -7.786  1.00 13.61 ?  148  ARG   B NE   1 
ATOM   6335 C  CZ   . ARG   B 1 148 ? 27.324 -17.151 -6.496  1.00 12.96 ?  148  ARG   B CZ   1 
ATOM   6336 N  NH1  . ARG   B 1 148 ? 27.283 -18.244 -5.745  1.00 12.96 ?  148  ARG   B NH1  1 
ATOM   6337 N  NH2  . ARG   B 1 148 ? 27.709 -15.999 -5.950  1.00 12.85 ?  148  ARG   B NH2  1 
ATOM   6338 H  H    . ARG   B 1 148 ? 31.017 -19.058 -8.136  1.00 14.24 ?  148  ARG   B H    1 
ATOM   6339 H  HA   . ARG   B 1 148 ? 29.865 -20.255 -10.276 1.00 14.17 ?  148  ARG   B HA   1 
ATOM   6340 H  HB2  . ARG   B 1 148 ? 29.199 -17.750 -9.146  1.00 14.70 ?  148  ARG   B HB2  1 
ATOM   6341 H  HB3  . ARG   B 1 148 ? 28.560 -18.295 -10.497 1.00 14.70 ?  148  ARG   B HB3  1 
ATOM   6342 H  HG2  . ARG   B 1 148 ? 27.548 -20.025 -9.353  1.00 15.82 ?  148  ARG   B HG2  1 
ATOM   6343 H  HG3  . ARG   B 1 148 ? 28.242 -19.565 -8.001  1.00 15.82 ?  148  ARG   B HG3  1 
ATOM   6344 H  HD2  . ARG   B 1 148 ? 26.231 -18.117 -9.348  1.00 17.04 ?  148  ARG   B HD2  1 
ATOM   6345 H  HD3  . ARG   B 1 148 ? 26.030 -18.896 -7.977  1.00 17.04 ?  148  ARG   B HD3  1 
ATOM   6346 H  HE   . ARG   B 1 148 ? 27.042 -16.442 -8.216  1.00 16.35 ?  148  ARG   B HE   1 
ATOM   6347 H  HH11 . ARG   B 1 148 ? 27.041 -18.995 -6.084  1.00 15.57 ?  148  ARG   B HH11 1 
ATOM   6348 H  HH12 . ARG   B 1 148 ? 27.487 -18.199 -4.907  1.00 15.57 ?  148  ARG   B HH12 1 
ATOM   6349 H  HH21 . ARG   B 1 148 ? 27.743 -15.288 -6.428  1.00 15.45 ?  148  ARG   B HH21 1 
ATOM   6350 H  HH22 . ARG   B 1 148 ? 27.910 -15.964 -5.113  1.00 15.45 ?  148  ARG   B HH22 1 
ATOM   6351 N  N    . THR   B 1 149 ? 32.233 -18.211 -10.349 1.00 11.71 ?  149  THR   B N    1 
ATOM   6352 C  CA   . THR   B 1 149 ? 33.273 -17.646 -11.194 1.00 11.77 ?  149  THR   B CA   1 
ATOM   6353 C  C    . THR   B 1 149 ? 34.156 -18.783 -11.706 1.00 11.53 ?  149  THR   B C    1 
ATOM   6354 O  O    . THR   B 1 149 ? 33.960 -19.953 -11.365 1.00 12.16 ?  149  THR   B O    1 
ATOM   6355 C  CB   . THR   B 1 149 ? 34.040 -16.592 -10.406 1.00 11.92 ?  149  THR   B CB   1 
ATOM   6356 O  OG1  . THR   B 1 149 ? 34.497 -17.197 -9.194  1.00 11.96 ?  149  THR   B OG1  1 
ATOM   6357 C  CG2  . THR   B 1 149 ? 33.152 -15.390 -10.095 1.00 12.84 ?  149  THR   B CG2  1 
ATOM   6358 H  H    . THR   B 1 149 ? 32.396 -18.136 -9.506  1.00 14.08 ?  149  THR   B H    1 
ATOM   6359 H  HA   . THR   B 1 149 ? 32.860 -17.210 -11.956 1.00 14.15 ?  149  THR   B HA   1 
ATOM   6360 H  HB   . THR   B 1 149 ? 34.801 -16.295 -10.922 1.00 14.33 ?  149  THR   B HB   1 
ATOM   6361 H  HG1  . THR   B 1 149 ? 34.918 -16.631 -8.732  1.00 14.37 ?  149  THR   B HG1  1 
ATOM   6362 H  HG21 . THR   B 1 149 ? 33.660 -14.723 -9.608  1.00 15.43 ?  149  THR   B HG21 1 
ATOM   6363 H  HG22 . THR   B 1 149 ? 32.825 -14.999 -10.919 1.00 15.43 ?  149  THR   B HG22 1 
ATOM   6364 H  HG23 . THR   B 1 149 ? 32.395 -15.666 -9.554  1.00 15.43 ?  149  THR   B HG23 1 
ATOM   6365 N  N    . ASN   B 1 150 ? 35.123 -18.461 -12.555 1.00 11.48 ?  150  ASN   B N    1 
ATOM   6366 C  CA   . ASN   B 1 150 ? 35.886 -19.487 -13.256 1.00 12.04 ?  150  ASN   B CA   1 
ATOM   6367 C  C    . ASN   B 1 150 ? 37.051 -19.939 -12.390 1.00 11.56 ?  150  ASN   B C    1 
ATOM   6368 O  O    . ASN   B 1 150 ? 37.984 -19.171 -12.143 1.00 12.42 ?  150  ASN   B O    1 
ATOM   6369 C  CB   . ASN   B 1 150 ? 36.356 -18.955 -14.602 1.00 14.00 ?  150  ASN   B CB   1 
ATOM   6370 C  CG   . ASN   B 1 150 ? 35.206 -18.735 -15.551 1.00 16.72 ?  150  ASN   B CG   1 
ATOM   6371 O  OD1  . ASN   B 1 150 ? 34.309 -19.571 -15.644 1.00 17.75 ?  150  ASN   B OD1  1 
ATOM   6372 N  ND2  . ASN   B 1 150 ? 35.200 -17.599 -16.232 1.00 18.52 ?  150  ASN   B ND2  1 
ATOM   6373 H  H    . ASN   B 1 150 ? 35.360 -17.654 -12.734 1.00 13.81 ?  150  ASN   B H    1 
ATOM   6374 H  HA   . ASN   B 1 150 ? 35.305 -20.253 -13.417 1.00 14.47 ?  150  ASN   B HA   1 
ATOM   6375 H  HB2  . ASN   B 1 150 ? 36.804 -18.106 -14.467 1.00 16.83 ?  150  ASN   B HB2  1 
ATOM   6376 H  HB3  . ASN   B 1 150 ? 36.963 -19.597 -15.000 1.00 16.83 ?  150  ASN   B HB3  1 
ATOM   6377 H  HD21 . ASN   B 1 150 ? 34.567 -17.429 -16.790 1.00 22.25 ?  150  ASN   B HD21 1 
ATOM   6378 H  HD22 . ASN   B 1 150 ? 35.842 -17.031 -16.129 1.00 22.25 ?  150  ASN   B HD22 1 
ATOM   6379 N  N    . VAL   B 1 151 ? 37.006 -21.183 -11.930 1.00 11.15 ?  151  VAL   B N    1 
ATOM   6380 C  CA   . VAL   B 1 151 ? 38.025 -21.719 -11.041 1.00 11.40 ?  151  VAL   B CA   1 
ATOM   6381 C  C    . VAL   B 1 151 ? 38.731 -22.884 -11.723 1.00 11.42 ?  151  VAL   B C    1 
ATOM   6382 O  O    . VAL   B 1 151 ? 38.091 -23.814 -12.233 1.00 12.45 ?  151  VAL   B O    1 
ATOM   6383 C  CB   . VAL   B 1 151 ? 37.465 -22.067 -9.647  1.00 12.74 ?  151  VAL   B CB   1 
ATOM   6384 C  CG1  . VAL   B 1 151 ? 36.313 -23.061 -9.736  1.00 13.55 ?  151  VAL   B CG1  1 
ATOM   6385 C  CG2  . VAL   B 1 151 ? 38.575 -22.574 -8.733  1.00 12.87 ?  151  VAL   B CG2  1 
ATOM   6386 H  H    . VAL   B 1 151 ? 36.383 -21.746 -12.122 1.00 13.41 ?  151  VAL   B H    1 
ATOM   6387 H  HA   . VAL   B 1 151 ? 38.696 -21.026 -10.903 1.00 13.70 ?  151  VAL   B HA   1 
ATOM   6388 H  HB   . VAL   B 1 151 ? 37.117 -21.256 -9.245  1.00 15.32 ?  151  VAL   B HB   1 
ATOM   6389 H  HG11 . VAL   B 1 151 ? 35.992 -23.260 -8.841  1.00 16.28 ?  151  VAL   B HG11 1 
ATOM   6390 H  HG12 . VAL   B 1 151 ? 35.597 -22.673 -10.263 1.00 16.28 ?  151  VAL   B HG12 1 
ATOM   6391 H  HG13 . VAL   B 1 151 ? 36.627 -23.878 -10.159 1.00 16.28 ?  151  VAL   B HG13 1 
ATOM   6392 H  HG21 . VAL   B 1 151 ? 38.222 -22.660 -7.831  1.00 15.47 ?  151  VAL   B HG21 1 
ATOM   6393 H  HG22 . VAL   B 1 151 ? 38.876 -23.441 -9.049  1.00 15.47 ?  151  VAL   B HG22 1 
ATOM   6394 H  HG23 . VAL   B 1 151 ? 39.308 -21.943 -8.741  1.00 15.47 ?  151  VAL   B HG23 1 
ATOM   6395 N  N    . TYR   B 1 152 ? 40.061 -22.799 -11.742 1.00 10.74 ?  152  TYR   B N    1 
ATOM   6396 C  CA   . TYR   B 1 152 ? 40.964 -23.779 -12.327 1.00 10.97 ?  152  TYR   B CA   1 
ATOM   6397 C  C    . TYR   B 1 152 ? 41.688 -24.458 -11.169 1.00 10.52 ?  152  TYR   B C    1 
ATOM   6398 O  O    . TYR   B 1 152 ? 42.540 -23.846 -10.513 1.00 10.96 ?  152  TYR   B O    1 
ATOM   6399 C  CB   . TYR   B 1 152 ? 41.937 -23.074 -13.276 1.00 11.87 ?  152  TYR   B CB   1 
ATOM   6400 C  CG   . TYR   B 1 152 ? 41.260 -22.612 -14.545 1.00 12.63 ?  152  TYR   B CG   1 
ATOM   6401 C  CD1  . TYR   B 1 152 ? 40.593 -21.388 -14.613 1.00 13.00 ?  152  TYR   B CD1  1 
ATOM   6402 C  CD2  . TYR   B 1 152 ? 41.272 -23.412 -15.675 1.00 13.69 ?  152  TYR   B CD2  1 
ATOM   6403 C  CE1  . TYR   B 1 152 ? 39.952 -20.986 -15.778 1.00 14.00 ?  152  TYR   B CE1  1 
ATOM   6404 C  CE2  . TYR   B 1 152 ? 40.635 -23.026 -16.838 1.00 14.46 ?  152  TYR   B CE2  1 
ATOM   6405 C  CZ   . TYR   B 1 152 ? 39.980 -21.808 -16.889 1.00 14.61 ?  152  TYR   B CZ   1 
ATOM   6406 O  OH   . TYR   B 1 152 ? 39.358 -21.434 -18.057 1.00 17.26 ?  152  TYR   B OH   1 
ATOM   6407 H  H    . TYR   B 1 152 ? 40.496 -22.132 -11.396 1.00 12.91 ?  152  TYR   B H    1 
ATOM   6408 H  HA   . TYR   B 1 152 ? 40.457 -24.443 -12.823 1.00 13.18 ?  152  TYR   B HA   1 
ATOM   6409 H  HB2  . TYR   B 1 152 ? 42.304 -22.297 -12.828 1.00 14.26 ?  152  TYR   B HB2  1 
ATOM   6410 H  HB3  . TYR   B 1 152 ? 42.649 -23.688 -13.516 1.00 14.26 ?  152  TYR   B HB3  1 
ATOM   6411 H  HD1  . TYR   B 1 152 ? 40.565 -20.841 -13.863 1.00 15.62 ?  152  TYR   B HD1  1 
ATOM   6412 H  HD2  . TYR   B 1 152 ? 41.705 -24.239 -15.645 1.00 16.45 ?  152  TYR   B HD2  1 
ATOM   6413 H  HE1  . TYR   B 1 152 ? 39.506 -20.172 -15.816 1.00 16.82 ?  152  TYR   B HE1  1 
ATOM   6414 H  HE2  . TYR   B 1 152 ? 40.660 -23.584 -17.584 1.00 17.37 ?  152  TYR   B HE2  1 
ATOM   6415 H  HH   . TYR   B 1 152 ? 39.462 -22.037 -18.639 1.00 20.74 ?  152  TYR   B HH   1 
ATOM   6416 N  N    . LEU   B 1 153 ? 41.323 -25.716 -10.908 1.00 10.76 ?  153  LEU   B N    1 
ATOM   6417 C  CA   . LEU   B 1 153 ? 41.826 -26.465 -9.766  1.00 10.53 ?  153  LEU   B CA   1 
ATOM   6418 C  C    . LEU   B 1 153 ? 43.057 -27.270 -10.152 1.00 10.81 ?  153  LEU   B C    1 
ATOM   6419 O  O    . LEU   B 1 153 ? 43.041 -28.005 -11.144 1.00 12.27 ?  153  LEU   B O    1 
ATOM   6420 C  CB   . LEU   B 1 153 ? 40.748 -27.425 -9.256  1.00 11.15 ?  153  LEU   B CB   1 
ATOM   6421 C  CG   . LEU   B 1 153 ? 39.495 -26.778 -8.670  1.00 11.91 ?  153  LEU   B CG   1 
ATOM   6422 C  CD1  . LEU   B 1 153 ? 38.400 -27.829 -8.512  1.00 12.90 ?  153  LEU   B CD1  1 
ATOM   6423 C  CD2  . LEU   B 1 153 ? 39.796 -26.105 -7.340  1.00 12.24 ?  153  LEU   B CD2  1 
ATOM   6424 H  H    . LEU   B 1 153 ? 40.762 -26.166 -11.390 1.00 12.93 ?  153  LEU   B H    1 
ATOM   6425 H  HA   . LEU   B 1 153 ? 42.052 -25.851 -9.052  1.00 12.66 ?  153  LEU   B HA   1 
ATOM   6426 H  HB2  . LEU   B 1 153 ? 40.464 -27.985 -9.993  1.00 13.40 ?  153  LEU   B HB2  1 
ATOM   6427 H  HB3  . LEU   B 1 153 ? 41.136 -27.979 -8.560  1.00 13.40 ?  153  LEU   B HB3  1 
ATOM   6428 H  HG   . LEU   B 1 153 ? 39.167 -26.099 -9.281  1.00 14.32 ?  153  LEU   B HG   1 
ATOM   6429 H  HD11 . LEU   B 1 153 ? 37.597 -27.398 -8.175  1.00 15.51 ?  153  LEU   B HD11 1 
ATOM   6430 H  HD12 . LEU   B 1 153 ? 38.225 -28.230 -9.373  1.00 15.51 ?  153  LEU   B HD12 1 
ATOM   6431 H  HD13 . LEU   B 1 153 ? 38.703 -28.501 -7.882  1.00 15.51 ?  153  LEU   B HD13 1 
ATOM   6432 H  HD21 . LEU   B 1 153 ? 38.976 -25.746 -6.968  1.00 14.71 ?  153  LEU   B HD21 1 
ATOM   6433 H  HD22 . LEU   B 1 153 ? 40.177 -26.759 -6.733  1.00 14.71 ?  153  LEU   B HD22 1 
ATOM   6434 H  HD23 . LEU   B 1 153 ? 40.433 -25.385 -7.489  1.00 14.71 ?  153  LEU   B HD23 1 
ATOM   6435 N  N    . ALA   B 1 154 ? 44.107 -27.160 -9.342  1.00 11.24 ?  154  ALA   B N    1 
ATOM   6436 C  CA   . ALA   B 1 154 ? 45.333 -27.921 -9.528  1.00 11.98 ?  154  ALA   B CA   1 
ATOM   6437 C  C    . ALA   B 1 154 ? 45.397 -29.007 -8.461  1.00 12.46 ?  154  ALA   B C    1 
ATOM   6438 O  O    . ALA   B 1 154 ? 45.312 -28.716 -7.259  1.00 13.68 ?  154  ALA   B O    1 
ATOM   6439 C  CB   . ALA   B 1 154 ? 46.558 -27.014 -9.464  1.00 13.03 ?  154  ALA   B CB   1 
ATOM   6440 H  H    . ALA   B 1 154 ? 44.127 -26.630 -8.657  1.00 13.51 ?  154  ALA   B H    1 
ATOM   6441 H  HA   . ALA   B 1 154 ? 45.315 -28.346 -10.395 1.00 14.40 ?  154  ALA   B HA   1 
ATOM   6442 H  HB1  . ALA   B 1 154 ? 47.355 -27.549 -9.591  1.00 15.66 ?  154  ALA   B HB1  1 
ATOM   6443 H  HB2  . ALA   B 1 154 ? 46.493 -26.345 -10.166 1.00 15.66 ?  154  ALA   B HB2  1 
ATOM   6444 H  HB3  . ALA   B 1 154 ? 46.586 -26.577 -8.597  1.00 15.66 ?  154  ALA   B HB3  1 
ATOM   6445 N  N    . VAL   B 1 155 ? 45.531 -30.252 -8.901  1.00 11.88 ?  155  VAL   B N    1 
ATOM   6446 C  CA   . VAL   B 1 155 ? 45.630 -31.404 -8.014  1.00 12.07 ?  155  VAL   B CA   1 
ATOM   6447 C  C    . VAL   B 1 155 ? 46.969 -32.079 -8.288  1.00 11.99 ?  155  VAL   B C    1 
ATOM   6448 O  O    . VAL   B 1 155 ? 47.210 -32.569 -9.400  1.00 14.07 ?  155  VAL   B O    1 
ATOM   6449 C  CB   . VAL   B 1 155 ? 44.468 -32.390 -8.225  1.00 13.26 ?  155  VAL   B CB   1 
ATOM   6450 C  CG1  . VAL   B 1 155 ? 44.637 -33.598 -7.321  1.00 13.52 ?  155  VAL   B CG1  1 
ATOM   6451 C  CG2  . VAL   B 1 155 ? 43.124 -31.693 -7.973  1.00 14.55 ?  155  VAL   B CG2  1 
ATOM   6452 H  H    . VAL   B 1 155 ? 45.580 -30.461 -9.734  1.00 14.28 ?  155  VAL   B H    1 
ATOM   6453 H  HA   . VAL   B 1 155 ? 45.612 -31.112 -7.093  1.00 14.51 ?  155  VAL   B HA   1 
ATOM   6454 H  HB   . VAL   B 1 155 ? 44.471 -32.696 -9.149  1.00 15.93 ?  155  VAL   B HB   1 
ATOM   6455 H  HG11 . VAL   B 1 155 ? 43.803 -34.098 -7.299  1.00 16.25 ?  155  VAL   B HG11 1 
ATOM   6456 H  HG12 . VAL   B 1 155 ? 45.345 -34.162 -7.671  1.00 16.25 ?  155  VAL   B HG12 1 
ATOM   6457 H  HG13 . VAL   B 1 155 ? 44.862 -33.297 -6.428  1.00 16.25 ?  155  VAL   B HG13 1 
ATOM   6458 H  HG21 . VAL   B 1 155 ? 42.407 -32.336 -8.075  1.00 17.48 ?  155  VAL   B HG21 1 
ATOM   6459 H  HG22 . VAL   B 1 155 ? 43.122 -31.330 -7.074  1.00 17.48 ?  155  VAL   B HG22 1 
ATOM   6460 H  HG23 . VAL   B 1 155 ? 43.015 -30.972 -8.618  1.00 17.48 ?  155  VAL   B HG23 1 
ATOM   6461 N  N    . PHE   B 1 156 ? 47.835 -32.112 -7.271  1.00 12.50 ?  156  PHE   B N    1 
ATOM   6462 C  CA   . PHE   B 1 156 ? 49.212 -32.568 -7.464  1.00 13.76 ?  156  PHE   B CA   1 
ATOM   6463 C  C    . PHE   B 1 156 ? 49.313 -34.063 -7.757  1.00 14.41 ?  156  PHE   B C    1 
ATOM   6464 O  O    . PHE   B 1 156 ? 50.048 -34.479 -8.663  1.00 15.94 ?  156  PHE   B O    1 
ATOM   6465 C  CB   . PHE   B 1 156 ? 50.037 -32.207 -6.231  1.00 13.84 ?  156  PHE   B CB   1 
ATOM   6466 C  CG   . PHE   B 1 156 ? 51.462 -32.670 -6.292  1.00 14.39 ?  156  PHE   B CG   1 
ATOM   6467 C  CD1  . PHE   B 1 156 ? 52.353 -32.108 -7.193  1.00 16.16 ?  156  PHE   B CD1  1 
ATOM   6468 C  CD2  . PHE   B 1 156 ? 51.919 -33.655 -5.435  1.00 15.02 ?  156  PHE   B CD2  1 
ATOM   6469 C  CE1  . PHE   B 1 156 ? 53.672 -32.524 -7.245  1.00 17.32 ?  156  PHE   B CE1  1 
ATOM   6470 C  CE2  . PHE   B 1 156 ? 53.240 -34.074 -5.483  1.00 16.14 ?  156  PHE   B CE2  1 
ATOM   6471 C  CZ   . PHE   B 1 156 ? 54.112 -33.505 -6.391  1.00 16.92 ?  156  PHE   B CZ   1 
ATOM   6472 H  H    . PHE   B 1 156 ? 47.644 -31.878 -6.461  1.00 15.03 ?  156  PHE   B H    1 
ATOM   6473 H  HA   . PHE   B 1 156 ? 49.585 -32.092 -8.214  1.00 16.54 ?  156  PHE   B HA   1 
ATOM   6474 H  HB2  . PHE   B 1 156 ? 50.045 -31.243 -6.132  1.00 16.63 ?  156  PHE   B HB2  1 
ATOM   6475 H  HB3  . PHE   B 1 156 ? 49.630 -32.613 -5.448  1.00 16.63 ?  156  PHE   B HB3  1 
ATOM   6476 H  HD1  . PHE   B 1 156 ? 52.056 -31.437 -7.771  1.00 19.42 ?  156  PHE   B HD1  1 
ATOM   6477 H  HD2  . PHE   B 1 156 ? 51.333 -34.043 -4.824  1.00 18.04 ?  156  PHE   B HD2  1 
ATOM   6478 H  HE1  . PHE   B 1 156 ? 54.258 -32.135 -7.857  1.00 20.81 ?  156  PHE   B HE1  1 
ATOM   6479 H  HE2  . PHE   B 1 156 ? 53.539 -34.743 -4.909  1.00 19.39 ?  156  PHE   B HE2  1 
ATOM   6480 H  HZ   . PHE   B 1 156 ? 54.998 -33.789 -6.426  1.00 20.33 ?  156  PHE   B HZ   1 
ATOM   6481 N  N    . ASP   B 1 157 ? 48.638 -34.890 -6.973  1.00 14.39 ?  157  ASP   B N    1 
ATOM   6482 C  CA   . ASP   B 1 157 ? 48.789 -36.337 -7.075  1.00 15.60 ?  157  ASP   B CA   1 
ATOM   6483 C  C    . ASP   B 1 157 ? 47.871 -36.883 -8.164  1.00 15.95 ?  157  ASP   B C    1 
ATOM   6484 O  O    . ASP   B 1 157 ? 46.645 -36.756 -8.069  1.00 15.41 ?  157  ASP   B O    1 
ATOM   6485 C  CB   . ASP   B 1 157 ? 48.446 -36.961 -5.726  1.00 17.18 ?  157  ASP   B CB   1 
ATOM   6486 C  CG   . ASP   B 1 157 ? 48.557 -38.477 -5.725  1.00 18.88 ?  157  ASP   B CG   1 
ATOM   6487 O  OD1  . ASP   B 1 157 ? 48.911 -39.084 -6.762  1.00 19.67 ?  157  ASP   B OD1  1 
ATOM   6488 O  OD2  . ASP   B 1 157 ? 48.297 -39.070 -4.659  1.00 20.86 -1 157  ASP   B OD2  1 
ATOM   6489 H  H    . ASP   B 1 157 ? 48.076 -34.642 -6.379  1.00 17.29 ?  157  ASP   B H    1 
ATOM   6490 H  HA   . ASP   B 1 157 ? 49.707 -36.563 -7.298  1.00 18.75 ?  157  ASP   B HA   1 
ATOM   6491 H  HB2  . ASP   B 1 157 ? 49.044 -36.599 -5.053  1.00 20.64 ?  157  ASP   B HB2  1 
ATOM   6492 H  HB3  . ASP   B 1 157 ? 47.529 -36.735 -5.502  1.00 20.64 ?  157  ASP   B HB3  1 
ATOM   6493 N  N    A LYS   B 1 158 ? 48.469 -37.504 -9.187  0.30 16.79 ?  158  LYS   B N    1 
ATOM   6494 N  N    B LYS   B 1 158 ? 48.465 -37.502 -9.191  0.70 17.11 ?  158  LYS   B N    1 
ATOM   6495 C  CA   A LYS   B 1 158 ? 47.698 -38.096 -10.278 0.30 17.59 ?  158  LYS   B CA   1 
ATOM   6496 C  CA   B LYS   B 1 158 ? 47.685 -38.092 -10.280 0.70 18.10 ?  158  LYS   B CA   1 
ATOM   6497 C  C    A LYS   B 1 158 ? 46.638 -39.064 -9.761  0.30 17.42 ?  158  LYS   B C    1 
ATOM   6498 C  C    B LYS   B 1 158 ? 46.634 -39.070 -9.762  0.70 17.60 ?  158  LYS   B C    1 
ATOM   6499 O  O    A LYS   B 1 158 ? 45.531 -39.136 -10.308 0.30 17.15 ?  158  LYS   B O    1 
ATOM   6500 O  O    B LYS   B 1 158 ? 45.531 -39.161 -10.314 0.70 17.35 ?  158  LYS   B O    1 
ATOM   6501 C  CB   A LYS   B 1 158 ? 48.652 -38.803 -11.247 0.30 18.63 ?  158  LYS   B CB   1 
ATOM   6502 C  CB   B LYS   B 1 158 ? 48.632 -38.787 -11.266 0.70 19.61 ?  158  LYS   B CB   1 
ATOM   6503 C  CG   A LYS   B 1 158 ? 47.987 -39.720 -12.267 0.30 19.87 ?  158  LYS   B CG   1 
ATOM   6504 C  CG   B LYS   B 1 158 ? 47.955 -39.656 -12.320 0.70 21.21 ?  158  LYS   B CG   1 
ATOM   6505 C  CD   A LYS   B 1 158 ? 47.081 -38.958 -13.216 0.30 21.09 ?  158  LYS   B CD   1 
ATOM   6506 C  CD   B LYS   B 1 158 ? 47.089 -38.847 -13.265 0.70 23.07 ?  158  LYS   B CD   1 
ATOM   6507 C  CE   A LYS   B 1 158 ? 46.514 -39.877 -14.286 0.30 22.02 ?  158  LYS   B CE   1 
ATOM   6508 C  CE   B LYS   B 1 158 ? 46.528 -39.726 -14.373 0.70 24.48 ?  158  LYS   B CE   1 
ATOM   6509 N  NZ   A LYS   B 1 158 ? 45.456 -39.208 -15.092 0.30 22.17 ?  158  LYS   B NZ   1 
ATOM   6510 N  NZ   B LYS   B 1 158 ? 45.452 -39.041 -15.144 0.70 24.74 ?  158  LYS   B NZ   1 
ATOM   6511 H  H    A LYS   B 1 158 ? 49.322 -37.593 -9.270  0.30 20.17 ?  158  LYS   B H    1 
ATOM   6512 H  H    B LYS   B 1 158 ? 49.318 -37.596 -9.276  0.70 20.56 ?  158  LYS   B H    1 
ATOM   6513 H  HA   A LYS   B 1 158 ? 47.248 -37.391 -10.768 0.30 21.13 ?  158  LYS   B HA   1 
ATOM   6514 H  HA   B LYS   B 1 158 ? 47.230 -37.384 -10.759 0.70 21.75 ?  158  LYS   B HA   1 
ATOM   6515 H  HB2  A LYS   B 1 158 ? 49.145 -38.129 -11.745 0.30 22.38 ?  158  LYS   B HB2  1 
ATOM   6516 H  HB2  B LYS   B 1 158 ? 49.142 -38.108 -11.740 0.70 23.56 ?  158  LYS   B HB2  1 
ATOM   6517 H  HB3  A LYS   B 1 158 ? 49.274 -39.343 -10.734 0.30 22.38 ?  158  LYS   B HB3  1 
ATOM   6518 H  HB3  B LYS   B 1 158 ? 49.240 -39.356 -10.768 0.70 23.56 ?  158  LYS   B HB3  1 
ATOM   6519 H  HG2  A LYS   B 1 158 ? 48.677 -40.149 -12.797 0.30 23.87 ?  158  LYS   B HG2  1 
ATOM   6520 H  HG2  B LYS   B 1 158 ? 48.641 -40.095 -12.849 0.70 25.48 ?  158  LYS   B HG2  1 
ATOM   6521 H  HG3  A LYS   B 1 158 ? 47.459 -40.396 -11.813 0.30 23.87 ?  158  LYS   B HG3  1 
ATOM   6522 H  HG3  B LYS   B 1 158 ? 47.400 -40.326 -11.890 0.70 25.48 ?  158  LYS   B HG3  1 
ATOM   6523 H  HD2  A LYS   B 1 158 ? 46.342 -38.574 -12.719 0.30 25.34 ?  158  LYS   B HD2  1 
ATOM   6524 H  HD2  B LYS   B 1 158 ? 46.347 -38.462 -12.774 0.70 27.71 ?  158  LYS   B HD2  1 
ATOM   6525 H  HD3  A LYS   B 1 158 ? 47.591 -38.258 -13.655 0.30 25.34 ?  158  LYS   B HD3  1 
ATOM   6526 H  HD3  B LYS   B 1 158 ? 47.624 -38.147 -13.673 0.70 27.71 ?  158  LYS   B HD3  1 
ATOM   6527 H  HE2  A LYS   B 1 158 ? 47.226 -40.144 -14.887 0.30 26.44 ?  158  LYS   B HE2  1 
ATOM   6528 H  HE2  B LYS   B 1 158 ? 47.239 -39.958 -14.989 0.70 29.40 ?  158  LYS   B HE2  1 
ATOM   6529 H  HE3  A LYS   B 1 158 ? 46.124 -40.658 -13.863 0.30 26.44 ?  158  LYS   B HE3  1 
ATOM   6530 H  HE3  B LYS   B 1 158 ? 46.150 -40.530 -13.981 0.70 29.40 ?  158  LYS   B HE3  1 
ATOM   6531 H  HZ1  A LYS   B 1 158 ? 45.142 -39.768 -15.708 0.30 26.63 ?  158  LYS   B HZ1  1 
ATOM   6532 H  HZ1  B LYS   B 1 158 ? 45.143 -39.579 -15.782 0.70 29.71 ?  158  LYS   B HZ1  1 
ATOM   6533 H  HZ2  A LYS   B 1 158 ? 44.785 -38.954 -14.564 0.30 26.63 ?  158  LYS   B HZ2  1 
ATOM   6534 H  HZ2  B LYS   B 1 158 ? 44.780 -38.821 -14.601 0.70 29.71 ?  158  LYS   B HZ2  1 
ATOM   6535 H  HZ3  A LYS   B 1 158 ? 45.791 -38.489 -15.498 0.30 26.63 ?  158  LYS   B HZ3  1 
ATOM   6536 H  HZ3  B LYS   B 1 158 ? 45.772 -38.300 -15.520 0.70 29.71 ?  158  LYS   B HZ3  1 
ATOM   6537 N  N    . ASN   B 1 159 ? 46.959 -39.828 -8.714  1.00 17.76 ?  159  ASN   B N    1 
ATOM   6538 C  CA   . ASN   B 1 159 ? 46.006 -40.810 -8.203  1.00 18.51 ?  159  ASN   B CA   1 
ATOM   6539 C  C    . ASN   B 1 159 ? 44.806 -40.138 -7.537  1.00 17.77 ?  159  ASN   B C    1 
ATOM   6540 O  O    . ASN   B 1 159 ? 43.672 -40.621 -7.661  1.00 18.15 ?  159  ASN   B O    1 
ATOM   6541 C  CB   . ASN   B 1 159 ? 46.706 -41.782 -7.261  1.00 20.14 ?  159  ASN   B CB   1 
ATOM   6542 C  CG   . ASN   B 1 159 ? 47.732 -42.630 -7.976  1.00 22.44 ?  159  ASN   B CG   1 
ATOM   6543 O  OD1  . ASN   B 1 159 ? 47.478 -43.144 -9.070  1.00 23.51 ?  159  ASN   B OD1  1 
ATOM   6544 N  ND2  . ASN   B 1 159 ? 48.902 -42.783 -7.366  1.00 23.07 ?  159  ASN   B ND2  1 
ATOM   6545 H  H    A ASN   B 1 159 ? 47.706 -39.791 -8.291  0.30 21.34 ?  159  ASN   B H    1 
ATOM   6546 H  H    B ASN   B 1 159 ? 47.705 -39.788 -8.290  0.70 21.34 ?  159  ASN   B H    1 
ATOM   6547 H  HA   . ASN   B 1 159 ? 45.669 -41.321 -8.955  1.00 22.24 ?  159  ASN   B HA   1 
ATOM   6548 H  HB2  . ASN   B 1 159 ? 47.156 -41.286 -6.564  1.00 24.20 ?  159  ASN   B HB2  1 
ATOM   6549 H  HB3  . ASN   B 1 159 ? 46.043 -42.378 -6.875  1.00 24.20 ?  159  ASN   B HB3  1 
ATOM   6550 H  HD21 . ASN   B 1 159 ? 49.524 -43.258 -7.732  1.00 27.70 ?  159  ASN   B HD21 1 
ATOM   6551 H  HD22 . ASN   B 1 159 ? 49.043 -42.417 -6.601  1.00 27.70 ?  159  ASN   B HD22 1 
ATOM   6552 N  N    . LEU   B 1 160 ? 45.019 -39.012 -6.845  1.00 16.69 ?  160  LEU   B N    1 
ATOM   6553 C  CA   . LEU   B 1 160 ? 43.885 -38.278 -6.292  1.00 15.81 ?  160  LEU   B CA   1 
ATOM   6554 C  C    . LEU   B 1 160 ? 43.087 -37.609 -7.398  1.00 15.26 ?  160  LEU   B C    1 
ATOM   6555 O  O    . LEU   B 1 160 ? 41.849 -37.614 -7.371  1.00 14.92 ?  160  LEU   B O    1 
ATOM   6556 C  CB   . LEU   B 1 160 ? 44.349 -37.246 -5.266  1.00 15.56 ?  160  LEU   B CB   1 
ATOM   6557 C  CG   . LEU   B 1 160 ? 43.219 -36.354 -4.735  1.00 15.46 ?  160  LEU   B CG   1 
ATOM   6558 C  CD1  . LEU   B 1 160 ? 42.092 -37.179 -4.112  1.00 15.84 ?  160  LEU   B CD1  1 
ATOM   6559 C  CD2  . LEU   B 1 160 ? 43.754 -35.335 -3.732  1.00 16.03 ?  160  LEU   B CD2  1 
ATOM   6560 H  H    . LEU   B 1 160 ? 45.791 -38.659 -6.697  1.00 20.05 ?  160  LEU   B H    1 
ATOM   6561 H  HA   . LEU   B 1 160 ? 43.302 -38.904 -5.847  1.00 19.00 ?  160  LEU   B HA   1 
ATOM   6562 H  HB2  . LEU   B 1 160 ? 44.741 -37.715 -4.512  1.00 18.69 ?  160  LEU   B HB2  1 
ATOM   6563 H  HB3  . LEU   B 1 160 ? 45.017 -36.672 -5.677  1.00 18.69 ?  160  LEU   B HB3  1 
ATOM   6564 H  HG   . LEU   B 1 160 ? 42.842 -35.852 -5.474  1.00 18.57 ?  160  LEU   B HG   1 
ATOM   6565 H  HD11 . LEU   B 1 160 ? 41.459 -36.576 -3.693  1.00 19.04 ?  160  LEU   B HD11 1 
ATOM   6566 H  HD12 . LEU   B 1 160 ? 41.652 -37.689 -4.808  1.00 19.04 ?  160  LEU   B HD12 1 
ATOM   6567 H  HD13 . LEU   B 1 160 ? 42.469 -37.776 -3.448  1.00 19.04 ?  160  LEU   B HD13 1 
ATOM   6568 H  HD21 . LEU   B 1 160 ? 43.021 -34.773 -3.433  1.00 19.26 ?  160  LEU   B HD21 1 
ATOM   6569 H  HD22 . LEU   B 1 160 ? 44.141 -35.804 -2.979  1.00 19.26 ?  160  LEU   B HD22 1 
ATOM   6570 H  HD23 . LEU   B 1 160 ? 44.430 -34.789 -4.166  1.00 19.26 ?  160  LEU   B HD23 1 
ATOM   6571 N  N    . TYR   B 1 161 ? 43.781 -37.035 -8.385  1.00 15.35 ?  161  TYR   B N    1 
ATOM   6572 C  CA   . TYR   B 1 161 ? 43.105 -36.467 -9.546  1.00 15.02 ?  161  TYR   B CA   1 
ATOM   6573 C  C    . TYR   B 1 161 ? 42.163 -37.487 -10.172 1.00 14.89 ?  161  TYR   B C    1 
ATOM   6574 O  O    . TYR   B 1 161 ? 40.994 -37.189 -10.443 1.00 14.71 ?  161  TYR   B O    1 
ATOM   6575 C  CB   . TYR   B 1 161 ? 44.148 -35.983 -10.560 1.00 15.51 ?  161  TYR   B CB   1 
ATOM   6576 C  CG   . TYR   B 1 161 ? 43.574 -35.510 -11.874 1.00 15.69 ?  161  TYR   B CG   1 
ATOM   6577 C  CD1  . TYR   B 1 161 ? 43.202 -34.186 -12.048 1.00 15.49 ?  161  TYR   B CD1  1 
ATOM   6578 C  CD2  . TYR   B 1 161 ? 43.389 -36.389 -12.936 1.00 16.36 ?  161  TYR   B CD2  1 
ATOM   6579 C  CE1  . TYR   B 1 161 ? 42.672 -33.749 -13.234 1.00 16.59 ?  161  TYR   B CE1  1 
ATOM   6580 C  CE2  . TYR   B 1 161 ? 42.853 -35.959 -14.126 1.00 17.39 ?  161  TYR   B CE2  1 
ATOM   6581 C  CZ   . TYR   B 1 161 ? 42.498 -34.637 -14.273 1.00 17.29 ?  161  TYR   B CZ   1 
ATOM   6582 O  OH   . TYR   B 1 161 ? 41.964 -34.195 -15.455 1.00 19.06 ?  161  TYR   B OH   1 
ATOM   6583 H  H    . TYR   B 1 161 ? 44.636 -36.969 -8.411  1.00 18.44 ?  161  TYR   B H    1 
ATOM   6584 H  HA   . TYR   B 1 161 ? 42.577 -35.702 -9.271  1.00 18.05 ?  161  TYR   B HA   1 
ATOM   6585 H  HB2  . TYR   B 1 161 ? 44.638 -35.238 -10.174 1.00 18.64 ?  161  TYR   B HB2  1 
ATOM   6586 H  HB3  . TYR   B 1 161 ? 44.759 -36.709 -10.755 1.00 18.64 ?  161  TYR   B HB3  1 
ATOM   6587 H  HD1  . TYR   B 1 161 ? 43.324 -33.579 -11.353 1.00 18.62 ?  161  TYR   B HD1  1 
ATOM   6588 H  HD2  . TYR   B 1 161 ? 43.618 -37.285 -12.840 1.00 19.66 ?  161  TYR   B HD2  1 
ATOM   6589 H  HE1  . TYR   B 1 161 ? 42.438 -32.852 -13.335 1.00 19.94 ?  161  TYR   B HE1  1 
ATOM   6590 H  HE2  . TYR   B 1 161 ? 42.729 -36.559 -14.828 1.00 20.89 ?  161  TYR   B HE2  1 
ATOM   6591 H  HH   . TYR   B 1 161 ? 41.912 -34.837 -15.995 1.00 22.89 ?  161  TYR   B HH   1 
ATOM   6592 N  N    . ASP   B 1 162 ? 42.661 -38.704 -10.400 1.00 15.26 ?  162  ASP   B N    1 
ATOM   6593 C  CA   . ASP   B 1 162 ? 41.832 -39.736 -11.016 1.00 15.85 ?  162  ASP   B CA   1 
ATOM   6594 C  C    . ASP   B 1 162 ? 40.627 -40.075 -10.145 1.00 15.09 ?  162  ASP   B C    1 
ATOM   6595 O  O    . ASP   B 1 162 ? 39.523 -40.290 -10.658 1.00 15.47 ?  162  ASP   B O    1 
ATOM   6596 C  CB   . ASP   B 1 162 ? 42.659 -40.998 -11.286 1.00 17.51 ?  162  ASP   B CB   1 
ATOM   6597 C  CG   . ASP   B 1 162 ? 43.660 -40.828 -12.419 1.00 18.92 ?  162  ASP   B CG   1 
ATOM   6598 O  OD1  . ASP   B 1 162 ? 43.530 -39.873 -13.211 1.00 18.92 ?  162  ASP   B OD1  1 
ATOM   6599 O  OD2  . ASP   B 1 162 ? 44.564 -41.688 -12.530 1.00 20.55 -1 162  ASP   B OD2  1 
ATOM   6600 H  H    . ASP   B 1 162 ? 43.462 -38.955 -10.211 1.00 18.34 ?  162  ASP   B H    1 
ATOM   6601 H  HA   . ASP   B 1 162 ? 41.497 -39.410 -11.863 1.00 19.05 ?  162  ASP   B HA   1 
ATOM   6602 H  HB2  . ASP   B 1 162 ? 43.154 -41.231 -10.490 1.00 21.03 ?  162  ASP   B HB2  1 
ATOM   6603 H  HB3  . ASP   B 1 162 ? 42.058 -41.722 -11.530 1.00 21.03 ?  162  ASP   B HB3  1 
ATOM   6604 N  N    . LYS   B 1 163 ? 40.820 -40.150 -8.826  1.00 14.65 ?  163  LYS   B N    1 
ATOM   6605 C  CA   . LYS   B 1 163 ? 39.696 -40.427 -7.933  1.00 15.57 ?  163  LYS   B CA   1 
ATOM   6606 C  C    . LYS   B 1 163 ? 38.649 -39.321 -7.998  1.00 14.66 ?  163  LYS   B C    1 
ATOM   6607 O  O    . LYS   B 1 163 ? 37.440 -39.592 -8.007  1.00 15.51 ?  163  LYS   B O    1 
ATOM   6608 C  CB   . LYS   B 1 163 ? 40.191 -40.606 -6.498  1.00 18.59 ?  163  LYS   B CB   1 
ATOM   6609 C  CG   . LYS   B 1 163 ? 39.102 -41.078 -5.560  1.00 25.01 ?  163  LYS   B CG   1 
ATOM   6610 C  CD   . LYS   B 1 163 ? 39.606 -41.342 -4.155  1.00 31.54 ?  163  LYS   B CD   1 
ATOM   6611 C  CE   . LYS   B 1 163 ? 38.521 -42.019 -3.327  1.00 37.02 ?  163  LYS   B CE   1 
ATOM   6612 N  NZ   . LYS   B 1 163 ? 38.550 -41.598 -1.900  1.00 40.18 ?  163  LYS   B NZ   1 
ATOM   6613 H  H    . LYS   B 1 163 ? 41.577 -40.044 -8.431  1.00 17.61 ?  163  LYS   B H    1 
ATOM   6614 H  HA   . LYS   B 1 163 ? 39.275 -41.253 -8.207  1.00 18.71 ?  163  LYS   B HA   1 
ATOM   6615 H  HB2  . LYS   B 1 163 ? 40.903 -41.269 -6.488  1.00 22.33 ?  163  LYS   B HB2  1 
ATOM   6616 H  HB3  . LYS   B 1 163 ? 40.526 -39.759 -6.167  1.00 22.33 ?  163  LYS   B HB3  1 
ATOM   6617 H  HG2  . LYS   B 1 163 ? 38.413 -40.399 -5.506  1.00 30.03 ?  163  LYS   B HG2  1 
ATOM   6618 H  HG3  . LYS   B 1 163 ? 38.726 -41.906 -5.903  1.00 30.03 ?  163  LYS   B HG3  1 
ATOM   6619 H  HD2  . LYS   B 1 163 ? 40.378 -41.930 -4.192  1.00 37.87 ?  163  LYS   B HD2  1 
ATOM   6620 H  HD3  . LYS   B 1 163 ? 39.839 -40.502 -3.731  1.00 37.87 ?  163  LYS   B HD3  1 
ATOM   6621 H  HE2  . LYS   B 1 163 ? 37.652 -41.793 -3.694  1.00 44.45 ?  163  LYS   B HE2  1 
ATOM   6622 H  HE3  . LYS   B 1 163 ? 38.652 -42.980 -3.359  1.00 44.45 ?  163  LYS   B HE3  1 
ATOM   6623 H  HZ1  . LYS   B 1 163 ? 37.903 -42.011 -1.449  1.00 48.23 ?  163  LYS   B HZ1  1 
ATOM   6624 H  HZ2  . LYS   B 1 163 ? 39.335 -41.806 -1.538  1.00 48.23 ?  163  LYS   B HZ2  1 
ATOM   6625 H  HZ3  . LYS   B 1 163 ? 38.427 -40.718 -1.842  1.00 48.23 ?  163  LYS   B HZ3  1 
ATOM   6626 N  N    . LEU   B 1 164 ? 39.102 -38.068 -8.040  1.00 13.40 ?  164  LEU   B N    1 
ATOM   6627 C  CA   . LEU   B 1 164 ? 38.194 -36.927 -8.093  1.00 12.95 ?  164  LEU   B CA   1 
ATOM   6628 C  C    . LEU   B 1 164 ? 37.406 -36.900 -9.398  1.00 12.94 ?  164  LEU   B C    1 
ATOM   6629 O  O    . LEU   B 1 164 ? 36.182 -36.707 -9.396  1.00 14.19 ?  164  LEU   B O    1 
ATOM   6630 C  CB   . LEU   B 1 164 ? 38.994 -35.632 -7.937  1.00 12.66 ?  164  LEU   B CB   1 
ATOM   6631 C  CG   . LEU   B 1 164 ? 39.538 -35.372 -6.537  1.00 13.26 ?  164  LEU   B CG   1 
ATOM   6632 C  CD1  . LEU   B 1 164 ? 40.620 -34.306 -6.594  1.00 13.61 ?  164  LEU   B CD1  1 
ATOM   6633 C  CD2  . LEU   B 1 164 ? 38.441 -34.952 -5.579  1.00 15.18 ?  164  LEU   B CD2  1 
ATOM   6634 H  H    . LEU   B 1 164 ? 39.940 -37.847 -8.041  1.00 16.10 ?  164  LEU   B H    1 
ATOM   6635 H  HA   . LEU   B 1 164 ? 37.571 -36.984 -7.357  1.00 15.56 ?  164  LEU   B HA   1 
ATOM   6636 H  HB2  . LEU   B 1 164 ? 39.755 -35.660 -8.545  1.00 15.22 ?  164  LEU   B HB2  1 
ATOM   6637 H  HB3  . LEU   B 1 164 ? 38.425 -34.884 -8.171  1.00 15.22 ?  164  LEU   B HB3  1 
ATOM   6638 H  HG   . LEU   B 1 164 ? 39.946 -36.181 -6.198  1.00 15.94 ?  164  LEU   B HG   1 
ATOM   6639 H  HD11 . LEU   B 1 164 ? 40.957 -34.140 -5.696  1.00 16.36 ?  164  LEU   B HD11 1 
ATOM   6640 H  HD12 . LEU   B 1 164 ? 41.351 -34.618 -7.159  1.00 16.36 ?  164  LEU   B HD12 1 
ATOM   6641 H  HD13 . LEU   B 1 164 ? 40.251 -33.488 -6.961  1.00 16.36 ?  164  LEU   B HD13 1 
ATOM   6642 H  HD21 . LEU   B 1 164 ? 38.835 -34.727 -4.721  1.00 18.24 ?  164  LEU   B HD21 1 
ATOM   6643 H  HD22 . LEU   B 1 164 ? 37.981 -34.179 -5.942  1.00 18.24 ?  164  LEU   B HD22 1 
ATOM   6644 H  HD23 . LEU   B 1 164 ? 37.819 -35.688 -5.474  1.00 18.24 ?  164  LEU   B HD23 1 
ATOM   6645 N  N    . VAL   B 1 165 ? 38.094 -37.061 -10.528 1.00 14.17 ?  165  VAL   B N    1 
ATOM   6646 C  CA   . VAL   B 1 165 ? 37.434 -36.996 -11.826 1.00 15.54 ?  165  VAL   B CA   1 
ATOM   6647 C  C    . VAL   B 1 165 ? 36.527 -38.201 -12.019 1.00 17.27 ?  165  VAL   B C    1 
ATOM   6648 O  O    . VAL   B 1 165 ? 35.371 -38.068 -12.435 1.00 18.34 ?  165  VAL   B O    1 
ATOM   6649 C  CB   . VAL   B 1 165 ? 38.473 -36.896 -12.957 1.00 16.59 ?  165  VAL   B CB   1 
ATOM   6650 C  CG1  . VAL   B 1 165 ? 37.797 -37.000 -14.306 1.00 18.23 ?  165  VAL   B CG1  1 
ATOM   6651 C  CG2  . VAL   B 1 165 ? 39.265 -35.614 -12.841 1.00 16.50 ?  165  VAL   B CG2  1 
ATOM   6652 H  H    . VAL   B 1 165 ? 38.939 -37.207 -10.565 1.00 17.02 ?  165  VAL   B H    1 
ATOM   6653 H  HA   . VAL   B 1 165 ? 36.879 -36.203 -11.858 1.00 18.67 ?  165  VAL   B HA   1 
ATOM   6654 H  HB   . VAL   B 1 165 ? 39.096 -37.634 -12.873 1.00 19.93 ?  165  VAL   B HB   1 
ATOM   6655 H  HG11 . VAL   B 1 165 ? 38.398 -36.667 -14.985 1.00 21.90 ?  165  VAL   B HG11 1 
ATOM   6656 H  HG12 . VAL   B 1 165 ? 37.590 -37.934 -14.480 1.00 21.90 ?  165  VAL   B HG12 1 
ATOM   6657 H  HG13 . VAL   B 1 165 ? 36.981 -36.478 -14.293 1.00 21.90 ?  165  VAL   B HG13 1 
ATOM   6658 H  HG21 . VAL   B 1 165 ? 39.897 -35.563 -13.574 1.00 19.83 ?  165  VAL   B HG21 1 
ATOM   6659 H  HG22 . VAL   B 1 165 ? 38.655 -34.858 -12.879 1.00 19.83 ?  165  VAL   B HG22 1 
ATOM   6660 H  HG23 . VAL   B 1 165 ? 39.741 -35.606 -11.994 1.00 19.83 ?  165  VAL   B HG23 1 
ATOM   6661 N  N    . SER   B 1 166 ? 37.047 -39.401 -11.730 1.00 18.31 ?  166  SER   B N    1 
ATOM   6662 C  CA   . SER   B 1 166 ? 36.299 -40.618 -12.018 1.00 19.74 ?  166  SER   B CA   1 
ATOM   6663 C  C    . SER   B 1 166 ? 35.031 -40.707 -11.184 1.00 19.99 ?  166  SER   B C    1 
ATOM   6664 O  O    . SER   B 1 166 ? 34.061 -41.332 -11.617 1.00 21.16 ?  166  SER   B O    1 
ATOM   6665 C  CB   . SER   B 1 166 ? 37.172 -41.869 -11.830 1.00 20.84 ?  166  SER   B CB   1 
ATOM   6666 O  OG   . SER   B 1 166 ? 37.499 -42.094 -10.469 1.00 21.15 ?  166  SER   B OG   1 
ATOM   6667 H  H    . SER   B 1 166 ? 37.823 -39.531 -11.378 1.00 21.99 ?  166  SER   B H    1 
ATOM   6668 H  HA   . SER   B 1 166 ? 36.034 -40.600 -12.949 1.00 23.72 ?  166  SER   B HA   1 
ATOM   6669 H  HB2  . SER   B 1 166 ? 36.693 -42.640 -12.168 1.00 25.03 ?  166  SER   B HB2  1 
ATOM   6670 H  HB3  . SER   B 1 166 ? 37.998 -41.752 -12.330 1.00 25.03 ?  166  SER   B HB3  1 
ATOM   6671 H  HG   . SER   B 1 166 ? 37.916 -41.432 -10.161 1.00 25.40 ?  166  SER   B HG   1 
ATOM   6672 N  N    . SER   B 1 167 ? 35.004 -40.090 -10.002 1.00 18.76 ?  167  SER   B N    1 
ATOM   6673 C  CA   . SER   B 1 167 ? 33.848 -40.156 -9.115  1.00 18.28 ?  167  SER   B CA   1 
ATOM   6674 C  C    . SER   B 1 167 ? 32.933 -38.934 -9.199  1.00 17.77 ?  167  SER   B C    1 
ATOM   6675 O  O    . SER   B 1 167 ? 31.865 -38.933 -8.577  1.00 17.83 ?  167  SER   B O    1 
ATOM   6676 C  CB   . SER   B 1 167 ? 34.293 -40.347 -7.659  1.00 17.79 ?  167  SER   B CB   1 
ATOM   6677 O  OG   . SER   B 1 167 ? 34.955 -39.186 -7.167  1.00 17.09 ?  167  SER   B OG   1 
ATOM   6678 H  H    . SER   B 1 167 ? 35.652 -39.625 -9.693  1.00 22.54 ?  167  SER   B H    1 
ATOM   6679 H  HA   . SER   B 1 167 ? 33.320 -40.932 -9.360  1.00 21.96 ?  167  SER   B HA   1 
ATOM   6680 H  HB2  . SER   B 1 167 ? 33.508 -40.522 -7.115  1.00 21.37 ?  167  SER   B HB2  1 
ATOM   6681 H  HB3  . SER   B 1 167 ? 34.895 -41.111 -7.616  1.00 21.37 ?  167  SER   B HB3  1 
ATOM   6682 H  HG   . SER   B 1 167 ? 35.645 -39.043 -7.625  1.00 20.53 ?  167  SER   B HG   1 
ATOM   6683 N  N    . PHE   B 1 168 ? 33.313 -37.895 -9.944  1.00 17.49 ?  168  PHE   B N    1 
ATOM   6684 C  CA   . PHE   B 1 168 ? 32.482 -36.691 -9.996  1.00 16.98 ?  168  PHE   B CA   1 
ATOM   6685 C  C    . PHE   B 1 168 ? 31.160 -36.948 -10.716 1.00 14.88 ?  168  PHE   B C    1 
ATOM   6686 O  O    . PHE   B 1 168 ? 30.126 -36.348 -10.370 1.00 15.51 ?  168  PHE   B O    1 
ATOM   6687 C  CB   . PHE   B 1 168 ? 33.240 -35.551 -10.673 1.00 17.58 ?  168  PHE   B CB   1 
ATOM   6688 C  CG   . PHE   B 1 168 ? 32.432 -34.304 -10.806 1.00 17.68 ?  168  PHE   B CG   1 
ATOM   6689 C  CD1  . PHE   B 1 168 ? 32.088 -33.570 -9.681  1.00 19.20 ?  168  PHE   B CD1  1 
ATOM   6690 C  CD2  . PHE   B 1 168 ? 31.989 -33.877 -12.039 1.00 17.12 ?  168  PHE   B CD2  1 
ATOM   6691 C  CE1  . PHE   B 1 168 ? 31.325 -32.423 -9.787  1.00 19.68 ?  168  PHE   B CE1  1 
ATOM   6692 C  CE2  . PHE   B 1 168 ? 31.241 -32.717 -12.159 1.00 18.28 ?  168  PHE   B CE2  1 
ATOM   6693 C  CZ   . PHE   B 1 168 ? 30.900 -31.990 -11.027 1.00 18.88 ?  168  PHE   B CZ   1 
ATOM   6694 H  H    . PHE   B 1 168 ? 34.039 -37.856 -10.409 1.00 21.02 ?  168  PHE   B H    1 
ATOM   6695 H  HA   . PHE   B 1 168 ? 32.275 -36.416 -9.094  1.00 20.40 ?  168  PHE   B HA   1 
ATOM   6696 H  HB2  . PHE   B 1 168 ? 34.024 -35.341 -10.143 1.00 21.12 ?  168  PHE   B HB2  1 
ATOM   6697 H  HB3  . PHE   B 1 168 ? 33.503 -35.829 -11.561 1.00 21.12 ?  168  PHE   B HB3  1 
ATOM   6698 H  HD1  . PHE   B 1 168 ? 32.366 -33.860 -8.843  1.00 23.07 ?  168  PHE   B HD1  1 
ATOM   6699 H  HD2  . PHE   B 1 168 ? 32.216 -34.352 -12.802 1.00 20.57 ?  168  PHE   B HD2  1 
ATOM   6700 H  HE1  . PHE   B 1 168 ? 31.100 -31.939 -9.023  1.00 23.64 ?  168  PHE   B HE1  1 
ATOM   6701 H  HE2  . PHE   B 1 168 ? 30.948 -32.429 -12.996 1.00 21.97 ?  168  PHE   B HE2  1 
ATOM   6702 H  HZ   . PHE   B 1 168 ? 30.385 -31.215 -11.105 1.00 22.68 ?  168  PHE   B HZ   1 
ATOM   6703 N  N    . LEU   B 1 169 ? 31.178 -37.833 -11.709 1.00 14.70 ?  169  LEU   B N    1 
ATOM   6704 C  CA   . LEU   B 1 169 ? 29.988 -38.141 -12.493 1.00 17.31 ?  169  LEU   B CA   1 
ATOM   6705 C  C    . LEU   B 1 169 ? 29.976 -39.575 -12.991 1.00 20.34 ?  169  LEU   B C    1 
ATOM   6706 O  O    . LEU   B 1 169 ? 29.044 -39.998 -13.673 1.00 22.87 ?  169  LEU   B O    1 
ATOM   6707 C  CB   . LEU   B 1 169 ? 29.904 -37.207 -13.697 1.00 19.19 ?  169  LEU   B CB   1 
ATOM   6708 C  CG   . LEU   B 1 169 ? 28.675 -36.305 -13.772 1.00 22.56 ?  169  LEU   B CG   1 
ATOM   6709 C  CD1  . LEU   B 1 169 ? 28.630 -35.608 -15.116 1.00 23.46 ?  169  LEU   B CD1  1 
ATOM   6710 C  CD2  . LEU   B 1 169 ? 27.402 -37.090 -13.529 1.00 22.90 ?  169  LEU   B CD2  1 
ATOM   6711 O  OXT  . LEU   B 1 169 ? 30.903 -40.331 -12.738 1.00 21.14 -1 169  LEU   B OXT  1 
ATOM   6712 H  H    . LEU   B 1 169 ? 31.879 -38.270 -11.958 1.00 17.66 ?  169  LEU   B H    1 
ATOM   6713 H  HA   . LEU   B 1 169 ? 29.208 -38.007 -11.937 1.00 20.79 ?  169  LEU   B HA   1 
ATOM   6714 H  HB2  . LEU   B 1 169 ? 30.684 -36.630 -13.694 1.00 23.06 ?  169  LEU   B HB2  1 
ATOM   6715 H  HB3  . LEU   B 1 169 ? 29.909 -37.747 -14.503 1.00 23.06 ?  169  LEU   B HB3  1 
ATOM   6716 H  HG   . LEU   B 1 169 ? 28.744 -35.622 -13.085 1.00 27.10 ?  169  LEU   B HG   1 
ATOM   6717 H  HD11 . LEU   B 1 169 ? 27.860 -35.020 -15.140 1.00 28.17 ?  169  LEU   B HD11 1 
ATOM   6718 H  HD12 . LEU   B 1 169 ? 29.444 -35.093 -15.231 1.00 28.17 ?  169  LEU   B HD12 1 
ATOM   6719 H  HD13 . LEU   B 1 169 ? 28.560 -36.277 -15.814 1.00 28.17 ?  169  LEU   B HD13 1 
ATOM   6720 H  HD21 . LEU   B 1 169 ? 26.659 -36.628 -13.942 1.00 27.51 ?  169  LEU   B HD21 1 
ATOM   6721 H  HD22 . LEU   B 1 169 ? 27.499 -37.976 -13.919 1.00 27.51 ?  169  LEU   B HD22 1 
ATOM   6722 H  HD23 . LEU   B 1 169 ? 27.258 -37.167 -12.574 1.00 27.51 ?  169  LEU   B HD23 1 
HETATM 6723 N  N2   B A1A92 C 2 .   ? 15.014 -0.135  3.905   0.70 12.07 ?  201  A1A92 A N2   1 
HETATM 6724 C  C3   B A1A92 C 2 .   ? 13.891 0.484   -0.166  0.70 13.47 ?  201  A1A92 A C3   1 
HETATM 6725 C  C6   B A1A92 C 2 .   ? 15.090 1.082   3.265   0.70 11.60 ?  201  A1A92 A C6   1 
HETATM 6726 C  C9   B A1A92 C 2 .   ? 15.278 2.259   4.054   0.70 11.24 ?  201  A1A92 A C9   1 
HETATM 6727 C  C1   B A1A92 C 2 .   ? 15.868 -0.847  0.634   0.70 13.82 ?  201  A1A92 A C1   1 
HETATM 6728 C  C10  B A1A92 C 2 .   ? 15.438 3.677   3.894   0.70 11.69 ?  201  A1A92 A C10  1 
HETATM 6729 C  C11  B A1A92 C 2 .   ? 15.579 4.265   5.132   0.70 11.83 ?  201  A1A92 A C11  1 
HETATM 6730 C  C2   B A1A92 C 2 .   ? 14.595 -0.083  1.076   0.70 12.67 ?  201  A1A92 A C2   1 
HETATM 6731 C  C4   B A1A92 C 2 .   ? 14.372 1.922   -0.284  0.70 13.15 ?  201  A1A92 A C4   1 
HETATM 6732 C  C5   B A1A92 C 2 .   ? 14.818 2.314   1.109   0.70 12.82 ?  201  A1A92 A C5   1 
HETATM 6733 C  C7   B A1A92 C 2 .   ? 15.081 -0.157  5.272   0.70 12.01 ?  201  A1A92 A C7   1 
HETATM 6734 C  C8   B A1A92 C 2 .   ? 15.326 2.041   5.416   0.70 11.06 ?  201  A1A92 A C8   1 
HETATM 6735 N  N1   B A1A92 C 2 .   ? 15.000 1.083   1.895   0.70 11.86 ?  201  A1A92 A N1   1 
HETATM 6736 N  N3   B A1A92 C 2 .   ? 15.233 0.862   6.115   0.70 11.63 ?  201  A1A92 A N3   1 
HETATM 6737 N  N4   B A1A92 C 2 .   ? 15.503 3.250   6.136   0.70 11.74 ?  201  A1A92 A N4   1 
HETATM 6738 O  O1   B A1A92 C 2 .   ? 15.488 -1.909  -0.174  0.70 14.80 ?  201  A1A92 A O1   1 
HETATM 6739 H  H5   B A1A92 C 2 .   ? 14.109 -0.093  -1.082  0.70 16.19 ?  201  A1A92 A H5   1 
HETATM 6740 H  H6   B A1A92 C 2 .   ? 12.784 0.407   -0.133  0.70 16.19 ?  201  A1A92 A H6   1 
HETATM 6741 H  H3   B A1A92 C 2 .   ? 16.570 -0.174  0.089   0.70 16.61 ?  201  A1A92 A H3   1 
HETATM 6742 H  H4   B A1A92 C 2 .   ? 16.403 -1.222  1.524   0.70 16.61 ?  201  A1A92 A H4   1 
HETATM 6743 H  H12  B A1A92 C 2 .   ? 15.445 4.261   3.002   0.70 14.05 ?  201  A1A92 A H12  1 
HETATM 6744 H  H13  B A1A92 C 2 .   ? 15.713 5.256   5.546   0.70 14.22 ?  201  A1A92 A H13  1 
HETATM 6745 H  H1   B A1A92 C 2 .   ? 13.887 -0.751  1.626   0.70 15.22 ?  201  A1A92 A H1   1 
HETATM 6746 H  H7   B A1A92 C 2 .   ? 13.592 2.602   -0.713  0.70 15.80 ?  201  A1A92 A H7   1 
HETATM 6747 H  H8   B A1A92 C 2 .   ? 15.166 2.035   -1.048  0.70 15.80 ?  201  A1A92 A H8   1 
HETATM 6748 H  H10  B A1A92 C 2 .   ? 14.049 2.966   1.562   0.70 15.41 ?  201  A1A92 A H10  1 
HETATM 6749 H  H9   B A1A92 C 2 .   ? 15.732 2.952   1.052   0.70 15.41 ?  201  A1A92 A H9   1 
HETATM 6750 H  H11  B A1A92 C 2 .   ? 14.997 -1.110  5.855   0.70 14.44 ?  201  A1A92 A H11  1 
HETATM 6751 H  H14  B A1A92 C 2 .   ? 15.586 3.343   7.101   0.70 14.11 ?  201  A1A92 A H14  1 
HETATM 6752 H  H2   B A1A92 C 2 .   ? 16.269 -2.438  -0.354  0.70 17.78 ?  201  A1A92 A H2   1 
HETATM 6753 CL CL   B CL    D 3 .   ? 18.210 2.101   -1.126  0.70 13.60 ?  202  CL    A CL   1 
HETATM 6754 O  O    . HOH   E 4 .   ? 11.722 -10.836 -9.978  1.00 49.27 ?  1301 HOH   A O    1 
HETATM 6755 O  O    . HOH   E 4 .   ? 14.740 -4.684  20.492  1.00 42.04 ?  1302 HOH   A O    1 
HETATM 6756 O  O    . HOH   E 4 .   ? 28.926 0.358   -9.764  1.00 19.72 ?  1303 HOH   A O    1 
HETATM 6757 O  O    . HOH   E 4 .   ? 15.181 -12.313 18.723  1.00 41.85 ?  1304 HOH   A O    1 
HETATM 6758 O  O    . HOH   E 4 .   ? 34.432 -1.811  12.585  1.00 37.07 ?  1305 HOH   A O    1 
HETATM 6759 O  O    . HOH   E 4 .   ? 28.384 -0.248  -13.433 1.00 32.70 ?  1306 HOH   A O    1 
HETATM 6760 O  O    . HOH   E 4 .   ? 11.008 1.531   12.466  1.00 21.61 ?  1307 HOH   A O    1 
HETATM 6761 O  O    . HOH   E 4 .   ? 4.765  3.863   0.535   1.00 26.52 ?  1308 HOH   A O    1 
HETATM 6762 O  O    . HOH   E 4 .   ? 28.286 -6.315  19.610  1.00 43.83 ?  1309 HOH   A O    1 
HETATM 6763 O  O    B HOH   E 4 .   ? 14.911 6.996   7.513   0.70 22.06 ?  1310 HOH   A O    1 
HETATM 6764 O  O    . HOH   E 4 .   ? 9.179  -10.225 19.374  1.00 42.17 ?  1311 HOH   A O    1 
HETATM 6765 O  O    . HOH   E 4 .   ? 25.783 -0.964  -7.535  1.00 17.22 ?  1312 HOH   A O    1 
HETATM 6766 O  O    . HOH   E 4 .   ? 14.883 3.839   17.552  1.00 36.87 ?  1313 HOH   A O    1 
HETATM 6767 O  O    . HOH   E 4 .   ? 14.734 -13.998 16.770  1.00 24.42 ?  1314 HOH   A O    1 
HETATM 6768 O  O    . HOH   E 4 .   ? 14.233 -4.538  -11.873 1.00 40.66 ?  1315 HOH   A O    1 
HETATM 6769 O  O    . HOH   E 4 .   ? -0.375 -3.039  3.055   1.00 44.36 ?  1316 HOH   A O    1 
HETATM 6770 O  O    . HOH   E 4 .   ? 17.296 -18.101 15.108  1.00 27.05 ?  1317 HOH   A O    1 
HETATM 6771 O  O    . HOH   E 4 .   ? 0.794  -4.845  0.165   1.00 34.44 ?  1318 HOH   A O    1 
HETATM 6772 O  O    . HOH   E 4 .   ? 30.350 -13.329 -8.475  1.00 20.08 ?  1319 HOH   A O    1 
HETATM 6773 O  O    . HOH   E 4 .   ? 42.400 10.586  5.239   1.00 19.91 ?  1320 HOH   A O    1 
HETATM 6774 O  O    . HOH   E 4 .   ? 12.048 0.259   14.743  1.00 34.63 ?  1321 HOH   A O    1 
HETATM 6775 O  O    . HOH   E 4 .   ? 23.940 -15.839 -9.144  1.00 33.82 ?  1322 HOH   A O    1 
HETATM 6776 O  O    . HOH   E 4 .   ? 36.224 -5.079  -0.516  1.00 28.31 ?  1323 HOH   A O    1 
HETATM 6777 O  O    B HOH   E 4 .   ? 19.183 -0.484  -2.563  0.70 19.90 ?  1324 HOH   A O    1 
HETATM 6778 O  O    . HOH   E 4 .   ? 22.387 5.320   19.053  1.00 45.18 ?  1325 HOH   A O    1 
HETATM 6779 O  O    . HOH   E 4 .   ? 31.073 -18.166 7.817   1.00 18.52 ?  1326 HOH   A O    1 
HETATM 6780 O  O    B HOH   E 4 .   ? 11.203 6.398   8.964   0.70 29.75 ?  1327 HOH   A O    1 
HETATM 6781 O  O    . HOH   E 4 .   ? 20.033 -12.697 -8.800  1.00 25.17 ?  1328 HOH   A O    1 
HETATM 6782 O  O    . HOH   E 4 .   ? 37.512 2.837   10.273  1.00 26.76 ?  1329 HOH   A O    1 
HETATM 6783 O  O    A HOH   E 4 .   ? 17.536 -1.784  0.451   0.30 14.44 ?  1330 HOH   A O    1 
HETATM 6784 O  O    . HOH   E 4 .   ? 34.055 -1.070  -8.916  1.00 25.61 ?  1331 HOH   A O    1 
HETATM 6785 O  O    B HOH   E 4 .   ? 13.268 -3.209  -0.938  0.70 22.79 ?  1332 HOH   A O    1 
HETATM 6786 O  O    . HOH   E 4 .   ? 18.792 -19.392 13.611  1.00 29.75 ?  1333 HOH   A O    1 
HETATM 6787 O  O    . HOH   E 4 .   ? 19.013 -22.034 6.850   1.00 28.03 ?  1334 HOH   A O    1 
HETATM 6788 O  O    . HOH   E 4 .   ? 22.615 -12.008 21.940  1.00 53.14 ?  1335 HOH   A O    1 
HETATM 6789 O  O    A HOH   E 4 .   ? 21.289 -2.456  -2.042  0.30 8.27  ?  1336 HOH   A O    1 
HETATM 6790 O  O    . HOH   E 4 .   ? 44.255 7.108   6.449   1.00 26.00 ?  1337 HOH   A O    1 
HETATM 6791 O  O    . HOH   E 4 .   ? 38.555 4.976   6.957   1.00 15.86 ?  1338 HOH   A O    1 
HETATM 6792 O  O    . HOH   E 4 .   ? 26.759 11.339  1.669   1.00 14.38 ?  1339 HOH   A O    1 
HETATM 6793 O  O    . HOH   E 4 .   ? 5.242  2.396   5.032   1.00 33.58 ?  1340 HOH   A O    1 
HETATM 6794 O  O    . HOH   E 4 .   ? 20.695 -19.771 -5.071  1.00 26.42 ?  1341 HOH   A O    1 
HETATM 6795 O  O    . HOH   E 4 .   ? 22.335 -19.359 11.390  1.00 32.31 ?  1342 HOH   A O    1 
HETATM 6796 O  O    . HOH   E 4 .   ? 27.273 13.700  2.860   1.00 26.91 ?  1343 HOH   A O    1 
HETATM 6797 O  O    B HOH   E 4 .   ? 14.996 -2.852  3.329   0.70 13.36 ?  1344 HOH   A O    1 
HETATM 6798 O  O    . HOH   E 4 .   ? 37.276 11.945  4.974   1.00 31.57 ?  1345 HOH   A O    1 
HETATM 6799 O  O    . HOH   E 4 .   ? 14.427 -24.785 11.628  1.00 35.97 ?  1346 HOH   A O    1 
HETATM 6800 O  O    . HOH   E 4 .   ? -0.781 -8.671  2.199   1.00 45.50 ?  1347 HOH   A O    1 
HETATM 6801 O  O    A HOH   E 4 .   ? 9.867  -21.433 5.719   0.30 10.65 ?  1348 HOH   A O    1 
HETATM 6802 O  O    . HOH   E 4 .   ? 31.681 8.210   14.828  1.00 23.61 ?  1349 HOH   A O    1 
HETATM 6803 O  O    . HOH   E 4 .   ? 8.038  -13.027 -0.936  1.00 24.63 ?  1350 HOH   A O    1 
HETATM 6804 O  O    B HOH   E 4 .   ? 9.256  2.153   7.766   0.70 31.99 ?  1351 HOH   A O    1 
HETATM 6805 O  O    . HOH   E 4 .   ? 38.275 10.141  7.161   1.00 39.05 ?  1352 HOH   A O    1 
HETATM 6806 O  O    . HOH   E 4 .   ? 14.497 -21.305 -4.345  1.00 26.32 ?  1353 HOH   A O    1 
HETATM 6807 O  O    . HOH   E 4 .   ? 10.364 -22.171 -1.241  1.00 58.83 ?  1354 HOH   A O    1 
HETATM 6808 O  O    . HOH   E 4 .   ? 35.869 -12.693 6.845   1.00 15.16 ?  1355 HOH   A O    1 
HETATM 6809 O  O    . HOH   E 4 .   ? 39.760 -1.006  -5.231  1.00 20.25 ?  1356 HOH   A O    1 
HETATM 6810 O  O    . HOH   E 4 .   ? 24.085 -2.199  -2.157  1.00 10.61 ?  1357 HOH   A O    1 
HETATM 6811 O  O    . HOH   E 4 .   ? 7.663  -6.362  -6.629  1.00 42.51 ?  1358 HOH   A O    1 
HETATM 6812 O  O    . HOH   E 4 .   ? 38.073 -1.293  -1.956  1.00 17.81 ?  1359 HOH   A O    1 
HETATM 6813 O  O    . HOH   E 4 .   ? 42.451 4.229   5.237   1.00 30.50 ?  1360 HOH   A O    1 
HETATM 6814 O  O    A HOH   E 4 .   ? 14.309 0.490   6.810   0.30 21.23 ?  1361 HOH   A O    1 
HETATM 6815 O  O    . HOH   E 4 .   ? 30.787 3.085   8.285   1.00 11.46 ?  1362 HOH   A O    1 
HETATM 6816 O  O    . HOH   E 4 .   ? 43.873 8.466   -3.091  1.00 25.38 ?  1363 HOH   A O    1 
HETATM 6817 O  O    . HOH   E 4 .   ? 31.172 -13.964 -2.429  1.00 12.67 ?  1364 HOH   A O    1 
HETATM 6818 O  O    . HOH   E 4 .   ? 17.275 -17.874 -5.027  1.00 26.88 ?  1365 HOH   A O    1 
HETATM 6819 O  O    . HOH   E 4 .   ? 33.720 -7.169  4.337   1.00 15.60 ?  1366 HOH   A O    1 
HETATM 6820 O  O    . HOH   E 4 .   ? 18.484 9.423   8.855   1.00 21.26 ?  1367 HOH   A O    1 
HETATM 6821 O  O    . HOH   E 4 .   ? -1.376 -5.174  7.496   1.00 37.68 ?  1368 HOH   A O    1 
HETATM 6822 O  O    A HOH   E 4 .   ? 3.654  -9.572  9.727   0.30 22.43 ?  1369 HOH   A O    1 
HETATM 6823 O  O    A HOH   E 4 .   ? 14.679 -3.733  3.103   0.30 15.20 ?  1370 HOH   A O    1 
HETATM 6824 O  O    . HOH   E 4 .   ? 13.477 -1.427  -6.666  1.00 19.38 ?  1371 HOH   A O    1 
HETATM 6825 O  O    B HOH   E 4 .   ? 21.238 -2.165  -2.792  0.70 15.20 ?  1372 HOH   A O    1 
HETATM 6826 O  O    . HOH   E 4 .   ? 27.554 -10.644 14.111  1.00 16.36 ?  1373 HOH   A O    1 
HETATM 6827 O  O    . HOH   E 4 .   ? 16.651 -22.129 1.016   1.00 28.76 ?  1374 HOH   A O    1 
HETATM 6828 O  O    . HOH   E 4 .   ? 43.326 7.840   2.656   1.00 24.93 ?  1375 HOH   A O    1 
HETATM 6829 O  O    . HOH   E 4 .   ? 8.432  -21.366 4.073   1.00 53.81 ?  1376 HOH   A O    1 
HETATM 6830 O  O    A HOH   E 4 .   ? 7.000  -8.266  11.847  0.30 12.67 ?  1377 HOH   A O    1 
HETATM 6831 O  O    . HOH   E 4 .   ? 31.967 -7.332  -9.790  1.00 21.11 ?  1378 HOH   A O    1 
HETATM 6832 O  O    . HOH   E 4 .   ? 17.132 -19.365 4.901   1.00 13.92 ?  1379 HOH   A O    1 
HETATM 6833 O  O    . HOH   E 4 .   ? 21.989 -21.975 8.469   1.00 28.09 ?  1380 HOH   A O    1 
HETATM 6834 O  O    . HOH   E 4 .   ? 22.762 12.476  1.602   1.00 13.48 ?  1381 HOH   A O    1 
HETATM 6835 O  O    . HOH   E 4 .   ? 8.766  -12.005 17.240  1.00 33.10 ?  1382 HOH   A O    1 
HETATM 6836 O  O    A HOH   E 4 .   ? 20.128 4.487   -7.529  0.30 17.43 ?  1383 HOH   A O    1 
HETATM 6837 O  O    . HOH   E 4 .   ? 21.153 10.105  15.053  1.00 36.07 ?  1384 HOH   A O    1 
HETATM 6838 O  O    . HOH   E 4 .   ? 37.337 -2.937  9.682   1.00 43.72 ?  1385 HOH   A O    1 
HETATM 6839 O  O    B HOH   E 4 .   ? 22.709 5.801   -1.819  0.70 18.36 ?  1386 HOH   A O    1 
HETATM 6840 O  O    B HOH   E 4 .   ? 21.182 2.718   -0.027  0.70 14.64 ?  1387 HOH   A O    1 
HETATM 6841 O  O    . HOH   E 4 .   ? 6.416  -5.737  11.064  1.00 20.53 ?  1388 HOH   A O    1 
HETATM 6842 O  O    A HOH   E 4 .   ? 24.121 3.908   -4.899  0.30 13.90 ?  1389 HOH   A O    1 
HETATM 6843 O  O    B HOH   E 4 .   ? 10.958 -1.181  1.720   0.70 17.74 ?  1390 HOH   A O    1 
HETATM 6844 O  O    . HOH   E 4 .   ? 13.577 -15.371 -7.411  1.00 26.01 ?  1391 HOH   A O    1 
HETATM 6845 O  O    . HOH   E 4 .   ? 24.595 1.893   -7.177  1.00 24.20 ?  1392 HOH   A O    1 
HETATM 6846 O  O    . HOH   E 4 .   ? 13.943 -4.992  17.462  1.00 26.79 ?  1393 HOH   A O    1 
HETATM 6847 O  O    . HOH   E 4 .   ? 30.652 1.877   16.734  1.00 21.11 ?  1394 HOH   A O    1 
HETATM 6848 O  O    . HOH   E 4 .   ? 24.318 -7.787  14.511  1.00 15.68 ?  1395 HOH   A O    1 
HETATM 6849 O  O    . HOH   E 4 .   ? 24.385 3.489   -1.855  1.00 13.74 ?  1396 HOH   A O    1 
HETATM 6850 O  O    . HOH   E 4 .   ? 32.865 -9.244  6.026   1.00 19.95 ?  1397 HOH   A O    1 
HETATM 6851 O  O    . HOH   E 4 .   ? 27.551 -6.269  -14.058 1.00 32.36 ?  1398 HOH   A O    1 
HETATM 6852 O  O    . HOH   E 4 .   ? 24.831 -17.626 12.718  1.00 22.68 ?  1399 HOH   A O    1 
HETATM 6853 O  O    . HOH   E 4 .   ? 26.996 -3.237  19.538  1.00 38.51 ?  1400 HOH   A O    1 
HETATM 6854 O  O    . HOH   E 4 .   ? 14.578 -0.489  -12.118 1.00 33.93 ?  1401 HOH   A O    1 
HETATM 6855 O  O    . HOH   E 4 .   ? 15.342 -21.616 14.285  1.00 17.26 ?  1402 HOH   A O    1 
HETATM 6856 O  O    . HOH   E 4 .   ? 28.717 -10.660 -14.125 1.00 41.14 ?  1403 HOH   A O    1 
HETATM 6857 O  O    . HOH   E 4 .   ? 30.132 -10.131 13.056  1.00 20.75 ?  1404 HOH   A O    1 
HETATM 6858 O  O    . HOH   E 4 .   ? 16.305 -14.138 20.236  1.00 44.47 ?  1405 HOH   A O    1 
HETATM 6859 O  O    . HOH   E 4 .   ? 19.618 -11.203 24.158  1.00 70.87 ?  1406 HOH   A O    1 
HETATM 6860 O  O    A HOH   E 4 .   ? 21.378 3.094   -0.334  0.30 5.15  ?  1407 HOH   A O    1 
HETATM 6861 O  O    A HOH   E 4 .   ? 18.997 -0.734  -1.615  0.30 10.78 ?  1408 HOH   A O    1 
HETATM 6862 O  O    . HOH   E 4 .   ? 15.436 11.911  7.723   1.00 30.82 ?  1409 HOH   A O    1 
HETATM 6863 O  O    . HOH   E 4 .   ? 21.299 -9.139  21.320  1.00 51.92 ?  1410 HOH   A O    1 
HETATM 6864 O  O    . HOH   E 4 .   ? 20.648 -20.066 2.769   1.00 16.99 ?  1411 HOH   A O    1 
HETATM 6865 O  O    . HOH   E 4 .   ? 37.585 -1.996  5.787   1.00 26.35 ?  1412 HOH   A O    1 
HETATM 6866 O  O    . HOH   E 4 .   ? 6.641  -3.584  12.855  1.00 31.89 ?  1413 HOH   A O    1 
HETATM 6867 O  O    . HOH   E 4 .   ? 23.430 11.360  4.056   1.00 11.49 ?  1414 HOH   A O    1 
HETATM 6868 O  O    . HOH   E 4 .   ? 14.241 -23.167 7.437   1.00 17.84 ?  1415 HOH   A O    1 
HETATM 6869 O  O    . HOH   E 4 .   ? 26.933 4.098   -0.672  1.00 11.75 ?  1416 HOH   A O    1 
HETATM 6870 O  O    . HOH   E 4 .   ? 10.516 -13.884 -1.805  1.00 17.50 ?  1417 HOH   A O    1 
HETATM 6871 O  O    . HOH   E 4 .   ? 30.408 -12.949 13.551  1.00 18.40 ?  1418 HOH   A O    1 
HETATM 6872 O  O    A HOH   E 4 .   ? 15.838 -1.024  5.279   0.30 25.24 ?  1419 HOH   A O    1 
HETATM 6873 O  O    B HOH   E 4 .   ? 12.252 -1.455  -2.945  0.70 18.27 ?  1420 HOH   A O    1 
HETATM 6874 O  O    . HOH   E 4 .   ? 30.824 6.253   -12.237 1.00 26.44 ?  1421 HOH   A O    1 
HETATM 6875 O  O    . HOH   E 4 .   ? 35.183 -5.240  -3.092  1.00 17.77 ?  1422 HOH   A O    1 
HETATM 6876 O  O    . HOH   E 4 .   ? 16.305 16.759  8.736   1.00 34.70 ?  1423 HOH   A O    1 
HETATM 6877 O  O    . HOH   E 4 .   ? 32.658 -10.674 3.211   1.00 30.98 ?  1424 HOH   A O    1 
HETATM 6878 O  O    . HOH   E 4 .   ? 27.158 2.355   18.748  1.00 32.07 ?  1425 HOH   A O    1 
HETATM 6879 O  O    A HOH   E 4 .   ? 18.619 -2.513  -16.330 0.30 20.50 ?  1426 HOH   A O    1 
HETATM 6880 O  O    . HOH   E 4 .   ? 24.025 -20.326 -1.327  1.00 15.31 ?  1427 HOH   A O    1 
HETATM 6881 O  O    . HOH   E 4 .   ? 41.027 -8.268  -6.830  1.00 36.28 ?  1428 HOH   A O    1 
HETATM 6882 O  O    . HOH   E 4 .   ? 15.932 2.075   24.780  1.00 50.76 ?  1429 HOH   A O    1 
HETATM 6883 O  O    . HOH   E 4 .   ? 11.791 -10.826 17.026  1.00 24.49 ?  1430 HOH   A O    1 
HETATM 6884 O  O    . HOH   E 4 .   ? 32.797 -4.468  -9.911  1.00 25.65 ?  1431 HOH   A O    1 
HETATM 6885 O  O    . HOH   E 4 .   ? 41.659 1.513   4.963   1.00 36.36 ?  1432 HOH   A O    1 
HETATM 6886 O  O    . HOH   E 4 .   ? 15.248 -8.168  -9.790  1.00 25.90 ?  1433 HOH   A O    1 
HETATM 6887 O  O    B HOH   E 4 .   ? 7.791  3.534   4.094   0.70 32.35 ?  1434 HOH   A O    1 
HETATM 6888 O  O    . HOH   E 4 .   ? 15.999 6.984   2.897   1.00 14.05 ?  1435 HOH   A O    1 
HETATM 6889 O  O    . HOH   E 4 .   ? 27.890 0.774   -7.217  1.00 14.10 ?  1436 HOH   A O    1 
HETATM 6890 O  O    . HOH   E 4 .   ? 36.775 -4.988  5.378   1.00 25.62 ?  1437 HOH   A O    1 
HETATM 6891 O  O    . HOH   E 4 .   ? 21.814 -14.010 -8.200  1.00 45.29 ?  1438 HOH   A O    1 
HETATM 6892 O  O    B HOH   E 4 .   ? 7.975  -0.399  -1.923  0.70 27.72 ?  1439 HOH   A O    1 
HETATM 6893 O  O    B HOH   E 4 .   ? 8.215  3.640   1.316   0.70 27.95 ?  1440 HOH   A O    1 
HETATM 6894 O  O    A HOH   E 4 .   ? 11.104 -0.465  1.942   0.30 16.03 ?  1441 HOH   A O    1 
HETATM 6895 O  O    . HOH   E 4 .   ? 23.590 -8.022  17.123  1.00 20.51 ?  1442 HOH   A O    1 
HETATM 6896 O  O    A HOH   E 4 .   ? 18.896 1.967   -0.738  0.30 13.52 ?  1443 HOH   A O    1 
HETATM 6897 O  O    A HOH   E 4 .   ? 16.289 2.877   -1.427  0.30 16.43 ?  1444 HOH   A O    1 
HETATM 6898 O  O    . HOH   E 4 .   ? 45.050 -0.598  2.972   1.00 39.11 ?  1445 HOH   A O    1 
HETATM 6899 O  O    . HOH   E 4 .   ? 22.547 8.105   18.409  1.00 47.74 ?  1446 HOH   A O    1 
HETATM 6900 O  O    . HOH   E 4 .   ? 20.543 -17.743 24.820  1.00 68.27 ?  1447 HOH   A O    1 
HETATM 6901 O  O    . HOH   E 4 .   ? 23.416 -21.007 1.333   1.00 17.20 ?  1448 HOH   A O    1 
HETATM 6902 O  O    A HOH   E 4 .   ? 23.222 7.458   -3.216  0.30 15.41 ?  1449 HOH   A O    1 
HETATM 6903 O  O    . HOH   E 4 .   ? 18.443 -16.052 16.354  1.00 34.93 ?  1450 HOH   A O    1 
HETATM 6904 O  O    . HOH   E 4 .   ? 37.830 -8.850  -3.467  1.00 23.46 ?  1451 HOH   A O    1 
HETATM 6905 O  O    . HOH   E 4 .   ? 34.536 -8.074  -0.442  1.00 29.21 ?  1452 HOH   A O    1 
HETATM 6906 O  O    A HOH   E 4 .   ? 9.458  -16.410 -1.992  0.30 28.68 ?  1453 HOH   A O    1 
HETATM 6907 O  O    . HOH   E 4 .   ? 18.470 4.914   -15.020 1.00 56.03 ?  1454 HOH   A O    1 
HETATM 6908 O  O    . HOH   E 4 .   ? 30.589 14.795  2.807   1.00 17.91 ?  1455 HOH   A O    1 
HETATM 6909 O  O    . HOH   E 4 .   ? 29.854 -2.044  -12.735 1.00 50.54 ?  1456 HOH   A O    1 
HETATM 6910 O  O    . HOH   E 4 .   ? 21.655 -14.765 17.985  1.00 51.43 ?  1457 HOH   A O    1 
HETATM 6911 O  O    . HOH   E 4 .   ? 31.425 -12.834 0.034   1.00 19.31 ?  1458 HOH   A O    1 
HETATM 6912 O  O    . HOH   E 4 .   ? 29.932 -16.001 10.698  1.00 31.99 ?  1459 HOH   A O    1 
HETATM 6913 O  O    A HOH   E 4 .   ? 14.064 -0.419  3.471   0.30 28.15 ?  1460 HOH   A O    1 
HETATM 6914 O  O    B HOH   E 4 .   ? 23.288 7.961   -3.571  0.70 29.71 ?  1461 HOH   A O    1 
HETATM 6915 O  O    . HOH   E 4 .   ? 27.659 6.914   -6.415  1.00 29.09 ?  1462 HOH   A O    1 
HETATM 6916 O  O    . HOH   E 4 .   ? 32.426 -16.025 10.884  1.00 35.42 ?  1463 HOH   A O    1 
HETATM 6917 O  O    . HOH   E 4 .   ? 20.004 -17.427 -5.071  1.00 25.27 ?  1464 HOH   A O    1 
HETATM 6918 O  O    . HOH   E 4 .   ? 24.752 5.548   20.719  1.00 55.85 ?  1465 HOH   A O    1 
HETATM 6919 O  O    . HOH   E 4 .   ? 25.454 8.347   -4.925  1.00 20.60 ?  1466 HOH   A O    1 
HETATM 6920 O  O    . HOH   E 4 .   ? 24.558 14.462  7.847   1.00 29.59 ?  1467 HOH   A O    1 
HETATM 6921 O  O    . HOH   E 4 .   ? 23.371 -22.372 -3.282  1.00 32.94 ?  1468 HOH   A O    1 
HETATM 6922 O  O    . HOH   E 4 .   ? 26.981 11.563  -1.165  1.00 27.74 ?  1469 HOH   A O    1 
HETATM 6923 O  O    . HOH   E 4 .   ? 18.828 10.925  11.180  1.00 32.08 ?  1470 HOH   A O    1 
HETATM 6924 O  O    B HOH   E 4 .   ? 12.688 -3.250  1.842   0.70 18.61 ?  1471 HOH   A O    1 
HETATM 6925 O  O    B HOH   E 4 .   ? 21.641 10.296  -3.998  0.70 22.14 ?  1472 HOH   A O    1 
HETATM 6926 O  O    . HOH   E 4 .   ? 12.024 -13.428 16.301  1.00 55.11 ?  1473 HOH   A O    1 
HETATM 6927 O  O    . HOH   E 4 .   ? 27.569 -11.479 16.585  1.00 38.27 ?  1474 HOH   A O    1 
HETATM 6928 O  O    . HOH   E 4 .   ? 15.894 -21.593 3.711   1.00 20.62 ?  1475 HOH   A O    1 
HETATM 6929 O  O    . HOH   E 4 .   ? 39.819 -7.107  -3.573  1.00 46.62 ?  1476 HOH   A O    1 
HETATM 6930 O  O    A HOH   E 4 .   ? 21.992 5.213   -5.818  0.30 20.07 ?  1477 HOH   A O    1 
HETATM 6931 O  O    . HOH   E 4 .   ? 23.452 13.689  5.525   1.00 18.78 ?  1478 HOH   A O    1 
HETATM 6932 O  O    . HOH   E 4 .   ? 12.261 1.436   17.257  1.00 41.55 ?  1479 HOH   A O    1 
HETATM 6933 O  O    A HOH   E 4 .   ? 25.844 10.755  -3.769  0.30 15.34 ?  1480 HOH   A O    1 
HETATM 6934 O  O    A HOH   E 4 .   ? 23.175 11.768  -4.093  0.30 12.32 ?  1481 HOH   A O    1 
HETATM 6935 O  O    B HOH   E 4 .   ? 26.115 10.931  -3.502  0.70 24.16 ?  1482 HOH   A O    1 
HETATM 6936 O  O    . HOH   E 4 .   ? 35.151 7.464   12.291  1.00 48.48 ?  1483 HOH   A O    1 
HETATM 6937 O  O    . HOH   E 4 .   ? 11.044 -15.190 -6.143  1.00 34.65 ?  1484 HOH   A O    1 
HETATM 6938 O  O    . HOH   E 4 .   ? 18.262 -16.331 -8.837  1.00 46.90 ?  1485 HOH   A O    1 
HETATM 6939 O  O    . HOH   E 4 .   ? 28.833 8.919   17.617  1.00 39.29 ?  1486 HOH   A O    1 
HETATM 6940 O  O    . HOH   E 4 .   ? 41.102 -3.981  -0.263  1.00 37.92 ?  1487 HOH   A O    1 
HETATM 6941 O  O    . HOH   E 4 .   ? 16.962 -20.585 16.216  1.00 31.07 ?  1488 HOH   A O    1 
HETATM 6942 O  O    B HOH   E 4 .   ? 15.966 8.696   9.405   0.70 35.01 ?  1489 HOH   A O    1 
HETATM 6943 O  O    . HOH   E 4 .   ? 28.652 -4.783  -12.319 1.00 38.89 ?  1490 HOH   A O    1 
HETATM 6944 O  O    . HOH   E 4 .   ? 30.806 0.738   19.177  1.00 38.06 ?  1491 HOH   A O    1 
HETATM 6945 O  O    B HOH   E 4 .   ? 16.734 10.194  6.373   0.70 20.82 ?  1492 HOH   A O    1 
HETATM 6946 O  O    . HOH   E 4 .   ? 17.375 -18.767 19.708  1.00 49.06 ?  1493 HOH   A O    1 
HETATM 6947 O  O    . HOH   E 4 .   ? 15.739 -17.335 -6.986  1.00 34.57 ?  1494 HOH   A O    1 
HETATM 6948 O  O    . HOH   E 4 .   ? 14.112 -10.402 -10.936 1.00 34.55 ?  1495 HOH   A O    1 
HETATM 6949 O  O    . HOH   E 4 .   ? 44.415 10.457  -1.681  1.00 33.13 ?  1496 HOH   A O    1 
HETATM 6950 O  O    . HOH   E 4 .   ? 41.647 9.401   -3.975  1.00 31.63 ?  1497 HOH   A O    1 
HETATM 6951 O  O    . HOH   E 4 .   ? 39.162 2.426   7.485   1.00 31.73 ?  1498 HOH   A O    1 
HETATM 6952 O  O    . HOH   E 4 .   ? 23.294 -12.899 19.314  1.00 46.83 ?  1499 HOH   A O    1 
HETATM 6953 O  O    . HOH   E 4 .   ? 31.538 -0.614  -10.532 1.00 25.00 ?  1500 HOH   A O    1 
HETATM 6954 O  O    . HOH   E 4 .   ? 28.833 -8.034  -15.196 1.00 46.80 ?  1501 HOH   A O    1 
HETATM 6955 O  O    . HOH   E 4 .   ? 16.213 -6.889  -11.820 1.00 44.77 ?  1502 HOH   A O    1 
HETATM 6956 O  O    . HOH   E 4 .   ? 40.505 -0.240  -7.838  1.00 31.39 ?  1503 HOH   A O    1 
HETATM 6957 O  O    . HOH   E 4 .   ? 20.150 -22.363 4.143   1.00 25.47 ?  1504 HOH   A O    1 
HETATM 6958 O  O    . HOH   E 4 .   ? 18.614 -23.323 1.933   1.00 41.81 ?  1505 HOH   A O    1 
HETATM 6959 O  O    . HOH   E 4 .   ? 14.062 -25.387 8.913   1.00 32.83 ?  1506 HOH   A O    1 
HETATM 6960 O  O    . HOH   E 4 .   ? 20.636 -16.023 -7.372  1.00 29.91 ?  1507 HOH   A O    1 
HETATM 6961 O  O    . HOH   E 4 .   ? 25.837 -19.000 -11.827 1.00 40.53 ?  1508 HOH   A O    1 
HETATM 6962 O  O    . HOH   E 4 .   ? 16.246 -23.422 5.720   1.00 26.06 ?  1509 HOH   A O    1 
HETATM 6963 O  O    B HOH   E 4 .   ? 23.638 12.319  -3.939  0.70 26.15 ?  1510 HOH   A O    1 
HETATM 6964 O  O    . HOH   E 4 .   ? 23.357 -23.861 1.742   1.00 28.25 ?  1511 HOH   A O    1 
HETATM 6965 O  O    . HOH   E 4 .   ? 30.837 -5.849  -11.892 1.00 52.04 ?  1512 HOH   A O    1 
HETATM 6966 O  O    . HOH   E 4 .   ? 37.469 -6.660  7.551   1.00 24.11 ?  1513 HOH   A O    1 
HETATM 6967 O  O    . HOH   E 4 .   ? 28.948 14.394  0.938   1.00 44.69 ?  1514 HOH   A O    1 
HETATM 6968 O  O    . HOH   E 4 .   ? 30.683 5.815   -14.793 1.00 36.12 ?  1515 HOH   A O    1 
HETATM 6969 O  O    . HOH   E 4 .   ? 39.598 -0.034  6.575   1.00 30.13 ?  1516 HOH   A O    1 
HETATM 6970 O  O    B HOH   E 4 .   ? 8.900  4.968   7.988   0.70 31.26 ?  1517 HOH   A O    1 
HETATM 6971 O  O    . HOH   E 4 .   ? 38.005 13.925  6.747   1.00 45.91 ?  1518 HOH   A O    1 
HETATM 6972 O  O    B HOH   E 4 .   ? 10.591 -0.320  -1.026  0.70 20.20 ?  1519 HOH   A O    1 
HETATM 6973 O  O    B HOH   E 4 .   ? 14.792 7.986   5.071   0.70 19.02 ?  1520 HOH   A O    1 
HETATM 6974 O  O    B HOH   E 4 .   ? 7.532  5.748   5.650   0.70 31.44 ?  1521 HOH   A O    1 
HETATM 6975 O  O    B HOH   E 4 .   ? 10.453 2.539   -0.980  0.70 36.81 ?  1522 HOH   A O    1 
HETATM 6976 O  O    B HOH   E 4 .   ? 8.837  2.284   -3.007  0.70 29.76 ?  1523 HOH   A O    1 
HETATM 6977 O  O    B HOH   E 4 .   ? 10.217 1.114   -5.356  0.70 23.55 ?  1524 HOH   A O    1 
HETATM 6978 O  O    . HOH   E 4 .   ? 22.161 -24.090 4.478   1.00 26.10 ?  1525 HOH   A O    1 
HETATM 6979 O  O    . HOH   E 4 .   ? 8.190  -2.961  -5.643  1.00 52.86 ?  1526 HOH   A O    1 
HETATM 6980 O  O    . HOH   E 4 .   ? 36.583 -6.508  10.217  1.00 41.87 ?  1527 HOH   A O    1 
HETATM 6981 O  O    . HOH   E 4 .   ? 17.421 -6.943  -14.200 1.00 45.13 ?  1528 HOH   A O    1 
HETATM 6982 O  O    A HOH   E 4 .   ? 14.868 8.570   4.908   0.30 14.78 ?  1529 HOH   A O    1 
HETATM 6983 O  O    . HOH   E 4 .   ? 16.253 -21.240 18.775  1.00 43.09 ?  1530 HOH   A O    1 
HETATM 6984 O  O    . HOH   E 4 .   ? 24.240 9.443   -7.199  1.00 32.55 ?  1531 HOH   A O    1 
HETATM 6985 O  O    . HOH   E 4 .   ? 15.974 -12.479 27.506  1.00 44.42 ?  1532 HOH   A O    1 
HETATM 6986 O  O    B HOH   E 4 .   ? 8.374  7.229   2.198   0.70 28.49 ?  1533 HOH   A O    1 
HETATM 6987 O  O    . HOH   E 4 .   ? 14.645 -22.762 19.878  1.00 33.81 ?  1534 HOH   A O    1 
HETATM 6988 O  O    . HOH   F 4 .   ? 29.904 -22.462 5.461   1.00 19.92 ?  201  HOH   B O    1 
HETATM 6989 O  O    . HOH   F 4 .   ? 27.884 -41.618 -15.189 1.00 33.83 ?  202  HOH   B O    1 
HETATM 6990 O  O    . HOH   F 4 .   ? 27.758 -29.174 -1.923  1.00 36.51 ?  203  HOH   B O    1 
HETATM 6991 O  O    . HOH   F 4 .   ? 59.248 -18.666 6.834   1.00 36.19 ?  204  HOH   B O    1 
HETATM 6992 O  O    . HOH   F 4 .   ? 49.434 -22.725 -19.750 1.00 53.27 ?  205  HOH   B O    1 
HETATM 6993 O  O    . HOH   F 4 .   ? 53.055 -13.420 -20.350 1.00 34.48 ?  206  HOH   B O    1 
HETATM 6994 O  O    . HOH   F 4 .   ? 41.873 -35.880 -17.390 1.00 27.63 ?  207  HOH   B O    1 
HETATM 6995 O  O    . HOH   F 4 .   ? 37.981 -39.489 -0.304  1.00 42.63 ?  208  HOH   B O    1 
HETATM 6996 O  O    . HOH   F 4 .   ? 48.117 -6.947  15.528  1.00 34.42 ?  209  HOH   B O    1 
HETATM 6997 O  O    . HOH   F 4 .   ? 47.484 -7.445  -3.893  1.00 42.07 ?  210  HOH   B O    1 
HETATM 6998 O  O    . HOH   F 4 .   ? 41.468 -7.798  5.493   1.00 38.01 ?  211  HOH   B O    1 
HETATM 6999 O  O    . HOH   F 4 .   ? 54.603 -9.381  -8.815  1.00 19.45 ?  212  HOH   B O    1 
HETATM 7000 O  O    . HOH   F 4 .   ? 58.348 -13.004 8.407   1.00 28.01 ?  213  HOH   B O    1 
HETATM 7001 O  O    . HOH   F 4 .   ? 44.622 -7.316  2.138   1.00 36.28 ?  214  HOH   B O    1 
HETATM 7002 O  O    . HOH   F 4 .   ? 45.023 -43.509 -10.668 1.00 26.10 ?  215  HOH   B O    1 
HETATM 7003 O  O    . HOH   F 4 .   ? 29.986 -26.350 3.991   1.00 27.66 ?  216  HOH   B O    1 
HETATM 7004 O  O    . HOH   F 4 .   ? 56.495 -19.756 7.251   1.00 31.29 ?  217  HOH   B O    1 
HETATM 7005 O  O    . HOH   F 4 .   ? 36.123 -43.317 -8.557  1.00 32.97 ?  218  HOH   B O    1 
HETATM 7006 O  O    . HOH   F 4 .   ? 56.820 -30.780 -7.835  1.00 31.58 ?  219  HOH   B O    1 
HETATM 7007 O  O    . HOH   F 4 .   ? 30.267 -41.017 -8.176  1.00 15.42 ?  220  HOH   B O    1 
HETATM 7008 O  O    . HOH   F 4 .   ? 29.776 -34.134 -0.397  1.00 32.20 ?  221  HOH   B O    1 
HETATM 7009 O  O    . HOH   F 4 .   ? 57.805 -24.505 5.033   1.00 37.24 ?  222  HOH   B O    1 
HETATM 7010 O  O    . HOH   F 4 .   ? 26.576 -19.372 -1.765  1.00 13.21 ?  223  HOH   B O    1 
HETATM 7011 O  O    . HOH   F 4 .   ? 55.622 -16.538 -14.310 1.00 38.19 ?  224  HOH   B O    1 
HETATM 7012 O  O    . HOH   F 4 .   ? 50.272 -3.478  7.114   1.00 34.46 ?  225  HOH   B O    1 
HETATM 7013 O  O    . HOH   F 4 .   ? 57.539 -16.260 -12.175 1.00 18.47 ?  226  HOH   B O    1 
HETATM 7014 O  O    . HOH   F 4 .   ? 32.278 -9.251  -6.504  1.00 22.22 ?  227  HOH   B O    1 
HETATM 7015 O  O    . HOH   F 4 .   ? 50.903 -6.111  0.213   1.00 25.66 ?  228  HOH   B O    1 
HETATM 7016 O  O    . HOH   F 4 .   ? 34.616 -36.412 -7.211  1.00 17.08 ?  229  HOH   B O    1 
HETATM 7017 O  O    . HOH   F 4 .   ? 48.669 -36.496 -15.530 1.00 37.55 ?  230  HOH   B O    1 
HETATM 7018 O  O    . HOH   F 4 .   ? 46.481 -1.620  13.246  1.00 26.19 ?  231  HOH   B O    1 
HETATM 7019 O  O    . HOH   F 4 .   ? 41.536 -39.167 -14.924 1.00 20.40 ?  232  HOH   B O    1 
HETATM 7020 O  O    . HOH   F 4 .   ? 41.483 -9.662  13.040  1.00 21.00 ?  233  HOH   B O    1 
HETATM 7021 O  O    . HOH   F 4 .   ? 35.222 -8.031  -2.967  1.00 18.31 ?  234  HOH   B O    1 
HETATM 7022 O  O    . HOH   F 4 .   ? 51.772 -6.525  4.422   1.00 18.83 ?  235  HOH   B O    1 
HETATM 7023 O  O    . HOH   F 4 .   ? 40.707 -16.067 14.152  1.00 23.36 ?  236  HOH   B O    1 
HETATM 7024 O  O    . HOH   F 4 .   ? 28.517 -19.690 -13.127 1.00 23.94 ?  237  HOH   B O    1 
HETATM 7025 O  O    . HOH   F 4 .   ? 30.954 -28.790 4.303   1.00 25.31 ?  238  HOH   B O    1 
HETATM 7026 O  O    . HOH   F 4 .   ? 41.952 -23.589 9.320   1.00 15.92 ?  239  HOH   B O    1 
HETATM 7027 O  O    . HOH   F 4 .   ? 44.600 -27.756 -0.667  1.00 21.24 ?  240  HOH   B O    1 
HETATM 7028 O  O    . HOH   F 4 .   ? 45.190 -34.929 6.767   1.00 37.76 ?  241  HOH   B O    1 
HETATM 7029 O  O    . HOH   F 4 .   ? 35.037 -24.647 13.879  1.00 29.35 ?  242  HOH   B O    1 
HETATM 7030 O  O    . HOH   F 4 .   ? 50.842 -13.000 -0.457  1.00 11.28 ?  243  HOH   B O    1 
HETATM 7031 O  O    . HOH   F 4 .   ? 57.734 -24.420 -3.786  1.00 22.12 ?  244  HOH   B O    1 
HETATM 7032 O  O    . HOH   F 4 .   ? 42.750 -22.907 3.874   1.00 10.99 ?  245  HOH   B O    1 
HETATM 7033 O  O    . HOH   F 4 .   ? 43.174 -43.265 -8.303  1.00 28.24 ?  246  HOH   B O    1 
HETATM 7034 O  O    . HOH   F 4 .   ? 38.562 -11.068 -2.234  1.00 17.91 ?  247  HOH   B O    1 
HETATM 7035 O  O    . HOH   F 4 .   ? 39.636 -11.165 0.331   1.00 15.76 ?  248  HOH   B O    1 
HETATM 7036 O  O    . HOH   F 4 .   ? 32.819 -43.796 -11.378 1.00 18.96 ?  249  HOH   B O    1 
HETATM 7037 O  O    . HOH   F 4 .   ? 48.052 -24.522 -17.778 1.00 29.64 ?  250  HOH   B O    1 
HETATM 7038 O  O    . HOH   F 4 .   ? 39.378 -10.841 6.142   1.00 22.03 ?  251  HOH   B O    1 
HETATM 7039 O  O    . HOH   F 4 .   ? 40.449 -12.777 -11.519 1.00 14.39 ?  252  HOH   B O    1 
HETATM 7040 O  O    . HOH   F 4 .   ? 25.514 -26.028 -1.334  1.00 32.06 ?  253  HOH   B O    1 
HETATM 7041 O  O    . HOH   F 4 .   ? 42.677 -25.405 2.661   1.00 14.06 ?  254  HOH   B O    1 
HETATM 7042 O  O    . HOH   F 4 .   ? 27.185 -31.808 -9.974  1.00 20.98 ?  255  HOH   B O    1 
HETATM 7043 O  O    . HOH   F 4 .   ? 58.270 -10.589 -4.053  1.00 20.02 ?  256  HOH   B O    1 
HETATM 7044 O  O    . HOH   F 4 .   ? 37.223 -19.656 -18.126 1.00 42.97 ?  257  HOH   B O    1 
HETATM 7045 O  O    . HOH   F 4 .   ? 51.049 -40.022 -8.270  1.00 27.99 ?  258  HOH   B O    1 
HETATM 7046 O  O    . HOH   F 4 .   ? 33.633 -17.051 8.094   1.00 18.46 ?  259  HOH   B O    1 
HETATM 7047 O  O    . HOH   F 4 .   ? 57.245 -26.725 -7.673  1.00 41.94 ?  260  HOH   B O    1 
HETATM 7048 O  O    . HOH   F 4 .   ? 57.613 -9.273  1.429   1.00 18.86 ?  261  HOH   B O    1 
HETATM 7049 O  O    . HOH   F 4 .   ? 49.848 -0.579  10.286  1.00 31.32 ?  262  HOH   B O    1 
HETATM 7050 O  O    . HOH   F 4 .   ? 29.809 -25.232 -10.805 1.00 16.02 ?  263  HOH   B O    1 
HETATM 7051 O  O    . HOH   F 4 .   ? 31.881 -17.949 -14.506 1.00 28.89 ?  264  HOH   B O    1 
HETATM 7052 O  O    . HOH   F 4 .   ? 49.429 -28.746 -6.931  1.00 14.69 ?  265  HOH   B O    1 
HETATM 7053 O  O    . HOH   F 4 .   ? 34.327 -18.533 11.451  1.00 24.01 ?  266  HOH   B O    1 
HETATM 7054 O  O    . HOH   F 4 .   ? 30.953 -15.752 2.678   1.00 12.61 ?  267  HOH   B O    1 
HETATM 7055 O  O    . HOH   F 4 .   ? 48.121 -22.803 5.846   1.00 15.65 ?  268  HOH   B O    1 
HETATM 7056 O  O    . HOH   F 4 .   ? 51.664 -13.859 11.020  1.00 24.59 ?  269  HOH   B O    1 
HETATM 7057 O  O    . HOH   F 4 .   ? 43.295 -32.370 -17.131 1.00 21.60 ?  270  HOH   B O    1 
HETATM 7058 O  O    . HOH   F 4 .   ? 46.698 -31.319 -4.819  1.00 17.42 ?  271  HOH   B O    1 
HETATM 7059 O  O    . HOH   F 4 .   ? 30.620 -42.237 -10.682 1.00 28.11 ?  272  HOH   B O    1 
HETATM 7060 O  O    . HOH   F 4 .   ? 42.444 -9.956  9.389   1.00 19.96 ?  273  HOH   B O    1 
HETATM 7061 O  O    . HOH   F 4 .   ? 28.556 -30.871 -14.850 1.00 30.58 ?  274  HOH   B O    1 
HETATM 7062 O  O    . HOH   F 4 .   ? 57.065 -8.660  8.445   1.00 19.22 ?  275  HOH   B O    1 
HETATM 7063 O  O    . HOH   F 4 .   ? 34.948 -33.325 -19.250 1.00 24.95 ?  276  HOH   B O    1 
HETATM 7064 O  O    . HOH   F 4 .   ? 34.594 -12.843 2.663   1.00 21.69 ?  277  HOH   B O    1 
HETATM 7065 O  O    . HOH   F 4 .   ? 43.490 -15.822 -12.162 1.00 13.87 ?  278  HOH   B O    1 
HETATM 7066 O  O    . HOH   F 4 .   ? 41.236 -5.603  11.578  1.00 43.12 ?  279  HOH   B O    1 
HETATM 7067 O  O    . HOH   F 4 .   ? 46.947 -29.618 9.809   1.00 32.82 ?  280  HOH   B O    1 
HETATM 7068 O  O    . HOH   F 4 .   ? 52.681 -10.423 12.982  1.00 20.62 ?  281  HOH   B O    1 
HETATM 7069 O  O    . HOH   F 4 .   ? 38.975 -12.013 12.398  1.00 35.03 ?  282  HOH   B O    1 
HETATM 7070 O  O    . HOH   F 4 .   ? 28.333 -34.325 -9.449  1.00 21.25 ?  283  HOH   B O    1 
HETATM 7071 O  O    . HOH   F 4 .   ? 42.491 -34.724 3.791   1.00 23.87 ?  284  HOH   B O    1 
HETATM 7072 O  O    . HOH   F 4 .   ? 51.713 -5.810  -7.925  1.00 50.59 ?  285  HOH   B O    1 
HETATM 7073 O  O    . HOH   F 4 .   ? 48.523 -25.088 3.077   1.00 12.88 ?  286  HOH   B O    1 
HETATM 7074 O  O    . HOH   F 4 .   ? 51.303 -37.661 -9.582  1.00 24.03 ?  287  HOH   B O    1 
HETATM 7075 O  O    . HOH   F 4 .   ? 56.318 -23.549 -14.751 1.00 27.86 ?  288  HOH   B O    1 
HETATM 7076 O  O    . HOH   F 4 .   ? 28.032 -22.901 -7.994  1.00 16.49 ?  289  HOH   B O    1 
HETATM 7077 O  O    . HOH   F 4 .   ? 57.251 -12.043 12.368  1.00 34.75 ?  290  HOH   B O    1 
HETATM 7078 O  O    . HOH   F 4 .   ? 42.341 -10.049 -14.869 1.00 34.96 ?  291  HOH   B O    1 
HETATM 7079 O  O    . HOH   F 4 .   ? 47.156 -34.046 -4.657  1.00 16.09 ?  292  HOH   B O    1 
HETATM 7080 O  O    . HOH   F 4 .   ? 27.698 -26.788 -15.680 1.00 31.90 ?  293  HOH   B O    1 
HETATM 7081 O  O    . HOH   F 4 .   ? 36.958 -12.791 -1.496  1.00 24.68 ?  294  HOH   B O    1 
HETATM 7082 O  O    . HOH   F 4 .   ? 33.609 -15.360 -13.962 1.00 20.42 ?  295  HOH   B O    1 
HETATM 7083 O  O    . HOH   F 4 .   ? 48.835 -20.080 5.925   1.00 13.35 ?  296  HOH   B O    1 
HETATM 7084 O  O    . HOH   F 4 .   ? 43.656 -15.360 18.193  1.00 28.57 ?  297  HOH   B O    1 
HETATM 7085 O  O    . HOH   F 4 .   ? 42.988 -20.287 -20.724 1.00 39.68 ?  298  HOH   B O    1 
HETATM 7086 O  O    . HOH   F 4 .   ? 45.474 -33.430 -15.952 1.00 21.89 ?  299  HOH   B O    1 
HETATM 7087 O  O    . HOH   F 4 .   ? 52.689 -35.673 -8.661  1.00 27.50 ?  300  HOH   B O    1 
HETATM 7088 O  O    . HOH   F 4 .   ? 45.941 -40.427 -3.643  1.00 27.50 ?  301  HOH   B O    1 
HETATM 7089 O  O    . HOH   F 4 .   ? 59.926 -15.265 8.185   1.00 31.15 ?  302  HOH   B O    1 
HETATM 7090 O  O    . HOH   F 4 .   ? 42.835 -12.186 -18.461 1.00 27.12 ?  303  HOH   B O    1 
HETATM 7091 O  O    . HOH   F 4 .   ? 45.826 -36.322 -16.121 1.00 33.65 ?  304  HOH   B O    1 
HETATM 7092 O  O    . HOH   F 4 .   ? 26.041 -21.509 -3.461  1.00 15.27 ?  305  HOH   B O    1 
HETATM 7093 O  O    . HOH   F 4 .   ? 35.154 -33.618 4.496   1.00 24.46 ?  306  HOH   B O    1 
HETATM 7094 O  O    . HOH   F 4 .   ? 41.314 -24.498 15.808  1.00 41.77 ?  307  HOH   B O    1 
HETATM 7095 O  O    . HOH   F 4 .   ? 44.719 -27.497 1.987   1.00 14.55 ?  308  HOH   B O    1 
HETATM 7096 O  O    . HOH   F 4 .   ? 53.498 -30.267 4.532   1.00 18.83 ?  309  HOH   B O    1 
HETATM 7097 O  O    . HOH   F 4 .   ? 44.121 -29.398 -4.667  1.00 22.37 ?  310  HOH   B O    1 
HETATM 7098 O  O    . HOH   F 4 .   ? 62.836 -13.606 4.811   1.00 27.71 ?  311  HOH   B O    1 
HETATM 7099 O  O    . HOH   F 4 .   ? 32.897 -34.617 -5.908  1.00 15.84 ?  312  HOH   B O    1 
HETATM 7100 O  O    . HOH   F 4 .   ? 37.936 -10.273 -10.699 1.00 16.07 ?  313  HOH   B O    1 
HETATM 7101 O  O    . HOH   F 4 .   ? 40.354 -10.846 -9.488  1.00 16.60 ?  314  HOH   B O    1 
HETATM 7102 O  O    . HOH   F 4 .   ? 37.575 -18.166 13.144  1.00 30.23 ?  315  HOH   B O    1 
HETATM 7103 O  O    . HOH   F 4 .   ? 41.844 -8.123  1.398   1.00 23.54 ?  316  HOH   B O    1 
HETATM 7104 O  O    . HOH   F 4 .   ? 52.689 -29.251 -13.026 1.00 24.05 ?  317  HOH   B O    1 
HETATM 7105 O  O    . HOH   F 4 .   ? 43.331 -21.456 10.698  1.00 15.07 ?  318  HOH   B O    1 
HETATM 7106 O  O    . HOH   F 4 .   ? 50.168 -24.617 5.853   1.00 34.31 ?  319  HOH   B O    1 
HETATM 7107 O  O    . HOH   F 4 .   ? 37.388 -35.751 7.203   1.00 35.92 ?  320  HOH   B O    1 
HETATM 7108 O  O    . HOH   F 4 .   ? 53.260 -16.052 -12.708 1.00 27.08 ?  321  HOH   B O    1 
HETATM 7109 O  O    . HOH   F 4 .   ? 51.481 -32.971 -10.789 1.00 37.82 ?  322  HOH   B O    1 
HETATM 7110 O  O    . HOH   F 4 .   ? 37.223 -30.572 -21.059 1.00 28.66 ?  323  HOH   B O    1 
HETATM 7111 O  O    . HOH   F 4 .   ? 38.446 -12.765 7.966   1.00 17.38 ?  324  HOH   B O    1 
HETATM 7112 O  O    . HOH   F 4 .   ? 26.438 -21.081 -6.208  1.00 15.02 ?  325  HOH   B O    1 
HETATM 7113 O  O    . HOH   F 4 .   ? 53.758 -12.465 -22.309 1.00 36.50 ?  326  HOH   B O    1 
HETATM 7114 O  O    . HOH   F 4 .   ? 63.049 -20.194 -0.858  1.00 39.78 ?  327  HOH   B O    1 
HETATM 7115 O  O    . HOH   F 4 .   ? 43.228 -34.586 0.023   1.00 21.12 ?  328  HOH   B O    1 
HETATM 7116 O  O    . HOH   F 4 .   ? 38.406 -9.390  -13.276 1.00 26.40 ?  329  HOH   B O    1 
HETATM 7117 O  O    . HOH   F 4 .   ? 44.714 -24.660 9.600   1.00 18.68 ?  330  HOH   B O    1 
HETATM 7118 O  O    . HOH   F 4 .   ? 57.684 -22.030 3.240   1.00 29.33 ?  331  HOH   B O    1 
HETATM 7119 O  O    . HOH   F 4 .   ? 33.685 -31.182 11.064  1.00 34.87 ?  332  HOH   B O    1 
HETATM 7120 O  O    . HOH   F 4 .   ? 36.836 -12.442 4.329   1.00 17.39 ?  333  HOH   B O    1 
HETATM 7121 O  O    . HOH   F 4 .   ? 48.132 -32.708 -16.669 1.00 40.79 ?  334  HOH   B O    1 
HETATM 7122 O  O    . HOH   F 4 .   ? 27.714 -14.755 -9.472  1.00 34.22 ?  335  HOH   B O    1 
HETATM 7123 O  O    . HOH   F 4 .   ? 44.213 -1.754  7.627   1.00 44.56 ?  336  HOH   B O    1 
HETATM 7124 O  O    . HOH   F 4 .   ? 39.575 -23.446 -20.348 1.00 35.64 ?  337  HOH   B O    1 
HETATM 7125 O  O    . HOH   F 4 .   ? 47.286 -24.537 8.169   1.00 25.05 ?  338  HOH   B O    1 
HETATM 7126 O  O    . HOH   F 4 .   ? 60.099 -17.241 -10.512 1.00 34.66 ?  339  HOH   B O    1 
HETATM 7127 O  O    . HOH   F 4 .   ? 47.579 -27.489 2.011   1.00 14.09 ?  340  HOH   B O    1 
HETATM 7128 O  O    . HOH   F 4 .   ? 48.720 -11.923 -13.849 1.00 26.54 ?  341  HOH   B O    1 
HETATM 7129 O  O    . HOH   F 4 .   ? 28.911 -42.853 -12.434 1.00 36.01 ?  342  HOH   B O    1 
HETATM 7130 O  O    . HOH   F 4 .   ? 37.053 -15.105 -16.517 1.00 37.61 ?  343  HOH   B O    1 
HETATM 7131 O  O    . HOH   F 4 .   ? 42.924 -43.522 -14.452 1.00 42.97 ?  344  HOH   B O    1 
HETATM 7132 O  O    . HOH   F 4 .   ? 46.970 -20.001 12.288  1.00 30.36 ?  345  HOH   B O    1 
HETATM 7133 O  O    . HOH   F 4 .   ? 39.828 -44.295 -11.214 1.00 40.71 ?  346  HOH   B O    1 
HETATM 7134 O  O    . HOH   F 4 .   ? 33.080 -14.713 1.071   1.00 17.50 ?  347  HOH   B O    1 
HETATM 7135 O  O    . HOH   F 4 .   ? 37.116 -45.334 -9.729  1.00 35.14 ?  348  HOH   B O    1 
HETATM 7136 O  O    . HOH   F 4 .   ? 44.237 -37.388 -17.788 1.00 32.72 ?  349  HOH   B O    1 
HETATM 7137 O  O    . HOH   F 4 .   ? 23.376 -23.745 6.860   1.00 32.50 ?  350  HOH   B O    1 
HETATM 7138 O  O    . HOH   F 4 .   ? 40.456 -43.499 -9.131  1.00 25.82 ?  351  HOH   B O    1 
HETATM 7139 O  O    . HOH   F 4 .   ? 38.592 -22.460 15.088  1.00 39.85 ?  352  HOH   B O    1 
HETATM 7140 O  O    . HOH   F 4 .   ? 55.732 -8.257  10.784  1.00 26.20 ?  353  HOH   B O    1 
HETATM 7141 O  O    . HOH   F 4 .   ? 27.878 -26.659 -0.613  1.00 28.30 ?  354  HOH   B O    1 
HETATM 7142 O  O    . HOH   F 4 .   ? 38.551 -12.278 -16.219 1.00 42.55 ?  355  HOH   B O    1 
HETATM 7143 O  O    . HOH   F 4 .   ? 62.641 -19.990 -4.908  1.00 47.74 ?  356  HOH   B O    1 
HETATM 7144 O  O    . HOH   F 4 .   ? 33.913 -9.183  -8.790  1.00 29.01 ?  357  HOH   B O    1 
HETATM 7145 O  O    . HOH   F 4 .   ? 34.681 -10.348 7.525   1.00 23.94 ?  358  HOH   B O    1 
HETATM 7146 O  O    . HOH   F 4 .   ? 36.289 -8.470  -9.627  1.00 28.68 ?  359  HOH   B O    1 
HETATM 7147 O  O    . HOH   F 4 .   ? 56.720 -7.284  3.064   1.00 26.59 ?  360  HOH   B O    1 
HETATM 7148 O  O    . HOH   F 4 .   ? 61.624 -19.909 1.657   1.00 35.76 ?  361  HOH   B O    1 
HETATM 7149 O  O    . HOH   F 4 .   ? 34.178 -7.789  11.555  1.00 39.89 ?  362  HOH   B O    1 
HETATM 7150 O  O    . HOH   F 4 .   ? 57.067 -21.456 -16.450 1.00 43.66 ?  363  HOH   B O    1 
HETATM 7151 O  O    . HOH   F 4 .   ? 43.233 -12.756 -21.224 1.00 39.26 ?  364  HOH   B O    1 
HETATM 7152 O  O    . HOH   F 4 .   ? 27.236 -25.922 -11.383 1.00 33.55 ?  365  HOH   B O    1 
HETATM 7153 O  O    . HOH   F 4 .   ? 40.312 -8.852  9.900   1.00 36.21 ?  366  HOH   B O    1 
HETATM 7154 O  O    . HOH   F 4 .   ? 32.586 -23.624 14.068  1.00 44.01 ?  367  HOH   B O    1 
HETATM 7155 O  O    . HOH   F 4 .   ? 59.155 -10.503 9.213   1.00 41.33 ?  368  HOH   B O    1 
HETATM 7156 O  O    . HOH   F 4 .   ? 48.452 -26.586 8.786   1.00 40.54 ?  369  HOH   B O    1 
HETATM 7157 O  O    . HOH   F 4 .   ? 54.349 -5.829  2.941   1.00 38.00 ?  370  HOH   B O    1 
HETATM 7158 O  O    . HOH   F 4 .   ? 39.920 -7.138  7.830   1.00 40.85 ?  371  HOH   B O    1 
HETATM 7159 O  O    . HOH   F 4 .   ? 40.147 -11.375 -13.957 1.00 29.81 ?  372  HOH   B O    1 
HETATM 7160 O  O    . HOH   F 4 .   ? 52.192 -12.898 13.281  1.00 28.98 ?  373  HOH   B O    1 
HETATM 7161 O  O    . HOH   F 4 .   ? 36.271 -8.673  8.953   1.00 39.64 ?  374  HOH   B O    1 
HETATM 7162 O  O    . HOH   F 4 .   ? 56.155 -7.822  -0.585  1.00 34.76 ?  375  HOH   B O    1 
HETATM 7163 O  O    . HOH   F 4 .   ? 40.191 -7.882  3.144   1.00 41.81 ?  376  HOH   B O    1 
HETATM 7164 O  O    . HOH   F 4 .   ? 41.922 -9.961  -17.418 1.00 59.65 ?  377  HOH   B O    1 
HETATM 7165 O  O    . HOH   F 4 .   ? 63.088 -12.407 7.033   1.00 36.65 ?  378  HOH   B O    1 
HETATM 7166 O  O    . HOH   F 4 .   ? 41.894 -6.838  -4.890  1.00 41.04 ?  379  HOH   B O    1 
HETATM 7167 O  O    . HOH   F 4 .   ? 38.153 -10.593 10.066  1.00 27.23 ?  380  HOH   B O    1 
HETATM 7168 O  O    . HOH   F 4 .   ? 36.643 -22.814 13.286  1.00 25.64 ?  381  HOH   B O    1 
HETATM 7169 O  O    . HOH   F 4 .   ? 42.798 -17.118 -23.211 1.00 43.60 ?  382  HOH   B O    1 
HETATM 7170 O  O    . HOH   F 4 .   ? 44.151 -5.621  -3.416  1.00 42.25 ?  383  HOH   B O    1 
HETATM 7171 O  O    . HOH   F 4 .   ? 39.677 -14.063 15.694  1.00 43.48 ?  384  HOH   B O    1 
HETATM 7172 O  O    . HOH   F 4 .   ? 52.921 -29.966 7.188   1.00 22.31 ?  385  HOH   B O    1 
HETATM 7173 O  O    . HOH   F 4 .   ? 60.544 -22.374 2.859   1.00 44.50 ?  386  HOH   B O    1 
HETATM 7174 O  O    . HOH   F 4 .   ? 46.753 -5.377  2.973   1.00 39.80 ?  387  HOH   B O    1 
HETATM 7175 O  O    . HOH   F 4 .   ? 41.071 -9.775  15.847  1.00 43.47 ?  388  HOH   B O    1 
HETATM 7176 O  O    . HOH   F 4 .   ? 35.381 -20.375 13.331  1.00 29.20 ?  389  HOH   B O    1 
HETATM 7177 O  O    . HOH   F 4 .   ? 35.420 -33.769 7.284   1.00 41.80 ?  390  HOH   B O    1 
HETATM 7178 O  O    . HOH   F 4 .   ? 24.027 -20.935 -7.678  1.00 26.07 ?  391  HOH   B O    1 
HETATM 7179 O  O    . HOH   F 4 .   ? 40.853 -6.625  -0.811  1.00 26.06 ?  392  HOH   B O    1 
HETATM 7180 O  O    . HOH   F 4 .   ? 44.249 -31.764 -3.811  1.00 33.70 ?  393  HOH   B O    1 
HETATM 7181 O  O    . HOH   F 4 .   ? 28.112 -27.085 2.249   1.00 31.86 ?  394  HOH   B O    1 
HETATM 7182 O  O    . HOH   F 4 .   ? 26.698 -27.960 -13.467 1.00 34.29 ?  395  HOH   B O    1 
HETATM 7183 O  O    . HOH   F 4 .   ? 24.708 -20.666 -10.453 1.00 35.29 ?  396  HOH   B O    1 
HETATM 7184 O  O    . HOH   F 4 .   ? 34.498 -33.488 9.649   1.00 32.31 ?  397  HOH   B O    1 
HETATM 7185 O  O    . HOH   F 4 .   ? 50.700 -30.934 8.735   1.00 28.32 ?  398  HOH   B O    1 
HETATM 7186 O  O    . HOH   F 4 .   ? 26.869 -30.594 -12.667 1.00 27.30 ?  399  HOH   B O    1 
HETATM 7187 O  O    . HOH   F 4 .   ? 45.771 -20.236 15.269  1.00 54.76 ?  400  HOH   B O    1 
HETATM 7188 O  O    . HOH   F 4 .   ? 57.717 -6.499  -2.366  1.00 32.56 ?  401  HOH   B O    1 
HETATM 7189 O  O    . HOH   F 4 .   ? 40.951 -11.885 -22.358 1.00 39.75 ?  402  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   ? 0.5906 0.5911 0.6734 -0.0072 -0.0139 0.0390  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.6310 0.6215 0.7104 -0.0028 -0.0294 0.0905  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.5875 0.5887 0.6670 -0.0089 -0.0126 0.0385  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6283 0.6198 0.7013 -0.0056 -0.0274 0.0898  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.5706 0.5743 0.6302 -0.0144 -0.0121 0.0385  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.6113 0.6067 0.6551 -0.0135 -0.0276 0.0890  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.5734 0.5775 0.6388 -0.0136 -0.0127 0.0389  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.6139 0.6098 0.6665 -0.0126 -0.0292 0.0897  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.5983 0.5982 0.6900 -0.0063 -0.0123 0.0376  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6394 0.6290 0.7291 -0.0024 -0.0262 0.0883  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6021 0.6014 0.6951 -0.0047 -0.0125 0.0372  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6433 0.6314 0.7353 -0.0001 -0.0267 0.0872  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6017 0.6014 0.6949 -0.0061 -0.0122 0.0371  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6431 0.6327 0.7346 -0.0024 -0.0260 0.0879  3    VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.5477 0.5540 0.5814 -0.0209 -0.0107 0.0373  4    ASN   A N   
32   N  N   B ASN   A 4   ? 0.5888 0.5878 0.5927 -0.0226 -0.0252 0.0859  4    ASN   A N   
33   C  CA  A ASN   A 4   ? 0.5221 0.5316 0.5290 -0.0279 -0.0087 0.0351  4    ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.5631 0.5663 0.5263 -0.0323 -0.0198 0.0817  4    ASN   A CA  
35   C  C   A ASN   A 4   ? 0.4861 0.5030 0.4916 -0.0371 -0.0050 0.0258  4    ASN   A C   
36   C  C   B ASN   A 4   ? 0.5269 0.5435 0.4902 -0.0431 -0.0027 0.0625  4    ASN   A C   
37   O  O   A ASN   A 4   ? 0.4872 0.5049 0.4931 -0.0386 -0.0045 0.0264  4    ASN   A O   
38   O  O   B ASN   A 4   ? 0.5272 0.5460 0.4880 -0.0454 -0.0013 0.0649  4    ASN   A O   
39   C  CB  A ASN   A 4   ? 0.5299 0.5363 0.5102 -0.0262 -0.0095 0.0420  4    ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.5701 0.5657 0.4938 -0.0318 -0.0288 0.0970  4    ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.5354 0.5397 0.4909 -0.0249 -0.0107 0.0484  4    ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.5741 0.5637 0.4607 -0.0317 -0.0392 0.1115  4    ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.5377 0.5416 0.4857 -0.0252 -0.0112 0.0504  4    ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.5760 0.5635 0.4521 -0.0336 -0.0442 0.1155  4    ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.5368 0.5402 0.4868 -0.0236 -0.0117 0.0510  4    ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.5746 0.5621 0.4527 -0.0293 -0.0437 0.1183  4    ASN   A ND2 
59   N  N   A SER   A 5   ? 0.4471 0.4705 0.4470 -0.0457 -0.0016 0.0158  5    SER   A N   
60   N  N   B SER   A 5   ? 0.4878 0.5153 0.4506 -0.0523 0.0143  0.0419  5    SER   A N   
61   C  CA  A SER   A 5   ? 0.4067 0.4374 0.3991 -0.0544 0.0043  0.0057  5    SER   A CA  
62   C  CA  B SER   A 5   ? 0.4452 0.4856 0.4088 -0.0622 0.0376  0.0215  5    SER   A CA  
63   C  C   A SER   A 5   ? 0.3649 0.4005 0.3496 -0.0596 0.0081  0.0000  5    SER   A C   
64   C  C   B SER   A 5   ? 0.3957 0.4468 0.3617 -0.0712 0.0616  0.0123  5    SER   A C   
65   O  O   A SER   A 5   ? 0.3657 0.4027 0.3468 -0.0593 0.0050  -0.0049 5    SER   A O   
66   O  O   B SER   A 5   ? 0.4013 0.4508 0.3538 -0.0650 0.0640  0.0015  5    SER   A O   
67   C  CB  A SER   A 5   ? 0.4075 0.4408 0.4069 -0.0577 0.0054  0.0016  5    SER   A CB  
68   C  CB  B SER   A 5   ? 0.4503 0.4928 0.4361 -0.0635 0.0359  0.0106  5    SER   A CB  
69   O  OG  A SER   A 5   ? 0.4075 0.4430 0.4071 -0.0597 0.0050  -0.0006 5    SER   A OG  
70   O  OG  B SER   A 5   ? 0.4526 0.4960 0.4448 -0.0648 0.0348  0.0057  5    SER   A OG  
81   N  N   A PHE   A 6   ? 0.3215 0.3606 0.2947 -0.0643 0.0173  0.0018  6    PHE   A N   
82   N  N   B PHE   A 6   ? 0.3380 0.4011 0.3014 -0.0883 0.0848  0.0189  6    PHE   A N   
83   C  CA  A PHE   A 6   ? 0.2809 0.3202 0.2433 -0.0653 0.0257  0.0058  6    PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.2854 0.3515 0.2609 -0.1000 0.0953  0.0285  6    PHE   A CA  
85   C  C   A PHE   A 6   ? 0.2660 0.3037 0.2267 -0.0718 0.0391  0.0093  6    PHE   A C   
86   C  C   B PHE   A 6   ? 0.2831 0.3491 0.2870 -0.1026 0.1142  0.0224  6    PHE   A C   
87   O  O   A PHE   A 6   ? 0.2680 0.3015 0.2219 -0.0785 0.0400  0.0161  6    PHE   A O   
88   O  O   B PHE   A 6   ? 0.2920 0.3470 0.3179 -0.1059 0.1084  0.0326  6    PHE   A O   
89   C  CB  A PHE   A 6   ? 0.2589 0.2973 0.2171 -0.0552 0.0206  0.0036  6    PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.2451 0.3066 0.2130 -0.0957 0.0694  0.0356  6    PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2415 0.2783 0.2025 -0.0428 0.0148  0.0013  6    PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2146 0.2723 0.1856 -0.0794 0.0385  0.0337  6    PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.2337 0.2707 0.1931 -0.0376 0.0115  0.0019  6    PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2031 0.2591 0.1699 -0.0678 0.0220  0.0370  6    PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2388 0.2700 0.2043 -0.0328 0.0171  -0.0010 6    PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2140 0.2608 0.2017 -0.0591 0.0343  0.0284  6    PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.2311 0.2654 0.1915 -0.0340 0.0107  0.0029  6    PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2002 0.2508 0.1838 -0.0614 0.0134  0.0425  6    PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2364 0.2655 0.2025 -0.0285 0.0178  -0.0010 6    PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2105 0.2533 0.2085 -0.0505 0.0283  0.0268  6    PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2333 0.2640 0.1951 -0.0301 0.0143  0.0012  6    PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2057 0.2497 0.1968 -0.0536 0.0198  0.0343  6    PHE   A CZ  
121  N  N   A SER   A 7   ? 0.2504 0.2885 0.2210 -0.0691 0.0466  0.0081  7    SER   A N   
122  N  N   B SER   A 7   ? 0.2721 0.3453 0.2882 -0.0963 0.1254  0.0098  7    SER   A N   
123  C  CA  A SER   A 7   ? 0.2396 0.2751 0.2251 -0.0604 0.0501  0.0008  7    SER   A CA  
124  C  CA  B SER   A 7   ? 0.2666 0.3421 0.3041 -0.0803 0.1215  -0.0104 7    SER   A CA  
125  C  C   A SER   A 7   ? 0.2229 0.2528 0.2217 -0.0560 0.0527  -0.0011 7    SER   A C   
126  C  C   B SER   A 7   ? 0.2444 0.3137 0.2865 -0.0802 0.1247  -0.0141 7    SER   A C   
127  O  O   A SER   A 7   ? 0.2269 0.2496 0.2188 -0.0555 0.0561  0.0006  7    SER   A O   
128  O  O   B SER   A 7   ? 0.2546 0.3097 0.2993 -0.0827 0.1181  -0.0151 7    SER   A O   
129  C  CB  A SER   A 7   ? 0.2451 0.2811 0.2290 -0.0543 0.0500  0.0042  7    SER   A CB  
130  C  CB  B SER   A 7   ? 0.2816 0.3615 0.3475 -0.0626 0.1076  -0.0129 7    SER   A CB  
131  O  OG  A SER   A 7   ? 0.2496 0.2824 0.2340 -0.0516 0.0485  0.0067  7    SER   A OG  
132  O  OG  B SER   A 7   ? 0.2920 0.3697 0.3817 -0.0537 0.0934  -0.0059 7    SER   A OG  
143  N  N   A GLY   A 8   ? 0.2073 0.2369 0.2281 -0.0494 0.0478  -0.0077 8    GLY   A N   
144  N  N   B GLY   A 8   ? 0.2226 0.2923 0.2806 -0.0735 0.1120  -0.0208 8    GLY   A N   
145  C  CA  A GLY   A 8   ? 0.1930 0.2225 0.2285 -0.0374 0.0502  -0.0054 8    GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2036 0.2705 0.2789 -0.0540 0.1037  -0.0153 8    GLY   A CA  
147  C  C   A GLY   A 8   ? 0.1779 0.2098 0.2207 -0.0265 0.0459  -0.0025 8    GLY   A C   
148  C  C   B GLY   A 8   ? 0.1815 0.2493 0.2634 -0.0375 0.0860  -0.0098 8    GLY   A C   
149  O  O   A GLY   A 8   ? 0.1729 0.2126 0.2316 -0.0221 0.0489  -0.0086 8    GLY   A O   
150  O  O   B GLY   A 8   ? 0.1762 0.2513 0.2800 -0.0272 0.0789  -0.0259 8    GLY   A O   
157  N  N   A TYR   A 9   ? 0.1673 0.1909 0.1970 -0.0213 0.0398  0.0056  9    TYR   A N   
158  N  N   B TYR   A 9   ? 0.1672 0.2210 0.2364 -0.0292 0.0740  0.0163  9    TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1568 0.1761 0.1813 -0.0147 0.0327  0.0085  9    TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1537 0.1983 0.2180 -0.0198 0.0593  0.0298  9    TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1598 0.1661 0.1903 -0.0093 0.0248  0.0138  9    TYR   A C   
162  C  C   B TYR   A 9   ? 0.1565 0.1780 0.2223 -0.0167 0.0572  0.0462  9    TYR   A C   
163  O  O   A TYR   A 9   ? 0.1681 0.1742 0.1988 -0.0138 0.0199  0.0114  9    TYR   A O   
164  O  O   B TYR   A 9   ? 0.1787 0.1912 0.2348 -0.0220 0.0479  0.0502  9    TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1506 0.1738 0.1761 -0.0122 0.0259  0.0028  9    TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1485 0.2004 0.2128 -0.0100 0.0384  0.0219  9    TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1471 0.1741 0.1761 -0.0088 0.0276  -0.0065 9    TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1422 0.2022 0.2063 -0.0071 0.0380  0.0102  9    TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1504 0.1759 0.1853 -0.0085 0.0304  -0.0128 9    TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1516 0.2100 0.2245 -0.0151 0.0442  0.0038  9    TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1428 0.1724 0.1754 -0.0105 0.0251  -0.0032 9    TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1304 0.1927 0.1996 -0.0061 0.0323  0.0185  9    TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1504 0.1784 0.1893 -0.0092 0.0295  -0.0153 9    TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1487 0.2075 0.2289 -0.0156 0.0453  -0.0010 9    TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1453 0.1763 0.1799 -0.0112 0.0276  -0.0083 9    TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1320 0.1944 0.2005 -0.0055 0.0381  0.0108  9    TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1517 0.1807 0.1958 -0.0161 0.0338  -0.0109 9    TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1371 0.1990 0.2237 -0.0193 0.0488  0.0093  9    TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1635 0.1861 0.2109 -0.0208 0.0379  -0.0127 9    TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1449 0.2011 0.2378 -0.0254 0.0425  0.0065  9    TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1594 0.1528 0.1979 -0.0028 0.0150  0.0139  10   LEU   A N   
200  N  N   B LEU   A 10  ? 0.1433 0.1558 0.2211 -0.0106 0.0440  0.0452  10   LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1576 0.1492 0.2067 -0.0017 0.0049  0.0170  10   LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1302 0.1581 0.2430 -0.0237 0.0345  0.0505  10   LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1547 0.1442 0.1948 -0.0013 0.0016  0.0189  10   LEU   A C   
204  C  C   B LEU   A 10  ? 0.1276 0.1508 0.2159 -0.0277 0.0301  0.0495  10   LEU   A C   
205  O  O   A LEU   A 10  ? 0.1566 0.1442 0.2036 0.0010  -0.0051 0.0187  10   LEU   A O   
206  O  O   B LEU   A 10  ? 0.1364 0.1473 0.2142 -0.0266 0.0470  0.0480  10   LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1620 0.1535 0.2309 0.0010  0.0020  0.0193  10   LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1281 0.1668 0.2790 -0.0254 0.0236  0.0605  10   LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1744 0.1606 0.2641 0.0028  -0.0070 0.0226  10   LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1591 0.1866 0.3355 -0.0239 -0.0070 0.0612  10   LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1821 0.1679 0.2805 0.0035  -0.0032 0.0241  10   LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1761 0.1988 0.3724 -0.0267 0.0052  0.0550  10   LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1841 0.1662 0.2800 0.0056  -0.0104 0.0123  10   LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1848 0.1971 0.3622 -0.0139 -0.0224 0.0502  10   LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1565 0.1397 0.1788 -0.0040 0.0094  0.0221  11   LYS   A N   
238  N  N   B LYS   A 11  ? 0.1386 0.1476 0.2263 -0.0319 0.0318  0.0533  11   LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1533 0.1368 0.1733 -0.0106 0.0137  0.0248  11   LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1395 0.1472 0.2281 -0.0311 0.0240  0.0489  11   LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1402 0.1327 0.1690 -0.0106 0.0137  0.0242  11   LYS   A C   
242  C  C   B LYS   A 11  ? 0.1321 0.1425 0.2215 -0.0310 0.0233  0.0513  11   LYS   A C   
243  O  O   A LYS   A 11  ? 0.1379 0.1218 0.1715 -0.0172 0.0110  0.0288  11   LYS   A O   
244  O  O   B LYS   A 11  ? 0.1257 0.1557 0.2593 -0.0362 0.0245  0.0378  11   LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1621 0.1361 0.1667 -0.0187 0.0176  0.0286  11   LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1446 0.1503 0.2136 -0.0267 0.0258  0.0459  11   LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1716 0.1349 0.1642 -0.0270 0.0235  0.0332  11   LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.1555 0.1533 0.1982 -0.0228 0.0279  0.0461  11   LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1809 0.1375 0.1719 -0.0284 0.0149  0.0317  11   LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.1674 0.1598 0.1926 -0.0183 0.0123  0.0457  11   LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.1836 0.1337 0.1779 -0.0294 0.0071  0.0318  11   LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.1755 0.1566 0.1870 -0.0079 0.0061  0.0507  11   LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.1827 0.1325 0.1850 -0.0239 0.0010  0.0263  11   LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.1723 0.1545 0.1951 -0.0006 0.0052  0.0499  11   LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1328 0.1369 0.1550 -0.0178 0.0143  0.0163  12   LEU   A N   
282  N  N   B LEU   A 12  ? 0.1298 0.1440 0.2094 -0.0309 0.0120  0.0362  12   LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1320 0.1484 0.1569 -0.0249 0.0079  0.0217  12   LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1399 0.1583 0.2004 -0.0277 -0.0000 0.0448  12   LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1293 0.1487 0.1690 -0.0292 0.0093  0.0233  12   LEU   A C   
286  C  C   B LEU   A 12  ? 0.1369 0.1548 0.1938 -0.0314 0.0009  0.0395  12   LEU   A C   
287  O  O   A LEU   A 12  ? 0.1280 0.1504 0.1644 -0.0288 0.0151  0.0190  12   LEU   A O   
288  O  O   B LEU   A 12  ? 0.1437 0.1600 0.1942 -0.0255 -0.0000 0.0346  12   LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1330 0.1522 0.1626 -0.0286 0.0040  0.0233  12   LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1525 0.1603 0.2184 -0.0244 0.0007  0.0507  12   LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1426 0.1580 0.1886 -0.0258 0.0007  0.0251  12   LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1715 0.1615 0.2601 -0.0149 0.0027  0.0549  12   LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1534 0.1619 0.1979 -0.0215 0.0087  0.0237  12   LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1905 0.1644 0.2715 -0.0096 0.0095  0.0567  12   LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1429 0.1616 0.2095 -0.0201 -0.0075 0.0216  12   LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1725 0.1651 0.2939 0.0009  -0.0037 0.0500  12   LEU   A CD2 
319  N  N   . THR   A 13  ? 0.1283 0.1515 0.1858 -0.0284 0.0067  0.0274  13   THR   A N   
320  C  CA  . THR   A 13  ? 0.1410 0.1422 0.1842 -0.0236 0.0153  0.0249  13   THR   A CA  
321  C  C   . THR   A 13  ? 0.1366 0.1456 0.1982 -0.0282 0.0154  0.0242  13   THR   A C   
322  O  O   . THR   A 13  ? 0.1401 0.1437 0.1908 -0.0200 0.0131  0.0314  13   THR   A O   
323  C  CB  . THR   A 13  ? 0.1497 0.1510 0.1922 -0.0202 0.0119  0.0318  13   THR   A CB  
324  O  OG1 . THR   A 13  ? 0.1417 0.1537 0.1962 -0.0269 0.0064  0.0322  13   THR   A OG1 
325  C  CG2 . THR   A 13  ? 0.1595 0.1708 0.2137 -0.0284 0.0259  0.0179  13   THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1419 0.1410 0.1940 -0.0210 0.0095  0.0185  14   ASP   A N   
335  N  N   B ASP   A 14  ? 0.1478 0.1473 0.1950 -0.0276 0.0147  0.0384  14   ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1435 0.1405 0.1997 -0.0124 -0.0011 0.0177  14   ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1486 0.1578 0.2079 -0.0214 0.0076  0.0508  14   ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1402 0.1423 0.1797 -0.0133 -0.0009 0.0301  14   ASP   A C   
339  C  C   B ASP   A 14  ? 0.1453 0.1559 0.1903 -0.0220 -0.0036 0.0512  14   ASP   A C   
340  O  O   A ASP   A 14  ? 0.1486 0.1475 0.1778 -0.0136 -0.0014 0.0323  14   ASP   A O   
341  O  O   B ASP   A 14  ? 0.1644 0.1707 0.2119 -0.0349 -0.0102 0.0652  14   ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1557 0.1462 0.2404 -0.0086 -0.0101 0.0143  14   ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1640 0.1823 0.2668 -0.0240 0.0168  0.0817  14   ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1667 0.1738 0.2904 -0.0113 -0.0182 0.0201  14   ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1736 0.2540 0.3497 -0.0296 0.0126  0.0871  14   ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.1679 0.1822 0.3093 -0.0121 -0.0255 0.0333  14   ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1726 0.2788 0.3817 -0.0358 0.0114  0.1009  14   ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.1811 0.1880 0.3132 -0.0123 -0.0192 0.0189  14   ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1914 0.2835 0.3959 -0.0233 0.0102  0.0797  14   ASP   A OD2 
358  N  N   . ASN   A 15  ? 0.1355 0.1423 0.1805 -0.0202 0.0058  0.0401  15   ASN   A N   
359  C  CA  . ASN   A 15  ? 0.1376 0.1415 0.1954 -0.0181 0.0014  0.0301  15   ASN   A CA  
360  C  C   . ASN   A 15  ? 0.1293 0.1379 0.2102 -0.0192 0.0070  0.0250  15   ASN   A C   
361  O  O   . ASN   A 15  ? 0.1345 0.1403 0.2506 -0.0190 -0.0128 0.0298  15   ASN   A O   
362  C  CB  . ASN   A 15  ? 0.1336 0.1397 0.1881 -0.0158 0.0070  0.0343  15   ASN   A CB  
363  C  CG  . ASN   A 15  ? 0.1341 0.1491 0.1914 -0.0104 0.0132  0.0228  15   ASN   A CG  
364  O  OD1 . ASN   A 15  ? 0.1413 0.1551 0.2100 -0.0229 0.0089  0.0284  15   ASN   A OD1 
365  N  ND2 . ASN   A 15  ? 0.1367 0.1574 0.1843 -0.0190 0.0116  0.0290  15   ASN   A ND2 
373  N  N   . VAL   A 16  ? 0.1311 0.1333 0.1949 -0.0196 0.0033  0.0290  16   VAL   A N   
374  C  CA  . VAL   A 16  ? 0.1302 0.1342 0.1935 -0.0177 0.0090  0.0389  16   VAL   A CA  
375  C  C   . VAL   A 16  ? 0.1262 0.1311 0.1834 -0.0159 0.0031  0.0411  16   VAL   A C   
376  O  O   . VAL   A 16  ? 0.1295 0.1335 0.2082 -0.0171 0.0105  0.0325  16   VAL   A O   
377  C  CB  . VAL   A 16  ? 0.1451 0.1453 0.1910 -0.0077 0.0181  0.0339  16   VAL   A CB  
378  C  CG1 . VAL   A 16  ? 0.1599 0.1549 0.1865 0.0012  0.0152  0.0340  16   VAL   A CG1 
379  C  CG2 . VAL   A 16  ? 0.1523 0.1620 0.2073 0.0021  0.0342  0.0375  16   VAL   A CG2 
389  N  N   A TYR   A 17  ? 0.1286 0.1260 0.1779 -0.0178 0.0100  0.0342  17   TYR   A N   
390  N  N   B TYR   A 17  ? 0.1176 0.1288 0.1866 -0.0136 0.0141  0.0395  17   TYR   A N   
391  C  CA  A TYR   A 17  ? 0.1369 0.1247 0.1652 -0.0215 0.0119  0.0278  17   TYR   A CA  
392  C  CA  B TYR   A 17  ? 0.1238 0.1386 0.1718 -0.0141 0.0150  0.0384  17   TYR   A CA  
393  C  C   A TYR   A 17  ? 0.1328 0.1179 0.1643 -0.0207 0.0144  0.0245  17   TYR   A C   
394  C  C   B TYR   A 17  ? 0.1224 0.1357 0.1816 -0.0154 0.0107  0.0373  17   TYR   A C   
395  O  O   A TYR   A 17  ? 0.1329 0.1145 0.1660 -0.0176 0.0172  0.0248  17   TYR   A O   
396  O  O   B TYR   A 17  ? 0.1188 0.1415 0.1871 -0.0148 0.0029  0.0374  17   TYR   A O   
397  C  CB  A TYR   A 17  ? 0.1499 0.1270 0.1673 -0.0253 0.0051  0.0278  17   TYR   A CB  
398  C  CB  B TYR   A 17  ? 0.1333 0.1465 0.1766 -0.0076 0.0122  0.0359  17   TYR   A CB  
399  C  CG  A TYR   A 17  ? 0.1618 0.1296 0.1720 -0.0309 -0.0047 0.0284  17   TYR   A CG  
400  C  CG  B TYR   A 17  ? 0.1482 0.1588 0.1773 -0.0114 0.0049  0.0357  17   TYR   A CG  
401  C  CD1 A TYR   A 17  ? 0.1674 0.1335 0.1783 -0.0293 -0.0104 0.0268  17   TYR   A CD1 
402  C  CD1 B TYR   A 17  ? 0.1636 0.1699 0.1885 0.0027  0.0029  0.0419  17   TYR   A CD1 
403  C  CD2 A TYR   A 17  ? 0.1683 0.1309 0.1676 -0.0426 -0.0094 0.0294  17   TYR   A CD2 
404  C  CD2 B TYR   A 17  ? 0.1608 0.1701 0.1666 -0.0239 0.0066  0.0389  17   TYR   A CD2 
405  C  CE1 A TYR   A 17  ? 0.1770 0.1316 0.1817 -0.0332 -0.0190 0.0295  17   TYR   A CE1 
406  C  CE1 B TYR   A 17  ? 0.1906 0.1777 0.1957 0.0030  -0.0010 0.0442  17   TYR   A CE1 
407  C  CE2 A TYR   A 17  ? 0.1792 0.1304 0.1761 -0.0432 -0.0176 0.0216  17   TYR   A CE2 
408  C  CE2 B TYR   A 17  ? 0.1810 0.1769 0.1738 -0.0192 0.0020  0.0312  17   TYR   A CE2 
409  C  CZ  A TYR   A 17  ? 0.1846 0.1276 0.1810 -0.0406 -0.0260 0.0272  17   TYR   A CZ  
410  C  CZ  B TYR   A 17  ? 0.1963 0.1787 0.1881 -0.0074 -0.0108 0.0409  17   TYR   A CZ  
411  O  OH  A TYR   A 17  ? 0.1978 0.1246 0.1898 -0.0391 -0.0365 0.0321  17   TYR   A OH  
412  O  OH  B TYR   A 17  ? 0.2102 0.1811 0.2127 -0.0083 -0.0107 0.0504  17   TYR   A OH  
431  N  N   A ILE   A 18  ? 0.1311 0.1218 0.1689 -0.0210 0.0109  0.0289  18   ILE   A N   
432  N  N   B ILE   A 18  ? 0.1257 0.1362 0.2041 -0.0108 0.0178  0.0417  18   ILE   A N   
433  C  CA  A ILE   A 18  ? 0.1304 0.1314 0.1756 -0.0228 0.0062  0.0313  18   ILE   A CA  
434  C  CA  B ILE   A 18  ? 0.1283 0.1407 0.2253 -0.0128 0.0227  0.0470  18   ILE   A CA  
435  C  C   A ILE   A 18  ? 0.1301 0.1393 0.1727 -0.0229 0.0082  0.0319  18   ILE   A C   
436  C  C   B ILE   A 18  ? 0.1332 0.1429 0.2438 -0.0157 0.0314  0.0400  18   ILE   A C   
437  O  O   A ILE   A 18  ? 0.1312 0.1436 0.1699 -0.0245 0.0076  0.0339  18   ILE   A O   
438  O  O   B ILE   A 18  ? 0.1377 0.1479 0.2491 -0.0198 0.0424  0.0411  18   ILE   A O   
439  C  CB  A ILE   A 18  ? 0.1403 0.1431 0.1831 -0.0173 0.0017  0.0353  18   ILE   A CB  
440  C  CB  B ILE   A 18  ? 0.1446 0.1546 0.2158 0.0025  0.0105  0.0676  18   ILE   A CB  
441  C  CG1 A ILE   A 18  ? 0.1499 0.1527 0.1953 -0.0203 0.0006  0.0310  18   ILE   A CG1 
442  C  CG1 B ILE   A 18  ? 0.1566 0.1656 0.2102 0.0011  0.0082  0.0883  18   ILE   A CG1 
443  C  CG2 A ILE   A 18  ? 0.1395 0.1465 0.1878 -0.0215 -0.0028 0.0384  18   ILE   A CG2 
444  C  CG2 B ILE   A 18  ? 0.1455 0.1571 0.2207 0.0006  0.0006  0.0619  18   ILE   A CG2 
445  C  CD1 A ILE   A 18  ? 0.1685 0.1679 0.2224 -0.0161 -0.0053 0.0256  18   ILE   A CD1 
446  C  CD1 B ILE   A 18  ? 0.1876 0.1846 0.2323 0.0044  0.0034  0.0956  18   ILE   A CD1 
469  N  N   A LYS   A 19  ? 0.1350 0.1453 0.1795 -0.0172 0.0230  0.0313  19   LYS   A N   
470  N  N   B LYS   A 19  ? 0.1386 0.1427 0.2535 -0.0109 0.0414  0.0408  19   LYS   A N   
471  C  CA  A LYS   A 19  ? 0.1444 0.1568 0.1990 -0.0082 0.0318  0.0309  19   LYS   A CA  
472  C  CA  B LYS   A 19  ? 0.1494 0.1538 0.2747 0.0000  0.0386  0.0383  19   LYS   A CA  
473  C  C   A LYS   A 19  ? 0.1438 0.1585 0.2105 0.0033  0.0354  0.0320  19   LYS   A C   
474  C  C   B LYS   A 19  ? 0.1343 0.1468 0.2844 0.0004  0.0428  0.0443  19   LYS   A C   
475  O  O   A LYS   A 19  ? 0.1369 0.1595 0.2148 0.0044  0.0363  0.0360  19   LYS   A O   
476  O  O   B LYS   A 19  ? 0.1236 0.1440 0.2779 -0.0024 0.0324  0.0508  19   LYS   A O   
477  C  CB  A LYS   A 19  ? 0.1513 0.1658 0.2087 -0.0119 0.0428  0.0326  19   LYS   A CB  
478  C  CB  B LYS   A 19  ? 0.1649 0.1720 0.2799 0.0056  0.0451  0.0299  19   LYS   A CB  
479  C  CG  A LYS   A 19  ? 0.1659 0.1732 0.2168 -0.0049 0.0465  0.0343  19   LYS   A CG  
480  C  CG  B LYS   A 19  ? 0.1827 0.1937 0.2899 0.0106  0.0436  0.0120  19   LYS   A CG  
481  C  CD  A LYS   A 19  ? 0.1732 0.1787 0.2138 -0.0025 0.0585  0.0366  19   LYS   A CD  
482  C  CD  B LYS   A 19  ? 0.2091 0.2160 0.2804 0.0098  0.0535  0.0014  19   LYS   A CD  
483  C  CE  A LYS   A 19  ? 0.1819 0.1796 0.2238 -0.0048 0.0479  0.0321  19   LYS   A CE  
484  C  CE  B LYS   A 19  ? 0.2273 0.2302 0.2820 -0.0030 0.0646  0.0015  19   LYS   A CE  
485  N  NZ  A LYS   A 19  ? 0.1867 0.1809 0.2293 -0.0101 0.0494  0.0314  19   LYS   A NZ  
486  N  NZ  B LYS   A 19  ? 0.2415 0.2410 0.2781 -0.0115 0.0659  -0.0058 19   LYS   A NZ  
513  N  N   A ASN   A 20  ? 0.1539 0.1633 0.2237 0.0080  0.0320  0.0261  20   ASN   A N   
514  N  N   B ASN   A 20  ? 0.1362 0.1536 0.3096 -0.0034 0.0410  0.0493  20   ASN   A N   
515  C  CA  A ASN   A 20  ? 0.1664 0.1716 0.2243 0.0201  0.0308  0.0181  20   ASN   A CA  
516  C  CA  B ASN   A 20  ? 0.1409 0.1665 0.3276 0.0100  0.0462  0.0451  20   ASN   A CA  
517  C  C   A ASN   A 20  ? 0.1806 0.1686 0.2093 0.0231  0.0320  0.0142  20   ASN   A C   
518  C  C   B ASN   A 20  ? 0.1576 0.1682 0.3193 0.0047  0.0665  0.0374  20   ASN   A C   
519  O  O   A ASN   A 20  ? 0.1912 0.1703 0.2101 0.0230  0.0346  0.0151  20   ASN   A O   
520  O  O   B ASN   A 20  ? 0.1815 0.1848 0.3330 -0.0069 0.0758  0.0356  20   ASN   A O   
521  C  CB  A ASN   A 20  ? 0.1726 0.1856 0.2462 0.0234  0.0271  0.0228  20   ASN   A CB  
522  C  CB  B ASN   A 20  ? 0.1386 0.1792 0.3527 0.0208  0.0417  0.0684  20   ASN   A CB  
523  C  CG  A ASN   A 20  ? 0.1829 0.1994 0.2690 0.0252  0.0201  0.0283  20   ASN   A CG  
524  C  CG  B ASN   A 20  ? 0.1447 0.1944 0.3876 0.0366  0.0328  0.0826  20   ASN   A CG  
525  O  OD1 A ASN   A 20  ? 0.1989 0.2086 0.2864 0.0287  0.0181  0.0242  20   ASN   A OD1 
526  O  OD1 B ASN   A 20  ? 0.1737 0.2104 0.4294 0.0466  0.0435  0.0644  20   ASN   A OD1 
527  N  ND2 A ASN   A 20  ? 0.1845 0.2033 0.2778 0.0228  0.0169  0.0309  20   ASN   A ND2 
528  N  ND2 B ASN   A 20  ? 0.1547 0.1988 0.4033 0.0338  0.0224  0.0899  20   ASN   A ND2 
541  N  N   A ALA   A 21  ? 0.1855 0.1690 0.1997 0.0193  0.0188  0.0066  21   ALA   A N   
542  N  N   B ALA   A 21  ? 0.1538 0.1592 0.2926 -0.0017 0.0577  0.0337  21   ALA   A N   
543  C  CA  A ALA   A 21  ? 0.1947 0.1721 0.1879 0.0185  0.0094  0.0026  21   ALA   A CA  
544  C  CA  B ALA   A 21  ? 0.1656 0.1555 0.2741 0.0017  0.0502  0.0353  21   ALA   A CA  
545  C  C   A ALA   A 21  ? 0.1945 0.1743 0.1744 0.0209  0.0097  0.0045  21   ALA   A C   
546  C  C   B ALA   A 21  ? 0.1534 0.1523 0.2466 -0.0055 0.0456  0.0302  21   ALA   A C   
547  O  O   A ALA   A 21  ? 0.1996 0.1806 0.1689 0.0177  0.0091  0.0014  21   ALA   A O   
548  O  O   B ALA   A 21  ? 0.1552 0.1576 0.2434 -0.0153 0.0361  0.0113  21   ALA   A O   
549  C  CB  A ALA   A 21  ? 0.2050 0.1784 0.2034 0.0116  -0.0064 -0.0003 21   ALA   A CB  
550  C  CB  B ALA   A 21  ? 0.1870 0.1643 0.2848 -0.0077 0.0409  0.0454  21   ALA   A CB  
561  N  N   A ASP   A 22  ? 0.1929 0.1736 0.1758 0.0224  0.0089  0.0068  22   ASP   A N   
562  N  N   B ASP   A 22  ? 0.1595 0.1505 0.2401 -0.0050 0.0353  0.0384  22   ASP   A N   
563  C  CA  A ASP   A 22  ? 0.1917 0.1782 0.1772 0.0200  0.0006  0.0079  22   ASP   A CA  
564  C  CA  B ASP   A 22  ? 0.1641 0.1492 0.2099 -0.0050 0.0217  0.0320  22   ASP   A CA  
565  C  C   A ASP   A 22  ? 0.1815 0.1838 0.1603 0.0171  0.0024  0.0151  22   ASP   A C   
566  C  C   B ASP   A 22  ? 0.1544 0.1569 0.1683 -0.0165 0.0272  0.0286  22   ASP   A C   
567  O  O   A ASP   A 22  ? 0.1814 0.1924 0.1639 0.0157  0.0001  0.0197  22   ASP   A O   
568  O  O   B ASP   A 22  ? 0.1563 0.1711 0.1651 -0.0242 0.0292  0.0280  22   ASP   A O   
569  C  CB  A ASP   A 22  ? 0.2048 0.1804 0.1961 0.0161  -0.0025 -0.0037 22   ASP   A CB  
570  C  CB  B ASP   A 22  ? 0.1847 0.1527 0.2352 0.0052  0.0296  0.0195  22   ASP   A CB  
571  C  CG  A ASP   A 22  ? 0.2129 0.1812 0.2037 0.0071  -0.0072 -0.0068 22   ASP   A CG  
572  C  CG  B ASP   A 22  ? 0.2014 0.1601 0.2447 0.0075  0.0406  0.0239  22   ASP   A CG  
573  O  OD1 A ASP   A 22  ? 0.2073 0.1807 0.2089 -0.0086 -0.0250 -0.0010 22   ASP   A OD1 
574  O  OD1 B ASP   A 22  ? 0.1889 0.1653 0.2073 -0.0016 0.0424  0.0402  22   ASP   A OD1 
575  O  OD2 A ASP   A 22  ? 0.2227 0.1819 0.2091 0.0110  0.0027  -0.0209 22   ASP   A OD2 
576  O  OD2 B ASP   A 22  ? 0.2275 0.1755 0.3059 0.0081  0.0387  0.0266  22   ASP   A OD2 
585  N  N   A ILE   A 23  ? 0.1747 0.1801 0.1478 0.0149  0.0092  0.0156  23   ILE   A N   
586  N  N   B ILE   A 23  ? 0.1516 0.1584 0.1641 -0.0162 0.0260  0.0301  23   ILE   A N   
587  C  CA  A ILE   A 23  ? 0.1673 0.1719 0.1362 0.0112  0.0150  0.0147  23   ILE   A CA  
588  C  CA  B ILE   A 23  ? 0.1453 0.1624 0.1624 -0.0175 0.0186  0.0324  23   ILE   A CA  
589  C  C   A ILE   A 23  ? 0.1603 0.1787 0.1382 0.0127  0.0172  0.0059  23   ILE   A C   
590  C  C   B ILE   A 23  ? 0.1440 0.1678 0.1622 -0.0208 0.0218  0.0221  23   ILE   A C   
591  O  O   A ILE   A 23  ? 0.1629 0.1846 0.1442 0.0125  0.0120  0.0107  23   ILE   A O   
592  O  O   B ILE   A 23  ? 0.1464 0.1739 0.1594 -0.0165 0.0161  0.0185  23   ILE   A O   
593  C  CB  A ILE   A 23  ? 0.1717 0.1616 0.1230 0.0071  0.0191  0.0257  23   ILE   A CB  
594  C  CB  B ILE   A 23  ? 0.1506 0.1644 0.1466 -0.0074 0.0145  0.0272  23   ILE   A CB  
595  C  CG1 A ILE   A 23  ? 0.1775 0.1605 0.1441 0.0049  0.0210  0.0207  23   ILE   A CG1 
596  C  CG1 B ILE   A 23  ? 0.1546 0.1649 0.1621 -0.0055 0.0097  0.0220  23   ILE   A CG1 
597  C  CG2 A ILE   A 23  ? 0.1672 0.1604 0.1106 0.0045  0.0198  0.0373  23   ILE   A CG2 
598  C  CG2 B ILE   A 23  ? 0.1512 0.1641 0.1486 -0.0020 0.0095  0.0207  23   ILE   A CG2 
599  C  CD1 A ILE   A 23  ? 0.1787 0.1586 0.1542 0.0034  0.0178  0.0164  23   ILE   A CD1 
600  C  CD1 B ILE   A 23  ? 0.1559 0.1675 0.1618 -0.0016 0.0079  0.0006  23   ILE   A CD1 
623  N  N   A VAL   A 24  ? 0.1599 0.1823 0.1425 0.0082  0.0126  -0.0062 24   VAL   A N   
624  N  N   B VAL   A 24  ? 0.1543 0.1734 0.1742 -0.0241 0.0153  0.0152  24   VAL   A N   
625  C  CA  A VAL   A 24  ? 0.1642 0.1900 0.1528 0.0017  0.0079  -0.0119 24   VAL   A CA  
626  C  CA  B VAL   A 24  ? 0.1707 0.1825 0.1927 -0.0274 0.0156  0.0123  24   VAL   A CA  
627  C  C   A VAL   A 24  ? 0.1710 0.2013 0.1608 -0.0049 -0.0051 -0.0105 24   VAL   A C   
628  C  C   B VAL   A 24  ? 0.1785 0.2017 0.1967 -0.0264 0.0238  0.0029  24   VAL   A C   
629  O  O   A VAL   A 24  ? 0.1715 0.2012 0.1575 -0.0034 -0.0056 -0.0057 24   VAL   A O   
630  O  O   B VAL   A 24  ? 0.1857 0.2013 0.1986 -0.0237 0.0266  0.0025  24   VAL   A O   
631  C  CB  A VAL   A 24  ? 0.1645 0.1898 0.1563 -0.0016 0.0205  -0.0127 24   VAL   A CB  
632  C  CB  B VAL   A 24  ? 0.1786 0.1863 0.2208 -0.0348 0.0111  0.0273  24   VAL   A CB  
633  C  CG1 A VAL   A 24  ? 0.1712 0.1937 0.1607 0.0017  0.0303  -0.0179 24   VAL   A CG1 
634  C  CG1 B VAL   A 24  ? 0.2026 0.1960 0.2634 -0.0315 -0.0056 0.0212  24   VAL   A CG1 
635  C  CG2 A VAL   A 24  ? 0.1685 0.1891 0.1572 -0.0029 0.0264  -0.0091 24   VAL   A CG2 
636  C  CG2 B VAL   A 24  ? 0.1887 0.1906 0.2259 -0.0338 0.0146  0.0369  24   VAL   A CG2 
655  N  N   A GLU   A 25  ? 0.1802 0.2161 0.1701 -0.0129 -0.0099 -0.0163 25   GLU   A N   
656  N  N   B GLU   A 25  ? 0.1818 0.2301 0.1988 -0.0233 0.0444  -0.0015 25   GLU   A N   
657  C  CA  A GLU   A 25  ? 0.1940 0.2322 0.1950 -0.0132 -0.0022 -0.0139 25   GLU   A CA  
658  C  CA  B GLU   A 25  ? 0.1934 0.2566 0.2037 -0.0234 0.0596  0.0005  25   GLU   A CA  
659  C  C   A GLU   A 25  ? 0.1870 0.2305 0.1739 -0.0207 0.0054  -0.0078 25   GLU   A C   
660  C  C   B GLU   A 25  ? 0.1861 0.2670 0.1742 -0.0302 0.0555  0.0027  25   GLU   A C   
661  O  O   A GLU   A 25  ? 0.1881 0.2364 0.1722 -0.0183 0.0035  -0.0061 25   GLU   A O   
662  O  O   B GLU   A 25  ? 0.1967 0.2771 0.1733 -0.0275 0.0565  -0.0008 25   GLU   A O   
663  C  CB  A GLU   A 25  ? 0.2178 0.2484 0.2444 -0.0087 0.0003  -0.0141 25   GLU   A CB  
664  C  CB  B GLU   A 25  ? 0.2186 0.2719 0.2462 -0.0229 0.0726  0.0047  25   GLU   A CB  
665  C  CG  A GLU   A 25  ? 0.2388 0.2634 0.2933 -0.0094 -0.0026 -0.0156 25   GLU   A CG  
666  C  CG  B GLU   A 25  ? 0.2529 0.2938 0.3304 -0.0255 0.0653  0.0057  25   GLU   A CG  
667  C  CD  A GLU   A 25  ? 0.2528 0.2775 0.3331 -0.0122 -0.0060 -0.0155 25   GLU   A CD  
668  C  CD  B GLU   A 25  ? 0.2820 0.3140 0.4013 -0.0253 0.0615  0.0097  25   GLU   A CD  
669  O  OE1 A GLU   A 25  ? 0.2590 0.2851 0.3439 -0.0110 -0.0112 -0.0200 25   GLU   A OE1 
670  O  OE1 B GLU   A 25  ? 0.2946 0.3225 0.4322 -0.0207 0.0551  0.0100  25   GLU   A OE1 
671  O  OE2 A GLU   A 25  ? 0.2563 0.2818 0.3504 -0.0148 -0.0055 -0.0176 25   GLU   A OE2 
672  O  OE2 B GLU   A 25  ? 0.2917 0.3202 0.4265 -0.0277 0.0604  0.0106  25   GLU   A OE2 
685  N  N   A GLU   A 26  ? 0.1822 0.2211 0.1722 -0.0357 0.0162  -0.0056 26   GLU   A N   
686  N  N   B GLU   A 26  ? 0.1801 0.2628 0.1827 -0.0443 0.0514  -0.0025 26   GLU   A N   
687  C  CA  A GLU   A 26  ? 0.1902 0.2154 0.1654 -0.0481 0.0240  0.0011  26   GLU   A CA  
688  C  CA  B GLU   A 26  ? 0.1941 0.2568 0.1720 -0.0535 0.0537  0.0061  26   GLU   A CA  
689  C  C   A GLU   A 26  ? 0.1856 0.2147 0.1434 -0.0451 0.0272  0.0078  26   GLU   A C   
690  C  C   B GLU   A 26  ? 0.1914 0.2367 0.1387 -0.0463 0.0463  0.0094  26   GLU   A C   
691  O  O   A GLU   A 26  ? 0.1882 0.2185 0.1383 -0.0481 0.0231  0.0138  26   GLU   A O   
692  O  O   B GLU   A 26  ? 0.2015 0.2416 0.1425 -0.0489 0.0446  0.0164  26   GLU   A O   
693  C  CB  A GLU   A 26  ? 0.2029 0.2076 0.1931 -0.0589 0.0256  0.0015  26   GLU   A CB  
694  C  CB  B GLU   A 26  ? 0.2127 0.2669 0.2103 -0.0593 0.0358  -0.0047 26   GLU   A CB  
695  C  CG  A GLU   A 26  ? 0.2164 0.2020 0.2428 -0.0665 0.0362  -0.0024 26   GLU   A CG  
696  C  CG  B GLU   A 26  ? 0.2246 0.2781 0.2566 -0.0567 0.0448  -0.0246 26   GLU   A CG  
697  C  CD  A GLU   A 26  ? 0.2257 0.1918 0.2719 -0.0739 0.0544  -0.0088 26   GLU   A CD  
698  C  CD  B GLU   A 26  ? 0.2294 0.2876 0.2786 -0.0577 0.0679  -0.0440 26   GLU   A CD  
699  O  OE1 A GLU   A 26  ? 0.2328 0.1924 0.2886 -0.0663 0.0498  -0.0408 26   GLU   A OE1 
700  O  OE1 B GLU   A 26  ? 0.2238 0.3079 0.2544 -0.0459 0.0975  -0.0746 26   GLU   A OE1 
701  O  OE2 A GLU   A 26  ? 0.2260 0.1886 0.2641 -0.0799 0.0725  0.0065  26   GLU   A OE2 
702  O  OE2 B GLU   A 26  ? 0.2356 0.2822 0.2722 -0.0632 0.0681  -0.0471 26   GLU   A OE2 
715  N  N   . ALA   A 27  ? 0.1771 0.2103 0.1445 -0.0424 0.0345  0.0105  27   ALA   A N   
716  C  CA  . ALA   A 27  ? 0.1798 0.2078 0.1388 -0.0302 0.0298  0.0057  27   ALA   A CA  
717  C  C   . ALA   A 27  ? 0.2103 0.2348 0.1457 -0.0363 0.0334  -0.0113 27   ALA   A C   
718  O  O   . ALA   A 27  ? 0.2064 0.2397 0.1419 -0.0472 0.0218  -0.0116 27   ALA   A O   
719  C  CB  . ALA   A 27  ? 0.1663 0.1900 0.1409 -0.0340 0.0194  0.0110  27   ALA   A CB  
726  N  N   A LYS   A 28  ? 0.2432 0.2642 0.1869 -0.0291 0.0288  -0.0166 28   LYS   A N   
727  N  N   B LYS   A 28  ? 0.2355 0.2495 0.1511 -0.0282 0.0262  -0.0439 28   LYS   A N   
728  C  CA  A LYS   A 28  ? 0.2812 0.2997 0.2356 -0.0204 0.0239  -0.0211 28   LYS   A CA  
729  C  CA  B LYS   A 28  ? 0.2762 0.2846 0.1781 -0.0139 0.0229  -0.0670 28   LYS   A CA  
730  C  C   A LYS   A 28  ? 0.3003 0.3217 0.2425 -0.0232 0.0250  -0.0177 28   LYS   A C   
731  C  C   B LYS   A 28  ? 0.2962 0.3141 0.1594 -0.0234 0.0340  -0.0570 28   LYS   A C   
732  O  O   A LYS   A 28  ? 0.3067 0.3271 0.2501 -0.0221 0.0185  -0.0197 28   LYS   A O   
733  O  O   B LYS   A 28  ? 0.3086 0.3282 0.1864 -0.0229 0.0119  -0.0583 28   LYS   A O   
734  C  CB  A LYS   A 28  ? 0.2998 0.3146 0.2806 -0.0094 0.0205  -0.0238 28   LYS   A CB  
735  C  CB  B LYS   A 28  ? 0.3004 0.2998 0.2321 0.0086  0.0184  -0.0805 28   LYS   A CB  
736  C  CG  A LYS   A 28  ? 0.3160 0.3274 0.3273 -0.0003 0.0181  -0.0210 28   LYS   A CG  
737  C  CG  B LYS   A 28  ? 0.3251 0.3179 0.3008 0.0236  0.0152  -0.0711 28   LYS   A CG  
738  C  CD  A LYS   A 28  ? 0.3285 0.3389 0.3713 0.0062  0.0140  -0.0170 28   LYS   A CD  
739  C  CD  B LYS   A 28  ? 0.3479 0.3394 0.3787 0.0331  0.0118  -0.0542 28   LYS   A CD  
740  C  CE  A LYS   A 28  ? 0.3371 0.3472 0.3996 0.0101  0.0112  -0.0174 28   LYS   A CE  
741  C  CE  B LYS   A 28  ? 0.3649 0.3560 0.4332 0.0357  0.0114  -0.0497 28   LYS   A CE  
742  N  NZ  A LYS   A 28  ? 0.3424 0.3512 0.4195 0.0130  0.0118  -0.0196 28   LYS   A NZ  
743  N  NZ  B LYS   A 28  ? 0.3732 0.3641 0.4639 0.0383  0.0122  -0.0538 28   LYS   A NZ  
770  N  N   A LYS   A 29  ? 0.3111 0.3375 0.2549 -0.0268 0.0345  -0.0081 29   LYS   A N   
771  N  N   B LYS   A 29  ? 0.3010 0.3341 0.1535 -0.0321 0.0716  -0.0241 29   LYS   A N   
772  C  CA  A LYS   A 29  ? 0.3252 0.3530 0.2754 -0.0290 0.0402  -0.0023 29   LYS   A CA  
773  C  CA  B LYS   A 29  ? 0.3135 0.3560 0.1654 -0.0383 0.0994  0.0010  29   LYS   A CA  
774  C  C   A LYS   A 29  ? 0.3181 0.3465 0.2388 -0.0364 0.0321  0.0012  29   LYS   A C   
775  C  C   B LYS   A 29  ? 0.3012 0.3456 0.1309 -0.0492 0.0793  0.0151  29   LYS   A C   
776  O  O   A LYS   A 29  ? 0.3224 0.3526 0.2404 -0.0338 0.0306  -0.0019 29   LYS   A O   
777  O  O   B LYS   A 29  ? 0.3169 0.3658 0.1349 -0.0428 0.0701  0.0060  29   LYS   A O   
778  C  CB  A LYS   A 29  ? 0.3437 0.3722 0.3292 -0.0237 0.0508  -0.0000 29   LYS   A CB  
779  C  CB  B LYS   A 29  ? 0.3377 0.3864 0.2323 -0.0343 0.1335  0.0106  29   LYS   A CB  
780  C  CG  A LYS   A 29  ? 0.3609 0.3896 0.3823 -0.0185 0.0548  0.0025  29   LYS   A CG  
781  C  CG  B LYS   A 29  ? 0.3641 0.4134 0.3128 -0.0273 0.1420  0.0139  29   LYS   A CG  
782  C  CD  A LYS   A 29  ? 0.3756 0.4047 0.4340 -0.0147 0.0560  0.0032  29   LYS   A CD  
783  C  CD  B LYS   A 29  ? 0.3861 0.4360 0.3972 -0.0208 0.1428  0.0134  29   LYS   A CD  
784  C  CE  A LYS   A 29  ? 0.3851 0.4153 0.4667 -0.0121 0.0580  0.0019  29   LYS   A CE  
785  C  CE  B LYS   A 29  ? 0.4013 0.4517 0.4458 -0.0168 0.1470  0.0081  29   LYS   A CE  
786  N  NZ  A LYS   A 29  ? 0.3896 0.4210 0.4891 -0.0105 0.0585  0.0003  29   LYS   A NZ  
787  N  NZ  B LYS   A 29  ? 0.4082 0.4598 0.4841 -0.0140 0.1476  0.0028  29   LYS   A NZ  
814  N  N   A VAL   A 30  ? 0.3066 0.3315 0.2161 -0.0452 0.0243  0.0060  30   VAL   A N   
815  N  N   B VAL   A 30  ? 0.2815 0.3244 0.1252 -0.0701 0.0602  0.0240  30   VAL   A N   
816  C  CA  A VAL   A 30  ? 0.2988 0.3165 0.1965 -0.0497 0.0141  0.0111  30   VAL   A CA  
817  C  CA  B VAL   A 30  ? 0.2720 0.3042 0.1187 -0.0825 0.0344  0.0413  30   VAL   A CA  
818  C  C   A VAL   A 30  ? 0.2927 0.3005 0.1720 -0.0469 0.0084  0.0166  30   VAL   A C   
819  C  C   B VAL   A 30  ? 0.2749 0.2887 0.1073 -0.0747 0.0247  0.0399  30   VAL   A C   
820  O  O   A VAL   A 30  ? 0.2941 0.3020 0.1730 -0.0451 0.0060  0.0180  30   VAL   A O   
821  O  O   B VAL   A 30  ? 0.2893 0.2959 0.1211 -0.0730 0.0092  0.0402  30   VAL   A O   
822  C  CB  A VAL   A 30  ? 0.2977 0.3171 0.2088 -0.0542 0.0063  0.0090  30   VAL   A CB  
823  C  CB  B VAL   A 30  ? 0.2707 0.3021 0.1502 -0.0915 0.0078  0.0415  30   VAL   A CB  
824  C  CG1 A VAL   A 30  ? 0.2984 0.3153 0.2151 -0.0546 0.0017  0.0092  30   VAL   A CG1 
825  C  CG1 B VAL   A 30  ? 0.2763 0.2994 0.1694 -0.0914 -0.0080 0.0436  30   VAL   A CG1 
826  C  CG2 A VAL   A 30  ? 0.2967 0.3194 0.2173 -0.0566 0.0049  0.0086  30   VAL   A CG2 
827  C  CG2 B VAL   A 30  ? 0.2682 0.3073 0.1752 -0.1011 0.0050  0.0397  30   VAL   A CG2 
846  N  N   A LYS   A 31  ? 0.2838 0.2830 0.1625 -0.0450 0.0023  0.0162  31   LYS   A N   
847  N  N   B LYS   A 31  ? 0.2691 0.2735 0.1010 -0.0709 0.0193  0.0385  31   LYS   A N   
848  C  CA  A LYS   A 31  ? 0.2802 0.2718 0.1726 -0.0384 -0.0099 0.0181  31   LYS   A CA  
849  C  CA  B LYS   A 31  ? 0.2752 0.2720 0.1163 -0.0546 -0.0026 0.0270  31   LYS   A CA  
850  C  C   A LYS   A 31  ? 0.2580 0.2440 0.1288 -0.0327 -0.0193 0.0336  31   LYS   A C   
851  C  C   B LYS   A 31  ? 0.2486 0.2565 0.1008 -0.0419 -0.0145 0.0462  31   LYS   A C   
852  O  O   A LYS   A 31  ? 0.2563 0.2457 0.1196 -0.0272 -0.0287 0.0463  31   LYS   A O   
853  O  O   B LYS   A 31  ? 0.2590 0.2700 0.1383 -0.0377 -0.0305 0.0485  31   LYS   A O   
854  C  CB  A LYS   A 31  ? 0.3001 0.2889 0.2404 -0.0368 -0.0135 0.0085  31   LYS   A CB  
855  C  CB  B LYS   A 31  ? 0.3122 0.2908 0.2043 -0.0525 -0.0140 0.0014  31   LYS   A CB  
856  C  CG  A LYS   A 31  ? 0.3203 0.3036 0.3181 -0.0307 -0.0164 0.0026  31   LYS   A CG  
857  C  CG  B LYS   A 31  ? 0.3517 0.3136 0.3237 -0.0441 -0.0277 -0.0143 31   LYS   A CG  
858  C  CD  A LYS   A 31  ? 0.3359 0.3148 0.3809 -0.0246 -0.0189 -0.0010 31   LYS   A CD  
859  C  CD  B LYS   A 31  ? 0.3841 0.3327 0.4148 -0.0386 -0.0391 -0.0260 31   LYS   A CD  
860  C  CE  A LYS   A 31  ? 0.3449 0.3221 0.4191 -0.0189 -0.0220 -0.0057 31   LYS   A CE  
861  C  CE  B LYS   A 31  ? 0.4068 0.3469 0.4749 -0.0367 -0.0486 -0.0379 31   LYS   A CE  
862  N  NZ  A LYS   A 31  ? 0.3493 0.3258 0.4450 -0.0145 -0.0259 -0.0094 31   LYS   A NZ  
863  N  NZ  B LYS   A 31  ? 0.4209 0.3551 0.5171 -0.0341 -0.0541 -0.0488 31   LYS   A NZ  
890  N  N   A PRO   A 32  ? 0.2383 0.2174 0.1276 -0.0343 -0.0192 0.0283  32   PRO   A N   
891  N  N   B PRO   A 32  ? 0.2144 0.2280 0.0940 -0.0366 -0.0020 0.0342  32   PRO   A N   
892  C  CA  A PRO   A 32  ? 0.2293 0.2024 0.1391 -0.0349 -0.0184 0.0338  32   PRO   A CA  
893  C  CA  B PRO   A 32  ? 0.2072 0.2131 0.1325 -0.0282 -0.0042 0.0483  32   PRO   A CA  
894  C  C   A PRO   A 32  ? 0.2211 0.1919 0.1326 -0.0311 -0.0197 0.0409  32   PRO   A C   
895  C  C   B PRO   A 32  ? 0.2077 0.2095 0.1435 -0.0137 -0.0089 0.0515  32   PRO   A C   
896  O  O   A PRO   A 32  ? 0.2177 0.1847 0.1254 -0.0385 -0.0228 0.0377  32   PRO   A O   
897  O  O   B PRO   A 32  ? 0.2107 0.2049 0.1697 -0.0118 -0.0257 0.0488  32   PRO   A O   
898  C  CB  A PRO   A 32  ? 0.2305 0.2050 0.1499 -0.0337 -0.0200 0.0264  32   PRO   A CB  
899  C  CB  B PRO   A 32  ? 0.2022 0.2124 0.1447 -0.0249 -0.0093 0.0300  32   PRO   A CB  
900  C  CG  A PRO   A 32  ? 0.2318 0.2091 0.1386 -0.0307 -0.0228 0.0262  32   PRO   A CG  
901  C  CG  B PRO   A 32  ? 0.2017 0.2170 0.0915 -0.0221 -0.0128 0.0188  32   PRO   A CG  
902  C  CD  A PRO   A 32  ? 0.2332 0.2114 0.1303 -0.0331 -0.0210 0.0289  32   PRO   A CD  
903  C  CD  B PRO   A 32  ? 0.2022 0.2199 0.0825 -0.0301 0.0037  0.0240  32   PRO   A CD  
918  N  N   A THR   A 33  ? 0.2162 0.1917 0.1325 -0.0231 -0.0201 0.0443  33   THR   A N   
919  N  N   B THR   A 33  ? 0.2107 0.2068 0.1392 -0.0095 -0.0053 0.0488  33   THR   A N   
920  C  CA  A THR   A 33  ? 0.2138 0.1965 0.1401 -0.0164 -0.0264 0.0414  33   THR   A CA  
921  C  CA  B THR   A 33  ? 0.2157 0.2058 0.1397 -0.0041 -0.0203 0.0473  33   THR   A CA  
922  C  C   A THR   A 33  ? 0.1923 0.1927 0.1296 -0.0184 -0.0299 0.0388  33   THR   A C   
923  C  C   B THR   A 33  ? 0.1937 0.1885 0.1379 -0.0165 -0.0291 0.0370  33   THR   A C   
924  O  O   A THR   A 33  ? 0.1837 0.1968 0.1278 -0.0103 -0.0398 0.0380  33   THR   A O   
925  O  O   B THR   A 33  ? 0.1893 0.1799 0.1542 -0.0162 -0.0323 0.0336  33   THR   A O   
926  C  CB  A THR   A 33  ? 0.2325 0.2044 0.1697 -0.0091 -0.0261 0.0409  33   THR   A CB  
927  C  CB  B THR   A 33  ? 0.2459 0.2229 0.1655 0.0073  -0.0196 0.0662  33   THR   A CB  
928  O  OG1 A THR   A 33  ? 0.2464 0.2086 0.1920 -0.0004 -0.0185 0.0436  33   THR   A OG1 
929  O  OG1 B THR   A 33  ? 0.2702 0.2357 0.1823 0.0208  -0.0111 0.0828  33   THR   A OG1 
930  C  CG2 A THR   A 33  ? 0.2358 0.2089 0.1737 -0.0075 -0.0323 0.0392  33   THR   A CG2 
931  C  CG2 B THR   A 33  ? 0.2521 0.2296 0.1810 0.0090  -0.0231 0.0600  33   THR   A CG2 
946  N  N   . VAL   A 34  ? 0.1762 0.1810 0.1216 -0.0260 -0.0180 0.0367  34   VAL   A N   
947  C  CA  . VAL   A 34  ? 0.1658 0.1621 0.1211 -0.0219 -0.0135 0.0346  34   VAL   A CA  
948  C  C   . VAL   A 34  ? 0.1544 0.1542 0.1117 -0.0234 -0.0075 0.0215  34   VAL   A C   
949  O  O   . VAL   A 34  ? 0.1556 0.1547 0.1347 -0.0266 -0.0071 0.0333  34   VAL   A O   
950  C  CB  . VAL   A 34  ? 0.1737 0.1629 0.1444 -0.0164 -0.0078 0.0269  34   VAL   A CB  
951  C  CG1 . VAL   A 34  ? 0.1867 0.1672 0.1327 -0.0106 0.0079  0.0171  34   VAL   A CG1 
952  C  CG2 . VAL   A 34  ? 0.1742 0.1755 0.1834 -0.0150 -0.0179 0.0257  34   VAL   A CG2 
963  N  N   . VAL   A 35  ? 0.1446 0.1458 0.1092 -0.0269 -0.0140 0.0207  35   VAL   A N   
964  C  CA  . VAL   A 35  ? 0.1362 0.1419 0.1073 -0.0175 -0.0069 0.0207  35   VAL   A CA  
965  C  C   . VAL   A 35  ? 0.1269 0.1311 0.1042 -0.0171 -0.0037 0.0220  35   VAL   A C   
966  O  O   . VAL   A 35  ? 0.1221 0.1393 0.1330 -0.0181 0.0029  0.0114  35   VAL   A O   
967  C  CB  . VAL   A 35  ? 0.1426 0.1544 0.1160 -0.0113 0.0028  0.0042  35   VAL   A CB  
968  C  CG1 . VAL   A 35  ? 0.1497 0.1539 0.1315 -0.0019 0.0022  -0.0023 35   VAL   A CG1 
969  C  CG2 . VAL   A 35  ? 0.1393 0.1504 0.1471 -0.0061 0.0154  0.0009  35   VAL   A CG2 
979  N  N   . VAL   A 36  ? 0.1220 0.1301 0.0997 -0.0139 0.0001  0.0241  36   VAL   A N   
980  C  CA  . VAL   A 36  ? 0.1124 0.1274 0.0964 -0.0079 -0.0004 0.0154  36   VAL   A CA  
981  C  C   . VAL   A 36  ? 0.1118 0.1264 0.1068 -0.0113 0.0053  0.0092  36   VAL   A C   
982  O  O   . VAL   A 36  ? 0.1145 0.1245 0.1351 -0.0054 0.0130  0.0103  36   VAL   A O   
983  C  CB  . VAL   A 36  ? 0.1145 0.1183 0.1090 -0.0127 0.0023  0.0162  36   VAL   A CB  
984  C  CG1 . VAL   A 36  ? 0.1163 0.1212 0.1402 -0.0113 -0.0007 0.0071  36   VAL   A CG1 
985  C  CG2 . VAL   A 36  ? 0.1244 0.1193 0.1311 -0.0086 -0.0051 0.0214  36   VAL   A CG2 
995  N  N   . ASN   A 37  ? 0.1067 0.1197 0.1076 0.0001  0.0018  0.0158  37   ASN   A N   
996  C  CA  . ASN   A 37  ? 0.1099 0.1194 0.1080 -0.0003 0.0005  0.0174  37   ASN   A CA  
997  C  C   . ASN   A 37  ? 0.1114 0.1187 0.1058 -0.0013 0.0063  0.0283  37   ASN   A C   
998  O  O   . ASN   A 37  ? 0.1176 0.1237 0.1125 0.0022  0.0071  0.0179  37   ASN   A O   
999  C  CB  . ASN   A 37  ? 0.1120 0.1117 0.1197 0.0045  0.0015  0.0124  37   ASN   A CB  
1000 C  CG  . ASN   A 37  ? 0.1155 0.1136 0.1296 0.0019  0.0040  0.0126  37   ASN   A CG  
1001 O  OD1 . ASN   A 37  ? 0.1161 0.1127 0.1561 -0.0009 0.0058  0.0190  37   ASN   A OD1 
1002 N  ND2 . ASN   A 37  ? 0.1127 0.1160 0.1329 -0.0042 -0.0016 0.0283  37   ASN   A ND2 
1009 N  N   A ALA   A 38  ? 0.1124 0.1242 0.1021 0.0037  0.0036  0.0130  38   ALA   A N   
1010 N  N   B ALA   A 38  ? 0.1114 0.1314 0.1155 -0.0017 0.0052  0.0248  38   ALA   A N   
1011 C  CA  A ALA   A 38  ? 0.1141 0.1256 0.1016 0.0060  -0.0010 -0.0004 38   ALA   A CA  
1012 C  CA  B ALA   A 38  ? 0.1147 0.1380 0.1275 -0.0051 0.0023  0.0286  38   ALA   A CA  
1013 C  C   A ALA   A 38  ? 0.1165 0.1245 0.1101 0.0090  -0.0001 -0.0030 38   ALA   A C   
1014 C  C   B ALA   A 38  ? 0.1150 0.1307 0.1132 0.0005  -0.0045 0.0148  38   ALA   A C   
1015 O  O   A ALA   A 38  ? 0.1203 0.1216 0.1046 0.0152  -0.0073 -0.0133 38   ALA   A O   
1016 O  O   B ALA   A 38  ? 0.1184 0.1320 0.1177 0.0024  -0.0139 0.0210  38   ALA   A O   
1017 C  CB  A ALA   A 38  ? 0.1172 0.1363 0.1005 0.0006  -0.0155 -0.0118 38   ALA   A CB  
1018 C  CB  B ALA   A 38  ? 0.1256 0.1634 0.1459 -0.0167 -0.0111 0.0230  38   ALA   A CB  
1029 N  N   . ALA   A 39  ? 0.1172 0.1268 0.1346 0.0031  0.0003  0.0149  39   ALA   A N   
1030 C  CA  . ALA   A 39  ? 0.1172 0.1228 0.1271 -0.0021 0.0047  0.0097  39   ALA   A CA  
1031 C  C   . ALA   A 39  ? 0.1189 0.1226 0.1194 -0.0042 0.0042  0.0121  39   ALA   A C   
1032 O  O   . ALA   A 39  ? 0.1324 0.1239 0.1266 -0.0062 0.0037  0.0134  39   ALA   A O   
1033 C  CB  . ALA   A 39  ? 0.1224 0.1399 0.1359 0.0005  -0.0008 0.0034  39   ALA   A CB  
1040 N  N   . ASN   A 40  ? 0.1359 0.1204 0.1224 -0.0074 0.0179  0.0083  40   ASN   A N   
1041 C  CA  . ASN   A 40  ? 0.1403 0.1190 0.1375 -0.0058 0.0018  0.0067  40   ASN   A CA  
1042 C  C   . ASN   A 40  ? 0.1448 0.1087 0.1272 -0.0009 0.0224  0.0176  40   ASN   A C   
1043 O  O   . ASN   A 40  ? 0.1380 0.1123 0.1252 -0.0042 0.0138  0.0183  40   ASN   A O   
1044 C  CB  . ASN   A 40  ? 0.1465 0.1311 0.1337 0.0027  -0.0032 0.0096  40   ASN   A CB  
1045 C  CG  . ASN   A 40  ? 0.1531 0.1249 0.1601 -0.0001 -0.0049 0.0158  40   ASN   A CG  
1046 O  OD1 . ASN   A 40  ? 0.1591 0.1320 0.1885 -0.0037 0.0142  0.0003  40   ASN   A OD1 
1047 N  ND2 . ASN   A 40  ? 0.1557 0.1375 0.1921 0.0075  -0.0055 -0.0045 40   ASN   A ND2 
1054 N  N   . VAL   A 41  ? 0.1490 0.1200 0.1265 -0.0019 0.0235  0.0209  41   VAL   A N   
1055 C  CA  . VAL   A 41  ? 0.1542 0.1208 0.1359 -0.0056 0.0323  0.0178  41   VAL   A CA  
1056 C  C   . VAL   A 41  ? 0.1470 0.1171 0.1317 -0.0032 0.0270  0.0156  41   VAL   A C   
1057 O  O   . VAL   A 41  ? 0.1477 0.1148 0.1698 0.0019  0.0290  0.0081  41   VAL   A O   
1058 C  CB  . VAL   A 41  ? 0.1755 0.1372 0.1426 -0.0106 0.0426  0.0092  41   VAL   A CB  
1059 C  CG1 . VAL   A 41  ? 0.1885 0.1388 0.1599 -0.0091 0.0438  0.0028  41   VAL   A CG1 
1060 C  CG2 . VAL   A 41  ? 0.2003 0.1490 0.1370 -0.0197 0.0460  0.0090  41   VAL   A CG2 
1070 N  N   . TYR   A 42  ? 0.1390 0.1171 0.1443 -0.0002 0.0293  0.0223  42   TYR   A N   
1071 C  CA  . TYR   A 42  ? 0.1386 0.1141 0.1489 -0.0069 0.0317  0.0230  42   TYR   A CA  
1072 C  C   . TYR   A 42  ? 0.1284 0.1109 0.1448 -0.0013 0.0232  0.0258  42   TYR   A C   
1073 O  O   . TYR   A 42  ? 0.1279 0.1163 0.1779 -0.0128 0.0252  0.0033  42   TYR   A O   
1074 C  CB  . TYR   A 42  ? 0.1624 0.1253 0.1477 -0.0077 0.0327  0.0228  42   TYR   A CB  
1075 C  CG  . TYR   A 42  ? 0.1835 0.1375 0.1327 -0.0080 0.0279  0.0281  42   TYR   A CG  
1076 C  CD1 . TYR   A 42  ? 0.1890 0.1529 0.1409 -0.0133 0.0256  0.0313  42   TYR   A CD1 
1077 C  CD2 . TYR   A 42  ? 0.1987 0.1567 0.1524 -0.0043 0.0212  0.0184  42   TYR   A CD2 
1078 C  CE1 . TYR   A 42  ? 0.1983 0.1645 0.1425 -0.0195 0.0296  0.0212  42   TYR   A CE1 
1079 C  CE2 . TYR   A 42  ? 0.2125 0.1715 0.1635 -0.0157 0.0246  0.0264  42   TYR   A CE2 
1080 C  CZ  . TYR   A 42  ? 0.2212 0.1745 0.1434 -0.0244 0.0333  0.0187  42   TYR   A CZ  
1081 O  OH  . TYR   A 42  ? 0.2412 0.1991 0.1629 -0.0352 0.0365  0.0071  42   TYR   A OH  
1091 N  N   . LEU   A 43  ? 0.1268 0.1171 0.1339 -0.0038 0.0165  0.0108  43   LEU   A N   
1092 C  CA  . LEU   A 43  ? 0.1198 0.1180 0.1267 -0.0077 0.0086  0.0128  43   LEU   A CA  
1093 C  C   . LEU   A 43  ? 0.1222 0.1216 0.1280 -0.0041 0.0084  0.0079  43   LEU   A C   
1094 O  O   . LEU   A 43  ? 0.1343 0.1242 0.1463 0.0000  -0.0045 0.0061  43   LEU   A O   
1095 C  CB  . LEU   A 43  ? 0.1201 0.1133 0.1437 -0.0101 0.0049  0.0128  43   LEU   A CB  
1096 C  CG  . LEU   A 43  ? 0.1240 0.1176 0.1501 -0.0003 0.0066  0.0095  43   LEU   A CG  
1097 C  CD1 . LEU   A 43  ? 0.1338 0.1259 0.1779 0.0020  -0.0003 0.0216  43   LEU   A CD1 
1098 C  CD2 . LEU   A 43  ? 0.1367 0.1159 0.1540 -0.0042 -0.0021 0.0173  43   LEU   A CD2 
1110 N  N   A LYS   A 44  ? 0.1382 0.1380 0.1452 -0.0048 0.0100  0.0048  44   LYS   A N   
1111 N  N   B LYS   A 44  ? 0.1198 0.1152 0.1327 -0.0009 0.0061  0.0142  44   LYS   A N   
1112 C  CA  A LYS   A 44  ? 0.1577 0.1541 0.1645 -0.0071 0.0118  0.0003  44   LYS   A CA  
1113 C  CA  B LYS   A 44  ? 0.1288 0.1112 0.1331 -0.0008 0.0105  0.0235  44   LYS   A CA  
1114 C  C   A LYS   A 44  ? 0.1523 0.1490 0.1438 -0.0027 0.0087  -0.0004 44   LYS   A C   
1115 C  C   B LYS   A 44  ? 0.1160 0.1052 0.1260 0.0041  0.0030  0.0173  44   LYS   A C   
1116 O  O   A LYS   A 44  ? 0.1573 0.1548 0.1443 -0.0047 0.0065  -0.0083 44   LYS   A O   
1117 O  O   B LYS   A 44  ? 0.1269 0.1254 0.1400 -0.0041 0.0008  -0.0026 44   LYS   A O   
1118 C  CB  A LYS   A 44  ? 0.1860 0.1783 0.2115 -0.0099 0.0153  -0.0036 44   LYS   A CB  
1119 C  CB  B LYS   A 44  ? 0.1652 0.1198 0.1701 0.0073  0.0240  0.0375  44   LYS   A CB  
1120 C  CG  A LYS   A 44  ? 0.2116 0.2034 0.2635 -0.0149 0.0259  -0.0031 44   LYS   A CG  
1121 C  CG  B LYS   A 44  ? 0.1920 0.1417 0.2340 -0.0081 0.0581  0.0500  44   LYS   A CG  
1122 C  CD  A LYS   A 44  ? 0.2358 0.2329 0.3231 -0.0162 0.0292  -0.0024 44   LYS   A CD  
1123 C  CD  B LYS   A 44  ? 0.2262 0.2057 0.3547 -0.0043 0.0525  0.0294  44   LYS   A CD  
1124 C  CE  A LYS   A 44  ? 0.2500 0.2507 0.3603 -0.0149 0.0312  -0.0006 44   LYS   A CE  
1125 C  CE  B LYS   A 44  ? 0.2388 0.2396 0.4218 -0.0007 0.0499  0.0196  44   LYS   A CE  
1126 N  NZ  A LYS   A 44  ? 0.2565 0.2611 0.3790 -0.0158 0.0313  0.0034  44   LYS   A NZ  
1127 N  NZ  B LYS   A 44  ? 0.2449 0.2607 0.4531 -0.0011 0.0445  0.0115  44   LYS   A NZ  
1154 N  N   A HIS   A 45  ? 0.1451 0.1458 0.1388 0.0014  0.0065  0.0056  45   HIS   A N   
1155 N  N   B HIS   A 45  ? 0.1068 0.1054 0.1229 -0.0002 -0.0015 0.0181  45   HIS   A N   
1156 C  CA  A HIS   A 45  ? 0.1431 0.1432 0.1372 0.0070  0.0012  0.0102  45   HIS   A CA  
1157 C  CA  B HIS   A 45  ? 0.1080 0.1052 0.1212 -0.0032 -0.0027 0.0150  45   HIS   A CA  
1158 C  C   A HIS   A 45  ? 0.1408 0.1467 0.1418 0.0128  -0.0016 0.0212  45   HIS   A C   
1159 C  C   B HIS   A 45  ? 0.1130 0.1180 0.1259 -0.0039 -0.0074 0.0093  45   HIS   A C   
1160 O  O   A HIS   A 45  ? 0.1449 0.1573 0.1577 0.0147  -0.0061 0.0161  45   HIS   A O   
1161 O  O   B HIS   A 45  ? 0.1261 0.1319 0.1635 0.0062  -0.0051 -0.0064 45   HIS   A O   
1162 C  CB  A HIS   A 45  ? 0.1452 0.1414 0.1352 0.0069  -0.0020 0.0066  45   HIS   A CB  
1163 C  CB  B HIS   A 45  ? 0.1095 0.1067 0.1269 -0.0078 -0.0006 0.0116  45   HIS   A CB  
1164 C  CG  A HIS   A 45  ? 0.1462 0.1383 0.1238 0.0050  -0.0018 0.0081  45   HIS   A CG  
1165 C  CG  B HIS   A 45  ? 0.1120 0.1051 0.1174 -0.0119 -0.0000 0.0163  45   HIS   A CG  
1166 N  ND1 A HIS   A 45  ? 0.1443 0.1400 0.1269 0.0048  -0.0013 0.0091  45   HIS   A ND1 
1167 N  ND1 B HIS   A 45  ? 0.1040 0.1132 0.1347 -0.0073 -0.0024 0.0192  45   HIS   A ND1 
1168 C  CD2 A HIS   A 45  ? 0.1458 0.1405 0.1274 0.0021  -0.0048 0.0119  45   HIS   A CD2 
1169 C  CD2 B HIS   A 45  ? 0.1090 0.1113 0.1287 -0.0208 -0.0114 0.0143  45   HIS   A CD2 
1170 C  CE1 A HIS   A 45  ? 0.1435 0.1406 0.1249 0.0037  -0.0023 0.0137  45   HIS   A CE1 
1171 C  CE1 B HIS   A 45  ? 0.1014 0.1101 0.1218 -0.0114 0.0021  0.0249  45   HIS   A CE1 
1172 N  NE2 A HIS   A 45  ? 0.1447 0.1414 0.1287 0.0048  -0.0030 0.0160  45   HIS   A NE2 
1173 N  NE2 B HIS   A 45  ? 0.1067 0.1139 0.1233 -0.0089 -0.0071 0.0215  45   HIS   A NE2 
1188 N  N   A GLY   A 46  ? 0.1371 0.1375 0.1389 0.0171  -0.0063 0.0297  46   GLY   A N   
1189 N  N   B GLY   A 46  ? 0.1238 0.1203 0.1436 -0.0023 -0.0155 0.0104  46   GLY   A N   
1190 C  CA  A GLY   A 46  ? 0.1317 0.1289 0.1389 0.0147  -0.0111 0.0299  46   GLY   A CA  
1191 C  CA  B GLY   A 46  ? 0.1260 0.1272 0.1656 0.0023  -0.0157 0.0180  46   GLY   A CA  
1192 C  C   A GLY   A 46  ? 0.1302 0.1262 0.1365 0.0155  -0.0165 0.0324  46   GLY   A C   
1193 C  C   B GLY   A 46  ? 0.1317 0.1299 0.1625 0.0070  -0.0170 0.0327  46   GLY   A C   
1194 O  O   A GLY   A 46  ? 0.1327 0.1228 0.1400 0.0214  -0.0234 0.0373  46   GLY   A O   
1195 O  O   B GLY   A 46  ? 0.1437 0.1345 0.2043 0.0049  -0.0248 0.0171  46   GLY   A O   
1202 N  N   A GLY   A 47  ? 0.1236 0.1263 0.1294 0.0100  -0.0093 0.0296  47   GLY   A N   
1203 N  N   B GLY   A 47  ? 0.1293 0.1329 0.1548 0.0111  -0.0006 0.0224  47   GLY   A N   
1204 C  CA  A GLY   A 47  ? 0.1227 0.1315 0.1287 0.0129  -0.0065 0.0162  47   GLY   A CA  
1205 C  CA  B GLY   A 47  ? 0.1268 0.1353 0.1582 0.0123  -0.0125 0.0182  47   GLY   A CA  
1206 C  C   A GLY   A 47  ? 0.1209 0.1286 0.1382 0.0116  -0.0032 0.0108  47   GLY   A C   
1207 C  C   B GLY   A 47  ? 0.1180 0.1227 0.1477 0.0139  -0.0176 0.0151  47   GLY   A C   
1208 O  O   A GLY   A 47  ? 0.1254 0.1290 0.1579 0.0151  0.0045  0.0034  47   GLY   A O   
1209 O  O   B GLY   A 47  ? 0.1161 0.1179 0.1512 0.0123  -0.0150 0.0194  47   GLY   A O   
1216 N  N   A GLY   A 48  ? 0.1171 0.1277 0.1372 0.0129  -0.0024 0.0092  48   GLY   A N   
1217 N  N   B GLY   A 48  ? 0.1178 0.1265 0.1547 0.0124  -0.0106 0.0101  48   GLY   A N   
1218 C  CA  A GLY   A 48  ? 0.1154 0.1290 0.1413 0.0061  0.0022  0.0031  48   GLY   A CA  
1219 C  CA  B GLY   A 48  ? 0.1216 0.1209 0.1664 0.0068  -0.0100 -0.0072 48   GLY   A CA  
1220 C  C   A GLY   A 48  ? 0.1215 0.1285 0.1204 0.0031  0.0012  0.0005  48   GLY   A C   
1221 C  C   B GLY   A 48  ? 0.1135 0.1196 0.1571 -0.0007 -0.0053 -0.0038 48   GLY   A C   
1222 O  O   A GLY   A 48  ? 0.1268 0.1327 0.1148 -0.0006 -0.0125 -0.0008 48   GLY   A O   
1223 O  O   B GLY   A 48  ? 0.1266 0.1231 0.1609 0.0030  -0.0018 -0.0028 48   GLY   A O   
1230 N  N   A VAL   A 49  ? 0.1314 0.1256 0.1328 0.0032  0.0055  0.0076  49   VAL   A N   
1231 N  N   B VAL   A 49  ? 0.1106 0.1171 0.1626 -0.0046 -0.0041 -0.0028 49   VAL   A N   
1232 C  CA  A VAL   A 49  ? 0.1416 0.1200 0.1278 0.0017  0.0143  0.0062  49   VAL   A CA  
1233 C  CA  B VAL   A 49  ? 0.1134 0.1165 0.1596 -0.0119 0.0020  0.0031  49   VAL   A CA  
1234 C  C   A VAL   A 49  ? 0.1366 0.1193 0.1118 0.0057  0.0057  0.0116  49   VAL   A C   
1235 C  C   B VAL   A 49  ? 0.1173 0.1136 0.1321 -0.0032 0.0050  0.0023  49   VAL   A C   
1236 O  O   A VAL   A 49  ? 0.1373 0.1252 0.1099 0.0043  0.0006  0.0096  49   VAL   A O   
1237 O  O   B VAL   A 49  ? 0.1203 0.1185 0.1357 -0.0097 0.0083  -0.0011 49   VAL   A O   
1238 C  CB  A VAL   A 49  ? 0.1536 0.1269 0.1479 0.0015  0.0226  -0.0013 49   VAL   A CB  
1239 C  CB  B VAL   A 49  ? 0.1113 0.1228 0.1743 -0.0077 -0.0053 0.0176  49   VAL   A CB  
1240 C  CG1 A VAL   A 49  ? 0.1573 0.1208 0.1639 0.0105  0.0284  0.0015  49   VAL   A CG1 
1241 C  CG1 B VAL   A 49  ? 0.1056 0.1171 0.1716 0.0018  -0.0036 0.0191  49   VAL   A CG1 
1242 C  CG2 A VAL   A 49  ? 0.1561 0.1356 0.1688 0.0000  0.0211  -0.0071 49   VAL   A CG2 
1243 C  CG2 B VAL   A 49  ? 0.1193 0.1300 0.1951 -0.0084 -0.0099 0.0142  49   VAL   A CG2 
1262 N  N   A ALA   A 50  ? 0.1292 0.1169 0.1129 0.0065  -0.0024 0.0151  50   ALA   A N   
1263 N  N   B ALA   A 50  ? 0.1106 0.1134 0.1279 -0.0010 -0.0041 0.0068  50   ALA   A N   
1264 C  CA  A ALA   A 50  ? 0.1243 0.1143 0.1199 0.0042  -0.0061 0.0179  50   ALA   A CA  
1265 C  CA  B ALA   A 50  ? 0.1119 0.1135 0.1293 -0.0067 -0.0015 0.0090  50   ALA   A CA  
1266 C  C   A ALA   A 50  ? 0.1171 0.1143 0.1272 0.0037  -0.0110 0.0165  50   ALA   A C   
1267 C  C   B ALA   A 50  ? 0.1081 0.1202 0.1239 -0.0062 -0.0021 0.0069  50   ALA   A C   
1268 O  O   A ALA   A 50  ? 0.1166 0.1136 0.1346 0.0082  -0.0204 0.0228  50   ALA   A O   
1269 O  O   B ALA   A 50  ? 0.1109 0.1229 0.1313 -0.0042 0.0025  0.0052  50   ALA   A O   
1270 C  CB  A ALA   A 50  ? 0.1236 0.1165 0.1189 0.0058  -0.0058 0.0172  50   ALA   A CB  
1271 C  CB  B ALA   A 50  ? 0.1096 0.1188 0.1266 -0.0051 -0.0012 0.0004  50   ALA   A CB  
1282 N  N   . GLY   A 51  ? 0.1153 0.1088 0.1396 0.0024  -0.0072 0.0108  51   GLY   A N   
1283 C  CA  . GLY   A 51  ? 0.1226 0.1114 0.1363 0.0065  -0.0071 0.0032  51   GLY   A CA  
1284 C  C   . GLY   A 51  ? 0.1147 0.1240 0.1422 0.0053  -0.0079 -0.0037 51   GLY   A C   
1285 O  O   . GLY   A 51  ? 0.1199 0.1268 0.1506 0.0004  -0.0097 -0.0028 51   GLY   A O   
1290 N  N   A ALA   A 52  ? 0.1182 0.1284 0.1370 0.0014  -0.0013 -0.0015 52   ALA   A N   
1291 N  N   B ALA   A 52  ? 0.1094 0.1272 0.1375 -0.0026 -0.0012 -0.0046 52   ALA   A N   
1292 C  CA  A ALA   A 52  ? 0.1248 0.1366 0.1378 -0.0010 0.0009  0.0014  52   ALA   A CA  
1293 C  CA  B ALA   A 52  ? 0.1150 0.1401 0.1434 -0.0036 -0.0034 -0.0023 52   ALA   A CA  
1294 C  C   A ALA   A 52  ? 0.1259 0.1370 0.1300 -0.0073 0.0043  0.0022  52   ALA   A C   
1295 C  C   B ALA   A 52  ? 0.1094 0.1373 0.1243 -0.0108 -0.0047 -0.0060 52   ALA   A C   
1296 O  O   A ALA   A 52  ? 0.1298 0.1394 0.1368 -0.0057 0.0069  0.0005  52   ALA   A O   
1297 O  O   B ALA   A 52  ? 0.1206 0.1456 0.1394 -0.0066 -0.0038 -0.0082 52   ALA   A O   
1298 C  CB  A ALA   A 52  ? 0.1304 0.1489 0.1436 -0.0021 -0.0032 0.0018  52   ALA   A CB  
1299 C  CB  B ALA   A 52  ? 0.1250 0.1649 0.1530 -0.0086 -0.0132 0.0002  52   ALA   A CB  
1310 N  N   A LEU   A 53  ? 0.1283 0.1336 0.1304 -0.0102 0.0057  0.0051  53   LEU   A N   
1311 N  N   B LEU   A 53  ? 0.1063 0.1268 0.1267 -0.0069 -0.0055 -0.0033 53   LEU   A N   
1312 C  CA  A LEU   A 53  ? 0.1365 0.1364 0.1316 -0.0133 0.0102  0.0089  53   LEU   A CA  
1313 C  CA  B LEU   A 53  ? 0.1180 0.1335 0.1205 -0.0047 0.0014  0.0022  53   LEU   A CA  
1314 C  C   A LEU   A 53  ? 0.1374 0.1361 0.1299 -0.0090 0.0104  0.0049  53   LEU   A C   
1315 C  C   B LEU   A 53  ? 0.1191 0.1343 0.1005 0.0089  -0.0047 0.0049  53   LEU   A C   
1316 O  O   A LEU   A 53  ? 0.1409 0.1353 0.1382 -0.0132 0.0176  0.0041  53   LEU   A O   
1317 O  O   B LEU   A 53  ? 0.1281 0.1414 0.1169 -0.0003 -0.0055 0.0055  53   LEU   A O   
1318 C  CB  A LEU   A 53  ? 0.1451 0.1364 0.1368 -0.0159 0.0075  0.0164  53   LEU   A CB  
1319 C  CB  B LEU   A 53  ? 0.1313 0.1295 0.1298 -0.0033 -0.0051 0.0086  53   LEU   A CB  
1320 C  CG  A LEU   A 53  ? 0.1519 0.1403 0.1352 -0.0220 0.0045  0.0225  53   LEU   A CG  
1321 C  CG  B LEU   A 53  ? 0.1432 0.1346 0.1344 -0.0056 -0.0071 0.0082  53   LEU   A CG  
1322 C  CD1 A LEU   A 53  ? 0.1569 0.1398 0.1418 -0.0238 0.0065  0.0278  53   LEU   A CD1 
1323 C  CD1 B LEU   A 53  ? 0.1582 0.1365 0.1516 -0.0017 -0.0070 0.0048  53   LEU   A CD1 
1324 C  CD2 A LEU   A 53  ? 0.1613 0.1488 0.1357 -0.0235 -0.0001 0.0209  53   LEU   A CD2 
1325 C  CD2 B LEU   A 53  ? 0.1539 0.1441 0.1535 -0.0157 -0.0003 -0.0096 53   LEU   A CD2 
1348 N  N   A ASN   A 54  ? 0.1325 0.1340 0.1318 -0.0119 0.0032  0.0060  54   ASN   A N   
1349 N  N   B ASN   A 54  ? 0.1084 0.1352 0.1073 -0.0015 -0.0026 0.0093  54   ASN   A N   
1350 C  CA  A ASN   A 54  ? 0.1306 0.1274 0.1407 -0.0118 -0.0032 0.0042  54   ASN   A CA  
1351 C  CA  B ASN   A 54  ? 0.1053 0.1273 0.1239 0.0002  0.0010  0.0016  54   ASN   A CA  
1352 C  C   A ASN   A 54  ? 0.1264 0.1288 0.1370 -0.0116 -0.0005 0.0039  54   ASN   A C   
1353 C  C   B ASN   A 54  ? 0.1168 0.1284 0.1245 -0.0116 0.0035  -0.0003 54   ASN   A C   
1354 O  O   A ASN   A 54  ? 0.1258 0.1352 0.1414 -0.0116 -0.0063 0.0059  54   ASN   A O   
1355 O  O   B ASN   A 54  ? 0.1190 0.1441 0.1244 -0.0061 -0.0055 -0.0071 54   ASN   A O   
1356 C  CB  A ASN   A 54  ? 0.1342 0.1189 0.1507 -0.0158 -0.0122 0.0035  54   ASN   A CB  
1357 C  CB  B ASN   A 54  ? 0.1003 0.1196 0.1233 0.0067  -0.0049 -0.0014 54   ASN   A CB  
1358 C  CG  A ASN   A 54  ? 0.1402 0.1158 0.1626 -0.0178 -0.0151 0.0046  54   ASN   A CG  
1359 C  CG  B ASN   A 54  ? 0.1022 0.1247 0.1178 0.0033  0.0014  -0.0051 54   ASN   A CG  
1360 O  OD1 A ASN   A 54  ? 0.1454 0.1172 0.1801 -0.0159 -0.0167 0.0137  54   ASN   A OD1 
1361 O  OD1 B ASN   A 54  ? 0.1033 0.1270 0.1123 0.0067  -0.0033 -0.0086 54   ASN   A OD1 
1362 N  ND2 A ASN   A 54  ? 0.1419 0.1151 0.1716 -0.0199 -0.0185 0.0063  54   ASN   A ND2 
1363 N  ND2 B ASN   A 54  ? 0.1115 0.1296 0.1366 -0.0051 -0.0006 0.0055  54   ASN   A ND2 
1376 N  N   . LYS   A 55  ? 0.1210 0.1300 0.1366 -0.0015 -0.0002 -0.0043 55   LYS   A N   
1377 C  CA  . LYS   A 55  ? 0.1297 0.1375 0.1365 0.0000  0.0013  -0.0104 55   LYS   A CA  
1378 C  C   . LYS   A 55  ? 0.1219 0.1501 0.1387 -0.0065 0.0011  -0.0186 55   LYS   A C   
1379 O  O   . LYS   A 55  ? 0.1311 0.1591 0.1415 0.0049  -0.0047 -0.0205 55   LYS   A O   
1380 C  CB  . LYS   A 55  ? 0.1396 0.1476 0.1603 0.0131  -0.0044 -0.0171 55   LYS   A CB  
1381 C  CG  . LYS   A 55  ? 0.1565 0.1669 0.1687 0.0266  -0.0235 -0.0333 55   LYS   A CG  
1382 C  CD  . LYS   A 55  ? 0.1691 0.1905 0.1856 0.0344  -0.0245 -0.0234 55   LYS   A CD  
1383 C  CE  . LYS   A 55  ? 0.1870 0.2178 0.2083 0.0450  -0.0281 -0.0238 55   LYS   A CE  
1384 N  NZ  . LYS   A 55  ? 0.1985 0.2370 0.2030 0.0536  -0.0244 -0.0198 55   LYS   A NZ  
1399 N  N   . ALA   A 56  ? 0.1269 0.1505 0.1449 -0.0103 0.0020  -0.0146 56   ALA   A N   
1400 C  CA  . ALA   A 56  ? 0.1390 0.1682 0.1336 -0.0097 0.0081  -0.0103 56   ALA   A CA  
1401 C  C   . ALA   A 56  ? 0.1467 0.1809 0.1089 -0.0107 0.0097  -0.0089 56   ALA   A C   
1402 O  O   . ALA   A 56  ? 0.1524 0.2177 0.1314 -0.0014 0.0079  -0.0088 56   ALA   A O   
1403 C  CB  . ALA   A 56  ? 0.1461 0.1839 0.1592 -0.0125 0.0030  0.0048  56   ALA   A CB  
1409 N  N   . THR   A 57  ? 0.1326 0.1582 0.1130 -0.0037 0.0051  -0.0110 57   THR   A N   
1410 C  CA  . THR   A 57  ? 0.1381 0.1586 0.1197 -0.0054 0.0017  -0.0120 57   THR   A CA  
1411 C  C   . THR   A 57  ? 0.1348 0.1644 0.1280 -0.0064 0.0000  -0.0203 57   THR   A C   
1412 O  O   . THR   A 57  ? 0.1362 0.1721 0.1401 -0.0126 -0.0108 -0.0264 57   THR   A O   
1413 C  CB  . THR   A 57  ? 0.1345 0.1591 0.1232 -0.0046 -0.0050 -0.0120 57   THR   A CB  
1414 O  OG1 . THR   A 57  ? 0.1273 0.1508 0.1209 -0.0056 -0.0010 -0.0063 57   THR   A OG1 
1415 C  CG2 . THR   A 57  ? 0.1427 0.1622 0.1163 -0.0056 -0.0009 0.0007  57   THR   A CG2 
1423 N  N   . ASN   A 58  ? 0.1403 0.1542 0.1475 -0.0093 0.0062  -0.0211 58   ASN   A N   
1424 C  CA  . ASN   A 58  ? 0.1609 0.1514 0.1721 -0.0106 0.0103  -0.0393 58   ASN   A CA  
1425 C  C   . ASN   A 58  ? 0.1415 0.1346 0.1737 -0.0005 -0.0019 -0.0204 58   ASN   A C   
1426 O  O   . ASN   A 58  ? 0.1422 0.1498 0.1772 -0.0119 -0.0028 -0.0284 58   ASN   A O   
1427 C  CB  . ASN   A 58  ? 0.2100 0.1770 0.2140 -0.0200 0.0377  -0.0518 58   ASN   A CB  
1428 C  CG  . ASN   A 58  ? 0.2654 0.1998 0.2950 -0.0173 0.0435  -0.0391 58   ASN   A CG  
1429 O  OD1 . ASN   A 58  ? 0.2828 0.1929 0.3418 0.0169  0.0862  -0.0257 58   ASN   A OD1 
1430 N  ND2 . ASN   A 58  ? 0.2889 0.2174 0.3174 -0.0258 0.0246  -0.0499 58   ASN   A ND2 
1437 N  N   . ASN   A 59  ? 0.1256 0.1302 0.1456 -0.0056 -0.0020 -0.0160 59   ASN   A N   
1438 C  CA  . ASN   A 59  ? 0.1264 0.1258 0.1458 -0.0043 -0.0067 -0.0104 59   ASN   A CA  
1439 C  C   . ASN   A 59  ? 0.1233 0.1233 0.1313 -0.0065 -0.0030 -0.0024 59   ASN   A C   
1440 O  O   . ASN   A 59  ? 0.1286 0.1327 0.1404 -0.0031 -0.0005 0.0090  59   ASN   A O   
1441 C  CB  . ASN   A 59  ? 0.1300 0.1266 0.1516 -0.0000 -0.0209 -0.0155 59   ASN   A CB  
1442 C  CG  . ASN   A 59  ? 0.1317 0.1262 0.1449 -0.0026 -0.0301 -0.0023 59   ASN   A CG  
1443 O  OD1 . ASN   A 59  ? 0.1433 0.1343 0.1413 -0.0082 -0.0199 0.0027  59   ASN   A OD1 
1444 N  ND2 . ASN   A 59  ? 0.1435 0.1332 0.1615 -0.0128 -0.0200 0.0041  59   ASN   A ND2 
1451 N  N   . ALA   A 60  ? 0.1183 0.1291 0.1354 -0.0019 -0.0099 -0.0014 60   ALA   A N   
1452 C  CA  . ALA   A 60  ? 0.1267 0.1311 0.1470 0.0007  -0.0084 -0.0007 60   ALA   A CA  
1453 C  C   . ALA   A 60  ? 0.1187 0.1303 0.1475 -0.0019 -0.0070 -0.0012 60   ALA   A C   
1454 O  O   . ALA   A 60  ? 0.1181 0.1301 0.1678 -0.0065 -0.0141 -0.0008 60   ALA   A O   
1455 C  CB  . ALA   A 60  ? 0.1315 0.1472 0.1460 -0.0018 -0.0167 -0.0103 60   ALA   A CB  
1461 N  N   . MET   A 61  ? 0.1169 0.1233 0.1368 -0.0046 -0.0011 -0.0045 61   MET   A N   
1462 C  CA  . MET   A 61  ? 0.1151 0.1207 0.1390 -0.0039 -0.0001 0.0028  61   MET   A CA  
1463 C  C   . MET   A 61  ? 0.1100 0.1133 0.1367 -0.0059 -0.0069 -0.0039 61   MET   A C   
1464 O  O   . MET   A 61  ? 0.1169 0.1216 0.1413 -0.0048 0.0019  0.0064  61   MET   A O   
1465 C  CB  . MET   A 61  ? 0.1224 0.1225 0.1258 -0.0056 0.0053  0.0019  61   MET   A CB  
1466 C  CG  . MET   A 61  ? 0.1225 0.1287 0.1463 -0.0030 0.0014  0.0022  61   MET   A CG  
1467 S  SD  . MET   A 61  ? 0.1244 0.1324 0.1679 -0.0097 -0.0042 -0.0139 61   MET   A SD  
1468 C  CE  . MET   A 61  ? 0.1411 0.1538 0.1820 -0.0157 0.0159  -0.0133 61   MET   A CE  
1478 N  N   . GLN   A 62  ? 0.1108 0.1198 0.1384 -0.0020 0.0031  -0.0025 62   GLN   A N   
1479 C  CA  . GLN   A 62  ? 0.1206 0.1197 0.1365 -0.0032 0.0018  -0.0023 62   GLN   A CA  
1480 C  C   . GLN   A 62  ? 0.1221 0.1096 0.1373 0.0009  0.0070  0.0012  62   GLN   A C   
1481 O  O   . GLN   A 62  ? 0.1219 0.1221 0.1487 -0.0042 0.0033  -0.0017 62   GLN   A O   
1482 C  CB  . GLN   A 62  ? 0.1201 0.1182 0.1428 -0.0006 -0.0014 0.0008  62   GLN   A CB  
1483 C  CG  . GLN   A 62  ? 0.1231 0.1132 0.1402 -0.0039 -0.0033 0.0095  62   GLN   A CG  
1484 C  CD  . GLN   A 62  ? 0.1252 0.1129 0.1492 -0.0055 0.0035  0.0146  62   GLN   A CD  
1485 O  OE1 . GLN   A 62  ? 0.1293 0.1267 0.1520 -0.0038 0.0029  0.0066  62   GLN   A OE1 
1486 N  NE2 . GLN   A 62  ? 0.1343 0.1234 0.1557 -0.0011 -0.0058 -0.0005 62   GLN   A NE2 
1495 N  N   . VAL   A 63  ? 0.1233 0.1172 0.1564 -0.0052 0.0112  -0.0159 63   VAL   A N   
1496 C  CA  . VAL   A 63  ? 0.1185 0.1285 0.1821 -0.0142 0.0020  -0.0126 63   VAL   A CA  
1497 C  C   . VAL   A 63  ? 0.1051 0.1292 0.1727 -0.0168 -0.0079 -0.0156 63   VAL   A C   
1498 O  O   . VAL   A 63  ? 0.1133 0.1267 0.1853 -0.0123 -0.0089 -0.0129 63   VAL   A O   
1499 C  CB  . VAL   A 63  ? 0.1326 0.1432 0.2123 -0.0149 0.0020  -0.0405 63   VAL   A CB  
1500 C  CG1 . VAL   A 63  ? 0.1446 0.1634 0.2405 -0.0167 -0.0083 -0.0645 63   VAL   A CG1 
1501 C  CG2 . VAL   A 63  ? 0.1404 0.1396 0.2358 -0.0157 0.0125  -0.0411 63   VAL   A CG2 
1511 N  N   . GLU   A 64  ? 0.1083 0.1351 0.1648 -0.0073 -0.0101 -0.0061 64   GLU   A N   
1512 C  CA  . GLU   A 64  ? 0.1138 0.1310 0.1547 -0.0101 -0.0130 0.0005  64   GLU   A CA  
1513 C  C   . GLU   A 64  ? 0.1121 0.1265 0.1520 -0.0057 -0.0002 0.0037  64   GLU   A C   
1514 O  O   . GLU   A 64  ? 0.1184 0.1302 0.1639 -0.0032 -0.0043 0.0055  64   GLU   A O   
1515 C  CB  . GLU   A 64  ? 0.1231 0.1439 0.1545 -0.0094 -0.0031 -0.0033 64   GLU   A CB  
1516 C  CG  . GLU   A 64  ? 0.1270 0.1438 0.1691 -0.0116 -0.0006 -0.0073 64   GLU   A CG  
1517 C  CD  . GLU   A 64  ? 0.1395 0.1481 0.1729 -0.0188 -0.0017 0.0015  64   GLU   A CD  
1518 O  OE1 . GLU   A 64  ? 0.1385 0.1581 0.2047 -0.0257 0.0008  0.0003  64   GLU   A OE1 
1519 O  OE2 . GLU   A 64  ? 0.1539 0.1519 0.1673 -0.0159 -0.0108 0.0096  64   GLU   A OE2 
1526 N  N   . SER   A 65  ? 0.1051 0.1297 0.1499 -0.0009 0.0053  -0.0017 65   SER   A N   
1527 C  CA  . SER   A 65  ? 0.1120 0.1218 0.1463 0.0013  0.0011  -0.0057 65   SER   A CA  
1528 C  C   . SER   A 65  ? 0.1082 0.1295 0.1522 -0.0007 -0.0022 -0.0022 65   SER   A C   
1529 O  O   . SER   A 65  ? 0.1152 0.1348 0.1703 -0.0009 0.0099  0.0026  65   SER   A O   
1530 C  CB  . SER   A 65  ? 0.1146 0.1198 0.1453 -0.0059 0.0031  0.0066  65   SER   A CB  
1531 O  OG  . SER   A 65  ? 0.1199 0.1270 0.1499 -0.0091 -0.0065 0.0132  65   SER   A OG  
1537 N  N   . ASP   A 66  ? 0.1138 0.1245 0.1566 -0.0021 0.0085  0.0060  66   ASP   A N   
1538 C  CA  . ASP   A 66  ? 0.1242 0.1309 0.1716 -0.0041 0.0099  0.0163  66   ASP   A CA  
1539 C  C   . ASP   A 66  ? 0.1237 0.1306 0.1745 -0.0035 0.0100  0.0119  66   ASP   A C   
1540 O  O   . ASP   A 66  ? 0.1276 0.1395 0.1977 -0.0003 0.0203  0.0220  66   ASP   A O   
1541 C  CB  . ASP   A 66  ? 0.1306 0.1405 0.2043 0.0021  0.0076  0.0320  66   ASP   A CB  
1542 C  CG  . ASP   A 66  ? 0.1562 0.1526 0.2255 0.0022  0.0002  0.0421  66   ASP   A CG  
1543 O  OD1 . ASP   A 66  ? 0.1563 0.1833 0.1909 -0.0098 -0.0067 0.0457  66   ASP   A OD1 
1544 O  OD2 . ASP   A 66  ? 0.1707 0.1610 0.3087 0.0204  -0.0190 0.0247  66   ASP   A OD2 
1549 N  N   . ASP   A 67  ? 0.1133 0.1354 0.1894 -0.0044 0.0075  0.0147  67   ASP   A N   
1550 C  CA  . ASP   A 67  ? 0.1158 0.1483 0.2043 -0.0021 0.0046  0.0240  67   ASP   A CA  
1551 C  C   . ASP   A 67  ? 0.1195 0.1503 0.1992 0.0001  0.0122  0.0274  67   ASP   A C   
1552 O  O   . ASP   A 67  ? 0.1163 0.1591 0.2205 -0.0013 0.0232  0.0326  67   ASP   A O   
1553 C  CB  . ASP   A 67  ? 0.1227 0.1590 0.2346 -0.0035 -0.0137 0.0311  67   ASP   A CB  
1554 C  CG  . ASP   A 67  ? 0.1238 0.1720 0.2704 -0.0066 -0.0330 0.0367  67   ASP   A CG  
1555 O  OD1 . ASP   A 67  ? 0.1305 0.1899 0.3557 -0.0136 -0.0382 0.0523  67   ASP   A OD1 
1556 O  OD2 . ASP   A 67  ? 0.1250 0.1726 0.2442 0.0010  -0.0264 0.0378  67   ASP   A OD2 
1561 N  N   A TYR   A 68  ? 0.1190 0.1391 0.1810 0.0026  0.0202  0.0231  68   TYR   A N   
1562 N  N   B TYR   A 68  ? 0.1208 0.1410 0.1856 0.0072  0.0168  0.0266  68   TYR   A N   
1563 C  CA  A TYR   A 68  ? 0.1238 0.1319 0.1685 0.0023  0.0277  0.0225  68   TYR   A CA  
1564 C  CA  B TYR   A 68  ? 0.1347 0.1415 0.1853 0.0068  0.0202  0.0322  68   TYR   A CA  
1565 C  C   A TYR   A 68  ? 0.1232 0.1293 0.1689 -0.0017 0.0290  0.0250  68   TYR   A C   
1566 C  C   B TYR   A 68  ? 0.1272 0.1350 0.1868 -0.0009 0.0288  0.0229  68   TYR   A C   
1567 O  O   A TYR   A 68  ? 0.1273 0.1304 0.1692 0.0009  0.0313  0.0311  68   TYR   A O   
1568 O  O   B TYR   A 68  ? 0.1306 0.1382 0.1987 0.0072  0.0291  0.0186  68   TYR   A O   
1569 C  CB  A TYR   A 68  ? 0.1239 0.1232 0.1701 0.0045  0.0397  0.0134  68   TYR   A CB  
1570 C  CB  B TYR   A 68  ? 0.1441 0.1411 0.1994 0.0094  0.0265  0.0383  68   TYR   A CB  
1571 C  CG  A TYR   A 68  ? 0.1216 0.1235 0.1859 -0.0025 0.0558  0.0105  68   TYR   A CG  
1572 C  CG  B TYR   A 68  ? 0.1507 0.1535 0.2071 0.0029  0.0300  0.0410  68   TYR   A CG  
1573 C  CD1 A TYR   A 68  ? 0.1166 0.1248 0.2028 -0.0254 0.0575  -0.0080 68   TYR   A CD1 
1574 C  CD1 B TYR   A 68  ? 0.1595 0.1566 0.2029 -0.0055 0.0229  0.0266  68   TYR   A CD1 
1575 C  CD2 A TYR   A 68  ? 0.1339 0.1242 0.2136 0.0025  0.0593  0.0139  68   TYR   A CD2 
1576 C  CD2 B TYR   A 68  ? 0.1663 0.1530 0.2342 0.0061  0.0233  0.0440  68   TYR   A CD2 
1577 C  CE1 A TYR   A 68  ? 0.1218 0.1359 0.2409 -0.0226 0.0511  -0.0232 68   TYR   A CE1 
1578 C  CE1 B TYR   A 68  ? 0.1711 0.1525 0.1999 -0.0014 0.0138  0.0438  68   TYR   A CE1 
1579 C  CE2 A TYR   A 68  ? 0.1356 0.1312 0.2352 0.0014  0.0650  0.0019  68   TYR   A CE2 
1580 C  CE2 B TYR   A 68  ? 0.1692 0.1540 0.1978 0.0049  0.0145  0.0357  68   TYR   A CE2 
1581 C  CZ  A TYR   A 68  ? 0.1275 0.1379 0.2640 -0.0130 0.0543  -0.0281 68   TYR   A CZ  
1582 C  CZ  B TYR   A 68  ? 0.1755 0.1469 0.1916 0.0019  0.0076  0.0398  68   TYR   A CZ  
1583 O  OH  A TYR   A 68  ? 0.1399 0.1502 0.3107 -0.0024 0.0370  -0.0541 68   TYR   A OH  
1584 O  OH  B TYR   A 68  ? 0.2095 0.1410 0.2042 0.0037  -0.0104 0.0348  68   TYR   A OH  
1603 N  N   . ILE   A 69  ? 0.1203 0.1254 0.1680 -0.0021 0.0192  0.0180  69   ILE   A N   
1604 C  CA  . ILE   A 69  ? 0.1287 0.1332 0.1640 0.0020  0.0179  0.0075  69   ILE   A CA  
1605 C  C   . ILE   A 69  ? 0.1328 0.1359 0.1624 0.0015  0.0143  0.0136  69   ILE   A C   
1606 O  O   . ILE   A 69  ? 0.1377 0.1457 0.1597 -0.0030 0.0248  0.0170  69   ILE   A O   
1607 C  CB  . ILE   A 69  ? 0.1356 0.1534 0.1763 0.0036  0.0096  0.0020  69   ILE   A CB  
1608 C  CG1 . ILE   A 69  ? 0.1303 0.1635 0.1810 0.0048  0.0128  -0.0103 69   ILE   A CG1 
1609 C  CG2 . ILE   A 69  ? 0.1510 0.1730 0.1997 0.0084  0.0082  -0.0081 69   ILE   A CG2 
1610 C  CD1 . ILE   A 69  ? 0.1343 0.1715 0.1981 -0.0015 0.0132  -0.0182 69   ILE   A CD1 
1623 N  N   . ALA   A 70  ? 0.1356 0.1350 0.1718 -0.0037 0.0136  0.0188  70   ALA   A N   
1624 C  CA  . ALA   A 70  ? 0.1317 0.1448 0.1898 -0.0125 0.0235  0.0265  70   ALA   A CA  
1625 C  C   . ALA   A 70  ? 0.1346 0.1620 0.1966 -0.0135 0.0248  0.0249  70   ALA   A C   
1626 O  O   . ALA   A 70  ? 0.1491 0.1961 0.2140 0.0111  0.0398  0.0377  70   ALA   A O   
1627 C  CB  . ALA   A 70  ? 0.1341 0.1417 0.2185 -0.0181 0.0240  0.0216  70   ALA   A CB  
1633 N  N   . THR   A 71  ? 0.1320 0.1620 0.1799 -0.0042 0.0167  0.0234  71   THR   A N   
1634 C  CA  . THR   A 71  ? 0.1344 0.1730 0.2016 0.0083  0.0183  0.0271  71   THR   A CA  
1635 C  C   . THR   A 71  ? 0.1265 0.1707 0.2289 0.0140  0.0305  0.0225  71   THR   A C   
1636 O  O   . THR   A 71  ? 0.1373 0.1940 0.2799 0.0141  0.0447  -0.0054 71   THR   A O   
1637 C  CB  . THR   A 71  ? 0.1667 0.1967 0.2203 0.0163  -0.0200 0.0305  71   THR   A CB  
1638 O  OG1 . THR   A 71  ? 0.2002 0.2181 0.2244 0.0107  -0.0362 0.0174  71   THR   A OG1 
1639 C  CG2 . THR   A 71  ? 0.1813 0.2130 0.2466 0.0184  -0.0284 0.0438  71   THR   A CG2 
1647 N  N   . ASN   A 72  ? 0.1294 0.1543 0.2044 0.0121  0.0269  0.0269  72   ASN   A N   
1648 C  CA  . ASN   A 72  ? 0.1434 0.1524 0.2018 0.0163  0.0389  0.0203  72   ASN   A CA  
1649 C  C   . ASN   A 72  ? 0.1558 0.1490 0.1949 0.0112  0.0420  0.0166  72   ASN   A C   
1650 O  O   . ASN   A 72  ? 0.1722 0.1520 0.2328 0.0123  0.0397  0.0015  72   ASN   A O   
1651 C  CB  . ASN   A 72  ? 0.1650 0.1584 0.2097 0.0209  0.0420  0.0187  72   ASN   A CB  
1652 C  CG  . ASN   A 72  ? 0.1817 0.1684 0.2137 0.0290  0.0382  0.0275  72   ASN   A CG  
1653 O  OD1 . ASN   A 72  ? 0.1998 0.1988 0.2365 0.0244  0.0454  0.0225  72   ASN   A OD1 
1654 N  ND2 . ASN   A 72  ? 0.1977 0.1761 0.2226 0.0503  0.0248  0.0149  72   ASN   A ND2 
1661 N  N   . GLY   A 73  ? 0.1527 0.1475 0.1778 0.0060  0.0407  0.0087  73   GLY   A N   
1662 C  CA  . GLY   A 73  ? 0.1628 0.1437 0.1632 -0.0064 0.0370  0.0122  73   GLY   A CA  
1663 C  C   . GLY   A 73  ? 0.1612 0.1344 0.1611 -0.0016 0.0483  0.0227  73   GLY   A C   
1664 O  O   . GLY   A 73  ? 0.1537 0.1398 0.1870 0.0060  0.0360  0.0213  73   GLY   A O   
1668 N  N   . PRO   A 74  ? 0.1693 0.1381 0.1774 -0.0104 0.0431  0.0156  74   PRO   A N   
1669 C  CA  . PRO   A 74  ? 0.1655 0.1358 0.1808 -0.0053 0.0492  0.0187  74   PRO   A CA  
1670 C  C   . PRO   A 74  ? 0.1559 0.1247 0.1736 0.0006  0.0368  0.0140  74   PRO   A C   
1671 O  O   . PRO   A 74  ? 0.1668 0.1321 0.1987 0.0043  0.0409  0.0025  74   PRO   A O   
1672 C  CB  . PRO   A 74  ? 0.1843 0.1648 0.1970 0.0005  0.0422  0.0361  74   PRO   A CB  
1673 C  CG  . PRO   A 74  ? 0.2062 0.1952 0.2462 -0.0143 0.0331  0.0296  74   PRO   A CG  
1674 C  CD  . PRO   A 74  ? 0.1898 0.1755 0.1978 -0.0223 0.0352  0.0224  74   PRO   A CD  
1682 N  N   . LEU   A 75  ? 0.1561 0.1169 0.1609 0.0018  0.0326  0.0092  75   LEU   A N   
1683 C  CA  . LEU   A 75  ? 0.1552 0.1204 0.1412 0.0005  0.0123  0.0133  75   LEU   A CA  
1684 C  C   . LEU   A 75  ? 0.1674 0.1261 0.1344 0.0025  0.0136  0.0141  75   LEU   A C   
1685 O  O   . LEU   A 75  ? 0.2026 0.1430 0.1403 0.0089  0.0075  0.0148  75   LEU   A O   
1686 C  CB  . LEU   A 75  ? 0.1625 0.1274 0.1278 -0.0079 0.0093  0.0190  75   LEU   A CB  
1687 C  CG  . LEU   A 75  ? 0.1742 0.1598 0.1360 -0.0360 0.0094  0.0155  75   LEU   A CG  
1688 C  CD1 . LEU   A 75  ? 0.1878 0.2065 0.1576 -0.0301 0.0082  -0.0048 75   LEU   A CD1 
1689 C  CD2 . LEU   A 75  ? 0.1975 0.2092 0.1935 -0.0118 0.0147  0.0195  75   LEU   A CD2 
1701 N  N   . LYS   A 76  ? 0.1685 0.1278 0.1439 0.0011  0.0123  0.0101  76   LYS   A N   
1702 C  CA  . LYS   A 76  ? 0.1662 0.1401 0.1542 -0.0053 0.0107  0.0037  76   LYS   A CA  
1703 C  C   . LYS   A 76  ? 0.1617 0.1303 0.1225 -0.0044 0.0090  0.0046  76   LYS   A C   
1704 O  O   . LYS   A 76  ? 0.1655 0.1276 0.1276 -0.0019 0.0171  0.0124  76   LYS   A O   
1705 C  CB  . LYS   A 76  ? 0.1672 0.1517 0.1912 0.0020  0.0086  -0.0166 76   LYS   A CB  
1706 C  CG  . LYS   A 76  ? 0.1776 0.1500 0.2353 0.0075  0.0001  -0.0199 76   LYS   A CG  
1707 C  CD  . LYS   A 76  ? 0.1839 0.1553 0.2674 0.0112  -0.0048 -0.0361 76   LYS   A CD  
1708 C  CE  . LYS   A 76  ? 0.1960 0.1746 0.3277 0.0068  -0.0013 -0.0325 76   LYS   A CE  
1709 N  NZ  . LYS   A 76  ? 0.1938 0.1721 0.3794 -0.0012 -0.0042 -0.0442 76   LYS   A NZ  
1723 N  N   . VAL   A 77  ? 0.1692 0.1367 0.1309 -0.0074 0.0229  0.0155  77   VAL   A N   
1724 C  CA  . VAL   A 77  ? 0.1698 0.1375 0.1327 0.0008  0.0144  0.0165  77   VAL   A CA  
1725 C  C   . VAL   A 77  ? 0.1669 0.1320 0.1261 0.0081  0.0102  0.0075  77   VAL   A C   
1726 O  O   . VAL   A 77  ? 0.1774 0.1359 0.1287 0.0096  0.0247  0.0033  77   VAL   A O   
1727 C  CB  . VAL   A 77  ? 0.1854 0.1568 0.1426 0.0022  -0.0013 0.0187  77   VAL   A CB  
1728 C  CG1 . VAL   A 77  ? 0.1878 0.1640 0.1696 0.0067  -0.0124 0.0118  77   VAL   A CG1 
1729 C  CG2 . VAL   A 77  ? 0.2024 0.1684 0.1405 0.0009  -0.0123 0.0253  77   VAL   A CG2 
1739 N  N   . GLY   A 78  ? 0.1600 0.1287 0.1188 0.0076  0.0146  0.0111  78   GLY   A N   
1740 C  CA  . GLY   A 78  ? 0.1531 0.1278 0.1286 -0.0030 0.0174  0.0130  78   GLY   A CA  
1741 C  C   . GLY   A 78  ? 0.1455 0.1234 0.1282 0.0038  0.0208  0.0143  78   GLY   A C   
1742 O  O   . GLY   A 78  ? 0.1386 0.1320 0.1493 -0.0016 0.0178  0.0239  78   GLY   A O   
1746 N  N   . GLY   A 79  ? 0.1484 0.1189 0.1323 -0.0005 0.0134  0.0072  79   GLY   A N   
1747 C  CA  . GLY   A 79  ? 0.1426 0.1210 0.1453 -0.0012 0.0192  0.0113  79   GLY   A CA  
1748 C  C   . GLY   A 79  ? 0.1316 0.1204 0.1332 0.0022  0.0173  0.0055  79   GLY   A C   
1749 O  O   . GLY   A 79  ? 0.1350 0.1307 0.1371 0.0171  0.0096  0.0072  79   GLY   A O   
1753 N  N   . SER   A 80  ? 0.1251 0.1319 0.1574 0.0006  0.0125  -0.0030 80   SER   A N   
1754 C  CA  . SER   A 80  ? 0.1186 0.1292 0.1436 0.0004  0.0033  0.0074  80   SER   A CA  
1755 C  C   . SER   A 80  ? 0.1171 0.1335 0.1391 -0.0023 0.0030  0.0129  80   SER   A C   
1756 O  O   . SER   A 80  ? 0.1138 0.1522 0.1773 0.0071  0.0096  -0.0011 80   SER   A O   
1757 C  CB  . SER   A 80  ? 0.1298 0.1244 0.1627 -0.0091 0.0000  0.0082  80   SER   A CB  
1758 O  OG  . SER   A 80  ? 0.1517 0.1286 0.2021 0.0020  -0.0060 0.0179  80   SER   A OG  
1764 N  N   . CYS   A 81  ? 0.1139 0.1274 0.1325 -0.0003 -0.0027 0.0114  81   CYS   A N   
1765 C  CA  . CYS   A 81  ? 0.1166 0.1342 0.1405 -0.0005 -0.0077 0.0197  81   CYS   A CA  
1766 C  C   . CYS   A 81  ? 0.1148 0.1259 0.1369 -0.0069 -0.0071 0.0252  81   CYS   A C   
1767 O  O   . CYS   A 81  ? 0.1120 0.1560 0.1496 0.0004  0.0023  0.0315  81   CYS   A O   
1768 C  CB  . CYS   A 81  ? 0.1227 0.1417 0.1547 -0.0121 -0.0037 0.0263  81   CYS   A CB  
1769 S  SG  . CYS   A 81  ? 0.1325 0.1270 0.1564 -0.0143 -0.0010 0.0156  81   CYS   A SG  
1775 N  N   . VAL   A 82  ? 0.1184 0.1357 0.1417 -0.0001 -0.0105 0.0192  82   VAL   A N   
1776 C  CA  . VAL   A 82  ? 0.1263 0.1403 0.1416 0.0014  -0.0140 0.0261  82   VAL   A CA  
1777 C  C   . VAL   A 82  ? 0.1225 0.1404 0.1513 -0.0016 -0.0108 0.0240  82   VAL   A C   
1778 O  O   . VAL   A 82  ? 0.1201 0.1535 0.1822 -0.0043 -0.0090 0.0044  82   VAL   A O   
1779 C  CB  . VAL   A 82  ? 0.1591 0.1517 0.1610 0.0050  -0.0077 0.0304  82   VAL   A CB  
1780 C  CG1 . VAL   A 82  ? 0.1853 0.1720 0.1804 0.0106  -0.0011 0.0344  82   VAL   A CG1 
1781 C  CG2 . VAL   A 82  ? 0.1728 0.1527 0.1917 -0.0011 -0.0109 0.0326  82   VAL   A CG2 
1791 N  N   . LEU   A 83  ? 0.1209 0.1356 0.1393 -0.0038 -0.0071 0.0175  83   LEU   A N   
1792 C  CA  . LEU   A 83  ? 0.1208 0.1399 0.1380 -0.0096 -0.0126 0.0142  83   LEU   A CA  
1793 C  C   . LEU   A 83  ? 0.1299 0.1451 0.1228 -0.0130 -0.0100 0.0186  83   LEU   A C   
1794 O  O   . LEU   A 83  ? 0.1362 0.1453 0.1417 -0.0116 -0.0072 0.0236  83   LEU   A O   
1795 C  CB  . LEU   A 83  ? 0.1326 0.1430 0.1470 -0.0134 -0.0155 0.0134  83   LEU   A CB  
1796 C  CG  . LEU   A 83  ? 0.1453 0.1513 0.1571 -0.0164 -0.0029 0.0096  83   LEU   A CG  
1797 C  CD1 . LEU   A 83  ? 0.1592 0.1569 0.1434 -0.0279 -0.0020 0.0192  83   LEU   A CD1 
1798 C  CD2 . LEU   A 83  ? 0.1473 0.1650 0.1729 -0.0107 0.0118  0.0148  83   LEU   A CD2 
1810 N  N   . SER   A 84  ? 0.1489 0.1513 0.1341 -0.0194 -0.0159 0.0165  84   SER   A N   
1811 C  CA  . SER   A 84  ? 0.1567 0.1593 0.1250 -0.0194 -0.0191 0.0184  84   SER   A CA  
1812 C  C   . SER   A 84  ? 0.1548 0.1494 0.1276 -0.0198 -0.0059 0.0118  84   SER   A C   
1813 O  O   . SER   A 84  ? 0.1454 0.1617 0.1241 -0.0141 -0.0159 0.0096  84   SER   A O   
1814 C  CB  . SER   A 84  ? 0.1608 0.1804 0.1412 -0.0196 -0.0191 0.0065  84   SER   A CB  
1815 O  OG  . SER   A 84  ? 0.1675 0.2023 0.1499 -0.0162 -0.0237 -0.0027 84   SER   A OG  
1821 N  N   . GLY   A 85  ? 0.1650 0.1629 0.1329 -0.0217 0.0051  0.0070  85   GLY   A N   
1822 C  CA  . GLY   A 85  ? 0.1660 0.1653 0.1451 -0.0262 0.0104  -0.0010 85   GLY   A CA  
1823 C  C   . GLY   A 85  ? 0.1670 0.1734 0.1269 -0.0200 -0.0050 -0.0003 85   GLY   A C   
1824 O  O   . GLY   A 85  ? 0.1669 0.1850 0.1403 -0.0240 0.0035  -0.0106 85   GLY   A O   
1828 N  N   . HIS   A 86  ? 0.1762 0.1669 0.1251 -0.0137 -0.0113 0.0078  86   HIS   A N   
1829 C  CA  . HIS   A 86  ? 0.1930 0.1741 0.1235 -0.0141 -0.0087 0.0039  86   HIS   A CA  
1830 C  C   . HIS   A 86  ? 0.2129 0.1926 0.1169 -0.0214 -0.0127 0.0075  86   HIS   A C   
1831 O  O   . HIS   A 86  ? 0.2209 0.2134 0.1218 -0.0128 -0.0041 0.0041  86   HIS   A O   
1832 C  CB  . HIS   A 86  ? 0.1874 0.1649 0.1399 -0.0118 -0.0067 0.0026  86   HIS   A CB  
1833 C  CG  . HIS   A 86  ? 0.1789 0.1614 0.1370 -0.0090 0.0006  0.0068  86   HIS   A CG  
1834 N  ND1 . HIS   A 86  ? 0.1860 0.1675 0.1689 -0.0212 -0.0021 0.0043  86   HIS   A ND1 
1835 C  CD2 . HIS   A 86  ? 0.1809 0.1534 0.1331 0.0006  -0.0024 0.0107  86   HIS   A CD2 
1836 C  CE1 . HIS   A 86  ? 0.1821 0.1687 0.1511 -0.0198 0.0114  0.0128  86   HIS   A CE1 
1837 N  NE2 . HIS   A 86  ? 0.1757 0.1549 0.1431 -0.0028 -0.0004 0.0192  86   HIS   A NE2 
1845 N  N   . ASN   A 87  ? 0.2308 0.1987 0.1119 -0.0101 0.0059  0.0007  87   ASN   A N   
1846 C  CA  . ASN   A 87  ? 0.2477 0.2070 0.1176 -0.0083 0.0278  -0.0101 87   ASN   A CA  
1847 C  C   . ASN   A 87  ? 0.2390 0.2189 0.1545 -0.0143 0.0483  -0.0029 87   ASN   A C   
1848 O  O   . ASN   A 87  ? 0.2704 0.2434 0.2099 -0.0308 0.0919  -0.0096 87   ASN   A O   
1849 C  CB  . ASN   A 87  ? 0.2678 0.2116 0.1359 0.0029  0.0362  -0.0097 87   ASN   A CB  
1850 C  CG  . ASN   A 87  ? 0.2873 0.2189 0.1486 0.0125  0.0467  -0.0028 87   ASN   A CG  
1851 O  OD1 . ASN   A 87  ? 0.3102 0.2120 0.1554 0.0321  0.0506  -0.0037 87   ASN   A OD1 
1852 N  ND2 . ASN   A 87  ? 0.2912 0.2464 0.1713 0.0108  0.0437  0.0031  87   ASN   A ND2 
1859 N  N   A LEU   A 88  ? 0.2192 0.2127 0.1509 -0.0137 0.0283  0.0122  88   LEU   A N   
1860 N  N   B LEU   A 88  ? 0.2088 0.2124 0.1476 -0.0143 0.0279  0.0058  88   LEU   A N   
1861 C  CA  A LEU   A 88  ? 0.2018 0.2070 0.1597 -0.0135 0.0183  0.0253  88   LEU   A CA  
1862 C  CA  B LEU   A 88  ? 0.1858 0.2071 0.1595 -0.0147 0.0277  0.0194  88   LEU   A CA  
1863 C  C   A LEU   A 88  ? 0.1886 0.2012 0.1580 -0.0132 0.0171  0.0274  88   LEU   A C   
1864 C  C   B LEU   A 88  ? 0.1782 0.2009 0.1568 -0.0138 0.0252  0.0381  88   LEU   A C   
1865 O  O   A LEU   A 88  ? 0.1875 0.2023 0.1769 -0.0124 0.0210  0.0296  88   LEU   A O   
1866 O  O   B LEU   A 88  ? 0.1786 0.2044 0.1949 -0.0114 0.0323  0.0568  88   LEU   A O   
1867 C  CB  A LEU   A 88  ? 0.2019 0.2095 0.1698 -0.0153 -0.0036 0.0390  88   LEU   A CB  
1868 C  CB  B LEU   A 88  ? 0.1856 0.2163 0.1675 -0.0201 -0.0053 0.0245  88   LEU   A CB  
1869 C  CG  A LEU   A 88  ? 0.2069 0.2148 0.1884 -0.0168 -0.0198 0.0476  88   LEU   A CG  
1870 C  CG  B LEU   A 88  ? 0.1974 0.2296 0.1874 -0.0197 -0.0185 0.0191  88   LEU   A CG  
1871 C  CD1 A LEU   A 88  ? 0.2082 0.2169 0.1905 -0.0178 -0.0242 0.0524  88   LEU   A CD1 
1872 C  CD1 B LEU   A 88  ? 0.2031 0.2377 0.1876 -0.0202 -0.0147 0.0116  88   LEU   A CD1 
1873 C  CD2 A LEU   A 88  ? 0.2142 0.2218 0.2093 -0.0148 -0.0226 0.0408  88   LEU   A CD2 
1874 C  CD2 B LEU   A 88  ? 0.2114 0.2396 0.2101 -0.0101 -0.0139 0.0095  88   LEU   A CD2 
1897 N  N   . ALA   A 89  ? 0.1806 0.1975 0.1474 -0.0144 0.0087  0.0212  89   ALA   A N   
1898 C  CA  . ALA   A 89  ? 0.1827 0.1957 0.1309 -0.0112 0.0010  0.0216  89   ALA   A CA  
1899 C  C   . ALA   A 89  ? 0.1870 0.2018 0.1459 -0.0106 -0.0119 0.0185  89   ALA   A C   
1900 O  O   . ALA   A 89  ? 0.1780 0.1969 0.1843 -0.0197 -0.0169 -0.0039 89   ALA   A O   
1901 C  CB  . ALA   A 89  ? 0.1753 0.1922 0.1274 -0.0098 0.0031  0.0112  89   ALA   A CB  
1908 N  N   A LYS   A 90  ? 0.1942 0.2134 0.1552 -0.0145 -0.0177 0.0157  90   LYS   A N   
1909 N  N   B LYS   A 90  ? 0.1901 0.2108 0.1325 -0.0145 -0.0225 0.0234  90   LYS   A N   
1910 C  CA  A LYS   A 90  ? 0.2035 0.2247 0.1711 -0.0155 -0.0238 0.0128  90   LYS   A CA  
1911 C  CA  B LYS   A 90  ? 0.1972 0.2203 0.1167 -0.0108 -0.0380 0.0268  90   LYS   A CA  
1912 C  C   A LYS   A 90  ? 0.1873 0.2128 0.1533 -0.0179 -0.0249 0.0068  90   LYS   A C   
1913 C  C   B LYS   A 90  ? 0.1826 0.2095 0.1293 -0.0151 -0.0327 0.0185  90   LYS   A C   
1914 O  O   A LYS   A 90  ? 0.1874 0.2252 0.1750 -0.0203 -0.0299 -0.0050 90   LYS   A O   
1915 O  O   B LYS   A 90  ? 0.1884 0.2179 0.1541 -0.0152 -0.0468 0.0196  90   LYS   A O   
1916 C  CB  A LYS   A 90  ? 0.2286 0.2499 0.2286 -0.0135 -0.0278 0.0185  90   LYS   A CB  
1917 C  CB  B LYS   A 90  ? 0.2200 0.2485 0.1659 -0.0020 -0.0483 0.0423  90   LYS   A CB  
1918 C  CG  A LYS   A 90  ? 0.2543 0.2737 0.2951 -0.0120 -0.0310 0.0229  90   LYS   A CG  
1919 C  CG  B LYS   A 90  ? 0.2499 0.2776 0.2630 0.0025  -0.0518 0.0539  90   LYS   A CG  
1920 C  CD  A LYS   A 90  ? 0.2758 0.2929 0.3521 -0.0122 -0.0306 0.0250  90   LYS   A CD  
1921 C  CD  B LYS   A 90  ? 0.2806 0.3019 0.3472 0.0030  -0.0471 0.0593  90   LYS   A CD  
1922 C  CE  A LYS   A 90  ? 0.2925 0.3074 0.3936 -0.0131 -0.0293 0.0248  90   LYS   A CE  
1923 C  CE  B LYS   A 90  ? 0.3091 0.3258 0.4091 0.0021  -0.0419 0.0575  90   LYS   A CE  
1924 N  NZ  A LYS   A 90  ? 0.3027 0.3161 0.4220 -0.0144 -0.0282 0.0250  90   LYS   A NZ  
1925 N  NZ  B LYS   A 90  ? 0.3292 0.3393 0.4539 -0.0003 -0.0386 0.0569  90   LYS   A NZ  
1952 N  N   . HIS   A 91  ? 0.1750 0.1867 0.1152 -0.0151 -0.0318 0.0174  91   HIS   A N   
1953 C  CA  . HIS   A 91  ? 0.1614 0.1727 0.1173 -0.0099 -0.0269 0.0209  91   HIS   A CA  
1954 C  C   . HIS   A 91  ? 0.1433 0.1597 0.1093 -0.0103 -0.0207 0.0129  91   HIS   A C   
1955 O  O   . HIS   A 91  ? 0.1392 0.1700 0.1286 -0.0197 -0.0069 0.0235  91   HIS   A O   
1956 C  CB  . HIS   A 91  ? 0.1787 0.1990 0.1608 0.0090  -0.0352 0.0235  91   HIS   A CB  
1957 C  CG  . HIS   A 91  ? 0.2157 0.2419 0.2265 0.0190  -0.0699 0.0127  91   HIS   A CG  
1958 N  ND1 . HIS   A 91  ? 0.2250 0.2718 0.2816 0.0193  -0.0786 -0.0093 91   HIS   A ND1 
1959 C  CD2 . HIS   A 91  ? 0.2468 0.2593 0.2500 0.0266  -0.0879 0.0256  91   HIS   A CD2 
1960 C  CE1 . HIS   A 91  ? 0.2424 0.2804 0.2985 0.0270  -0.0753 0.0053  91   HIS   A CE1 
1961 N  NE2 . HIS   A 91  ? 0.2589 0.2766 0.2831 0.0327  -0.0823 0.0169  91   HIS   A NE2 
1970 N  N   . CYS   A 92  ? 0.1338 0.1515 0.1151 -0.0169 -0.0096 0.0129  92   CYS   A N   
1971 C  CA  . CYS   A 92  ? 0.1292 0.1450 0.1179 -0.0151 -0.0010 0.0153  92   CYS   A CA  
1972 C  C   . CYS   A 92  ? 0.1214 0.1396 0.1069 -0.0154 -0.0032 0.0274  92   CYS   A C   
1973 O  O   . CYS   A 92  ? 0.1232 0.1484 0.1363 -0.0203 -0.0054 0.0127  92   CYS   A O   
1974 C  CB  . CYS   A 92  ? 0.1330 0.1422 0.1359 -0.0072 -0.0120 0.0055  92   CYS   A CB  
1975 S  SG  . CYS   A 92  ? 0.1310 0.1308 0.1279 -0.0116 -0.0050 0.0136  92   CYS   A SG  
1981 N  N   . LEU   A 93  ? 0.1189 0.1276 0.1196 -0.0114 0.0031  0.0203  93   LEU   A N   
1982 C  CA  . LEU   A 93  ? 0.1141 0.1231 0.1254 -0.0049 0.0032  0.0151  93   LEU   A CA  
1983 C  C   . LEU   A 93  ? 0.1086 0.1166 0.1194 -0.0022 -0.0033 0.0133  93   LEU   A C   
1984 O  O   . LEU   A 93  ? 0.1096 0.1231 0.1244 0.0003  0.0008  0.0175  93   LEU   A O   
1985 C  CB  . LEU   A 93  ? 0.1179 0.1248 0.1305 0.0003  -0.0026 0.0214  93   LEU   A CB  
1986 C  CG  . LEU   A 93  ? 0.1283 0.1267 0.1306 0.0000  0.0005  0.0275  93   LEU   A CG  
1987 C  CD1 . LEU   A 93  ? 0.1274 0.1318 0.1621 -0.0012 0.0099  0.0191  93   LEU   A CD1 
1988 C  CD2 . LEU   A 93  ? 0.1419 0.1233 0.1468 -0.0039 0.0045  0.0178  93   LEU   A CD2 
2000 N  N   . HIS   A 94  ? 0.1064 0.1142 0.1226 -0.0071 0.0000  0.0155  94   HIS   A N   
2001 C  CA  . HIS   A 94  ? 0.1089 0.1112 0.1134 0.0008  -0.0004 0.0147  94   HIS   A CA  
2002 C  C   . HIS   A 94  ? 0.1113 0.1123 0.1113 -0.0041 -0.0005 0.0173  94   HIS   A C   
2003 O  O   . HIS   A 94  ? 0.1079 0.1309 0.1565 0.0048  -0.0015 -0.0044 94   HIS   A O   
2004 C  CB  . HIS   A 94  ? 0.1121 0.1118 0.1329 -0.0025 -0.0020 0.0111  94   HIS   A CB  
2005 C  CG  . HIS   A 94  ? 0.1104 0.1128 0.1334 -0.0034 -0.0021 0.0143  94   HIS   A CG  
2006 N  ND1 . HIS   A 94  ? 0.1128 0.1098 0.1422 -0.0044 -0.0023 0.0188  94   HIS   A ND1 
2007 C  CD2 . HIS   A 94  ? 0.1203 0.1259 0.1341 -0.0030 -0.0109 0.0098  94   HIS   A CD2 
2008 C  CE1 . HIS   A 94  ? 0.1165 0.1100 0.1363 -0.0085 -0.0052 0.0105  94   HIS   A CE1 
2009 N  NE2 . HIS   A 94  ? 0.1227 0.1206 0.1305 -0.0088 -0.0078 0.0120  94   HIS   A NE2 
2017 N  N   . VAL   A 95  ? 0.1047 0.1069 0.1145 -0.0020 0.0085  0.0083  95   VAL   A N   
2018 C  CA  . VAL   A 95  ? 0.1124 0.1130 0.1091 -0.0072 0.0108  0.0118  95   VAL   A CA  
2019 C  C   . VAL   A 95  ? 0.1202 0.1160 0.0960 -0.0119 0.0027  0.0093  95   VAL   A C   
2020 O  O   . VAL   A 95  ? 0.1213 0.1227 0.1220 0.0083  0.0014  0.0101  95   VAL   A O   
2021 C  CB  . VAL   A 95  ? 0.1161 0.1182 0.1352 -0.0107 0.0116  0.0071  95   VAL   A CB  
2022 C  CG1 . VAL   A 95  ? 0.1307 0.1171 0.1459 -0.0126 0.0032  0.0042  95   VAL   A CG1 
2023 C  CG2 . VAL   A 95  ? 0.1218 0.1169 0.1394 -0.0105 0.0086  0.0231  95   VAL   A CG2 
2033 N  N   . VAL   A 96  ? 0.1232 0.1155 0.0930 -0.0050 -0.0002 0.0198  96   VAL   A N   
2034 C  CA  . VAL   A 96  ? 0.1281 0.1211 0.1192 -0.0017 0.0052  0.0190  96   VAL   A CA  
2035 C  C   . VAL   A 96  ? 0.1322 0.1270 0.1199 -0.0033 0.0088  0.0267  96   VAL   A C   
2036 O  O   . VAL   A 96  ? 0.1396 0.1296 0.1446 -0.0046 0.0094  0.0031  96   VAL   A O   
2037 C  CB  . VAL   A 96  ? 0.1366 0.1233 0.1240 -0.0038 0.0146  0.0128  96   VAL   A CB  
2038 C  CG1 . VAL   A 96  ? 0.1451 0.1280 0.1122 -0.0003 0.0118  0.0118  96   VAL   A CG1 
2039 C  CG2 . VAL   A 96  ? 0.1351 0.1312 0.1325 -0.0103 0.0078  0.0095  96   VAL   A CG2 
2049 N  N   A GLY   A 97  ? 0.1341 0.1298 0.1234 -0.0015 0.0098  0.0230  97   GLY   A N   
2050 N  N   B GLY   A 97  ? 0.1287 0.1304 0.1248 -0.0091 0.0004  0.0183  97   GLY   A N   
2051 C  CA  A GLY   A 97  ? 0.1415 0.1382 0.1213 0.0017  0.0024  0.0250  97   GLY   A CA  
2052 C  CA  B GLY   A 97  ? 0.1363 0.1438 0.1329 -0.0151 -0.0143 0.0211  97   GLY   A CA  
2053 C  C   A GLY   A 97  ? 0.1444 0.1418 0.1096 0.0079  0.0036  0.0204  97   GLY   A C   
2054 C  C   B GLY   A 97  ? 0.1408 0.1476 0.1261 -0.0078 -0.0088 0.0101  97   GLY   A C   
2055 O  O   A GLY   A 97  ? 0.1491 0.1386 0.1030 0.0101  0.0136  0.0244  97   GLY   A O   
2056 O  O   B GLY   A 97  ? 0.1527 0.1438 0.1382 -0.0097 -0.0050 0.0131  97   GLY   A O   
2063 N  N   A PRO   A 98  ? 0.1444 0.1438 0.0753 0.0132  -0.0059 0.0210  98   PRO   A N   
2064 N  N   B PRO   A 98  ? 0.1504 0.1515 0.1337 -0.0018 -0.0085 0.0174  98   PRO   A N   
2065 C  CA  A PRO   A 98  ? 0.1440 0.1508 0.0650 0.0143  -0.0077 0.0198  98   PRO   A CA  
2066 C  CA  B PRO   A 98  ? 0.1594 0.1624 0.1497 0.0005  -0.0025 0.0130  98   PRO   A CA  
2067 C  C   A PRO   A 98  ? 0.1415 0.1573 0.0501 0.0050  -0.0018 0.0308  98   PRO   A C   
2068 C  C   B PRO   A 98  ? 0.1698 0.1602 0.1446 0.0003  -0.0019 0.0228  98   PRO   A C   
2069 O  O   A PRO   A 98  ? 0.1335 0.1479 0.0531 0.0063  0.0016  0.0268  98   PRO   A O   
2070 O  O   B PRO   A 98  ? 0.1688 0.1607 0.1774 0.0009  0.0052  0.0183  98   PRO   A O   
2071 C  CB  A PRO   A 98  ? 0.1465 0.1501 0.0586 0.0229  -0.0128 0.0024  98   PRO   A CB  
2072 C  CB  B PRO   A 98  ? 0.1640 0.1628 0.1609 0.0067  -0.0067 0.0114  98   PRO   A CB  
2073 C  CG  A PRO   A 98  ? 0.1454 0.1407 0.0720 0.0237  -0.0149 -0.0015 98   PRO   A CG  
2074 C  CG  B PRO   A 98  ? 0.1670 0.1585 0.1800 0.0020  -0.0132 0.0114  98   PRO   A CG  
2075 C  CD  A PRO   A 98  ? 0.1446 0.1367 0.0724 0.0179  -0.0067 0.0194  98   PRO   A CD  
2076 C  CD  B PRO   A 98  ? 0.1534 0.1465 0.1533 0.0016  -0.0165 0.0181  98   PRO   A CD  
2091 N  N   A ASN   A 99  ? 0.1450 0.1751 0.0648 0.0025  0.0043  0.0339  99   ASN   A N   
2092 N  N   B ASN   A 99  ? 0.1906 0.1645 0.1430 0.0020  -0.0055 0.0331  99   ASN   A N   
2093 C  CA  A ASN   A 99  ? 0.1597 0.1912 0.0874 -0.0018 0.0024  0.0386  99   ASN   A CA  
2094 C  CA  B ASN   A 99  ? 0.2168 0.1683 0.1443 0.0055  -0.0072 0.0493  99   ASN   A CA  
2095 C  C   A ASN   A 99  ? 0.1827 0.2107 0.1063 -0.0086 -0.0013 0.0373  99   ASN   A C   
2096 C  C   B ASN   A 99  ? 0.2299 0.1807 0.1362 0.0040  -0.0150 0.0583  99   ASN   A C   
2097 O  O   A ASN   A 99  ? 0.1945 0.2218 0.1077 -0.0007 0.0018  0.0267  99   ASN   A O   
2098 O  O   B ASN   A 99  ? 0.2340 0.1787 0.1452 0.0172  -0.0214 0.0427  99   ASN   A O   
2099 C  CB  A ASN   A 99  ? 0.1563 0.1929 0.0911 -0.0001 -0.0032 0.0401  99   ASN   A CB  
2100 C  CB  B ASN   A 99  ? 0.2343 0.1685 0.1762 0.0093  -0.0190 0.0390  99   ASN   A CB  
2101 C  CG  A ASN   A 99  ? 0.1561 0.1952 0.1010 0.0076  0.0018  0.0272  99   ASN   A CG  
2102 C  CG  B ASN   A 99  ? 0.2499 0.1791 0.1930 0.0081  -0.0226 0.0428  99   ASN   A CG  
2103 O  OD1 A ASN   A 99  ? 0.1655 0.1992 0.0935 0.0195  0.0020  0.0161  99   ASN   A OD1 
2104 O  OD1 B ASN   A 99  ? 0.2548 0.1931 0.1828 0.0100  -0.0281 0.0522  99   ASN   A OD1 
2105 N  ND2 A ASN   A 99  ? 0.1523 0.1959 0.1044 0.0086  0.0010  0.0350  99   ASN   A ND2 
2106 N  ND2 B ASN   A 99  ? 0.2537 0.1780 0.2270 0.0204  -0.0309 0.0227  99   ASN   A ND2 
2119 N  N   A VAL   A 100 ? 0.1930 0.2199 0.1395 -0.0186 -0.0210 0.0346  100  VAL   A N   
2120 N  N   B VAL   A 100 ? 0.2472 0.2065 0.1556 -0.0061 -0.0303 0.0603  100  VAL   A N   
2121 C  CA  A VAL   A 100 ? 0.2045 0.2312 0.1652 -0.0186 -0.0217 0.0302  100  VAL   A CA  
2122 C  CA  B VAL   A 100 ? 0.2811 0.2247 0.1869 -0.0095 -0.0501 0.0514  100  VAL   A CA  
2123 C  C   A VAL   A 100 ? 0.2109 0.2433 0.1614 -0.0251 -0.0096 0.0441  100  VAL   A C   
2124 C  C   B VAL   A 100 ? 0.2910 0.2223 0.1826 0.0037  -0.0580 0.0557  100  VAL   A C   
2125 O  O   A VAL   A 100 ? 0.2112 0.2466 0.1408 -0.0259 0.0011  0.0540  100  VAL   A O   
2126 O  O   B VAL   A 100 ? 0.2991 0.2277 0.2000 0.0035  -0.0569 0.0413  100  VAL   A O   
2127 C  CB  A VAL   A 100 ? 0.2114 0.2311 0.1997 -0.0150 -0.0251 0.0173  100  VAL   A CB  
2128 C  CB  B VAL   A 100 ? 0.3032 0.2479 0.2344 -0.0179 -0.0469 0.0467  100  VAL   A CB  
2129 C  CG1 A VAL   A 100 ? 0.2108 0.2333 0.2176 -0.0166 -0.0227 0.0099  100  VAL   A CG1 
2130 C  CG1 B VAL   A 100 ? 0.3066 0.2503 0.2617 -0.0180 -0.0480 0.0535  100  VAL   A CG1 
2131 C  CG2 A VAL   A 100 ? 0.2173 0.2311 0.2088 -0.0154 -0.0240 0.0170  100  VAL   A CG2 
2132 C  CG2 B VAL   A 100 ? 0.3108 0.2576 0.2512 -0.0158 -0.0474 0.0409  100  VAL   A CG2 
2151 N  N   A ASN   A 101 ? 0.2183 0.2501 0.1759 -0.0285 -0.0067 0.0502  101  ASN   A N   
2152 N  N   B ASN   A 101 ? 0.2957 0.2250 0.1744 0.0129  -0.0624 0.0606  101  ASN   A N   
2153 C  CA  A ASN   A 101 ? 0.2305 0.2560 0.1923 -0.0287 -0.0057 0.0505  101  ASN   A CA  
2154 C  CA  B ASN   A 101 ? 0.3070 0.2404 0.1808 0.0205  -0.0490 0.0654  101  ASN   A CA  
2155 C  C   A ASN   A 101 ? 0.2441 0.2687 0.2035 -0.0237 0.0057  0.0582  101  ASN   A C   
2156 C  C   B ASN   A 101 ? 0.3315 0.2623 0.1779 0.0239  -0.0249 0.0839  101  ASN   A C   
2157 O  O   A ASN   A 101 ? 0.2535 0.2736 0.2142 -0.0189 -0.0000 0.0537  101  ASN   A O   
2158 O  O   B ASN   A 101 ? 0.3410 0.2678 0.1959 0.0269  -0.0204 0.0774  101  ASN   A O   
2159 C  CB  A ASN   A 101 ? 0.2305 0.2475 0.1800 -0.0315 -0.0204 0.0383  101  ASN   A CB  
2160 C  CB  B ASN   A 101 ? 0.2951 0.2369 0.1953 0.0190  -0.0494 0.0655  101  ASN   A CB  
2161 C  CG  A ASN   A 101 ? 0.2306 0.2394 0.1662 -0.0320 -0.0362 0.0137  101  ASN   A CG  
2162 C  CG  B ASN   A 101 ? 0.2879 0.2489 0.2258 0.0130  -0.0535 0.0533  101  ASN   A CG  
2163 O  OD1 A ASN   A 101 ? 0.2282 0.2389 0.1667 -0.0267 -0.0389 -0.0052 101  ASN   A OD1 
2164 O  OD1 B ASN   A 101 ? 0.2932 0.2620 0.2552 0.0011  -0.0481 0.0375  101  ASN   A OD1 
2165 N  ND2 A ASN   A 101 ? 0.2347 0.2363 0.1605 -0.0329 -0.0447 0.0101  101  ASN   A ND2 
2166 N  ND2 B ASN   A 101 ? 0.2843 0.2461 0.2513 0.0153  -0.0455 0.0491  101  ASN   A ND2 
2179 N  N   A LYS   A 102 ? 0.2478 0.2780 0.2099 -0.0230 0.0171  0.0639  102  LYS   A N   
2180 N  N   B LYS   A 102 ? 0.3433 0.2816 0.2085 0.0228  -0.0069 0.0916  102  LYS   A N   
2181 C  CA  A LYS   A 102 ? 0.2570 0.2872 0.2235 -0.0183 0.0172  0.0586  102  LYS   A CA  
2182 C  CA  B LYS   A 102 ? 0.3594 0.3025 0.2198 0.0171  0.0130  0.0977  102  LYS   A CA  
2183 C  C   A LYS   A 102 ? 0.2679 0.2978 0.2133 -0.0071 0.0124  0.0479  102  LYS   A C   
2184 C  C   B LYS   A 102 ? 0.3605 0.3058 0.2042 0.0221  0.0001  0.1041  102  LYS   A C   
2185 O  O   A LYS   A 102 ? 0.2686 0.3029 0.2133 -0.0026 0.0142  0.0449  102  LYS   A O   
2186 O  O   B LYS   A 102 ? 0.3621 0.3130 0.2209 0.0219  0.0112  0.1014  102  LYS   A O   
2187 C  CB  A LYS   A 102 ? 0.2575 0.2858 0.2478 -0.0229 0.0185  0.0575  102  LYS   A CB  
2188 C  CB  B LYS   A 102 ? 0.3766 0.3215 0.2902 0.0079  0.0281  0.0720  102  LYS   A CB  
2189 C  CG  A LYS   A 102 ? 0.2586 0.2813 0.2602 -0.0258 0.0167  0.0595  102  LYS   A CG  
2190 C  CG  B LYS   A 102 ? 0.3932 0.3405 0.3653 -0.0000 0.0367  0.0441  102  LYS   A CG  
2191 C  CD  A LYS   A 102 ? 0.2614 0.2797 0.2708 -0.0251 0.0165  0.0556  102  LYS   A CD  
2192 C  CD  B LYS   A 102 ? 0.4103 0.3624 0.4380 -0.0052 0.0437  0.0172  102  LYS   A CD  
2193 C  CE  A LYS   A 102 ? 0.2643 0.2782 0.2845 -0.0235 0.0133  0.0521  102  LYS   A CE  
2194 C  CE  B LYS   A 102 ? 0.4234 0.3805 0.4921 -0.0080 0.0502  0.0000  102  LYS   A CE  
2195 N  NZ  A LYS   A 102 ? 0.2662 0.2770 0.2882 -0.0233 0.0132  0.0503  102  LYS   A NZ  
2196 N  NZ  B LYS   A 102 ? 0.4318 0.3919 0.5245 -0.0091 0.0522  -0.0050 102  LYS   A NZ  
2223 N  N   A GLY   A 103 ? 0.2788 0.3035 0.2189 0.0010  0.0049  0.0326  103  GLY   A N   
2224 N  N   B GLY   A 103 ? 0.3579 0.3031 0.1709 0.0274  -0.0272 0.0927  103  GLY   A N   
2225 C  CA  A GLY   A 103 ? 0.2887 0.3091 0.2304 0.0069  -0.0011 0.0230  103  GLY   A CA  
2226 C  CA  B GLY   A 103 ? 0.3487 0.2961 0.1897 0.0284  -0.0339 0.0766  103  GLY   A CA  
2227 C  C   A GLY   A 103 ? 0.2942 0.3142 0.2376 0.0087  -0.0018 0.0181  103  GLY   A C   
2228 C  C   B GLY   A 103 ? 0.3280 0.2842 0.1826 0.0258  -0.0311 0.0607  103  GLY   A C   
2229 O  O   A GLY   A 103 ? 0.2971 0.3147 0.2511 0.0092  -0.0040 0.0151  103  GLY   A O   
2230 O  O   B GLY   A 103 ? 0.3394 0.2932 0.2024 0.0306  -0.0271 0.0568  103  GLY   A O   
2237 N  N   A GLU   A 104 ? 0.2952 0.3177 0.2275 0.0067  0.0022  0.0126  104  GLU   A N   
2238 N  N   B GLU   A 104 ? 0.2891 0.2600 0.1596 0.0182  -0.0396 0.0576  104  GLU   A N   
2239 C  CA  A GLU   A 104 ? 0.2948 0.3202 0.2236 0.0022  0.0061  0.0097  104  GLU   A CA  
2240 C  CA  B GLU   A 104 ? 0.2543 0.2323 0.1434 0.0026  -0.0362 0.0494  104  GLU   A CA  
2241 C  C   A GLU   A 104 ? 0.2980 0.3264 0.2235 -0.0037 0.0009  0.0040  104  GLU   A C   
2242 C  C   B GLU   A 104 ? 0.2493 0.2299 0.1529 0.0011  -0.0305 0.0330  104  GLU   A C   
2243 O  O   A GLU   A 104 ? 0.2982 0.3269 0.2233 -0.0057 -0.0022 0.0013  104  GLU   A O   
2244 O  O   B GLU   A 104 ? 0.2447 0.2333 0.1968 0.0022  -0.0368 0.0310  104  GLU   A O   
2245 C  CB  A GLU   A 104 ? 0.2910 0.3171 0.2285 0.0032  0.0110  0.0131  104  GLU   A CB  
2246 C  CB  B GLU   A 104 ? 0.2317 0.2141 0.1394 -0.0080 -0.0279 0.0535  104  GLU   A CB  
2247 C  CG  A GLU   A 104 ? 0.2896 0.3139 0.2390 0.0051  0.0163  0.0151  104  GLU   A CG  
2248 C  CG  B GLU   A 104 ? 0.2193 0.2152 0.1613 -0.0183 -0.0198 0.0508  104  GLU   A CG  
2249 C  CD  A GLU   A 104 ? 0.2887 0.3116 0.2462 0.0068  0.0239  0.0203  104  GLU   A CD  
2250 C  CD  B GLU   A 104 ? 0.2082 0.2205 0.1479 -0.0295 -0.0082 0.0605  104  GLU   A CD  
2251 O  OE1 A GLU   A 104 ? 0.2865 0.3112 0.2420 0.0076  0.0321  0.0268  104  GLU   A OE1 
2252 O  OE1 B GLU   A 104 ? 0.2017 0.2249 0.1504 -0.0328 -0.0141 0.0622  104  GLU   A OE1 
2253 O  OE2 A GLU   A 104 ? 0.2938 0.3109 0.2611 0.0080  0.0229  0.0166  104  GLU   A OE2 
2254 O  OE2 B GLU   A 104 ? 0.2218 0.2271 0.1586 -0.0368 0.0110  0.0533  104  GLU   A OE2 
2267 N  N   A ASP   A 105 ? 0.3021 0.3325 0.2304 -0.0048 -0.0004 -0.0005 105  ASP   A N   
2268 N  N   B ASP   A 105 ? 0.2613 0.2256 0.1566 -0.0021 -0.0098 0.0240  105  ASP   A N   
2269 C  CA  A ASP   A 105 ? 0.3043 0.3377 0.2450 -0.0074 -0.0042 -0.0098 105  ASP   A CA  
2270 C  CA  B ASP   A 105 ? 0.2693 0.2235 0.1809 0.0033  0.0025  -0.0050 105  ASP   A CA  
2271 C  C   A ASP   A 105 ? 0.2919 0.3337 0.2384 -0.0136 -0.0144 -0.0164 105  ASP   A C   
2272 C  C   B ASP   A 105 ? 0.2505 0.2035 0.1501 -0.0065 -0.0032 -0.0126 105  ASP   A C   
2273 O  O   A ASP   A 105 ? 0.2890 0.3341 0.2268 -0.0148 -0.0158 -0.0178 105  ASP   A O   
2274 O  O   B ASP   A 105 ? 0.2383 0.1912 0.1230 -0.0023 -0.0074 -0.0179 105  ASP   A O   
2275 C  CB  A ASP   A 105 ? 0.3170 0.3458 0.2705 -0.0040 0.0020  -0.0120 105  ASP   A CB  
2276 C  CB  B ASP   A 105 ? 0.2926 0.2506 0.2398 0.0187  0.0208  -0.0313 105  ASP   A CB  
2277 C  CG  A ASP   A 105 ? 0.3279 0.3522 0.2948 -0.0007 0.0002  -0.0147 105  ASP   A CG  
2278 C  CG  B ASP   A 105 ? 0.3125 0.2756 0.2983 0.0330  0.0229  -0.0569 105  ASP   A CG  
2279 O  OD1 A ASP   A 105 ? 0.3294 0.3551 0.2982 0.0020  -0.0049 -0.0228 105  ASP   A OD1 
2280 O  OD1 B ASP   A 105 ? 0.3239 0.2821 0.2959 0.0251  0.0077  -0.0702 105  ASP   A OD1 
2281 O  OD2 A ASP   A 105 ? 0.3355 0.3543 0.3148 -0.0005 0.0023  -0.0069 105  ASP   A OD2 
2282 O  OD2 B ASP   A 105 ? 0.3191 0.2894 0.3494 0.0436  0.0263  -0.0483 105  ASP   A OD2 
2291 N  N   A ILE   A 106 ? 0.2818 0.3272 0.2471 -0.0190 -0.0259 -0.0237 106  ILE   A N   
2292 N  N   B ILE   A 106 ? 0.2415 0.2101 0.1700 -0.0115 -0.0273 0.0048  106  ILE   A N   
2293 C  CA  A ILE   A 106 ? 0.2680 0.3188 0.2542 -0.0232 -0.0344 -0.0313 106  ILE   A CA  
2294 C  CA  B ILE   A 106 ? 0.2250 0.2191 0.1877 -0.0243 -0.0396 0.0002  106  ILE   A CA  
2295 C  C   A ILE   A 106 ? 0.2586 0.3091 0.2558 -0.0303 -0.0333 -0.0421 106  ILE   A C   
2296 C  C   B ILE   A 106 ? 0.2071 0.2086 0.1811 -0.0300 -0.0401 0.0043  106  ILE   A C   
2297 O  O   A ILE   A 106 ? 0.2503 0.3061 0.2490 -0.0324 -0.0334 -0.0476 106  ILE   A O   
2298 O  O   B ILE   A 106 ? 0.1886 0.2147 0.1927 -0.0349 -0.0266 0.0021  106  ILE   A O   
2299 C  CB  A ILE   A 106 ? 0.2646 0.3188 0.2663 -0.0179 -0.0434 -0.0228 106  ILE   A CB  
2300 C  CB  B ILE   A 106 ? 0.2359 0.2512 0.2427 -0.0227 -0.0536 -0.0005 106  ILE   A CB  
2301 C  CG1 A ILE   A 106 ? 0.2589 0.3159 0.2750 -0.0112 -0.0457 -0.0137 106  ILE   A CG1 
2302 C  CG1 B ILE   A 106 ? 0.2329 0.2691 0.2668 -0.0069 -0.0564 0.0132  106  ILE   A CG1 
2303 C  CG2 A ILE   A 106 ? 0.2660 0.3201 0.2653 -0.0171 -0.0489 -0.0237 106  ILE   A CG2 
2304 C  CG2 B ILE   A 106 ? 0.2442 0.2616 0.2509 -0.0287 -0.0602 -0.0130 106  ILE   A CG2 
2305 C  CD1 A ILE   A 106 ? 0.2561 0.3136 0.2816 -0.0064 -0.0411 -0.0087 106  ILE   A CD1 
2306 C  CD1 B ILE   A 106 ? 0.2312 0.2756 0.2858 0.0030  -0.0495 0.0229  106  ILE   A CD1 
2329 N  N   A GLN   A 107 ? 0.2622 0.3029 0.2729 -0.0324 -0.0252 -0.0486 107  GLN   A N   
2330 N  N   B GLN   A 107 ? 0.2229 0.1971 0.1868 -0.0182 -0.0404 0.0035  107  GLN   A N   
2331 C  CA  A GLN   A 107 ? 0.2659 0.2954 0.3000 -0.0288 -0.0142 -0.0460 107  GLN   A CA  
2332 C  CA  B GLN   A 107 ? 0.2456 0.2041 0.2513 -0.0097 -0.0293 0.0103  107  GLN   A CA  
2333 C  C   A GLN   A 107 ? 0.2400 0.2669 0.2721 -0.0296 -0.0010 -0.0410 107  GLN   A C   
2334 C  C   B GLN   A 107 ? 0.2170 0.1754 0.2148 0.0005  -0.0168 0.0323  107  GLN   A C   
2335 O  O   A GLN   A 107 ? 0.2423 0.2703 0.2930 -0.0304 0.0067  -0.0446 107  GLN   A O   
2336 O  O   B GLN   A 107 ? 0.2299 0.1793 0.2407 -0.0053 -0.0104 0.0310  107  GLN   A O   
2337 C  CB  A GLN   A 107 ? 0.2937 0.3165 0.3630 -0.0264 -0.0171 -0.0457 107  GLN   A CB  
2338 C  CB  B GLN   A 107 ? 0.2967 0.2573 0.3584 -0.0197 -0.0308 0.0007  107  GLN   A CB  
2339 C  CG  A GLN   A 107 ? 0.3184 0.3365 0.4247 -0.0226 -0.0192 -0.0416 107  GLN   A CG  
2340 C  CG  B GLN   A 107 ? 0.3455 0.3123 0.4610 -0.0258 -0.0323 0.0071  107  GLN   A CG  
2341 C  CD  A GLN   A 107 ? 0.3395 0.3517 0.4757 -0.0192 -0.0209 -0.0359 107  GLN   A CD  
2342 C  CD  B GLN   A 107 ? 0.3916 0.3603 0.5510 -0.0281 -0.0324 0.0159  107  GLN   A CD  
2343 O  OE1 A GLN   A 107 ? 0.3452 0.3587 0.4975 -0.0187 -0.0215 -0.0350 107  GLN   A OE1 
2344 O  OE1 B GLN   A 107 ? 0.4107 0.3756 0.5776 -0.0272 -0.0305 0.0245  107  GLN   A OE1 
2345 N  NE2 A GLN   A 107 ? 0.3454 0.3553 0.4937 -0.0184 -0.0224 -0.0348 107  GLN   A NE2 
2346 N  NE2 B GLN   A 107 ? 0.3995 0.3819 0.5748 -0.0302 -0.0361 0.0163  107  GLN   A NE2 
2363 N  N   A LEU   A 108 ? 0.2137 0.2330 0.2286 -0.0273 0.0038  -0.0347 108  LEU   A N   
2364 N  N   B LEU   A 108 ? 0.1931 0.1637 0.1781 -0.0102 0.0061  0.0132  108  LEU   A N   
2365 C  CA  A LEU   A 108 ? 0.1931 0.2027 0.2033 -0.0173 0.0064  -0.0131 108  LEU   A CA  
2366 C  CA  B LEU   A 108 ? 0.1809 0.1581 0.1771 -0.0082 0.0170  0.0163  108  LEU   A CA  
2367 C  C   A LEU   A 108 ? 0.1719 0.1713 0.1809 -0.0088 0.0083  0.0035  108  LEU   A C   
2368 C  C   B LEU   A 108 ? 0.1646 0.1404 0.1643 -0.0102 0.0149  0.0238  108  LEU   A C   
2369 O  O   A LEU   A 108 ? 0.1699 0.1720 0.1901 -0.0066 0.0075  0.0009  108  LEU   A O   
2370 O  O   B LEU   A 108 ? 0.1649 0.1444 0.1895 -0.0112 0.0180  0.0309  108  LEU   A O   
2371 C  CB  A LEU   A 108 ? 0.1957 0.2057 0.1922 -0.0183 0.0075  -0.0104 108  LEU   A CB  
2372 C  CB  B LEU   A 108 ? 0.1904 0.1761 0.1584 -0.0117 0.0232  0.0083  108  LEU   A CB  
2373 C  CG  A LEU   A 108 ? 0.2032 0.2111 0.1996 -0.0148 0.0116  -0.0044 108  LEU   A CG  
2374 C  CG  B LEU   A 108 ? 0.2117 0.1949 0.1827 -0.0033 0.0288  0.0115  108  LEU   A CG  
2375 C  CD1 A LEU   A 108 ? 0.2071 0.2128 0.2077 -0.0182 0.0157  -0.0036 108  LEU   A CD1 
2376 C  CD1 B LEU   A 108 ? 0.2218 0.2006 0.1976 -0.0107 0.0359  0.0107  108  LEU   A CD1 
2377 C  CD2 A LEU   A 108 ? 0.2062 0.2199 0.2131 -0.0091 0.0123  0.0029  108  LEU   A CD2 
2378 C  CD2 B LEU   A 108 ? 0.2196 0.2183 0.2174 0.0104  0.0251  0.0176  108  LEU   A CD2 
2401 N  N   . LEU   A 109 ? 0.1555 0.1486 0.1694 -0.0007 0.0123  0.0224  109  LEU   A N   
2402 C  CA  . LEU   A 109 ? 0.1521 0.1410 0.1492 -0.0027 -0.0040 0.0234  109  LEU   A CA  
2403 C  C   . LEU   A 109 ? 0.1344 0.1354 0.1395 -0.0053 0.0032  0.0108  109  LEU   A C   
2404 O  O   . LEU   A 109 ? 0.1407 0.1238 0.1612 -0.0060 -0.0080 0.0062  109  LEU   A O   
2405 C  CB  . LEU   A 109 ? 0.1539 0.1454 0.1729 0.0049  -0.0097 0.0283  109  LEU   A CB  
2406 C  CG  . LEU   A 109 ? 0.1490 0.1508 0.1807 0.0024  -0.0019 0.0303  109  LEU   A CG  
2407 C  CD1 . LEU   A 109 ? 0.1546 0.1425 0.1990 -0.0042 0.0130  0.0232  109  LEU   A CD1 
2408 C  CD2 . LEU   A 109 ? 0.1480 0.1686 0.1964 0.0015  0.0019  0.0323  109  LEU   A CD2 
2421 N  N   . LYS   A 110 ? 0.1401 0.1308 0.1436 -0.0077 -0.0012 0.0154  110  LYS   A N   
2422 C  CA  . LYS   A 110 ? 0.1350 0.1246 0.1657 -0.0103 0.0061  0.0092  110  LYS   A CA  
2423 C  C   . LYS   A 110 ? 0.1335 0.1191 0.1409 -0.0106 0.0026  0.0047  110  LYS   A C   
2424 O  O   . LYS   A 110 ? 0.1301 0.1207 0.1503 -0.0071 0.0042  0.0037  110  LYS   A O   
2425 C  CB  . LYS   A 110 ? 0.1445 0.1282 0.1818 -0.0101 -0.0043 0.0014  110  LYS   A CB  
2426 C  CG  . LYS   A 110 ? 0.1441 0.1272 0.1817 -0.0059 0.0001  -0.0053 110  LYS   A CG  
2427 C  CD  . LYS   A 110 ? 0.1459 0.1321 0.1971 -0.0084 -0.0019 -0.0075 110  LYS   A CD  
2428 C  CE  . LYS   A 110 ? 0.1569 0.1386 0.2032 -0.0073 0.0071  -0.0014 110  LYS   A CE  
2429 N  NZ  . LYS   A 110 ? 0.1526 0.1374 0.2119 -0.0145 0.0196  0.0037  110  LYS   A NZ  
2443 N  N   . SER   A 111 ? 0.1350 0.1253 0.1370 -0.0042 0.0018  0.0081  111  SER   A N   
2444 C  CA  . SER   A 111 ? 0.1305 0.1307 0.1482 -0.0033 0.0068  0.0088  111  SER   A CA  
2445 C  C   . SER   A 111 ? 0.1223 0.1220 0.1453 -0.0080 0.0034  0.0132  111  SER   A C   
2446 O  O   . SER   A 111 ? 0.1347 0.1126 0.1695 -0.0052 0.0044  0.0098  111  SER   A O   
2447 C  CB  . SER   A 111 ? 0.1501 0.1500 0.1691 -0.0092 0.0194  -0.0073 111  SER   A CB  
2448 O  OG  . SER   A 111 ? 0.1931 0.1675 0.1765 -0.0029 0.0271  -0.0110 111  SER   A OG  
2454 N  N   . ALA   A 112 ? 0.1267 0.1156 0.1435 -0.0005 0.0122  0.0064  112  ALA   A N   
2455 C  CA  . ALA   A 112 ? 0.1283 0.1158 0.1407 -0.0021 0.0096  0.0062  112  ALA   A CA  
2456 C  C   . ALA   A 112 ? 0.1195 0.1065 0.1483 -0.0021 0.0056  0.0095  112  ALA   A C   
2457 O  O   . ALA   A 112 ? 0.1242 0.1132 0.1563 -0.0109 0.0071  0.0088  112  ALA   A O   
2458 C  CB  . ALA   A 112 ? 0.1402 0.1258 0.1464 -0.0069 0.0054  0.0124  112  ALA   A CB  
2464 N  N   . TYR   A 113 ? 0.1178 0.1139 0.1502 -0.0037 0.0056  0.0149  113  TYR   A N   
2465 C  CA  . TYR   A 113 ? 0.1151 0.1151 0.1473 -0.0045 0.0128  0.0143  113  TYR   A CA  
2466 C  C   . TYR   A 113 ? 0.1153 0.1079 0.1355 -0.0114 0.0064  0.0103  113  TYR   A C   
2467 O  O   . TYR   A 113 ? 0.1204 0.1149 0.1496 -0.0033 0.0147  0.0113  113  TYR   A O   
2468 C  CB  . TYR   A 113 ? 0.1153 0.1203 0.1526 -0.0025 0.0028  0.0198  113  TYR   A CB  
2469 C  CG  . TYR   A 113 ? 0.1194 0.1300 0.1540 -0.0109 0.0071  0.0201  113  TYR   A CG  
2470 C  CD1 . TYR   A 113 ? 0.1249 0.1408 0.1501 -0.0016 0.0027  0.0182  113  TYR   A CD1 
2471 C  CD2 . TYR   A 113 ? 0.1231 0.1306 0.1525 -0.0119 -0.0017 0.0144  113  TYR   A CD2 
2472 C  CE1 . TYR   A 113 ? 0.1288 0.1478 0.1527 0.0021  0.0019  0.0072  113  TYR   A CE1 
2473 C  CE2 . TYR   A 113 ? 0.1226 0.1405 0.1670 -0.0071 -0.0023 0.0183  113  TYR   A CE2 
2474 C  CZ  . TYR   A 113 ? 0.1192 0.1406 0.1653 0.0021  0.0021  0.0200  113  TYR   A CZ  
2475 O  OH  . TYR   A 113 ? 0.1209 0.1511 0.1983 0.0113  -0.0003 0.0206  113  TYR   A OH  
2485 N  N   . GLU   A 114 ? 0.1136 0.1112 0.1419 -0.0023 0.0144  0.0115  114  GLU   A N   
2486 C  CA  . GLU   A 114 ? 0.1188 0.1105 0.1564 0.0029  0.0071  0.0178  114  GLU   A CA  
2487 C  C   . GLU   A 114 ? 0.1162 0.1157 0.1547 0.0014  0.0118  0.0104  114  GLU   A C   
2488 O  O   . GLU   A 114 ? 0.1269 0.1165 0.1527 0.0006  0.0051  0.0149  114  GLU   A O   
2489 C  CB  . GLU   A 114 ? 0.1196 0.1135 0.1555 -0.0025 0.0069  0.0141  114  GLU   A CB  
2490 C  CG  . GLU   A 114 ? 0.1253 0.1140 0.1585 -0.0033 0.0053  0.0007  114  GLU   A CG  
2491 C  CD  . GLU   A 114 ? 0.1343 0.1115 0.1651 -0.0021 0.0024  0.0060  114  GLU   A CD  
2492 O  OE1 . GLU   A 114 ? 0.1383 0.1211 0.1734 -0.0092 0.0136  -0.0063 114  GLU   A OE1 
2493 O  OE2 . GLU   A 114 ? 0.1533 0.1212 0.1883 -0.0073 0.0078  -0.0058 114  GLU   A OE2 
2500 N  N   . ASN   A 115 ? 0.1171 0.1124 0.1448 -0.0058 0.0071  0.0060  115  ASN   A N   
2501 C  CA  . ASN   A 115 ? 0.1237 0.1169 0.1485 -0.0053 0.0100  0.0125  115  ASN   A CA  
2502 C  C   . ASN   A 115 ? 0.1186 0.1114 0.1431 -0.0067 0.0018  0.0133  115  ASN   A C   
2503 O  O   . ASN   A 115 ? 0.1223 0.1294 0.1417 -0.0096 0.0082  0.0172  115  ASN   A O   
2504 C  CB  . ASN   A 115 ? 0.1291 0.1244 0.1484 -0.0110 0.0112  0.0127  115  ASN   A CB  
2505 C  CG  . ASN   A 115 ? 0.1267 0.1419 0.1636 -0.0104 0.0132  0.0162  115  ASN   A CG  
2506 O  OD1 . ASN   A 115 ? 0.1285 0.2337 0.1881 -0.0089 0.0197  0.0313  115  ASN   A OD1 
2507 N  ND2 . ASN   A 115 ? 0.1323 0.1242 0.1465 -0.0102 0.0200  0.0131  115  ASN   A ND2 
2514 N  N   . PHE   A 116 ? 0.1140 0.1164 0.1396 -0.0000 0.0088  0.0184  116  PHE   A N   
2515 C  CA  . PHE   A 116 ? 0.1190 0.1218 0.1341 -0.0009 0.0070  0.0182  116  PHE   A CA  
2516 C  C   . PHE   A 116 ? 0.1128 0.1264 0.1424 -0.0018 0.0090  0.0186  116  PHE   A C   
2517 O  O   . PHE   A 116 ? 0.1241 0.1327 0.1532 0.0041  0.0116  0.0220  116  PHE   A O   
2518 C  CB  . PHE   A 116 ? 0.1177 0.1178 0.1509 -0.0029 0.0186  0.0157  116  PHE   A CB  
2519 C  CG  . PHE   A 116 ? 0.1180 0.1164 0.1433 -0.0052 0.0103  0.0088  116  PHE   A CG  
2520 C  CD1 . PHE   A 116 ? 0.1166 0.1193 0.1543 -0.0060 0.0075  0.0151  116  PHE   A CD1 
2521 C  CD2 . PHE   A 116 ? 0.1236 0.1183 0.1674 -0.0020 0.0138  0.0168  116  PHE   A CD2 
2522 C  CE1 . PHE   A 116 ? 0.1195 0.1159 0.1603 -0.0117 0.0034  0.0132  116  PHE   A CE1 
2523 C  CE2 . PHE   A 116 ? 0.1209 0.1133 0.1767 -0.0067 0.0092  0.0124  116  PHE   A CE2 
2524 C  CZ  . PHE   A 116 ? 0.1268 0.1093 0.1702 -0.0017 0.0001  0.0118  116  PHE   A CZ  
2534 N  N   . ASN   A 117 ? 0.1181 0.1220 0.1477 -0.0017 0.0087  0.0170  117  ASN   A N   
2535 C  CA  . ASN   A 117 ? 0.1254 0.1179 0.1516 0.0013  0.0110  0.0226  117  ASN   A CA  
2536 C  C   . ASN   A 117 ? 0.1237 0.1271 0.1669 0.0042  0.0152  0.0217  117  ASN   A C   
2537 O  O   . ASN   A 117 ? 0.1296 0.1357 0.1837 0.0024  -0.0034 0.0380  117  ASN   A O   
2538 C  CB  . ASN   A 117 ? 0.1236 0.1221 0.1551 0.0000  0.0099  0.0278  117  ASN   A CB  
2539 C  CG  . ASN   A 117 ? 0.1183 0.1256 0.1583 0.0004  0.0133  0.0261  117  ASN   A CG  
2540 O  OD1 . ASN   A 117 ? 0.1226 0.1466 0.1639 -0.0117 0.0167  0.0166  117  ASN   A OD1 
2541 N  ND2 . ASN   A 117 ? 0.1110 0.1316 0.1653 0.0023  0.0135  0.0279  117  ASN   A ND2 
2548 N  N   . GLN   A 118 ? 0.1149 0.1249 0.1726 -0.0018 0.0024  0.0269  118  GLN   A N   
2549 C  CA  . GLN   A 118 ? 0.1243 0.1359 0.1749 -0.0049 -0.0026 0.0158  118  GLN   A CA  
2550 C  C   . GLN   A 118 ? 0.1240 0.1466 0.1625 -0.0044 -0.0067 0.0253  118  GLN   A C   
2551 O  O   . GLN   A 118 ? 0.1290 0.1722 0.1880 0.0052  -0.0086 0.0073  118  GLN   A O   
2552 C  CB  . GLN   A 118 ? 0.1252 0.1410 0.1902 -0.0008 0.0107  0.0195  118  GLN   A CB  
2553 C  CG  . GLN   A 118 ? 0.1250 0.1408 0.1795 0.0052  0.0115  0.0235  118  GLN   A CG  
2554 C  CD  . GLN   A 118 ? 0.1204 0.1439 0.1861 0.0053  0.0056  0.0186  118  GLN   A CD  
2555 O  OE1 . GLN   A 118 ? 0.1264 0.1622 0.1974 0.0118  -0.0035 0.0156  118  GLN   A OE1 
2556 N  NE2 . GLN   A 118 ? 0.1280 0.1405 0.1910 0.0070  0.0029  0.0226  118  GLN   A NE2 
2565 N  N   . HIS   A 119 ? 0.1285 0.1426 0.1506 -0.0021 0.0036  0.0331  119  HIS   A N   
2566 C  CA  . HIS   A 119 ? 0.1374 0.1482 0.1615 -0.0023 0.0039  0.0330  119  HIS   A CA  
2567 C  C   . HIS   A 119 ? 0.1471 0.1568 0.1545 -0.0046 0.0089  0.0342  119  HIS   A C   
2568 O  O   . HIS   A 119 ? 0.1451 0.1634 0.1629 -0.0182 0.0049  0.0276  119  HIS   A O   
2569 C  CB  . HIS   A 119 ? 0.1357 0.1473 0.1739 -0.0010 0.0178  0.0324  119  HIS   A CB  
2570 C  CG  . HIS   A 119 ? 0.1409 0.1452 0.2230 0.0073  0.0139  0.0435  119  HIS   A CG  
2571 N  ND1 . HIS   A 119 ? 0.1525 0.1614 0.2821 -0.0051 0.0105  0.0273  119  HIS   A ND1 
2572 C  CD2 . HIS   A 119 ? 0.1538 0.1560 0.2514 0.0133  0.0321  0.0681  119  HIS   A CD2 
2573 C  CE1 . HIS   A 119 ? 0.1543 0.1615 0.3059 -0.0091 0.0244  0.0491  119  HIS   A CE1 
2574 N  NE2 . HIS   A 119 ? 0.1629 0.1616 0.2915 0.0030  0.0426  0.0672  119  HIS   A NE2 
2582 N  N   A GLU   A 120 ? 0.1615 0.1787 0.1768 -0.0014 0.0063  0.0336  120  GLU   A N   
2583 N  N   B GLU   A 120 ? 0.1449 0.1685 0.1441 0.0045  -0.0012 0.0523  120  GLU   A N   
2584 C  CA  A GLU   A 120 ? 0.1818 0.2042 0.2105 0.0007  0.0051  0.0425  120  GLU   A CA  
2585 C  CA  B GLU   A 120 ? 0.1610 0.1894 0.1725 0.0135  -0.0004 0.0868  120  GLU   A CA  
2586 C  C   A GLU   A 120 ? 0.1654 0.1954 0.1776 -0.0031 0.0026  0.0479  120  GLU   A C   
2587 C  C   B GLU   A 120 ? 0.1487 0.1791 0.1587 -0.0003 0.0002  0.0767  120  GLU   A C   
2588 O  O   A GLU   A 120 ? 0.1665 0.1973 0.1805 -0.0034 0.0018  0.0409  120  GLU   A O   
2589 O  O   B GLU   A 120 ? 0.1432 0.1668 0.1783 -0.0021 0.0042  0.0739  120  GLU   A O   
2590 C  CB  A GLU   A 120 ? 0.2193 0.2423 0.2783 0.0068  0.0063  0.0500  120  GLU   A CB  
2591 C  CB  B GLU   A 120 ? 0.2001 0.2376 0.2227 0.0316  0.0048  0.1343  120  GLU   A CB  
2592 C  CG  A GLU   A 120 ? 0.2640 0.2803 0.3531 0.0141  0.0043  0.0507  120  GLU   A CG  
2593 C  CG  B GLU   A 120 ? 0.2693 0.2939 0.3299 0.0509  0.0022  0.1431  120  GLU   A CG  
2594 C  CD  A GLU   A 120 ? 0.3110 0.3189 0.4215 0.0206  0.0041  0.0466  120  GLU   A CD  
2595 C  CD  B GLU   A 120 ? 0.3461 0.3519 0.4410 0.0684  0.0138  0.1285  120  GLU   A CD  
2596 O  OE1 A GLU   A 120 ? 0.3198 0.3249 0.4420 0.0220  0.0030  0.0456  120  GLU   A OE1 
2597 O  OE1 B GLU   A 120 ? 0.3660 0.3621 0.4698 0.0707  0.0176  0.1218  120  GLU   A OE1 
2598 O  OE2 A GLU   A 120 ? 0.3311 0.3329 0.4433 0.0205  0.0033  0.0446  120  GLU   A OE2 
2599 O  OE2 B GLU   A 120 ? 0.3819 0.3817 0.4936 0.0729  0.0165  0.1241  120  GLU   A OE2 
2612 N  N   . VAL   A 121 ? 0.1502 0.1850 0.1542 -0.0030 0.0040  0.0572  121  VAL   A N   
2613 C  CA  . VAL   A 121 ? 0.1533 0.1918 0.1395 0.0012  0.0165  0.0590  121  VAL   A CA  
2614 C  C   . VAL   A 121 ? 0.1398 0.1736 0.1346 -0.0105 0.0159  0.0434  121  VAL   A C   
2615 O  O   . VAL   A 121 ? 0.1417 0.1767 0.1559 -0.0236 -0.0044 0.0320  121  VAL   A O   
2616 C  CB  . VAL   A 121 ? 0.1964 0.2300 0.1894 0.0131  0.0326  0.0703  121  VAL   A CB  
2617 C  CG1 . VAL   A 121 ? 0.2011 0.2415 0.1927 0.0243  0.0460  0.0691  121  VAL   A CG1 
2618 C  CG2 . VAL   A 121 ? 0.2213 0.2519 0.2509 0.0078  0.0263  0.0587  121  VAL   A CG2 
2629 N  N   . LEU   A 122 ? 0.1346 0.1448 0.1467 -0.0113 0.0069  0.0413  122  LEU   A N   
2630 C  CA  . LEU   A 122 ? 0.1418 0.1374 0.1475 -0.0121 0.0239  0.0345  122  LEU   A CA  
2631 C  C   . LEU   A 122 ? 0.1361 0.1379 0.1363 -0.0130 0.0091  0.0303  122  LEU   A C   
2632 O  O   . LEU   A 122 ? 0.1353 0.1452 0.1719 -0.0226 0.0047  0.0307  122  LEU   A O   
2633 C  CB  . LEU   A 122 ? 0.1624 0.1410 0.1794 -0.0041 0.0159  0.0358  122  LEU   A CB  
2634 C  CG  . LEU   A 122 ? 0.1684 0.1529 0.1687 -0.0066 0.0214  0.0247  122  LEU   A CG  
2635 C  CD1 . LEU   A 122 ? 0.1856 0.1540 0.1699 -0.0147 0.0144  0.0295  122  LEU   A CD1 
2636 C  CD2 . LEU   A 122 ? 0.1644 0.1406 0.1642 -0.0020 0.0374  0.0231  122  LEU   A CD2 
2648 N  N   A LEU   A 123 ? 0.1337 0.1340 0.1300 -0.0160 0.0098  0.0326  123  LEU   A N   
2649 N  N   B LEU   A 123 ? 0.1282 0.1366 0.1369 -0.0157 -0.0040 0.0263  123  LEU   A N   
2650 C  CA  A LEU   A 123 ? 0.1329 0.1320 0.1218 -0.0165 0.0165  0.0346  123  LEU   A CA  
2651 C  CA  B LEU   A 123 ? 0.1264 0.1421 0.1174 -0.0136 0.0003  0.0228  123  LEU   A CA  
2652 C  C   A LEU   A 123 ? 0.1263 0.1247 0.1194 -0.0140 0.0184  0.0281  123  LEU   A C   
2653 C  C   B LEU   A 123 ? 0.1228 0.1380 0.1066 -0.0048 0.0034  0.0133  123  LEU   A C   
2654 O  O   A LEU   A 123 ? 0.1192 0.1235 0.1113 -0.0197 0.0274  0.0277  123  LEU   A O   
2655 O  O   B LEU   A 123 ? 0.1167 0.1436 0.1280 -0.0160 0.0036  0.0059  123  LEU   A O   
2656 C  CB  A LEU   A 123 ? 0.1410 0.1365 0.1269 -0.0166 0.0251  0.0355  123  LEU   A CB  
2657 C  CB  B LEU   A 123 ? 0.1339 0.1528 0.1206 -0.0136 0.0068  0.0243  123  LEU   A CB  
2658 C  CG  A LEU   A 123 ? 0.1476 0.1451 0.1372 -0.0106 0.0228  0.0228  123  LEU   A CG  
2659 C  CG  B LEU   A 123 ? 0.1410 0.1658 0.1380 -0.0113 0.0043  0.0175  123  LEU   A CG  
2660 C  CD1 A LEU   A 123 ? 0.1504 0.1460 0.1363 -0.0052 0.0201  0.0182  123  LEU   A CD1 
2661 C  CD1 B LEU   A 123 ? 0.1471 0.1687 0.1581 -0.0007 0.0015  0.0136  123  LEU   A CD1 
2662 C  CD2 A LEU   A 123 ? 0.1513 0.1501 0.1487 -0.0070 0.0182  0.0185  123  LEU   A CD2 
2663 C  CD2 B LEU   A 123 ? 0.1494 0.1741 0.1521 -0.0068 0.0001  0.0070  123  LEU   A CD2 
2686 N  N   A ALA   A 124 ? 0.1286 0.1257 0.1290 -0.0196 0.0094  0.0302  124  ALA   A N   
2687 N  N   B ALA   A 124 ? 0.1240 0.1324 0.1094 -0.0083 0.0057  0.0140  124  ALA   A N   
2688 C  CA  A ALA   A 124 ? 0.1251 0.1286 0.1457 -0.0235 0.0003  0.0275  124  ALA   A CA  
2689 C  CA  B ALA   A 124 ? 0.1123 0.1277 0.1094 -0.0068 0.0082  0.0168  124  ALA   A CA  
2690 C  C   A ALA   A 124 ? 0.1143 0.1219 0.1460 -0.0196 -0.0038 0.0179  124  ALA   A C   
2691 C  C   B ALA   A 124 ? 0.1122 0.1133 0.1260 -0.0075 0.0165  0.0146  124  ALA   A C   
2692 O  O   A ALA   A 124 ? 0.1092 0.1173 0.1562 -0.0155 -0.0038 0.0161  124  ALA   A O   
2693 O  O   B ALA   A 124 ? 0.1144 0.1217 0.1353 -0.0060 0.0252  0.0166  124  ALA   A O   
2694 C  CB  A ALA   A 124 ? 0.1327 0.1264 0.1545 -0.0271 -0.0006 0.0331  124  ALA   A CB  
2695 C  CB  B ALA   A 124 ? 0.1097 0.1229 0.1231 -0.0007 0.0045  0.0240  124  ALA   A CB  
2706 N  N   A PRO   A 125 ? 0.1058 0.1278 0.1318 -0.0077 -0.0070 0.0139  125  PRO   A N   
2707 N  N   B PRO   A 125 ? 0.1142 0.1151 0.1278 -0.0044 0.0121  0.0348  125  PRO   A N   
2708 C  CA  A PRO   A 125 ? 0.1044 0.1316 0.1230 -0.0067 -0.0043 0.0085  125  PRO   A CA  
2709 C  CA  B PRO   A 125 ? 0.1279 0.1197 0.1438 -0.0082 0.0053  0.0230  125  PRO   A CA  
2710 C  C   A PRO   A 125 ? 0.0963 0.1375 0.1172 -0.0070 -0.0082 0.0038  125  PRO   A C   
2711 C  C   B PRO   A 125 ? 0.1275 0.1296 0.1400 -0.0117 0.0027  0.0223  125  PRO   A C   
2712 O  O   A PRO   A 125 ? 0.0952 0.1368 0.1310 -0.0024 -0.0129 -0.0035 125  PRO   A O   
2713 O  O   B PRO   A 125 ? 0.1313 0.1234 0.1509 -0.0067 0.0092  0.0178  125  PRO   A O   
2714 C  CB  A PRO   A 125 ? 0.1127 0.1294 0.1203 -0.0088 -0.0046 0.0099  125  PRO   A CB  
2715 C  CB  B PRO   A 125 ? 0.1383 0.1178 0.1417 -0.0135 0.0091  0.0274  125  PRO   A CB  
2716 C  CG  A PRO   A 125 ? 0.1141 0.1308 0.1349 -0.0116 -0.0042 0.0118  125  PRO   A CG  
2717 C  CG  B PRO   A 125 ? 0.1372 0.1247 0.1616 -0.0163 0.0090  0.0277  125  PRO   A CG  
2718 C  CD  A PRO   A 125 ? 0.1083 0.1318 0.1346 -0.0109 -0.0055 0.0140  125  PRO   A CD  
2719 C  CD  B PRO   A 125 ? 0.1232 0.1291 0.1475 -0.0124 0.0112  0.0332  125  PRO   A CD  
2734 N  N   A LEU   A 126 ? 0.0962 0.1441 0.1141 -0.0059 -0.0023 -0.0002 126  LEU   A N   
2735 N  N   B LEU   A 126 ? 0.1346 0.1486 0.1473 -0.0103 -0.0012 0.0181  126  LEU   A N   
2736 C  CA  A LEU   A 126 ? 0.1003 0.1428 0.1201 -0.0066 -0.0017 0.0029  126  LEU   A CA  
2737 C  CA  B LEU   A 126 ? 0.1468 0.1494 0.1725 -0.0166 -0.0086 0.0201  126  LEU   A CA  
2738 C  C   A LEU   A 126 ? 0.0957 0.1338 0.1095 -0.0020 -0.0021 -0.0001 126  LEU   A C   
2739 C  C   B LEU   A 126 ? 0.1646 0.1481 0.2048 -0.0080 0.0046  0.0229  126  LEU   A C   
2740 O  O   A LEU   A 126 ? 0.0854 0.1262 0.1069 -0.0049 -0.0050 0.0012  126  LEU   A O   
2741 O  O   B LEU   A 126 ? 0.1932 0.1483 0.2477 -0.0082 0.0276  0.0187  126  LEU   A O   
2742 C  CB  A LEU   A 126 ? 0.1159 0.1578 0.1349 -0.0126 0.0019  0.0024  126  LEU   A CB  
2743 C  CB  B LEU   A 126 ? 0.1595 0.1684 0.1818 -0.0209 -0.0152 0.0233  126  LEU   A CB  
2744 C  CG  A LEU   A 126 ? 0.1176 0.1708 0.1481 -0.0100 -0.0002 0.0080  126  LEU   A CG  
2745 C  CG  B LEU   A 126 ? 0.1549 0.1799 0.2089 -0.0169 -0.0124 0.0337  126  LEU   A CG  
2746 C  CD1 A LEU   A 126 ? 0.1181 0.1721 0.1584 -0.0125 -0.0025 0.0240  126  LEU   A CD1 
2747 C  CD1 B LEU   A 126 ? 0.1538 0.1793 0.2374 -0.0156 -0.0184 0.0272  126  LEU   A CD1 
2748 C  CD2 A LEU   A 126 ? 0.1257 0.1739 0.1567 -0.0140 -0.0002 0.0096  126  LEU   A CD2 
2749 C  CD2 B LEU   A 126 ? 0.1533 0.1839 0.2200 -0.0285 -0.0023 0.0484  126  LEU   A CD2 
2772 N  N   A LEU   A 127 ? 0.0965 0.1332 0.1079 -0.0029 -0.0001 0.0029  127  LEU   A N   
2773 N  N   B LEU   A 127 ? 0.1482 0.1491 0.1726 -0.0058 -0.0007 0.0318  127  LEU   A N   
2774 C  CA  A LEU   A 127 ? 0.1090 0.1347 0.1080 -0.0015 0.0048  0.0047  127  LEU   A CA  
2775 C  CA  B LEU   A 127 ? 0.1443 0.1579 0.1654 -0.0043 -0.0063 0.0351  127  LEU   A CA  
2776 C  C   A LEU   A 127 ? 0.1126 0.1319 0.0927 0.0041  0.0093  0.0097  127  LEU   A C   
2777 C  C   B LEU   A 127 ? 0.1446 0.1422 0.1715 -0.0076 -0.0164 0.0202  127  LEU   A C   
2778 O  O   A LEU   A 127 ? 0.1188 0.1345 0.1050 0.0047  0.0138  0.0080  127  LEU   A O   
2779 O  O   B LEU   A 127 ? 0.1506 0.1384 0.1716 -0.0155 -0.0222 0.0163  127  LEU   A O   
2780 C  CB  A LEU   A 127 ? 0.1160 0.1280 0.1089 0.0018  0.0052  0.0110  127  LEU   A CB  
2781 C  CB  B LEU   A 127 ? 0.1399 0.1808 0.1797 -0.0034 -0.0061 0.0321  127  LEU   A CB  
2782 C  CG  A LEU   A 127 ? 0.1209 0.1125 0.1071 0.0018  -0.0005 0.0153  127  LEU   A CG  
2783 C  CG  B LEU   A 127 ? 0.1465 0.2036 0.1860 0.0019  -0.0103 0.0366  127  LEU   A CG  
2784 C  CD1 A LEU   A 127 ? 0.1189 0.1086 0.1187 -0.0041 -0.0024 0.0097  127  LEU   A CD1 
2785 C  CD1 B LEU   A 127 ? 0.1469 0.2161 0.1898 0.0099  0.0023  0.0424  127  LEU   A CD1 
2786 C  CD2 A LEU   A 127 ? 0.1257 0.0999 0.1138 0.0097  -0.0097 0.0270  127  LEU   A CD2 
2787 C  CD2 B LEU   A 127 ? 0.1582 0.2161 0.2019 -0.0000 -0.0220 0.0180  127  LEU   A CD2 
2810 N  N   A SER   A 128 ? 0.1179 0.1277 0.0926 0.0017  0.0079  0.0159  128  SER   A N   
2811 N  N   B SER   A 128 ? 0.1524 0.1350 0.1804 -0.0109 -0.0193 0.0221  128  SER   A N   
2812 C  CA  A SER   A 128 ? 0.1251 0.1301 0.0942 0.0004  0.0062  0.0189  128  SER   A CA  
2813 C  CA  B SER   A 128 ? 0.1537 0.1446 0.1795 -0.0079 -0.0232 0.0274  128  SER   A CA  
2814 C  C   A SER   A 128 ? 0.1286 0.1353 0.1125 0.0005  0.0060  0.0141  128  SER   A C   
2815 C  C   B SER   A 128 ? 0.1580 0.1490 0.1885 -0.0074 -0.0346 0.0291  128  SER   A C   
2816 O  O   A SER   A 128 ? 0.1316 0.1469 0.1198 0.0046  0.0132  0.0132  128  SER   A O   
2817 O  O   B SER   A 128 ? 0.1635 0.1687 0.1912 -0.0146 -0.0411 0.0388  128  SER   A O   
2818 C  CB  A SER   A 128 ? 0.1292 0.1264 0.0920 0.0013  -0.0058 0.0167  128  SER   A CB  
2819 C  CB  B SER   A 128 ? 0.1551 0.1560 0.1822 -0.0125 -0.0247 0.0287  128  SER   A CB  
2820 O  OG  A SER   A 128 ? 0.1248 0.1280 0.0984 0.0040  -0.0123 0.0056  128  SER   A OG  
2821 O  OG  B SER   A 128 ? 0.1488 0.1679 0.1736 -0.0099 -0.0165 0.0253  128  SER   A OG  
2832 N  N   A ALA   A 129 ? 0.1259 0.1353 0.1174 -0.0052 0.0018  0.0131  129  ALA   A N   
2833 N  N   B ALA   A 129 ? 0.1537 0.1456 0.2029 0.0021  -0.0290 0.0254  129  ALA   A N   
2834 C  CA  A ALA   A 129 ? 0.1191 0.1371 0.1067 -0.0032 -0.0014 0.0122  129  ALA   A CA  
2835 C  CA  B ALA   A 129 ? 0.1560 0.1490 0.2269 0.0023  -0.0223 0.0122  129  ALA   A CA  
2836 C  C   A ALA   A 129 ? 0.1257 0.1386 0.1075 0.0030  -0.0069 -0.0025 129  ALA   A C   
2837 C  C   B ALA   A 129 ? 0.1593 0.1568 0.2209 -0.0015 -0.0226 0.0112  129  ALA   A C   
2838 O  O   A ALA   A 129 ? 0.1286 0.1375 0.0970 0.0035  -0.0056 0.0030  129  ALA   A O   
2839 O  O   B ALA   A 129 ? 0.1607 0.1597 0.2088 -0.0023 -0.0232 0.0149  129  ALA   A O   
2840 C  CB  A ALA   A 129 ? 0.1132 0.1441 0.1086 0.0074  -0.0055 0.0150  129  ALA   A CB  
2841 C  CB  B ALA   A 129 ? 0.1594 0.1677 0.2635 -0.0026 -0.0038 0.0038  129  ALA   A CB  
2852 N  N   A GLY   A 130 ? 0.1311 0.1383 0.1289 0.0035  0.0030  -0.0104 130  GLY   A N   
2853 N  N   B GLY   A 130 ? 0.1644 0.1600 0.2323 -0.0076 -0.0099 0.0056  130  GLY   A N   
2854 C  CA  A GLY   A 130 ? 0.1472 0.1405 0.1539 0.0025  -0.0021 -0.0100 130  GLY   A CA  
2855 C  CA  B GLY   A 130 ? 0.1697 0.1624 0.2456 -0.0060 0.0012  0.0086  130  GLY   A CA  
2856 C  C   A GLY   A 130 ? 0.1531 0.1428 0.1541 -0.0033 -0.0086 0.0022  130  GLY   A C   
2857 C  C   B GLY   A 130 ? 0.1681 0.1556 0.2445 -0.0040 -0.0123 0.0235  130  GLY   A C   
2858 O  O   A GLY   A 130 ? 0.1445 0.1410 0.1512 -0.0123 -0.0153 0.0105  130  GLY   A O   
2859 O  O   B GLY   A 130 ? 0.1713 0.1562 0.2447 -0.0005 -0.0366 0.0320  130  GLY   A O   
2866 N  N   A ILE   A 131 ? 0.1616 0.1431 0.1656 -0.0074 -0.0171 0.0060  131  ILE   A N   
2867 N  N   B ILE   A 131 ? 0.1665 0.1442 0.2507 -0.0030 -0.0000 0.0278  131  ILE   A N   
2868 C  CA  A ILE   A 131 ? 0.1695 0.1425 0.1510 -0.0086 -0.0274 0.0010  131  ILE   A CA  
2869 C  CA  B ILE   A 131 ? 0.1663 0.1434 0.2313 0.0017  -0.0161 0.0384  131  ILE   A CA  
2870 C  C   A ILE   A 131 ? 0.1718 0.1463 0.1452 -0.0127 -0.0270 -0.0034 131  ILE   A C   
2871 C  C   B ILE   A 131 ? 0.1711 0.1541 0.2185 0.0071  -0.0148 0.0452  131  ILE   A C   
2872 O  O   A ILE   A 131 ? 0.1767 0.1489 0.1467 -0.0125 -0.0315 -0.0084 131  ILE   A O   
2873 O  O   B ILE   A 131 ? 0.1860 0.1733 0.2210 0.0110  -0.0081 0.0509  131  ILE   A O   
2874 C  CB  A ILE   A 131 ? 0.1728 0.1470 0.1721 -0.0020 -0.0311 -0.0120 131  ILE   A CB  
2875 C  CB  B ILE   A 131 ? 0.1747 0.1579 0.2500 0.0012  -0.0276 0.0251  131  ILE   A CB  
2876 C  CG1 A ILE   A 131 ? 0.1810 0.1672 0.1881 -0.0007 -0.0423 -0.0133 131  ILE   A CG1 
2877 C  CG1 B ILE   A 131 ? 0.1768 0.1764 0.2677 -0.0104 -0.0218 0.0228  131  ILE   A CG1 
2878 C  CG2 A ILE   A 131 ? 0.1676 0.1384 0.1781 -0.0010 -0.0286 -0.0231 131  ILE   A CG2 
2879 C  CG2 B ILE   A 131 ? 0.1833 0.1581 0.2603 0.0101  -0.0248 0.0113  131  ILE   A CG2 
2880 C  CD1 A ILE   A 131 ? 0.1854 0.1773 0.2087 -0.0029 -0.0413 -0.0141 131  ILE   A CD1 
2881 C  CD1 B ILE   A 131 ? 0.1825 0.1890 0.2998 -0.0189 -0.0196 0.0092  131  ILE   A CD1 
2904 N  N   A PHE   A 132 ? 0.1693 0.1492 0.1413 -0.0106 -0.0189 -0.0055 132  PHE   A N   
2905 N  N   B PHE   A 132 ? 0.1649 0.1499 0.2069 0.0162  -0.0300 0.0354  132  PHE   A N   
2906 C  CA  A PHE   A 132 ? 0.1701 0.1579 0.1327 -0.0072 -0.0063 -0.0137 132  PHE   A CA  
2907 C  CA  B PHE   A 132 ? 0.1686 0.1646 0.2157 0.0116  -0.0311 0.0172  132  PHE   A CA  
2908 C  C   A PHE   A 132 ? 0.1676 0.1645 0.1227 -0.0058 -0.0113 -0.0097 132  PHE   A C   
2909 C  C   B PHE   A 132 ? 0.1790 0.1819 0.2202 0.0203  -0.0376 0.0186  132  PHE   A C   
2910 O  O   A PHE   A 132 ? 0.1687 0.1725 0.1250 -0.0080 -0.0060 -0.0035 132  PHE   A O   
2911 O  O   B PHE   A 132 ? 0.1986 0.2077 0.2356 0.0161  -0.0267 0.0033  132  PHE   A O   
2912 C  CB  A PHE   A 132 ? 0.1692 0.1618 0.1353 -0.0035 -0.0058 -0.0091 132  PHE   A CB  
2913 C  CB  B PHE   A 132 ? 0.1638 0.1573 0.1844 0.0104  -0.0321 0.0281  132  PHE   A CB  
2914 C  CG  A PHE   A 132 ? 0.1624 0.1633 0.1196 -0.0014 -0.0019 -0.0067 132  PHE   A CG  
2915 C  CG  B PHE   A 132 ? 0.1687 0.1556 0.1749 0.0144  -0.0360 0.0239  132  PHE   A CG  
2916 C  CD1 A PHE   A 132 ? 0.1617 0.1670 0.1133 0.0024  -0.0019 -0.0077 132  PHE   A CD1 
2917 C  CD1 B PHE   A 132 ? 0.1738 0.1670 0.1907 0.0145  -0.0292 0.0163  132  PHE   A CD1 
2918 C  CD2 A PHE   A 132 ? 0.1570 0.1681 0.1170 -0.0014 -0.0028 -0.0028 132  PHE   A CD2 
2919 C  CD2 B PHE   A 132 ? 0.1719 0.1693 0.1903 0.0148  -0.0388 0.0231  132  PHE   A CD2 
2920 C  CE1 A PHE   A 132 ? 0.1520 0.1679 0.1011 0.0027  0.0033  -0.0061 132  PHE   A CE1 
2921 C  CE1 B PHE   A 132 ? 0.1793 0.1738 0.1983 0.0107  -0.0462 0.0202  132  PHE   A CE1 
2922 C  CE2 A PHE   A 132 ? 0.1510 0.1702 0.1084 0.0031  -0.0004 -0.0007 132  PHE   A CE2 
2923 C  CE2 B PHE   A 132 ? 0.1744 0.1807 0.2108 0.0109  -0.0431 0.0219  132  PHE   A CE2 
2924 C  CZ  A PHE   A 132 ? 0.1488 0.1680 0.0947 0.0034  0.0005  -0.0011 132  PHE   A CZ  
2925 C  CZ  B PHE   A 132 ? 0.1780 0.1786 0.2131 0.0100  -0.0536 0.0274  132  PHE   A CZ  
2944 N  N   A GLY   A 133 ? 0.1673 0.1690 0.1248 -0.0028 -0.0243 -0.0075 133  GLY   A N   
2945 N  N   B GLY   A 133 ? 0.1806 0.1820 0.2117 0.0188  -0.0431 0.0296  133  GLY   A N   
2946 C  CA  A GLY   A 133 ? 0.1708 0.1806 0.1454 -0.0035 -0.0327 -0.0120 133  GLY   A CA  
2947 C  CA  B GLY   A 133 ? 0.1889 0.1968 0.2176 0.0114  -0.0511 0.0104  133  GLY   A CA  
2948 C  C   A GLY   A 133 ? 0.1728 0.1906 0.1664 -0.0044 -0.0396 -0.0124 133  GLY   A C   
2949 C  C   B GLY   A 133 ? 0.1917 0.2051 0.2118 0.0050  -0.0686 0.0016  133  GLY   A C   
2950 O  O   A GLY   A 133 ? 0.1758 0.1988 0.1782 -0.0003 -0.0386 -0.0234 133  GLY   A O   
2951 O  O   B GLY   A 133 ? 0.2001 0.2245 0.2203 -0.0021 -0.0716 -0.0061 133  GLY   A O   
2958 N  N   A ALA   A 134 ? 0.1714 0.1880 0.1742 -0.0108 -0.0332 -0.0022 134  ALA   A N   
2959 N  N   B ALA   A 134 ? 0.1872 0.1839 0.2053 0.0048  -0.0526 0.0026  134  ALA   A N   
2960 C  CA  A ALA   A 134 ? 0.1717 0.1930 0.1865 -0.0122 -0.0314 -0.0001 134  ALA   A CA  
2961 C  CA  B ALA   A 134 ? 0.1906 0.1810 0.2149 -0.0032 -0.0529 0.0049  134  ALA   A CA  
2962 C  C   A ALA   A 134 ? 0.1742 0.2021 0.1960 -0.0152 -0.0314 0.0057  134  ALA   A C   
2963 C  C   B ALA   A 134 ? 0.1926 0.1921 0.2193 -0.0121 -0.0541 0.0306  134  ALA   A C   
2964 O  O   A ALA   A 134 ? 0.1747 0.2063 0.2056 -0.0121 -0.0151 0.0084  134  ALA   A O   
2965 O  O   B ALA   A 134 ? 0.1946 0.1937 0.2343 -0.0142 -0.0375 0.0468  134  ALA   A O   
2966 C  CB  A ALA   A 134 ? 0.1732 0.1929 0.1899 -0.0082 -0.0291 -0.0006 134  ALA   A CB  
2967 C  CB  B ALA   A 134 ? 0.1980 0.1761 0.2364 -0.0034 -0.0496 -0.0102 134  ALA   A CB  
2978 N  N   A ASP   A 135 ? 0.1791 0.2078 0.1980 -0.0178 -0.0373 0.0155  135  ASP   A N   
2979 N  N   B ASP   A 135 ? 0.1996 0.2024 0.2357 -0.0196 -0.0622 0.0433  135  ASP   A N   
2980 C  CA  A ASP   A 135 ? 0.1801 0.2125 0.2066 -0.0186 -0.0471 0.0282  135  ASP   A CA  
2981 C  CA  B ASP   A 135 ? 0.1989 0.2134 0.2685 -0.0287 -0.0741 0.0483  135  ASP   A CA  
2982 C  C   A ASP   A 135 ? 0.1766 0.2111 0.2153 -0.0119 -0.0369 0.0366  135  ASP   A C   
2983 C  C   B ASP   A 135 ? 0.1839 0.2013 0.2661 -0.0241 -0.0645 0.0599  135  ASP   A C   
2984 O  O   A ASP   A 135 ? 0.1729 0.2092 0.2150 -0.0103 -0.0377 0.0368  135  ASP   A O   
2985 O  O   B ASP   A 135 ? 0.1797 0.1900 0.2615 -0.0319 -0.0644 0.0584  135  ASP   A O   
2986 C  CB  A ASP   A 135 ? 0.1860 0.2177 0.2124 -0.0222 -0.0626 0.0313  135  ASP   A CB  
2987 C  CB  B ASP   A 135 ? 0.2167 0.2380 0.3015 -0.0388 -0.0866 0.0437  135  ASP   A CB  
2988 C  CG  A ASP   A 135 ? 0.1921 0.2213 0.2295 -0.0277 -0.0632 0.0306  135  ASP   A CG  
2989 C  CG  B ASP   A 135 ? 0.2344 0.2684 0.3445 -0.0462 -0.0854 0.0366  135  ASP   A CG  
2990 O  OD1 A ASP   A 135 ? 0.1883 0.2232 0.2335 -0.0370 -0.0787 0.0361  135  ASP   A OD1 
2991 O  OD1 B ASP   A 135 ? 0.2409 0.2775 0.3742 -0.0469 -0.0738 0.0438  135  ASP   A OD1 
2992 O  OD2 A ASP   A 135 ? 0.2076 0.2254 0.2542 -0.0215 -0.0297 0.0297  135  ASP   A OD2 
2993 O  OD2 B ASP   A 135 ? 0.2464 0.2860 0.3673 -0.0479 -0.0864 0.0313  135  ASP   A OD2 
3002 N  N   A PRO   A 136 ? 0.1754 0.2103 0.2255 -0.0064 -0.0225 0.0458  136  PRO   A N   
3003 N  N   B PRO   A 136 ? 0.1690 0.1940 0.2754 -0.0145 -0.0494 0.0779  136  PRO   A N   
3004 C  CA  A PRO   A 136 ? 0.1703 0.2050 0.2255 -0.0042 -0.0104 0.0433  136  PRO   A CA  
3005 C  CA  B PRO   A 136 ? 0.1565 0.1936 0.2805 -0.0080 -0.0310 0.0710  136  PRO   A CA  
3006 C  C   A PRO   A 136 ? 0.1585 0.1981 0.2187 -0.0053 -0.0067 0.0424  136  PRO   A C   
3007 C  C   B PRO   A 136 ? 0.1319 0.1917 0.2814 -0.0100 -0.0289 0.0566  136  PRO   A C   
3008 O  O   A PRO   A 136 ? 0.1526 0.1949 0.2083 -0.0060 0.0009  0.0456  136  PRO   A O   
3009 O  O   B PRO   A 136 ? 0.1261 0.1865 0.2589 -0.0045 -0.0158 0.0571  136  PRO   A O   
3010 C  CB  A PRO   A 136 ? 0.1799 0.2078 0.2353 -0.0044 -0.0095 0.0396  136  PRO   A CB  
3011 C  CB  B PRO   A 136 ? 0.1791 0.1933 0.2975 -0.0069 -0.0276 0.0676  136  PRO   A CB  
3012 C  CG  A PRO   A 136 ? 0.1836 0.2130 0.2433 -0.0056 -0.0163 0.0412  136  PRO   A CG  
3013 C  CG  B PRO   A 136 ? 0.1900 0.1993 0.3117 -0.0063 -0.0398 0.0686  136  PRO   A CG  
3014 C  CD  A PRO   A 136 ? 0.1807 0.2123 0.2347 -0.0041 -0.0206 0.0501  136  PRO   A CD  
3015 C  CD  B PRO   A 136 ? 0.1783 0.1916 0.2955 -0.0093 -0.0475 0.0871  136  PRO   A CD  
3030 N  N   A ILE   A 137 ? 0.1586 0.1987 0.2192 -0.0046 -0.0172 0.0431  137  ILE   A N   
3031 N  N   B ILE   A 137 ? 0.1330 0.1993 0.2888 -0.0159 -0.0433 0.0455  137  ILE   A N   
3032 C  CA  A ILE   A 137 ? 0.1553 0.2005 0.2138 -0.0068 -0.0245 0.0458  137  ILE   A CA  
3033 C  CA  B ILE   A 137 ? 0.1353 0.2144 0.2732 -0.0254 -0.0426 0.0362  137  ILE   A CA  
3034 C  C   A ILE   A 137 ? 0.1584 0.1952 0.2004 -0.0078 -0.0205 0.0461  137  ILE   A C   
3035 C  C   B ILE   A 137 ? 0.1370 0.2123 0.2528 -0.0305 -0.0341 0.0372  137  ILE   A C   
3036 O  O   A ILE   A 137 ? 0.1587 0.1873 0.1891 -0.0057 -0.0149 0.0441  137  ILE   A O   
3037 O  O   B ILE   A 137 ? 0.1315 0.2050 0.2516 -0.0364 -0.0230 0.0306  137  ILE   A O   
3038 C  CB  A ILE   A 137 ? 0.1543 0.2120 0.2317 -0.0090 -0.0395 0.0488  137  ILE   A CB  
3039 C  CB  B ILE   A 137 ? 0.1542 0.2386 0.3039 -0.0288 -0.0558 0.0308  137  ILE   A CB  
3040 C  CG1 A ILE   A 137 ? 0.1595 0.2188 0.2505 -0.0103 -0.0363 0.0555  137  ILE   A CG1 
3041 C  CG1 B ILE   A 137 ? 0.1821 0.2607 0.3204 -0.0109 -0.0573 0.0439  137  ILE   A CG1 
3042 C  CG2 A ILE   A 137 ? 0.1563 0.2159 0.2404 -0.0061 -0.0495 0.0450  137  ILE   A CG2 
3043 C  CG2 B ILE   A 137 ? 0.1660 0.2402 0.3178 -0.0317 -0.0622 0.0259  137  ILE   A CG2 
3044 C  CD1 A ILE   A 137 ? 0.1662 0.2217 0.2596 -0.0090 -0.0322 0.0620  137  ILE   A CD1 
3045 C  CD1 B ILE   A 137 ? 0.2028 0.2743 0.3422 -0.0033 -0.0429 0.0484  137  ILE   A CD1 
3068 N  N   A HIS   A 138 ? 0.1576 0.2019 0.1964 -0.0093 -0.0154 0.0395  138  HIS   A N   
3069 N  N   B HIS   A 138 ? 0.1398 0.2257 0.2275 -0.0265 -0.0259 0.0316  138  HIS   A N   
3070 C  CA  A HIS   A 138 ? 0.1574 0.2062 0.1942 -0.0103 -0.0174 0.0320  138  HIS   A CA  
3071 C  CA  B HIS   A 138 ? 0.1480 0.2293 0.2083 -0.0223 -0.0287 0.0303  138  HIS   A CA  
3072 C  C   A HIS   A 138 ? 0.1457 0.1980 0.1882 -0.0098 -0.0169 0.0328  138  HIS   A C   
3073 C  C   B HIS   A 138 ? 0.1403 0.2078 0.1917 -0.0182 -0.0199 0.0333  138  HIS   A C   
3074 O  O   A HIS   A 138 ? 0.1503 0.1973 0.1907 -0.0085 -0.0142 0.0262  138  HIS   A O   
3075 O  O   B HIS   A 138 ? 0.1501 0.2052 0.1982 -0.0191 -0.0066 0.0254  138  HIS   A O   
3076 C  CB  A HIS   A 138 ? 0.1690 0.2156 0.1999 -0.0129 -0.0208 0.0255  138  HIS   A CB  
3077 C  CB  B HIS   A 138 ? 0.1675 0.2477 0.2066 -0.0249 -0.0397 0.0269  138  HIS   A CB  
3078 C  CG  A HIS   A 138 ? 0.1801 0.2218 0.2052 -0.0150 -0.0166 0.0213  138  HIS   A CG  
3079 C  CG  B HIS   A 138 ? 0.1879 0.2606 0.2088 -0.0269 -0.0297 0.0268  138  HIS   A CG  
3080 N  ND1 A HIS   A 138 ? 0.1863 0.2256 0.2155 -0.0161 -0.0123 0.0128  138  HIS   A ND1 
3081 N  ND1 B HIS   A 138 ? 0.1989 0.2685 0.2255 -0.0281 -0.0226 0.0139  138  HIS   A ND1 
3082 C  CD2 A HIS   A 138 ? 0.1837 0.2266 0.2023 -0.0151 -0.0165 0.0242  138  HIS   A CD2 
3083 C  CD2 B HIS   A 138 ? 0.1943 0.2697 0.1993 -0.0259 -0.0288 0.0342  138  HIS   A CD2 
3084 C  CE1 A HIS   A 138 ? 0.1887 0.2293 0.2132 -0.0166 -0.0113 0.0124  138  HIS   A CE1 
3085 C  CE1 B HIS   A 138 ? 0.2038 0.2753 0.2197 -0.0272 -0.0190 0.0152  138  HIS   A CE1 
3086 N  NE2 A HIS   A 138 ? 0.1866 0.2297 0.2082 -0.0157 -0.0148 0.0189  138  HIS   A NE2 
3087 N  NE2 B HIS   A 138 ? 0.1994 0.2752 0.2069 -0.0260 -0.0242 0.0267  138  HIS   A NE2 
3102 N  N   . SER   A 139 ? 0.1338 0.1921 0.1844 -0.0103 -0.0127 0.0378  139  SER   A N   
3103 C  CA  . SER   A 139 ? 0.1244 0.1848 0.1809 -0.0125 -0.0112 0.0424  139  SER   A CA  
3104 C  C   . SER   A 139 ? 0.1197 0.1666 0.1930 -0.0116 -0.0072 0.0321  139  SER   A C   
3105 O  O   . SER   A 139 ? 0.1207 0.1550 0.2015 -0.0119 -0.0086 0.0346  139  SER   A O   
3106 C  CB  . SER   A 139 ? 0.1329 0.1785 0.1932 -0.0170 -0.0126 0.0476  139  SER   A CB  
3107 O  OG  . SER   A 139 ? 0.1336 0.1717 0.2062 -0.0197 -0.0215 0.0516  139  SER   A OG  
3114 N  N   A LEU   A 140 ? 0.1215 0.1682 0.1782 -0.0090 -0.0078 0.0242  140  LEU   A N   
3115 N  N   B LEU   A 140 ? 0.1192 0.1709 0.1861 -0.0076 -0.0093 0.0327  140  LEU   A N   
3116 C  CA  A LEU   A 140 ? 0.1228 0.1638 0.1694 -0.0101 -0.0087 0.0186  140  LEU   A CA  
3117 C  CA  B LEU   A 140 ? 0.1180 0.1601 0.1776 -0.0111 -0.0057 0.0427  140  LEU   A CA  
3118 C  C   A LEU   A 140 ? 0.1208 0.1629 0.1665 -0.0160 -0.0087 0.0090  140  LEU   A C   
3119 C  C   B LEU   A 140 ? 0.1145 0.1631 0.1685 -0.0167 0.0037  0.0373  140  LEU   A C   
3120 O  O   A LEU   A 140 ? 0.1203 0.1623 0.1738 -0.0146 -0.0092 0.0055  140  LEU   A O   
3121 O  O   B LEU   A 140 ? 0.1207 0.1606 0.1910 -0.0094 0.0001  0.0337  140  LEU   A O   
3122 C  CB  A LEU   A 140 ? 0.1261 0.1677 0.1731 -0.0087 -0.0063 0.0140  140  LEU   A CB  
3123 C  CB  B LEU   A 140 ? 0.1202 0.1653 0.1933 -0.0150 -0.0020 0.0374  140  LEU   A CB  
3124 C  CG  A LEU   A 140 ? 0.1310 0.1709 0.1783 -0.0102 0.0001  0.0066  140  LEU   A CG  
3125 C  CG  B LEU   A 140 ? 0.1250 0.1677 0.2065 -0.0255 0.0083  0.0353  140  LEU   A CG  
3126 C  CD1 A LEU   A 140 ? 0.1338 0.1700 0.1862 -0.0070 -0.0021 0.0024  140  LEU   A CD1 
3127 C  CD1 B LEU   A 140 ? 0.1274 0.1655 0.2181 -0.0231 0.0102  0.0357  140  LEU   A CD1 
3128 C  CD2 A LEU   A 140 ? 0.1365 0.1779 0.1860 -0.0091 0.0044  0.0067  140  LEU   A CD2 
3129 C  CD2 B LEU   A 140 ? 0.1357 0.1817 0.2209 -0.0204 0.0121  0.0356  140  LEU   A CD2 
3152 N  N   A ARG   A 141 ? 0.1248 0.1656 0.1699 -0.0201 -0.0127 0.0032  141  ARG   A N   
3153 N  N   B ARG   A 141 ? 0.1195 0.1766 0.1782 -0.0162 -0.0016 0.0272  141  ARG   A N   
3154 C  CA  A ARG   A 141 ? 0.1337 0.1688 0.1763 -0.0270 -0.0199 -0.0058 141  ARG   A CA  
3155 C  CA  B ARG   A 141 ? 0.1379 0.1881 0.1903 -0.0269 -0.0047 0.0193  141  ARG   A CA  
3156 C  C   A ARG   A 141 ? 0.1276 0.1596 0.1745 -0.0188 -0.0150 -0.0001 141  ARG   A C   
3157 C  C   B ARG   A 141 ? 0.1357 0.1704 0.1800 -0.0239 -0.0042 0.0201  141  ARG   A C   
3158 O  O   A ARG   A 141 ? 0.1229 0.1556 0.1758 -0.0134 -0.0133 0.0028  141  ARG   A O   
3159 O  O   B ARG   A 141 ? 0.1359 0.1629 0.1892 -0.0244 0.0060  0.0115  141  ARG   A O   
3160 C  CB  A ARG   A 141 ? 0.1452 0.1784 0.1890 -0.0338 -0.0180 -0.0127 141  ARG   A CB  
3161 C  CB  B ARG   A 141 ? 0.1508 0.2128 0.2028 -0.0292 0.0089  0.0174  141  ARG   A CB  
3162 C  CG  A ARG   A 141 ? 0.1586 0.1919 0.2015 -0.0371 -0.0156 -0.0136 141  ARG   A CG  
3163 C  CG  B ARG   A 141 ? 0.1682 0.2277 0.2282 -0.0239 0.0164  0.0167  141  ARG   A CG  
3164 C  CD  A ARG   A 141 ? 0.1629 0.2021 0.1942 -0.0468 -0.0154 -0.0152 141  ARG   A CD  
3165 C  CD  B ARG   A 141 ? 0.1758 0.2295 0.2457 -0.0235 0.0099  0.0171  141  ARG   A CD  
3166 N  NE  A ARG   A 141 ? 0.1609 0.2115 0.1978 -0.0530 -0.0089 -0.0173 141  ARG   A NE  
3167 N  NE  B ARG   A 141 ? 0.1849 0.2432 0.2502 -0.0209 0.0105  0.0159  141  ARG   A NE  
3168 C  CZ  A ARG   A 141 ? 0.1555 0.2250 0.2041 -0.0612 -0.0069 -0.0183 141  ARG   A CZ  
3169 C  CZ  B ARG   A 141 ? 0.1907 0.2461 0.2570 -0.0291 0.0167  0.0238  141  ARG   A CZ  
3170 N  NH1 A ARG   A 141 ? 0.1601 0.2304 0.2174 -0.0569 -0.0114 -0.0121 141  ARG   A NH1 
3171 N  NH1 B ARG   A 141 ? 0.1975 0.2519 0.2585 -0.0335 0.0168  0.0170  141  ARG   A NH1 
3172 N  NH2 A ARG   A 141 ? 0.1514 0.2329 0.2055 -0.0615 -0.0021 -0.0211 141  ARG   A NH2 
3173 N  NH2 B ARG   A 141 ? 0.1952 0.2506 0.2640 -0.0236 0.0180  0.0329  141  ARG   A NH2 
3200 N  N   A VAL   A 142 ? 0.1217 0.1559 0.1762 -0.0150 -0.0100 0.0048  142  VAL   A N   
3201 N  N   B VAL   A 142 ? 0.1274 0.1645 0.1826 -0.0155 -0.0073 0.0228  142  VAL   A N   
3202 C  CA  A VAL   A 142 ? 0.1202 0.1517 0.1703 -0.0132 0.0008  0.0046  142  VAL   A CA  
3203 C  CA  B VAL   A 142 ? 0.1290 0.1578 0.1821 -0.0141 0.0072  0.0155  142  VAL   A CA  
3204 C  C   A VAL   A 142 ? 0.1168 0.1473 0.1721 -0.0126 0.0006  0.0084  142  VAL   A C   
3205 C  C   B VAL   A 142 ? 0.1175 0.1509 0.1842 -0.0150 0.0046  0.0129  142  VAL   A C   
3206 O  O   A VAL   A 142 ? 0.1211 0.1485 0.1674 -0.0082 -0.0003 0.0101  142  VAL   A O   
3207 O  O   B VAL   A 142 ? 0.1270 0.1551 0.1817 -0.0063 0.0002  0.0167  142  VAL   A O   
3208 C  CB  A VAL   A 142 ? 0.1223 0.1567 0.1622 -0.0123 0.0028  0.0075  142  VAL   A CB  
3209 C  CB  B VAL   A 142 ? 0.1426 0.1682 0.1722 -0.0129 0.0025  0.0271  142  VAL   A CB  
3210 C  CG1 A VAL   A 142 ? 0.1245 0.1523 0.1631 -0.0147 0.0073  0.0072  142  VAL   A CG1 
3211 C  CG1 B VAL   A 142 ? 0.1479 0.1618 0.1722 -0.0159 0.0035  0.0259  142  VAL   A CG1 
3212 C  CG2 A VAL   A 142 ? 0.1287 0.1649 0.1751 -0.0102 0.0006  0.0084  142  VAL   A CG2 
3213 C  CG2 B VAL   A 142 ? 0.1608 0.1835 0.2014 -0.0092 -0.0021 0.0257  142  VAL   A CG2 
3232 N  N   . CYS   A 143 ? 0.1183 0.1431 0.1736 -0.0100 0.0008  0.0115  143  CYS   A N   
3233 C  CA  . CYS   A 143 ? 0.1152 0.1444 0.1816 -0.0085 0.0053  0.0117  143  CYS   A CA  
3234 C  C   . CYS   A 143 ? 0.1207 0.1427 0.1777 -0.0075 0.0039  0.0157  143  CYS   A C   
3235 O  O   . CYS   A 143 ? 0.1198 0.1391 0.1750 -0.0066 0.0009  0.0219  143  CYS   A O   
3236 C  CB  . CYS   A 143 ? 0.1281 0.1509 0.1907 -0.0065 0.0057  0.0247  143  CYS   A CB  
3237 S  SG  . CYS   A 143 ? 0.1484 0.1522 0.1783 0.0046  0.0071  0.0120  143  CYS   A SG  
3244 N  N   . VAL   A 144 ? 0.1194 0.1403 0.1896 -0.0089 0.0094  0.0175  144  VAL   A N   
3245 C  CA  . VAL   A 144 ? 0.1242 0.1521 0.2157 -0.0135 0.0189  0.0138  144  VAL   A CA  
3246 C  C   . VAL   A 144 ? 0.1271 0.1401 0.2027 -0.0239 0.0006  0.0149  144  VAL   A C   
3247 O  O   . VAL   A 144 ? 0.1404 0.1465 0.2214 -0.0070 0.0053  0.0225  144  VAL   A O   
3248 C  CB  . VAL   A 144 ? 0.1453 0.1778 0.2738 -0.0071 0.0329  0.0107  144  VAL   A CB  
3249 C  CG1 . VAL   A 144 ? 0.1558 0.1964 0.3104 -0.0179 0.0211  0.0068  144  VAL   A CG1 
3250 C  CG2 . VAL   A 144 ? 0.1400 0.1808 0.2777 -0.0084 0.0349  0.0211  144  VAL   A CG2 
3260 N  N   . ASP   A 145 ? 0.1348 0.1387 0.2028 -0.0214 0.0080  0.0091  145  ASP   A N   
3261 C  CA  . ASP   A 145 ? 0.1450 0.1515 0.2111 -0.0227 0.0042  -0.0026 145  ASP   A CA  
3262 C  C   . ASP   A 145 ? 0.1354 0.1418 0.2173 -0.0200 0.0087  -0.0030 145  ASP   A C   
3263 O  O   . ASP   A 145 ? 0.1492 0.1497 0.2778 -0.0189 0.0087  -0.0350 145  ASP   A O   
3264 C  CB  . ASP   A 145 ? 0.1520 0.1814 0.2210 -0.0295 0.0037  -0.0127 145  ASP   A CB  
3265 C  CG  . ASP   A 145 ? 0.1656 0.2133 0.2461 -0.0468 -0.0065 -0.0123 145  ASP   A CG  
3266 O  OD1 . ASP   A 145 ? 0.1650 0.2252 0.2724 -0.0579 -0.0011 0.0012  145  ASP   A OD1 
3267 O  OD2 . ASP   A 145 ? 0.1909 0.2361 0.2706 -0.0497 -0.0286 -0.0087 145  ASP   A OD2 
3272 N  N   . THR   A 146 ? 0.1299 0.1286 0.1814 -0.0127 0.0150  0.0077  146  THR   A N   
3273 C  CA  . THR   A 146 ? 0.1218 0.1270 0.1741 -0.0084 0.0063  0.0118  146  THR   A CA  
3274 C  C   . THR   A 146 ? 0.1189 0.1233 0.1792 -0.0076 0.0097  0.0209  146  THR   A C   
3275 O  O   . THR   A 146 ? 0.1315 0.1411 0.1893 0.0015  -0.0001 0.0130  146  THR   A O   
3276 C  CB  . THR   A 146 ? 0.1247 0.1347 0.1708 -0.0052 0.0103  0.0139  146  THR   A CB  
3277 O  OG1 . THR   A 146 ? 0.1263 0.1514 0.1742 -0.0051 0.0051  0.0038  146  THR   A OG1 
3278 C  CG2 . THR   A 146 ? 0.1346 0.1329 0.1858 -0.0061 0.0055  0.0143  146  THR   A CG2 
3286 N  N   . VAL   A 147 ? 0.1211 0.1305 0.1702 -0.0056 0.0114  0.0211  147  VAL   A N   
3287 C  CA  . VAL   A 147 ? 0.1186 0.1305 0.1635 -0.0095 0.0197  0.0189  147  VAL   A CA  
3288 C  C   . VAL   A 147 ? 0.1243 0.1270 0.1864 -0.0119 0.0135  0.0206  147  VAL   A C   
3289 O  O   . VAL   A 147 ? 0.1283 0.1340 0.1966 -0.0134 0.0128  0.0242  147  VAL   A O   
3290 C  CB  . VAL   A 147 ? 0.1328 0.1324 0.1655 -0.0126 0.0082  0.0266  147  VAL   A CB  
3291 C  CG1 . VAL   A 147 ? 0.1566 0.1371 0.1813 -0.0106 0.0066  0.0391  147  VAL   A CG1 
3292 C  CG2 . VAL   A 147 ? 0.1352 0.1305 0.1604 -0.0121 0.0011  0.0180  147  VAL   A CG2 
3302 N  N   . ARG   A 148 ? 0.1253 0.1315 0.1826 -0.0093 0.0137  0.0365  148  ARG   A N   
3303 C  CA  . ARG   A 148 ? 0.1287 0.1320 0.1860 -0.0068 0.0121  0.0463  148  ARG   A CA  
3304 C  C   . ARG   A 148 ? 0.1446 0.1319 0.1794 -0.0068 0.0140  0.0498  148  ARG   A C   
3305 O  O   . ARG   A 148 ? 0.1740 0.1451 0.1921 -0.0142 0.0153  0.0421  148  ARG   A O   
3306 C  CB  . ARG   A 148 ? 0.1392 0.1330 0.2094 -0.0041 0.0196  0.0379  148  ARG   A CB  
3307 C  CG  . ARG   A 148 ? 0.1502 0.1380 0.2284 -0.0096 0.0361  0.0309  148  ARG   A CG  
3308 C  CD  . ARG   A 148 ? 0.1645 0.1378 0.2480 -0.0056 0.0389  0.0487  148  ARG   A CD  
3309 N  NE  . ARG   A 148 ? 0.1568 0.1401 0.2559 0.0031  0.0399  0.0459  148  ARG   A NE  
3310 C  CZ  . ARG   A 148 ? 0.1518 0.1318 0.2430 0.0069  0.0370  0.0318  148  ARG   A CZ  
3311 N  NH1 . ARG   A 148 ? 0.1611 0.1337 0.2452 -0.0078 0.0356  0.0116  148  ARG   A NH1 
3312 N  NH2 . ARG   A 148 ? 0.1492 0.1494 0.2382 0.0149  0.0395  0.0384  148  ARG   A NH2 
3326 N  N   . THR   A 149 ? 0.1377 0.1395 0.1783 -0.0137 0.0055  0.0475  149  THR   A N   
3327 C  CA  . THR   A 149 ? 0.1383 0.1498 0.1754 -0.0079 0.0039  0.0453  149  THR   A CA  
3328 C  C   . THR   A 149 ? 0.1329 0.1436 0.1613 -0.0164 0.0056  0.0432  149  THR   A C   
3329 O  O   . THR   A 149 ? 0.1342 0.1487 0.1875 -0.0193 0.0049  0.0375  149  THR   A O   
3330 C  CB  . THR   A 149 ? 0.1389 0.1560 0.1754 -0.0120 0.0062  0.0356  149  THR   A CB  
3331 O  OG1 . THR   A 149 ? 0.1444 0.1474 0.1910 -0.0228 0.0056  0.0273  149  THR   A OG1 
3332 C  CG2 . THR   A 149 ? 0.1414 0.1701 0.1999 -0.0044 0.0052  0.0313  149  THR   A CG2 
3340 N  N   . ASN   A 150 ? 0.1360 0.1418 0.1756 -0.0065 -0.0002 0.0424  150  ASN   A N   
3341 C  CA  . ASN   A 150 ? 0.1481 0.1513 0.1782 -0.0101 0.0135  0.0396  150  ASN   A CA  
3342 C  C   . ASN   A 150 ? 0.1329 0.1426 0.1755 -0.0125 0.0031  0.0382  150  ASN   A C   
3343 O  O   . ASN   A 150 ? 0.1455 0.1486 0.2150 -0.0128 -0.0107 0.0360  150  ASN   A O   
3344 C  CB  . ASN   A 150 ? 0.1914 0.1769 0.1906 -0.0154 0.0276  0.0572  150  ASN   A CB  
3345 C  CG  . ASN   A 150 ? 0.2470 0.2161 0.2439 -0.0126 0.0206  0.0633  150  ASN   A CG  
3346 O  OD1 . ASN   A 150 ? 0.2654 0.2270 0.2705 -0.0186 0.0286  0.0778  150  ASN   A OD1 
3347 N  ND2 . ASN   A 150 ? 0.2759 0.2405 0.2686 -0.0050 0.0044  0.0732  150  ASN   A ND2 
3354 N  N   . VAL   A 151 ? 0.1304 0.1304 0.1778 -0.0146 0.0049  0.0366  151  VAL   A N   
3355 C  CA  . VAL   A 151 ? 0.1299 0.1382 0.1642 -0.0165 0.0092  0.0325  151  VAL   A CA  
3356 C  C   . VAL   A 151 ? 0.1268 0.1361 0.1715 -0.0191 0.0084  0.0354  151  VAL   A C   
3357 O  O   . VAL   A 151 ? 0.1318 0.1398 0.2062 -0.0175 0.0129  0.0288  151  VAL   A O   
3358 C  CB  . VAL   A 151 ? 0.1523 0.1572 0.1632 -0.0052 0.0128  0.0403  151  VAL   A CB  
3359 C  CG1 . VAL   A 151 ? 0.1578 0.1755 0.1904 -0.0092 0.0120  0.0329  151  VAL   A CG1 
3360 C  CG2 . VAL   A 151 ? 0.1577 0.1589 0.1759 -0.0009 0.0304  0.0355  151  VAL   A CG2 
3370 N  N   . TYR   A 152 ? 0.1243 0.1350 0.1670 -0.0126 0.0059  0.0362  152  TYR   A N   
3371 C  CA  . TYR   A 152 ? 0.1230 0.1378 0.1525 -0.0195 0.0112  0.0275  152  TYR   A CA  
3372 C  C   . TYR   A 152 ? 0.1227 0.1312 0.1472 -0.0123 0.0140  0.0315  152  TYR   A C   
3373 O  O   . TYR   A 152 ? 0.1328 0.1368 0.1598 -0.0262 0.0117  0.0282  152  TYR   A O   
3374 C  CB  . TYR   A 152 ? 0.1332 0.1496 0.1531 -0.0082 0.0186  0.0303  152  TYR   A CB  
3375 C  CG  . TYR   A 152 ? 0.1542 0.1705 0.1543 -0.0127 0.0231  0.0393  152  TYR   A CG  
3376 C  CD1 . TYR   A 152 ? 0.1749 0.1861 0.1696 0.0006  0.0292  0.0468  152  TYR   A CD1 
3377 C  CD2 . TYR   A 152 ? 0.1573 0.1787 0.1536 -0.0213 0.0226  0.0368  152  TYR   A CD2 
3378 C  CE1 . TYR   A 152 ? 0.2017 0.1990 0.1855 0.0023  0.0181  0.0584  152  TYR   A CE1 
3379 C  CE2 . TYR   A 152 ? 0.1851 0.1927 0.1609 -0.0304 0.0174  0.0442  152  TYR   A CE2 
3380 C  CZ  . TYR   A 152 ? 0.2203 0.2000 0.1699 -0.0171 0.0167  0.0681  152  TYR   A CZ  
3381 O  OH  . TYR   A 152 ? 0.2577 0.2213 0.2111 -0.0139 0.0223  0.0817  152  TYR   A OH  
3391 N  N   A LEU   A 153 ? 0.1238 0.1268 0.1503 -0.0068 0.0124  0.0289  153  LEU   A N   
3392 N  N   B LEU   A 153 ? 0.1206 0.1340 0.1728 -0.0165 0.0155  0.0316  153  LEU   A N   
3393 C  CA  A LEU   A 153 ? 0.1247 0.1195 0.1530 -0.0002 0.0081  0.0342  153  LEU   A CA  
3394 C  CA  B LEU   A 153 ? 0.1158 0.1312 0.1892 -0.0139 0.0140  0.0396  153  LEU   A CA  
3395 C  C   A LEU   A 153 ? 0.1287 0.1207 0.1534 0.0067  0.0081  0.0351  153  LEU   A C   
3396 C  C   B LEU   A 153 ? 0.1154 0.1370 0.2041 -0.0156 0.0254  0.0386  153  LEU   A C   
3397 O  O   A LEU   A 153 ? 0.1352 0.1306 0.1663 0.0050  0.0173  0.0287  153  LEU   A O   
3398 O  O   B LEU   A 153 ? 0.1190 0.1486 0.2386 -0.0147 0.0337  0.0378  153  LEU   A O   
3399 C  CB  A LEU   A 153 ? 0.1247 0.1157 0.1556 -0.0040 0.0043  0.0326  153  LEU   A CB  
3400 C  CB  B LEU   A 153 ? 0.1146 0.1386 0.1947 -0.0131 0.0065  0.0349  153  LEU   A CB  
3401 C  CG  A LEU   A 153 ? 0.1319 0.1147 0.1586 -0.0079 0.0074  0.0261  153  LEU   A CG  
3402 C  CG  B LEU   A 153 ? 0.1269 0.1435 0.1871 -0.0171 0.0087  0.0296  153  LEU   A CG  
3403 C  CD1 A LEU   A 153 ? 0.1383 0.1182 0.1619 -0.0129 0.0058  0.0275  153  LEU   A CD1 
3404 C  CD1 B LEU   A 153 ? 0.1403 0.1512 0.1888 -0.0172 -0.0010 0.0330  153  LEU   A CD1 
3405 C  CD2 A LEU   A 153 ? 0.1343 0.1190 0.1641 -0.0073 0.0118  0.0126  153  LEU   A CD2 
3406 C  CD2 B LEU   A 153 ? 0.1286 0.1560 0.1901 -0.0211 0.0190  0.0222  153  LEU   A CD2 
3429 N  N   A ALA   A 154 ? 0.1310 0.1181 0.1551 0.0140  0.0028  0.0342  154  ALA   A N   
3430 N  N   B ALA   A 154 ? 0.1141 0.1380 0.1990 -0.0136 0.0359  0.0301  154  ALA   A N   
3431 C  CA  A ALA   A 154 ? 0.1380 0.1223 0.1634 0.0189  0.0026  0.0346  154  ALA   A CA  
3432 C  CA  B ALA   A 154 ? 0.1258 0.1389 0.2226 -0.0100 0.0315  0.0311  154  ALA   A CA  
3433 C  C   A ALA   A 154 ? 0.1422 0.1297 0.1648 0.0226  0.0014  0.0376  154  ALA   A C   
3434 C  C   B ALA   A 154 ? 0.1293 0.1375 0.2244 -0.0079 0.0333  0.0451  154  ALA   A C   
3435 O  O   A ALA   A 154 ? 0.1464 0.1339 0.1648 0.0222  0.0016  0.0395  154  ALA   A O   
3436 O  O   B ALA   A 154 ? 0.1409 0.1495 0.2168 -0.0094 0.0345  0.0526  154  ALA   A O   
3437 C  CB  A ALA   A 154 ? 0.1415 0.1245 0.1612 0.0213  -0.0005 0.0264  154  ALA   A CB  
3438 C  CB  B ALA   A 154 ? 0.1343 0.1421 0.2243 -0.0077 0.0321  0.0149  154  ALA   A CB  
3449 N  N   A VAL   A 155 ? 0.1482 0.1406 0.1668 0.0242  -0.0041 0.0419  155  VAL   A N   
3450 N  N   B VAL   A 155 ? 0.1328 0.1401 0.2454 -0.0072 0.0251  0.0497  155  VAL   A N   
3451 C  CA  A VAL   A 155 ? 0.1579 0.1516 0.1750 0.0284  -0.0099 0.0456  155  VAL   A CA  
3452 C  CA  B VAL   A 155 ? 0.1402 0.1422 0.2626 -0.0104 0.0260  0.0571  155  VAL   A CA  
3453 C  C   A VAL   A 155 ? 0.1706 0.1653 0.1829 0.0333  -0.0219 0.0415  155  VAL   A C   
3454 C  C   B VAL   A 155 ? 0.1419 0.1434 0.2773 -0.0091 0.0249  0.0586  155  VAL   A C   
3455 O  O   A VAL   A 155 ? 0.1725 0.1748 0.1895 0.0387  -0.0238 0.0334  155  VAL   A O   
3456 O  O   B VAL   A 155 ? 0.1447 0.1462 0.2898 -0.0012 0.0315  0.0581  155  VAL   A O   
3457 C  CB  A VAL   A 155 ? 0.1594 0.1566 0.1840 0.0239  -0.0131 0.0402  155  VAL   A CB  
3458 C  CB  B VAL   A 155 ? 0.1558 0.1412 0.2707 -0.0131 0.0035  0.0504  155  VAL   A CB  
3459 C  CG1 A VAL   A 155 ? 0.1637 0.1620 0.1888 0.0214  -0.0214 0.0366  155  VAL   A CG1 
3460 C  CG1 B VAL   A 155 ? 0.1687 0.1424 0.2794 -0.0148 -0.0098 0.0520  155  VAL   A CG1 
3461 C  CG2 A VAL   A 155 ? 0.1652 0.1587 0.1931 0.0253  -0.0098 0.0365  155  VAL   A CG2 
3462 C  CG2 B VAL   A 155 ? 0.1707 0.1466 0.2796 0.0001  -0.0047 0.0413  155  VAL   A CG2 
3481 N  N   A PHE   A 156 ? 0.1794 0.1656 0.1794 0.0358  -0.0246 0.0446  156  PHE   A N   
3482 N  N   B PHE   A 156 ? 0.1491 0.1418 0.2887 -0.0112 0.0245  0.0555  156  PHE   A N   
3483 C  CA  A PHE   A 156 ? 0.1939 0.1706 0.1968 0.0388  -0.0222 0.0461  156  PHE   A CA  
3484 C  CA  B PHE   A 156 ? 0.1621 0.1502 0.2881 -0.0123 0.0156  0.0535  156  PHE   A CA  
3485 C  C   A PHE   A 156 ? 0.1894 0.1685 0.2026 0.0448  -0.0186 0.0565  156  PHE   A C   
3486 C  C   B PHE   A 156 ? 0.1670 0.1634 0.3124 -0.0048 0.0170  0.0612  156  PHE   A C   
3487 O  O   A PHE   A 156 ? 0.1927 0.1772 0.2095 0.0460  -0.0072 0.0442  156  PHE   A O   
3488 O  O   B PHE   A 156 ? 0.1816 0.1938 0.3432 0.0047  0.0340  0.0551  156  PHE   A O   
3489 C  CB  A PHE   A 156 ? 0.2108 0.1767 0.2068 0.0402  -0.0268 0.0435  156  PHE   A CB  
3490 C  CB  B PHE   A 156 ? 0.1705 0.1488 0.2560 -0.0105 0.0001  0.0602  156  PHE   A CB  
3491 C  CG  A PHE   A 156 ? 0.2257 0.1839 0.2288 0.0445  -0.0263 0.0317  156  PHE   A CG  
3492 C  CG  B PHE   A 156 ? 0.1870 0.1643 0.2477 -0.0041 -0.0026 0.0601  156  PHE   A CG  
3493 C  CD1 A PHE   A 156 ? 0.2328 0.1873 0.2392 0.0470  -0.0222 0.0264  156  PHE   A CD1 
3494 C  CD1 B PHE   A 156 ? 0.1954 0.1750 0.2691 0.0090  0.0025  0.0584  156  PHE   A CD1 
3495 C  CD2 A PHE   A 156 ? 0.2360 0.1931 0.2388 0.0438  -0.0243 0.0260  156  PHE   A CD2 
3496 C  CD2 B PHE   A 156 ? 0.2047 0.1726 0.2549 -0.0025 -0.0056 0.0562  156  PHE   A CD2 
3497 C  CE1 A PHE   A 156 ? 0.2392 0.1923 0.2501 0.0490  -0.0182 0.0223  156  PHE   A CE1 
3498 C  CE1 B PHE   A 156 ? 0.2004 0.1840 0.2838 0.0053  0.0045  0.0499  156  PHE   A CE1 
3499 C  CE2 A PHE   A 156 ? 0.2398 0.1980 0.2463 0.0449  -0.0209 0.0208  156  PHE   A CE2 
3500 C  CE2 B PHE   A 156 ? 0.2081 0.1789 0.2664 -0.0016 -0.0086 0.0588  156  PHE   A CE2 
3501 C  CZ  A PHE   A 156 ? 0.2403 0.1968 0.2505 0.0497  -0.0185 0.0196  156  PHE   A CZ  
3502 C  CZ  B PHE   A 156 ? 0.2051 0.1833 0.2891 -0.0077 -0.0025 0.0488  156  PHE   A CZ  
3521 N  N   A ASP   A 157 ? 0.1860 0.1661 0.2006 0.0439  -0.0286 0.0791  157  ASP   A N   
3522 N  N   B ASP   A 157 ? 0.1752 0.1752 0.3346 -0.0110 -0.0048 0.0672  157  ASP   A N   
3523 C  CA  A ASP   A 157 ? 0.1845 0.1819 0.2167 0.0364  -0.0282 0.0775  157  ASP   A CA  
3524 C  CA  B ASP   A 157 ? 0.1838 0.1863 0.3489 -0.0150 -0.0208 0.0556  157  ASP   A CA  
3525 C  C   A ASP   A 157 ? 0.1747 0.1940 0.2221 0.0465  -0.0173 0.0732  157  ASP   A C   
3526 C  C   B ASP   A 157 ? 0.1749 0.1836 0.3364 -0.0124 -0.0187 0.0478  157  ASP   A C   
3527 O  O   A ASP   A 157 ? 0.1694 0.1912 0.2157 0.0507  -0.0094 0.0731  157  ASP   A O   
3528 O  O   B ASP   A 157 ? 0.1703 0.1731 0.3030 -0.0105 -0.0225 0.0586  157  ASP   A O   
3529 C  CB  A ASP   A 157 ? 0.1897 0.1838 0.2353 0.0269  -0.0410 0.0831  157  ASP   A CB  
3530 C  CB  B ASP   A 157 ? 0.2031 0.1981 0.3697 -0.0113 -0.0287 0.0577  157  ASP   A CB  
3531 C  CG  A ASP   A 157 ? 0.1965 0.1853 0.2617 0.0257  -0.0537 0.0864  157  ASP   A CG  
3532 C  CG  B ASP   A 157 ? 0.2281 0.2084 0.3951 0.0008  -0.0419 0.0592  157  ASP   A CG  
3533 O  OD1 A ASP   A 157 ? 0.1982 0.1825 0.2717 0.0237  -0.0542 0.0803  157  ASP   A OD1 
3534 O  OD1 B ASP   A 157 ? 0.2241 0.2009 0.3936 0.0103  -0.0372 0.0615  157  ASP   A OD1 
3535 O  OD2 A ASP   A 157 ? 0.1978 0.1851 0.2704 0.0194  -0.0592 0.0880  157  ASP   A OD2 
3536 O  OD2 B ASP   A 157 ? 0.2536 0.2206 0.4203 -0.0005 -0.0549 0.0580  157  ASP   A OD2 
3545 N  N   A LYS   A 158 ? 0.1735 0.2095 0.2450 0.0536  -0.0134 0.0632  158  LYS   A N   
3546 N  N   B LYS   A 158 ? 0.1756 0.1931 0.3637 -0.0114 -0.0070 0.0380  158  LYS   A N   
3547 C  CA  A LYS   A 158 ? 0.1696 0.2241 0.2629 0.0629  -0.0050 0.0547  158  LYS   A CA  
3548 C  CA  B LYS   A 158 ? 0.1745 0.2138 0.3838 -0.0060 0.0007  0.0389  158  LYS   A CA  
3549 C  C   A LYS   A 158 ? 0.1682 0.2380 0.2565 0.0637  -0.0064 0.0512  158  LYS   A C   
3550 C  C   B LYS   A 158 ? 0.1632 0.2088 0.3646 -0.0071 -0.0159 0.0441  158  LYS   A C   
3551 O  O   A LYS   A 158 ? 0.1690 0.2423 0.2587 0.0587  0.0034  0.0448  158  LYS   A O   
3552 O  O   B LYS   A 158 ? 0.1575 0.1965 0.3599 -0.0130 -0.0103 0.0478  158  LYS   A O   
3553 C  CB  A LYS   A 158 ? 0.1747 0.2256 0.2797 0.0643  0.0084  0.0543  158  LYS   A CB  
3554 C  CB  B LYS   A 158 ? 0.1918 0.2405 0.4173 -0.0035 0.0227  0.0568  158  LYS   A CB  
3555 C  CG  A LYS   A 158 ? 0.1817 0.2307 0.3076 0.0628  0.0142  0.0536  158  LYS   A CG  
3556 C  CG  B LYS   A 158 ? 0.2117 0.2668 0.4537 0.0014  0.0371  0.0733  158  LYS   A CG  
3557 C  CD  A LYS   A 158 ? 0.1905 0.2355 0.3290 0.0580  0.0237  0.0583  158  LYS   A CD  
3558 C  CD  B LYS   A 158 ? 0.2249 0.2936 0.4870 0.0004  0.0527  0.0884  158  LYS   A CD  
3559 C  CE  A LYS   A 158 ? 0.1962 0.2386 0.3477 0.0520  0.0267  0.0667  158  LYS   A CE  
3560 C  CE  B LYS   A 158 ? 0.2306 0.3104 0.5017 -0.0004 0.0695  0.1110  158  LYS   A CE  
3561 N  NZ  A LYS   A 158 ? 0.1971 0.2398 0.3584 0.0499  0.0305  0.0723  158  LYS   A NZ  
3562 N  NZ  B LYS   A 158 ? 0.2259 0.3188 0.5092 -0.0030 0.0823  0.1283  158  LYS   A NZ  
3589 N  N   A ASN   A 159 ? 0.1715 0.2493 0.2567 0.0602  -0.0192 0.0575  159  ASN   A N   
3590 N  N   B ASN   A 159 ? 0.1730 0.2275 0.3659 -0.0014 -0.0327 0.0438  159  ASN   A N   
3591 C  CA  A ASN   A 159 ? 0.1724 0.2560 0.2541 0.0560  -0.0244 0.0563  159  ASN   A CA  
3592 C  CA  B ASN   A 159 ? 0.1880 0.2506 0.3809 0.0080  -0.0423 0.0515  159  ASN   A CA  
3593 C  C   A ASN   A 159 ? 0.1693 0.2489 0.2439 0.0493  -0.0186 0.0565  159  ASN   A C   
3594 C  C   B ASN   A 159 ? 0.1656 0.2326 0.3573 -0.0071 -0.0402 0.0474  159  ASN   A C   
3595 O  O   A ASN   A 159 ? 0.1703 0.2566 0.2430 0.0507  -0.0223 0.0562  159  ASN   A O   
3596 O  O   B ASN   A 159 ? 0.1634 0.2455 0.3632 -0.0101 -0.0469 0.0428  159  ASN   A O   
3597 C  CB  A ASN   A 159 ? 0.1758 0.2647 0.2655 0.0555  -0.0286 0.0568  159  ASN   A CB  
3598 C  CB  B ASN   A 159 ? 0.2252 0.2874 0.4222 0.0244  -0.0542 0.0544  159  ASN   A CB  
3599 C  CG  A ASN   A 159 ? 0.1875 0.2702 0.2754 0.0489  -0.0289 0.0536  159  ASN   A CG  
3600 C  CG  B ASN   A 159 ? 0.2597 0.3219 0.4621 0.0242  -0.0594 0.0493  159  ASN   A CG  
3601 O  OD1 A ASN   A 159 ? 0.1906 0.2747 0.2863 0.0409  -0.0256 0.0510  159  ASN   A OD1 
3602 O  OD1 B ASN   A 159 ? 0.2762 0.3388 0.4828 0.0172  -0.0670 0.0455  159  ASN   A OD1 
3603 N  ND2 A ASN   A 159 ? 0.1941 0.2729 0.2840 0.0448  -0.0270 0.0488  159  ASN   A ND2 
3604 N  ND2 B ASN   A 159 ? 0.2613 0.3291 0.4783 0.0305  -0.0651 0.0483  159  ASN   A ND2 
3617 N  N   A LEU   A 160 ? 0.1637 0.2292 0.2357 0.0430  -0.0172 0.0582  160  LEU   A N   
3618 N  N   B LEU   A 160 ? 0.1506 0.2092 0.3471 -0.0153 -0.0382 0.0565  160  LEU   A N   
3619 C  CA  A LEU   A 160 ? 0.1606 0.2108 0.2246 0.0304  -0.0084 0.0613  160  LEU   A CA  
3620 C  CA  B LEU   A 160 ? 0.1500 0.1953 0.3358 -0.0156 -0.0247 0.0524  160  LEU   A CA  
3621 C  C   A LEU   A 160 ? 0.1474 0.2015 0.2087 0.0230  -0.0012 0.0607  160  LEU   A C   
3622 C  C   B LEU   A 160 ? 0.1358 0.1871 0.3317 -0.0115 -0.0076 0.0444  160  LEU   A C   
3623 O  O   A LEU   A 160 ? 0.1470 0.2043 0.2074 0.0193  -0.0037 0.0515  160  LEU   A O   
3624 O  O   B LEU   A 160 ? 0.1427 0.1785 0.3471 -0.0249 0.0023  0.0290  160  LEU   A O   
3625 C  CB  A LEU   A 160 ? 0.1670 0.2040 0.2242 0.0219  0.0035  0.0588  160  LEU   A CB  
3626 C  CB  B LEU   A 160 ? 0.1636 0.1903 0.3301 -0.0222 -0.0247 0.0623  160  LEU   A CB  
3627 C  CG  A LEU   A 160 ? 0.1725 0.1994 0.2323 0.0130  0.0094  0.0503  160  LEU   A CG  
3628 C  CG  B LEU   A 160 ? 0.1711 0.1951 0.3384 -0.0287 -0.0219 0.0684  160  LEU   A CG  
3629 C  CD1 A LEU   A 160 ? 0.1765 0.1940 0.2373 0.0128  0.0104  0.0439  160  LEU   A CD1 
3630 C  CD1 B LEU   A 160 ? 0.1755 0.2046 0.3476 -0.0320 -0.0154 0.0712  160  LEU   A CD1 
3631 C  CD2 A LEU   A 160 ? 0.1729 0.1994 0.2363 0.0065  0.0158  0.0403  160  LEU   A CD2 
3632 C  CD2 B LEU   A 160 ? 0.1775 0.1941 0.3396 -0.0299 -0.0264 0.0695  160  LEU   A CD2 
3655 N  N   A TYR   A 161 ? 0.1443 0.1927 0.2173 0.0209  0.0020  0.0671  161  TYR   A N   
3656 N  N   B TYR   A 161 ? 0.1289 0.1853 0.3228 -0.0049 0.0074  0.0560  161  TYR   A N   
3657 C  CA  A TYR   A 161 ? 0.1415 0.1849 0.2200 0.0177  0.0071  0.0685  161  TYR   A CA  
3658 C  CA  B TYR   A 161 ? 0.1361 0.1843 0.3183 -0.0060 0.0087  0.0676  161  TYR   A CA  
3659 C  C   A TYR   A 161 ? 0.1381 0.1983 0.2288 0.0181  0.0176  0.0674  161  TYR   A C   
3660 C  C   B TYR   A 161 ? 0.1293 0.1867 0.3265 -0.0107 0.0128  0.0530  161  TYR   A C   
3661 O  O   A TYR   A 161 ? 0.1342 0.1996 0.2254 0.0176  0.0178  0.0654  161  TYR   A O   
3662 O  O   B TYR   A 161 ? 0.1306 0.1839 0.3186 -0.0150 0.0116  0.0466  161  TYR   A O   
3663 C  CB  A TYR   A 161 ? 0.1442 0.1685 0.2362 0.0080  -0.0007 0.0563  161  TYR   A CB  
3664 C  CB  B TYR   A 161 ? 0.1442 0.1854 0.3314 0.0027  0.0110  0.0723  161  TYR   A CB  
3665 C  CG  A TYR   A 161 ? 0.1388 0.1584 0.2402 -0.0001 -0.0059 0.0429  161  TYR   A CG  
3666 C  CG  B TYR   A 161 ? 0.1513 0.1941 0.3445 0.0078  0.0051  0.0782  161  TYR   A CG  
3667 C  CD1 A TYR   A 161 ? 0.1350 0.1496 0.2463 -0.0030 -0.0087 0.0318  161  TYR   A CD1 
3668 C  CD1 B TYR   A 161 ? 0.1522 0.1991 0.3584 0.0118  0.0067  0.0730  161  TYR   A CD1 
3669 C  CD2 A TYR   A 161 ? 0.1352 0.1625 0.2375 -0.0037 -0.0152 0.0375  161  TYR   A CD2 
3670 C  CD2 B TYR   A 161 ? 0.1566 0.2082 0.3522 0.0085  -0.0065 0.0844  161  TYR   A CD2 
3671 C  CE1 A TYR   A 161 ? 0.1377 0.1444 0.2477 -0.0073 -0.0142 0.0303  161  TYR   A CE1 
3672 C  CE1 B TYR   A 161 ? 0.1667 0.2036 0.3608 0.0115  -0.0028 0.0812  161  TYR   A CE1 
3673 C  CE2 A TYR   A 161 ? 0.1354 0.1528 0.2431 -0.0076 -0.0158 0.0338  161  TYR   A CE2 
3674 C  CE2 B TYR   A 161 ? 0.1663 0.2062 0.3583 0.0099  -0.0155 0.0979  161  TYR   A CE2 
3675 C  CZ  A TYR   A 161 ? 0.1390 0.1413 0.2461 -0.0058 -0.0199 0.0353  161  TYR   A CZ  
3676 C  CZ  B TYR   A 161 ? 0.1801 0.2047 0.3636 0.0080  -0.0128 0.0958  161  TYR   A CZ  
3677 O  OH  A TYR   A 161 ? 0.1407 0.1274 0.2482 -0.0028 -0.0257 0.0341  161  TYR   A OH  
3678 O  OH  B TYR   A 161 ? 0.1985 0.2061 0.3810 0.0091  -0.0188 0.0913  161  TYR   A OH  
3697 N  N   A ASP   A 162 ? 0.1391 0.2120 0.2406 0.0186  0.0196  0.0643  162  ASP   A N   
3698 N  N   B ASP   A 162 ? 0.1280 0.1966 0.3543 -0.0071 0.0115  0.0481  162  ASP   A N   
3699 C  CA  A ASP   A 162 ? 0.1421 0.2269 0.2475 0.0171  0.0207  0.0594  162  ASP   A CA  
3700 C  CA  B ASP   A 162 ? 0.1308 0.2172 0.3608 -0.0106 0.0069  0.0460  162  ASP   A CA  
3701 C  C   A ASP   A 162 ? 0.1481 0.2410 0.2524 0.0132  0.0190  0.0571  162  ASP   A C   
3702 C  C   B ASP   A 162 ? 0.1342 0.2289 0.3609 -0.0215 -0.0000 0.0425  162  ASP   A C   
3703 O  O   A ASP   A 162 ? 0.1481 0.2415 0.2621 0.0146  0.0245  0.0516  162  ASP   A O   
3704 O  O   B ASP   A 162 ? 0.1395 0.2207 0.3801 -0.0323 0.0106  0.0408  162  ASP   A O   
3705 C  CB  A ASP   A 162 ? 0.1460 0.2330 0.2566 0.0168  0.0223  0.0535  162  ASP   A CB  
3706 C  CB  B ASP   A 162 ? 0.1477 0.2428 0.3880 0.0037  -0.0009 0.0328  162  ASP   A CB  
3707 C  CG  A ASP   A 162 ? 0.1486 0.2380 0.2635 0.0168  0.0304  0.0578  162  ASP   A CG  
3708 C  CG  B ASP   A 162 ? 0.1678 0.2672 0.4104 0.0175  0.0038  0.0232  162  ASP   A CG  
3709 O  OD1 A ASP   A 162 ? 0.1496 0.2409 0.2719 0.0096  0.0284  0.0534  162  ASP   A OD1 
3710 O  OD1 B ASP   A 162 ? 0.1678 0.2749 0.4196 0.0151  0.0031  0.0183  162  ASP   A OD1 
3711 O  OD2 A ASP   A 162 ? 0.1461 0.2389 0.2568 0.0205  0.0505  0.0682  162  ASP   A OD2 
3712 O  OD2 B ASP   A 162 ? 0.1845 0.2791 0.4193 0.0280  0.0169  0.0189  162  ASP   A OD2 
3721 N  N   A LYS   A 163 ? 0.1576 0.2514 0.2547 0.0071  0.0096  0.0564  163  LYS   A N   
3722 N  N   B LYS   A 163 ? 0.1431 0.2489 0.3491 -0.0238 -0.0243 0.0474  163  LYS   A N   
3723 C  CA  A LYS   A 163 ? 0.1696 0.2591 0.2529 -0.0005 0.0026  0.0520  163  LYS   A CA  
3724 C  CA  B LYS   A 163 ? 0.1661 0.2735 0.3458 -0.0292 -0.0320 0.0458  163  LYS   A CA  
3725 C  C   A LYS   A 163 ? 0.1614 0.2530 0.2386 -0.0035 0.0148  0.0511  163  LYS   A C   
3726 C  C   B LYS   A 163 ? 0.1482 0.2419 0.3169 -0.0342 -0.0057 0.0354  163  LYS   A C   
3727 O  O   A LYS   A 163 ? 0.1566 0.2581 0.2511 -0.0080 0.0152  0.0519  163  LYS   A O   
3728 O  O   B LYS   A 163 ? 0.1562 0.2385 0.3281 -0.0387 -0.0020 0.0304  163  LYS   A O   
3729 C  CB  A LYS   A 163 ? 0.1924 0.2709 0.2813 -0.0029 -0.0053 0.0454  163  LYS   A CB  
3730 C  CB  B LYS   A 163 ? 0.2177 0.3310 0.3956 -0.0316 -0.0504 0.0531  163  LYS   A CB  
3731 C  CG  A LYS   A 163 ? 0.2124 0.2802 0.3126 -0.0055 -0.0070 0.0386  163  LYS   A CG  
3732 C  CG  B LYS   A 163 ? 0.2729 0.3856 0.4475 -0.0362 -0.0518 0.0587  163  LYS   A CG  
3733 C  CD  A LYS   A 163 ? 0.2268 0.2873 0.3458 -0.0080 -0.0100 0.0293  163  LYS   A CD  
3734 C  CD  B LYS   A 163 ? 0.3288 0.4339 0.5001 -0.0412 -0.0553 0.0594  163  LYS   A CD  
3735 C  CE  A LYS   A 163 ? 0.2401 0.2914 0.3729 -0.0086 -0.0087 0.0255  163  LYS   A CE  
3736 C  CE  B LYS   A 163 ? 0.3813 0.4676 0.5452 -0.0431 -0.0578 0.0593  163  LYS   A CE  
3737 N  NZ  A LYS   A 163 ? 0.2489 0.2938 0.3877 -0.0094 -0.0087 0.0262  163  LYS   A NZ  
3738 N  NZ  B LYS   A 163 ? 0.4124 0.4865 0.5685 -0.0438 -0.0580 0.0595  163  LYS   A NZ  
3765 N  N   A LEU   A 164 ? 0.1592 0.2392 0.2200 -0.0066 0.0210  0.0480  164  LEU   A N   
3766 N  N   B LEU   A 164 ? 0.1356 0.2251 0.3020 -0.0274 -0.0003 0.0288  164  LEU   A N   
3767 C  CA  A LEU   A 164 ? 0.1620 0.2275 0.2136 -0.0113 0.0301  0.0412  164  LEU   A CA  
3768 C  CA  B LEU   A 164 ? 0.1364 0.2062 0.2913 -0.0226 0.0215  0.0370  164  LEU   A CA  
3769 C  C   A LEU   A 164 ? 0.1623 0.2263 0.2224 -0.0130 0.0339  0.0442  164  LEU   A C   
3770 C  C   B LEU   A 164 ? 0.1404 0.1960 0.2876 -0.0192 0.0306  0.0346  164  LEU   A C   
3771 O  O   A LEU   A 164 ? 0.1605 0.2292 0.2338 -0.0111 0.0404  0.0435  164  LEU   A O   
3772 O  O   B LEU   A 164 ? 0.1592 0.1987 0.2952 -0.0093 0.0400  0.0278  164  LEU   A O   
3773 C  CB  A LEU   A 164 ? 0.1669 0.2213 0.2031 -0.0123 0.0306  0.0327  164  LEU   A CB  
3774 C  CB  B LEU   A 164 ? 0.1397 0.1998 0.2872 -0.0260 0.0245  0.0471  164  LEU   A CB  
3775 C  CG  A LEU   A 164 ? 0.1763 0.2192 0.2053 -0.0142 0.0272  0.0234  164  LEU   A CG  
3776 C  CG  B LEU   A 164 ? 0.1442 0.2010 0.2871 -0.0237 0.0202  0.0480  164  LEU   A CG  
3777 C  CD1 A LEU   A 164 ? 0.1758 0.2190 0.2087 -0.0097 0.0241  0.0211  164  LEU   A CD1 
3778 C  CD1 B LEU   A 164 ? 0.1463 0.1995 0.2919 -0.0258 0.0034  0.0475  164  LEU   A CD1 
3779 C  CD2 A LEU   A 164 ? 0.1824 0.2171 0.2009 -0.0162 0.0297  0.0204  164  LEU   A CD2 
3780 C  CD2 B LEU   A 164 ? 0.1592 0.2101 0.2814 -0.0138 0.0315  0.0404  164  LEU   A CD2 
3803 N  N   A VAL   A 165 ? 0.1652 0.2248 0.2235 -0.0155 0.0328  0.0456  165  VAL   A N   
3804 N  N   B VAL   A 165 ? 0.1440 0.1964 0.2903 -0.0115 0.0277  0.0403  165  VAL   A N   
3805 C  CA  A VAL   A 165 ? 0.1716 0.2264 0.2206 -0.0197 0.0315  0.0438  165  VAL   A CA  
3806 C  CA  B VAL   A 165 ? 0.1488 0.2007 0.2784 -0.0164 0.0296  0.0467  165  VAL   A CA  
3807 C  C   A VAL   A 165 ? 0.1667 0.2271 0.2173 -0.0164 0.0336  0.0515  165  VAL   A C   
3808 C  C   B VAL   A 165 ? 0.1360 0.2003 0.2730 -0.0166 0.0150  0.0503  165  VAL   A C   
3809 O  O   A VAL   A 165 ? 0.1697 0.2310 0.2197 -0.0179 0.0379  0.0611  165  VAL   A O   
3810 O  O   B VAL   A 165 ? 0.1420 0.2003 0.2708 -0.0211 0.0081  0.0506  165  VAL   A O   
3811 C  CB  A VAL   A 165 ? 0.1867 0.2312 0.2259 -0.0199 0.0200  0.0303  165  VAL   A CB  
3812 C  CB  B VAL   A 165 ? 0.1814 0.2201 0.2880 -0.0134 0.0332  0.0389  165  VAL   A CB  
3813 C  CG1 A VAL   A 165 ? 0.1890 0.2337 0.2309 -0.0199 0.0207  0.0246  165  VAL   A CG1 
3814 C  CG1 B VAL   A 165 ? 0.1874 0.2281 0.2897 -0.0143 0.0397  0.0362  165  VAL   A CG1 
3815 C  CG2 A VAL   A 165 ? 0.1938 0.2319 0.2315 -0.0202 0.0132  0.0278  165  VAL   A CG2 
3816 C  CG2 B VAL   A 165 ? 0.1929 0.2241 0.2927 -0.0139 0.0321  0.0435  165  VAL   A CG2 
3835 N  N   A SER   A 166 ? 0.1648 0.2257 0.2287 -0.0092 0.0304  0.0505  166  SER   A N   
3836 N  N   B SER   A 166 ? 0.1321 0.2073 0.2981 -0.0159 0.0160  0.0442  166  SER   A N   
3837 C  CA  A SER   A 166 ? 0.1689 0.2303 0.2434 -0.0100 0.0197  0.0438  166  SER   A CA  
3838 C  CA  B SER   A 166 ? 0.1403 0.2236 0.3187 -0.0100 0.0050  0.0313  166  SER   A CA  
3839 C  C   A SER   A 166 ? 0.1679 0.2261 0.2374 -0.0101 0.0023  0.0443  166  SER   A C   
3840 C  C   B SER   A 166 ? 0.1429 0.2316 0.3104 -0.0204 0.0084  0.0276  166  SER   A C   
3841 O  O   A SER   A 166 ? 0.1695 0.2235 0.2485 -0.0076 -0.0002 0.0435  166  SER   A O   
3842 O  O   B SER   A 166 ? 0.1478 0.2335 0.3193 -0.0317 0.0102  0.0287  166  SER   A O   
3843 C  CB  A SER   A 166 ? 0.1808 0.2431 0.2635 -0.0044 0.0214  0.0353  166  SER   A CB  
3844 C  CB  B SER   A 166 ? 0.1704 0.2466 0.3529 0.0053  -0.0054 0.0300  166  SER   A CB  
3845 O  OG  A SER   A 166 ? 0.1893 0.2565 0.2879 -0.0034 0.0305  0.0443  166  SER   A OG  
3846 O  OG  B SER   A 166 ? 0.2089 0.2799 0.4033 0.0101  -0.0111 0.0257  166  SER   A OG  
3857 N  N   A SER   A 167 ? 0.1719 0.2247 0.2238 -0.0092 -0.0073 0.0398  167  SER   A N   
3858 N  N   B SER   A 167 ? 0.1485 0.2406 0.2933 -0.0148 0.0135  0.0287  167  SER   A N   
3859 C  CA  A SER   A 167 ? 0.1844 0.2227 0.2133 -0.0076 -0.0101 0.0297  167  SER   A CA  
3860 C  CA  B SER   A 167 ? 0.1727 0.2550 0.2738 -0.0084 0.0179  0.0293  167  SER   A CA  
3861 C  C   A SER   A 167 ? 0.1893 0.2183 0.2189 -0.0115 -0.0043 0.0312  167  SER   A C   
3862 C  C   B SER   A 167 ? 0.1754 0.2627 0.2591 -0.0000 0.0212  0.0253  167  SER   A C   
3863 O  O   A SER   A 167 ? 0.1964 0.2124 0.2256 -0.0121 -0.0055 0.0301  167  SER   A O   
3864 O  O   B SER   A 167 ? 0.1875 0.2709 0.2674 0.0028  0.0339  0.0209  167  SER   A O   
3865 C  CB  A SER   A 167 ? 0.1880 0.2245 0.2061 -0.0031 -0.0144 0.0213  167  SER   A CB  
3866 C  CB  B SER   A 167 ? 0.1837 0.2653 0.2824 -0.0020 0.0234  0.0288  167  SER   A CB  
3867 O  OG  A SER   A 167 ? 0.1922 0.2263 0.2064 -0.0008 -0.0067 0.0196  167  SER   A OG  
3868 O  OG  B SER   A 167 ? 0.1928 0.2695 0.2831 0.0040  0.0399  0.0259  167  SER   A OG  
3879 N  N   A PHE   A 168 ? 0.1870 0.2194 0.2239 -0.0165 -0.0026 0.0313  168  PHE   A N   
3880 N  N   B PHE   A 168 ? 0.1724 0.2637 0.2562 0.0047  0.0184  0.0177  168  PHE   A N   
3881 C  CA  A PHE   A 168 ? 0.1919 0.2234 0.2435 -0.0171 0.0038  0.0222  168  PHE   A CA  
3882 C  CA  B PHE   A 168 ? 0.1712 0.2619 0.2529 0.0003  0.0374  0.0081  168  PHE   A CA  
3883 C  C   A PHE   A 168 ? 0.2065 0.2366 0.2747 -0.0209 0.0173  0.0095  168  PHE   A C   
3884 C  C   B PHE   A 168 ? 0.1904 0.2684 0.2965 -0.0172 0.0565  0.0104  168  PHE   A C   
3885 O  O   A PHE   A 168 ? 0.2054 0.2364 0.2911 -0.0246 0.0146  0.0095  168  PHE   A O   
3886 O  O   B PHE   A 168 ? 0.1871 0.2648 0.3009 -0.0186 0.0741  0.0086  168  PHE   A O   
3887 C  CB  A PHE   A 168 ? 0.1811 0.2142 0.2285 -0.0171 -0.0048 0.0224  168  PHE   A CB  
3888 C  CB  B PHE   A 168 ? 0.1683 0.2632 0.2478 -0.0014 0.0254  0.0102  168  PHE   A CB  
3889 C  CG  A PHE   A 168 ? 0.1736 0.2074 0.2107 -0.0156 -0.0128 0.0186  168  PHE   A CG  
3890 C  CG  B PHE   A 168 ? 0.1673 0.2609 0.2338 -0.0047 0.0199  0.0269  168  PHE   A CG  
3891 C  CD1 A PHE   A 168 ? 0.1723 0.2061 0.2011 -0.0142 -0.0189 0.0226  168  PHE   A CD1 
3892 C  CD1 B PHE   A 168 ? 0.1677 0.2649 0.2326 -0.0071 0.0161  0.0423  168  PHE   A CD1 
3893 C  CD2 A PHE   A 168 ? 0.1719 0.2008 0.2008 -0.0137 -0.0125 0.0111  168  PHE   A CD2 
3894 C  CD2 B PHE   A 168 ? 0.1684 0.2519 0.2217 -0.0057 0.0163  0.0287  168  PHE   A CD2 
3895 C  CE1 A PHE   A 168 ? 0.1697 0.2031 0.1900 -0.0133 -0.0253 0.0200  168  PHE   A CE1 
3896 C  CE1 B PHE   A 168 ? 0.1625 0.2651 0.2353 -0.0152 0.0114  0.0455  168  PHE   A CE1 
3897 C  CE2 A PHE   A 168 ? 0.1725 0.1947 0.1927 -0.0133 -0.0143 0.0122  168  PHE   A CE2 
3898 C  CE2 B PHE   A 168 ? 0.1687 0.2515 0.2242 -0.0082 0.0115  0.0285  168  PHE   A CE2 
3899 C  CZ  A PHE   A 168 ? 0.1698 0.1971 0.1864 -0.0110 -0.0253 0.0145  168  PHE   A CZ  
3900 C  CZ  B PHE   A 168 ? 0.1678 0.2583 0.2358 -0.0110 0.0123  0.0344  168  PHE   A CZ  
3919 N  N   A LEU   A 169 ? 0.2226 0.2426 0.2857 -0.0205 0.0308  -0.0051 169  LEU   A N   
3920 N  N   B LEU   A 169 ? 0.2197 0.2879 0.3321 -0.0258 0.0655  0.0122  169  LEU   A N   
3921 C  CA  A LEU   A 169 ? 0.2369 0.2466 0.2988 -0.0183 0.0415  -0.0075 169  LEU   A CA  
3922 C  CA  B LEU   A 169 ? 0.2576 0.3158 0.3781 -0.0334 0.0662  0.0058  169  LEU   A CA  
3923 C  C   A LEU   A 169 ? 0.2385 0.2434 0.2998 -0.0186 0.0641  -0.0035 169  LEU   A C   
3924 C  C   B LEU   A 169 ? 0.2786 0.3354 0.4180 -0.0316 0.0572  -0.0119 169  LEU   A C   
3925 O  O   A LEU   A 169 ? 0.2464 0.2468 0.3012 -0.0143 0.0591  -0.0028 169  LEU   A O   
3926 O  O   B LEU   A 169 ? 0.2955 0.3480 0.4389 -0.0285 0.0507  -0.0195 169  LEU   A O   
3927 C  CB  A LEU   A 169 ? 0.2480 0.2537 0.3022 -0.0135 0.0356  -0.0107 169  LEU   A CB  
3928 C  CB  B LEU   A 169 ? 0.2844 0.3267 0.3803 -0.0385 0.0673  0.0147  169  LEU   A CB  
3929 C  CG  A LEU   A 169 ? 0.2553 0.2573 0.3088 -0.0092 0.0327  -0.0154 169  LEU   A CG  
3930 C  CG  B LEU   A 169 ? 0.3087 0.3392 0.3853 -0.0418 0.0688  0.0236  169  LEU   A CG  
3931 C  CD1 A LEU   A 169 ? 0.2573 0.2599 0.3142 -0.0069 0.0302  -0.0144 169  LEU   A CD1 
3932 C  CD1 B LEU   A 169 ? 0.3258 0.3517 0.3998 -0.0416 0.0691  0.0234  169  LEU   A CD1 
3933 C  CD2 A LEU   A 169 ? 0.2561 0.2559 0.3051 -0.0082 0.0350  -0.0169 169  LEU   A CD2 
3934 C  CD2 B LEU   A 169 ? 0.3148 0.3405 0.3814 -0.0389 0.0672  0.0247  169  LEU   A CD2 
3935 O  OXT A LEU   A 169 ? 0.2295 0.2396 0.2937 -0.0228 0.0980  -0.0089 169  LEU   A OXT 
3936 O  OXT B LEU   A 169 ? 0.2724 0.3425 0.4267 -0.0375 0.0483  -0.0124 169  LEU   A OXT 
3959 N  N   A SER   B 1   ? 0.3690 0.3664 0.3982 -0.0821 -0.0570 0.0230  1    SER   B N   
3960 N  N   B SER   B 1   ? 0.3650 0.3663 0.3879 -0.1263 -0.0866 0.0206  1    SER   B N   
3961 C  CA  A SER   B 1   ? 0.3640 0.3644 0.3964 -0.0839 -0.0555 0.0246  1    SER   B CA  
3962 C  CA  B SER   B 1   ? 0.3540 0.3669 0.3846 -0.1320 -0.0896 0.0227  1    SER   B CA  
3963 C  C   A SER   B 1   ? 0.3493 0.3566 0.3791 -0.0852 -0.0563 0.0374  1    SER   B C   
3964 C  C   B SER   B 1   ? 0.3220 0.3613 0.3477 -0.1409 -0.0987 0.0528  1    SER   B C   
3965 O  O   A SER   B 1   ? 0.3537 0.3578 0.3665 -0.0840 -0.0569 0.0366  1    SER   B O   
3966 O  O   B SER   B 1   ? 0.3251 0.3616 0.3111 -0.1410 -0.1067 0.0535  1    SER   B O   
3967 C  CB  A SER   B 1   ? 0.3705 0.3667 0.3985 -0.0839 -0.0514 0.0181  1    SER   B CB  
3968 C  CB  B SER   B 1   ? 0.3700 0.3671 0.3960 -0.1286 -0.0801 0.0035  1    SER   B CB  
3969 O  OG  A SER   B 1   ? 0.3771 0.3713 0.4200 -0.0827 -0.0491 0.0178  1    SER   B OG  
3970 O  OG  B SER   B 1   ? 0.3861 0.3745 0.4377 -0.1210 -0.0777 -0.0020 1    SER   B OG  
3985 N  N   A MET   B 2   ? 0.3301 0.3464 0.3661 -0.0848 -0.0543 0.0563  2    MET   B N   
3986 N  N   B MET   B 2   ? 0.2905 0.3566 0.3333 -0.1373 -0.0944 0.0959  2    MET   B N   
3987 C  CA  A MET   B 2   ? 0.3136 0.3368 0.3630 -0.0780 -0.0519 0.0685  2    MET   B CA  
3988 C  CA  B MET   B 2   ? 0.2693 0.3570 0.3322 -0.1142 -0.0901 0.1189  2    MET   B CA  
3989 C  C   A MET   B 2   ? 0.2818 0.3124 0.3174 -0.0771 -0.0618 0.0823  2    MET   B C   
3990 C  C   B MET   B 2   ? 0.2340 0.3411 0.2912 -0.0928 -0.0984 0.1379  2    MET   B C   
3991 O  O   A MET   B 2   ? 0.2779 0.3153 0.3052 -0.0792 -0.0654 0.0819  2    MET   B O   
3992 O  O   B MET   B 2   ? 0.2283 0.3586 0.3002 -0.0751 -0.1031 0.1235  2    MET   B O   
3993 C  CB  A MET   B 2   ? 0.3318 0.3531 0.4109 -0.0658 -0.0391 0.0598  2    MET   B CB  
3994 C  CB  B MET   B 2   ? 0.2969 0.3823 0.3948 -0.0927 -0.0786 0.1054  2    MET   B CB  
3995 C  CG  A MET   B 2   ? 0.3496 0.3681 0.4559 -0.0525 -0.0264 0.0538  2    MET   B CG  
3996 C  CG  B MET   B 2   ? 0.3235 0.4071 0.4496 -0.0684 -0.0640 0.1068  2    MET   B CG  
3997 S  SD  A MET   B 2   ? 0.3652 0.3810 0.5066 -0.0413 -0.0180 0.0510  2    MET   B SD  
3998 S  SD  B MET   B 2   ? 0.3491 0.4318 0.5001 -0.0481 -0.0600 0.1090  2    MET   B SD  
3999 C  CE  A MET   B 2   ? 0.3681 0.3851 0.5056 -0.0385 -0.0143 0.0527  2    MET   B CE  
4000 C  CE  B MET   B 2   ? 0.3528 0.4382 0.5117 -0.0455 -0.0584 0.0996  2    MET   B CE  
4019 N  N   A VAL   B 3   ? 0.2537 0.2810 0.2912 -0.0767 -0.0619 0.0938  3    VAL   B N   
4020 N  N   B VAL   B 3   ? 0.2061 0.3002 0.2753 -0.0990 -0.0877 0.1554  3    VAL   B N   
4021 C  CA  A VAL   B 3   ? 0.2312 0.2537 0.2713 -0.0693 -0.0587 0.0953  3    VAL   B CA  
4022 C  CA  B VAL   B 3   ? 0.2056 0.2670 0.2850 -0.0766 -0.0704 0.1309  3    VAL   B CA  
4023 C  C   A VAL   B 3   ? 0.2033 0.2344 0.2413 -0.0637 -0.0590 0.1052  3    VAL   B C   
4024 C  C   B VAL   B 3   ? 0.1908 0.2511 0.2581 -0.0634 -0.0624 0.1155  3    VAL   B C   
4025 O  O   A VAL   B 3   ? 0.1993 0.2273 0.2303 -0.0642 -0.0658 0.1240  3    VAL   B O   
4026 O  O   B VAL   B 3   ? 0.1893 0.2636 0.2636 -0.0570 -0.0701 0.1142  3    VAL   B O   
4027 C  CB  A VAL   B 3   ? 0.2393 0.2504 0.2895 -0.0687 -0.0550 0.0850  3    VAL   B CB  
4028 C  CB  B VAL   B 3   ? 0.2273 0.2574 0.3309 -0.0669 -0.0596 0.1153  3    VAL   B CB  
4029 C  CG1 A VAL   B 3   ? 0.2448 0.2504 0.3005 -0.0689 -0.0545 0.0800  3    VAL   B CG1 
4030 C  CG1 B VAL   B 3   ? 0.2413 0.2557 0.3517 -0.0672 -0.0547 0.1077  3    VAL   B CG1 
4031 C  CG2 A VAL   B 3   ? 0.2382 0.2499 0.2942 -0.0690 -0.0531 0.0861  3    VAL   B CG2 
4032 C  CG2 B VAL   B 3   ? 0.2244 0.2559 0.3358 -0.0618 -0.0577 0.1214  3    VAL   B CG2 
4051 N  N   . ASN   B 4   ? 0.1805 0.2228 0.2194 -0.0609 -0.0560 0.0986  4    ASN   B N   
4052 C  CA  . ASN   B 4   ? 0.1820 0.2166 0.1692 -0.0509 -0.0403 0.0509  4    ASN   B CA  
4053 C  C   . ASN   B 4   ? 0.1904 0.2285 0.1625 -0.0534 -0.0292 0.0358  4    ASN   B C   
4054 O  O   . ASN   B 4   ? 0.1890 0.2315 0.1956 -0.0549 -0.0212 0.0071  4    ASN   B O   
4055 C  CB  . ASN   B 4   ? 0.1784 0.2053 0.1556 -0.0490 -0.0410 0.0344  4    ASN   B CB  
4056 C  CG  . ASN   B 4   ? 0.1762 0.1881 0.1482 -0.0465 -0.0385 0.0331  4    ASN   B CG  
4057 O  OD1 . ASN   B 4   ? 0.1736 0.1754 0.1583 -0.0453 -0.0478 0.0354  4    ASN   B OD1 
4058 N  ND2 . ASN   B 4   ? 0.1918 0.1901 0.1634 -0.0234 -0.0309 0.0256  4    ASN   B ND2 
4066 N  N   . SER   B 5   ? 0.1990 0.2412 0.1834 -0.0555 -0.0267 0.0417  5    SER   B N   
4067 C  CA  . SER   B 5   ? 0.2203 0.2733 0.2112 -0.0409 -0.0071 0.0409  5    SER   B CA  
4068 C  C   . SER   B 5   ? 0.2387 0.2749 0.2379 -0.0566 0.0222  0.0287  5    SER   B C   
4069 O  O   . SER   B 5   ? 0.2586 0.2692 0.3176 -0.0572 0.0537  0.0256  5    SER   B O   
4070 C  CB  . SER   B 5   ? 0.2299 0.2933 0.2312 -0.0289 -0.0027 0.0484  5    SER   B CB  
4071 O  OG  . SER   B 5   ? 0.2486 0.3136 0.2831 -0.0195 -0.0017 0.0426  5    SER   B OG  
4077 N  N   . PHE   B 6   ? 0.2534 0.2920 0.2046 -0.0572 0.0404  0.0294  6    PHE   B N   
4078 C  CA  . PHE   B 6   ? 0.2654 0.2979 0.1679 -0.0758 0.0407  0.0114  6    PHE   B CA  
4079 C  C   . PHE   B 6   ? 0.3221 0.3326 0.2080 -0.0851 0.0642  -0.0077 6    PHE   B C   
4080 O  O   . PHE   B 6   ? 0.3383 0.3641 0.2481 -0.0841 0.0487  -0.0245 6    PHE   B O   
4081 C  CB  . PHE   B 6   ? 0.2307 0.2722 0.1531 -0.0711 0.0157  0.0089  6    PHE   B CB  
4082 C  CG  . PHE   B 6   ? 0.2004 0.2411 0.1581 -0.0628 -0.0029 0.0100  6    PHE   B CG  
4083 C  CD1 . PHE   B 6   ? 0.1985 0.2107 0.1469 -0.0559 -0.0075 0.0061  6    PHE   B CD1 
4084 C  CD2 . PHE   B 6   ? 0.1815 0.2385 0.1665 -0.0511 -0.0058 0.0319  6    PHE   B CD2 
4085 C  CE1 . PHE   B 6   ? 0.1895 0.1932 0.1584 -0.0456 -0.0021 0.0033  6    PHE   B CE1 
4086 C  CE2 . PHE   B 6   ? 0.1766 0.2226 0.1858 -0.0353 0.0126  0.0336  6    PHE   B CE2 
4087 C  CZ  . PHE   B 6   ? 0.1764 0.1988 0.1722 -0.0423 0.0051  0.0072  6    PHE   B CZ  
4097 N  N   . SER   B 7   ? 0.3613 0.3190 0.2295 -0.1028 0.1001  -0.0197 7    SER   B N   
4098 C  CA  . SER   B 7   ? 0.3938 0.3264 0.2846 -0.1037 0.1228  -0.0275 7    SER   B CA  
4099 C  C   . SER   B 7   ? 0.3898 0.3055 0.2788 -0.1116 0.1360  -0.0429 7    SER   B C   
4100 O  O   . SER   B 7   ? 0.3920 0.3032 0.3250 -0.1170 0.1252  -0.0413 7    SER   B O   
4101 C  CB  . SER   B 7   ? 0.4152 0.3542 0.3593 -0.0999 0.1300  -0.0242 7    SER   B CB  
4102 O  OG  . SER   B 7   ? 0.4297 0.3740 0.4269 -0.0957 0.1251  -0.0183 7    SER   B OG  
4108 N  N   . GLY   B 8   ? 0.3894 0.2936 0.2888 -0.0997 0.1461  -0.0586 8    GLY   B N   
4109 C  CA  . GLY   B 8   ? 0.3736 0.2728 0.2863 -0.0942 0.1489  -0.0636 8    GLY   B CA  
4110 C  C   . GLY   B 8   ? 0.3481 0.2449 0.2780 -0.0885 0.1431  -0.0551 8    GLY   B C   
4111 O  O   . GLY   B 8   ? 0.3566 0.2525 0.3081 -0.0783 0.1417  -0.0587 8    GLY   B O   
4115 N  N   . TYR   B 9   ? 0.3208 0.2188 0.2552 -0.0765 0.1169  -0.0660 9    TYR   B N   
4116 C  CA  . TYR   B 9   ? 0.2952 0.1925 0.2226 -0.0607 0.0824  -0.0474 9    TYR   B CA  
4117 C  C   . TYR   B 9   ? 0.2880 0.1981 0.1979 -0.0541 0.0448  -0.0306 9    TYR   B C   
4118 O  O   . TYR   B 9   ? 0.3050 0.2259 0.2313 -0.0638 0.0502  -0.0086 9    TYR   B O   
4119 C  CB  . TYR   B 9   ? 0.2865 0.1753 0.2289 -0.0526 0.0784  -0.0383 9    TYR   B CB  
4120 C  CG  . TYR   B 9   ? 0.2769 0.1629 0.2344 -0.0548 0.0739  -0.0382 9    TYR   B CG  
4121 C  CD1 . TYR   B 9   ? 0.2831 0.1631 0.2477 -0.0675 0.0780  -0.0393 9    TYR   B CD1 
4122 C  CD2 . TYR   B 9   ? 0.2628 0.1576 0.2269 -0.0507 0.0702  -0.0454 9    TYR   B CD2 
4123 C  CE1 . TYR   B 9   ? 0.2789 0.1765 0.2468 -0.0751 0.0785  -0.0513 9    TYR   B CE1 
4124 C  CE2 . TYR   B 9   ? 0.2649 0.1652 0.2352 -0.0566 0.0689  -0.0451 9    TYR   B CE2 
4125 C  CZ  . TYR   B 9   ? 0.2734 0.1804 0.2448 -0.0717 0.0794  -0.0617 9    TYR   B CZ  
4126 O  OH  . TYR   B 9   ? 0.2804 0.1975 0.2608 -0.0840 0.0770  -0.0744 9    TYR   B OH  
4136 N  N   . LEU   B 10  ? 0.2594 0.1736 0.1753 -0.0433 0.0172  -0.0352 10   LEU   B N   
4137 C  CA  . LEU   B 10  ? 0.2548 0.1699 0.1732 -0.0479 -0.0094 -0.0326 10   LEU   B CA  
4138 C  C   . LEU   B 10  ? 0.2413 0.1665 0.1773 -0.0447 -0.0171 -0.0295 10   LEU   B C   
4139 O  O   . LEU   B 10  ? 0.2285 0.1711 0.1801 -0.0342 -0.0077 -0.0238 10   LEU   B O   
4140 C  CB  . LEU   B 10  ? 0.2717 0.1696 0.1968 -0.0506 -0.0237 -0.0132 10   LEU   B CB  
4141 C  CG  . LEU   B 10  ? 0.2888 0.1797 0.2289 -0.0423 -0.0559 -0.0000 10   LEU   B CG  
4142 C  CD1 . LEU   B 10  ? 0.3004 0.1905 0.2483 -0.0395 -0.0520 -0.0005 10   LEU   B CD1 
4143 C  CD2 . LEU   B 10  ? 0.2932 0.1823 0.2574 -0.0444 -0.0611 0.0170  10   LEU   B CD2 
4155 N  N   . LYS   B 11  ? 0.2578 0.1890 0.1832 -0.0348 -0.0235 -0.0195 11   LYS   B N   
4156 C  CA  . LYS   B 11  ? 0.2808 0.2203 0.2086 -0.0288 -0.0389 -0.0225 11   LYS   B CA  
4157 C  C   . LYS   B 11  ? 0.2664 0.2030 0.2124 -0.0569 -0.0321 -0.0280 11   LYS   B C   
4158 O  O   . LYS   B 11  ? 0.2840 0.2236 0.2508 -0.0784 -0.0306 -0.0602 11   LYS   B O   
4159 C  CB  . LYS   B 11  ? 0.3203 0.2758 0.2764 -0.0017 -0.0488 -0.0285 11   LYS   B CB  
4160 C  CG  . LYS   B 11  ? 0.3550 0.3108 0.3499 0.0133  -0.0503 -0.0366 11   LYS   B CG  
4161 C  CD  . LYS   B 11  ? 0.3855 0.3342 0.4205 0.0219  -0.0515 -0.0429 11   LYS   B CD  
4162 C  CE  . LYS   B 11  ? 0.4097 0.3501 0.4747 0.0206  -0.0557 -0.0492 11   LYS   B CE  
4163 N  NZ  . LYS   B 11  ? 0.4233 0.3599 0.5056 0.0177  -0.0597 -0.0496 11   LYS   B NZ  
4177 N  N   . LEU   B 12  ? 0.2364 0.1829 0.2085 -0.0492 -0.0301 -0.0279 12   LEU   B N   
4178 C  CA  . LEU   B 12  ? 0.2190 0.1649 0.2299 -0.0437 -0.0164 -0.0304 12   LEU   B CA  
4179 C  C   . LEU   B 12  ? 0.2015 0.1650 0.2380 -0.0461 -0.0320 -0.0289 12   LEU   B C   
4180 O  O   . LEU   B 12  ? 0.2010 0.1716 0.2681 -0.0559 -0.0498 -0.0217 12   LEU   B O   
4181 C  CB  . LEU   B 12  ? 0.2175 0.1470 0.2240 -0.0338 -0.0078 -0.0326 12   LEU   B CB  
4182 C  CG  . LEU   B 12  ? 0.2166 0.1505 0.2273 -0.0359 -0.0124 -0.0262 12   LEU   B CG  
4183 C  CD1 . LEU   B 12  ? 0.2279 0.1560 0.2209 -0.0234 -0.0196 -0.0117 12   LEU   B CD1 
4184 C  CD2 . LEU   B 12  ? 0.2181 0.1572 0.2404 -0.0372 -0.0131 -0.0298 12   LEU   B CD2 
4196 N  N   . THR   B 13  ? 0.1924 0.1715 0.2319 -0.0430 -0.0388 -0.0341 13   THR   B N   
4197 C  CA  . THR   B 13  ? 0.1928 0.1794 0.2190 -0.0509 -0.0460 -0.0261 13   THR   B CA  
4198 C  C   . THR   B 13  ? 0.2263 0.1980 0.2370 -0.0580 -0.0612 -0.0177 13   THR   B C   
4199 O  O   . THR   B 13  ? 0.2434 0.1995 0.2610 -0.0518 -0.0256 -0.0255 13   THR   B O   
4200 C  CB  . THR   B 13  ? 0.1828 0.1865 0.2265 -0.0492 -0.0428 -0.0163 13   THR   B CB  
4201 O  OG1 . THR   B 13  ? 0.1764 0.1797 0.2359 -0.0472 -0.0332 -0.0159 13   THR   B OG1 
4202 C  CG2 . THR   B 13  ? 0.1963 0.1944 0.2456 -0.0430 -0.0310 -0.0142 13   THR   B CG2 
4210 N  N   A ASP   B 14  ? 0.2370 0.2073 0.2579 -0.0586 -0.0728 -0.0072 14   ASP   B N   
4211 N  N   B ASP   B 14  ? 0.2402 0.2138 0.2467 -0.0643 -0.0953 -0.0031 14   ASP   B N   
4212 C  CA  A ASP   B 14  ? 0.2494 0.2173 0.2775 -0.0589 -0.0755 0.0018  14   ASP   B CA  
4213 C  CA  B ASP   B 14  ? 0.2569 0.2305 0.2580 -0.0654 -0.1068 0.0140  14   ASP   B CA  
4214 C  C   A ASP   B 14  ? 0.2400 0.2033 0.2418 -0.0591 -0.0699 0.0127  14   ASP   B C   
4215 C  C   B ASP   B 14  ? 0.2489 0.2112 0.2301 -0.0669 -0.0842 0.0236  14   ASP   B C   
4216 O  O   A ASP   B 14  ? 0.2558 0.2155 0.2498 -0.0625 -0.0660 0.0206  14   ASP   B O   
4217 O  O   B ASP   B 14  ? 0.2793 0.2318 0.2468 -0.0735 -0.0729 0.0389  14   ASP   B O   
4218 C  CB  A ASP   B 14  ? 0.2709 0.2425 0.3416 -0.0579 -0.0787 -0.0007 14   ASP   B CB  
4219 C  CB  B ASP   B 14  ? 0.2810 0.2701 0.3334 -0.0596 -0.1201 0.0160  14   ASP   B CB  
4220 C  CG  A ASP   B 14  ? 0.2916 0.2646 0.3960 -0.0563 -0.0750 -0.0059 14   ASP   B CG  
4221 C  CG  B ASP   B 14  ? 0.3090 0.3073 0.4060 -0.0510 -0.1068 0.0092  14   ASP   B CG  
4222 O  OD1 A ASP   B 14  ? 0.2998 0.2675 0.4062 -0.0621 -0.0771 -0.0138 14   ASP   B OD1 
4223 O  OD1 B ASP   B 14  ? 0.3234 0.3155 0.4150 -0.0510 -0.1002 -0.0038 14   ASP   B OD1 
4224 O  OD2 A ASP   B 14  ? 0.2976 0.2756 0.4190 -0.0537 -0.0701 -0.0028 14   ASP   B OD2 
4225 O  OD2 B ASP   B 14  ? 0.3170 0.3219 0.4400 -0.0489 -0.0975 0.0157  14   ASP   B OD2 
4234 N  N   . ASN   B 15  ? 0.2163 0.1835 0.2061 -0.0511 -0.0675 0.0195  15   ASN   B N   
4235 C  CA  . ASN   B 15  ? 0.1749 0.1603 0.1975 -0.0303 -0.0395 0.0037  15   ASN   B CA  
4236 C  C   . ASN   B 15  ? 0.1565 0.1480 0.1873 -0.0214 -0.0316 -0.0042 15   ASN   B C   
4237 O  O   . ASN   B 15  ? 0.1537 0.1430 0.2039 -0.0265 -0.0348 -0.0143 15   ASN   B O   
4238 C  CB  . ASN   B 15  ? 0.1674 0.1532 0.2162 -0.0110 -0.0449 0.0019  15   ASN   B CB  
4239 C  CG  . ASN   B 15  ? 0.1580 0.1597 0.2146 -0.0192 -0.0231 0.0076  15   ASN   B CG  
4240 O  OD1 . ASN   B 15  ? 0.1574 0.1875 0.2590 -0.0366 -0.0298 0.0068  15   ASN   B OD1 
4241 N  ND2 . ASN   B 15  ? 0.1582 0.1388 0.2130 -0.0136 0.0081  -0.0083 15   ASN   B ND2 
4249 N  N   . VAL   B 16  ? 0.1568 0.1398 0.2012 -0.0307 -0.0449 -0.0020 16   VAL   B N   
4250 C  CA  . VAL   B 16  ? 0.1583 0.1398 0.1839 -0.0263 -0.0292 -0.0173 16   VAL   B CA  
4251 C  C   . VAL   B 16  ? 0.1637 0.1436 0.1850 -0.0323 -0.0300 -0.0172 16   VAL   B C   
4252 O  O   . VAL   B 16  ? 0.1688 0.1522 0.2059 -0.0286 -0.0281 -0.0265 16   VAL   B O   
4253 C  CB  . VAL   B 16  ? 0.1645 0.1428 0.1948 -0.0143 -0.0138 -0.0171 16   VAL   B CB  
4254 C  CG1 . VAL   B 16  ? 0.1738 0.1442 0.1897 -0.0027 -0.0058 -0.0142 16   VAL   B CG1 
4255 C  CG2 . VAL   B 16  ? 0.1680 0.1429 0.2076 -0.0066 -0.0108 -0.0204 16   VAL   B CG2 
4265 N  N   . TYR   B 17  ? 0.1682 0.1519 0.1762 -0.0330 -0.0200 -0.0189 17   TYR   B N   
4266 C  CA  . TYR   B 17  ? 0.1712 0.1715 0.1716 -0.0362 -0.0194 -0.0021 17   TYR   B CA  
4267 C  C   . TYR   B 17  ? 0.1658 0.1427 0.1710 -0.0351 -0.0160 -0.0112 17   TYR   B C   
4268 O  O   . TYR   B 17  ? 0.1671 0.1494 0.1744 -0.0265 -0.0234 -0.0336 17   TYR   B O   
4269 C  CB  . TYR   B 17  ? 0.1928 0.2089 0.1968 -0.0217 -0.0171 0.0300  17   TYR   B CB  
4270 C  CG  . TYR   B 17  ? 0.2205 0.2515 0.2295 -0.0143 -0.0269 0.0423  17   TYR   B CG  
4271 C  CD1 . TYR   B 17  ? 0.2371 0.2660 0.2558 -0.0148 -0.0414 0.0495  17   TYR   B CD1 
4272 C  CD2 . TYR   B 17  ? 0.2427 0.2815 0.2517 -0.0064 -0.0421 0.0428  17   TYR   B CD2 
4273 C  CE1 . TYR   B 17  ? 0.2594 0.2946 0.2719 -0.0071 -0.0538 0.0464  17   TYR   B CE1 
4274 C  CE2 . TYR   B 17  ? 0.2641 0.3029 0.2767 0.0032  -0.0569 0.0464  17   TYR   B CE2 
4275 C  CZ  . TYR   B 17  ? 0.2726 0.3180 0.2810 0.0046  -0.0646 0.0490  17   TYR   B CZ  
4276 O  OH  . TYR   B 17  ? 0.2890 0.3421 0.3018 0.0128  -0.0681 0.0497  17   TYR   B OH  
4286 N  N   . ILE   B 18  ? 0.1721 0.1428 0.1623 -0.0293 -0.0025 -0.0172 18   ILE   B N   
4287 C  CA  . ILE   B 18  ? 0.1741 0.1429 0.1615 -0.0298 -0.0066 -0.0190 18   ILE   B CA  
4288 C  C   . ILE   B 18  ? 0.1867 0.1482 0.1512 -0.0383 -0.0041 -0.0255 18   ILE   B C   
4289 O  O   . ILE   B 18  ? 0.2060 0.1607 0.1670 -0.0363 0.0064  -0.0246 18   ILE   B O   
4290 C  CB  . ILE   B 18  ? 0.1793 0.1464 0.1780 -0.0385 -0.0087 -0.0200 18   ILE   B CB  
4291 C  CG1 . ILE   B 18  ? 0.1860 0.1572 0.1920 -0.0395 0.0003  -0.0092 18   ILE   B CG1 
4292 C  CG2 . ILE   B 18  ? 0.1877 0.1543 0.1865 -0.0354 -0.0147 -0.0179 18   ILE   B CG2 
4293 C  CD1 . ILE   B 18  ? 0.1948 0.1816 0.2172 -0.0423 -0.0104 0.0122  18   ILE   B CD1 
4305 N  N   . LYS   B 19  ? 0.1897 0.1464 0.1737 -0.0243 0.0253  -0.0303 19   LYS   B N   
4306 C  CA  . LYS   B 19  ? 0.1951 0.1537 0.1878 -0.0270 0.0180  -0.0357 19   LYS   B CA  
4307 C  C   . LYS   B 19  ? 0.1840 0.1548 0.2105 -0.0216 0.0257  -0.0463 19   LYS   B C   
4308 O  O   . LYS   B 19  ? 0.1799 0.1615 0.1964 -0.0148 0.0272  -0.0448 19   LYS   B O   
4309 C  CB  . LYS   B 19  ? 0.2096 0.1713 0.1981 -0.0308 0.0295  -0.0242 19   LYS   B CB  
4310 C  CG  . LYS   B 19  ? 0.2314 0.1964 0.2230 -0.0394 0.0453  -0.0242 19   LYS   B CG  
4311 C  CD  . LYS   B 19  ? 0.2625 0.2284 0.2288 -0.0432 0.0527  -0.0230 19   LYS   B CD  
4312 C  CE  . LYS   B 19  ? 0.2908 0.2522 0.2604 -0.0404 0.0541  -0.0294 19   LYS   B CE  
4313 N  NZ  . LYS   B 19  ? 0.3102 0.2661 0.2646 -0.0412 0.0499  -0.0315 19   LYS   B NZ  
4327 N  N   . ASN   B 20  ? 0.1808 0.1592 0.2226 -0.0172 0.0306  -0.0597 20   ASN   B N   
4328 C  CA  . ASN   B 20  ? 0.1808 0.1721 0.2390 -0.0083 0.0350  -0.0693 20   ASN   B CA  
4329 C  C   . ASN   B 20  ? 0.1810 0.1886 0.2450 -0.0173 0.0480  -0.0700 20   ASN   B C   
4330 O  O   . ASN   B 20  ? 0.1992 0.2245 0.2660 -0.0280 0.0455  -0.0696 20   ASN   B O   
4331 C  CB  . ASN   B 20  ? 0.2063 0.1800 0.2807 0.0115  0.0161  -0.0659 20   ASN   B CB  
4332 C  CG  . ASN   B 20  ? 0.2323 0.1884 0.3073 0.0392  0.0112  -0.0748 20   ASN   B CG  
4333 O  OD1 . ASN   B 20  ? 0.2562 0.2212 0.3315 0.0560  0.0045  -0.0808 20   ASN   B OD1 
4334 N  ND2 . ASN   B 20  ? 0.2277 0.1831 0.3013 0.0316  0.0109  -0.0582 20   ASN   B ND2 
4341 N  N   . ALA   B 21  ? 0.1839 0.1787 0.2257 -0.0244 0.0466  -0.0588 21   ALA   B N   
4342 C  CA  . ALA   B 21  ? 0.1871 0.1813 0.2503 -0.0279 0.0379  -0.0502 21   ALA   B CA  
4343 C  C   . ALA   B 21  ? 0.1830 0.1610 0.2534 -0.0183 0.0338  -0.0331 21   ALA   B C   
4344 O  O   . ALA   B 21  ? 0.1916 0.1494 0.2387 -0.0298 0.0313  -0.0275 21   ALA   B O   
4345 C  CB  . ALA   B 21  ? 0.2047 0.2057 0.2659 -0.0405 0.0317  -0.0337 21   ALA   B CB  
4351 N  N   . ASP   B 22  ? 0.1716 0.1586 0.2423 -0.0186 0.0311  -0.0308 22   ASP   B N   
4352 C  CA  . ASP   B 22  ? 0.1699 0.1453 0.2204 -0.0068 0.0164  -0.0232 22   ASP   B CA  
4353 C  C   . ASP   B 22  ? 0.1684 0.1478 0.1770 -0.0144 0.0196  -0.0063 22   ASP   B C   
4354 O  O   . ASP   B 22  ? 0.1740 0.1495 0.1850 -0.0126 0.0163  -0.0062 22   ASP   B O   
4355 C  CB  . ASP   B 22  ? 0.1817 0.1528 0.2621 -0.0021 0.0138  -0.0190 22   ASP   B CB  
4356 C  CG  . ASP   B 22  ? 0.1827 0.1712 0.3072 0.0056  0.0005  -0.0138 22   ASP   B CG  
4357 O  OD1 . ASP   B 22  ? 0.1957 0.1661 0.3086 0.0041  -0.0179 -0.0111 22   ASP   B OD1 
4358 O  OD2 . ASP   B 22  ? 0.1903 0.2021 0.3683 0.0157  -0.0157 -0.0320 22   ASP   B OD2 
4363 N  N   . ILE   B 23  ? 0.1782 0.1399 0.1661 -0.0105 0.0083  0.0048  23   ILE   B N   
4364 C  CA  . ILE   B 23  ? 0.1665 0.1348 0.1635 -0.0117 0.0008  -0.0004 23   ILE   B CA  
4365 C  C   . ILE   B 23  ? 0.1617 0.1356 0.1652 -0.0046 -0.0094 0.0030  23   ILE   B C   
4366 O  O   . ILE   B 23  ? 0.1518 0.1363 0.1568 -0.0053 -0.0075 0.0036  23   ILE   B O   
4367 C  CB  . ILE   B 23  ? 0.1569 0.1382 0.1651 -0.0174 0.0052  0.0104  23   ILE   B CB  
4368 C  CG1 . ILE   B 23  ? 0.1590 0.1549 0.1786 -0.0132 0.0051  0.0184  23   ILE   B CG1 
4369 C  CG2 . ILE   B 23  ? 0.1661 0.1553 0.1783 -0.0131 0.0005  0.0075  23   ILE   B CG2 
4370 C  CD1 . ILE   B 23  ? 0.1700 0.1691 0.1905 0.0000  0.0137  0.0207  23   ILE   B CD1 
4382 N  N   . VAL   B 24  ? 0.1635 0.1375 0.1606 -0.0061 -0.0086 0.0007  24   VAL   B N   
4383 C  CA  . VAL   B 24  ? 0.1558 0.1450 0.1877 -0.0069 -0.0113 -0.0012 24   VAL   B CA  
4384 C  C   . VAL   B 24  ? 0.1558 0.1415 0.1899 -0.0109 -0.0094 0.0029  24   VAL   B C   
4385 O  O   . VAL   B 24  ? 0.1529 0.1510 0.1986 -0.0168 -0.0040 0.0174  24   VAL   B O   
4386 C  CB  . VAL   B 24  ? 0.1660 0.1667 0.1925 0.0022  -0.0222 -0.0056 24   VAL   B CB  
4387 C  CG1 . VAL   B 24  ? 0.1662 0.1685 0.2078 -0.0103 -0.0296 -0.0033 24   VAL   B CG1 
4388 C  CG2 . VAL   B 24  ? 0.1752 0.1960 0.1982 0.0088  -0.0247 -0.0093 24   VAL   B CG2 
4398 N  N   . GLU   B 25  ? 0.1785 0.1534 0.1914 -0.0092 0.0015  -0.0013 25   GLU   B N   
4399 C  CA  . GLU   B 25  ? 0.1914 0.1830 0.2177 0.0052  0.0160  -0.0075 25   GLU   B CA  
4400 C  C   . GLU   B 25  ? 0.1802 0.1747 0.1860 -0.0079 0.0138  -0.0044 25   GLU   B C   
4401 O  O   . GLU   B 25  ? 0.1808 0.1866 0.2017 -0.0122 0.0329  0.0019  25   GLU   B O   
4402 C  CB  . GLU   B 25  ? 0.2489 0.2391 0.2902 0.0333  0.0303  -0.0155 25   GLU   B CB  
4403 C  CG  . GLU   B 25  ? 0.3171 0.3133 0.4201 0.0408  0.0317  -0.0184 25   GLU   B CG  
4404 C  CD  . GLU   B 25  ? 0.3670 0.3835 0.5274 0.0371  0.0269  -0.0192 25   GLU   B CD  
4405 O  OE1 . GLU   B 25  ? 0.4007 0.4225 0.5577 0.0396  0.0293  -0.0196 25   GLU   B OE1 
4406 O  OE2 . GLU   B 25  ? 0.3987 0.4175 0.5606 0.0322  0.0205  -0.0215 25   GLU   B OE2 
4413 N  N   . GLU   B 26  ? 0.1737 0.1686 0.1736 -0.0252 0.0133  -0.0004 26   GLU   B N   
4414 C  CA  . GLU   B 26  ? 0.1727 0.1809 0.1810 -0.0323 -0.0032 -0.0002 26   GLU   B CA  
4415 C  C   . GLU   B 26  ? 0.1585 0.1747 0.1666 -0.0242 0.0029  0.0102  26   GLU   B C   
4416 O  O   . GLU   B 26  ? 0.1765 0.1983 0.1708 -0.0206 -0.0007 0.0204  26   GLU   B O   
4417 C  CB  . GLU   B 26  ? 0.2057 0.2031 0.1970 -0.0424 0.0023  0.0097  26   GLU   B CB  
4418 C  CG  . GLU   B 26  ? 0.2469 0.2360 0.2632 -0.0467 0.0087  -0.0192 26   GLU   B CG  
4419 C  CD  . GLU   B 26  ? 0.2696 0.2591 0.2669 -0.0670 0.0280  -0.0515 26   GLU   B CD  
4420 O  OE1 . GLU   B 26  ? 0.2883 0.2415 0.2642 -0.0750 0.0717  -0.0528 26   GLU   B OE1 
4421 O  OE2 . GLU   B 26  ? 0.2743 0.2988 0.3215 -0.0595 0.0255  -0.0447 26   GLU   B OE2 
4428 N  N   . ALA   B 27  ? 0.1459 0.1572 0.1608 -0.0196 0.0055  0.0187  27   ALA   B N   
4429 C  CA  . ALA   B 27  ? 0.1498 0.1584 0.1793 -0.0106 -0.0019 0.0352  27   ALA   B CA  
4430 C  C   . ALA   B 27  ? 0.1534 0.1711 0.2054 -0.0119 0.0182  0.0433  27   ALA   B C   
4431 O  O   . ALA   B 27  ? 0.1588 0.1791 0.2144 -0.0036 0.0164  0.0438  27   ALA   B O   
4432 C  CB  . ALA   B 27  ? 0.1660 0.1476 0.1788 -0.0104 0.0003  0.0365  27   ALA   B CB  
4438 N  N   . LYS   B 28  ? 0.1477 0.1887 0.2430 -0.0181 0.0216  0.0547  28   LYS   B N   
4439 C  CA  . LYS   B 28  ? 0.1643 0.2246 0.2694 -0.0106 0.0571  0.0836  28   LYS   B CA  
4440 C  C   . LYS   B 28  ? 0.1883 0.2408 0.2518 0.0017  0.0659  0.0740  28   LYS   B C   
4441 O  O   . LYS   B 28  ? 0.2103 0.2439 0.2594 -0.0001 0.0672  0.0721  28   LYS   B O   
4442 C  CB  . LYS   B 28  ? 0.1924 0.2659 0.3381 0.0008  0.0852  0.1053  28   LYS   B CB  
4443 C  CG  . LYS   B 28  ? 0.2299 0.3158 0.3885 0.0164  0.0981  0.1199  28   LYS   B CG  
4444 C  CD  . LYS   B 28  ? 0.2935 0.3784 0.4476 0.0211  0.1186  0.1288  28   LYS   B CD  
4445 C  CE  . LYS   B 28  ? 0.3612 0.4341 0.5027 0.0259  0.1196  0.1362  28   LYS   B CE  
4446 N  NZ  . LYS   B 28  ? 0.4068 0.4684 0.5186 0.0280  0.1128  0.1421  28   LYS   B NZ  
4460 N  N   . LYS   B 29  ? 0.2051 0.2659 0.2486 0.0226  0.0606  0.0646  29   LYS   B N   
4461 C  CA  . LYS   B 29  ? 0.2425 0.3017 0.2765 0.0251  0.0605  0.0656  29   LYS   B CA  
4462 C  C   . LYS   B 29  ? 0.2330 0.3004 0.2399 0.0193  0.0435  0.0801  29   LYS   B C   
4463 O  O   . LYS   B 29  ? 0.2506 0.3250 0.2450 0.0249  0.0354  0.0806  29   LYS   B O   
4464 C  CB  . LYS   B 29  ? 0.2969 0.3468 0.3608 0.0283  0.0618  0.0480  29   LYS   B CB  
4465 C  CG  . LYS   B 29  ? 0.3465 0.3863 0.4543 0.0260  0.0612  0.0405  29   LYS   B CG  
4466 C  CD  . LYS   B 29  ? 0.3932 0.4191 0.5320 0.0198  0.0696  0.0332  29   LYS   B CD  
4467 C  CE  . LYS   B 29  ? 0.4365 0.4494 0.5793 0.0144  0.0789  0.0291  29   LYS   B CE  
4468 N  NZ  . LYS   B 29  ? 0.4613 0.4661 0.6185 0.0119  0.0809  0.0258  29   LYS   B NZ  
4482 N  N   . VAL   B 30  ? 0.2065 0.2770 0.2277 0.0012  0.0355  0.0854  30   VAL   B N   
4483 C  CA  . VAL   B 30  ? 0.1989 0.2690 0.2719 -0.0113 0.0016  0.0860  30   VAL   B CA  
4484 C  C   . VAL   B 30  ? 0.1790 0.2615 0.2686 -0.0127 0.0105  0.1074  30   VAL   B C   
4485 O  O   . VAL   B 30  ? 0.1905 0.2778 0.2723 -0.0079 0.0196  0.1188  30   VAL   B O   
4486 C  CB  . VAL   B 30  ? 0.2091 0.2635 0.3129 -0.0267 -0.0234 0.0794  30   VAL   B CB  
4487 C  CG1 . VAL   B 30  ? 0.2182 0.2685 0.3197 -0.0267 -0.0225 0.0721  30   VAL   B CG1 
4488 C  CG2 . VAL   B 30  ? 0.2206 0.2653 0.3411 -0.0334 -0.0326 0.0595  30   VAL   B CG2 
4498 N  N   . LYS   B 31  ? 0.1661 0.2260 0.2971 -0.0230 0.0112  0.1115  31   LYS   B N   
4499 C  CA  . LYS   B 31  ? 0.1570 0.2219 0.3331 -0.0298 0.0056  0.1133  31   LYS   B CA  
4500 C  C   . LYS   B 31  ? 0.1502 0.1905 0.2791 -0.0341 -0.0221 0.0905  31   LYS   B C   
4501 O  O   . LYS   B 31  ? 0.1560 0.2075 0.3008 -0.0214 -0.0167 0.1081  31   LYS   B O   
4502 C  CB  . LYS   B 31  ? 0.1680 0.2666 0.3954 -0.0197 0.0337  0.1238  31   LYS   B CB  
4503 C  CG  . LYS   B 31  ? 0.2043 0.3099 0.4353 -0.0221 0.0596  0.1236  31   LYS   B CG  
4504 C  CD  . LYS   B 31  ? 0.2520 0.3608 0.4764 -0.0201 0.0705  0.1079  31   LYS   B CD  
4505 C  CE  . LYS   B 31  ? 0.2847 0.4003 0.5192 -0.0191 0.0665  0.0930  31   LYS   B CE  
4506 N  NZ  . LYS   B 31  ? 0.3189 0.4305 0.5295 -0.0134 0.0561  0.0840  31   LYS   B NZ  
4520 N  N   . PRO   B 32  ? 0.1622 0.1516 0.2065 -0.0362 -0.0361 0.0505  32   PRO   B N   
4521 C  CA  . PRO   B 32  ? 0.1661 0.1505 0.1692 -0.0372 -0.0387 0.0295  32   PRO   B CA  
4522 C  C   . PRO   B 32  ? 0.1802 0.1431 0.1721 -0.0357 -0.0489 0.0368  32   PRO   B C   
4523 O  O   . PRO   B 32  ? 0.1908 0.1374 0.2107 -0.0380 -0.0687 0.0381  32   PRO   B O   
4524 C  CB  . PRO   B 32  ? 0.1861 0.1436 0.1672 -0.0420 -0.0291 0.0134  32   PRO   B CB  
4525 C  CG  . PRO   B 32  ? 0.2007 0.1341 0.1742 -0.0327 -0.0435 0.0200  32   PRO   B CG  
4526 C  CD  . PRO   B 32  ? 0.1852 0.1385 0.1979 -0.0257 -0.0512 0.0291  32   PRO   B CD  
4534 N  N   . THR   B 33  ? 0.1854 0.1349 0.1418 -0.0342 -0.0462 0.0243  33   THR   B N   
4535 C  CA  . THR   B 33  ? 0.1953 0.1394 0.1419 -0.0406 -0.0433 0.0275  33   THR   B CA  
4536 C  C   . THR   B 33  ? 0.2000 0.1290 0.1389 -0.0387 -0.0427 0.0146  33   THR   B C   
4537 O  O   . THR   B 33  ? 0.2191 0.1376 0.1562 -0.0478 -0.0504 0.0216  33   THR   B O   
4538 C  CB  . THR   B 33  ? 0.2015 0.1469 0.1564 -0.0218 -0.0473 0.0302  33   THR   B CB  
4539 O  OG1 . THR   B 33  ? 0.1879 0.1580 0.1706 -0.0240 -0.0421 0.0370  33   THR   B OG1 
4540 C  CG2 . THR   B 33  ? 0.2283 0.1549 0.1695 -0.0141 -0.0462 0.0186  33   THR   B CG2 
4548 N  N   . VAL   B 34  ? 0.1784 0.1246 0.1341 -0.0317 -0.0377 0.0101  34   VAL   B N   
4549 C  CA  . VAL   B 34  ? 0.1653 0.1235 0.1306 -0.0272 -0.0341 0.0046  34   VAL   B CA  
4550 C  C   . VAL   B 34  ? 0.1502 0.1199 0.1153 -0.0277 -0.0194 0.0083  34   VAL   B C   
4551 O  O   . VAL   B 34  ? 0.1696 0.1253 0.1193 -0.0229 -0.0279 0.0059  34   VAL   B O   
4552 C  CB  . VAL   B 34  ? 0.1676 0.1337 0.1647 -0.0119 -0.0282 0.0030  34   VAL   B CB  
4553 C  CG1 . VAL   B 34  ? 0.1607 0.1496 0.1662 -0.0075 -0.0106 0.0073  34   VAL   B CG1 
4554 C  CG2 . VAL   B 34  ? 0.1763 0.1448 0.1938 -0.0141 -0.0319 0.0056  34   VAL   B CG2 
4564 N  N   . VAL   B 35  ? 0.1425 0.1173 0.1129 -0.0244 -0.0135 0.0095  35   VAL   B N   
4565 C  CA  . VAL   B 35  ? 0.1371 0.1195 0.1088 -0.0169 -0.0066 0.0044  35   VAL   B CA  
4566 C  C   . VAL   B 35  ? 0.1298 0.1132 0.1068 -0.0175 -0.0105 0.0014  35   VAL   B C   
4567 O  O   . VAL   B 35  ? 0.1317 0.1212 0.1271 -0.0188 -0.0026 -0.0020 35   VAL   B O   
4568 C  CB  . VAL   B 35  ? 0.1367 0.1348 0.1174 -0.0136 0.0071  0.0049  35   VAL   B CB  
4569 C  CG1 . VAL   B 35  ? 0.1290 0.1435 0.1482 -0.0214 -0.0026 -0.0001 35   VAL   B CG1 
4570 C  CG2 . VAL   B 35  ? 0.1409 0.1394 0.1429 -0.0078 -0.0018 0.0018  35   VAL   B CG2 
4580 N  N   . VAL   B 36  ? 0.1356 0.1124 0.1101 -0.0161 -0.0145 0.0045  36   VAL   B N   
4581 C  CA  . VAL   B 36  ? 0.1277 0.1114 0.1096 -0.0120 0.0010  0.0047  36   VAL   B CA  
4582 C  C   . VAL   B 36  ? 0.1207 0.1153 0.0964 -0.0084 0.0040  0.0060  36   VAL   B C   
4583 O  O   . VAL   B 36  ? 0.1295 0.1251 0.1231 -0.0085 0.0017  -0.0051 36   VAL   B O   
4584 C  CB  . VAL   B 36  ? 0.1279 0.1141 0.1184 -0.0149 -0.0032 0.0031  36   VAL   B CB  
4585 C  CG1 . VAL   B 36  ? 0.1268 0.1333 0.1329 -0.0141 -0.0042 0.0069  36   VAL   B CG1 
4586 C  CG2 . VAL   B 36  ? 0.1301 0.1226 0.1391 -0.0130 -0.0120 0.0078  36   VAL   B CG2 
4596 N  N   . ASN   B 37  ? 0.1280 0.1182 0.1039 0.0006  -0.0040 0.0035  37   ASN   B N   
4597 C  CA  . ASN   B 37  ? 0.1259 0.1174 0.1111 0.0035  -0.0098 -0.0005 37   ASN   B CA  
4598 C  C   . ASN   B 37  ? 0.1272 0.1231 0.1074 0.0086  -0.0038 -0.0036 37   ASN   B C   
4599 O  O   . ASN   B 37  ? 0.1371 0.1267 0.1245 0.0049  0.0055  0.0082  37   ASN   B O   
4600 C  CB  . ASN   B 37  ? 0.1287 0.1215 0.1164 0.0060  -0.0103 0.0022  37   ASN   B CB  
4601 C  CG  . ASN   B 37  ? 0.1277 0.1259 0.1233 0.0039  -0.0069 0.0043  37   ASN   B CG  
4602 O  OD1 . ASN   B 37  ? 0.1381 0.1257 0.1345 0.0156  -0.0102 0.0014  37   ASN   B OD1 
4603 N  ND2 . ASN   B 37  ? 0.1351 0.1221 0.1285 0.0011  -0.0147 0.0027  37   ASN   B ND2 
4610 N  N   . ALA   B 38  ? 0.1387 0.1206 0.1125 0.0091  0.0054  0.0042  38   ALA   B N   
4611 C  CA  . ALA   B 38  ? 0.1441 0.1249 0.1264 -0.0009 0.0106  0.0087  38   ALA   B CA  
4612 C  C   . ALA   B 38  ? 0.1363 0.1165 0.1203 0.0000  0.0084  0.0125  38   ALA   B C   
4613 O  O   . ALA   B 38  ? 0.1444 0.1279 0.1410 0.0118  0.0027  0.0116  38   ALA   B O   
4614 C  CB  . ALA   B 38  ? 0.1611 0.1314 0.1385 -0.0115 0.0147  0.0051  38   ALA   B CB  
4620 N  N   . ALA   B 39  ? 0.1387 0.1268 0.1141 0.0048  0.0028  0.0027  39   ALA   B N   
4621 C  CA  . ALA   B 39  ? 0.1440 0.1327 0.1214 0.0075  -0.0066 -0.0037 39   ALA   B CA  
4622 C  C   . ALA   B 39  ? 0.1469 0.1371 0.0974 0.0070  -0.0014 -0.0034 39   ALA   B C   
4623 O  O   . ALA   B 39  ? 0.1492 0.1366 0.1289 -0.0037 0.0039  0.0051  39   ALA   B O   
4624 C  CB  . ALA   B 39  ? 0.1485 0.1372 0.1420 -0.0039 -0.0018 0.0002  39   ALA   B CB  
4630 N  N   . ASN   B 40  ? 0.1525 0.1528 0.1090 -0.0040 0.0072  -0.0068 40   ASN   B N   
4631 C  CA  . ASN   B 40  ? 0.1598 0.1560 0.1250 0.0065  -0.0005 -0.0063 40   ASN   B CA  
4632 C  C   . ASN   B 40  ? 0.1602 0.1590 0.1101 0.0109  -0.0061 0.0016  40   ASN   B C   
4633 O  O   . ASN   B 40  ? 0.1526 0.1514 0.1290 0.0106  -0.0103 0.0042  40   ASN   B O   
4634 C  CB  . ASN   B 40  ? 0.1680 0.1564 0.1462 0.0108  -0.0022 0.0073  40   ASN   B CB  
4635 C  CG  . ASN   B 40  ? 0.1716 0.1667 0.1793 0.0058  -0.0176 0.0117  40   ASN   B CG  
4636 O  OD1 . ASN   B 40  ? 0.1695 0.1638 0.2614 -0.0013 -0.0316 0.0112  40   ASN   B OD1 
4637 N  ND2 . ASN   B 40  ? 0.1759 0.1708 0.1812 0.0097  -0.0127 0.0095  40   ASN   B ND2 
4644 N  N   . VAL   B 41  ? 0.1679 0.1692 0.1096 0.0170  0.0075  0.0022  41   VAL   B N   
4645 C  CA  . VAL   B 41  ? 0.1720 0.1799 0.1188 0.0182  0.0019  -0.0083 41   VAL   B CA  
4646 C  C   . VAL   B 41  ? 0.1682 0.1743 0.1221 0.0257  -0.0066 -0.0112 41   VAL   B C   
4647 O  O   . VAL   B 41  ? 0.1649 0.1716 0.1269 0.0192  -0.0074 -0.0123 41   VAL   B O   
4648 C  CB  . VAL   B 41  ? 0.1852 0.1947 0.1466 -0.0013 0.0176  -0.0159 41   VAL   B CB  
4649 C  CG1 . VAL   B 41  ? 0.1870 0.1988 0.1559 -0.0030 0.0270  -0.0227 41   VAL   B CG1 
4650 C  CG2 . VAL   B 41  ? 0.1957 0.2118 0.1500 -0.0056 0.0240  -0.0141 41   VAL   B CG2 
4660 N  N   . TYR   B 42  ? 0.1764 0.1731 0.1272 0.0229  -0.0166 -0.0051 42   TYR   B N   
4661 C  CA  . TYR   B 42  ? 0.1797 0.1806 0.1314 0.0208  -0.0247 -0.0155 42   TYR   B CA  
4662 C  C   . TYR   B 42  ? 0.1589 0.1628 0.1390 0.0243  -0.0205 -0.0142 42   TYR   B C   
4663 O  O   . TYR   B 42  ? 0.1606 0.1676 0.1746 0.0196  -0.0299 -0.0272 42   TYR   B O   
4664 C  CB  . TYR   B 42  ? 0.2020 0.2146 0.1492 0.0120  -0.0270 -0.0006 42   TYR   B CB  
4665 C  CG  . TYR   B 42  ? 0.2069 0.2328 0.1383 0.0002  -0.0226 0.0135  42   TYR   B CG  
4666 C  CD1 . TYR   B 42  ? 0.2008 0.2325 0.1074 -0.0045 -0.0085 0.0103  42   TYR   B CD1 
4667 C  CD2 . TYR   B 42  ? 0.2209 0.2473 0.1828 -0.0053 -0.0041 0.0235  42   TYR   B CD2 
4668 C  CE1 . TYR   B 42  ? 0.2184 0.2549 0.1155 -0.0040 -0.0019 0.0064  42   TYR   B CE1 
4669 C  CE2 . TYR   B 42  ? 0.2242 0.2637 0.1768 -0.0054 0.0214  0.0382  42   TYR   B CE2 
4670 C  CZ  . TYR   B 42  ? 0.2403 0.2811 0.1565 0.0097  0.0238  0.0168  42   TYR   B CZ  
4671 O  OH  . TYR   B 42  ? 0.2768 0.3162 0.2152 0.0321  0.0351  0.0162  42   TYR   B OH  
4681 N  N   . LEU   B 43  ? 0.1512 0.1529 0.1234 0.0163  -0.0141 -0.0175 43   LEU   B N   
4682 C  CA  . LEU   B 43  ? 0.1555 0.1522 0.1256 0.0079  -0.0107 -0.0048 43   LEU   B CA  
4683 C  C   . LEU   B 43  ? 0.1556 0.1480 0.1308 0.0107  -0.0133 -0.0012 43   LEU   B C   
4684 O  O   . LEU   B 43  ? 0.1560 0.1500 0.1530 0.0088  -0.0188 0.0096  43   LEU   B O   
4685 C  CB  . LEU   B 43  ? 0.1517 0.1413 0.1355 0.0032  -0.0173 -0.0116 43   LEU   B CB  
4686 C  CG  . LEU   B 43  ? 0.1569 0.1396 0.1364 0.0014  -0.0238 -0.0066 43   LEU   B CG  
4687 C  CD1 . LEU   B 43  ? 0.1681 0.1529 0.1827 -0.0065 -0.0372 -0.0124 43   LEU   B CD1 
4688 C  CD2 . LEU   B 43  ? 0.1554 0.1379 0.1426 -0.0007 -0.0342 -0.0035 43   LEU   B CD2 
4700 N  N   . LYS   B 44  ? 0.1587 0.1485 0.1284 0.0118  -0.0044 -0.0026 44   LYS   B N   
4701 C  CA  . LYS   B 44  ? 0.1674 0.1591 0.1352 0.0179  -0.0126 0.0030  44   LYS   B CA  
4702 C  C   . LYS   B 44  ? 0.1599 0.1480 0.1341 0.0200  -0.0150 0.0019  44   LYS   B C   
4703 O  O   . LYS   B 44  ? 0.1806 0.1486 0.1595 0.0094  0.0001  0.0026  44   LYS   B O   
4704 C  CB  . LYS   B 44  ? 0.1914 0.1854 0.1424 0.0229  -0.0283 0.0080  44   LYS   B CB  
4705 C  CG  . LYS   B 44  ? 0.2287 0.2179 0.1816 0.0136  -0.0433 0.0003  44   LYS   B CG  
4706 C  CD  . LYS   B 44  ? 0.2632 0.2365 0.2511 0.0030  -0.0453 -0.0083 44   LYS   B CD  
4707 C  CE  . LYS   B 44  ? 0.2891 0.2502 0.3022 -0.0011 -0.0537 0.0026  44   LYS   B CE  
4708 N  NZ  . LYS   B 44  ? 0.2971 0.2516 0.3221 0.0033  -0.0721 0.0252  44   LYS   B NZ  
4722 N  N   . HIS   B 45  ? 0.1505 0.1501 0.1246 0.0136  -0.0002 -0.0003 45   HIS   B N   
4723 C  CA  . HIS   B 45  ? 0.1570 0.1516 0.1286 0.0146  -0.0095 -0.0057 45   HIS   B CA  
4724 C  C   . HIS   B 45  ? 0.1826 0.1721 0.1685 0.0204  -0.0164 -0.0036 45   HIS   B C   
4725 O  O   . HIS   B 45  ? 0.1985 0.2075 0.2110 0.0480  0.0116  -0.0033 45   HIS   B O   
4726 C  CB  . HIS   B 45  ? 0.1469 0.1595 0.1346 0.0009  -0.0089 -0.0062 45   HIS   B CB  
4727 C  CG  . HIS   B 45  ? 0.1470 0.1534 0.1333 -0.0016 -0.0113 -0.0011 45   HIS   B CG  
4728 N  ND1 . HIS   B 45  ? 0.1515 0.1485 0.1410 0.0042  -0.0160 -0.0043 45   HIS   B ND1 
4729 C  CD2 . HIS   B 45  ? 0.1633 0.1532 0.1458 -0.0069 -0.0154 0.0001  45   HIS   B CD2 
4730 C  CE1 . HIS   B 45  ? 0.1612 0.1425 0.1235 -0.0006 -0.0172 -0.0012 45   HIS   B CE1 
4731 N  NE2 . HIS   B 45  ? 0.1673 0.1405 0.1350 -0.0014 -0.0183 0.0009  45   HIS   B NE2 
4739 N  N   A GLY   B 46  ? 0.1895 0.1760 0.1964 0.0184  -0.0217 0.0001  46   GLY   B N   
4740 N  N   B GLY   B 46  ? 0.1890 0.1651 0.1969 0.0279  -0.0298 0.0138  46   GLY   B N   
4741 C  CA  A GLY   B 46  ? 0.2011 0.1883 0.2278 0.0136  -0.0236 -0.0001 46   GLY   B CA  
4742 C  CA  B GLY   B 46  ? 0.2067 0.1826 0.2307 0.0219  -0.0336 0.0144  46   GLY   B CA  
4743 C  C   A GLY   B 46  ? 0.2093 0.2036 0.2632 0.0129  -0.0224 -0.0034 46   GLY   B C   
4744 C  C   B GLY   B 46  ? 0.2156 0.2063 0.2769 0.0222  -0.0334 0.0084  46   GLY   B C   
4745 O  O   A GLY   B 46  ? 0.2155 0.2121 0.3081 0.0159  -0.0163 -0.0172 46   GLY   B O   
4746 O  O   B GLY   B 46  ? 0.2317 0.2268 0.3464 0.0249  -0.0225 -0.0094 46   GLY   B O   
4753 N  N   . GLY   B 47  ? 0.2123 0.2110 0.2563 0.0027  -0.0172 -0.0036 47   GLY   B N   
4754 C  CA  . GLY   B 47  ? 0.1988 0.1797 0.2101 -0.0042 -0.0141 -0.0092 47   GLY   B CA  
4755 C  C   . GLY   B 47  ? 0.1764 0.1533 0.1772 -0.0012 -0.0030 0.0092  47   GLY   B C   
4756 O  O   . GLY   B 47  ? 0.1882 0.1470 0.1835 0.0001  -0.0063 0.0042  47   GLY   B O   
4761 N  N   . GLY   B 48  ? 0.1588 0.1428 0.1676 0.0024  -0.0120 0.0135  48   GLY   B N   
4762 C  CA  . GLY   B 48  ? 0.1562 0.1398 0.1730 -0.0012 -0.0073 0.0073  48   GLY   B CA  
4763 C  C   . GLY   B 48  ? 0.1497 0.1349 0.1587 0.0000  -0.0032 0.0036  48   GLY   B C   
4764 O  O   . GLY   B 48  ? 0.1447 0.1372 0.1772 0.0060  -0.0079 0.0033  48   GLY   B O   
4768 N  N   . VAL   B 49  ? 0.1503 0.1427 0.1463 0.0090  0.0009  0.0023  49   VAL   B N   
4769 C  CA  . VAL   B 49  ? 0.1516 0.1488 0.1427 0.0143  -0.0072 -0.0086 49   VAL   B CA  
4770 C  C   . VAL   B 49  ? 0.1400 0.1407 0.1300 0.0143  -0.0004 0.0050  49   VAL   B C   
4771 O  O   . VAL   B 49  ? 0.1513 0.1476 0.1456 0.0054  -0.0012 0.0037  49   VAL   B O   
4772 C  CB  . VAL   B 49  ? 0.1540 0.1649 0.1644 0.0039  -0.0189 -0.0025 49   VAL   B CB  
4773 C  CG1 . VAL   B 49  ? 0.1519 0.1738 0.1683 0.0088  -0.0279 0.0017  49   VAL   B CG1 
4774 C  CG2 . VAL   B 49  ? 0.1675 0.1812 0.1716 -0.0074 -0.0331 -0.0057 49   VAL   B CG2 
4784 N  N   . ALA   B 50  ? 0.1323 0.1376 0.1397 0.0062  -0.0005 0.0041  50   ALA   B N   
4785 C  CA  . ALA   B 50  ? 0.1360 0.1271 0.1395 0.0074  -0.0039 0.0066  50   ALA   B CA  
4786 C  C   . ALA   B 50  ? 0.1386 0.1346 0.1324 0.0092  0.0021  0.0045  50   ALA   B C   
4787 O  O   . ALA   B 50  ? 0.1396 0.1387 0.1327 0.0076  0.0022  0.0013  50   ALA   B O   
4788 C  CB  . ALA   B 50  ? 0.1438 0.1315 0.1375 0.0001  -0.0059 0.0154  50   ALA   B CB  
4794 N  N   . GLY   B 51  ? 0.1493 0.1456 0.1373 0.0159  -0.0044 0.0038  51   GLY   B N   
4795 C  CA  . GLY   B 51  ? 0.1488 0.1487 0.1746 0.0207  -0.0076 0.0085  51   GLY   B CA  
4796 C  C   . GLY   B 51  ? 0.1437 0.1453 0.1709 0.0212  -0.0038 0.0021  51   GLY   B C   
4797 O  O   . GLY   B 51  ? 0.1453 0.1533 0.1839 0.0132  -0.0055 -0.0038 51   GLY   B O   
4801 N  N   . ALA   B 52  ? 0.1437 0.1445 0.1523 0.0146  -0.0051 0.0034  52   ALA   B N   
4802 C  CA  . ALA   B 52  ? 0.1484 0.1448 0.1544 0.0161  -0.0002 -0.0009 52   ALA   B CA  
4803 C  C   . ALA   B 52  ? 0.1418 0.1451 0.1507 0.0107  0.0116  -0.0015 52   ALA   B C   
4804 O  O   . ALA   B 52  ? 0.1420 0.1510 0.1570 0.0123  0.0078  0.0044  52   ALA   B O   
4805 C  CB  . ALA   B 52  ? 0.1622 0.1467 0.1735 0.0057  0.0054  -0.0043 52   ALA   B CB  
4811 N  N   . LEU   B 53  ? 0.1382 0.1425 0.1384 0.0193  0.0062  0.0027  53   LEU   B N   
4812 C  CA  . LEU   B 53  ? 0.1363 0.1547 0.1373 0.0131  0.0009  0.0017  53   LEU   B CA  
4813 C  C   . LEU   B 53  ? 0.1387 0.1468 0.1380 0.0120  0.0085  0.0029  53   LEU   B C   
4814 O  O   . LEU   B 53  ? 0.1411 0.1585 0.1516 0.0014  0.0091  0.0065  53   LEU   B O   
4815 C  CB  . LEU   B 53  ? 0.1328 0.1577 0.1456 0.0105  0.0041  0.0149  53   LEU   B CB  
4816 C  CG  . LEU   B 53  ? 0.1356 0.1651 0.1502 0.0040  0.0057  0.0256  53   LEU   B CG  
4817 C  CD1 . LEU   B 53  ? 0.1433 0.1828 0.1821 0.0129  -0.0027 0.0066  53   LEU   B CD1 
4818 C  CD2 . LEU   B 53  ? 0.1439 0.1903 0.1731 -0.0037 -0.0049 -0.0030 53   LEU   B CD2 
4830 N  N   . ASN   B 54  ? 0.1384 0.1371 0.1340 0.0060  0.0013  0.0093  54   ASN   B N   
4831 C  CA  . ASN   B 54  ? 0.1389 0.1504 0.1418 0.0042  -0.0013 -0.0031 54   ASN   B CA  
4832 C  C   . ASN   B 54  ? 0.1376 0.1522 0.1570 0.0013  0.0027  0.0010  54   ASN   B C   
4833 O  O   . ASN   B 54  ? 0.1365 0.1559 0.1691 -0.0004 0.0054  0.0003  54   ASN   B O   
4834 C  CB  . ASN   B 54  ? 0.1413 0.1557 0.1505 0.0066  0.0087  -0.0071 54   ASN   B CB  
4835 C  CG  . ASN   B 54  ? 0.1433 0.1637 0.1537 0.0040  -0.0068 0.0046  54   ASN   B CG  
4836 O  OD1 . ASN   B 54  ? 0.1388 0.1624 0.1704 0.0008  -0.0101 -0.0113 54   ASN   B OD1 
4837 N  ND2 . ASN   B 54  ? 0.1578 0.1823 0.1838 0.0023  -0.0203 0.0222  54   ASN   B ND2 
4844 N  N   . LYS   B 55  ? 0.1391 0.1602 0.1801 0.0117  0.0016  0.0020  55   LYS   B N   
4845 C  CA  . LYS   B 55  ? 0.1452 0.1763 0.1934 0.0265  0.0027  -0.0027 55   LYS   B CA  
4846 C  C   . LYS   B 55  ? 0.1405 0.1784 0.1913 0.0171  0.0055  -0.0126 55   LYS   B C   
4847 O  O   . LYS   B 55  ? 0.1375 0.1890 0.2008 0.0173  0.0052  -0.0078 55   LYS   B O   
4848 C  CB  . LYS   B 55  ? 0.1621 0.1852 0.2215 0.0351  0.0163  0.0000  55   LYS   B CB  
4849 C  CG  . LYS   B 55  ? 0.2023 0.2138 0.2990 0.0372  0.0324  0.0062  55   LYS   B CG  
4850 C  CD  . LYS   B 55  ? 0.2384 0.2408 0.3606 0.0463  0.0537  0.0080  55   LYS   B CD  
4851 C  CE  . LYS   B 55  ? 0.2587 0.2598 0.4306 0.0512  0.0663  0.0133  55   LYS   B CE  
4852 N  NZ  . LYS   B 55  ? 0.2646 0.2763 0.4612 0.0508  0.0489  0.0269  55   LYS   B NZ  
4866 N  N   . ALA   B 56  ? 0.1377 0.1807 0.1752 0.0176  0.0058  -0.0116 56   ALA   B N   
4867 C  CA  . ALA   B 56  ? 0.1519 0.1960 0.1716 0.0068  0.0045  -0.0043 56   ALA   B CA  
4868 C  C   . ALA   B 56  ? 0.1522 0.1915 0.1671 0.0050  0.0160  0.0010  56   ALA   B C   
4869 O  O   . ALA   B 56  ? 0.1594 0.1947 0.1844 0.0092  0.0278  0.0079  56   ALA   B O   
4870 C  CB  . ALA   B 56  ? 0.1649 0.2130 0.1758 -0.0109 0.0016  -0.0048 56   ALA   B CB  
4876 N  N   . THR   B 57  ? 0.1517 0.1804 0.1640 0.0097  0.0150  -0.0033 57   THR   B N   
4877 C  CA  . THR   B 57  ? 0.1552 0.1780 0.1623 0.0004  0.0198  0.0030  57   THR   B CA  
4878 C  C   . THR   B 57  ? 0.1583 0.1879 0.1889 -0.0037 0.0285  0.0003  57   THR   B C   
4879 O  O   . THR   B 57  ? 0.1651 0.1827 0.1940 -0.0137 0.0195  -0.0007 57   THR   B O   
4880 C  CB  . THR   B 57  ? 0.1604 0.1650 0.1471 0.0017  0.0166  0.0083  57   THR   B CB  
4881 O  OG1 . THR   B 57  ? 0.1580 0.1530 0.1643 0.0020  0.0183  0.0080  57   THR   B OG1 
4882 C  CG2 . THR   B 57  ? 0.1601 0.1688 0.1574 0.0034  0.0206  0.0125  57   THR   B CG2 
4890 N  N   . ASN   B 58  ? 0.1431 0.2062 0.2120 -0.0094 0.0202  -0.0210 58   ASN   B N   
4891 C  CA  . ASN   B 58  ? 0.1607 0.2423 0.2457 -0.0205 0.0432  -0.0182 58   ASN   B CA  
4892 C  C   . ASN   B 58  ? 0.1415 0.2144 0.2070 -0.0152 0.0125  -0.0135 58   ASN   B C   
4893 O  O   . ASN   B 58  ? 0.1424 0.2190 0.2184 -0.0143 0.0108  -0.0112 58   ASN   B O   
4894 C  CB  . ASN   B 58  ? 0.2531 0.3203 0.3691 -0.0337 0.0812  0.0001  58   ASN   B CB  
4895 C  CG  . ASN   B 58  ? 0.3858 0.4126 0.5167 -0.0383 0.0945  0.0282  58   ASN   B CG  
4896 O  OD1 . ASN   B 58  ? 0.4333 0.4450 0.5709 -0.0399 0.0999  0.0360  58   ASN   B OD1 
4897 N  ND2 . ASN   B 58  ? 0.4238 0.4352 0.5671 -0.0395 0.0974  0.0346  58   ASN   B ND2 
4904 N  N   . ASN   B 59  ? 0.1362 0.1981 0.1860 -0.0135 0.0070  -0.0087 59   ASN   B N   
4905 C  CA  . ASN   B 59  ? 0.1428 0.1970 0.1844 -0.0093 -0.0113 0.0021  59   ASN   B CA  
4906 C  C   . ASN   B 59  ? 0.1393 0.1896 0.1775 -0.0123 -0.0097 -0.0045 59   ASN   B C   
4907 O  O   . ASN   B 59  ? 0.1454 0.1895 0.1658 -0.0128 -0.0083 -0.0009 59   ASN   B O   
4908 C  CB  . ASN   B 59  ? 0.1541 0.2180 0.1903 -0.0021 -0.0208 0.0094  59   ASN   B CB  
4909 C  CG  . ASN   B 59  ? 0.1695 0.2329 0.2005 0.0080  -0.0340 0.0144  59   ASN   B CG  
4910 O  OD1 . ASN   B 59  ? 0.1723 0.2357 0.2117 0.0135  -0.0138 0.0273  59   ASN   B OD1 
4911 N  ND2 . ASN   B 59  ? 0.1780 0.2449 0.2087 0.0059  -0.0315 0.0048  59   ASN   B ND2 
4918 N  N   . ALA   B 60  ? 0.1407 0.1757 0.1753 -0.0125 0.0044  -0.0072 60   ALA   B N   
4919 C  CA  . ALA   B 60  ? 0.1528 0.1664 0.1832 -0.0178 0.0002  0.0052  60   ALA   B CA  
4920 C  C   . ALA   B 60  ? 0.1525 0.1535 0.1574 -0.0089 0.0016  0.0061  60   ALA   B C   
4921 O  O   . ALA   B 60  ? 0.1557 0.1598 0.1741 -0.0080 -0.0004 -0.0032 60   ALA   B O   
4922 C  CB  . ALA   B 60  ? 0.1709 0.1688 0.2064 -0.0173 0.0081  0.0122  60   ALA   B CB  
4928 N  N   . MET   B 61  ? 0.1407 0.1495 0.1563 -0.0070 -0.0003 0.0081  61   MET   B N   
4929 C  CA  . MET   B 61  ? 0.1393 0.1456 0.1505 -0.0044 -0.0086 0.0028  61   MET   B CA  
4930 C  C   . MET   B 61  ? 0.1402 0.1431 0.1453 -0.0101 -0.0067 0.0013  61   MET   B C   
4931 O  O   . MET   B 61  ? 0.1462 0.1452 0.1421 -0.0034 -0.0051 -0.0132 61   MET   B O   
4932 C  CB  . MET   B 61  ? 0.1345 0.1511 0.1455 0.0052  -0.0051 -0.0059 61   MET   B CB  
4933 C  CG  . MET   B 61  ? 0.1337 0.1507 0.1385 0.0025  -0.0032 -0.0037 61   MET   B CG  
4934 S  SD  . MET   B 61  ? 0.1363 0.1500 0.1691 -0.0025 -0.0021 -0.0085 61   MET   B SD  
4935 C  CE  . MET   B 61  ? 0.1484 0.1685 0.1891 -0.0008 0.0003  -0.0192 61   MET   B CE  
4945 N  N   . GLN   B 62  ? 0.1398 0.1504 0.1415 -0.0009 -0.0145 0.0070  62   GLN   B N   
4946 C  CA  . GLN   B 62  ? 0.1432 0.1533 0.1441 -0.0014 -0.0107 -0.0002 62   GLN   B CA  
4947 C  C   . GLN   B 62  ? 0.1462 0.1573 0.1457 0.0014  -0.0195 -0.0028 62   GLN   B C   
4948 O  O   . GLN   B 62  ? 0.1546 0.1633 0.1493 0.0004  -0.0180 -0.0056 62   GLN   B O   
4949 C  CB  . GLN   B 62  ? 0.1436 0.1512 0.1565 0.0052  -0.0082 -0.0010 62   GLN   B CB  
4950 C  CG  . GLN   B 62  ? 0.1488 0.1564 0.1614 0.0077  -0.0185 0.0019  62   GLN   B CG  
4951 C  CD  . GLN   B 62  ? 0.1525 0.1548 0.1433 0.0049  -0.0243 0.0063  62   GLN   B CD  
4952 O  OE1 . GLN   B 62  ? 0.1548 0.1549 0.1607 0.0079  -0.0288 -0.0021 62   GLN   B OE1 
4953 N  NE2 . GLN   B 62  ? 0.1594 0.1602 0.1505 0.0074  -0.0212 -0.0104 62   GLN   B NE2 
4962 N  N   . VAL   B 63  ? 0.1415 0.1623 0.1753 -0.0087 -0.0234 -0.0062 63   VAL   B N   
4963 C  CA  . VAL   B 63  ? 0.1533 0.1690 0.1855 -0.0146 -0.0302 -0.0030 63   VAL   B CA  
4964 C  C   . VAL   B 63  ? 0.1551 0.1596 0.1612 -0.0176 -0.0242 -0.0100 63   VAL   B C   
4965 O  O   . VAL   B 63  ? 0.1613 0.1588 0.1759 -0.0122 -0.0327 -0.0078 63   VAL   B O   
4966 C  CB  . VAL   B 63  ? 0.1566 0.1828 0.2101 -0.0153 -0.0267 -0.0050 63   VAL   B CB  
4967 C  CG1 . VAL   B 63  ? 0.1586 0.1888 0.2395 -0.0233 -0.0173 -0.0023 63   VAL   B CG1 
4968 C  CG2 . VAL   B 63  ? 0.1546 0.1981 0.2280 -0.0100 -0.0241 -0.0081 63   VAL   B CG2 
4978 N  N   . GLU   B 64  ? 0.1513 0.1498 0.1612 -0.0086 -0.0225 -0.0039 64   GLU   B N   
4979 C  CA  . GLU   B 64  ? 0.1514 0.1428 0.1565 -0.0111 -0.0273 -0.0078 64   GLU   B CA  
4980 C  C   . GLU   B 64  ? 0.1520 0.1445 0.1486 -0.0025 -0.0322 -0.0123 64   GLU   B C   
4981 O  O   . GLU   B 64  ? 0.1654 0.1507 0.1497 -0.0085 -0.0227 -0.0145 64   GLU   B O   
4982 C  CB  . GLU   B 64  ? 0.1500 0.1487 0.1616 -0.0083 -0.0115 -0.0051 64   GLU   B CB  
4983 C  CG  . GLU   B 64  ? 0.1563 0.1482 0.1570 -0.0168 -0.0191 -0.0135 64   GLU   B CG  
4984 C  CD  . GLU   B 64  ? 0.1599 0.1637 0.1663 -0.0249 -0.0221 -0.0135 64   GLU   B CD  
4985 O  OE1 . GLU   B 64  ? 0.1638 0.1769 0.1823 -0.0305 -0.0136 -0.0337 64   GLU   B OE1 
4986 O  OE2 . GLU   B 64  ? 0.1791 0.1761 0.1675 -0.0253 -0.0305 -0.0190 64   GLU   B OE2 
4993 N  N   . SER   B 65  ? 0.1515 0.1409 0.1399 -0.0085 -0.0161 -0.0088 65   SER   B N   
4994 C  CA  . SER   B 65  ? 0.1458 0.1421 0.1496 -0.0027 -0.0123 -0.0150 65   SER   B CA  
4995 C  C   . SER   B 65  ? 0.1475 0.1376 0.1488 0.0018  -0.0186 -0.0148 65   SER   B C   
4996 O  O   . SER   B 65  ? 0.1540 0.1498 0.1461 0.0046  -0.0189 -0.0194 65   SER   B O   
4997 C  CB  . SER   B 65  ? 0.1535 0.1459 0.1576 -0.0093 -0.0097 -0.0086 65   SER   B CB  
4998 O  OG  . SER   B 65  ? 0.1518 0.1487 0.1491 -0.0056 -0.0126 -0.0230 65   SER   B OG  
5004 N  N   . ASP   B 66  ? 0.1587 0.1496 0.1419 -0.0003 -0.0201 -0.0159 66   ASP   B N   
5005 C  CA  . ASP   B 66  ? 0.1714 0.1559 0.1417 0.0043  -0.0293 -0.0158 66   ASP   B CA  
5006 C  C   . ASP   B 66  ? 0.1695 0.1566 0.1426 -0.0016 -0.0250 -0.0142 66   ASP   B C   
5007 O  O   . ASP   B 66  ? 0.1757 0.1554 0.1577 0.0044  -0.0260 -0.0180 66   ASP   B O   
5008 C  CB  . ASP   B 66  ? 0.1862 0.1696 0.1552 0.0115  -0.0436 -0.0156 66   ASP   B CB  
5009 C  CG  . ASP   B 66  ? 0.2001 0.1853 0.1874 0.0144  -0.0618 -0.0061 66   ASP   B CG  
5010 O  OD1 . ASP   B 66  ? 0.2178 0.1851 0.2013 0.0066  -0.0575 -0.0063 66   ASP   B OD1 
5011 O  OD2 . ASP   B 66  ? 0.2099 0.2069 0.2574 0.0365  -0.0560 -0.0021 66   ASP   B OD2 
5016 N  N   . ASP   B 67  ? 0.1615 0.1490 0.1420 -0.0058 -0.0262 -0.0210 67   ASP   B N   
5017 C  CA  . ASP   B 67  ? 0.1752 0.1518 0.1509 -0.0080 -0.0271 -0.0185 67   ASP   B CA  
5018 C  C   . ASP   B 67  ? 0.1774 0.1505 0.1646 0.0050  -0.0275 -0.0197 67   ASP   B C   
5019 O  O   . ASP   B 67  ? 0.1867 0.1595 0.1789 0.0033  -0.0253 -0.0256 67   ASP   B O   
5020 C  CB  . ASP   B 67  ? 0.1934 0.1605 0.1639 -0.0163 -0.0407 -0.0076 67   ASP   B CB  
5021 C  CG  . ASP   B 67  ? 0.2337 0.1666 0.1686 -0.0116 -0.0663 -0.0090 67   ASP   B CG  
5022 O  OD1 . ASP   B 67  ? 0.2554 0.1668 0.1920 -0.0124 -0.0651 -0.0066 67   ASP   B OD1 
5023 O  OD2 . ASP   B 67  ? 0.2507 0.1717 0.1989 0.0017  -0.0707 -0.0046 67   ASP   B OD2 
5028 N  N   . TYR   B 68  ? 0.1697 0.1527 0.1487 0.0049  -0.0355 -0.0256 68   TYR   B N   
5029 C  CA  . TYR   B 68  ? 0.1684 0.1619 0.1665 0.0070  -0.0336 -0.0315 68   TYR   B CA  
5030 C  C   . TYR   B 68  ? 0.1592 0.1526 0.1638 0.0030  -0.0285 -0.0395 68   TYR   B C   
5031 O  O   . TYR   B 68  ? 0.1678 0.1668 0.1686 0.0101  -0.0297 -0.0478 68   TYR   B O   
5032 C  CB  . TYR   B 68  ? 0.1717 0.1816 0.1702 0.0095  -0.0357 -0.0365 68   TYR   B CB  
5033 C  CG  . TYR   B 68  ? 0.1837 0.1970 0.1767 0.0140  -0.0330 -0.0582 68   TYR   B CG  
5034 C  CD1 . TYR   B 68  ? 0.1827 0.1975 0.1951 0.0015  -0.0266 -0.0568 68   TYR   B CD1 
5035 C  CD2 . TYR   B 68  ? 0.1906 0.2136 0.1864 0.0182  -0.0508 -0.0488 68   TYR   B CD2 
5036 C  CE1 . TYR   B 68  ? 0.1912 0.2119 0.2100 0.0017  -0.0308 -0.0429 68   TYR   B CE1 
5037 C  CE2 . TYR   B 68  ? 0.1952 0.2168 0.1841 0.0205  -0.0388 -0.0474 68   TYR   B CE2 
5038 C  CZ  . TYR   B 68  ? 0.1915 0.2208 0.1963 0.0064  -0.0368 -0.0459 68   TYR   B CZ  
5039 O  OH  . TYR   B 68  ? 0.1870 0.2377 0.2235 0.0065  -0.0351 -0.0299 68   TYR   B OH  
5049 N  N   . ILE   B 69  ? 0.1617 0.1479 0.1644 0.0062  -0.0286 -0.0298 69   ILE   B N   
5050 C  CA  . ILE   B 69  ? 0.1619 0.1583 0.1606 0.0014  -0.0245 -0.0323 69   ILE   B CA  
5051 C  C   . ILE   B 69  ? 0.1633 0.1582 0.1632 0.0070  -0.0305 -0.0284 69   ILE   B C   
5052 O  O   . ILE   B 69  ? 0.1654 0.1687 0.1581 0.0055  -0.0208 -0.0328 69   ILE   B O   
5053 C  CB  . ILE   B 69  ? 0.1699 0.1650 0.1860 0.0019  0.0029  -0.0286 69   ILE   B CB  
5054 C  CG1 . ILE   B 69  ? 0.1711 0.1703 0.2053 -0.0008 0.0097  -0.0345 69   ILE   B CG1 
5055 C  CG2 . ILE   B 69  ? 0.1809 0.1756 0.2044 0.0078  -0.0007 -0.0118 69   ILE   B CG2 
5056 C  CD1 . ILE   B 69  ? 0.1684 0.1742 0.2208 -0.0098 0.0059  -0.0400 69   ILE   B CD1 
5068 N  N   . ALA   B 70  ? 0.1581 0.1586 0.1637 0.0078  -0.0336 -0.0304 70   ALA   B N   
5069 C  CA  . ALA   B 70  ? 0.1681 0.1636 0.1514 0.0078  -0.0290 -0.0294 70   ALA   B CA  
5070 C  C   . ALA   B 70  ? 0.1779 0.1610 0.1579 -0.0010 -0.0373 -0.0378 70   ALA   B C   
5071 O  O   . ALA   B 70  ? 0.1837 0.1639 0.1676 0.0043  -0.0334 -0.0416 70   ALA   B O   
5072 C  CB  . ALA   B 70  ? 0.1645 0.1781 0.1553 0.0042  -0.0263 -0.0249 70   ALA   B CB  
5078 N  N   . THR   B 71  ? 0.1792 0.1569 0.1714 0.0025  -0.0440 -0.0381 71   THR   B N   
5079 C  CA  . THR   B 71  ? 0.1910 0.1574 0.1869 0.0075  -0.0591 -0.0309 71   THR   B CA  
5080 C  C   . THR   B 71  ? 0.1887 0.1615 0.2102 0.0222  -0.0592 -0.0481 71   THR   B C   
5081 O  O   . THR   B 71  ? 0.2028 0.1694 0.2443 0.0247  -0.0519 -0.0608 71   THR   B O   
5082 C  CB  . THR   B 71  ? 0.2142 0.1854 0.2064 0.0047  -0.0659 -0.0077 71   THR   B CB  
5083 O  OG1 . THR   B 71  ? 0.2248 0.2180 0.2339 -0.0123 -0.0591 0.0133  71   THR   B OG1 
5084 C  CG2 . THR   B 71  ? 0.2384 0.1828 0.2337 0.0166  -0.0558 -0.0021 71   THR   B CG2 
5092 N  N   . ASN   B 72  ? 0.1767 0.1628 0.2053 0.0155  -0.0519 -0.0624 72   ASN   B N   
5093 C  CA  . ASN   B 72  ? 0.1793 0.1831 0.2212 0.0160  -0.0475 -0.0690 72   ASN   B CA  
5094 C  C   . ASN   B 72  ? 0.1729 0.1938 0.2173 0.0075  -0.0245 -0.0709 72   ASN   B C   
5095 O  O   . ASN   B 72  ? 0.1715 0.2053 0.2520 0.0057  -0.0125 -0.0643 72   ASN   B O   
5096 C  CB  . ASN   B 72  ? 0.1880 0.1950 0.2260 0.0090  -0.0586 -0.0601 72   ASN   B CB  
5097 C  CG  . ASN   B 72  ? 0.2020 0.2107 0.2408 0.0222  -0.0616 -0.0389 72   ASN   B CG  
5098 O  OD1 . ASN   B 72  ? 0.2234 0.2292 0.2443 0.0132  -0.0424 -0.0478 72   ASN   B OD1 
5099 N  ND2 . ASN   B 72  ? 0.2044 0.2165 0.2820 0.0403  -0.0486 -0.0095 72   ASN   B ND2 
5106 N  N   . GLY   B 73  ? 0.1763 0.1972 0.1855 0.0041  -0.0242 -0.0616 73   GLY   B N   
5107 C  CA  . GLY   B 73  ? 0.1736 0.2065 0.1647 0.0025  -0.0188 -0.0569 73   GLY   B CA  
5108 C  C   . GLY   B 73  ? 0.1691 0.2033 0.1234 0.0110  -0.0203 -0.0524 73   GLY   B C   
5109 O  O   . GLY   B 73  ? 0.1636 0.1900 0.1492 0.0092  -0.0222 -0.0378 73   GLY   B O   
5113 N  N   . PRO   B 74  ? 0.1730 0.2082 0.1304 0.0087  -0.0194 -0.0400 74   PRO   B N   
5114 C  CA  . PRO   B 74  ? 0.1653 0.2079 0.1147 0.0098  -0.0118 -0.0257 74   PRO   B CA  
5115 C  C   . PRO   B 74  ? 0.1514 0.1944 0.1228 0.0089  -0.0142 -0.0204 74   PRO   B C   
5116 O  O   . PRO   B 74  ? 0.1598 0.1972 0.1715 0.0139  -0.0075 -0.0378 74   PRO   B O   
5117 C  CB  . PRO   B 74  ? 0.1784 0.2239 0.1151 0.0087  -0.0110 -0.0197 74   PRO   B CB  
5118 C  CG  . PRO   B 74  ? 0.2018 0.2337 0.1503 0.0071  -0.0083 -0.0189 74   PRO   B CG  
5119 C  CD  . PRO   B 74  ? 0.1997 0.2300 0.1361 0.0060  -0.0060 -0.0329 74   PRO   B CD  
5127 N  N   . LEU   B 75  ? 0.1506 0.1829 0.1117 0.0107  -0.0127 -0.0222 75   LEU   B N   
5128 C  CA  . LEU   B 75  ? 0.1493 0.1788 0.1262 0.0057  -0.0163 -0.0064 75   LEU   B CA  
5129 C  C   . LEU   B 75  ? 0.1555 0.1869 0.1365 0.0080  -0.0097 -0.0103 75   LEU   B C   
5130 O  O   . LEU   B 75  ? 0.1731 0.1981 0.1422 0.0025  -0.0086 0.0027  75   LEU   B O   
5131 C  CB  . LEU   B 75  ? 0.1618 0.1841 0.1095 -0.0051 -0.0180 0.0029  75   LEU   B CB  
5132 C  CG  . LEU   B 75  ? 0.1954 0.2037 0.1359 -0.0267 -0.0124 -0.0056 75   LEU   B CG  
5133 C  CD1 . LEU   B 75  ? 0.2236 0.2178 0.1544 -0.0351 0.0153  -0.0101 75   LEU   B CD1 
5134 C  CD2 . LEU   B 75  ? 0.2321 0.2227 0.2127 -0.0178 0.0055  0.0014  75   LEU   B CD2 
5146 N  N   . LYS   B 76  ? 0.1591 0.2041 0.1578 0.0069  0.0057  -0.0016 76   LYS   B N   
5147 C  CA  . LYS   B 76  ? 0.1692 0.2151 0.1703 0.0077  0.0225  -0.0086 76   LYS   B CA  
5148 C  C   . LYS   B 76  ? 0.1612 0.2053 0.1364 0.0108  0.0021  0.0173  76   LYS   B C   
5149 O  O   . LYS   B 76  ? 0.1611 0.1893 0.1339 0.0052  -0.0034 0.0123  76   LYS   B O   
5150 C  CB  . LYS   B 76  ? 0.1878 0.2282 0.2551 0.0020  0.0361  -0.0452 76   LYS   B CB  
5151 C  CG  . LYS   B 76  ? 0.2002 0.2474 0.3012 0.0068  0.0288  -0.0514 76   LYS   B CG  
5152 C  CD  . LYS   B 76  ? 0.1997 0.2616 0.3421 0.0073  0.0116  -0.0600 76   LYS   B CD  
5153 C  CE  . LYS   B 76  ? 0.2054 0.2789 0.3967 0.0071  -0.0036 -0.0742 76   LYS   B CE  
5154 N  NZ  . LYS   B 76  ? 0.1986 0.2888 0.4068 0.0024  -0.0233 -0.0919 76   LYS   B NZ  
5168 N  N   . VAL   B 77  ? 0.1676 0.2131 0.1414 0.0186  0.0130  0.0223  77   VAL   B N   
5169 C  CA  . VAL   B 77  ? 0.1680 0.1986 0.1506 0.0230  0.0169  0.0424  77   VAL   B CA  
5170 C  C   . VAL   B 77  ? 0.1539 0.1772 0.1486 0.0182  0.0238  0.0248  77   VAL   B C   
5171 O  O   . VAL   B 77  ? 0.1584 0.1753 0.1582 0.0176  0.0256  0.0199  77   VAL   B O   
5172 C  CB  . VAL   B 77  ? 0.1815 0.2076 0.1807 0.0185  0.0250  0.0580  77   VAL   B CB  
5173 C  CG1 . VAL   B 77  ? 0.1813 0.2011 0.2113 0.0115  0.0287  0.0754  77   VAL   B CG1 
5174 C  CG2 . VAL   B 77  ? 0.1900 0.2245 0.2023 0.0182  0.0115  0.0527  77   VAL   B CG2 
5184 N  N   . GLY   B 78  ? 0.1494 0.1685 0.1424 0.0178  0.0136  0.0219  78   GLY   B N   
5185 C  CA  . GLY   B 78  ? 0.1525 0.1650 0.1392 0.0153  0.0218  0.0117  78   GLY   B CA  
5186 C  C   . GLY   B 78  ? 0.1463 0.1580 0.1328 0.0102  0.0141  0.0224  78   GLY   B C   
5187 O  O   . GLY   B 78  ? 0.1475 0.1524 0.1528 0.0113  0.0117  0.0217  78   GLY   B O   
5191 N  N   . GLY   B 79  ? 0.1428 0.1569 0.1309 0.0123  0.0178  0.0126  79   GLY   B N   
5192 C  CA  . GLY   B 79  ? 0.1427 0.1481 0.1396 0.0159  0.0071  0.0111  79   GLY   B CA  
5193 C  C   . GLY   B 79  ? 0.1349 0.1402 0.1352 0.0146  0.0106  0.0057  79   GLY   B C   
5194 O  O   . GLY   B 79  ? 0.1446 0.1424 0.1511 0.0144  0.0161  0.0100  79   GLY   B O   
5198 N  N   . SER   B 80  ? 0.1346 0.1389 0.1402 0.0126  0.0162  0.0062  80   SER   B N   
5199 C  CA  . SER   B 80  ? 0.1303 0.1309 0.1473 0.0050  0.0053  0.0026  80   SER   B CA  
5200 C  C   . SER   B 80  ? 0.1326 0.1299 0.1394 0.0094  -0.0048 -0.0007 80   SER   B C   
5201 O  O   . SER   B 80  ? 0.1438 0.1368 0.1684 0.0066  0.0017  -0.0098 80   SER   B O   
5202 C  CB  . SER   B 80  ? 0.1374 0.1312 0.1448 -0.0035 -0.0017 0.0035  80   SER   B CB  
5203 O  OG  . SER   B 80  ? 0.1466 0.1478 0.1630 -0.0028 -0.0100 0.0063  80   SER   B OG  
5209 N  N   . CYS   B 81  ? 0.1341 0.1231 0.1412 0.0023  -0.0059 -0.0029 81   CYS   B N   
5210 C  CA  . CYS   B 81  ? 0.1402 0.1223 0.1576 0.0050  -0.0098 -0.0030 81   CYS   B CA  
5211 C  C   . CYS   B 81  ? 0.1373 0.1193 0.1267 0.0049  -0.0137 -0.0014 81   CYS   B C   
5212 O  O   . CYS   B 81  ? 0.1584 0.1217 0.1457 0.0095  -0.0009 -0.0035 81   CYS   B O   
5213 C  CB  . CYS   B 81  ? 0.1525 0.1335 0.1531 -0.0027 -0.0148 -0.0036 81   CYS   B CB  
5214 S  SG  . CYS   B 81  ? 0.1524 0.1497 0.1467 -0.0016 -0.0255 -0.0115 81   CYS   B SG  
5220 N  N   . VAL   B 82  ? 0.1434 0.1180 0.1447 -0.0007 -0.0119 -0.0023 82   VAL   B N   
5221 C  CA  . VAL   B 82  ? 0.1487 0.1244 0.1388 -0.0012 -0.0049 0.0039  82   VAL   B CA  
5222 C  C   . VAL   B 82  ? 0.1537 0.1112 0.1407 -0.0035 -0.0115 0.0001  82   VAL   B C   
5223 O  O   . VAL   B 82  ? 0.1609 0.1200 0.1712 -0.0052 -0.0024 -0.0164 82   VAL   B O   
5224 C  CB  . VAL   B 82  ? 0.1537 0.1430 0.1561 0.0018  -0.0074 0.0072  82   VAL   B CB  
5225 C  CG1 . VAL   B 82  ? 0.1684 0.1680 0.1739 0.0051  -0.0081 0.0192  82   VAL   B CG1 
5226 C  CG2 . VAL   B 82  ? 0.1575 0.1596 0.1703 -0.0043 -0.0287 0.0105  82   VAL   B CG2 
5236 N  N   . LEU   B 83  ? 0.1431 0.1152 0.1448 -0.0108 -0.0201 -0.0058 83   LEU   B N   
5237 C  CA  . LEU   B 83  ? 0.1446 0.1230 0.1331 -0.0090 -0.0204 -0.0010 83   LEU   B CA  
5238 C  C   . LEU   B 83  ? 0.1446 0.1232 0.1385 -0.0197 -0.0217 -0.0029 83   LEU   B C   
5239 O  O   . LEU   B 83  ? 0.1463 0.1298 0.1284 -0.0149 -0.0151 -0.0024 83   LEU   B O   
5240 C  CB  . LEU   B 83  ? 0.1493 0.1367 0.1373 -0.0093 -0.0161 -0.0072 83   LEU   B CB  
5241 C  CG  . LEU   B 83  ? 0.1669 0.1538 0.1569 -0.0084 -0.0143 -0.0058 83   LEU   B CG  
5242 C  CD1 . LEU   B 83  ? 0.1784 0.1542 0.1513 -0.0112 -0.0263 0.0037  83   LEU   B CD1 
5243 C  CD2 . LEU   B 83  ? 0.1847 0.1613 0.1799 -0.0025 -0.0110 -0.0196 83   LEU   B CD2 
5255 N  N   . SER   B 84  ? 0.1442 0.1335 0.1578 -0.0257 -0.0162 0.0029  84   SER   B N   
5256 C  CA  . SER   B 84  ? 0.1479 0.1532 0.1423 -0.0268 -0.0099 0.0130  84   SER   B CA  
5257 C  C   . SER   B 84  ? 0.1403 0.1691 0.1027 -0.0207 -0.0108 0.0108  84   SER   B C   
5258 O  O   . SER   B 84  ? 0.1514 0.1509 0.1082 -0.0188 -0.0118 -0.0004 84   SER   B O   
5259 C  CB  . SER   B 84  ? 0.1656 0.1577 0.1869 -0.0312 0.0076  0.0168  84   SER   B CB  
5260 O  OG  . SER   B 84  ? 0.1701 0.1708 0.2466 -0.0398 0.0091  0.0276  84   SER   B OG  
5266 N  N   . GLY   B 85  ? 0.1476 0.1897 0.1233 -0.0245 -0.0128 0.0178  85   GLY   B N   
5267 C  CA  . GLY   B 85  ? 0.1479 0.1919 0.1382 -0.0316 -0.0023 -0.0104 85   GLY   B CA  
5268 C  C   . GLY   B 85  ? 0.1413 0.1779 0.1326 -0.0408 -0.0029 0.0092  85   GLY   B C   
5269 O  O   . GLY   B 85  ? 0.1524 0.1763 0.1461 -0.0538 0.0142  -0.0046 85   GLY   B O   
5273 N  N   . HIS   B 86  ? 0.1402 0.1654 0.1475 -0.0350 -0.0138 0.0168  86   HIS   B N   
5274 C  CA  . HIS   B 86  ? 0.1491 0.1662 0.1362 -0.0362 -0.0177 0.0186  86   HIS   B CA  
5275 C  C   . HIS   B 86  ? 0.1525 0.1713 0.1383 -0.0427 -0.0106 0.0350  86   HIS   B C   
5276 O  O   . HIS   B 86  ? 0.1642 0.1818 0.1442 -0.0360 0.0044  0.0253  86   HIS   B O   
5277 C  CB  . HIS   B 86  ? 0.1565 0.1655 0.1488 -0.0256 -0.0232 0.0067  86   HIS   B CB  
5278 C  CG  . HIS   B 86  ? 0.1541 0.1711 0.1437 -0.0136 -0.0179 0.0086  86   HIS   B CG  
5279 N  ND1 . HIS   B 86  ? 0.1693 0.1881 0.1657 -0.0201 -0.0266 -0.0095 86   HIS   B ND1 
5280 C  CD2 . HIS   B 86  ? 0.1563 0.1789 0.1542 -0.0071 -0.0120 0.0052  86   HIS   B CD2 
5281 C  CE1 . HIS   B 86  ? 0.1735 0.1869 0.1555 -0.0132 -0.0175 -0.0253 86   HIS   B CE1 
5282 N  NE2 . HIS   B 86  ? 0.1713 0.1781 0.1425 -0.0021 -0.0093 -0.0042 86   HIS   B NE2 
5290 N  N   . ASN   B 87  ? 0.1491 0.1730 0.1536 -0.0373 0.0004  0.0293  87   ASN   B N   
5291 C  CA  . ASN   B 87  ? 0.1599 0.1911 0.1427 -0.0358 0.0256  0.0201  87   ASN   B CA  
5292 C  C   . ASN   B 87  ? 0.1691 0.1746 0.1336 -0.0328 0.0228  0.0125  87   ASN   B C   
5293 O  O   . ASN   B 87  ? 0.1925 0.1802 0.1667 -0.0246 0.0419  0.0054  87   ASN   B O   
5294 C  CB  . ASN   B 87  ? 0.1591 0.2229 0.1759 -0.0292 0.0300  0.0140  87   ASN   B CB  
5295 C  CG  . ASN   B 87  ? 0.1691 0.2403 0.1956 0.0040  0.0358  0.0280  87   ASN   B CG  
5296 O  OD1 . ASN   B 87  ? 0.1623 0.2237 0.1876 0.0100  0.0521  0.0405  87   ASN   B OD1 
5297 N  ND2 . ASN   B 87  ? 0.2051 0.2551 0.2361 0.0173  0.0448  0.0258  87   ASN   B ND2 
5304 N  N   . LEU   B 88  ? 0.1588 0.1624 0.1275 -0.0378 0.0175  0.0104  88   LEU   B N   
5305 C  CA  . LEU   B 88  ? 0.1711 0.1579 0.1320 -0.0314 0.0059  0.0043  88   LEU   B CA  
5306 C  C   . LEU   B 88  ? 0.1720 0.1492 0.1280 -0.0356 0.0012  0.0018  88   LEU   B C   
5307 O  O   . LEU   B 88  ? 0.1935 0.1544 0.1577 -0.0251 -0.0281 -0.0028 88   LEU   B O   
5308 C  CB  . LEU   B 88  ? 0.1834 0.1667 0.1521 -0.0425 -0.0137 0.0178  88   LEU   B CB  
5309 C  CG  . LEU   B 88  ? 0.2166 0.1991 0.1687 -0.0326 -0.0224 0.0401  88   LEU   B CG  
5310 C  CD1 . LEU   B 88  ? 0.2229 0.2312 0.1891 -0.0417 -0.0106 0.0500  88   LEU   B CD1 
5311 C  CD2 . LEU   B 88  ? 0.2509 0.2214 0.2419 0.0039  -0.0419 0.0215  88   LEU   B CD2 
5323 N  N   . ALA   B 89  ? 0.1512 0.1454 0.1293 -0.0379 0.0152  0.0017  89   ALA   B N   
5324 C  CA  . ALA   B 89  ? 0.1524 0.1462 0.1190 -0.0337 -0.0002 0.0088  89   ALA   B CA  
5325 C  C   . ALA   B 89  ? 0.1604 0.1478 0.1166 -0.0449 0.0159  -0.0011 89   ALA   B C   
5326 O  O   . ALA   B 89  ? 0.1560 0.1597 0.1490 -0.0466 0.0150  -0.0245 89   ALA   B O   
5327 C  CB  . ALA   B 89  ? 0.1410 0.1449 0.1375 -0.0346 -0.0036 0.0174  89   ALA   B CB  
5333 N  N   . LYS   B 90  ? 0.1926 0.1361 0.1293 -0.0435 -0.0072 0.0079  90   LYS   B N   
5334 C  CA  . LYS   B 90  ? 0.2101 0.1378 0.1340 -0.0396 -0.0079 0.0066  90   LYS   B CA  
5335 C  C   . LYS   B 90  ? 0.1984 0.1279 0.1407 -0.0402 -0.0070 -0.0063 90   LYS   B C   
5336 O  O   . LYS   B 90  ? 0.2040 0.1494 0.1547 -0.0568 0.0012  -0.0010 90   LYS   B O   
5337 C  CB  . LYS   B 90  ? 0.2265 0.1370 0.1689 -0.0310 0.0006  0.0175  90   LYS   B CB  
5338 C  CG  . LYS   B 90  ? 0.2263 0.1542 0.1889 -0.0197 0.0204  0.0058  90   LYS   B CG  
5339 C  CD  . LYS   B 90  ? 0.2497 0.1841 0.2419 -0.0118 0.0513  -0.0072 90   LYS   B CD  
5340 C  CE  . LYS   B 90  ? 0.2593 0.1991 0.2940 -0.0130 0.0664  -0.0089 90   LYS   B CE  
5341 N  NZ  . LYS   B 90  ? 0.2659 0.1957 0.3055 -0.0213 0.0842  0.0048  90   LYS   B NZ  
5355 N  N   . HIS   B 91  ? 0.1734 0.1185 0.1176 -0.0304 -0.0153 0.0004  91   HIS   B N   
5356 C  CA  . HIS   B 91  ? 0.1636 0.1243 0.1302 -0.0214 -0.0137 0.0007  91   HIS   B CA  
5357 C  C   . HIS   B 91  ? 0.1484 0.1238 0.1071 -0.0255 -0.0060 -0.0053 91   HIS   B C   
5358 O  O   . HIS   B 91  ? 0.1589 0.1298 0.1142 -0.0272 -0.0073 -0.0045 91   HIS   B O   
5359 C  CB  . HIS   B 91  ? 0.1753 0.1239 0.1759 -0.0055 -0.0105 0.0103  91   HIS   B CB  
5360 C  CG  . HIS   B 91  ? 0.2155 0.1419 0.2470 0.0036  0.0257  0.0227  91   HIS   B CG  
5361 N  ND1 . HIS   B 91  ? 0.2458 0.1499 0.3146 0.0031  0.0377  0.0115  91   HIS   B ND1 
5362 C  CD2 . HIS   B 91  ? 0.2249 0.1681 0.2921 0.0169  0.0184  0.0513  91   HIS   B CD2 
5363 C  CE1 . HIS   B 91  ? 0.2457 0.1658 0.3288 0.0210  0.0352  0.0165  91   HIS   B CE1 
5364 N  NE2 . HIS   B 91  ? 0.2387 0.1790 0.3275 0.0291  0.0307  0.0504  91   HIS   B NE2 
5372 N  N   . CYS   B 92  ? 0.1383 0.1234 0.1118 -0.0241 -0.0060 -0.0077 92   CYS   B N   
5373 C  CA  . CYS   B 92  ? 0.1351 0.1253 0.1107 -0.0175 0.0003  0.0009  92   CYS   B CA  
5374 C  C   . CYS   B 92  ? 0.1335 0.1155 0.1062 -0.0056 -0.0079 0.0032  92   CYS   B C   
5375 O  O   . CYS   B 92  ? 0.1414 0.1241 0.1325 -0.0110 -0.0002 -0.0031 92   CYS   B O   
5376 C  CB  . CYS   B 92  ? 0.1330 0.1349 0.1228 -0.0125 -0.0060 0.0036  92   CYS   B CB  
5377 S  SG  . CYS   B 92  ? 0.1361 0.1331 0.1253 -0.0093 -0.0085 0.0047  92   CYS   B SG  
5383 N  N   . LEU   B 93  ? 0.1246 0.1175 0.1186 -0.0100 -0.0069 -0.0050 93   LEU   B N   
5384 C  CA  . LEU   B 93  ? 0.1263 0.1187 0.1146 -0.0012 -0.0061 -0.0023 93   LEU   B CA  
5385 C  C   . LEU   B 93  ? 0.1220 0.1159 0.1064 -0.0022 -0.0041 0.0066  93   LEU   B C   
5386 O  O   . LEU   B 93  ? 0.1330 0.1148 0.1200 -0.0039 -0.0022 0.0014  93   LEU   B O   
5387 C  CB  . LEU   B 93  ? 0.1282 0.1148 0.1233 -0.0015 -0.0074 0.0009  93   LEU   B CB  
5388 C  CG  . LEU   B 93  ? 0.1293 0.1277 0.1368 -0.0043 -0.0058 0.0126  93   LEU   B CG  
5389 C  CD1 . LEU   B 93  ? 0.1361 0.1402 0.1395 0.0047  -0.0044 -0.0011 93   LEU   B CD1 
5390 C  CD2 . LEU   B 93  ? 0.1328 0.1316 0.1646 -0.0045 -0.0078 0.0056  93   LEU   B CD2 
5402 N  N   . HIS   B 94  ? 0.1271 0.1126 0.1128 -0.0060 -0.0130 0.0110  94   HIS   B N   
5403 C  CA  . HIS   B 94  ? 0.1274 0.1162 0.1112 0.0012  -0.0048 0.0039  94   HIS   B CA  
5404 C  C   . HIS   B 94  ? 0.1246 0.1205 0.1162 0.0002  -0.0027 0.0115  94   HIS   B C   
5405 O  O   . HIS   B 94  ? 0.1260 0.1255 0.1610 0.0010  0.0124  -0.0104 94   HIS   B O   
5406 C  CB  . HIS   B 94  ? 0.1298 0.1198 0.1221 0.0029  -0.0124 0.0064  94   HIS   B CB  
5407 C  CG  . HIS   B 94  ? 0.1320 0.1150 0.1150 -0.0018 -0.0182 -0.0014 94   HIS   B CG  
5408 N  ND1 . HIS   B 94  ? 0.1355 0.1253 0.1172 -0.0022 -0.0168 0.0055  94   HIS   B ND1 
5409 C  CD2 . HIS   B 94  ? 0.1325 0.1261 0.1294 -0.0031 -0.0141 0.0039  94   HIS   B CD2 
5410 C  CE1 . HIS   B 94  ? 0.1361 0.1257 0.1231 -0.0119 -0.0167 0.0072  94   HIS   B CE1 
5411 N  NE2 . HIS   B 94  ? 0.1276 0.1317 0.1296 -0.0131 -0.0110 0.0048  94   HIS   B NE2 
5419 N  N   . VAL   B 95  ? 0.1187 0.1179 0.1235 0.0003  -0.0014 0.0038  95   VAL   B N   
5420 C  CA  . VAL   B 95  ? 0.1256 0.1225 0.1220 0.0006  -0.0011 0.0088  95   VAL   B CA  
5421 C  C   . VAL   B 95  ? 0.1335 0.1236 0.1160 0.0031  0.0073  0.0030  95   VAL   B C   
5422 O  O   . VAL   B 95  ? 0.1356 0.1208 0.1375 0.0087  0.0055  0.0121  95   VAL   B O   
5423 C  CB  . VAL   B 95  ? 0.1315 0.1230 0.1226 0.0012  -0.0088 0.0046  95   VAL   B CB  
5424 C  CG1 . VAL   B 95  ? 0.1424 0.1334 0.1323 -0.0042 -0.0011 0.0100  95   VAL   B CG1 
5425 C  CG2 . VAL   B 95  ? 0.1319 0.1203 0.1249 -0.0008 -0.0145 0.0035  95   VAL   B CG2 
5435 N  N   . VAL   B 96  ? 0.1372 0.1290 0.1266 0.0113  0.0075  0.0148  96   VAL   B N   
5436 C  CA  . VAL   B 96  ? 0.1422 0.1442 0.1136 0.0089  0.0084  0.0128  96   VAL   B CA  
5437 C  C   . VAL   B 96  ? 0.1453 0.1454 0.1249 0.0113  0.0138  0.0144  96   VAL   B C   
5438 O  O   . VAL   B 96  ? 0.1436 0.1526 0.1448 0.0046  0.0159  -0.0002 96   VAL   B O   
5439 C  CB  . VAL   B 96  ? 0.1480 0.1604 0.1221 0.0128  0.0083  0.0092  96   VAL   B CB  
5440 C  CG1 . VAL   B 96  ? 0.1462 0.1732 0.1343 0.0108  0.0119  0.0097  96   VAL   B CG1 
5441 C  CG2 . VAL   B 96  ? 0.1634 0.1615 0.1396 0.0079  0.0056  0.0027  96   VAL   B CG2 
5451 N  N   . GLY   B 97  ? 0.1464 0.1408 0.1331 0.0088  0.0098  0.0115  97   GLY   B N   
5452 C  CA  . GLY   B 97  ? 0.1597 0.1432 0.1297 0.0057  0.0135  0.0139  97   GLY   B CA  
5453 C  C   . GLY   B 97  ? 0.1775 0.1515 0.1387 0.0138  0.0142  0.0132  97   GLY   B C   
5454 O  O   . GLY   B 97  ? 0.1837 0.1591 0.1419 0.0071  0.0083  0.0164  97   GLY   B O   
5458 N  N   . PRO   B 98  ? 0.1852 0.1549 0.1566 0.0164  0.0292  0.0271  98   PRO   B N   
5459 C  CA  . PRO   B 98  ? 0.2006 0.1696 0.1642 0.0214  0.0386  0.0285  98   PRO   B CA  
5460 C  C   . PRO   B 98  ? 0.2121 0.1771 0.1239 0.0332  0.0410  0.0397  98   PRO   B C   
5461 O  O   . PRO   B 98  ? 0.2032 0.1716 0.1499 0.0339  0.0392  0.0376  98   PRO   B O   
5462 C  CB  . PRO   B 98  ? 0.1909 0.1767 0.1908 0.0144  0.0503  0.0353  98   PRO   B CB  
5463 C  CG  . PRO   B 98  ? 0.1845 0.1718 0.1889 0.0125  0.0425  0.0389  98   PRO   B CG  
5464 C  CD  . PRO   B 98  ? 0.1709 0.1596 0.1759 0.0166  0.0341  0.0352  98   PRO   B CD  
5472 N  N   . ASN   B 99  ? 0.2245 0.1913 0.1379 0.0401  0.0382  0.0237  99   ASN   B N   
5473 C  CA  . ASN   B 99  ? 0.2454 0.1946 0.1389 0.0479  0.0320  0.0374  99   ASN   B CA  
5474 C  C   . ASN   B 99  ? 0.2692 0.2195 0.1635 0.0404  0.0569  0.0622  99   ASN   B C   
5475 O  O   . ASN   B 99  ? 0.2853 0.2259 0.1750 0.0405  0.0470  0.0561  99   ASN   B O   
5476 C  CB  . ASN   B 99  ? 0.2494 0.1907 0.1569 0.0534  0.0186  0.0358  99   ASN   B CB  
5477 C  CG  . ASN   B 99  ? 0.2544 0.2000 0.1819 0.0497  0.0104  0.0294  99   ASN   B CG  
5478 O  OD1 . ASN   B 99  ? 0.2620 0.1965 0.2027 0.0564  0.0029  0.0318  99   ASN   B OD1 
5479 N  ND2 . ASN   B 99  ? 0.2538 0.2065 0.1875 0.0467  -0.0097 0.0240  99   ASN   B ND2 
5486 N  N   A VAL   B 100 ? 0.2891 0.2356 0.2117 0.0328  0.0511  0.0737  100  VAL   B N   
5487 N  N   B VAL   B 100 ? 0.2818 0.2318 0.2177 0.0271  0.0617  0.0825  100  VAL   B N   
5488 C  CA  A VAL   B 100 ? 0.3126 0.2517 0.2591 0.0284  0.0464  0.0851  100  VAL   B CA  
5489 C  CA  B VAL   B 100 ? 0.3041 0.2492 0.2732 0.0196  0.0657  0.0954  100  VAL   B CA  
5490 C  C   A VAL   B 100 ? 0.3311 0.2554 0.2567 0.0351  0.0495  0.1045  100  VAL   B C   
5491 C  C   B VAL   B 100 ? 0.3261 0.2517 0.2536 0.0303  0.0676  0.1111  100  VAL   B C   
5492 O  O   A VAL   B 100 ? 0.3366 0.2632 0.2615 0.0350  0.0512  0.0991  100  VAL   B O   
5493 O  O   B VAL   B 100 ? 0.3349 0.2656 0.2613 0.0296  0.0747  0.1001  100  VAL   B O   
5494 C  CB  A VAL   B 100 ? 0.3201 0.2634 0.3107 0.0179  0.0382  0.0821  100  VAL   B CB  
5495 C  CB  B VAL   B 100 ? 0.3125 0.2652 0.3524 0.0008  0.0604  0.1039  100  VAL   B CB  
5496 C  CG1 A VAL   B 100 ? 0.3233 0.2669 0.3294 0.0164  0.0369  0.0818  100  VAL   B CG1 
5497 C  CG1 B VAL   B 100 ? 0.3186 0.2718 0.3811 0.0001  0.0609  0.1085  100  VAL   B CG1 
5498 C  CG2 A VAL   B 100 ? 0.3222 0.2677 0.3276 0.0135  0.0362  0.0821  100  VAL   B CG2 
5499 C  CG2 B VAL   B 100 ? 0.3128 0.2696 0.3769 -0.0093 0.0610  0.1109  100  VAL   B CG2 
5518 N  N   . ASN   B 101 ? 0.3452 0.2569 0.2561 0.0411  0.0470  0.1212  101  ASN   B N   
5519 C  CA  . ASN   B 101 ? 0.3910 0.2852 0.2776 0.0447  0.0128  0.1262  101  ASN   B CA  
5520 C  C   . ASN   B 101 ? 0.4443 0.3353 0.2853 0.0434  -0.0056 0.1308  101  ASN   B C   
5521 O  O   . ASN   B 101 ? 0.4532 0.3497 0.2950 0.0502  -0.0093 0.1130  101  ASN   B O   
5522 C  CB  . ASN   B 101 ? 0.3855 0.2677 0.2989 0.0411  0.0095  0.1144  101  ASN   B CB  
5523 C  CG  . ASN   B 101 ? 0.3807 0.2541 0.2929 0.0337  0.0210  0.1127  101  ASN   B CG  
5524 O  OD1 . ASN   B 101 ? 0.3859 0.2542 0.3209 0.0239  0.0414  0.1049  101  ASN   B OD1 
5525 N  ND2 . ASN   B 101 ? 0.3753 0.2572 0.2776 0.0312  0.0120  0.0993  101  ASN   B ND2 
5533 N  N   A LYS   B 102 ? 0.4621 0.3590 0.3168 0.0349  -0.0038 0.1183  102  LYS   B N   
5534 N  N   B LYS   B 102 ? 0.4665 0.3545 0.3035 0.0362  -0.0011 0.1272  102  LYS   B N   
5535 C  CA  A LYS   B 102 ? 0.4775 0.3849 0.3444 0.0255  0.0040  0.0956  102  LYS   B CA  
5536 C  CA  B LYS   B 102 ? 0.4862 0.3839 0.3305 0.0245  0.0064  0.0967  102  LYS   B CA  
5537 C  C   A LYS   B 102 ? 0.4763 0.3858 0.3211 0.0247  0.0138  0.0987  102  LYS   B C   
5538 C  C   B LYS   B 102 ? 0.4833 0.3870 0.3027 0.0250  0.0130  0.0971  102  LYS   B C   
5539 O  O   A LYS   B 102 ? 0.4807 0.3900 0.3288 0.0247  0.0046  0.0940  102  LYS   B O   
5540 O  O   B LYS   B 102 ? 0.4914 0.3934 0.3124 0.0259  -0.0013 0.0861  102  LYS   B O   
5541 C  CB  A LYS   B 102 ? 0.4914 0.4070 0.4006 0.0182  0.0077  0.0676  102  LYS   B CB  
5542 C  CB  B LYS   B 102 ? 0.5049 0.4087 0.3964 0.0125  0.0149  0.0606  102  LYS   B CB  
5543 C  CG  A LYS   B 102 ? 0.5032 0.4261 0.4482 0.0127  0.0144  0.0424  102  LYS   B CG  
5544 C  CG  B LYS   B 102 ? 0.5214 0.4316 0.4563 0.0029  0.0278  0.0302  102  LYS   B CG  
5545 C  CD  A LYS   B 102 ? 0.5135 0.4415 0.4938 0.0088  0.0204  0.0221  102  LYS   B CD  
5546 C  CD  B LYS   B 102 ? 0.5370 0.4517 0.5190 -0.0044 0.0415  0.0079  102  LYS   B CD  
5547 C  CE  A LYS   B 102 ? 0.5211 0.4522 0.5265 0.0058  0.0227  0.0058  102  LYS   B CE  
5548 C  CE  B LYS   B 102 ? 0.5497 0.4670 0.5646 -0.0099 0.0473  -0.0119 102  LYS   B CE  
5549 N  NZ  A LYS   B 102 ? 0.5254 0.4580 0.5428 0.0044  0.0224  -0.0040 102  LYS   B NZ  
5550 N  NZ  B LYS   B 102 ? 0.5573 0.4757 0.5885 -0.0120 0.0463  -0.0258 102  LYS   B NZ  
5577 N  N   . GLY   B 103 ? 0.4676 0.3792 0.2961 0.0250  0.0331  0.1021  103  GLY   B N   
5578 C  CA  . GLY   B 103 ? 0.4422 0.3679 0.3007 0.0266  0.0608  0.0817  103  GLY   B CA  
5579 C  C   . GLY   B 103 ? 0.4116 0.3521 0.2883 0.0250  0.0874  0.0584  103  GLY   B C   
5580 O  O   . GLY   B 103 ? 0.4170 0.3593 0.2987 0.0268  0.0890  0.0534  103  GLY   B O   
5585 N  N   A GLU   B 104 ? 0.4005 0.3496 0.3012 0.0224  0.0770  0.0430  104  GLU   B N   
5586 N  N   B GLU   B 104 ? 0.3847 0.3294 0.2600 0.0258  0.1180  0.0448  104  GLU   B N   
5587 C  CA  A GLU   B 104 ? 0.3885 0.3472 0.3015 0.0202  0.0656  0.0260  104  GLU   B CA  
5588 C  CA  B GLU   B 104 ? 0.3590 0.3112 0.2237 0.0291  0.1322  0.0311  104  GLU   B CA  
5589 C  C   A GLU   B 104 ? 0.3876 0.3498 0.3171 0.0129  0.0727  0.0199  104  GLU   B C   
5590 C  C   B GLU   B 104 ? 0.3626 0.3151 0.2540 0.0138  0.1538  0.0335  104  GLU   B C   
5591 O  O   A GLU   B 104 ? 0.3897 0.3526 0.3236 0.0122  0.0705  0.0183  104  GLU   B O   
5592 O  O   B GLU   B 104 ? 0.3704 0.3207 0.2846 0.0111  0.1452  0.0307  104  GLU   B O   
5593 C  CB  A GLU   B 104 ? 0.3794 0.3418 0.2924 0.0247  0.0461  0.0114  104  GLU   B CB  
5594 C  CB  B GLU   B 104 ? 0.3382 0.2893 0.2033 0.0456  0.0984  0.0048  104  GLU   B CB  
5595 C  CG  A GLU   B 104 ? 0.3725 0.3389 0.2820 0.0293  0.0257  -0.0044 104  GLU   B CG  
5596 C  CG  B GLU   B 104 ? 0.3211 0.2762 0.1811 0.0603  0.0514  -0.0219 104  GLU   B CG  
5597 C  CD  A GLU   B 104 ? 0.3690 0.3379 0.2765 0.0327  0.0076  -0.0138 104  GLU   B CD  
5598 C  CD  B GLU   B 104 ? 0.3112 0.2683 0.1594 0.0665  0.0114  -0.0281 104  GLU   B CD  
5599 O  OE1 A GLU   B 104 ? 0.3656 0.3357 0.2672 0.0319  0.0073  -0.0137 104  GLU   B OE1 
5600 O  OE1 B GLU   B 104 ? 0.2918 0.2585 0.1293 0.0691  0.0168  -0.0207 104  GLU   B OE1 
5601 O  OE2 A GLU   B 104 ? 0.3701 0.3415 0.2831 0.0352  -0.0064 -0.0208 104  GLU   B OE2 
5602 O  OE2 B GLU   B 104 ? 0.3205 0.2795 0.1650 0.0596  -0.0245 -0.0360 104  GLU   B OE2 
5615 N  N   A ASP   B 105 ? 0.3845 0.3499 0.3248 0.0059  0.0787  0.0159  105  ASP   B N   
5616 N  N   B ASP   B 105 ? 0.3581 0.3142 0.2572 -0.0011 0.1695  0.0415  105  ASP   B N   
5617 C  CA  A ASP   B 105 ? 0.3834 0.3497 0.3404 -0.0006 0.0792  0.0077  105  ASP   B CA  
5618 C  CA  B ASP   B 105 ? 0.3619 0.3126 0.2791 -0.0130 0.1774  0.0352  105  ASP   B CA  
5619 C  C   A ASP   B 105 ? 0.3762 0.3379 0.3178 -0.0061 0.0779  0.0017  105  ASP   B C   
5620 C  C   B ASP   B 105 ? 0.3539 0.2787 0.2494 -0.0282 0.1669  0.0223  105  ASP   B C   
5621 O  O   A ASP   B 105 ? 0.3753 0.3364 0.3079 -0.0064 0.0798  0.0007  105  ASP   B O   
5622 O  O   B ASP   B 105 ? 0.3302 0.2661 0.2489 -0.0311 0.1633  0.0153  105  ASP   B O   
5623 C  CB  A ASP   B 105 ? 0.3883 0.3593 0.3782 -0.0007 0.0796  0.0037  105  ASP   B CB  
5624 C  CB  B ASP   B 105 ? 0.3763 0.3394 0.3505 -0.0079 0.1819  0.0277  105  ASP   B CB  
5625 C  CG  A ASP   B 105 ? 0.3929 0.3673 0.4147 -0.0030 0.0839  0.0015  105  ASP   B CG  
5626 C  CG  B ASP   B 105 ? 0.3896 0.3609 0.4115 -0.0102 0.1984  0.0278  105  ASP   B CG  
5627 O  OD1 A ASP   B 105 ? 0.3952 0.3702 0.4226 -0.0065 0.0874  0.0042  105  ASP   B OD1 
5628 O  OD1 B ASP   B 105 ? 0.3920 0.3675 0.4150 -0.0217 0.2093  0.0414  105  ASP   B OD1 
5629 O  OD2 A ASP   B 105 ? 0.3937 0.3703 0.4319 -0.0021 0.0824  -0.0027 105  ASP   B OD2 
5630 O  OD2 B ASP   B 105 ? 0.3933 0.3712 0.4476 -0.0065 0.2038  0.0207  105  ASP   B OD2 
5639 N  N   A ILE   B 106 ? 0.3683 0.3268 0.3113 -0.0102 0.0712  -0.0014 106  ILE   B N   
5640 N  N   B ILE   B 106 ? 0.3536 0.2597 0.2664 -0.0372 0.1529  0.0190  106  ILE   B N   
5641 C  CA  A ILE   B 106 ? 0.3570 0.3147 0.3080 -0.0140 0.0681  -0.0055 106  ILE   B CA  
5642 C  CA  B ILE   B 106 ? 0.3454 0.2380 0.2714 -0.0494 0.1525  0.0096  106  ILE   B CA  
5643 C  C   A ILE   B 106 ? 0.3401 0.3090 0.3049 -0.0118 0.0665  -0.0125 106  ILE   B C   
5644 C  C   B ILE   B 106 ? 0.3182 0.2365 0.2578 -0.0455 0.1583  -0.0066 106  ILE   B C   
5645 O  O   A ILE   B 106 ? 0.3384 0.3042 0.3072 -0.0123 0.0632  -0.0163 106  ILE   B O   
5646 O  O   B ILE   B 106 ? 0.3095 0.2178 0.2555 -0.0511 0.1601  -0.0096 106  ILE   B O   
5647 C  CB  A ILE   B 106 ? 0.3617 0.3100 0.3103 -0.0193 0.0677  -0.0029 106  ILE   B CB  
5648 C  CB  B ILE   B 106 ? 0.3646 0.2296 0.2923 -0.0607 0.1441  0.0160  106  ILE   B CB  
5649 C  CG1 A ILE   B 106 ? 0.3618 0.3062 0.3074 -0.0178 0.0664  -0.0022 106  ILE   B CG1 
5650 C  CG1 B ILE   B 106 ? 0.3730 0.2294 0.3000 -0.0490 0.1344  0.0109  106  ILE   B CG1 
5651 C  CG2 A ILE   B 106 ? 0.3654 0.3118 0.3177 -0.0231 0.0673  -0.0017 106  ILE   B CG2 
5652 C  CG2 B ILE   B 106 ? 0.3727 0.2341 0.3160 -0.0729 0.1400  0.0185  106  ILE   B CG2 
5653 C  CD1 A ILE   B 106 ? 0.3612 0.3043 0.3034 -0.0159 0.0645  0.0000  106  ILE   B CD1 
5654 C  CD1 B ILE   B 106 ? 0.3764 0.2311 0.2984 -0.0397 0.1275  0.0132  106  ILE   B CD1 
5677 N  N   A GLN   B 107 ? 0.3256 0.3089 0.3139 -0.0107 0.0669  -0.0139 107  GLN   B N   
5678 N  N   B GLN   B 107 ? 0.3031 0.2579 0.2846 -0.0392 0.1519  -0.0144 107  GLN   B N   
5679 C  CA  A GLN   B 107 ? 0.3097 0.3064 0.3239 -0.0086 0.0659  -0.0102 107  GLN   B CA  
5680 C  CA  B GLN   B 107 ? 0.2839 0.2794 0.3087 -0.0333 0.1455  -0.0073 107  GLN   B CA  
5681 C  C   A GLN   B 107 ? 0.2724 0.2781 0.2877 -0.0039 0.0698  -0.0116 107  GLN   B C   
5682 C  C   B GLN   B 107 ? 0.2524 0.2644 0.2806 -0.0188 0.1129  -0.0127 107  GLN   B C   
5683 O  O   A GLN   B 107 ? 0.2696 0.2790 0.3010 -0.0002 0.0558  -0.0250 107  GLN   B O   
5684 O  O   B GLN   B 107 ? 0.2435 0.2678 0.3225 -0.0094 0.0805  -0.0420 107  GLN   B O   
5685 C  CB  A GLN   B 107 ? 0.3314 0.3310 0.3777 -0.0077 0.0547  -0.0064 107  GLN   B CB  
5686 C  CB  B GLN   B 107 ? 0.3136 0.3187 0.3831 -0.0290 0.1280  -0.0019 107  GLN   B CB  
5687 C  CG  A GLN   B 107 ? 0.3493 0.3515 0.4304 -0.0059 0.0399  -0.0022 107  GLN   B CG  
5688 C  CG  B GLN   B 107 ? 0.3461 0.3554 0.4641 -0.0198 0.0896  0.0004  107  GLN   B CG  
5689 C  CD  A GLN   B 107 ? 0.3607 0.3666 0.4742 -0.0063 0.0299  0.0034  107  GLN   B CD  
5690 C  CD  B GLN   B 107 ? 0.3691 0.3851 0.5278 -0.0169 0.0640  0.0077  107  GLN   B CD  
5691 O  OE1 A GLN   B 107 ? 0.3653 0.3733 0.4902 -0.0077 0.0292  0.0046  107  GLN   B OE1 
5692 O  OE1 B GLN   B 107 ? 0.3805 0.3974 0.5505 -0.0194 0.0617  0.0094  107  GLN   B OE1 
5693 N  NE2 A GLN   B 107 ? 0.3650 0.3707 0.4899 -0.0043 0.0250  0.0068  107  GLN   B NE2 
5694 N  NE2 B GLN   B 107 ? 0.3775 0.3936 0.5501 -0.0112 0.0518  0.0124  107  GLN   B NE2 
5711 N  N   . LEU   B 108 ? 0.2388 0.2491 0.2542 0.0007  0.0834  -0.0065 108  LEU   B N   
5712 C  CA  . LEU   B 108 ? 0.2148 0.2228 0.2070 0.0216  0.0587  0.0052  108  LEU   B CA  
5713 C  C   . LEU   B 108 ? 0.1895 0.1836 0.2074 0.0288  0.0342  0.0244  108  LEU   B C   
5714 O  O   . LEU   B 108 ? 0.1863 0.1749 0.1984 0.0314  0.0271  0.0217  108  LEU   B O   
5715 C  CB  . LEU   B 108 ? 0.2297 0.2417 0.1831 0.0209  0.0620  0.0066  108  LEU   B CB  
5716 C  CG  . LEU   B 108 ? 0.2423 0.2698 0.1984 0.0222  0.0499  -0.0193 108  LEU   B CG  
5717 C  CD1 . LEU   B 108 ? 0.2494 0.2814 0.1829 0.0143  0.0428  -0.0115 108  LEU   B CD1 
5718 C  CD2 . LEU   B 108 ? 0.2536 0.2799 0.2158 0.0302  0.0397  -0.0344 108  LEU   B CD2 
5731 N  N   . LEU   B 109 ? 0.1777 0.1567 0.1979 0.0254  0.0330  0.0330  109  LEU   B N   
5732 C  CA  . LEU   B 109 ? 0.1598 0.1392 0.2081 0.0170  0.0359  0.0290  109  LEU   B CA  
5733 C  C   . LEU   B 109 ? 0.1481 0.1227 0.2035 0.0065  0.0359  0.0213  109  LEU   B C   
5734 O  O   . LEU   B 109 ? 0.1437 0.1249 0.1991 0.0073  0.0322  0.0281  109  LEU   B O   
5735 C  CB  . LEU   B 109 ? 0.1706 0.1341 0.2026 0.0070  0.0257  0.0319  109  LEU   B CB  
5736 C  CG  . LEU   B 109 ? 0.1713 0.1324 0.1961 0.0072  0.0176  0.0174  109  LEU   B CG  
5737 C  CD1 . LEU   B 109 ? 0.1668 0.1431 0.1884 0.0042  0.0249  0.0222  109  LEU   B CD1 
5738 C  CD2 . LEU   B 109 ? 0.1833 0.1384 0.2094 0.0045  0.0165  0.0170  109  LEU   B CD2 
5750 N  N   . LYS   B 110 ? 0.1416 0.1280 0.1990 -0.0021 0.0334  0.0230  110  LYS   B N   
5751 C  CA  . LYS   B 110 ? 0.1431 0.1243 0.2027 0.0000  0.0282  0.0128  110  LYS   B CA  
5752 C  C   . LYS   B 110 ? 0.1340 0.1264 0.1920 0.0030  0.0282  0.0110  110  LYS   B C   
5753 O  O   . LYS   B 110 ? 0.1333 0.1275 0.1862 -0.0027 0.0213  0.0113  110  LYS   B O   
5754 C  CB  . LYS   B 110 ? 0.1461 0.1256 0.2165 -0.0027 0.0285  0.0090  110  LYS   B CB  
5755 C  CG  . LYS   B 110 ? 0.1410 0.1300 0.2253 -0.0071 0.0118  0.0154  110  LYS   B CG  
5756 C  CD  . LYS   B 110 ? 0.1457 0.1305 0.2232 -0.0078 0.0191  0.0138  110  LYS   B CD  
5757 C  CE  . LYS   B 110 ? 0.1453 0.1435 0.2509 -0.0055 0.0131  0.0046  110  LYS   B CE  
5758 N  NZ  . LYS   B 110 ? 0.1443 0.1511 0.2447 0.0045  0.0104  0.0046  110  LYS   B NZ  
5772 N  N   . SER   B 111 ? 0.1389 0.1267 0.1960 0.0019  0.0259  0.0151  111  SER   B N   
5773 C  CA  . SER   B 111 ? 0.1455 0.1305 0.1826 0.0037  0.0176  0.0196  111  SER   B CA  
5774 C  C   . SER   B 111 ? 0.1393 0.1284 0.1668 0.0006  0.0108  0.0078  111  SER   B C   
5775 O  O   . SER   B 111 ? 0.1388 0.1326 0.1788 -0.0043 0.0087  0.0081  111  SER   B O   
5776 C  CB  . SER   B 111 ? 0.1640 0.1511 0.1864 0.0103  0.0320  0.0282  111  SER   B CB  
5777 O  OG  . SER   B 111 ? 0.1869 0.1870 0.1947 0.0103  0.0370  0.0253  111  SER   B OG  
5783 N  N   . ALA   B 112 ? 0.1351 0.1319 0.1749 0.0058  0.0226  0.0201  112  ALA   B N   
5784 C  CA  . ALA   B 112 ? 0.1331 0.1336 0.1631 0.0022  0.0090  0.0073  112  ALA   B CA  
5785 C  C   . ALA   B 112 ? 0.1287 0.1177 0.1627 0.0048  0.0114  0.0074  112  ALA   B C   
5786 O  O   . ALA   B 112 ? 0.1287 0.1235 0.1709 -0.0030 0.0102  0.0066  112  ALA   B O   
5787 C  CB  . ALA   B 112 ? 0.1431 0.1436 0.1708 0.0066  0.0155  0.0206  112  ALA   B CB  
5793 N  N   . TYR   B 113 ? 0.1223 0.1100 0.1732 -0.0004 0.0130  0.0130  113  TYR   B N   
5794 C  CA  . TYR   B 113 ? 0.1238 0.1154 0.1632 -0.0025 0.0168  0.0028  113  TYR   B CA  
5795 C  C   . TYR   B 113 ? 0.1195 0.1127 0.1579 -0.0075 0.0120  0.0001  113  TYR   B C   
5796 O  O   . TYR   B 113 ? 0.1217 0.1145 0.1635 -0.0044 0.0105  -0.0004 113  TYR   B O   
5797 C  CB  . TYR   B 113 ? 0.1294 0.1113 0.1713 0.0017  0.0211  0.0085  113  TYR   B CB  
5798 C  CG  . TYR   B 113 ? 0.1297 0.1108 0.1801 -0.0007 0.0095  0.0126  113  TYR   B CG  
5799 C  CD1 . TYR   B 113 ? 0.1357 0.1080 0.1910 -0.0018 0.0115  0.0170  113  TYR   B CD1 
5800 C  CD2 . TYR   B 113 ? 0.1337 0.1157 0.1774 -0.0046 0.0048  0.0082  113  TYR   B CD2 
5801 C  CE1 . TYR   B 113 ? 0.1350 0.1151 0.1861 -0.0033 0.0158  0.0098  113  TYR   B CE1 
5802 C  CE2 . TYR   B 113 ? 0.1378 0.1082 0.1863 0.0000  0.0114  0.0117  113  TYR   B CE2 
5803 C  CZ  . TYR   B 113 ? 0.1361 0.1185 0.1999 0.0062  0.0129  0.0020  113  TYR   B CZ  
5804 O  OH  . TYR   B 113 ? 0.1456 0.1177 0.2163 0.0091  0.0212  0.0062  113  TYR   B OH  
5814 N  N   . GLU   B 114 ? 0.1188 0.1081 0.1699 -0.0025 0.0113  0.0005  114  GLU   B N   
5815 C  CA  . GLU   B 114 ? 0.1208 0.1070 0.1655 0.0037  0.0028  0.0043  114  GLU   B CA  
5816 C  C   . GLU   B 114 ? 0.1213 0.1069 0.1567 -0.0017 0.0129  -0.0014 114  GLU   B C   
5817 O  O   . GLU   B 114 ? 0.1240 0.1100 0.1711 -0.0016 0.0079  0.0108  114  GLU   B O   
5818 C  CB  . GLU   B 114 ? 0.1206 0.1109 0.1673 -0.0009 0.0083  0.0063  114  GLU   B CB  
5819 C  CG  . GLU   B 114 ? 0.1267 0.1147 0.1822 0.0002  0.0100  0.0076  114  GLU   B CG  
5820 C  CD  . GLU   B 114 ? 0.1211 0.1194 0.1878 -0.0037 0.0093  0.0005  114  GLU   B CD  
5821 O  OE1 . GLU   B 114 ? 0.1229 0.1348 0.1780 -0.0018 0.0180  0.0068  114  GLU   B OE1 
5822 O  OE2 . GLU   B 114 ? 0.1217 0.1370 0.2138 -0.0132 0.0128  0.0120  114  GLU   B OE2 
5829 N  N   . ASN   B 115 ? 0.1142 0.1123 0.1628 -0.0067 0.0038  0.0085  115  ASN   B N   
5830 C  CA  . ASN   B 115 ? 0.1216 0.1145 0.1546 -0.0081 0.0030  0.0014  115  ASN   B CA  
5831 C  C   . ASN   B 115 ? 0.1219 0.1093 0.1552 -0.0063 -0.0009 0.0039  115  ASN   B C   
5832 O  O   . ASN   B 115 ? 0.1296 0.1186 0.1553 -0.0137 0.0040  0.0023  115  ASN   B O   
5833 C  CB  . ASN   B 115 ? 0.1301 0.1225 0.1616 -0.0069 0.0073  -0.0028 115  ASN   B CB  
5834 C  CG  . ASN   B 115 ? 0.1388 0.1260 0.1607 0.0022  0.0045  -0.0048 115  ASN   B CG  
5835 O  OD1 . ASN   B 115 ? 0.1785 0.1434 0.1684 -0.0029 0.0079  -0.0099 115  ASN   B OD1 
5836 N  ND2 . ASN   B 115 ? 0.1380 0.1345 0.1594 -0.0013 0.0031  0.0081  115  ASN   B ND2 
5843 N  N   . PHE   B 116 ? 0.1241 0.1121 0.1421 -0.0042 -0.0070 0.0024  116  PHE   B N   
5844 C  CA  . PHE   B 116 ? 0.1206 0.1157 0.1466 -0.0114 -0.0073 0.0057  116  PHE   B CA  
5845 C  C   . PHE   B 116 ? 0.1248 0.1091 0.1474 -0.0065 -0.0019 0.0071  116  PHE   B C   
5846 O  O   . PHE   B 116 ? 0.1288 0.1205 0.1532 -0.0064 0.0009  0.0045  116  PHE   B O   
5847 C  CB  . PHE   B 116 ? 0.1189 0.1129 0.1422 0.0006  -0.0081 0.0024  116  PHE   B CB  
5848 C  CG  . PHE   B 116 ? 0.1156 0.1138 0.1395 -0.0070 -0.0043 0.0012  116  PHE   B CG  
5849 C  CD1 . PHE   B 116 ? 0.1324 0.1159 0.1597 -0.0001 0.0024  0.0047  116  PHE   B CD1 
5850 C  CD2 . PHE   B 116 ? 0.1233 0.1238 0.1367 -0.0035 0.0022  0.0018  116  PHE   B CD2 
5851 C  CE1 . PHE   B 116 ? 0.1307 0.1194 0.1643 -0.0016 -0.0077 0.0082  116  PHE   B CE1 
5852 C  CE2 . PHE   B 116 ? 0.1247 0.1217 0.1421 -0.0000 0.0049  -0.0023 116  PHE   B CE2 
5853 C  CZ  . PHE   B 116 ? 0.1184 0.1234 0.1524 -0.0004 -0.0031 0.0072  116  PHE   B CZ  
5863 N  N   . ASN   B 117 ? 0.1235 0.1133 0.1631 -0.0052 -0.0098 0.0057  117  ASN   B N   
5864 C  CA  . ASN   B 117 ? 0.1293 0.1158 0.1599 0.0003  -0.0080 0.0001  117  ASN   B CA  
5865 C  C   . ASN   B 117 ? 0.1321 0.1140 0.1659 -0.0003 -0.0085 0.0093  117  ASN   B C   
5866 O  O   . ASN   B 117 ? 0.1380 0.1207 0.1929 -0.0031 -0.0274 0.0099  117  ASN   B O   
5867 C  CB  . ASN   B 117 ? 0.1259 0.1195 0.1584 -0.0026 -0.0046 0.0023  117  ASN   B CB  
5868 C  CG  . ASN   B 117 ? 0.1281 0.1189 0.1776 0.0024  0.0004  -0.0026 117  ASN   B CG  
5869 O  OD1 . ASN   B 117 ? 0.1441 0.1212 0.1845 -0.0141 0.0045  -0.0029 117  ASN   B OD1 
5870 N  ND2 . ASN   B 117 ? 0.1285 0.1261 0.1726 -0.0060 0.0029  -0.0026 117  ASN   B ND2 
5877 N  N   . GLN   B 118 ? 0.1321 0.1107 0.1551 -0.0041 -0.0136 0.0041  118  GLN   B N   
5878 C  CA  . GLN   B 118 ? 0.1350 0.1153 0.1692 -0.0011 -0.0065 0.0029  118  GLN   B CA  
5879 C  C   . GLN   B 118 ? 0.1359 0.1092 0.1772 -0.0012 -0.0011 0.0029  118  GLN   B C   
5880 O  O   . GLN   B 118 ? 0.1510 0.1179 0.2113 -0.0058 0.0063  0.0057  118  GLN   B O   
5881 C  CB  . GLN   B 118 ? 0.1433 0.1157 0.1797 0.0038  -0.0132 0.0037  118  GLN   B CB  
5882 C  CG  . GLN   B 118 ? 0.1532 0.1217 0.1716 0.0105  -0.0028 -0.0079 118  GLN   B CG  
5883 C  CD  . GLN   B 118 ? 0.1545 0.1194 0.1683 0.0066  -0.0020 -0.0043 118  GLN   B CD  
5884 O  OE1 . GLN   B 118 ? 0.1574 0.1153 0.1966 0.0037  0.0099  0.0051  118  GLN   B OE1 
5885 N  NE2 . GLN   B 118 ? 0.1595 0.1198 0.1829 0.0025  -0.0176 0.0109  118  GLN   B NE2 
5894 N  N   . HIS   B 119 ? 0.1392 0.1128 0.1529 -0.0106 -0.0057 0.0111  119  HIS   B N   
5895 C  CA  . HIS   B 119 ? 0.1544 0.1264 0.1462 -0.0042 -0.0085 0.0094  119  HIS   B CA  
5896 C  C   . HIS   B 119 ? 0.1525 0.1263 0.1494 -0.0028 -0.0201 0.0080  119  HIS   B C   
5897 O  O   . HIS   B 119 ? 0.1603 0.1313 0.1608 -0.0253 -0.0094 0.0081  119  HIS   B O   
5898 C  CB  . HIS   B 119 ? 0.1565 0.1426 0.1510 0.0061  -0.0115 0.0051  119  HIS   B CB  
5899 C  CG  . HIS   B 119 ? 0.1598 0.1631 0.1667 0.0124  -0.0353 -0.0103 119  HIS   B CG  
5900 N  ND1 . HIS   B 119 ? 0.1684 0.1787 0.2138 0.0055  -0.0466 -0.0279 119  HIS   B ND1 
5901 C  CD2 . HIS   B 119 ? 0.1763 0.1822 0.1619 0.0334  -0.0391 -0.0145 119  HIS   B CD2 
5902 C  CE1 . HIS   B 119 ? 0.1847 0.1900 0.2050 0.0175  -0.0535 -0.0384 119  HIS   B CE1 
5903 N  NE2 . HIS   B 119 ? 0.1927 0.2015 0.1886 0.0312  -0.0439 -0.0265 119  HIS   B NE2 
5911 N  N   . GLU   B 120 ? 0.1720 0.1324 0.1396 -0.0105 -0.0296 0.0144  120  GLU   B N   
5912 C  CA  . GLU   B 120 ? 0.1945 0.1434 0.1530 -0.0052 -0.0367 0.0232  120  GLU   B CA  
5913 C  C   . GLU   B 120 ? 0.1735 0.1363 0.1428 -0.0117 -0.0280 0.0243  120  GLU   B C   
5914 O  O   . GLU   B 120 ? 0.1654 0.1474 0.1474 -0.0139 -0.0304 0.0091  120  GLU   B O   
5915 C  CB  . GLU   B 120 ? 0.2495 0.1748 0.2202 0.0123  -0.0703 0.0428  120  GLU   B CB  
5916 C  CG  . GLU   B 120 ? 0.3011 0.2490 0.3256 0.0273  -0.0955 0.0649  120  GLU   B CG  
5917 C  CD  . GLU   B 120 ? 0.3504 0.3243 0.4328 0.0297  -0.1036 0.0902  120  GLU   B CD  
5918 O  OE1 . GLU   B 120 ? 0.3788 0.3669 0.4616 0.0277  -0.1012 0.1083  120  GLU   B OE1 
5919 O  OE2 . GLU   B 120 ? 0.3630 0.3501 0.4891 0.0241  -0.1044 0.0836  120  GLU   B OE2 
5926 N  N   . VAL   B 121 ? 0.1615 0.1300 0.1475 -0.0176 -0.0188 0.0215  121  VAL   B N   
5927 C  CA  . VAL   B 121 ? 0.1574 0.1371 0.1332 -0.0151 -0.0169 0.0152  121  VAL   B CA  
5928 C  C   . VAL   B 121 ? 0.1548 0.1341 0.1228 -0.0206 -0.0120 0.0087  121  VAL   B C   
5929 O  O   . VAL   B 121 ? 0.1645 0.1304 0.1462 -0.0253 -0.0193 0.0078  121  VAL   B O   
5930 C  CB  . VAL   B 121 ? 0.1789 0.1727 0.1565 -0.0063 -0.0249 0.0201  121  VAL   B CB  
5931 C  CG1 . VAL   B 121 ? 0.1837 0.1814 0.1920 -0.0166 -0.0127 0.0243  121  VAL   B CG1 
5932 C  CG2 . VAL   B 121 ? 0.2030 0.1946 0.1661 0.0015  -0.0127 0.0090  121  VAL   B CG2 
5942 N  N   . LEU   B 122 ? 0.1481 0.1256 0.1224 -0.0137 -0.0182 0.0045  122  LEU   B N   
5943 C  CA  . LEU   B 122 ? 0.1381 0.1304 0.1156 -0.0198 -0.0085 0.0027  122  LEU   B CA  
5944 C  C   . LEU   B 122 ? 0.1360 0.1210 0.1199 -0.0257 -0.0098 0.0100  122  LEU   B C   
5945 O  O   . LEU   B 122 ? 0.1473 0.1267 0.1549 -0.0283 -0.0185 0.0054  122  LEU   B O   
5946 C  CB  . LEU   B 122 ? 0.1583 0.1449 0.1478 -0.0053 -0.0137 0.0088  122  LEU   B CB  
5947 C  CG  . LEU   B 122 ? 0.1479 0.1542 0.1582 -0.0078 -0.0026 0.0074  122  LEU   B CG  
5948 C  CD1 . LEU   B 122 ? 0.1523 0.1791 0.1588 -0.0126 -0.0048 0.0007  122  LEU   B CD1 
5949 C  CD2 . LEU   B 122 ? 0.1460 0.1540 0.1455 -0.0092 -0.0060 -0.0002 122  LEU   B CD2 
5961 N  N   . LEU   B 123 ? 0.1364 0.1151 0.1207 -0.0264 -0.0106 0.0043  123  LEU   B N   
5962 C  CA  . LEU   B 123 ? 0.1428 0.1200 0.1227 -0.0221 -0.0170 -0.0077 123  LEU   B CA  
5963 C  C   . LEU   B 123 ? 0.1318 0.1166 0.1202 -0.0194 -0.0094 -0.0026 123  LEU   B C   
5964 O  O   . LEU   B 123 ? 0.1458 0.1206 0.1244 -0.0279 -0.0131 -0.0005 123  LEU   B O   
5965 C  CB  . LEU   B 123 ? 0.1404 0.1245 0.1391 -0.0199 -0.0078 -0.0026 123  LEU   B CB  
5966 C  CG  . LEU   B 123 ? 0.1449 0.1300 0.1426 -0.0125 -0.0025 0.0062  123  LEU   B CG  
5967 C  CD1 . LEU   B 123 ? 0.1552 0.1320 0.1450 -0.0160 0.0024  -0.0093 123  LEU   B CD1 
5968 C  CD2 . LEU   B 123 ? 0.1514 0.1387 0.1665 -0.0174 0.0019  0.0224  123  LEU   B CD2 
5980 N  N   . ALA   B 124 ? 0.1288 0.1155 0.1319 -0.0199 0.0045  -0.0012 124  ALA   B N   
5981 C  CA  . ALA   B 124 ? 0.1304 0.1151 0.1337 -0.0133 -0.0024 -0.0057 124  ALA   B CA  
5982 C  C   . ALA   B 124 ? 0.1243 0.1181 0.1340 -0.0183 -0.0053 -0.0074 124  ALA   B C   
5983 O  O   . ALA   B 124 ? 0.1359 0.1191 0.1456 -0.0140 -0.0061 0.0006  124  ALA   B O   
5984 C  CB  . ALA   B 124 ? 0.1323 0.1190 0.1348 -0.0059 0.0086  -0.0010 124  ALA   B CB  
5990 N  N   . PRO   B 125 ? 0.1350 0.1224 0.1314 -0.0164 -0.0103 0.0052  125  PRO   B N   
5991 C  CA  . PRO   B 125 ? 0.1415 0.1256 0.1425 -0.0177 -0.0124 0.0185  125  PRO   B CA  
5992 C  C   . PRO   B 125 ? 0.1391 0.1154 0.1474 -0.0159 -0.0040 0.0075  125  PRO   B C   
5993 O  O   . PRO   B 125 ? 0.1394 0.1130 0.1741 -0.0068 0.0018  0.0120  125  PRO   B O   
5994 C  CB  . PRO   B 125 ? 0.1444 0.1442 0.1651 -0.0218 -0.0162 0.0329  125  PRO   B CB  
5995 C  CG  . PRO   B 125 ? 0.1570 0.1474 0.1443 -0.0291 -0.0148 0.0149  125  PRO   B CG  
5996 C  CD  . PRO   B 125 ? 0.1504 0.1281 0.1377 -0.0303 -0.0106 0.0056  125  PRO   B CD  
6004 N  N   . LEU   B 126 ? 0.1469 0.1087 0.1746 -0.0102 0.0075  0.0127  126  LEU   B N   
6005 C  CA  . LEU   B 126 ? 0.1511 0.1235 0.1786 -0.0084 0.0216  0.0096  126  LEU   B CA  
6006 C  C   . LEU   B 126 ? 0.1470 0.1285 0.1863 0.0010  0.0178  0.0185  126  LEU   B C   
6007 O  O   . LEU   B 126 ? 0.1667 0.1539 0.1999 0.0206  -0.0006 -0.0049 126  LEU   B O   
6008 C  CB  . LEU   B 126 ? 0.1659 0.1247 0.2065 -0.0156 0.0330  0.0069  126  LEU   B CB  
6009 C  CG  . LEU   B 126 ? 0.1822 0.1347 0.2148 -0.0238 0.0334  -0.0082 126  LEU   B CG  
6010 C  CD1 . LEU   B 126 ? 0.1965 0.1392 0.2680 -0.0174 0.0249  -0.0228 126  LEU   B CD1 
6011 C  CD2 . LEU   B 126 ? 0.1876 0.1522 0.2094 -0.0341 0.0223  -0.0039 126  LEU   B CD2 
6023 N  N   . LEU   B 127 ? 0.1412 0.1195 0.1842 0.0014  0.0237  0.0062  127  LEU   B N   
6024 C  CA  . LEU   B 127 ? 0.1436 0.1290 0.1838 -0.0031 0.0194  0.0187  127  LEU   B CA  
6025 C  C   . LEU   B 127 ? 0.1416 0.1225 0.1847 -0.0010 0.0167  0.0169  127  LEU   B C   
6026 O  O   . LEU   B 127 ? 0.1439 0.1244 0.1900 -0.0143 0.0091  0.0166  127  LEU   B O   
6027 C  CB  . LEU   B 127 ? 0.1538 0.1245 0.1901 -0.0022 0.0234  0.0191  127  LEU   B CB  
6028 C  CG  . LEU   B 127 ? 0.1644 0.1281 0.2048 0.0002  0.0281  0.0125  127  LEU   B CG  
6029 C  CD1 . LEU   B 127 ? 0.1652 0.1248 0.2077 0.0030  0.0184  0.0051  127  LEU   B CD1 
6030 C  CD2 . LEU   B 127 ? 0.1693 0.1375 0.2187 -0.0015 0.0341  0.0270  127  LEU   B CD2 
6042 N  N   . SER   B 128 ? 0.1430 0.1220 0.1839 0.0049  0.0041  0.0137  128  SER   B N   
6043 C  CA  . SER   B 128 ? 0.1533 0.1322 0.1816 0.0139  0.0011  0.0145  128  SER   B CA  
6044 C  C   . SER   B 128 ? 0.1689 0.1386 0.1995 0.0089  -0.0187 0.0167  128  SER   B C   
6045 O  O   . SER   B 128 ? 0.1813 0.1373 0.2507 0.0099  -0.0137 0.0241  128  SER   B O   
6046 C  CB  . SER   B 128 ? 0.1619 0.1382 0.1849 0.0104  0.0105  0.0251  128  SER   B CB  
6047 O  OG  . SER   B 128 ? 0.1719 0.1523 0.1867 0.0122  0.0099  0.0291  128  SER   B OG  
6053 N  N   . ALA   B 129 ? 0.1821 0.1411 0.2092 0.0302  -0.0103 0.0016  129  ALA   B N   
6054 C  CA  . ALA   B 129 ? 0.2032 0.1475 0.2225 0.0344  -0.0105 -0.0095 129  ALA   B CA  
6055 C  C   . ALA   B 129 ? 0.1881 0.1428 0.2212 0.0294  0.0083  -0.0064 129  ALA   B C   
6056 O  O   . ALA   B 129 ? 0.1747 0.1472 0.2195 0.0201  0.0009  0.0046  129  ALA   B O   
6057 C  CB  . ALA   B 129 ? 0.2306 0.1617 0.2573 0.0415  0.0017  -0.0269 129  ALA   B CB  
6063 N  N   . GLY   B 130 ? 0.1837 0.1402 0.2284 0.0285  0.0088  -0.0068 130  GLY   B N   
6064 C  CA  . GLY   B 130 ? 0.1894 0.1493 0.2312 0.0266  0.0240  0.0034  130  GLY   B CA  
6065 C  C   . GLY   B 130 ? 0.1915 0.1496 0.2349 0.0262  0.0125  0.0058  130  GLY   B C   
6066 O  O   . GLY   B 130 ? 0.2068 0.1625 0.2388 0.0245  0.0068  0.0134  130  GLY   B O   
6070 N  N   . ILE   B 131 ? 0.1828 0.1648 0.2421 0.0371  0.0040  0.0086  131  ILE   B N   
6071 C  CA  . ILE   B 131 ? 0.1972 0.1841 0.2376 0.0334  -0.0047 0.0210  131  ILE   B CA  
6072 C  C   . ILE   B 131 ? 0.2114 0.1739 0.2036 0.0246  -0.0056 0.0295  131  ILE   B C   
6073 O  O   . ILE   B 131 ? 0.2313 0.1863 0.2055 0.0282  -0.0209 0.0265  131  ILE   B O   
6074 C  CB  . ILE   B 131 ? 0.1958 0.2255 0.2770 0.0313  -0.0123 0.0253  131  ILE   B CB  
6075 C  CG1 . ILE   B 131 ? 0.1999 0.2521 0.2907 0.0017  -0.0041 0.0339  131  ILE   B CG1 
6076 C  CG2 . ILE   B 131 ? 0.2006 0.2434 0.3033 0.0376  -0.0021 0.0143  131  ILE   B CG2 
6077 C  CD1 . ILE   B 131 ? 0.2081 0.2748 0.3023 -0.0173 0.0031  0.0415  131  ILE   B CD1 
6089 N  N   . PHE   B 132 ? 0.1972 0.1520 0.1969 0.0211  0.0104  0.0250  132  PHE   B N   
6090 C  CA  . PHE   B 132 ? 0.2050 0.1568 0.1886 0.0060  0.0293  0.0152  132  PHE   B CA  
6091 C  C   . PHE   B 132 ? 0.2244 0.1681 0.1982 0.0087  0.0397  0.0144  132  PHE   B C   
6092 O  O   . PHE   B 132 ? 0.2396 0.1892 0.2277 0.0086  0.0487  0.0211  132  PHE   B O   
6093 C  CB  . PHE   B 132 ? 0.1881 0.1537 0.1760 0.0106  0.0343  0.0175  132  PHE   B CB  
6094 C  CG  . PHE   B 132 ? 0.1809 0.1529 0.1663 0.0181  0.0280  0.0129  132  PHE   B CG  
6095 C  CD1 . PHE   B 132 ? 0.1937 0.1593 0.2136 0.0137  0.0269  0.0152  132  PHE   B CD1 
6096 C  CD2 . PHE   B 132 ? 0.1857 0.1577 0.1426 0.0200  0.0209  0.0224  132  PHE   B CD2 
6097 C  CE1 . PHE   B 132 ? 0.1996 0.1591 0.2259 0.0100  0.0215  0.0137  132  PHE   B CE1 
6098 C  CE2 . PHE   B 132 ? 0.1933 0.1610 0.1537 0.0198  0.0184  0.0154  132  PHE   B CE2 
6099 C  CZ  . PHE   B 132 ? 0.1983 0.1576 0.1934 0.0126  0.0056  0.0238  132  PHE   B CZ  
6109 N  N   . GLY   B 133 ? 0.2238 0.1564 0.2036 0.0099  0.0288  0.0273  133  GLY   B N   
6110 C  CA  . GLY   B 133 ? 0.2282 0.1660 0.2277 -0.0072 0.0309  0.0446  133  GLY   B CA  
6111 C  C   . GLY   B 133 ? 0.2316 0.1807 0.2294 -0.0226 0.0373  0.0443  133  GLY   B C   
6112 O  O   . GLY   B 133 ? 0.2483 0.1951 0.2841 -0.0403 0.0269  0.0595  133  GLY   B O   
6116 N  N   . ALA   B 134 ? 0.2143 0.1750 0.2285 -0.0194 0.0376  0.0200  134  ALA   B N   
6117 C  CA  . ALA   B 134 ? 0.2096 0.1721 0.2357 -0.0159 0.0362  0.0081  134  ALA   B CA  
6118 C  C   . ALA   B 134 ? 0.2162 0.1613 0.2243 -0.0083 0.0335  0.0084  134  ALA   B C   
6119 O  O   . ALA   B 134 ? 0.2191 0.1829 0.2255 0.0017  0.0256  0.0058  134  ALA   B O   
6120 C  CB  . ALA   B 134 ? 0.2028 0.1758 0.2518 -0.0106 0.0172  0.0092  134  ALA   B CB  
6126 N  N   . ASP   B 135 ? 0.2284 0.1569 0.2242 -0.0149 0.0175  0.0146  135  ASP   B N   
6127 C  CA  . ASP   B 135 ? 0.2427 0.1497 0.2422 -0.0094 0.0080  0.0224  135  ASP   B CA  
6128 C  C   . ASP   B 135 ? 0.2255 0.1411 0.2230 -0.0013 0.0110  0.0274  135  ASP   B C   
6129 O  O   . ASP   B 135 ? 0.2161 0.1411 0.2368 -0.0018 0.0155  0.0281  135  ASP   B O   
6130 C  CB  . ASP   B 135 ? 0.2674 0.1604 0.2674 -0.0294 0.0032  0.0202  135  ASP   B CB  
6131 C  CG  . ASP   B 135 ? 0.2882 0.1694 0.3091 -0.0477 0.0018  0.0134  135  ASP   B CG  
6132 O  OD1 . ASP   B 135 ? 0.2949 0.1589 0.2917 -0.0343 0.0038  0.0082  135  ASP   B OD1 
6133 O  OD2 . ASP   B 135 ? 0.3036 0.2060 0.3592 -0.0591 -0.0032 0.0021  135  ASP   B OD2 
6138 N  N   . PRO   B 136 ? 0.2191 0.1455 0.2286 0.0138  -0.0028 0.0229  136  PRO   B N   
6139 C  CA  . PRO   B 136 ? 0.2043 0.1446 0.2356 0.0176  -0.0039 0.0127  136  PRO   B CA  
6140 C  C   . PRO   B 136 ? 0.1863 0.1277 0.2342 0.0147  0.0026  0.0058  136  PRO   B C   
6141 O  O   . PRO   B 136 ? 0.1691 0.1257 0.2245 0.0106  -0.0007 0.0103  136  PRO   B O   
6142 C  CB  . PRO   B 136 ? 0.2094 0.1655 0.2581 0.0309  -0.0041 0.0048  136  PRO   B CB  
6143 C  CG  . PRO   B 136 ? 0.2272 0.1704 0.2741 0.0345  0.0061  0.0000  136  PRO   B CG  
6144 C  CD  . PRO   B 136 ? 0.2301 0.1591 0.2559 0.0348  0.0045  0.0121  136  PRO   B CD  
6152 N  N   . ILE   B 137 ? 0.1974 0.1163 0.2402 0.0095  -0.0004 0.0019  137  ILE   B N   
6153 C  CA  . ILE   B 137 ? 0.2020 0.1191 0.2574 -0.0013 0.0060  -0.0037 137  ILE   B CA  
6154 C  C   . ILE   B 137 ? 0.1834 0.1219 0.2441 -0.0066 0.0133  0.0077  137  ILE   B C   
6155 O  O   . ILE   B 137 ? 0.1721 0.1286 0.2555 -0.0089 0.0086  0.0029  137  ILE   B O   
6156 C  CB  . ILE   B 137 ? 0.2306 0.1269 0.3088 0.0007  0.0025  0.0031  137  ILE   B CB  
6157 C  CG1 . ILE   B 137 ? 0.2530 0.1420 0.3569 0.0066  0.0047  -0.0098 137  ILE   B CG1 
6158 C  CG2 . ILE   B 137 ? 0.2400 0.1320 0.3129 -0.0279 0.0011  0.0077  137  ILE   B CG2 
6159 C  CD1 . ILE   B 137 ? 0.2699 0.1713 0.3975 0.0161  0.0016  -0.0070 137  ILE   B CD1 
6171 N  N   . HIS   B 138 ? 0.1913 0.1216 0.2373 -0.0102 0.0137  0.0122  138  HIS   B N   
6172 C  CA  . HIS   B 138 ? 0.1976 0.1336 0.2370 -0.0032 0.0281  0.0132  138  HIS   B CA  
6173 C  C   . HIS   B 138 ? 0.1818 0.1287 0.2272 -0.0020 0.0314  0.0262  138  HIS   B C   
6174 O  O   . HIS   B 138 ? 0.1754 0.1374 0.2340 0.0043  0.0371  0.0386  138  HIS   B O   
6175 C  CB  . HIS   B 138 ? 0.2267 0.1452 0.2553 -0.0041 0.0446  0.0093  138  HIS   B CB  
6176 C  CG  . HIS   B 138 ? 0.2473 0.1611 0.2518 -0.0088 0.0565  0.0336  138  HIS   B CG  
6177 N  ND1 . HIS   B 138 ? 0.2573 0.1824 0.2850 -0.0057 0.0717  0.0214  138  HIS   B ND1 
6178 C  CD2 . HIS   B 138 ? 0.2631 0.1708 0.2435 -0.0094 0.0622  0.0240  138  HIS   B CD2 
6179 C  CE1 . HIS   B 138 ? 0.2653 0.1843 0.2776 -0.0035 0.0792  0.0230  138  HIS   B CE1 
6180 N  NE2 . HIS   B 138 ? 0.2718 0.1708 0.2568 -0.0011 0.0703  0.0182  138  HIS   B NE2 
6188 N  N   . SER   B 139 ? 0.1773 0.1206 0.2354 0.0027  0.0222  0.0133  139  SER   B N   
6189 C  CA  . SER   B 139 ? 0.1680 0.1074 0.2279 0.0044  0.0186  0.0008  139  SER   B CA  
6190 C  C   . SER   B 139 ? 0.1478 0.1080 0.2203 -0.0042 0.0234  0.0036  139  SER   B C   
6191 O  O   . SER   B 139 ? 0.1493 0.1137 0.2171 -0.0040 0.0071  0.0008  139  SER   B O   
6192 C  CB  . SER   B 139 ? 0.1773 0.1137 0.2307 0.0003  0.0111  0.0011  139  SER   B CB  
6193 O  OG  . SER   B 139 ? 0.1755 0.1211 0.2215 -0.0080 -0.0064 0.0107  139  SER   B OG  
6199 N  N   . LEU   B 140 ? 0.1484 0.1036 0.2334 -0.0030 0.0193  -0.0004 140  LEU   B N   
6200 C  CA  . LEU   B 140 ? 0.1494 0.1119 0.2250 -0.0045 0.0179  -0.0015 140  LEU   B CA  
6201 C  C   . LEU   B 140 ? 0.1455 0.1086 0.2302 -0.0042 0.0115  -0.0120 140  LEU   B C   
6202 O  O   . LEU   B 140 ? 0.1457 0.1138 0.2263 -0.0031 0.0021  0.0032  140  LEU   B O   
6203 C  CB  . LEU   B 140 ? 0.1475 0.1162 0.2201 -0.0113 0.0177  -0.0055 140  LEU   B CB  
6204 C  CG  . LEU   B 140 ? 0.1551 0.1154 0.2071 -0.0097 0.0050  0.0064  140  LEU   B CG  
6205 C  CD1 . LEU   B 140 ? 0.1650 0.1253 0.2298 -0.0111 0.0136  0.0017  140  LEU   B CD1 
6206 C  CD2 . LEU   B 140 ? 0.1670 0.1178 0.2289 -0.0048 0.0032  0.0001  140  LEU   B CD2 
6218 N  N   . ARG   B 141 ? 0.1441 0.1140 0.2359 -0.0137 0.0127  -0.0052 141  ARG   B N   
6219 C  CA  . ARG   B 141 ? 0.1420 0.1208 0.2736 -0.0177 0.0264  -0.0041 141  ARG   B CA  
6220 C  C   . ARG   B 141 ? 0.1341 0.1126 0.2535 -0.0158 0.0144  -0.0019 141  ARG   B C   
6221 O  O   . ARG   B 141 ? 0.1400 0.1191 0.2546 -0.0082 0.0088  -0.0086 141  ARG   B O   
6222 C  CB  . ARG   B 141 ? 0.1548 0.1282 0.3065 -0.0271 0.0345  -0.0075 141  ARG   B CB  
6223 C  CG  . ARG   B 141 ? 0.1890 0.1595 0.3406 -0.0289 0.0365  0.0011  141  ARG   B CG  
6224 C  CD  . ARG   B 141 ? 0.2315 0.1836 0.3379 -0.0165 0.0243  -0.0174 141  ARG   B CD  
6225 N  NE  . ARG   B 141 ? 0.2526 0.1784 0.3364 -0.0275 0.0350  -0.0160 141  ARG   B NE  
6226 C  CZ  . ARG   B 141 ? 0.2738 0.1537 0.3174 -0.0193 0.0448  -0.0303 141  ARG   B CZ  
6227 N  NH1 . ARG   B 141 ? 0.2904 0.1519 0.3067 -0.0160 0.0444  -0.0316 141  ARG   B NH1 
6228 N  NH2 . ARG   B 141 ? 0.2927 0.1658 0.3435 -0.0047 0.0285  -0.0129 141  ARG   B NH2 
6242 N  N   . VAL   B 142 ? 0.1385 0.1161 0.2353 -0.0080 0.0118  -0.0023 142  VAL   B N   
6243 C  CA  . VAL   B 142 ? 0.1352 0.1162 0.2269 -0.0045 0.0199  -0.0004 142  VAL   B CA  
6244 C  C   . VAL   B 142 ? 0.1337 0.1143 0.2301 -0.0055 0.0167  -0.0060 142  VAL   B C   
6245 O  O   . VAL   B 142 ? 0.1408 0.1135 0.2446 0.0027  0.0194  0.0041  142  VAL   B O   
6246 C  CB  . VAL   B 142 ? 0.1510 0.1261 0.2334 -0.0019 0.0260  0.0081  142  VAL   B CB  
6247 C  CG1 . VAL   B 142 ? 0.1455 0.1296 0.2403 0.0004  0.0306  0.0049  142  VAL   B CG1 
6248 C  CG2 . VAL   B 142 ? 0.1750 0.1309 0.2437 -0.0024 0.0179  0.0071  142  VAL   B CG2 
6258 N  N   . CYS   B 143 ? 0.1331 0.1130 0.2140 -0.0046 0.0086  0.0023  143  CYS   B N   
6259 C  CA  . CYS   B 143 ? 0.1294 0.1167 0.2118 -0.0081 0.0097  0.0042  143  CYS   B CA  
6260 C  C   . CYS   B 143 ? 0.1274 0.1195 0.2176 -0.0104 0.0124  -0.0047 143  CYS   B C   
6261 O  O   . CYS   B 143 ? 0.1341 0.1187 0.2248 -0.0037 0.0055  -0.0030 143  CYS   B O   
6262 C  CB  . CYS   B 143 ? 0.1340 0.1252 0.2110 -0.0094 0.0049  0.0013  143  CYS   B CB  
6263 S  SG  . CYS   B 143 ? 0.1390 0.1362 0.2080 -0.0049 0.0112  0.0055  143  CYS   B SG  
6269 N  N   . VAL   B 144 ? 0.1345 0.1197 0.2248 -0.0039 0.0037  -0.0038 144  VAL   B N   
6270 C  CA  . VAL   B 144 ? 0.1394 0.1276 0.2484 -0.0100 -0.0072 -0.0182 144  VAL   B CA  
6271 C  C   . VAL   B 144 ? 0.1361 0.1236 0.2553 -0.0077 0.0014  0.0004  144  VAL   B C   
6272 O  O   . VAL   B 144 ? 0.1465 0.1474 0.2791 0.0063  0.0067  0.0110  144  VAL   B O   
6273 C  CB  . VAL   B 144 ? 0.1601 0.1371 0.3214 -0.0083 -0.0208 -0.0268 144  VAL   B CB  
6274 C  CG1 . VAL   B 144 ? 0.1914 0.1756 0.3555 -0.0020 -0.0224 -0.0135 144  VAL   B CG1 
6275 C  CG2 . VAL   B 144 ? 0.1760 0.1420 0.3266 0.0020  -0.0337 -0.0347 144  VAL   B CG2 
6285 N  N   . ASP   B 145 ? 0.1345 0.1221 0.2572 -0.0116 0.0084  -0.0093 145  ASP   B N   
6286 C  CA  . ASP   B 145 ? 0.1341 0.1300 0.2825 -0.0078 0.0116  -0.0132 145  ASP   B CA  
6287 C  C   . ASP   B 145 ? 0.1250 0.1339 0.2671 -0.0120 0.0128  -0.0078 145  ASP   B C   
6288 O  O   . ASP   B 145 ? 0.1298 0.1434 0.3328 -0.0131 0.0154  -0.0260 145  ASP   B O   
6289 C  CB  . ASP   B 145 ? 0.1520 0.1364 0.3194 -0.0128 0.0252  -0.0002 145  ASP   B CB  
6290 C  CG  . ASP   B 145 ? 0.1726 0.1444 0.3640 -0.0261 0.0248  0.0065  145  ASP   B CG  
6291 O  OD1 . ASP   B 145 ? 0.1700 0.1440 0.3682 -0.0218 -0.0052 -0.0064 145  ASP   B OD1 
6292 O  OD2 . ASP   B 145 ? 0.1973 0.1537 0.4075 -0.0378 0.0345  0.0167  145  ASP   B OD2 
6297 N  N   . THR   B 146 ? 0.1243 0.1207 0.2242 -0.0080 0.0070  0.0017  146  THR   B N   
6298 C  CA  . THR   B 146 ? 0.1333 0.1159 0.2091 -0.0071 0.0155  -0.0018 146  THR   B CA  
6299 C  C   . THR   B 146 ? 0.1295 0.1170 0.2011 -0.0089 0.0064  0.0012  146  THR   B C   
6300 O  O   . THR   B 146 ? 0.1334 0.1181 0.2098 -0.0056 0.0055  0.0049  146  THR   B O   
6301 C  CB  . THR   B 146 ? 0.1378 0.1198 0.2202 -0.0057 0.0215  0.0025  146  THR   B CB  
6302 O  OG1 . THR   B 146 ? 0.1367 0.1181 0.2188 -0.0091 0.0209  0.0139  146  THR   B OG1 
6303 C  CG2 . THR   B 146 ? 0.1460 0.1256 0.2113 -0.0036 0.0124  -0.0011 146  THR   B CG2 
6311 N  N   . VAL   B 147 ? 0.1354 0.1208 0.1830 -0.0076 0.0150  0.0021  147  VAL   B N   
6312 C  CA  . VAL   B 147 ? 0.1334 0.1178 0.1910 -0.0138 0.0006  -0.0014 147  VAL   B CA  
6313 C  C   . VAL   B 147 ? 0.1305 0.1197 0.1991 -0.0195 -0.0061 -0.0078 147  VAL   B C   
6314 O  O   . VAL   B 147 ? 0.1418 0.1304 0.1903 -0.0166 -0.0156 -0.0039 147  VAL   B O   
6315 C  CB  . VAL   B 147 ? 0.1323 0.1275 0.1748 -0.0073 0.0019  0.0015  147  VAL   B CB  
6316 C  CG1 . VAL   B 147 ? 0.1379 0.1510 0.1710 -0.0054 -0.0015 0.0065  147  VAL   B CG1 
6317 C  CG2 . VAL   B 147 ? 0.1387 0.1295 0.1756 -0.0138 0.0019  0.0051  147  VAL   B CG2 
6327 N  N   . ARG   B 148 ? 0.1280 0.1194 0.2027 -0.0072 -0.0118 -0.0044 148  ARG   B N   
6328 C  CA  . ARG   B 148 ? 0.1373 0.1274 0.1831 -0.0056 -0.0180 -0.0129 148  ARG   B CA  
6329 C  C   . ARG   B 148 ? 0.1391 0.1349 0.1708 -0.0068 -0.0187 -0.0049 148  ARG   B C   
6330 O  O   . ARG   B 148 ? 0.1610 0.1664 0.1784 -0.0202 -0.0243 -0.0000 148  ARG   B O   
6331 C  CB  . ARG   B 148 ? 0.1366 0.1401 0.1880 -0.0035 -0.0206 -0.0158 148  ARG   B CB  
6332 C  CG  . ARG   B 148 ? 0.1422 0.1555 0.2025 -0.0070 -0.0257 -0.0324 148  ARG   B CG  
6333 C  CD  . ARG   B 148 ? 0.1515 0.1747 0.2126 0.0075  -0.0276 -0.0311 148  ARG   B CD  
6334 N  NE  . ARG   B 148 ? 0.1546 0.1677 0.1947 0.0247  -0.0257 -0.0329 148  ARG   B NE  
6335 C  CZ  . ARG   B 148 ? 0.1490 0.1585 0.1849 0.0173  -0.0158 -0.0195 148  ARG   B CZ  
6336 N  NH1 . ARG   B 148 ? 0.1376 0.1614 0.1933 -0.0015 -0.0016 -0.0203 148  ARG   B NH1 
6337 N  NH2 . ARG   B 148 ? 0.1624 0.1417 0.1843 0.0167  -0.0179 -0.0090 148  ARG   B NH2 
6351 N  N   . THR   B 149 ? 0.1402 0.1321 0.1728 -0.0115 -0.0188 0.0012  149  THR   B N   
6352 C  CA  . THR   B 149 ? 0.1490 0.1303 0.1680 -0.0139 -0.0235 0.0064  149  THR   B CA  
6353 C  C   . THR   B 149 ? 0.1447 0.1296 0.1637 -0.0194 -0.0212 0.0090  149  THR   B C   
6354 O  O   . THR   B 149 ? 0.1548 0.1331 0.1740 -0.0195 -0.0046 0.0005  149  THR   B O   
6355 C  CB  . THR   B 149 ? 0.1485 0.1302 0.1742 -0.0160 -0.0211 0.0023  149  THR   B CB  
6356 O  OG1 . THR   B 149 ? 0.1516 0.1353 0.1673 -0.0164 -0.0236 -0.0005 149  THR   B OG1 
6357 C  CG2 . THR   B 149 ? 0.1593 0.1351 0.1935 -0.0072 -0.0127 0.0061  149  THR   B CG2 
6365 N  N   . ASN   B 150 ? 0.1531 0.1286 0.1546 -0.0154 -0.0257 0.0023  150  ASN   B N   
6366 C  CA  . ASN   B 150 ? 0.1593 0.1447 0.1533 -0.0166 -0.0240 -0.0031 150  ASN   B CA  
6367 C  C   . ASN   B 150 ? 0.1493 0.1405 0.1495 -0.0144 -0.0173 -0.0049 150  ASN   B C   
6368 O  O   . ASN   B 150 ? 0.1532 0.1352 0.1836 -0.0248 -0.0323 -0.0034 150  ASN   B O   
6369 C  CB  . ASN   B 150 ? 0.1836 0.1803 0.1681 -0.0139 -0.0210 0.0102  150  ASN   B CB  
6370 C  CG  . ASN   B 150 ? 0.2140 0.2199 0.2012 -0.0150 -0.0315 0.0270  150  ASN   B CG  
6371 O  OD1 . ASN   B 150 ? 0.2239 0.2375 0.2130 -0.0263 -0.0537 0.0219  150  ASN   B OD1 
6372 N  ND2 . ASN   B 150 ? 0.2263 0.2406 0.2368 -0.0040 -0.0386 0.0677  150  ASN   B ND2 
6379 N  N   . VAL   B 151 ? 0.1432 0.1354 0.1452 -0.0178 -0.0165 0.0032  151  VAL   B N   
6380 C  CA  . VAL   B 151 ? 0.1431 0.1336 0.1564 -0.0217 -0.0097 0.0017  151  VAL   B CA  
6381 C  C   . VAL   B 151 ? 0.1474 0.1265 0.1602 -0.0271 -0.0200 -0.0042 151  VAL   B C   
6382 O  O   . VAL   B 151 ? 0.1508 0.1396 0.1828 -0.0246 -0.0060 -0.0087 151  VAL   B O   
6383 C  CB  . VAL   B 151 ? 0.1623 0.1532 0.1687 -0.0074 -0.0071 0.0005  151  VAL   B CB  
6384 C  CG1 . VAL   B 151 ? 0.1704 0.1543 0.1900 -0.0123 0.0031  -0.0157 151  VAL   B CG1 
6385 C  CG2 . VAL   B 151 ? 0.1677 0.1679 0.1535 0.0075  -0.0035 0.0143  151  VAL   B CG2 
6395 N  N   . TYR   B 152 ? 0.1442 0.1207 0.1431 -0.0232 -0.0112 -0.0082 152  TYR   B N   
6396 C  CA  . TYR   B 152 ? 0.1457 0.1323 0.1387 -0.0248 -0.0043 -0.0067 152  TYR   B CA  
6397 C  C   . TYR   B 152 ? 0.1404 0.1243 0.1350 -0.0202 -0.0060 -0.0086 152  TYR   B C   
6398 O  O   . TYR   B 152 ? 0.1469 0.1228 0.1466 -0.0243 -0.0089 -0.0001 152  TYR   B O   
6399 C  CB  . TYR   B 152 ? 0.1578 0.1422 0.1509 -0.0233 -0.0041 -0.0016 152  TYR   B CB  
6400 C  CG  . TYR   B 152 ? 0.1737 0.1535 0.1527 -0.0345 -0.0103 -0.0020 152  TYR   B CG  
6401 C  CD1 . TYR   B 152 ? 0.1781 0.1640 0.1517 -0.0225 -0.0276 0.0006  152  TYR   B CD1 
6402 C  CD2 . TYR   B 152 ? 0.1893 0.1715 0.1593 -0.0359 -0.0088 -0.0065 152  TYR   B CD2 
6403 C  CE1 . TYR   B 152 ? 0.1912 0.1806 0.1600 -0.0192 -0.0270 0.0136  152  TYR   B CE1 
6404 C  CE2 . TYR   B 152 ? 0.2024 0.1907 0.1562 -0.0293 -0.0148 -0.0103 152  TYR   B CE2 
6405 C  CZ  . TYR   B 152 ? 0.2046 0.2045 0.1461 -0.0260 -0.0371 0.0093  152  TYR   B CZ  
6406 O  OH  . TYR   B 152 ? 0.2378 0.2429 0.1752 -0.0168 -0.0390 0.0132  152  TYR   B OH  
6416 N  N   . LEU   B 153 ? 0.1472 0.1209 0.1407 -0.0225 -0.0068 -0.0044 153  LEU   B N   
6417 C  CA  . LEU   B 153 ? 0.1506 0.1194 0.1301 -0.0169 0.0045  -0.0088 153  LEU   B CA  
6418 C  C   . LEU   B 153 ? 0.1515 0.1176 0.1415 -0.0202 0.0014  -0.0086 153  LEU   B C   
6419 O  O   . LEU   B 153 ? 0.1605 0.1419 0.1639 -0.0141 -0.0035 -0.0317 153  LEU   B O   
6420 C  CB  . LEU   B 153 ? 0.1474 0.1242 0.1520 -0.0244 0.0033  -0.0031 153  LEU   B CB  
6421 C  CG  . LEU   B 153 ? 0.1397 0.1371 0.1758 -0.0232 -0.0012 -0.0069 153  LEU   B CG  
6422 C  CD1 . LEU   B 153 ? 0.1464 0.1545 0.1892 -0.0227 0.0012  0.0037  153  LEU   B CD1 
6423 C  CD2 . LEU   B 153 ? 0.1417 0.1442 0.1792 -0.0240 0.0107  -0.0004 153  LEU   B CD2 
6435 N  N   . ALA   B 154 ? 0.1446 0.1213 0.1612 -0.0064 -0.0054 -0.0030 154  ALA   B N   
6436 C  CA  . ALA   B 154 ? 0.1525 0.1304 0.1723 -0.0038 -0.0115 -0.0150 154  ALA   B CA  
6437 C  C   . ALA   B 154 ? 0.1645 0.1305 0.1783 0.0029  -0.0222 -0.0270 154  ALA   B C   
6438 O  O   . ALA   B 154 ? 0.1896 0.1367 0.1934 0.0086  -0.0077 -0.0111 154  ALA   B O   
6439 C  CB  . ALA   B 154 ? 0.1544 0.1483 0.1923 -0.0040 -0.0043 -0.0233 154  ALA   B CB  
6445 N  N   . VAL   B 155 ? 0.1409 0.1232 0.1871 0.0026  -0.0064 -0.0162 155  VAL   B N   
6446 C  CA  . VAL   B 155 ? 0.1324 0.1281 0.1981 -0.0005 -0.0114 -0.0084 155  VAL   B CA  
6447 C  C   . VAL   B 155 ? 0.1342 0.1255 0.1959 -0.0030 -0.0063 -0.0179 155  VAL   B C   
6448 O  O   . VAL   B 155 ? 0.1493 0.1483 0.2371 0.0064  -0.0064 -0.0326 155  VAL   B O   
6449 C  CB  . VAL   B 155 ? 0.1387 0.1369 0.2282 -0.0033 -0.0104 0.0053  155  VAL   B CB  
6450 C  CG1 . VAL   B 155 ? 0.1430 0.1353 0.2354 -0.0069 -0.0092 -0.0057 155  VAL   B CG1 
6451 C  CG2 . VAL   B 155 ? 0.1376 0.1531 0.2621 -0.0078 -0.0129 0.0278  155  VAL   B CG2 
6461 N  N   . PHE   B 156 ? 0.1285 0.1350 0.2115 0.0025  -0.0005 -0.0192 156  PHE   B N   
6462 C  CA  . PHE   B 156 ? 0.1343 0.1419 0.2467 0.0096  -0.0016 -0.0183 156  PHE   B CA  
6463 C  C   . PHE   B 156 ? 0.1321 0.1481 0.2675 0.0119  -0.0026 -0.0364 156  PHE   B C   
6464 O  O   . PHE   B 156 ? 0.1532 0.1627 0.2899 0.0204  0.0034  -0.0376 156  PHE   B O   
6465 C  CB  . PHE   B 156 ? 0.1388 0.1386 0.2483 0.0035  -0.0192 -0.0113 156  PHE   B CB  
6466 C  CG  . PHE   B 156 ? 0.1420 0.1447 0.2602 0.0024  -0.0245 -0.0023 156  PHE   B CG  
6467 C  CD1 . PHE   B 156 ? 0.1434 0.1731 0.2976 0.0089  -0.0069 0.0308  156  PHE   B CD1 
6468 C  CD2 . PHE   B 156 ? 0.1521 0.1563 0.2622 0.0084  -0.0305 -0.0005 156  PHE   B CD2 
6469 C  CE1 . PHE   B 156 ? 0.1495 0.1910 0.3176 0.0072  -0.0085 0.0344  156  PHE   B CE1 
6470 C  CE2 . PHE   B 156 ? 0.1532 0.1793 0.2806 0.0131  -0.0235 0.0160  156  PHE   B CE2 
6471 C  CZ  . PHE   B 156 ? 0.1446 0.1890 0.3093 0.0127  -0.0220 0.0248  156  PHE   B CZ  
6481 N  N   . ASP   B 157 ? 0.1310 0.1368 0.2789 0.0055  -0.0143 -0.0204 157  ASP   B N   
6482 C  CA  . ASP   B 157 ? 0.1438 0.1440 0.3051 0.0101  -0.0227 -0.0278 157  ASP   B CA  
6483 C  C   . ASP   B 157 ? 0.1453 0.1448 0.3159 0.0063  -0.0164 -0.0447 157  ASP   B C   
6484 O  O   . ASP   B 157 ? 0.1361 0.1403 0.3091 0.0045  -0.0198 -0.0349 157  ASP   B O   
6485 C  CB  . ASP   B 157 ? 0.1658 0.1644 0.3225 0.0107  -0.0396 -0.0119 157  ASP   B CB  
6486 C  CG  . ASP   B 157 ? 0.1935 0.1846 0.3391 0.0076  -0.0242 -0.0049 157  ASP   B CG  
6487 O  OD1 . ASP   B 157 ? 0.2049 0.1830 0.3594 0.0204  -0.0108 0.0027  157  ASP   B OD1 
6488 O  OD2 . ASP   B 157 ? 0.2284 0.1973 0.3667 0.0009  -0.0131 -0.0005 157  ASP   B OD2 
6493 N  N   A LYS   B 158 ? 0.1569 0.1626 0.3184 0.0039  -0.0118 -0.0535 158  LYS   B N   
6494 N  N   B LYS   B 158 ? 0.1461 0.1694 0.3347 0.0046  -0.0073 -0.0606 158  LYS   B N   
6495 C  CA  A LYS   B 158 ? 0.1706 0.1761 0.3214 0.0059  -0.0107 -0.0585 158  LYS   B CA  
6496 C  CA  B LYS   B 158 ? 0.1564 0.1850 0.3463 0.0107  -0.0020 -0.0726 158  LYS   B CA  
6497 C  C   A LYS   B 158 ? 0.1675 0.1678 0.3264 0.0051  -0.0120 -0.0579 158  LYS   B C   
6498 C  C   B LYS   B 158 ? 0.1583 0.1669 0.3437 0.0053  -0.0074 -0.0695 158  LYS   B C   
6499 O  O   A LYS   B 158 ? 0.1684 0.1669 0.3162 0.0015  -0.0088 -0.0638 158  LYS   B O   
6500 O  O   B LYS   B 158 ? 0.1576 0.1599 0.3418 -0.0057 -0.0024 -0.0834 158  LYS   B O   
6501 C  CB  A LYS   B 158 ? 0.1909 0.1968 0.3200 0.0071  -0.0102 -0.0665 158  LYS   B CB  
6502 C  CB  B LYS   B 158 ? 0.1785 0.2180 0.3487 0.0175  0.0023  -0.0912 158  LYS   B CB  
6503 C  CG  A LYS   B 158 ? 0.2108 0.2188 0.3254 0.0071  -0.0059 -0.0703 158  LYS   B CG  
6504 C  CG  B LYS   B 158 ? 0.2039 0.2534 0.3486 0.0199  0.0121  -0.1024 158  LYS   B CG  
6505 C  CD  A LYS   B 158 ? 0.2247 0.2408 0.3360 0.0077  -0.0054 -0.0674 158  LYS   B CD  
6506 C  CD  B LYS   B 158 ? 0.2218 0.2979 0.3568 0.0192  0.0096  -0.0961 158  LYS   B CD  
6507 C  CE  A LYS   B 158 ? 0.2343 0.2560 0.3462 0.0109  -0.0072 -0.0653 158  LYS   B CE  
6508 C  CE  B LYS   B 158 ? 0.2348 0.3290 0.3663 0.0248  0.0041  -0.0912 158  LYS   B CE  
6509 N  NZ  A LYS   B 158 ? 0.2328 0.2621 0.3476 0.0098  -0.0080 -0.0669 158  LYS   B NZ  
6510 N  NZ  B LYS   B 158 ? 0.2308 0.3469 0.3623 0.0260  0.0070  -0.0914 158  LYS   B NZ  
6537 N  N   . ASN   B 159 ? 0.1652 0.1622 0.3474 0.0074  -0.0140 -0.0560 159  ASN   B N   
6538 C  CA  . ASN   B 159 ? 0.1760 0.1556 0.3718 0.0237  -0.0299 -0.0442 159  ASN   B CA  
6539 C  C   . ASN   B 159 ? 0.1666 0.1427 0.3659 0.0165  -0.0385 -0.0415 159  ASN   B C   
6540 O  O   . ASN   B 159 ? 0.1688 0.1381 0.3828 -0.0004 -0.0415 -0.0312 159  ASN   B O   
6541 C  CB  . ASN   B 159 ? 0.1921 0.1671 0.4062 0.0299  -0.0301 -0.0421 159  ASN   B CB  
6542 C  CG  . ASN   B 159 ? 0.2218 0.1858 0.4448 0.0285  -0.0465 -0.0584 159  ASN   B CG  
6543 O  OD1 . ASN   B 159 ? 0.2421 0.1971 0.4543 0.0313  -0.0431 -0.0710 159  ASN   B OD1 
6544 N  ND2 . ASN   B 159 ? 0.2201 0.1953 0.4609 0.0296  -0.0623 -0.0501 159  ASN   B ND2 
6552 N  N   . LEU   B 160 ? 0.1582 0.1422 0.3337 0.0142  -0.0357 -0.0389 160  LEU   B N   
6553 C  CA  . LEU   B 160 ? 0.1547 0.1441 0.3020 0.0118  -0.0395 -0.0199 160  LEU   B CA  
6554 C  C   . LEU   B 160 ? 0.1444 0.1346 0.3009 -0.0011 -0.0240 -0.0259 160  LEU   B C   
6555 O  O   . LEU   B 160 ? 0.1336 0.1390 0.2945 -0.0059 -0.0264 -0.0102 160  LEU   B O   
6556 C  CB  . LEU   B 160 ? 0.1503 0.1527 0.2882 0.0081  -0.0382 -0.0175 160  LEU   B CB  
6557 C  CG  . LEU   B 160 ? 0.1495 0.1638 0.2740 0.0109  -0.0361 -0.0099 160  LEU   B CG  
6558 C  CD1 . LEU   B 160 ? 0.1638 0.1742 0.2640 0.0028  -0.0207 -0.0092 160  LEU   B CD1 
6559 C  CD2 . LEU   B 160 ? 0.1578 0.1629 0.2883 0.0231  -0.0324 -0.0183 160  LEU   B CD2 
6571 N  N   . TYR   B 161 ? 0.1401 0.1405 0.3027 -0.0060 -0.0024 -0.0305 161  TYR   B N   
6572 C  CA  . TYR   B 161 ? 0.1456 0.1430 0.2820 -0.0116 0.0177  -0.0317 161  TYR   B CA  
6573 C  C   . TYR   B 161 ? 0.1514 0.1395 0.2749 -0.0113 0.0163  -0.0312 161  TYR   B C   
6574 O  O   . TYR   B 161 ? 0.1550 0.1426 0.2614 -0.0207 0.0105  -0.0285 161  TYR   B O   
6575 C  CB  . TYR   B 161 ? 0.1608 0.1459 0.2827 -0.0232 0.0246  -0.0405 161  TYR   B CB  
6576 C  CG  . TYR   B 161 ? 0.1794 0.1495 0.2673 -0.0273 0.0278  -0.0407 161  TYR   B CG  
6577 C  CD1 . TYR   B 161 ? 0.1879 0.1482 0.2526 -0.0326 0.0264  -0.0373 161  TYR   B CD1 
6578 C  CD2 . TYR   B 161 ? 0.2014 0.1619 0.2583 -0.0225 0.0229  -0.0447 161  TYR   B CD2 
6579 C  CE1 . TYR   B 161 ? 0.2015 0.1670 0.2620 -0.0329 0.0236  -0.0337 161  TYR   B CE1 
6580 C  CE2 . TYR   B 161 ? 0.2155 0.1751 0.2700 -0.0297 0.0236  -0.0373 161  TYR   B CE2 
6581 C  CZ  . TYR   B 161 ? 0.2159 0.1770 0.2642 -0.0373 0.0204  -0.0365 161  TYR   B CZ  
6582 O  OH  . TYR   B 161 ? 0.2437 0.2000 0.2803 -0.0358 0.0169  -0.0443 161  TYR   B OH  
6592 N  N   . ASP   B 162 ? 0.1536 0.1355 0.2906 -0.0082 0.0042  -0.0421 162  ASP   B N   
6593 C  CA  . ASP   B 162 ? 0.1657 0.1453 0.2914 -0.0079 -0.0017 -0.0429 162  ASP   B CA  
6594 C  C   . ASP   B 162 ? 0.1590 0.1332 0.2811 -0.0137 -0.0088 -0.0370 162  ASP   B C   
6595 O  O   . ASP   B 162 ? 0.1698 0.1406 0.2775 -0.0183 -0.0205 -0.0232 162  ASP   B O   
6596 C  CB  . ASP   B 162 ? 0.1862 0.1604 0.3186 -0.0051 -0.0052 -0.0530 162  ASP   B CB  
6597 C  CG  . ASP   B 162 ? 0.1961 0.1814 0.3413 0.0027  -0.0022 -0.0746 162  ASP   B CG  
6598 O  OD1 . ASP   B 162 ? 0.1926 0.2010 0.3252 -0.0029 0.0085  -0.0712 162  ASP   B OD1 
6599 O  OD2 . ASP   B 162 ? 0.2068 0.2044 0.3698 0.0200  -0.0062 -0.0814 162  ASP   B OD2 
6604 N  N   . LYS   B 163 ? 0.1541 0.1282 0.2745 -0.0073 -0.0171 -0.0244 163  LYS   B N   
6605 C  CA  . LYS   B 163 ? 0.1651 0.1370 0.2895 -0.0151 -0.0200 -0.0103 163  LYS   B CA  
6606 C  C   . LYS   B 163 ? 0.1436 0.1346 0.2787 -0.0157 -0.0157 -0.0033 163  LYS   B C   
6607 O  O   . LYS   B 163 ? 0.1482 0.1428 0.2983 -0.0212 -0.0145 0.0065  163  LYS   B O   
6608 C  CB  . LYS   B 163 ? 0.2074 0.1615 0.3374 -0.0121 -0.0240 0.0036  163  LYS   B CB  
6609 C  CG  . LYS   B 163 ? 0.2902 0.2479 0.4121 -0.0152 -0.0062 0.0082  163  LYS   B CG  
6610 C  CD  . LYS   B 163 ? 0.3702 0.3381 0.4899 -0.0223 -0.0009 0.0101  163  LYS   B CD  
6611 C  CE  . LYS   B 163 ? 0.4445 0.4224 0.5397 -0.0285 0.0054  0.0065  163  LYS   B CE  
6612 N  NZ  . LYS   B 163 ? 0.4826 0.4693 0.5746 -0.0310 0.0095  -0.0041 163  LYS   B NZ  
6626 N  N   . LEU   B 164 ? 0.1368 0.1255 0.2467 -0.0126 -0.0124 -0.0067 164  LEU   B N   
6627 C  CA  . LEU   B 164 ? 0.1370 0.1278 0.2272 -0.0083 -0.0201 -0.0011 164  LEU   B CA  
6628 C  C   . LEU   B 164 ? 0.1437 0.1271 0.2207 -0.0118 -0.0209 0.0031  164  LEU   B C   
6629 O  O   . LEU   B 164 ? 0.1466 0.1510 0.2414 -0.0143 -0.0213 0.0047  164  LEU   B O   
6630 C  CB  . LEU   B 164 ? 0.1340 0.1290 0.2182 -0.0035 -0.0130 -0.0052 164  LEU   B CB  
6631 C  CG  . LEU   B 164 ? 0.1405 0.1435 0.2199 -0.0060 -0.0084 0.0007  164  LEU   B CG  
6632 C  CD1 . LEU   B 164 ? 0.1497 0.1396 0.2279 -0.0132 -0.0155 -0.0116 164  LEU   B CD1 
6633 C  CD2 . LEU   B 164 ? 0.1568 0.1781 0.2419 -0.0074 -0.0094 -0.0154 164  LEU   B CD2 
6645 N  N   . VAL   B 165 ? 0.1662 0.1350 0.2371 -0.0179 -0.0216 -0.0071 165  VAL   B N   
6646 C  CA  . VAL   B 165 ? 0.2003 0.1439 0.2463 -0.0316 -0.0406 -0.0043 165  VAL   B CA  
6647 C  C   . VAL   B 165 ? 0.2268 0.1562 0.2732 -0.0441 -0.0631 -0.0004 165  VAL   B C   
6648 O  O   . VAL   B 165 ? 0.2387 0.1784 0.2795 -0.0492 -0.0634 -0.0025 165  VAL   B O   
6649 C  CB  . VAL   B 165 ? 0.2192 0.1609 0.2504 -0.0194 -0.0151 -0.0102 165  VAL   B CB  
6650 C  CG1 . VAL   B 165 ? 0.2411 0.1697 0.2819 -0.0190 -0.0123 -0.0139 165  VAL   B CG1 
6651 C  CG2 . VAL   B 165 ? 0.2121 0.1704 0.2446 -0.0230 0.0051  -0.0124 165  VAL   B CG2 
6661 N  N   . SER   B 166 ? 0.2373 0.1457 0.3126 -0.0435 -0.0702 -0.0232 166  SER   B N   
6662 C  CA  . SER   B 166 ? 0.2305 0.1507 0.3690 -0.0432 -0.0574 -0.0328 166  SER   B CA  
6663 C  C   . SER   B 166 ? 0.2158 0.1650 0.3787 -0.0466 -0.0561 -0.0194 166  SER   B C   
6664 O  O   . SER   B 166 ? 0.2162 0.1842 0.4037 -0.0527 -0.0559 -0.0445 166  SER   B O   
6665 C  CB  . SER   B 166 ? 0.2288 0.1621 0.4009 -0.0342 -0.0534 -0.0429 166  SER   B CB  
6666 O  OG  . SER   B 166 ? 0.2227 0.1632 0.4176 -0.0243 -0.0472 -0.0236 166  SER   B OG  
6672 N  N   . SER   B 167 ? 0.2054 0.1543 0.3531 -0.0496 -0.0595 0.0251  167  SER   B N   
6673 C  CA  . SER   B 167 ? 0.2000 0.1620 0.3325 -0.0476 -0.0409 0.0200  167  SER   B CA  
6674 C  C   . SER   B 167 ? 0.1923 0.1667 0.3163 -0.0509 -0.0369 0.0404  167  SER   B C   
6675 O  O   . SER   B 167 ? 0.1947 0.1774 0.3052 -0.0496 -0.0337 0.0392  167  SER   B O   
6676 C  CB  . SER   B 167 ? 0.1953 0.1703 0.3102 -0.0398 -0.0121 0.0149  167  SER   B CB  
6677 O  OG  . SER   B 167 ? 0.1873 0.1787 0.2833 -0.0288 -0.0082 0.0176  167  SER   B OG  
6683 N  N   . PHE   B 168 ? 0.1932 0.1638 0.3078 -0.0466 -0.0325 0.0457  168  PHE   B N   
6684 C  CA  . PHE   B 168 ? 0.1989 0.1641 0.2821 -0.0449 -0.0230 0.0313  168  PHE   B CA  
6685 C  C   . PHE   B 168 ? 0.1754 0.1502 0.2397 -0.0213 -0.0028 0.0099  168  PHE   B C   
6686 O  O   . PHE   B 168 ? 0.2061 0.1451 0.2382 -0.0012 -0.0007 -0.0037 168  PHE   B O   
6687 C  CB  . PHE   B 168 ? 0.2073 0.1729 0.2877 -0.0523 -0.0499 0.0438  168  PHE   B CB  
6688 C  CG  . PHE   B 168 ? 0.2330 0.1593 0.2795 -0.0521 -0.0518 0.0254  168  PHE   B CG  
6689 C  CD1 . PHE   B 168 ? 0.2644 0.1658 0.2994 -0.0434 -0.0597 0.0157  168  PHE   B CD1 
6690 C  CD2 . PHE   B 168 ? 0.2176 0.1503 0.2826 -0.0413 -0.0504 0.0388  168  PHE   B CD2 
6691 C  CE1 . PHE   B 168 ? 0.2760 0.1694 0.3024 -0.0299 -0.0549 0.0231  168  PHE   B CE1 
6692 C  CE2 . PHE   B 168 ? 0.2443 0.1579 0.2925 -0.0248 -0.0546 0.0290  168  PHE   B CE2 
6693 C  CZ  . PHE   B 168 ? 0.2653 0.1580 0.2940 -0.0177 -0.0586 0.0340  168  PHE   B CZ  
6703 N  N   . LEU   B 169 ? 0.1654 0.1578 0.2353 -0.0028 0.0099  0.0029  169  LEU   B N   
6704 C  CA  . LEU   B 169 ? 0.1937 0.1901 0.2738 -0.0134 0.0040  -0.0264 169  LEU   B CA  
6705 C  C   . LEU   B 169 ? 0.2195 0.2191 0.3344 0.0014  0.0018  -0.0541 169  LEU   B C   
6706 O  O   . LEU   B 169 ? 0.2392 0.2397 0.3901 -0.0062 -0.0086 -0.0822 169  LEU   B O   
6707 C  CB  . LEU   B 169 ? 0.2114 0.2298 0.2881 -0.0212 -0.0103 0.0011  169  LEU   B CB  
6708 C  CG  . LEU   B 169 ? 0.2508 0.2711 0.3353 -0.0097 -0.0050 0.0132  169  LEU   B CG  
6709 C  CD1 . LEU   B 169 ? 0.2623 0.2882 0.3408 -0.0072 -0.0137 0.0292  169  LEU   B CD1 
6710 C  CD2 . LEU   B 169 ? 0.2486 0.2777 0.3439 -0.0006 0.0111  0.0073  169  LEU   B CD2 
6711 O  OXT . LEU   B 169 ? 0.2366 0.2345 0.3321 0.0339  0.0054  -0.0528 169  LEU   B OXT 
6723 N  N2  B A1A92 C .   ? 0.1375 0.1398 0.1813 -0.0075 -0.0145 0.0291  201  A1A92 A N2  
6724 C  C3  B A1A92 C .   ? 0.1704 0.1478 0.1938 -0.0170 -0.0100 0.0228  201  A1A92 A C3  
6725 C  C6  B A1A92 C .   ? 0.1412 0.1357 0.1637 -0.0050 -0.0114 0.0361  201  A1A92 A C6  
6726 C  C9  B A1A92 C .   ? 0.1346 0.1365 0.1558 -0.0047 -0.0053 0.0311  201  A1A92 A C9  
6727 C  C1  B A1A92 C .   ? 0.1705 0.1592 0.1956 -0.0247 -0.0100 0.0062  201  A1A92 A C1  
6728 C  C10 B A1A92 C .   ? 0.1430 0.1438 0.1573 -0.0094 0.0020  0.0364  201  A1A92 A C10 
6729 C  C11 B A1A92 C .   ? 0.1376 0.1444 0.1676 -0.0141 0.0006  0.0286  201  A1A92 A C11 
6730 C  C2  B A1A92 C .   ? 0.1614 0.1433 0.1767 -0.0209 -0.0054 0.0257  201  A1A92 A C2  
6731 C  C4  B A1A92 C .   ? 0.1692 0.1390 0.1913 -0.0111 -0.0064 0.0310  201  A1A92 A C4  
6732 C  C5  B A1A92 C .   ? 0.1567 0.1278 0.2027 -0.0074 -0.0133 0.0376  201  A1A92 A C5  
6733 C  C7  B A1A92 C .   ? 0.1345 0.1484 0.1735 -0.0042 -0.0034 0.0334  201  A1A92 A C7  
6734 C  C8  B A1A92 C .   ? 0.1343 0.1325 0.1537 -0.0085 0.0049  0.0283  201  A1A92 A C8  
6735 N  N1  B A1A92 C .   ? 0.1474 0.1282 0.1750 -0.0054 -0.0134 0.0351  201  A1A92 A N1  
6736 N  N3  B A1A92 C .   ? 0.1420 0.1400 0.1600 -0.0086 0.0089  0.0391  201  A1A92 A N3  
6737 N  N4  B A1A92 C .   ? 0.1405 0.1371 0.1683 -0.0109 -0.0067 0.0300  201  A1A92 A N4  
6738 O  O1  B A1A92 C .   ? 0.1723 0.1757 0.2143 -0.0228 -0.0052 -0.0054 201  A1A92 A O1  
6753 CL CL  B CL    D .   ? 0.1693 0.1390 0.2083 -0.0077 0.0089  0.0002  202  CL    A CL  
6754 O  O   . HOH   E .   ? 0.6364 0.7122 0.5235 -0.0641 -0.1447 -0.0930 1301 HOH   A O   
6755 O  O   . HOH   E .   ? 0.4053 0.7580 0.4340 -0.1089 0.0341  0.1188  1302 HOH   A O   
6756 O  O   . HOH   E .   ? 0.3080 0.2694 0.1720 -0.0464 0.0381  0.0338  1303 HOH   A O   
6757 O  O   . HOH   E .   ? 0.5994 0.4124 0.5782 -0.0571 0.1364  0.1762  1304 HOH   A O   
6758 O  O   . HOH   E .   ? 0.6087 0.4991 0.3007 0.2250  -0.1071 0.0564  1305 HOH   A O   
6759 O  O   . HOH   E .   ? 0.3977 0.5050 0.3399 -0.1258 0.0883  0.0598  1306 HOH   A O   
6760 O  O   . HOH   E .   ? 0.2344 0.2659 0.3207 0.0023  0.0914  -0.0177 1307 HOH   A O   
6761 O  O   . HOH   E .   ? 0.3789 0.2119 0.4169 -0.0345 -0.1293 0.0438  1308 HOH   A O   
6762 O  O   . HOH   E .   ? 0.6488 0.6430 0.3734 -0.0707 -0.0563 0.1340  1309 HOH   A O   
6763 O  O   B HOH   E .   ? 0.3712 0.2258 0.2411 -0.1078 -0.0268 0.0529  1310 HOH   A O   
6764 O  O   . HOH   E .   ? 0.6537 0.4897 0.4587 -0.1391 0.1568  0.1796  1311 HOH   A O   
6765 O  O   . HOH   E .   ? 0.1991 0.2330 0.2222 -0.0441 -0.0242 0.0989  1312 HOH   A O   
6766 O  O   . HOH   E .   ? 0.4417 0.5620 0.3970 0.2070  0.0749  0.0026  1313 HOH   A O   
6767 O  O   . HOH   E .   ? 0.3110 0.3213 0.2957 -0.1280 -0.0060 0.0936  1314 HOH   A O   
6768 O  O   . HOH   E .   ? 0.5368 0.4904 0.5176 -0.1321 -0.0935 0.0048  1315 HOH   A O   
6769 O  O   . HOH   E .   ? 0.3324 0.6683 0.6847 0.0858  0.0883  0.1068  1316 HOH   A O   
6770 O  O   . HOH   E .   ? 0.2628 0.2621 0.5029 -0.0128 -0.0910 0.1341  1317 HOH   A O   
6771 O  O   . HOH   E .   ? 0.2455 0.6075 0.4557 -0.0152 -0.0728 0.0960  1318 HOH   A O   
6772 O  O   . HOH   E .   ? 0.1725 0.3286 0.2617 0.0364  -0.0041 -0.0020 1319 HOH   A O   
6773 O  O   . HOH   E .   ? 0.1978 0.1832 0.3756 -0.0425 0.0105  -0.0106 1320 HOH   A O   
6774 O  O   . HOH   E .   ? 0.4175 0.3081 0.5901 0.0161  0.1368  -0.0180 1321 HOH   A O   
6775 O  O   . HOH   E .   ? 0.4865 0.3686 0.4299 0.0682  -0.1152 0.0148  1322 HOH   A O   
6776 O  O   . HOH   E .   ? 0.3027 0.4524 0.3206 -0.0776 0.1199  0.0656  1323 HOH   A O   
6777 O  O   B HOH   E .   ? 0.1855 0.1755 0.3950 0.0161  -0.0067 0.0030  1324 HOH   A O   
6778 O  O   . HOH   E .   ? 0.6195 0.5757 0.5215 -0.0428 0.2794  -0.1380 1325 HOH   A O   
6779 O  O   . HOH   E .   ? 0.2310 0.2155 0.2570 0.0405  0.0216  0.0359  1326 HOH   A O   
6780 O  O   B HOH   E .   ? 0.2765 0.3062 0.5478 0.0443  0.0012  -0.0025 1327 HOH   A O   
6781 O  O   . HOH   E .   ? 0.1993 0.3367 0.4205 -0.0382 0.0293  -0.1053 1328 HOH   A O   
6782 O  O   . HOH   E .   ? 0.2207 0.4179 0.3781 -0.0201 -0.0626 0.1546  1329 HOH   A O   
6783 O  O   A HOH   E .   ? 0.2869 0.1068 0.1547 0.0217  0.0075  0.0065  1330 HOH   A O   
6784 O  O   . HOH   E .   ? 0.3271 0.4282 0.2179 -0.0307 0.0916  0.0457  1331 HOH   A O   
6785 O  O   B HOH   E .   ? 0.2401 0.2144 0.4114 -0.0734 0.0263  0.0305  1332 HOH   A O   
6786 O  O   . HOH   E .   ? 0.3132 0.3938 0.4235 -0.1395 -0.1055 0.2195  1333 HOH   A O   
6787 O  O   . HOH   E .   ? 0.4310 0.1719 0.4622 0.0423  0.0146  0.0091  1334 HOH   A O   
6788 O  O   . HOH   E .   ? 0.6405 0.6593 0.7193 -0.0720 -0.0549 0.2387  1335 HOH   A O   
6789 O  O   A HOH   E .   ? 0.0848 0.0876 0.1417 0.0168  -0.0359 -0.0102 1336 HOH   A O   
6790 O  O   . HOH   E .   ? 0.2237 0.4192 0.3450 0.0883  -0.0493 0.0067  1337 HOH   A O   
6791 O  O   . HOH   E .   ? 0.1430 0.2302 0.2294 0.0095  -0.0043 0.0694  1338 HOH   A O   
6792 O  O   . HOH   E .   ? 0.1751 0.1648 0.2066 0.0116  -0.0179 0.0145  1339 HOH   A O   
6793 O  O   . HOH   E .   ? 0.2851 0.2895 0.7013 0.0707  0.0988  -0.0102 1340 HOH   A O   
6794 O  O   . HOH   E .   ? 0.2526 0.3950 0.3563 -0.0872 -0.0339 -0.0423 1341 HOH   A O   
6795 O  O   . HOH   E .   ? 0.5834 0.3542 0.2901 0.0599  0.1220  0.1041  1342 HOH   A O   
6796 O  O   . HOH   E .   ? 0.4632 0.1676 0.3915 0.0370  -0.1134 0.0269  1343 HOH   A O   
6797 O  O   B HOH   E .   ? 0.1417 0.1608 0.2049 -0.0009 -0.0098 0.0286  1344 HOH   A O   
6798 O  O   . HOH   E .   ? 0.5351 0.2681 0.3963 -0.1673 0.1979  -0.0882 1345 HOH   A O   
6799 O  O   . HOH   E .   ? 0.3344 0.4207 0.6115 0.1027  0.0893  -0.1224 1346 HOH   A O   
6800 O  O   . HOH   E .   ? 0.6333 0.5118 0.5838 -0.0901 -0.0915 0.0802  1347 HOH   A O   
6801 O  O   A HOH   E .   ? 0.1717 0.1350 0.0980 -0.0332 0.0127  -0.0120 1348 HOH   A O   
6802 O  O   . HOH   E .   ? 0.3335 0.3428 0.2206 -0.0612 -0.0503 -0.0850 1349 HOH   A O   
6803 O  O   . HOH   E .   ? 0.1490 0.4729 0.3140 -0.0374 0.0332  0.0055  1350 HOH   A O   
6804 O  O   B HOH   E .   ? 0.3461 0.4448 0.4247 0.1406  -0.0647 -0.0069 1351 HOH   A O   
6805 O  O   . HOH   E .   ? 0.5688 0.5052 0.4099 0.0920  -0.1601 -0.1175 1352 HOH   A O   
6806 O  O   . HOH   E .   ? 0.2589 0.3154 0.4259 -0.0236 -0.0854 -0.1094 1353 HOH   A O   
6807 O  O   . HOH   E .   ? 0.8211 0.7500 0.6642 -0.1343 0.0335  -0.0228 1354 HOH   A O   
6808 O  O   . HOH   E .   ? 0.1397 0.1783 0.2581 0.0099  -0.0076 -0.0015 1355 HOH   A O   
6809 O  O   . HOH   E .   ? 0.2005 0.1884 0.3807 0.0109  0.0881  -0.0250 1356 HOH   A O   
6810 O  O   . HOH   E .   ? 0.1300 0.1300 0.1432 -0.0034 0.0047  0.0140  1357 HOH   A O   
6811 O  O   . HOH   E .   ? 0.3361 0.6709 0.6082 -0.0302 -0.1045 0.2609  1358 HOH   A O   
6812 O  O   . HOH   E .   ? 0.2457 0.2005 0.2306 -0.0463 -0.0016 0.0433  1359 HOH   A O   
6813 O  O   . HOH   E .   ? 0.3554 0.4939 0.3095 0.2032  0.0590  0.0369  1360 HOH   A O   
6814 O  O   A HOH   E .   ? 0.2116 0.3798 0.2154 0.0631  0.0094  -0.0121 1361 HOH   A O   
6815 O  O   . HOH   E .   ? 0.1386 0.1522 0.1447 -0.0066 -0.0166 0.0036  1362 HOH   A O   
6816 O  O   . HOH   E .   ? 0.2819 0.4002 0.2824 0.0571  0.0807  0.1627  1363 HOH   A O   
6817 O  O   . HOH   E .   ? 0.1525 0.1350 0.1941 -0.0052 0.0255  -0.0107 1364 HOH   A O   
6818 O  O   . HOH   E .   ? 0.2612 0.4537 0.3065 -0.0745 0.0630  -0.0149 1365 HOH   A O   
6819 O  O   . HOH   E .   ? 0.1763 0.1817 0.2346 -0.0260 0.0068  0.0303  1366 HOH   A O   
6820 O  O   . HOH   E .   ? 0.1945 0.2252 0.3882 0.0257  0.0927  -0.0356 1367 HOH   A O   
6821 O  O   . HOH   E .   ? 0.2814 0.6629 0.4873 0.0630  0.0398  0.2424  1368 HOH   A O   
6822 O  O   A HOH   E .   ? 0.2304 0.3202 0.3017 -0.0919 0.0548  0.0877  1369 HOH   A O   
6823 O  O   A HOH   E .   ? 0.1227 0.3088 0.1461 0.0817  0.0311  0.0471  1370 HOH   A O   
6824 O  O   . HOH   E .   ? 0.2324 0.2088 0.2952 0.0157  -0.0611 -0.0168 1371 HOH   A O   
6825 O  O   B HOH   E .   ? 0.1951 0.2116 0.1710 -0.0282 -0.0159 0.0275  1372 HOH   A O   
6826 O  O   . HOH   E .   ? 0.1959 0.2185 0.2072 -0.0213 -0.0468 0.0392  1373 HOH   A O   
6827 O  O   . HOH   E .   ? 0.3547 0.2211 0.5171 -0.0850 -0.0733 -0.0011 1374 HOH   A O   
6828 O  O   . HOH   E .   ? 0.2258 0.3813 0.3401 -0.0768 -0.0368 0.0676  1375 HOH   A O   
6829 O  O   . HOH   E .   ? 0.8474 0.4387 0.7585 -0.1272 -0.1163 0.0793  1376 HOH   A O   
6830 O  O   A HOH   E .   ? 0.1344 0.1278 0.2190 0.0004  0.0520  0.0437  1377 HOH   A O   
6831 O  O   . HOH   E .   ? 0.3235 0.2680 0.2106 0.0404  0.0768  0.0258  1378 HOH   A O   
6832 O  O   . HOH   E .   ? 0.1585 0.1578 0.2127 -0.0106 0.0164  0.0280  1379 HOH   A O   
6833 O  O   . HOH   E .   ? 0.4029 0.1978 0.4666 -0.0921 0.1294  0.0138  1380 HOH   A O   
6834 O  O   . HOH   E .   ? 0.1651 0.1527 0.1942 0.0131  -0.0221 0.0188  1381 HOH   A O   
6835 O  O   . HOH   E .   ? 0.4817 0.3624 0.4137 -0.1415 0.0708  0.0601  1382 HOH   A O   
6836 O  O   A HOH   E .   ? 0.2421 0.2477 0.1723 0.0592  -0.0263 0.0961  1383 HOH   A O   
6837 O  O   . HOH   E .   ? 0.2936 0.5847 0.4920 0.1397  0.0792  -0.0703 1384 HOH   A O   
6838 O  O   . HOH   E .   ? 0.3762 0.6232 0.6618 -0.0745 -0.1494 0.0026  1385 HOH   A O   
6839 O  O   B HOH   E .   ? 0.2147 0.2768 0.2060 0.0817  0.0285  0.0829  1386 HOH   A O   
6840 O  O   B HOH   E .   ? 0.1773 0.1437 0.2353 -0.0241 -0.0039 0.0259  1387 HOH   A O   
6841 O  O   . HOH   E .   ? 0.1558 0.2398 0.3845 0.0020  0.0668  0.0768  1388 HOH   A O   
6842 O  O   A HOH   E .   ? 0.1577 0.1495 0.2210 -0.0117 -0.0191 -0.0360 1389 HOH   A O   
6843 O  O   B HOH   E .   ? 0.1755 0.2149 0.2838 -0.0155 0.0047  0.0617  1390 HOH   A O   
6844 O  O   . HOH   E .   ? 0.3272 0.3094 0.3518 -0.0912 -0.0220 0.0028  1391 HOH   A O   
6845 O  O   . HOH   E .   ? 0.2440 0.2516 0.4239 0.0352  -0.0846 0.0329  1392 HOH   A O   
6846 O  O   . HOH   E .   ? 0.2842 0.3210 0.4127 -0.0947 0.1356  -0.0324 1393 HOH   A O   
6847 O  O   . HOH   E .   ? 0.3135 0.2374 0.2511 -0.0655 -0.1089 0.0281  1394 HOH   A O   
6848 O  O   . HOH   E .   ? 0.2304 0.1766 0.1887 -0.0365 0.0201  0.0292  1395 HOH   A O   
6849 O  O   . HOH   E .   ? 0.1695 0.1760 0.1766 -0.0005 0.0020  0.0181  1396 HOH   A O   
6850 O  O   . HOH   E .   ? 0.1770 0.1776 0.4033 0.0380  0.1064  0.1095  1397 HOH   A O   
6851 O  O   . HOH   E .   ? 0.3322 0.5513 0.3460 0.0053  0.0052  0.0946  1398 HOH   A O   
6852 O  O   . HOH   E .   ? 0.3240 0.2267 0.3111 -0.0015 -0.0230 0.0762  1399 HOH   A O   
6853 O  O   . HOH   E .   ? 0.5281 0.5176 0.4174 -0.0956 -0.1844 0.0489  1400 HOH   A O   
6854 O  O   . HOH   E .   ? 0.4462 0.5766 0.2663 -0.1310 -0.1273 -0.0194 1401 HOH   A O   
6855 O  O   . HOH   E .   ? 0.1979 0.2016 0.2564 -0.0079 -0.0059 0.0797  1402 HOH   A O   
6856 O  O   . HOH   E .   ? 0.5145 0.6417 0.4068 0.1887  -0.0512 -0.0513 1403 HOH   A O   
6857 O  O   . HOH   E .   ? 0.1715 0.2436 0.3732 -0.0088 -0.0185 0.0359  1404 HOH   A O   
6858 O  O   . HOH   E .   ? 0.4840 0.5724 0.6330 -0.0330 -0.0246 -0.0216 1405 HOH   A O   
6859 O  O   . HOH   E .   ? 0.9547 0.9312 0.8069 -0.0823 -0.0314 0.0039  1406 HOH   A O   
6860 O  O   A HOH   E .   ? 0.0688 0.0683 0.0586 0.0010  0.0091  0.0227  1407 HOH   A O   
6861 O  O   A HOH   E .   ? 0.1104 0.0982 0.2009 0.0052  -0.0672 0.0014  1408 HOH   A O   
6862 O  O   . HOH   E .   ? 0.2000 0.5399 0.4310 0.0345  0.0172  0.0090  1409 HOH   A O   
6863 O  O   . HOH   E .   ? 0.6361 0.6964 0.6401 -0.1444 0.0854  -0.1334 1410 HOH   A O   
6864 O  O   . HOH   E .   ? 0.1961 0.1565 0.2928 0.0019  -0.0263 0.0026  1411 HOH   A O   
6865 O  O   . HOH   E .   ? 0.2267 0.4096 0.3649 -0.0404 0.1016  -0.1115 1412 HOH   A O   
6866 O  O   . HOH   E .   ? 0.2977 0.3538 0.5599 0.0109  0.0664  -0.0666 1413 HOH   A O   
6867 O  O   . HOH   E .   ? 0.1336 0.1362 0.1668 0.0017  -0.0192 0.0078  1414 HOH   A O   
6868 O  O   . HOH   E .   ? 0.2509 0.1756 0.2515 -0.0208 0.0153  0.0272  1415 HOH   A O   
6869 O  O   . HOH   E .   ? 0.1582 0.1414 0.1466 -0.0240 0.0054  0.0080  1416 HOH   A O   
6870 O  O   . HOH   E .   ? 0.1668 0.2287 0.2695 -0.0269 -0.0056 0.0363  1417 HOH   A O   
6871 O  O   . HOH   E .   ? 0.2090 0.2451 0.2452 0.0021  -0.0568 0.0380  1418 HOH   A O   
6872 O  O   A HOH   E .   ? 0.2920 0.3890 0.2779 0.0112  0.0908  0.0218  1419 HOH   A O   
6873 O  O   B HOH   E .   ? 0.1417 0.2493 0.3032 0.0181  -0.0145 0.0575  1420 HOH   A O   
6874 O  O   . HOH   E .   ? 0.4360 0.2749 0.2939 -0.1169 0.0341  0.0529  1421 HOH   A O   
6875 O  O   . HOH   E .   ? 0.3558 0.1267 0.1926 -0.0076 -0.0601 0.0116  1422 HOH   A O   
6876 O  O   . HOH   E .   ? 0.5272 0.4527 0.3386 0.1881  -0.1111 -0.1642 1423 HOH   A O   
6877 O  O   . HOH   E .   ? 0.4486 0.2223 0.5061 -0.0815 -0.2280 0.1083  1424 HOH   A O   
6878 O  O   . HOH   E .   ? 0.5591 0.4580 0.2013 -0.0102 0.0452  0.1249  1425 HOH   A O   
6879 O  O   A HOH   E .   ? 0.3460 0.2386 0.1943 -0.0355 0.0291  0.0469  1426 HOH   A O   
6880 O  O   . HOH   E .   ? 0.1560 0.1594 0.2664 -0.0028 0.0085  0.0193  1427 HOH   A O   
6881 O  O   . HOH   E .   ? 0.2450 0.3572 0.7763 -0.0419 0.0479  -0.0484 1428 HOH   A O   
6882 O  O   . HOH   E .   ? 0.5788 0.7353 0.6147 0.1440  -0.0373 0.0740  1429 HOH   A O   
6883 O  O   . HOH   E .   ? 0.3827 0.2732 0.2745 -0.0260 0.0201  0.0217  1430 HOH   A O   
6884 O  O   . HOH   E .   ? 0.2818 0.5319 0.1606 -0.0438 0.0558  0.0245  1431 HOH   A O   
6885 O  O   . HOH   E .   ? 0.4207 0.6465 0.3144 -0.1112 -0.0209 0.1042  1432 HOH   A O   
6886 O  O   . HOH   E .   ? 0.2618 0.3502 0.3719 -0.0131 -0.0485 -0.0441 1433 HOH   A O   
6887 O  O   B HOH   E .   ? 0.4446 0.2244 0.5600 -0.1109 0.0006  0.0143  1434 HOH   A O   
6888 O  O   . HOH   E .   ? 0.1573 0.1597 0.2168 0.0166  -0.0297 0.0188  1435 HOH   A O   
6889 O  O   . HOH   E .   ? 0.2220 0.1606 0.1533 -0.0116 0.0160  0.0172  1436 HOH   A O   
6890 O  O   . HOH   E .   ? 0.2550 0.4489 0.2695 0.1861  0.0054  0.0298  1437 HOH   A O   
6891 O  O   . HOH   E .   ? 0.5306 0.5817 0.6083 0.2279  0.1648  0.1339  1438 HOH   A O   
6892 O  O   B HOH   E .   ? 0.3502 0.3745 0.3285 0.1133  -0.0319 0.1047  1439 HOH   A O   
6893 O  O   B HOH   E .   ? 0.4831 0.2171 0.3618 0.0589  -0.1318 0.0463  1440 HOH   A O   
6894 O  O   A HOH   E .   ? 0.2110 0.1531 0.2451 0.0006  -0.0047 0.0804  1441 HOH   A O   
6895 O  O   . HOH   E .   ? 0.3709 0.2420 0.1663 -0.0918 0.0485  0.0299  1442 HOH   A O   
6896 O  O   A HOH   E .   ? 0.1148 0.2291 0.1699 0.0391  -0.0663 -0.0438 1443 HOH   A O   
6897 O  O   A HOH   E .   ? 0.3138 0.1290 0.1815 -0.0342 -0.0868 -0.0257 1444 HOH   A O   
6898 O  O   . HOH   E .   ? 0.6510 0.3518 0.4832 0.1571  -0.0968 0.0854  1445 HOH   A O   
6899 O  O   . HOH   E .   ? 0.6407 0.7465 0.4265 -0.0033 0.2819  -0.0407 1446 HOH   A O   
6900 O  O   . HOH   E .   ? 0.9292 0.8265 0.8381 0.0822  0.0459  -0.0255 1447 HOH   A O   
6901 O  O   . HOH   E .   ? 0.2368 0.1524 0.2641 0.0077  0.0032  0.0065  1448 HOH   A O   
6902 O  O   A HOH   E .   ? 0.1374 0.2104 0.2375 0.0230  0.0332  -0.0763 1449 HOH   A O   
6903 O  O   . HOH   E .   ? 0.3758 0.4793 0.4720 -0.0176 -0.0858 -0.1314 1450 HOH   A O   
6904 O  O   . HOH   E .   ? 0.1771 0.2016 0.5125 -0.0241 -0.0966 0.0398  1451 HOH   A O   
6905 O  O   . HOH   E .   ? 0.4296 0.3675 0.3128 0.2358  -0.0362 -0.0263 1452 HOH   A O   
6906 O  O   A HOH   E .   ? 0.3834 0.2545 0.4516 0.0702  -0.0127 -0.0438 1453 HOH   A O   
6907 O  O   . HOH   E .   ? 0.7746 0.8203 0.5342 0.2984  -0.0903 0.2039  1454 HOH   A O   
6908 O  O   . HOH   E .   ? 0.2134 0.2210 0.2462 0.0201  0.0186  0.0347  1455 HOH   A O   
6909 O  O   . HOH   E .   ? 0.6804 0.7077 0.5322 -0.1016 0.1381  0.1925  1456 HOH   A O   
6910 O  O   . HOH   E .   ? 0.5018 0.6367 0.8157 0.0249  -0.1162 0.2194  1457 HOH   A O   
6911 O  O   . HOH   E .   ? 0.1969 0.2827 0.2541 -0.0024 0.0054  -0.0463 1458 HOH   A O   
6912 O  O   . HOH   E .   ? 0.4374 0.3320 0.4462 0.1266  0.1157  0.1637  1459 HOH   A O   
6913 O  O   A HOH   E .   ? 0.4094 0.3345 0.3257 0.0140  0.0871  0.0978  1460 HOH   A O   
6914 O  O   B HOH   E .   ? 0.2897 0.4222 0.4170 0.0220  -0.0088 -0.0143 1461 HOH   A O   
6915 O  O   . HOH   E .   ? 0.3768 0.3400 0.3883 0.0394  -0.0311 0.1241  1462 HOH   A O   
6916 O  O   . HOH   E .   ? 0.5351 0.3750 0.4356 0.0762  0.1006  -0.0010 1463 HOH   A O   
6917 O  O   . HOH   E .   ? 0.2868 0.2947 0.3787 -0.0701 0.0687  -0.0911 1464 HOH   A O   
6918 O  O   . HOH   E .   ? 0.7643 0.8319 0.5258 -0.0665 -0.0851 0.0759  1465 HOH   A O   
6919 O  O   . HOH   E .   ? 0.2371 0.2364 0.3090 0.0379  -0.0313 -0.0276 1466 HOH   A O   
6920 O  O   . HOH   E .   ? 0.3230 0.3644 0.4370 0.0343  -0.1704 0.0102  1467 HOH   A O   
6921 O  O   . HOH   E .   ? 0.2948 0.4239 0.5328 -0.1154 0.0702  -0.1804 1468 HOH   A O   
6922 O  O   . HOH   E .   ? 0.3554 0.4171 0.2815 -0.1258 -0.0571 0.0529  1469 HOH   A O   
6923 O  O   . HOH   E .   ? 0.2529 0.4976 0.4686 0.0465  0.0224  -0.2148 1470 HOH   A O   
6924 O  O   B HOH   E .   ? 0.1954 0.1797 0.3322 -0.0155 -0.0282 0.0411  1471 HOH   A O   
6925 O  O   B HOH   E .   ? 0.2566 0.3281 0.2567 0.0879  -0.0427 -0.0437 1472 HOH   A O   
6926 O  O   . HOH   E .   ? 0.7461 0.6664 0.6815 0.1544  0.1790  0.2087  1473 HOH   A O   
6927 O  O   . HOH   E .   ? 0.3639 0.6537 0.4366 -0.0146 -0.0819 0.2586  1474 HOH   A O   
6928 O  O   . HOH   E .   ? 0.2483 0.2436 0.2914 -0.0714 0.0224  -0.0143 1475 HOH   A O   
6929 O  O   . HOH   E .   ? 0.6830 0.3331 0.7554 0.0636  0.0545  0.2387  1476 HOH   A O   
6930 O  O   A HOH   E .   ? 0.2650 0.1874 0.3103 0.0471  -0.1073 -0.0532 1477 HOH   A O   
6931 O  O   . HOH   E .   ? 0.2916 0.1812 0.2407 0.0398  -0.0984 -0.0253 1478 HOH   A O   
6932 O  O   . HOH   E .   ? 0.5790 0.5436 0.4562 0.0268  0.1569  0.0597  1479 HOH   A O   
6933 O  O   A HOH   E .   ? 0.1947 0.1481 0.2400 -0.0006 0.0223  -0.0213 1480 HOH   A O   
6934 O  O   A HOH   E .   ? 0.1859 0.1586 0.1237 0.0504  0.0070  0.0116  1481 HOH   A O   
6935 O  O   B HOH   E .   ? 0.2718 0.3561 0.2902 0.0464  0.0005  0.0821  1482 HOH   A O   
6936 O  O   . HOH   E .   ? 0.5782 0.6967 0.5669 -0.1608 -0.1393 0.0001  1483 HOH   A O   
6937 O  O   . HOH   E .   ? 0.4305 0.5269 0.3592 0.0473  -0.0798 -0.0745 1484 HOH   A O   
6938 O  O   . HOH   E .   ? 0.6480 0.6583 0.4757 0.1944  -0.0875 -0.0514 1485 HOH   A O   
6939 O  O   . HOH   E .   ? 0.4036 0.5520 0.5373 -0.2145 -0.0485 -0.0248 1486 HOH   A O   
6940 O  O   . HOH   E .   ? 0.5722 0.4141 0.4546 0.0079  -0.0714 -0.1215 1487 HOH   A O   
6941 O  O   . HOH   E .   ? 0.4984 0.2663 0.4157 -0.0262 -0.0933 0.0984  1488 HOH   A O   
6942 O  O   B HOH   E .   ? 0.2061 0.5617 0.5624 -0.0311 -0.0710 -0.1405 1489 HOH   A O   
6943 O  O   . HOH   E .   ? 0.5852 0.3881 0.5045 -0.0200 0.0893  0.0323  1490 HOH   A O   
6944 O  O   . HOH   E .   ? 0.7726 0.3632 0.3103 -0.0647 -0.1255 0.0193  1491 HOH   A O   
6945 O  O   B HOH   E .   ? 0.3407 0.1963 0.2541 -0.0204 -0.0439 -0.0005 1492 HOH   A O   
6946 O  O   . HOH   E .   ? 0.6421 0.4705 0.7515 -0.0981 0.0276  -0.0601 1493 HOH   A O   
6947 O  O   . HOH   E .   ? 0.4611 0.5721 0.2803 0.0209  -0.0396 0.0477  1494 HOH   A O   
6948 O  O   . HOH   E .   ? 0.4930 0.4186 0.4013 -0.0335 -0.0484 -0.0504 1495 HOH   A O   
6949 O  O   . HOH   E .   ? 0.3462 0.4407 0.4719 0.0286  0.1262  0.1793  1496 HOH   A O   
6950 O  O   . HOH   E .   ? 0.2711 0.5532 0.3774 0.1055  0.0931  0.2524  1497 HOH   A O   
6951 O  O   . HOH   E .   ? 0.2673 0.2475 0.6909 -0.0058 -0.1610 0.0161  1498 HOH   A O   
6952 O  O   . HOH   E .   ? 0.7217 0.5823 0.4753 -0.0804 0.1738  0.0451  1499 HOH   A O   
6953 O  O   . HOH   E .   ? 0.3785 0.3155 0.2560 -0.0557 0.1183  -0.0210 1500 HOH   A O   
6954 O  O   . HOH   E .   ? 0.5094 0.5687 0.7001 0.0069  0.2231  -0.1262 1501 HOH   A O   
6955 O  O   . HOH   E .   ? 0.6120 0.5192 0.5699 -0.1057 -0.0752 -0.0968 1502 HOH   A O   
6956 O  O   . HOH   E .   ? 0.5028 0.2894 0.4005 -0.0441 0.1776  0.0393  1503 HOH   A O   
6957 O  O   . HOH   E .   ? 0.2675 0.1838 0.5166 -0.0044 0.0816  0.0478  1504 HOH   A O   
6958 O  O   . HOH   E .   ? 0.4814 0.6018 0.5054 0.0041  -0.0937 0.0109  1505 HOH   A O   
6959 O  O   . HOH   E .   ? 0.4741 0.3357 0.4376 -0.1122 0.0540  0.1284  1506 HOH   A O   
6960 O  O   . HOH   E .   ? 0.2924 0.5158 0.3281 -0.0429 -0.0393 -0.0422 1507 HOH   A O   
6961 O  O   . HOH   E .   ? 0.5816 0.5659 0.3926 0.0042  -0.0675 -0.0378 1508 HOH   A O   
6962 O  O   . HOH   E .   ? 0.2606 0.2511 0.4785 0.0033  0.0769  -0.0414 1509 HOH   A O   
6963 O  O   B HOH   E .   ? 0.2893 0.4072 0.2970 -0.0090 -0.0473 0.0528  1510 HOH   A O   
6964 O  O   . HOH   E .   ? 0.4606 0.2210 0.3917 -0.1188 0.0449  -0.0085 1511 HOH   A O   
6965 O  O   . HOH   E .   ? 0.4342 0.9448 0.5982 -0.0961 -0.0904 0.1822  1512 HOH   A O   
6966 O  O   . HOH   E .   ? 0.2308 0.3213 0.3641 0.0324  -0.0813 0.0470  1513 HOH   A O   
6967 O  O   . HOH   E .   ? 0.4787 0.6774 0.5420 0.0809  0.0179  0.1130  1514 HOH   A O   
6968 O  O   . HOH   E .   ? 0.6344 0.2642 0.4737 -0.1010 0.1057  0.0366  1515 HOH   A O   
6969 O  O   . HOH   E .   ? 0.2783 0.4086 0.4580 0.0215  -0.0782 -0.0012 1516 HOH   A O   
6970 O  O   B HOH   E .   ? 0.4029 0.4196 0.3651 -0.0695 0.0357  -0.0318 1517 HOH   A O   
6971 O  O   . HOH   E .   ? 0.6436 0.5753 0.5255 -0.0016 -0.0019 0.0941  1518 HOH   A O   
6972 O  O   B HOH   E .   ? 0.2102 0.2514 0.3058 -0.0242 -0.0332 0.0979  1519 HOH   A O   
6973 O  O   B HOH   E .   ? 0.2443 0.2232 0.2553 0.0537  0.0235  0.0276  1520 HOH   A O   
6974 O  O   B HOH   E .   ? 0.4391 0.3077 0.4477 -0.1262 0.1210  0.0717  1521 HOH   A O   
6975 O  O   B HOH   E .   ? 0.2725 0.6079 0.5182 -0.0968 -0.0501 0.0326  1522 HOH   A O   
6976 O  O   B HOH   E .   ? 0.2649 0.6166 0.2490 0.1007  -0.0050 0.0030  1523 HOH   A O   
6977 O  O   B HOH   E .   ? 0.2745 0.1897 0.4306 0.0475  -0.0281 0.0683  1524 HOH   A O   
6978 O  O   . HOH   E .   ? 0.2587 0.2049 0.5282 0.0064  0.0518  0.0660  1525 HOH   A O   
6979 O  O   . HOH   E .   ? 0.6211 0.7052 0.6823 0.1752  -0.1345 0.0738  1526 HOH   A O   
6980 O  O   . HOH   E .   ? 0.4991 0.6671 0.4245 0.3274  -0.0494 0.0235  1527 HOH   A O   
6981 O  O   . HOH   E .   ? 0.5474 0.6936 0.4737 -0.0786 -0.0982 -0.1106 1528 HOH   A O   
6982 O  O   A HOH   E .   ? 0.1897 0.2433 0.1285 0.0378  -0.0310 -0.0329 1529 HOH   A O   
6983 O  O   . HOH   E .   ? 0.5352 0.6007 0.5014 0.1168  0.0659  0.0307  1530 HOH   A O   
6984 O  O   . HOH   E .   ? 0.2488 0.6867 0.3013 0.0752  -0.0501 -0.0121 1531 HOH   A O   
6985 O  O   . HOH   E .   ? 0.5388 0.6292 0.5198 -0.0631 0.0197  0.1195  1532 HOH   A O   
6986 O  O   B HOH   E .   ? 0.3008 0.4011 0.3805 0.0736  -0.0554 0.0813  1533 HOH   A O   
6987 O  O   . HOH   E .   ? 0.4034 0.4026 0.4786 -0.0600 -0.0758 0.2279  1534 HOH   A O   
6988 O  O   . HOH   F .   ? 0.2363 0.1972 0.3233 0.0172  0.0984  0.0234  201  HOH   B O   
6989 O  O   . HOH   F .   ? 0.3104 0.5026 0.4724 0.0255  0.1470  -0.1866 202  HOH   B O   
6990 O  O   . HOH   F .   ? 0.3489 0.3280 0.7105 -0.0379 0.0938  0.0127  203  HOH   B O   
6991 O  O   . HOH   F .   ? 0.2856 0.6676 0.4220 0.0889  0.0337  0.2476  204  HOH   B O   
6992 O  O   . HOH   F .   ? 0.6735 0.7129 0.6378 0.2683  -0.0669 -0.0042 205  HOH   B O   
6993 O  O   . HOH   F .   ? 0.3070 0.4359 0.5672 -0.0935 0.0205  -0.1042 206  HOH   B O   
6994 O  O   . HOH   F .   ? 0.3623 0.3160 0.3716 -0.0289 -0.0176 -0.1209 207  HOH   B O   
6995 O  O   . HOH   F .   ? 0.7065 0.4233 0.4900 -0.0751 0.1395  -0.0079 208  HOH   B O   
6996 O  O   . HOH   F .   ? 0.5626 0.5020 0.2434 0.0392  0.0152  -0.1116 209  HOH   B O   
6997 O  O   . HOH   F .   ? 0.6042 0.4148 0.5795 0.0304  -0.1115 0.2635  210  HOH   B O   
6998 O  O   . HOH   F .   ? 0.4978 0.6160 0.3305 0.3184  -0.0740 -0.0395 211  HOH   B O   
6999 O  O   . HOH   F .   ? 0.2120 0.2269 0.3001 0.0123  0.0177  -0.0380 212  HOH   B O   
7000 O  O   . HOH   F .   ? 0.3029 0.3943 0.3670 0.0361  -0.0816 0.0850  213  HOH   B O   
7001 O  O   . HOH   F .   ? 0.5081 0.4650 0.4053 0.0683  0.1317  -0.1438 214  HOH   B O   
7002 O  O   . HOH   F .   ? 0.3768 0.2265 0.3884 0.0649  -0.0163 -0.0499 215  HOH   B O   
7003 O  O   . HOH   F .   ? 0.3226 0.1977 0.5306 0.0073  0.1941  0.0570  216  HOH   B O   
7004 O  O   . HOH   F .   ? 0.2522 0.2717 0.6649 0.0522  -0.0854 0.0427  217  HOH   B O   
7005 O  O   . HOH   F .   ? 0.2722 0.3839 0.5966 -0.0195 0.1291  0.0515  218  HOH   B O   
7006 O  O   . HOH   F .   ? 0.3535 0.3190 0.5272 -0.0271 -0.1130 -0.0097 219  HOH   B O   
7007 O  O   . HOH   F .   ? 0.1601 0.1877 0.2382 -0.0232 -0.0067 0.0088  220  HOH   B O   
7008 O  O   . HOH   F .   ? 0.3739 0.3633 0.4863 -0.1449 0.0006  0.0711  221  HOH   B O   
7009 O  O   . HOH   F .   ? 0.3511 0.5781 0.4857 0.2418  -0.0018 -0.0943 222  HOH   B O   
7010 O  O   . HOH   F .   ? 0.1489 0.1483 0.2047 -0.0238 0.0071  0.0078  223  HOH   B O   
7011 O  O   . HOH   F .   ? 0.6416 0.3124 0.4970 -0.2298 -0.0260 -0.0248 224  HOH   B O   
7012 O  O   . HOH   F .   ? 0.3922 0.4635 0.4535 0.2079  0.0219  -0.0109 225  HOH   B O   
7013 O  O   . HOH   F .   ? 0.2562 0.1701 0.2754 -0.0277 0.1178  0.0006  226  HOH   B O   
7014 O  O   . HOH   F .   ? 0.4146 0.2175 0.2123 0.1414  0.0531  0.0291  227  HOH   B O   
7015 O  O   . HOH   F .   ? 0.5052 0.1987 0.2709 -0.0002 -0.1059 0.0270  228  HOH   B O   
7016 O  O   . HOH   F .   ? 0.1759 0.2069 0.2662 -0.0172 0.0201  -0.0188 229  HOH   B O   
7017 O  O   . HOH   F .   ? 0.5595 0.4117 0.4556 0.1231  0.0083  -0.0128 230  HOH   B O   
7018 O  O   . HOH   F .   ? 0.3470 0.2442 0.4039 0.0033  -0.0293 -0.1129 231  HOH   B O   
7019 O  O   . HOH   F .   ? 0.2066 0.2091 0.3595 -0.0310 -0.0109 -0.0461 232  HOH   B O   
7020 O  O   . HOH   F .   ? 0.2517 0.2504 0.2957 0.0182  0.0417  -0.0689 233  HOH   B O   
7021 O  O   . HOH   F .   ? 0.2134 0.1231 0.3592 0.0157  -0.0646 -0.0176 234  HOH   B O   
7022 O  O   . HOH   F .   ? 0.3600 0.1847 0.1707 0.0161  -0.0860 -0.0193 235  HOH   B O   
7023 O  O   . HOH   F .   ? 0.3555 0.3231 0.2091 0.0366  0.0674  0.0403  236  HOH   B O   
7024 O  O   . HOH   F .   ? 0.2018 0.3727 0.3351 -0.0516 -0.0414 -0.0787 237  HOH   B O   
7025 O  O   . HOH   F .   ? 0.3047 0.2165 0.4404 0.0003  0.1665  -0.0099 238  HOH   B O   
7026 O  O   . HOH   F .   ? 0.2230 0.2032 0.1788 0.0107  -0.0041 -0.0022 239  HOH   B O   
7027 O  O   . HOH   F .   ? 0.1902 0.3859 0.2310 -0.0283 -0.0199 0.0603  240  HOH   B O   
7028 O  O   . HOH   F .   ? 0.5306 0.5952 0.3089 0.0963  0.0148  -0.0567 241  HOH   B O   
7029 O  O   . HOH   F .   ? 0.5124 0.3565 0.2462 0.0082  0.0964  -0.0260 242  HOH   B O   
7030 O  O   . HOH   F .   ? 0.1432 0.1376 0.1477 -0.0075 -0.0037 -0.0028 243  HOH   B O   
7031 O  O   . HOH   F .   ? 0.2907 0.2364 0.3135 0.0955  0.1053  0.0355  244  HOH   B O   
7032 O  O   . HOH   F .   ? 0.1454 0.1272 0.1451 -0.0022 0.0017  0.0077  245  HOH   B O   
7033 O  O   . HOH   F .   ? 0.3150 0.1730 0.5849 0.0013  -0.1536 -0.0482 246  HOH   B O   
7034 O  O   . HOH   F .   ? 0.2277 0.2206 0.2321 0.0811  -0.0726 -0.0666 247  HOH   B O   
7035 O  O   . HOH   F .   ? 0.2048 0.1899 0.2041 -0.0251 -0.0361 0.0050  248  HOH   B O   
7036 O  O   . HOH   F .   ? 0.2076 0.2312 0.2815 -0.0451 0.0120  -0.0214 249  HOH   B O   
7037 O  O   . HOH   F .   ? 0.4364 0.3681 0.3217 -0.0960 0.1082  -0.0604 250  HOH   B O   
7038 O  O   . HOH   F .   ? 0.2613 0.3361 0.2398 -0.0637 0.0200  -0.0440 251  HOH   B O   
7039 O  O   . HOH   F .   ? 0.2068 0.1494 0.1904 -0.0233 -0.0336 0.0269  252  HOH   B O   
7040 O  O   . HOH   F .   ? 0.5335 0.3094 0.3752 -0.2215 0.0633  -0.0107 253  HOH   B O   
7041 O  O   . HOH   F .   ? 0.1507 0.1495 0.2339 -0.0155 0.0120  -0.0140 254  HOH   B O   
7042 O  O   . HOH   F .   ? 0.2171 0.1861 0.3939 0.0139  -0.0541 -0.0244 255  HOH   B O   
7043 O  O   . HOH   F .   ? 0.2311 0.3185 0.2112 -0.0640 0.0165  0.0553  256  HOH   B O   
7044 O  O   . HOH   F .   ? 0.5294 0.7242 0.3791 0.3463  0.0347  -0.0054 257  HOH   B O   
7045 O  O   . HOH   F .   ? 0.2405 0.3106 0.5124 0.0691  -0.0538 -0.1267 258  HOH   B O   
7046 O  O   . HOH   F .   ? 0.1730 0.2586 0.2699 0.0460  0.0417  0.0904  259  HOH   B O   
7047 O  O   . HOH   F .   ? 0.4961 0.4642 0.6332 -0.0061 -0.1556 -0.1404 260  HOH   B O   
7048 O  O   . HOH   F .   ? 0.2426 0.1969 0.2769 -0.0529 0.0228  -0.0064 261  HOH   B O   
7049 O  O   . HOH   F .   ? 0.3841 0.3289 0.4773 -0.0297 -0.0971 -0.0813 262  HOH   B O   
7050 O  O   . HOH   F .   ? 0.1591 0.1655 0.2843 -0.0226 -0.0153 0.0183  263  HOH   B O   
7051 O  O   . HOH   F .   ? 0.2925 0.5139 0.2915 -0.0494 -0.0734 0.0950  264  HOH   B O   
7052 O  O   . HOH   F .   ? 0.1988 0.1518 0.2076 -0.0291 -0.0158 0.0178  265  HOH   B O   
7053 O  O   . HOH   F .   ? 0.3777 0.3169 0.2177 0.0467  0.0948  0.0102  266  HOH   B O   
7054 O  O   . HOH   F .   ? 0.1293 0.1575 0.1923 -0.0055 0.0051  0.0129  267  HOH   B O   
7055 O  O   . HOH   F .   ? 0.2224 0.2004 0.1718 0.0230  0.0041  0.0018  268  HOH   B O   
7056 O  O   . HOH   F .   ? 0.2646 0.3993 0.2705 -0.0793 -0.0359 -0.0453 269  HOH   B O   
7057 O  O   . HOH   F .   ? 0.3067 0.2374 0.2766 -0.0451 0.0325  -0.0596 270  HOH   B O   
7058 O  O   . HOH   F .   ? 0.2037 0.2313 0.2268 0.0539  -0.0246 -0.0048 271  HOH   B O   
7059 O  O   . HOH   F .   ? 0.4488 0.3392 0.2801 0.0746  -0.0135 -0.0963 272  HOH   B O   
7060 O  O   . HOH   F .   ? 0.2612 0.2702 0.2270 -0.0431 -0.0799 0.0187  273  HOH   B O   
7061 O  O   . HOH   F .   ? 0.2249 0.4948 0.4423 -0.0879 -0.0429 -0.1341 274  HOH   B O   
7062 O  O   . HOH   F .   ? 0.2290 0.2746 0.2267 -0.0568 -0.0648 -0.0264 275  HOH   B O   
7063 O  O   . HOH   F .   ? 0.2981 0.2825 0.3674 -0.0048 -0.0091 -0.1069 276  HOH   B O   
7064 O  O   . HOH   F .   ? 0.2244 0.3093 0.2903 -0.0362 0.0499  -0.0928 277  HOH   B O   
7065 O  O   . HOH   F .   ? 0.1857 0.1751 0.1662 -0.0396 -0.0413 0.0104  278  HOH   B O   
7066 O  O   . HOH   F .   ? 0.3107 0.6250 0.7025 0.1450  0.0192  -0.1076 279  HOH   B O   
7067 O  O   . HOH   F .   ? 0.3372 0.3671 0.5429 0.1344  -0.0701 -0.1116 280  HOH   B O   
7068 O  O   . HOH   F .   ? 0.3359 0.2485 0.1989 0.0237  -0.0821 -0.0135 281  HOH   B O   
7069 O  O   . HOH   F .   ? 0.3347 0.4346 0.5619 0.0934  -0.0296 -0.1238 282  HOH   B O   
7070 O  O   . HOH   F .   ? 0.1692 0.1343 0.5040 -0.0048 -0.0339 -0.0279 283  HOH   B O   
7071 O  O   . HOH   F .   ? 0.2752 0.2064 0.4254 0.0259  0.0676  0.0404  284  HOH   B O   
7072 O  O   . HOH   F .   ? 0.7634 0.5697 0.5890 0.2904  -0.0518 -0.0359 285  HOH   B O   
7073 O  O   . HOH   F .   ? 0.1642 0.1470 0.1783 0.0046  0.0052  0.0000  286  HOH   B O   
7074 O  O   . HOH   F .   ? 0.1684 0.2866 0.4578 0.0136  -0.0192 -0.1323 287  HOH   B O   
7075 O  O   . HOH   F .   ? 0.2686 0.4001 0.3900 0.0564  0.1278  0.0445  288  HOH   B O   
7076 O  O   . HOH   F .   ? 0.1635 0.1462 0.3168 -0.0138 0.0207  -0.0102 289  HOH   B O   
7077 O  O   . HOH   F .   ? 0.3919 0.4783 0.4501 0.0060  -0.1652 -0.0120 290  HOH   B O   
7078 O  O   . HOH   F .   ? 0.3599 0.6676 0.3008 0.2448  -0.0662 -0.0280 291  HOH   B O   
7079 O  O   . HOH   F .   ? 0.1693 0.1822 0.2600 0.0189  -0.0121 -0.0004 292  HOH   B O   
7080 O  O   . HOH   F .   ? 0.2494 0.4574 0.5054 -0.0987 -0.1124 0.0604  293  HOH   B O   
7081 O  O   . HOH   F .   ? 0.3614 0.2190 0.3573 -0.0909 -0.1846 0.0812  294  HOH   B O   
7082 O  O   . HOH   F .   ? 0.2490 0.2502 0.2767 0.0412  -0.0482 0.0154  295  HOH   B O   
7083 O  O   . HOH   F .   ? 0.1596 0.1943 0.1534 -0.0161 -0.0123 0.0033  296  HOH   B O   
7084 O  O   . HOH   F .   ? 0.5050 0.3422 0.2382 0.0992  -0.0728 -0.0056 297  HOH   B O   
7085 O  O   . HOH   F .   ? 0.5079 0.7108 0.2892 0.0108  -0.1182 0.1163  298  HOH   B O   
7086 O  O   . HOH   F .   ? 0.2835 0.2809 0.2673 -0.0109 0.0087  -0.1221 299  HOH   B O   
7087 O  O   . HOH   F .   ? 0.2147 0.2738 0.5562 0.0487  -0.0794 -0.1436 300  HOH   B O   
7088 O  O   . HOH   F .   ? 0.2830 0.2649 0.4969 0.0014  -0.0422 0.0974  301  HOH   B O   
7089 O  O   . HOH   F .   ? 0.2484 0.6954 0.2398 0.0878  -0.0261 -0.0702 302  HOH   B O   
7090 O  O   . HOH   F .   ? 0.4106 0.3927 0.2269 0.0989  -0.0558 0.0845  303  HOH   B O   
7091 O  O   . HOH   F .   ? 0.5038 0.3316 0.4433 0.0264  0.1003  -0.1494 304  HOH   B O   
7092 O  O   . HOH   F .   ? 0.1555 0.1423 0.2823 0.0031  0.0048  -0.0047 305  HOH   B O   
7093 O  O   . HOH   F .   ? 0.2740 0.2747 0.3807 -0.0540 0.0845  -0.0151 306  HOH   B O   
7094 O  O   . HOH   F .   ? 0.5722 0.5707 0.4443 -0.1184 -0.0097 0.1273  307  HOH   B O   
7095 O  O   . HOH   F .   ? 0.1752 0.1532 0.2244 0.0121  0.0121  0.0191  308  HOH   B O   
7096 O  O   . HOH   F .   ? 0.2177 0.1546 0.3432 0.0341  -0.1098 -0.0066 309  HOH   B O   
7097 O  O   . HOH   F .   ? 0.3474 0.1797 0.3229 0.0740  0.1366  0.0503  310  HOH   B O   
7098 O  O   . HOH   F .   ? 0.2136 0.3192 0.5200 -0.0202 -0.0897 -0.0012 311  HOH   B O   
7099 O  O   . HOH   F .   ? 0.1607 0.1894 0.2517 -0.0212 -0.0130 0.0105  312  HOH   B O   
7100 O  O   . HOH   F .   ? 0.2307 0.1475 0.2325 -0.0177 -0.0074 0.0235  313  HOH   B O   
7101 O  O   . HOH   F .   ? 0.2098 0.1635 0.2575 -0.0259 -0.0246 -0.0090 314  HOH   B O   
7102 O  O   . HOH   F .   ? 0.4190 0.5198 0.2097 0.0278  0.0759  0.0927  315  HOH   B O   
7103 O  O   . HOH   F .   ? 0.3794 0.2308 0.2842 0.1391  0.0933  0.0280  316  HOH   B O   
7104 O  O   . HOH   F .   ? 0.2871 0.2772 0.3496 -0.0528 0.1147  -0.0821 317  HOH   B O   
7105 O  O   . HOH   F .   ? 0.2108 0.1879 0.1739 -0.0033 0.0215  0.0217  318  HOH   B O   
7106 O  O   . HOH   F .   ? 0.5816 0.3908 0.3312 0.2670  0.1068  0.0844  319  HOH   B O   
7107 O  O   . HOH   F .   ? 0.4887 0.3710 0.5050 -0.1005 0.0435  0.1727  320  HOH   B O   
7108 O  O   . HOH   F .   ? 0.4816 0.2863 0.2609 -0.1774 0.0909  -0.0249 321  HOH   B O   
7109 O  O   . HOH   F .   ? 0.3178 0.3323 0.7869 0.0061  -0.0872 0.1631  322  HOH   B O   
7110 O  O   . HOH   F .   ? 0.4552 0.3836 0.2503 0.0692  -0.0000 -0.0623 323  HOH   B O   
7111 O  O   . HOH   F .   ? 0.1528 0.2880 0.2194 -0.0068 -0.0180 0.0560  324  HOH   B O   
7112 O  O   . HOH   F .   ? 0.1502 0.1618 0.2587 -0.0144 -0.0036 -0.0172 325  HOH   B O   
7113 O  O   . HOH   F .   ? 0.2428 0.6673 0.4766 -0.1195 0.0171  -0.0368 326  HOH   B O   
7114 O  O   . HOH   F .   ? 0.4654 0.4079 0.6381 0.0671  0.0210  0.0103  327  HOH   B O   
7115 O  O   . HOH   F .   ? 0.2062 0.3033 0.2929 0.0381  -0.0016 -0.0884 328  HOH   B O   
7116 O  O   . HOH   F .   ? 0.4492 0.2404 0.3137 0.0448  0.0875  0.0909  329  HOH   B O   
7117 O  O   . HOH   F .   ? 0.2635 0.2147 0.2317 0.0031  -0.0254 0.0280  330  HOH   B O   
7118 O  O   . HOH   F .   ? 0.2846 0.3101 0.5196 -0.0550 -0.1721 0.1772  331  HOH   B O   
7119 O  O   . HOH   F .   ? 0.6391 0.3334 0.3525 -0.0167 0.1266  0.1229  332  HOH   B O   
7120 O  O   . HOH   F .   ? 0.1862 0.1934 0.2810 0.0341  0.0355  0.0092  333  HOH   B O   
7121 O  O   . HOH   F .   ? 0.5488 0.4278 0.5733 0.1546  0.1259  0.0180  334  HOH   B O   
7122 O  O   . HOH   F .   ? 0.7296 0.2308 0.3399 -0.0161 -0.0463 -0.0178 335  HOH   B O   
7123 O  O   . HOH   F .   ? 0.5272 0.5663 0.5997 0.1601  -0.0988 0.1817  336  HOH   B O   
7124 O  O   . HOH   F .   ? 0.4859 0.5371 0.3310 0.0206  -0.0868 -0.0091 337  HOH   B O   
7125 O  O   . HOH   F .   ? 0.2588 0.2000 0.4930 -0.0010 0.0094  0.0302  338  HOH   B O   
7126 O  O   . HOH   F .   ? 0.4637 0.3019 0.5514 0.1206  0.2387  0.1782  339  HOH   B O   
7127 O  O   . HOH   F .   ? 0.1790 0.1430 0.2132 0.0122  -0.0144 0.0059  340  HOH   B O   
7128 O  O   . HOH   F .   ? 0.2325 0.2167 0.5592 -0.0426 0.0174  0.1256  341  HOH   B O   
7129 O  O   . HOH   F .   ? 0.2153 0.5636 0.5894 0.0306  0.1160  0.0245  342  HOH   B O   
7130 O  O   . HOH   F .   ? 0.4136 0.6799 0.3354 -0.0453 -0.0671 0.1530  343  HOH   B O   
7131 O  O   . HOH   F .   ? 0.6234 0.3904 0.6190 -0.0697 -0.0974 -0.1074 344  HOH   B O   
7132 O  O   . HOH   F .   ? 0.4992 0.3628 0.2913 0.0511  -0.0761 -0.0797 345  HOH   B O   
7133 O  O   . HOH   F .   ? 0.4670 0.5914 0.4885 0.0405  -0.0340 0.1004  346  HOH   B O   
7134 O  O   . HOH   F .   ? 0.2154 0.1970 0.2526 -0.0084 0.0516  -0.0136 347  HOH   B O   
7135 O  O   . HOH   F .   ? 0.3692 0.5524 0.4134 -0.0630 -0.1138 -0.0783 348  HOH   B O   
7136 O  O   . HOH   F .   ? 0.3143 0.4592 0.4697 -0.1548 0.0520  -0.0288 349  HOH   B O   
7137 O  O   . HOH   F .   ? 0.5174 0.2364 0.4809 -0.0837 0.1572  0.0217  350  HOH   B O   
7138 O  O   . HOH   F .   ? 0.2740 0.1933 0.5136 -0.0236 -0.0806 -0.0171 351  HOH   B O   
7139 O  O   . HOH   F .   ? 0.5417 0.5636 0.4089 -0.1191 0.0514  0.1107  352  HOH   B O   
7140 O  O   . HOH   F .   ? 0.3858 0.2309 0.3788 -0.0870 0.0342  -0.1034 353  HOH   B O   
7141 O  O   . HOH   F .   ? 0.2308 0.3623 0.4820 0.0196  0.0353  -0.0141 354  HOH   B O   
7142 O  O   . HOH   F .   ? 0.6147 0.6589 0.3433 0.0344  -0.0669 0.1977  355  HOH   B O   
7143 O  O   . HOH   F .   ? 0.4576 0.6313 0.7251 0.0306  0.1200  -0.0788 356  HOH   B O   
7144 O  O   . HOH   F .   ? 0.2029 0.5829 0.3163 0.1189  -0.0333 -0.1380 357  HOH   B O   
7145 O  O   . HOH   F .   ? 0.3067 0.1938 0.4089 0.0561  -0.1520 -0.0641 358  HOH   B O   
7146 O  O   . HOH   F .   ? 0.4121 0.3167 0.3608 -0.0086 0.0923  -0.0513 359  HOH   B O   
7147 O  O   . HOH   F .   ? 0.3863 0.2613 0.3629 -0.0877 -0.0229 -0.0692 360  HOH   B O   
7148 O  O   . HOH   F .   ? 0.5281 0.3853 0.4455 0.0453  -0.1661 -0.0663 361  HOH   B O   
7149 O  O   . HOH   F .   ? 0.4747 0.5268 0.5143 0.1768  -0.1288 0.1381  362  HOH   B O   
7150 O  O   . HOH   F .   ? 0.5513 0.4498 0.6580 0.1104  0.1629  0.1254  363  HOH   B O   
7151 O  O   . HOH   F .   ? 0.5544 0.4456 0.4915 0.0345  0.1047  0.0556  364  HOH   B O   
7152 O  O   . HOH   F .   ? 0.2201 0.3788 0.6760 -0.0774 -0.0633 -0.0700 365  HOH   B O   
7153 O  O   . HOH   F .   ? 0.5066 0.5519 0.3171 0.2175  -0.0222 0.0313  366  HOH   B O   
7154 O  O   . HOH   F .   ? 0.6607 0.5630 0.4485 0.2454  0.1081  0.0982  367  HOH   B O   
7155 O  O   . HOH   F .   ? 0.5480 0.6594 0.3628 0.1810  -0.1159 0.1177  368  HOH   B O   
7156 O  O   . HOH   F .   ? 0.4920 0.6156 0.4327 -0.0224 -0.0612 -0.1152 369  HOH   B O   
7157 O  O   . HOH   F .   ? 0.5185 0.3094 0.6161 -0.1259 -0.0164 0.0061  370  HOH   B O   
7158 O  O   . HOH   F .   ? 0.4485 0.6089 0.4946 0.2920  -0.0086 0.0931  371  HOH   B O   
7159 O  O   . HOH   F .   ? 0.5986 0.2185 0.3157 0.0005  0.0130  0.0595  372  HOH   B O   
7160 O  O   . HOH   F .   ? 0.4394 0.3330 0.3287 0.0588  -0.1615 -0.0432 373  HOH   B O   
7161 O  O   . HOH   F .   ? 0.5310 0.4323 0.5428 0.0275  -0.1637 -0.0018 374  HOH   B O   
7162 O  O   . HOH   F .   ? 0.6186 0.4111 0.2912 -0.1401 -0.0944 -0.0512 375  HOH   B O   
7163 O  O   . HOH   F .   ? 0.3849 0.6638 0.5398 0.1127  -0.0591 -0.0107 376  HOH   B O   
7164 O  O   . HOH   F .   ? 0.8666 0.8237 0.5760 0.1612  -0.1393 -0.0155 377  HOH   B O   
7165 O  O   . HOH   F .   ? 0.4536 0.4818 0.4572 -0.0839 -0.0397 0.0251  378  HOH   B O   
7166 O  O   . HOH   F .   ? 0.3909 0.6513 0.5172 0.0963  -0.0006 0.2229  379  HOH   B O   
7167 O  O   . HOH   F .   ? 0.2403 0.3689 0.4254 0.0259  -0.0642 -0.0658 380  HOH   B O   
7168 O  O   . HOH   F .   ? 0.3153 0.4413 0.2178 0.0103  -0.0038 -0.0083 381  HOH   B O   
7169 O  O   . HOH   F .   ? 0.5179 0.7410 0.3975 -0.1452 0.0212  -0.1491 382  HOH   B O   
7170 O  O   . HOH   F .   ? 0.6886 0.2974 0.6194 -0.0894 -0.1012 -0.0089 383  HOH   B O   
7171 O  O   . HOH   F .   ? 0.4343 0.6194 0.5985 0.0111  0.1533  0.1267  384  HOH   B O   
7172 O  O   . HOH   F .   ? 0.2695 0.2495 0.3286 0.0084  0.0041  0.0008  385  HOH   B O   
7173 O  O   . HOH   F .   ? 0.4171 0.7333 0.5405 0.1897  0.1549  0.0511  386  HOH   B O   
7174 O  O   . HOH   F .   ? 0.7280 0.3244 0.4597 -0.0073 0.0250  -0.1291 387  HOH   B O   
7175 O  O   . HOH   F .   ? 0.7108 0.5543 0.3866 0.2018  0.0827  -0.0218 388  HOH   B O   
7176 O  O   . HOH   F .   ? 0.4296 0.4009 0.2790 0.0250  0.0553  0.0161  389  HOH   B O   
7177 O  O   . HOH   F .   ? 0.5425 0.4533 0.5924 -0.0901 -0.0018 -0.0069 390  HOH   B O   
7178 O  O   . HOH   F .   ? 0.2159 0.4108 0.3637 -0.0542 -0.0752 -0.0209 391  HOH   B O   
7179 O  O   . HOH   F .   ? 0.4810 0.2131 0.2962 0.1137  -0.0276 0.0121  392  HOH   B O   
7180 O  O   . HOH   F .   ? 0.4307 0.4161 0.4336 -0.0194 0.0712  0.0485  393  HOH   B O   
7181 O  O   . HOH   F .   ? 0.5054 0.2262 0.4788 -0.0766 0.0241  0.0887  394  HOH   B O   
7182 O  O   . HOH   F .   ? 0.2306 0.3949 0.6774 -0.0993 -0.0783 -0.0095 395  HOH   B O   
7183 O  O   . HOH   F .   ? 0.3551 0.5900 0.3957 0.0103  -0.0265 -0.1006 396  HOH   B O   
7184 O  O   . HOH   F .   ? 0.4017 0.4240 0.4022 0.0126  0.0446  0.0463  397  HOH   B O   
7185 O  O   . HOH   F .   ? 0.3372 0.3890 0.3497 0.0043  0.0606  -0.0851 398  HOH   B O   
7186 O  O   . HOH   F .   ? 0.2228 0.2659 0.5485 -0.0501 -0.0612 -0.0159 399  HOH   B O   
7187 O  O   . HOH   F .   ? 0.6049 0.7240 0.7518 0.0678  -0.1343 0.3103  400  HOH   B O   
7188 O  O   . HOH   F .   ? 0.5623 0.3838 0.2910 -0.1997 -0.0196 0.0549  401  HOH   B O   
7189 O  O   . HOH   F .   ? 0.5606 0.5874 0.3621 0.2007  -0.0043 -0.0458 402  HOH   B O   
# 
