data_7HFM
# 
_entry.id   7HFM 
# 
_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   7HFM         pdb_00007hfm 10.2210/pdb7hfm/pdb 
WWPDB D_1001407412 ?            ?                   
# 
_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                        7HFM 
_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 '(1R,2R,4S)-2-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}bicyclo[2.2.2]octan-2-ol' 272.346   1   ? ? ? ? 
3 water       nat water                                                                                   18.015    408 ? ? ? ? 
# 
_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 '(1R,2R,4S)-2-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}bicyclo[2.2.2]octan-2-ol' A1BBN 
3 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 
A1BBN non-polymer         . '(1R,2R,4S)-2-{[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}bicyclo[2.2.2]octan-2-ol' ? 
'C15 H20 N4 O'   272.346 
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 
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 A1BBN 1   201 201  A1BBN LA1 A . 
D 3 HOH   1   301 136  HOH   HOH A . 
D 3 HOH   2   302 292  HOH   HOH A . 
D 3 HOH   3   303 1290 HOH   HOH A . 
D 3 HOH   4   304 153  HOH   HOH A . 
D 3 HOH   5   305 196  HOH   HOH A . 
D 3 HOH   6   306 296  HOH   HOH A . 
D 3 HOH   7   307 229  HOH   HOH A . 
D 3 HOH   8   308 409  HOH   HOH A . 
D 3 HOH   9   309 661  HOH   HOH A . 
D 3 HOH   10  310 625  HOH   HOH A . 
D 3 HOH   11  311 209  HOH   HOH A . 
D 3 HOH   12  312 85   HOH   HOH A . 
D 3 HOH   13  313 93   HOH   HOH A . 
D 3 HOH   14  314 1301 HOH   HOH A . 
D 3 HOH   15  315 337  HOH   HOH A . 
D 3 HOH   16  316 109  HOH   HOH A . 
D 3 HOH   17  317 57   HOH   HOH A . 
D 3 HOH   18  318 247  HOH   HOH A . 
D 3 HOH   19  319 36   HOH   HOH A . 
D 3 HOH   20  320 40   HOH   HOH A . 
D 3 HOH   21  321 393  HOH   HOH A . 
D 3 HOH   22  322 49   HOH   HOH A . 
D 3 HOH   23  323 1310 HOH   HOH A . 
D 3 HOH   24  324 281  HOH   HOH A . 
D 3 HOH   25  325 124  HOH   HOH A . 
D 3 HOH   26  326 105  HOH   HOH A . 
D 3 HOH   27  327 76   HOH   HOH A . 
D 3 HOH   28  328 1300 HOH   HOH A . 
D 3 HOH   29  329 86   HOH   HOH A . 
D 3 HOH   30  330 192  HOH   HOH A . 
D 3 HOH   31  331 34   HOH   HOH A . 
D 3 HOH   32  332 469  HOH   HOH A . 
D 3 HOH   33  333 39   HOH   HOH A . 
D 3 HOH   34  334 964  HOH   HOH A . 
D 3 HOH   35  335 1295 HOH   HOH A . 
D 3 HOH   36  336 151  HOH   HOH A . 
D 3 HOH   37  337 164  HOH   HOH A . 
D 3 HOH   38  338 218  HOH   HOH A . 
D 3 HOH   39  339 15   HOH   HOH A . 
D 3 HOH   40  340 225  HOH   HOH A . 
D 3 HOH   41  341 21   HOH   HOH A . 
D 3 HOH   42  342 18   HOH   HOH A . 
D 3 HOH   43  343 199  HOH   HOH A . 
D 3 HOH   44  344 140  HOH   HOH A . 
D 3 HOH   45  345 195  HOH   HOH A . 
D 3 HOH   46  346 241  HOH   HOH A . 
D 3 HOH   47  347 236  HOH   HOH A . 
D 3 HOH   48  348 630  HOH   HOH A . 
D 3 HOH   49  349 165  HOH   HOH A . 
D 3 HOH   50  350 102  HOH   HOH A . 
D 3 HOH   51  351 493  HOH   HOH A . 
D 3 HOH   52  352 320  HOH   HOH A . 
D 3 HOH   53  353 42   HOH   HOH A . 
D 3 HOH   54  354 17   HOH   HOH A . 
D 3 HOH   55  355 33   HOH   HOH A . 
D 3 HOH   56  356 1283 HOH   HOH A . 
D 3 HOH   57  357 939  HOH   HOH A . 
D 3 HOH   58  358 56   HOH   HOH A . 
D 3 HOH   59  359 662  HOH   HOH A . 
D 3 HOH   60  360 354  HOH   HOH A . 
D 3 HOH   61  361 92   HOH   HOH A . 
D 3 HOH   62  362 396  HOH   HOH A . 
D 3 HOH   63  363 169  HOH   HOH A . 
D 3 HOH   64  364 66   HOH   HOH A . 
D 3 HOH   65  365 8    HOH   HOH A . 
D 3 HOH   66  366 461  HOH   HOH A . 
D 3 HOH   67  367 26   HOH   HOH A . 
D 3 HOH   68  368 2    HOH   HOH A . 
D 3 HOH   69  369 148  HOH   HOH A . 
D 3 HOH   70  370 19   HOH   HOH A . 
D 3 HOH   71  371 139  HOH   HOH A . 
D 3 HOH   72  372 81   HOH   HOH A . 
D 3 HOH   73  373 5    HOH   HOH A . 
D 3 HOH   74  374 138  HOH   HOH A . 
D 3 HOH   75  375 155  HOH   HOH A . 
D 3 HOH   76  376 27   HOH   HOH A . 
D 3 HOH   77  377 1309 HOH   HOH A . 
D 3 HOH   78  378 1296 HOH   HOH A . 
D 3 HOH   79  379 6    HOH   HOH A . 
D 3 HOH   80  380 162  HOH   HOH A . 
D 3 HOH   81  381 46   HOH   HOH A . 
D 3 HOH   82  382 366  HOH   HOH A . 
D 3 HOH   83  383 4    HOH   HOH A . 
D 3 HOH   84  384 45   HOH   HOH A . 
D 3 HOH   85  385 35   HOH   HOH A . 
D 3 HOH   86  386 78   HOH   HOH A . 
D 3 HOH   87  387 154  HOH   HOH A . 
D 3 HOH   88  388 1308 HOH   HOH A . 
D 3 HOH   89  389 159  HOH   HOH A . 
D 3 HOH   90  390 186  HOH   HOH A . 
D 3 HOH   91  391 116  HOH   HOH A . 
D 3 HOH   92  392 1275 HOH   HOH A . 
D 3 HOH   93  393 134  HOH   HOH A . 
D 3 HOH   94  394 12   HOH   HOH A . 
D 3 HOH   95  395 132  HOH   HOH A . 
D 3 HOH   96  396 278  HOH   HOH A . 
D 3 HOH   97  397 24   HOH   HOH A . 
D 3 HOH   98  398 74   HOH   HOH A . 
D 3 HOH   99  399 1313 HOH   HOH A . 
D 3 HOH   100 400 7    HOH   HOH A . 
D 3 HOH   101 401 83   HOH   HOH A . 
D 3 HOH   102 402 58   HOH   HOH A . 
D 3 HOH   103 403 3    HOH   HOH A . 
D 3 HOH   104 404 333  HOH   HOH A . 
D 3 HOH   105 405 351  HOH   HOH A . 
D 3 HOH   106 406 68   HOH   HOH A . 
D 3 HOH   107 407 67   HOH   HOH A . 
D 3 HOH   108 408 96   HOH   HOH A . 
D 3 HOH   109 409 303  HOH   HOH A . 
D 3 HOH   110 410 25   HOH   HOH A . 
D 3 HOH   111 411 1068 HOH   HOH A . 
D 3 HOH   112 412 123  HOH   HOH A . 
D 3 HOH   113 413 1315 HOH   HOH A . 
D 3 HOH   114 414 397  HOH   HOH A . 
D 3 HOH   115 415 381  HOH   HOH A . 
D 3 HOH   116 416 53   HOH   HOH A . 
D 3 HOH   117 417 405  HOH   HOH A . 
D 3 HOH   118 418 70   HOH   HOH A . 
D 3 HOH   119 419 121  HOH   HOH A . 
D 3 HOH   120 420 115  HOH   HOH A . 
D 3 HOH   121 421 95   HOH   HOH A . 
D 3 HOH   122 422 125  HOH   HOH A . 
D 3 HOH   123 423 51   HOH   HOH A . 
D 3 HOH   124 424 1289 HOH   HOH A . 
D 3 HOH   125 425 1279 HOH   HOH A . 
D 3 HOH   126 426 156  HOH   HOH A . 
D 3 HOH   127 427 944  HOH   HOH A . 
D 3 HOH   128 428 122  HOH   HOH A . 
D 3 HOH   129 429 1222 HOH   HOH A . 
D 3 HOH   130 430 1286 HOH   HOH A . 
D 3 HOH   131 431 16   HOH   HOH A . 
D 3 HOH   132 432 73   HOH   HOH A . 
D 3 HOH   133 433 80   HOH   HOH A . 
D 3 HOH   134 434 582  HOH   HOH A . 
D 3 HOH   135 435 212  HOH   HOH A . 
D 3 HOH   136 436 71   HOH   HOH A . 
D 3 HOH   137 437 1238 HOH   HOH A . 
D 3 HOH   138 438 94   HOH   HOH A . 
D 3 HOH   139 439 104  HOH   HOH A . 
D 3 HOH   140 440 1189 HOH   HOH A . 
D 3 HOH   141 441 1094 HOH   HOH A . 
D 3 HOH   142 442 188  HOH   HOH A . 
D 3 HOH   143 443 97   HOH   HOH A . 
D 3 HOH   144 444 952  HOH   HOH A . 
D 3 HOH   145 445 1134 HOH   HOH A . 
D 3 HOH   146 446 79   HOH   HOH A . 
D 3 HOH   147 447 576  HOH   HOH A . 
D 3 HOH   148 448 330  HOH   HOH A . 
D 3 HOH   149 449 509  HOH   HOH A . 
D 3 HOH   150 450 107  HOH   HOH A . 
D 3 HOH   151 451 1119 HOH   HOH A . 
D 3 HOH   152 452 726  HOH   HOH A . 
D 3 HOH   153 453 163  HOH   HOH A . 
D 3 HOH   154 454 408  HOH   HOH A . 
D 3 HOH   155 455 756  HOH   HOH A . 
D 3 HOH   156 456 342  HOH   HOH A . 
D 3 HOH   157 457 280  HOH   HOH A . 
D 3 HOH   158 458 319  HOH   HOH A . 
D 3 HOH   159 459 361  HOH   HOH A . 
D 3 HOH   160 460 126  HOH   HOH A . 
D 3 HOH   161 461 63   HOH   HOH A . 
D 3 HOH   162 462 556  HOH   HOH A . 
D 3 HOH   163 463 801  HOH   HOH A . 
D 3 HOH   164 464 1307 HOH   HOH A . 
D 3 HOH   165 465 370  HOH   HOH A . 
D 3 HOH   166 466 250  HOH   HOH A . 
D 3 HOH   167 467 1276 HOH   HOH A . 
D 3 HOH   168 468 135  HOH   HOH A . 
D 3 HOH   169 469 202  HOH   HOH A . 
D 3 HOH   170 470 1287 HOH   HOH A . 
D 3 HOH   171 471 1306 HOH   HOH A . 
D 3 HOH   172 472 521  HOH   HOH A . 
D 3 HOH   173 473 224  HOH   HOH A . 
D 3 HOH   174 474 674  HOH   HOH A . 
D 3 HOH   175 475 1284 HOH   HOH A . 
D 3 HOH   176 476 318  HOH   HOH A . 
D 3 HOH   177 477 919  HOH   HOH A . 
D 3 HOH   178 478 208  HOH   HOH A . 
D 3 HOH   179 479 981  HOH   HOH A . 
D 3 HOH   180 480 152  HOH   HOH A . 
D 3 HOH   181 481 695  HOH   HOH A . 
D 3 HOH   182 482 267  HOH   HOH A . 
D 3 HOH   183 483 1314 HOH   HOH A . 
D 3 HOH   184 484 941  HOH   HOH A . 
D 3 HOH   185 485 711  HOH   HOH A . 
D 3 HOH   186 486 309  HOH   HOH A . 
D 3 HOH   187 487 331  HOH   HOH A . 
D 3 HOH   188 488 1299 HOH   HOH A . 
D 3 HOH   189 489 805  HOH   HOH A . 
D 3 HOH   190 490 315  HOH   HOH A . 
D 3 HOH   191 491 356  HOH   HOH A . 
D 3 HOH   192 492 263  HOH   HOH A . 
D 3 HOH   193 493 1    HOH   HOH A . 
D 3 HOH   194 494 180  HOH   HOH A . 
D 3 HOH   195 495 1071 HOH   HOH A . 
D 3 HOH   196 496 363  HOH   HOH A . 
D 3 HOH   197 497 371  HOH   HOH A . 
D 3 HOH   198 498 326  HOH   HOH A . 
D 3 HOH   199 499 313  HOH   HOH A . 
D 3 HOH   200 500 185  HOH   HOH A . 
D 3 HOH   201 501 429  HOH   HOH A . 
D 3 HOH   202 502 376  HOH   HOH A . 
D 3 HOH   203 503 772  HOH   HOH A . 
D 3 HOH   204 504 1074 HOH   HOH A . 
D 3 HOH   205 505 1292 HOH   HOH A . 
D 3 HOH   206 506 346  HOH   HOH A . 
D 3 HOH   207 507 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 240  HOH   HOH B . 
E 3 HOH   3   203 549  HOH   HOH B . 
E 3 HOH   4   204 398  HOH   HOH B . 
E 3 HOH   5   205 364  HOH   HOH B . 
E 3 HOH   6   206 205  HOH   HOH B . 
E 3 HOH   7   207 1249 HOH   HOH B . 
E 3 HOH   8   208 358  HOH   HOH B . 
E 3 HOH   9   209 758  HOH   HOH B . 
E 3 HOH   10  210 353  HOH   HOH B . 
E 3 HOH   11  211 900  HOH   HOH B . 
E 3 HOH   12  212 50   HOH   HOH B . 
E 3 HOH   13  213 232  HOH   HOH B . 
E 3 HOH   14  214 120  HOH   HOH B . 
E 3 HOH   15  215 264  HOH   HOH B . 
E 3 HOH   16  216 332  HOH   HOH B . 
E 3 HOH   17  217 531  HOH   HOH B . 
E 3 HOH   18  218 743  HOH   HOH B . 
E 3 HOH   19  219 452  HOH   HOH B . 
E 3 HOH   20  220 75   HOH   HOH B . 
E 3 HOH   21  221 654  HOH   HOH B . 
E 3 HOH   22  222 1312 HOH   HOH B . 
E 3 HOH   23  223 1278 HOH   HOH B . 
E 3 HOH   24  224 82   HOH   HOH B . 
E 3 HOH   25  225 131  HOH   HOH B . 
E 3 HOH   26  226 172  HOH   HOH B . 
E 3 HOH   27  227 723  HOH   HOH B . 
E 3 HOH   28  228 127  HOH   HOH B . 
E 3 HOH   29  229 54   HOH   HOH B . 
E 3 HOH   30  230 110  HOH   HOH B . 
E 3 HOH   31  231 300  HOH   HOH B . 
E 3 HOH   32  232 1140 HOH   HOH B . 
E 3 HOH   33  233 444  HOH   HOH B . 
E 3 HOH   34  234 41   HOH   HOH B . 
E 3 HOH   35  235 325  HOH   HOH B . 
E 3 HOH   36  236 69   HOH   HOH B . 
E 3 HOH   37  237 60   HOH   HOH B . 
E 3 HOH   38  238 343  HOH   HOH B . 
E 3 HOH   39  239 272  HOH   HOH B . 
E 3 HOH   40  240 129  HOH   HOH B . 
E 3 HOH   41  241 166  HOH   HOH B . 
E 3 HOH   42  242 128  HOH   HOH B . 
E 3 HOH   43  243 1    HOH   HOH B . 
E 3 HOH   44  244 9    HOH   HOH B . 
E 3 HOH   45  245 416  HOH   HOH B . 
E 3 HOH   46  246 144  HOH   HOH B . 
E 3 HOH   47  247 30   HOH   HOH B . 
E 3 HOH   48  248 276  HOH   HOH B . 
E 3 HOH   49  249 14   HOH   HOH B . 
E 3 HOH   50  250 221  HOH   HOH B . 
E 3 HOH   51  251 133  HOH   HOH B . 
E 3 HOH   52  252 231  HOH   HOH B . 
E 3 HOH   53  253 52   HOH   HOH B . 
E 3 HOH   54  254 391  HOH   HOH B . 
E 3 HOH   55  255 72   HOH   HOH B . 
E 3 HOH   56  256 287  HOH   HOH B . 
E 3 HOH   57  257 47   HOH   HOH B . 
E 3 HOH   58  258 181  HOH   HOH B . 
E 3 HOH   59  259 31   HOH   HOH B . 
E 3 HOH   60  260 143  HOH   HOH B . 
E 3 HOH   61  261 103  HOH   HOH B . 
E 3 HOH   62  262 150  HOH   HOH B . 
E 3 HOH   63  263 243  HOH   HOH B . 
E 3 HOH   64  264 62   HOH   HOH B . 
E 3 HOH   65  265 302  HOH   HOH B . 
E 3 HOH   66  266 10   HOH   HOH B . 
E 3 HOH   67  267 271  HOH   HOH B . 
E 3 HOH   68  268 347  HOH   HOH B . 
E 3 HOH   69  269 242  HOH   HOH B . 
E 3 HOH   70  270 59   HOH   HOH B . 
E 3 HOH   71  271 20   HOH   HOH B . 
E 3 HOH   72  272 1277 HOH   HOH B . 
E 3 HOH   73  273 61   HOH   HOH B . 
E 3 HOH   74  274 11   HOH   HOH B . 
E 3 HOH   75  275 147  HOH   HOH B . 
E 3 HOH   76  276 117  HOH   HOH B . 
E 3 HOH   77  277 114  HOH   HOH B . 
E 3 HOH   78  278 282  HOH   HOH B . 
E 3 HOH   79  279 1305 HOH   HOH B . 
E 3 HOH   80  280 84   HOH   HOH B . 
E 3 HOH   81  281 1106 HOH   HOH B . 
E 3 HOH   82  282 207  HOH   HOH B . 
E 3 HOH   83  283 77   HOH   HOH B . 
E 3 HOH   84  284 22   HOH   HOH B . 
E 3 HOH   85  285 252  HOH   HOH B . 
E 3 HOH   86  286 175  HOH   HOH B . 
E 3 HOH   87  287 43   HOH   HOH B . 
E 3 HOH   88  288 235  HOH   HOH B . 
E 3 HOH   89  289 99   HOH   HOH B . 
E 3 HOH   90  290 13   HOH   HOH B . 
E 3 HOH   91  291 89   HOH   HOH B . 
E 3 HOH   92  292 160  HOH   HOH B . 
E 3 HOH   93  293 106  HOH   HOH B . 
E 3 HOH   94  294 216  HOH   HOH B . 
E 3 HOH   95  295 137  HOH   HOH B . 
E 3 HOH   96  296 311  HOH   HOH B . 
E 3 HOH   97  297 1066 HOH   HOH B . 
E 3 HOH   98  298 88   HOH   HOH B . 
E 3 HOH   99  299 112  HOH   HOH B . 
E 3 HOH   100 300 215  HOH   HOH B . 
E 3 HOH   101 301 297  HOH   HOH B . 
E 3 HOH   102 302 316  HOH   HOH B . 
E 3 HOH   103 303 220  HOH   HOH B . 
E 3 HOH   104 304 1291 HOH   HOH B . 
E 3 HOH   105 305 101  HOH   HOH B . 
E 3 HOH   106 306 1285 HOH   HOH B . 
E 3 HOH   107 307 197  HOH   HOH B . 
E 3 HOH   108 308 170  HOH   HOH B . 
E 3 HOH   109 309 32   HOH   HOH B . 
E 3 HOH   110 310 38   HOH   HOH B . 
E 3 HOH   111 311 142  HOH   HOH B . 
E 3 HOH   112 312 299  HOH   HOH B . 
E 3 HOH   113 313 177  HOH   HOH B . 
E 3 HOH   114 314 23   HOH   HOH B . 
E 3 HOH   115 315 44   HOH   HOH B . 
E 3 HOH   116 316 48   HOH   HOH B . 
E 3 HOH   117 317 118  HOH   HOH B . 
E 3 HOH   118 318 182  HOH   HOH B . 
E 3 HOH   119 319 37   HOH   HOH B . 
E 3 HOH   120 320 91   HOH   HOH B . 
E 3 HOH   121 321 28   HOH   HOH B . 
E 3 HOH   122 322 100  HOH   HOH B . 
E 3 HOH   123 323 635  HOH   HOH B . 
E 3 HOH   124 324 387  HOH   HOH B . 
E 3 HOH   125 325 445  HOH   HOH B . 
E 3 HOH   126 326 98   HOH   HOH B . 
E 3 HOH   127 327 1294 HOH   HOH B . 
E 3 HOH   128 328 1274 HOH   HOH B . 
E 3 HOH   129 329 29   HOH   HOH B . 
E 3 HOH   130 330 704  HOH   HOH B . 
E 3 HOH   131 331 55   HOH   HOH B . 
E 3 HOH   132 332 717  HOH   HOH B . 
E 3 HOH   133 333 141  HOH   HOH B . 
E 3 HOH   134 334 161  HOH   HOH B . 
E 3 HOH   135 335 334  HOH   HOH B . 
E 3 HOH   136 336 960  HOH   HOH B . 
E 3 HOH   137 337 87   HOH   HOH B . 
E 3 HOH   138 338 341  HOH   HOH B . 
E 3 HOH   139 339 65   HOH   HOH B . 
E 3 HOH   140 340 1293 HOH   HOH B . 
E 3 HOH   141 341 234  HOH   HOH B . 
E 3 HOH   142 342 362  HOH   HOH B . 
E 3 HOH   143 343 619  HOH   HOH B . 
E 3 HOH   144 344 1126 HOH   HOH B . 
E 3 HOH   145 345 178  HOH   HOH B . 
E 3 HOH   146 346 339  HOH   HOH B . 
E 3 HOH   147 347 90   HOH   HOH B . 
E 3 HOH   148 348 463  HOH   HOH B . 
E 3 HOH   149 349 191  HOH   HOH B . 
E 3 HOH   150 350 1304 HOH   HOH B . 
E 3 HOH   151 351 1280 HOH   HOH B . 
E 3 HOH   152 352 1046 HOH   HOH B . 
E 3 HOH   153 353 623  HOH   HOH B . 
E 3 HOH   154 354 335  HOH   HOH B . 
E 3 HOH   155 355 304  HOH   HOH B . 
E 3 HOH   156 356 1077 HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 203  HOH   HOH B . 
E 3 HOH   159 359 541  HOH   HOH B . 
E 3 HOH   160 360 389  HOH   HOH B . 
E 3 HOH   161 361 718  HOH   HOH B . 
E 3 HOH   162 362 283  HOH   HOH B . 
E 3 HOH   163 363 1072 HOH   HOH B . 
E 3 HOH   164 364 291  HOH   HOH B . 
E 3 HOH   165 365 479  HOH   HOH B . 
E 3 HOH   166 366 615  HOH   HOH B . 
E 3 HOH   167 367 340  HOH   HOH B . 
E 3 HOH   168 368 1316 HOH   HOH B . 
E 3 HOH   169 369 898  HOH   HOH B . 
E 3 HOH   170 370 373  HOH   HOH B . 
E 3 HOH   171 371 667  HOH   HOH B . 
E 3 HOH   172 372 310  HOH   HOH B . 
E 3 HOH   173 373 190  HOH   HOH B . 
E 3 HOH   174 374 1303 HOH   HOH B . 
E 3 HOH   175 375 431  HOH   HOH B . 
E 3 HOH   176 376 183  HOH   HOH B . 
E 3 HOH   177 377 418  HOH   HOH B . 
E 3 HOH   178 378 1000 HOH   HOH B . 
E 3 HOH   179 379 149  HOH   HOH B . 
E 3 HOH   180 380 1173 HOH   HOH B . 
E 3 HOH   181 381 1163 HOH   HOH B . 
E 3 HOH   182 382 1311 HOH   HOH B . 
E 3 HOH   183 383 176  HOH   HOH B . 
E 3 HOH   184 384 491  HOH   HOH B . 
E 3 HOH   185 385 424  HOH   HOH B . 
E 3 HOH   186 386 1298 HOH   HOH B . 
E 3 HOH   187 387 248  HOH   HOH B . 
E 3 HOH   188 388 470  HOH   HOH B . 
E 3 HOH   189 389 265  HOH   HOH B . 
E 3 HOH   190 390 184  HOH   HOH B . 
E 3 HOH   191 391 350  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 314  HOH   HOH B . 
E 3 HOH   196 396 274  HOH   HOH B . 
E 3 HOH   197 397 566  HOH   HOH B . 
E 3 HOH   198 398 157  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFM 
_cell.length_a           88.769 
_cell.length_b           88.769 
_cell.length_c           39.404 
_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                         7HFM 
_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          7HFM 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.49 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-10-07 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.380 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   169855 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.500 
_reflns.pdbx_Rmerge_I_obs            0.060 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.400 
_reflns.B_iso_Wilson_estimate        12.340 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.065 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1064934 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.990 1.010  ? 32109 7699 ? 1.567 ? ? ? 4.200 ? 0.500  ? ? ? ? ? ? 91.500 1.790 0.843 0.471 
1 2 5.420 44.380 ? 7758  1132 ? 0.042 ? ? ? 6.900 ? 35.600 ? ? ? ? ? ? 99.900 0.046 0.018 0.995 
# 
_refine.entry_id                                 7HFM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.3800 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3400 
_refine.ls_number_reflns_obs                     169565 
_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                          0.1497 
_refine.ls_R_factor_R_work                       0.1490 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1632 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8178 
_refine.ls_number_reflns_R_work                  161387 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.7907 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1300 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                81.400 
_refine.B_iso_min                                9.660 
_refine.pdbx_overall_phase_error                 19.9000 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        44.3800 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             408 
_refine_hist.number_atoms_total               2990 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           23.63 
_refine_hist.pdbx_B_iso_mean_solvent          32.21 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9900 1.0000  30 87.0000  4686 . 0.4671 0.4587 . 240 0.0000 4926 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 96.0000  5174 . 0.4170 0.3798 . 263 0.0000 5437 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 100.0000 5371 . 0.3570 0.3575 . 239 0.0000 5610 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5393 . 0.3198 0.3065 . 278 0.0000 5671 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5342 . 0.2841 0.2988 . 286 0.0000 5628 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5373 . 0.2776 0.2967 . 322 0.0000 5695 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5362 . 0.2380 0.2540 . 272 0.0000 5634 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5422 . 0.2218 0.2579 . 248 0.0000 5670 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5351 . 0.1907 0.2102 . 290 0.0000 5641 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5401 . 0.1719 0.1904 . 249 0.0000 5650 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5419 . 0.1631 0.1747 . 263 0.0000 5682 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5402 . 0.1485 0.1786 . 271 0.0000 5673 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5408 . 0.1406 0.1843 . 273 0.0000 5681 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5343 . 0.1294 0.1499 . 295 0.0000 5638 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5408 . 0.1314 0.1593 . 253 0.0000 5661 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5429 . 0.1342 0.1557 . 268 0.0000 5697 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5396 . 0.1301 0.1443 . 267 0.0000 5663 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5384 . 0.1354 0.1645 . 282 0.0000 5666 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5374 . 0.1328 0.1560 . 287 0.0000 5661 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5438 . 0.1307 0.1522 . 257 0.0000 5695 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5425 . 0.1261 0.1329 . 273 0.0000 5698 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5388 . 0.1207 0.1261 . 285 0.0000 5673 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5397 . 0.1198 0.1285 . 276 0.0000 5673 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5434 . 0.1258 0.1451 . 266 0.0000 5700 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5463 . 0.1345 0.1420 . 256 0.0000 5719 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5410 . 0.1352 0.1322 . 300 0.0000 5710 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5423 . 0.1403 0.1471 . 273 0.0000 5696 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5446 . 0.1383 0.1494 . 294 0.0000 5740 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5493 . 0.1488 0.1692 . 282 0.0000 5775 . 'X-RAY DIFFRACTION' 
3.0800 44.3800 30 100.0000 5632 . 0.1509 0.1704 . 270 0.0000 5902 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFM 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004320' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFM 
_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 3 ? 
# 
_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 7HFM A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFM 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 7HFM SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFM MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFM SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFM 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 
2 1 B,E   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N ALA A 124 ? N ALA A 124 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HH  A TYR 152 ? B O A HOH 301 ? ? 1.52 
2 1 HZ3 A LYS 55  ? B O A HOH 306 ? ? 1.59 
3 1 O   B HOH 217 ? ? O B HOH 307 ? ? 2.13 
# 
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  ? ? 55.71   -132.25 
2 1 SER A 128 ? B 69.37   -6.44   
3 1 PHE A 156 ? B -87.81  48.91   
4 1 ASP A 157 ? B -160.00 116.76  
5 1 HIS B 86  ? ? 57.61   -127.64 
# 
_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 505 ? 5.90 . 
2 1 O ? A HOH 506 ? 6.07 . 
3 1 O ? A HOH 507 ? 7.62 . 
4 1 O ? B HOH 401 ? 6.55 . 
# 
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 
A1BBN N2   N Y N 1   
A1BBN C3   C Y N 2   
A1BBN C6   C Y N 3   
A1BBN C9   C N N 4   
A1BBN C12  C N N 5   
A1BBN C14  C N N 6   
A1BBN C1   C N R 7   
A1BBN C10  C N N 8   
A1BBN C11  C N N 9   
A1BBN C13  C N N 10  
A1BBN C15  C N N 11  
A1BBN C2   C N N 12  
A1BBN C4   C Y N 13  
A1BBN C5   C Y N 14  
A1BBN C7   C Y N 15  
A1BBN C8   C Y N 16  
A1BBN N1   N N N 17  
A1BBN N3   N Y N 18  
A1BBN N4   N Y N 19  
A1BBN O1   O N N 20  
A1BBN H7   H N N 21  
A1BBN H6   H N N 22  
A1BBN H10  H N N 23  
A1BBN H9   H N N 24  
A1BBN H15  H N N 25  
A1BBN H14  H N N 26  
A1BBN H17  H N N 27  
A1BBN H18  H N N 28  
A1BBN H11  H N N 29  
A1BBN H12  H N N 30  
A1BBN H13  H N N 31  
A1BBN H16  H N N 32  
A1BBN H19  H N N 33  
A1BBN H20  H N N 34  
A1BBN H3   H N N 35  
A1BBN H2   H N N 36  
A1BBN H5   H N N 37  
A1BBN H8   H N N 38  
A1BBN H4   H N N 39  
A1BBN H1   H N N 40  
ALA   N    N N N 41  
ALA   CA   C N S 42  
ALA   C    C N N 43  
ALA   O    O N N 44  
ALA   CB   C N N 45  
ALA   OXT  O N N 46  
ALA   H    H N N 47  
ALA   H2   H N N 48  
ALA   HA   H N N 49  
ALA   HB1  H N N 50  
ALA   HB2  H N N 51  
ALA   HB3  H N N 52  
ALA   HXT  H N N 53  
ARG   N    N N N 54  
ARG   CA   C N S 55  
ARG   C    C N N 56  
ARG   O    O N N 57  
ARG   CB   C N N 58  
ARG   CG   C N N 59  
ARG   CD   C N N 60  
ARG   NE   N N N 61  
ARG   CZ   C N N 62  
ARG   NH1  N N N 63  
ARG   NH2  N N N 64  
ARG   OXT  O N N 65  
ARG   H    H N N 66  
ARG   H2   H N N 67  
ARG   HA   H N N 68  
ARG   HB2  H N N 69  
ARG   HB3  H N N 70  
ARG   HG2  H N N 71  
ARG   HG3  H N N 72  
ARG   HD2  H N N 73  
ARG   HD3  H N N 74  
ARG   HE   H N N 75  
ARG   HH11 H N N 76  
ARG   HH12 H N N 77  
ARG   HH21 H N N 78  
ARG   HH22 H N N 79  
ARG   HXT  H N N 80  
ASN   N    N N N 81  
ASN   CA   C N S 82  
ASN   C    C N N 83  
ASN   O    O N N 84  
ASN   CB   C N N 85  
ASN   CG   C N N 86  
ASN   OD1  O N N 87  
ASN   ND2  N N N 88  
ASN   OXT  O N N 89  
ASN   H    H N N 90  
ASN   H2   H N N 91  
ASN   HA   H N N 92  
ASN   HB2  H N N 93  
ASN   HB3  H N N 94  
ASN   HD21 H N N 95  
ASN   HD22 H N N 96  
ASN   HXT  H N N 97  
ASP   N    N N N 98  
ASP   CA   C N S 99  
ASP   C    C N N 100 
ASP   O    O N N 101 
ASP   CB   C N N 102 
ASP   CG   C N N 103 
ASP   OD1  O N N 104 
ASP   OD2  O N N 105 
ASP   OXT  O N N 106 
ASP   H    H N N 107 
ASP   H2   H N N 108 
ASP   HA   H N N 109 
ASP   HB2  H N N 110 
ASP   HB3  H N N 111 
ASP   HD2  H N N 112 
ASP   HXT  H N N 113 
CYS   N    N N N 114 
CYS   CA   C N R 115 
CYS   C    C N N 116 
CYS   O    O N N 117 
CYS   CB   C N N 118 
CYS   SG   S N N 119 
CYS   OXT  O N N 120 
CYS   H    H N N 121 
CYS   H2   H N N 122 
CYS   HA   H N N 123 
CYS   HB2  H N N 124 
CYS   HB3  H N N 125 
CYS   HG   H N N 126 
CYS   HXT  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
THR   N    N N N 344 
THR   CA   C N S 345 
THR   C    C N N 346 
THR   O    O N N 347 
THR   CB   C N R 348 
THR   OG1  O N N 349 
THR   CG2  C N N 350 
THR   OXT  O N N 351 
THR   H    H N N 352 
THR   H2   H N N 353 
THR   HA   H N N 354 
THR   HB   H N N 355 
THR   HG1  H N N 356 
THR   HG21 H N N 357 
THR   HG22 H N N 358 
THR   HG23 H N N 359 
THR   HXT  H N N 360 
TYR   N    N N N 361 
TYR   CA   C N S 362 
TYR   C    C N N 363 
TYR   O    O N N 364 
TYR   CB   C N N 365 
TYR   CG   C Y N 366 
TYR   CD1  C Y N 367 
TYR   CD2  C Y N 368 
TYR   CE1  C Y N 369 
TYR   CE2  C Y N 370 
TYR   CZ   C Y N 371 
TYR   OH   O N N 372 
TYR   OXT  O N N 373 
TYR   H    H N N 374 
TYR   H2   H N N 375 
TYR   HA   H N N 376 
TYR   HB2  H N N 377 
TYR   HB3  H N N 378 
TYR   HD1  H N N 379 
TYR   HD2  H N N 380 
TYR   HE1  H N N 381 
TYR   HE2  H N N 382 
TYR   HH   H N N 383 
TYR   HXT  H N N 384 
VAL   N    N N N 385 
VAL   CA   C N S 386 
VAL   C    C N N 387 
VAL   O    O N N 388 
VAL   CB   C N N 389 
VAL   CG1  C N N 390 
VAL   CG2  C N N 391 
VAL   OXT  O N N 392 
VAL   H    H N N 393 
VAL   H2   H N N 394 
VAL   HA   H N N 395 
VAL   HB   H N N 396 
VAL   HG11 H N N 397 
VAL   HG12 H N N 398 
VAL   HG13 H N N 399 
VAL   HG21 H N N 400 
VAL   HG22 H N N 401 
VAL   HG23 H N N 402 
VAL   HXT  H N N 403 
# 
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 
A1BBN C15 C14  sing N N 1   
A1BBN C15 C10  sing N N 2   
A1BBN C14 C13  sing N N 3   
A1BBN O1  C1   sing N N 4   
A1BBN C9  C10  sing N N 5   
A1BBN C9  C1   sing N N 6   
A1BBN C10 C11  sing N N 7   
A1BBN C1  C13  sing N N 8   
A1BBN C1  C2   sing N N 9   
A1BBN C13 C12  sing N N 10  
A1BBN C11 C12  sing N N 11  
A1BBN C2  N1   sing N N 12  
A1BBN N1  C3   sing N N 13  
A1BBN C3  N4   doub Y N 14  
A1BBN C3  C4   sing Y N 15  
A1BBN C5  C4   sing Y N 16  
A1BBN C5  C6   doub Y N 17  
A1BBN N4  C8   sing Y N 18  
A1BBN C4  C7   doub Y N 19  
A1BBN C6  N2   sing Y N 20  
A1BBN C8  N3   doub Y N 21  
A1BBN C7  N2   sing Y N 22  
A1BBN C7  N3   sing Y N 23  
A1BBN N2  H7   sing N N 24  
A1BBN C6  H6   sing N N 25  
A1BBN C9  H10  sing N N 26  
A1BBN C9  H9   sing N N 27  
A1BBN C12 H15  sing N N 28  
A1BBN C12 H14  sing N N 29  
A1BBN C14 H17  sing N N 30  
A1BBN C14 H18  sing N N 31  
A1BBN C10 H11  sing N N 32  
A1BBN C11 H12  sing N N 33  
A1BBN C11 H13  sing N N 34  
A1BBN C13 H16  sing N N 35  
A1BBN C15 H19  sing N N 36  
A1BBN C15 H20  sing N N 37  
A1BBN C2  H3   sing N N 38  
A1BBN C2  H2   sing N N 39  
A1BBN C5  H5   sing N N 40  
A1BBN C8  H8   sing N N 41  
A1BBN N1  H4   sing N N 42  
A1BBN O1  H1   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_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                    7HFM 
_atom_sites.fract_transf_matrix[1][1]   0.011265 
_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]   0.011265 
_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]   0.025378 
_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 
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   ? 19.675 -16.173 22.222  0.72 64.50 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.617 -16.117 22.342  0.28 63.34 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.693 -15.108 22.380  0.72 63.99 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.647 -15.043 22.514  0.28 62.94 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.337 -13.751 22.108  0.72 62.10 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.290 -13.697 22.201  0.28 61.44 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.447 -13.478 22.567  0.72 62.82 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.363 -13.381 22.716  0.28 61.99 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.036 -15.154 23.776  0.72 64.85 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.047 -15.052 23.934  0.28 63.69 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.001 -14.046 23.918  0.72 65.15 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.027 -13.933 24.087  0.28 63.95 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.397 -16.515 24.019  0.72 65.11 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.416 -16.403 24.238  0.28 63.92 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.990 -15.232 21.726  0.72 76.82 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.920 -15.175 21.890  0.28 75.57 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.716 -15.018 24.454  0.72 77.86 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.755 -14.901 24.580  0.28 76.47 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.489 -14.195 24.728  0.72 78.21 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.532 -14.068 24.910  0.28 76.78 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.456 -13.191 23.969  0.72 78.21 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.491 -13.082 24.116  0.28 76.78 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.412 -14.064 23.147  0.72 78.21 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.420 -13.955 23.330  0.28 76.78 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.928 -16.497 24.868  0.72 78.18 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.979 -16.359 25.103  0.28 76.74 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.773 -16.703 23.300  0.72 78.18 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.766 -16.608 23.548  0.28 76.74 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.092 -17.192 24.039  0.72 78.18 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.110 -17.080 24.251  0.28 76.74 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.635 -12.908 21.353  1.00 58.88 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.087 -11.558 21.033  1.00 52.85 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.963 -10.564 21.311  1.00 47.14 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.849 -10.939 21.690  1.00 47.40 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.623 -11.445 19.597  1.00 52.22 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.614 -11.871 18.555  1.00 51.58 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.458 -11.449 18.580  1.00 51.25 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.051 -12.714 17.625  1.00 51.41 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.870 -13.103 21.009  0.72 70.70 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.911 -13.138 20.946  0.28 70.70 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.819 -11.337 21.619  1.00 63.45 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.866 -10.520 19.420  1.00 62.70 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.406 -12.011 19.505  1.00 62.70 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.520 -12.986 17.006  1.00 61.73 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.867 -12.989 17.641  1.00 61.73 ?  4   ASN   A HD22 1 
ATOM   46   N N    A SER   A 1 5   ? 18.236 -9.282  21.069  0.72 43.90 ?  5   SER   A N    1 
ATOM   47   N N    B SER   A 1 5   ? 18.296 -9.283  21.169  0.28 44.22 ?  5   SER   A N    1 
ATOM   48   C CA   A SER   A 1 5   ? 17.318 -8.211  21.434  0.72 40.54 ?  5   SER   A CA   1 
ATOM   49   C CA   B SER   A 1 5   ? 17.409 -8.192  21.546  0.28 41.17 ?  5   SER   A CA   1 
ATOM   50   C C    A SER   A 1 5   ? 16.462 -7.708  20.273  0.72 36.04 ?  5   SER   A C    1 
ATOM   51   C C    B SER   A 1 5   ? 16.512 -7.734  20.406  0.28 37.28 ?  5   SER   A C    1 
ATOM   52   O O    A SER   A 1 5   ? 15.851 -6.642  20.392  0.72 36.24 ?  5   SER   A O    1 
ATOM   53   O O    B SER   A 1 5   ? 15.774 -6.758  20.571  0.28 37.31 ?  5   SER   A O    1 
ATOM   54   C CB   A SER   A 1 5   ? 18.085 -7.043  22.059  0.72 41.56 ?  5   SER   A CB   1 
ATOM   55   C CB   B SER   A 1 5   ? 18.220 -7.007  22.084  0.28 41.87 ?  5   SER   A CB   1 
ATOM   56   O OG   A SER   A 1 5   ? 19.085 -6.561  21.180  0.72 42.30 ?  5   SER   A OG   1 
ATOM   57   O OG   B SER   A 1 5   ? 19.108 -6.504  21.101  0.28 42.31 ?  5   SER   A OG   1 
ATOM   58   H H    A SER   A 1 5   ? 18.954 -9.010  20.683  0.72 52.72 ?  5   SER   A H    1 
ATOM   59   H H    B SER   A 1 5   ? 19.045 -9.018  20.844  0.28 53.10 ?  5   SER   A H    1 
ATOM   60   H HA   A SER   A 1 5   ? 16.716 -8.549  22.115  0.72 48.68 ?  5   SER   A HA   1 
ATOM   61   H HA   B SER   A 1 5   ? 16.834 -8.496  22.262  0.28 49.44 ?  5   SER   A HA   1 
ATOM   62   H HB2  A SER   A 1 5   ? 17.461 -6.323  22.251  0.72 49.91 ?  5   SER   A HB2  1 
ATOM   63   H HB2  B SER   A 1 5   ? 17.609 -6.302  22.350  0.28 50.28 ?  5   SER   A HB2  1 
ATOM   64   H HB3  A SER   A 1 5   ? 18.502 -7.344  22.881  0.72 49.91 ?  5   SER   A HB3  1 
ATOM   65   H HB3  B SER   A 1 5   ? 18.736 -7.303  22.852  0.28 50.28 ?  5   SER   A HB3  1 
ATOM   66   H HG   A SER   A 1 5   ? 19.497 -5.922  21.538  0.72 50.79 ?  5   SER   A HG   1 
ATOM   67   H HG   B SER   A 1 5   ? 19.542 -5.855  21.413  0.28 50.81 ?  5   SER   A HG   1 
ATOM   68   N N    A PHE   A 1 6   ? 16.402 -8.434  19.158  0.72 31.26 ?  6   PHE   A N    1 
ATOM   69   N N    B PHE   A 1 6   ? 16.559 -8.406  19.260  0.28 33.38 ?  6   PHE   A N    1 
ATOM   70   C CA   A PHE   A 1 6   ? 15.501 -8.059  18.073  0.72 26.70 ?  6   PHE   A CA   1 
ATOM   71   C CA   B PHE   A 1 6   ? 15.600 -8.127  18.204  0.28 29.61 ?  6   PHE   A CA   1 
ATOM   72   C C    A PHE   A 1 6   ? 14.066 -8.415  18.450  0.72 26.19 ?  6   PHE   A C    1 
ATOM   73   C C    B PHE   A 1 6   ? 14.223 -8.613  18.634  0.28 28.36 ?  6   PHE   A C    1 
ATOM   74   O O    A PHE   A 1 6   ? 13.804 -9.517  18.940  0.72 27.06 ?  6   PHE   A O    1 
ATOM   75   O O    B PHE   A 1 6   ? 14.090 -9.662  19.272  0.28 28.84 ?  6   PHE   A O    1 
ATOM   76   C CB   A PHE   A 1 6   ? 15.893 -8.770  16.780  0.72 23.74 ?  6   PHE   A CB   1 
ATOM   77   C CB   B PHE   A 1 6   ? 16.011 -8.841  16.918  0.28 27.34 ?  6   PHE   A CB   1 
ATOM   78   C CG   A PHE   A 1 6   ? 17.160 -8.244  16.156  0.72 21.56 ?  6   PHE   A CG   1 
ATOM   79   C CG   B PHE   A 1 6   ? 17.317 -8.368  16.347  0.28 25.45 ?  6   PHE   A CG   1 
ATOM   80   C CD1  A PHE   A 1 6   ? 17.146 -7.083  15.400  0.72 20.35 ?  6   PHE   A CD1  1 
ATOM   81   C CD1  B PHE   A 1 6   ? 17.426 -7.107  15.784  0.28 24.53 ?  6   PHE   A CD1  1 
ATOM   82   C CD2  A PHE   A 1 6   ? 18.357 -8.915  16.319  0.72 21.68 ?  6   PHE   A CD2  1 
ATOM   83   C CD2  B PHE   A 1 6   ? 18.430 -9.191  16.355  0.28 24.95 ?  6   PHE   A CD2  1 
ATOM   84   C CE1  A PHE   A 1 6   ? 18.309 -6.598  14.824  0.72 19.97 ?  6   PHE   A CE1  1 
ATOM   85   C CE1  B PHE   A 1 6   ? 18.626 -6.672  15.252  0.28 24.10 ?  6   PHE   A CE1  1 
ATOM   86   C CE2  A PHE   A 1 6   ? 19.518 -8.442  15.745  0.72 21.47 ?  6   PHE   A CE2  1 
ATOM   87   C CE2  B PHE   A 1 6   ? 19.632 -8.763  15.824  0.28 24.47 ?  6   PHE   A CE2  1 
ATOM   88   C CZ   A PHE   A 1 6   ? 19.496 -7.281  14.996  0.72 20.47 ?  6   PHE   A CZ   1 
ATOM   89   C CZ   B PHE   A 1 6   ? 19.730 -7.502  15.271  0.28 24.12 ?  6   PHE   A CZ   1 
ATOM   90   H H    A PHE   A 1 6   ? 16.876 -9.140  19.002  0.72 37.55 ?  6   PHE   A H    1 
ATOM   91   H H    B PHE   A 1 6   ? 17.129 -9.024  19.074  0.28 40.09 ?  6   PHE   A H    1 
ATOM   92   H HA   A PHE   A 1 6   ? 15.550 -7.105  17.931  0.72 32.08 ?  6   PHE   A HA   1 
ATOM   93   H HA   B PHE   A 1 6   ? 15.560 -7.173  18.038  0.28 35.57 ?  6   PHE   A HA   1 
ATOM   94   H HB2  A PHE   A 1 6   ? 16.026 -9.714  16.969  0.72 28.53 ?  6   PHE   A HB2  1 
ATOM   95   H HB2  B PHE   A 1 6   ? 16.096 -9.789  17.104  0.28 32.85 ?  6   PHE   A HB2  1 
ATOM   96   H HB3  A PHE   A 1 6   ? 15.176 -8.664  16.136  0.72 28.53 ?  6   PHE   A HB3  1 
ATOM   97   H HB3  B PHE   A 1 6   ? 15.325 -8.697  16.251  0.28 32.85 ?  6   PHE   A HB3  1 
ATOM   98   H HD1  A PHE   A 1 6   ? 16.344 -6.622  15.279  0.72 24.46 ?  6   PHE   A HD1  1 
ATOM   99   H HD1  B PHE   A 1 6   ? 16.687 -6.545  15.771  0.28 29.48 ?  6   PHE   A HD1  1 
ATOM   100  H HD2  A PHE   A 1 6   ? 18.378 -9.695  16.824  0.72 26.06 ?  6   PHE   A HD2  1 
ATOM   101  H HD2  B PHE   A 1 6   ? 18.370 -10.041 16.726  0.28 29.98 ?  6   PHE   A HD2  1 
ATOM   102  H HE1  A PHE   A 1 6   ? 18.288 -5.817  14.315  0.72 24.00 ?  6   PHE   A HE1  1 
ATOM   103  H HE1  B PHE   A 1 6   ? 18.691 -5.822  14.880  0.28 28.96 ?  6   PHE   A HE1  1 
ATOM   104  H HE2  A PHE   A 1 6   ? 20.319 -8.898  15.865  0.72 25.80 ?  6   PHE   A HE2  1 
ATOM   105  H HE2  B PHE   A 1 6   ? 20.374 -9.325  15.838  0.28 29.40 ?  6   PHE   A HE2  1 
ATOM   106  H HZ   A PHE   A 1 6   ? 20.276 -6.956  14.609  0.72 24.61 ?  6   PHE   A HZ   1 
ATOM   107  H HZ   B PHE   A 1 6   ? 20.539 -7.212  14.912  0.28 28.98 ?  6   PHE   A HZ   1 
ATOM   108  N N    A SER   A 1 7   ? 13.136 -7.488  18.214  0.72 25.13 ?  7   SER   A N    1 
ATOM   109  N N    B SER   A 1 7   ? 13.193 -7.844  18.290  0.28 26.72 ?  7   SER   A N    1 
ATOM   110  C CA   A SER   A 1 7   ? 11.761 -7.619  18.681  0.72 24.94 ?  7   SER   A CA   1 
ATOM   111  C CA   B SER   A 1 7   ? 11.838 -8.192  18.688  0.28 25.33 ?  7   SER   A CA   1 
ATOM   112  C C    A SER   A 1 7   ? 10.774 -7.359  17.548  0.72 23.28 ?  7   SER   A C    1 
ATOM   113  C C    B SER   A 1 7   ? 10.860 -7.719  17.623  0.28 23.61 ?  7   SER   A C    1 
ATOM   114  O O    A SER   A 1 7   ? 10.998 -6.493  16.699  0.72 23.28 ?  7   SER   A O    1 
ATOM   115  O O    B SER   A 1 7   ? 11.125 -6.756  16.898  0.28 23.58 ?  7   SER   A O    1 
ATOM   116  C CB   A SER   A 1 7   ? 11.497 -6.639  19.832  0.72 26.39 ?  7   SER   A CB   1 
ATOM   117  C CB   B SER   A 1 7   ? 11.480 -7.578  20.048  0.28 25.83 ?  7   SER   A CB   1 
ATOM   118  O OG   A SER   A 1 7   ? 10.163 -6.744  20.292  0.72 27.88 ?  7   SER   A OG   1 
ATOM   119  O OG   B SER   A 1 7   ? 10.411 -8.275  20.662  0.28 26.29 ?  7   SER   A OG   1 
ATOM   120  H H    A SER   A 1 7   ? 13.289 -6.763  17.773  0.72 30.19 ?  7   SER   A H    1 
ATOM   121  H H    B SER   A 1 7   ? 13.256 -7.122  17.826  0.28 32.10 ?  7   SER   A H    1 
ATOM   122  H HA   A SER   A 1 7   ? 11.618 -8.518  19.009  0.72 29.96 ?  7   SER   A HA   1 
ATOM   123  H HA   B SER   A 1 7   ? 11.767 -9.155  18.762  0.28 30.44 ?  7   SER   A HA   1 
ATOM   124  H HB2  A SER   A 1 7   ? 12.099 -6.845  20.568  0.72 31.70 ?  7   SER   A HB2  1 
ATOM   125  H HB2  B SER   A 1 7   ? 12.257 -7.620  20.627  0.28 31.03 ?  7   SER   A HB2  1 
ATOM   126  H HB3  A SER   A 1 7   ? 11.661 -5.734  19.520  0.72 31.70 ?  7   SER   A HB3  1 
ATOM   127  H HB3  B SER   A 1 7   ? 11.213 -6.657  19.917  0.28 31.03 ?  7   SER   A HB3  1 
ATOM   128  H HG   A SER   A 1 7   ? 10.033 -6.196  20.916  0.72 33.49 ?  7   SER   A HG   1 
ATOM   129  H HG   B SER   A 1 7   ? 9.733  -8.257  20.169  0.28 31.59 ?  7   SER   A HG   1 
ATOM   130  N N    A GLY   A 1 8   ? 9.679  -8.116  17.540  0.72 22.17 ?  8   GLY   A N    1 
ATOM   131  N N    B GLY   A 1 8   ? 9.726  -8.412  17.536  0.28 22.21 ?  8   GLY   A N    1 
ATOM   132  C CA   A GLY   A 1 8   ? 8.596  -7.875  16.608  0.72 21.28 ?  8   GLY   A CA   1 
ATOM   133  C CA   B GLY   A 1 8   ? 8.689  -8.046  16.593  0.28 20.95 ?  8   GLY   A CA   1 
ATOM   134  C C    A GLY   A 1 8   ? 8.799  -8.396  15.204  0.72 19.95 ?  8   GLY   A C    1 
ATOM   135  C C    B GLY   A 1 8   ? 8.898  -8.537  15.179  0.28 19.67 ?  8   GLY   A C    1 
ATOM   136  O O    A GLY   A 1 8   ? 8.067  -7.984  14.299  0.72 20.54 ?  8   GLY   A O    1 
ATOM   137  O O    B GLY   A 1 8   ? 8.246  -8.030  14.260  0.28 19.92 ?  8   GLY   A O    1 
ATOM   138  H H    A GLY   A 1 8   ? 9.548  -8.769  18.072  0.72 26.64 ?  8   GLY   A H    1 
ATOM   139  H H    B GLY   A 1 8   ? 9.537  -9.097  18.021  0.28 26.70 ?  8   GLY   A H    1 
ATOM   140  H HA2  A GLY   A 1 8   ? 7.791  -8.281  16.967  0.72 25.58 ?  8   GLY   A HA2  1 
ATOM   141  H HA2  B GLY   A 1 8   ? 7.843  -8.397  16.910  0.28 25.18 ?  8   GLY   A HA2  1 
ATOM   142  H HA3  A GLY   A 1 8   ? 8.442  -6.920  16.545  0.72 25.58 ?  8   GLY   A HA3  1 
ATOM   143  H HA3  B GLY   A 1 8   ? 8.620  -7.079  16.567  0.28 25.18 ?  8   GLY   A HA3  1 
ATOM   144  N N    A TYR   A 1 9   ? 9.765  -9.289  14.985  0.72 18.35 ?  9   TYR   A N    1 
ATOM   145  N N    B TYR   A 1 9   ? 9.778  -9.513  14.974  0.28 18.16 ?  9   TYR   A N    1 
ATOM   146  C CA   A TYR   A 1 9   ? 10.027 -9.823  13.655  0.72 17.04 ?  9   TYR   A CA   1 
ATOM   147  C CA   B TYR   A 1 9   ? 10.093 -10.013 13.644  0.28 16.86 ?  9   TYR   A CA   1 
ATOM   148  C C    A TYR   A 1 9   ? 9.171  -11.053 13.389  0.72 16.22 ?  9   TYR   A C    1 
ATOM   149  C C    B TYR   A 1 9   ? 9.242  -11.227 13.295  0.28 16.43 ?  9   TYR   A C    1 
ATOM   150  O O    A TYR   A 1 9   ? 8.934  -11.872 14.284  0.72 18.02 ?  9   TYR   A O    1 
ATOM   151  O O    B TYR   A 1 9   ? 8.878  -12.032 14.157  0.28 16.77 ?  9   TYR   A O    1 
ATOM   152  C CB   A TYR   A 1 9   ? 11.503 -10.203 13.494  0.72 17.49 ?  9   TYR   A CB   1 
ATOM   153  C CB   B TYR   A 1 9   ? 11.571 -10.400 13.547  0.28 16.29 ?  9   TYR   A CB   1 
ATOM   154  C CG   A TYR   A 1 9   ? 12.412 -9.008  13.316  0.72 17.65 ?  9   TYR   A CG   1 
ATOM   155  C CG   B TYR   A 1 9   ? 12.502 -9.218  13.433  0.28 15.51 ?  9   TYR   A CG   1 
ATOM   156  C CD1  A TYR   A 1 9   ? 12.717 -8.191  14.392  0.72 18.14 ?  9   TYR   A CD1  1 
ATOM   157  C CD1  B TYR   A 1 9   ? 12.877 -8.498  14.556  0.28 15.11 ?  9   TYR   A CD1  1 
ATOM   158  C CD2  A TYR   A 1 9   ? 12.934 -8.684  12.071  0.72 17.26 ?  9   TYR   A CD2  1 
ATOM   159  C CD2  B TYR   A 1 9   ? 13.004 -8.823  12.201  0.28 15.29 ?  9   TYR   A CD2  1 
ATOM   160  C CE1  A TYR   A 1 9   ? 13.519 -7.084  14.237  0.72 18.35 ?  9   TYR   A CE1  1 
ATOM   161  C CE1  B TYR   A 1 9   ? 13.723 -7.413  14.457  0.28 15.19 ?  9   TYR   A CE1  1 
ATOM   162  C CE2  A TYR   A 1 9   ? 13.742 -7.581  11.906  0.72 17.58 ?  9   TYR   A CE2  1 
ATOM   163  C CE2  B TYR   A 1 9   ? 13.851 -7.741  12.091  0.28 15.39 ?  9   TYR   A CE2  1 
ATOM   164  C CZ   A TYR   A 1 9   ? 14.028 -6.785  12.990  0.72 17.84 ?  9   TYR   A CZ   1 
ATOM   165  C CZ   B TYR   A 1 9   ? 14.207 -7.039  13.222  0.28 15.70 ?  9   TYR   A CZ   1 
ATOM   166  O OH   A TYR   A 1 9   ? 14.821 -5.681  12.820  0.72 18.43 ?  9   TYR   A OH   1 
ATOM   167  O OH   B TYR   A 1 9   ? 15.051 -5.961  13.113  0.28 16.77 ?  9   TYR   A OH   1 
ATOM   168  H H    A TYR   A 1 9   ? 10.281 -9.606  15.595  0.72 22.05 ?  9   TYR   A H    1 
ATOM   169  H H    B TYR   A 1 9   ? 10.209 -9.907  15.601  0.28 21.83 ?  9   TYR   A H    1 
ATOM   170  H HA   A TYR   A 1 9   ? 9.813  -9.143  12.992  0.72 20.49 ?  9   TYR   A HA   1 
ATOM   171  H HA   B TYR   A 1 9   ? 9.917  -9.323  12.989  0.28 20.27 ?  9   TYR   A HA   1 
ATOM   172  H HB2  A TYR   A 1 9   ? 11.789 -10.699 14.279  0.72 21.03 ?  9   TYR   A HB2  1 
ATOM   173  H HB2  B TYR   A 1 9   ? 11.820 -10.896 14.341  0.28 19.59 ?  9   TYR   A HB2  1 
ATOM   174  H HB3  A TYR   A 1 9   ? 11.576 -10.761 12.705  0.72 21.03 ?  9   TYR   A HB3  1 
ATOM   175  H HB3  B TYR   A 1 9   ? 11.698 -10.952 12.760  0.28 19.59 ?  9   TYR   A HB3  1 
ATOM   176  H HD1  A TYR   A 1 9   ? 12.361 -8.394  15.233  0.72 21.80 ?  9   TYR   A HD1  1 
ATOM   177  H HD1  B TYR   A 1 9   ? 12.545 -8.746  15.390  0.28 18.16 ?  9   TYR   A HD1  1 
ATOM   178  H HD2  A TYR   A 1 9   ? 12.731 -9.221  11.339  0.72 20.75 ?  9   TYR   A HD2  1 
ATOM   179  H HD2  B TYR   A 1 9   ? 12.765 -9.295  11.436  0.28 18.39 ?  9   TYR   A HD2  1 
ATOM   180  H HE1  A TYR   A 1 9   ? 13.716 -6.549  14.970  0.72 22.06 ?  9   TYR   A HE1  1 
ATOM   181  H HE1  B TYR   A 1 9   ? 13.964 -6.938  15.218  0.28 18.26 ?  9   TYR   A HE1  1 
ATOM   182  H HE2  A TYR   A 1 9   ? 14.089 -7.375  11.069  0.72 21.14 ?  9   TYR   A HE2  1 
ATOM   183  H HE2  B TYR   A 1 9   ? 14.183 -7.488  11.260  0.28 18.50 ?  9   TYR   A HE2  1 
ATOM   184  H HH   A TYR   A 1 9   ? 14.932 -5.292  13.557  0.72 22.15 ?  9   TYR   A HH   1 
ATOM   185  H HH   B TYR   A 1 9   ? 15.273 -5.854  12.309  0.28 20.16 ?  9   TYR   A HH   1 
ATOM   186  N N    A LEU   A 1 10  ? 8.721  -11.179 12.144  0.72 15.73 ?  10  LEU   A N    1 
ATOM   187  N N    B LEU   A 1 10  ? 8.948  -11.357 12.006  0.28 16.11 ?  10  LEU   A N    1 
ATOM   188  C CA   A LEU   A 1 10  ? 8.150  -12.426 11.661  0.72 15.27 ?  10  LEU   A CA   1 
ATOM   189  C CA   B LEU   A 1 10  ? 8.246  -12.509 11.459  0.28 15.79 ?  10  LEU   A CA   1 
ATOM   190  C C    A LEU   A 1 10  ? 9.295  -13.351 11.254  0.72 14.53 ?  10  LEU   A C    1 
ATOM   191  C C    B LEU   A 1 10  ? 9.276  -13.479 10.897  0.28 14.82 ?  10  LEU   A C    1 
ATOM   192  O O    A LEU   A 1 10  ? 10.275 -12.912 10.641  0.72 14.16 ?  10  LEU   A O    1 
ATOM   193  O O    B LEU   A 1 10  ? 10.155 -13.080 10.123  0.28 14.38 ?  10  LEU   A O    1 
ATOM   194  C CB   A LEU   A 1 10  ? 7.254  -12.138 10.456  0.72 16.50 ?  10  LEU   A CB   1 
ATOM   195  C CB   B LEU   A 1 10  ? 7.297  -12.055 10.350  0.28 16.97 ?  10  LEU   A CB   1 
ATOM   196  C CG   A LEU   A 1 10  ? 6.580  -13.331 9.779   0.72 17.85 ?  10  LEU   A CG   1 
ATOM   197  C CG   B LEU   A 1 10  ? 6.147  -12.979 9.954   0.28 17.86 ?  10  LEU   A CG   1 
ATOM   198  C CD1  A LEU   A 1 10  ? 5.481  -13.898 10.662  0.72 19.37 ?  10  LEU   A CD1  1 
ATOM   199  C CD1  B LEU   A 1 10  ? 5.007  -12.163 9.370   0.28 18.24 ?  10  LEU   A CD1  1 
ATOM   200  C CD2  A LEU   A 1 10  ? 6.029  -12.947 8.411   0.72 19.71 ?  10  LEU   A CD2  1 
ATOM   201  C CD2  B LEU   A 1 10  ? 6.606  -14.008 8.948   0.28 18.26 ?  10  LEU   A CD2  1 
ATOM   202  H H    A LEU   A 1 10  ? 8.731  -10.539 11.552  0.72 18.91 ?  10  LEU   A H    1 
ATOM   203  H H    B LEU   A 1 10  ? 9.151  -10.773 11.410  0.28 19.37 ?  10  LEU   A H    1 
ATOM   204  H HA   A LEU   A 1 10  ? 7.619  -12.838 12.367  0.72 18.37 ?  10  LEU   A HA   1 
ATOM   205  H HA   B LEU   A 1 10  ? 7.736  -12.953 12.155  0.28 18.99 ?  10  LEU   A HA   1 
ATOM   206  H HB2  A LEU   A 1 10  ? 6.543  -11.540 10.737  0.72 19.83 ?  10  LEU   A HB2  1 
ATOM   207  H HB2  B LEU   A 1 10  ? 6.907  -11.216 10.625  0.28 20.40 ?  10  LEU   A HB2  1 
ATOM   208  H HB3  A LEU   A 1 10  ? 7.792  -11.701 9.782   0.72 19.83 ?  10  LEU   A HB3  1 
ATOM   209  H HB3  B LEU   A 1 10  ? 7.828  -11.914 9.551   0.28 20.40 ?  10  LEU   A HB3  1 
ATOM   210  H HG   A LEU   A 1 10  ? 7.240  -14.031 9.648   0.72 21.46 ?  10  LEU   A HG   1 
ATOM   211  H HG   B LEU   A 1 10  ? 5.814  -13.440 10.740  0.28 21.47 ?  10  LEU   A HG   1 
ATOM   212  H HD11 A LEU   A 1 10  ? 5.119  -14.697 10.245  0.72 23.28 ?  10  LEU   A HD11 1 
ATOM   213  H HD11 B LEU   A 1 10  ? 4.296  -12.762 9.093   0.28 21.93 ?  10  LEU   A HD11 1 
ATOM   214  H HD12 A LEU   A 1 10  ? 5.855  -14.122 11.531  0.72 23.28 ?  10  LEU   A HD12 1 
ATOM   215  H HD12 B LEU   A 1 10  ? 4.677  -11.547 10.043  0.28 21.93 ?  10  LEU   A HD12 1 
ATOM   216  H HD13 A LEU   A 1 10  ? 4.784  -13.233 10.766  0.72 23.28 ?  10  LEU   A HD13 1 
ATOM   217  H HD13 B LEU   A 1 10  ? 5.335  -11.666 8.602   0.28 21.93 ?  10  LEU   A HD13 1 
ATOM   218  H HD21 A LEU   A 1 10  ? 5.609  -13.725 8.015   0.72 23.69 ?  10  LEU   A HD21 1 
ATOM   219  H HD21 B LEU   A 1 10  ? 5.848  -14.559 8.695   0.28 21.95 ?  10  LEU   A HD21 1 
ATOM   220  H HD22 A LEU   A 1 10  ? 5.382  -12.238 8.524   0.72 23.69 ?  10  LEU   A HD22 1 
ATOM   221  H HD22 B LEU   A 1 10  ? 6.958  -13.551 8.169   0.28 21.95 ?  10  LEU   A HD22 1 
ATOM   222  H HD23 A LEU   A 1 10  ? 6.764  -12.646 7.856   0.72 23.69 ?  10  LEU   A HD23 1 
ATOM   223  H HD23 B LEU   A 1 10  ? 7.293  -14.554 9.354   0.28 21.95 ?  10  LEU   A HD23 1 
ATOM   224  N N    A LYS   A 1 11  ? 9.181  -14.629 11.617  0.72 14.75 ?  11  LYS   A N    1 
ATOM   225  N N    B LYS   A 1 11  ? 9.168  -14.744 11.295  0.28 14.31 ?  11  LYS   A N    1 
ATOM   226  C CA   A LYS   A 1 11  ? 10.205 -15.620 11.304  0.72 14.68 ?  11  LYS   A CA   1 
ATOM   227  C CA   B LYS   A 1 11  ? 10.114 -15.766 10.878  0.28 14.08 ?  11  LYS   A CA   1 
ATOM   228  C C    A LYS   A 1 11  ? 9.873  -16.220 9.943   0.72 14.58 ?  11  LYS   A C    1 
ATOM   229  C C    B LYS   A 1 11  ? 9.738  -16.263 9.488   0.28 13.78 ?  11  LYS   A C    1 
ATOM   230  O O    A LYS   A 1 11  ? 8.840  -16.880 9.783   0.72 15.69 ?  11  LYS   A O    1 
ATOM   231  O O    B LYS   A 1 11  ? 8.575  -16.588 9.234   0.28 14.67 ?  11  LYS   A O    1 
ATOM   232  C CB   A LYS   A 1 11  ? 10.263 -16.692 12.390  0.72 14.54 ?  11  LYS   A CB   1 
ATOM   233  C CB   B LYS   A 1 11  ? 10.062 -16.914 11.885  0.28 14.13 ?  11  LYS   A CB   1 
ATOM   234  C CG   A LYS   A 1 11  ? 11.285 -17.804 12.156  0.72 14.85 ?  11  LYS   A CG   1 
ATOM   235  C CG   B LYS   A 1 11  ? 11.187 -17.917 11.812  0.28 14.05 ?  11  LYS   A CG   1 
ATOM   236  C CD   A LYS   A 1 11  ? 11.417 -18.683 13.405  0.72 14.96 ?  11  LYS   A CD   1 
ATOM   237  C CD   B LYS   A 1 11  ? 11.148 -18.788 13.060  0.28 14.64 ?  11  LYS   A CD   1 
ATOM   238  C CE   A LYS   A 1 11  ? 12.399 -19.843 13.219  0.72 15.55 ?  11  LYS   A CE   1 
ATOM   239  C CE   B LYS   A 1 11  ? 12.199 -19.876 13.033  0.28 14.98 ?  11  LYS   A CE   1 
ATOM   240  N NZ   A LYS   A 1 11  ? 13.788 -19.379 12.967  0.72 15.72 ?  11  LYS   A NZ   1 
ATOM   241  N NZ   B LYS   A 1 11  ? 13.565 -19.320 12.843  0.28 15.29 ?  11  LYS   A NZ   1 
ATOM   242  H H    A LYS   A 1 11  ? 8.502  -14.943 12.040  0.72 17.74 ?  11  LYS   A H    1 
ATOM   243  H H    B LYS   A 1 11  ? 8.542  -15.042 11.812  0.28 17.21 ?  11  LYS   A H    1 
ATOM   244  H HA   A LYS   A 1 11  ? 11.069 -15.175 11.252  0.72 17.66 ?  11  LYS   A HA   1 
ATOM   245  H HA   B LYS   A 1 11  ? 11.014 -15.404 10.856  0.28 16.94 ?  11  LYS   A HA   1 
ATOM   246  H HB2  A LYS   A 1 11  ? 10.484 -16.259 13.233  0.72 17.49 ?  11  LYS   A HB2  1 
ATOM   247  H HB2  B LYS   A 1 11  ? 10.072 -16.540 12.780  0.28 16.99 ?  11  LYS   A HB2  1 
ATOM   248  H HB3  A LYS   A 1 11  ? 9.388  -17.101 12.458  0.72 17.49 ?  11  LYS   A HB3  1 
ATOM   249  H HB3  B LYS   A 1 11  ? 9.236  -17.404 11.751  0.28 16.99 ?  11  LYS   A HB3  1 
ATOM   250  H HG2  A LYS   A 1 11  ? 10.993 -18.359 11.417  0.72 17.86 ?  11  LYS   A HG2  1 
ATOM   251  H HG2  B LYS   A 1 11  ? 11.076 -18.486 11.035  0.28 16.90 ?  11  LYS   A HG2  1 
ATOM   252  H HG3  A LYS   A 1 11  ? 12.152 -17.411 11.964  0.72 17.86 ?  11  LYS   A HG3  1 
ATOM   253  H HG3  B LYS   A 1 11  ? 12.040 -17.456 11.783  0.28 16.90 ?  11  LYS   A HG3  1 
ATOM   254  H HD2  A LYS   A 1 11  ? 11.732 -18.140 14.144  0.72 17.99 ?  11  LYS   A HD2  1 
ATOM   255  H HD2  B LYS   A 1 11  ? 11.306 -18.232 13.840  0.28 17.60 ?  11  LYS   A HD2  1 
ATOM   256  H HD3  A LYS   A 1 11  ? 10.547 -19.059 13.619  0.72 17.99 ?  11  LYS   A HD3  1 
ATOM   257  H HD3  B LYS   A 1 11  ? 10.275 -19.210 13.125  0.28 17.60 ?  11  LYS   A HD3  1 
ATOM   258  H HE2  A LYS   A 1 11  ? 12.406 -20.388 14.023  0.72 18.69 ?  11  LYS   A HE2  1 
ATOM   259  H HE2  B LYS   A 1 11  ? 12.181 -20.356 13.876  0.28 18.01 ?  11  LYS   A HE2  1 
ATOM   260  H HE3  A LYS   A 1 11  ? 12.119 -20.380 12.460  0.72 18.69 ?  11  LYS   A HE3  1 
ATOM   261  H HE3  B LYS   A 1 11  ? 12.011 -20.480 12.299  0.28 18.01 ?  11  LYS   A HE3  1 
ATOM   262  H HZ1  A LYS   A 1 11  ? 14.320 -20.079 12.814  0.72 18.91 ?  11  LYS   A HZ1  1 
ATOM   263  H HZ1  B LYS   A 1 11  ? 14.163 -19.978 12.854  0.28 18.39 ?  11  LYS   A HZ1  1 
ATOM   264  H HZ2  A LYS   A 1 11  ? 13.806 -18.844 12.256  0.72 18.91 ?  11  LYS   A HZ2  1 
ATOM   265  H HZ2  B LYS   A 1 11  ? 13.615 -18.896 12.062  0.28 18.39 ?  11  LYS   A HZ2  1 
ATOM   266  H HZ3  A LYS   A 1 11  ? 14.095 -18.935 13.673  0.72 18.91 ?  11  LYS   A HZ3  1 
ATOM   267  H HZ3  B LYS   A 1 11  ? 13.753 -18.746 13.497  0.28 18.39 ?  11  LYS   A HZ3  1 
ATOM   268  N N    A LEU   A 1 12  ? 10.734 -15.981 8.954   0.72 14.00 ?  12  LEU   A N    1 
ATOM   269  N N    B LEU   A 1 12  ? 10.717 -16.307 8.585   0.28 12.96 ?  12  LEU   A N    1 
ATOM   270  C CA   A LEU   A 1 12  ? 10.491 -16.549 7.634   0.72 14.19 ?  12  LEU   A CA   1 
ATOM   271  C CA   B LEU   A 1 12  ? 10.516 -16.865 7.250   0.28 12.67 ?  12  LEU   A CA   1 
ATOM   272  C C    A LEU   A 1 12  ? 11.068 -17.954 7.499   0.72 13.98 ?  12  LEU   A C    1 
ATOM   273  C C    B LEU   A 1 12  ? 11.129 -18.246 7.081   0.28 12.21 ?  12  LEU   A C    1 
ATOM   274  O O    A LEU   A 1 12  ? 10.431 -18.829 6.902   0.72 14.68 ?  12  LEU   A O    1 
ATOM   275  O O    B LEU   A 1 12  ? 10.505 -19.120 6.474   0.28 12.15 ?  12  LEU   A O    1 
ATOM   276  C CB   A LEU   A 1 12  ? 11.068 -15.641 6.548   0.72 15.21 ?  12  LEU   A CB   1 
ATOM   277  C CB   B LEU   A 1 12  ? 11.098 -15.941 6.177   0.28 12.94 ?  12  LEU   A CB   1 
ATOM   278  C CG   A LEU   A 1 12  ? 10.394 -14.284 6.365   0.72 16.09 ?  12  LEU   A CG   1 
ATOM   279  C CG   B LEU   A 1 12  ? 10.384 -14.611 5.922   0.28 13.60 ?  12  LEU   A CG   1 
ATOM   280  C CD1  A LEU   A 1 12  ? 11.139 -13.495 5.298   0.72 16.91 ?  12  LEU   A CD1  1 
ATOM   281  C CD1  B LEU   A 1 12  ? 11.098 -13.833 4.833   0.28 13.91 ?  12  LEU   A CD1  1 
ATOM   282  C CD2  A LEU   A 1 12  ? 8.923  -14.444 5.999   0.72 16.64 ?  12  LEU   A CD2  1 
ATOM   283  C CD2  B LEU   A 1 12  ? 8.927  -14.825 5.543   0.28 14.11 ?  12  LEU   A CD2  1 
ATOM   284  H H    A LEU   A 1 12  ? 11.449 -15.488 9.016   0.72 16.84 ?  12  LEU   A H    1 
ATOM   285  H H    B LEU   A 1 12  ? 11.511 -16.014 8.725   0.28 15.59 ?  12  LEU   A H    1 
ATOM   286  H HA   A LEU   A 1 12  ? 9.534  -16.602 7.497   0.72 17.06 ?  12  LEU   A HA   1 
ATOM   287  H HA   B LEU   A 1 12  ? 9.567  -16.955 7.092   0.28 15.24 ?  12  LEU   A HA   1 
ATOM   288  H HB2  A LEU   A 1 12  ? 12.000 -15.468 6.756   0.72 18.29 ?  12  LEU   A HB2  1 
ATOM   289  H HB2  B LEU   A 1 12  ? 12.012 -15.735 6.427   0.28 15.56 ?  12  LEU   A HB2  1 
ATOM   290  H HB3  A LEU   A 1 12  ? 11.008 -16.105 5.701   0.72 18.29 ?  12  LEU   A HB3  1 
ATOM   291  H HB3  B LEU   A 1 12  ? 11.102 -16.431 5.339   0.28 15.56 ?  12  LEU   A HB3  1 
ATOM   292  H HG   A LEU   A 1 12  ? 10.447 -13.783 7.194   0.72 19.35 ?  12  LEU   A HG   1 
ATOM   293  H HG   B LEU   A 1 12  ? 10.410 -14.082 6.732   0.28 16.36 ?  12  LEU   A HG   1 
ATOM   294  H HD11 A LEU   A 1 12  ? 10.708 -12.637 5.172   0.72 20.33 ?  12  LEU   A HD11 1 
ATOM   295  H HD11 B LEU   A 1 12  ? 10.635 -12.994 4.688   0.28 16.73 ?  12  LEU   A HD11 1 
ATOM   296  H HD12 A LEU   A 1 12  ? 12.060 -13.364 5.584   0.72 20.33 ?  12  LEU   A HD12 1 
ATOM   297  H HD12 B LEU   A 1 12  ? 12.013 -13.662 5.111   0.28 16.73 ?  12  LEU   A HD12 1 
ATOM   298  H HD13 A LEU   A 1 12  ? 11.126 -13.996 4.465   0.72 20.33 ?  12  LEU   A HD13 1 
ATOM   299  H HD13 B LEU   A 1 12  ? 11.097 -14.357 4.015   0.28 16.73 ?  12  LEU   A HD13 1 
ATOM   300  H HD21 A LEU   A 1 12  ? 8.572  -13.584 5.722   0.72 20.01 ?  12  LEU   A HD21 1 
ATOM   301  H HD21 B LEU   A 1 12  ? 8.552  -13.981 5.249   0.28 16.98 ?  12  LEU   A HD21 1 
ATOM   302  H HD22 A LEU   A 1 12  ? 8.850  -15.082 5.273   0.72 20.01 ?  12  LEU   A HD22 1 
ATOM   303  H HD22 B LEU   A 1 12  ? 8.881  -15.476 4.824   0.28 16.98 ?  12  LEU   A HD22 1 
ATOM   304  H HD23 A LEU   A 1 12  ? 8.442  -14.767 6.775   0.72 20.01 ?  12  LEU   A HD23 1 
ATOM   305  H HD23 B LEU   A 1 12  ? 8.444  -15.153 6.316   0.28 16.98 ?  12  LEU   A HD23 1 
ATOM   306  N N    A THR   A 1 13  ? 12.276 -18.172 8.020   0.72 13.58 ?  13  THR   A N    1 
ATOM   307  N N    B THR   A 1 13  ? 12.343 -18.455 7.583   0.28 12.22 ?  13  THR   A N    1 
ATOM   308  C CA   A THR   A 1 13  ? 12.960 -19.457 7.941   0.72 13.65 ?  13  THR   A CA   1 
ATOM   309  C CA   B THR   A 1 13  ? 13.026 -19.740 7.494   0.28 12.47 ?  13  THR   A CA   1 
ATOM   310  C C    A THR   A 1 13  ? 13.710 -19.679 9.248   0.72 13.65 ?  13  THR   A C    1 
ATOM   311  C C    B THR   A 1 13  ? 13.805 -19.937 8.786   0.28 12.45 ?  13  THR   A C    1 
ATOM   312  O O    A THR   A 1 13  ? 13.606 -18.898 10.199  0.72 13.65 ?  13  THR   A O    1 
ATOM   313  O O    B THR   A 1 13  ? 13.698 -19.144 9.726   0.28 12.36 ?  13  THR   A O    1 
ATOM   314  C CB   A THR   A 1 13  ? 13.940 -19.504 6.761   0.72 14.48 ?  13  THR   A CB   1 
ATOM   315  C CB   B THR   A 1 13  ? 13.979 -19.792 6.291   0.28 13.10 ?  13  THR   A CB   1 
ATOM   316  O OG1  A THR   A 1 13  ? 14.982 -18.560 6.994   0.72 14.45 ?  13  THR   A OG1  1 
ATOM   317  O OG1  B THR   A 1 13  ? 15.066 -18.886 6.511   0.28 13.43 ?  13  THR   A OG1  1 
ATOM   318  C CG2  A THR   A 1 13  ? 13.261 -19.185 5.432   0.72 15.65 ?  13  THR   A CG2  1 
ATOM   319  C CG2  B THR   A 1 13  ? 13.272 -19.409 5.004   0.28 13.44 ?  13  THR   A CG2  1 
ATOM   320  H H    A THR   A 1 13  ? 12.736 -17.561 8.426   0.72 16.33 ?  13  THR   A H    1 
ATOM   321  H H    B THR   A 1 13  ? 12.805 -17.860 7.998   0.28 14.70 ?  13  THR   A H    1 
ATOM   322  H HA   A THR   A 1 13  ? 12.312 -20.160 7.830   0.72 16.42 ?  13  THR   A HA   1 
ATOM   323  H HA   B THR   A 1 13  ? 12.378 -20.461 7.412   0.28 15.01 ?  13  THR   A HA   1 
ATOM   324  H HB   A THR   A 1 13  ? 14.326 -20.391 6.695   0.72 17.42 ?  13  THR   A HB   1 
ATOM   325  H HB   B THR   A 1 13  ? 14.321 -20.700 6.197   0.28 15.76 ?  13  THR   A HB   1 
ATOM   326  H HG1  A THR   A 1 13  ? 15.604 -18.911 7.430   0.72 17.38 ?  13  THR   A HG1  1 
ATOM   327  H HG1  B THR   A 1 13  ? 15.605 -18.924 5.869   0.28 16.15 ?  13  THR   A HG1  1 
ATOM   328  H HG21 A THR   A 1 13  ? 13.893 -19.293 4.699   0.72 18.82 ?  13  THR   A HG21 1 
ATOM   329  H HG21 B THR   A 1 13  ? 13.818 -19.664 4.243   0.28 16.17 ?  13  THR   A HG21 1 
ATOM   330  H HG22 A THR   A 1 13  ? 12.518 -19.796 5.290   0.72 18.82 ?  13  THR   A HG22 1 
ATOM   331  H HG22 B THR   A 1 13  ? 12.420 -19.865 4.947   0.28 16.17 ?  13  THR   A HG22 1 
ATOM   332  H HG23 A THR   A 1 13  ? 12.930 -18.279 5.432   0.72 18.82 ?  13  THR   A HG23 1 
ATOM   333  H HG23 B THR   A 1 13  ? 13.124 -18.452 4.983   0.28 16.17 ?  13  THR   A HG23 1 
ATOM   334  N N    A ASP   A 1 14  ? 14.501 -20.748 9.269   0.72 14.35 ?  14  ASP   A N    1 
ATOM   335  N N    B ASP   A 1 14  ? 14.625 -20.989 8.817   0.28 13.17 ?  14  ASP   A N    1 
ATOM   336  C CA   A ASP   A 1 14  ? 15.363 -21.027 10.407  0.72 15.34 ?  14  ASP   A CA   1 
ATOM   337  C CA   B ASP   A 1 14  ? 15.429 -21.254 10.003  0.28 13.69 ?  14  ASP   A CA   1 
ATOM   338  C C    A ASP   A 1 14  ? 16.175 -19.802 10.824  0.72 14.60 ?  14  ASP   A C    1 
ATOM   339  C C    B ASP   A 1 14  ? 16.311 -20.064 10.377  0.28 12.19 ?  14  ASP   A C    1 
ATOM   340  O O    A ASP   A 1 14  ? 16.360 -19.552 12.021  0.72 15.36 ?  14  ASP   A O    1 
ATOM   341  O O    B ASP   A 1 14  ? 16.620 -19.878 11.559  0.28 12.34 ?  14  ASP   A O    1 
ATOM   342  C CB   A ASP   A 1 14  ? 16.300 -22.178 10.052  0.72 18.22 ?  14  ASP   A CB   1 
ATOM   343  C CB   B ASP   A 1 14  ? 16.272 -22.512 9.783   0.28 16.19 ?  14  ASP   A CB   1 
ATOM   344  C CG   A ASP   A 1 14  ? 17.200 -22.539 11.194  0.72 22.47 ?  14  ASP   A CG   1 
ATOM   345  C CG   B ASP   A 1 14  ? 17.386 -22.645 10.792  0.28 18.92 ?  14  ASP   A CG   1 
ATOM   346  O OD1  A ASP   A 1 14  ? 16.680 -23.062 12.203  0.72 23.46 ?  14  ASP   A OD1  1 
ATOM   347  O OD1  B ASP   A 1 14  ? 17.091 -22.626 12.005  0.28 19.77 ?  14  ASP   A OD1  1 
ATOM   348  O OD2  A ASP   A 1 14  ? 18.411 -22.265 11.095  0.72 24.85 -1 14  ASP   A OD2  1 
ATOM   349  O OD2  B ASP   A 1 14  ? 18.554 -22.775 10.376  0.28 20.29 -1 14  ASP   A OD2  1 
ATOM   350  H H    A ASP   A 1 14  ? 14.563 -21.311 8.633   0.72 17.25 ?  14  ASP   A H    1 
ATOM   351  H H    B ASP   A 1 14  ? 14.739 -21.557 8.175   0.28 15.84 ?  14  ASP   A H    1 
ATOM   352  H HA   A ASP   A 1 14  ? 14.818 -21.302 11.161  0.72 18.45 ?  14  ASP   A HA   1 
ATOM   353  H HA   B ASP   A 1 14  ? 14.842 -21.438 10.753  0.28 16.46 ?  14  ASP   A HA   1 
ATOM   354  H HB2  A ASP   A 1 14  ? 15.766 -22.957 9.815   0.72 21.91 ?  14  ASP   A HB2  1 
ATOM   355  H HB2  B ASP   A 1 14  ? 15.710 -23.304 9.878   0.28 19.47 ?  14  ASP   A HB2  1 
ATOM   356  H HB3  A ASP   A 1 14  ? 16.847 -21.918 9.288   0.72 21.91 ?  14  ASP   A HB3  1 
ATOM   357  H HB3  B ASP   A 1 14  ? 16.655 -22.493 8.890   0.28 19.47 ?  14  ASP   A HB3  1 
ATOM   358  N N    A ASN   A 1 15  ? 16.664 -19.018 9.855   0.72 14.28 ?  15  ASN   A N    1 
ATOM   359  N N    B ASN   A 1 15  ? 16.717 -19.242 9.398   0.28 11.03 ?  15  ASN   A N    1 
ATOM   360  C CA   A ASN   A 1 15  ? 17.643 -17.976 10.140  0.72 14.12 ?  15  ASN   A CA   1 
ATOM   361  C CA   B ASN   A 1 15  ? 17.713 -18.203 9.640   0.28 11.18 ?  15  ASN   A CA   1 
ATOM   362  C C    A ASN   A 1 15  ? 17.275 -16.584 9.642   0.72 14.00 ?  15  ASN   A C    1 
ATOM   363  C C    B ASN   A 1 15  ? 17.357 -16.823 9.091   0.28 11.00 ?  15  ASN   A C    1 
ATOM   364  O O    A ASN   A 1 15  ? 18.037 -15.647 9.899   0.72 14.71 ?  15  ASN   A O    1 
ATOM   365  O O    B ASN   A 1 15  ? 18.154 -15.891 9.258   0.28 11.06 ?  15  ASN   A O    1 
ATOM   366  C CB   A ASN   A 1 15  ? 19.024 -18.355 9.570   0.72 14.33 ?  15  ASN   A CB   1 
ATOM   367  C CB   B ASN   A 1 15  ? 19.078 -18.628 9.070   0.28 11.18 ?  15  ASN   A CB   1 
ATOM   368  C CG   A ASN   A 1 15  ? 19.017 -18.510 8.055   0.72 14.67 ?  15  ASN   A CG   1 
ATOM   369  C CG   B ASN   A 1 15  ? 19.089 -18.645 7.555   0.28 11.64 ?  15  ASN   A CG   1 
ATOM   370  O OD1  A ASN   A 1 15  ? 18.266 -19.321 7.502   0.72 14.83 ?  15  ASN   A OD1  1 
ATOM   371  O OD1  B ASN   A 1 15  ? 18.508 -19.536 6.933   0.28 11.83 ?  15  ASN   A OD1  1 
ATOM   372  N ND2  A ASN   A 1 15  ? 19.840 -17.716 7.372   0.72 15.36 ?  15  ASN   A ND2  1 
ATOM   373  N ND2  B ASN   A 1 15  ? 19.739 -17.653 6.951   0.28 12.06 ?  15  ASN   A ND2  1 
ATOM   374  H H    A ASN   A 1 15  ? 16.444 -19.075 9.037   0.72 17.17 ?  15  ASN   A H    1 
ATOM   375  H H    B ASN   A 1 15  ? 16.426 -19.282 8.591   0.28 13.28 ?  15  ASN   A H    1 
ATOM   376  H HA   A ASN   A 1 15  ? 17.748 -17.901 11.102  0.72 16.98 ?  15  ASN   A HA   1 
ATOM   377  H HA   B ASN   A 1 15  ? 17.828 -18.116 10.595  0.28 13.45 ?  15  ASN   A HA   1 
ATOM   378  H HB2  A ASN   A 1 15  ? 19.664 -17.654 9.800   0.72 17.23 ?  15  ASN   A HB2  1 
ATOM   379  H HB2  B ASN   A 1 15  ? 19.760 -18.002 9.372   0.28 13.45 ?  15  ASN   A HB2  1 
ATOM   380  H HB3  A ASN   A 1 15  ? 19.306 -19.195 9.960   0.72 17.23 ?  15  ASN   A HB3  1 
ATOM   381  H HB3  B ASN   A 1 15  ? 19.303 -19.525 9.387   0.28 13.45 ?  15  ASN   A HB3  1 
ATOM   382  H HD21 A ASN   A 1 15  ? 19.868 -17.764 6.512   0.72 18.47 ?  15  ASN   A HD21 1 
ATOM   383  H HD21 B ASN   A 1 15  ? 19.774 -17.621 6.093   0.28 14.51 ?  15  ASN   A HD21 1 
ATOM   384  H HD22 A ASN   A 1 15  ? 20.343 -17.152 7.784   0.72 18.47 ?  15  ASN   A HD22 1 
ATOM   385  H HD22 B ASN   A 1 15  ? 20.123 -17.042 7.420   0.28 14.51 ?  15  ASN   A HD22 1 
ATOM   386  N N    A VAL   A 1 16  ? 16.147 -16.408 8.954   0.72 13.92 ?  16  VAL   A N    1 
ATOM   387  N N    B VAL   A 1 16  ? 16.202 -16.659 8.446   0.28 10.94 ?  16  VAL   A N    1 
ATOM   388  C CA   A VAL   A 1 16  ? 15.765 -15.125 8.375   0.72 13.36 ?  16  VAL   A CA   1 
ATOM   389  C CA   B VAL   A 1 16  ? 15.798 -15.389 7.848   0.28 10.87 ?  16  VAL   A CA   1 
ATOM   390  C C    A VAL   A 1 16  ? 14.481 -14.631 9.031   0.72 13.39 ?  16  VAL   A C    1 
ATOM   391  C C    B VAL   A 1 16  ? 14.539 -14.877 8.543   0.28 10.61 ?  16  VAL   A C    1 
ATOM   392  O O    A VAL   A 1 16  ? 13.482 -15.361 9.106   0.72 13.66 ?  16  VAL   A O    1 
ATOM   393  O O    B VAL   A 1 16  ? 13.541 -15.599 8.651   0.28 10.85 ?  16  VAL   A O    1 
ATOM   394  C CB   A VAL   A 1 16  ? 15.620 -15.195 6.844   0.72 13.37 ?  16  VAL   A CB   1 
ATOM   395  C CB   B VAL   A 1 16  ? 15.572 -15.522 6.330   0.28 11.15 ?  16  VAL   A CB   1 
ATOM   396  C CG1  A VAL   A 1 16  ? 15.217 -13.821 6.279   0.72 13.74 ?  16  VAL   A CG1  1 
ATOM   397  C CG1  B VAL   A 1 16  ? 15.076 -14.205 5.754   0.28 11.56 ?  16  VAL   A CG1  1 
ATOM   398  C CG2  A VAL   A 1 16  ? 16.916 -15.687 6.203   0.72 14.50 ?  16  VAL   A CG2  1 
ATOM   399  C CG2  B VAL   A 1 16  ? 16.849 -15.971 5.634   0.28 10.95 ?  16  VAL   A CG2  1 
ATOM   400  H H    A VAL   A 1 16  ? 15.576 -17.033 8.809   0.72 16.74 ?  16  VAL   A H    1 
ATOM   401  H H    B VAL   A 1 16  ? 15.631 -17.296 8.342   0.28 13.17 ?  16  VAL   A H    1 
ATOM   402  H HA   A VAL   A 1 16  ? 16.459 -14.475 8.568   0.72 16.07 ?  16  VAL   A HA   1 
ATOM   403  H HA   B VAL   A 1 16  ? 16.509 -14.745 7.989   0.28 13.08 ?  16  VAL   A HA   1 
ATOM   404  H HB   A VAL   A 1 16  ? 14.921 -15.825 6.621   0.72 16.08 ?  16  VAL   A HB   1 
ATOM   405  H HB   B VAL   A 1 16  ? 14.899 -16.204 6.171   0.28 13.42 ?  16  VAL   A HB   1 
ATOM   406  H HG11 A VAL   A 1 16  ? 15.298 -13.841 5.313   0.72 16.53 ?  16  VAL   A HG11 1 
ATOM   407  H HG11 B VAL   A 1 16  ? 15.110 -14.251 4.788   0.28 13.91 ?  16  VAL   A HG11 1 
ATOM   408  H HG12 A VAL   A 1 16  ? 14.299 -13.633 6.528   0.72 16.53 ?  16  VAL   A HG12 1 
ATOM   409  H HG12 B VAL   A 1 16  ? 14.163 -14.060 6.045   0.28 13.91 ?  16  VAL   A HG12 1 
ATOM   410  H HG13 A VAL   A 1 16  ? 15.806 -13.143 6.645   0.72 16.53 ?  16  VAL   A HG13 1 
ATOM   411  H HG13 B VAL   A 1 16  ? 15.647 -13.490 6.073   0.28 13.91 ?  16  VAL   A HG13 1 
ATOM   412  H HG21 A VAL   A 1 16  ? 16.932 -15.429 5.267   0.72 17.44 ?  16  VAL   A HG21 1 
ATOM   413  H HG21 B VAL   A 1 16  ? 16.871 -15.598 4.740   0.28 13.18 ?  16  VAL   A HG21 1 
ATOM   414  H HG22 A VAL   A 1 16  ? 17.672 -15.292 6.667   0.72 17.44 ?  16  VAL   A HG22 1 
ATOM   415  H HG22 B VAL   A 1 16  ? 17.615 -15.650 6.139   0.28 13.18 ?  16  VAL   A HG22 1 
ATOM   416  H HG23 A VAL   A 1 16  ? 16.959 -16.654 6.279   0.72 17.44 ?  16  VAL   A HG23 1 
ATOM   417  H HG23 B VAL   A 1 16  ? 16.871 -16.941 5.592   0.28 13.18 ?  16  VAL   A HG23 1 
ATOM   418  N N    A TYR   A 1 17  ? 14.513 -13.370 9.463   0.72 13.28 ?  17  TYR   A N    1 
ATOM   419  N N    B TYR   A 1 17  ? 14.581 -13.613 8.967   0.28 11.03 ?  17  TYR   A N    1 
ATOM   420  C CA   A TYR   A 1 17  ? 13.429 -12.686 10.149  0.72 13.38 ?  17  TYR   A CA   1 
ATOM   421  C CA   B TYR   A 1 17  ? 13.505 -12.946 9.685   0.28 11.85 ?  17  TYR   A CA   1 
ATOM   422  C C    A TYR   A 1 17  ? 13.169 -11.374 9.428   0.72 13.84 ?  17  TYR   A C    1 
ATOM   423  C C    B TYR   A 1 17  ? 13.224 -11.606 9.007   0.28 12.25 ?  17  TYR   A C    1 
ATOM   424  O O    A TYR   A 1 17  ? 14.087 -10.802 8.837   0.72 13.70 ?  17  TYR   A O    1 
ATOM   425  O O    B TYR   A 1 17  ? 14.093 -11.043 8.335   0.28 11.64 ?  17  TYR   A O    1 
ATOM   426  C CB   A TYR   A 1 17  ? 13.840 -12.411 11.597  0.72 13.35 ?  17  TYR   A CB   1 
ATOM   427  C CB   B TYR   A 1 17  ? 13.915 -12.706 11.147  0.28 12.28 ?  17  TYR   A CB   1 
ATOM   428  C CG   A TYR   A 1 17  ? 14.021 -13.679 12.390  0.72 14.01 ?  17  TYR   A CG   1 
ATOM   429  C CG   B TYR   A 1 17  ? 14.217 -13.966 11.945  0.28 13.34 ?  17  TYR   A CG   1 
ATOM   430  C CD1  A TYR   A 1 17  ? 15.189 -14.431 12.299  0.72 14.95 ?  17  TYR   A CD1  1 
ATOM   431  C CD1  B TYR   A 1 17  ? 15.449 -14.608 11.849  0.28 14.29 ?  17  TYR   A CD1  1 
ATOM   432  C CD2  A TYR   A 1 17  ? 13.002 -14.148 13.202  0.72 14.34 ?  17  TYR   A CD2  1 
ATOM   433  C CD2  B TYR   A 1 17  ? 13.270 -14.505 12.808  0.28 13.64 ?  17  TYR   A CD2  1 
ATOM   434  C CE1  A TYR   A 1 17  ? 15.338 -15.615 13.011  0.72 15.50 ?  17  TYR   A CE1  1 
ATOM   435  C CE1  B TYR   A 1 17  ? 15.722 -15.760 12.584  0.28 14.51 ?  17  TYR   A CE1  1 
ATOM   436  C CE2  A TYR   A 1 17  ? 13.140 -15.333 13.920  0.72 14.96 ?  17  TYR   A CE2  1 
ATOM   437  C CE2  B TYR   A 1 17  ? 13.534 -15.650 13.546  0.28 14.04 ?  17  TYR   A CE2  1 
ATOM   438  C CZ   A TYR   A 1 17  ? 14.311 -16.060 13.825  0.72 15.40 ?  17  TYR   A CZ   1 
ATOM   439  C CZ   B TYR   A 1 17  ? 14.759 -16.272 13.431  0.28 14.35 ?  17  TYR   A CZ   1 
ATOM   440  O OH   A TYR   A 1 17  ? 14.458 -17.231 14.537  0.72 16.17 ?  17  TYR   A OH   1 
ATOM   441  O OH   B TYR   A 1 17  ? 15.009 -17.410 14.169  0.28 14.62 ?  17  TYR   A OH   1 
ATOM   442  H H    A TYR   A 1 17  ? 15.200 -12.851 9.345   0.72 15.97 ?  17  TYR   A H    1 
ATOM   443  H H    B TYR   A 1 17  ? 15.262 -13.111 8.838   0.28 13.27 ?  17  TYR   A H    1 
ATOM   444  H HA   A TYR   A 1 17  ? 12.625 -13.220 10.131  0.72 16.10 ?  17  TYR   A HA   1 
ATOM   445  H HA   B TYR   A 1 17  ? 12.706 -13.503 9.668   0.28 14.26 ?  17  TYR   A HA   1 
ATOM   446  H HB2  A TYR   A 1 17  ? 14.682 -11.925 11.598  0.72 16.05 ?  17  TYR   A HB2  1 
ATOM   447  H HB2  B TYR   A 1 17  ? 14.716 -12.159 11.156  0.28 14.78 ?  17  TYR   A HB2  1 
ATOM   448  H HB3  A TYR   A 1 17  ? 13.156 -11.876 12.026  0.72 16.05 ?  17  TYR   A HB3  1 
ATOM   449  H HB3  B TYR   A 1 17  ? 13.195 -12.243 11.596  0.28 14.78 ?  17  TYR   A HB3  1 
ATOM   450  H HD1  A TYR   A 1 17  ? 15.882 -14.132 11.748  0.72 17.98 ?  17  TYR   A HD1  1 
ATOM   451  H HD1  B TYR   A 1 17  ? 16.102 -14.269 11.282  0.28 17.19 ?  17  TYR   A HD1  1 
ATOM   452  H HD2  A TYR   A 1 17  ? 12.211 -13.659 13.270  0.72 17.25 ?  17  TYR   A HD2  1 
ATOM   453  H HD2  B TYR   A 1 17  ? 12.443 -14.096 12.893  0.28 16.40 ?  17  TYR   A HD2  1 
ATOM   454  H HE1  A TYR   A 1 17  ? 16.131 -16.102 12.943  0.72 18.64 ?  17  TYR   A HE1  1 
ATOM   455  H HE1  B TYR   A 1 17  ? 16.553 -16.182 12.511  0.28 17.45 ?  17  TYR   A HE1  1 
ATOM   456  H HE2  A TYR   A 1 17  ? 12.448 -15.621 14.466  0.72 17.99 ?  17  TYR   A HE2  1 
ATOM   457  H HE2  B TYR   A 1 17  ? 12.889 -16.002 14.119  0.28 16.89 ?  17  TYR   A HE2  1 
ATOM   458  H HH   A TYR   A 1 17  ? 13.706 -17.481 14.816  0.72 19.45 ?  17  TYR   A HH   1 
ATOM   459  H HH   B TYR   A 1 17  ? 15.772 -17.722 13.979  0.28 17.58 ?  17  TYR   A HH   1 
ATOM   460  N N    A ILE   A 1 18  ? 11.927 -10.882 9.470   0.72 14.23 ?  18  ILE   A N    1 
ATOM   461  N N    B ILE   A 1 18  ? 12.008 -11.076 9.195   0.28 13.56 ?  18  ILE   A N    1 
ATOM   462  C CA   A ILE   A 1 18  ? 11.552 -9.698  8.698   0.72 14.63 ?  18  ILE   A CA   1 
ATOM   463  C CA   B ILE   A 1 18  ? 11.578 -9.864  8.496   0.28 14.43 ?  18  ILE   A CA   1 
ATOM   464  C C    A ILE   A 1 18  ? 10.579 -8.834  9.492   0.72 15.54 ?  18  ILE   A C    1 
ATOM   465  C C    B ILE   A 1 18  ? 10.674 -9.017  9.391   0.28 14.92 ?  18  ILE   A C    1 
ATOM   466  O O    A ILE   A 1 18  ? 9.707  -9.349  10.199  0.72 16.08 ?  18  ILE   A O    1 
ATOM   467  O O    B ILE   A 1 18  ? 10.007 -9.523  10.296  0.28 15.10 ?  18  ILE   A O    1 
ATOM   468  C CB   A ILE   A 1 18  ? 11.014 -10.090 7.304   0.72 14.88 ?  18  ILE   A CB   1 
ATOM   469  C CB   B ILE   A 1 18  ? 10.871 -10.208 7.160   0.28 15.04 ?  18  ILE   A CB   1 
ATOM   470  C CG1  A ILE   A 1 18  ? 10.910 -8.875  6.387   0.72 16.01 ?  18  ILE   A CG1  1 
ATOM   471  C CG1  B ILE   A 1 18  ? 10.909 -9.019  6.200   0.28 15.53 ?  18  ILE   A CG1  1 
ATOM   472  C CG2  A ILE   A 1 18  ? 9.694  -10.867 7.406   0.72 15.67 ?  18  ILE   A CG2  1 
ATOM   473  C CG2  B ILE   A 1 18  ? 9.439  -10.665 7.408   0.28 15.47 ?  18  ILE   A CG2  1 
ATOM   474  C CD1  A ILE   A 1 18  ? 10.742 -9.256  4.943   0.72 17.26 ?  18  ILE   A CD1  1 
ATOM   475  C CD1  B ILE   A 1 18  ? 10.307 -9.319  4.845   0.28 16.17 ?  18  ILE   A CD1  1 
ATOM   476  H H    A ILE   A 1 18  ? 11.280 -11.226 9.925   0.72 17.11 ?  18  ILE   A H    1 
ATOM   477  H H    B ILE   A 1 18  ? 11.422 -11.413 9.725   0.28 16.31 ?  18  ILE   A H    1 
ATOM   478  H HA   A ILE   A 1 18  ? 12.352 -9.169  8.552   0.72 17.60 ?  18  ILE   A HA   1 
ATOM   479  H HA   B ILE   A 1 18  ? 12.368 -9.344  8.284   0.28 17.36 ?  18  ILE   A HA   1 
ATOM   480  H HB   A ILE   A 1 18  ? 11.662 -10.688 6.908   0.72 17.90 ?  18  ILE   A HB   1 
ATOM   481  H HB   B ILE   A 1 18  ? 11.350 -10.941 6.746   0.28 18.09 ?  18  ILE   A HB   1 
ATOM   482  H HG12 A ILE   A 1 18  ? 10.145 -8.341  6.646   0.72 19.25 ?  18  ILE   A HG12 1 
ATOM   483  H HG12 B ILE   A 1 18  ? 10.413 -8.283  6.586   0.28 18.67 ?  18  ILE   A HG12 1 
ATOM   484  H HG13 A ILE   A 1 18  ? 11.724 -8.351  6.460   0.72 19.25 ?  18  ILE   A HG13 1 
ATOM   485  H HG13 B ILE   A 1 18  ? 11.834 -8.757  6.060   0.28 18.67 ?  18  ILE   A HG13 1 
ATOM   486  H HG21 A ILE   A 1 18  ? 9.448  -11.192 6.523   0.72 18.84 ?  18  ILE   A HG21 1 
ATOM   487  H HG21 B ILE   A 1 18  ? 9.110  -11.113 6.613   0.28 18.60 ?  18  ILE   A HG21 1 
ATOM   488  H HG22 A ILE   A 1 18  ? 9.816  -11.618 8.008   0.72 18.84 ?  18  ILE   A HG22 1 
ATOM   489  H HG22 B ILE   A 1 18  ? 9.433  -11.278 8.159   0.28 18.60 ?  18  ILE   A HG22 1 
ATOM   490  H HG23 A ILE   A 1 18  ? 9.002  -10.280 7.745   0.72 18.84 ?  18  ILE   A HG23 1 
ATOM   491  H HG23 B ILE   A 1 18  ? 8.886  -9.893  7.606   0.28 18.60 ?  18  ILE   A HG23 1 
ATOM   492  H HD11 A ILE   A 1 18  ? 10.759 -8.451  4.401   0.72 20.75 ?  18  ILE   A HD11 1 
ATOM   493  H HD11 B ILE   A 1 18  ? 10.470 -8.565  4.255   0.28 19.44 ?  18  ILE   A HD11 1 
ATOM   494  H HD12 A ILE   A 1 18  ? 11.465 -9.845  4.685   0.72 20.75 ?  18  ILE   A HD12 1 
ATOM   495  H HD12 B ILE   A 1 18  ? 10.724 -10.117 4.485   0.28 19.44 ?  18  ILE   A HD12 1 
ATOM   496  H HD13 A ILE   A 1 18  ? 9.889  -9.708  4.834   0.72 20.75 ?  18  ILE   A HD13 1 
ATOM   497  H HD13 B ILE   A 1 18  ? 9.354  -9.459  4.947   0.28 19.44 ?  18  ILE   A HD13 1 
ATOM   498  N N    A LYS   A 1 19  ? 10.732 -7.512  9.362   0.72 15.67 ?  19  LYS   A N    1 
ATOM   499  N N    B LYS   A 1 19  ? 10.636 -7.711  9.104   0.28 15.48 ?  19  LYS   A N    1 
ATOM   500  C CA   A LYS   A 1 19  ? 9.922  -6.551  10.100  0.72 16.86 ?  19  LYS   A CA   1 
ATOM   501  C CA   B LYS   A 1 19  ? 9.824  -6.754  9.851   0.28 16.04 ?  19  LYS   A CA   1 
ATOM   502  C C    A LYS   A 1 19  ? 9.706  -5.312  9.241   0.72 16.96 ?  19  LYS   A C    1 
ATOM   503  C C    B LYS   A 1 19  ? 9.667  -5.471  9.035   0.28 15.81 ?  19  LYS   A C    1 
ATOM   504  O O    A LYS   A 1 19  ? 10.606 -4.900  8.504   0.72 17.16 ?  19  LYS   A O    1 
ATOM   505  O O    B LYS   A 1 19  ? 10.590 -5.068  8.321   0.28 15.72 ?  19  LYS   A O    1 
ATOM   506  C CB   A LYS   A 1 19  ? 10.660 -6.146  11.381  0.72 17.45 ?  19  LYS   A CB   1 
ATOM   507  C CB   B LYS   A 1 19  ? 10.468 -6.437  11.212  0.28 16.81 ?  19  LYS   A CB   1 
ATOM   508  C CG   A LYS   A 1 19  ? 9.918  -5.242  12.344  0.72 18.94 ?  19  LYS   A CG   1 
ATOM   509  C CG   B LYS   A 1 19  ? 9.723  -5.401  12.051  0.28 17.58 ?  19  LYS   A CG   1 
ATOM   510  C CD   A LYS   A 1 19  ? 10.832 -4.967  13.528  0.72 20.05 ?  19  LYS   A CD   1 
ATOM   511  C CD   B LYS   A 1 19  ? 10.462 -5.103  13.352  0.28 17.96 ?  19  LYS   A CD   1 
ATOM   512  C CE   A LYS   A 1 19  ? 10.210 -4.078  14.580  0.72 20.86 ?  19  LYS   A CE   1 
ATOM   513  C CE   B LYS   A 1 19  ? 9.732  -4.064  14.197  0.28 18.14 ?  19  LYS   A CE   1 
ATOM   514  N NZ   A LYS   A 1 19  ? 11.148 -3.908  15.729  0.72 21.21 ?  19  LYS   A NZ   1 
ATOM   515  N NZ   B LYS   A 1 19  ? 10.493 -3.706  15.430  0.28 18.09 ?  19  LYS   A NZ   1 
ATOM   516  H H    A LYS   A 1 19  ? 11.321 -7.139  8.847   0.72 18.84 ?  19  LYS   A H    1 
ATOM   517  H H    B LYS   A 1 19  ? 11.078 -7.358  8.461   0.28 18.62 ?  19  LYS   A H    1 
ATOM   518  H HA   A LYS   A 1 19  ? 9.067  -6.945  10.334  0.72 20.27 ?  19  LYS   A HA   1 
ATOM   519  H HA   B LYS   A 1 19  ? 8.947  -7.134  10.010  0.28 19.28 ?  19  LYS   A HA   1 
ATOM   520  H HB2  A LYS   A 1 19  ? 10.883 -6.952  11.868  0.72 20.98 ?  19  LYS   A HB2  1 
ATOM   521  H HB2  B LYS   A 1 19  ? 10.513 -7.257  11.734  0.28 20.21 ?  19  LYS   A HB2  1 
ATOM   522  H HB3  A LYS   A 1 19  ? 11.477 -5.686  11.127  0.72 20.98 ?  19  LYS   A HB3  1 
ATOM   523  H HB3  B LYS   A 1 19  ? 11.365 -6.102  11.061  0.28 20.21 ?  19  LYS   A HB3  1 
ATOM   524  H HG2  A LYS   A 1 19  ? 9.701  -4.402  11.909  0.72 22.76 ?  19  LYS   A HG2  1 
ATOM   525  H HG2  B LYS   A 1 19  ? 9.648  -4.573  11.553  0.28 21.14 ?  19  LYS   A HG2  1 
ATOM   526  H HG3  A LYS   A 1 19  ? 9.115  -5.687  12.660  0.72 22.76 ?  19  LYS   A HG3  1 
ATOM   527  H HG3  B LYS   A 1 19  ? 8.842  -5.741  12.274  0.28 21.14 ?  19  LYS   A HG3  1 
ATOM   528  H HD2  A LYS   A 1 19  ? 11.058 -5.811  13.947  0.72 24.10 ?  19  LYS   A HD2  1 
ATOM   529  H HD2  B LYS   A 1 19  ? 10.536 -5.918  13.873  0.28 21.59 ?  19  LYS   A HD2  1 
ATOM   530  H HD3  A LYS   A 1 19  ? 11.637 -4.533  13.205  0.72 24.10 ?  19  LYS   A HD3  1 
ATOM   531  H HD3  B LYS   A 1 19  ? 11.346 -4.757  13.146  0.28 21.59 ?  19  LYS   A HD3  1 
ATOM   532  H HE2  A LYS   A 1 19  ? 10.027 -3.205  14.198  0.72 25.07 ?  19  LYS   A HE2  1 
ATOM   533  H HE2  B LYS   A 1 19  ? 9.611  -3.256  13.674  0.28 21.80 ?  19  LYS   A HE2  1 
ATOM   534  H HE3  A LYS   A 1 19  ? 9.392  -4.485  14.905  0.72 25.07 ?  19  LYS   A HE3  1 
ATOM   535  H HE3  B LYS   A 1 19  ? 8.872  -4.420  14.468  0.28 21.80 ?  19  LYS   A HE3  1 
ATOM   536  H HZ1  A LYS   A 1 19  ? 10.742 -3.472  16.389  0.72 25.49 ?  19  LYS   A HZ1  1 
ATOM   537  H HZ1  B LYS   A 1 19  ? 10.045 -3.099  15.902  0.28 21.74 ?  19  LYS   A HZ1  1 
ATOM   538  H HZ2  A LYS   A 1 19  ? 11.411 -4.704  16.026  0.72 25.49 ?  19  LYS   A HZ2  1 
ATOM   539  H HZ2  B LYS   A 1 19  ? 10.616 -4.430  15.934  0.28 21.74 ?  19  LYS   A HZ2  1 
ATOM   540  H HZ3  A LYS   A 1 19  ? 11.862 -3.445  15.472  0.72 25.49 ?  19  LYS   A HZ3  1 
ATOM   541  H HZ3  B LYS   A 1 19  ? 11.289 -3.370  15.211  0.28 21.74 ?  19  LYS   A HZ3  1 
ATOM   542  N N    A ASN   A 1 20  ? 8.512  -4.724  9.333   0.72 18.00 ?  20  ASN   A N    1 
ATOM   543  N N    B ASN   A 1 20  ? 8.489  -4.843  9.138   0.28 16.17 ?  20  ASN   A N    1 
ATOM   544  C CA   A ASN   A 1 20  ? 8.278  -3.396  8.773   0.72 19.10 ?  20  ASN   A CA   1 
ATOM   545  C CA   B ASN   A 1 20  ? 8.220  -3.537  8.525   0.28 16.42 ?  20  ASN   A CA   1 
ATOM   546  C C    A ASN   A 1 20  ? 8.917  -2.399  9.730   0.72 19.48 ?  20  ASN   A C    1 
ATOM   547  C C    B ASN   A 1 20  ? 8.763  -2.452  9.450   0.28 17.25 ?  20  ASN   A C    1 
ATOM   548  O O    A ASN   A 1 20  ? 8.423  -2.189  10.842  0.72 20.58 ?  20  ASN   A O    1 
ATOM   549  O O    B ASN   A 1 20  ? 8.123  -2.085  10.438  0.28 18.32 ?  20  ASN   A O    1 
ATOM   550  C CB   A ASN   A 1 20  ? 6.782  -3.143  8.596   0.72 20.27 ?  20  ASN   A CB   1 
ATOM   551  C CB   B ASN   A 1 20  ? 6.718  -3.362  8.294   0.28 16.16 ?  20  ASN   A CB   1 
ATOM   552  C CG   A ASN   A 1 20  ? 6.460  -1.704  8.207   0.72 21.85 ?  20  ASN   A CG   1 
ATOM   553  C CG   B ASN   A 1 20  ? 6.333  -1.952  7.827   0.28 16.39 ?  20  ASN   A CG   1 
ATOM   554  O OD1  A ASN   A 1 20  ? 5.542  -1.101  8.761   0.72 23.61 ?  20  ASN   A OD1  1 
ATOM   555  O OD1  B ASN   A 1 20  ? 5.198  -1.504  8.039   0.28 16.57 ?  20  ASN   A OD1  1 
ATOM   556  N ND2  A ASN   A 1 20  ? 7.209  -1.153  7.254   0.72 22.68 ?  20  ASN   A ND2  1 
ATOM   557  N ND2  B ASN   A 1 20  ? 7.265  -1.257  7.182   0.28 17.10 ?  20  ASN   A ND2  1 
ATOM   558  H H    A ASN   A 1 20  ? 7.822  -5.075  9.716   0.72 21.64 ?  20  ASN   A H    1 
ATOM   559  H H    B ASN   A 1 20  ? 7.811  -5.176  9.551   0.28 19.44 ?  20  ASN   A H    1 
ATOM   560  H HA   A ASN   A 1 20  ? 8.711  -3.329  7.910   0.72 22.96 ?  20  ASN   A HA   1 
ATOM   561  H HA   B ASN   A 1 20  ? 8.676  -3.480  7.671   0.28 19.74 ?  20  ASN   A HA   1 
ATOM   562  H HB2  A ASN   A 1 20  ? 6.446  -3.728  7.895   0.72 24.36 ?  20  ASN   A HB2  1 
ATOM   563  H HB2  B ASN   A 1 20  ? 6.426  -3.982  7.611   0.28 19.43 ?  20  ASN   A HB2  1 
ATOM   564  H HB3  A ASN   A 1 20  ? 6.328  -3.337  9.430   0.72 24.36 ?  20  ASN   A HB3  1 
ATOM   565  H HB3  B ASN   A 1 20  ? 6.246  -3.545  9.122   0.28 19.43 ?  20  ASN   A HB3  1 
ATOM   566  H HD21 A ASN   A 1 20  ? 7.059  -0.346  7.002   0.72 27.25 ?  20  ASN   A HD21 1 
ATOM   567  H HD21 B ASN   A 1 20  ? 7.089  -0.464  6.906   0.28 20.56 ?  20  ASN   A HD21 1 
ATOM   568  H HD22 A ASN   A 1 20  ? 7.847  -1.605  6.892   0.72 27.25 ?  20  ASN   A HD22 1 
ATOM   569  H HD22 B ASN   A 1 20  ? 8.043  -1.596  7.046   0.28 20.56 ?  20  ASN   A HD22 1 
ATOM   570  N N    A ALA   A 1 21  ? 10.050 -1.827  9.331   0.72 19.42 ?  21  ALA   A N    1 
ATOM   571  N N    B ALA   A 1 21  ? 9.942  -1.921  9.126   0.28 17.30 ?  21  ALA   A N    1 
ATOM   572  C CA   A ALA   A 1 21  ? 10.764 -0.941  10.236  0.72 19.42 ?  21  ALA   A CA   1 
ATOM   573  C CA   B ALA   A 1 21  ? 10.573 -0.925  9.984   0.28 17.47 ?  21  ALA   A CA   1 
ATOM   574  C C    A ALA   A 1 21  ? 11.703 -0.048  9.449   0.72 18.93 ?  21  ALA   A C    1 
ATOM   575  C C    B ALA   A 1 21  ? 11.651 -0.177  9.212   0.28 16.67 ?  21  ALA   A C    1 
ATOM   576  O O    A ALA   A 1 21  ? 12.158 -0.404  8.358   0.72 19.06 ?  21  ALA   A O    1 
ATOM   577  O O    B ALA   A 1 21  ? 12.123 -0.629  8.165   0.28 16.40 ?  21  ALA   A O    1 
ATOM   578  C CB   A ALA   A 1 21  ? 11.554 -1.735  11.278  0.72 20.10 ?  21  ALA   A CB   1 
ATOM   579  C CB   B ALA   A 1 21  ? 11.172 -1.568  11.240  0.28 18.15 ?  21  ALA   A CB   1 
ATOM   580  H H    A ALA   A 1 21  ? 10.419 -1.937  8.561   0.72 23.35 ?  21  ALA   A H    1 
ATOM   581  H H    B ALA   A 1 21  ? 10.385 -2.118  8.417   0.28 20.80 ?  21  ALA   A H    1 
ATOM   582  H HA   A ALA   A 1 21  ? 10.120 -0.380  10.701  0.72 23.35 ?  21  ALA   A HA   1 
ATOM   583  H HA   B ALA   A 1 21  ? 9.901  -0.289  10.267  0.28 21.01 ?  21  ALA   A HA   1 
ATOM   584  H HB1  A ALA   A 1 21  ? 11.933 -1.114  11.914  0.72 24.16 ?  21  ALA   A HB1  1 
ATOM   585  H HB1  B ALA   A 1 21  ? 11.581 -0.877  11.782  0.28 21.82 ?  21  ALA   A HB1  1 
ATOM   586  H HB2  A ALA   A 1 21  ? 10.945 -2.343  11.735  0.72 24.16 ?  21  ALA   A HB2  1 
ATOM   587  H HB2  B ALA   A 1 21  ? 10.465 -2.007  11.741  0.28 21.82 ?  21  ALA   A HB2  1 
ATOM   588  H HB3  A ALA   A 1 21  ? 12.248 -2.238  10.833  0.72 24.16 ?  21  ALA   A HB3  1 
ATOM   589  H HB3  B ALA   A 1 21  ? 11.841 -2.220  10.975  0.28 21.82 ?  21  ALA   A HB3  1 
ATOM   590  N N    A ASP   A 1 22  ? 11.971 1.121   10.026  0.72 19.04 ?  22  ASP   A N    1 
ATOM   591  N N    B ASP   A 1 22  ? 12.022 0.986   9.751   0.28 16.72 ?  22  ASP   A N    1 
ATOM   592  C CA   A ASP   A 1 22  ? 13.013 2.023   9.552   0.72 18.57 ?  22  ASP   A CA   1 
ATOM   593  C CA   B ASP   A 1 22  ? 13.160 1.756   9.261   0.28 16.82 ?  22  ASP   A CA   1 
ATOM   594  C C    A ASP   A 1 22  ? 14.341 1.529   10.111  0.72 17.12 ?  22  ASP   A C    1 
ATOM   595  C C    B ASP   A 1 22  ? 14.434 1.196   9.886   0.28 15.80 ?  22  ASP   A C    1 
ATOM   596  O O    A ASP   A 1 22  ? 14.546 1.538   11.328  0.72 17.85 ?  22  ASP   A O    1 
ATOM   597  O O    B ASP   A 1 22  ? 14.558 1.144   11.114  0.28 15.89 ?  22  ASP   A O    1 
ATOM   598  C CB   A ASP   A 1 22  ? 12.703 3.426   10.063  0.72 20.85 ?  22  ASP   A CB   1 
ATOM   599  C CB   B ASP   A 1 22  ? 12.983 3.226   9.647   0.28 18.18 ?  22  ASP   A CB   1 
ATOM   600  C CG   A ASP   A 1 22  ? 13.691 4.466   9.571   0.72 22.51 ?  22  ASP   A CG   1 
ATOM   601  C CG   B ASP   A 1 22  ? 14.113 4.115   9.153   0.28 19.44 ?  22  ASP   A CG   1 
ATOM   602  O OD1  A ASP   A 1 22  ? 14.816 4.115   9.172   0.72 22.18 ?  22  ASP   A OD1  1 
ATOM   603  O OD1  B ASP   A 1 22  ? 15.067 3.594   8.542   0.28 19.53 ?  22  ASP   A OD1  1 
ATOM   604  O OD2  A ASP   A 1 22  ? 13.339 5.660   9.593   0.72 24.25 -1 22  ASP   A OD2  1 
ATOM   605  O OD2  B ASP   A 1 22  ? 14.046 5.343   9.381   0.28 20.51 -1 22  ASP   A OD2  1 
ATOM   606  H H    A ASP   A 1 22  ? 11.534 1.423   10.709  0.72 22.88 ?  22  ASP   A H    1 
ATOM   607  H H    B ASP   A 1 22  ? 11.609 1.357   10.411  0.28 20.10 ?  22  ASP   A H    1 
ATOM   608  H HA   A ASP   A 1 22  ? 13.043 2.020   8.583   0.72 22.32 ?  22  ASP   A HA   1 
ATOM   609  H HA   B ASP   A 1 22  ? 13.215 1.681   8.293   0.28 20.23 ?  22  ASP   A HA   1 
ATOM   610  H HB2  A ASP   A 1 22  ? 11.812 3.678   9.767   0.72 25.05 ?  22  ASP   A HB2  1 
ATOM   611  H HB2  B ASP   A 1 22  ? 12.155 3.555   9.272   0.28 21.85 ?  22  ASP   A HB2  1 
ATOM   612  H HB3  A ASP   A 1 22  ? 12.729 3.413   11.036  0.72 25.05 ?  22  ASP   A HB3  1 
ATOM   613  H HB3  B ASP   A 1 22  ? 12.967 3.296   10.612  0.28 21.85 ?  22  ASP   A HB3  1 
ATOM   614  N N    A ILE   A 1 23  ? 15.244 1.094   9.224   0.72 16.46 ?  23  ILE   A N    1 
ATOM   615  N N    B ILE   A 1 23  ? 15.379 0.771   9.042   0.28 15.18 ?  23  ILE   A N    1 
ATOM   616  C CA   A ILE   A 1 23  ? 16.501 0.488   9.658   0.72 15.99 ?  23  ILE   A CA   1 
ATOM   617  C CA   B ILE   A 1 23  ? 16.626 0.197   9.535   0.28 14.95 ?  23  ILE   A CA   1 
ATOM   618  C C    A ILE   A 1 23  ? 17.303 1.441   10.534  0.72 16.14 ?  23  ILE   A C    1 
ATOM   619  C C    B ILE   A 1 23  ? 17.363 1.185   10.426  0.28 15.60 ?  23  ILE   A C    1 
ATOM   620  O O    A ILE   A 1 23  ? 18.019 0.999   11.442  0.72 16.84 ?  23  ILE   A O    1 
ATOM   621  O O    B ILE   A 1 23  ? 18.073 0.782   11.356  0.28 15.53 ?  23  ILE   A O    1 
ATOM   622  C CB   A ILE   A 1 23  ? 17.305 -0.027  8.442   0.72 15.67 ?  23  ILE   A CB   1 
ATOM   623  C CB   B ILE   A 1 23  ? 17.506 -0.310  8.369   0.28 14.21 ?  23  ILE   A CB   1 
ATOM   624  C CG1  A ILE   A 1 23  ? 18.482 -0.896  8.904   0.72 15.36 ?  23  ILE   A CG1  1 
ATOM   625  C CG1  B ILE   A 1 23  ? 18.555 -1.297  8.891   0.28 13.81 ?  23  ILE   A CG1  1 
ATOM   626  C CG2  A ILE   A 1 23  ? 17.757 1.132   7.556   0.72 15.67 ?  23  ILE   A CG2  1 
ATOM   627  C CG2  B ILE   A 1 23  ? 18.185 0.849   7.641   0.28 13.98 ?  23  ILE   A CG2  1 
ATOM   628  C CD1  A ILE   A 1 23  ? 19.168 -1.649  7.780   0.72 15.87 ?  23  ILE   A CD1  1 
ATOM   629  C CD1  B ILE   A 1 23  ? 19.444 -1.890  7.811   0.28 13.82 ?  23  ILE   A CD1  1 
ATOM   630  H H    A ILE   A 1 23  ? 15.140 1.137   8.379   0.72 19.79 ?  23  ILE   A H    1 
ATOM   631  H H    B ILE   A 1 23  ? 15.317 0.796   8.198   0.28 18.26 ?  23  ILE   A H    1 
ATOM   632  H HA   A ILE   A 1 23  ? 16.290 -0.282  10.206  0.72 19.22 ?  23  ILE   A HA   1 
ATOM   633  H HA   B ILE   A 1 23  ? 16.406 -0.573  10.077  0.28 17.98 ?  23  ILE   A HA   1 
ATOM   634  H HB   A ILE   A 1 23  ? 16.711 -0.587  7.918   0.72 18.84 ?  23  ILE   A HB   1 
ATOM   635  H HB   B ILE   A 1 23  ? 16.941 -0.779  7.735   0.28 17.09 ?  23  ILE   A HB   1 
ATOM   636  H HG12 A ILE   A 1 23  ? 19.142 -0.327  9.327   0.72 18.47 ?  23  ILE   A HG12 1 
ATOM   637  H HG12 B ILE   A 1 23  ? 19.132 -0.843  9.524   0.28 16.61 ?  23  ILE   A HG12 1 
ATOM   638  H HG13 A ILE   A 1 23  ? 18.154 -1.550  9.542   0.72 18.47 ?  23  ILE   A HG13 1 
ATOM   639  H HG13 B ILE   A 1 23  ? 18.103 -2.036  9.331   0.28 16.61 ?  23  ILE   A HG13 1 
ATOM   640  H HG21 A ILE   A 1 23  ? 18.142 0.773   6.742   0.72 18.84 ?  23  ILE   A HG21 1 
ATOM   641  H HG21 B ILE   A 1 23  ? 18.525 0.530   6.787   0.28 16.82 ?  23  ILE   A HG21 1 
ATOM   642  H HG22 A ILE   A 1 23  ? 16.985 1.682   7.339   0.72 18.84 ?  23  ILE   A HG22 1 
ATOM   643  H HG22 B ILE   A 1 23  ? 17.536 1.551   7.495   0.28 16.82 ?  23  ILE   A HG22 1 
ATOM   644  H HG23 A ILE   A 1 23  ? 18.414 1.659   8.032   0.72 18.84 ?  23  ILE   A HG23 1 
ATOM   645  H HG23 B ILE   A 1 23  ? 18.918 1.180   8.182   0.28 16.82 ?  23  ILE   A HG23 1 
ATOM   646  H HD11 A ILE   A 1 23  ? 19.862 -2.211  8.158   0.72 19.08 ?  23  ILE   A HD11 1 
ATOM   647  H HD11 B ILE   A 1 23  ? 19.996 -2.588  8.201   0.28 16.63 ?  23  ILE   A HD11 1 
ATOM   648  H HD12 A ILE   A 1 23  ? 18.511 -2.196  7.321   0.72 19.08 ?  23  ILE   A HD12 1 
ATOM   649  H HD12 B ILE   A 1 23  ? 18.885 -2.265  7.113   0.28 16.63 ?  23  ILE   A HD12 1 
ATOM   650  H HD13 A ILE   A 1 23  ? 19.556 -1.010  7.164   0.72 19.08 ?  23  ILE   A HD13 1 
ATOM   651  H HD13 B ILE   A 1 23  ? 20.007 -1.191  7.445   0.28 16.63 ?  23  ILE   A HD13 1 
ATOM   652  N N    A VAL   A 1 24  ? 17.182 2.751   10.303  0.72 16.81 ?  24  VAL   A N    1 
ATOM   653  N N    B VAL   A 1 24  ? 17.194 2.485   10.176  0.28 16.72 ?  24  VAL   A N    1 
ATOM   654  C CA   A VAL   A 1 24  ? 17.870 3.720   11.154  0.72 18.07 ?  24  VAL   A CA   1 
ATOM   655  C CA   B VAL   A 1 24  ? 17.858 3.495   10.994  0.28 17.90 ?  24  VAL   A CA   1 
ATOM   656  C C    A VAL   A 1 24  ? 17.344 3.636   12.580  0.72 18.71 ?  24  VAL   A C    1 
ATOM   657  C C    B VAL   A 1 24  ? 17.312 3.470   12.416  0.28 18.94 ?  24  VAL   A C    1 
ATOM   658  O O    A VAL   A 1 24  ? 18.113 3.558   13.546  0.72 19.14 ?  24  VAL   A O    1 
ATOM   659  O O    B VAL   A 1 24  ? 18.072 3.474   13.391  0.28 19.17 ?  24  VAL   A O    1 
ATOM   660  C CB   A VAL   A 1 24  ? 17.724 5.141   10.579  0.72 18.82 ?  24  VAL   A CB   1 
ATOM   661  C CB   B VAL   A 1 24  ? 17.715 4.884   10.348  0.28 18.25 ?  24  VAL   A CB   1 
ATOM   662  C CG1  A VAL   A 1 24  ? 18.176 6.188   11.596  0.72 19.28 ?  24  VAL   A CG1  1 
ATOM   663  C CG1  B VAL   A 1 24  ? 18.397 5.940   11.201  0.28 18.82 ?  24  VAL   A CG1  1 
ATOM   664  C CG2  A VAL   A 1 24  ? 18.506 5.273   9.283   0.72 19.73 ?  24  VAL   A CG2  1 
ATOM   665  C CG2  B VAL   A 1 24  ? 18.283 4.869   8.938   0.28 18.08 ?  24  VAL   A CG2  1 
ATOM   666  H H    A VAL   A 1 24  ? 16.712 3.099   9.674   0.72 20.21 ?  24  VAL   A H    1 
ATOM   667  H H    B VAL   A 1 24  ? 16.703 2.804   9.548   0.28 20.10 ?  24  VAL   A H    1 
ATOM   668  H HA   A VAL   A 1 24  ? 18.815 3.507   11.174  0.72 21.73 ?  24  VAL   A HA   1 
ATOM   669  H HA   B VAL   A 1 24  ? 18.802 3.287   11.040  0.28 21.51 ?  24  VAL   A HA   1 
ATOM   670  H HB   A VAL   A 1 24  ? 16.791 5.306   10.376  0.72 22.63 ?  24  VAL   A HB   1 
ATOM   671  H HB   B VAL   A 1 24  ? 16.774 5.110   10.289  0.28 21.94 ?  24  VAL   A HB   1 
ATOM   672  H HG11 A VAL   A 1 24  ? 18.351 7.021   11.131  0.72 23.17 ?  24  VAL   A HG11 1 
ATOM   673  H HG11 B VAL   A 1 24  ? 18.460 6.761   10.692  0.28 22.62 ?  24  VAL   A HG11 1 
ATOM   674  H HG12 A VAL   A 1 24  ? 17.473 6.316   12.250  0.72 23.17 ?  24  VAL   A HG12 1 
ATOM   675  H HG12 B VAL   A 1 24  ? 17.871 6.087   12.003  0.28 22.62 ?  24  VAL   A HG12 1 
ATOM   676  H HG13 A VAL   A 1 24  ? 18.986 5.876   12.029  0.72 23.17 ?  24  VAL   A HG13 1 
ATOM   677  H HG13 B VAL   A 1 24  ? 19.284 5.627   11.437  0.28 22.62 ?  24  VAL   A HG13 1 
ATOM   678  H HG21 A VAL   A 1 24  ? 18.312 6.134   8.878   0.72 23.71 ?  24  VAL   A HG21 1 
ATOM   679  H HG21 B VAL   A 1 24  ? 18.328 5.779   8.608   0.28 21.74 ?  24  VAL   A HG21 1 
ATOM   680  H HG22 A VAL   A 1 24  ? 19.456 5.209   9.477   0.72 23.71 ?  24  VAL   A HG22 1 
ATOM   681  H HG22 B VAL   A 1 24  ? 19.172 4.482   8.962   0.28 21.74 ?  24  VAL   A HG22 1 
ATOM   682  H HG23 A VAL   A 1 24  ? 18.245 4.559   8.678   0.72 23.71 ?  24  VAL   A HG23 1 
ATOM   683  H HG23 B VAL   A 1 24  ? 17.705 4.337   8.370   0.28 21.74 ?  24  VAL   A HG23 1 
ATOM   684  N N    A GLU   A 1 25  ? 16.018 3.660   12.732  0.72 19.80 ?  25  GLU   A N    1 
ATOM   685  N N    B GLU   A 1 25  ? 15.984 3.443   12.556  0.28 20.10 ?  25  GLU   A N    1 
ATOM   686  C CA   A GLU   A 1 25  ? 15.425 3.578   14.062  0.72 21.62 ?  25  GLU   A CA   1 
ATOM   687  C CA   B GLU   A 1 25  ? 15.390 3.396   13.888  0.28 21.52 ?  25  GLU   A CA   1 
ATOM   688  C C    A GLU   A 1 25  ? 15.668 2.212   14.691  0.72 20.47 ?  25  GLU   A C    1 
ATOM   689  C C    B GLU   A 1 25  ? 15.624 2.052   14.562  0.28 20.89 ?  25  GLU   A C    1 
ATOM   690  O O    A GLU   A 1 25  ? 15.919 2.119   15.898  0.72 21.12 ?  25  GLU   A O    1 
ATOM   691  O O    B GLU   A 1 25  ? 15.779 1.994   15.787  0.28 21.32 ?  25  GLU   A O    1 
ATOM   692  C CB   A GLU   A 1 25  ? 13.933 3.915   13.995  0.72 24.66 ?  25  GLU   A CB   1 
ATOM   693  C CB   B GLU   A 1 25  ? 13.894 3.713   13.818  0.28 23.66 ?  25  GLU   A CB   1 
ATOM   694  C CG   A GLU   A 1 25  ? 13.658 5.360   13.593  0.72 28.46 ?  25  GLU   A CG   1 
ATOM   695  C CG   B GLU   A 1 25  ? 13.598 5.171   13.494  0.28 26.06 ?  25  GLU   A CG   1 
ATOM   696  C CD   A GLU   A 1 25  ? 14.393 6.364   14.463  0.72 31.88 ?  25  GLU   A CD   1 
ATOM   697  C CD   B GLU   A 1 25  ? 14.404 6.141   14.336  0.28 28.11 ?  25  GLU   A CD   1 
ATOM   698  O OE1  A GLU   A 1 25  ? 14.455 6.159   15.695  0.72 32.88 ?  25  GLU   A OE1  1 
ATOM   699  O OE1  B GLU   A 1 25  ? 14.510 5.922   15.562  0.28 28.84 ?  25  GLU   A OE1  1 
ATOM   700  O OE2  A GLU   A 1 25  ? 14.927 7.348   13.911  0.72 33.50 -1 25  GLU   A OE2  1 
ATOM   701  O OE2  B GLU   A 1 25  ? 14.945 7.113   13.769  0.28 28.93 -1 25  GLU   A OE2  1 
ATOM   702  H H    A GLU   A 1 25  ? 15.451 3.730   12.091  0.72 23.80 ?  25  GLU   A H    1 
ATOM   703  H H    B GLU   A 1 25  ? 15.418 3.454   11.908  0.28 24.16 ?  25  GLU   A H    1 
ATOM   704  H HA   A GLU   A 1 25  ? 15.849 4.231   14.638  0.72 25.98 ?  25  GLU   A HA   1 
ATOM   705  H HA   B GLU   A 1 25  ? 15.821 4.063   14.440  0.28 25.86 ?  25  GLU   A HA   1 
ATOM   706  H HB2  A GLU   A 1 25  ? 13.505 3.343   13.337  0.72 29.64 ?  25  GLU   A HB2  1 
ATOM   707  H HB2  B GLU   A 1 25  ? 13.488 3.166   13.122  0.28 28.43 ?  25  GLU   A HB2  1 
ATOM   708  H HB3  A GLU   A 1 25  ? 13.530 3.772   14.866  0.72 29.64 ?  25  GLU   A HB3  1 
ATOM   709  H HB3  B GLU   A 1 25  ? 13.486 3.506   14.673  0.28 28.43 ?  25  GLU   A HB3  1 
ATOM   710  H HG2  A GLU   A 1 25  ? 13.952 5.494   12.680  0.72 34.19 ?  25  GLU   A HG2  1 
ATOM   711  H HG2  B GLU   A 1 25  ? 13.802 5.333   12.562  0.28 31.31 ?  25  GLU   A HG2  1 
ATOM   712  H HG3  A GLU   A 1 25  ? 12.705 5.533   13.664  0.72 34.19 ?  25  GLU   A HG3  1 
ATOM   713  H HG3  B GLU   A 1 25  ? 12.665 5.351   13.674  0.28 31.31 ?  25  GLU   A HG3  1 
ATOM   714  N N    A GLU   A 1 26  ? 15.616 1.142   13.891  0.72 19.86 ?  26  GLU   A N    1 
ATOM   715  N N    B GLU   A 1 26  ? 15.651 0.967   13.788  0.28 20.09 ?  26  GLU   A N    1 
ATOM   716  C CA   A GLU   A 1 26  ? 15.938 -0.185  14.412  0.72 20.02 ?  26  GLU   A CA   1 
ATOM   717  C CA   B GLU   A 1 26  ? 15.963 -0.337  14.363  0.28 19.53 ?  26  GLU   A CA   1 
ATOM   718  C C    A GLU   A 1 26  ? 17.359 -0.216  14.960  0.72 18.95 ?  26  GLU   A C    1 
ATOM   719  C C    B GLU   A 1 26  ? 17.399 -0.398  14.860  0.28 18.64 ?  26  GLU   A C    1 
ATOM   720  O O    A GLU   A 1 26  ? 17.601 -0.688  16.076  0.72 18.67 ?  26  GLU   A O    1 
ATOM   721  O O    B GLU   A 1 26  ? 17.681 -1.063  15.863  0.28 18.53 ?  26  GLU   A O    1 
ATOM   722  C CB   A GLU   A 1 26  ? 15.790 -1.241  13.311  0.72 22.01 ?  26  GLU   A CB   1 
ATOM   723  C CB   B GLU   A 1 26  ? 15.722 -1.436  13.330  0.28 20.01 ?  26  GLU   A CB   1 
ATOM   724  C CG   A GLU   A 1 26  ? 14.415 -1.864  13.162  0.72 24.67 ?  26  GLU   A CG   1 
ATOM   725  C CG   B GLU   A 1 26  ? 14.258 -1.752  13.100  0.28 20.95 ?  26  GLU   A CG   1 
ATOM   726  C CD   A GLU   A 1 26  ? 13.975 -2.662  14.386  0.72 25.82 ?  26  GLU   A CD   1 
ATOM   727  C CD   B GLU   A 1 26  ? 13.574 -2.278  14.340  0.28 21.05 ?  26  GLU   A CD   1 
ATOM   728  O OE1  A GLU   A 1 26  ? 14.412 -3.821  14.587  0.72 25.84 ?  26  GLU   A OE1  1 
ATOM   729  O OE1  B GLU   A 1 26  ? 14.248 -2.939  15.155  0.28 20.91 ?  26  GLU   A OE1  1 
ATOM   730  O OE2  A GLU   A 1 26  ? 13.176 -2.114  15.158  0.72 26.51 -1 26  GLU   A OE2  1 
ATOM   731  O OE2  B GLU   A 1 26  ? 12.367 -2.010  14.502  0.28 21.04 -1 26  GLU   A OE2  1 
ATOM   732  H H    A GLU   A 1 26  ? 15.401 1.164   13.057  0.72 23.87 ?  26  GLU   A H    1 
ATOM   733  H H    B GLU   A 1 26  ? 15.494 0.962   12.944  0.28 24.15 ?  26  GLU   A H    1 
ATOM   734  H HA   A GLU   A 1 26  ? 15.324 -0.401  15.129  0.72 24.06 ?  26  GLU   A HA   1 
ATOM   735  H HA   B GLU   A 1 26  ? 15.379 -0.494  15.118  0.28 23.47 ?  26  GLU   A HA   1 
ATOM   736  H HB2  A GLU   A 1 26  ? 16.017 -0.828  12.461  0.72 26.45 ?  26  GLU   A HB2  1 
ATOM   737  H HB2  B GLU   A 1 26  ? 16.100 -1.153  12.480  0.28 24.05 ?  26  GLU   A HB2  1 
ATOM   738  H HB3  A GLU   A 1 26  ? 16.415 -1.957  13.497  0.72 26.45 ?  26  GLU   A HB3  1 
ATOM   739  H HB3  B GLU   A 1 26  ? 16.162 -2.247  13.629  0.28 24.05 ?  26  GLU   A HB3  1 
ATOM   740  H HG2  A GLU   A 1 26  ? 13.773 -1.151  13.014  0.72 29.64 ?  26  GLU   A HG2  1 
ATOM   741  H HG2  B GLU   A 1 26  ? 13.796 -0.943  12.844  0.28 25.18 ?  26  GLU   A HG2  1 
ATOM   742  H HG3  A GLU   A 1 26  ? 14.422 -2.465  12.401  0.72 29.64 ?  26  GLU   A HG3  1 
ATOM   743  H HG3  B GLU   A 1 26  ? 14.186 -2.421  12.403  0.28 25.18 ?  26  GLU   A HG3  1 
ATOM   744  N N    . ALA   A 1 27  ? 18.317 0.287   14.180  1.00 17.84 ?  27  ALA   A N    1 
ATOM   745  C CA   . ALA   A 1 27  ? 19.707 0.274   14.619  1.00 18.19 ?  27  ALA   A CA   1 
ATOM   746  C C    . ALA   A 1 27  ? 19.889 1.077   15.903  1.00 20.20 ?  27  ALA   A C    1 
ATOM   747  O O    . ALA   A 1 27  ? 20.564 0.625   16.834  1.00 19.97 ?  27  ALA   A O    1 
ATOM   748  C CB   . ALA   A 1 27  ? 20.621 0.801   13.509  1.00 17.57 ?  27  ALA   A CB   1 
ATOM   749  H H    A ALA   A 1 27  ? 18.187 0.643   13.407  0.72 21.45 ?  27  ALA   A H    1 
ATOM   750  H H    B ALA   A 1 27  ? 18.161 0.761   13.478  0.28 21.45 ?  27  ALA   A H    1 
ATOM   751  H HA   . ALA   A 1 27  ? 19.964 -0.639  14.803  1.00 21.87 ?  27  ALA   A HA   1 
ATOM   752  H HB1  . ALA   A 1 27  ? 21.541 0.783   13.820  1.00 21.12 ?  27  ALA   A HB1  1 
ATOM   753  H HB2  . ALA   A 1 27  ? 20.527 0.235   12.726  1.00 21.12 ?  27  ALA   A HB2  1 
ATOM   754  H HB3  . ALA   A 1 27  ? 20.366 1.712   13.290  1.00 21.12 ?  27  ALA   A HB3  1 
ATOM   755  N N    A LYS   A 1 28  ? 19.280 2.262   15.982  0.72 22.24 ?  28  LYS   A N    1 
ATOM   756  N N    B LYS   A 1 28  ? 19.286 2.267   15.975  0.28 22.85 ?  28  LYS   A N    1 
ATOM   757  C CA   A LYS   A 1 28  ? 19.431 3.079   17.183  0.72 25.07 ?  28  LYS   A CA   1 
ATOM   758  C CA   B LYS   A 1 28  ? 19.421 3.093   17.171  0.28 25.90 ?  28  LYS   A CA   1 
ATOM   759  C C    A LYS   A 1 28  ? 18.864 2.389   18.417  0.72 26.28 ?  28  LYS   A C    1 
ATOM   760  C C    B LYS   A 1 28  ? 18.835 2.409   18.399  0.28 27.25 ?  28  LYS   A C    1 
ATOM   761  O O    A LYS   A 1 28  ? 19.361 2.607   19.528  0.72 27.57 ?  28  LYS   A O    1 
ATOM   762  O O    B LYS   A 1 28  ? 19.360 2.570   19.507  0.28 27.69 ?  28  LYS   A O    1 
ATOM   763  C CB   A LYS   A 1 28  ? 18.798 4.457   16.979  0.72 27.46 ?  28  LYS   A CB   1 
ATOM   764  C CB   B LYS   A 1 28  ? 18.765 4.458   16.951  0.28 27.77 ?  28  LYS   A CB   1 
ATOM   765  C CG   A LYS   A 1 28  ? 19.623 5.353   16.073  0.72 29.74 ?  28  LYS   A CG   1 
ATOM   766  C CG   B LYS   A 1 28  ? 19.549 5.370   16.020  0.28 29.55 ?  28  LYS   A CG   1 
ATOM   767  C CD   A LYS   A 1 28  ? 19.179 6.801   16.127  0.72 32.15 ?  28  LYS   A CD   1 
ATOM   768  C CD   B LYS   A 1 28  ? 19.076 6.815   16.097  0.28 31.23 ?  28  LYS   A CD   1 
ATOM   769  C CE   A LYS   A 1 28  ? 17.871 7.003   15.397  0.72 34.07 ?  28  LYS   A CE   1 
ATOM   770  C CE   B LYS   A 1 28  ? 17.768 7.026   15.356  0.28 32.57 ?  28  LYS   A CE   1 
ATOM   771  N NZ   A LYS   A 1 28  ? 17.538 8.448   15.280  0.72 35.28 ?  28  LYS   A NZ   1 
ATOM   772  N NZ   B LYS   A 1 28  ? 17.451 8.476   15.209  0.28 33.36 ?  28  LYS   A NZ   1 
ATOM   773  H H    A LYS   A 1 28  ? 18.788 2.608   15.371  0.72 26.72 ?  28  LYS   A H    1 
ATOM   774  H H    B LYS   A 1 28  ? 18.802 2.611   15.357  0.28 27.46 ?  28  LYS   A H    1 
ATOM   775  H HA   A LYS   A 1 28  ? 20.373 3.217   17.347  0.72 30.12 ?  28  LYS   A HA   1 
ATOM   776  H HA   B LYS   A 1 28  ? 20.361 3.245   17.344  0.28 31.11 ?  28  LYS   A HA   1 
ATOM   777  H HB2  A LYS   A 1 28  ? 17.923 4.350   16.577  0.72 32.99 ?  28  LYS   A HB2  1 
ATOM   778  H HB2  B LYS   A 1 28  ? 17.886 4.326   16.563  0.28 33.36 ?  28  LYS   A HB2  1 
ATOM   779  H HB3  A LYS   A 1 28  ? 18.714 4.899   17.840  0.72 32.99 ?  28  LYS   A HB3  1 
ATOM   780  H HB3  B LYS   A 1 28  ? 18.682 4.909   17.806  0.28 33.36 ?  28  LYS   A HB3  1 
ATOM   781  H HG2  A LYS   A 1 28  ? 20.551 5.313   16.349  0.72 35.73 ?  28  LYS   A HG2  1 
ATOM   782  H HG2  B LYS   A 1 28  ? 20.486 5.347   16.267  0.28 35.49 ?  28  LYS   A HG2  1 
ATOM   783  H HG3  A LYS   A 1 28  ? 19.533 5.044   15.159  0.72 35.73 ?  28  LYS   A HG3  1 
ATOM   784  H HG3  B LYS   A 1 28  ? 19.436 5.065   15.106  0.28 35.49 ?  28  LYS   A HG3  1 
ATOM   785  H HD2  A LYS   A 1 28  ? 19.055 7.067   17.052  0.72 38.62 ?  28  LYS   A HD2  1 
ATOM   786  H HD2  B LYS   A 1 28  ? 18.938 7.058   17.027  0.28 37.52 ?  28  LYS   A HD2  1 
ATOM   787  H HD3  A LYS   A 1 28  ? 19.852 7.359   15.705  0.72 38.62 ?  28  LYS   A HD3  1 
ATOM   788  H HD3  B LYS   A 1 28  ? 19.745 7.392   15.699  0.28 37.52 ?  28  LYS   A HD3  1 
ATOM   789  H HE2  A LYS   A 1 28  ? 17.943 6.632   14.503  0.72 40.92 ?  28  LYS   A HE2  1 
ATOM   790  H HE2  B LYS   A 1 28  ? 17.837 6.640   14.469  0.28 39.13 ?  28  LYS   A HE2  1 
ATOM   791  H HE3  A LYS   A 1 28  ? 17.159 6.563   15.888  0.72 40.92 ?  28  LYS   A HE3  1 
ATOM   792  H HE3  B LYS   A 1 28  ? 17.047 6.607   15.851  0.28 39.13 ?  28  LYS   A HE3  1 
ATOM   793  H HZ1  A LYS   A 1 28  ? 16.767 8.548   14.848  0.72 42.37 ?  28  LYS   A HZ1  1 
ATOM   794  H HZ1  B LYS   A 1 28  ? 16.683 8.578   14.772  0.28 40.07 ?  28  LYS   A HZ1  1 
ATOM   795  H HZ2  A LYS   A 1 28  ? 17.466 8.810   16.090  0.72 42.37 ?  28  LYS   A HZ2  1 
ATOM   796  H HZ2  B LYS   A 1 28  ? 17.380 8.855   16.011  0.28 40.07 ?  28  LYS   A HZ2  1 
ATOM   797  H HZ3  A LYS   A 1 28  ? 18.179 8.872   14.830  0.72 42.37 ?  28  LYS   A HZ3  1 
ATOM   798  H HZ3  B LYS   A 1 28  ? 18.099 8.884   14.754  0.28 40.07 ?  28  LYS   A HZ3  1 
ATOM   799  N N    A LYS   A 1 29  ? 17.840 1.551   18.248  0.72 26.76 ?  29  LYS   A N    1 
ATOM   800  N N    B LYS   A 1 29  ? 17.758 1.643   18.227  0.28 28.29 ?  29  LYS   A N    1 
ATOM   801  C CA   A LYS   A 1 29  ? 17.249 0.845   19.381  0.72 28.72 ?  29  LYS   A CA   1 
ATOM   802  C CA   B LYS   A 1 29  ? 17.132 0.965   19.357  0.28 29.53 ?  29  LYS   A CA   1 
ATOM   803  C C    A LYS   A 1 29  ? 18.076 -0.376  19.769  0.72 28.09 ?  29  LYS   A C    1 
ATOM   804  C C    B LYS   A 1 29  ? 17.921 -0.271  19.772  0.28 28.57 ?  29  LYS   A C    1 
ATOM   805  O O    A LYS   A 1 29  ? 18.425 -0.552  20.942  0.72 29.43 ?  29  LYS   A O    1 
ATOM   806  O O    B LYS   A 1 29  ? 18.149 -0.498  20.965  0.28 28.75 ?  29  LYS   A O    1 
ATOM   807  C CB   A LYS   A 1 29  ? 15.819 0.422   19.037  0.72 31.42 ?  29  LYS   A CB   1 
ATOM   808  C CB   B LYS   A 1 29  ? 15.698 0.574   18.997  0.28 31.74 ?  29  LYS   A CB   1 
ATOM   809  C CG   A LYS   A 1 29  ? 15.092 -0.295  20.166  0.72 34.58 ?  29  LYS   A CG   1 
ATOM   810  C CG   B LYS   A 1 29  ? 14.925 -0.091  20.126  0.28 33.81 ?  29  LYS   A CG   1 
ATOM   811  C CD   A LYS   A 1 29  ? 14.768 0.661   21.300  0.72 37.43 ?  29  LYS   A CD   1 
ATOM   812  C CD   B LYS   A 1 29  ? 14.644 0.888   21.252  0.28 35.62 ?  29  LYS   A CD   1 
ATOM   813  C CE   A LYS   A 1 29  ? 13.886 0.005   22.349  0.72 39.39 ?  29  LYS   A CE   1 
ATOM   814  C CE   B LYS   A 1 29  ? 13.786 0.254   22.333  0.28 36.91 ?  29  LYS   A CE   1 
ATOM   815  N NZ   A LYS   A 1 29  ? 13.436 0.986   23.374  0.72 40.46 ?  29  LYS   A NZ   1 
ATOM   816  N NZ   B LYS   A 1 29  ? 13.465 1.221   23.417  0.28 37.58 ?  29  LYS   A NZ   1 
ATOM   817  H H    A LYS   A 1 29  ? 17.472 1.375   17.492  0.72 32.15 ?  29  LYS   A H    1 
ATOM   818  H H    B LYS   A 1 29  ? 17.373 1.504   17.472  0.28 33.98 ?  29  LYS   A H    1 
ATOM   819  H HA   A LYS   A 1 29  ? 17.212 1.438   20.145  0.72 34.50 ?  29  LYS   A HA   1 
ATOM   820  H HA   B LYS   A 1 29  ? 17.101 1.571   20.114  0.28 35.48 ?  29  LYS   A HA   1 
ATOM   821  H HB2  A LYS   A 1 29  ? 15.304 1.215   18.818  0.72 37.75 ?  29  LYS   A HB2  1 
ATOM   822  H HB2  B LYS   A 1 29  ? 15.213 1.373   18.743  0.28 38.12 ?  29  LYS   A HB2  1 
ATOM   823  H HB3  A LYS   A 1 29  ? 15.842 -0.176  18.276  0.72 37.75 ?  29  LYS   A HB3  1 
ATOM   824  H HB3  B LYS   A 1 29  ? 15.723 -0.047  18.253  0.28 38.12 ?  29  LYS   A HB3  1 
ATOM   825  H HG2  A LYS   A 1 29  ? 14.259 -0.659  19.828  0.72 41.53 ?  29  LYS   A HG2  1 
ATOM   826  H HG2  B LYS   A 1 29  ? 14.076 -0.412  19.784  0.28 40.61 ?  29  LYS   A HG2  1 
ATOM   827  H HG3  A LYS   A 1 29  ? 15.648 -1.010  20.517  0.72 41.53 ?  29  LYS   A HG3  1 
ATOM   828  H HG3  B LYS   A 1 29  ? 15.441 -0.831  20.486  0.28 40.61 ?  29  LYS   A HG3  1 
ATOM   829  H HD2  A LYS   A 1 29  ? 15.592 0.942   21.728  0.72 44.95 ?  29  LYS   A HD2  1 
ATOM   830  H HD2  B LYS   A 1 29  ? 15.482 1.166   21.653  0.28 42.78 ?  29  LYS   A HD2  1 
ATOM   831  H HD3  A LYS   A 1 29  ? 14.296 1.430   20.943  0.72 44.95 ?  29  LYS   A HD3  1 
ATOM   832  H HD3  B LYS   A 1 29  ? 14.169 1.656   20.896  0.28 42.78 ?  29  LYS   A HD3  1 
ATOM   833  H HE2  A LYS   A 1 29  ? 13.101 -0.369  21.918  0.72 47.31 ?  29  LYS   A HE2  1 
ATOM   834  H HE2  B LYS   A 1 29  ? 12.952 -0.052  21.942  0.28 44.33 ?  29  LYS   A HE2  1 
ATOM   835  H HE3  A LYS   A 1 29  ? 14.388 -0.695  22.796  0.72 47.31 ?  29  LYS   A HE3  1 
ATOM   836  H HE3  B LYS   A 1 29  ? 14.266 -0.493  22.725  0.28 44.33 ?  29  LYS   A HE3  1 
ATOM   837  H HZ1  A LYS   A 1 29  ? 12.921 0.581   23.977  0.72 48.59 ?  29  LYS   A HZ1  1 
ATOM   838  H HZ1  B LYS   A 1 29  ? 12.963 0.827   24.037  0.28 45.14 ?  29  LYS   A HZ1  1 
ATOM   839  H HZ2  A LYS   A 1 29  ? 14.140 1.341   23.786  0.72 48.59 ?  29  LYS   A HZ2  1 
ATOM   840  H HZ2  B LYS   A 1 29  ? 14.216 1.514   23.795  0.28 45.14 ?  29  LYS   A HZ2  1 
ATOM   841  H HZ3  A LYS   A 1 29  ? 12.968 1.637   22.987  0.72 48.59 ?  29  LYS   A HZ3  1 
ATOM   842  H HZ3  B LYS   A 1 29  ? 13.020 1.915   23.083  0.28 45.14 ?  29  LYS   A HZ3  1 
ATOM   843  N N    A VAL   A 1 30  ? 18.371 -1.243  18.800  0.72 26.39 ?  30  VAL   A N    1 
ATOM   844  N N    B VAL   A 1 30  ? 18.333 -1.085  18.804  0.28 27.47 ?  30  VAL   A N    1 
ATOM   845  C CA   A VAL   A 1 30  ? 19.046 -2.503  19.097  0.72 25.09 ?  30  VAL   A CA   1 
ATOM   846  C CA   B VAL   A 1 30  ? 18.968 -2.364  19.113  0.28 26.52 ?  30  VAL   A CA   1 
ATOM   847  C C    A VAL   A 1 30  ? 20.544 -2.309  19.312  0.72 23.53 ?  30  VAL   A C    1 
ATOM   848  C C    B VAL   A 1 30  ? 20.471 -2.212  19.323  0.28 25.76 ?  30  VAL   A C    1 
ATOM   849  O O    A VAL   A 1 30  ? 21.152 -3.021  20.118  0.72 23.83 ?  30  VAL   A O    1 
ATOM   850  O O    B VAL   A 1 30  ? 21.057 -2.904  20.158  0.28 25.65 ?  30  VAL   A O    1 
ATOM   851  C CB   A VAL   A 1 30  ? 18.765 -3.519  17.975  0.72 25.53 ?  30  VAL   A CB   1 
ATOM   852  C CB   B VAL   A 1 30  ? 18.652 -3.386  18.002  0.28 26.48 ?  30  VAL   A CB   1 
ATOM   853  C CG1  A VAL   A 1 30  ? 19.560 -4.802  18.195  0.72 26.19 ?  30  VAL   A CG1  1 
ATOM   854  C CG1  B VAL   A 1 30  ? 19.380 -4.697  18.259  0.28 26.59 ?  30  VAL   A CG1  1 
ATOM   855  C CG2  A VAL   A 1 30  ? 17.276 -3.815  17.883  0.72 25.89 ?  30  VAL   A CG2  1 
ATOM   856  C CG2  B VAL   A 1 30  ? 17.151 -3.614  17.896  0.28 26.50 ?  30  VAL   A CG2  1 
ATOM   857  H H    A VAL   A 1 30  ? 18.170 -1.137  17.972  0.72 31.70 ?  30  VAL   A H    1 
ATOM   858  H H    B VAL   A 1 30  ? 18.252 -0.925  17.960  0.28 33.01 ?  30  VAL   A H    1 
ATOM   859  H HA   A VAL   A 1 30  ? 18.674 -2.867  19.915  0.72 30.14 ?  30  VAL   A HA   1 
ATOM   860  H HA   B VAL   A 1 30  ? 18.581 -2.703  19.935  0.28 31.87 ?  30  VAL   A HA   1 
ATOM   861  H HB   A VAL   A 1 30  ? 19.051 -3.138  17.129  0.72 30.68 ?  30  VAL   A HB   1 
ATOM   862  H HB   B VAL   A 1 30  ? 18.964 -3.035  17.154  0.28 31.81 ?  30  VAL   A HB   1 
ATOM   863  H HG11 A VAL   A 1 30  ? 19.205 -5.495  17.615  0.72 31.47 ?  30  VAL   A HG11 1 
ATOM   864  H HG11 B VAL   A 1 30  ? 18.983 -5.390  17.708  0.28 31.95 ?  30  VAL   A HG11 1 
ATOM   865  H HG12 A VAL   A 1 30  ? 20.494 -4.644  17.983  0.72 31.47 ?  30  VAL   A HG12 1 
ATOM   866  H HG12 B VAL   A 1 30  ? 20.317 -4.592  18.032  0.28 31.95 ?  30  VAL   A HG12 1 
ATOM   867  H HG13 A VAL   A 1 30  ? 19.472 -5.074  19.122  0.72 31.47 ?  30  VAL   A HG13 1 
ATOM   868  H HG13 B VAL   A 1 30  ? 19.289 -4.930  19.196  0.28 31.95 ?  30  VAL   A HG13 1 
ATOM   869  H HG21 A VAL   A 1 30  ? 17.132 -4.492  17.204  0.72 31.10 ?  30  VAL   A HG21 1 
ATOM   870  H HG21 B VAL   A 1 30  ? 16.983 -4.294  17.224  0.28 31.83 ?  30  VAL   A HG21 1 
ATOM   871  H HG22 A VAL   A 1 30  ? 16.967 -4.136  18.744  0.72 31.10 ?  30  VAL   A HG22 1 
ATOM   872  H HG22 B VAL   A 1 30  ? 16.816 -3.910  18.757  0.28 31.83 ?  30  VAL   A HG22 1 
ATOM   873  H HG23 A VAL   A 1 30  ? 16.808 -3.001  17.644  0.72 31.10 ?  30  VAL   A HG23 1 
ATOM   874  H HG23 B VAL   A 1 30  ? 16.723 -2.783  17.641  0.28 31.83 ?  30  VAL   A HG23 1 
ATOM   875  N N    A LYS   A 1 31  ? 21.160 -1.360  18.614  0.72 22.73 ?  31  LYS   A N    1 
ATOM   876  N N    B LYS   A 1 31  ? 21.108 -1.312  18.582  0.28 25.38 ?  31  LYS   A N    1 
ATOM   877  C CA   A LYS   A 1 31  ? 22.612 -1.240  18.554  0.72 23.65 ?  31  LYS   A CA   1 
ATOM   878  C CA   B LYS   A 1 31  ? 22.562 -1.224  18.512  0.28 25.41 ?  31  LYS   A CA   1 
ATOM   879  C C    A LYS   A 1 31  ? 23.233 -2.600  18.224  0.72 21.16 ?  31  LYS   A C    1 
ATOM   880  C C    B LYS   A 1 31  ? 23.173 -2.601  18.238  0.28 22.51 ?  31  LYS   A C    1 
ATOM   881  O O    A LYS   A 1 31  ? 24.016 -3.141  19.012  0.72 21.71 ?  31  LYS   A O    1 
ATOM   882  O O    B LYS   A 1 31  ? 23.897 -3.147  19.077  0.28 22.72 ?  31  LYS   A O    1 
ATOM   883  C CB   A LYS   A 1 31  ? 23.191 -0.677  19.844  0.72 28.29 ?  31  LYS   A CB   1 
ATOM   884  C CB   B LYS   A 1 31  ? 23.158 -0.598  19.764  0.28 28.61 ?  31  LYS   A CB   1 
ATOM   885  C CG   A LYS   A 1 31  ? 22.503 0.581   20.340  0.72 33.09 ?  31  LYS   A CG   1 
ATOM   886  C CG   B LYS   A 1 31  ? 22.490 0.697   20.191  0.28 31.73 ?  31  LYS   A CG   1 
ATOM   887  C CD   A LYS   A 1 31  ? 23.510 1.640   20.758  0.72 36.71 ?  31  LYS   A CD   1 
ATOM   888  C CD   B LYS   A 1 31  ? 23.507 1.707   20.693  0.28 34.22 ?  31  LYS   A CD   1 
ATOM   889  C CE   A LYS   A 1 31  ? 22.877 2.670   21.680  0.72 39.13 ?  31  LYS   A CE   1 
ATOM   890  C CE   B LYS   A 1 31  ? 22.854 2.766   21.566  0.28 35.93 ?  31  LYS   A CE   1 
ATOM   891  N NZ   A LYS   A 1 31  ? 21.641 3.266   21.104  0.72 40.37 ?  31  LYS   A NZ   1 
ATOM   892  N NZ   B LYS   A 1 31  ? 21.624 3.343   20.954  0.28 36.82 ?  31  LYS   A NZ   1 
ATOM   893  H H    A LYS   A 1 31  ? 20.746 -0.760  18.160  0.72 27.31 ?  31  LYS   A H    1 
ATOM   894  H H    B LYS   A 1 31  ? 20.706 -0.726  18.100  0.28 30.50 ?  31  LYS   A H    1 
ATOM   895  H HA   A LYS   A 1 31  ? 22.837 -0.628  17.840  0.72 28.42 ?  31  LYS   A HA   1 
ATOM   896  H HA   B LYS   A 1 31  ? 22.789 -0.648  17.774  0.28 30.53 ?  31  LYS   A HA   1 
ATOM   897  H HB2  A LYS   A 1 31  ? 23.116 -1.350  20.535  0.72 33.98 ?  31  LYS   A HB2  1 
ATOM   898  H HB2  B LYS   A 1 31  ? 23.044 -1.226  20.480  0.28 34.36 ?  31  LYS   A HB2  1 
ATOM   899  H HB3  A LYS   A 1 31  ? 24.126 -0.463  19.695  0.72 33.98 ?  31  LYS   A HB3  1 
ATOM   900  H HB3  B LYS   A 1 31  ? 24.106 -0.422  19.618  0.28 34.36 ?  31  LYS   A HB3  1 
ATOM   901  H HG2  A LYS   A 1 31  ? 21.953 0.947   19.631  0.72 39.74 ?  31  LYS   A HG2  1 
ATOM   902  H HG2  B LYS   A 1 31  ? 22.025 1.082   19.433  0.28 38.12 ?  31  LYS   A HG2  1 
ATOM   903  H HG3  A LYS   A 1 31  ? 21.956 0.363   21.111  0.72 39.74 ?  31  LYS   A HG3  1 
ATOM   904  H HG3  B LYS   A 1 31  ? 21.865 0.511   20.910  0.28 38.12 ?  31  LYS   A HG3  1 
ATOM   905  H HD2  A LYS   A 1 31  ? 24.245 1.219   21.231  0.72 44.09 ?  31  LYS   A HD2  1 
ATOM   906  H HD2  B LYS   A 1 31  ? 24.180 1.250   21.222  0.28 41.11 ?  31  LYS   A HD2  1 
ATOM   907  H HD3  A LYS   A 1 31  ? 23.839 2.100   19.968  0.72 44.09 ?  31  LYS   A HD3  1 
ATOM   908  H HD3  B LYS   A 1 31  ? 23.919 2.150   19.935  0.28 41.11 ?  31  LYS   A HD3  1 
ATOM   909  H HE2  A LYS   A 1 31  ? 22.643 2.242   22.518  0.72 46.99 ?  31  LYS   A HE2  1 
ATOM   910  H HE2  B LYS   A 1 31  ? 22.613 2.367   22.414  0.28 43.16 ?  31  LYS   A HE2  1 
ATOM   911  H HE3  A LYS   A 1 31  ? 23.511 3.387   21.837  0.72 46.99 ?  31  LYS   A HE3  1 
ATOM   912  H HE3  B LYS   A 1 31  ? 23.483 3.489   21.708  0.28 43.16 ?  31  LYS   A HE3  1 
ATOM   913  H HZ1  A LYS   A 1 31  ? 21.319 3.888   21.653  0.72 48.48 ?  31  LYS   A HZ1  1 
ATOM   914  H HZ1  B LYS   A 1 31  ? 21.306 3.996   21.468  0.28 44.22 ?  31  LYS   A HZ1  1 
ATOM   915  H HZ2  A LYS   A 1 31  ? 21.821 3.640   20.317  0.72 48.48 ?  31  LYS   A HZ2  1 
ATOM   916  H HZ2  B LYS   A 1 31  ? 21.812 3.674   20.150  0.28 44.22 ?  31  LYS   A HZ2  1 
ATOM   917  H HZ3  A LYS   A 1 31  ? 21.023 2.635   20.989  0.72 48.48 ?  31  LYS   A HZ3  1 
ATOM   918  H HZ3  B LYS   A 1 31  ? 21.001 2.713   20.869  0.28 44.22 ?  31  LYS   A HZ3  1 
ATOM   919  N N    . PRO   A 1 32  ? 22.898 -3.178  17.074  1.00 19.79 ?  32  PRO   A N    1 
ATOM   920  C CA   . PRO   A 1 32  ? 23.380 -4.523  16.767  1.00 19.24 ?  32  PRO   A CA   1 
ATOM   921  C C    . PRO   A 1 32  ? 24.881 -4.541  16.554  1.00 19.12 ?  32  PRO   A C    1 
ATOM   922  O O    . PRO   A 1 32  ? 25.524 -3.513  16.337  1.00 18.86 ?  32  PRO   A O    1 
ATOM   923  C CB   . PRO   A 1 32  ? 22.652 -4.851  15.459  1.00 19.18 ?  32  PRO   A CB   1 
ATOM   924  C CG   . PRO   A 1 32  ? 22.484 -3.515  14.806  1.00 18.43 ?  32  PRO   A CG   1 
ATOM   925  C CD   . PRO   A 1 32  ? 22.175 -2.583  15.940  1.00 18.50 ?  32  PRO   A CD   1 
ATOM   926  H HA   . PRO   A 1 32  ? 23.126 -5.153  17.460  1.00 23.13 ?  32  PRO   A HA   1 
ATOM   927  H HB2  . PRO   A 1 32  ? 23.199 -5.442  14.914  1.00 23.06 ?  32  PRO   A HB2  1 
ATOM   928  H HB3  . PRO   A 1 32  ? 21.790 -5.258  15.650  1.00 23.06 ?  32  PRO   A HB3  1 
ATOM   929  H HG2  . PRO   A 1 32  ? 23.307 -3.270  14.359  1.00 22.15 ?  32  PRO   A HG2  1 
ATOM   930  H HG3  . PRO   A 1 32  ? 21.747 -3.558  14.174  1.00 22.15 ?  32  PRO   A HG3  1 
ATOM   931  H HD2  . PRO   A 1 32  ? 22.518 -1.698  15.732  1.00 22.24 ?  32  PRO   A HD2  1 
ATOM   932  H HD3  . PRO   A 1 32  ? 21.222 -2.567  16.106  1.00 22.24 ?  32  PRO   A HD3  1 
ATOM   933  N N    . THR   A 1 33  ? 25.433 -5.751  16.581  1.00 18.86 ?  33  THR   A N    1 
ATOM   934  C CA   . THR   A 1 33  ? 26.845 -5.914  16.270  1.00 18.62 ?  33  THR   A CA   1 
ATOM   935  C C    . THR   A 1 33  ? 27.151 -5.451  14.851  1.00 17.30 ?  33  THR   A C    1 
ATOM   936  O O    . THR   A 1 33  ? 28.178 -4.802  14.608  1.00 17.17 ?  33  THR   A O    1 
ATOM   937  C CB   . THR   A 1 33  ? 27.254 -7.373  16.467  1.00 20.57 ?  33  THR   A CB   1 
ATOM   938  O OG1  . THR   A 1 33  ? 26.947 -7.781  17.805  1.00 22.46 ?  33  THR   A OG1  1 
ATOM   939  C CG2  . THR   A 1 33  ? 28.739 -7.549  16.227  1.00 21.19 ?  33  THR   A CG2  1 
ATOM   940  H H    . THR   A 1 33  ? 25.013 -6.478  16.764  1.00 22.67 ?  33  THR   A H    1 
ATOM   941  H HA   . THR   A 1 33  ? 27.365 -5.371  16.882  1.00 22.38 ?  33  THR   A HA   1 
ATOM   942  H HB   . THR   A 1 33  ? 26.767 -7.934  15.839  1.00 24.73 ?  33  THR   A HB   1 
ATOM   943  H HG1  . THR   A 1 33  ? 27.362 -7.300  18.356  1.00 26.99 ?  33  THR   A HG1  1 
ATOM   944  H HG21 . THR   A 1 33  ? 29.015 -8.433  16.514  1.00 25.47 ?  33  THR   A HG21 1 
ATOM   945  H HG22 . THR   A 1 33  ? 28.937 -7.448  15.284  1.00 25.47 ?  33  THR   A HG22 1 
ATOM   946  H HG23 . THR   A 1 33  ? 29.233 -6.884  16.729  1.00 25.47 ?  33  THR   A HG23 1 
ATOM   947  N N    . VAL   A 1 34  ? 26.271 -5.774  13.901  1.00 15.50 ?  34  VAL   A N    1 
ATOM   948  C CA   . VAL   A 1 34  ? 26.469 -5.447  12.494  1.00 14.19 ?  34  VAL   A CA   1 
ATOM   949  C C    . VAL   A 1 34  ? 25.170 -4.895  11.919  1.00 13.82 ?  34  VAL   A C    1 
ATOM   950  O O    . VAL   A 1 34  ? 24.131 -5.569  11.959  1.00 14.60 ?  34  VAL   A O    1 
ATOM   951  C CB   . VAL   A 1 34  ? 26.927 -6.659  11.661  1.00 14.66 ?  34  VAL   A CB   1 
ATOM   952  C CG1  . VAL   A 1 34  ? 27.103 -6.262  10.196  1.00 14.92 ?  34  VAL   A CG1  1 
ATOM   953  C CG2  . VAL   A 1 34  ? 28.211 -7.273  12.231  1.00 16.02 ?  34  VAL   A CG2  1 
ATOM   954  H H    . VAL   A 1 34  ? 25.541 -6.203  14.053  1.00 18.63 ?  34  VAL   A H    1 
ATOM   955  H HA   . VAL   A 1 34  ? 27.146 -4.755  12.419  1.00 17.07 ?  34  VAL   A HA   1 
ATOM   956  H HB   . VAL   A 1 34  ? 26.237 -7.337  11.704  1.00 17.63 ?  34  VAL   A HB   1 
ATOM   957  H HG11 . VAL   A 1 34  ? 27.599 -6.960  9.740   1.00 17.94 ?  34  VAL   A HG11 1 
ATOM   958  H HG12 . VAL   A 1 34  ? 26.232 -6.155  9.787   1.00 17.94 ?  34  VAL   A HG12 1 
ATOM   959  H HG13 . VAL   A 1 34  ? 27.598 -5.427  10.152  1.00 17.94 ?  34  VAL   A HG13 1 
ATOM   960  H HG21 . VAL   A 1 34  ? 28.489 -8.007  11.663  1.00 19.26 ?  34  VAL   A HG21 1 
ATOM   961  H HG22 . VAL   A 1 34  ? 28.904 -6.593  12.256  1.00 19.26 ?  34  VAL   A HG22 1 
ATOM   962  H HG23 . VAL   A 1 34  ? 28.037 -7.598  13.130  1.00 19.26 ?  34  VAL   A HG23 1 
ATOM   963  N N    . VAL   A 1 35  ? 25.235 -3.685  11.360  1.00 12.85 ?  35  VAL   A N    1 
ATOM   964  C CA   . VAL   A 1 35  ? 24.206 -3.164  10.471  1.00 12.74 ?  35  VAL   A CA   1 
ATOM   965  C C    . VAL   A 1 35  ? 24.759 -3.166  9.052   1.00 12.06 ?  35  VAL   A C    1 
ATOM   966  O O    . VAL   A 1 35  ? 25.906 -2.764  8.824   1.00 12.78 ?  35  VAL   A O    1 
ATOM   967  C CB   . VAL   A 1 35  ? 23.673 -1.772  10.883  1.00 13.49 ?  35  VAL   A CB   1 
ATOM   968  C CG1  . VAL   A 1 35  ? 24.736 -0.680  10.748  1.00 14.04 ?  35  VAL   A CG1  1 
ATOM   969  C CG2  . VAL   A 1 35  ? 22.434 -1.420  10.058  1.00 14.12 ?  35  VAL   A CG2  1 
ATOM   970  H H    . VAL   A 1 35  ? 25.885 -3.135  11.479  1.00 15.45 ?  35  VAL   A H    1 
ATOM   971  H HA   . VAL   A 1 35  ? 23.449 -3.775  10.489  1.00 15.33 ?  35  VAL   A HA   1 
ATOM   972  H HB   . VAL   A 1 35  ? 23.396 -1.805  11.809  1.00 16.23 ?  35  VAL   A HB   1 
ATOM   973  H HG11 . VAL   A 1 35  ? 24.387 0.146   11.120  1.00 16.88 ?  35  VAL   A HG11 1 
ATOM   974  H HG12 . VAL   A 1 35  ? 25.527 -0.954  11.230  1.00 16.88 ?  35  VAL   A HG12 1 
ATOM   975  H HG13 . VAL   A 1 35  ? 24.945 -0.554  9.808   1.00 16.88 ?  35  VAL   A HG13 1 
ATOM   976  H HG21 . VAL   A 1 35  ? 22.075 -0.577  10.367  1.00 16.99 ?  35  VAL   A HG21 1 
ATOM   977  H HG22 . VAL   A 1 35  ? 22.685 -1.351  9.121   1.00 16.99 ?  35  VAL   A HG22 1 
ATOM   978  H HG23 . VAL   A 1 35  ? 21.771 -2.124  10.166  1.00 16.99 ?  35  VAL   A HG23 1 
ATOM   979  N N    . VAL   A 1 36  ? 23.946 -3.621  8.104   1.00 11.51 ?  36  VAL   A N    1 
ATOM   980  C CA   . VAL   A 1 36  ? 24.320 -3.633  6.697   1.00 11.41 ?  36  VAL   A CA   1 
ATOM   981  C C    . VAL   A 1 36  ? 23.867 -2.341  6.035   1.00 11.79 ?  36  VAL   A C    1 
ATOM   982  O O    . VAL   A 1 36  ? 22.707 -1.932  6.171   1.00 12.16 ?  36  VAL   A O    1 
ATOM   983  C CB   . VAL   A 1 36  ? 23.717 -4.848  5.978   1.00 11.29 ?  36  VAL   A CB   1 
ATOM   984  C CG1  . VAL   A 1 36  ? 23.972 -4.767  4.491   1.00 12.00 ?  36  VAL   A CG1  1 
ATOM   985  C CG2  . VAL   A 1 36  ? 24.272 -6.141  6.552   1.00 12.24 ?  36  VAL   A CG2  1 
ATOM   986  H H    . VAL   A 1 36  ? 23.149 -3.930  8.254   1.00 13.85 ?  36  VAL   A H    1 
ATOM   987  H HA   . VAL   A 1 36  ? 25.287 -3.694  6.628   1.00 13.74 ?  36  VAL   A HA   1 
ATOM   988  H HB   . VAL   A 1 36  ? 22.755 -4.849  6.117   1.00 13.58 ?  36  VAL   A HB   1 
ATOM   989  H HG11 . VAL   A 1 36  ? 23.839 -5.645  4.098   1.00 14.44 ?  36  VAL   A HG11 1 
ATOM   990  H HG12 . VAL   A 1 36  ? 23.351 -4.135  4.092   1.00 14.44 ?  36  VAL   A HG12 1 
ATOM   991  H HG13 . VAL   A 1 36  ? 24.884 -4.475  4.341   1.00 14.44 ?  36  VAL   A HG13 1 
ATOM   992  H HG21 . VAL   A 1 36  ? 23.880 -6.896  6.077   1.00 14.72 ?  36  VAL   A HG21 1 
ATOM   993  H HG22 . VAL   A 1 36  ? 25.234 -6.152  6.447   1.00 14.72 ?  36  VAL   A HG22 1 
ATOM   994  H HG23 . VAL   A 1 36  ? 24.041 -6.199  7.495   1.00 14.72 ?  36  VAL   A HG23 1 
ATOM   995  N N    . ASN   A 1 37  ? 24.787 -1.713  5.303   1.00 10.65 ?  37  ASN   A N    1 
ATOM   996  C CA   . ASN   A 1 37  ? 24.469 -0.590  4.435   1.00 10.50 ?  37  ASN   A CA   1 
ATOM   997  C C    . ASN   A 1 37  ? 24.339 -1.054  2.993   1.00 10.41 ?  37  ASN   A C    1 
ATOM   998  O O    . ASN   A 1 37  ? 25.118 -1.890  2.521   1.00 11.04 ?  37  ASN   A O    1 
ATOM   999  C CB   . ASN   A 1 37  ? 25.544 0.489   4.524   1.00 10.95 ?  37  ASN   A CB   1 
ATOM   1000 C CG   . ASN   A 1 37  ? 25.226 1.690   3.668   1.00 11.46 ?  37  ASN   A CG   1 
ATOM   1001 O OD1  . ASN   A 1 37  ? 24.050 2.029   3.480   1.00 11.92 ?  37  ASN   A OD1  1 
ATOM   1002 N ND2  . ASN   A 1 37  ? 26.263 2.342   3.148   1.00 11.57 ?  37  ASN   A ND2  1 
ATOM   1003 H H    . ASN   A 1 37  ? 25.626 -1.920  5.304   1.00 12.82 ?  37  ASN   A H    1 
ATOM   1004 H HA   . ASN   A 1 37  ? 23.628 -0.201  4.712   1.00 12.63 ?  37  ASN   A HA   1 
ATOM   1005 H HB2  . ASN   A 1 37  ? 25.618 0.793   5.444   1.00 13.18 ?  37  ASN   A HB2  1 
ATOM   1006 H HB3  . ASN   A 1 37  ? 26.394 0.122   4.228   1.00 13.18 ?  37  ASN   A HB3  1 
ATOM   1007 H HD21 . ASN   A 1 37  ? 26.129 3.029   2.645   1.00 13.92 ?  37  ASN   A HD21 1 
ATOM   1008 H HD22 . ASN   A 1 37  ? 27.061 2.078   3.298   1.00 13.92 ?  37  ASN   A HD22 1 
ATOM   1009 N N    A ALA   A 1 38  ? 23.325 -0.509  2.314   0.72 11.24 ?  38  ALA   A N    1 
ATOM   1010 N N    B ALA   A 1 38  ? 23.337 -0.527  2.291   0.28 10.85 ?  38  ALA   A N    1 
ATOM   1011 C CA   A ALA   A 1 38  ? 23.135 -0.636  0.870   0.72 11.41 ?  38  ALA   A CA   1 
ATOM   1012 C CA   B ALA   A 1 38  ? 23.182 -0.803  0.863   0.28 11.18 ?  38  ALA   A CA   1 
ATOM   1013 C C    A ALA   A 1 38  ? 24.069 0.349   0.165   0.72 11.15 ?  38  ALA   A C    1 
ATOM   1014 C C    B ALA   A 1 38  ? 23.970 0.252   0.087   0.28 11.37 ?  38  ALA   A C    1 
ATOM   1015 O O    A ALA   A 1 38  ? 23.677 1.444   -0.250  0.72 11.04 ?  38  ALA   A O    1 
ATOM   1016 O O    B ALA   A 1 38  ? 23.445 1.278   -0.355  0.28 11.61 ?  38  ALA   A O    1 
ATOM   1017 C CB   A ALA   A 1 38  ? 21.679 -0.358  0.511   0.72 12.31 ?  38  ALA   A CB   1 
ATOM   1018 C CB   B ALA   A 1 38  ? 21.709 -0.815  0.478   0.28 11.68 ?  38  ALA   A CB   1 
ATOM   1019 H H    A ALA   A 1 38  ? 22.721 -0.025  2.691   0.72 13.52 ?  38  ALA   A H    1 
ATOM   1020 H H    B ALA   A 1 38  ? 22.738 -0.005  2.625   0.28 13.05 ?  38  ALA   A H    1 
ATOM   1021 H HA   A ALA   A 1 38  ? 23.363 -1.531  0.589   0.72 13.73 ?  38  ALA   A HA   1 
ATOM   1022 H HA   B ALA   A 1 38  ? 23.555 -1.680  0.668   0.28 13.46 ?  38  ALA   A HA   1 
ATOM   1023 H HB1  A ALA   A 1 38  ? 21.567 -0.449  -0.447  0.72 14.81 ?  38  ALA   A HB1  1 
ATOM   1024 H HB1  B ALA   A 1 38  ? 21.645 -0.886  -0.486  0.28 14.05 ?  38  ALA   A HB1  1 
ATOM   1025 H HB2  A ALA   A 1 38  ? 21.114 -0.997  0.974   0.72 14.81 ?  38  ALA   A HB2  1 
ATOM   1026 H HB2  B ALA   A 1 38  ? 21.272 -1.573  0.898   0.28 14.05 ?  38  ALA   A HB2  1 
ATOM   1027 H HB3  A ALA   A 1 38  ? 21.450 0.545   0.787   0.72 14.81 ?  38  ALA   A HB3  1 
ATOM   1028 H HB3  B ALA   A 1 38  ? 21.301 0.013   0.774   0.28 14.05 ?  38  ALA   A HB3  1 
ATOM   1029 N N    A ALA   A 1 39  ? 25.337 -0.049  0.042   0.72 11.35 ?  39  ALA   A N    1 
ATOM   1030 N N    B ALA   A 1 39  ? 25.264 -0.010  -0.076  0.28 11.55 ?  39  ALA   A N    1 
ATOM   1031 C CA   A ALA   A 1 39  ? 26.399 0.816   -0.444  0.72 10.71 ?  39  ALA   A CA   1 
ATOM   1032 C CA   B ALA   A 1 39  ? 26.196 0.977   -0.594  0.28 11.76 ?  39  ALA   A CA   1 
ATOM   1033 C C    A ALA   A 1 39  ? 26.512 0.769   -1.962  0.72 10.79 ?  39  ALA   A C    1 
ATOM   1034 C C    B ALA   A 1 39  ? 26.424 0.798   -2.089  0.28 11.44 ?  39  ALA   A C    1 
ATOM   1035 O O    A ALA   A 1 39  ? 25.994 -0.135  -2.630  0.72 11.72 ?  39  ALA   A O    1 
ATOM   1036 O O    B ALA   A 1 39  ? 26.108 -0.240  -2.677  0.28 11.52 ?  39  ALA   A O    1 
ATOM   1037 C CB   A ALA   A 1 39  ? 27.730 0.405   0.192   0.72 10.94 ?  39  ALA   A CB   1 
ATOM   1038 C CB   B ALA   A 1 39  ? 27.535 0.874   0.138   0.28 12.62 ?  39  ALA   A CB   1 
ATOM   1039 H H    A ALA   A 1 39  ? 25.609 -0.843  0.252   0.72 13.66 ?  39  ALA   A H    1 
ATOM   1040 H H    B ALA   A 1 39  ? 25.630 -0.770  0.110   0.28 13.90 ?  39  ALA   A H    1 
ATOM   1041 H HA   A ALA   A 1 39  ? 26.210 1.729   -0.179  0.72 12.89 ?  39  ALA   A HA   1 
ATOM   1042 H HA   B ALA   A 1 39  ? 25.829 1.862   -0.435  0.28 14.15 ?  39  ALA   A HA   1 
ATOM   1043 H HB1  A ALA   A 1 39  ? 28.431 0.993   -0.139  0.72 13.16 ?  39  ALA   A HB1  1 
ATOM   1044 H HB1  B ALA   A 1 39  ? 28.139 1.540   -0.223  0.28 15.19 ?  39  ALA   A HB1  1 
ATOM   1045 H HB2  A ALA   A 1 39  ? 27.662 0.495   1.160   0.72 13.16 ?  39  ALA   A HB2  1 
ATOM   1046 H HB2  B ALA   A 1 39  ? 27.391 1.033   1.084   0.28 15.19 ?  39  ALA   A HB2  1 
ATOM   1047 H HB3  A ALA   A 1 39  ? 27.927 -0.511  -0.041  0.72 13.16 ?  39  ALA   A HB3  1 
ATOM   1048 H HB3  B ALA   A 1 39  ? 27.899 -0.014  0.003   0.28 15.19 ?  39  ALA   A HB3  1 
ATOM   1049 N N    A ASN   A 1 40  ? 27.205 1.773   -2.505  0.72 11.30 ?  40  ASN   A N    1 
ATOM   1050 N N    B ASN   A 1 40  ? 26.978 1.840   -2.699  0.28 11.13 ?  40  ASN   A N    1 
ATOM   1051 C CA   A ASN   A 1 40  ? 27.754 1.726   -3.855  0.72 11.54 ?  40  ASN   A CA   1 
ATOM   1052 C CA   B ASN   A 1 40  ? 27.529 1.761   -4.043  0.28 11.07 ?  40  ASN   A CA   1 
ATOM   1053 C C    A ASN   A 1 40  ? 29.280 1.614   -3.783  0.72 10.95 ?  40  ASN   A C    1 
ATOM   1054 C C    B ASN   A 1 40  ? 29.046 1.603   -3.954  0.28 10.81 ?  40  ASN   A C    1 
ATOM   1055 O O    A ASN   A 1 40  ? 29.878 1.720   -2.709  0.72 11.31 ?  40  ASN   A O    1 
ATOM   1056 O O    B ASN   A 1 40  ? 29.641 1.671   -2.877  0.28 10.85 ?  40  ASN   A O    1 
ATOM   1057 C CB   A ASN   A 1 40  ? 27.275 2.908   -4.716  0.72 12.81 ?  40  ASN   A CB   1 
ATOM   1058 C CB   B ASN   A 1 40  ? 27.148 2.995   -4.871  0.28 11.46 ?  40  ASN   A CB   1 
ATOM   1059 C CG   A ASN   A 1 40  ? 27.630 4.260   -4.129  0.72 13.77 ?  40  ASN   A CG   1 
ATOM   1060 C CG   B ASN   A 1 40  ? 27.569 4.296   -4.216  0.28 11.47 ?  40  ASN   A CG   1 
ATOM   1061 O OD1  A ASN   A 1 40  ? 28.787 4.517   -3.790  0.72 14.43 ?  40  ASN   A OD1  1 
ATOM   1062 O OD1  B ASN   A 1 40  ? 28.759 4.554   -4.030  0.28 11.60 ?  40  ASN   A OD1  1 
ATOM   1063 N ND2  A ASN   A 1 40  ? 26.632 5.138   -4.016  0.72 14.73 ?  40  ASN   A ND2  1 
ATOM   1064 N ND2  B ASN   A 1 40  ? 26.591 5.134   -3.881  0.28 12.22 ?  40  ASN   A ND2  1 
ATOM   1065 H H    A ASN   A 1 40  ? 27.377 2.509   -2.097  0.72 13.59 ?  40  ASN   A H    1 
ATOM   1066 H H    B ASN   A 1 40  ? 27.046 2.619   -2.342  0.28 13.39 ?  40  ASN   A H    1 
ATOM   1067 H HA   A ASN   A 1 40  ? 27.430 0.919   -4.284  0.72 13.88 ?  40  ASN   A HA   1 
ATOM   1068 H HA   B ASN   A 1 40  ? 27.160 0.977   -4.488  0.28 13.32 ?  40  ASN   A HA   1 
ATOM   1069 H HB2  A ASN   A 1 40  ? 27.683 2.841   -5.601  0.72 15.42 ?  40  ASN   A HB2  1 
ATOM   1070 H HB2  B ASN   A 1 40  ? 27.585 2.939   -5.733  0.28 13.79 ?  40  ASN   A HB2  1 
ATOM   1071 H HB3  A ASN   A 1 40  ? 26.309 2.867   -4.804  0.72 15.42 ?  40  ASN   A HB3  1 
ATOM   1072 H HB3  B ASN   A 1 40  ? 26.185 3.013   -4.989  0.28 13.79 ?  40  ASN   A HB3  1 
ATOM   1073 H HD21 A ASN   A 1 40  ? 26.785 5.923   -3.694  0.72 17.71 ?  40  ASN   A HD21 1 
ATOM   1074 H HD21 B ASN   A 1 40  ? 26.780 5.885   -3.505  0.28 14.70 ?  40  ASN   A HD21 1 
ATOM   1075 H HD22 A ASN   A 1 40  ? 25.835 4.917   -4.246  0.72 17.71 ?  40  ASN   A HD22 1 
ATOM   1076 H HD22 B ASN   A 1 40  ? 25.772 4.923   -4.032  0.28 14.70 ?  40  ASN   A HD22 1 
ATOM   1077 N N    A VAL   A 1 41  ? 29.904 1.353   -4.936  0.72 11.48 ?  41  VAL   A N    1 
ATOM   1078 N N    B VAL   A 1 41  ? 29.675 1.383   -5.110  0.28 11.01 ?  41  VAL   A N    1 
ATOM   1079 C CA   A VAL   A 1 41  ? 31.336 1.038   -4.961  0.72 12.10 ?  41  VAL   A CA   1 
ATOM   1080 C CA   B VAL   A 1 41  ? 31.100 1.055   -5.116  0.28 11.64 ?  41  VAL   A CA   1 
ATOM   1081 C C    A VAL   A 1 41  ? 32.192 2.191   -4.481  0.72 12.03 ?  41  VAL   A C    1 
ATOM   1082 C C    B VAL   A 1 41  ? 31.978 2.201   -4.630  0.28 11.56 ?  41  VAL   A C    1 
ATOM   1083 O O    A VAL   A 1 41  ? 33.330 1.975   -4.048  0.72 12.35 ?  41  VAL   A O    1 
ATOM   1084 O O    B VAL   A 1 41  ? 33.135 1.969   -4.258  0.28 11.73 ?  41  VAL   A O    1 
ATOM   1085 C CB   A VAL   A 1 41  ? 31.830 0.561   -6.349  0.72 12.88 ?  41  VAL   A CB   1 
ATOM   1086 C CB   B VAL   A 1 41  ? 31.580 0.560   -6.494  0.28 12.66 ?  41  VAL   A CB   1 
ATOM   1087 C CG1  A VAL   A 1 41  ? 31.146 -0.733  -6.751  0.72 13.40 ?  41  VAL   A CG1  1 
ATOM   1088 C CG1  B VAL   A 1 41  ? 30.815 -0.686  -6.911  0.28 13.48 ?  41  VAL   A CG1  1 
ATOM   1089 C CG2  A VAL   A 1 41  ? 31.665 1.642   -7.416  0.72 13.84 ?  41  VAL   A CG2  1 
ATOM   1090 C CG2  B VAL   A 1 41  ? 31.472 1.658   -7.544  0.28 13.13 ?  41  VAL   A CG2  1 
ATOM   1091 H H    A VAL   A 1 41  ? 29.535 1.342   -5.708  0.72 13.82 ?  41  VAL   A H    1 
ATOM   1092 H H    B VAL   A 1 41  ? 29.298 1.401   -5.882  0.28 13.25 ?  41  VAL   A H    1 
ATOM   1093 H HA   A VAL   A 1 41  ? 31.498 0.304   -4.344  0.72 14.56 ?  41  VAL   A HA   1 
ATOM   1094 H HA   B VAL   A 1 41  ? 31.224 0.320   -4.495  0.28 14.00 ?  41  VAL   A HA   1 
ATOM   1095 H HB   A VAL   A 1 41  ? 32.781 0.369   -6.286  0.72 15.50 ?  41  VAL   A HB   1 
ATOM   1096 H HB   B VAL   A 1 41  ? 32.514 0.315   -6.418  0.28 15.24 ?  41  VAL   A HB   1 
ATOM   1097 H HG11 A VAL   A 1 41  ? 31.479 -1.016  -7.617  0.72 16.12 ?  41  VAL   A HG11 1 
ATOM   1098 H HG11 B VAL   A 1 41  ? 31.096 -0.943  -7.801  0.28 16.22 ?  41  VAL   A HG11 1 
ATOM   1099 H HG12 A VAL   A 1 41  ? 31.335 -1.413  -6.086  0.72 16.12 ?  41  VAL   A HG12 1 
ATOM   1100 H HG12 B VAL   A 1 41  ? 31.012 -1.400  -6.283  0.28 16.22 ?  41  VAL   A HG12 1 
ATOM   1101 H HG13 A VAL   A 1 41  ? 30.187 -0.581  -6.802  0.72 16.12 ?  41  VAL   A HG13 1 
ATOM   1102 H HG13 B VAL   A 1 41  ? 29.866 -0.496  -6.904  0.28 16.22 ?  41  VAL   A HG13 1 
ATOM   1103 H HG21 A VAL   A 1 41  ? 31.898 1.266   -8.282  0.72 16.65 ?  41  VAL   A HG21 1 
ATOM   1104 H HG21 B VAL   A 1 41  ? 31.695 1.282   -8.411  0.28 15.80 ?  41  VAL   A HG21 1 
ATOM   1105 H HG22 A VAL   A 1 41  ? 30.746 1.941   -7.422  0.72 16.65 ?  41  VAL   A HG22 1 
ATOM   1106 H HG22 B VAL   A 1 41  ? 30.567 1.999   -7.553  0.28 15.80 ?  41  VAL   A HG22 1 
ATOM   1107 H HG23 A VAL   A 1 41  ? 32.257 2.382   -7.210  0.72 16.65 ?  41  VAL   A HG23 1 
ATOM   1108 H HG23 B VAL   A 1 41  ? 32.095 2.368   -7.323  0.28 15.80 ?  41  VAL   A HG23 1 
ATOM   1109 N N    A TYR   A 1 42  ? 31.681 3.415   -4.563  0.72 12.21 ?  42  TYR   A N    1 
ATOM   1110 N N    B TYR   A 1 42  ? 31.475 3.436   -4.636  0.28 11.58 ?  42  TYR   A N    1 
ATOM   1111 C CA   A TYR   A 1 42  ? 32.405 4.609   -4.145  0.72 12.30 ?  42  TYR   A CA   1 
ATOM   1112 C CA   B TYR   A 1 42  ? 32.262 4.597   -4.231  0.28 11.63 ?  42  TYR   A CA   1 
ATOM   1113 C C    A TYR   A 1 42  ? 32.124 4.979   -2.702  0.72 11.79 ?  42  TYR   A C    1 
ATOM   1114 C C    B TYR   A 1 42  ? 32.054 4.989   -2.772  0.28 11.48 ?  42  TYR   A C    1 
ATOM   1115 O O    A TYR   A 1 42  ? 32.691 5.961   -2.198  0.72 12.86 ?  42  TYR   A O    1 
ATOM   1116 O O    B TYR   A 1 42  ? 32.625 5.990   -2.324  0.28 12.02 ?  42  TYR   A O    1 
ATOM   1117 C CB   A TYR   A 1 42  ? 32.053 5.791   -5.070  0.72 12.77 ?  42  TYR   A CB   1 
ATOM   1118 C CB   B TYR   A 1 42  ? 31.925 5.796   -5.124  0.28 11.81 ?  42  TYR   A CB   1 
ATOM   1119 C CG   A TYR   A 1 42  ? 32.257 5.473   -6.539  0.72 13.52 ?  42  TYR   A CG   1 
ATOM   1120 C CG   B TYR   A 1 42  ? 32.027 5.502   -6.603  0.28 12.22 ?  42  TYR   A CG   1 
ATOM   1121 C CD1  A TYR   A 1 42  ? 33.528 5.281   -7.055  0.72 14.10 ?  42  TYR   A CD1  1 
ATOM   1122 C CD1  B TYR   A 1 42  ? 33.261 5.306   -7.208  0.28 12.20 ?  42  TYR   A CD1  1 
ATOM   1123 C CD2  A TYR   A 1 42  ? 31.177 5.335   -7.403  0.72 14.76 ?  42  TYR   A CD2  1 
ATOM   1124 C CD2  B TYR   A 1 42  ? 30.890 5.423   -7.395  0.28 13.17 ?  42  TYR   A CD2  1 
ATOM   1125 C CE1  A TYR   A 1 42  ? 33.721 4.967   -8.390  0.72 14.40 ?  42  TYR   A CE1  1 
ATOM   1126 C CE1  B TYR   A 1 42  ? 33.360 5.033   -8.559  0.28 12.42 ?  42  TYR   A CE1  1 
ATOM   1127 C CE2  A TYR   A 1 42  ? 31.363 5.033   -8.743  0.72 15.23 ?  42  TYR   A CE2  1 
ATOM   1128 C CE2  B TYR   A 1 42  ? 30.979 5.159   -8.747  0.28 13.50 ?  42  TYR   A CE2  1 
ATOM   1129 C CZ   A TYR   A 1 42  ? 32.638 4.847   -9.230  0.72 14.68 ?  42  TYR   A CZ   1 
ATOM   1130 C CZ   B TYR   A 1 42  ? 32.216 4.962   -9.324  0.28 12.95 ?  42  TYR   A CZ   1 
ATOM   1131 O OH   A TYR   A 1 42  ? 32.825 4.537   -10.558 0.72 16.39 ?  42  TYR   A OH   1 
ATOM   1132 O OH   B TYR   A 1 42  ? 32.315 4.698   -10.670 0.28 13.43 ?  42  TYR   A OH   1 
ATOM   1133 H H    A TYR   A 1 42  ? 30.902 3.583   -4.868  0.72 14.69 ?  42  TYR   A H    1 
ATOM   1134 H H    B TYR   A 1 42  ? 30.671 3.629   -4.892  0.28 13.94 ?  42  TYR   A H    1 
ATOM   1135 H HA   A TYR   A 1 42  ? 33.360 4.453   -4.224  0.72 14.80 ?  42  TYR   A HA   1 
ATOM   1136 H HA   B TYR   A 1 42  ? 33.200 4.387   -4.363  0.28 14.00 ?  42  TYR   A HA   1 
ATOM   1137 H HB2  A TYR   A 1 42  ? 31.120 6.026   -4.942  0.72 15.36 ?  42  TYR   A HB2  1 
ATOM   1138 H HB2  B TYR   A 1 42  ? 31.015 6.077   -4.937  0.28 14.20 ?  42  TYR   A HB2  1 
ATOM   1139 H HB3  A TYR   A 1 42  ? 32.618 6.549   -4.848  0.72 15.36 ?  42  TYR   A HB3  1 
ATOM   1140 H HB3  B TYR   A 1 42  ? 32.541 6.516   -4.919  0.28 14.20 ?  42  TYR   A HB3  1 
ATOM   1141 H HD1  A TYR   A 1 42  ? 34.268 5.359   -6.495  0.72 16.96 ?  42  TYR   A HD1  1 
ATOM   1142 H HD1  B TYR   A 1 42  ? 34.035 5.350   -6.693  0.28 14.68 ?  42  TYR   A HD1  1 
ATOM   1143 H HD2  A TYR   A 1 42  ? 30.313 5.464   -7.077  0.72 17.75 ?  42  TYR   A HD2  1 
ATOM   1144 H HD2  B TYR   A 1 42  ? 30.054 5.557   -7.009  0.28 15.84 ?  42  TYR   A HD2  1 
ATOM   1145 H HE1  A TYR   A 1 42  ? 34.582 4.848   -8.723  0.72 17.32 ?  42  TYR   A HE1  1 
ATOM   1146 H HE1  B TYR   A 1 42  ? 34.195 4.903   -8.951  0.28 14.94 ?  42  TYR   A HE1  1 
ATOM   1147 H HE2  A TYR   A 1 42  ? 30.626 4.952   -9.310  0.72 18.32 ?  42  TYR   A HE2  1 
ATOM   1148 H HE2  B TYR   A 1 42  ? 30.209 5.111   -9.266  0.28 16.24 ?  42  TYR   A HE2  1 
ATOM   1149 H HH   A TYR   A 1 42  ? 33.645 4.418   -10.710 0.72 19.71 ?  42  TYR   A HH   1 
ATOM   1150 H HH   B TYR   A 1 42  ? 31.553 4.685   -11.019 0.28 16.16 ?  42  TYR   A HH   1 
ATOM   1151 N N    . LEU   A 1 43  ? 31.242 4.232   -2.036  1.00 11.42 ?  43  LEU   A N    1 
ATOM   1152 C CA   . LEU   A 1 43  ? 30.806 4.575   -0.686  1.00 11.20 ?  43  LEU   A CA   1 
ATOM   1153 C C    . LEU   A 1 43  ? 30.317 6.021   -0.597  1.00 11.65 ?  43  LEU   A C    1 
ATOM   1154 O O    . LEU   A 1 43  ? 30.568 6.723   0.383   1.00 12.63 ?  43  LEU   A O    1 
ATOM   1155 C CB   . LEU   A 1 43  ? 31.851 4.263   0.379   1.00 11.79 ?  43  LEU   A CB   1 
ATOM   1156 C CG   . LEU   A 1 43  ? 32.339 2.812   0.468   1.00 12.27 ?  43  LEU   A CG   1 
ATOM   1157 C CD1  . LEU   A 1 43  ? 33.378 2.702   1.571   1.00 12.98 ?  43  LEU   A CD1  1 
ATOM   1158 C CD2  . LEU   A 1 43  ? 31.191 1.832   0.697   1.00 12.67 ?  43  LEU   A CD2  1 
ATOM   1159 H H    A LEU   A 1 43  ? 30.887 3.508   -2.344  0.72 13.74 ?  43  LEU   A H    1 
ATOM   1160 H H    B LEU   A 1 43  ? 30.901 3.490   -2.316  0.28 13.74 ?  43  LEU   A H    1 
ATOM   1161 H HA   . LEU   A 1 43  ? 30.037 4.016   -0.484  1.00 13.48 ?  43  LEU   A HA   1 
ATOM   1162 H HB2  . LEU   A 1 43  ? 32.624 4.820   0.220   1.00 14.18 ?  43  LEU   A HB2  1 
ATOM   1163 H HB3  . LEU   A 1 43  ? 31.468 4.483   1.246   1.00 14.18 ?  43  LEU   A HB3  1 
ATOM   1164 H HG   . LEU   A 1 43  ? 32.771 2.575   -0.370  1.00 14.76 ?  43  LEU   A HG   1 
ATOM   1165 H HD11 . LEU   A 1 43  ? 33.691 1.787   1.623   1.00 15.61 ?  43  LEU   A HD11 1 
ATOM   1166 H HD12 . LEU   A 1 43  ? 34.122 3.294   1.365   1.00 15.61 ?  43  LEU   A HD12 1 
ATOM   1167 H HD13 . LEU   A 1 43  ? 32.973 2.964   2.412   1.00 15.61 ?  43  LEU   A HD13 1 
ATOM   1168 H HD21 . LEU   A 1 43  ? 31.559 0.947   0.844   1.00 15.25 ?  43  LEU   A HD21 1 
ATOM   1169 H HD22 . LEU   A 1 43  ? 30.690 2.118   1.476   1.00 15.25 ?  43  LEU   A HD22 1 
ATOM   1170 H HD23 . LEU   A 1 43  ? 30.621 1.830   -0.085  1.00 15.25 ?  43  LEU   A HD23 1 
ATOM   1171 N N    A LYS   A 1 44  ? 29.607 6.461   -1.636  0.72 11.00 ?  44  LYS   A N    1 
ATOM   1172 N N    B LYS   A 1 44  ? 29.597 6.460   -1.630  0.28 12.52 ?  44  LYS   A N    1 
ATOM   1173 C CA   A LYS   A 1 44  ? 28.968 7.776   -1.649  0.72 11.57 ?  44  LYS   A CA   1 
ATOM   1174 C CA   B LYS   A 1 44  ? 28.944 7.768   -1.632  0.28 14.09 ?  44  LYS   A CA   1 
ATOM   1175 C C    A LYS   A 1 44  ? 27.539 7.597   -1.151  0.72 10.81 ?  44  LYS   A C    1 
ATOM   1176 C C    B LYS   A 1 44  ? 27.520 7.572   -1.134  0.28 13.39 ?  44  LYS   A C    1 
ATOM   1177 O O    A LYS   A 1 44  ? 26.676 7.073   -1.863  0.72 12.21 ?  44  LYS   A O    1 
ATOM   1178 O O    B LYS   A 1 44  ? 26.658 7.064   -1.857  0.28 13.58 ?  44  LYS   A O    1 
ATOM   1179 C CB   A LYS   A 1 44  ? 29.016 8.381   -3.045  0.72 13.78 ?  44  LYS   A CB   1 
ATOM   1180 C CB   B LYS   A 1 44  ? 28.976 8.391   -3.023  0.28 16.56 ?  44  LYS   A CB   1 
ATOM   1181 C CG   A LYS   A 1 44  ? 30.393 8.862   -3.468  0.72 17.36 ?  44  LYS   A CG   1 
ATOM   1182 C CG   B LYS   A 1 44  ? 30.341 8.912   -3.440  0.28 19.14 ?  44  LYS   A CG   1 
ATOM   1183 C CD   A LYS   A 1 44  ? 31.032 9.789   -2.438  0.72 22.80 ?  44  LYS   A CD   1 
ATOM   1184 C CD   B LYS   A 1 44  ? 30.957 9.791   -2.358  0.28 21.73 ?  44  LYS   A CD   1 
ATOM   1185 C CE   A LYS   A 1 44  ? 32.334 10.367  -2.956  0.72 26.22 ?  44  LYS   A CE   1 
ATOM   1186 C CE   B LYS   A 1 44  ? 32.291 10.351  -2.792  0.28 23.28 ?  44  LYS   A CE   1 
ATOM   1187 N NZ   A LYS   A 1 44  ? 33.154 10.950  -1.863  0.72 27.94 ?  44  LYS   A NZ   1 
ATOM   1188 N NZ   B LYS   A 1 44  ? 33.180 10.606  -1.627  0.28 23.83 ?  44  LYS   A NZ   1 
ATOM   1189 H H    A LYS   A 1 44  ? 29.481 6.007   -2.358  0.72 13.24 ?  44  LYS   A H    1 
ATOM   1190 H H    B LYS   A 1 44  ? 29.466 6.011   -2.353  0.28 15.07 ?  44  LYS   A H    1 
ATOM   1191 H HA   A LYS   A 1 44  ? 29.423 8.360   -1.024  0.72 13.93 ?  44  LYS   A HA   1 
ATOM   1192 H HA   B LYS   A 1 44  ? 29.385 8.352   -0.997  0.28 16.94 ?  44  LYS   A HA   1 
ATOM   1193 H HB2  A LYS   A 1 44  ? 28.725 7.715   -3.684  0.72 16.57 ?  44  LYS   A HB2  1 
ATOM   1194 H HB2  B LYS   A 1 44  ? 28.705 7.721   -3.673  0.28 19.91 ?  44  LYS   A HB2  1 
ATOM   1195 H HB3  A LYS   A 1 44  ? 28.417 9.145   -3.071  0.72 16.57 ?  44  LYS   A HB3  1 
ATOM   1196 H HB3  B LYS   A 1 44  ? 28.356 9.138   -3.049  0.28 19.91 ?  44  LYS   A HB3  1 
ATOM   1197 H HG2  A LYS   A 1 44  ? 30.977 8.096   -3.587  0.72 20.88 ?  44  LYS   A HG2  1 
ATOM   1198 H HG2  B LYS   A 1 44  ? 30.933 8.161   -3.599  0.28 23.01 ?  44  LYS   A HG2  1 
ATOM   1199 H HG3  A LYS   A 1 44  ? 30.318 9.353   -4.303  0.72 20.88 ?  44  LYS   A HG3  1 
ATOM   1200 H HG3  B LYS   A 1 44  ? 30.247 9.443   -4.248  0.28 23.01 ?  44  LYS   A HG3  1 
ATOM   1201 H HD2  A LYS   A 1 44  ? 30.421 10.514  -2.237  0.72 27.40 ?  44  LYS   A HD2  1 
ATOM   1202 H HD2  B LYS   A 1 44  ? 30.351 10.524  -2.158  0.28 26.11 ?  44  LYS   A HD2  1 
ATOM   1203 H HD3  A LYS   A 1 44  ? 31.231 9.282   -1.632  0.72 27.40 ?  44  LYS   A HD3  1 
ATOM   1204 H HD3  B LYS   A 1 44  ? 31.118 9.261   -1.562  0.28 26.11 ?  44  LYS   A HD3  1 
ATOM   1205 H HE2  A LYS   A 1 44  ? 32.850 9.660   -3.378  0.72 31.51 ?  44  LYS   A HE2  1 
ATOM   1206 H HE2  B LYS   A 1 44  ? 32.730 9.712   -3.374  0.28 27.97 ?  44  LYS   A HE2  1 
ATOM   1207 H HE3  A LYS   A 1 44  ? 32.137 11.065  -3.597  0.72 31.51 ?  44  LYS   A HE3  1 
ATOM   1208 H HE3  B LYS   A 1 44  ? 32.148 11.188  -3.257  0.28 27.97 ?  44  LYS   A HE3  1 
ATOM   1209 H HZ1  A LYS   A 1 44  ? 33.910 11.279  -2.194  0.72 33.57 ?  44  LYS   A HZ1  1 
ATOM   1210 H HZ1  B LYS   A 1 44  ? 33.957 10.936  -1.907  0.28 28.63 ?  44  LYS   A HZ1  1 
ATOM   1211 H HZ2  A LYS   A 1 44  ? 32.703 11.606  -1.463  0.72 33.57 ?  44  LYS   A HZ2  1 
ATOM   1212 H HZ2  B LYS   A 1 44  ? 32.798 11.194  -1.077  0.28 28.63 ?  44  LYS   A HZ2  1 
ATOM   1213 H HZ3  A LYS   A 1 44  ? 33.349 10.324  -1.261  0.72 33.57 ?  44  LYS   A HZ3  1 
ATOM   1214 H HZ3  B LYS   A 1 44  ? 33.327 9.849   -1.184  0.28 28.63 ?  44  LYS   A HZ3  1 
ATOM   1215 N N    A HIS   A 1 45  ? 27.303 7.988   0.097   0.72 10.52 ?  45  HIS   A N    1 
ATOM   1216 N N    B HIS   A 1 45  ? 27.276 7.972   0.110   0.28 13.17 ?  45  HIS   A N    1 
ATOM   1217 C CA   A HIS   A 1 45  ? 26.063 7.646   0.796   0.72 10.86 ?  45  HIS   A CA   1 
ATOM   1218 C CA   B HIS   A 1 45  ? 26.005 7.696   0.776   0.28 13.01 ?  45  HIS   A CA   1 
ATOM   1219 C C    A HIS   A 1 45  ? 25.033 8.768   0.636   0.72 11.85 ?  45  HIS   A C    1 
ATOM   1220 C C    B HIS   A 1 45  ? 25.081 8.883   0.554   0.28 13.37 ?  45  HIS   A C    1 
ATOM   1221 O O    A HIS   A 1 45  ? 24.666 9.475   1.579   0.72 12.65 ?  45  HIS   A O    1 
ATOM   1222 O O    B HIS   A 1 45  ? 25.038 9.824   1.348   0.28 13.86 ?  45  HIS   A O    1 
ATOM   1223 C CB   A HIS   A 1 45  ? 26.359 7.375   2.261   0.72 10.69 ?  45  HIS   A CB   1 
ATOM   1224 C CB   B HIS   A 1 45  ? 26.242 7.444   2.256   0.28 12.37 ?  45  HIS   A CB   1 
ATOM   1225 C CG   A HIS   A 1 45  ? 27.470 6.399   2.481   0.72 10.81 ?  45  HIS   A CG   1 
ATOM   1226 C CG   B HIS   A 1 45  ? 27.370 6.501   2.527   0.28 11.65 ?  45  HIS   A CG   1 
ATOM   1227 N ND1  A HIS   A 1 45  ? 27.454 5.112   1.978   0.72 11.63 ?  45  HIS   A ND1  1 
ATOM   1228 N ND1  B HIS   A 1 45  ? 27.405 5.217   2.024   0.28 11.58 ?  45  HIS   A ND1  1 
ATOM   1229 C CD2  A HIS   A 1 45  ? 28.640 6.534   3.152   0.72 11.11 ?  45  HIS   A CD2  1 
ATOM   1230 C CD2  B HIS   A 1 45  ? 28.511 6.661   3.239   0.28 11.15 ?  45  HIS   A CD2  1 
ATOM   1231 C CE1  A HIS   A 1 45  ? 28.568 4.500   2.342   0.72 11.46 ?  45  HIS   A CE1  1 
ATOM   1232 C CE1  B HIS   A 1 45  ? 28.517 4.626   2.423   0.28 10.86 ?  45  HIS   A CE1  1 
ATOM   1233 N NE2  A HIS   A 1 45  ? 29.304 5.339   3.051   0.72 11.45 ?  45  HIS   A NE2  1 
ATOM   1234 N NE2  B HIS   A 1 45  ? 29.205 5.480   3.161   0.28 10.74 ?  45  HIS   A NE2  1 
ATOM   1235 H H    A HIS   A 1 45  ? 27.845 8.467   0.567   0.72 12.67 ?  45  HIS   A H    1 
ATOM   1236 H H    B HIS   A 1 45  ? 27.835 8.419   0.596   0.28 15.84 ?  45  HIS   A H    1 
ATOM   1237 H HA   A HIS   A 1 45  ? 25.692 6.839   0.410   0.72 13.07 ?  45  HIS   A HA   1 
ATOM   1238 H HA   B HIS   A 1 45  ? 25.602 6.905   0.386   0.28 15.65 ?  45  HIS   A HA   1 
ATOM   1239 H HB2  A HIS   A 1 45  ? 26.603 8.206   2.694   0.72 12.87 ?  45  HIS   A HB2  1 
ATOM   1240 H HB2  B HIS   A 1 45  ? 26.449 8.288   2.688   0.28 14.89 ?  45  HIS   A HB2  1 
ATOM   1241 H HB3  A HIS   A 1 45  ? 25.559 7.010   2.680   0.72 12.87 ?  45  HIS   A HB3  1 
ATOM   1242 H HB3  B HIS   A 1 45  ? 25.436 7.067   2.642   0.28 14.89 ?  45  HIS   A HB3  1 
ATOM   1243 H HD2  A HIS   A 1 45  ? 28.941 7.296   3.594   0.72 13.37 ?  45  HIS   A HD2  1 
ATOM   1244 H HD2  B HIS   A 1 45  ? 28.771 7.430   3.695   0.28 13.42 ?  45  HIS   A HD2  1 
ATOM   1245 H HE1  A HIS   A 1 45  ? 28.794 3.618   2.143   0.72 13.79 ?  45  HIS   A HE1  1 
ATOM   1246 H HE1  B HIS   A 1 45  ? 28.770 3.758   2.222   0.28 13.07 ?  45  HIS   A HE1  1 
ATOM   1247 H HE2  A HIS   A 1 45  ? 30.077 5.163   3.394   0.72 13.78 ?  45  HIS   A HE2  1 
ATOM   1248 H HE2  B HIS   A 1 45  ? 29.963 5.325   3.531   0.28 12.92 ?  45  HIS   A HE2  1 
ATOM   1249 N N    A GLY   A 1 46  ? 24.548 8.914   -0.592  0.72 13.32 ?  46  GLY   A N    1 
ATOM   1250 N N    B GLY   A 1 46  ? 24.328 8.842   -0.540  0.28 13.22 ?  46  GLY   A N    1 
ATOM   1251 C CA   A GLY   A 1 46  ? 23.758 10.083  -0.936  0.72 14.37 ?  46  GLY   A CA   1 
ATOM   1252 C CA   B GLY   A 1 46  ? 23.473 9.960   -0.884  0.28 12.81 ?  46  GLY   A CA   1 
ATOM   1253 C C    A GLY   A 1 46  ? 22.264 9.955   -0.711  0.72 14.24 ?  46  GLY   A C    1 
ATOM   1254 C C    B GLY   A 1 46  ? 22.025 9.806   -0.466  0.28 12.17 ?  46  GLY   A C    1 
ATOM   1255 O O    A GLY   A 1 46  ? 21.587 10.955  -0.447  0.72 14.71 ?  46  GLY   A O    1 
ATOM   1256 O O    B GLY   A 1 46  ? 21.420 10.757  0.040   0.28 12.31 ?  46  GLY   A O    1 
ATOM   1257 H H    A GLY   A 1 46  ? 24.650 8.350   -1.230  0.72 16.02 ?  46  GLY   A H    1 
ATOM   1258 H H    B GLY   A 1 46  ? 24.305 8.186   -1.099  0.28 15.91 ?  46  GLY   A H    1 
ATOM   1259 H HA2  A GLY   A 1 46  ? 24.077 10.838  -0.415  0.72 17.28 ?  46  GLY   A HA2  1 
ATOM   1260 H HA2  B GLY   A 1 46  ? 23.818 10.762  -0.460  0.28 15.42 ?  46  GLY   A HA2  1 
ATOM   1261 H HA3  A GLY   A 1 46  ? 23.898 10.286  -1.872  0.72 17.28 ?  46  GLY   A HA3  1 
ATOM   1262 H HA3  B GLY   A 1 46  ? 23.500 10.091  -1.841  0.28 15.42 ?  46  GLY   A HA3  1 
ATOM   1263 N N    A GLY   A 1 47  ? 21.734 8.746   -0.845  0.72 13.82 ?  47  GLY   A N    1 
ATOM   1264 N N    B GLY   A 1 47  ? 21.450 8.623   -0.674  0.28 12.18 ?  47  GLY   A N    1 
ATOM   1265 C CA   A GLY   A 1 47  ? 20.300 8.543   -0.819  0.72 13.87 ?  47  GLY   A CA   1 
ATOM   1266 C CA   B GLY   A 1 47  ? 20.034 8.431   -0.449  0.28 12.22 ?  47  GLY   A CA   1 
ATOM   1267 C C    A GLY   A 1 47  ? 19.979 7.105   -0.472  0.72 13.19 ?  47  GLY   A C    1 
ATOM   1268 C C    B GLY   A 1 47  ? 19.703 6.998   -0.093  0.28 11.36 ?  47  GLY   A C    1 
ATOM   1269 O O    A GLY   A 1 47  ? 20.866 6.284   -0.224  0.72 13.56 ?  47  GLY   A O    1 
ATOM   1270 O O    B GLY   A 1 47  ? 20.585 6.145   0.042   0.28 11.28 ?  47  GLY   A O    1 
ATOM   1271 H H    A GLY   A 1 47  ? 22.188 8.029   -0.935  0.72 16.62 ?  47  GLY   A H    1 
ATOM   1272 H H    B GLY   A 1 47  ? 21.868 7.917   -0.938  0.28 14.66 ?  47  GLY   A H    1 
ATOM   1273 H HA2  A GLY   A 1 47  ? 19.888 9.134   -0.161  0.72 16.69 ?  47  GLY   A HA2  1 
ATOM   1274 H HA2  B GLY   A 1 47  ? 19.739 9.002   0.275   0.28 14.71 ?  47  GLY   A HA2  1 
ATOM   1275 H HA3  A GLY   A 1 47  ? 19.929 8.752   -1.694  0.72 16.69 ?  47  GLY   A HA3  1 
ATOM   1276 H HA3  B GLY   A 1 47  ? 19.543 8.669   -1.251  0.28 14.71 ?  47  GLY   A HA3  1 
ATOM   1277 N N    A GLY   A 1 48  ? 18.687 6.799   -0.476  0.72 12.72 ?  48  GLY   A N    1 
ATOM   1278 N N    B GLY   A 1 48  ? 18.403 6.738   0.048   0.28 11.04 ?  48  GLY   A N    1 
ATOM   1279 C CA   A GLY   A 1 48  ? 18.268 5.466   -0.107  0.72 12.71 ?  48  GLY   A CA   1 
ATOM   1280 C CA   B GLY   A 1 48  ? 17.958 5.416   0.452   0.28 10.63 ?  48  GLY   A CA   1 
ATOM   1281 C C    A GLY   A 1 48  ? 18.650 5.150   1.324   0.72 11.88 ?  48  GLY   A C    1 
ATOM   1282 C C    B GLY   A 1 48  ? 18.538 5.041   1.801   0.28 10.77 ?  48  GLY   A C    1 
ATOM   1283 O O    A GLY   A 1 48  ? 18.789 6.042   2.174   0.72 12.16 ?  48  GLY   A O    1 
ATOM   1284 O O    B GLY   A 1 48  ? 18.666 5.873   2.708   0.28 10.72 ?  48  GLY   A O    1 
ATOM   1285 H H    A GLY   A 1 48  ? 18.058 7.336   -0.683  0.72 15.30 ?  48  GLY   A H    1 
ATOM   1286 H H    B GLY   A 1 48  ? 17.759 7.303   -0.084  0.28 13.28 ?  48  GLY   A H    1 
ATOM   1287 H HA2  A GLY   A 1 48  ? 17.315 5.387   -0.192  0.72 15.30 ?  48  GLY   A HA2  1 
ATOM   1288 H HA2  B GLY   A 1 48  ? 16.985 5.390   0.502   0.28 12.79 ?  48  GLY   A HA2  1 
ATOM   1289 H HA3  A GLY   A 1 48  ? 18.698 4.814   -0.681  0.72 15.30 ?  48  GLY   A HA3  1 
ATOM   1290 H HA3  B GLY   A 1 48  ? 18.246 4.757   -0.202  0.28 12.79 ?  48  GLY   A HA3  1 
ATOM   1291 N N    A VAL   A 1 49  ? 18.822 3.853   1.597   0.72 12.48 ?  49  VAL   A N    1 
ATOM   1292 N N    B VAL   A 1 49  ? 18.901 3.765   1.933   0.28 10.77 ?  49  VAL   A N    1 
ATOM   1293 C CA   A VAL   A 1 49  ? 19.267 3.418   2.919   0.72 12.62 ?  49  VAL   A CA   1 
ATOM   1294 C CA   B VAL   A 1 49  ? 19.491 3.266   3.172   0.28 10.95 ?  49  VAL   A CA   1 
ATOM   1295 C C    A VAL   A 1 49  ? 20.593 4.074   3.293   0.72 11.75 ?  49  VAL   A C    1 
ATOM   1296 C C    B VAL   A 1 49  ? 20.756 4.043   3.518   0.28 10.50 ?  49  VAL   A C    1 
ATOM   1297 O O    A VAL   A 1 49  ? 20.791 4.474   4.443   0.72 12.20 ?  49  VAL   A O    1 
ATOM   1298 O O    B VAL   A 1 49  ? 20.947 4.471   4.663   0.28 10.49 ?  49  VAL   A O    1 
ATOM   1299 C CB   A VAL   A 1 49  ? 19.357 1.879   2.972   0.72 13.60 ?  49  VAL   A CB   1 
ATOM   1300 C CB   B VAL   A 1 49  ? 19.773 1.758   3.050   0.28 11.63 ?  49  VAL   A CB   1 
ATOM   1301 C CG1  A VAL   A 1 49  ? 20.113 1.412   4.221   0.72 14.42 ?  49  VAL   A CG1  1 
ATOM   1302 C CG1  B VAL   A 1 49  ? 20.589 1.277   4.240   0.28 11.36 ?  49  VAL   A CG1  1 
ATOM   1303 C CG2  A VAL   A 1 49  ? 17.963 1.261   2.926   0.72 15.05 ?  49  VAL   A CG2  1 
ATOM   1304 C CG2  B VAL   A 1 49  ? 18.475 0.975   2.926   0.28 12.51 ?  49  VAL   A CG2  1 
ATOM   1305 H H    A VAL   A 1 49  ? 18.694 3.209   1.041   0.72 15.02 ?  49  VAL   A H    1 
ATOM   1306 H H    B VAL   A 1 49  ? 18.818 3.170   1.319   0.28 12.96 ?  49  VAL   A H    1 
ATOM   1307 H HA   A VAL   A 1 49  ? 18.611 3.684   3.579   0.72 15.18 ?  49  VAL   A HA   1 
ATOM   1308 H HA   B VAL   A 1 49  ? 18.861 3.391   3.897   0.28 13.18 ?  49  VAL   A HA   1 
ATOM   1309 H HB   A VAL   A 1 49  ? 19.850 1.558   2.201   0.72 16.36 ?  49  VAL   A HB   1 
ATOM   1310 H HB   B VAL   A 1 49  ? 20.295 1.597   2.247   0.28 13.99 ?  49  VAL   A HB   1 
ATOM   1311 H HG11 A VAL   A 1 49  ? 19.921 0.472   4.376   0.72 17.35 ?  49  VAL   A HG11 1 
ATOM   1312 H HG11 B VAL   A 1 49  ? 20.504 0.313   4.311   0.28 13.67 ?  49  VAL   A HG11 1 
ATOM   1313 H HG12 A VAL   A 1 49  ? 21.063 1.536   4.087   0.72 17.35 ?  49  VAL   A HG12 1 
ATOM   1314 H HG12 B VAL   A 1 49  ? 21.521 1.514   4.104   0.28 13.67 ?  49  VAL   A HG12 1 
ATOM   1315 H HG13 A VAL   A 1 49  ? 19.811 1.934   4.984   0.72 17.35 ?  49  VAL   A HG13 1 
ATOM   1316 H HG13 B VAL   A 1 49  ? 20.251 1.697   5.045   0.28 13.67 ?  49  VAL   A HG13 1 
ATOM   1317 H HG21 A VAL   A 1 49  ? 18.043 0.293   2.957   0.72 18.09 ?  49  VAL   A HG21 1 
ATOM   1318 H HG21 B VAL   A 1 49  ? 18.683 0.039   2.782   0.28 15.04 ?  49  VAL   A HG21 1 
ATOM   1319 H HG22 A VAL   A 1 49  ? 17.456 1.573   3.691   0.72 18.09 ?  49  VAL   A HG22 1 
ATOM   1320 H HG22 B VAL   A 1 49  ? 17.967 1.079   3.746   0.28 15.04 ?  49  VAL   A HG22 1 
ATOM   1321 H HG23 A VAL   A 1 49  ? 17.530 1.531   2.105   0.72 18.09 ?  49  VAL   A HG23 1 
ATOM   1322 H HG23 B VAL   A 1 49  ? 17.968 1.320   2.174   0.28 15.04 ?  49  VAL   A HG23 1 
ATOM   1323 N N    A ALA   A 1 50  ? 21.539 4.139   2.350   0.72 11.09 ?  50  ALA   A N    1 
ATOM   1324 N N    B ALA   A 1 50  ? 21.651 4.211   2.540   0.28 10.09 ?  50  ALA   A N    1 
ATOM   1325 C CA   A ALA   A 1 50  ? 22.859 4.685   2.658   0.72 11.05 ?  50  ALA   A CA   1 
ATOM   1326 C CA   B ALA   A 1 50  ? 22.960 4.791   2.826   0.28 10.13 ?  50  ALA   A CA   1 
ATOM   1327 C C    A ALA   A 1 50  ? 22.770 6.147   3.063   0.72 11.25 ?  50  ALA   A C    1 
ATOM   1328 C C    B ALA   A 1 50  ? 22.833 6.233   3.296   0.28 9.98  ?  50  ALA   A C    1 
ATOM   1329 O O    A ALA   A 1 50  ? 23.413 6.576   4.028   0.72 11.63 ?  50  ALA   A O    1 
ATOM   1330 O O    B ALA   A 1 50  ? 23.439 6.626   4.301   0.28 9.66  ?  50  ALA   A O    1 
ATOM   1331 C CB   A ALA   A 1 50  ? 23.777 4.531   1.451   0.72 11.50 ?  50  ALA   A CB   1 
ATOM   1332 C CB   B ALA   A 1 50  ? 23.852 4.699   1.588   0.28 10.04 ?  50  ALA   A CB   1 
ATOM   1333 H H    A ALA   A 1 50  ? 21.438 3.873   1.544   0.72 13.34 ?  50  ALA   A H    1 
ATOM   1334 H H    B ALA   A 1 50  ? 21.519 4.012   1.712   0.28 12.14 ?  50  ALA   A H    1 
ATOM   1335 H HA   A ALA   A 1 50  ? 23.239 4.193   3.405   0.72 13.30 ?  50  ALA   A HA   1 
ATOM   1336 H HA   B ALA   A 1 50  ? 23.377 4.291   3.538   0.28 12.20 ?  50  ALA   A HA   1 
ATOM   1337 H HB1  A ALA   A 1 50  ? 24.645 4.900   1.673   0.72 13.84 ?  50  ALA   A HB1  1 
ATOM   1338 H HB1  B ALA   A 1 50  ? 24.723 5.070   1.798   0.28 12.08 ?  50  ALA   A HB1  1 
ATOM   1339 H HB2  A ALA   A 1 50  ? 23.857 3.590   1.238   0.72 13.84 ?  50  ALA   A HB2  1 
ATOM   1340 H HB2  B ALA   A 1 50  ? 23.942 3.767   1.336   0.28 12.08 ?  50  ALA   A HB2  1 
ATOM   1341 H HB3  A ALA   A 1 50  ? 23.390 5.012   0.705   0.72 13.84 ?  50  ALA   A HB3  1 
ATOM   1342 H HB3  B ALA   A 1 50  ? 23.444 5.199   0.864   0.28 12.08 ?  50  ALA   A HB3  1 
ATOM   1343 N N    A GLY   A 1 51  ? 21.998 6.937   2.318   0.72 10.91 ?  51  GLY   A N    1 
ATOM   1344 N N    B GLY   A 1 51  ? 22.046 7.037   2.579   0.28 10.74 ?  51  GLY   A N    1 
ATOM   1345 C CA   A GLY   A 1 51  ? 21.832 8.330   2.686   0.72 11.73 ?  51  GLY   A CA   1 
ATOM   1346 C CA   B GLY   A 1 51  ? 21.877 8.423   2.977   0.28 10.71 ?  51  GLY   A CA   1 
ATOM   1347 C C    A GLY   A 1 51  ? 21.232 8.488   4.067   0.72 11.13 ?  51  GLY   A C    1 
ATOM   1348 C C    B GLY   A 1 51  ? 21.243 8.552   4.348   0.28 10.97 ?  51  GLY   A C    1 
ATOM   1349 O O    A GLY   A 1 51  ? 21.628 9.376   4.829   0.72 11.95 ?  51  GLY   A O    1 
ATOM   1350 O O    B GLY   A 1 51  ? 21.597 9.441   5.128   0.28 11.12 ?  51  GLY   A O    1 
ATOM   1351 H H    A GLY   A 1 51  ? 21.574 6.695   1.614   0.72 13.13 ?  51  GLY   A H    1 
ATOM   1352 H H    B GLY   A 1 51  ? 21.600 6.805   1.876   0.28 12.93 ?  51  GLY   A H    1 
ATOM   1353 H HA2  A GLY   A 1 51  ? 22.691 8.776   2.677   0.72 14.11 ?  51  GLY   A HA2  1 
ATOM   1354 H HA2  B GLY   A 1 51  ? 22.743 8.860   2.990   0.28 12.89 ?  51  GLY   A HA2  1 
ATOM   1355 H HA3  A GLY   A 1 51  ? 21.247 8.769   2.050   0.72 14.11 ?  51  GLY   A HA3  1 
ATOM   1356 H HA3  B GLY   A 1 51  ? 21.316 8.880   2.324   0.28 12.89 ?  51  GLY   A HA3  1 
ATOM   1357 N N    A ALA   A 1 52  ? 20.260 7.633   4.405   0.72 11.29 ?  52  ALA   A N    1 
ATOM   1358 N N    B ALA   A 1 52  ? 20.306 7.656   4.665   0.28 11.28 ?  52  ALA   A N    1 
ATOM   1359 C CA   A ALA   A 1 52  ? 19.614 7.700   5.711   0.72 12.20 ?  52  ALA   A CA   1 
ATOM   1360 C CA   B ALA   A 1 52  ? 19.630 7.715   5.955   0.28 11.80 ?  52  ALA   A CA   1 
ATOM   1361 C C    A ALA   A 1 52  ? 20.563 7.277   6.831   0.72 11.73 ?  52  ALA   A C    1 
ATOM   1362 C C    B ALA   A 1 52  ? 20.559 7.287   7.089   0.28 11.20 ?  52  ALA   A C    1 
ATOM   1363 O O    A ALA   A 1 52  ? 20.637 7.937   7.872   0.72 12.41 ?  52  ALA   A O    1 
ATOM   1364 O O    B ALA   A 1 52  ? 20.595 7.928   8.145   0.28 11.75 ?  52  ALA   A O    1 
ATOM   1365 C CB   A ALA   A 1 52  ? 18.347 6.842   5.706   0.72 13.51 ?  52  ALA   A CB   1 
ATOM   1366 C CB   B ALA   A 1 52  ? 18.371 6.851   5.917   0.28 12.58 ?  52  ALA   A CB   1 
ATOM   1367 H H    A ALA   A 1 52  ? 19.974 7.001   3.902   0.72 13.58 ?  52  ALA   A H    1 
ATOM   1368 H H    B ALA   A 1 52  ? 20.058 7.010   4.153   0.28 13.57 ?  52  ALA   A H    1 
ATOM   1369 H HA   A ALA   A 1 52  ? 19.347 8.612   5.880   0.72 14.68 ?  52  ALA   A HA   1 
ATOM   1370 H HA   B ALA   A 1 52  ? 19.360 8.630   6.116   0.28 14.20 ?  52  ALA   A HA   1 
ATOM   1371 H HB1  A ALA   A 1 52  ? 17.923 6.894   6.580   0.72 16.24 ?  52  ALA   A HB1  1 
ATOM   1372 H HB1  B ALA   A 1 52  ? 17.899 6.949   6.757   0.28 15.13 ?  52  ALA   A HB1  1 
ATOM   1373 H HB2  A ALA   A 1 52  ? 17.741 7.175   5.027   0.72 16.24 ?  52  ALA   A HB2  1 
ATOM   1374 H HB2  B ALA   A 1 52  ? 17.807 7.148   5.185   0.28 15.13 ?  52  ALA   A HB2  1 
ATOM   1375 H HB3  A ALA   A 1 52  ? 18.584 5.920   5.513   0.72 16.24 ?  52  ALA   A HB3  1 
ATOM   1376 H HB3  B ALA   A 1 52  ? 18.625 5.925   5.781   0.28 15.13 ?  52  ALA   A HB3  1 
ATOM   1377 N N    A LEU   A 1 53  ? 21.285 6.169   6.653   0.72 11.63 ?  53  LEU   A N    1 
ATOM   1378 N N    B LEU   A 1 53  ? 21.313 6.202   6.895   0.28 10.81 ?  53  LEU   A N    1 
ATOM   1379 C CA   A LEU   A 1 53  ? 22.236 5.749   7.681   0.72 12.02 ?  53  LEU   A CA   1 
ATOM   1380 C CA   B LEU   A 1 53  ? 22.298 5.805   7.898   0.28 10.99 ?  53  LEU   A CA   1 
ATOM   1381 C C    A LEU   A 1 53  ? 23.294 6.820   7.892   0.72 11.06 ?  53  LEU   A C    1 
ATOM   1382 C C    B LEU   A 1 53  ? 23.327 6.909   8.106   0.28 11.37 ?  53  LEU   A C    1 
ATOM   1383 O O    A LEU   A 1 53  ? 23.616 7.175   9.028   0.72 12.09 ?  53  LEU   A O    1 
ATOM   1384 O O    B LEU   A 1 53  ? 23.639 7.279   9.244   0.28 12.35 ?  53  LEU   A O    1 
ATOM   1385 C CB   A LEU   A 1 53  ? 22.889 4.412   7.312   0.72 12.88 ?  53  LEU   A CB   1 
ATOM   1386 C CB   B LEU   A 1 53  ? 22.990 4.501   7.485   0.28 11.01 ?  53  LEU   A CB   1 
ATOM   1387 C CG   A LEU   A 1 53  ? 21.993 3.169   7.355   0.72 13.21 ?  53  LEU   A CG   1 
ATOM   1388 C CG   B LEU   A 1 53  ? 22.212 3.181   7.536   0.28 11.27 ?  53  LEU   A CG   1 
ATOM   1389 C CD1  A LEU   A 1 53  ? 22.708 1.973   6.758   0.72 12.97 ?  53  LEU   A CD1  1 
ATOM   1390 C CD1  B LEU   A 1 53  ? 23.058 2.051   6.965   0.28 11.72 ?  53  LEU   A CD1  1 
ATOM   1391 C CD2  A LEU   A 1 53  ? 21.539 2.858   8.774   0.72 14.99 ?  53  LEU   A CD2  1 
ATOM   1392 C CD2  B LEU   A 1 53  ? 21.778 2.845   8.951   0.28 11.78 ?  53  LEU   A CD2  1 
ATOM   1393 H H    A LEU   A 1 53  ? 21.251 5.659   5.966   0.72 13.99 ?  53  LEU   A H    1 
ATOM   1394 H H    B LEU   A 1 53  ? 21.272 5.692   6.202   0.28 13.01 ?  53  LEU   A H    1 
ATOM   1395 H HA   A LEU   A 1 53  ? 21.764 5.628   8.520   0.72 14.46 ?  53  LEU   A HA   1 
ATOM   1396 H HA   B LEU   A 1 53  ? 21.846 5.657   8.737   0.28 13.23 ?  53  LEU   A HA   1 
ATOM   1397 H HB2  A LEU   A 1 53  ? 23.239 4.484   6.409   0.72 15.49 ?  53  LEU   A HB2  1 
ATOM   1398 H HB2  B LEU   A 1 53  ? 23.296 4.607   6.571   0.28 13.25 ?  53  LEU   A HB2  1 
ATOM   1399 H HB3  A LEU   A 1 53  ? 23.627 4.253   7.925   0.72 15.49 ?  53  LEU   A HB3  1 
ATOM   1400 H HB3  B LEU   A 1 53  ? 23.762 4.388   8.061   0.28 13.25 ?  53  LEU   A HB3  1 
ATOM   1401 H HG   A LEU   A 1 53  ? 21.202 3.339   6.818   0.72 15.89 ?  53  LEU   A HG   1 
ATOM   1402 H HG   B LEU   A 1 53  ? 21.419 3.262   6.985   0.28 13.56 ?  53  LEU   A HG   1 
ATOM   1403 H HD11 A LEU   A 1 53  ? 22.118 1.204   6.798   0.72 15.60 ?  53  LEU   A HD11 1 
ATOM   1404 H HD11 B LEU   A 1 53  ? 22.550 1.225   7.006   0.28 14.10 ?  53  LEU   A HD11 1 
ATOM   1405 H HD12 A LEU   A 1 53  ? 22.938 2.170   5.838   0.72 15.60 ?  53  LEU   A HD12 1 
ATOM   1406 H HD12 B LEU   A 1 53  ? 23.283 2.256   6.044   0.28 14.10 ?  53  LEU   A HD12 1 
ATOM   1407 H HD13 A LEU   A 1 53  ? 23.512 1.801   7.273   0.72 15.60 ?  53  LEU   A HD13 1 
ATOM   1408 H HD13 B LEU   A 1 53  ? 23.869 1.966   7.492   0.28 14.10 ?  53  LEU   A HD13 1 
ATOM   1409 H HD21 A LEU   A 1 53  ? 21.036 2.028   8.770   0.72 18.02 ?  53  LEU   A HD21 1 
ATOM   1410 H HD21 B LEU   A 1 53  ? 21.262 2.023   8.934   0.28 14.17 ?  53  LEU   A HD21 1 
ATOM   1411 H HD22 A LEU   A 1 53  ? 22.319 2.769   9.343   0.72 18.02 ?  53  LEU   A HD22 1 
ATOM   1412 H HD22 B LEU   A 1 53  ? 22.564 2.732   9.504   0.28 14.17 ?  53  LEU   A HD22 1 
ATOM   1413 H HD23 A LEU   A 1 53  ? 20.978 3.582   9.094   0.72 18.02 ?  53  LEU   A HD23 1 
ATOM   1414 H HD23 B LEU   A 1 53  ? 21.230 3.569   9.293   0.28 14.17 ?  53  LEU   A HD23 1 
ATOM   1415 N N    A ASN   A 1 54  ? 23.838 7.357   6.803   0.72 10.82 ?  54  ASN   A N    1 
ATOM   1416 N N    B ASN   A 1 54  ? 23.854 7.457   7.010   0.28 11.85 ?  54  ASN   A N    1 
ATOM   1417 C CA   A ASN   A 1 54  ? 24.895 8.347   6.949   0.72 10.96 ?  54  ASN   A CA   1 
ATOM   1418 C CA   B ASN   A 1 54  ? 24.897 8.467   7.133   0.28 11.95 ?  54  ASN   A CA   1 
ATOM   1419 C C    A ASN   A 1 54  ? 24.387 9.601   7.665   0.72 11.51 ?  54  ASN   A C    1 
ATOM   1420 C C    B ASN   A 1 54  ? 24.375 9.709   7.843   0.28 11.74 ?  54  ASN   A C    1 
ATOM   1421 O O    A ASN   A 1 54  ? 25.079 10.157  8.528   0.72 12.12 ?  54  ASN   A O    1 
ATOM   1422 O O    B ASN   A 1 54  ? 25.043 10.258  8.728   0.28 11.51 ?  54  ASN   A O    1 
ATOM   1423 C CB   A ASN   A 1 54  ? 25.480 8.700   5.591   0.72 11.24 ?  54  ASN   A CB   1 
ATOM   1424 C CB   B ASN   A 1 54  ? 25.455 8.824   5.758   0.28 11.85 ?  54  ASN   A CB   1 
ATOM   1425 C CG   A ASN   A 1 54  ? 26.506 9.791   5.704   0.72 11.61 ?  54  ASN   A CG   1 
ATOM   1426 C CG   B ASN   A 1 54  ? 26.449 9.960   5.826   0.28 11.13 ?  54  ASN   A CG   1 
ATOM   1427 O OD1  A ASN   A 1 54  ? 27.493 9.647   6.437   0.72 11.88 ?  54  ASN   A OD1  1 
ATOM   1428 O OD1  B ASN   A 1 54  ? 27.513 9.827   6.433   0.28 10.59 ?  54  ASN   A OD1  1 
ATOM   1429 N ND2  A ASN   A 1 54  ? 26.283 10.901  5.016   0.72 12.03 ?  54  ASN   A ND2  1 
ATOM   1430 N ND2  B ASN   A 1 54  ? 26.108 11.090  5.221   0.28 11.10 ?  54  ASN   A ND2  1 
ATOM   1431 H H    A ASN   A 1 54  ? 23.611 7.173   5.998   0.72 13.02 ?  54  ASN   A H    1 
ATOM   1432 H H    B ASN   A 1 54  ? 23.619 7.277   6.201   0.28 14.26 ?  54  ASN   A H    1 
ATOM   1433 H HA   A ASN   A 1 54  ? 25.598 7.966   7.491   0.72 13.19 ?  54  ASN   A HA   1 
ATOM   1434 H HA   B ASN   A 1 54  ? 25.621 8.110   7.662   0.28 14.38 ?  54  ASN   A HA   1 
ATOM   1435 H HB2  A ASN   A 1 54  ? 25.907 7.912   5.221   0.72 13.53 ?  54  ASN   A HB2  1 
ATOM   1436 H HB2  B ASN   A 1 54  ? 25.908 8.047   5.388   0.28 14.26 ?  54  ASN   A HB2  1 
ATOM   1437 H HB3  A ASN   A 1 54  ? 24.772 9.008   5.009   0.72 13.53 ?  54  ASN   A HB3  1 
ATOM   1438 H HB3  B ASN   A 1 54  ? 24.728 9.093   5.175   0.28 14.26 ?  54  ASN   A HB3  1 
ATOM   1439 H HD21 A ASN   A 1 54  ? 26.844 11.547  5.058   0.72 14.47 ?  54  ASN   A HD21 1 
ATOM   1440 H HD21 B ASN   A 1 54  ? 26.642 11.764  5.235   0.28 13.36 ?  54  ASN   A HD21 1 
ATOM   1441 H HD22 A ASN   A 1 54  ? 25.581 10.963  4.526   0.72 14.47 ?  54  ASN   A HD22 1 
ATOM   1442 H HD22 B ASN   A 1 54  ? 25.355 11.146  4.809   0.28 13.36 ?  54  ASN   A HD22 1 
ATOM   1443 N N    A LYS   A 1 55  ? 23.179 10.065  7.321   0.72 11.57 ?  55  LYS   A N    1 
ATOM   1444 N N    B LYS   A 1 55  ? 23.177 10.166  7.469   0.28 11.86 ?  55  LYS   A N    1 
ATOM   1445 C CA   A LYS   A 1 55  ? 22.604 11.232  7.986   0.72 12.24 ?  55  LYS   A CA   1 
ATOM   1446 C CA   B LYS   A 1 55  ? 22.571 11.299  8.159   0.28 12.69 ?  55  LYS   A CA   1 
ATOM   1447 C C    A LYS   A 1 55  ? 22.508 11.011  9.490   0.72 12.31 ?  55  LYS   A C    1 
ATOM   1448 C C    B LYS   A 1 55  ? 22.455 11.023  9.652   0.28 12.98 ?  55  LYS   A C    1 
ATOM   1449 O O    A LYS   A 1 55  ? 22.804 11.914  10.282  0.72 13.27 ?  55  LYS   A O    1 
ATOM   1450 O O    B LYS   A 1 55  ? 22.699 11.909  10.479  0.28 13.05 ?  55  LYS   A O    1 
ATOM   1451 C CB   A LYS   A 1 55  ? 21.228 11.533  7.385   0.72 12.76 ?  55  LYS   A CB   1 
ATOM   1452 C CB   B LYS   A 1 55  ? 21.198 11.581  7.550   0.28 13.75 ?  55  LYS   A CB   1 
ATOM   1453 C CG   A LYS   A 1 55  ? 20.551 12.800  7.910   0.72 14.11 ?  55  LYS   A CG   1 
ATOM   1454 C CG   B LYS   A 1 55  ? 20.347 12.570  8.323   0.28 14.57 ?  55  LYS   A CG   1 
ATOM   1455 C CD   A LYS   A 1 55  ? 19.187 13.008  7.243   0.72 15.33 ?  55  LYS   A CD   1 
ATOM   1456 C CD   B LYS   A 1 55  ? 18.996 12.757  7.649   0.28 16.18 ?  55  LYS   A CD   1 
ATOM   1457 C CE   A LYS   A 1 55  ? 18.375 14.120  7.892   0.72 16.85 ?  55  LYS   A CE   1 
ATOM   1458 C CE   B LYS   A 1 55  ? 18.113 13.723  8.416   0.28 17.54 ?  55  LYS   A CE   1 
ATOM   1459 N NZ   A LYS   A 1 55  ? 17.034 14.263  7.251   0.72 17.49 ?  55  LYS   A NZ   1 
ATOM   1460 N NZ   B LYS   A 1 55  ? 16.754 13.821  7.818   0.28 18.39 ?  55  LYS   A NZ   1 
ATOM   1461 H H    A LYS   A 1 55  ? 22.674 9.717   6.720   0.72 13.92 ?  55  LYS   A H    1 
ATOM   1462 H H    B LYS   A 1 55  ? 22.696 9.835   6.834   0.28 14.28 ?  55  LYS   A H    1 
ATOM   1463 H HA   A LYS   A 1 55  ? 23.175 11.999  7.829   0.72 14.72 ?  55  LYS   A HA   1 
ATOM   1464 H HA   B LYS   A 1 55  ? 23.126 12.085  8.031   0.28 15.27 ?  55  LYS   A HA   1 
ATOM   1465 H HB2  A LYS   A 1 55  ? 21.322 11.627  6.426   0.72 15.35 ?  55  LYS   A HB2  1 
ATOM   1466 H HB2  B LYS   A 1 55  ? 21.323 11.940  6.657   0.28 16.54 ?  55  LYS   A HB2  1 
ATOM   1467 H HB3  A LYS   A 1 55  ? 20.634 10.789  7.582   0.72 15.35 ?  55  LYS   A HB3  1 
ATOM   1468 H HB3  B LYS   A 1 55  ? 20.705 10.748  7.500   0.28 16.54 ?  55  LYS   A HB3  1 
ATOM   1469 H HG2  A LYS   A 1 55  ? 20.417 12.726  8.865   0.72 16.97 ?  55  LYS   A HG2  1 
ATOM   1470 H HG2  B LYS   A 1 55  ? 20.191 12.236  9.220   0.28 17.52 ?  55  LYS   A HG2  1 
ATOM   1471 H HG3  A LYS   A 1 55  ? 21.111 13.569  7.705   0.72 16.97 ?  55  LYS   A HG3  1 
ATOM   1472 H HG3  B LYS   A 1 55  ? 20.798 13.427  8.354   0.28 17.52 ?  55  LYS   A HG3  1 
ATOM   1473 H HD2  A LYS   A 1 55  ? 19.324 13.240  6.310   0.72 18.44 ?  55  LYS   A HD2  1 
ATOM   1474 H HD2  B LYS   A 1 55  ? 19.133 13.109  6.756   0.28 19.46 ?  55  LYS   A HD2  1 
ATOM   1475 H HD3  A LYS   A 1 55  ? 18.679 12.185  7.308   0.72 18.44 ?  55  LYS   A HD3  1 
ATOM   1476 H HD3  B LYS   A 1 55  ? 18.543 11.899  7.603   0.28 19.46 ?  55  LYS   A HD3  1 
ATOM   1477 H HE2  A LYS   A 1 55  ? 18.242 13.913  8.831   0.72 20.26 ?  55  LYS   A HE2  1 
ATOM   1478 H HE2  B LYS   A 1 55  ? 18.022 13.414  9.332   0.28 21.08 ?  55  LYS   A HE2  1 
ATOM   1479 H HE3  A LYS   A 1 55  ? 18.849 14.961  7.798   0.72 20.26 ?  55  LYS   A HE3  1 
ATOM   1480 H HE3  B LYS   A 1 55  ? 18.518 14.605  8.400   0.28 21.08 ?  55  LYS   A HE3  1 
ATOM   1481 H HZ1  A LYS   A 1 55  ? 16.476 14.684  7.802   0.72 21.03 ?  55  LYS   A HZ1  1 
ATOM   1482 H HZ1  B LYS   A 1 55  ? 16.435 14.646  7.920   0.28 22.10 ?  55  LYS   A HZ1  1 
ATOM   1483 H HZ2  A LYS   A 1 55  ? 17.104 14.732  6.498   0.72 21.03 ?  55  LYS   A HZ2  1 
ATOM   1484 H HZ2  B LYS   A 1 55  ? 16.789 13.630  6.949   0.28 22.10 ?  55  LYS   A HZ2  1 
ATOM   1485 H HZ3  A LYS   A 1 55  ? 16.699 13.459  7.062   0.72 21.03 ?  55  LYS   A HZ3  1 
ATOM   1486 H HZ3  B LYS   A 1 55  ? 16.206 13.247  8.218   0.28 22.10 ?  55  LYS   A HZ3  1 
ATOM   1487 N N    A ALA   A 1 56  ? 22.106 9.806   9.905   0.72 12.91 ?  56  ALA   A N    1 
ATOM   1488 N N    B ALA   A 1 56  ? 22.092 9.791   10.015  0.28 13.03 ?  56  ALA   A N    1 
ATOM   1489 C CA   A ALA   A 1 56  ? 21.968 9.505   11.326  0.72 13.84 ?  56  ALA   A CA   1 
ATOM   1490 C CA   B ALA   A 1 56  ? 21.972 9.430   11.420  0.28 13.41 ?  56  ALA   A CA   1 
ATOM   1491 C C    A ALA   A 1 56  ? 23.303 9.560   12.069  0.72 13.51 ?  56  ALA   A C    1 
ATOM   1492 C C    B ALA   A 1 56  ? 23.320 9.375   12.123  0.28 12.81 ?  56  ALA   A C    1 
ATOM   1493 O O    A ALA   A 1 56  ? 23.322 9.816   13.278  0.72 14.14 ?  56  ALA   A O    1 
ATOM   1494 O O    B ALA   A 1 56  ? 23.356 9.353   13.357  0.28 12.67 ?  56  ALA   A O    1 
ATOM   1495 C CB   A ALA   A 1 56  ? 21.277 8.149   11.508  0.72 14.87 ?  56  ALA   A CB   1 
ATOM   1496 C CB   B ALA   A 1 56  ? 21.257 8.087   11.562  0.28 13.96 ?  56  ALA   A CB   1 
ATOM   1497 H H    A ALA   A 1 56  ? 21.903 9.160   9.381   0.72 15.53 ?  56  ALA   A H    1 
ATOM   1498 H H    B ALA   A 1 56  ? 21.915 9.155   9.467   0.28 15.67 ?  56  ALA   A H    1 
ATOM   1499 H HA   A ALA   A 1 56  ? 21.399 10.171  11.728  0.72 16.65 ?  56  ALA   A HA   1 
ATOM   1500 H HA   B ALA   A 1 56  ? 21.436 10.101  11.866  0.28 16.13 ?  56  ALA   A HA   1 
ATOM   1501 H HB1  A ALA   A 1 56  ? 21.196 7.957   12.456  0.72 17.88 ?  56  ALA   A HB1  1 
ATOM   1502 H HB1  B ALA   A 1 56  ? 21.187 7.867   12.504  0.28 16.79 ?  56  ALA   A HB1  1 
ATOM   1503 H HB2  A ALA   A 1 56  ? 20.394 8.189   11.104  0.72 17.88 ?  56  ALA   A HB2  1 
ATOM   1504 H HB2  B ALA   A 1 56  ? 20.373 8.163   11.172  0.28 16.79 ?  56  ALA   A HB2  1 
ATOM   1505 H HB3  A ALA   A 1 56  ? 21.804 7.458   11.076  0.72 17.88 ?  56  ALA   A HB3  1 
ATOM   1506 H HB3  B ALA   A 1 56  ? 21.769 7.407   11.098  0.28 16.79 ?  56  ALA   A HB3  1 
ATOM   1507 N N    . THR   A 1 57  ? 24.424 9.327   11.374  1.00 12.61 ?  57  THR   A N    1 
ATOM   1508 C CA   . THR   A 1 57  ? 25.764 9.451   11.953  1.00 12.99 ?  57  THR   A CA   1 
ATOM   1509 C C    . THR   A 1 57  ? 26.322 10.868  11.876  1.00 13.19 ?  57  THR   A C    1 
ATOM   1510 O O    . THR   A 1 57  ? 27.508 11.072  12.163  1.00 13.74 ?  57  THR   A O    1 
ATOM   1511 C CB   . THR   A 1 57  ? 26.775 8.500   11.288  1.00 12.89 ?  57  THR   A CB   1 
ATOM   1512 O OG1  . THR   A 1 57  ? 27.163 8.989   9.991   1.00 12.35 ?  57  THR   A OG1  1 
ATOM   1513 C CG2  . THR   A 1 57  ? 26.250 7.076   11.187  1.00 13.08 ?  57  THR   A CG2  1 
ATOM   1514 H H    A THR   A 1 57  ? 24.434 9.077   10.551  0.72 15.18 ?  57  THR   A H    1 
ATOM   1515 H H    B THR   A 1 57  ? 24.426 9.195   10.526  0.28 15.18 ?  57  THR   A H    1 
ATOM   1516 H HA   . THR   A 1 57  ? 25.720 9.197   12.895  1.00 15.63 ?  57  THR   A HA   1 
ATOM   1517 H HB   . THR   A 1 57  ? 27.573 8.462   11.845  1.00 15.51 ?  57  THR   A HB   1 
ATOM   1518 H HG1  . THR   A 1 57  ? 26.489 9.058   9.497   1.00 14.86 ?  57  THR   A HG1  1 
ATOM   1519 H HG21 . THR   A 1 57  ? 26.982 6.444   11.117  1.00 15.73 ?  57  THR   A HG21 1 
ATOM   1520 H HG22 . THR   A 1 57  ? 25.721 6.857   11.972  1.00 15.73 ?  57  THR   A HG22 1 
ATOM   1521 H HG23 . THR   A 1 57  ? 25.684 6.984   10.400  1.00 15.73 ?  57  THR   A HG23 1 
ATOM   1522 N N    . ASN   A 1 58  ? 25.515 11.845  11.470  1.00 13.81 ?  58  ASN   A N    1 
ATOM   1523 C CA   . ASN   A 1 58  ? 25.988 13.222  11.382  1.00 14.73 ?  58  ASN   A CA   1 
ATOM   1524 C C    . ASN   A 1 58  ? 27.128 13.351  10.366  1.00 13.46 ?  58  ASN   A C    1 
ATOM   1525 O O    . ASN   A 1 58  ? 28.017 14.192  10.514  1.00 14.22 ?  58  ASN   A O    1 
ATOM   1526 C CB   . ASN   A 1 58  ? 26.383 13.743  12.781  1.00 16.60 ?  58  ASN   A CB   1 
ATOM   1527 C CG   . ASN   A 1 58  ? 26.804 15.201  12.795  1.00 19.64 ?  58  ASN   A CG   1 
ATOM   1528 O OD1  . ASN   A 1 58  ? 26.170 16.039  12.166  1.00 21.36 ?  58  ASN   A OD1  1 
ATOM   1529 N ND2  . ASN   A 1 58  ? 27.866 15.515  13.548  1.00 20.30 ?  58  ASN   A ND2  1 
ATOM   1530 H H    . ASN   A 1 58  ? 24.695 11.727  11.233  1.00 16.61 ?  58  ASN   A H    1 
ATOM   1531 H HA   . ASN   A 1 58  ? 25.254 13.767  11.067  1.00 17.71 ?  58  ASN   A HA   1 
ATOM   1532 H HB2  . ASN   A 1 58  ? 25.617 13.647  13.378  1.00 19.95 ?  58  ASN   A HB2  1 
ATOM   1533 H HB3  . ASN   A 1 58  ? 27.123 13.222  13.121  1.00 19.95 ?  58  ASN   A HB3  1 
ATOM   1534 H HD21 . ASN   A 1 58  ? 28.136 16.331  13.590  1.00 24.40 ?  58  ASN   A HD21 1 
ATOM   1535 H HD22 . ASN   A 1 58  ? 28.279 14.901  13.981  1.00 24.40 ?  58  ASN   A HD22 1 
ATOM   1536 N N    . ASN   A 1 59  ? 27.111 12.523  9.317   1.00 12.37 ?  59  ASN   A N    1 
ATOM   1537 C CA   . ASN   A 1 59  ? 28.092 12.492  8.222   1.00 12.02 ?  59  ASN   A CA   1 
ATOM   1538 C C    . ASN   A 1 59  ? 29.407 11.811  8.617   1.00 11.87 ?  59  ASN   A C    1 
ATOM   1539 O O    . ASN   A 1 59  ? 30.336 11.768  7.799   1.00 11.96 ?  59  ASN   A O    1 
ATOM   1540 C CB   . ASN   A 1 59  ? 28.389 13.874  7.611   1.00 12.47 ?  59  ASN   A CB   1 
ATOM   1541 C CG   . ASN   A 1 59  ? 28.742 13.801  6.140   1.00 12.53 ?  59  ASN   A CG   1 
ATOM   1542 O OD1  . ASN   A 1 59  ? 28.027 13.181  5.350   1.00 12.90 ?  59  ASN   A OD1  1 
ATOM   1543 N ND2  . ASN   A 1 59  ? 29.835 14.458  5.756   1.00 13.20 ?  59  ASN   A ND2  1 
ATOM   1544 H H    . ASN   A 1 59  ? 26.498 11.931  9.209   1.00 14.88 ?  59  ASN   A H    1 
ATOM   1545 H HA   . ASN   A 1 59  ? 27.709 11.963  7.512   1.00 14.47 ?  59  ASN   A HA   1 
ATOM   1546 H HB2  . ASN   A 1 59  ? 27.609 14.443  7.699   1.00 15.00 ?  59  ASN   A HB2  1 
ATOM   1547 H HB3  . ASN   A 1 59  ? 29.144 14.276  8.075   1.00 15.00 ?  59  ASN   A HB3  1 
ATOM   1548 H HD21 . ASN   A 1 59  ? 30.077 14.455  4.927   1.00 15.88 ?  59  ASN   A HD21 1 
ATOM   1549 H HD22 . ASN   A 1 59  ? 30.312 14.889  6.332   1.00 15.88 ?  59  ASN   A HD22 1 
ATOM   1550 N N    . ALA   A 1 60  ? 29.520 11.273  9.828   1.00 11.84 ?  60  ALA   A N    1 
ATOM   1551 C CA   . ALA   A 1 60  ? 30.759 10.599  10.197  1.00 12.23 ?  60  ALA   A CA   1 
ATOM   1552 C C    . ALA   A 1 60  ? 30.994 9.357   9.344   1.00 12.26 ?  60  ALA   A C    1 
ATOM   1553 O O    . ALA   A 1 60  ? 32.145 9.035   9.020   1.00 12.51 ?  60  ALA   A O    1 
ATOM   1554 C CB   . ALA   A 1 60  ? 30.750 10.245  11.679  1.00 12.86 ?  60  ALA   A CB   1 
ATOM   1555 H H    . ALA   A 1 60  ? 28.916 11.280  10.439  1.00 14.25 ?  60  ALA   A H    1 
ATOM   1556 H HA   . ALA   A 1 60  ? 31.503 11.205  10.044  1.00 14.71 ?  60  ALA   A HA   1 
ATOM   1557 H HB1  . ALA   A 1 60  ? 31.578 9.801   11.908  1.00 15.47 ?  60  ALA   A HB1  1 
ATOM   1558 H HB2  . ALA   A 1 60  ? 30.658 11.063  12.199  1.00 15.47 ?  60  ALA   A HB2  1 
ATOM   1559 H HB3  . ALA   A 1 60  ? 29.996 9.659   11.859  1.00 15.47 ?  60  ALA   A HB3  1 
ATOM   1560 N N    . MET   A 1 61  ? 29.925 8.654   8.959   1.00 11.81 ?  61  MET   A N    1 
ATOM   1561 C CA   . MET   A 1 61  ? 30.070 7.515   8.058   1.00 11.83 ?  61  MET   A CA   1 
ATOM   1562 C C    . MET   A 1 61  ? 30.708 7.934   6.737   1.00 11.54 ?  61  MET   A C    1 
ATOM   1563 O O    . MET   A 1 61  ? 31.608 7.254   6.232   1.00 11.67 ?  61  MET   A O    1 
ATOM   1564 C CB   . MET   A 1 61  ? 28.706 6.858   7.839   1.00 11.60 ?  61  MET   A CB   1 
ATOM   1565 C CG   . MET   A 1 61  ? 28.722 5.682   6.869   1.00 12.24 ?  61  MET   A CG   1 
ATOM   1566 S SD   . MET   A 1 61  ? 27.094 4.947   6.629   1.00 13.42 ?  61  MET   A SD   1 
ATOM   1567 C CE   . MET   A 1 61  ? 26.937 4.054   8.186   1.00 14.85 ?  61  MET   A CE   1 
ATOM   1568 H H    . MET   A 1 61  ? 29.117 8.821   9.197   1.00 14.22 ?  61  MET   A H    1 
ATOM   1569 H HA   . MET   A 1 61  ? 30.642 6.856   8.480   1.00 14.23 ?  61  MET   A HA   1 
ATOM   1570 H HB2  . MET   A 1 61  ? 28.374 6.529   8.688   1.00 13.95 ?  61  MET   A HB2  1 
ATOM   1571 H HB3  . MET   A 1 61  ? 28.090 7.517   7.481   1.00 13.95 ?  61  MET   A HB3  1 
ATOM   1572 H HG2  . MET   A 1 61  ? 29.032 5.978   6.001   1.00 14.72 ?  61  MET   A HG2  1 
ATOM   1573 H HG3  . MET   A 1 61  ? 29.307 4.989   7.214   1.00 14.72 ?  61  MET   A HG3  1 
ATOM   1574 H HE1  . MET   A 1 61  ? 26.093 3.578   8.194   1.00 17.86 ?  61  MET   A HE1  1 
ATOM   1575 H HE2  . MET   A 1 61  ? 27.674 3.431   8.266   1.00 17.86 ?  61  MET   A HE2  1 
ATOM   1576 H HE3  . MET   A 1 61  ? 26.963 4.692   8.921   1.00 17.86 ?  61  MET   A HE3  1 
ATOM   1577 N N    . GLN   A 1 62  ? 30.268 9.064   6.173   1.00 11.58 ?  62  GLN   A N    1 
ATOM   1578 C CA   . GLN   A 1 62  ? 30.838 9.532   4.913   1.00 11.83 ?  62  GLN   A CA   1 
ATOM   1579 C C    . GLN   A 1 62  ? 32.309 9.909   5.063   1.00 11.55 ?  62  GLN   A C    1 
ATOM   1580 O O    . GLN   A 1 62  ? 33.123 9.593   4.188   1.00 11.84 ?  62  GLN   A O    1 
ATOM   1581 C CB   . GLN   A 1 62  ? 30.039 10.716  4.371   1.00 11.84 ?  62  GLN   A CB   1 
ATOM   1582 C CG   . GLN   A 1 62  ? 30.427 11.079  2.950   1.00 11.87 ?  62  GLN   A CG   1 
ATOM   1583 C CD   . GLN   A 1 62  ? 30.105 9.952   1.996   1.00 11.89 ?  62  GLN   A CD   1 
ATOM   1584 O OE1  . GLN   A 1 62  ? 28.929 9.649   1.768   1.00 12.90 ?  62  GLN   A OE1  1 
ATOM   1585 N NE2  . GLN   A 1 62  ? 31.131 9.275   1.485   1.00 12.59 ?  62  GLN   A NE2  1 
ATOM   1586 H H    . GLN   A 1 62  ? 29.650 9.564   6.499   1.00 13.93 ?  62  GLN   A H    1 
ATOM   1587 H HA   . GLN   A 1 62  ? 30.787 8.813   4.269   1.00 14.23 ?  62  GLN   A HA   1 
ATOM   1588 H HB2  . GLN   A 1 62  ? 29.096 10.492  4.379   1.00 14.25 ?  62  GLN   A HB2  1 
ATOM   1589 H HB3  . GLN   A 1 62  ? 30.201 11.493  4.929   1.00 14.25 ?  62  GLN   A HB3  1 
ATOM   1590 H HG2  . GLN   A 1 62  ? 29.920 11.857  2.666   1.00 14.28 ?  62  GLN   A HG2  1 
ATOM   1591 H HG3  . GLN   A 1 62  ? 31.375 11.257  2.902   1.00 14.28 ?  62  GLN   A HG3  1 
ATOM   1592 H HE21 . GLN   A 1 62  ? 31.935 9.502   1.683   1.00 15.14 ?  62  GLN   A HE21 1 
ATOM   1593 H HE22 . GLN   A 1 62  ? 30.989 8.619   0.947   1.00 15.14 ?  62  GLN   A HE22 1 
ATOM   1594 N N    . VAL   A 1 63  ? 32.665 10.589  6.156   1.00 12.07 ?  63  VAL   A N    1 
ATOM   1595 C CA   . VAL   A 1 63  ? 34.058 10.979  6.378   1.00 12.78 ?  63  VAL   A CA   1 
ATOM   1596 C C    . VAL   A 1 63  ? 34.953 9.739   6.451   1.00 12.44 ?  63  VAL   A C    1 
ATOM   1597 O O    . VAL   A 1 63  ? 36.010 9.664   5.804   1.00 13.05 ?  63  VAL   A O    1 
ATOM   1598 C CB   . VAL   A 1 63  ? 34.158 11.860  7.639   1.00 14.38 ?  63  VAL   A CB   1 
ATOM   1599 C CG1  . VAL   A 1 63  ? 35.598 12.086  8.034   1.00 16.13 ?  63  VAL   A CG1  1 
ATOM   1600 C CG2  . VAL   A 1 63  ? 33.456 13.201  7.397   1.00 14.56 ?  63  VAL   A CG2  1 
ATOM   1601 H H    . VAL   A 1 63  ? 32.123 10.831  6.783   1.00 14.52 ?  63  VAL   A H    1 
ATOM   1602 H HA   . VAL   A 1 63  ? 34.353 11.509  5.628   1.00 15.37 ?  63  VAL   A HA   1 
ATOM   1603 H HB   . VAL   A 1 63  ? 33.707 11.421  8.377   1.00 17.29 ?  63  VAL   A HB   1 
ATOM   1604 H HG11 . VAL   A 1 63  ? 35.637 12.825  8.666   1.00 19.40 ?  63  VAL   A HG11 1 
ATOM   1605 H HG12 . VAL   A 1 63  ? 35.944 11.283  8.444   1.00 19.40 ?  63  VAL   A HG12 1 
ATOM   1606 H HG13 . VAL   A 1 63  ? 36.109 12.308  7.241   1.00 19.40 ?  63  VAL   A HG13 1 
ATOM   1607 H HG21 . VAL   A 1 63  ? 33.533 13.748  8.197   1.00 17.50 ?  63  VAL   A HG21 1 
ATOM   1608 H HG22 . VAL   A 1 63  ? 33.883 13.650  6.650   1.00 17.50 ?  63  VAL   A HG22 1 
ATOM   1609 H HG23 . VAL   A 1 63  ? 32.522 13.040  7.197   1.00 17.50 ?  63  VAL   A HG23 1 
ATOM   1610 N N    . GLU   A 1 64  ? 34.524 8.732   7.220   1.00 12.30 ?  64  GLU   A N    1 
ATOM   1611 C CA   . GLU   A 1 64  ? 35.284 7.493   7.318   1.00 12.29 ?  64  GLU   A CA   1 
ATOM   1612 C C    . GLU   A 1 64  ? 35.381 6.810   5.960   1.00 12.00 ?  64  GLU   A C    1 
ATOM   1613 O O    . GLU   A 1 64  ? 36.439 6.269   5.586   1.00 12.57 ?  64  GLU   A O    1 
ATOM   1614 C CB   . GLU   A 1 64  ? 34.595 6.579   8.333   1.00 13.16 ?  64  GLU   A CB   1 
ATOM   1615 C CG   . GLU   A 1 64  ? 35.243 5.230   8.471   1.00 13.59 ?  64  GLU   A CG   1 
ATOM   1616 C CD   . GLU   A 1 64  ? 34.380 4.238   9.217   1.00 14.49 ?  64  GLU   A CD   1 
ATOM   1617 O OE1  . GLU   A 1 64  ? 33.140 4.334   9.103   1.00 15.21 ?  64  GLU   A OE1  1 
ATOM   1618 O OE2  . GLU   A 1 64  ? 34.944 3.349   9.898   1.00 14.76 -1 64  GLU   A OE2  1 
ATOM   1619 H H    . GLU   A 1 64  ? 33.793 8.741   7.681   1.00 14.80 ?  64  GLU   A H    1 
ATOM   1620 H HA   . GLU   A 1 64  ? 36.179 7.693   7.642   1.00 14.79 ?  64  GLU   A HA   1 
ATOM   1621 H HB2  . GLU   A 1 64  ? 34.616 7.012   9.209   1.00 15.83 ?  64  GLU   A HB2  1 
ATOM   1622 H HB3  . GLU   A 1 64  ? 33.673 6.454   8.060   1.00 15.83 ?  64  GLU   A HB3  1 
ATOM   1623 H HG2  . GLU   A 1 64  ? 35.416 4.860   7.587   1.00 16.35 ?  64  GLU   A HG2  1 
ATOM   1624 H HG3  . GLU   A 1 64  ? 36.073 5.326   8.955   1.00 16.35 ?  64  GLU   A HG3  1 
ATOM   1625 N N    . SER   A 1 65  ? 34.266 6.800   5.222   1.00 11.72 ?  65  SER   A N    1 
ATOM   1626 C CA   . SER   A 1 65  ? 34.220 6.141   3.923   1.00 11.85 ?  65  SER   A CA   1 
ATOM   1627 C C    . SER   A 1 65  ? 35.151 6.804   2.917   1.00 12.09 ?  65  SER   A C    1 
ATOM   1628 O O    . SER   A 1 65  ? 35.795 6.120   2.114   1.00 12.74 ?  65  SER   A O    1 
ATOM   1629 C CB   . SER   A 1 65  ? 32.793 6.155   3.386   1.00 11.87 ?  65  SER   A CB   1 
ATOM   1630 O OG   . SER   A 1 65  ? 31.932 5.339   4.172   1.00 12.07 ?  65  SER   A OG   1 
ATOM   1631 H H    . SER   A 1 65  ? 33.526 7.167   5.460   1.00 14.10 ?  65  SER   A H    1 
ATOM   1632 H HA   . SER   A 1 65  ? 34.500 5.220   4.023   1.00 14.26 ?  65  SER   A HA   1 
ATOM   1633 H HB2  . SER   A 1 65  ? 32.459 7.062   3.397   1.00 14.28 ?  65  SER   A HB2  1 
ATOM   1634 H HB3  . SER   A 1 65  ? 32.801 5.815   2.476   1.00 14.28 ?  65  SER   A HB3  1 
ATOM   1635 H HG   . SER   A 1 65  ? 31.924 5.617   4.968   1.00 14.52 ?  65  SER   A HG   1 
ATOM   1636 N N    . ASP   A 1 66  ? 35.223 8.138   2.927   1.00 12.27 ?  66  ASP   A N    1 
ATOM   1637 C CA   . ASP   A 1 66  ? 36.094 8.834   1.986   1.00 13.11 ?  66  ASP   A CA   1 
ATOM   1638 C C    . ASP   A 1 66  ? 37.557 8.485   2.242   1.00 12.86 ?  66  ASP   A C    1 
ATOM   1639 O O    . ASP   A 1 66  ? 38.339 8.308   1.298   1.00 13.72 ?  66  ASP   A O    1 
ATOM   1640 C CB   . ASP   A 1 66  ? 35.864 10.341  2.073   1.00 14.33 ?  66  ASP   A CB   1 
ATOM   1641 C CG   . ASP   A 1 66  ? 34.533 10.789  1.448   1.00 16.21 ?  66  ASP   A CG   1 
ATOM   1642 O OD1  . ASP   A 1 66  ? 33.838 9.990   0.776   1.00 16.57 ?  66  ASP   A OD1  1 
ATOM   1643 O OD2  . ASP   A 1 66  ? 34.212 11.984  1.613   1.00 19.47 -1 66  ASP   A OD2  1 
ATOM   1644 H H    . ASP   A 1 66  ? 34.772 8.657   3.454   1.00 14.77 ?  66  ASP   A H    1 
ATOM   1645 H HA   . ASP   A 1 66  ? 35.873 8.553   1.088   1.00 15.77 ?  66  ASP   A HA   1 
ATOM   1646 H HB2  . ASP   A 1 66  ? 35.852 10.610  3.005   1.00 17.23 ?  66  ASP   A HB2  1 
ATOM   1647 H HB3  . ASP   A 1 66  ? 36.584 10.798  1.607   1.00 17.23 ?  66  ASP   A HB3  1 
ATOM   1648 N N    . ASP   A 1 67  ? 37.941 8.366   3.512   1.00 12.73 ?  67  ASP   A N    1 
ATOM   1649 C CA   . ASP   A 1 67  ? 39.297 7.921   3.826   1.00 13.69 ?  67  ASP   A CA   1 
ATOM   1650 C C    . ASP   A 1 67  ? 39.531 6.488   3.354   1.00 13.72 ?  67  ASP   A C    1 
ATOM   1651 O O    . ASP   A 1 67  ? 40.598 6.167   2.813   1.00 14.41 ?  67  ASP   A O    1 
ATOM   1652 C CB   . ASP   A 1 67  ? 39.553 8.059   5.327   1.00 14.93 ?  67  ASP   A CB   1 
ATOM   1653 C CG   . ASP   A 1 67  ? 40.851 7.413   5.762   1.00 16.28 ?  67  ASP   A CG   1 
ATOM   1654 O OD1  . ASP   A 1 67  ? 41.917 8.068   5.667   1.00 18.70 ?  67  ASP   A OD1  1 
ATOM   1655 O OD2  . ASP   A 1 67  ? 40.803 6.243   6.202   1.00 16.35 -1 67  ASP   A OD2  1 
ATOM   1656 H H    . ASP   A 1 67  ? 37.451 8.535   4.197   1.00 15.31 ?  67  ASP   A H    1 
ATOM   1657 H HA   . ASP   A 1 67  ? 39.932 8.490   3.365   1.00 16.47 ?  67  ASP   A HA   1 
ATOM   1658 H HB2  . ASP   A 1 67  ? 39.596 8.996   5.555   1.00 17.96 ?  67  ASP   A HB2  1 
ATOM   1659 H HB3  . ASP   A 1 67  ? 38.828 7.628   5.810   1.00 17.96 ?  67  ASP   A HB3  1 
ATOM   1660 N N    . TYR   A 1 68  ? 38.537 5.610   3.530   1.00 13.31 ?  68  TYR   A N    1 
ATOM   1661 C CA   . TYR   A 1 68  ? 38.666 4.228   3.062   1.00 13.50 ?  68  TYR   A CA   1 
ATOM   1662 C C    . TYR   A 1 68  ? 38.903 4.175   1.553   1.00 13.32 ?  68  TYR   A C    1 
ATOM   1663 O O    . TYR   A 1 68  ? 39.787 3.448   1.079   1.00 13.97 ?  68  TYR   A O    1 
ATOM   1664 C CB   . TYR   A 1 68  ? 37.422 3.400   3.449   1.00 14.07 ?  68  TYR   A CB   1 
ATOM   1665 C CG   . TYR   A 1 68  ? 37.448 2.009   2.819   1.00 15.40 ?  68  TYR   A CG   1 
ATOM   1666 C CD1  . TYR   A 1 68  ? 36.984 1.813   1.522   1.00 16.78 ?  68  TYR   A CD1  1 
ATOM   1667 C CD2  . TYR   A 1 68  ? 37.991 0.923   3.485   1.00 17.11 ?  68  TYR   A CD2  1 
ATOM   1668 C CE1  . TYR   A 1 68  ? 37.057 0.596   0.902   1.00 18.26 ?  68  TYR   A CE1  1 
ATOM   1669 C CE2  . TYR   A 1 68  ? 38.050 -0.337  2.868   1.00 18.03 ?  68  TYR   A CE2  1 
ATOM   1670 C CZ   . TYR   A 1 68  ? 37.589 -0.474  1.575   1.00 18.43 ?  68  TYR   A CZ   1 
ATOM   1671 O OH   . TYR   A 1 68  ? 37.666 -1.688  0.938   1.00 19.76 ?  68  TYR   A OH   1 
ATOM   1672 H H    . TYR   A 1 68  ? 37.782 5.786   3.915   1.00 16.01 ?  68  TYR   A H    1 
ATOM   1673 H HA   . TYR   A 1 68  ? 39.430 3.824   3.495   1.00 16.24 ?  68  TYR   A HA   1 
ATOM   1674 H HB2  . TYR   A 1 68  ? 37.394 3.292   4.414   1.00 16.92 ?  68  TYR   A HB2  1 
ATOM   1675 H HB3  . TYR   A 1 68  ? 36.621 3.856   3.142   1.00 16.92 ?  68  TYR   A HB3  1 
ATOM   1676 H HD1  . TYR   A 1 68  ? 36.636 2.542   1.055   1.00 20.17 ?  68  TYR   A HD1  1 
ATOM   1677 H HD2  . TYR   A 1 68  ? 38.324 1.026   4.345   1.00 20.57 ?  68  TYR   A HD2  1 
ATOM   1678 H HE1  . TYR   A 1 68  ? 36.736 0.494   0.036   1.00 21.95 ?  68  TYR   A HE1  1 
ATOM   1679 H HE2  . TYR   A 1 68  ? 38.425 -1.067  3.306   1.00 21.67 ?  68  TYR   A HE2  1 
ATOM   1680 H HH   . TYR   A 1 68  ? 38.006 -2.261  1.456   1.00 23.75 ?  68  TYR   A HH   1 
ATOM   1681 N N    . ILE   A 1 69  ? 38.113 4.931   0.777   1.00 12.71 ?  69  ILE   A N    1 
ATOM   1682 C CA   . ILE   A 1 69  ? 38.256 4.912   -0.679  1.00 12.83 ?  69  ILE   A CA   1 
ATOM   1683 C C    . ILE   A 1 69  ? 39.587 5.525   -1.109  1.00 12.77 ?  69  ILE   A C    1 
ATOM   1684 O O    . ILE   A 1 69  ? 40.233 5.045   -2.049  1.00 13.30 ?  69  ILE   A O    1 
ATOM   1685 C CB   . ILE   A 1 69  ? 37.057 5.613   -1.349  1.00 13.71 ?  69  ILE   A CB   1 
ATOM   1686 C CG1  . ILE   A 1 69  ? 35.744 4.876   -1.064  1.00 14.41 ?  69  ILE   A CG1  1 
ATOM   1687 C CG2  . ILE   A 1 69  ? 37.299 5.778   -2.858  1.00 15.26 ?  69  ILE   A CG2  1 
ATOM   1688 C CD1  . ILE   A 1 69  ? 35.585 3.579   -1.825  1.00 15.25 ?  69  ILE   A CD1  1 
ATOM   1689 H H    . ILE   A 1 69  ? 37.499 5.459   1.068   1.00 15.29 ?  69  ILE   A H    1 
ATOM   1690 H HA   . ILE   A 1 69  ? 38.256 3.990   -0.974  1.00 15.44 ?  69  ILE   A HA   1 
ATOM   1691 H HB   . ILE   A 1 69  ? 36.981 6.498   -0.971  1.00 16.49 ?  69  ILE   A HB   1 
ATOM   1692 H HG12 . ILE   A 1 69  ? 35.705 4.669   -0.116  1.00 17.33 ?  69  ILE   A HG12 1 
ATOM   1693 H HG13 . ILE   A 1 69  ? 35.004 5.454   -1.304  1.00 17.33 ?  69  ILE   A HG13 1 
ATOM   1694 H HG21 . ILE   A 1 69  ? 36.453 5.973   -3.297  1.00 18.35 ?  69  ILE   A HG21 1 
ATOM   1695 H HG22 . ILE   A 1 69  ? 37.917 6.515   -3.003  1.00 18.35 ?  69  ILE   A HG22 1 
ATOM   1696 H HG23 . ILE   A 1 69  ? 37.672 4.959   -3.217  1.00 18.35 ?  69  ILE   A HG23 1 
ATOM   1697 H HD11 . ILE   A 1 69  ? 34.794 3.121   -1.501  1.00 18.34 ?  69  ILE   A HD11 1 
ATOM   1698 H HD12 . ILE   A 1 69  ? 35.485 3.777   -2.771  1.00 18.34 ?  69  ILE   A HD12 1 
ATOM   1699 H HD13 . ILE   A 1 69  ? 36.367 3.027   -1.682  1.00 18.34 ?  69  ILE   A HD13 1 
ATOM   1700 N N    . ALA   A 1 70  ? 40.003 6.604   -0.450  1.00 13.63 ?  70  ALA   A N    1 
ATOM   1701 C CA   . ALA   A 1 70  ? 41.274 7.225   -0.802  1.00 14.37 ?  70  ALA   A CA   1 
ATOM   1702 C C    . ALA   A 1 70  ? 42.436 6.257   -0.626  1.00 14.68 ?  70  ALA   A C    1 
ATOM   1703 O O    . ALA   A 1 70  ? 43.420 6.329   -1.367  1.00 16.92 ?  70  ALA   A O    1 
ATOM   1704 C CB   . ALA   A 1 70  ? 41.492 8.489   0.032   1.00 15.12 ?  70  ALA   A CB   1 
ATOM   1705 H H    . ALA   A 1 70  ? 39.574 6.993   0.181   1.00 16.40 ?  70  ALA   A H    1 
ATOM   1706 H HA   . ALA   A 1 70  ? 41.249 7.494   -1.738  1.00 17.28 ?  70  ALA   A HA   1 
ATOM   1707 H HB1  . ALA   A 1 70  ? 42.348 8.886   -0.214  1.00 18.18 ?  70  ALA   A HB1  1 
ATOM   1708 H HB2  . ALA   A 1 70  ? 40.777 9.116   -0.143  1.00 18.18 ?  70  ALA   A HB2  1 
ATOM   1709 H HB3  . ALA   A 1 70  ? 41.504 8.248   0.971   1.00 18.18 ?  70  ALA   A HB3  1 
ATOM   1710 N N    . THR   A 1 71  ? 42.336 5.340   0.332   1.00 14.28 ?  71  THR   A N    1 
ATOM   1711 C CA   . THR   A 1 71  ? 43.388 4.368   0.596   1.00 16.05 ?  71  THR   A CA   1 
ATOM   1712 C C    . THR   A 1 71  ? 43.276 3.132   -0.285  1.00 16.08 ?  71  THR   A C    1 
ATOM   1713 O O    . THR   A 1 71  ? 44.292 2.611   -0.763  1.00 18.32 ?  71  THR   A O    1 
ATOM   1714 C CB   . THR   A 1 71  ? 43.311 3.928   2.057   1.00 18.74 ?  71  THR   A CB   1 
ATOM   1715 O OG1  . THR   A 1 71  ? 43.541 5.057   2.904   1.00 20.28 ?  71  THR   A OG1  1 
ATOM   1716 C CG2  . THR   A 1 71  ? 44.327 2.829   2.361   1.00 20.42 ?  71  THR   A CG2  1 
ATOM   1717 H H    . THR   A 1 71  ? 41.648 5.250   0.840   1.00 17.17 ?  71  THR   A H    1 
ATOM   1718 H HA   . THR   A 1 71  ? 44.250 4.776   0.438   1.00 19.30 ?  71  THR   A HA   1 
ATOM   1719 H HB   . THR   A 1 71  ? 42.425 3.571   2.234   1.00 22.52 ?  71  THR   A HB   1 
ATOM   1720 H HG1  . THR   A 1 71  ? 42.961 5.643   2.760   1.00 24.38 ?  71  THR   A HG1  1 
ATOM   1721 H HG21 . THR   A 1 71  ? 44.459 2.757   3.320   1.00 24.54 ?  71  THR   A HG21 1 
ATOM   1722 H HG22 . THR   A 1 71  ? 44.014 1.973   2.025   1.00 24.54 ?  71  THR   A HG22 1 
ATOM   1723 H HG23 . THR   A 1 71  ? 45.179 3.038   1.944   1.00 24.54 ?  71  THR   A HG23 1 
ATOM   1724 N N    . ASN   A 1 72  ? 42.056 2.636   -0.496  1.00 14.76 ?  72  ASN   A N    1 
ATOM   1725 C CA   . ASN   A 1 72  ? 41.837 1.307   -1.054  1.00 15.32 ?  72  ASN   A CA   1 
ATOM   1726 C C    . ASN   A 1 72  ? 41.219 1.294   -2.440  1.00 15.30 ?  72  ASN   A C    1 
ATOM   1727 O O    . ASN   A 1 72  ? 41.219 0.235   -3.084  1.00 16.35 ?  72  ASN   A O    1 
ATOM   1728 C CB   . ASN   A 1 72  ? 40.937 0.496   -0.114  1.00 16.14 ?  72  ASN   A CB   1 
ATOM   1729 C CG   . ASN   A 1 72  ? 41.552 0.331   1.252   1.00 17.28 ?  72  ASN   A CG   1 
ATOM   1730 O OD1  . ASN   A 1 72  ? 41.110 0.934   2.228   1.00 19.18 ?  72  ASN   A OD1  1 
ATOM   1731 N ND2  . ASN   A 1 72  ? 42.597 -0.463  1.325   1.00 17.97 ?  72  ASN   A ND2  1 
ATOM   1732 H H    . ASN   A 1 72  ? 41.323 3.062   -0.321  1.00 17.74 ?  72  ASN   A H    1 
ATOM   1733 H HA   . ASN   A 1 72  ? 42.686 0.854   -1.114  1.00 18.42 ?  72  ASN   A HA   1 
ATOM   1734 H HB2  . ASN   A 1 72  ? 40.085 0.953   -0.014  1.00 19.40 ?  72  ASN   A HB2  1 
ATOM   1735 H HB3  . ASN   A 1 72  ? 40.798 -0.387  -0.493  1.00 19.40 ?  72  ASN   A HB3  1 
ATOM   1736 H HD21 . ASN   A 1 72  ? 42.987 -0.584  2.081   1.00 21.60 ?  72  ASN   A HD21 1 
ATOM   1737 H HD22 . ASN   A 1 72  ? 42.884 -0.861  0.621   1.00 21.60 ?  72  ASN   A HD22 1 
ATOM   1738 N N    . GLY   A 1 73  ? 40.670 2.407   -2.907  1.00 14.68 ?  73  GLY   A N    1 
ATOM   1739 C CA   . GLY   A 1 73  ? 39.938 2.412   -4.147  1.00 14.38 ?  73  GLY   A CA   1 
ATOM   1740 C C    . GLY   A 1 73  ? 38.545 1.835   -3.976  1.00 13.79 ?  73  GLY   A C    1 
ATOM   1741 O O    . GLY   A 1 73  ? 38.155 1.393   -2.892  1.00 14.23 ?  73  GLY   A O    1 
ATOM   1742 H H    . GLY   A 1 73  ? 40.717 3.183   -2.525  1.00 17.66 ?  73  GLY   A H    1 
ATOM   1743 H HA2  . GLY   A 1 73  ? 39.865 3.327   -4.476  1.00 17.29 ?  73  GLY   A HA2  1 
ATOM   1744 H HA3  . GLY   A 1 73  ? 40.414 1.888   -4.810  1.00 17.29 ?  73  GLY   A HA3  1 
ATOM   1745 N N    . PRO   A 1 74  ? 37.771 1.838   -5.058  1.00 14.15 ?  74  PRO   A N    1 
ATOM   1746 C CA   . PRO   A 1 74  ? 36.372 1.413   -4.974  1.00 14.28 ?  74  PRO   A CA   1 
ATOM   1747 C C    . PRO   A 1 74  ? 36.216 -0.068  -4.657  1.00 13.46 ?  74  PRO   A C    1 
ATOM   1748 O O    . PRO   A 1 74  ? 37.082 -0.905  -4.940  1.00 14.44 ?  74  PRO   A O    1 
ATOM   1749 C CB   . PRO   A 1 74  ? 35.828 1.713   -6.377  1.00 15.90 ?  74  PRO   A CB   1 
ATOM   1750 C CG   . PRO   A 1 74  ? 36.788 2.672   -6.991  1.00 18.87 ?  74  PRO   A CG   1 
ATOM   1751 C CD   . PRO   A 1 74  ? 38.119 2.344   -6.396  1.00 16.26 ?  74  PRO   A CD   1 
ATOM   1752 H HA   . PRO   A 1 74  ? 35.892 1.941   -4.314  1.00 17.17 ?  74  PRO   A HA   1 
ATOM   1753 H HB2  . PRO   A 1 74  ? 35.786 0.890   -6.887  1.00 19.11 ?  74  PRO   A HB2  1 
ATOM   1754 H HB3  . PRO   A 1 74  ? 34.946 2.112   -6.300  1.00 19.11 ?  74  PRO   A HB3  1 
ATOM   1755 H HG2  . PRO   A 1 74  ? 36.805 2.546   -7.951  1.00 22.68 ?  74  PRO   A HG2  1 
ATOM   1756 H HG3  . PRO   A 1 74  ? 36.532 3.578   -6.766  1.00 22.68 ?  74  PRO   A HG3  1 
ATOM   1757 H HD2  . PRO   A 1 74  ? 38.566 1.651   -6.914  1.00 19.56 ?  74  PRO   A HD2  1 
ATOM   1758 H HD3  . PRO   A 1 74  ? 38.666 3.145   -6.337  1.00 19.56 ?  74  PRO   A HD3  1 
ATOM   1759 N N    . LEU   A 1 75  ? 35.070 -0.388  -4.073  1.00 12.92 ?  75  LEU   A N    1 
ATOM   1760 C CA   . LEU   A 1 75  ? 34.666 -1.778  -3.929  1.00 12.57 ?  75  LEU   A CA   1 
ATOM   1761 C C    . LEU   A 1 75  ? 34.289 -2.355  -5.291  1.00 13.01 ?  75  LEU   A C    1 
ATOM   1762 O O    . LEU   A 1 75  ? 34.147 -1.640  -6.285  1.00 14.17 ?  75  LEU   A O    1 
ATOM   1763 C CB   . LEU   A 1 75  ? 33.473 -1.899  -2.984  1.00 12.70 ?  75  LEU   A CB   1 
ATOM   1764 C CG   . LEU   A 1 75  ? 33.677 -1.498  -1.529  1.00 14.46 ?  75  LEU   A CG   1 
ATOM   1765 C CD1  . LEU   A 1 75  ? 32.388 -1.717  -0.744  1.00 16.55 ?  75  LEU   A CD1  1 
ATOM   1766 C CD2  . LEU   A 1 75  ? 34.816 -2.214  -0.868  1.00 17.63 ?  75  LEU   A CD2  1 
ATOM   1767 H H    . LEU   A 1 75  ? 34.512 0.181   -3.749  1.00 15.54 ?  75  LEU   A H    1 
ATOM   1768 H HA   . LEU   A 1 75  ? 35.405 -2.292  -3.573  1.00 15.12 ?  75  LEU   A HA   1 
ATOM   1769 H HB2  . LEU   A 1 75  ? 32.757 -1.352  -3.331  1.00 15.28 ?  75  LEU   A HB2  1 
ATOM   1770 H HB3  . LEU   A 1 75  ? 33.192 -2.831  -2.982  1.00 15.28 ?  75  LEU   A HB3  1 
ATOM   1771 H HG   . LEU   A 1 75  ? 33.883 -0.550  -1.499  1.00 17.39 ?  75  LEU   A HG   1 
ATOM   1772 H HD11 . LEU   A 1 75  ? 32.534 -1.454  0.179   1.00 19.90 ?  75  LEU   A HD11 1 
ATOM   1773 H HD12 . LEU   A 1 75  ? 31.689 -1.175  -1.138  1.00 19.90 ?  75  LEU   A HD12 1 
ATOM   1774 H HD13 . LEU   A 1 75  ? 32.150 -2.654  -0.788  1.00 19.90 ?  75  LEU   A HD13 1 
ATOM   1775 H HD21 . LEU   A 1 75  ? 34.861 -1.949  0.065   1.00 21.20 ?  75  LEU   A HD21 1 
ATOM   1776 H HD22 . LEU   A 1 75  ? 34.672 -3.171  -0.933  1.00 21.20 ?  75  LEU   A HD22 1 
ATOM   1777 H HD23 . LEU   A 1 75  ? 35.648 -1.976  -1.315  1.00 21.20 ?  75  LEU   A HD23 1 
ATOM   1778 N N    . LYS   A 1 76  ? 34.119 -3.679  -5.314  1.00 13.28 ?  76  LYS   A N    1 
ATOM   1779 C CA   . LYS   A 1 76  ? 33.524 -4.405  -6.430  1.00 13.82 ?  76  LYS   A CA   1 
ATOM   1780 C C    . LYS   A 1 76  ? 32.009 -4.470  -6.249  1.00 12.57 ?  76  LYS   A C    1 
ATOM   1781 O O    . LYS   A 1 76  ? 31.515 -4.573  -5.131  1.00 12.88 ?  76  LYS   A O    1 
ATOM   1782 C CB   . LYS   A 1 76  ? 34.062 -5.847  -6.464  1.00 14.98 ?  76  LYS   A CB   1 
ATOM   1783 C CG   . LYS   A 1 76  ? 35.567 -5.958  -6.691  1.00 16.52 ?  76  LYS   A CG   1 
ATOM   1784 C CD   . LYS   A 1 76  ? 36.082 -7.355  -6.459  1.00 17.89 ?  76  LYS   A CD   1 
ATOM   1785 C CE   . LYS   A 1 76  ? 37.583 -7.419  -6.660  1.00 20.31 ?  76  LYS   A CE   1 
ATOM   1786 N NZ   . LYS   A 1 76  ? 38.120 -8.769  -6.420  1.00 21.33 ?  76  LYS   A NZ   1 
ATOM   1787 H H    . LYS   A 1 76  ? 34.357 -4.197  -4.664  1.00 15.97 ?  76  LYS   A H    1 
ATOM   1788 H HA   . LYS   A 1 76  ? 33.736 -3.966  -7.267  1.00 16.62 ?  76  LYS   A HA   1 
ATOM   1789 H HB2  . LYS   A 1 76  ? 33.860 -6.272  -5.615  1.00 18.01 ?  76  LYS   A HB2  1 
ATOM   1790 H HB3  . LYS   A 1 76  ? 33.619 -6.323  -7.182  1.00 18.01 ?  76  LYS   A HB3  1 
ATOM   1791 H HG2  . LYS   A 1 76  ? 35.769 -5.710  -7.607  1.00 19.86 ?  76  LYS   A HG2  1 
ATOM   1792 H HG3  . LYS   A 1 76  ? 36.027 -5.362  -6.077  1.00 19.86 ?  76  LYS   A HG3  1 
ATOM   1793 H HD2  . LYS   A 1 76  ? 35.883 -7.627  -5.549  1.00 21.51 ?  76  LYS   A HD2  1 
ATOM   1794 H HD3  . LYS   A 1 76  ? 35.663 -7.963  -7.090  1.00 21.51 ?  76  LYS   A HD3  1 
ATOM   1795 H HE2  . LYS   A 1 76  ? 37.793 -7.169  -7.572  1.00 24.41 ?  76  LYS   A HE2  1 
ATOM   1796 H HE3  . LYS   A 1 76  ? 38.013 -6.814  -6.037  1.00 24.41 ?  76  LYS   A HE3  1 
ATOM   1797 H HZ1  . LYS   A 1 76  ? 39.001 -8.783  -6.547  1.00 25.64 ?  76  LYS   A HZ1  1 
ATOM   1798 H HZ2  . LYS   A 1 76  ? 37.945 -9.034  -5.587  1.00 25.64 ?  76  LYS   A HZ2  1 
ATOM   1799 H HZ3  . LYS   A 1 76  ? 37.745 -9.357  -6.985  1.00 25.64 ?  76  LYS   A HZ3  1 
ATOM   1800 N N    . VAL   A 1 77  ? 31.269 -4.438  -7.361  1.00 13.19 ?  77  VAL   A N    1 
ATOM   1801 C CA   . VAL   A 1 77  ? 29.857 -4.812  -7.286  1.00 13.22 ?  77  VAL   A CA   1 
ATOM   1802 C C    . VAL   A 1 77  ? 29.785 -6.267  -6.842  1.00 13.04 ?  77  VAL   A C    1 
ATOM   1803 O O    . VAL   A 1 77  ? 30.442 -7.143  -7.421  1.00 13.48 ?  77  VAL   A O    1 
ATOM   1804 C CB   . VAL   A 1 77  ? 29.151 -4.605  -8.632  1.00 14.22 ?  77  VAL   A CB   1 
ATOM   1805 C CG1  . VAL   A 1 77  ? 27.684 -5.010  -8.529  1.00 15.14 ?  77  VAL   A CG1  1 
ATOM   1806 C CG2  . VAL   A 1 77  ? 29.279 -3.162  -9.081  1.00 15.67 ?  77  VAL   A CG2  1 
ATOM   1807 H H    . VAL   A 1 77  ? 31.554 -4.211  -8.140  1.00 15.86 ?  77  VAL   A H    1 
ATOM   1808 H HA   . VAL   A 1 77  ? 29.417 -4.266  -6.618  1.00 15.90 ?  77  VAL   A HA   1 
ATOM   1809 H HB   . VAL   A 1 77  ? 29.574 -5.164  -9.301  1.00 17.10 ?  77  VAL   A HB   1 
ATOM   1810 H HG11 . VAL   A 1 77  ? 27.223 -4.714  -9.326  1.00 18.21 ?  77  VAL   A HG11 1 
ATOM   1811 H HG12 . VAL   A 1 77  ? 27.630 -5.975  -8.452  1.00 18.21 ?  77  VAL   A HG12 1 
ATOM   1812 H HG13 . VAL   A 1 77  ? 27.299 -4.591  -7.745  1.00 18.21 ?  77  VAL   A HG13 1 
ATOM   1813 H HG21 . VAL   A 1 77  ? 28.763 -3.040  -9.892  1.00 18.84 ?  77  VAL   A HG21 1 
ATOM   1814 H HG22 . VAL   A 1 77  ? 28.941 -2.585  -8.380  1.00 18.84 ?  77  VAL   A HG22 1 
ATOM   1815 H HG23 . VAL   A 1 77  ? 30.214 -2.966  -9.249  1.00 18.84 ?  77  VAL   A HG23 1 
ATOM   1816 N N    . GLY   A 1 78  ? 28.992 -6.532  -5.803  1.00 12.35 ?  78  GLY   A N    1 
ATOM   1817 C CA   . GLY   A 1 78  ? 28.970 -7.824  -5.150  1.00 12.72 ?  78  GLY   A CA   1 
ATOM   1818 C C    . GLY   A 1 78  ? 29.876 -7.918  -3.944  1.00 12.45 ?  78  GLY   A C    1 
ATOM   1819 O O    . GLY   A 1 78  ? 29.812 -8.926  -3.218  1.00 13.10 ?  78  GLY   A O    1 
ATOM   1820 H H    . GLY   A 1 78  ? 28.444 -5.959  -5.461  1.00 14.86 ?  78  GLY   A H    1 
ATOM   1821 H HA2  . GLY   A 1 78  ? 28.066 -8.016  -4.869  1.00 15.30 ?  78  GLY   A HA2  1 
ATOM   1822 H HA3  . GLY   A 1 78  ? 29.241 -8.501  -5.791  1.00 15.30 ?  78  GLY   A HA3  1 
ATOM   1823 N N    . GLY   A 1 79  ? 30.730 -6.914  -3.716  1.00 12.38 ?  79  GLY   A N    1 
ATOM   1824 C CA   . GLY   A 1 79  ? 31.683 -6.933  -2.632  1.00 12.51 ?  79  GLY   A CA   1 
ATOM   1825 C C    . GLY   A 1 79  ? 31.225 -6.134  -1.419  1.00 11.81 ?  79  GLY   A C    1 
ATOM   1826 O O    . GLY   A 1 79  ? 30.106 -5.624  -1.348  1.00 12.63 ?  79  GLY   A O    1 
ATOM   1827 H H    . GLY   A 1 79  ? 30.776 -6.202  -4.198  1.00 14.89 ?  79  GLY   A H    1 
ATOM   1828 H HA2  . GLY   A 1 79  ? 31.835 -7.859  -2.358  1.00 15.05 ?  79  GLY   A HA2  1 
ATOM   1829 H HA3  . GLY   A 1 79  ? 32.528 -6.572  -2.938  1.00 15.05 ?  79  GLY   A HA3  1 
ATOM   1830 N N    . SER   A 1 80  ? 32.126 -6.045  -0.441  1.00 12.76 ?  80  SER   A N    1 
ATOM   1831 C CA   . SER   A 1 80  ? 31.802 -5.412  0.829   1.00 12.26 ?  80  SER   A CA   1 
ATOM   1832 C C    . SER   A 1 80  ? 33.071 -4.958  1.533   1.00 12.22 ?  80  SER   A C    1 
ATOM   1833 O O    . SER   A 1 80  ? 34.186 -5.397  1.219   1.00 13.56 ?  80  SER   A O    1 
ATOM   1834 C CB   . SER   A 1 80  ? 31.035 -6.369  1.747   1.00 13.21 ?  80  SER   A CB   1 
ATOM   1835 O OG   . SER   A 1 80  ? 31.855 -7.431  2.216   1.00 14.94 ?  80  SER   A OG   1 
ATOM   1836 H H    . SER   A 1 80  ? 32.936 -6.324  -0.498  1.00 15.35 ?  80  SER   A H    1 
ATOM   1837 H HA   . SER   A 1 80  ? 31.247 -4.636  0.653   1.00 14.75 ?  80  SER   A HA   1 
ATOM   1838 H HB2  . SER   A 1 80  ? 30.705 -5.873  2.509   1.00 15.90 ?  80  SER   A HB2  1 
ATOM   1839 H HB3  . SER   A 1 80  ? 30.292 -6.747  1.251   1.00 15.90 ?  80  SER   A HB3  1 
ATOM   1840 H HG   . SER   A 1 80  ? 32.150 -7.873  1.562   1.00 17.96 ?  80  SER   A HG   1 
ATOM   1841 N N    . CYS   A 1 81  ? 32.875 -4.107  2.537   1.00 11.88 ?  81  CYS   A N    1 
ATOM   1842 C CA   . CYS   A 1 81  ? 33.921 -3.821  3.504   1.00 11.96 ?  81  CYS   A CA   1 
ATOM   1843 C C    . CYS   A 1 81  ? 33.278 -3.586  4.862   1.00 11.94 ?  81  CYS   A C    1 
ATOM   1844 O O    . CYS   A 1 81  ? 32.111 -3.187  4.950   1.00 13.26 ?  81  CYS   A O    1 
ATOM   1845 C CB   . CYS   A 1 81  ? 34.796 -2.640  3.079   1.00 13.04 ?  81  CYS   A CB   1 
ATOM   1846 S SG   . CYS   A 1 81  ? 33.908 -1.057  3.093   1.00 13.03 ?  81  CYS   A SG   1 
ATOM   1847 H H    . CYS   A 1 81  ? 32.135 -3.689  2.685   1.00 14.29 ?  81  CYS   A H    1 
ATOM   1848 H HA   . CYS   A 1 81  ? 34.495 -4.596  3.580   1.00 14.39 ?  81  CYS   A HA   1 
ATOM   1849 H HB2  . CYS   A 1 81  ? 35.553 -2.574  3.689   1.00 15.69 ?  81  CYS   A HB2  1 
ATOM   1850 H HB3  . CYS   A 1 81  ? 35.123 -2.800  2.176   1.00 15.69 ?  81  CYS   A HB3  1 
ATOM   1851 H HG   . CYS   A 1 81  ? 34.661 -0.185  2.753   1.00 15.68 ?  81  CYS   A HG   1 
ATOM   1852 N N    . VAL   A 1 82  ? 34.041 -3.860  5.919   1.00 12.40 ?  82  VAL   A N    1 
ATOM   1853 C CA   . VAL   A 1 82  ? 33.614 -3.614  7.289   1.00 12.71 ?  82  VAL   A CA   1 
ATOM   1854 C C    . VAL   A 1 82  ? 34.211 -2.299  7.759   1.00 12.85 ?  82  VAL   A C    1 
ATOM   1855 O O    . VAL   A 1 82  ? 35.436 -2.127  7.744   1.00 13.95 ?  82  VAL   A O    1 
ATOM   1856 C CB   . VAL   A 1 82  ? 34.035 -4.754  8.224   1.00 14.21 ?  82  VAL   A CB   1 
ATOM   1857 C CG1  . VAL   A 1 82  ? 33.596 -4.456  9.650   1.00 15.93 ?  82  VAL   A CG1  1 
ATOM   1858 C CG2  . VAL   A 1 82  ? 33.462 -6.076  7.751   1.00 15.36 ?  82  VAL   A CG2  1 
ATOM   1859 H H    . VAL   A 1 82  ? 34.830 -4.208  5.862   1.00 14.91 ?  82  VAL   A H    1 
ATOM   1860 H HA   . VAL   A 1 82  ? 32.645 -3.535  7.311   1.00 15.29 ?  82  VAL   A HA   1 
ATOM   1861 H HB   . VAL   A 1 82  ? 35.001 -4.821  8.216   1.00 17.09 ?  82  VAL   A HB   1 
ATOM   1862 H HG11 . VAL   A 1 82  ? 33.682 -5.262  10.178  1.00 19.16 ?  82  VAL   A HG11 1 
ATOM   1863 H HG12 . VAL   A 1 82  ? 34.163 -3.758  10.019  1.00 19.16 ?  82  VAL   A HG12 1 
ATOM   1864 H HG13 . VAL   A 1 82  ? 32.672 -4.160  9.642   1.00 19.16 ?  82  VAL   A HG13 1 
ATOM   1865 H HG21 . VAL   A 1 82  ? 33.705 -6.768  8.385   1.00 18.47 ?  82  VAL   A HG21 1 
ATOM   1866 H HG22 . VAL   A 1 82  ? 32.496 -6.001  7.695   1.00 18.47 ?  82  VAL   A HG22 1 
ATOM   1867 H HG23 . VAL   A 1 82  ? 33.828 -6.285  6.877   1.00 18.47 ?  82  VAL   A HG23 1 
ATOM   1868 N N    . LEU   A 1 83  ? 33.355 -1.374  8.176   1.00 12.35 ?  83  LEU   A N    1 
ATOM   1869 C CA   . LEU   A 1 83  ? 33.779 -0.110  8.758   1.00 12.46 ?  83  LEU   A CA   1 
ATOM   1870 C C    . LEU   A 1 83  ? 33.055 0.075   10.088  1.00 12.58 ?  83  LEU   A C    1 
ATOM   1871 O O    . LEU   A 1 83  ? 32.324 -0.810  10.549  1.00 13.16 ?  83  LEU   A O    1 
ATOM   1872 C CB   . LEU   A 1 83  ? 33.530 1.044   7.779   1.00 13.06 ?  83  LEU   A CB   1 
ATOM   1873 C CG   . LEU   A 1 83  ? 34.434 1.046   6.540   1.00 13.74 ?  83  LEU   A CG   1 
ATOM   1874 C CD1  . LEU   A 1 83  ? 34.008 2.120   5.560   1.00 14.53 ?  83  LEU   A CD1  1 
ATOM   1875 C CD2  . LEU   A 1 83  ? 35.906 1.239   6.927   1.00 14.49 ?  83  LEU   A CD2  1 
ATOM   1876 H H    . LEU   A 1 83  ? 32.499 -1.448  8.120   1.00 14.86 ?  83  LEU   A H    1 
ATOM   1877 H HA   . LEU   A 1 83  ? 34.730 -0.136  8.938   1.00 15.00 ?  83  LEU   A HA   1 
ATOM   1878 H HB2  . LEU   A 1 83  ? 32.610 1.000   7.461   1.00 15.72 ?  83  LEU   A HB2  1 
ATOM   1879 H HB3  . LEU   A 1 83  ? 33.667 1.891   8.235   1.00 15.72 ?  83  LEU   A HB3  1 
ATOM   1880 H HG   . LEU   A 1 83  ? 34.355 0.192   6.091   1.00 16.53 ?  83  LEU   A HG   1 
ATOM   1881 H HD11 . LEU   A 1 83  ? 34.596 2.095   4.787   1.00 17.47 ?  83  LEU   A HD11 1 
ATOM   1882 H HD12 . LEU   A 1 83  ? 33.094 1.955   5.286   1.00 17.47 ?  83  LEU   A HD12 1 
ATOM   1883 H HD13 . LEU   A 1 83  ? 34.074 2.987   5.992   1.00 17.47 ?  83  LEU   A HD13 1 
ATOM   1884 H HD21 . LEU   A 1 83  ? 36.429 1.408   6.124   1.00 17.43 ?  83  LEU   A HD21 1 
ATOM   1885 H HD22 . LEU   A 1 83  ? 35.981 1.999   7.529   1.00 17.43 ?  83  LEU   A HD22 1 
ATOM   1886 H HD23 . LEU   A 1 83  ? 36.229 0.439   7.367   1.00 17.43 ?  83  LEU   A HD23 1 
ATOM   1887 N N    . SER   A 1 84  ? 33.271 1.225   10.722  1.00 13.41 ?  84  SER   A N    1 
ATOM   1888 C CA   . SER   A 1 84  ? 32.618 1.486   11.995  1.00 13.59 ?  84  SER   A CA   1 
ATOM   1889 C C    . SER   A 1 84  ? 31.101 1.576   11.835  1.00 13.52 ?  84  SER   A C    1 
ATOM   1890 O O    . SER   A 1 84  ? 30.585 2.031   10.815  1.00 13.58 ?  84  SER   A O    1 
ATOM   1891 C CB   . SER   A 1 84  ? 33.120 2.805   12.568  1.00 14.83 ?  84  SER   A CB   1 
ATOM   1892 O OG   . SER   A 1 84  ? 32.472 3.095   13.787  1.00 15.84 ?  84  SER   A OG   1 
ATOM   1893 H H    . SER   A 1 84  ? 33.781 1.861   10.439  1.00 16.14 ?  84  SER   A H    1 
ATOM   1894 H HA   . SER   A 1 84  ? 32.826 0.770   12.616  1.00 16.35 ?  84  SER   A HA   1 
ATOM   1895 H HB2  . SER   A 1 84  ? 34.078 2.743   12.711  1.00 17.83 ?  84  SER   A HB2  1 
ATOM   1896 H HB3  . SER   A 1 84  ? 32.922 3.517   11.943  1.00 17.83 ?  84  SER   A HB3  1 
ATOM   1897 H HG   . SER   A 1 84  ? 32.771 3.811   14.111  1.00 19.05 ?  84  SER   A HG   1 
ATOM   1898 N N    . GLY   A 1 85  ? 30.381 1.167   12.878  1.00 14.27 ?  85  GLY   A N    1 
ATOM   1899 C CA   . GLY   A 1 85  ? 28.957 1.412   12.952  1.00 15.26 ?  85  GLY   A CA   1 
ATOM   1900 C C    . GLY   A 1 85  ? 28.579 2.726   13.599  1.00 14.90 ?  85  GLY   A C    1 
ATOM   1901 O O    . GLY   A 1 85  ? 27.387 3.037   13.701  1.00 15.59 ?  85  GLY   A O    1 
ATOM   1902 H H    . GLY   A 1 85  ? 30.701 0.740   13.552  1.00 17.16 ?  85  GLY   A H    1 
ATOM   1903 H HA2  . GLY   A 1 85  ? 28.586 1.400   12.054  1.00 18.35 ?  85  GLY   A HA2  1 
ATOM   1904 H HA3  . GLY   A 1 85  ? 28.539 0.702   13.457  1.00 18.35 ?  85  GLY   A HA3  1 
ATOM   1905 N N    . HIS   A 1 86  ? 29.560 3.503   14.049  1.00 14.31 ?  86  HIS   A N    1 
ATOM   1906 C CA   . HIS   A 1 86  ? 29.330 4.840   14.611  1.00 14.66 ?  86  HIS   A CA   1 
ATOM   1907 C C    . HIS   A 1 86  ? 28.334 4.719   15.758  1.00 15.58 ?  86  HIS   A C    1 
ATOM   1908 O O    . HIS   A 1 86  ? 28.518 3.853   16.628  1.00 17.02 ?  86  HIS   A O    1 
ATOM   1909 C CB   . HIS   A 1 86  ? 28.964 5.813   13.499  1.00 14.94 ?  86  HIS   A CB   1 
ATOM   1910 C CG   . HIS   A 1 86  ? 30.031 5.914   12.471  1.00 14.99 ?  86  HIS   A CG   1 
ATOM   1911 N ND1  . HIS   A 1 86  ? 31.118 6.751   12.612  1.00 15.99 ?  86  HIS   A ND1  1 
ATOM   1912 C CD2  . HIS   A 1 86  ? 30.223 5.229   11.322  1.00 14.86 ?  86  HIS   A CD2  1 
ATOM   1913 C CE1  . HIS   A 1 86  ? 31.924 6.586   11.579  1.00 15.74 ?  86  HIS   A CE1  1 
ATOM   1914 N NE2  . HIS   A 1 86  ? 31.411 5.661   10.789  1.00 15.31 ?  86  HIS   A NE2  1 
ATOM   1915 H H    . HIS   A 1 86  ? 30.384 3.282   14.046  1.00 17.21 ?  86  HIS   A H    1 
ATOM   1916 H HA   . HIS   A 1 86  ? 30.160 5.158   14.989  1.00 17.63 ?  86  HIS   A HA   1 
ATOM   1917 H HB2  . HIS   A 1 86  ? 28.147 5.520   13.062  1.00 17.97 ?  86  HIS   A HB2  1 
ATOM   1918 H HB3  . HIS   A 1 86  ? 28.827 6.704   13.875  1.00 17.97 ?  86  HIS   A HB3  1 
ATOM   1919 H HD2  . HIS   A 1 86  ? 29.662 4.572   10.964  1.00 17.87 ?  86  HIS   A HD2  1 
ATOM   1920 H HE1  . HIS   A 1 86  ? 32.719 7.041   11.424  1.00 18.93 ?  86  HIS   A HE1  1 
ATOM   1921 H HE2  . HIS   A 1 86  ? 31.753 5.388   10.040  1.00 18.41 ?  86  HIS   A HE2  1 
ATOM   1922 N N    . ASN   A 1 87  ? 27.306 5.558   15.811  1.00 16.71 ?  87  ASN   A N    1 
ATOM   1923 C CA   . ASN   A 1 87  ? 26.316 5.544   16.872  1.00 17.65 ?  87  ASN   A CA   1 
ATOM   1924 C C    . ASN   A 1 87  ? 25.190 4.555   16.617  1.00 18.62 ?  87  ASN   A C    1 
ATOM   1925 O O    . ASN   A 1 87  ? 24.244 4.505   17.406  1.00 21.14 ?  87  ASN   A O    1 
ATOM   1926 C CB   . ASN   A 1 87  ? 25.716 6.947   17.033  1.00 18.54 ?  87  ASN   A CB   1 
ATOM   1927 C CG   . ASN   A 1 87  ? 25.214 7.523   15.717  1.00 19.01 ?  87  ASN   A CG   1 
ATOM   1928 O OD1  . ASN   A 1 87  ? 25.865 7.400   14.685  1.00 19.66 ?  87  ASN   A OD1  1 
ATOM   1929 N ND2  . ASN   A 1 87  ? 24.051 8.151   15.752  1.00 20.16 ?  87  ASN   A ND2  1 
ATOM   1930 H H    . ASN   A 1 87  ? 27.153 6.164   15.221  1.00 20.09 ?  87  ASN   A H    1 
ATOM   1931 H HA   . ASN   A 1 87  ? 26.740 5.301   17.712  1.00 21.22 ?  87  ASN   A HA   1 
ATOM   1932 H HB2  . ASN   A 1 87  ? 24.964 6.900   17.650  1.00 22.29 ?  87  ASN   A HB2  1 
ATOM   1933 H HB3  . ASN   A 1 87  ? 26.395 7.540   17.385  1.00 22.29 ?  87  ASN   A HB3  1 
ATOM   1934 H HD21 . ASN   A 1 87  ? 23.729 8.491   15.034  1.00 24.23 ?  87  ASN   A HD21 1 
ATOM   1935 H HD22 . ASN   A 1 87  ? 23.626 8.226   16.496  1.00 24.23 ?  87  ASN   A HD22 1 
ATOM   1936 N N    . LEU   A 1 88  ? 25.263 3.771   15.547  1.00 17.29 ?  88  LEU   A N    1 
ATOM   1937 C CA   . LEU   A 1 88  ? 24.165 2.902   15.142  1.00 17.19 ?  88  LEU   A CA   1 
ATOM   1938 C C    . LEU   A 1 88  ? 24.387 1.427   15.438  1.00 17.10 ?  88  LEU   A C    1 
ATOM   1939 O O    . LEU   A 1 88  ? 23.411 0.691   15.585  1.00 18.02 ?  88  LEU   A O    1 
ATOM   1940 C CB   . LEU   A 1 88  ? 23.913 3.056   13.641  1.00 17.46 ?  88  LEU   A CB   1 
ATOM   1941 C CG   . LEU   A 1 88  ? 23.640 4.484   13.161  1.00 18.79 ?  88  LEU   A CG   1 
ATOM   1942 C CD1  . LEU   A 1 88  ? 23.477 4.513   11.656  1.00 19.22 ?  88  LEU   A CD1  1 
ATOM   1943 C CD2  . LEU   A 1 88  ? 22.406 5.069   13.842  1.00 20.42 ?  88  LEU   A CD2  1 
ATOM   1944 H H    . LEU   A 1 88  ? 25.953 3.722   15.035  1.00 20.78 ?  88  LEU   A H    1 
ATOM   1945 H HA   . LEU   A 1 88  ? 23.363 3.178   15.608  1.00 20.66 ?  88  LEU   A HA   1 
ATOM   1946 H HB2  . LEU   A 1 88  ? 24.688 2.736   13.161  1.00 20.99 ?  88  LEU   A HB2  1 
ATOM   1947 H HB3  . LEU   A 1 88  ? 23.138 2.523   13.405  1.00 20.99 ?  88  LEU   A HB3  1 
ATOM   1948 H HG   . LEU   A 1 88  ? 24.398 5.045   13.386  1.00 22.59 ?  88  LEU   A HG   1 
ATOM   1949 H HD11 . LEU   A 1 88  ? 23.357 5.432   11.366  1.00 23.10 ?  88  LEU   A HD11 1 
ATOM   1950 H HD12 . LEU   A 1 88  ? 24.269 4.137   11.244  1.00 23.10 ?  88  LEU   A HD12 1 
ATOM   1951 H HD13 . LEU   A 1 88  ? 22.697 3.987   11.413  1.00 23.10 ?  88  LEU   A HD13 1 
ATOM   1952 H HD21 . LEU   A 1 88  ? 22.203 5.927   13.438  1.00 24.55 ?  88  LEU   A HD21 1 
ATOM   1953 H HD22 . LEU   A 1 88  ? 21.664 4.460   13.720  1.00 24.55 ?  88  LEU   A HD22 1 
ATOM   1954 H HD23 . LEU   A 1 88  ? 22.595 5.183   14.785  1.00 24.55 ?  88  LEU   A HD23 1 
ATOM   1955 N N    . ALA   A 1 89  ? 25.639 0.983   15.507  1.00 16.19 ?  89  ALA   A N    1 
ATOM   1956 C CA   . ALA   A 1 89  ? 25.988 -0.427  15.614  1.00 16.05 ?  89  ALA   A CA   1 
ATOM   1957 C C    . ALA   A 1 89  ? 27.469 -0.485  15.950  1.00 16.39 ?  89  ALA   A C    1 
ATOM   1958 O O    . ALA   A 1 89  ? 28.182 0.514   15.839  1.00 17.10 ?  89  ALA   A O    1 
ATOM   1959 C CB   . ALA   A 1 89  ? 25.732 -1.146  14.292  1.00 15.57 ?  89  ALA   A CB   1 
ATOM   1960 H H    . ALA   A 1 89  ? 26.324 1.502   15.491  1.00 19.46 ?  89  ALA   A H    1 
ATOM   1961 H HA   . ALA   A 1 89  ? 25.476 -0.850  16.321  1.00 19.29 ?  89  ALA   A HA   1 
ATOM   1962 H HB1  . ALA   A 1 89  ? 25.981 -2.080  14.386  1.00 18.73 ?  89  ALA   A HB1  1 
ATOM   1963 H HB2  . ALA   A 1 89  ? 24.789 -1.079  14.068  1.00 18.73 ?  89  ALA   A HB2  1 
ATOM   1964 H HB3  . ALA   A 1 89  ? 26.266 -0.732  13.596  1.00 18.73 ?  89  ALA   A HB3  1 
ATOM   1965 N N    . LYS   A 1 90  ? 27.945 -1.664  16.345  1.00 16.95 ?  90  LYS   A N    1 
ATOM   1966 C CA   . LYS   A 1 90  ? 29.389 -1.812  16.499  1.00 18.10 ?  90  LYS   A CA   1 
ATOM   1967 C C    . LYS   A 1 90  ? 30.096 -1.627  15.160  1.00 16.52 ?  90  LYS   A C    1 
ATOM   1968 O O    . LYS   A 1 90  ? 31.029 -0.813  15.034  1.00 17.58 ?  90  LYS   A O    1 
ATOM   1969 C CB   . LYS   A 1 90  ? 29.728 -3.168  17.117  1.00 21.51 ?  90  LYS   A CB   1 
ATOM   1970 C CG   . LYS   A 1 90  ? 31.208 -3.315  17.452  1.00 26.95 ?  90  LYS   A CG   1 
ATOM   1971 C CD   . LYS   A 1 90  ? 31.463 -4.553  18.299  1.00 32.52 ?  90  LYS   A CD   1 
ATOM   1972 C CE   . LYS   A 1 90  ? 32.866 -4.555  18.895  1.00 37.05 ?  90  LYS   A CE   1 
ATOM   1973 N NZ   . LYS   A 1 90  ? 33.911 -4.959  17.915  1.00 39.59 ?  90  LYS   A NZ   1 
ATOM   1974 H H    . LYS   A 1 90  ? 27.472 -2.355  16.528  1.00 20.37 ?  90  LYS   A H    1 
ATOM   1975 H HA   . LYS   A 1 90  ? 29.710 -1.123  17.096  1.00 21.76 ?  90  LYS   A HA   1 
ATOM   1976 H HB2  . LYS   A 1 90  ? 29.221 -3.274  17.939  1.00 25.86 ?  90  LYS   A HB2  1 
ATOM   1977 H HB3  . LYS   A 1 90  ? 29.489 -3.870  16.491  1.00 25.86 ?  90  LYS   A HB3  1 
ATOM   1978 H HG2  . LYS   A 1 90  ? 31.716 -3.397  16.629  1.00 32.37 ?  90  LYS   A HG2  1 
ATOM   1979 H HG3  . LYS   A 1 90  ? 31.502 -2.536  17.951  1.00 32.37 ?  90  LYS   A HG3  1 
ATOM   1980 H HD2  . LYS   A 1 90  ? 30.823 -4.579  19.029  1.00 39.07 ?  90  LYS   A HD2  1 
ATOM   1981 H HD3  . LYS   A 1 90  ? 31.368 -5.344  17.745  1.00 39.07 ?  90  LYS   A HD3  1 
ATOM   1982 H HE2  . LYS   A 1 90  ? 33.077 -3.660  19.206  1.00 44.50 ?  90  LYS   A HE2  1 
ATOM   1983 H HE3  . LYS   A 1 90  ? 32.893 -5.178  19.637  1.00 44.50 ?  90  LYS   A HE3  1 
ATOM   1984 H HZ1  . LYS   A 1 90  ? 33.746 -5.781  17.616  1.00 47.55 ?  90  LYS   A HZ1  1 
ATOM   1985 H HZ2  . LYS   A 1 90  ? 33.918 -4.396  17.227  1.00 47.55 ?  90  LYS   A HZ2  1 
ATOM   1986 H HZ3  . LYS   A 1 90  ? 34.712 -4.949  18.305  1.00 47.55 ?  90  LYS   A HZ3  1 
ATOM   1987 N N    . HIS   A 1 91  ? 29.634 -2.350  14.138  1.00 14.51 ?  91  HIS   A N    1 
ATOM   1988 C CA   . HIS   A 1 91  ? 30.211 -2.335  12.808  1.00 13.79 ?  91  HIS   A CA   1 
ATOM   1989 C C    . HIS   A 1 91  ? 29.130 -2.063  11.778  1.00 13.03 ?  91  HIS   A C    1 
ATOM   1990 O O    . HIS   A 1 91  ? 27.963 -2.428  11.961  1.00 13.91 ?  91  HIS   A O    1 
ATOM   1991 C CB   . HIS   A 1 91  ? 30.809 -3.699  12.449  1.00 16.19 ?  91  HIS   A CB   1 
ATOM   1992 C CG   . HIS   A 1 91  ? 31.797 -4.211  13.445  1.00 20.35 ?  91  HIS   A CG   1 
ATOM   1993 N ND1  . HIS   A 1 91  ? 33.083 -3.724  13.535  1.00 22.48 ?  91  HIS   A ND1  1 
ATOM   1994 C CD2  . HIS   A 1 91  ? 31.693 -5.175  14.390  1.00 22.14 ?  91  HIS   A CD2  1 
ATOM   1995 C CE1  . HIS   A 1 91  ? 33.729 -4.363  14.494  1.00 23.56 ?  91  HIS   A CE1  1 
ATOM   1996 N NE2  . HIS   A 1 91  ? 32.908 -5.251  15.029  1.00 23.59 ?  91  HIS   A NE2  1 
ATOM   1997 H H    . HIS   A 1 91  ? 28.949 -2.889  14.203  1.00 17.44 ?  91  HIS   A H    1 
ATOM   1998 H HA   . HIS   A 1 91  ? 30.895 -1.660  12.746  1.00 16.58 ?  91  HIS   A HA   1 
ATOM   1999 H HB2  . HIS   A 1 91  ? 30.091 -4.350  12.385  1.00 19.46 ?  91  HIS   A HB2  1 
ATOM   2000 H HB3  . HIS   A 1 91  ? 31.259 -3.625  11.594  1.00 19.46 ?  91  HIS   A HB3  1 
ATOM   2001 H HD1  . HIS   A 1 91  ? 33.414 -3.099  13.039  1.00 27.01 ?  91  HIS   A HD1  1 
ATOM   2002 H HD2  . HIS   A 1 91  ? 30.945 -5.689  14.575  1.00 26.61 ?  91  HIS   A HD2  1 
ATOM   2003 H HE1  . HIS   A 1 91  ? 34.614 -4.209  14.745  1.00 28.31 ?  91  HIS   A HE1  1 
ATOM   2004 N N    . CYS   A 1 92  ? 29.540 -1.457  10.672  1.00 12.76 ?  92  CYS   A N    1 
ATOM   2005 C CA   . CYS   A 1 92  ? 28.717 -1.389  9.474   1.00 12.57 ?  92  CYS   A CA   1 
ATOM   2006 C C    . CYS   A 1 92  ? 29.370 -2.213  8.373   1.00 12.09 ?  92  CYS   A C    1 
ATOM   2007 O O    . CYS   A 1 92  ? 30.524 -1.958  8.003   1.00 12.87 ?  92  CYS   A O    1 
ATOM   2008 C CB   . CYS   A 1 92  ? 28.502 0.054   9.011   1.00 12.99 ?  92  CYS   A CB   1 
ATOM   2009 S SG   . CYS   A 1 92  ? 27.500 0.167   7.489   1.00 12.55 ?  92  CYS   A SG   1 
ATOM   2010 H H    . CYS   A 1 92  ? 30.303 -1.065  10.595  1.00 15.36 ?  92  CYS   A H    1 
ATOM   2011 H HA   . CYS   A 1 92  ? 27.849 -1.771  9.663   1.00 15.12 ?  92  CYS   A HA   1 
ATOM   2012 H HB2  . CYS   A 1 92  ? 28.037 0.550   9.708   1.00 15.62 ?  92  CYS   A HB2  1 
ATOM   2013 H HB3  . CYS   A 1 92  ? 29.361 0.468   8.832   1.00 15.62 ?  92  CYS   A HB3  1 
ATOM   2014 H HG   . CYS   A 1 92  ? 27.362 1.323   7.198   1.00 15.10 ?  92  CYS   A HG   1 
ATOM   2015 N N    . LEU   A 1 93  ? 28.629 -3.193  7.863   1.00 11.82 ?  93  LEU   A N    1 
ATOM   2016 C CA   . LEU   A 1 93  ? 29.032 -3.951  6.685   1.00 11.68 ?  93  LEU   A CA   1 
ATOM   2017 C C    . LEU   A 1 93  ? 28.445 -3.258  5.459   1.00 11.26 ?  93  LEU   A C    1 
ATOM   2018 O O    . LEU   A 1 93  ? 27.232 -3.318  5.221   1.00 11.46 ?  93  LEU   A O    1 
ATOM   2019 C CB   . LEU   A 1 93  ? 28.552 -5.398  6.794   1.00 12.11 ?  93  LEU   A CB   1 
ATOM   2020 C CG   . LEU   A 1 93  ? 28.945 -6.297  5.623   1.00 12.34 ?  93  LEU   A CG   1 
ATOM   2021 C CD1  . LEU   A 1 93  ? 30.451 -6.562  5.609   1.00 13.29 ?  93  LEU   A CD1  1 
ATOM   2022 C CD2  . LEU   A 1 93  ? 28.171 -7.613  5.668   1.00 13.25 ?  93  LEU   A CD2  1 
ATOM   2023 H H    . LEU   A 1 93  ? 27.870 -3.435  8.196   1.00 14.22 ?  93  LEU   A H    1 
ATOM   2024 H HA   . LEU   A 1 93  ? 29.995 -3.942  6.619   1.00 14.05 ?  93  LEU   A HA   1 
ATOM   2025 H HB2  . LEU   A 1 93  ? 28.927 -5.783  7.605   1.00 14.57 ?  93  LEU   A HB2  1 
ATOM   2026 H HB3  . LEU   A 1 93  ? 27.586 -5.398  6.854   1.00 14.57 ?  93  LEU   A HB3  1 
ATOM   2027 H HG   . LEU   A 1 93  ? 28.724 -5.850  4.800   1.00 14.85 ?  93  LEU   A HG   1 
ATOM   2028 H HD11 . LEU   A 1 93  ? 30.663 -7.168  4.884   1.00 15.99 ?  93  LEU   A HD11 1 
ATOM   2029 H HD12 . LEU   A 1 93  ? 30.925 -5.722  5.486   1.00 15.99 ?  93  LEU   A HD12 1 
ATOM   2030 H HD13 . LEU   A 1 93  ? 30.717 -6.962  6.458   1.00 15.99 ?  93  LEU   A HD13 1 
ATOM   2031 H HD21 . LEU   A 1 93  ? 28.448 -8.164  4.917   1.00 15.94 ?  93  LEU   A HD21 1 
ATOM   2032 H HD22 . LEU   A 1 93  ? 28.369 -8.072  6.501   1.00 15.94 ?  93  LEU   A HD22 1 
ATOM   2033 H HD23 . LEU   A 1 93  ? 27.225 -7.424  5.609   1.00 15.94 ?  93  LEU   A HD23 1 
ATOM   2034 N N    . HIS   A 1 94  ? 29.301 -2.563  4.708   1.00 10.94 ?  94  HIS   A N    1 
ATOM   2035 C CA   . HIS   A 1 94  ? 28.889 -1.892  3.478   1.00 11.38 ?  94  HIS   A CA   1 
ATOM   2036 C C    . HIS   A 1 94  ? 28.899 -2.929  2.367   1.00 11.11 ?  94  HIS   A C    1 
ATOM   2037 O O    . HIS   A 1 94  ? 29.967 -3.445  2.024   1.00 12.39 ?  94  HIS   A O    1 
ATOM   2038 C CB   . HIS   A 1 94  ? 29.853 -0.750  3.154   1.00 11.11 ?  94  HIS   A CB   1 
ATOM   2039 C CG   . HIS   A 1 94  ? 29.836 0.349   4.164   1.00 11.05 ?  94  HIS   A CG   1 
ATOM   2040 N ND1  . HIS   A 1 94  ? 28.956 1.410   4.106   1.00 11.36 ?  94  HIS   A ND1  1 
ATOM   2041 C CD2  . HIS   A 1 94  ? 30.572 0.519   5.285   1.00 11.88 ?  94  HIS   A CD2  1 
ATOM   2042 C CE1  . HIS   A 1 94  ? 29.171 2.196   5.146   1.00 11.61 ?  94  HIS   A CE1  1 
ATOM   2043 N NE2  . HIS   A 1 94  ? 30.145 1.678   5.875   1.00 11.92 ?  94  HIS   A NE2  1 
ATOM   2044 H H    . HIS   A 1 94  ? 30.135 -2.458  4.897   1.00 13.16 ?  94  HIS   A H    1 
ATOM   2045 H HA   . HIS   A 1 94  ? 27.988 -1.536  3.575   1.00 13.69 ?  94  HIS   A HA   1 
ATOM   2046 H HB2  . HIS   A 1 94  ? 30.750 -1.101  3.113   1.00 13.37 ?  94  HIS   A HB2  1 
ATOM   2047 H HB3  . HIS   A 1 94  ? 29.602 -0.365  2.299   1.00 13.37 ?  94  HIS   A HB3  1 
ATOM   2048 H HD2  . HIS   A 1 94  ? 31.249 -0.032  5.594   1.00 14.30 ?  94  HIS   A HD2  1 
ATOM   2049 H HE1  . HIS   A 1 94  ? 28.703 2.983   5.331   1.00 13.97 ?  94  HIS   A HE1  1 
ATOM   2050 H HE2  . HIS   A 1 94  ? 30.457 2.026   6.597   1.00 14.34 ?  94  HIS   A HE2  1 
ATOM   2051 N N    . VAL   A 1 95  ? 27.728 -3.249  1.812   1.00 10.48 ?  95  VAL   A N    1 
ATOM   2052 C CA   . VAL   A 1 95  ? 27.588 -4.291  0.796   1.00 10.75 ?  95  VAL   A CA   1 
ATOM   2053 C C    . VAL   A 1 95  ? 27.049 -3.656  -0.474  1.00 10.73 ?  95  VAL   A C    1 
ATOM   2054 O O    . VAL   A 1 95  ? 26.050 -2.926  -0.425  1.00 11.47 ?  95  VAL   A O    1 
ATOM   2055 C CB   . VAL   A 1 95  ? 26.653 -5.428  1.248   1.00 11.39 ?  95  VAL   A CB   1 
ATOM   2056 C CG1  . VAL   A 1 95  ? 26.547 -6.472  0.148   1.00 12.42 ?  95  VAL   A CG1  1 
ATOM   2057 C CG2  . VAL   A 1 95  ? 27.146 -6.043  2.537   1.00 11.71 ?  95  VAL   A CG2  1 
ATOM   2058 H H    . VAL   A 1 95  ? 26.982 -2.872  2.018   1.00 12.61 ?  95  VAL   A H    1 
ATOM   2059 H HA   . VAL   A 1 95  ? 28.456 -4.669  0.599   1.00 12.94 ?  95  VAL   A HA   1 
ATOM   2060 H HB   . VAL   A 1 95  ? 25.768 -5.070  1.403   1.00 13.71 ?  95  VAL   A HB   1 
ATOM   2061 H HG11 . VAL   A 1 95  ? 26.156 -7.283  0.514   1.00 14.95 ?  95  VAL   A HG11 1 
ATOM   2062 H HG12 . VAL   A 1 95  ? 25.988 -6.134  -0.569  1.00 14.95 ?  95  VAL   A HG12 1 
ATOM   2063 H HG13 . VAL   A 1 95  ? 27.437 -6.669  -0.195  1.00 14.95 ?  95  VAL   A HG13 1 
ATOM   2064 H HG21 . VAL   A 1 95  ? 26.579 -6.797  2.762   1.00 14.09 ?  95  VAL   A HG21 1 
ATOM   2065 H HG22 . VAL   A 1 95  ? 28.061 -6.336  2.419   1.00 14.09 ?  95  VAL   A HG22 1 
ATOM   2066 H HG23 . VAL   A 1 95  ? 27.099 -5.373  3.239   1.00 14.09 ?  95  VAL   A HG23 1 
ATOM   2067 N N    . VAL   A 1 96  ? 27.686 -3.949  -1.609  1.00 10.62 ?  96  VAL   A N    1 
ATOM   2068 C CA   . VAL   A 1 96  ? 27.282 -3.402  -2.899  1.00 11.35 ?  96  VAL   A CA   1 
ATOM   2069 C C    . VAL   A 1 96  ? 26.485 -4.451  -3.666  1.00 11.56 ?  96  VAL   A C    1 
ATOM   2070 O O    . VAL   A 1 96  ? 27.049 -5.400  -4.219  1.00 12.46 ?  96  VAL   A O    1 
ATOM   2071 C CB   . VAL   A 1 96  ? 28.482 -2.931  -3.721  1.00 11.65 ?  96  VAL   A CB   1 
ATOM   2072 C CG1  . VAL   A 1 96  ? 27.982 -2.292  -4.998  1.00 11.88 ?  96  VAL   A CG1  1 
ATOM   2073 C CG2  . VAL   A 1 96  ? 29.340 -1.957  -2.925  1.00 12.26 ?  96  VAL   A CG2  1 
ATOM   2074 H H    . VAL   A 1 96  ? 28.378 -4.469  -1.648  1.00 12.78 ?  96  VAL   A H    1 
ATOM   2075 H HA   . VAL   A 1 96  ? 26.708 -2.641  -2.743  1.00 13.66 ?  96  VAL   A HA   1 
ATOM   2076 H HB   . VAL   A 1 96  ? 29.027 -3.689  -3.958  1.00 14.02 ?  96  VAL   A HB   1 
ATOM   2077 H HG11 . VAL   A 1 96  ? 28.716 -1.808  -5.413  1.00 14.29 ?  96  VAL   A HG11 1 
ATOM   2078 H HG12 . VAL   A 1 96  ? 27.663 -2.982  -5.596  1.00 14.29 ?  96  VAL   A HG12 1 
ATOM   2079 H HG13 . VAL   A 1 96  ? 27.264 -1.674  -4.786  1.00 14.29 ?  96  VAL   A HG13 1 
ATOM   2080 H HG21 . VAL   A 1 96  ? 30.044 -1.616  -3.496  1.00 14.75 ?  96  VAL   A HG21 1 
ATOM   2081 H HG22 . VAL   A 1 96  ? 28.785 -1.226  -2.610  1.00 14.75 ?  96  VAL   A HG22 1 
ATOM   2082 H HG23 . VAL   A 1 96  ? 29.727 -2.426  -2.167  1.00 14.75 ?  96  VAL   A HG23 1 
ATOM   2083 N N    A GLY   A 1 97  ? 25.165 -4.304  -3.674  0.72 11.92 ?  97  GLY   A N    1 
ATOM   2084 N N    B GLY   A 1 97  ? 25.171 -4.267  -3.745  0.28 11.71 ?  97  GLY   A N    1 
ATOM   2085 C CA   A GLY   A 1 97  ? 24.343 -5.053  -4.587  0.72 12.58 ?  97  GLY   A CA   1 
ATOM   2086 C CA   B GLY   A 1 97  ? 24.365 -5.050  -4.649  0.28 11.87 ?  97  GLY   A CA   1 
ATOM   2087 C C    A GLY   A 1 97  ? 24.335 -4.372  -5.940  0.72 12.62 ?  97  GLY   A C    1 
ATOM   2088 C C    B GLY   A 1 97  ? 24.449 -4.503  -6.063  0.28 12.11 ?  97  GLY   A C    1 
ATOM   2089 O O    A GLY   A 1 97  ? 24.606 -3.171  -6.052  0.72 13.06 ?  97  GLY   A O    1 
ATOM   2090 O O    B GLY   A 1 97  ? 24.819 -3.344  -6.283  0.28 12.62 ?  97  GLY   A O    1 
ATOM   2091 H H    A GLY   A 1 97  ? 24.729 -3.770  -3.155  0.72 14.34 ?  97  GLY   A H    1 
ATOM   2092 H H    B GLY   A 1 97  ? 24.727 -3.695  -3.276  0.28 14.09 ?  97  GLY   A H    1 
ATOM   2093 H HA2  A GLY   A 1 97  ? 24.701 -5.947  -4.681  0.72 15.14 ?  97  GLY   A HA2  1 
ATOM   2094 H HA2  B GLY   A 1 97  ? 24.678 -5.970  -4.638  0.28 14.28 ?  97  GLY   A HA2  1 
ATOM   2095 H HA3  A GLY   A 1 97  ? 23.437 -5.107  -4.245  0.72 15.14 ?  97  GLY   A HA3  1 
ATOM   2096 H HA3  B GLY   A 1 97  ? 23.439 -5.035  -4.361  0.28 14.28 ?  97  GLY   A HA3  1 
ATOM   2097 N N    A PRO   A 1 98  ? 24.017 -5.115  -6.996  0.72 12.68 ?  98  PRO   A N    1 
ATOM   2098 N N    B PRO   A 1 98  ? 24.109 -5.325  -7.053  0.28 12.47 ?  98  PRO   A N    1 
ATOM   2099 C CA   A PRO   A 1 98  ? 23.913 -4.491  -8.318  0.72 13.38 ?  98  PRO   A CA   1 
ATOM   2100 C CA   B PRO   A 1 98  ? 24.109 -4.842  -8.440  0.28 13.09 ?  98  PRO   A CA   1 
ATOM   2101 C C    A PRO   A 1 98  ? 22.797 -3.457  -8.355  0.72 13.35 ?  98  PRO   A C    1 
ATOM   2102 C C    B PRO   A 1 98  ? 23.032 -3.789  -8.674  0.28 13.19 ?  98  PRO   A C    1 
ATOM   2103 O O    A PRO   A 1 98  ? 21.720 -3.649  -7.782  0.72 13.12 ?  98  PRO   A O    1 
ATOM   2104 O O    B PRO   A 1 98  ? 21.910 -3.891  -8.171  0.28 13.59 ?  98  PRO   A O    1 
ATOM   2105 C CB   A PRO   A 1 98  ? 23.615 -5.674  -9.247  0.72 13.54 ?  98  PRO   A CB   1 
ATOM   2106 C CB   B PRO   A 1 98  ? 23.830 -6.110  -9.257  0.28 13.13 ?  98  PRO   A CB   1 
ATOM   2107 C CG   A PRO   A 1 98  ? 22.985 -6.703  -8.361  0.72 13.69 ?  98  PRO   A CG   1 
ATOM   2108 C CG   B PRO   A 1 98  ? 23.143 -7.038  -8.295  0.28 13.36 ?  98  PRO   A CG   1 
ATOM   2109 C CD   A PRO   A 1 98  ? 23.687 -6.551  -7.029  0.72 13.14 ?  98  PRO   A CD   1 
ATOM   2110 C CD   B PRO   A 1 98  ? 23.788 -6.761  -6.968  0.28 12.65 ?  98  PRO   A CD   1 
ATOM   2111 H HA   A PRO   A 1 98  ? 24.755 -4.080  -8.563  0.72 16.09 ?  98  PRO   A HA   1 
ATOM   2112 H HA   B PRO   A 1 98  ? 24.984 -4.486  -8.680  0.28 15.74 ?  98  PRO   A HA   1 
ATOM   2113 H HB2  A PRO   A 1 98  ? 22.998 -5.396  -9.939  0.72 16.29 ?  98  PRO   A HB2  1 
ATOM   2114 H HB2  B PRO   A 1 98  ? 23.250 -5.895  -10.002 0.28 15.79 ?  98  PRO   A HB2  1 
ATOM   2115 H HB3  A PRO   A 1 98  ? 24.441 -6.007  -9.628  0.72 16.29 ?  98  PRO   A HB3  1 
ATOM   2116 H HB3  B PRO   A 1 98  ? 24.665 -6.495  -9.568  0.28 15.79 ?  98  PRO   A HB3  1 
ATOM   2117 H HG2  A PRO   A 1 98  ? 22.038 -6.526  -8.270  0.72 16.47 ?  98  PRO   A HG2  1 
ATOM   2118 H HG2  B PRO   A 1 98  ? 22.195 -6.834  -8.264  0.28 16.07 ?  98  PRO   A HG2  1 
ATOM   2119 H HG3  A PRO   A 1 98  ? 23.140 -7.589  -8.725  0.72 16.47 ?  98  PRO   A HG3  1 
ATOM   2120 H HG3  B PRO   A 1 98  ? 23.289 -7.958  -8.564  0.28 16.07 ?  98  PRO   A HG3  1 
ATOM   2121 H HD2  A PRO   A 1 98  ? 23.085 -6.783  -6.297  0.72 15.81 ?  98  PRO   A HD2  1 
ATOM   2122 H HD2  B PRO   A 1 98  ? 23.163 -6.927  -6.243  0.28 15.21 ?  98  PRO   A HD2  1 
ATOM   2123 H HD3  A PRO   A 1 98  ? 24.497 -7.086  -6.999  0.72 15.81 ?  98  PRO   A HD3  1 
ATOM   2124 H HD3  B PRO   A 1 98  ? 24.597 -7.292  -6.865  0.28 15.21 ?  98  PRO   A HD3  1 
ATOM   2125 N N    A ASN   A 1 99  ? 23.071 -2.347  -9.035  0.72 13.79 ?  99  ASN   A N    1 
ATOM   2126 N N    B ASN   A 1 99  ? 23.386 -2.771  -9.455  0.28 13.35 ?  99  ASN   A N    1 
ATOM   2127 C CA   A ASN   A 1 99  ? 22.092 -1.289  -9.264  0.72 15.13 ?  99  ASN   A CA   1 
ATOM   2128 C CA   B ASN   A 1 99  ? 22.468 -1.698  -9.840  0.28 14.17 ?  99  ASN   A CA   1 
ATOM   2129 C C    A ASN   A 1 99  ? 21.528 -1.467  -10.669 0.72 16.39 ?  99  ASN   A C    1 
ATOM   2130 C C    B ASN   A 1 99  ? 21.934 -2.027  -11.231 0.28 14.73 ?  99  ASN   A C    1 
ATOM   2131 O O    A ASN   A 1 99  ? 22.212 -1.193  -11.663 0.72 17.77 ?  99  ASN   A O    1 
ATOM   2132 O O    B ASN   A 1 99  ? 22.635 -1.863  -12.232 0.28 14.20 ?  99  ASN   A O    1 
ATOM   2133 C CB   A ASN   A 1 99  ? 22.733 0.087   -9.094  0.72 15.17 ?  99  ASN   A CB   1 
ATOM   2134 C CB   B ASN   A 1 99  ? 23.188 -0.353  -9.837  0.28 14.74 ?  99  ASN   A CB   1 
ATOM   2135 C CG   A ASN   A 1 99  ? 21.707 1.224   -9.086  0.72 15.62 ?  99  ASN   A CG   1 
ATOM   2136 C CG   B ASN   A 1 99  ? 22.254 0.813   -10.095 0.28 15.40 ?  99  ASN   A CG   1 
ATOM   2137 O OD1  A ASN   A 1 99  ? 20.702 1.178   -9.798  0.72 16.06 ?  99  ASN   A OD1  1 
ATOM   2138 O OD1  B ASN   A 1 99  ? 21.190 0.652   -10.688 0.28 15.02 ?  99  ASN   A OD1  1 
ATOM   2139 N ND2  A ASN   A 1 99  ? 21.961 2.246   -8.278  0.72 16.49 ?  99  ASN   A ND2  1 
ATOM   2140 N ND2  B ASN   A 1 99  ? 22.655 2.000   -9.658  0.28 16.56 ?  99  ASN   A ND2  1 
ATOM   2141 H H    A ASN   A 1 99  ? 23.846 -2.174  -9.363  0.72 16.59 ?  99  ASN   A H    1 
ATOM   2142 H H    B ASN   A 1 99  ? 24.177 -2.676  -9.773  0.28 16.06 ?  99  ASN   A H    1 
ATOM   2143 H HA   A ASN   A 1 99  ? 21.367 -1.377  -8.622  0.72 18.19 ?  99  ASN   A HA   1 
ATOM   2144 H HA   B ASN   A 1 99  ? 21.724 -1.668  -9.216  0.28 17.04 ?  99  ASN   A HA   1 
ATOM   2145 H HB2  A ASN   A 1 99  ? 23.219 0.110   -8.256  0.72 18.24 ?  99  ASN   A HB2  1 
ATOM   2146 H HB2  B ASN   A 1 99  ? 23.605 -0.223  -8.974  0.28 17.73 ?  99  ASN   A HB2  1 
ATOM   2147 H HB3  A ASN   A 1 99  ? 23.341 0.241   -9.835  0.72 18.24 ?  99  ASN   A HB3  1 
ATOM   2148 H HB3  B ASN   A 1 99  ? 23.860 -0.359  -10.535 0.28 17.73 ?  99  ASN   A HB3  1 
ATOM   2149 H HD21 A ASN   A 1 99  ? 21.414 2.907   -8.234  0.72 19.83 ?  99  ASN   A HD21 1 
ATOM   2150 H HD21 B ASN   A 1 99  ? 22.161 2.694   -9.778  0.28 19.91 ?  99  ASN   A HD21 1 
ATOM   2151 H HD22 A ASN   A 1 99  ? 22.676 2.247   -7.796  0.72 19.83 ?  99  ASN   A HD22 1 
ATOM   2152 H HD22 B ASN   A 1 99  ? 23.411 2.075   -9.258  0.28 19.91 ?  99  ASN   A HD22 1 
ATOM   2153 N N    A VAL   A 1 100 ? 20.279 -1.936  -10.743 0.72 17.10 ?  100 VAL   A N    1 
ATOM   2154 N N    B VAL   A 1 100 ? 20.681 -2.486  -11.289 0.28 16.62 ?  100 VAL   A N    1 
ATOM   2155 C CA   A VAL   A 1 100 ? 19.637 -2.188  -12.031 0.72 18.97 ?  100 VAL   A CA   1 
ATOM   2156 C CA   B VAL   A 1 100 ? 20.081 -2.866  -12.566 0.28 19.00 ?  100 VAL   A CA   1 
ATOM   2157 C C    A VAL   A 1 100 ? 19.528 -0.904  -12.840 0.72 20.07 ?  100 VAL   A C    1 
ATOM   2158 C C    B VAL   A 1 100 ? 19.946 -1.666  -13.492 0.28 19.50 ?  100 VAL   A C    1 
ATOM   2159 O O    A VAL   A 1 100 ? 19.596 -0.929  -14.075 0.72 21.40 ?  100 VAL   A O    1 
ATOM   2160 O O    B VAL   A 1 100 ? 19.964 -1.818  -14.720 0.28 19.63 ?  100 VAL   A O    1 
ATOM   2161 C CB   A VAL   A 1 100 ? 18.268 -2.879  -11.823 0.72 20.46 ?  100 VAL   A CB   1 
ATOM   2162 C CB   B VAL   A 1 100 ? 18.734 -3.577  -12.329 0.28 20.80 ?  100 VAL   A CB   1 
ATOM   2163 C CG1  A VAL   A 1 100 ? 17.533 -3.051  -13.144 0.72 21.59 ?  100 VAL   A CG1  1 
ATOM   2164 C CG1  B VAL   A 1 100 ? 17.799 -3.415  -13.526 0.28 21.47 ?  100 VAL   A CG1  1 
ATOM   2165 C CG2  A VAL   A 1 100 ? 18.458 -4.232  -11.149 0.72 20.64 ?  100 VAL   A CG2  1 
ATOM   2166 C CG2  B VAL   A 1 100 ? 18.974 -5.041  -12.043 0.28 21.57 ?  100 VAL   A CG2  1 
ATOM   2167 H H    A VAL   A 1 100 ? 19.780 -2.113  -10.059 0.72 20.56 ?  100 VAL   A H    1 
ATOM   2168 H H    B VAL   A 1 100 ? 20.163 -2.589  -10.610 0.28 19.99 ?  100 VAL   A H    1 
ATOM   2169 H HA   A VAL   A 1 100 ? 20.189 -2.804  -12.533 0.72 22.80 ?  100 VAL   A HA   1 
ATOM   2170 H HA   B VAL   A 1 100 ? 20.669 -3.499  -13.003 0.28 22.84 ?  100 VAL   A HA   1 
ATOM   2171 H HB   A VAL   A 1 100 ? 17.717 -2.333  -11.242 0.72 24.59 ?  100 VAL   A HB   1 
ATOM   2172 H HB   B VAL   A 1 100 ? 18.300 -3.181  -11.558 0.28 24.99 ?  100 VAL   A HB   1 
ATOM   2173 H HG11 A VAL   A 1 100 ? 16.781 -3.653  -13.013 0.72 25.95 ?  100 VAL   A HG11 1 
ATOM   2174 H HG11 B VAL   A 1 100 ? 17.063 -4.041  -13.431 0.28 25.80 ?  100 VAL   A HG11 1 
ATOM   2175 H HG12 A VAL   A 1 100 ? 17.213 -2.188  -13.446 0.72 25.95 ?  100 VAL   A HG12 1 
ATOM   2176 H HG12 B VAL   A 1 100 ? 17.452 -2.507  -13.545 0.28 25.80 ?  100 VAL   A HG12 1 
ATOM   2177 H HG13 A VAL   A 1 100 ? 18.143 -3.428  -13.798 0.72 25.95 ?  100 VAL   A HG13 1 
ATOM   2178 H HG13 B VAL   A 1 100 ? 18.287 -3.604  -14.342 0.28 25.80 ?  100 VAL   A HG13 1 
ATOM   2179 H HG21 A VAL   A 1 100 ? 17.595 -4.668  -11.063 0.72 24.81 ?  100 VAL   A HG21 1 
ATOM   2180 H HG21 B VAL   A 1 100 ? 18.138 -5.447  -11.774 0.28 25.93 ?  100 VAL   A HG21 1 
ATOM   2181 H HG22 A VAL   A 1 100 ? 19.049 -4.776  -11.694 0.72 24.81 ?  100 VAL   A HG22 1 
ATOM   2182 H HG22 B VAL   A 1 100 ? 19.308 -5.468  -12.848 0.28 25.93 ?  100 VAL   A HG22 1 
ATOM   2183 H HG23 A VAL   A 1 100 ? 18.849 -4.096  -10.272 0.72 24.81 ?  100 VAL   A HG23 1 
ATOM   2184 H HG23 B VAL   A 1 100 ? 19.626 -5.117  -11.331 0.28 25.93 ?  100 VAL   A HG23 1 
ATOM   2185 N N    A ASN   A 1 101 ? 19.355 0.235   -12.173 0.72 21.61 ?  101 ASN   A N    1 
ATOM   2186 N N    B ASN   A 1 101 ? 19.802 -0.462  -12.932 0.28 20.39 ?  101 ASN   A N    1 
ATOM   2187 C CA   A ASN   A 1 101 ? 19.290 1.505   -12.884 0.72 23.45 ?  101 ASN   A CA   1 
ATOM   2188 C CA   B ASN   A 1 101 ? 19.737 0.737   -13.760 0.28 21.63 ?  101 ASN   A CA   1 
ATOM   2189 C C    A ASN   A 1 101 ? 20.644 1.941   -13.439 0.72 25.70 ?  101 ASN   A C    1 
ATOM   2190 C C    B ASN   A 1 101 ? 21.090 1.096   -14.360 0.28 22.53 ?  101 ASN   A C    1 
ATOM   2191 O O    A ASN   A 1 101 ? 20.709 2.973   -14.119 0.72 27.13 ?  101 ASN   A O    1 
ATOM   2192 O O    B ASN   A 1 101 ? 21.138 1.877   -15.316 0.28 22.32 ?  101 ASN   A O    1 
ATOM   2193 C CB   A ASN   A 1 101 ? 18.684 2.571   -11.971 0.72 22.82 ?  101 ASN   A CB   1 
ATOM   2194 C CB   B ASN   A 1 101 ? 19.177 1.914   -12.954 0.28 22.49 ?  101 ASN   A CB   1 
ATOM   2195 C CG   A ASN   A 1 101 ? 17.320 2.162   -11.430 0.72 22.48 ?  101 ASN   A CG   1 
ATOM   2196 C CG   B ASN   A 1 101 ? 18.025 1.507   -12.053 0.28 23.62 ?  101 ASN   A CG   1 
ATOM   2197 O OD1  A ASN   A 1 101 ? 16.465 1.661   -12.167 0.72 23.19 ?  101 ASN   A OD1  1 
ATOM   2198 O OD1  B ASN   A 1 101 ? 16.900 1.301   -12.511 0.28 24.31 ?  101 ASN   A OD1  1 
ATOM   2199 N ND2  A ASN   A 1 101 ? 17.116 2.361   -10.137 0.72 22.84 ?  101 ASN   A ND2  1 
ATOM   2200 N ND2  B ASN   A 1 101 ? 18.305 1.385   -10.760 0.28 24.05 ?  101 ASN   A ND2  1 
ATOM   2201 H H    A ASN   A 1 101 ? 19.263 0.294   -11.322 0.72 25.97 ?  101 ASN   A H    1 
ATOM   2202 H H    B ASN   A 1 101 ? 19.732 -0.318  -12.088 0.28 24.51 ?  101 ASN   A H    1 
ATOM   2203 H HA   A ASN   A 1 101 ? 18.694 1.401   -13.639 0.72 28.17 ?  101 ASN   A HA   1 
ATOM   2204 H HA   B ASN   A 1 101 ? 19.135 0.576   -14.498 0.28 25.99 ?  101 ASN   A HA   1 
ATOM   2205 H HB2  A ASN   A 1 101 ? 19.274 2.723   -11.219 0.72 27.42 ?  101 ASN   A HB2  1 
ATOM   2206 H HB2  B ASN   A 1 101 ? 19.878 2.284   -12.396 0.28 27.03 ?  101 ASN   A HB2  1 
ATOM   2207 H HB3  A ASN   A 1 101 ? 18.573 3.395   -12.478 0.72 27.42 ?  101 ASN   A HB3  1 
ATOM   2208 H HB3  B ASN   A 1 101 ? 18.848 2.591   -13.568 0.28 27.03 ?  101 ASN   A HB3  1 
ATOM   2209 H HD21 A ASN   A 1 101 ? 16.362 2.148   -9.785  0.72 27.44 ?  101 ASN   A HD21 1 
ATOM   2210 H HD21 B ASN   A 1 101 ? 17.690 1.154   -10.206 0.28 28.90 ?  101 ASN   A HD21 1 
ATOM   2211 H HD22 A ASN   A 1 101 ? 17.735 2.708   -9.651  0.72 27.44 ?  101 ASN   A HD22 1 
ATOM   2212 H HD22 B ASN   A 1 101 ? 19.104 1.537   -10.477 0.28 28.90 ?  101 ASN   A HD22 1 
ATOM   2213 N N    A LYS   A 1 102 ? 21.711 1.181   -13.176 0.72 27.78 ?  102 LYS   A N    1 
ATOM   2214 N N    B LYS   A 1 102 ? 22.182 0.545   -13.829 0.28 23.98 ?  102 LYS   A N    1 
ATOM   2215 C CA   A LYS   A 1 102 ? 23.000 1.365   -13.832 0.72 29.56 ?  102 LYS   A CA   1 
ATOM   2216 C CA   B LYS   A 1 102 ? 23.516 0.727   -14.385 0.28 25.19 ?  102 LYS   A CA   1 
ATOM   2217 C C    A LYS   A 1 102 ? 23.323 0.252   -14.819 0.72 29.82 ?  102 LYS   A C    1 
ATOM   2218 C C    B LYS   A 1 102 ? 23.904 -0.389  -15.350 0.28 24.96 ?  102 LYS   A C    1 
ATOM   2219 O O    A LYS   A 1 102 ? 24.415 0.257   -15.395 0.72 30.36 ?  102 LYS   A O    1 
ATOM   2220 O O    B LYS   A 1 102 ? 25.071 -0.475  -15.745 0.28 25.13 ?  102 LYS   A O    1 
ATOM   2221 C CB   A LYS   A 1 102 ? 24.128 1.444   -12.796 0.72 31.55 ?  102 LYS   A CB   1 
ATOM   2222 C CB   B LYS   A 1 102 ? 24.563 0.789   -13.267 0.28 26.66 ?  102 LYS   A CB   1 
ATOM   2223 C CG   A LYS   A 1 102 ? 23.996 2.567   -11.788 0.72 33.29 ?  102 LYS   A CG   1 
ATOM   2224 C CG   B LYS   A 1 102 ? 24.567 2.063   -12.440 0.28 28.17 ?  102 LYS   A CG   1 
ATOM   2225 C CD   A LYS   A 1 102 ? 25.164 2.548   -10.811 0.72 35.08 ?  102 LYS   A CD   1 
ATOM   2226 C CD   B LYS   A 1 102 ? 25.723 2.039   -11.444 0.28 29.69 ?  102 LYS   A CD   1 
ATOM   2227 C CE   A LYS   A 1 102 ? 25.077 3.680   -9.801  0.72 36.53 ?  102 LYS   A CE   1 
ATOM   2228 C CE   B LYS   A 1 102 ? 25.620 3.156   -10.421 0.28 30.84 ?  102 LYS   A CE   1 
ATOM   2229 N NZ   A LYS   A 1 102 ? 26.197 3.622   -8.818  0.72 37.29 ?  102 LYS   A NZ   1 
ATOM   2230 N NZ   B LYS   A 1 102 ? 25.811 2.638   -9.035  0.28 31.55 ?  102 LYS   A NZ   1 
ATOM   2231 H H    A LYS   A 1 102 ? 21.711 0.534   -12.607 0.72 33.37 ?  102 LYS   A H    1 
ATOM   2232 H H    B LYS   A 1 102 ? 22.171 0.042   -13.131 0.28 28.82 ?  102 LYS   A H    1 
ATOM   2233 H HA   A LYS   A 1 102 ? 22.987 2.200   -14.320 0.72 35.51 ?  102 LYS   A HA   1 
ATOM   2234 H HA   B LYS   A 1 102 ? 23.544 1.576   -14.858 0.28 30.27 ?  102 LYS   A HA   1 
ATOM   2235 H HB2  A LYS   A 1 102 ? 24.155 0.609   -12.303 0.72 37.90 ?  102 LYS   A HB2  1 
ATOM   2236 H HB2  B LYS   A 1 102 ? 24.408 0.048   -12.661 0.28 32.03 ?  102 LYS   A HB2  1 
ATOM   2237 H HB3  A LYS   A 1 102 ? 24.969 1.571   -13.266 0.72 37.90 ?  102 LYS   A HB3  1 
ATOM   2238 H HB3  B LYS   A 1 102 ? 25.444 0.702   -13.664 0.28 32.03 ?  102 LYS   A HB3  1 
ATOM   2239 H HG2  A LYS   A 1 102 ? 23.996 3.418   -12.252 0.72 39.99 ?  102 LYS   A HG2  1 
ATOM   2240 H HG2  B LYS   A 1 102 ? 24.683 2.830   -13.022 0.28 33.84 ?  102 LYS   A HG2  1 
ATOM   2241 H HG3  A LYS   A 1 102 ? 23.174 2.454   -11.287 0.72 39.99 ?  102 LYS   A HG3  1 
ATOM   2242 H HG3  B LYS   A 1 102 ? 23.736 2.136   -11.947 0.28 33.84 ?  102 LYS   A HG3  1 
ATOM   2243 H HD2  A LYS   A 1 102 ? 25.161 1.707   -10.326 0.72 42.14 ?  102 LYS   A HD2  1 
ATOM   2244 H HD2  B LYS   A 1 102 ? 25.719 1.193   -10.970 0.28 35.66 ?  102 LYS   A HD2  1 
ATOM   2245 H HD3  A LYS   A 1 102 ? 25.995 2.645   -11.305 0.72 42.14 ?  102 LYS   A HD3  1 
ATOM   2246 H HD3  B LYS   A 1 102 ? 26.560 2.146   -11.925 0.28 35.66 ?  102 LYS   A HD3  1 
ATOM   2247 H HE2  A LYS   A 1 102 ? 25.125 4.530   -10.268 0.72 43.87 ?  102 LYS   A HE2  1 
ATOM   2248 H HE2  B LYS   A 1 102 ? 26.312 3.815   -10.596 0.28 37.04 ?  102 LYS   A HE2  1 
ATOM   2249 H HE3  A LYS   A 1 102 ? 24.240 3.612   -9.315  0.72 43.87 ?  102 LYS   A HE3  1 
ATOM   2250 H HE3  B LYS   A 1 102 ? 24.744 3.565   -10.477 0.28 37.04 ?  102 LYS   A HE3  1 
ATOM   2251 H HZ1  A LYS   A 1 102 ? 26.127 4.291   -8.237  0.72 44.79 ?  102 LYS   A HZ1  1 
ATOM   2252 H HZ1  B LYS   A 1 102 ? 25.614 3.272   -8.443  0.28 37.89 ?  102 LYS   A HZ1  1 
ATOM   2253 H HZ2  A LYS   A 1 102 ? 26.171 2.850   -8.375  0.72 44.79 ?  102 LYS   A HZ2  1 
ATOM   2254 H HZ2  B LYS   A 1 102 ? 25.278 1.938   -8.897  0.28 37.89 ?  102 LYS   A HZ2  1 
ATOM   2255 H HZ3  A LYS   A 1 102 ? 26.977 3.685   -9.242  0.72 44.79 ?  102 LYS   A HZ3  1 
ATOM   2256 H HZ3  B LYS   A 1 102 ? 26.655 2.383   -8.918  0.28 37.89 ?  102 LYS   A HZ3  1 
ATOM   2257 N N    A GLY   A 1 103 ? 22.422 -0.709  -15.016 0.72 30.09 ?  103 GLY   A N    1 
ATOM   2258 N N    B GLY   A 1 103 ? 22.963 -1.253  -15.723 0.28 24.78 ?  103 GLY   A N    1 
ATOM   2259 C CA   A GLY   A 1 103 ? 22.675 -1.801  -15.937 0.72 30.07 ?  103 GLY   A CA   1 
ATOM   2260 C CA   B GLY   A 1 103 ? 23.285 -2.359  -16.604 0.28 24.87 ?  103 GLY   A CA   1 
ATOM   2261 C C    A GLY   A 1 103 ? 23.504 -2.935  -15.378 0.72 30.03 ?  103 GLY   A C    1 
ATOM   2262 C C    B GLY   A 1 103 ? 24.056 -3.482  -15.953 0.28 24.84 ?  103 GLY   A C    1 
ATOM   2263 O O    A GLY   A 1 103 ? 24.022 -3.747  -16.151 0.72 31.18 ?  103 GLY   A O    1 
ATOM   2264 O O    B GLY   A 1 103 ? 24.691 -4.275  -16.654 0.28 25.47 ?  103 GLY   A O    1 
ATOM   2265 H H    A GLY   A 1 103 ? 21.657 -0.749  -14.627 0.72 36.14 ?  103 GLY   A H    1 
ATOM   2266 H H    B GLY   A 1 103 ? 22.139 -1.209  -15.481 0.28 29.77 ?  103 GLY   A H    1 
ATOM   2267 H HA2  A GLY   A 1 103 ? 21.826 -2.160  -16.246 0.72 36.12 ?  103 GLY   A HA2  1 
ATOM   2268 H HA2  B GLY   A 1 103 ? 22.466 -2.717  -16.985 0.28 29.88 ?  103 GLY   A HA2  1 
ATOM   2269 H HA3  A GLY   A 1 103 ? 23.146 -1.452  -16.712 0.72 36.12 ?  103 GLY   A HA3  1 
ATOM   2270 H HA3  B GLY   A 1 103 ? 23.837 -2.017  -17.324 0.28 29.88 ?  103 GLY   A HA3  1 
ATOM   2271 N N    A GLU   A 1 104 ? 23.643 -3.025  -14.059 0.72 27.95 ?  104 GLU   A N    1 
ATOM   2272 N N    B GLU   A 1 104 ? 24.018 -3.578  -14.630 0.28 23.77 ?  104 GLU   A N    1 
ATOM   2273 C CA   A GLU   A 1 104 ? 24.522 -4.016  -13.452 0.72 26.15 ?  104 GLU   A CA   1 
ATOM   2274 C CA   B GLU   A 1 104 ? 24.844 -4.532  -13.906 0.28 22.66 ?  104 GLU   A CA   1 
ATOM   2275 C C    A GLU   A 1 104 ? 23.841 -5.381  -13.344 0.72 26.14 ?  104 GLU   A C    1 
ATOM   2276 C C    B GLU   A 1 104 ? 24.132 -5.869  -13.730 0.28 21.96 ?  104 GLU   A C    1 
ATOM   2277 O O    A GLU   A 1 104 ? 22.624 -5.487  -13.168 0.72 26.18 ?  104 GLU   A O    1 
ATOM   2278 O O    B GLU   A 1 104 ? 22.901 -5.953  -13.712 0.28 21.72 ?  104 GLU   A O    1 
ATOM   2279 C CB   A GLU   A 1 104 ? 25.010 -3.511  -12.091 0.72 23.96 ?  104 GLU   A CB   1 
ATOM   2280 C CB   B GLU   A 1 104 ? 25.259 -3.960  -12.552 0.28 22.38 ?  104 GLU   A CB   1 
ATOM   2281 C CG   A GLU   A 1 104 ? 25.880 -2.254  -12.245 0.72 22.87 ?  104 GLU   A CG   1 
ATOM   2282 C CG   B GLU   A 1 104 ? 26.239 -2.801  -12.688 0.28 22.33 ?  104 GLU   A CG   1 
ATOM   2283 C CD   A GLU   A 1 104 ? 26.279 -1.562  -10.945 0.72 21.68 ?  104 GLU   A CD   1 
ATOM   2284 C CD   B GLU   A 1 104 ? 26.444 -2.026  -11.402 0.28 22.47 ?  104 GLU   A CD   1 
ATOM   2285 O OE1  A GLU   A 1 104 ? 25.717 -1.863  -9.874  0.72 20.01 ?  104 GLU   A OE1  1 
ATOM   2286 O OE1  B GLU   A 1 104 ? 25.913 -2.442  -10.352 0.28 22.79 ?  104 GLU   A OE1  1 
ATOM   2287 O OE2  A GLU   A 1 104 ? 27.167 -0.679  -11.017 0.72 22.64 -1 104 GLU   A OE2  1 
ATOM   2288 O OE2  B GLU   A 1 104 ? 27.142 -0.990  -11.446 0.28 22.38 -1 104 GLU   A OE2  1 
ATOM   2289 H H    A GLU   A 1 104 ? 23.244 -2.512  -13.499 0.72 33.57 ?  104 GLU   A H    1 
ATOM   2290 H H    B GLU   A 1 104 ? 23.520 -3.088  -14.132 0.28 28.56 ?  104 GLU   A H    1 
ATOM   2291 H HA   A GLU   A 1 104 ? 25.298 -4.121  -14.022 0.72 31.42 ?  104 GLU   A HA   1 
ATOM   2292 H HA   B GLU   A 1 104 ? 25.652 -4.682  -14.422 0.28 27.23 ?  104 GLU   A HA   1 
ATOM   2293 H HB2  A GLU   A 1 104 ? 24.243 -3.293  -11.540 0.72 28.79 ?  104 GLU   A HB2  1 
ATOM   2294 H HB2  B GLU   A 1 104 ? 24.471 -3.640  -12.088 0.28 26.89 ?  104 GLU   A HB2  1 
ATOM   2295 H HB3  A GLU   A 1 104 ? 25.541 -4.205  -11.672 0.72 28.79 ?  104 GLU   A HB3  1 
ATOM   2296 H HB3  B GLU   A 1 104 ? 25.688 -4.662  -12.038 0.28 26.89 ?  104 GLU   A HB3  1 
ATOM   2297 H HG2  A GLU   A 1 104 ? 26.694 -2.502  -12.705 0.72 27.49 ?  104 GLU   A HG2  1 
ATOM   2298 H HG2  B GLU   A 1 104 ? 27.101 -3.150  -12.963 0.28 26.83 ?  104 GLU   A HG2  1 
ATOM   2299 H HG3  A GLU   A 1 104 ? 25.388 -1.607  -12.775 0.72 27.49 ?  104 GLU   A HG3  1 
ATOM   2300 H HG3  B GLU   A 1 104 ? 25.904 -2.189  -13.363 0.28 26.83 ?  104 GLU   A HG3  1 
ATOM   2301 N N    A ASP   A 1 105 ? 24.654 -6.431  -13.449 0.72 26.71 ?  105 ASP   A N    1 
ATOM   2302 N N    B ASP   A 1 105 ? 24.939 -6.915  -13.575 0.28 22.08 ?  105 ASP   A N    1 
ATOM   2303 C CA   A ASP   A 1 105 ? 24.157 -7.795  -13.603 0.72 27.66 ?  105 ASP   A CA   1 
ATOM   2304 C CA   B ASP   A 1 105 ? 24.469 -8.294  -13.633 0.28 22.58 ?  105 ASP   A CA   1 
ATOM   2305 C C    A ASP   A 1 105 ? 23.491 -8.277  -12.316 0.72 25.42 ?  105 ASP   A C    1 
ATOM   2306 C C    B ASP   A 1 105 ? 23.687 -8.641  -12.370 0.28 21.77 ?  105 ASP   A C    1 
ATOM   2307 O O    A ASP   A 1 105 ? 24.128 -8.337  -11.260 0.72 23.98 ?  105 ASP   A O    1 
ATOM   2308 O O    B ASP   A 1 105 ? 24.241 -8.635  -11.266 0.28 20.56 ?  105 ASP   A O    1 
ATOM   2309 C CB   A ASP   A 1 105 ? 25.326 -8.706  -13.969 0.72 30.75 ?  105 ASP   A CB   1 
ATOM   2310 C CB   B ASP   A 1 105 ? 25.689 -9.204  -13.766 0.28 24.06 ?  105 ASP   A CB   1 
ATOM   2311 C CG   A ASP   A 1 105 ? 24.907 -10.142 -14.173 0.72 33.24 ?  105 ASP   A CG   1 
ATOM   2312 C CG   B ASP   A 1 105 ? 25.319 -10.649 -14.017 0.28 25.38 ?  105 ASP   A CG   1 
ATOM   2313 O OD1  A ASP   A 1 105 ? 23.689 -10.395 -14.286 0.72 33.79 ?  105 ASP   A OD1  1 
ATOM   2314 O OD1  B ASP   A 1 105 ? 24.113 -10.961 -14.097 0.28 25.58 ?  105 ASP   A OD1  1 
ATOM   2315 O OD2  A ASP   A 1 105 ? 25.799 -11.017 -14.217 0.72 34.70 -1 105 ASP   A OD2  1 
ATOM   2316 O OD2  B ASP   A 1 105 ? 26.246 -11.480 -14.128 0.28 25.85 -1 105 ASP   A OD2  1 
ATOM   2317 H H    A ASP   A 1 105 ? 25.510 -6.375  -13.435 0.72 32.09 ?  105 ASP   A H    1 
ATOM   2318 H H    B ASP   A 1 105 ? 25.777 -6.842  -13.425 0.28 26.53 ?  105 ASP   A H    1 
ATOM   2319 H HA   A ASP   A 1 105 ? 23.503 -7.828  -14.320 0.72 33.23 ?  105 ASP   A HA   1 
ATOM   2320 H HA   B ASP   A 1 105 ? 23.896 -8.423  -14.408 0.28 27.13 ?  105 ASP   A HA   1 
ATOM   2321 H HB2  A ASP   A 1 105 ? 25.727 -8.390  -14.795 0.72 36.94 ?  105 ASP   A HB2  1 
ATOM   2322 H HB2  B ASP   A 1 105 ? 26.246 -8.882  -14.499 0.28 28.91 ?  105 ASP   A HB2  1 
ATOM   2323 H HB3  A ASP   A 1 105 ? 25.980 -8.685  -13.255 0.72 36.94 ?  105 ASP   A HB3  1 
ATOM   2324 H HB3  B ASP   A 1 105 ? 26.194 -9.178  -12.939 0.28 28.91 ?  105 ASP   A HB3  1 
ATOM   2325 N N    A ILE   A 1 106 ? 22.212 -8.651  -12.411 0.72 24.83 ?  106 ILE   A N    1 
ATOM   2326 N N    B ILE   A 1 106 ? 22.399 -8.960  -12.529 0.28 22.43 ?  106 ILE   A N    1 
ATOM   2327 C CA   A ILE   A 1 106 ? 21.456 -9.062  -11.232 0.72 23.74 ?  106 ILE   A CA   1 
ATOM   2328 C CA   B ILE   A 1 106 ? 21.585 -9.342  -11.379 0.28 23.11 ?  106 ILE   A CA   1 
ATOM   2329 C C    A ILE   A 1 106 ? 21.985 -10.357 -10.630 0.72 22.41 ?  106 ILE   A C    1 
ATOM   2330 C C    B ILE   A 1 106 ? 22.115 -10.606 -10.722 0.28 23.50 ?  106 ILE   A C    1 
ATOM   2331 O O    A ILE   A 1 106 ? 21.762 -10.612 -9.443  0.72 21.74 ?  106 ILE   A O    1 
ATOM   2332 O O    B ILE   A 1 106 ? 21.874 -10.829 -9.531  0.28 23.58 ?  106 ILE   A O    1 
ATOM   2333 C CB   A ILE   A 1 106 ? 19.949 -9.132  -11.560 0.72 25.37 ?  106 ILE   A CB   1 
ATOM   2334 C CB   B ILE   A 1 106 ? 20.097 -9.484  -11.762 0.28 23.73 ?  106 ILE   A CB   1 
ATOM   2335 C CG1  A ILE   A 1 106 ? 19.109 -9.201  -10.281 0.72 26.11 ?  106 ILE   A CG1  1 
ATOM   2336 C CG1  B ILE   A 1 106 ? 19.209 -9.374  -10.521 0.28 24.16 ?  106 ILE   A CG1  1 
ATOM   2337 C CG2  A ILE   A 1 106 ? 19.652 -10.327 -12.442 0.72 26.12 ?  106 ILE   A CG2  1 
ATOM   2338 C CG2  B ILE   A 1 106 ? 19.841 -10.817 -12.423 0.28 23.95 ?  106 ILE   A CG2  1 
ATOM   2339 C CD1  A ILE   A 1 106 ? 19.225 -7.973  -9.399  0.72 26.59 ?  106 ILE   A CD1  1 
ATOM   2340 C CD1  B ILE   A 1 106 ? 19.054 -7.969  -9.995  0.28 24.38 ?  106 ILE   A CD1  1 
ATOM   2341 H H    A ILE   A 1 106 ? 21.766 -8.667  -13.143 0.72 29.84 ?  106 ILE   A H    1 
ATOM   2342 H H    B ILE   A 1 106 ? 21.984 -8.959  -13.280 0.28 26.96 ?  106 ILE   A H    1 
ATOM   2343 H HA   A ILE   A 1 106 ? 21.574 -8.381  -10.558 0.72 28.52 ?  106 ILE   A HA   1 
ATOM   2344 H HA   B ILE   A 1 106 ? 21.649 -8.639  -10.719 0.28 27.77 ?  106 ILE   A HA   1 
ATOM   2345 H HB   A ILE   A 1 106 ? 19.709 -8.326  -12.041 0.72 30.48 ?  106 ILE   A HB   1 
ATOM   2346 H HB   B ILE   A 1 106 ? 19.864 -8.773  -12.380 0.28 28.51 ?  106 ILE   A HB   1 
ATOM   2347 H HG12 A ILE   A 1 106 ? 18.176 -9.296  -10.529 0.72 31.37 ?  106 ILE   A HG12 1 
ATOM   2348 H HG12 B ILE   A 1 106 ? 18.325 -9.704  -10.741 0.28 29.03 ?  106 ILE   A HG12 1 
ATOM   2349 H HG13 A ILE   A 1 106 ? 19.390 -9.968  -9.760  0.72 31.37 ?  106 ILE   A HG13 1 
ATOM   2350 H HG13 B ILE   A 1 106 ? 19.592 -9.913  -9.811  0.28 29.03 ?  106 ILE   A HG13 1 
ATOM   2351 H HG21 A ILE   A 1 106 ? 18.752 -10.240 -12.788 0.72 31.38 ?  106 ILE   A HG21 1 
ATOM   2352 H HG21 B ILE   A 1 106 ? 19.004 -10.767 -12.908 0.28 28.78 ?  106 ILE   A HG21 1 
ATOM   2353 H HG22 A ILE   A 1 106 ? 20.290 -10.343 -13.170 0.72 31.38 ?  106 ILE   A HG22 1 
ATOM   2354 H HG22 B ILE   A 1 106 ? 20.569 -11.009 -13.030 0.28 28.78 ?  106 ILE   A HG22 1 
ATOM   2355 H HG23 A ILE   A 1 106 ? 19.729 -11.135 -11.912 0.72 31.38 ?  106 ILE   A HG23 1 
ATOM   2356 H HG23 B ILE   A 1 106 ? 19.787 -11.502 -11.738 0.28 28.78 ?  106 ILE   A HG23 1 
ATOM   2357 H HD11 A ILE   A 1 106 ? 18.508 -7.984  -8.748  0.72 31.95 ?  106 ILE   A HD11 1 
ATOM   2358 H HD11 B ILE   A 1 106 ? 18.461 -7.984  -9.227  0.28 29.30 ?  106 ILE   A HD11 1 
ATOM   2359 H HD12 A ILE   A 1 106 ? 20.083 -7.989  -8.944  0.72 31.95 ?  106 ILE   A HD12 1 
ATOM   2360 H HD12 B ILE   A 1 106 ? 19.924 -7.628  -9.734  0.28 29.30 ?  106 ILE   A HD12 1 
ATOM   2361 H HD13 A ILE   A 1 106 ? 19.159 -7.179  -9.952  0.72 31.95 ?  106 ILE   A HD13 1 
ATOM   2362 H HD13 B ILE   A 1 106 ? 18.676 -7.413  -10.693 0.28 29.30 ?  106 ILE   A HD13 1 
ATOM   2363 N N    A GLN   A 1 107 ? 22.713 -11.168 -11.410 0.72 23.32 ?  107 GLN   A N    1 
ATOM   2364 N N    B GLN   A 1 107 ? 22.839 -11.445 -11.470 0.28 24.06 ?  107 GLN   A N    1 
ATOM   2365 C CA   A GLN   A 1 107 ? 23.309 -12.389 -10.872 0.72 25.88 ?  107 GLN   A CA   1 
ATOM   2366 C CA   B GLN   A 1 107 ? 23.509 -12.589 -10.866 0.28 25.28 ?  107 GLN   A CA   1 
ATOM   2367 C C    A GLN   A 1 107 ? 24.280 -12.083 -9.734  0.72 23.26 ?  107 GLN   A C    1 
ATOM   2368 C C    B GLN   A 1 107 ? 24.469 -12.161 -9.766  0.28 22.78 ?  107 GLN   A C    1 
ATOM   2369 O O    A GLN   A 1 107 ? 24.477 -12.911 -8.838  0.72 24.45 ?  107 GLN   A O    1 
ATOM   2370 O O    B GLN   A 1 107 ? 24.854 -12.993 -8.937  0.28 23.41 ?  107 GLN   A O    1 
ATOM   2371 C CB   A GLN   A 1 107 ? 24.009 -13.155 -12.001 0.72 30.83 ?  107 GLN   A CB   1 
ATOM   2372 C CB   B GLN   A 1 107 ? 24.271 -13.381 -11.933 0.28 28.72 ?  107 GLN   A CB   1 
ATOM   2373 C CG   A GLN   A 1 107 ? 23.134 -13.359 -13.237 0.72 36.02 ?  107 GLN   A CG   1 
ATOM   2374 C CG   B GLN   A 1 107 ? 23.388 -13.966 -13.023 0.28 31.96 ?  107 GLN   A CG   1 
ATOM   2375 C CD   A GLN   A 1 107 ? 21.844 -14.091 -12.921 0.72 40.40 ?  107 GLN   A CD   1 
ATOM   2376 C CD   B GLN   A 1 107 ? 22.454 -15.040 -12.501 0.28 34.74 ?  107 GLN   A CD   1 
ATOM   2377 O OE1  A GLN   A 1 107 ? 21.855 -15.139 -12.273 0.72 42.09 ?  107 GLN   A OE1  1 
ATOM   2378 O OE1  B GLN   A 1 107 ? 22.832 -15.852 -11.657 0.28 35.77 ?  107 GLN   A OE1  1 
ATOM   2379 N NE2  A GLN   A 1 107 ? 20.722 -13.539 -13.371 0.72 41.93 ?  107 GLN   A NE2  1 
ATOM   2380 N NE2  B GLN   A 1 107 ? 21.223 -15.045 -12.999 0.28 35.71 ?  107 GLN   A NE2  1 
ATOM   2381 H H    A GLN   A 1 107 ? 22.890 -11.022 -12.239 0.72 28.02 ?  107 GLN   A H    1 
ATOM   2382 H H    B GLN   A 1 107 ? 22.961 -11.373 -12.317 0.28 28.91 ?  107 GLN   A H    1 
ATOM   2383 H HA   A GLN   A 1 107 ? 22.612 -12.958 -10.522 0.72 31.09 ?  107 GLN   A HA   1 
ATOM   2384 H HA   B GLN   A 1 107 ? 22.846 -13.180 -10.475 0.28 30.37 ?  107 GLN   A HA   1 
ATOM   2385 H HB2  A GLN   A 1 107 ? 24.799 -12.665 -12.281 0.72 37.03 ?  107 GLN   A HB2  1 
ATOM   2386 H HB2  B GLN   A 1 107 ? 24.914 -12.795 -12.360 0.28 34.50 ?  107 GLN   A HB2  1 
ATOM   2387 H HB3  A GLN   A 1 107 ? 24.266 -14.035 -11.682 0.72 37.03 ?  107 GLN   A HB3  1 
ATOM   2388 H HB3  B GLN   A 1 107 ? 24.735 -14.120 -11.506 0.28 34.50 ?  107 GLN   A HB3  1 
ATOM   2389 H HG2  A GLN   A 1 107 ? 22.902 -12.495 -13.616 0.72 43.26 ?  107 GLN   A HG2  1 
ATOM   2390 H HG2  B GLN   A 1 107 ? 22.847 -13.259 -13.407 0.28 38.39 ?  107 GLN   A HG2  1 
ATOM   2391 H HG3  A GLN   A 1 107 ? 23.624 -13.881 -13.891 0.72 43.26 ?  107 GLN   A HG3  1 
ATOM   2392 H HG3  B GLN   A 1 107 ? 23.950 -14.363 -13.708 0.28 38.39 ?  107 GLN   A HG3  1 
ATOM   2393 H HE21 A GLN   A 1 107 ? 20.752 -12.805 -13.819 0.72 50.36 ?  107 GLN   A HE21 1 
ATOM   2394 H HE21 B GLN   A 1 107 ? 20.995 -14.460 -13.586 0.28 42.88 ?  107 GLN   A HE21 1 
ATOM   2395 H HE22 A GLN   A 1 107 ? 19.966 -13.917 -13.216 0.72 50.36 ?  107 GLN   A HE22 1 
ATOM   2396 H HE22 B GLN   A 1 107 ? 20.656 -15.634 -12.735 0.28 42.88 ?  107 GLN   A HE22 1 
ATOM   2397 N N    . LEU   A 1 108 ? 24.870 -10.887 -9.735  1.00 20.09 ?  108 LEU   A N    1 
ATOM   2398 C CA   . LEU   A 1 108 ? 25.760 -10.438 -8.675  1.00 16.65 ?  108 LEU   A CA   1 
ATOM   2399 C C    . LEU   A 1 108 ? 25.041 -10.254 -7.346  1.00 15.00 ?  108 LEU   A C    1 
ATOM   2400 O O    . LEU   A 1 108 ? 25.709 -10.084 -6.324  1.00 15.23 ?  108 LEU   A O    1 
ATOM   2401 C CB   . LEU   A 1 108 ? 26.479 -9.145  -9.082  1.00 16.75 ?  108 LEU   A CB   1 
ATOM   2402 C CG   . LEU   A 1 108 ? 27.503 -9.345  -10.201 1.00 18.28 ?  108 LEU   A CG   1 
ATOM   2403 C CD1  . LEU   A 1 108 ? 27.986 -8.014  -10.749 1.00 19.25 ?  108 LEU   A CD1  1 
ATOM   2404 C CD2  . LEU   A 1 108 ? 28.684 -10.172 -9.715  1.00 20.02 ?  108 LEU   A CD2  1 
ATOM   2405 H H    A LEU   A 1 108 ? 24.760 -10.311 -10.356 0.72 24.15 ?  108 LEU   A H    1 
ATOM   2406 H H    B LEU   A 1 108 ? 24.653 -10.292 -10.307 0.28 24.15 ?  108 LEU   A H    1 
ATOM   2407 H HA   . LEU   A 1 108 ? 26.436 -11.119 -8.536  1.00 20.02 ?  108 LEU   A HA   1 
ATOM   2408 H HB2  . LEU   A 1 108 ? 25.819 -8.507  -9.392  1.00 20.14 ?  108 LEU   A HB2  1 
ATOM   2409 H HB3  . LEU   A 1 108 ? 26.944 -8.794  -8.311  1.00 20.14 ?  108 LEU   A HB3  1 
ATOM   2410 H HG   . LEU   A 1 108 ? 27.083 -9.830  -10.928 1.00 21.97 ?  108 LEU   A HG   1 
ATOM   2411 H HD11 . LEU   A 1 108 ? 28.618 -8.179  -11.470 1.00 23.14 ?  108 LEU   A HD11 1 
ATOM   2412 H HD12 . LEU   A 1 108 ? 27.228 -7.513  -11.084 1.00 23.14 ?  108 LEU   A HD12 1 
ATOM   2413 H HD13 . LEU   A 1 108 ? 28.424 -7.518  -10.038 1.00 23.14 ?  108 LEU   A HD13 1 
ATOM   2414 H HD21 . LEU   A 1 108 ? 29.393 -10.123 -10.372 1.00 24.06 ?  108 LEU   A HD21 1 
ATOM   2415 H HD22 . LEU   A 1 108 ? 28.990 -9.812  -8.867  1.00 24.06 ?  108 LEU   A HD22 1 
ATOM   2416 H HD23 . LEU   A 1 108 ? 28.399 -11.092 -9.599  1.00 24.06 ?  108 LEU   A HD23 1 
ATOM   2417 N N    . LEU   A 1 109 ? 23.705 -10.306 -7.327  1.00 14.22 ?  109 LEU   A N    1 
ATOM   2418 C CA   . LEU   A 1 109 ? 22.989 -10.181 -6.063  1.00 13.89 ?  109 LEU   A CA   1 
ATOM   2419 C C    . LEU   A 1 109 ? 23.325 -11.331 -5.116  1.00 13.46 ?  109 LEU   A C    1 
ATOM   2420 O O    . LEU   A 1 109 ? 23.456 -11.131 -3.904  1.00 13.80 ?  109 LEU   A O    1 
ATOM   2421 C CB   . LEU   A 1 109 ? 21.486 -10.107 -6.330  1.00 14.72 ?  109 LEU   A CB   1 
ATOM   2422 C CG   . LEU   A 1 109 ? 20.586 -9.811  -5.133  1.00 14.93 ?  109 LEU   A CG   1 
ATOM   2423 C CD1  . LEU   A 1 109 ? 21.029 -8.547  -4.412  1.00 14.86 ?  109 LEU   A CD1  1 
ATOM   2424 C CD2  . LEU   A 1 109 ? 19.126 -9.686  -5.592  1.00 15.99 ?  109 LEU   A CD2  1 
ATOM   2425 H H    . LEU   A 1 109 ? 23.200 -10.415 -8.015  1.00 17.10 ?  109 LEU   A H    1 
ATOM   2426 H HA   . LEU   A 1 109 ? 23.260 -9.354  -5.636  1.00 16.71 ?  109 LEU   A HA   1 
ATOM   2427 H HB2  . LEU   A 1 109 ? 21.330 -9.409  -6.982  1.00 17.70 ?  109 LEU   A HB2  1 
ATOM   2428 H HB3  . LEU   A 1 109 ? 21.200 -10.958 -6.691  1.00 17.70 ?  109 LEU   A HB3  1 
ATOM   2429 H HG   . LEU   A 1 109 ? 20.636 -10.542 -4.502  1.00 17.96 ?  109 LEU   A HG   1 
ATOM   2430 H HD11 . LEU   A 1 109 ? 20.342 -8.272  -3.786  1.00 17.87 ?  109 LEU   A HD11 1 
ATOM   2431 H HD12 . LEU   A 1 109 ? 21.858 -8.724  -3.938  1.00 17.87 ?  109 LEU   A HD12 1 
ATOM   2432 H HD13 . LEU   A 1 109 ? 21.173 -7.841  -5.069  1.00 17.87 ?  109 LEU   A HD13 1 
ATOM   2433 H HD21 . LEU   A 1 109 ? 18.580 -9.379  -4.848  1.00 19.23 ?  109 LEU   A HD21 1 
ATOM   2434 H HD22 . LEU   A 1 109 ? 19.073 -9.046  -6.320  1.00 19.23 ?  109 LEU   A HD22 1 
ATOM   2435 H HD23 . LEU   A 1 109 ? 18.812 -10.554 -5.893  1.00 19.23 ?  109 LEU   A HD23 1 
ATOM   2436 N N    . LYS   A 1 110 ? 23.470 -12.547 -5.643  1.00 13.28 ?  110 LYS   A N    1 
ATOM   2437 C CA   . LYS   A 1 110 ? 23.844 -13.663 -4.779  1.00 13.34 ?  110 LYS   A CA   1 
ATOM   2438 C C    . LYS   A 1 110 ? 25.222 -13.437 -4.168  1.00 12.77 ?  110 LYS   A C    1 
ATOM   2439 O O    . LYS   A 1 110 ? 25.415 -13.642 -2.967  1.00 13.08 ?  110 LYS   A O    1 
ATOM   2440 C CB   . LYS   A 1 110 ? 23.769 -14.987 -5.543  1.00 14.34 ?  110 LYS   A CB   1 
ATOM   2441 C CG   . LYS   A 1 110 ? 23.958 -16.204 -4.642  1.00 14.67 ?  110 LYS   A CG   1 
ATOM   2442 C CD   . LYS   A 1 110 ? 23.715 -17.519 -5.368  1.00 15.20 ?  110 LYS   A CD   1 
ATOM   2443 C CE   . LYS   A 1 110 ? 23.847 -18.700 -4.422  1.00 16.12 ?  110 LYS   A CE   1 
ATOM   2444 N NZ   . LYS   A 1 110 ? 22.674 -18.850 -3.526  1.00 16.21 ?  110 LYS   A NZ   1 
ATOM   2445 H H    . LYS   A 1 110 ? 23.351 -12.748 -6.466  1.00 15.97 ?  110 LYS   A H    1 
ATOM   2446 H HA   . LYS   A 1 110 ? 23.202 -13.714 -4.048  1.00 16.05 ?  110 LYS   A HA   1 
ATOM   2447 H HB2  . LYS   A 1 110 ? 22.898 -15.060 -5.966  1.00 17.24 ?  110 LYS   A HB2  1 
ATOM   2448 H HB3  . LYS   A 1 110 ? 24.466 -15.002 -6.214  1.00 17.24 ?  110 LYS   A HB3  1 
ATOM   2449 H HG2  . LYS   A 1 110 ? 24.864 -16.207 -4.301  1.00 17.64 ?  110 LYS   A HG2  1 
ATOM   2450 H HG3  . LYS   A 1 110 ? 23.327 -16.148 -3.904  1.00 17.64 ?  110 LYS   A HG3  1 
ATOM   2451 H HD2  . LYS   A 1 110 ? 22.819 -17.524 -5.735  1.00 18.28 ?  110 LYS   A HD2  1 
ATOM   2452 H HD3  . LYS   A 1 110 ? 24.372 -17.617 -6.075  1.00 18.28 ?  110 LYS   A HD3  1 
ATOM   2453 H HE2  . LYS   A 1 110 ? 23.944 -19.513 -4.941  1.00 19.38 ?  110 LYS   A HE2  1 
ATOM   2454 H HE3  . LYS   A 1 110 ? 24.638 -18.570 -3.865  1.00 19.38 ?  110 LYS   A HE3  1 
ATOM   2455 H HZ1  . LYS   A 1 110 ? 22.786 -19.549 -2.988  1.00 19.49 ?  110 LYS   A HZ1  1 
ATOM   2456 H HZ2  . LYS   A 1 110 ? 22.569 -18.117 -3.032  1.00 19.49 ?  110 LYS   A HZ2  1 
ATOM   2457 H HZ3  . LYS   A 1 110 ? 21.937 -18.976 -4.013  1.00 19.49 ?  110 LYS   A HZ3  1 
ATOM   2458 N N    . SER   A 1 111 ? 26.185 -12.991 -4.978  1.00 12.90 ?  111 SER   A N    1 
ATOM   2459 C CA   . SER   A 1 111 ? 27.514 -12.690 -4.451  1.00 13.04 ?  111 SER   A CA   1 
ATOM   2460 C C    . SER   A 1 111 ? 27.447 -11.638 -3.346  1.00 12.41 ?  111 SER   A C    1 
ATOM   2461 O O    . SER   A 1 111 ? 28.142 -11.743 -2.331  1.00 13.12 ?  111 SER   A O    1 
ATOM   2462 C CB   . SER   A 1 111 ? 28.419 -12.210 -5.587  1.00 14.24 ?  111 SER   A CB   1 
ATOM   2463 O OG   . SER   A 1 111 ? 28.490 -13.192 -6.610  1.00 16.31 ?  111 SER   A OG   1 
ATOM   2464 H H    . SER   A 1 111 ? 26.089 -12.852 -5.819  1.00 15.52 ?  111 SER   A H    1 
ATOM   2465 H HA   . SER   A 1 111 ? 27.897 -13.501 -4.078  1.00 15.69 ?  111 SER   A HA   1 
ATOM   2466 H HB2  . SER   A 1 111 ? 28.048 -11.404 -5.970  1.00 17.13 ?  111 SER   A HB2  1 
ATOM   2467 H HB3  . SER   A 1 111 ? 29.306 -12.040 -5.233  1.00 17.13 ?  111 SER   A HB3  1 
ATOM   2468 H HG   . SER   A 1 111 ? 29.014 -12.931 -7.221  1.00 19.61 ?  111 SER   A HG   1 
ATOM   2469 N N    . ALA   A 1 112 ? 26.607 -10.616 -3.529  1.00 12.49 ?  112 ALA   A N    1 
ATOM   2470 C CA   . ALA   A 1 112 ? 26.457 -9.580  -2.512  1.00 12.33 ?  112 ALA   A CA   1 
ATOM   2471 C C    . ALA   A 1 112 ? 25.970 -10.182 -1.197  1.00 12.15 ?  112 ALA   A C    1 
ATOM   2472 O O    . ALA   A 1 112 ? 26.513 -9.886  -0.126  1.00 12.62 ?  112 ALA   A O    1 
ATOM   2473 C CB   . ALA   A 1 112 ? 25.504 -8.492  -3.014  1.00 12.72 ?  112 ALA   A CB   1 
ATOM   2474 H H    . ALA   A 1 112 ? 26.120 -10.501 -4.227  1.00 15.03 ?  112 ALA   A H    1 
ATOM   2475 H HA   . ALA   A 1 112 ? 27.320 -9.166  -2.351  1.00 14.84 ?  112 ALA   A HA   1 
ATOM   2476 H HB1  . ALA   A 1 112 ? 25.427 -7.799  -2.335  1.00 15.31 ?  112 ALA   A HB1  1 
ATOM   2477 H HB2  . ALA   A 1 112 ? 25.853 -8.113  -3.833  1.00 15.31 ?  112 ALA   A HB2  1 
ATOM   2478 H HB3  . ALA   A 1 112 ? 24.630 -8.886  -3.178  1.00 15.31 ?  112 ALA   A HB3  1 
ATOM   2479 N N    . TYR   A 1 113 ? 24.932 -11.025 -1.258  1.00 12.45 ?  113 TYR   A N    1 
ATOM   2480 C CA   . TYR   A 1 113 ? 24.411 -11.640 -0.039  1.00 12.26 ?  113 TYR   A CA   1 
ATOM   2481 C C    . TYR   A 1 113 ? 25.415 -12.586 0.616   1.00 11.83 ?  113 TYR   A C    1 
ATOM   2482 O O    . TYR   A 1 113 ? 25.369 -12.770 1.836   1.00 12.49 ?  113 TYR   A O    1 
ATOM   2483 C CB   . TYR   A 1 113 ? 23.098 -12.374 -0.325  1.00 12.26 ?  113 TYR   A CB   1 
ATOM   2484 C CG   . TYR   A 1 113 ? 21.879 -11.484 -0.246  1.00 12.55 ?  113 TYR   A CG   1 
ATOM   2485 C CD1  . TYR   A 1 113 ? 21.504 -10.888 0.955   1.00 13.11 ?  113 TYR   A CD1  1 
ATOM   2486 C CD2  . TYR   A 1 113 ? 21.079 -11.260 -1.361  1.00 12.95 ?  113 TYR   A CD2  1 
ATOM   2487 C CE1  . TYR   A 1 113 ? 20.375 -10.095 1.041   1.00 13.64 ?  113 TYR   A CE1  1 
ATOM   2488 C CE2  . TYR   A 1 113 ? 19.931 -10.460 -1.281  1.00 13.29 ?  113 TYR   A CE2  1 
ATOM   2489 C CZ   . TYR   A 1 113 ? 19.593 -9.883  -0.076  1.00 13.29 ?  113 TYR   A CZ   1 
ATOM   2490 O OH   . TYR   A 1 113 ? 18.464 -9.096  0.038   1.00 14.47 ?  113 TYR   A OH   1 
ATOM   2491 H H    . TYR   A 1 113 ? 24.530 -11.253 -1.984  1.00 14.98 ?  113 TYR   A H    1 
ATOM   2492 H HA   . TYR   A 1 113 ? 24.227 -10.941 0.596   1.00 14.75 ?  113 TYR   A HA   1 
ATOM   2493 H HB2  . TYR   A 1 113 ? 23.132 -12.745 -1.220  1.00 14.75 ?  113 TYR   A HB2  1 
ATOM   2494 H HB3  . TYR   A 1 113 ? 22.992 -13.087 0.323   1.00 14.75 ?  113 TYR   A HB3  1 
ATOM   2495 H HD1  . TYR   A 1 113 ? 22.023 -11.032 1.717   1.00 15.77 ?  113 TYR   A HD1  1 
ATOM   2496 H HD2  . TYR   A 1 113 ? 21.302 -11.657 -2.168  1.00 15.58 ?  113 TYR   A HD2  1 
ATOM   2497 H HE1  . TYR   A 1 113 ? 20.143 -9.706  1.853   1.00 16.41 ?  113 TYR   A HE1  1 
ATOM   2498 H HE2  . TYR   A 1 113 ? 19.402 -10.317 -2.030  1.00 15.98 ?  113 TYR   A HE2  1 
ATOM   2499 H HH   . TYR   A 1 113 ? 18.082 -9.045  -0.713  1.00 17.40 ?  113 TYR   A HH   1 
ATOM   2500 N N    . GLU   A 1 114 ? 26.325 -13.195 -0.160  1.00 12.16 ?  114 GLU   A N    1 
ATOM   2501 C CA   . GLU   A 1 114 ? 27.313 -14.093 0.443   1.00 12.73 ?  114 GLU   A CA   1 
ATOM   2502 C C    . GLU   A 1 114 ? 28.156 -13.381 1.495   1.00 12.37 ?  114 GLU   A C    1 
ATOM   2503 O O    . GLU   A 1 114 ? 28.632 -14.016 2.443   1.00 12.75 ?  114 GLU   A O    1 
ATOM   2504 C CB   . GLU   A 1 114 ? 28.192 -14.741 -0.638  1.00 12.55 ?  114 GLU   A CB   1 
ATOM   2505 C CG   . GLU   A 1 114 ? 27.435 -15.792 -1.433  1.00 13.52 ?  114 GLU   A CG   1 
ATOM   2506 C CD   . GLU   A 1 114 ? 28.151 -16.320 -2.667  1.00 13.99 ?  114 GLU   A CD   1 
ATOM   2507 O OE1  . GLU   A 1 114 ? 29.106 -15.689 -3.158  1.00 13.90 ?  114 GLU   A OE1  1 
ATOM   2508 O OE2  . GLU   A 1 114 ? 27.715 -17.383 -3.167  1.00 15.07 -1 114 GLU   A OE2  1 
ATOM   2509 H H    . GLU   A 1 114 ? 26.387 -13.105 -1.019  1.00 14.63 ?  114 GLU   A H    1 
ATOM   2510 H HA   . GLU   A 1 114 ? 26.837 -14.806 0.888   1.00 15.32 ?  114 GLU   A HA   1 
ATOM   2511 H HB2  . GLU   A 1 114 ? 28.496 -14.056 -1.258  1.00 15.10 ?  114 GLU   A HB2  1 
ATOM   2512 H HB3  . GLU   A 1 114 ? 28.950 -15.170 -0.218  1.00 15.10 ?  114 GLU   A HB3  1 
ATOM   2513 H HG2  . GLU   A 1 114 ? 27.263 -16.547 -0.856  1.00 16.26 ?  114 GLU   A HG2  1 
ATOM   2514 H HG3  . GLU   A 1 114 ? 26.592 -15.407 -1.726  1.00 16.26 ?  114 GLU   A HG3  1 
ATOM   2515 N N    . ASN   A 1 115 ? 28.342 -12.064 1.361   1.00 12.44 ?  115 ASN   A N    1 
ATOM   2516 C CA   . ASN   A 1 115 ? 29.104 -11.334 2.369   1.00 12.84 ?  115 ASN   A CA   1 
ATOM   2517 C C    . ASN   A 1 115 ? 28.480 -11.461 3.755   1.00 12.29 ?  115 ASN   A C    1 
ATOM   2518 O O    . ASN   A 1 115 ? 29.184 -11.384 4.768   1.00 12.85 ?  115 ASN   A O    1 
ATOM   2519 C CB   . ASN   A 1 115 ? 29.217 -9.857  1.985   1.00 12.87 ?  115 ASN   A CB   1 
ATOM   2520 C CG   . ASN   A 1 115 ? 30.010 -9.652  0.725   1.00 13.49 ?  115 ASN   A CG   1 
ATOM   2521 O OD1  . ASN   A 1 115 ? 31.228 -9.796  0.734   1.00 16.59 ?  115 ASN   A OD1  1 
ATOM   2522 N ND2  . ASN   A 1 115 ? 29.343 -9.328  -0.362  1.00 13.23 ?  115 ASN   A ND2  1 
ATOM   2523 H H    . ASN   A 1 115 ? 28.035 -11.579 0.718   1.00 14.97 ?  115 ASN   A H    1 
ATOM   2524 H HA   . ASN   A 1 115 ? 29.994 -11.705 2.414   1.00 15.45 ?  115 ASN   A HA   1 
ATOM   2525 H HB2  . ASN   A 1 115 ? 28.326 -9.497  1.857   1.00 15.49 ?  115 ASN   A HB2  1 
ATOM   2526 H HB3  . ASN   A 1 115 ? 29.663 -9.383  2.708   1.00 15.49 ?  115 ASN   A HB3  1 
ATOM   2527 H HD21 . ASN   A 1 115 ? 29.758 -9.202  -1.103  1.00 15.91 ?  115 ASN   A HD21 1 
ATOM   2528 H HD22 . ASN   A 1 115 ? 28.484 -9.248  -0.331  1.00 15.91 ?  115 ASN   A HD22 1 
ATOM   2529 N N    . PHE   A 1 116 ? 27.152 -11.629 3.826   1.00 12.60 ?  116 PHE   A N    1 
ATOM   2530 C CA   . PHE   A 1 116 ? 26.487 -11.732 5.124   1.00 12.49 ?  116 PHE   A CA   1 
ATOM   2531 C C    . PHE   A 1 116 ? 26.962 -12.962 5.900   1.00 12.71 ?  116 PHE   A C    1 
ATOM   2532 O O    . PHE   A 1 116 ? 26.891 -12.981 7.132   1.00 13.36 ?  116 PHE   A O    1 
ATOM   2533 C CB   . PHE   A 1 116 ? 24.960 -11.863 4.968   1.00 12.64 ?  116 PHE   A CB   1 
ATOM   2534 C CG   . PHE   A 1 116 ? 24.205 -10.613 4.505   1.00 12.37 ?  116 PHE   A CG   1 
ATOM   2535 C CD1  . PHE   A 1 116 ? 24.783 -9.588  3.762   1.00 12.64 ?  116 PHE   A CD1  1 
ATOM   2536 C CD2  . PHE   A 1 116 ? 22.848 -10.511 4.819   1.00 12.95 ?  116 PHE   A CD2  1 
ATOM   2537 C CE1  . PHE   A 1 116 ? 24.015 -8.513  3.346   1.00 12.91 ?  116 PHE   A CE1  1 
ATOM   2538 C CE2  . PHE   A 1 116 ? 22.088 -9.433  4.414   1.00 13.07 ?  116 PHE   A CE2  1 
ATOM   2539 C CZ   . PHE   A 1 116 ? 22.666 -8.436  3.677   1.00 12.67 ?  116 PHE   A CZ   1 
ATOM   2540 H H    . PHE   A 1 116 ? 26.618 -11.675 3.148   1.00 15.16 ?  116 PHE   A H    1 
ATOM   2541 H HA   . PHE   A 1 116 ? 26.674 -10.942 5.651   1.00 15.02 ?  116 PHE   A HA   1 
ATOM   2542 H HB2  . PHE   A 1 116 ? 24.780 -12.568 4.323   1.00 15.21 ?  116 PHE   A HB2  1 
ATOM   2543 H HB3  . PHE   A 1 116 ? 24.590 -12.125 5.829   1.00 15.21 ?  116 PHE   A HB3  1 
ATOM   2544 H HD1  . PHE   A 1 116 ? 25.677 -9.647  3.529   1.00 15.21 ?  116 PHE   A HD1  1 
ATOM   2545 H HD2  . PHE   A 1 116 ? 22.443 -11.198 5.313   1.00 15.58 ?  116 PHE   A HD2  1 
ATOM   2546 H HE1  . PHE   A 1 116 ? 24.411 -7.833  2.854   1.00 15.53 ?  116 PHE   A HE1  1 
ATOM   2547 H HE2  . PHE   A 1 116 ? 21.181 -9.391  4.642   1.00 15.73 ?  116 PHE   A HE2  1 
ATOM   2548 H HZ   . PHE   A 1 116 ? 22.159 -7.704  3.411   1.00 15.24 ?  116 PHE   A HZ   1 
ATOM   2549 N N    . ASN   A 1 117 ? 27.405 -14.012 5.200   1.00 12.88 ?  117 ASN   A N    1 
ATOM   2550 C CA   . ASN   A 1 117 ? 27.772 -15.254 5.872   1.00 13.30 ?  117 ASN   A CA   1 
ATOM   2551 C C    . ASN   A 1 117 ? 29.031 -15.136 6.709   1.00 13.59 ?  117 ASN   A C    1 
ATOM   2552 O O    . ASN   A 1 117 ? 29.333 -16.060 7.476   1.00 14.51 ?  117 ASN   A O    1 
ATOM   2553 C CB   . ASN   A 1 117 ? 27.899 -16.377 4.852   1.00 13.34 ?  117 ASN   A CB   1 
ATOM   2554 C CG   . ASN   A 1 117 ? 26.554 -16.769 4.299   1.00 13.35 ?  117 ASN   A CG   1 
ATOM   2555 O OD1  . ASN   A 1 117 ? 25.567 -16.799 5.035   1.00 14.40 ?  117 ASN   A OD1  1 
ATOM   2556 N ND2  . ASN   A 1 117 ? 26.486 -17.026 3.007   1.00 13.29 ?  117 ASN   A ND2  1 
ATOM   2557 H H    . ASN   A 1 117 ? 27.485 -14.031 4.341   1.00 15.49 ?  117 ASN   A H    1 
ATOM   2558 H HA   . ASN   A 1 117 ? 27.047 -15.489 6.473   1.00 15.99 ?  117 ASN   A HA   1 
ATOM   2559 H HB2  . ASN   A 1 117 ? 28.458 -16.076 4.118   1.00 16.05 ?  117 ASN   A HB2  1 
ATOM   2560 H HB3  . ASN   A 1 117 ? 28.290 -17.148 5.282   1.00 16.05 ?  117 ASN   A HB3  1 
ATOM   2561 H HD21 . ASN   A 1 117 ? 25.741 -17.244 2.654   1.00 15.98 ?  117 ASN   A HD21 1 
ATOM   2562 H HD22 . ASN   A 1 117 ? 27.200 -16.977 2.525   1.00 15.98 ?  117 ASN   A HD22 1 
ATOM   2563 N N    . GLN   A 1 118 ? 29.758 -14.027 6.595   1.00 13.33 ?  118 GLN   A N    1 
ATOM   2564 C CA   . GLN   A 1 118 ? 30.930 -13.792 7.426   1.00 14.12 ?  118 GLN   A CA   1 
ATOM   2565 C C    . GLN   A 1 118 ? 30.578 -13.227 8.796   1.00 14.22 ?  118 GLN   A C    1 
ATOM   2566 O O    . GLN   A 1 118 ? 31.488 -12.942 9.582   1.00 15.41 ?  118 GLN   A O    1 
ATOM   2567 C CB   . GLN   A 1 118 ? 31.926 -12.883 6.699   1.00 14.47 ?  118 GLN   A CB   1 
ATOM   2568 C CG   . GLN   A 1 118 ? 32.408 -13.463 5.376   1.00 14.32 ?  118 GLN   A CG   1 
ATOM   2569 C CD   . GLN   A 1 118 ? 33.259 -14.712 5.554   1.00 14.64 ?  118 GLN   A CD   1 
ATOM   2570 O OE1  . GLN   A 1 118 ? 34.119 -14.776 6.444   1.00 15.30 ?  118 GLN   A OE1  1 
ATOM   2571 N NE2  . GLN   A 1 118 ? 33.020 -15.716 4.712   1.00 14.91 ?  118 GLN   A NE2  1 
ATOM   2572 H H    . GLN   A 1 118 ? 29.586 -13.381 6.044   1.00 16.03 ?  118 GLN   A H    1 
ATOM   2573 H HA   . GLN   A 1 118 ? 31.365 -14.645 7.571   1.00 16.98 ?  118 GLN   A HA   1 
ATOM   2574 H HB2  . GLN   A 1 118 ? 31.498 -12.033 6.517   1.00 17.41 ?  118 GLN   A HB2  1 
ATOM   2575 H HB3  . GLN   A 1 118 ? 32.699 -12.752 7.269   1.00 17.41 ?  118 GLN   A HB3  1 
ATOM   2576 H HG2  . GLN   A 1 118 ? 31.641 -13.698 4.829   1.00 17.22 ?  118 GLN   A HG2  1 
ATOM   2577 H HG3  . GLN   A 1 118 ? 32.948 -12.800 4.917   1.00 17.22 ?  118 GLN   A HG3  1 
ATOM   2578 H HE21 . GLN   A 1 118 ? 32.407 -15.637 4.110   1.00 17.93 ?  118 GLN   A HE21 1 
ATOM   2579 H HE22 . GLN   A 1 118 ? 33.467 -16.447 4.772   1.00 17.93 ?  118 GLN   A HE22 1 
ATOM   2580 N N    . HIS   A 1 119 ? 29.289 -13.063 9.099   1.00 13.91 ?  119 HIS   A N    1 
ATOM   2581 C CA   . HIS   A 1 119 ? 28.839 -12.451 10.343  1.00 14.02 ?  119 HIS   A CA   1 
ATOM   2582 C C    . HIS   A 1 119 ? 27.696 -13.270 10.919  1.00 14.30 ?  119 HIS   A C    1 
ATOM   2583 O O    . HIS   A 1 119 ? 26.748 -13.606 10.203  1.00 15.03 ?  119 HIS   A O    1 
ATOM   2584 C CB   . HIS   A 1 119 ? 28.385 -11.017 10.065  1.00 14.37 ?  119 HIS   A CB   1 
ATOM   2585 C CG   . HIS   A 1 119 ? 29.463 -10.213 9.437   1.00 15.66 ?  119 HIS   A CG   1 
ATOM   2586 N ND1  . HIS   A 1 119 ? 30.441 -9.594  10.179  1.00 18.03 ?  119 HIS   A ND1  1 
ATOM   2587 C CD2  . HIS   A 1 119 ? 29.795 -10.034 8.139   1.00 16.87 ?  119 HIS   A CD2  1 
ATOM   2588 C CE1  . HIS   A 1 119 ? 31.303 -9.017  9.361   1.00 17.94 ?  119 HIS   A CE1  1 
ATOM   2589 N NE2  . HIS   A 1 119 ? 30.943 -9.283  8.118   1.00 17.97 ?  119 HIS   A NE2  1 
ATOM   2590 H H    . HIS   A 1 119 ? 28.640 -13.318 8.588   1.00 16.73 ?  119 HIS   A H    1 
ATOM   2591 H HA   . HIS   A 1 119 ? 29.569 -12.437 10.980  1.00 16.86 ?  119 HIS   A HA   1 
ATOM   2592 H HB2  . HIS   A 1 119 ? 27.626 -11.037 9.463   1.00 17.28 ?  119 HIS   A HB2  1 
ATOM   2593 H HB3  . HIS   A 1 119 ? 28.142 -10.599 10.904  1.00 17.28 ?  119 HIS   A HB3  1 
ATOM   2594 H HD2  . HIS   A 1 119 ? 29.334 -10.358 7.397   1.00 20.29 ?  119 HIS   A HD2  1 
ATOM   2595 H HE1  . HIS   A 1 119 ? 32.044 -8.514  9.612   1.00 21.57 ?  119 HIS   A HE1  1 
ATOM   2596 H HE2  . HIS   A 1 119 ? 31.345 -8.999  7.408   1.00 21.60 ?  119 HIS   A HE2  1 
ATOM   2597 N N    . GLU   A 1 120 ? 27.783 -13.578 12.214  1.00 15.27 ?  120 GLU   A N    1 
ATOM   2598 C CA   . GLU   A 1 120 ? 26.823 -14.501 12.821  1.00 17.81 ?  120 GLU   A CA   1 
ATOM   2599 C C    . GLU   A 1 120 ? 25.406 -13.937 12.854  1.00 16.45 ?  120 GLU   A C    1 
ATOM   2600 O O    . GLU   A 1 120 ? 24.432 -14.696 12.741  1.00 16.78 ?  120 GLU   A O    1 
ATOM   2601 C CB   . GLU   A 1 120 ? 27.273 -14.869 14.236  1.00 23.33 ?  120 GLU   A CB   1 
ATOM   2602 C CG   . GLU   A 1 120 ? 28.477 -15.793 14.289  1.00 30.81 ?  120 GLU   A CG   1 
ATOM   2603 C CD   . GLU   A 1 120 ? 28.581 -16.544 15.602  1.00 37.41 ?  120 GLU   A CD   1 
ATOM   2604 O OE1  . GLU   A 1 120 ? 28.159 -15.993 16.641  1.00 39.39 ?  120 GLU   A OE1  1 
ATOM   2605 O OE2  . GLU   A 1 120 ? 29.088 -17.687 15.595  1.00 41.56 -1 120 GLU   A OE2  1 
ATOM   2606 H H    . GLU   A 1 120 ? 28.387 -13.276 12.754  1.00 18.36 ?  120 GLU   A H    1 
ATOM   2607 H HA   . GLU   A 1 120 ? 26.808 -15.316 12.303  1.00 21.41 ?  120 GLU   A HA   1 
ATOM   2608 H HB2  . GLU   A 1 120 ? 27.507 -14.061 14.718  1.00 28.03 ?  120 GLU   A HB2  1 
ATOM   2609 H HB3  . GLU   A 1 120 ? 26.541 -15.319 14.691  1.00 28.03 ?  120 GLU   A HB3  1 
ATOM   2610 H HG2  . GLU   A 1 120 ? 28.418 -16.430 13.559  1.00 37.01 ?  120 GLU   A HG2  1 
ATOM   2611 H HG3  . GLU   A 1 120 ? 29.284 -15.268 14.214  1.00 37.01 ?  120 GLU   A HG3  1 
ATOM   2612 N N    . VAL   A 1 121 ? 25.271 -12.625 13.060  1.00 15.64 ?  121 VAL   A N    1 
ATOM   2613 C CA   . VAL   A 1 121 ? 23.976 -11.959 13.175  1.00 15.79 ?  121 VAL   A CA   1 
ATOM   2614 C C    . VAL   A 1 121 ? 24.083 -10.581 12.530  1.00 14.49 ?  121 VAL   A C    1 
ATOM   2615 O O    . VAL   A 1 121 ? 25.049 -9.850  12.779  1.00 15.03 ?  121 VAL   A O    1 
ATOM   2616 C CB   . VAL   A 1 121 ? 23.536 -11.807 14.650  1.00 18.70 ?  121 VAL   A CB   1 
ATOM   2617 C CG1  . VAL   A 1 121 ? 22.150 -11.179 14.739  1.00 19.00 ?  121 VAL   A CG1  1 
ATOM   2618 C CG2  . VAL   A 1 121 ? 23.551 -13.132 15.386  1.00 21.05 ?  121 VAL   A CG2  1 
ATOM   2619 H H    . VAL   A 1 121 ? 25.936 -12.084 13.141  1.00 18.81 ?  121 VAL   A H    1 
ATOM   2620 H HA   . VAL   A 1 121 ? 23.303 -12.476 12.706  1.00 18.98 ?  121 VAL   A HA   1 
ATOM   2621 H HB   . VAL   A 1 121 ? 24.155 -11.216 15.103  1.00 22.48 ?  121 VAL   A HB   1 
ATOM   2622 H HG11 . VAL   A 1 121 ? 21.835 -11.233 15.657  1.00 22.84 ?  121 VAL   A HG11 1 
ATOM   2623 H HG12 . VAL   A 1 121 ? 22.203 -10.251 14.465  1.00 22.84 ?  121 VAL   A HG12 1 
ATOM   2624 H HG13 . VAL   A 1 121 ? 21.544 -11.664 14.156  1.00 22.84 ?  121 VAL   A HG13 1 
ATOM   2625 H HG21 . VAL   A 1 121 ? 23.203 -13.002 16.288  1.00 25.30 ?  121 VAL   A HG21 1 
ATOM   2626 H HG22 . VAL   A 1 121 ? 22.988 -13.768 14.913  1.00 25.30 ?  121 VAL   A HG22 1 
ATOM   2627 H HG23 . VAL   A 1 121 ? 24.458 -13.465 15.432  1.00 25.30 ?  121 VAL   A HG23 1 
ATOM   2628 N N    . LEU   A 1 122 ? 23.072 -10.201 11.739  1.00 13.70 ?  122 LEU   A N    1 
ATOM   2629 C CA   . LEU   A 1 122 ? 23.078 -8.905  11.065  1.00 13.46 ?  122 LEU   A CA   1 
ATOM   2630 C C    . LEU   A 1 122 ? 21.683 -8.307  11.016  1.00 13.66 ?  122 LEU   A C    1 
ATOM   2631 O O    . LEU   A 1 122 ? 20.691 -9.026  10.889  1.00 14.68 ?  122 LEU   A O    1 
ATOM   2632 C CB   . LEU   A 1 122 ? 23.507 -9.010  9.595   1.00 14.91 ?  122 LEU   A CB   1 
ATOM   2633 C CG   . LEU   A 1 122 ? 24.718 -9.857  9.241   1.00 14.86 ?  122 LEU   A CG   1 
ATOM   2634 C CD1  . LEU   A 1 122 ? 24.310 -11.310 9.014   1.00 15.75 ?  122 LEU   A CD1  1 
ATOM   2635 C CD2  . LEU   A 1 122 ? 25.424 -9.292  8.014   1.00 14.31 ?  122 LEU   A CD2  1 
ATOM   2636 H H    . LEU   A 1 122 ? 22.371 -10.676 11.581  1.00 16.48 ?  122 LEU   A H    1 
ATOM   2637 H HA   . LEU   A 1 122 ? 23.679 -8.293  11.524  1.00 16.19 ?  122 LEU   A HA   1 
ATOM   2638 H HB2  . LEU   A 1 122 ? 22.770 -9.378  9.093   1.00 17.93 ?  122 LEU   A HB2  1 
ATOM   2639 H HB3  . LEU   A 1 122 ? 23.703 -8.120  9.273   1.00 17.93 ?  122 LEU   A HB3  1 
ATOM   2640 H HG   . LEU   A 1 122 ? 25.358 -9.845  9.974   1.00 17.87 ?  122 LEU   A HG   1 
ATOM   2641 H HD11 . LEU   A 1 122 ? 25.088 -11.831 8.758   1.00 18.94 ?  122 LEU   A HD11 1 
ATOM   2642 H HD12 . LEU   A 1 122 ? 23.933 -11.663 9.835   1.00 18.94 ?  122 LEU   A HD12 1 
ATOM   2643 H HD13 . LEU   A 1 122 ? 23.646 -11.343 8.306   1.00 18.94 ?  122 LEU   A HD13 1 
ATOM   2644 H HD21 . LEU   A 1 122 ? 26.178 -9.869  7.780   1.00 17.21 ?  122 LEU   A HD21 1 
ATOM   2645 H HD22 . LEU   A 1 122 ? 24.800 -9.260  7.275   1.00 17.21 ?  122 LEU   A HD22 1 
ATOM   2646 H HD23 . LEU   A 1 122 ? 25.750 -8.402  8.217   1.00 17.21 ?  122 LEU   A HD23 1 
ATOM   2647 N N    A LEU   A 1 123 ? 21.621 -6.984  11.148  0.72 13.13 ?  123 LEU   A N    1 
ATOM   2648 N N    B LEU   A 1 123 ? 21.630 -6.976  11.068  0.28 13.35 ?  123 LEU   A N    1 
ATOM   2649 C CA   A LEU   A 1 123 ? 20.461 -6.187  10.764  0.72 12.82 ?  123 LEU   A CA   1 
ATOM   2650 C CA   B LEU   A 1 123 ? 20.434 -6.194  10.772  0.28 13.27 ?  123 LEU   A CA   1 
ATOM   2651 C C    A LEU   A 1 123 ? 20.714 -5.683  9.354   0.72 12.42 ?  123 LEU   A C    1 
ATOM   2652 C C    B LEU   A 1 123 ? 20.642 -5.567  9.398   0.28 12.52 ?  123 LEU   A C    1 
ATOM   2653 O O    A LEU   A 1 123 ? 21.783 -5.136  9.085   0.72 12.55 ?  123 LEU   A O    1 
ATOM   2654 O O    B LEU   A 1 123 ? 21.611 -4.830  9.199   0.28 12.20 ?  123 LEU   A O    1 
ATOM   2655 C CB   A LEU   A 1 123 ? 20.319 -4.993  11.708  0.72 13.43 ?  123 LEU   A CB   1 
ATOM   2656 C CB   B LEU   A 1 123 ? 20.242 -5.106  11.831  0.28 14.14 ?  123 LEU   A CB   1 
ATOM   2657 C CG   A LEU   A 1 123 ? 19.256 -3.947  11.368  0.72 14.51 ?  123 LEU   A CG   1 
ATOM   2658 C CG   B LEU   A 1 123 ? 19.244 -4.002  11.468  0.28 14.63 ?  123 LEU   A CG   1 
ATOM   2659 C CD1  A LEU   A 1 123 ? 17.851 -4.551  11.386  0.72 15.41 ?  123 LEU   A CD1  1 
ATOM   2660 C CD1  B LEU   A 1 123 ? 17.834 -4.568  11.362  0.28 15.00 ?  123 LEU   A CD1  1 
ATOM   2661 C CD2  A LEU   A 1 123 ? 19.352 -2.770  12.329  0.72 15.05 ?  123 LEU   A CD2  1 
ATOM   2662 C CD2  B LEU   A 1 123 ? 19.296 -2.847  12.459  0.28 15.16 ?  123 LEU   A CD2  1 
ATOM   2663 H H    A LEU   A 1 123 ? 22.269 -6.512  11.469  0.72 15.80 ?  123 LEU   A H    1 
ATOM   2664 H H    B LEU   A 1 123 ? 22.311 -6.484  11.271  0.28 16.06 ?  123 LEU   A H    1 
ATOM   2665 H HA   A LEU   A 1 123 ? 19.660 -6.729  10.781  0.72 15.42 ?  123 LEU   A HA   1 
ATOM   2666 H HA   B LEU   A 1 123 ? 19.654 -6.766  10.752  0.28 15.96 ?  123 LEU   A HA   1 
ATOM   2667 H HB2  A LEU   A 1 123 ? 20.106 -5.337  12.589  0.72 16.15 ?  123 LEU   A HB2  1 
ATOM   2668 H HB2  B LEU   A 1 123 ? 19.928 -5.528  12.651  0.28 17.00 ?  123 LEU   A HB2  1 
ATOM   2669 H HB3  A LEU   A 1 123 ? 21.169 -4.533  11.740  0.72 16.15 ?  123 LEU   A HB3  1 
ATOM   2670 H HB3  B LEU   A 1 123 ? 21.100 -4.683  12.001  0.28 17.00 ?  123 LEU   A HB3  1 
ATOM   2671 H HG   A LEU   A 1 123 ? 19.418 -3.609  10.472  0.72 17.45 ?  123 LEU   A HG   1 
ATOM   2672 H HG   B LEU   A 1 123 ? 19.477 -3.638  10.601  0.28 17.60 ?  123 LEU   A HG   1 
ATOM   2673 H HD11 A LEU   A 1 123 ? 17.204 -3.858  11.184  0.72 18.53 ?  123 LEU   A HD11 1 
ATOM   2674 H HD11 B LEU   A 1 123 ? 17.209 -3.835  11.264  0.28 18.03 ?  123 LEU   A HD11 1 
ATOM   2675 H HD12 A LEU   A 1 123 ? 17.800 -5.254  10.717  0.72 18.53 ?  123 LEU   A HD12 1 
ATOM   2676 H HD12 B LEU   A 1 123 ? 17.785 -5.151  10.587  0.28 18.03 ?  123 LEU   A HD12 1 
ATOM   2677 H HD13 A LEU   A 1 123 ? 17.677 -4.921  12.266  0.72 18.53 ?  123 LEU   A HD13 1 
ATOM   2678 H HD13 B LEU   A 1 123 ? 17.633 -5.071  12.167  0.28 18.03 ?  123 LEU   A HD13 1 
ATOM   2679 H HD21 A LEU   A 1 123 ? 18.670 -2.121  12.101  0.72 18.09 ?  123 LEU   A HD21 1 
ATOM   2680 H HD21 B LEU   A 1 123 ? 18.653 -2.173  12.187  0.28 18.23 ?  123 LEU   A HD21 1 
ATOM   2681 H HD22 A LEU   A 1 123 ? 19.209 -3.096  13.234  0.72 18.09 ?  123 LEU   A HD22 1 
ATOM   2682 H HD22 B LEU   A 1 123 ? 19.076 -3.178  13.343  0.28 18.23 ?  123 LEU   A HD22 1 
ATOM   2683 H HD23 A LEU   A 1 123 ? 20.231 -2.375  12.254  0.72 18.09 ?  123 LEU   A HD23 1 
ATOM   2684 H HD23 B LEU   A 1 123 ? 20.190 -2.471  12.458  0.28 18.23 ?  123 LEU   A HD23 1 
ATOM   2685 N N    . ALA   A 1 124 ? 19.746 -5.854  8.455   1.00 12.35 ?  124 ALA   A N    1 
ATOM   2686 C CA   . ALA   A 1 124 ? 20.012 -5.555  7.055   1.00 12.16 ?  124 ALA   A CA   1 
ATOM   2687 C C    . ALA   A 1 124 ? 18.779 -5.107  6.285   1.00 12.22 ?  124 ALA   A C    1 
ATOM   2688 O O    . ALA   A 1 124 ? 17.649 -5.462  6.645   1.00 12.91 ?  124 ALA   A O    1 
ATOM   2689 C CB   . ALA   A 1 124 ? 20.596 -6.781  6.338   1.00 12.93 ?  124 ALA   A CB   1 
ATOM   2690 H H    A ALA   A 1 124 ? 18.950 -6.127  8.631   0.72 14.85 ?  124 ALA   A H    1 
ATOM   2691 H H    B ALA   A 1 124 ? 18.989 -6.234  8.600   0.28 14.85 ?  124 ALA   A H    1 
ATOM   2692 H HA   . ALA   A 1 124 ? 20.679 -4.852  7.026   1.00 14.63 ?  124 ALA   A HA   1 
ATOM   2693 H HB1  . ALA   A 1 124 ? 20.769 -6.557  5.408   1.00 15.56 ?  124 ALA   A HB1  1 
ATOM   2694 H HB2  . ALA   A 1 124 ? 21.434 -7.035  6.770   1.00 15.56 ?  124 ALA   A HB2  1 
ATOM   2695 H HB3  . ALA   A 1 124 ? 19.967 -7.513  6.391   1.00 15.56 ?  124 ALA   A HB3  1 
ATOM   2696 N N    A PRO   A 1 125 ? 18.974 -4.347  5.212   0.72 11.95 ?  125 PRO   A N    1 
ATOM   2697 N N    B PRO   A 1 125 ? 18.975 -4.336  5.214   0.28 12.80 ?  125 PRO   A N    1 
ATOM   2698 C CA   A PRO   A 1 125 ? 17.924 -4.114  4.222   0.72 12.33 ?  125 PRO   A CA   1 
ATOM   2699 C CA   B PRO   A 1 125 ? 17.870 -4.013  4.311   0.28 13.46 ?  125 PRO   A CA   1 
ATOM   2700 C C    A PRO   A 1 125 ? 17.987 -5.194  3.148   0.72 12.00 ?  125 PRO   A C    1 
ATOM   2701 C C    B PRO   A 1 125 ? 17.832 -4.994  3.153   0.28 13.92 ?  125 PRO   A C    1 
ATOM   2702 O O    A PRO   A 1 125 ? 18.964 -5.937  3.036   0.72 12.41 ?  125 PRO   A O    1 
ATOM   2703 O O    B PRO   A 1 125 ? 18.687 -5.882  3.057   0.28 14.25 ?  125 PRO   A O    1 
ATOM   2704 C CB   A PRO   A 1 125 ? 18.373 -2.779  3.611   0.72 12.70 ?  125 PRO   A CB   1 
ATOM   2705 C CB   B PRO   A 1 125 ? 18.257 -2.619  3.813   0.28 13.58 ?  125 PRO   A CB   1 
ATOM   2706 C CG   A PRO   A 1 125 ? 19.885 -2.932  3.545   0.72 12.56 ?  125 PRO   A CG   1 
ATOM   2707 C CG   B PRO   A 1 125 ? 19.761 -2.717  3.696   0.28 13.56 ?  125 PRO   A CG   1 
ATOM   2708 C CD   A PRO   A 1 125 ? 20.244 -3.707  4.814   0.72 12.46 ?  125 PRO   A CD   1 
ATOM   2709 C CD   B PRO   A 1 125 ? 20.219 -3.659  4.802   0.28 13.21 ?  125 PRO   A CD   1 
ATOM   2710 H HA   A PRO   A 1 125 ? 17.042 -4.055  4.619   0.72 14.84 ?  125 PRO   A HA   1 
ATOM   2711 H HA   B PRO   A 1 125 ? 17.020 -3.985  4.785   0.28 16.19 ?  125 PRO   A HA   1 
ATOM   2712 H HB2  A PRO   A 1 125 ? 17.985 -2.675  2.725   0.72 15.28 ?  125 PRO   A HB2  1 
ATOM   2713 H HB2  B PRO   A 1 125 ? 17.846 -2.450  2.949   0.28 16.33 ?  125 PRO   A HB2  1 
ATOM   2714 H HB3  A PRO   A 1 125 ? 18.114 -2.049  4.193   0.72 15.28 ?  125 PRO   A HB3  1 
ATOM   2715 H HB3  B PRO   A 1 125 ? 17.996 -1.946  4.462   0.28 16.33 ?  125 PRO   A HB3  1 
ATOM   2716 H HG2  A PRO   A 1 125 ? 20.134 -3.434  2.748   0.72 15.11 ?  125 PRO   A HG2  1 
ATOM   2717 H HG2  B PRO   A 1 125 ? 19.994 -3.079  2.827   0.28 16.30 ?  125 PRO   A HG2  1 
ATOM   2718 H HG3  A PRO   A 1 125 ? 20.305 -2.055  3.538   0.72 15.11 ?  125 PRO   A HG3  1 
ATOM   2719 H HG3  B PRO   A 1 125 ? 20.153 -1.840  3.815   0.28 16.30 ?  125 PRO   A HG3  1 
ATOM   2720 H HD2  A PRO   A 1 125 ? 20.924 -4.374  4.621   0.72 14.99 ?  125 PRO   A HD2  1 
ATOM   2721 H HD2  B PRO   A 1 125 ? 20.860 -4.303  4.453   0.28 15.89 ?  125 PRO   A HD2  1 
ATOM   2722 H HD3  A PRO   A 1 125 ? 20.541 -3.094  5.507   0.72 14.99 ?  125 PRO   A HD3  1 
ATOM   2723 H HD3  B PRO   A 1 125 ? 20.594 -3.154  5.541   0.28 15.89 ?  125 PRO   A HD3  1 
ATOM   2724 N N    A LEU   A 1 126 ? 16.936 -5.245  2.332   0.72 12.21 ?  126 LEU   A N    1 
ATOM   2725 N N    B LEU   A 1 126 ? 16.866 -4.828  2.255   0.28 14.56 ?  126 LEU   A N    1 
ATOM   2726 C CA   A LEU   A 1 126 ? 16.976 -6.071  1.135   0.72 12.47 ?  126 LEU   A CA   1 
ATOM   2727 C CA   B LEU   A 1 126 ? 16.752 -5.672  1.070   0.28 15.16 ?  126 LEU   A CA   1 
ATOM   2728 C C    A LEU   A 1 126 ? 17.925 -5.456  0.116   0.72 12.68 ?  126 LEU   A C    1 
ATOM   2729 C C    B LEU   A 1 126 ? 17.710 -5.151  0.001   0.28 14.37 ?  126 LEU   A C    1 
ATOM   2730 O O    A LEU   A 1 126 ? 17.722 -4.325  -0.334  0.72 13.59 ?  126 LEU   A O    1 
ATOM   2731 O O    B LEU   A 1 126 ? 17.494 -4.072  -0.558  0.28 14.71 ?  126 LEU   A O    1 
ATOM   2732 C CB   A LEU   A 1 126 ? 15.578 -6.221  0.546   0.72 12.67 ?  126 LEU   A CB   1 
ATOM   2733 C CB   B LEU   A 1 126 ? 15.312 -5.616  0.571   0.28 17.18 ?  126 LEU   A CB   1 
ATOM   2734 C CG   A LEU   A 1 126 ? 14.636 -7.147  1.318   0.72 14.20 ?  126 LEU   A CG   1 
ATOM   2735 C CG   B LEU   A 1 126 ? 14.698 -6.828  -0.127  0.28 18.79 ?  126 LEU   A CG   1 
ATOM   2736 C CD1  A LEU   A 1 126 ? 13.219 -7.012  0.797   0.72 15.36 ?  126 LEU   A CD1  1 
ATOM   2737 C CD1  B LEU   A 1 126 ? 14.941 -8.093  0.664   0.28 19.10 ?  126 LEU   A CD1  1 
ATOM   2738 C CD2  A LEU   A 1 126 ? 15.112 -8.602  1.224   0.72 14.50 ?  126 LEU   A CD2  1 
ATOM   2739 C CD2  B LEU   A 1 126 ? 13.209 -6.603  -0.298  0.28 19.09 ?  126 LEU   A CD2  1 
ATOM   2740 H H    A LEU   A 1 126 ? 16.204 -4.812  2.441   0.72 14.69 ?  126 LEU   A H    1 
ATOM   2741 H H    B LEU   A 1 126 ? 16.248 -4.229  2.320   0.28 17.51 ?  126 LEU   A H    1 
ATOM   2742 H HA   A LEU   A 1 126 ? 17.307 -6.953  1.358   0.72 15.01 ?  126 LEU   A HA   1 
ATOM   2743 H HA   B LEU   A 1 126 ? 16.988 -6.586  1.300   0.28 18.23 ?  126 LEU   A HA   1 
ATOM   2744 H HB2  A LEU   A 1 126 ? 15.158 -5.346  0.519   0.72 15.24 ?  126 LEU   A HB2  1 
ATOM   2745 H HB2  B LEU   A 1 126 ? 14.743 -5.424  1.331   0.28 20.65 ?  126 LEU   A HB2  1 
ATOM   2746 H HB3  A LEU   A 1 126 ? 15.652 -6.572  -0.354  0.72 15.24 ?  126 LEU   A HB3  1 
ATOM   2747 H HB3  B LEU   A 1 126 ? 15.254 -4.879  -0.056  0.28 20.65 ?  126 LEU   A HB3  1 
ATOM   2748 H HG   A LEU   A 1 126 ? 14.638 -6.894  2.255   0.72 17.08 ?  126 LEU   A HG   1 
ATOM   2749 H HG   B LEU   A 1 126 ? 15.097 -6.925  -1.007  0.28 22.58 ?  126 LEU   A HG   1 
ATOM   2750 H HD11 A LEU   A 1 126 ? 12.641 -7.610  1.295   0.72 18.47 ?  126 LEU   A HD11 1 
ATOM   2751 H HD11 B LEU   A 1 126 ? 14.346 -8.784  0.340   0.28 22.96 ?  126 LEU   A HD11 1 
ATOM   2752 H HD12 A LEU   A 1 126 ? 12.929 -6.095  0.912   0.72 18.47 ?  126 LEU   A HD12 1 
ATOM   2753 H HD12 B LEU   A 1 126 ? 15.863 -8.366  0.547   0.28 22.96 ?  126 LEU   A HD12 1 
ATOM   2754 H HD13 A LEU   A 1 126 ? 13.207 -7.249  -0.145  0.72 18.47 ?  126 LEU   A HD13 1 
ATOM   2755 H HD13 B LEU   A 1 126 ? 14.762 -7.913  1.601   0.28 22.96 ?  126 LEU   A HD13 1 
ATOM   2756 H HD21 A LEU   A 1 126 ? 14.433 -9.184  1.597   0.72 17.44 ?  126 LEU   A HD21 1 
ATOM   2757 H HD21 B LEU   A 1 126 ? 12.826 -7.362  -0.764  0.28 22.95 ?  126 LEU   A HD21 1 
ATOM   2758 H HD22 A LEU   A 1 126 ? 15.265 -8.825  0.292   0.72 17.44 ?  126 LEU   A HD22 1 
ATOM   2759 H HD22 B LEU   A 1 126 ? 12.803 -6.514  0.580   0.28 22.95 ?  126 LEU   A HD22 1 
ATOM   2760 H HD23 A LEU   A 1 126 ? 15.940 -8.699  1.724   0.72 17.44 ?  126 LEU   A HD23 1 
ATOM   2761 H HD23 B LEU   A 1 126 ? 13.068 -5.793  -0.811  0.28 22.95 ?  126 LEU   A HD23 1 
ATOM   2762 N N    A LEU   A 1 127 ? 18.959 -6.208  -0.253  0.72 12.46 ?  127 LEU   A N    1 
ATOM   2763 N N    B LEU   A 1 127 ? 18.758 -5.914  -0.304  0.28 13.69 ?  127 LEU   A N    1 
ATOM   2764 C CA   A LEU   A 1 127 ? 19.952 -5.710  -1.191  0.72 12.10 ?  127 LEU   A CA   1 
ATOM   2765 C CA   B LEU   A 1 127 ? 19.772 -5.429  -1.232  0.28 13.43 ?  127 LEU   A CA   1 
ATOM   2766 C C    A LEU   A 1 127 ? 19.332 -5.496  -2.560  0.72 12.00 ?  127 LEU   A C    1 
ATOM   2767 C C    B LEU   A 1 127 ? 19.232 -5.350  -2.661  0.28 13.65 ?  127 LEU   A C    1 
ATOM   2768 O O    A LEU   A 1 127 ? 18.500 -6.283  -3.026  0.72 12.50 ?  127 LEU   A O    1 
ATOM   2769 O O    B LEU   A 1 127 ? 18.383 -6.142  -3.082  0.28 13.70 ?  127 LEU   A O    1 
ATOM   2770 C CB   A LEU   A 1 127 ? 21.114 -6.694  -1.300  0.72 13.16 ?  127 LEU   A CB   1 
ATOM   2771 C CB   B LEU   A 1 127 ? 21.016 -6.321  -1.194  0.28 13.72 ?  127 LEU   A CB   1 
ATOM   2772 C CG   A LEU   A 1 127 ? 21.908 -6.944  -0.022  0.72 13.30 ?  127 LEU   A CG   1 
ATOM   2773 C CG   B LEU   A 1 127 ? 21.849 -6.316  0.095   0.28 13.70 ?  127 LEU   A CG   1 
ATOM   2774 C CD1  A LEU   A 1 127 ? 23.003 -7.942  -0.306  0.72 13.53 ?  127 LEU   A CD1  1 
ATOM   2775 C CD1  B LEU   A 1 127 ? 23.032 -7.271  -0.021  0.28 14.22 ?  127 LEU   A CD1  1 
ATOM   2776 C CD2  A LEU   A 1 127 ? 22.503 -5.658  0.511   0.72 14.13 ?  127 LEU   A CD2  1 
ATOM   2777 C CD2  B LEU   A 1 127 ? 22.325 -4.909  0.437   0.28 13.75 ?  127 LEU   A CD2  1 
ATOM   2778 H H    A LEU   A 1 127 ? 19.104 -7.008  0.032   0.72 15.00 ?  127 LEU   A H    1 
ATOM   2779 H H    B LEU   A 1 127 ? 18.906 -6.702  0.018   0.28 16.47 ?  127 LEU   A H    1 
ATOM   2780 H HA   A LEU   A 1 127 ? 20.293 -4.867  -0.878  0.72 14.56 ?  127 LEU   A HA   1 
ATOM   2781 H HA   B LEU   A 1 127 ? 20.034 -4.536  -0.960  0.28 16.16 ?  127 LEU   A HA   1 
ATOM   2782 H HB2  A LEU   A 1 127 ? 20.764 -7.551  -1.596  0.72 15.82 ?  127 LEU   A HB2  1 
ATOM   2783 H HB2  B LEU   A 1 127 ? 20.736 -7.236  -1.348  0.28 16.51 ?  127 LEU   A HB2  1 
ATOM   2784 H HB3  A LEU   A 1 127 ? 21.736 -6.356  -1.961  0.72 15.82 ?  127 LEU   A HB3  1 
ATOM   2785 H HB3  B LEU   A 1 127 ? 21.603 -6.041  -1.914  0.28 16.51 ?  127 LEU   A HB3  1 
ATOM   2786 H HG   A LEU   A 1 127 ? 21.320 -7.323  0.656   0.72 16.00 ?  127 LEU   A HG   1 
ATOM   2787 H HG   B LEU   A 1 127 ? 21.295 -6.624  0.827   0.28 16.48 ?  127 LEU   A HG   1 
ATOM   2788 H HD11 A LEU   A 1 127 ? 23.478 -8.136  0.519   0.72 16.27 ?  127 LEU   A HD11 1 
ATOM   2789 H HD11 B LEU   A 1 127 ? 23.545 -7.241  0.803   0.28 17.10 ?  127 LEU   A HD11 1 
ATOM   2790 H HD12 A LEU   A 1 127 ? 22.608 -8.760  -0.655  0.72 16.27 ?  127 LEU   A HD12 1 
ATOM   2791 H HD12 B LEU   A 1 127 ? 22.698 -8.170  -0.168  0.28 17.10 ?  127 LEU   A HD12 1 
ATOM   2792 H HD13 A LEU   A 1 127 ? 23.611 -7.566  -0.958  0.72 16.27 ?  127 LEU   A HD13 1 
ATOM   2793 H HD13 B LEU   A 1 127 ? 23.589 -6.998  -0.766  0.28 17.10 ?  127 LEU   A HD13 1 
ATOM   2794 H HD21 A LEU   A 1 127 ? 23.110 -5.871  1.238   0.72 16.99 ?  127 LEU   A HD21 1 
ATOM   2795 H HD21 B LEU   A 1 127 ? 22.964 -4.960  1.165   0.28 16.53 ?  127 LEU   A HD21 1 
ATOM   2796 H HD22 A LEU   A 1 127 ? 22.992 -5.222  -0.207  0.72 16.99 ?  127 LEU   A HD22 1 
ATOM   2797 H HD22 B LEU   A 1 127 ? 22.745 -4.519  -0.345  0.28 16.53 ?  127 LEU   A HD22 1 
ATOM   2798 H HD23 A LEU   A 1 127 ? 21.792 -5.086  0.826   0.72 16.99 ?  127 LEU   A HD23 1 
ATOM   2799 H HD23 B LEU   A 1 127 ? 21.561 -4.374  0.704   0.28 16.53 ?  127 LEU   A HD23 1 
ATOM   2800 N N    A SER   A 1 128 ? 19.762 -4.421  -3.206  0.72 12.31 ?  128 SER   A N    1 
ATOM   2801 N N    B SER   A 1 128 ? 19.743 -4.364  -3.402  0.28 13.78 ?  128 SER   A N    1 
ATOM   2802 C CA   A SER   A 1 128 ? 19.350 -4.005  -4.539  0.72 12.18 ?  128 SER   A CA   1 
ATOM   2803 C CA   B SER   A 1 128 ? 19.456 -4.139  -4.818  0.28 13.53 ?  128 SER   A CA   1 
ATOM   2804 C C    A SER   A 1 128 ? 17.894 -3.558  -4.620  0.72 12.22 ?  128 SER   A C    1 
ATOM   2805 C C    B SER   A 1 128 ? 18.035 -3.668  -5.114  0.28 13.76 ?  128 SER   A C    1 
ATOM   2806 O O    A SER   A 1 128 ? 17.420 -3.259  -5.717  0.72 13.03 ?  128 SER   A O    1 
ATOM   2807 O O    B SER   A 1 128 ? 17.731 -3.315  -6.259  0.28 13.60 ?  128 SER   A O    1 
ATOM   2808 C CB   A SER   A 1 128 ? 19.686 -5.031  -5.629  0.72 12.68 ?  128 SER   A CB   1 
ATOM   2809 C CB   B SER   A 1 128 ? 19.809 -5.366  -5.664  0.28 13.36 ?  128 SER   A CB   1 
ATOM   2810 O OG   A SER   A 1 128 ? 21.094 -5.236  -5.706  0.72 13.11 ?  128 SER   A OG   1 
ATOM   2811 O OG   B SER   A 1 128 ? 21.216 -5.523  -5.748  0.28 12.98 ?  128 SER   A OG   1 
ATOM   2812 H H    A SER   A 1 128 ? 20.343 -3.884  -2.866  0.72 14.81 ?  128 SER   A H    1 
ATOM   2813 H H    B SER   A 1 128 ? 20.300 -3.794  -3.086  0.28 16.57 ?  128 SER   A H    1 
ATOM   2814 H HA   A SER   A 1 128 ? 19.867 -3.221  -4.749  0.72 14.66 ?  128 SER   A HA   1 
ATOM   2815 H HA   B SER   A 1 128 ? 20.038 -3.428  -5.112  0.28 16.27 ?  128 SER   A HA   1 
ATOM   2816 H HB2  A SER   A 1 128 ? 19.247 -5.869  -5.422  0.72 15.26 ?  128 SER   A HB2  1 
ATOM   2817 H HB2  B SER   A 1 128 ? 19.423 -6.157  -5.264  0.28 16.07 ?  128 SER   A HB2  1 
ATOM   2818 H HB3  A SER   A 1 128 ? 19.375 -4.691  -6.484  0.72 15.26 ?  128 SER   A HB3  1 
ATOM   2819 H HB3  B SER   A 1 128 ? 19.454 -5.239  -6.561  0.28 16.07 ?  128 SER   A HB3  1 
ATOM   2820 H HG   A SER   A 1 128 ? 21.480 -4.503  -5.856  0.72 15.78 ?  128 SER   A HG   1 
ATOM   2821 H HG   B SER   A 1 128 ? 21.558 -4.836  -6.091  0.28 15.62 ?  128 SER   A HG   1 
ATOM   2822 N N    A ALA   A 1 129 ? 17.184 -3.476  -3.494  0.72 12.64 ?  129 ALA   A N    1 
ATOM   2823 N N    B ALA   A 1 129 ? 17.169 -3.633  -4.108  0.28 14.48 ?  129 ALA   A N    1 
ATOM   2824 C CA   A ALA   A 1 129 ? 15.826 -2.955  -3.502  0.72 13.17 ?  129 ALA   A CA   1 
ATOM   2825 C CA   B ALA   A 1 129 ? 15.795 -3.199  -4.310  0.28 15.59 ?  129 ALA   A CA   1 
ATOM   2826 C C    A ALA   A 1 129 ? 15.855 -1.425  -3.517  0.72 13.09 ?  129 ALA   A C    1 
ATOM   2827 C C    B ALA   A 1 129 ? 15.691 -1.695  -4.037  0.28 16.56 ?  129 ALA   A C    1 
ATOM   2828 O O    A ALA   A 1 129 ? 16.914 -0.791  -3.611  0.72 13.16 ?  129 ALA   A O    1 
ATOM   2829 O O    B ALA   A 1 129 ? 16.697 -0.993  -3.907  0.28 16.52 ?  129 ALA   A O    1 
ATOM   2830 C CB   A ALA   A 1 129 ? 15.027 -3.516  -2.325  0.72 14.03 ?  129 ALA   A CB   1 
ATOM   2831 C CB   B ALA   A 1 129 ? 14.848 -4.046  -3.459  0.28 16.32 ?  129 ALA   A CB   1 
ATOM   2832 H H    A ALA   A 1 129 ? 17.470 -3.704  -2.709  0.72 15.20 ?  129 ALA   A H    1 
ATOM   2833 H H    B ALA   A 1 129 ? 17.350 -3.852  -3.295  0.28 17.42 ?  129 ALA   A H    1 
ATOM   2834 H HA   A ALA   A 1 129 ? 15.390 -3.238  -4.310  0.72 15.84 ?  129 ALA   A HA   1 
ATOM   2835 H HA   B ALA   A 1 129 ? 15.561 -3.359  -5.240  0.28 18.75 ?  129 ALA   A HA   1 
ATOM   2836 H HB1  A ALA   A 1 129 ? 14.122 -3.160  -2.355  0.72 16.88 ?  129 ALA   A HB1  1 
ATOM   2837 H HB1  B ALA   A 1 129 ? 13.934 -3.757  -3.617  0.28 19.62 ?  129 ALA   A HB1  1 
ATOM   2838 H HB2  A ALA   A 1 129 ? 15.002 -4.482  -2.392  0.72 16.88 ?  129 ALA   A HB2  1 
ATOM   2839 H HB2  B ALA   A 1 129 ? 14.943 -4.980  -3.715  0.28 19.62 ?  129 ALA   A HB2  1 
ATOM   2840 H HB3  A ALA   A 1 129 ? 15.452 -3.254  -1.491  0.72 16.88 ?  129 ALA   A HB3  1 
ATOM   2841 H HB3  B ALA   A 1 129 ? 15.075 -3.935  -2.525  0.28 19.62 ?  129 ALA   A HB3  1 
ATOM   2842 N N    A GLY   A 1 130 ? 14.671 -0.824  -3.450  0.72 14.32 ?  130 GLY   A N    1 
ATOM   2843 N N    B GLY   A 1 130 ? 14.464 -1.185  -3.954  0.28 17.11 ?  130 GLY   A N    1 
ATOM   2844 C CA   A GLY   A 1 130 ? 14.593 0.627   -3.444  0.72 15.65 ?  130 GLY   A CA   1 
ATOM   2845 C CA   B GLY   A 1 130 ? 14.269 0.235   -3.724  0.28 17.49 ?  130 GLY   A CA   1 
ATOM   2846 C C    A GLY   A 1 130 ? 15.221 1.221   -4.688  0.72 15.38 ?  130 GLY   A C    1 
ATOM   2847 C C    B GLY   A 1 130 ? 14.840 1.050   -4.863  0.28 17.93 ?  130 GLY   A C    1 
ATOM   2848 O O    A GLY   A 1 130 ? 14.981 0.765   -5.810  0.72 16.29 ?  130 GLY   A O    1 
ATOM   2849 O O    B GLY   A 1 130 ? 14.670 0.718   -6.041  0.28 17.87 ?  130 GLY   A O    1 
ATOM   2850 H H    A GLY   A 1 130 ? 13.907 -1.224  -3.415  0.72 17.23 ?  130 GLY   A H    1 
ATOM   2851 H H    B GLY   A 1 130 ? 13.739 -1.634  -4.028  0.28 20.57 ?  130 GLY   A H    1 
ATOM   2852 H HA2  A GLY   A 1 130 ? 13.664 0.909   -3.407  0.72 18.82 ?  130 GLY   A HA2  1 
ATOM   2853 H HA2  B GLY   A 1 130 ? 13.317 0.421   -3.625  0.28 21.03 ?  130 GLY   A HA2  1 
ATOM   2854 H HA3  A GLY   A 1 130 ? 15.057 0.979   -2.675  0.72 18.82 ?  130 GLY   A HA3  1 
ATOM   2855 H HA3  B GLY   A 1 130 ? 14.722 0.506   -2.918  0.28 21.03 ?  130 GLY   A HA3  1 
ATOM   2856 N N    A ILE   A 1 131 ? 16.041 2.259   -4.492  0.72 14.78 ?  131 ILE   A N    1 
ATOM   2857 N N    B ILE   A 1 131 ? 15.553 2.125   -4.517  0.28 18.47 ?  131 ILE   A N    1 
ATOM   2858 C CA   A ILE   A 1 131 ? 16.622 2.994   -5.614  0.72 14.45 ?  131 ILE   A CA   1 
ATOM   2859 C CA   B ILE   A 1 131 ? 16.111 3.012   -5.535  0.28 18.69 ?  131 ILE   A CA   1 
ATOM   2860 C C    A ILE   A 1 131 ? 17.631 2.190   -6.417  0.72 14.11 ?  131 ILE   A C    1 
ATOM   2861 C C    B ILE   A 1 131 ? 17.225 2.327   -6.321  0.28 18.28 ?  131 ILE   A C    1 
ATOM   2862 O O    A ILE   A 1 131 ? 18.051 2.656   -7.482  0.72 14.77 ?  131 ILE   A O    1 
ATOM   2863 O O    B ILE   A 1 131 ? 17.794 2.923   -7.244  0.28 18.26 ?  131 ILE   A O    1 
ATOM   2864 C CB   A ILE   A 1 131 ? 17.219 4.351   -5.185  0.72 15.49 ?  131 ILE   A CB   1 
ATOM   2865 C CB   B ILE   A 1 131 ? 16.566 4.366   -4.951  0.28 19.45 ?  131 ILE   A CB   1 
ATOM   2866 C CG1  A ILE   A 1 131 ? 18.474 4.158   -4.324  0.72 16.59 ?  131 ILE   A CG1  1 
ATOM   2867 C CG1  B ILE   A 1 131 ? 17.811 4.209   -4.074  0.28 20.04 ?  131 ILE   A CG1  1 
ATOM   2868 C CG2  A ILE   A 1 131 ? 16.168 5.175   -4.455  0.72 15.94 ?  131 ILE   A CG2  1 
ATOM   2869 C CG2  B ILE   A 1 131 ? 15.432 5.017   -4.165  0.28 19.69 ?  131 ILE   A CG2  1 
ATOM   2870 C CD1  A ILE   A 1 131 ? 19.147 5.472   -3.919  0.72 17.80 ?  131 ILE   A CD1  1 
ATOM   2871 C CD1  B ILE   A 1 131 ? 18.416 5.534   -3.645  0.28 20.52 ?  131 ILE   A CD1  1 
ATOM   2872 H H    A ILE   A 1 131 ? 16.267 2.559   -3.725  0.72 17.77 ?  131 ILE   A H    1 
ATOM   2873 H H    B ILE   A 1 131 ? 15.713 2.368   -3.703  0.28 22.21 ?  131 ILE   A H    1 
ATOM   2874 H HA   A ILE   A 1 131 ? 15.915 3.193   -6.235  0.72 17.38 ?  131 ILE   A HA   1 
ATOM   2875 H HA   B ILE   A 1 131 ? 15.411 3.208   -6.168  0.28 22.47 ?  131 ILE   A HA   1 
ATOM   2876 H HB   A ILE   A 1 131 ? 17.478 4.833   -5.986  0.72 18.62 ?  131 ILE   A HB   1 
ATOM   2877 H HB   B ILE   A 1 131 ? 16.789 4.954   -5.688  0.28 23.38 ?  131 ILE   A HB   1 
ATOM   2878 H HG12 A ILE   A 1 131 ? 18.231 3.688   -3.512  0.72 19.95 ?  131 ILE   A HG12 1 
ATOM   2879 H HG12 B ILE   A 1 131 ? 17.573 3.716   -3.274  0.28 24.08 ?  131 ILE   A HG12 1 
ATOM   2880 H HG13 A ILE   A 1 131 ? 19.129 3.640   -4.820  0.72 19.95 ?  131 ILE   A HG13 1 
ATOM   2881 H HG13 B ILE   A 1 131 ? 18.491 3.728   -4.568  0.28 24.08 ?  131 ILE   A HG13 1 
ATOM   2882 H HG21 A ILE   A 1 131 ? 16.497 6.077   -4.342  0.72 19.16 ?  131 ILE   A HG21 1 
ATOM   2883 H HG21 B ILE   A 1 131 ? 15.706 5.905   -3.885  0.28 23.66 ?  131 ILE   A HG21 1 
ATOM   2884 H HG22 A ILE   A 1 131 ? 15.354 5.178   -4.981  0.72 19.16 ?  131 ILE   A HG22 1 
ATOM   2885 H HG22 B ILE   A 1 131 ? 14.652 5.081   -4.738  0.28 23.66 ?  131 ILE   A HG22 1 
ATOM   2886 H HG23 A ILE   A 1 131 ? 15.999 4.768   -3.589  0.72 19.16 ?  131 ILE   A HG23 1 
ATOM   2887 H HG23 B ILE   A 1 131 ? 15.230 4.473   -3.388  0.28 23.66 ?  131 ILE   A HG23 1 
ATOM   2888 H HD11 A ILE   A 1 131 ? 19.990 5.275   -3.480  0.72 21.40 ?  131 ILE   A HD11 1 
ATOM   2889 H HD11 B ILE   A 1 131 ? 19.267 5.365   -3.212  0.28 24.66 ?  131 ILE   A HD11 1 
ATOM   2890 H HD12 A ILE   A 1 131 ? 19.307 6.004   -4.715  0.72 21.40 ?  131 ILE   A HD12 1 
ATOM   2891 H HD12 B ILE   A 1 131 ? 18.549 6.088   -4.431  0.28 24.66 ?  131 ILE   A HD12 1 
ATOM   2892 H HD13 A ILE   A 1 131 ? 18.563 5.953   -3.312  0.72 21.40 ?  131 ILE   A HD13 1 
ATOM   2893 H HD13 B ILE   A 1 131 ? 17.811 5.974   -3.029  0.28 24.66 ?  131 ILE   A HD13 1 
ATOM   2894 N N    A PHE   A 1 132 ? 18.033 1.000   -5.950  0.72 13.69 ?  132 PHE   A N    1 
ATOM   2895 N N    B PHE   A 1 132 ? 17.545 1.074   -5.983  0.28 17.98 ?  132 PHE   A N    1 
ATOM   2896 C CA   A PHE   A 1 132 ? 18.870 0.128   -6.775  0.72 14.23 ?  132 PHE   A CA   1 
ATOM   2897 C CA   B PHE   A 1 132 ? 18.598 0.365   -6.700  0.28 17.67 ?  132 PHE   A CA   1 
ATOM   2898 C C    A PHE   A 1 132 ? 18.066 -0.632  -7.827  0.72 14.94 ?  132 PHE   A C    1 
ATOM   2899 C C    B PHE   A 1 132 ? 18.116 -0.330  -7.970  0.28 17.82 ?  132 PHE   A C    1 
ATOM   2900 O O    A PHE   A 1 132 ? 18.668 -1.275  -8.694  0.72 15.26 ?  132 PHE   A O    1 
ATOM   2901 O O    B PHE   A 1 132 ? 18.947 -0.678  -8.816  0.28 18.35 ?  132 PHE   A O    1 
ATOM   2902 C CB   A PHE   A 1 132 ? 19.693 -0.853  -5.924  0.72 12.98 ?  132 PHE   A CB   1 
ATOM   2903 C CB   B PHE   A 1 132 ? 19.307 -0.634  -5.782  0.28 16.98 ?  132 PHE   A CB   1 
ATOM   2904 C CG   A PHE   A 1 132 ? 20.904 -0.239  -5.246  0.72 12.83 ?  132 PHE   A CG   1 
ATOM   2905 C CG   B PHE   A 1 132 ? 20.527 -0.076  -5.102  0.28 16.56 ?  132 PHE   A CG   1 
ATOM   2906 C CD1  A PHE   A 1 132 ? 20.778 0.800   -4.338  0.72 13.67 ?  132 PHE   A CD1  1 
ATOM   2907 C CD1  B PHE   A 1 132 ? 20.411 0.885   -4.109  0.28 16.62 ?  132 PHE   A CD1  1 
ATOM   2908 C CD2  A PHE   A 1 132 ? 22.174 -0.752  -5.485  0.72 13.38 ?  132 PHE   A CD2  1 
ATOM   2909 C CD2  B PHE   A 1 132 ? 21.790 -0.522  -5.451  0.28 16.49 ?  132 PHE   A CD2  1 
ATOM   2910 C CE1  A PHE   A 1 132 ? 21.901 1.340   -3.711  0.72 14.29 ?  132 PHE   A CE1  1 
ATOM   2911 C CE1  B PHE   A 1 132 ? 21.535 1.394   -3.484  0.28 16.76 ?  132 PHE   A CE1  1 
ATOM   2912 C CE2  A PHE   A 1 132 ? 23.294 -0.223  -4.859  0.72 14.08 ?  132 PHE   A CE2  1 
ATOM   2913 C CE2  B PHE   A 1 132 ? 22.915 -0.020  -4.830  0.28 16.80 ?  132 PHE   A CE2  1 
ATOM   2914 C CZ   A PHE   A 1 132 ? 23.153 0.826   -3.970  0.72 13.86 ?  132 PHE   A CZ   1 
ATOM   2915 C CZ   B PHE   A 1 132 ? 22.788 0.941   -3.844  0.28 16.57 ?  132 PHE   A CZ   1 
ATOM   2916 H H    A PHE   A 1 132 ? 17.856 0.679   -5.164  0.72 16.47 ?  132 PHE   A H    1 
ATOM   2917 H H    B PHE   A 1 132 ? 17.178 0.619   -5.345  0.28 21.61 ?  132 PHE   A H    1 
ATOM   2918 H HA   A PHE   A 1 132 ? 19.508 0.678   -7.248  0.72 17.11 ?  132 PHE   A HA   1 
ATOM   2919 H HA   B PHE   A 1 132 ? 19.261 1.021   -6.960  0.28 21.24 ?  132 PHE   A HA   1 
ATOM   2920 H HB2  A PHE   A 1 132 ? 19.130 -1.217  -5.228  0.72 15.62 ?  132 PHE   A HB2  1 
ATOM   2921 H HB2  B PHE   A 1 132 ? 18.694 -0.922  -5.092  0.28 20.41 ?  132 PHE   A HB2  1 
ATOM   2922 H HB3  A PHE   A 1 132 ? 20.016 -1.581  -6.494  0.72 15.62 ?  132 PHE   A HB3  1 
ATOM   2923 H HB3  B PHE   A 1 132 ? 19.587 -1.393  -6.313  0.28 20.41 ?  132 PHE   A HB3  1 
ATOM   2924 H HD1  A PHE   A 1 132 ? 19.942 1.149   -4.158  0.72 16.44 ?  132 PHE   A HD1  1 
ATOM   2925 H HD1  B PHE   A 1 132 ? 19.568 1.196   -3.863  0.28 19.98 ?  132 PHE   A HD1  1 
ATOM   2926 H HD2  A PHE   A 1 132 ? 22.286 -1.463  -6.083  0.72 16.09 ?  132 PHE   A HD2  1 
ATOM   2927 H HD2  B PHE   A 1 132 ? 21.879 -1.167  -6.115  0.28 19.83 ?  132 PHE   A HD2  1 
ATOM   2928 H HE1  A PHE   A 1 132 ? 21.807 2.042   -3.111  0.72 17.19 ?  132 PHE   A HE1  1 
ATOM   2929 H HE1  B PHE   A 1 132 ? 21.447 2.040   -2.819  0.28 20.15 ?  132 PHE   A HE1  1 
ATOM   2930 H HE2  A PHE   A 1 132 ? 24.141 -0.577  -5.043  0.72 16.93 ?  132 PHE   A HE2  1 
ATOM   2931 H HE2  B PHE   A 1 132 ? 23.757 -0.327  -5.076  0.28 20.19 ?  132 PHE   A HE2  1 
ATOM   2932 H HZ   A PHE   A 1 132 ? 23.910 1.182   -3.553  0.72 16.67 ?  132 PHE   A HZ   1 
ATOM   2933 H HZ   B PHE   A 1 132 ? 23.544 1.280   -3.425  0.28 19.92 ?  132 PHE   A HZ   1 
ATOM   2934 N N    A GLY   A 1 133 ? 16.732 -0.585  -7.768  0.72 15.19 ?  133 GLY   A N    1 
ATOM   2935 N N    B GLY   A 1 133 ? 16.810 -0.559  -8.126  0.28 17.23 ?  133 GLY   A N    1 
ATOM   2936 C CA   A GLY   A 1 133 ? 15.891 -0.950  -8.891  0.72 15.39 ?  133 GLY   A CA   1 
ATOM   2937 C CA   B GLY   A 1 133 ? 16.229 -0.918  -9.405  0.28 16.86 ?  133 GLY   A CA   1 
ATOM   2938 C C    A GLY   A 1 133 ? 15.587 -2.421  -9.085  0.72 15.70 ?  133 GLY   A C    1 
ATOM   2939 C C    B GLY   A 1 133 ? 15.655 -2.317  -9.503  0.28 16.75 ?  133 GLY   A C    1 
ATOM   2940 O O    A GLY   A 1 133 ? 14.932 -2.759  -10.077 0.72 17.10 ?  133 GLY   A O    1 
ATOM   2941 O O    B GLY   A 1 133 ? 14.848 -2.569  -10.409 0.28 16.99 ?  133 GLY   A O    1 
ATOM   2942 H H    A GLY   A 1 133 ? 16.286 -0.333  -7.073  0.72 18.26 ?  133 GLY   A H    1 
ATOM   2943 H H    B GLY   A 1 133 ? 16.239 -0.517  -7.485  0.28 20.71 ?  133 GLY   A H    1 
ATOM   2944 H HA2  A GLY   A 1 133 ? 15.035 -0.496  -8.804  0.72 18.50 ?  133 GLY   A HA2  1 
ATOM   2945 H HA2  B GLY   A 1 133 ? 15.516 -0.296  -9.612  0.28 20.27 ?  133 GLY   A HA2  1 
ATOM   2946 H HA3  A GLY   A 1 133 ? 16.304 -0.635  -9.709  0.72 18.50 ?  133 GLY   A HA3  1 
ATOM   2947 H HA3  B GLY   A 1 133 ? 16.905 -0.831  -10.093 0.28 20.27 ?  133 GLY   A HA3  1 
ATOM   2948 N N    A ALA   A 1 134 ? 16.025 -3.311  -8.198  0.72 15.14 ?  134 ALA   A N    1 
ATOM   2949 N N    B ALA   A 1 134 ? 16.036 -3.234  -8.617  0.28 16.46 ?  134 ALA   A N    1 
ATOM   2950 C CA   A ALA   A 1 134 ? 15.682 -4.716  -8.363  0.72 15.25 ?  134 ALA   A CA   1 
ATOM   2951 C CA   B ALA   A 1 134 ? 15.636 -4.626  -8.766  0.28 16.53 ?  134 ALA   A CA   1 
ATOM   2952 C C    A ALA   A 1 134 ? 14.319 -5.014  -7.739  0.72 15.55 ?  134 ALA   A C    1 
ATOM   2953 C C    B ALA   A 1 134 ? 14.306 -4.911  -8.065  0.28 16.76 ?  134 ALA   A C    1 
ATOM   2954 O O    A ALA   A 1 134 ? 13.783 -4.237  -6.944  0.72 17.04 ?  134 ALA   A O    1 
ATOM   2955 O O    B ALA   A 1 134 ? 13.783 -4.101  -7.296  0.28 17.15 ?  134 ALA   A O    1 
ATOM   2956 C CB   A ALA   A 1 134 ? 16.746 -5.620  -7.742  0.72 15.61 ?  134 ALA   A CB   1 
ATOM   2957 C CB   B ALA   A 1 134 ? 16.732 -5.563  -8.257  0.28 16.62 ?  134 ALA   A CB   1 
ATOM   2958 H H    A ALA   A 1 134 ? 16.516 -3.128  -7.507  0.72 18.21 ?  134 ALA   A H    1 
ATOM   2959 H H    B ALA   A 1 134 ? 16.528 -3.074  -7.926  0.28 19.78 ?  134 ALA   A H    1 
ATOM   2960 H HA   A ALA   A 1 134 ? 15.638 -4.914  -9.314  0.72 18.34 ?  134 ALA   A HA   1 
ATOM   2961 H HA   B ALA   A 1 134 ? 15.509 -4.809  -9.707  0.28 19.87 ?  134 ALA   A HA   1 
ATOM   2962 H HB1  A ALA   A 1 134 ? 16.491 -6.543  -7.887  0.72 18.78 ?  134 ALA   A HB1  1 
ATOM   2963 H HB1  B ALA   A 1 134 ? 16.442 -6.480  -8.379  0.28 19.98 ?  134 ALA   A HB1  1 
ATOM   2964 H HB2  A ALA   A 1 134 ? 17.599 -5.440  -8.169  0.72 18.78 ?  134 ALA   A HB2  1 
ATOM   2965 H HB2  B ALA   A 1 134 ? 17.542 -5.401  -8.767  0.28 19.98 ?  134 ALA   A HB2  1 
ATOM   2966 H HB3  A ALA   A 1 134 ? 16.802 -5.432  -6.795  0.72 18.78 ?  134 ALA   A HB3  1 
ATOM   2967 H HB3  B ALA   A 1 134 ? 16.890 -5.386  -7.319  0.28 19.98 ?  134 ALA   A HB3  1 
ATOM   2968 N N    A ASP   A 1 135 ? 13.760 -6.159  -8.123  0.72 16.51 ?  135 ASP   A N    1 
ATOM   2969 N N    B ASP   A 1 135 ? 13.758 -6.089  -8.357  0.28 17.08 ?  135 ASP   A N    1 
ATOM   2970 C CA   A ASP   A 1 135 ? 12.500 -6.632  -7.558  0.72 17.87 ?  135 ASP   A CA   1 
ATOM   2971 C CA   B ASP   A 1 135 ? 12.482 -6.512  -7.794  0.28 17.53 ?  135 ASP   A CA   1 
ATOM   2972 C C    A ASP   A 1 135 ? 12.736 -7.084  -6.121  0.72 17.22 ?  135 ASP   A C    1 
ATOM   2973 C C    B ASP   A 1 135 ? 12.690 -6.980  -6.357  0.28 16.98 ?  135 ASP   A C    1 
ATOM   2974 O O    A ASP   A 1 135 ? 13.494 -8.038  -5.900  0.72 16.75 ?  135 ASP   A O    1 
ATOM   2975 O O    B ASP   A 1 135 ? 13.489 -7.894  -6.125  0.28 16.65 ?  135 ASP   A O    1 
ATOM   2976 C CB   A ASP   A 1 135 ? 12.006 -7.803  -8.410  0.72 20.61 ?  135 ASP   A CB   1 
ATOM   2977 C CB   B ASP   A 1 135 ? 11.918 -7.657  -8.627  0.28 18.75 ?  135 ASP   A CB   1 
ATOM   2978 C CG   A ASP   A 1 135 ? 10.787 -8.509  -7.826  0.72 23.06 ?  135 ASP   A CG   1 
ATOM   2979 C CG   B ASP   A 1 135 ? 10.505 -8.048  -8.214  0.28 19.85 ?  135 ASP   A CG   1 
ATOM   2980 O OD1  A ASP   A 1 135 ? 10.187 -8.014  -6.848  0.72 23.06 ?  135 ASP   A OD1  1 
ATOM   2981 O OD1  B ASP   A 1 135 ? 10.030 -7.575  -7.160  0.28 20.44 ?  135 ASP   A OD1  1 
ATOM   2982 O OD2  A ASP   A 1 135 ? 10.438 -9.584  -8.360  0.72 25.68 -1 135 ASP   A OD2  1 
ATOM   2983 O OD2  B ASP   A 1 135 ? 9.861  -8.824  -8.953  0.28 20.33 -1 135 ASP   A OD2  1 
ATOM   2984 H H    A ASP   A 1 135 ? 14.095 -6.683  -8.719  0.72 19.85 ?  135 ASP   A H    1 
ATOM   2985 H H    B ASP   A 1 135 ? 14.105 -6.664  -8.888  0.28 20.54 ?  135 ASP   A H    1 
ATOM   2986 H HA   A ASP   A 1 135 ? 11.838 -5.918  -7.591  0.72 21.48 ?  135 ASP   A HA   1 
ATOM   2987 H HA   B ASP   A 1 135 ? 11.851 -5.776  -7.816  0.28 21.08 ?  135 ASP   A HA   1 
ATOM   2988 H HB2  A ASP   A 1 135 ? 11.788 -7.475  -9.299  0.72 24.77 ?  135 ASP   A HB2  1 
ATOM   2989 H HB2  B ASP   A 1 135 ? 11.898 -7.388  -9.559  0.28 22.54 ?  135 ASP   A HB2  1 
ATOM   2990 H HB3  A ASP   A 1 135 ? 12.705 -8.467  -8.464  0.72 24.77 ?  135 ASP   A HB3  1 
ATOM   2991 H HB3  B ASP   A 1 135 ? 12.492 -8.436  -8.523  0.28 22.54 ?  135 ASP   A HB3  1 
ATOM   2992 N N    A PRO   A 1 136 ? 12.134 -6.435  -5.121  0.72 17.10 ?  136 PRO   A N    1 
ATOM   2993 N N    B PRO   A 1 136 ? 11.998 -6.396  -5.375  0.28 17.00 ?  136 PRO   A N    1 
ATOM   2994 C CA   A PRO   A 1 136 ? 12.379 -6.849  -3.727  0.72 17.11 ?  136 PRO   A CA   1 
ATOM   2995 C CA   B PRO   A 1 136 ? 12.199 -6.835  -3.982  0.28 16.96 ?  136 PRO   A CA   1 
ATOM   2996 C C    A PRO   A 1 136 ? 11.925 -8.266  -3.411  0.72 15.90 ?  136 PRO   A C    1 
ATOM   2997 C C    B PRO   A 1 136 ? 11.854 -8.296  -3.741  0.28 16.70 ?  136 PRO   A C    1 
ATOM   2998 O O    A PRO   A 1 136 ? 12.492 -8.898  -2.512  0.72 15.21 ?  136 PRO   A O    1 
ATOM   2999 O O    B PRO   A 1 136 ? 12.516 -8.951  -2.928  0.28 16.59 ?  136 PRO   A O    1 
ATOM   3000 C CB   A PRO   A 1 136 ? 11.610 -5.801  -2.911  0.72 18.03 ?  136 PRO   A CB   1 
ATOM   3001 C CB   B PRO   A 1 136 ? 11.301 -5.878  -3.182  0.28 17.24 ?  136 PRO   A CB   1 
ATOM   3002 C CG   A PRO   A 1 136 ? 10.575 -5.267  -3.857  0.72 19.48 ?  136 PRO   A CG   1 
ATOM   3003 C CG   B PRO   A 1 136 ? 10.287 -5.388  -4.177  0.28 17.52 ?  136 PRO   A CG   1 
ATOM   3004 C CD   A PRO   A 1 136 ? 11.216 -5.285  -5.207  0.72 18.27 ?  136 PRO   A CD   1 
ATOM   3005 C CD   B PRO   A 1 136 ? 11.023 -5.297  -5.470  0.28 17.34 ?  136 PRO   A CD   1 
ATOM   3006 H HA   A PRO   A 1 136 ? 13.326 -6.768  -3.517  0.72 20.57 ?  136 PRO   A HA   1 
ATOM   3007 H HA   B PRO   A 1 136 ? 13.121 -6.690  -3.714  0.28 20.39 ?  136 PRO   A HA   1 
ATOM   3008 H HB2  A PRO   A 1 136 ? 11.188 -6.225  -2.149  0.72 21.68 ?  136 PRO   A HB2  1 
ATOM   3009 H HB2  B PRO   A 1 136 ? 10.869 -6.355  -2.457  0.28 20.73 ?  136 PRO   A HB2  1 
ATOM   3010 H HB3  A PRO   A 1 136 ? 12.211 -5.095  -2.628  0.72 21.68 ?  136 PRO   A HB3  1 
ATOM   3011 H HB3  B PRO   A 1 136 ? 11.831 -5.139  -2.839  0.28 20.73 ?  136 PRO   A HB3  1 
ATOM   3012 H HG2  A PRO   A 1 136 ? 9.795  -5.841  -3.847  0.72 23.41 ?  136 PRO   A HG2  1 
ATOM   3013 H HG2  B PRO   A 1 136 ? 9.560  -6.025  -4.240  0.28 21.07 ?  136 PRO   A HG2  1 
ATOM   3014 H HG3  A PRO   A 1 136 ? 10.340 -4.361  -3.608  0.72 23.41 ?  136 PRO   A HG3  1 
ATOM   3015 H HG3  B PRO   A 1 136 ? 9.960  -4.516  -3.911  0.28 21.07 ?  136 PRO   A HG3  1 
ATOM   3016 H HD2  A PRO   A 1 136 ? 10.549 -5.443  -5.898  0.72 21.97 ?  136 PRO   A HD2  1 
ATOM   3017 H HD2  B PRO   A 1 136 ? 10.418 -5.444  -6.213  0.28 20.85 ?  136 PRO   A HD2  1 
ATOM   3018 H HD3  A PRO   A 1 136 ? 11.706 -4.462  -5.371  0.72 21.97 ?  136 PRO   A HD3  1 
ATOM   3019 H HD3  B PRO   A 1 136 ? 11.484 -4.447  -5.546  0.28 20.85 ?  136 PRO   A HD3  1 
ATOM   3020 N N    A ILE   A 1 137 ? 10.897 -8.777  -4.097  0.72 16.28 ?  137 ILE   A N    1 
ATOM   3021 N N    B ILE   A 1 137 ? 10.831 -8.827  -4.415  0.28 16.82 ?  137 ILE   A N    1 
ATOM   3022 C CA   A ILE   A 1 137 ? 10.511 -10.174 -3.909  0.72 16.94 ?  137 ILE   A CA   1 
ATOM   3023 C CA   B ILE   A 1 137 ? 10.479 -10.235 -4.237  0.28 17.15 ?  137 ILE   A CA   1 
ATOM   3024 C C    A ILE   A 1 137 ? 11.660 -11.094 -4.308  0.72 16.33 ?  137 ILE   A C    1 
ATOM   3025 C C    B ILE   A 1 137 ? 11.665 -11.124 -4.589  0.28 16.84 ?  137 ILE   A C    1 
ATOM   3026 O O    A ILE   A 1 137 ? 11.980 -12.067 -3.609  0.72 16.55 ?  137 ILE   A O    1 
ATOM   3027 O O    B ILE   A 1 137 ? 11.927 -12.134 -3.923  0.28 16.96 ?  137 ILE   A O    1 
ATOM   3028 C CB   A ILE   A 1 137 ? 9.219  -10.485 -4.691  0.72 18.47 ?  137 ILE   A CB   1 
ATOM   3029 C CB   B ILE   A 1 137 ? 9.227  -10.583 -5.065  0.28 18.02 ?  137 ILE   A CB   1 
ATOM   3030 C CG1  A ILE   A 1 137 ? 8.055  -9.613  -4.198  0.72 20.39 ?  137 ILE   A CG1  1 
ATOM   3031 C CG1  B ILE   A 1 137 ? 8.027  -9.762  -4.584  0.28 18.69 ?  137 ILE   A CG1  1 
ATOM   3032 C CG2  A ILE   A 1 137 ? 8.870  -11.965 -4.580  0.72 19.00 ?  137 ILE   A CG2  1 
ATOM   3033 C CG2  B ILE   A 1 137 ? 8.921  -12.074 -4.979  0.28 18.29 ?  137 ILE   A CG2  1 
ATOM   3034 C CD1  A ILE   A 1 137 ? 6.754  -9.848  -4.942  0.72 21.80 ?  137 ILE   A CD1  1 
ATOM   3035 C CD1  B ILE   A 1 137 ? 6.753  -10.013 -5.366  0.28 19.28 ?  137 ILE   A CD1  1 
ATOM   3036 H H    A ILE   A 1 137 ? 10.422 -8.337  -4.667  0.72 19.57 ?  137 ILE   A H    1 
ATOM   3037 H H    B ILE   A 1 137 ? 10.339 -8.405  -4.977  0.28 20.22 ?  137 ILE   A H    1 
ATOM   3038 H HA   A ILE   A 1 137 ? 10.328 -10.317 -2.972  0.72 20.36 ?  137 ILE   A HA   1 
ATOM   3039 H HA   B ILE   A 1 137 ? 10.266 -10.391 -3.305  0.28 20.62 ?  137 ILE   A HA   1 
ATOM   3040 H HB   A ILE   A 1 137 ? 9.368  -10.274 -5.626  0.72 22.20 ?  137 ILE   A HB   1 
ATOM   3041 H HB   B ILE   A 1 137 ? 9.398  -10.360 -5.992  0.28 21.66 ?  137 ILE   A HB   1 
ATOM   3042 H HG12 A ILE   A 1 137 ? 7.900  -9.794  -3.260  0.72 24.51 ?  137 ILE   A HG12 1 
ATOM   3043 H HG12 B ILE   A 1 137 ? 7.853  -9.979  -3.655  0.28 22.46 ?  137 ILE   A HG12 1 
ATOM   3044 H HG13 A ILE   A 1 137 ? 8.292  -8.675  -4.315  0.72 24.51 ?  137 ILE   A HG13 1 
ATOM   3045 H HG13 B ILE   A 1 137 ? 8.242  -8.819  -4.666  0.28 22.46 ?  137 ILE   A HG13 1 
ATOM   3046 H HG21 A ILE   A 1 137 ? 8.021  -12.136 -5.016  0.72 22.84 ?  137 ILE   A HG21 1 
ATOM   3047 H HG21 B ILE   A 1 137 ? 8.097  -12.260 -5.455  0.28 21.98 ?  137 ILE   A HG21 1 
ATOM   3048 H HG22 A ILE   A 1 137 ? 9.562  -12.481 -5.013  0.72 22.84 ?  137 ILE   A HG22 1 
ATOM   3049 H HG22 B ILE   A 1 137 ? 9.646  -12.571 -5.383  0.28 21.98 ?  137 ILE   A HG22 1 
ATOM   3050 H HG23 A ILE   A 1 137 ? 8.811  -12.198 -3.644  0.72 22.84 ?  137 ILE   A HG23 1 
ATOM   3051 H HG23 B ILE   A 1 137 ? 8.825  -12.320 -4.046  0.28 21.98 ?  137 ILE   A HG23 1 
ATOM   3052 H HD11 A ILE   A 1 137 ? 6.098  -10.218 -4.329  0.72 26.19 ?  137 ILE   A HD11 1 
ATOM   3053 H HD11 B ILE   A 1 137 ? 6.123  -9.302  -5.177  0.28 23.18 ?  137 ILE   A HD11 1 
ATOM   3054 H HD12 A ILE   A 1 137 ? 6.450  -9.003  -5.293  0.72 26.19 ?  137 ILE   A HD12 1 
ATOM   3055 H HD12 B ILE   A 1 137 ? 6.963  -10.029 -6.312  0.28 23.18 ?  137 ILE   A HD12 1 
ATOM   3056 H HD13 A ILE   A 1 137 ? 6.907  -10.465 -5.677  0.72 26.19 ?  137 ILE   A HD13 1 
ATOM   3057 H HD13 B ILE   A 1 137 ? 6.380  -10.867 -5.095  0.28 23.18 ?  137 ILE   A HD13 1 
ATOM   3058 N N    A HIS   A 1 138 ? 12.294 -10.799 -5.444  0.72 16.80 ?  138 HIS   A N    1 
ATOM   3059 N N    B HIS   A 1 138 ? 12.397 -10.764 -5.642  0.28 16.82 ?  138 HIS   A N    1 
ATOM   3060 C CA   A HIS   A 1 138 ? 13.460 -11.566 -5.867  0.72 16.78 ?  138 HIS   A CA   1 
ATOM   3061 C CA   B HIS   A 1 138 ? 13.578 -11.534 -6.013  0.28 16.51 ?  138 HIS   A CA   1 
ATOM   3062 C C    A HIS   A 1 138 ? 14.610 -11.420 -4.876  0.72 15.99 ?  138 HIS   A C    1 
ATOM   3063 C C    B HIS   A 1 138 ? 14.683 -11.398 -4.969  0.28 15.73 ?  138 HIS   A C    1 
ATOM   3064 O O    A HIS   A 1 138 ? 15.264 -12.409 -4.519  0.72 16.18 ?  138 HIS   A O    1 
ATOM   3065 O O    B HIS   A 1 138 ? 15.368 -12.379 -4.653  0.28 15.60 ?  138 HIS   A O    1 
ATOM   3066 C CB   A HIS   A 1 138 ? 13.878 -11.128 -7.268  0.72 17.57 ?  138 HIS   A CB   1 
ATOM   3067 C CB   B HIS   A 1 138 ? 14.068 -11.097 -7.392  0.28 17.26 ?  138 HIS   A CB   1 
ATOM   3068 C CG   A HIS   A 1 138 ? 15.157 -11.750 -7.733  0.72 18.70 ?  138 HIS   A CG   1 
ATOM   3069 C CG   B HIS   A 1 138 ? 15.317 -11.793 -7.833  0.28 17.90 ?  138 HIS   A CG   1 
ATOM   3070 N ND1  A HIS   A 1 138 ? 15.278 -13.099 -7.991  0.72 19.78 ?  138 HIS   A ND1  1 
ATOM   3071 N ND1  B HIS   A 1 138 ? 15.382 -13.157 -8.025  0.28 18.46 ?  138 HIS   A ND1  1 
ATOM   3072 C CD2  A HIS   A 1 138 ? 16.373 -11.208 -7.974  0.72 18.92 ?  138 HIS   A CD2  1 
ATOM   3073 C CD2  B HIS   A 1 138 ? 16.551 -11.314 -8.113  0.28 18.21 ?  138 HIS   A CD2  1 
ATOM   3074 C CE1  A HIS   A 1 138 ? 16.515 -13.360 -8.377  0.72 20.20 ?  138 HIS   A CE1  1 
ATOM   3075 C CE1  B HIS   A 1 138 ? 16.603 -13.486 -8.407  0.28 18.76 ?  138 HIS   A CE1  1 
ATOM   3076 N NE2  A HIS   A 1 138 ? 17.200 -12.230 -8.373  0.72 19.66 ?  138 HIS   A NE2  1 
ATOM   3077 N NE2  B HIS   A 1 138 ? 17.332 -12.387 -8.467  0.28 18.65 ?  138 HIS   A NE2  1 
ATOM   3078 H H    A HIS   A 1 138 ? 12.069 -10.163 -5.987  0.72 20.20 ?  138 HIS   A H    1 
ATOM   3079 H H    B HIS   A 1 138 ? 12.226 -10.094 -6.156  0.28 20.22 ?  138 HIS   A H    1 
ATOM   3080 H HA   A HIS   A 1 138 ? 13.218 -12.500 -5.910  0.72 20.18 ?  138 HIS   A HA   1 
ATOM   3081 H HA   B HIS   A 1 138 ? 13.336 -12.469 -6.069  0.28 19.85 ?  138 HIS   A HA   1 
ATOM   3082 H HB2  A HIS   A 1 138 ? 13.180 -11.377 -7.898  0.72 21.12 ?  138 HIS   A HB2  1 
ATOM   3083 H HB2  B HIS   A 1 138 ? 13.375 -11.288 -8.045  0.28 20.75 ?  138 HIS   A HB2  1 
ATOM   3084 H HB3  A HIS   A 1 138 ? 13.997 -10.164 -7.278  0.72 21.12 ?  138 HIS   A HB3  1 
ATOM   3085 H HB3  B HIS   A 1 138 ? 14.249 -10.144 -7.375  0.28 20.75 ?  138 HIS   A HB3  1 
ATOM   3086 H HD1  A HIS   A 1 138 ? 14.645 -13.679 -7.915  0.72 23.77 ?  138 HIS   A HD1  1 
ATOM   3087 H HD2  A HIS   A 1 138 ? 16.604 -10.313 -7.888  0.72 22.74 ?  138 HIS   A HD2  1 
ATOM   3088 H HD2  B HIS   A 1 138 ? 16.818 -10.425 -8.073  0.28 21.90 ?  138 HIS   A HD2  1 
ATOM   3089 H HE1  A HIS   A 1 138 ? 16.845 -14.198 -8.609  0.72 24.28 ?  138 HIS   A HE1  1 
ATOM   3090 H HE1  B HIS   A 1 138 ? 16.896 -14.346 -8.600  0.28 22.55 ?  138 HIS   A HE1  1 
ATOM   3091 H HE2  B HIS   A 1 138 ? 18.159 -12.347 -8.693  0.28 22.41 ?  138 HIS   A HE2  1 
ATOM   3092 N N    . SER   A 1 139 ? 14.871 -10.197 -4.416  1.00 15.25 ?  139 SER   A N    1 
ATOM   3093 C CA   . SER   A 1 139 ? 15.934 -10.001 -3.440  1.00 15.10 ?  139 SER   A CA   1 
ATOM   3094 C C    . SER   A 1 139 ? 15.709 -10.847 -2.193  1.00 14.65 ?  139 SER   A C    1 
ATOM   3095 O O    . SER   A 1 139 ? 16.656 -11.441 -1.658  1.00 14.54 ?  139 SER   A O    1 
ATOM   3096 C CB   . SER   A 1 139 ? 16.052 -8.521  -3.080  1.00 14.90 ?  139 SER   A CB   1 
ATOM   3097 O OG   . SER   A 1 139 ? 17.132 -8.349  -2.178  1.00 15.18 ?  139 SER   A OG   1 
ATOM   3098 H H    A SER   A 1 139 ? 14.455 -9.479  -4.644  0.72 18.34 ?  139 SER   A H    1 
ATOM   3099 H H    B SER   A 1 139 ? 14.406 -9.493  -4.587  0.28 18.34 ?  139 SER   A H    1 
ATOM   3100 H HA   . SER   A 1 139 ? 16.781 -10.271 -3.831  1.00 18.15 ?  139 SER   A HA   1 
ATOM   3101 H HB2  . SER   A 1 139 ? 16.228 -8.000  -3.880  1.00 17.92 ?  139 SER   A HB2  1 
ATOM   3102 H HB3  . SER   A 1 139 ? 15.231 -8.225  -2.661  1.00 17.92 ?  139 SER   A HB3  1 
ATOM   3103 H HG   . SER   A 1 139 ? 17.216 -7.535  -1.962  1.00 18.26 ?  139 SER   A HG   1 
ATOM   3104 N N    . LEU   A 1 140 ? 14.465 -10.909 -1.710  1.00 14.63 ?  140 LEU   A N    1 
ATOM   3105 C CA   . LEU   A 1 140 ? 14.183 -11.725 -0.534  1.00 14.53 ?  140 LEU   A CA   1 
ATOM   3106 C C    . LEU   A 1 140 ? 14.449 -13.199 -0.813  1.00 14.36 ?  140 LEU   A C    1 
ATOM   3107 O O    . LEU   A 1 140 ? 14.995 -13.914 0.038   1.00 14.97 ?  140 LEU   A O    1 
ATOM   3108 C CB   . LEU   A 1 140 ? 12.741 -11.501 -0.088  1.00 15.09 ?  140 LEU   A CB   1 
ATOM   3109 C CG   . LEU   A 1 140 ? 12.264 -12.358 1.084   1.00 15.44 ?  140 LEU   A CG   1 
ATOM   3110 C CD1  . LEU   A 1 140 ? 13.174 -12.196 2.295   1.00 16.08 ?  140 LEU   A CD1  1 
ATOM   3111 C CD2  . LEU   A 1 140 ? 10.804 -12.015 1.435   1.00 16.25 ?  140 LEU   A CD2  1 
ATOM   3112 H H    . LEU   A 1 140 ? 13.789 -10.488 -2.033  1.00 17.59 ?  140 LEU   A H    1 
ATOM   3113 H HA   . LEU   A 1 140 ? 14.762 -11.448 0.193   1.00 17.47 ?  140 LEU   A HA   1 
ATOM   3114 H HB2  . LEU   A 1 140 ? 12.637 -10.578 0.177   1.00 18.14 ?  140 LEU   A HB2  1 
ATOM   3115 H HB3  . LEU   A 1 140 ? 12.156 -11.691 -0.839  1.00 18.14 ?  140 LEU   A HB3  1 
ATOM   3116 H HG   . LEU   A 1 140 ? 12.276 -13.296 0.816   1.00 18.57 ?  140 LEU   A HG   1 
ATOM   3117 H HD11 . LEU   A 1 140 ? 12.784 -12.674 3.046   1.00 19.33 ?  140 LEU   A HD11 1 
ATOM   3118 H HD12 . LEU   A 1 140 ? 14.042 -12.577 2.083   1.00 19.33 ?  140 LEU   A HD12 1 
ATOM   3119 H HD13 . LEU   A 1 140 ? 13.257 -11.260 2.502   1.00 19.33 ?  140 LEU   A HD13 1 
ATOM   3120 H HD21 . LEU   A 1 140 ? 10.514 -12.571 2.178   1.00 19.53 ?  140 LEU   A HD21 1 
ATOM   3121 H HD22 . LEU   A 1 140 ? 10.750 -11.080 1.685   1.00 19.53 ?  140 LEU   A HD22 1 
ATOM   3122 H HD23 . LEU   A 1 140 ? 10.238 -12.183 0.663   1.00 19.53 ?  140 LEU   A HD23 1 
ATOM   3123 N N    . ARG   A 1 141 ? 14.065 -13.669 -2.001  1.00 14.82 ?  141 ARG   A N    1 
ATOM   3124 C CA   . ARG   A 1 141 ? 14.309 -15.060 -2.368  1.00 16.34 ?  141 ARG   A CA   1 
ATOM   3125 C C    . ARG   A 1 141 ? 15.804 -15.368 -2.367  1.00 15.40 ?  141 ARG   A C    1 
ATOM   3126 O O    . ARG   A 1 141 ? 16.247 -16.384 -1.817  1.00 15.47 ?  141 ARG   A O    1 
ATOM   3127 C CB   . ARG   A 1 141 ? 13.701 -15.321 -3.747  1.00 18.36 ?  141 ARG   A CB   1 
ATOM   3128 C CG   . ARG   A 1 141 ? 13.739 -16.763 -4.204  1.00 21.46 ?  141 ARG   A CG   1 
ATOM   3129 C CD   . ARG   A 1 141 ? 12.693 -17.565 -3.490  1.00 23.82 ?  141 ARG   A CD   1 
ATOM   3130 N NE   . ARG   A 1 141 ? 13.271 -18.356 -2.415  1.00 24.60 ?  141 ARG   A NE   1 
ATOM   3131 C CZ   . ARG   A 1 141 ? 12.564 -18.901 -1.432  1.00 25.34 ?  141 ARG   A CZ   1 
ATOM   3132 N NH1  . ARG   A 1 141 ? 11.272 -18.649 -1.286  1.00 24.91 ?  141 ARG   A NH1  1 
ATOM   3133 N NH2  . ARG   A 1 141 ? 13.172 -19.702 -0.562  1.00 26.51 ?  141 ARG   A NH2  1 
ATOM   3134 H H    . ARG   A 1 141 ? 13.658 -13.205 -2.605  1.00 17.83 ?  141 ARG   A H    1 
ATOM   3135 H HA   . ARG   A 1 141 ? 13.878 -15.641 -1.730  1.00 19.65 ?  141 ARG   A HA   1 
ATOM   3136 H HB2  . ARG   A 1 141 ? 12.771 -15.037 -3.738  1.00 22.07 ?  141 ARG   A HB2  1 
ATOM   3137 H HB3  . ARG   A 1 141 ? 14.186 -14.797 -4.404  1.00 22.07 ?  141 ARG   A HB3  1 
ATOM   3138 H HG2  . ARG   A 1 141 ? 13.563 -16.807 -5.159  1.00 25.80 ?  141 ARG   A HG2  1 
ATOM   3139 H HG3  . ARG   A 1 141 ? 14.610 -17.147 -4.006  1.00 25.80 ?  141 ARG   A HG3  1 
ATOM   3140 H HD2  . ARG   A 1 141 ? 12.037 -16.968 -3.096  1.00 28.62 ?  141 ARG   A HD2  1 
ATOM   3141 H HD3  . ARG   A 1 141 ? 12.257 -18.162 -4.123  1.00 28.62 ?  141 ARG   A HD3  1 
ATOM   3142 H HE   . ARG   A 1 141 ? 14.094 -18.588 -2.486  1.00 29.56 ?  141 ARG   A HE   1 
ATOM   3143 H HH11 . ARG   A 1 141 ? 10.861 -18.143 -1.847  1.00 29.92 ?  141 ARG   A HH11 1 
ATOM   3144 H HH12 . ARG   A 1 141 ? 10.834 -19.006 -0.634  1.00 29.92 ?  141 ARG   A HH12 1 
ATOM   3145 H HH21 . ARG   A 1 141 ? 14.009 -19.870 -0.645  1.00 31.86 ?  141 ARG   A HH21 1 
ATOM   3146 H HH22 . ARG   A 1 141 ? 12.727 -20.046 0.091   1.00 31.86 ?  141 ARG   A HH22 1 
ATOM   3147 N N    . VAL   A 1 142 ? 16.606 -14.501 -2.990  1.00 14.79 ?  142 VAL   A N    1 
ATOM   3148 C CA   . VAL   A 1 142 ? 18.052 -14.716 -3.008  1.00 14.45 ?  142 VAL   A CA   1 
ATOM   3149 C C    . VAL   A 1 142 ? 18.612 -14.693 -1.592  1.00 13.97 ?  142 VAL   A C    1 
ATOM   3150 O O    . VAL   A 1 142 ? 19.473 -15.503 -1.236  1.00 14.33 ?  142 VAL   A O    1 
ATOM   3151 C CB   . VAL   A 1 142 ? 18.757 -13.696 -3.920  1.00 14.92 ?  142 VAL   A CB   1 
ATOM   3152 C CG1  . VAL   A 1 142 ? 20.272 -13.913 -3.870  1.00 14.64 ?  142 VAL   A CG1  1 
ATOM   3153 C CG2  . VAL   A 1 142 ? 18.266 -13.818 -5.350  1.00 16.27 ?  142 VAL   A CG2  1 
ATOM   3154 H H    . VAL   A 1 142 ? 16.345 -13.785 -3.404  1.00 17.78 ?  142 VAL   A H    1 
ATOM   3155 H HA   . VAL   A 1 142 ? 18.226 -15.589 -3.376  1.00 17.37 ?  142 VAL   A HA   1 
ATOM   3156 H HB   . VAL   A 1 142 ? 18.577 -12.791 -3.610  1.00 17.94 ?  142 VAL   A HB   1 
ATOM   3157 H HG11 . VAL   A 1 142 ? 20.689 -13.430 -4.601  1.00 17.61 ?  142 VAL   A HG11 1 
ATOM   3158 H HG12 . VAL   A 1 142 ? 20.616 -13.582 -3.022  1.00 17.61 ?  142 VAL   A HG12 1 
ATOM   3159 H HG13 . VAL   A 1 142 ? 20.457 -14.861 -3.954  1.00 17.61 ?  142 VAL   A HG13 1 
ATOM   3160 H HG21 . VAL   A 1 142 ? 18.734 -13.166 -5.900  1.00 19.56 ?  142 VAL   A HG21 1 
ATOM   3161 H HG22 . VAL   A 1 142 ? 18.460 -14.714 -5.667  1.00 19.56 ?  142 VAL   A HG22 1 
ATOM   3162 H HG23 . VAL   A 1 142 ? 17.318 -13.651 -5.370  1.00 19.56 ?  142 VAL   A HG23 1 
ATOM   3163 N N    . CYS   A 1 143 ? 18.141 -13.760 -0.764  1.00 13.72 ?  143 CYS   A N    1 
ATOM   3164 C CA   . CYS   A 1 143 ? 18.589 -13.709 0.623   1.00 13.91 ?  143 CYS   A CA   1 
ATOM   3165 C C    . CYS   A 1 143 ? 18.362 -15.050 1.313   1.00 13.91 ?  143 CYS   A C    1 
ATOM   3166 O O    . CYS   A 1 143 ? 19.279 -15.628 1.907   1.00 13.87 ?  143 CYS   A O    1 
ATOM   3167 C CB   . CYS   A 1 143 ? 17.843 -12.599 1.360   1.00 14.43 ?  143 CYS   A CB   1 
ATOM   3168 S SG   . CYS   A 1 143 ? 18.321 -12.416 3.084   1.00 14.71 ?  143 CYS   A SG   1 
ATOM   3169 H H    . CYS   A 1 143 ? 17.563 -13.161 -0.976  1.00 16.50 ?  143 CYS   A H    1 
ATOM   3170 H HA   . CYS   A 1 143 ? 19.536 -13.515 0.649   1.00 16.74 ?  143 CYS   A HA   1 
ATOM   3171 H HB2  . CYS   A 1 143 ? 18.012 -11.758 0.908   1.00 17.36 ?  143 CYS   A HB2  1 
ATOM   3172 H HB3  . CYS   A 1 143 ? 16.894 -12.795 1.334   1.00 17.36 ?  143 CYS   A HB3  1 
ATOM   3173 H HG   . CYS   A 1 143 ? 17.757 -11.464 3.542   1.00 17.69 ?  143 CYS   A HG   1 
ATOM   3174 N N    . VAL   A 1 144 ? 17.135 -15.563 1.237   1.00 14.79 ?  144 VAL   A N    1 
ATOM   3175 C CA   . VAL   A 1 144 ? 16.787 -16.795 1.935   1.00 16.07 ?  144 VAL   A CA   1 
ATOM   3176 C C    . VAL   A 1 144 ? 17.613 -17.965 1.422   1.00 15.45 ?  144 VAL   A C    1 
ATOM   3177 O O    . VAL   A 1 144 ? 17.967 -18.875 2.184   1.00 16.30 ?  144 VAL   A O    1 
ATOM   3178 C CB   . VAL   A 1 144 ? 15.273 -17.038 1.783   1.00 18.62 ?  144 VAL   A CB   1 
ATOM   3179 C CG1  . VAL   A 1 144 ? 14.917 -18.490 2.046   1.00 20.26 ?  144 VAL   A CG1  1 
ATOM   3180 C CG2  . VAL   A 1 144 ? 14.505 -16.072 2.687   1.00 18.43 ?  144 VAL   A CG2  1 
ATOM   3181 H H    . VAL   A 1 144 ? 16.481 -15.210 0.790   1.00 17.78 ?  144 VAL   A H    1 
ATOM   3182 H HA   . VAL   A 1 144 ? 16.969 -16.686 2.876   1.00 19.32 ?  144 VAL   A HA   1 
ATOM   3183 H HB   . VAL   A 1 144 ? 15.012 -16.834 0.866   1.00 22.38 ?  144 VAL   A HB   1 
ATOM   3184 H HG11 . VAL   A 1 144 ? 13.960 -18.555 2.206   1.00 24.35 ?  144 VAL   A HG11 1 
ATOM   3185 H HG12 . VAL   A 1 144 ? 15.153 -19.020 1.269   1.00 24.35 ?  144 VAL   A HG12 1 
ATOM   3186 H HG13 . VAL   A 1 144 ? 15.402 -18.795 2.824   1.00 24.35 ?  144 VAL   A HG13 1 
ATOM   3187 H HG21 . VAL   A 1 144 ? 13.548 -16.237 2.596   1.00 22.15 ?  144 VAL   A HG21 1 
ATOM   3188 H HG22 . VAL   A 1 144 ? 14.772 -16.214 3.607   1.00 22.15 ?  144 VAL   A HG22 1 
ATOM   3189 H HG23 . VAL   A 1 144 ? 14.700 -15.157 2.423   1.00 22.15 ?  144 VAL   A HG23 1 
ATOM   3190 N N    . ASP   A 1 145 ? 17.882 -17.992 0.121   1.00 16.03 ?  145 ASP   A N    1 
ATOM   3191 C CA   . ASP   A 1 145 ? 18.603 -19.095 -0.503  1.00 16.57 ?  145 ASP   A CA   1 
ATOM   3192 C C    . ASP   A 1 145 ? 20.120 -18.944 -0.442  1.00 16.19 ?  145 ASP   A C    1 
ATOM   3193 O O    . ASP   A 1 145 ? 20.833 -19.834 -0.921  1.00 17.97 ?  145 ASP   A O    1 
ATOM   3194 C CB   . ASP   A 1 145 ? 18.174 -19.230 -1.968  1.00 18.43 ?  145 ASP   A CB   1 
ATOM   3195 C CG   . ASP   A 1 145 ? 16.731 -19.688 -2.119  1.00 20.83 ?  145 ASP   A CG   1 
ATOM   3196 O OD1  . ASP   A 1 145 ? 16.150 -20.227 -1.150  1.00 21.34 ?  145 ASP   A OD1  1 
ATOM   3197 O OD2  . ASP   A 1 145 ? 16.171 -19.504 -3.219  1.00 22.21 -1 145 ASP   A OD2  1 
ATOM   3198 H H    . ASP   A 1 145 ? 17.637 -17.378 -0.434  1.00 19.28 ?  145 ASP   A H    1 
ATOM   3199 H HA   . ASP   A 1 145 ? 18.363 -19.918 -0.050  1.00 19.93 ?  145 ASP   A HA   1 
ATOM   3200 H HB2  . ASP   A 1 145 ? 18.268 -18.367 -2.405  1.00 22.15 ?  145 ASP   A HB2  1 
ATOM   3201 H HB3  . ASP   A 1 145 ? 18.745 -19.883 -2.402  1.00 22.15 ?  145 ASP   A HB3  1 
ATOM   3202 N N    . THR   A 1 146 ? 20.636 -17.848 0.114   1.00 14.58 ?  146 THR   A N    1 
ATOM   3203 C CA   . THR   A 1 146 ? 22.074 -17.592 0.140   1.00 14.01 ?  146 THR   A CA   1 
ATOM   3204 C C    . THR   A 1 146 ? 22.616 -17.404 1.546   1.00 13.85 ?  146 THR   A C    1 
ATOM   3205 O O    . THR   A 1 146 ? 23.693 -17.934 1.868   1.00 14.89 ?  146 THR   A O    1 
ATOM   3206 C CB   . THR   A 1 146 ? 22.397 -16.341 -0.697  1.00 14.12 ?  146 THR   A CB   1 
ATOM   3207 O OG1  . THR   A 1 146 ? 21.882 -16.508 -2.019  1.00 14.77 ?  146 THR   A OG1  1 
ATOM   3208 C CG2  . THR   A 1 146 ? 23.903 -16.095 -0.767  1.00 14.41 ?  146 THR   A CG2  1 
ATOM   3209 H H    . THR   A 1 146 ? 20.164 -17.222 0.476   1.00 17.54 ?  146 THR   A H    1 
ATOM   3210 H HA   . THR   A 1 146 ? 22.539 -18.341 -0.256  1.00 16.85 ?  146 THR   A HA   1 
ATOM   3211 H HB   . THR   A 1 146 ? 21.984 -15.564 -0.287  1.00 16.98 ?  146 THR   A HB   1 
ATOM   3212 H HG1  . THR   A 1 146 ? 21.050 -16.589 -1.993  1.00 17.76 ?  146 THR   A HG1  1 
ATOM   3213 H HG21 . THR   A 1 146 ? 24.096 -15.431 -1.446  1.00 17.33 ?  146 THR   A HG21 1 
ATOM   3214 H HG22 . THR   A 1 146 ? 24.227 -15.772 0.090   1.00 17.33 ?  146 THR   A HG22 1 
ATOM   3215 H HG23 . THR   A 1 146 ? 24.361 -16.918 -0.989  1.00 17.33 ?  146 THR   A HG23 1 
ATOM   3216 N N    . VAL   A 1 147 ? 21.935 -16.619 2.374   1.00 13.60 ?  147 VAL   A N    1 
ATOM   3217 C CA   . VAL   A 1 147 ? 22.425 -16.321 3.712   1.00 13.83 ?  147 VAL   A CA   1 
ATOM   3218 C C    . VAL   A 1 147 ? 22.104 -17.487 4.638   1.00 14.14 ?  147 VAL   A C    1 
ATOM   3219 O O    . VAL   A 1 147 ? 20.962 -17.969 4.686   1.00 14.72 ?  147 VAL   A O    1 
ATOM   3220 C CB   . VAL   A 1 147 ? 21.805 -15.016 4.226   1.00 13.92 ?  147 VAL   A CB   1 
ATOM   3221 C CG1  . VAL   A 1 147 ? 22.334 -14.695 5.600   1.00 14.78 ?  147 VAL   A CG1  1 
ATOM   3222 C CG2  . VAL   A 1 147 ? 22.049 -13.872 3.238   1.00 14.32 ?  147 VAL   A CG2  1 
ATOM   3223 H H    . VAL   A 1 147 ? 21.180 -16.251 2.187   1.00 16.36 ?  147 VAL   A H    1 
ATOM   3224 H HA   . VAL   A 1 147 ? 23.388 -16.211 3.681   1.00 16.63 ?  147 VAL   A HA   1 
ATOM   3225 H HB   . VAL   A 1 147 ? 20.849 -15.141 4.305   1.00 16.75 ?  147 VAL   A HB   1 
ATOM   3226 H HG11 . VAL   A 1 147 ? 22.084 -13.789 5.829   1.00 17.77 ?  147 VAL   A HG11 1 
ATOM   3227 H HG12 . VAL   A 1 147 ? 21.949 -15.317 6.240   1.00 17.77 ?  147 VAL   A HG12 1 
ATOM   3228 H HG13 . VAL   A 1 147 ? 23.300 -14.783 5.595   1.00 17.77 ?  147 VAL   A HG13 1 
ATOM   3229 H HG21 . VAL   A 1 147 ? 21.730 -13.046 3.633   1.00 17.22 ?  147 VAL   A HG21 1 
ATOM   3230 H HG22 . VAL   A 1 147 ? 22.993 -13.812 3.049   1.00 17.22 ?  147 VAL   A HG22 1 
ATOM   3231 H HG23 . VAL   A 1 147 ? 21.556 -14.056 2.420   1.00 17.22 ?  147 VAL   A HG23 1 
ATOM   3232 N N    . ARG   A 1 148 ? 23.124 -17.949 5.365   1.00 14.34 ?  148 ARG   A N    1 
ATOM   3233 C CA   . ARG   A 1 148 ? 22.993 -19.025 6.335   1.00 14.46 ?  148 ARG   A CA   1 
ATOM   3234 C C    . ARG   A 1 148 ? 23.106 -18.550 7.773   1.00 14.84 ?  148 ARG   A C    1 
ATOM   3235 O O    . ARG   A 1 148 ? 22.686 -19.272 8.686   1.00 16.36 ?  148 ARG   A O    1 
ATOM   3236 C CB   . ARG   A 1 148 ? 24.045 -20.110 6.075   1.00 15.32 ?  148 ARG   A CB   1 
ATOM   3237 C CG   . ARG   A 1 148 ? 23.908 -20.761 4.715   1.00 16.54 ?  148 ARG   A CG   1 
ATOM   3238 C CD   . ARG   A 1 148 ? 25.015 -21.782 4.459   1.00 17.56 ?  148 ARG   A CD   1 
ATOM   3239 N NE   . ARG   A 1 148 ? 26.349 -21.192 4.496   1.00 17.41 ?  148 ARG   A NE   1 
ATOM   3240 C CZ   . ARG   A 1 148 ? 26.866 -20.464 3.516   1.00 16.56 ?  148 ARG   A CZ   1 
ATOM   3241 N NH1  . ARG   A 1 148 ? 26.205 -20.260 2.388   1.00 16.76 ?  148 ARG   A NH1  1 
ATOM   3242 N NH2  . ARG   A 1 148 ? 28.077 -19.924 3.671   1.00 16.86 ?  148 ARG   A NH2  1 
ATOM   3243 H H    . ARG   A 1 148 ? 23.928 -17.641 5.301   1.00 17.24 ?  148 ARG   A H    1 
ATOM   3244 H HA   . ARG   A 1 148 ? 22.122 -19.430 6.233   1.00 17.38 ?  148 ARG   A HA   1 
ATOM   3245 H HB2  . ARG   A 1 148 ? 24.929 -19.723 6.131   1.00 18.42 ?  148 ARG   A HB2  1 
ATOM   3246 H HB3  . ARG   A 1 148 ? 23.947 -20.812 6.743   1.00 18.42 ?  148 ARG   A HB3  1 
ATOM   3247 H HG2  . ARG   A 1 148 ? 23.050 -21.210 4.666   1.00 19.88 ?  148 ARG   A HG2  1 
ATOM   3248 H HG3  . ARG   A 1 148 ? 23.962 -20.068 4.034   1.00 19.88 ?  148 ARG   A HG3  1 
ATOM   3249 H HD2  . ARG   A 1 148 ? 24.968 -22.465 5.143   1.00 21.11 ?  148 ARG   A HD2  1 
ATOM   3250 H HD3  . ARG   A 1 148 ? 24.878 -22.172 3.584   1.00 21.11 ?  148 ARG   A HD3  1 
ATOM   3251 H HE   . ARG   A 1 148 ? 26.822 -21.316 5.200   1.00 20.92 ?  148 ARG   A HE   1 
ATOM   3252 H HH11 . ARG   A 1 148 ? 25.424 -20.590 2.278   1.00 20.15 ?  148 ARG   A HH11 1 
ATOM   3253 H HH12 . ARG   A 1 148 ? 26.562 -19.779 1.767   1.00 20.15 ?  148 ARG   A HH12 1 
ATOM   3254 H HH21 . ARG   A 1 148 ? 28.512 -20.049 4.402   1.00 20.27 ?  148 ARG   A HH21 1 
ATOM   3255 H HH22 . ARG   A 1 148 ? 28.422 -19.450 3.041   1.00 20.27 ?  148 ARG   A HH22 1 
ATOM   3256 N N    . THR   A 1 149 ? 23.658 -17.359 7.986   1.00 14.67 ?  149 THR   A N    1 
ATOM   3257 C CA   . THR   A 1 149 ? 23.720 -16.752 9.299   1.00 14.76 ?  149 THR   A CA   1 
ATOM   3258 C C    . THR   A 1 149 ? 22.391 -16.051 9.592   1.00 14.60 ?  149 THR   A C    1 
ATOM   3259 O O    . THR   A 1 149 ? 21.463 -16.048 8.770   1.00 15.07 ?  149 THR   A O    1 
ATOM   3260 C CB   . THR   A 1 149 ? 24.917 -15.810 9.361   1.00 15.32 ?  149 THR   A CB   1 
ATOM   3261 O OG1  . THR   A 1 149 ? 24.799 -14.881 8.281   1.00 15.44 ?  149 THR   A OG1  1 
ATOM   3262 C CG2  . THR   A 1 149 ? 26.240 -16.597 9.250   1.00 15.62 ?  149 THR   A CG2  1 
ATOM   3263 H H    . THR   A 1 149 ? 24.014 -16.866 7.366   1.00 17.64 ?  149 THR   A H    1 
ATOM   3264 H HA   . THR   A 1 149 ? 23.848 -17.450 9.960   1.00 17.75 ?  149 THR   A HA   1 
ATOM   3265 H HB   . THR   A 1 149 ? 24.911 -15.335 10.204  1.00 18.43 ?  149 THR   A HB   1 
ATOM   3266 H HG1  . THR   A 1 149 ? 25.451 -14.351 8.285   1.00 18.56 ?  149 THR   A HG1  1 
ATOM   3267 H HG21 . THR   A 1 149 ? 26.996 -15.991 9.304   1.00 18.78 ?  149 THR   A HG21 1 
ATOM   3268 H HG22 . THR   A 1 149 ? 26.308 -17.247 9.970   1.00 18.78 ?  149 THR   A HG22 1 
ATOM   3269 H HG23 . THR   A 1 149 ? 26.281 -17.071 8.401   1.00 18.78 ?  149 THR   A HG23 1 
ATOM   3270 N N    . ASN   A 1 150 ? 22.263 -15.513 10.799  1.00 15.28 ?  150 ASN   A N    1 
ATOM   3271 C CA   . ASN   A 1 150 ? 20.980 -14.994 11.267  1.00 15.60 ?  150 ASN   A CA   1 
ATOM   3272 C C    . ASN   A 1 150 ? 20.808 -13.554 10.800  1.00 14.58 ?  150 ASN   A C    1 
ATOM   3273 O O    . ASN   A 1 150 ? 21.566 -12.663 11.208  1.00 15.84 ?  150 ASN   A O    1 
ATOM   3274 C CB   . ASN   A 1 150 ? 20.894 -15.100 12.786  1.00 17.95 ?  150 ASN   A CB   1 
ATOM   3275 C CG   . ASN   A 1 150 ? 20.777 -16.533 13.252  1.00 21.49 ?  150 ASN   A CG   1 
ATOM   3276 O OD1  . ASN   A 1 150 ? 20.184 -17.364 12.567  1.00 22.62 ?  150 ASN   A OD1  1 
ATOM   3277 N ND2  . ASN   A 1 150 ? 21.358 -16.838 14.409  1.00 23.94 ?  150 ASN   A ND2  1 
ATOM   3278 H H    . ASN   A 1 150 ? 22.905 -15.438 11.368  1.00 18.37 ?  150 ASN   A H    1 
ATOM   3279 H HA   . ASN   A 1 150 ? 20.264 -15.529 10.890  1.00 18.76 ?  150 ASN   A HA   1 
ATOM   3280 H HB2  . ASN   A 1 150 ? 21.695 -14.725 13.182  1.00 21.58 ?  150 ASN   A HB2  1 
ATOM   3281 H HB3  . ASN   A 1 150 ? 20.109 -14.628 13.099  1.00 21.58 ?  150 ASN   A HB3  1 
ATOM   3282 H HD21 . ASN   A 1 150 ? 21.325 -17.645 14.718  1.00 28.76 ?  150 ASN   A HD21 1 
ATOM   3283 H HD22 . ASN   A 1 150 ? 21.768 -16.230 14.860  1.00 28.76 ?  150 ASN   A HD22 1 
ATOM   3284 N N    . VAL   A 1 151 ? 19.816 -13.323 9.946   1.00 14.21 ?  151 VAL   A N    1 
ATOM   3285 C CA   . VAL   A 1 151 ? 19.607 -12.021 9.334   1.00 14.56 ?  151 VAL   A CA   1 
ATOM   3286 C C    . VAL   A 1 151 ? 18.221 -11.498 9.694   1.00 14.52 ?  151 VAL   A C    1 
ATOM   3287 O O    . VAL   A 1 151 ? 17.209 -12.209 9.561   1.00 15.86 ?  151 VAL   A O    1 
ATOM   3288 C CB   . VAL   A 1 151 ? 19.898 -12.028 7.819   1.00 15.88 ?  151 VAL   A CB   1 
ATOM   3289 C CG1  . VAL   A 1 151 ? 19.081 -13.066 7.082   1.00 16.86 ?  151 VAL   A CG1  1 
ATOM   3290 C CG2  . VAL   A 1 151 ? 19.705 -10.624 7.224   1.00 16.06 ?  151 VAL   A CG2  1 
ATOM   3291 H H    . VAL   A 1 151 ? 19.240 -13.916 9.707   1.00 17.09 ?  151 VAL   A H    1 
ATOM   3292 H HA   . VAL   A 1 151 ? 20.250 -11.406 9.728   1.00 17.51 ?  151 VAL   A HA   1 
ATOM   3293 H HB   . VAL   A 1 151 ? 20.836 -12.261 7.694   1.00 19.10 ?  151 VAL   A HB   1 
ATOM   3294 H HG11 . VAL   A 1 151 ? 19.260 -12.999 6.131   1.00 20.27 ?  151 VAL   A HG11 1 
ATOM   3295 H HG12 . VAL   A 1 151 ? 19.336 -13.952 7.400   1.00 20.27 ?  151 VAL   A HG12 1 
ATOM   3296 H HG13 . VAL   A 1 151 ? 18.141 -12.915 7.256   1.00 20.27 ?  151 VAL   A HG13 1 
ATOM   3297 H HG21 . VAL   A 1 151 ? 20.021 -10.626 6.304   1.00 19.31 ?  151 VAL   A HG21 1 
ATOM   3298 H HG22 . VAL   A 1 151 ? 18.763 -10.398 7.246   1.00 19.31 ?  151 VAL   A HG22 1 
ATOM   3299 H HG23 . VAL   A 1 151 ? 20.215 -9.985  7.743   1.00 19.31 ?  151 VAL   A HG23 1 
ATOM   3300 N N    A TYR   A 1 152 ? 18.203 -10.260 10.179  0.72 14.54 ?  152 TYR   A N    1 
ATOM   3301 N N    B TYR   A 1 152 ? 18.191 -10.236 10.137  0.28 14.65 ?  152 TYR   A N    1 
ATOM   3302 C CA   A TYR   A 1 152 ? 17.002 -9.530  10.550  0.72 13.92 ?  152 TYR   A CA   1 
ATOM   3303 C CA   B TYR   A 1 152 ? 16.984 -9.527  10.550  0.28 14.50 ?  152 TYR   A CA   1 
ATOM   3304 C C    A TYR   A 1 152 ? 16.810 -8.432  9.514   0.72 13.65 ?  152 TYR   A C    1 
ATOM   3305 C C    B TYR   A 1 152 ? 16.758 -8.392  9.561   0.28 14.20 ?  152 TYR   A C    1 
ATOM   3306 O O    A TYR   A 1 152 ? 17.605 -7.486  9.449   0.72 13.87 ?  152 TYR   A O    1 
ATOM   3307 O O    B TYR   A 1 152 ? 17.452 -7.371  9.604   0.28 14.45 ?  152 TYR   A O    1 
ATOM   3308 C CB   A TYR   A 1 152 ? 17.163 -8.988  11.967  0.72 14.86 ?  152 TYR   A CB   1 
ATOM   3309 C CB   B TYR   A 1 152 ? 17.145 -9.003  11.973  0.28 15.17 ?  152 TYR   A CB   1 
ATOM   3310 C CG   A TYR   A 1 152 ? 17.165 -10.116 12.968  0.72 15.47 ?  152 TYR   A CG   1 
ATOM   3311 C CG   B TYR   A 1 152 ? 16.995 -10.086 13.008  0.28 15.77 ?  152 TYR   A CG   1 
ATOM   3312 C CD1  A TYR   A 1 152 ? 18.326 -10.820 13.266  0.72 16.97 ?  152 TYR   A CD1  1 
ATOM   3313 C CD1  B TYR   A 1 152 ? 18.049 -10.938 13.308  0.28 16.34 ?  152 TYR   A CD1  1 
ATOM   3314 C CD2  A TYR   A 1 152 ? 15.990 -10.516 13.583  0.72 15.49 ?  152 TYR   A CD2  1 
ATOM   3315 C CD2  B TYR   A 1 152 ? 15.793 -10.269 13.676  0.28 15.86 ?  152 TYR   A CD2  1 
ATOM   3316 C CE1  A TYR   A 1 152 ? 18.319 -11.880 14.162  0.72 17.81 ?  152 TYR   A CE1  1 
ATOM   3317 C CE1  B TYR   A 1 152 ? 17.912 -11.940 14.250  0.28 16.87 ?  152 TYR   A CE1  1 
ATOM   3318 C CE2  A TYR   A 1 152 ? 15.969 -11.580 14.480  0.72 16.63 ?  152 TYR   A CE2  1 
ATOM   3319 C CE2  B TYR   A 1 152 ? 15.646 -11.268 14.621  0.28 16.55 ?  152 TYR   A CE2  1 
ATOM   3320 C CZ   A TYR   A 1 152 ? 17.139 -12.258 14.767  0.72 17.56 ?  152 TYR   A CZ   1 
ATOM   3321 C CZ   B TYR   A 1 152 ? 16.708 -12.101 14.902  0.28 17.01 ?  152 TYR   A CZ   1 
ATOM   3322 O OH   A TYR   A 1 152 ? 17.133 -13.314 15.660  0.72 19.33 ?  152 TYR   A OH   1 
ATOM   3323 O OH   B TYR   A 1 152 ? 16.565 -13.093 15.842  0.28 18.07 ?  152 TYR   A OH   1 
ATOM   3324 H H    A TYR   A 1 152 ? 18.925 -9.791  10.296  0.72 17.48 ?  152 TYR   A H    1 
ATOM   3325 H H    B TYR   A 1 152 ? 18.901 -9.740  10.197  0.28 17.62 ?  152 TYR   A H    1 
ATOM   3326 H HA   A TYR   A 1 152 ? 16.243 -10.130 10.523  0.72 16.74 ?  152 TYR   A HA   1 
ATOM   3327 H HA   B TYR   A 1 152 ? 16.226 -10.121 10.518  0.28 17.43 ?  152 TYR   A HA   1 
ATOM   3328 H HB2  A TYR   A 1 152 ? 18.005 -8.519  12.039  0.72 17.87 ?  152 TYR   A HB2  1 
ATOM   3329 H HB2  B TYR   A 1 152 ? 18.029 -8.619  12.070  0.28 18.25 ?  152 TYR   A HB2  1 
ATOM   3330 H HB3  A TYR   A 1 152 ? 16.422 -8.402  12.168  0.72 17.87 ?  152 TYR   A HB3  1 
ATOM   3331 H HB3  B TYR   A 1 152 ? 16.472 -8.326  12.142  0.28 18.25 ?  152 TYR   A HB3  1 
ATOM   3332 H HD1  A TYR   A 1 152 ? 19.122 -10.577 12.858  0.72 20.41 ?  152 TYR   A HD1  1 
ATOM   3333 H HD1  B TYR   A 1 152 ? 18.861 -10.829 12.864  0.28 19.65 ?  152 TYR   A HD1  1 
ATOM   3334 H HD2  A TYR   A 1 152 ? 15.194 -10.072 13.388  0.72 18.63 ?  152 TYR   A HD2  1 
ATOM   3335 H HD2  B TYR   A 1 152 ? 15.073 -9.709  13.485  0.28 19.07 ?  152 TYR   A HD2  1 
ATOM   3336 H HE1  A TYR   A 1 152 ? 19.104 -12.335 14.359  0.72 21.41 ?  152 TYR   A HE1  1 
ATOM   3337 H HE1  B TYR   A 1 152 ? 18.629 -12.500 14.441  0.28 20.28 ?  152 TYR   A HE1  1 
ATOM   3338 H HE2  A TYR   A 1 152 ? 15.168 -11.829 14.889  0.72 20.00 ?  152 TYR   A HE2  1 
ATOM   3339 H HE2  B TYR   A 1 152 ? 14.835 -11.380 15.063  0.28 19.89 ?  152 TYR   A HE2  1 
ATOM   3340 H HH   A TYR   A 1 152 ? 16.348 -13.424 15.956  0.72 23.24 ?  152 TYR   A HH   1 
ATOM   3341 H HH   B TYR   A 1 152 ? 15.820 -13.459 15.754  0.28 21.72 ?  152 TYR   A HH   1 
ATOM   3342 N N    A LEU   A 1 153 ? 15.790 -8.596  8.674   0.72 13.94 ?  153 LEU   A N    1 
ATOM   3343 N N    B LEU   A 1 153 ? 15.791 -8.580  8.667   0.28 14.06 ?  153 LEU   A N    1 
ATOM   3344 C CA   A LEU   A 1 153 ? 15.542 -7.720  7.537   0.72 13.91 ?  153 LEU   A CA   1 
ATOM   3345 C CA   B LEU   A 1 153 ? 15.515 -7.627  7.604   0.28 13.80 ?  153 LEU   A CA   1 
ATOM   3346 C C    A LEU   A 1 153 ? 14.537 -6.644  7.918   0.72 14.32 ?  153 LEU   A C    1 
ATOM   3347 C C    B LEU   A 1 153 ? 14.545 -6.556  8.085   0.28 13.83 ?  153 LEU   A C    1 
ATOM   3348 O O    A LEU   A 1 153 ? 13.414 -6.954  8.339   0.72 15.27 ?  153 LEU   A O    1 
ATOM   3349 O O    B LEU   A 1 153 ? 13.529 -6.865  8.719   0.28 13.95 ?  153 LEU   A O    1 
ATOM   3350 C CB   A LEU   A 1 153 ? 14.988 -8.521  6.361   0.72 13.84 ?  153 LEU   A CB   1 
ATOM   3351 C CB   B LEU   A 1 153 ? 14.929 -8.350  6.391   0.28 13.88 ?  153 LEU   A CB   1 
ATOM   3352 C CG   A LEU   A 1 153 ? 15.935 -9.514  5.691   0.72 13.83 ?  153 LEU   A CG   1 
ATOM   3353 C CG   B LEU   A 1 153 ? 15.852 -9.389  5.752   0.28 14.00 ?  153 LEU   A CG   1 
ATOM   3354 C CD1  A LEU   A 1 153 ? 15.146 -10.432 4.772   0.72 13.84 ?  153 LEU   A CD1  1 
ATOM   3355 C CD1  B LEU   A 1 153 ? 15.139 -10.108 4.613   0.28 14.41 ?  153 LEU   A CD1  1 
ATOM   3356 C CD2  A LEU   A 1 153 ? 17.010 -8.774  4.910   0.72 13.84 ?  153 LEU   A CD2  1 
ATOM   3357 C CD2  B LEU   A 1 153 ? 17.147 -8.742  5.267   0.28 14.09 ?  153 LEU   A CD2  1 
ATOM   3358 H H    A LEU   A 1 153 ? 15.206 -9.233  8.747   0.72 16.76 ?  153 LEU   A H    1 
ATOM   3359 H H    B LEU   A 1 153 ? 15.276 -9.268  8.654   0.28 16.91 ?  153 LEU   A H    1 
ATOM   3360 H HA   A LEU   A 1 153 ? 16.374 -7.299  7.272   0.72 16.73 ?  153 LEU   A HA   1 
ATOM   3361 H HA   B LEU   A 1 153 ? 16.337 -7.197  7.338   0.28 16.59 ?  153 LEU   A HA   1 
ATOM   3362 H HB2  A LEU   A 1 153 ? 14.218 -9.020  6.674   0.72 16.65 ?  153 LEU   A HB2  1 
ATOM   3363 H HB2  B LEU   A 1 153 ? 14.119 -8.808  6.666   0.28 16.69 ?  153 LEU   A HB2  1 
ATOM   3364 H HB3  A LEU   A 1 153 ? 14.706 -7.891  5.679   0.72 16.65 ?  153 LEU   A HB3  1 
ATOM   3365 H HB3  B LEU   A 1 153 ? 14.714 -7.692  5.711   0.28 16.69 ?  153 LEU   A HB3  1 
ATOM   3366 H HG   A LEU   A 1 153 ? 16.366 -10.057 6.373   0.72 16.63 ?  153 LEU   A HG   1 
ATOM   3367 H HG   B LEU   A 1 153 ? 16.085 -10.052 6.420   0.28 16.84 ?  153 LEU   A HG   1 
ATOM   3368 H HD11 A LEU   A 1 153 ? 15.740 -11.114 4.422   0.72 16.65 ?  153 LEU   A HD11 1 
ATOM   3369 H HD11 B LEU   A 1 153 ? 15.717 -10.805 4.266   0.28 17.33 ?  153 LEU   A HD11 1 
ATOM   3370 H HD12 A LEU   A 1 153 ? 14.428 -10.844 5.274   0.72 16.65 ?  153 LEU   A HD12 1 
ATOM   3371 H HD12 B LEU   A 1 153 ? 14.317 -10.498 4.951   0.28 17.33 ?  153 LEU   A HD12 1 
ATOM   3372 H HD13 A LEU   A 1 153 ? 14.781 -9.905  4.042   0.72 16.65 ?  153 LEU   A HD13 1 
ATOM   3373 H HD13 B LEU   A 1 153 ? 14.935 -9.467  3.913   0.28 17.33 ?  153 LEU   A HD13 1 
ATOM   3374 H HD21 A LEU   A 1 153 ? 17.590 -9.424  4.493   0.72 16.65 ?  153 LEU   A HD21 1 
ATOM   3375 H HD21 B LEU   A 1 153 ? 17.637 -9.383  4.730   0.28 16.95 ?  153 LEU   A HD21 1 
ATOM   3376 H HD22 A LEU   A 1 153 ? 16.577 -8.228  4.238   0.72 16.65 ?  153 LEU   A HD22 1 
ATOM   3377 H HD22 B LEU   A 1 153 ? 16.929 -7.961  4.736   0.28 16.95 ?  153 LEU   A HD22 1 
ATOM   3378 H HD23 A LEU   A 1 153 ? 17.511 -8.218  5.523   0.72 16.65 ?  153 LEU   A HD23 1 
ATOM   3379 H HD23 B LEU   A 1 153 ? 17.678 -8.481  6.037   0.28 16.95 ?  153 LEU   A HD23 1 
ATOM   3380 N N    A ALA   A 1 154 ? 14.934 -5.389  7.737   0.72 14.39 ?  154 ALA   A N    1 
ATOM   3381 N N    B ALA   A 1 154 ? 14.870 -5.299  7.781   0.28 14.13 ?  154 ALA   A N    1 
ATOM   3382 C CA   A ALA   A 1 154 ? 14.069 -4.239  7.948   0.72 15.19 ?  154 ALA   A CA   1 
ATOM   3383 C CA   B ALA   A 1 154 ? 14.015 -4.149  8.059   0.28 14.73 ?  154 ALA   A CA   1 
ATOM   3384 C C    A ALA   A 1 154 ? 13.570 -3.742  6.599   0.72 15.38 ?  154 ALA   A C    1 
ATOM   3385 C C    B ALA   A 1 154 ? 13.567 -3.572  6.720   0.28 15.10 ?  154 ALA   A C    1 
ATOM   3386 O O    A ALA   A 1 154 ? 14.373 -3.416  5.715   0.72 15.75 ?  154 ALA   A O    1 
ATOM   3387 O O    B ALA   A 1 154 ? 14.388 -3.049  5.959   0.28 15.02 ?  154 ALA   A O    1 
ATOM   3388 C CB   A ALA   A 1 154 ? 14.828 -3.121  8.660   0.72 15.71 ?  154 ALA   A CB   1 
ATOM   3389 C CB   B ALA   A 1 154 ? 14.779 -3.108  8.876   0.28 14.84 ?  154 ALA   A CB   1 
ATOM   3390 H H    A ALA   A 1 154 ? 15.732 -5.176  7.484   0.72 17.30 ?  154 ALA   A H    1 
ATOM   3391 H H    B ALA   A 1 154 ? 15.615 -5.080  7.406   0.28 17.00 ?  154 ALA   A H    1 
ATOM   3392 H HA   A ALA   A 1 154 ? 13.308 -4.498  8.487   0.72 18.27 ?  154 ALA   A HA   1 
ATOM   3393 H HA   B ALA   A 1 154 ? 13.235 -4.430  8.564   0.28 17.71 ?  154 ALA   A HA   1 
ATOM   3394 H HB1  A ALA   A 1 154 ? 14.232 -2.367  8.784   0.72 18.89 ?  154 ALA   A HB1  1 
ATOM   3395 H HB1  B ALA   A 1 154 ? 14.197 -2.354  9.054   0.28 17.84 ?  154 ALA   A HB1  1 
ATOM   3396 H HB2  A ALA   A 1 154 ? 15.138 -3.447  9.518   0.72 18.89 ?  154 ALA   A HB2  1 
ATOM   3397 H HB2  B ALA   A 1 154 ? 15.068 -3.507  9.714   0.28 17.84 ?  154 ALA   A HB2  1 
ATOM   3398 H HB3  A ALA   A 1 154 ? 15.586 -2.856  8.113   0.72 18.89 ?  154 ALA   A HB3  1 
ATOM   3399 H HB3  B ALA   A 1 154 ? 15.555 -2.815  8.369   0.28 17.84 ?  154 ALA   A HB3  1 
ATOM   3400 N N    A VAL   A 1 155 ? 12.252 -3.676  6.454   0.72 15.80 ?  155 VAL   A N    1 
ATOM   3401 N N    B VAL   A 1 155 ? 12.270 -3.672  6.434   0.28 15.66 ?  155 VAL   A N    1 
ATOM   3402 C CA   A VAL   A 1 155 ? 11.595 -3.190  5.249   0.72 16.55 ?  155 VAL   A CA   1 
ATOM   3403 C CA   B VAL   A 1 155 ? 11.689 -3.251  5.161   0.28 16.36 ?  155 VAL   A CA   1 
ATOM   3404 C C    A VAL   A 1 155 ? 10.861 -1.910  5.622   0.72 17.37 ?  155 VAL   A C    1 
ATOM   3405 C C    B VAL   A 1 155 ? 10.878 -1.986  5.414   0.28 17.37 ?  155 VAL   A C    1 
ATOM   3406 O O    A VAL   A 1 155 ? 9.930  -1.938  6.435   0.72 17.83 ?  155 VAL   A O    1 
ATOM   3407 O O    B VAL   A 1 155 ? 9.821  -2.031  6.055   0.28 17.28 ?  155 VAL   A O    1 
ATOM   3408 C CB   A VAL   A 1 155 ? 10.642 -4.247  4.668   0.72 16.48 ?  155 VAL   A CB   1 
ATOM   3409 C CB   B VAL   A 1 155 ? 10.822 -4.356  4.541   0.28 15.97 ?  155 VAL   A CB   1 
ATOM   3410 C CG1  A VAL   A 1 155 ? 9.912  -3.701  3.455   0.72 17.46 ?  155 VAL   A CG1  1 
ATOM   3411 C CG1  B VAL   A 1 155 ? 10.196 -3.879  3.237   0.28 15.88 ?  155 VAL   A CG1  1 
ATOM   3412 C CG2  A VAL   A 1 155 ? 11.423 -5.505  4.296   0.72 16.99 ?  155 VAL   A CG2  1 
ATOM   3413 C CG2  B VAL   A 1 155 ? 11.649 -5.612  4.304   0.28 16.25 ?  155 VAL   A CG2  1 
ATOM   3414 H H    A VAL   A 1 155 ? 11.698 -3.921  7.067   0.72 19.00 ?  155 VAL   A H    1 
ATOM   3415 H H    B VAL   A 1 155 ? 11.694 -3.993  6.982   0.28 18.82 ?  155 VAL   A H    1 
ATOM   3416 H HA   A VAL   A 1 155 ? 12.260 -2.977  4.582   0.72 19.90 ?  155 VAL   A HA   1 
ATOM   3417 H HA   B VAL   A 1 155 ? 12.402 -3.039  4.537   0.28 19.67 ?  155 VAL   A HA   1 
ATOM   3418 H HB   A VAL   A 1 155 ? 9.980  -4.486  5.339   0.72 19.81 ?  155 VAL   A HB   1 
ATOM   3419 H HB   B VAL   A 1 155 ? 10.107 -4.581  5.157   0.28 19.20 ?  155 VAL   A HB   1 
ATOM   3420 H HG11 A VAL   A 1 155 ? 9.442  -4.429  3.017   0.72 20.99 ?  155 VAL   A HG11 1 
ATOM   3421 H HG11 B VAL   A 1 155 ? 9.811  -4.641  2.775   0.28 19.09 ?  155 VAL   A HG11 1 
ATOM   3422 H HG12 A VAL   A 1 155 ? 9.275  -3.026  3.741   0.72 20.99 ?  155 VAL   A HG12 1 
ATOM   3423 H HG12 B VAL   A 1 155 ? 9.502  -3.230  3.436   0.28 19.09 ?  155 VAL   A HG12 1 
ATOM   3424 H HG13 A VAL   A 1 155 ? 10.557 -3.312  2.846   0.72 20.99 ?  155 VAL   A HG13 1 
ATOM   3425 H HG13 B VAL   A 1 155 ? 10.883 -3.473  2.687   0.28 19.09 ?  155 VAL   A HG13 1 
ATOM   3426 H HG21 A VAL   A 1 155 ? 10.821 -6.142  3.884   0.72 20.43 ?  155 VAL   A HG21 1 
ATOM   3427 H HG21 B VAL   A 1 155 ? 11.092 -6.280  3.875   0.28 19.54 ?  155 VAL   A HG21 1 
ATOM   3428 H HG22 A VAL   A 1 155 ? 12.128 -5.264  3.673   0.72 20.43 ?  155 VAL   A HG22 1 
ATOM   3429 H HG22 B VAL   A 1 155 ? 12.400 -5.391  3.732   0.28 19.54 ?  155 VAL   A HG22 1 
ATOM   3430 H HG23 A VAL   A 1 155 ? 11.811 -5.887  5.099   0.72 20.43 ?  155 VAL   A HG23 1 
ATOM   3431 H HG23 B VAL   A 1 155 ? 11.969 -5.946  5.156   0.28 19.54 ?  155 VAL   A HG23 1 
ATOM   3432 N N    A PHE   A 1 156 ? 11.295 -0.787  5.043   0.72 18.27 ?  156 PHE   A N    1 
ATOM   3433 N N    B PHE   A 1 156 ? 11.359 -0.861  4.891   0.28 19.02 ?  156 PHE   A N    1 
ATOM   3434 C CA   A PHE   A 1 156 ? 10.753 0.519   5.418   0.72 19.90 ?  156 PHE   A CA   1 
ATOM   3435 C CA   B PHE   A 1 156 ? 10.792 0.465   5.155   0.28 20.71 ?  156 PHE   A CA   1 
ATOM   3436 C C    A PHE   A 1 156 ? 9.293  0.664   5.010   0.72 20.16 ?  156 PHE   A C    1 
ATOM   3437 C C    B PHE   A 1 156 ? 9.669  0.818   4.181   0.28 21.39 ?  156 PHE   A C    1 
ATOM   3438 O O    A PHE   A 1 156 ? 8.478  1.199   5.771   0.72 20.56 ?  156 PHE   A O    1 
ATOM   3439 O O    B PHE   A 1 156 ? 9.643  1.902   3.598   0.28 22.24 ?  156 PHE   A O    1 
ATOM   3440 C CB   A PHE   A 1 156 ? 11.592 1.616   4.758   0.72 20.82 ?  156 PHE   A CB   1 
ATOM   3441 C CB   B PHE   A 1 156 ? 11.913 1.499   5.108   0.28 21.49 ?  156 PHE   A CB   1 
ATOM   3442 C CG   A PHE   A 1 156 ? 11.114 3.012   5.053   0.72 22.34 ?  156 PHE   A CG   1 
ATOM   3443 C CG   B PHE   A 1 156 ? 11.530 2.862   5.618   0.28 22.25 ?  156 PHE   A CG   1 
ATOM   3444 C CD1  A PHE   A 1 156 ? 11.086 3.477   6.357   0.72 23.59 ?  156 PHE   A CD1  1 
ATOM   3445 C CD1  B PHE   A 1 156 ? 10.718 3.010   6.730   0.28 22.53 ?  156 PHE   A CD1  1 
ATOM   3446 C CD2  A PHE   A 1 156 ? 10.709 3.860   4.032   0.72 22.97 ?  156 PHE   A CD2  1 
ATOM   3447 C CD2  B PHE   A 1 156 ? 12.022 4.001   5.000   0.28 22.61 ?  156 PHE   A CD2  1 
ATOM   3448 C CE1  A PHE   A 1 156 ? 10.655 4.756   6.640   0.72 24.53 ?  156 PHE   A CE1  1 
ATOM   3449 C CE1  B PHE   A 1 156 ? 10.382 4.268   7.198   0.28 22.80 ?  156 PHE   A CE1  1 
ATOM   3450 C CE2  A PHE   A 1 156 ? 10.276 5.146   4.308   0.72 23.93 ?  156 PHE   A CE2  1 
ATOM   3451 C CE2  B PHE   A 1 156 ? 11.692 5.261   5.464   0.28 22.77 ?  156 PHE   A CE2  1 
ATOM   3452 C CZ   A PHE   A 1 156 ? 10.254 5.595   5.614   0.72 24.53 ?  156 PHE   A CZ   1 
ATOM   3453 C CZ   B PHE   A 1 156 ? 10.872 5.395   6.564   0.28 22.92 ?  156 PHE   A CZ   1 
ATOM   3454 H H    A PHE   A 1 156 ? 11.906 -0.757  4.435   0.72 21.97 ?  156 PHE   A H    1 
ATOM   3455 H H    B PHE   A 1 156 ? 12.038 -0.840  4.370   0.28 22.87 ?  156 PHE   A H    1 
ATOM   3456 H HA   A PHE   A 1 156 ? 10.821 0.631   6.380   0.72 23.92 ?  156 PHE   A HA   1 
ATOM   3457 H HA   B PHE   A 1 156 ? 10.420 0.464   6.048   0.28 24.89 ?  156 PHE   A HA   1 
ATOM   3458 H HB2  A PHE   A 1 156 ? 12.510 1.543   5.072   0.72 25.03 ?  156 PHE   A HB2  1 
ATOM   3459 H HB2  B PHE   A 1 156 ? 12.641 1.184   5.659   0.28 25.82 ?  156 PHE   A HB2  1 
ATOM   3460 H HB3  A PHE   A 1 156 ? 11.568 1.491   3.796   0.72 25.03 ?  156 PHE   A HB3  1 
ATOM   3461 H HB3  B PHE   A 1 156 ? 12.215 1.605   4.192   0.28 25.82 ?  156 PHE   A HB3  1 
ATOM   3462 H HD1  A PHE   A 1 156 ? 11.361 2.916   7.050   0.72 28.34 ?  156 PHE   A HD1  1 
ATOM   3463 H HD1  B PHE   A 1 156 ? 10.386 2.254   7.158   0.28 27.08 ?  156 PHE   A HD1  1 
ATOM   3464 H HD2  A PHE   A 1 156 ? 10.727 3.554   3.153   0.72 27.61 ?  156 PHE   A HD2  1 
ATOM   3465 H HD2  B PHE   A 1 156 ? 12.575 3.917   4.256   0.28 27.17 ?  156 PHE   A HD2  1 
ATOM   3466 H HE1  A PHE   A 1 156 ? 10.641 5.056   7.521   0.72 29.47 ?  156 PHE   A HE1  1 
ATOM   3467 H HE1  B PHE   A 1 156 ? 9.831  4.356   7.941   0.28 27.40 ?  156 PHE   A HE1  1 
ATOM   3468 H HE2  A PHE   A 1 156 ? 10.005 5.700   3.617   0.72 28.76 ?  156 PHE   A HE2  1 
ATOM   3469 H HE2  B PHE   A 1 156 ? 12.023 6.017   5.035   0.28 27.36 ?  156 PHE   A HE2  1 
ATOM   3470 H HZ   A PHE   A 1 156 ? 9.960  6.454   5.806   0.72 29.47 ?  156 PHE   A HZ   1 
ATOM   3471 H HZ   B PHE   A 1 156 ? 10.649 6.241   6.878   0.28 27.54 ?  156 PHE   A HZ   1 
ATOM   3472 N N    A ASP   A 1 157 ? 8.958  0.240   3.799   0.72 20.35 ?  157 ASP   A N    1 
ATOM   3473 N N    B ASP   A 1 157 ? 8.722  -0.101  4.001   0.28 21.07 ?  157 ASP   A N    1 
ATOM   3474 C CA   A ASP   A 1 157 ? 7.638  0.485   3.234   0.72 21.83 ?  157 ASP   A CA   1 
ATOM   3475 C CA   B ASP   A 1 157 ? 7.554  0.159   3.161   0.28 20.54 ?  157 ASP   A CA   1 
ATOM   3476 C C    A ASP   A 1 157 ? 6.657  -0.568  3.742   0.72 21.86 ?  157 ASP   A C    1 
ATOM   3477 C C    B ASP   A 1 157 ? 6.464  -0.828  3.543   0.28 20.31 ?  157 ASP   A C    1 
ATOM   3478 O O    A ASP   A 1 157 ? 6.832  -1.765  3.480   0.72 21.67 ?  157 ASP   A O    1 
ATOM   3479 O O    B ASP   A 1 157 ? 6.633  -2.040  3.369   0.28 20.24 ?  157 ASP   A O    1 
ATOM   3480 C CB   A ASP   A 1 157 ? 7.745  0.419   1.715   0.72 23.41 ?  157 ASP   A CB   1 
ATOM   3481 C CB   B ASP   A 1 157 ? 7.904  0.038   1.678   0.28 20.17 ?  157 ASP   A CB   1 
ATOM   3482 C CG   A ASP   A 1 157 ? 6.507  0.928   1.024   0.72 25.47 ?  157 ASP   A CG   1 
ATOM   3483 C CG   B ASP   A 1 157 ? 6.815  0.598   0.778   0.28 19.98 ?  157 ASP   A CG   1 
ATOM   3484 O OD1  A ASP   A 1 157 ? 6.320  2.156   0.989   0.72 27.06 ?  157 ASP   A OD1  1 
ATOM   3485 O OD1  B ASP   A 1 157 ? 5.720  0.003   0.736   0.28 20.49 ?  157 ASP   A OD1  1 
ATOM   3486 O OD2  A ASP   A 1 157 ? 5.717  0.101   0.524   0.72 26.21 -1 157 ASP   A OD2  1 
ATOM   3487 O OD2  B ASP   A 1 157 ? 7.041  1.648   0.135   0.28 19.21 -1 157 ASP   A OD2  1 
ATOM   3488 H H    A ASP   A 1 157 ? 9.494  -0.182  3.274   0.72 24.46 ?  157 ASP   A H    1 
ATOM   3489 H H    B ASP   A 1 157 ? 8.729  -0.885  4.356   0.28 25.32 ?  157 ASP   A H    1 
ATOM   3490 H HA   A ASP   A 1 157 ? 7.328  1.371   3.494   0.72 26.23 ?  157 ASP   A HA   1 
ATOM   3491 H HA   B ASP   A 1 157 ? 7.226  1.056   3.327   0.28 24.69 ?  157 ASP   A HA   1 
ATOM   3492 H HB2  A ASP   A 1 157 ? 8.517  0.941   1.431   0.72 28.13 ?  157 ASP   A HB2  1 
ATOM   3493 H HB2  B ASP   A 1 157 ? 8.715  0.535   1.503   0.28 24.24 ?  157 ASP   A HB2  1 
ATOM   3494 H HB3  A ASP   A 1 157 ? 7.858  -0.502  1.452   0.72 28.13 ?  157 ASP   A HB3  1 
ATOM   3495 H HB3  B ASP   A 1 157 ? 8.036  -0.902  1.462   0.28 24.24 ?  157 ASP   A HB3  1 
ATOM   3496 N N    A LYS   A 1 158 ? 5.626  -0.127  4.471   0.72 23.26 ?  158 LYS   A N    1 
ATOM   3497 N N    B LYS   A 1 158 ? 5.346  -0.304  4.048   0.28 20.44 ?  158 LYS   A N    1 
ATOM   3498 C CA   A LYS   A 1 158 ? 4.663  -1.076  5.024   0.72 24.32 ?  158 LYS   A CA   1 
ATOM   3499 C CA   B LYS   A 1 158 ? 4.294  -1.145  4.612   0.28 20.69 ?  158 LYS   A CA   1 
ATOM   3500 C C    A LYS   A 1 158 ? 3.929  -1.816  3.915   0.72 23.88 ?  158 LYS   A C    1 
ATOM   3501 C C    B LYS   A 1 158 ? 3.726  -2.101  3.569   0.28 20.37 ?  158 LYS   A C    1 
ATOM   3502 O O    A LYS   A 1 158 ? 3.707  -3.030  4.007   0.72 24.08 ?  158 LYS   A O    1 
ATOM   3503 O O    B LYS   A 1 158 ? 3.671  -3.318  3.784   0.28 20.15 ?  158 LYS   A O    1 
ATOM   3504 C CB   A LYS   A 1 158 ? 3.676  -0.355  5.945   0.72 25.62 ?  158 LYS   A CB   1 
ATOM   3505 C CB   B LYS   A 1 158 ? 3.196  -0.243  5.179   0.28 21.48 ?  158 LYS   A CB   1 
ATOM   3506 C CG   A LYS   A 1 158 ? 2.449  -1.180  6.351   0.72 27.17 ?  158 LYS   A CG   1 
ATOM   3507 C CG   B LYS   A 1 158 ? 1.905  -0.951  5.513   0.28 22.40 ?  158 LYS   A CG   1 
ATOM   3508 C CD   A LYS   A 1 158 ? 2.813  -2.446  7.131   0.72 28.03 ?  158 LYS   A CD   1 
ATOM   3509 C CD   B LYS   A 1 158 ? 0.840  0.037   5.967   0.28 23.15 ?  158 LYS   A CD   1 
ATOM   3510 C CE   A LYS   A 1 158 ? 1.555  -3.142  7.659   0.72 28.50 ?  158 LYS   A CE   1 
ATOM   3511 C CE   B LYS   A 1 158 ? -0.193 -0.656  6.819   0.28 23.82 ?  158 LYS   A CE   1 
ATOM   3512 N NZ   A LYS   A 1 158 ? 1.817  -4.504  8.216   0.72 28.74 ?  158 LYS   A NZ   1 
ATOM   3513 N NZ   B LYS   A 1 158 ? 0.502  -1.430  7.873   0.28 24.26 ?  158 LYS   A NZ   1 
ATOM   3514 H H    A LYS   A 1 158 ? 5.470  0.698   4.655   0.72 27.95 ?  158 LYS   A H    1 
ATOM   3515 H H    B LYS   A 1 158 ? 5.171  0.535   4.074   0.28 24.57 ?  158 LYS   A H    1 
ATOM   3516 H HA   A LYS   A 1 158 ? 5.139  -1.731  5.558   0.72 29.23 ?  158 LYS   A HA   1 
ATOM   3517 H HA   B LYS   A 1 158 ? 4.654  -1.672  5.342   0.28 24.86 ?  158 LYS   A HA   1 
ATOM   3518 H HB2  A LYS   A 1 158 ? 4.139  -0.101  6.761   0.72 30.78 ?  158 LYS   A HB2  1 
ATOM   3519 H HB2  B LYS   A 1 158 ? 3.522  0.169   6.000   0.28 25.81 ?  158 LYS   A HB2  1 
ATOM   3520 H HB3  A LYS   A 1 158 ? 3.357  0.443   5.494   0.72 30.78 ?  158 LYS   A HB3  1 
ATOM   3521 H HB3  B LYS   A 1 158 ? 2.990  0.448   4.533   0.28 25.81 ?  158 LYS   A HB3  1 
ATOM   3522 H HG2  A LYS   A 1 158 ? 1.884  -0.636  6.919   0.72 32.65 ?  158 LYS   A HG2  1 
ATOM   3523 H HG2  B LYS   A 1 158 ? 1.555  -1.395  4.730   0.28 26.92 ?  158 LYS   A HG2  1 
ATOM   3524 H HG3  A LYS   A 1 158 ? 1.955  -1.443  5.557   0.72 32.65 ?  158 LYS   A HG3  1 
ATOM   3525 H HG3  B LYS   A 1 158 ? 2.079  -1.602  6.211   0.28 26.92 ?  158 LYS   A HG3  1 
ATOM   3526 H HD2  A LYS   A 1 158 ? 3.281  -3.062  6.546   0.72 33.67 ?  158 LYS   A HD2  1 
ATOM   3527 H HD2  B LYS   A 1 158 ? 1.249  0.742   6.493   0.28 27.82 ?  158 LYS   A HD2  1 
ATOM   3528 H HD3  A LYS   A 1 158 ? 3.372  -2.206  7.887   0.72 33.67 ?  158 LYS   A HD3  1 
ATOM   3529 H HD3  B LYS   A 1 158 ? 0.394  0.413   5.188   0.28 27.82 ?  158 LYS   A HD3  1 
ATOM   3530 H HE2  A LYS   A 1 158 ? 1.167  -2.601  8.365   0.72 34.24 ?  158 LYS   A HE2  1 
ATOM   3531 H HE2  B LYS   A 1 158 ? -0.770 0.002   7.242   0.28 28.62 ?  158 LYS   A HE2  1 
ATOM   3532 H HE3  A LYS   A 1 158 ? 0.922  -3.236  6.933   0.72 34.24 ?  158 LYS   A HE3  1 
ATOM   3533 H HE3  B LYS   A 1 158 ? -0.715 -1.266  6.273   0.28 28.62 ?  158 LYS   A HE3  1 
ATOM   3534 H HZ1  A LYS   A 1 158 ? 1.057  -4.864  8.509   0.72 34.53 ?  158 LYS   A HZ1  1 
ATOM   3535 H HZ1  B LYS   A 1 158 ? 0.048  -1.382  8.620   0.28 29.15 ?  158 LYS   A HZ1  1 
ATOM   3536 H HZ2  A LYS   A 1 158 ? 2.161  -5.030  7.584   0.72 34.53 ?  158 LYS   A HZ2  1 
ATOM   3537 H HZ2  B LYS   A 1 158 ? 0.582  -2.283  7.629   0.28 29.15 ?  158 LYS   A HZ2  1 
ATOM   3538 H HZ3  A LYS   A 1 158 ? 2.392  -4.452  8.893   0.72 34.53 ?  158 LYS   A HZ3  1 
ATOM   3539 H HZ3  B LYS   A 1 158 ? 1.315  -1.090  8.015   0.28 29.15 ?  158 LYS   A HZ3  1 
ATOM   3540 N N    A ASN   A 1 159 ? 3.539  -1.105  2.857   0.72 23.83 ?  159 ASN   A N    1 
ATOM   3541 N N    B ASN   A 1 159 ? 3.280  -1.564  2.434   0.28 20.77 ?  159 ASN   A N    1 
ATOM   3542 C CA   A ASN   A 1 159 ? 2.883  -1.785  1.748   0.72 23.87 ?  159 ASN   A CA   1 
ATOM   3543 C CA   B ASN   A 1 159 ? 2.600  -2.398  1.451   0.28 21.16 ?  159 ASN   A CA   1 
ATOM   3544 C C    A ASN   A 1 159 ? 3.786  -2.862  1.158   0.72 22.45 ?  159 ASN   A C    1 
ATOM   3545 C C    B ASN   A 1 159 ? 3.553  -3.401  0.806   0.28 19.34 ?  159 ASN   A C    1 
ATOM   3546 O O    A ASN   A 1 159 ? 3.336  -3.981  0.884   0.72 21.46 ?  159 ASN   A O    1 
ATOM   3547 O O    B ASN   A 1 159 ? 3.135  -4.506  0.439   0.28 19.18 ?  159 ASN   A O    1 
ATOM   3548 C CB   A ASN   A 1 159 ? 2.430  -0.773  0.693   0.72 26.12 ?  159 ASN   A CB   1 
ATOM   3549 C CB   B ASN   A 1 159 ? 1.906  -1.508  0.422   0.28 23.58 ?  159 ASN   A CB   1 
ATOM   3550 C CG   A ASN   A 1 159 ? 1.146  -0.056  1.087   0.72 29.47 ?  159 ASN   A CG   1 
ATOM   3551 C CG   B ASN   A 1 159 ? 1.111  -0.377  1.069   0.28 25.95 ?  159 ASN   A CG   1 
ATOM   3552 O OD1  A ASN   A 1 159 ? 0.277  -0.636  1.738   0.72 31.07 ?  159 ASN   A OD1  1 
ATOM   3553 O OD1  B ASN   A 1 159 ? 1.204  0.774   0.648   0.28 27.06 ?  159 ASN   A OD1  1 
ATOM   3554 N ND2  A ASN   A 1 159 ? 1.018  1.205   0.689   0.72 30.84 ?  159 ASN   A ND2  1 
ATOM   3555 N ND2  B ASN   A 1 159 ? 0.329  -0.703  2.096   0.28 26.57 ?  159 ASN   A ND2  1 
ATOM   3556 H H    A ASN   A 1 159 ? 3.642  -0.253  2.765   0.72 28.64 ?  159 ASN   A H    1 
ATOM   3557 H H    B ASN   A 1 159 ? 3.358  -0.732  2.219   0.28 24.97 ?  159 ASN   A H    1 
ATOM   3558 H HA   A ASN   A 1 159 ? 2.093  -2.225  2.087   0.72 28.68 ?  159 ASN   A HA   1 
ATOM   3559 H HA   B ASN   A 1 159 ? 1.907  -2.898  1.898   0.28 25.43 ?  159 ASN   A HA   1 
ATOM   3560 H HB2  A ASN   A 1 159 ? 3.116  -0.100  0.574   0.72 31.38 ?  159 ASN   A HB2  1 
ATOM   3561 H HB2  B ASN   A 1 159 ? 2.574  -1.101  -0.153  0.28 28.34 ?  159 ASN   A HB2  1 
ATOM   3562 H HB3  A ASN   A 1 159 ? 2.266  -1.237  -0.141  0.72 31.38 ?  159 ASN   A HB3  1 
ATOM   3563 H HB3  B ASN   A 1 159 ? 1.287  -2.035  -0.107  0.28 28.34 ?  159 ASN   A HB3  1 
ATOM   3564 H HD21 A ASN   A 1 159 ? 0.310  1.647   0.890   0.72 37.04 ?  159 ASN   A HD21 1 
ATOM   3565 H HD21 B ASN   A 1 159 ? -0.143 -0.099  2.495   0.28 31.92 ?  159 ASN   A HD21 1 
ATOM   3566 H HD22 A ASN   A 1 159 ? 1.647  1.575   0.239   0.72 37.04 ?  159 ASN   A HD22 1 
ATOM   3567 H HD22 B ASN   A 1 159 ? 0.292  -1.517  2.362   0.28 31.92 ?  159 ASN   A HD22 1 
ATOM   3568 N N    A LEU   A 1 160 ? 5.074  -2.565  0.997   0.72 21.39 ?  160 LEU   A N    1 
ATOM   3569 N N    B LEU   A 1 160 ? 4.836  -3.052  0.690   0.28 18.13 ?  160 LEU   A N    1 
ATOM   3570 C CA   A LEU   A 1 160 ? 5.977  -3.582  0.469   0.72 20.57 ?  160 LEU   A CA   1 
ATOM   3571 C CA   B LEU   A 1 160 ? 5.814  -4.002  0.171   0.28 17.70 ?  160 LEU   A CA   1 
ATOM   3572 C C    A LEU   A 1 160 ? 6.141  -4.735  1.448   0.72 20.10 ?  160 LEU   A C    1 
ATOM   3573 C C    B LEU   A 1 160 ? 6.054  -5.128  1.171   0.28 17.29 ?  160 LEU   A C    1 
ATOM   3574 O O    A LEU   A 1 160 ? 6.186  -5.902  1.041   0.72 20.81 ?  160 LEU   A O    1 
ATOM   3575 O O    B LEU   A 1 160 ? 6.066  -6.310  0.804   0.28 17.31 ?  160 LEU   A O    1 
ATOM   3576 C CB   A LEU   A 1 160 ? 7.331  -2.970  0.124   0.72 20.23 ?  160 LEU   A CB   1 
ATOM   3577 C CB   B LEU   A 1 160 ? 7.123  -3.272  -0.131  0.28 18.07 ?  160 LEU   A CB   1 
ATOM   3578 C CG   A LEU   A 1 160 ? 8.378  -4.000  -0.303  0.72 20.15 ?  160 LEU   A CG   1 
ATOM   3579 C CG   B LEU   A 1 160 ? 7.940  -3.687  -1.357  0.28 19.11 ?  160 LEU   A CG   1 
ATOM   3580 C CD1  A LEU   A 1 160 ? 7.941  -4.723  -1.556  0.72 21.05 ?  160 LEU   A CD1  1 
ATOM   3581 C CD1  B LEU   A 1 160 ? 9.423  -3.480  -1.076  0.28 19.12 ?  160 LEU   A CD1  1 
ATOM   3582 C CD2  A LEU   A 1 160 ? 9.718  -3.326  -0.518  0.72 19.96 ?  160 LEU   A CD2  1 
ATOM   3583 C CD2  B LEU   A 1 160 ? 7.657  -5.116  -1.784  0.28 19.57 ?  160 LEU   A CD2  1 
ATOM   3584 H H    A LEU   A 1 160 ? 5.443  -1.802  1.194   0.72 25.70 ?  160 LEU   A H    1 
ATOM   3585 H H    B LEU   A 1 160 ? 5.162  -2.287  0.911   0.28 21.80 ?  160 LEU   A H    1 
ATOM   3586 H HA   A LEU   A 1 160 ? 5.596  -3.926  -0.348  0.72 24.73 ?  160 LEU   A HA   1 
ATOM   3587 H HA   B LEU   A 1 160 ? 5.469  -4.384  -0.650  0.28 21.28 ?  160 LEU   A HA   1 
ATOM   3588 H HB2  A LEU   A 1 160 ? 7.223  -2.329  -0.605  0.72 24.32 ?  160 LEU   A HB2  1 
ATOM   3589 H HB2  B LEU   A 1 160 ? 6.918  -2.330  -0.243  0.28 21.72 ?  160 LEU   A HB2  1 
ATOM   3590 H HB3  A LEU   A 1 160 ? 7.678  -2.514  0.906   0.72 24.32 ?  160 LEU   A HB3  1 
ATOM   3591 H HB3  B LEU   A 1 160 ? 7.703  -3.376  0.639   0.28 21.72 ?  160 LEU   A HB3  1 
ATOM   3592 H HG   A LEU   A 1 160 ? 8.494  -4.654  0.401   0.72 24.22 ?  160 LEU   A HG   1 
ATOM   3593 H HG   B LEU   A 1 160 ? 7.703  -3.105  -2.095  0.28 22.97 ?  160 LEU   A HG   1 
ATOM   3594 H HD11 A LEU   A 1 160 ? 8.661  -5.294  -1.857  0.72 25.30 ?  160 LEU   A HD11 1 
ATOM   3595 H HD11 B LEU   A 1 160 ? 9.925  -3.629  -1.892  0.28 22.99 ?  160 LEU   A HD11 1 
ATOM   3596 H HD12 A LEU   A 1 160 ? 7.156  -5.259  -1.354  0.72 25.30 ?  160 LEU   A HD12 1 
ATOM   3597 H HD12 B LEU   A 1 160 ? 9.563  -2.572  -0.764  0.28 22.99 ?  160 LEU   A HD12 1 
ATOM   3598 H HD13 A LEU   A 1 160 ? 7.726  -4.069  -2.240  0.72 25.30 ?  160 LEU   A HD13 1 
ATOM   3599 H HD13 B LEU   A 1 160 ? 9.706  -4.110  -0.394  0.28 22.99 ?  160 LEU   A HD13 1 
ATOM   3600 H HD21 A LEU   A 1 160 ? 10.368 -3.996  -0.785  0.72 23.99 ?  160 LEU   A HD21 1 
ATOM   3601 H HD21 B LEU   A 1 160 ? 8.393  -5.440  -2.322  0.28 23.52 ?  160 LEU   A HD21 1 
ATOM   3602 H HD22 A LEU   A 1 160 ? 9.628  -2.658  -1.216  0.72 23.99 ?  160 LEU   A HD22 1 
ATOM   3603 H HD22 B LEU   A 1 160 ? 7.562  -5.661  -0.993  0.28 23.52 ?  160 LEU   A HD22 1 
ATOM   3604 H HD23 A LEU   A 1 160 ? 9.998  -2.905  0.309   0.72 23.99 ?  160 LEU   A HD23 1 
ATOM   3605 H HD23 B LEU   A 1 160 ? 6.834  -5.135  -2.298  0.28 23.52 ?  160 LEU   A HD23 1 
ATOM   3606 N N    A TYR   A 1 161 ? 6.245  -4.429  2.741   0.72 19.45 ?  161 TYR   A N    1 
ATOM   3607 N N    B TYR   A 1 161 ? 6.255  -4.773  2.442   0.28 17.20 ?  161 TYR   A N    1 
ATOM   3608 C CA   A TYR   A 1 161 ? 6.385  -5.481  3.740   0.72 19.20 ?  161 TYR   A CA   1 
ATOM   3609 C CA   B TYR   A 1 161 ? 6.378  -5.773  3.498   0.28 17.38 ?  161 TYR   A CA   1 
ATOM   3610 C C    A TYR   A 1 161 ? 5.258  -6.508  3.635   0.72 19.99 ?  161 TYR   A C    1 
ATOM   3611 C C    B TYR   A 1 161 ? 5.174  -6.705  3.492   0.28 18.10 ?  161 TYR   A C    1 
ATOM   3612 O O    A TYR   A 1 161 ? 5.499  -7.721  3.672   0.72 19.55 ?  161 TYR   A O    1 
ATOM   3613 O O    B TYR   A 1 161 ? 5.314  -7.929  3.391   0.28 17.52 ?  161 TYR   A O    1 
ATOM   3614 C CB   A TYR   A 1 161 ? 6.444  -4.872  5.142   0.72 19.69 ?  161 TYR   A CB   1 
ATOM   3615 C CB   B TYR   A 1 161 ? 6.505  -5.072  4.853   0.28 17.20 ?  161 TYR   A CB   1 
ATOM   3616 C CG   A TYR   A 1 161 ? 6.354  -5.922  6.213   0.72 19.40 ?  161 TYR   A CG   1 
ATOM   3617 C CG   B TYR   A 1 161 ? 6.349  -5.992  6.047   0.28 17.09 ?  161 TYR   A CG   1 
ATOM   3618 C CD1  A TYR   A 1 161 ? 7.484  -6.610  6.634   0.72 18.96 ?  161 TYR   A CD1  1 
ATOM   3619 C CD1  B TYR   A 1 161 ? 7.438  -6.677  6.568   0.28 17.23 ?  161 TYR   A CD1  1 
ATOM   3620 C CD2  A TYR   A 1 161 ? 5.131  -6.248  6.788   0.72 19.45 ?  161 TYR   A CD2  1 
ATOM   3621 C CD2  B TYR   A 1 161 ? 5.114  -6.156  6.671   0.28 17.12 ?  161 TYR   A CD2  1 
ATOM   3622 C CE1  A TYR   A 1 161 ? 7.400  -7.589  7.598   0.72 18.85 ?  161 TYR   A CE1  1 
ATOM   3623 C CE1  B TYR   A 1 161 ? 7.303  -7.513  7.660   0.28 17.42 ?  161 TYR   A CE1  1 
ATOM   3624 C CE2  A TYR   A 1 161 ? 5.036  -7.226  7.755   0.72 19.22 ?  161 TYR   A CE2  1 
ATOM   3625 C CE2  B TYR   A 1 161 ? 4.970  -6.993  7.768   0.28 17.30 ?  161 TYR   A CE2  1 
ATOM   3626 C CZ   A TYR   A 1 161 ? 6.175  -7.893  8.157   0.72 19.21 ?  161 TYR   A CZ   1 
ATOM   3627 C CZ   B TYR   A 1 161 ? 6.068  -7.667  8.257   0.28 17.81 ?  161 TYR   A CZ   1 
ATOM   3628 O OH   A TYR   A 1 161 ? 6.097  -8.867  9.122   0.72 19.43 ?  161 TYR   A OH   1 
ATOM   3629 O OH   B TYR   A 1 161 ? 5.939  -8.499  9.346   0.28 18.74 ?  161 TYR   A OH   1 
ATOM   3630 H H    A TYR   A 1 161 ? 6.236  -3.627  3.060   0.72 23.38 ?  161 TYR   A H    1 
ATOM   3631 H H    B TYR   A 1 161 ? 6.315  -3.964  2.717   0.28 20.68 ?  161 TYR   A H    1 
ATOM   3632 H HA   A TYR   A 1 161 ? 7.214  -5.945  3.587   0.72 23.08 ?  161 TYR   A HA   1 
ATOM   3633 H HA   B TYR   A 1 161 ? 7.176  -6.304  3.352   0.28 20.90 ?  161 TYR   A HA   1 
ATOM   3634 H HB2  A TYR   A 1 161 ? 7.285  -4.400  5.250   0.72 23.67 ?  161 TYR   A HB2  1 
ATOM   3635 H HB2  B TYR   A 1 161 ? 7.382  -4.662  4.911   0.28 20.68 ?  161 TYR   A HB2  1 
ATOM   3636 H HB3  A TYR   A 1 161 ? 5.701  -4.255  5.260   0.72 23.67 ?  161 TYR   A HB3  1 
ATOM   3637 H HB3  B TYR   A 1 161 ? 5.820  -4.388  4.916   0.28 20.68 ?  161 TYR   A HB3  1 
ATOM   3638 H HD1  A TYR   A 1 161 ? 8.310  -6.409  6.258   0.72 22.79 ?  161 TYR   A HD1  1 
ATOM   3639 H HD1  B TYR   A 1 161 ? 8.271  -6.578  6.171   0.28 20.71 ?  161 TYR   A HD1  1 
ATOM   3640 H HD2  A TYR   A 1 161 ? 4.360  -5.803  6.517   0.72 23.38 ?  161 TYR   A HD2  1 
ATOM   3641 H HD2  B TYR   A 1 161 ? 4.369  -5.704  6.348   0.28 20.58 ?  161 TYR   A HD2  1 
ATOM   3642 H HE1  A TYR   A 1 161 ? 8.162  -8.044  7.877   0.72 22.66 ?  161 TYR   A HE1  1 
ATOM   3643 H HE1  B TYR   A 1 161 ? 8.040  -7.969  7.995   0.28 20.94 ?  161 TYR   A HE1  1 
ATOM   3644 H HE2  A TYR   A 1 161 ? 4.206  -7.434  8.133   0.72 23.11 ?  161 TYR   A HE2  1 
ATOM   3645 H HE2  B TYR   A 1 161 ? 4.137  -7.098  8.176   0.28 20.80 ?  161 TYR   A HE2  1 
ATOM   3646 H HH   A TYR   A 1 161 ? 6.845  -9.199  9.271   0.72 23.35 ?  161 TYR   A HH   1 
ATOM   3647 H HH   B TYR   A 1 161 ? 5.142  -8.503  9.620   0.28 22.53 ?  161 TYR   A HH   1 
ATOM   3648 N N    A ASP   A 1 162 ? 4.012  -6.039  3.500   0.72 20.88 ?  162 ASP   A N    1 
ATOM   3649 N N    B ASP   A 1 162 ? 3.973  -6.128  3.609   0.28 19.53 ?  162 ASP   A N    1 
ATOM   3650 C CA   A ASP   A 1 162 ? 2.880  -6.966  3.457   0.72 21.86 ?  162 ASP   A CA   1 
ATOM   3651 C CA   B ASP   A 1 162 ? 2.752  -6.918  3.487   0.28 20.84 ?  162 ASP   A CA   1 
ATOM   3652 C C    A ASP   A 1 162 ? 2.925  -7.836  2.206   0.72 21.66 ?  162 ASP   A C    1 
ATOM   3653 C C    B ASP   A 1 162 ? 2.786  -7.774  2.230   0.28 21.34 ?  162 ASP   A C    1 
ATOM   3654 O O    A ASP   A 1 162 ? 2.577  -9.023  2.253   0.72 22.51 ?  162 ASP   A O    1 
ATOM   3655 O O    B ASP   A 1 162 ? 2.437  -8.960  2.263   0.28 21.56 ?  162 ASP   A O    1 
ATOM   3656 C CB   A ASP   A 1 162 ? 1.553  -6.202  3.526   0.72 22.89 ?  162 ASP   A CB   1 
ATOM   3657 C CB   B ASP   A 1 162 ? 1.531  -5.992  3.454   0.28 21.73 ?  162 ASP   A CB   1 
ATOM   3658 C CG   A ASP   A 1 162 ? 1.253  -5.652  4.905   0.72 24.17 ?  162 ASP   A CG   1 
ATOM   3659 C CG   B ASP   A 1 162 ? 1.290  -5.284  4.773   0.28 22.55 ?  162 ASP   A CG   1 
ATOM   3660 O OD1  A ASP   A 1 162 ? 1.912  -6.058  5.882   0.72 25.27 ?  162 ASP   A OD1  1 
ATOM   3661 O OD1  B ASP   A 1 162 ? 1.780  -5.763  5.815   0.28 22.96 ?  162 ASP   A OD1  1 
ATOM   3662 O OD2  A ASP   A 1 162 ? 0.325  -4.818  5.009   0.72 24.80 -1 162 ASP   A OD2  1 
ATOM   3663 O OD2  B ASP   A 1 162 ? 0.594  -4.245  4.766   0.28 22.88 -1 162 ASP   A OD2  1 
ATOM   3664 H H    A ASP   A 1 162 ? 3.795  -5.204  3.432   0.72 25.09 ?  162 ASP   A H    1 
ATOM   3665 H H    B ASP   A 1 162 ? 3.844  -5.291  3.757   0.28 23.48 ?  162 ASP   A H    1 
ATOM   3666 H HA   A ASP   A 1 162 ? 2.923  -7.551  4.227   0.72 26.27 ?  162 ASP   A HA   1 
ATOM   3667 H HA   B ASP   A 1 162 ? 2.669  -7.501  4.257   0.28 25.04 ?  162 ASP   A HA   1 
ATOM   3668 H HB2  A ASP   A 1 162 ? 1.575  -5.462  2.903   0.72 27.50 ?  162 ASP   A HB2  1 
ATOM   3669 H HB2  B ASP   A 1 162 ? 1.668  -5.306  2.784   0.28 26.11 ?  162 ASP   A HB2  1 
ATOM   3670 H HB3  A ASP   A 1 162 ? 0.826  -6.803  3.310   0.72 27.50 ?  162 ASP   A HB3  1 
ATOM   3671 H HB3  B ASP   A 1 162 ? 0.743  -6.515  3.237   0.28 26.11 ?  162 ASP   A HB3  1 
ATOM   3672 N N    A LYS   A 1 163 ? 3.356  -7.267  1.079   0.72 22.58 ?  163 LYS   A N    1 
ATOM   3673 N N    B LYS   A 1 163 ? 3.204  -7.187  1.108   0.28 22.04 ?  163 LYS   A N    1 
ATOM   3674 C CA   A LYS   A 1 163 ? 3.442  -8.047  -0.151  0.72 22.91 ?  163 LYS   A CA   1 
ATOM   3675 C CA   B LYS   A 1 163 ? 3.295  -7.942  -0.137  0.28 22.62 ?  163 LYS   A CA   1 
ATOM   3676 C C    A LYS   A 1 163 ? 4.534  -9.107  -0.061  0.72 22.14 ?  163 LYS   A C    1 
ATOM   3677 C C    B LYS   A 1 163 ? 4.356  -9.033  -0.046  0.28 21.91 ?  163 LYS   A C    1 
ATOM   3678 O O    A LYS   A 1 163 ? 4.382  -10.211 -0.596  0.72 22.76 ?  163 LYS   A O    1 
ATOM   3679 O O    B LYS   A 1 163 ? 4.112  -10.184 -0.427  0.28 22.25 ?  163 LYS   A O    1 
ATOM   3680 C CB   A LYS   A 1 163 ? 3.686  -7.114  -1.338  0.72 25.71 ?  163 LYS   A CB   1 
ATOM   3681 C CB   B LYS   A 1 163 ? 3.586  -6.989  -1.296  0.28 24.18 ?  163 LYS   A CB   1 
ATOM   3682 C CG   A LYS   A 1 163 ? 3.770  -7.827  -2.676  0.72 29.07 ?  163 LYS   A CG   1 
ATOM   3683 C CG   B LYS   A 1 163 ? 3.710  -7.649  -2.656  0.28 25.69 ?  163 LYS   A CG   1 
ATOM   3684 C CD   A LYS   A 1 163 ? 4.142  -6.867  -3.790  0.72 32.23 ?  163 LYS   A CD   1 
ATOM   3685 C CD   B LYS   A 1 163 ? 3.450  -6.632  -3.759  0.28 27.02 ?  163 LYS   A CD   1 
ATOM   3686 C CE   A LYS   A 1 163 ? 4.058  -7.541  -5.148  0.72 34.79 ?  163 LYS   A CE   1 
ATOM   3687 C CE   B LYS   A 1 163 ? 4.374  -6.832  -4.948  0.28 27.96 ?  163 LYS   A CE   1 
ATOM   3688 N NZ   A LYS   A 1 163 ? 4.728  -6.742  -6.211  0.72 36.00 ?  163 LYS   A NZ   1 
ATOM   3689 N NZ   B LYS   A 1 163 ? 5.762  -6.372  -4.658  0.28 28.39 ?  163 LYS   A NZ   1 
ATOM   3690 H H    A LYS   A 1 163 ? 3.601  -6.443  1.004   0.72 27.14 ?  163 LYS   A H    1 
ATOM   3691 H H    B LYS   A 1 163 ? 3.430  -6.356  1.044   0.28 26.49 ?  163 LYS   A H    1 
ATOM   3692 H HA   A LYS   A 1 163 ? 2.596  -8.496  -0.293  0.72 27.53 ?  163 LYS   A HA   1 
ATOM   3693 H HA   B LYS   A 1 163 ? 2.440  -8.365  -0.304  0.28 27.18 ?  163 LYS   A HA   1 
ATOM   3694 H HB2  A LYS   A 1 163 ? 2.953  -6.475  -1.390  0.72 30.89 ?  163 LYS   A HB2  1 
ATOM   3695 H HB2  B LYS   A 1 163 ? 2.866  -6.344  -1.350  0.28 29.05 ?  163 LYS   A HB2  1 
ATOM   3696 H HB3  A LYS   A 1 163 ? 4.520  -6.641  -1.200  0.72 30.89 ?  163 LYS   A HB3  1 
ATOM   3697 H HB3  B LYS   A 1 163 ? 4.422  -6.534  -1.117  0.28 29.05 ?  163 LYS   A HB3  1 
ATOM   3698 H HG2  A LYS   A 1 163 ? 4.450  -8.517  -2.634  0.72 34.93 ?  163 LYS   A HG2  1 
ATOM   3699 H HG2  B LYS   A 1 163 ? 4.608  -8.002  -2.766  0.28 30.86 ?  163 LYS   A HG2  1 
ATOM   3700 H HG3  A LYS   A 1 163 ? 2.907  -8.219  -2.886  0.72 34.93 ?  163 LYS   A HG3  1 
ATOM   3701 H HG3  B LYS   A 1 163 ? 3.055  -8.362  -2.733  0.28 30.86 ?  163 LYS   A HG3  1 
ATOM   3702 H HD2  A LYS   A 1 163 ? 3.527  -6.116  -3.786  0.72 38.71 ?  163 LYS   A HD2  1 
ATOM   3703 H HD2  B LYS   A 1 163 ? 2.535  -6.722  -4.067  0.28 32.46 ?  163 LYS   A HD2  1 
ATOM   3704 H HD3  A LYS   A 1 163 ? 5.052  -6.557  -3.656  0.72 38.71 ?  163 LYS   A HD3  1 
ATOM   3705 H HD3  B LYS   A 1 163 ? 3.598  -5.738  -3.409  0.28 32.46 ?  163 LYS   A HD3  1 
ATOM   3706 H HE2  A LYS   A 1 163 ? 4.475  -8.415  -5.101  0.72 41.78 ?  163 LYS   A HE2  1 
ATOM   3707 H HE2  B LYS   A 1 163 ? 4.407  -7.776  -5.170  0.28 33.59 ?  163 LYS   A HE2  1 
ATOM   3708 H HE3  A LYS   A 1 163 ? 3.128  -7.637  -5.393  0.72 41.78 ?  163 LYS   A HE3  1 
ATOM   3709 H HE3  B LYS   A 1 163 ? 4.038  -6.323  -5.702  0.28 33.59 ?  163 LYS   A HE3  1 
ATOM   3710 H HZ1  A LYS   A 1 163 ? 4.665  -7.163  -6.993  0.72 43.24 ?  163 LYS   A HZ1  1 
ATOM   3711 H HZ1  B LYS   A 1 163 ? 6.279  -6.501  -5.370  0.28 34.11 ?  163 LYS   A HZ1  1 
ATOM   3712 H HZ2  A LYS   A 1 163 ? 4.339  -5.944  -6.279  0.72 43.24 ?  163 LYS   A HZ2  1 
ATOM   3713 H HZ2  B LYS   A 1 163 ? 5.758  -5.505  -4.456  0.28 34.11 ?  163 LYS   A HZ2  1 
ATOM   3714 H HZ3  A LYS   A 1 163 ? 5.588  -6.628  -6.012  0.72 43.24 ?  163 LYS   A HZ3  1 
ATOM   3715 H HZ3  B LYS   A 1 163 ? 6.095  -6.828  -3.971  0.28 34.11 ?  163 LYS   A HZ3  1 
ATOM   3716 N N    A LEU   A 1 164 ? 5.648  -8.786  0.604   0.72 20.34 ?  164 LEU   A N    1 
ATOM   3717 N N    B LEU   A 1 164 ? 5.545  -8.691  0.455   0.28 20.68 ?  164 LEU   A N    1 
ATOM   3718 C CA   A LEU   A 1 164 ? 6.746  -9.742  0.736   0.72 19.52 ?  164 LEU   A CA   1 
ATOM   3719 C CA   B LEU   A 1 164 ? 6.598  -9.692  0.605   0.28 19.95 ?  164 LEU   A CA   1 
ATOM   3720 C C    A LEU   A 1 164 ? 6.320  -10.961 1.544   0.72 19.64 ?  164 LEU   A C    1 
ATOM   3721 C C    B LEU   A 1 164 ? 6.166  -10.800 1.555   0.28 19.98 ?  164 LEU   A C    1 
ATOM   3722 O O    A LEU   A 1 164 ? 6.648  -12.100 1.194   0.72 19.92 ?  164 LEU   A O    1 
ATOM   3723 O O    B LEU   A 1 164 ? 6.329  -11.989 1.255   0.28 19.92 ?  164 LEU   A O    1 
ATOM   3724 C CB   A LEU   A 1 164 ? 7.939  -9.057  1.404   0.72 18.62 ?  164 LEU   A CB   1 
ATOM   3725 C CB   B LEU   A 1 164 ? 7.881  -9.035  1.107   0.28 19.10 ?  164 LEU   A CB   1 
ATOM   3726 C CG   A LEU   A 1 164 ? 8.702  -8.030  0.561   0.72 18.47 ?  164 LEU   A CG   1 
ATOM   3727 C CG   B LEU   A 1 164 ? 8.638  -8.171  0.104   0.28 18.09 ?  164 LEU   A CG   1 
ATOM   3728 C CD1  A LEU   A 1 164 ? 9.615  -7.163  1.427   0.72 17.77 ?  164 LEU   A CD1  1 
ATOM   3729 C CD1  B LEU   A 1 164 ? 9.742  -7.415  0.817   0.28 17.29 ?  164 LEU   A CD1  1 
ATOM   3730 C CD2  A LEU   A 1 164 ? 9.510  -8.734  -0.521  0.72 18.57 ?  164 LEU   A CD2  1 
ATOM   3731 C CD2  B LEU   A 1 164 ? 9.207  -9.018  -1.020  0.28 18.07 ?  164 LEU   A CD2  1 
ATOM   3732 H H    A LEU   A 1 164 ? 5.789  -8.030  0.991   0.72 24.44 ?  164 LEU   A H    1 
ATOM   3733 H H    B LEU   A 1 164 ? 5.764  -7.899  0.711   0.28 24.86 ?  164 LEU   A H    1 
ATOM   3734 H HA   A LEU   A 1 164 ? 7.019  -10.041 -0.143  0.72 23.46 ?  164 LEU   A HA   1 
ATOM   3735 H HA   B LEU   A 1 164 ? 6.777  -10.092 -0.259  0.28 23.98 ?  164 LEU   A HA   1 
ATOM   3736 H HB2  A LEU   A 1 164 ? 7.622  -8.596  2.196   0.72 22.39 ?  164 LEU   A HB2  1 
ATOM   3737 H HB2  B LEU   A 1 164 ? 7.660  -8.471  1.862   0.28 22.96 ?  164 LEU   A HB2  1 
ATOM   3738 H HB3  A LEU   A 1 164 ? 8.576  -9.740  1.664   0.72 22.39 ?  164 LEU   A HB3  1 
ATOM   3739 H HB3  B LEU   A 1 164 ? 8.488  -9.735  1.394   0.28 22.96 ?  164 LEU   A HB3  1 
ATOM   3740 H HG   A LEU   A 1 164 ? 8.067  -7.441  0.127   0.72 22.20 ?  164 LEU   A HG   1 
ATOM   3741 H HG   B LEU   A 1 164 ? 8.025  -7.530  -0.281  0.28 21.75 ?  164 LEU   A HG   1 
ATOM   3742 H HD11 A LEU   A 1 164 ? 10.082 -6.525  0.862   0.72 21.36 ?  164 LEU   A HD11 1 
ATOM   3743 H HD11 B LEU   A 1 164 ? 10.221 -6.873  0.173   0.28 20.79 ?  164 LEU   A HD11 1 
ATOM   3744 H HD12 A LEU   A 1 164 ? 9.076  -6.687  2.082   0.72 21.36 ?  164 LEU   A HD12 1 
ATOM   3745 H HD12 B LEU   A 1 164 ? 9.348  -6.850  1.500   0.28 20.79 ?  164 LEU   A HD12 1 
ATOM   3746 H HD13 A LEU   A 1 164 ? 10.258 -7.731  1.882   0.72 21.36 ?  164 LEU   A HD13 1 
ATOM   3747 H HD13 B LEU   A 1 164 ? 10.346 -8.055  1.227   0.28 20.79 ?  164 LEU   A HD13 1 
ATOM   3748 H HD21 A LEU   A 1 164 ? 10.027 -8.072  -1.009  0.72 22.32 ?  164 LEU   A HD21 1 
ATOM   3749 H HD21 B LEU   A 1 164 ? 9.768  -8.461  -1.580  0.28 21.72 ?  164 LEU   A HD21 1 
ATOM   3750 H HD22 A LEU   A 1 164 ? 10.104 -9.376  -0.105  0.72 22.32 ?  164 LEU   A HD22 1 
ATOM   3751 H HD22 B LEU   A 1 164 ? 9.731  -9.737  -0.636  0.28 21.72 ?  164 LEU   A HD22 1 
ATOM   3752 H HD23 A LEU   A 1 164 ? 8.899  -9.185  -1.123  0.72 22.32 ?  164 LEU   A HD23 1 
ATOM   3753 H HD23 B LEU   A 1 164 ? 8.475  -9.382  -1.541  0.28 21.72 ?  164 LEU   A HD23 1 
ATOM   3754 N N    A VAL   A 1 165 ? 5.602  -10.735 2.640   0.72 19.22 ?  165 VAL   A N    1 
ATOM   3755 N N    B VAL   A 1 165 ? 5.629  -10.430 2.718   0.28 19.92 ?  165 VAL   A N    1 
ATOM   3756 C CA   A VAL   A 1 165 ? 5.153  -11.830 3.491   0.72 18.92 ?  165 VAL   A CA   1 
ATOM   3757 C CA   B VAL   A 1 165 ? 5.128  -11.439 3.647   0.28 19.88 ?  165 VAL   A CA   1 
ATOM   3758 C C    A VAL   A 1 165 ? 4.121  -12.682 2.763   0.72 19.28 ?  165 VAL   A C    1 
ATOM   3759 C C    B VAL   A 1 165 ? 4.030  -12.259 2.987   0.28 20.30 ?  165 VAL   A C    1 
ATOM   3760 O O    A VAL   A 1 165 ? 4.212  -13.914 2.729   0.72 19.41 ?  165 VAL   A O    1 
ATOM   3761 O O    B VAL   A 1 165 ? 4.099  -13.492 2.930   0.28 20.06 ?  165 VAL   A O    1 
ATOM   3762 C CB   A VAL   A 1 165 ? 4.589  -11.257 4.804   0.72 19.28 ?  165 VAL   A CB   1 
ATOM   3763 C CB   B VAL   A 1 165 ? 4.648  -10.789 4.957   0.28 19.82 ?  165 VAL   A CB   1 
ATOM   3764 C CG1  A VAL   A 1 165 ? 3.870  -12.335 5.602   0.72 19.90 ?  165 VAL   A CG1  1 
ATOM   3765 C CG1  B VAL   A 1 165 ? 3.909  -11.813 5.817   0.28 19.94 ?  165 VAL   A CG1  1 
ATOM   3766 C CG2  A VAL   A 1 165 ? 5.693  -10.606 5.626   0.72 19.51 ?  165 VAL   A CG2  1 
ATOM   3767 C CG2  B VAL   A 1 165 ? 5.825  -10.204 5.719   0.28 19.84 ?  165 VAL   A CG2  1 
ATOM   3768 H H    A VAL   A 1 165 ? 5.351  -9.964  2.910   0.72 23.10 ?  165 VAL   A H    1 
ATOM   3769 H H    B VAL   A 1 165 ? 5.543  -9.617  2.988   0.28 23.94 ?  165 VAL   A H    1 
ATOM   3770 H HA   A VAL   A 1 165 ? 5.909  -12.401 3.713   0.72 22.74 ?  165 VAL   A HA   1 
ATOM   3771 H HA   B VAL   A 1 165 ? 5.853  -12.040 3.871   0.28 23.90 ?  165 VAL   A HA   1 
ATOM   3772 H HB   A VAL   A 1 165 ? 3.938  -10.574 4.589   0.72 23.17 ?  165 VAL   A HB   1 
ATOM   3773 H HB   B VAL   A 1 165 ? 4.031  -10.068 4.753   0.28 23.82 ?  165 VAL   A HB   1 
ATOM   3774 H HG11 A VAL   A 1 165 ? 3.769  -12.032 6.519   0.72 23.92 ?  165 VAL   A HG11 1 
ATOM   3775 H HG11 B VAL   A 1 165 ? 3.833  -11.471 6.722   0.28 23.97 ?  165 VAL   A HG11 1 
ATOM   3776 H HG12 A VAL   A 1 165 ? 2.993  -12.488 5.211   0.72 23.92 ?  165 VAL   A HG12 1 
ATOM   3777 H HG12 B VAL   A 1 165 ? 3.024  -11.964 5.449   0.28 23.97 ?  165 VAL   A HG12 1 
ATOM   3778 H HG13 A VAL   A 1 165 ? 4.392  -13.150 5.578   0.72 23.92 ?  165 VAL   A HG13 1 
ATOM   3779 H HG13 B VAL   A 1 165 ? 4.412  -12.643 5.823   0.28 23.97 ?  165 VAL   A HG13 1 
ATOM   3780 H HG21 A VAL   A 1 165 ? 5.314  -10.257 6.449   0.72 23.45 ?  165 VAL   A HG21 1 
ATOM   3781 H HG21 B VAL   A 1 165 ? 5.505  -9.830  6.555   0.28 23.85 ?  165 VAL   A HG21 1 
ATOM   3782 H HG22 A VAL   A 1 165 ? 6.371  -11.269 5.830   0.72 23.45 ?  165 VAL   A HG22 1 
ATOM   3783 H HG22 B VAL   A 1 165 ? 6.466  -10.911 5.897   0.28 23.85 ?  165 VAL   A HG22 1 
ATOM   3784 H HG23 A VAL   A 1 165 ? 6.083  -9.882  5.111   0.72 23.45 ?  165 VAL   A HG23 1 
ATOM   3785 H HG23 B VAL   A 1 165 ? 6.235  -9.511  5.181   0.28 23.85 ?  165 VAL   A HG23 1 
ATOM   3786 N N    A SER   A 1 166 ? 3.114  -12.035 2.179   0.72 19.57 ?  166 SER   A N    1 
ATOM   3787 N N    B SER   A 1 166 ? 3.008  -11.585 2.456   0.28 21.27 ?  166 SER   A N    1 
ATOM   3788 C CA   A SER   A 1 166 ? 1.991  -12.766 1.600   0.72 20.92 ?  166 SER   A CA   1 
ATOM   3789 C CA   B SER   A 1 166 ? 1.845  -12.304 1.950   0.28 22.35 ?  166 SER   A CA   1 
ATOM   3790 C C    A SER   A 1 166 ? 2.402  -13.572 0.382   0.72 21.65 ?  166 SER   A C    1 
ATOM   3791 C C    B SER   A 1 166 ? 2.187  -13.170 0.746   0.28 22.64 ?  166 SER   A C    1 
ATOM   3792 O O    A SER   A 1 166 ? 1.728  -14.553 0.038   0.72 23.45 ?  166 SER   A O    1 
ATOM   3793 O O    B SER   A 1 166 ? 1.570  -14.223 0.554   0.28 22.67 ?  166 SER   A O    1 
ATOM   3794 C CB   A SER   A 1 166 ? 0.877  -11.796 1.203   0.72 22.54 ?  166 SER   A CB   1 
ATOM   3795 C CB   B SER   A 1 166 ? 0.717  -11.334 1.596   0.28 23.38 ?  166 SER   A CB   1 
ATOM   3796 O OG   A SER   A 1 166 ? 0.305  -11.177 2.343   0.72 24.65 ?  166 SER   A OG   1 
ATOM   3797 O OG   B SER   A 1 166 ? 0.375  -10.515 2.700   0.28 24.32 ?  166 SER   A OG   1 
ATOM   3798 H H    A SER   A 1 166 ? 3.042  -11.196 2.128   0.72 23.52 ?  166 SER   A H    1 
ATOM   3799 H H    B SER   A 1 166 ? 2.967  -10.730 2.379   0.28 25.57 ?  166 SER   A H    1 
ATOM   3800 H HA   A SER   A 1 166 ? 1.618  -13.385 2.257   0.72 25.14 ?  166 SER   A HA   1 
ATOM   3801 H HA   B SER   A 1 166 ? 1.521  -12.884 2.649   0.28 26.86 ?  166 SER   A HA   1 
ATOM   3802 H HB2  A SER   A 1 166 ? 1.247  -11.118 0.614   0.72 27.08 ?  166 SER   A HB2  1 
ATOM   3803 H HB2  B SER   A 1 166 ? 1.003  -10.771 0.863   0.28 28.09 ?  166 SER   A HB2  1 
ATOM   3804 H HB3  A SER   A 1 166 ? 0.176  -12.283 0.734   0.72 27.08 ?  166 SER   A HB3  1 
ATOM   3805 H HB3  B SER   A 1 166 ? -0.066 -11.849 1.333   0.28 28.09 ?  166 SER   A HB3  1 
ATOM   3806 H HG   A SER   A 1 166 ? 0.893  -10.723 2.744   0.72 29.62 ?  166 SER   A HG   1 
ATOM   3807 H HG   B SER   A 1 166 ? 1.042  -10.065 2.940   0.28 29.22 ?  166 SER   A HG   1 
ATOM   3808 N N    A SER   A 1 167 ? 3.467  -13.162 -0.300  0.72 21.14 ?  167 SER   A N    1 
ATOM   3809 N N    B SER   A 1 167 ? 3.152  -12.757 -0.071  0.28 23.32 ?  167 SER   A N    1 
ATOM   3810 C CA   A SER   A 1 167 ? 3.953  -13.874 -1.467  0.72 21.89 ?  167 SER   A CA   1 
ATOM   3811 C CA   B SER   A 1 167 ? 3.463  -13.480 -1.297  0.28 24.08 ?  167 SER   A CA   1 
ATOM   3812 C C    A SER   A 1 167 ? 5.118  -14.792 -1.144  0.72 21.82 ?  167 SER   A C    1 
ATOM   3813 C C    B SER   A 1 167 ? 4.578  -14.505 -1.127  0.28 24.75 ?  167 SER   A C    1 
ATOM   3814 O O    A SER   A 1 167 ? 5.628  -15.456 -2.050  0.72 22.26 ?  167 SER   A O    1 
ATOM   3815 O O    B SER   A 1 167 ? 4.961  -15.147 -2.110  0.28 24.51 ?  167 SER   A O    1 
ATOM   3816 C CB   A SER   A 1 167 ? 4.361  -12.885 -2.567  0.72 22.43 ?  167 SER   A CB   1 
ATOM   3817 C CB   B SER   A 1 167 ? 3.827  -12.504 -2.421  0.28 24.43 ?  167 SER   A CB   1 
ATOM   3818 O OG   A SER   A 1 167 ? 5.439  -12.067 -2.145  0.72 22.66 ?  167 SER   A OG   1 
ATOM   3819 O OG   B SER   A 1 167 ? 5.021  -11.803 -2.123  0.28 24.81 ?  167 SER   A OG   1 
ATOM   3820 H H    A SER   A 1 167 ? 3.915  -12.457 -0.108  0.72 25.41 ?  167 SER   A H    1 
ATOM   3821 H H    B SER   A 1 167 ? 3.640  -12.060 0.067   0.28 28.03 ?  167 SER   A H    1 
ATOM   3822 H HA   A SER   A 1 167 ? 3.247  -14.428 -1.818  0.72 26.30 ?  167 SER   A HA   1 
ATOM   3823 H HA   B SER   A 1 167 ? 2.664  -13.954 -1.576  0.28 28.94 ?  167 SER   A HA   1 
ATOM   3824 H HB2  A SER   A 1 167 ? 4.633  -13.384 -3.355  0.72 26.95 ?  167 SER   A HB2  1 
ATOM   3825 H HB2  B SER   A 1 167 ? 3.950  -13.008 -3.242  0.28 29.35 ?  167 SER   A HB2  1 
ATOM   3826 H HB3  A SER   A 1 167 ? 3.595  -12.327 -2.782  0.72 26.95 ?  167 SER   A HB3  1 
ATOM   3827 H HB3  B SER   A 1 167 ? 3.103  -11.867 -2.532  0.28 29.35 ?  167 SER   A HB3  1 
ATOM   3828 H HG   A SER   A 1 167 ? 5.207  -11.617 -1.473  0.72 27.23 ?  167 SER   A HG   1 
ATOM   3829 H HG   B SER   A 1 167 ? 4.926  -11.369 -1.411  0.28 29.81 ?  167 SER   A HG   1 
ATOM   3830 N N    A PHE   A 1 168 ? 5.548  -14.853 0.115   0.72 21.34 ?  168 PHE   A N    1 
ATOM   3831 N N    B PHE   A 1 168 ? 5.106  -14.677 0.082   0.28 25.92 ?  168 PHE   A N    1 
ATOM   3832 C CA   A PHE   A 1 168 ? 6.731  -15.637 0.446   0.72 21.33 ?  168 PHE   A CA   1 
ATOM   3833 C CA   B PHE   A 1 168 ? 6.141  -15.675 0.298   0.28 27.17 ?  168 PHE   A CA   1 
ATOM   3834 C C    A PHE   A 1 168 ? 6.430  -17.125 0.335   0.72 23.26 ?  168 PHE   A C    1 
ATOM   3835 C C    B PHE   A 1 168 ? 5.565  -17.077 0.129   0.28 29.51 ?  168 PHE   A C    1 
ATOM   3836 O O    A PHE   A 1 168 ? 5.446  -17.622 0.896   0.72 24.58 ?  168 PHE   A O    1 
ATOM   3837 O O    B PHE   A 1 168 ? 4.376  -17.319 0.355   0.28 29.97 ?  168 PHE   A O    1 
ATOM   3838 C CB   A PHE   A 1 168 ? 7.239  -15.326 1.854   0.72 20.20 ?  168 PHE   A CB   1 
ATOM   3839 C CB   B PHE   A 1 168 ? 6.745  -15.524 1.694   0.28 25.93 ?  168 PHE   A CB   1 
ATOM   3840 C CG   A PHE   A 1 168 ? 8.503  -16.067 2.197   0.72 18.96 ?  168 PHE   A CG   1 
ATOM   3841 C CG   B PHE   A 1 168 ? 8.080  -16.198 1.852   0.28 24.75 ?  168 PHE   A CG   1 
ATOM   3842 C CD1  A PHE   A 1 168 ? 9.693  -15.707 1.600   0.72 18.87 ?  168 PHE   A CD1  1 
ATOM   3843 C CD1  B PHE   A 1 168 ? 9.211  -15.664 1.258   0.28 24.29 ?  168 PHE   A CD1  1 
ATOM   3844 C CD2  A PHE   A 1 168 ? 8.508  -17.139 3.079   0.72 18.09 ?  168 PHE   A CD2  1 
ATOM   3845 C CD2  B PHE   A 1 168 ? 8.206  -17.359 2.597   0.28 24.10 ?  168 PHE   A CD2  1 
ATOM   3846 C CE1  A PHE   A 1 168 ? 10.865 -16.381 1.884   0.72 18.32 ?  168 PHE   A CE1  1 
ATOM   3847 C CE1  B PHE   A 1 168 ? 10.441 -16.277 1.399   0.28 23.95 ?  168 PHE   A CE1  1 
ATOM   3848 C CE2  A PHE   A 1 168 ? 9.689  -17.819 3.369   0.72 18.26 ?  168 PHE   A CE2  1 
ATOM   3849 C CE2  B PHE   A 1 168 ? 9.435  -17.976 2.742   0.28 23.82 ?  168 PHE   A CE2  1 
ATOM   3850 C CZ   A PHE   A 1 168 ? 10.863 -17.437 2.769   0.72 18.35 ?  168 PHE   A CZ   1 
ATOM   3851 C CZ   B PHE   A 1 168 ? 10.554 -17.433 2.142   0.28 23.74 ?  168 PHE   A CZ   1 
ATOM   3852 H H    A PHE   A 1 168 ? 5.193  -14.454 0.785   0.72 25.64 ?  168 PHE   A H    1 
ATOM   3853 H H    B PHE   A 1 168 ? 4.888  -14.228 0.783   0.28 31.15 ?  168 PHE   A H    1 
ATOM   3854 H HA   A PHE   A 1 168 ? 7.450  -15.425 -0.179  0.72 25.64 ?  168 PHE   A HA   1 
ATOM   3855 H HA   B PHE   A 1 168 ? 6.843  -15.553 -0.357  0.28 32.65 ?  168 PHE   A HA   1 
ATOM   3856 H HB2  A PHE   A 1 168 ? 7.430  -14.376 1.924   0.72 24.28 ?  168 PHE   A HB2  1 
ATOM   3857 H HB2  B PHE   A 1 168 ? 6.863  -14.581 1.881   0.28 31.15 ?  168 PHE   A HB2  1 
ATOM   3858 H HB3  A PHE   A 1 168 ? 6.568  -15.579 2.500   0.72 24.28 ?  168 PHE   A HB3  1 
ATOM   3859 H HB3  B PHE   A 1 168 ? 6.136  -15.914 2.341   0.28 31.15 ?  168 PHE   A HB3  1 
ATOM   3860 H HD1  A PHE   A 1 168 ? 9.723  -14.996 1.004   0.72 22.69 ?  168 PHE   A HD1  1 
ATOM   3861 H HD1  B PHE   A 1 168 ? 9.140  -14.885 0.754   0.28 29.19 ?  168 PHE   A HD1  1 
ATOM   3862 H HD2  A PHE   A 1 168 ? 7.719  -17.401 3.490   0.72 21.74 ?  168 PHE   A HD2  1 
ATOM   3863 H HD2  B PHE   A 1 168 ? 7.454  -17.729 3.002   0.28 28.95 ?  168 PHE   A HD2  1 
ATOM   3864 H HE1  A PHE   A 1 168 ? 11.672 -16.126 1.482   0.72 22.02 ?  168 PHE   A HE1  1 
ATOM   3865 H HE1  B PHE   A 1 168 ? 11.192 -15.908 0.994   0.28 28.78 ?  168 PHE   A HE1  1 
ATOM   3866 H HE2  A PHE   A 1 168 ? 9.681  -18.534 3.967   0.72 21.95 ?  168 PHE   A HE2  1 
ATOM   3867 H HE2  B PHE   A 1 168 ? 9.508  -18.756 3.244   0.28 28.62 ?  168 PHE   A HE2  1 
ATOM   3868 H HZ   A PHE   A 1 168 ? 11.658 -17.892 2.961   0.72 22.06 ?  168 PHE   A HZ   1 
ATOM   3869 H HZ   B PHE   A 1 168 ? 11.382 -17.846 2.238   0.28 28.53 ?  168 PHE   A HZ   1 
ATOM   3870 N N    A LEU   A 1 169 ? 7.301  -17.837 -0.377  0.72 25.80 ?  169 LEU   A N    1 
ATOM   3871 N N    B LEU   A 1 169 ? 6.425  -18.006 -0.276  0.28 31.16 ?  169 LEU   A N    1 
ATOM   3872 C CA   A LEU   A 1 169 ? 7.148  -19.272 -0.533  0.72 30.08 ?  169 LEU   A CA   1 
ATOM   3873 C CA   B LEU   A 1 169 ? 5.998  -19.375 -0.548  0.28 32.46 ?  169 LEU   A CA   1 
ATOM   3874 C C    A LEU   A 1 169 ? 8.061  -19.998 0.438   0.72 32.15 ?  169 LEU   A C    1 
ATOM   3875 C C    B LEU   A 1 169 ? 5.915  -20.207 0.728   0.28 32.92 ?  169 LEU   A C    1 
ATOM   3876 O O    A LEU   A 1 169 ? 7.621  -20.438 1.500   0.72 32.78 ?  169 LEU   A O    1 
ATOM   3877 O O    B LEU   A 1 169 ? 4.952  -20.949 0.927   0.28 33.25 ?  169 LEU   A O    1 
ATOM   3878 C CB   A LEU   A 1 169 ? 7.458  -19.695 -1.970  0.72 31.84 ?  169 LEU   A CB   1 
ATOM   3879 C CB   B LEU   A 1 169 ? 6.945  -20.037 -1.553  0.28 33.13 ?  169 LEU   A CB   1 
ATOM   3880 C CG   A LEU   A 1 169 ? 7.145  -21.153 -2.315  0.72 33.26 ?  169 LEU   A CG   1 
ATOM   3881 C CG   B LEU   A 1 169 ? 6.459  -20.116 -3.003  0.28 33.63 ?  169 LEU   A CG   1 
ATOM   3882 C CD1  A LEU   A 1 169 ? 5.735  -21.515 -1.875  0.72 33.95 ?  169 LEU   A CD1  1 
ATOM   3883 C CD1  B LEU   A 1 169 ? 5.356  -21.154 -3.136  0.28 33.79 ?  169 LEU   A CD1  1 
ATOM   3884 C CD2  A LEU   A 1 169 ? 7.315  -21.393 -3.807  0.72 33.63 ?  169 LEU   A CD2  1 
ATOM   3885 C CD2  B LEU   A 1 169 ? 5.980  -18.759 -3.495  0.28 33.79 ?  169 LEU   A CD2  1 
ATOM   3886 O OXT  A LEU   A 1 169 ? 9.253  -20.150 0.185   0.72 32.53 -1 169 LEU   A OXT  1 
ATOM   3887 O OXT  B LEU   A 1 169 ? 6.795  -20.160 1.588   0.28 32.95 -1 169 LEU   A OXT  1 
ATOM   3888 H H    A LEU   A 1 169 ? 7.992  -17.511 -0.783  0.72 31.00 ?  169 LEU   A H    1 
ATOM   3889 H H    B LEU   A 1 169 ? 7.265  -17.867 -0.399  0.28 37.43 ?  169 LEU   A H    1 
ATOM   3890 H HA   A LEU   A 1 169 ? 6.237  -19.511 -0.323  0.72 36.14 ?  169 LEU   A HA   1 
ATOM   3891 H HA   B LEU   A 1 169 ? 5.114  -19.356 -0.939  0.28 38.99 ?  169 LEU   A HA   1 
ATOM   3892 H HB2  A LEU   A 1 169 ? 6.938  -19.140 -2.570  0.72 38.25 ?  169 LEU   A HB2  1 
ATOM   3893 H HB2  B LEU   A 1 169 ? 7.779  -19.542 -1.560  0.28 39.79 ?  169 LEU   A HB2  1 
ATOM   3894 H HB3  A LEU   A 1 169 ? 8.403  -19.557 -2.136  0.72 38.25 ?  169 LEU   A HB3  1 
ATOM   3895 H HB3  B LEU   A 1 169 ? 7.114  -20.944 -1.259  0.28 39.79 ?  169 LEU   A HB3  1 
ATOM   3896 H HG   A LEU   A 1 169 ? 7.766  -21.734 -1.846  0.72 39.95 ?  169 LEU   A HG   1 
ATOM   3897 H HG   B LEU   A 1 169 ? 7.198  -20.393 -3.568  0.28 40.39 ?  169 LEU   A HG   1 
ATOM   3898 H HD11 A LEU   A 1 169 ? 5.471  -22.339 -2.311  0.72 40.78 ?  169 LEU   A HD11 1 
ATOM   3899 H HD11 B LEU   A 1 169 ? 5.078  -21.202 -4.064  0.28 40.59 ?  169 LEU   A HD11 1 
ATOM   3900 H HD12 A LEU   A 1 169 ? 5.725  -21.632 -0.912  0.72 40.78 ?  169 LEU   A HD12 1 
ATOM   3901 H HD12 B LEU   A 1 169 ? 5.697  -22.015 -2.848  0.28 40.59 ?  169 LEU   A HD12 1 
ATOM   3902 H HD13 A LEU   A 1 169 ? 5.133  -20.798 -2.131  0.72 40.78 ?  169 LEU   A HD13 1 
ATOM   3903 H HD13 B LEU   A 1 169 ? 4.607  -20.892 -2.579  0.28 40.59 ?  169 LEU   A HD13 1 
ATOM   3904 H HD21 A LEU   A 1 169 ? 7.120  -22.323 -4.002  0.72 40.40 ?  169 LEU   A HD21 1 
ATOM   3905 H HD21 B LEU   A 1 169 ? 5.837  -18.804 -4.453  0.28 40.59 ?  169 LEU   A HD21 1 
ATOM   3906 H HD22 A LEU   A 1 169 ? 6.699  -20.818 -4.289  0.72 40.40 ?  169 LEU   A HD22 1 
ATOM   3907 H HD22 B LEU   A 1 169 ? 5.148  -18.535 -3.048  0.28 40.59 ?  169 LEU   A HD22 1 
ATOM   3908 H HD23 A LEU   A 1 169 ? 8.228  -21.185 -4.058  0.72 40.40 ?  169 LEU   A HD23 1 
ATOM   3909 H HD23 B LEU   A 1 169 ? 6.655  -18.093 -3.293  0.28 40.59 ?  169 LEU   A HD23 1 
ATOM   3910 N N    A SER   B 1 1   ? 50.876 -9.262  -23.753 0.72 27.08 ?  1   SER   B N    1 
ATOM   3911 N N    B SER   B 1 1   ? 50.799 -9.303  -23.739 0.28 26.82 ?  1   SER   B N    1 
ATOM   3912 C CA   A SER   B 1 1   ? 51.354 -10.302 -22.820 0.72 27.07 ?  1   SER   B CA   1 
ATOM   3913 C CA   B SER   B 1 1   ? 51.289 -10.278 -22.741 0.28 26.79 ?  1   SER   B CA   1 
ATOM   3914 C C    A SER   B 1 1   ? 50.280 -11.357 -22.571 0.72 26.31 ?  1   SER   B C    1 
ATOM   3915 C C    B SER   B 1 1   ? 50.260 -11.376 -22.527 0.28 26.38 ?  1   SER   B C    1 
ATOM   3916 O O    A SER   B 1 1   ? 49.079 -11.144 -22.810 0.72 26.47 ?  1   SER   B O    1 
ATOM   3917 O O    B SER   B 1 1   ? 49.060 -11.180 -22.744 0.28 26.28 ?  1   SER   B O    1 
ATOM   3918 C CB   A SER   B 1 1   ? 51.797 -9.681  -21.496 0.72 28.10 ?  1   SER   B CB   1 
ATOM   3919 C CB   B SER   B 1 1   ? 51.583 -9.585  -21.415 0.28 27.32 ?  1   SER   B CB   1 
ATOM   3920 O OG   A SER   B 1 1   ? 50.693 -9.475  -20.635 0.72 29.92 ?  1   SER   B OG   1 
ATOM   3921 O OG   B SER   B 1 1   ? 50.394 -9.401  -20.667 0.28 28.02 ?  1   SER   B OG   1 
ATOM   3922 H H1   A SER   B 1 1   ? 50.758 -9.626  -24.555 0.72 32.54 ?  1   SER   B H1   1 
ATOM   3923 H H1   B SER   B 1 1   ? 50.756 -9.698  -24.533 0.28 32.23 ?  1   SER   B H1   1 
ATOM   3924 H H2   A SER   B 1 1   ? 50.111 -8.934  -23.452 0.72 32.54 ?  1   SER   B H2   1 
ATOM   3925 H H2   B SER   B 1 1   ? 49.995 -9.021  -23.496 0.28 32.23 ?  1   SER   B H2   1 
ATOM   3926 H H3   A SER   B 1 1   ? 51.486 -8.617  -23.803 0.72 32.54 ?  1   SER   B H3   1 
ATOM   3927 H H3   B SER   B 1 1   ? 51.365 -8.620  -23.772 0.28 32.23 ?  1   SER   B H3   1 
ATOM   3928 H HA   A SER   B 1 1   ? 52.123 -10.731 -23.222 0.72 32.52 ?  1   SER   B HA   1 
ATOM   3929 H HA   B SER   B 1 1   ? 52.104 -10.675 -23.076 0.28 32.18 ?  1   SER   B HA   1 
ATOM   3930 H HB2  A SER   B 1 1   ? 52.418 -10.285 -21.064 0.72 33.75 ?  1   SER   B HB2  1 
ATOM   3931 H HB2  B SER   B 1 1   ? 52.202 -10.135 -20.913 0.28 32.82 ?  1   SER   B HB2  1 
ATOM   3932 H HB3  A SER   B 1 1   ? 52.232 -8.830  -21.674 0.72 33.75 ?  1   SER   B HB3  1 
ATOM   3933 H HB3  B SER   B 1 1   ? 51.975 -8.716  -21.592 0.28 32.82 ?  1   SER   B HB3  1 
ATOM   3934 H HG   A SER   B 1 1   ? 50.953 -9.092  -19.931 0.72 35.94 ?  1   SER   B HG   1 
ATOM   3935 H HG   B SER   B 1 1   ? 50.573 -9.021  -19.940 0.28 33.66 ?  1   SER   B HG   1 
ATOM   3936 N N    A MET   B 1 2   ? 50.737 -12.503 -22.084 0.72 25.92 ?  2   MET   B N    1 
ATOM   3937 N N    B MET   B 1 2   ? 50.741 -12.534 -22.092 0.28 26.10 ?  2   MET   B N    1 
ATOM   3938 C CA   A MET   B 1 2   ? 49.914 -13.692 -21.919 0.72 26.33 ?  2   MET   B CA   1 
ATOM   3939 C CA   B MET   B 1 2   ? 49.908 -13.714 -21.909 0.28 25.92 ?  2   MET   B CA   1 
ATOM   3940 C C    A MET   B 1 2   ? 49.652 -13.892 -20.432 0.72 24.40 ?  2   MET   B C    1 
ATOM   3941 C C    B MET   B 1 2   ? 49.650 -13.899 -20.423 0.28 24.17 ?  2   MET   B C    1 
ATOM   3942 O O    A MET   B 1 2   ? 50.580 -14.158 -19.665 0.72 24.69 ?  2   MET   B O    1 
ATOM   3943 O O    B MET   B 1 2   ? 50.576 -14.168 -19.651 0.28 24.42 ?  2   MET   B O    1 
ATOM   3944 C CB   A MET   B 1 2   ? 50.652 -14.886 -22.511 0.72 30.15 ?  2   MET   B CB   1 
ATOM   3945 C CB   B MET   B 1 2   ? 50.612 -14.928 -22.493 0.28 27.85 ?  2   MET   B CB   1 
ATOM   3946 C CG   A MET   B 1 2   ? 49.828 -16.155 -22.630 0.72 33.72 ?  2   MET   B CG   1 
ATOM   3947 C CG   B MET   B 1 2   ? 49.698 -16.109 -22.792 0.28 29.40 ?  2   MET   B CG   1 
ATOM   3948 S SD   A MET   B 1 2   ? 50.659 -17.367 -23.674 0.72 37.24 ?  2   MET   B SD   1 
ATOM   3949 S SD   B MET   B 1 2   ? 50.512 -17.338 -23.823 0.28 30.76 ?  2   MET   B SD   1 
ATOM   3950 C CE   A MET   B 1 2   ? 51.162 -16.303 -25.016 0.72 37.74 ?  2   MET   B CE   1 
ATOM   3951 C CE   B MET   B 1 2   ? 51.677 -16.289 -24.681 0.28 31.04 ?  2   MET   B CE   1 
ATOM   3952 H H    A MET   B 1 2   ? 51.556 -12.626 -21.837 0.72 31.15 ?  2   MET   B H    1 
ATOM   3953 H H    B MET   B 1 2   ? 51.570 -12.667 -21.898 0.28 31.36 ?  2   MET   B H    1 
ATOM   3954 H HA   A MET   B 1 2   ? 49.078 -13.587 -22.396 0.72 31.63 ?  2   MET   B HA   1 
ATOM   3955 H HA   B MET   B 1 2   ? 49.072 -13.607 -22.387 0.28 31.14 ?  2   MET   B HA   1 
ATOM   3956 H HB2  A MET   B 1 2   ? 50.948 -14.608 -23.387 0.72 36.22 ?  2   MET   B HB2  1 
ATOM   3957 H HB2  B MET   B 1 2   ? 50.990 -14.587 -23.309 0.28 33.45 ?  2   MET   B HB2  1 
ATOM   3958 H HB3  A MET   B 1 2   ? 51.419 -15.102 -21.965 0.72 36.22 ?  2   MET   B HB3  1 
ATOM   3959 H HB3  B MET   B 1 2   ? 51.315 -15.246 -21.903 0.28 33.45 ?  2   MET   B HB3  1 
ATOM   3960 H HG2  A MET   B 1 2   ? 49.700 -16.541 -21.743 0.72 40.50 ?  2   MET   B HG2  1 
ATOM   3961 H HG2  B MET   B 1 2   ? 49.436 -16.535 -21.957 0.28 35.32 ?  2   MET   B HG2  1 
ATOM   3962 H HG3  A MET   B 1 2   ? 48.971 -15.955 -23.035 0.72 40.50 ?  2   MET   B HG3  1 
ATOM   3963 H HG3  B MET   B 1 2   ? 48.916 -15.801 -23.268 0.28 35.32 ?  2   MET   B HG3  1 
ATOM   3964 H HE1  A MET   B 1 2   ? 51.311 -16.844 -25.790 0.72 45.33 ?  2   MET   B HE1  1 
ATOM   3965 H HE1  B MET   B 1 2   ? 52.084 -16.809 -25.360 0.28 37.29 ?  2   MET   B HE1  1 
ATOM   3966 H HE2  A MET   B 1 2   ? 50.447 -15.663 -25.182 0.72 45.33 ?  2   MET   B HE2  1 
ATOM   3967 H HE2  B MET   B 1 2   ? 51.195 -15.539 -25.080 0.28 37.29 ?  2   MET   B HE2  1 
ATOM   3968 H HE3  A MET   B 1 2   ? 51.978 -15.829 -24.772 0.72 45.33 ?  2   MET   B HE3  1 
ATOM   3969 H HE3  B MET   B 1 2   ? 52.361 -15.963 -24.061 0.28 37.29 ?  2   MET   B HE3  1 
ATOM   3970 N N    . VAL   B 1 3   ? 48.392 -13.746 -20.028 1.00 22.15 ?  3   VAL   B N    1 
ATOM   3971 C CA   . VAL   B 1 3   ? 47.974 -13.960 -18.651 1.00 20.76 ?  3   VAL   B CA   1 
ATOM   3972 C C    . VAL   B 1 3   ? 46.741 -14.851 -18.660 1.00 19.11 ?  3   VAL   B C    1 
ATOM   3973 O O    . VAL   B 1 3   ? 46.016 -14.940 -19.654 1.00 19.87 ?  3   VAL   B O    1 
ATOM   3974 C CB   . VAL   B 1 3   ? 47.677 -12.635 -17.917 1.00 22.68 ?  3   VAL   B CB   1 
ATOM   3975 C CG1  . VAL   B 1 3   ? 48.940 -11.772 -17.810 1.00 23.58 ?  3   VAL   B CG1  1 
ATOM   3976 C CG2  . VAL   B 1 3   ? 46.556 -11.890 -18.621 1.00 23.32 ?  3   VAL   B CG2  1 
ATOM   3977 H H    A VAL   B 1 3   ? 47.750 -13.524 -20.556 0.72 26.62 ?  3   VAL   B H    1 
ATOM   3978 H H    B VAL   B 1 3   ? 47.753 -13.517 -20.556 0.28 26.62 ?  3   VAL   B H    1 
ATOM   3979 H HA   . VAL   B 1 3   ? 48.679 -14.422 -18.172 1.00 24.94 ?  3   VAL   B HA   1 
ATOM   3980 H HB   . VAL   B 1 3   ? 47.379 -12.844 -17.017 1.00 27.25 ?  3   VAL   B HB   1 
ATOM   3981 H HG11 . VAL   B 1 3   ? 48.717 -10.957 -17.336 1.00 28.34 ?  3   VAL   B HG11 1 
ATOM   3982 H HG12 . VAL   B 1 3   ? 49.615 -12.267 -17.322 1.00 28.34 ?  3   VAL   B HG12 1 
ATOM   3983 H HG13 . VAL   B 1 3   ? 49.253 -11.567 -18.702 1.00 28.34 ?  3   VAL   B HG13 1 
ATOM   3984 H HG21 . VAL   B 1 3   ? 46.478 -11.007 -18.237 1.00 28.02 ?  3   VAL   B HG21 1 
ATOM   3985 H HG22 . VAL   B 1 3   ? 46.761 -11.827 -19.566 1.00 28.02 ?  3   VAL   B HG22 1 
ATOM   3986 H HG23 . VAL   B 1 3   ? 45.723 -12.379 -18.498 1.00 28.02 ?  3   VAL   B HG23 1 
ATOM   3987 N N    . ASN   B 1 4   ? 46.509 -15.519 -17.530 1.00 17.32 ?  4   ASN   B N    1 
ATOM   3988 C CA   . ASN   B 1 4   ? 45.374 -16.428 -17.388 1.00 16.41 ?  4   ASN   B CA   1 
ATOM   3989 C C    . ASN   B 1 4   ? 45.307 -17.401 -18.561 1.00 16.81 ?  4   ASN   B C    1 
ATOM   3990 O O    . ASN   B 1 4   ? 44.245 -17.646 -19.129 1.00 17.61 ?  4   ASN   B O    1 
ATOM   3991 C CB   . ASN   B 1 4   ? 44.058 -15.659 -17.233 1.00 16.08 ?  4   ASN   B CB   1 
ATOM   3992 C CG   . ASN   B 1 4   ? 44.007 -14.847 -15.949 1.00 15.26 ?  4   ASN   B CG   1 
ATOM   3993 O OD1  . ASN   B 1 4   ? 44.291 -15.353 -14.871 1.00 15.26 ?  4   ASN   B OD1  1 
ATOM   3994 N ND2  . ASN   B 1 4   ? 43.651 -13.571 -16.069 1.00 16.31 ?  4   ASN   B ND2  1 
ATOM   3995 H H    . ASN   B 1 4   ? 47.002 -15.460 -16.830 1.00 20.82 ?  4   ASN   B H    1 
ATOM   3996 H HA   . ASN   B 1 4   ? 45.506 -16.952 -16.584 1.00 19.73 ?  4   ASN   B HA   1 
ATOM   3997 H HB2  . ASN   B 1 4   ? 43.957 -15.050 -17.982 1.00 19.34 ?  4   ASN   B HB2  1 
ATOM   3998 H HB3  . ASN   B 1 4   ? 43.323 -16.294 -17.222 1.00 19.34 ?  4   ASN   B HB3  1 
ATOM   3999 H HD21 . ASN   B 1 4   ? 43.608 -13.066 -15.370 1.00 19.61 ?  4   ASN   B HD21 1 
ATOM   4000 H HD22 . ASN   B 1 4   ? 43.464 -13.242 -16.842 1.00 19.61 ?  4   ASN   B HD22 1 
ATOM   4001 N N    . SER   B 1 5   ? 46.462 -17.951 -18.934 1.00 17.68 ?  5   SER   B N    1 
ATOM   4002 C CA   . SER   B 1 5   ? 46.553 -18.871 -20.067 1.00 19.59 ?  5   SER   B CA   1 
ATOM   4003 C C    . SER   B 1 5   ? 46.520 -20.301 -19.540 1.00 21.41 ?  5   SER   B C    1 
ATOM   4004 O O    . SER   B 1 5   ? 47.524 -21.002 -19.485 1.00 23.93 ?  5   SER   B O    1 
ATOM   4005 C CB   . SER   B 1 5   ? 47.819 -18.596 -20.878 1.00 20.93 ?  5   SER   B CB   1 
ATOM   4006 O OG   . SER   B 1 5   ? 48.996 -18.786 -20.106 1.00 24.43 ?  5   SER   B OG   1 
ATOM   4007 H H    . SER   B 1 5   ? 47.217 -17.809 -18.545 1.00 21.26 ?  5   SER   B H    1 
ATOM   4008 H HA   . SER   B 1 5   ? 45.787 -18.749 -20.646 1.00 23.55 ?  5   SER   B HA   1 
ATOM   4009 H HB2  . SER   B 1 5   ? 47.837 -19.200 -21.641 1.00 25.15 ?  5   SER   B HB2  1 
ATOM   4010 H HB3  . SER   B 1 5   ? 47.779 -17.679 -21.189 1.00 25.15 ?  5   SER   B HB3  1 
ATOM   4011 H HG   . SER   B 1 5   ? 49.034 -19.581 -19.848 1.00 29.35 ?  5   SER   B HG   1 
ATOM   4012 N N    . PHE   B 1 6   ? 45.329 -20.699 -19.106 1.00 22.32 ?  6   PHE   B N    1 
ATOM   4013 C CA   . PHE   B 1 6   ? 45.098 -22.047 -18.608 1.00 22.02 ?  6   PHE   B CA   1 
ATOM   4014 C C    . PHE   B 1 6   ? 44.980 -22.995 -19.790 1.00 26.07 ?  6   PHE   B C    1 
ATOM   4015 O O    . PHE   B 1 6   ? 44.291 -22.692 -20.769 1.00 27.84 ?  6   PHE   B O    1 
ATOM   4016 C CB   . PHE   B 1 6   ? 43.815 -22.084 -17.779 1.00 20.35 ?  6   PHE   B CB   1 
ATOM   4017 C CG   . PHE   B 1 6   ? 43.864 -21.229 -16.542 1.00 18.90 ?  6   PHE   B CG   1 
ATOM   4018 C CD1  . PHE   B 1 6   ? 44.379 -21.728 -15.360 1.00 17.73 ?  6   PHE   B CD1  1 
ATOM   4019 C CD2  . PHE   B 1 6   ? 43.400 -19.922 -16.568 1.00 18.04 ?  6   PHE   B CD2  1 
ATOM   4020 C CE1  . PHE   B 1 6   ? 44.421 -20.938 -14.218 1.00 17.15 ?  6   PHE   B CE1  1 
ATOM   4021 C CE2  . PHE   B 1 6   ? 43.443 -19.129 -15.438 1.00 18.28 ?  6   PHE   B CE2  1 
ATOM   4022 C CZ   . PHE   B 1 6   ? 43.959 -19.627 -14.265 1.00 17.22 ?  6   PHE   B CZ   1 
ATOM   4023 H H    . PHE   B 1 6   ? 44.633 -20.202 -19.093 1.00 26.83 ?  6   PHE   B H    1 
ATOM   4024 H HA   . PHE   B 1 6   ? 45.836 -22.332 -18.053 1.00 26.46 ?  6   PHE   B HA   1 
ATOM   4025 H HB2  . PHE   B 1 6   ? 43.076 -21.771 -18.326 1.00 24.46 ?  6   PHE   B HB2  1 
ATOM   4026 H HB3  . PHE   B 1 6   ? 43.645 -22.999 -17.498 1.00 24.46 ?  6   PHE   B HB3  1 
ATOM   4027 H HD1  . PHE   B 1 6   ? 44.699 -22.602 -15.328 1.00 21.31 ?  6   PHE   B HD1  1 
ATOM   4028 H HD2  . PHE   B 1 6   ? 43.049 -19.579 -17.357 1.00 21.69 ?  6   PHE   B HD2  1 
ATOM   4029 H HE1  . PHE   B 1 6   ? 44.777 -21.278 -13.426 1.00 20.62 ?  6   PHE   B HE1  1 
ATOM   4030 H HE2  . PHE   B 1 6   ? 43.122 -18.256 -15.472 1.00 21.98 ?  6   PHE   B HE2  1 
ATOM   4031 H HZ   . PHE   B 1 6   ? 43.985 -19.097 -13.500 1.00 20.70 ?  6   PHE   B HZ   1 
ATOM   4032 N N    A SER   B 1 7   ? 45.660 -24.138 -19.692 0.72 27.24 ?  7   SER   B N    1 
ATOM   4033 N N    B SER   B 1 7   ? 45.660 -24.138 -19.712 0.28 26.90 ?  7   SER   B N    1 
ATOM   4034 C CA   A SER   B 1 7   ? 45.747 -25.108 -20.771 0.72 29.70 ?  7   SER   B CA   1 
ATOM   4035 C CA   B SER   B 1 7   ? 45.678 -25.080 -20.821 0.28 28.21 ?  7   SER   B CA   1 
ATOM   4036 C C    A SER   B 1 7   ? 45.698 -26.513 -20.190 0.72 29.05 ?  7   SER   B C    1 
ATOM   4037 C C    B SER   B 1 7   ? 45.593 -26.506 -20.299 0.28 27.80 ?  7   SER   B C    1 
ATOM   4038 O O    A SER   B 1 7   ? 46.310 -26.790 -19.155 0.72 29.87 ?  7   SER   B O    1 
ATOM   4039 O O    B SER   B 1 7   ? 46.225 -26.850 -19.296 0.28 28.12 ?  7   SER   B O    1 
ATOM   4040 C CB   A SER   B 1 7   ? 47.051 -24.922 -21.562 0.72 32.47 ?  7   SER   B CB   1 
ATOM   4041 C CB   B SER   B 1 7   ? 46.946 -24.913 -21.671 0.28 29.66 ?  7   SER   B CB   1 
ATOM   4042 O OG   A SER   B 1 7   ? 47.170 -25.882 -22.597 0.72 34.65 ?  7   SER   B OG   1 
ATOM   4043 O OG   B SER   B 1 7   ? 46.821 -25.594 -22.908 0.28 30.59 ?  7   SER   B OG   1 
ATOM   4044 H H    A SER   B 1 7   ? 46.096 -24.375 -18.988 0.72 32.72 ?  7   SER   B H    1 
ATOM   4045 H H    B SER   B 1 7   ? 46.122 -24.388 -19.029 0.28 32.31 ?  7   SER   B H    1 
ATOM   4046 H HA   A SER   B 1 7   ? 45.001 -24.999 -21.377 0.72 35.68 ?  7   SER   B HA   1 
ATOM   4047 H HA   B SER   B 1 7   ? 44.912 -24.924 -21.391 0.28 33.89 ?  7   SER   B HA   1 
ATOM   4048 H HB2  A SER   B 1 7   ? 47.057 -24.034 -21.958 0.72 39.01 ?  7   SER   B HB2  1 
ATOM   4049 H HB2  B SER   B 1 7   ? 47.087 -23.968 -21.845 0.28 35.63 ?  7   SER   B HB2  1 
ATOM   4050 H HB3  A SER   B 1 7   ? 47.806 -25.014 -20.957 0.72 39.01 ?  7   SER   B HB3  1 
ATOM   4051 H HB3  B SER   B 1 7   ? 47.704 -25.276 -21.186 0.28 35.63 ?  7   SER   B HB3  1 
ATOM   4052 H HG   A SER   B 1 7   ? 47.890 -25.765 -23.016 0.72 41.62 ?  7   SER   B HG   1 
ATOM   4053 H HG   B SER   B 1 7   ? 47.521 -25.494 -23.363 0.28 36.75 ?  7   SER   B HG   1 
ATOM   4054 N N    A GLY   B 1 8   ? 44.963 -27.396 -20.859 0.72 28.46 ?  8   GLY   B N    1 
ATOM   4055 N N    B GLY   B 1 8   ? 44.806 -27.329 -20.987 0.28 27.20 ?  8   GLY   B N    1 
ATOM   4056 C CA   A GLY   B 1 8   ? 44.938 -28.787 -20.469 0.72 27.30 ?  8   GLY   B CA   1 
ATOM   4057 C CA   B GLY   B 1 8   ? 44.722 -28.735 -20.654 0.28 26.38 ?  8   GLY   B CA   1 
ATOM   4058 C C    A GLY   B 1 8   ? 44.014 -29.114 -19.326 0.72 25.95 ?  8   GLY   B C    1 
ATOM   4059 C C    B GLY   B 1 8   ? 43.855 -29.062 -19.462 0.28 25.52 ?  8   GLY   B C    1 
ATOM   4060 O O    A GLY   B 1 8   ? 44.174 -30.172 -18.705 0.72 27.56 ?  8   GLY   B O    1 
ATOM   4061 O O    B GLY   B 1 8   ? 44.065 -30.098 -18.823 0.28 26.23 ?  8   GLY   B O    1 
ATOM   4062 H H    A GLY   B 1 8   ? 44.476 -27.205 -21.536 0.72 34.19 ?  8   GLY   B H    1 
ATOM   4063 H H    B GLY   B 1 8   ? 44.318 -27.091 -21.653 0.28 32.68 ?  8   GLY   B H    1 
ATOM   4064 H HA2  A GLY   B 1 8   ? 44.664 -29.321 -21.226 0.72 32.80 ?  8   GLY   B HA2  1 
ATOM   4065 H HA2  B GLY   B 1 8   ? 44.366 -29.217 -21.414 0.28 31.70 ?  8   GLY   B HA2  1 
ATOM   4066 H HA3  A GLY   B 1 8   ? 45.832 -29.061 -20.211 0.72 32.80 ?  8   GLY   B HA3  1 
ATOM   4067 H HA3  B GLY   B 1 8   ? 45.614 -29.071 -20.475 0.28 31.70 ?  8   GLY   B HA3  1 
ATOM   4068 N N    A TYR   B 1 9   ? 43.033 -28.263 -19.038 0.72 23.88 ?  9   TYR   B N    1 
ATOM   4069 N N    B TYR   B 1 9   ? 42.875 -28.221 -19.149 0.28 24.02 ?  9   TYR   B N    1 
ATOM   4070 C CA   A TYR   B 1 9   ? 42.097 -28.538 -17.961 0.72 21.81 ?  9   TYR   B CA   1 
ATOM   4071 C CA   B TYR   B 1 9   ? 41.984 -28.481 -18.029 0.28 22.49 ?  9   TYR   B CA   1 
ATOM   4072 C C    A TYR   B 1 9   ? 40.907 -29.334 -18.462 0.72 21.27 ?  9   TYR   B C    1 
ATOM   4073 C C    B TYR   B 1 9   ? 40.761 -29.263 -18.482 0.28 22.29 ?  9   TYR   B C    1 
ATOM   4074 O O    A TYR   B 1 9   ? 40.490 -29.219 -19.618 0.72 22.47 ?  9   TYR   B O    1 
ATOM   4075 O O    B TYR   B 1 9   ? 40.256 -29.085 -19.595 0.28 22.68 ?  9   TYR   B O    1 
ATOM   4076 C CB   A TYR   B 1 9   ? 41.604 -27.251 -17.304 0.72 21.06 ?  9   TYR   B CB   1 
ATOM   4077 C CB   B TYR   B 1 9   ? 41.525 -27.180 -17.377 0.28 21.47 ?  9   TYR   B CB   1 
ATOM   4078 C CG   A TYR   B 1 9   ? 42.639 -26.640 -16.393 0.72 20.53 ?  9   TYR   B CG   1 
ATOM   4079 C CG   B TYR   B 1 9   ? 42.560 -26.562 -16.471 0.28 20.60 ?  9   TYR   B CG   1 
ATOM   4080 C CD1  A TYR   B 1 9   ? 43.747 -25.988 -16.914 0.72 20.80 ?  9   TYR   B CD1  1 
ATOM   4081 C CD1  B TYR   B 1 9   ? 43.637 -25.865 -16.995 0.28 20.39 ?  9   TYR   B CD1  1 
ATOM   4082 C CD2  A TYR   B 1 9   ? 42.523 -26.729 -15.014 0.72 19.97 ?  9   TYR   B CD2  1 
ATOM   4083 C CD2  B TYR   B 1 9   ? 42.462 -26.677 -15.091 0.28 19.94 ?  9   TYR   B CD2  1 
ATOM   4084 C CE1  A TYR   B 1 9   ? 44.712 -25.440 -16.089 0.72 21.05 ?  9   TYR   B CE1  1 
ATOM   4085 C CE1  B TYR   B 1 9   ? 44.591 -25.299 -16.172 0.28 20.25 ?  9   TYR   B CE1  1 
ATOM   4086 C CE2  A TYR   B 1 9   ? 43.484 -26.180 -14.179 0.72 20.18 ?  9   TYR   B CE2  1 
ATOM   4087 C CE2  B TYR   B 1 9   ? 43.414 -26.116 -14.258 0.28 19.78 ?  9   TYR   B CE2  1 
ATOM   4088 C CZ   A TYR   B 1 9   ? 44.576 -25.530 -14.723 0.72 20.80 ?  9   TYR   B CZ   1 
ATOM   4089 C CZ   B TYR   B 1 9   ? 44.475 -25.425 -14.806 0.28 19.96 ?  9   TYR   B CZ   1 
ATOM   4090 O OH   A TYR   B 1 9   ? 45.534 -24.992 -13.898 0.72 21.26 ?  9   TYR   B OH   1 
ATOM   4091 O OH   B TYR   B 1 9   ? 45.425 -24.863 -13.985 0.28 20.15 ?  9   TYR   B OH   1 
ATOM   4092 H H    A TYR   B 1 9   ? 42.874 -27.532 -19.464 0.72 28.69 ?  9   TYR   B H    1 
ATOM   4093 H H    B TYR   B 1 9   ? 42.702 -27.493 -19.574 0.28 28.86 ?  9   TYR   B H    1 
ATOM   4094 H HA   A TYR   B 1 9   ? 42.536 -29.066 -17.281 0.72 26.21 ?  9   TYR   B HA   1 
ATOM   4095 H HA   B TYR   B 1 9   ? 42.449 -29.006 -17.361 0.28 27.03 ?  9   TYR   B HA   1 
ATOM   4096 H HB2  A TYR   B 1 9   ? 41.378 -26.601 -17.987 0.72 25.31 ?  9   TYR   B HB2  1 
ATOM   4097 H HB2  B TYR   B 1 9   ? 41.300 -26.534 -18.065 0.28 25.80 ?  9   TYR   B HB2  1 
ATOM   4098 H HB3  A TYR   B 1 9   ? 40.823 -27.457 -16.768 0.72 25.31 ?  9   TYR   B HB3  1 
ATOM   4099 H HB3  B TYR   B 1 9   ? 40.747 -27.378 -16.839 0.28 25.80 ?  9   TYR   B HB3  1 
ATOM   4100 H HD1  A TYR   B 1 9   ? 43.843 -25.926 -17.837 0.72 25.00 ?  9   TYR   B HD1  1 
ATOM   4101 H HD1  B TYR   B 1 9   ? 43.720 -25.779 -17.916 0.28 24.51 ?  9   TYR   B HD1  1 
ATOM   4102 H HD2  A TYR   B 1 9   ? 41.783 -27.167 -14.644 0.72 24.00 ?  9   TYR   B HD2  1 
ATOM   4103 H HD2  B TYR   B 1 9   ? 41.745 -27.142 -14.719 0.28 23.97 ?  9   TYR   B HD2  1 
ATOM   4104 H HE1  A TYR   B 1 9   ? 45.441 -25.008 -16.457 0.72 25.30 ?  9   TYR   B HE1  1 
ATOM   4105 H HE1  B TYR   B 1 9   ? 45.308 -24.837 -16.538 0.28 24.34 ?  9   TYR   B HE1  1 
ATOM   4106 H HE2  A TYR   B 1 9   ? 43.381 -26.249 -13.255 0.72 24.26 ?  9   TYR   B HE2  1 
ATOM   4107 H HE2  B TYR   B 1 9   ? 43.333 -26.201 -13.334 0.28 23.77 ?  9   TYR   B HE2  1 
ATOM   4108 H HH   A TYR   B 1 9   ? 46.126 -24.635 -14.361 0.72 25.56 ?  9   TYR   B HH   1 
ATOM   4109 H HH   B TYR   B 1 9   ? 46.008 -24.479 -14.449 0.28 24.22 ?  9   TYR   B HH   1 
ATOM   4110 N N    A LEU   B 1 10  ? 40.374 -30.164 -17.570 0.72 20.01 ?  10  LEU   B N    1 
ATOM   4111 N N    B LEU   B 1 10  ? 40.284 -30.133 -17.597 0.28 22.04 ?  10  LEU   B N    1 
ATOM   4112 C CA   A LEU   B 1 10  ? 39.167 -30.929 -17.825 0.72 19.91 ?  10  LEU   B CA   1 
ATOM   4113 C CA   B LEU   B 1 10  ? 39.071 -30.899 -17.835 0.28 22.19 ?  10  LEU   B CA   1 
ATOM   4114 C C    A LEU   B 1 10  ? 37.981 -30.157 -17.269 0.72 19.52 ?  10  LEU   B C    1 
ATOM   4115 C C    B LEU   B 1 10  ? 37.883 -30.123 -17.284 0.28 21.99 ?  10  LEU   B C    1 
ATOM   4116 O O    A LEU   B 1 10  ? 37.994 -29.737 -16.107 0.72 19.10 ?  10  LEU   B O    1 
ATOM   4117 O O    B LEU   B 1 10  ? 37.898 -29.691 -16.127 0.28 21.61 ?  10  LEU   B O    1 
ATOM   4118 C CB   A LEU   B 1 10  ? 39.266 -32.291 -17.138 0.72 21.00 ?  10  LEU   B CB   1 
ATOM   4119 C CB   B LEU   B 1 10  ? 39.164 -32.259 -17.144 0.28 22.92 ?  10  LEU   B CB   1 
ATOM   4120 C CG   A LEU   B 1 10  ? 38.129 -33.265 -17.446 0.72 22.50 ?  10  LEU   B CG   1 
ATOM   4121 C CG   B LEU   B 1 10  ? 38.058 -33.250 -17.502 0.28 23.70 ?  10  LEU   B CG   1 
ATOM   4122 C CD1  A LEU   B 1 10  ? 38.222 -33.742 -18.888 0.72 23.63 ?  10  LEU   B CD1  1 
ATOM   4123 C CD1  B LEU   B 1 10  ? 38.267 -33.801 -18.905 0.28 24.10 ?  10  LEU   B CD1  1 
ATOM   4124 C CD2  A LEU   B 1 10  ? 38.132 -34.439 -16.481 0.72 23.46 ?  10  LEU   B CD2  1 
ATOM   4125 C CD2  B LEU   B 1 10  ? 37.989 -34.372 -16.482 0.28 24.04 ?  10  LEU   B CD2  1 
ATOM   4126 H H    A LEU   B 1 10  ? 40.695 -30.297 -16.780 0.72 24.05 ?  10  LEU   B H    1 
ATOM   4127 H H    B LEU   B 1 10  ? 40.651 -30.298 -16.835 0.28 26.48 ?  10  LEU   B H    1 
ATOM   4128 H HA   A LEU   B 1 10  ? 39.040 -31.059 -18.775 0.72 23.93 ?  10  LEU   B HA   1 
ATOM   4129 H HA   B LEU   B 1 10  ? 38.946 -31.035 -18.786 0.28 26.67 ?  10  LEU   B HA   1 
ATOM   4130 H HB2  A LEU   B 1 10  ? 40.095 -32.711 -17.413 0.72 25.23 ?  10  LEU   B HB2  1 
ATOM   4131 H HB2  B LEU   B 1 10  ? 40.010 -32.667 -17.384 0.28 27.54 ?  10  LEU   B HB2  1 
ATOM   4132 H HB3  A LEU   B 1 10  ? 39.279 -32.152 -16.175 0.72 25.23 ?  10  LEU   B HB3  1 
ATOM   4133 H HB3  B LEU   B 1 10  ? 39.132 -32.120 -16.185 0.28 27.54 ?  10  LEU   B HB3  1 
ATOM   4134 H HG   A LEU   B 1 10  ? 37.284 -32.801 -17.341 0.72 27.04 ?  10  LEU   B HG   1 
ATOM   4135 H HG   B LEU   B 1 10  ? 37.206 -32.788 -17.489 0.28 28.48 ?  10  LEU   B HG   1 
ATOM   4136 H HD11 A LEU   B 1 10  ? 37.547 -34.421 -19.037 0.72 28.40 ?  10  LEU   B HD11 1 
ATOM   4137 H HD11 B LEU   B 1 10  ? 37.578 -34.458 -19.091 0.28 28.95 ?  10  LEU   B HD11 1 
ATOM   4138 H HD12 A LEU   B 1 10  ? 38.069 -32.987 -19.479 0.72 28.40 ?  10  LEU   B HD12 1 
ATOM   4139 H HD12 B LEU   B 1 10  ? 38.210 -33.072 -19.542 0.28 28.95 ?  10  LEU   B HD12 1 
ATOM   4140 H HD13 A LEU   B 1 10  ? 39.105 -34.110 -19.041 0.72 28.40 ?  10  LEU   B HD13 1 
ATOM   4141 H HD13 B LEU   B 1 10  ? 39.142 -34.216 -18.954 0.28 28.95 ?  10  LEU   B HD13 1 
ATOM   4142 H HD21 A LEU   B 1 10  ? 37.399 -35.031 -16.709 0.72 28.19 ?  10  LEU   B HD21 1 
ATOM   4143 H HD21 B LEU   B 1 10  ? 37.283 -34.985 -16.739 0.28 28.89 ?  10  LEU   B HD21 1 
ATOM   4144 H HD22 A LEU   B 1 10  ? 38.976 -34.906 -16.559 0.72 28.19 ?  10  LEU   B HD22 1 
ATOM   4145 H HD22 B LEU   B 1 10  ? 38.841 -34.832 -16.464 0.28 28.89 ?  10  LEU   B HD22 1 
ATOM   4146 H HD23 A LEU   B 1 10  ? 38.018 -34.102 -15.578 0.72 28.19 ?  10  LEU   B HD23 1 
ATOM   4147 H HD23 B LEU   B 1 10  ? 37.797 -33.991 -15.611 0.28 28.89 ?  10  LEU   B HD23 1 
ATOM   4148 N N    A LYS   B 1 11  ? 36.965 -29.966 -18.102 0.72 20.77 ?  11  LYS   B N    1 
ATOM   4149 N N    B LYS   B 1 11  ? 36.862 -29.946 -18.116 0.28 22.57 ?  11  LYS   B N    1 
ATOM   4150 C CA   A LYS   B 1 11  ? 35.757 -29.274 -17.687 0.72 23.01 ?  11  LYS   B CA   1 
ATOM   4151 C CA   B LYS   B 1 11  ? 35.668 -29.208 -17.727 0.28 23.53 ?  11  LYS   B CA   1 
ATOM   4152 C C    A LYS   B 1 11  ? 34.922 -30.204 -16.815 0.72 21.73 ?  11  LYS   B C    1 
ATOM   4153 C C    B LYS   B 1 11  ? 34.762 -30.104 -16.889 0.28 21.80 ?  11  LYS   B C    1 
ATOM   4154 O O    A LYS   B 1 11  ? 34.643 -31.347 -17.199 0.72 23.06 ?  11  LYS   B O    1 
ATOM   4155 O O    B LYS   B 1 11  ? 34.256 -31.117 -17.384 0.28 21.92 ?  11  LYS   B O    1 
ATOM   4156 C CB   A LYS   B 1 11  ? 34.973 -28.861 -18.935 0.72 27.10 ?  11  LYS   B CB   1 
ATOM   4157 C CB   B LYS   B 1 11  ? 34.932 -28.754 -18.984 0.28 26.36 ?  11  LYS   B CB   1 
ATOM   4158 C CG   A LYS   B 1 11  ? 33.921 -27.792 -18.718 0.72 30.82 ?  11  LYS   B CG   1 
ATOM   4159 C CG   B LYS   B 1 11  ? 33.831 -27.742 -18.744 0.28 28.98 ?  11  LYS   B CG   1 
ATOM   4160 C CD   A LYS   B 1 11  ? 33.211 -27.474 -20.029 0.72 33.62 ?  11  LYS   B CD   1 
ATOM   4161 C CD   B LYS   B 1 11  ? 33.121 -27.400 -20.043 0.28 31.06 ?  11  LYS   B CD   1 
ATOM   4162 C CE   A LYS   B 1 11  ? 32.192 -26.358 -19.865 0.72 35.65 ?  11  LYS   B CE   1 
ATOM   4163 C CE   B LYS   B 1 11  ? 32.105 -26.289 -19.849 0.28 32.55 ?  11  LYS   B CE   1 
ATOM   4164 N NZ   A LYS   B 1 11  ? 32.838 -25.043 -19.605 0.72 36.77 ?  11  LYS   B NZ   1 
ATOM   4165 N NZ   B LYS   B 1 11  ? 32.756 -24.998 -19.495 0.28 33.35 ?  11  LYS   B NZ   1 
ATOM   4166 H H    A LYS   B 1 11  ? 36.944 -30.237 -18.920 0.72 24.96 ?  11  LYS   B H    1 
ATOM   4167 H H    B LYS   B 1 11  ? 36.841 -30.240 -18.926 0.28 27.12 ?  11  LYS   B H    1 
ATOM   4168 H HA   A LYS   B 1 11  ? 35.983 -28.478 -17.182 0.72 27.65 ?  11  LYS   B HA   1 
ATOM   4169 H HA   B LYS   B 1 11  ? 35.916 -28.427 -17.205 0.28 28.28 ?  11  LYS   B HA   1 
ATOM   4170 H HB2  A LYS   B 1 11  ? 35.600 -28.515 -19.593 0.72 32.56 ?  11  LYS   B HB2  1 
ATOM   4171 H HB2  B LYS   B 1 11  ? 35.572 -28.352 -19.590 0.28 31.67 ?  11  LYS   B HB2  1 
ATOM   4172 H HB3  A LYS   B 1 11  ? 34.524 -29.639 -19.295 0.72 32.56 ?  11  LYS   B HB3  1 
ATOM   4173 H HB3  B LYS   B 1 11  ? 34.528 -29.531 -19.402 0.28 31.67 ?  11  LYS   B HB3  1 
ATOM   4174 H HG2  A LYS   B 1 11  ? 33.262 -28.111 -18.083 0.72 37.02 ?  11  LYS   B HG2  1 
ATOM   4175 H HG2  B LYS   B 1 11  ? 33.181 -28.114 -18.128 0.28 34.82 ?  11  LYS   B HG2  1 
ATOM   4176 H HG3  A LYS   B 1 11  ? 34.342 -26.981 -18.394 0.72 37.02 ?  11  LYS   B HG3  1 
ATOM   4177 H HG3  B LYS   B 1 11  ? 34.216 -26.930 -18.381 0.28 34.82 ?  11  LYS   B HG3  1 
ATOM   4178 H HD2  A LYS   B 1 11  ? 33.867 -27.192 -20.687 0.72 40.39 ?  11  LYS   B HD2  1 
ATOM   4179 H HD2  B LYS   B 1 11  ? 33.775 -27.104 -20.696 0.28 37.31 ?  11  LYS   B HD2  1 
ATOM   4180 H HD3  A LYS   B 1 11  ? 32.747 -28.267 -20.341 0.72 40.39 ?  11  LYS   B HD3  1 
ATOM   4181 H HD3  B LYS   B 1 11  ? 32.655 -28.186 -20.369 0.28 37.31 ?  11  LYS   B HD3  1 
ATOM   4182 H HE2  A LYS   B 1 11  ? 31.669 -26.283 -20.678 0.72 42.81 ?  11  LYS   B HE2  1 
ATOM   4183 H HE2  B LYS   B 1 11  ? 31.609 -26.162 -20.672 0.28 39.10 ?  11  LYS   B HE2  1 
ATOM   4184 H HE3  A LYS   B 1 11  ? 31.614 -26.567 -19.115 0.72 42.81 ?  11  LYS   B HE3  1 
ATOM   4185 H HE3  B LYS   B 1 11  ? 31.502 -26.535 -19.130 0.28 39.10 ?  11  LYS   B HE3  1 
ATOM   4186 H HZ1  A LYS   B 1 11  ? 32.217 -24.412 -19.518 0.72 44.16 ?  11  LYS   B HZ1  1 
ATOM   4187 H HZ1  B LYS   B 1 11  ? 32.144 -24.354 -19.442 0.28 40.06 ?  11  LYS   B HZ1  1 
ATOM   4188 H HZ2  A LYS   B 1 11  ? 33.318 -25.083 -18.858 0.72 44.16 ?  11  LYS   B HZ2  1 
ATOM   4189 H HZ2  B LYS   B 1 11  ? 33.169 -25.070 -18.710 0.28 40.06 ?  11  LYS   B HZ2  1 
ATOM   4190 H HZ3  A LYS   B 1 11  ? 33.374 -24.830 -20.283 0.72 44.16 ?  11  LYS   B HZ3  1 
ATOM   4191 H HZ3  B LYS   B 1 11  ? 33.353 -24.779 -20.117 0.28 40.06 ?  11  LYS   B HZ3  1 
ATOM   4192 N N    . LEU   B 1 12  ? 34.543 -29.725 -15.629 1.00 20.24 ?  12  LEU   B N    1 
ATOM   4193 C CA   . LEU   B 1 12  ? 33.598 -30.439 -14.774 1.00 19.04 ?  12  LEU   B CA   1 
ATOM   4194 C C    . LEU   B 1 12  ? 32.212 -29.822 -14.850 1.00 19.13 ?  12  LEU   B C    1 
ATOM   4195 O O    . LEU   B 1 12  ? 31.223 -30.531 -15.020 1.00 19.70 ?  12  LEU   B O    1 
ATOM   4196 C CB   . LEU   B 1 12  ? 34.068 -30.474 -13.315 1.00 18.33 ?  12  LEU   B CB   1 
ATOM   4197 C CG   . LEU   B 1 12  ? 35.409 -31.150 -13.057 1.00 18.41 ?  12  LEU   B CG   1 
ATOM   4198 C CD1  . LEU   B 1 12  ? 35.770 -31.080 -11.582 1.00 18.65 ?  12  LEU   B CD1  1 
ATOM   4199 C CD2  . LEU   B 1 12  ? 35.404 -32.591 -13.545 1.00 19.06 ?  12  LEU   B CD2  1 
ATOM   4200 H H    A LEU   B 1 12  ? 34.825 -28.982 -15.295 0.72 24.33 ?  12  LEU   B H    1 
ATOM   4201 H H    B LEU   B 1 12  ? 34.911 -29.043 -15.254 0.28 24.33 ?  12  LEU   B H    1 
ATOM   4202 H HA   . LEU   B 1 12  ? 33.521 -31.350 -15.082 1.00 22.89 ?  12  LEU   B HA   1 
ATOM   4203 H HB2  . LEU   B 1 12  ? 34.131 -29.563 -12.992 1.00 22.03 ?  12  LEU   B HB2  1 
ATOM   4204 H HB3  . LEU   B 1 12  ? 33.397 -30.951 -12.795 1.00 22.03 ?  12  LEU   B HB3  1 
ATOM   4205 H HG   . LEU   B 1 12  ? 36.090 -30.672 -13.551 1.00 22.13 ?  12  LEU   B HG   1 
ATOM   4206 H HD11 . LEU   B 1 12  ? 36.628 -31.513 -11.448 1.00 22.42 ?  12  LEU   B HD11 1 
ATOM   4207 H HD12 . LEU   B 1 12  ? 35.825 -30.148 -11.313 1.00 22.42 ?  12  LEU   B HD12 1 
ATOM   4208 H HD13 . LEU   B 1 12  ? 35.087 -31.533 -11.065 1.00 22.42 ?  12  LEU   B HD13 1 
ATOM   4209 H HD21 . LEU   B 1 12  ? 36.221 -33.024 -13.256 1.00 22.91 ?  12  LEU   B HD21 1 
ATOM   4210 H HD22 . LEU   B 1 12  ? 34.635 -33.050 -13.171 1.00 22.91 ?  12  LEU   B HD22 1 
ATOM   4211 H HD23 . LEU   B 1 12  ? 35.352 -32.596 -14.515 1.00 22.91 ?  12  LEU   B HD23 1 
ATOM   4212 N N    . THR   B 1 13  ? 32.133 -28.506 -14.723 1.00 19.13 ?  13  THR   B N    1 
ATOM   4213 C CA   . THR   B 1 13  ? 30.913 -27.751 -14.932 1.00 19.34 ?  13  THR   B CA   1 
ATOM   4214 C C    . THR   B 1 13  ? 31.263 -26.571 -15.831 1.00 21.81 ?  13  THR   B C    1 
ATOM   4215 O O    . THR   B 1 13  ? 32.413 -26.400 -16.252 1.00 22.75 ?  13  THR   B O    1 
ATOM   4216 C CB   . THR   B 1 13  ? 30.325 -27.257 -13.607 1.00 18.60 ?  13  THR   B CB   1 
ATOM   4217 O OG1  . THR   B 1 13  ? 31.189 -26.250 -13.066 1.00 18.06 ?  13  THR   B OG1  1 
ATOM   4218 C CG2  . THR   B 1 13  ? 30.188 -28.397 -12.604 1.00 19.12 ?  13  THR   B CG2  1 
ATOM   4219 H H    . THR   B 1 13  ? 32.797 -28.012 -14.500 1.00 23.00 ?  13  THR   B H    1 
ATOM   4220 H HA   . THR   B 1 13  ? 30.248 -28.306 -15.374 1.00 23.24 ?  13  THR   B HA   1 
ATOM   4221 H HB   . THR   B 1 13  ? 29.440 -26.875 -13.761 1.00 22.36 ?  13  THR   B HB   1 
ATOM   4222 H HG1  . THR   B 1 13  ? 30.890 -25.478 -13.258 1.00 21.71 ?  13  THR   B HG1  1 
ATOM   4223 H HG21 . THR   B 1 13  ? 29.693 -28.095 -11.824 1.00 22.98 ?  13  THR   B HG21 1 
ATOM   4224 H HG22 . THR   B 1 13  ? 29.712 -29.136 -13.010 1.00 22.98 ?  13  THR   B HG22 1 
ATOM   4225 H HG23 . THR   B 1 13  ? 31.064 -28.697 -12.324 1.00 22.98 ?  13  THR   B HG23 1 
ATOM   4226 N N    A ASP   B 1 14  ? 30.262 -25.741 -16.119 0.72 22.71 ?  14  ASP   B N    1 
ATOM   4227 N N    B ASP   B 1 14  ? 30.265 -25.729 -16.108 0.28 22.73 ?  14  ASP   B N    1 
ATOM   4228 C CA   A ASP   B 1 14  ? 30.507 -24.591 -16.979 0.72 24.27 ?  14  ASP   B CA   1 
ATOM   4229 C CA   B ASP   B 1 14  ? 30.493 -24.580 -16.978 0.28 23.77 ?  14  ASP   B CA   1 
ATOM   4230 C C    A ASP   B 1 14  ? 31.614 -23.697 -16.434 0.72 22.27 ?  14  ASP   B C    1 
ATOM   4231 C C    B ASP   B 1 14  ? 31.521 -23.608 -16.416 0.28 21.80 ?  14  ASP   B C    1 
ATOM   4232 O O    A ASP   B 1 14  ? 32.314 -23.044 -17.218 0.72 23.71 ?  14  ASP   B O    1 
ATOM   4233 O O    B ASP   B 1 14  ? 32.047 -22.786 -17.174 0.28 22.20 ?  14  ASP   B O    1 
ATOM   4234 C CB   A ASP   B 1 14  ? 29.220 -23.792 -17.180 0.72 28.30 ?  14  ASP   B CB   1 
ATOM   4235 C CB   B ASP   B 1 14  ? 29.186 -23.831 -17.234 0.28 26.83 ?  14  ASP   B CB   1 
ATOM   4236 C CG   A ASP   B 1 14  ? 28.232 -24.493 -18.087 0.72 32.18 ?  14  ASP   B CG   1 
ATOM   4237 C CG   B ASP   B 1 14  ? 28.273 -24.562 -18.199 0.28 29.42 ?  14  ASP   B CG   1 
ATOM   4238 O OD1  A ASP   B 1 14  ? 28.643 -25.394 -18.850 0.72 33.56 ?  14  ASP   B OD1  1 
ATOM   4239 O OD1  B ASP   B 1 14  ? 28.789 -25.285 -19.077 0.28 30.22 ?  14  ASP   B OD1  1 
ATOM   4240 O OD2  A ASP   B 1 14  ? 27.036 -24.141 -18.033 0.72 33.79 -1 14  ASP   B OD2  1 
ATOM   4241 O OD2  B ASP   B 1 14  ? 27.039 -24.416 -18.080 0.28 30.47 -1 14  ASP   B OD2  1 
ATOM   4242 H H    A ASP   B 1 14  ? 29.458 -25.807 -15.826 0.72 27.29 ?  14  ASP   B H    1 
ATOM   4243 H H    B ASP   B 1 14  ? 29.463 -25.796 -15.809 0.28 27.31 ?  14  ASP   B H    1 
ATOM   4244 H HA   A ASP   B 1 14  ? 30.801 -24.904 -17.846 0.72 29.16 ?  14  ASP   B HA   1 
ATOM   4245 H HA   B ASP   B 1 14  ? 30.824 -24.898 -17.829 0.28 28.57 ?  14  ASP   B HA   1 
ATOM   4246 H HB2  A ASP   B 1 14  ? 28.780 -23.674 -16.327 0.72 34.00 ?  14  ASP   B HB2  1 
ATOM   4247 H HB2  B ASP   B 1 14  ? 28.712 -23.730 -16.395 0.28 32.24 ?  14  ASP   B HB2  1 
ATOM   4248 H HB3  A ASP   B 1 14  ? 29.435 -22.929 -17.569 0.72 34.00 ?  14  ASP   B HB3  1 
ATOM   4249 H HB3  B ASP   B 1 14  ? 29.395 -22.955 -17.603 0.28 32.24 ?  14  ASP   B HB3  1 
ATOM   4250 N N    . ASN   B 1 15  ? 31.801 -23.659 -15.109 1.00 19.80 ?  15  ASN   B N    1 
ATOM   4251 C CA   . ASN   B 1 15  ? 32.770 -22.747 -14.499 1.00 17.17 ?  15  ASN   B CA   1 
ATOM   4252 C C    . ASN   B 1 15  ? 33.860 -23.412 -13.669 1.00 15.78 ?  15  ASN   B C    1 
ATOM   4253 O O    . ASN   B 1 15  ? 34.739 -22.698 -13.172 1.00 15.75 ?  15  ASN   B O    1 
ATOM   4254 C CB   . ASN   B 1 15  ? 32.065 -21.691 -13.629 1.00 16.92 ?  15  ASN   B CB   1 
ATOM   4255 C CG   . ASN   B 1 15  ? 31.446 -22.292 -12.384 1.00 16.72 ?  15  ASN   B CG   1 
ATOM   4256 O OD1  . ASN   B 1 15  ? 30.494 -23.079 -12.468 1.00 18.63 ?  15  ASN   B OD1  1 
ATOM   4257 N ND2  . ASN   B 1 15  ? 31.988 -21.955 -11.226 1.00 15.89 ?  15  ASN   B ND2  1 
ATOM   4258 H H    A ASN   B 1 15  ? 31.369 -24.145 -14.543 0.72 23.80 ?  15  ASN   B H    1 
ATOM   4259 H H    B ASN   B 1 15  ? 31.415 -24.189 -14.550 0.28 23.80 ?  15  ASN   B H    1 
ATOM   4260 H HA   . ASN   B 1 15  ? 33.213 -22.260 -15.202 1.00 20.64 ?  15  ASN   B HA   1 
ATOM   4261 H HB2  . ASN   B 1 15  ? 32.715 -21.015 -13.354 1.00 20.35 ?  15  ASN   B HB2  1 
ATOM   4262 H HB3  . ASN   B 1 15  ? 31.356 -21.262 -14.142 1.00 20.35 ?  15  ASN   B HB3  1 
ATOM   4263 H HD21 . ASN   B 1 15  ? 31.671 -22.263 -10.489 1.00 19.11 ?  15  ASN   B HD21 1 
ATOM   4264 H HD22 . ASN   B 1 15  ? 32.665 -21.410 -11.198 1.00 19.11 ?  15  ASN   B HD22 1 
ATOM   4265 N N    . VAL   B 1 16  ? 33.837 -24.731 -13.485 1.00 15.53 ?  16  VAL   B N    1 
ATOM   4266 C CA   . VAL   B 1 16  ? 34.844 -25.422 -12.683 1.00 15.45 ?  16  VAL   B CA   1 
ATOM   4267 C C    . VAL   B 1 16  ? 35.631 -26.358 -13.584 1.00 15.44 ?  16  VAL   B C    1 
ATOM   4268 O O    . VAL   B 1 16  ? 35.052 -27.239 -14.240 1.00 16.40 ?  16  VAL   B O    1 
ATOM   4269 C CB   . VAL   B 1 16  ? 34.228 -26.191 -11.505 1.00 15.74 ?  16  VAL   B CB   1 
ATOM   4270 C CG1  . VAL   B 1 16  ? 35.322 -26.932 -10.723 1.00 15.84 ?  16  VAL   B CG1  1 
ATOM   4271 C CG2  . VAL   B 1 16  ? 33.431 -25.252 -10.602 1.00 16.63 ?  16  VAL   B CG2  1 
ATOM   4272 H H    . VAL   B 1 16  ? 33.229 -25.251 -13.810 1.00 18.67 ?  16  VAL   B H    1 
ATOM   4273 H HA   . VAL   B 1 16  ? 35.455 -24.765 -12.318 1.00 18.58 ?  16  VAL   B HA   1 
ATOM   4274 H HB   . VAL   B 1 16  ? 33.612 -26.860 -11.854 1.00 18.93 ?  16  VAL   B HB   1 
ATOM   4275 H HG11 . VAL   B 1 16  ? 34.950 -27.235 -9.878  1.00 19.04 ?  16  VAL   B HG11 1 
ATOM   4276 H HG12 . VAL   B 1 16  ? 35.624 -27.691 -11.241 1.00 19.04 ?  16  VAL   B HG12 1 
ATOM   4277 H HG13 . VAL   B 1 16  ? 36.056 -26.321 -10.560 1.00 19.04 ?  16  VAL   B HG13 1 
ATOM   4278 H HG21 . VAL   B 1 16  ? 33.096 -25.756 -9.840  1.00 19.99 ?  16  VAL   B HG21 1 
ATOM   4279 H HG22 . VAL   B 1 16  ? 34.005 -24.538 -10.301 1.00 19.99 ?  16  VAL   B HG22 1 
ATOM   4280 H HG23 . VAL   B 1 16  ? 32.682 -24.890 -11.106 1.00 19.99 ?  16  VAL   B HG23 1 
ATOM   4281 N N    . TYR   B 1 17  ? 36.951 -26.184 -13.578 1.00 15.93 ?  17  TYR   B N    1 
ATOM   4282 C CA   . TYR   B 1 17  ? 37.892 -26.938 -14.389 1.00 16.39 ?  17  TYR   B CA   1 
ATOM   4283 C C    . TYR   B 1 17  ? 38.952 -27.551 -13.483 1.00 15.07 ?  17  TYR   B C    1 
ATOM   4284 O O    . TYR   B 1 17  ? 39.243 -27.027 -12.407 1.00 15.73 ?  17  TYR   B O    1 
ATOM   4285 C CB   . TYR   B 1 17  ? 38.595 -26.018 -15.399 1.00 20.07 ?  17  TYR   B CB   1 
ATOM   4286 C CG   . TYR   B 1 17  ? 37.671 -25.240 -16.304 1.00 24.16 ?  17  TYR   B CG   1 
ATOM   4287 C CD1  . TYR   B 1 17  ? 37.112 -24.037 -15.896 1.00 26.19 ?  17  TYR   B CD1  1 
ATOM   4288 C CD2  . TYR   B 1 17  ? 37.367 -25.707 -17.576 1.00 26.44 ?  17  TYR   B CD2  1 
ATOM   4289 C CE1  . TYR   B 1 17  ? 36.266 -23.321 -16.728 1.00 28.04 ?  17  TYR   B CE1  1 
ATOM   4290 C CE2  . TYR   B 1 17  ? 36.527 -25.001 -18.414 1.00 28.08 ?  17  TYR   B CE2  1 
ATOM   4291 C CZ   . TYR   B 1 17  ? 35.977 -23.810 -17.985 1.00 29.10 ?  17  TYR   B CZ   1 
ATOM   4292 O OH   . TYR   B 1 17  ? 35.141 -23.106 -18.820 1.00 30.53 ?  17  TYR   B OH   1 
ATOM   4293 H H    . TYR   B 1 17  ? 37.344 -25.591 -13.084 1.00 19.16 ?  17  TYR   B H    1 
ATOM   4294 H HA   . TYR   B 1 17  ? 37.420 -27.639 -14.870 1.00 19.70 ?  17  TYR   B HA   1 
ATOM   4295 H HB2  . TYR   B 1 17  ? 39.154 -25.387 -14.922 1.00 24.12 ?  17  TYR   B HB2  1 
ATOM   4296 H HB3  . TYR   B 1 17  ? 39.136 -26.572 -15.971 1.00 24.12 ?  17  TYR   B HB3  1 
ATOM   4297 H HD1  . TYR   B 1 17  ? 37.306 -23.707 -15.050 1.00 31.46 ?  17  TYR   B HD1  1 
ATOM   4298 H HD2  . TYR   B 1 17  ? 37.731 -26.510 -17.870 1.00 31.77 ?  17  TYR   B HD2  1 
ATOM   4299 H HE1  . TYR   B 1 17  ? 35.898 -22.517 -16.441 1.00 33.69 ?  17  TYR   B HE1  1 
ATOM   4300 H HE2  . TYR   B 1 17  ? 36.327 -25.328 -19.264 1.00 33.74 ?  17  TYR   B HE2  1 
ATOM   4301 H HH   . TYR   B 1 17  ? 34.883 -22.402 -18.438 1.00 36.67 ?  17  TYR   B HH   1 
ATOM   4302 N N    . ILE   B 1 18  ? 39.554 -28.655 -13.924 1.00 15.21 ?  18  ILE   B N    1 
ATOM   4303 C CA   . ILE   B 1 18  ? 40.479 -29.393 -13.071 1.00 15.43 ?  18  ILE   B CA   1 
ATOM   4304 C C    . ILE   B 1 18  ? 41.626 -29.951 -13.900 1.00 15.90 ?  18  ILE   B C    1 
ATOM   4305 O O    . ILE   B 1 18  ? 41.456 -30.332 -15.063 1.00 17.01 ?  18  ILE   B O    1 
ATOM   4306 C CB   . ILE   B 1 18  ? 39.733 -30.498 -12.275 1.00 16.01 ?  18  ILE   B CB   1 
ATOM   4307 C CG1  . ILE   B 1 18  ? 40.600 -31.060 -11.143 1.00 16.15 ?  18  ILE   B CG1  1 
ATOM   4308 C CG2  . ILE   B 1 18  ? 39.220 -31.608 -13.207 1.00 16.35 ?  18  ILE   B CG2  1 
ATOM   4309 C CD1  . ILE   B 1 18  ? 39.803 -31.861 -10.120 1.00 17.23 ?  18  ILE   B CD1  1 
ATOM   4310 H H    . ILE   B 1 18  ? 39.436 -28.993 -14.703 1.00 18.29 ?  18  ILE   B H    1 
ATOM   4311 H HA   . ILE   B 1 18  ? 40.846 -28.779 -12.418 1.00 18.56 ?  18  ILE   B HA   1 
ATOM   4312 H HB   . ILE   B 1 18  ? 38.951 -30.096 -11.860 1.00 19.25 ?  18  ILE   B HB   1 
ATOM   4313 H HG12 . ILE   B 1 18  ? 41.273 -31.643 -11.519 1.00 19.42 ?  18  ILE   B HG12 1 
ATOM   4314 H HG13 . ILE   B 1 18  ? 41.020 -30.320 -10.676 1.00 19.42 ?  18  ILE   B HG13 1 
ATOM   4315 H HG21 . ILE   B 1 18  ? 38.634 -32.199 -12.707 1.00 19.66 ?  18  ILE   B HG21 1 
ATOM   4316 H HG22 . ILE   B 1 18  ? 38.726 -31.198 -13.937 1.00 19.66 ?  18  ILE   B HG22 1 
ATOM   4317 H HG23 . ILE   B 1 18  ? 39.974 -32.104 -13.556 1.00 19.66 ?  18  ILE   B HG23 1 
ATOM   4318 H HD11 . ILE   B 1 18  ? 40.401 -32.155 -9.414  1.00 20.71 ?  18  ILE   B HD11 1 
ATOM   4319 H HD12 . ILE   B 1 18  ? 39.106 -31.297 -9.748  1.00 20.71 ?  18  ILE   B HD12 1 
ATOM   4320 H HD13 . ILE   B 1 18  ? 39.407 -32.629 -10.559 1.00 20.71 ?  18  ILE   B HD13 1 
ATOM   4321 N N    . LYS   B 1 19  ? 42.809 -29.989 -13.290 1.00 16.19 ?  19  LYS   B N    1 
ATOM   4322 C CA   . LYS   B 1 19  ? 44.012 -30.469 -13.955 1.00 17.03 ?  19  LYS   B CA   1 
ATOM   4323 C C    . LYS   B 1 19  ? 44.922 -31.146 -12.938 1.00 16.86 ?  19  LYS   B C    1 
ATOM   4324 O O    . LYS   B 1 19  ? 45.015 -30.719 -11.784 1.00 16.76 ?  19  LYS   B O    1 
ATOM   4325 C CB   . LYS   B 1 19  ? 44.774 -29.312 -14.615 1.00 19.26 ?  19  LYS   B CB   1 
ATOM   4326 C CG   . LYS   B 1 19  ? 45.957 -29.731 -15.467 1.00 21.75 ?  19  LYS   B CG   1 
ATOM   4327 C CD   . LYS   B 1 19  ? 46.696 -28.512 -15.994 1.00 23.98 ?  19  LYS   B CD   1 
ATOM   4328 C CE   . LYS   B 1 19  ? 47.832 -28.891 -16.922 1.00 26.11 ?  19  LYS   B CE   1 
ATOM   4329 N NZ   . LYS   B 1 19  ? 48.583 -27.691 -17.382 1.00 27.41 ?  19  LYS   B NZ   1 
ATOM   4330 H H    . LYS   B 1 19  ? 42.925 -29.738 -12.477 1.00 19.47 ?  19  LYS   B H    1 
ATOM   4331 H HA   . LYS   B 1 19  ? 43.757 -31.113 -14.639 1.00 20.47 ?  19  LYS   B HA   1 
ATOM   4332 H HB2  . LYS   B 1 19  ? 44.157 -28.833 -15.188 1.00 23.15 ?  19  LYS   B HB2  1 
ATOM   4333 H HB3  . LYS   B 1 19  ? 45.096 -28.725 -13.914 1.00 23.15 ?  19  LYS   B HB3  1 
ATOM   4334 H HG2  . LYS   B 1 19  ? 46.563 -30.262 -14.930 1.00 26.14 ?  19  LYS   B HG2  1 
ATOM   4335 H HG3  . LYS   B 1 19  ? 45.630 -30.253 -16.222 1.00 26.14 ?  19  LYS   B HG3  1 
ATOM   4336 H HD2  . LYS   B 1 19  ? 46.072 -27.952 -16.485 1.00 28.81 ?  19  LYS   B HD2  1 
ATOM   4337 H HD3  . LYS   B 1 19  ? 47.063 -28.019 -15.243 1.00 28.81 ?  19  LYS   B HD3  1 
ATOM   4338 H HE2  . LYS   B 1 19  ? 48.446 -29.476 -16.450 1.00 31.37 ?  19  LYS   B HE2  1 
ATOM   4339 H HE3  . LYS   B 1 19  ? 47.470 -29.344 -17.701 1.00 31.37 ?  19  LYS   B HE3  1 
ATOM   4340 H HZ1  . LYS   B 1 19  ? 49.233 -27.935 -17.941 1.00 32.93 ?  19  LYS   B HZ1  1 
ATOM   4341 H HZ2  . LYS   B 1 19  ? 48.035 -27.131 -17.805 1.00 32.93 ?  19  LYS   B HZ2  1 
ATOM   4342 H HZ3  . LYS   B 1 19  ? 48.945 -27.272 -16.686 1.00 32.93 ?  19  LYS   B HZ3  1 
ATOM   4343 N N    . ASN   B 1 20  ? 45.595 -32.204 -13.375 1.00 18.40 ?  20  ASN   B N    1 
ATOM   4344 C CA   . ASN   B 1 20  ? 46.633 -32.833 -12.567 1.00 19.49 ?  20  ASN   B CA   1 
ATOM   4345 C C    . ASN   B 1 20  ? 47.913 -32.019 -12.744 1.00 19.90 ?  20  ASN   B C    1 
ATOM   4346 O O    . ASN   B 1 20  ? 48.556 -32.089 -13.799 1.00 22.14 ?  20  ASN   B O    1 
ATOM   4347 C CB   . ASN   B 1 20  ? 46.805 -34.285 -13.016 1.00 21.55 ?  20  ASN   B CB   1 
ATOM   4348 C CG   . ASN   B 1 20  ? 47.964 -35.002 -12.326 1.00 23.32 ?  20  ASN   B CG   1 
ATOM   4349 O OD1  . ASN   B 1 20  ? 48.615 -35.864 -12.928 1.00 25.41 ?  20  ASN   B OD1  1 
ATOM   4350 N ND2  . ASN   B 1 20  ? 48.213 -34.672 -11.067 1.00 23.18 ?  20  ASN   B ND2  1 
ATOM   4351 H H    . ASN   B 1 20  ? 45.456 -32.578 -14.137 1.00 22.12 ?  20  ASN   B H    1 
ATOM   4352 H HA   . ASN   B 1 20  ? 46.359 -32.819 -11.631 1.00 23.42 ?  20  ASN   B HA   1 
ATOM   4353 H HB2  . ASN   B 1 20  ? 45.982 -34.771 -12.823 1.00 25.90 ?  20  ASN   B HB2  1 
ATOM   4354 H HB3  . ASN   B 1 20  ? 46.968 -34.293 -13.970 1.00 25.90 ?  20  ASN   B HB3  1 
ATOM   4355 H HD21 . ASN   B 1 20  ? 48.852 -35.051 -10.642 1.00 27.85 ?  20  ASN   B HD21 1 
ATOM   4356 H HD22 . ASN   B 1 20  ? 47.738 -34.065 -10.670 1.00 27.85 ?  20  ASN   B HD22 1 
ATOM   4357 N N    . ALA   B 1 21  ? 48.277 -31.231 -11.731 1.00 19.47 ?  21  ALA   B N    1 
ATOM   4358 C CA   . ALA   B 1 21  ? 49.405 -30.325 -11.877 1.00 20.23 ?  21  ALA   B CA   1 
ATOM   4359 C C    . ALA   B 1 21  ? 49.869 -29.818 -10.517 1.00 19.02 ?  21  ALA   B C    1 
ATOM   4360 O O    . ALA   B 1 21  ? 49.125 -29.829 -9.532  1.00 18.67 ?  21  ALA   B O    1 
ATOM   4361 C CB   . ALA   B 1 21  ? 49.037 -29.157 -12.791 1.00 21.93 ?  21  ALA   B CB   1 
ATOM   4362 H H    . ALA   B 1 21  ? 47.883 -31.204 -10.963 1.00 23.41 ?  21  ALA   B H    1 
ATOM   4363 H HA   . ALA   B 1 21  ? 50.137 -30.811 -12.283 1.00 24.31 ?  21  ALA   B HA   1 
ATOM   4364 H HB1  . ALA   B 1 21  ? 49.837 -28.647 -12.964 1.00 26.35 ?  21  ALA   B HB1  1 
ATOM   4365 H HB2  . ALA   B 1 21  ? 48.683 -29.515 -13.621 1.00 26.35 ?  21  ALA   B HB2  1 
ATOM   4366 H HB3  . ALA   B 1 21  ? 48.368 -28.614 -12.353 1.00 26.35 ?  21  ALA   B HB3  1 
ATOM   4367 N N    . ASP   B 1 22  ? 51.127 -29.373 -10.498 1.00 17.82 ?  22  ASP   B N    1 
ATOM   4368 C CA   . ASP   B 1 22  ? 51.751 -28.687 -9.370  1.00 17.32 ?  22  ASP   B CA   1 
ATOM   4369 C C    . ASP   B 1 22  ? 51.350 -27.213 -9.436  1.00 15.80 ?  22  ASP   B C    1 
ATOM   4370 O O    . ASP   B 1 22  ? 51.658 -26.530 -10.417 1.00 16.21 ?  22  ASP   B O    1 
ATOM   4371 C CB   . ASP   B 1 22  ? 53.269 -28.870 -9.530  1.00 18.82 ?  22  ASP   B CB   1 
ATOM   4372 C CG   . ASP   B 1 22  ? 54.106 -28.119 -8.498  1.00 20.41 ?  22  ASP   B CG   1 
ATOM   4373 O OD1  . ASP   B 1 22  ? 53.746 -27.002 -8.098  1.00 20.15 ?  22  ASP   B OD1  1 
ATOM   4374 O OD2  . ASP   B 1 22  ? 55.180 -28.639 -8.118  1.00 22.85 -1 22  ASP   B OD2  1 
ATOM   4375 H H    . ASP   B 1 22  ? 51.665 -29.473 -11.164 1.00 21.42 ?  22  ASP   B H    1 
ATOM   4376 H HA   . ASP   B 1 22  ? 51.464 -29.076 -8.527  1.00 20.82 ?  22  ASP   B HA   1 
ATOM   4377 H HB2  . ASP   B 1 22  ? 53.487 -29.808 -9.457  1.00 22.62 ?  22  ASP   B HB2  1 
ATOM   4378 H HB3  . ASP   B 1 22  ? 53.531 -28.535 -10.403 1.00 22.62 ?  22  ASP   B HB3  1 
ATOM   4379 N N    . ILE   B 1 23  ? 50.643 -26.730 -8.408  1.00 14.86 ?  23  ILE   B N    1 
ATOM   4380 C CA   . ILE   B 1 23  ? 50.061 -25.383 -8.466  1.00 14.17 ?  23  ILE   B CA   1 
ATOM   4381 C C    . ILE   B 1 23  ? 51.124 -24.298 -8.604  1.00 13.88 ?  23  ILE   B C    1 
ATOM   4382 O O    . ILE   B 1 23  ? 50.867 -23.251 -9.209  1.00 13.37 ?  23  ILE   B O    1 
ATOM   4383 C CB   . ILE   B 1 23  ? 49.132 -25.133 -7.262  1.00 14.32 ?  23  ILE   B CB   1 
ATOM   4384 C CG1  . ILE   B 1 23  ? 48.314 -23.854 -7.463  1.00 15.12 ?  23  ILE   B CG1  1 
ATOM   4385 C CG2  . ILE   B 1 23  ? 49.910 -25.109 -5.962  1.00 15.30 ?  23  ILE   B CG2  1 
ATOM   4386 C CD1  . ILE   B 1 23  ? 47.187 -23.690 -6.449  1.00 15.92 ?  23  ILE   B CD1  1 
ATOM   4387 H H    . ILE   B 1 23  ? 50.488 -27.155 -7.683  1.00 17.88 ?  23  ILE   B H    1 
ATOM   4388 H HA   . ILE   B 1 23  ? 49.512 -25.331 -9.260  1.00 17.05 ?  23  ILE   B HA   1 
ATOM   4389 H HB   . ILE   B 1 23  ? 48.507 -25.874 -7.220  1.00 17.22 ?  23  ILE   B HB   1 
ATOM   4390 H HG12 . ILE   B 1 23  ? 48.909 -23.088 -7.379  1.00 18.18 ?  23  ILE   B HG12 1 
ATOM   4391 H HG13 . ILE   B 1 23  ? 47.924 -23.867 -8.352  1.00 18.18 ?  23  ILE   B HG13 1 
ATOM   4392 H HG21 . ILE   B 1 23  ? 49.286 -25.102 -5.221  1.00 18.39 ?  23  ILE   B HG21 1 
ATOM   4393 H HG22 . ILE   B 1 23  ? 50.469 -25.902 -5.915  1.00 18.39 ?  23  ILE   B HG22 1 
ATOM   4394 H HG23 . ILE   B 1 23  ? 50.464 -24.314 -5.939  1.00 18.39 ?  23  ILE   B HG23 1 
ATOM   4395 H HD11 . ILE   B 1 23  ? 46.676 -22.901 -6.677  1.00 19.14 ?  23  ILE   B HD11 1 
ATOM   4396 H HD12 . ILE   B 1 23  ? 46.623 -24.477 -6.487  1.00 19.14 ?  23  ILE   B HD12 1 
ATOM   4397 H HD13 . ILE   B 1 23  ? 47.573 -23.598 -5.566  1.00 19.14 ?  23  ILE   B HD13 1 
ATOM   4398 N N    . VAL   B 1 24  ? 52.319 -24.509 -8.046  1.00 14.05 ?  24  VAL   B N    1 
ATOM   4399 C CA   . VAL   B 1 24  ? 53.397 -23.530 -8.206  1.00 14.77 ?  24  VAL   B CA   1 
ATOM   4400 C C    . VAL   B 1 24  ? 53.853 -23.479 -9.657  1.00 15.02 ?  24  VAL   B C    1 
ATOM   4401 O O    . VAL   B 1 24  ? 53.987 -22.400 -10.249 1.00 15.55 ?  24  VAL   B O    1 
ATOM   4402 C CB   . VAL   B 1 24  ? 54.572 -23.848 -7.257  1.00 15.56 ?  24  VAL   B CB   1 
ATOM   4403 C CG1  . VAL   B 1 24  ? 55.788 -22.970 -7.577  1.00 16.47 ?  24  VAL   B CG1  1 
ATOM   4404 C CG2  . VAL   B 1 24  ? 54.153 -23.667 -5.815  1.00 16.44 ?  24  VAL   B CG2  1 
ATOM   4405 H H    . VAL   B 1 24  ? 52.533 -25.199 -7.582  1.00 16.90 ?  24  VAL   B H    1 
ATOM   4406 H HA   . VAL   B 1 24  ? 53.061 -22.651 -7.971  1.00 17.77 ?  24  VAL   B HA   1 
ATOM   4407 H HB   . VAL   B 1 24  ? 54.836 -24.772 -7.374  1.00 18.71 ?  24  VAL   B HB   1 
ATOM   4408 H HG11 . VAL   B 1 24  ? 56.388 -22.974 -6.812  1.00 19.80 ?  24  VAL   B HG11 1 
ATOM   4409 H HG12 . VAL   B 1 24  ? 56.243 -23.331 -8.352  1.00 19.80 ?  24  VAL   B HG12 1 
ATOM   4410 H HG13 . VAL   B 1 24  ? 55.488 -22.065 -7.754  1.00 19.80 ?  24  VAL   B HG13 1 
ATOM   4411 H HG21 . VAL   B 1 24  ? 54.884 -23.931 -5.235  1.00 19.76 ?  24  VAL   B HG21 1 
ATOM   4412 H HG22 . VAL   B 1 24  ? 53.935 -22.732 -5.665  1.00 19.76 ?  24  VAL   B HG22 1 
ATOM   4413 H HG23 . VAL   B 1 24  ? 53.375 -24.219 -5.641  1.00 19.76 ?  24  VAL   B HG23 1 
ATOM   4414 N N    . GLU   B 1 25  ? 54.119 -24.649 -10.249 1.00 15.91 ?  25  GLU   B N    1 
ATOM   4415 C CA   . GLU   B 1 25  ? 54.516 -24.681 -11.651 1.00 17.76 ?  25  GLU   B CA   1 
ATOM   4416 C C    . GLU   B 1 25  ? 53.404 -24.145 -12.541 1.00 16.42 ?  25  GLU   B C    1 
ATOM   4417 O O    . GLU   B 1 25  ? 53.669 -23.432 -13.520 1.00 17.34 ?  25  GLU   B O    1 
ATOM   4418 C CB   . GLU   B 1 25  ? 54.921 -26.098 -12.051 1.00 22.32 ?  25  GLU   B CB   1 
ATOM   4419 C CG   . GLU   B 1 25  ? 56.223 -26.546 -11.394 1.00 28.40 ?  25  GLU   B CG   1 
ATOM   4420 C CD   . GLU   B 1 25  ? 57.331 -25.505 -11.480 1.00 33.78 ?  25  GLU   B CD   1 
ATOM   4421 O OE1  . GLU   B 1 25  ? 57.721 -25.135 -12.608 1.00 35.74 ?  25  GLU   B OE1  1 
ATOM   4422 O OE2  . GLU   B 1 25  ? 57.798 -25.038 -10.416 1.00 35.67 -1 25  GLU   B OE2  1 
ATOM   4423 H H    . GLU   B 1 25  ? 54.080 -25.415 -9.864  1.00 19.14 ?  25  GLU   B H    1 
ATOM   4424 H HA   . GLU   B 1 25  ? 55.271 -24.091 -11.774 1.00 21.35 ?  25  GLU   B HA   1 
ATOM   4425 H HB2  . GLU   B 1 25  ? 54.222 -26.716 -11.779 1.00 26.83 ?  25  GLU   B HB2  1 
ATOM   4426 H HB3  . GLU   B 1 25  ? 55.037 -26.134 -13.013 1.00 26.83 ?  25  GLU   B HB3  1 
ATOM   4427 H HG2  . GLU   B 1 25  ? 56.064 -26.709 -10.457 1.00 34.11 ?  25  GLU   B HG2  1 
ATOM   4428 H HG3  . GLU   B 1 25  ? 56.534 -27.351 -11.834 1.00 34.11 ?  25  GLU   B HG3  1 
ATOM   4429 N N    A GLU   B 1 26  ? 52.152 -24.468 -12.212 0.72 15.43 ?  26  GLU   B N    1 
ATOM   4430 N N    B GLU   B 1 26  ? 52.150 -24.464 -12.210 0.28 16.01 ?  26  GLU   B N    1 
ATOM   4431 C CA   A GLU   B 1 26  ? 51.023 -23.942 -12.973 0.72 16.43 ?  26  GLU   B CA   1 
ATOM   4432 C CA   B GLU   B 1 26  ? 51.024 -23.940 -12.976 0.28 16.28 ?  26  GLU   B CA   1 
ATOM   4433 C C    A GLU   B 1 26  ? 50.974 -22.424 -12.901 0.72 15.44 ?  26  GLU   B C    1 
ATOM   4434 C C    B GLU   B 1 26  ? 50.973 -22.421 -12.902 0.28 15.30 ?  26  GLU   B C    1 
ATOM   4435 O O    A GLU   B 1 26  ? 50.766 -21.753 -13.916 0.72 16.62 ?  26  GLU   B O    1 
ATOM   4436 O O    B GLU   B 1 26  ? 50.783 -21.746 -13.918 0.28 15.80 ?  26  GLU   B O    1 
ATOM   4437 C CB   A GLU   B 1 26  ? 49.713 -24.522 -12.441 0.72 18.77 ?  26  GLU   B CB   1 
ATOM   4438 C CB   B GLU   B 1 26  ? 49.712 -24.535 -12.462 0.28 17.71 ?  26  GLU   B CB   1 
ATOM   4439 C CG   A GLU   B 1 26  ? 49.283 -25.813 -13.098 0.72 22.56 ?  26  GLU   B CG   1 
ATOM   4440 C CG   B GLU   B 1 26  ? 49.276 -25.789 -13.189 0.28 19.65 ?  26  GLU   B CG   1 
ATOM   4441 C CD   A GLU   B 1 26  ? 49.025 -25.662 -14.595 0.72 24.77 ?  26  GLU   B CD   1 
ATOM   4442 C CD   B GLU   B 1 26  ? 48.979 -25.540 -14.666 0.28 20.52 ?  26  GLU   B CD   1 
ATOM   4443 O OE1  A GLU   B 1 26  ? 48.117 -24.902 -14.994 0.72 25.62 ?  26  GLU   B OE1  1 
ATOM   4444 O OE1  B GLU   B 1 26  ? 47.911 -24.970 -14.984 0.28 20.93 ?  26  GLU   B OE1  1 
ATOM   4445 O OE2  A GLU   B 1 26  ? 49.732 -26.320 -15.376 0.72 26.24 -1 26  GLU   B OE2  1 
ATOM   4446 O OE2  B GLU   B 1 26  ? 49.816 -25.911 -15.509 0.28 21.27 -1 26  GLU   B OE2  1 
ATOM   4447 H H    A GLU   B 1 26  ? 51.929 -24.984 -11.557 0.72 18.55 ?  26  GLU   B H    1 
ATOM   4448 H H    B GLU   B 1 26  ? 51.927 -24.976 -11.553 0.28 19.24 ?  26  GLU   B H    1 
ATOM   4449 H HA   A GLU   B 1 26  ? 51.119 -24.198 -13.901 0.72 19.75 ?  26  GLU   B HA   1 
ATOM   4450 H HA   B GLU   B 1 26  ? 51.131 -24.189 -13.904 0.28 19.58 ?  26  GLU   B HA   1 
ATOM   4451 H HB2  A GLU   B 1 26  ? 49.810 -24.691 -11.490 0.72 22.56 ?  26  GLU   B HB2  1 
ATOM   4452 H HB2  B GLU   B 1 26  ? 49.814 -24.755 -11.522 0.28 21.29 ?  26  GLU   B HB2  1 
ATOM   4453 H HB3  A GLU   B 1 26  ? 49.005 -23.870 -12.582 0.72 22.56 ?  26  GLU   B HB3  1 
ATOM   4454 H HB3  B GLU   B 1 26  ? 49.007 -23.875 -12.567 0.28 21.29 ?  26  GLU   B HB3  1 
ATOM   4455 H HG2  A GLU   B 1 26  ? 49.983 -26.467 -12.963 0.72 27.11 ?  26  GLU   B HG2  1 
ATOM   4456 H HG2  B GLU   B 1 26  ? 49.980 -26.450 -13.099 0.28 23.62 ?  26  GLU   B HG2  1 
ATOM   4457 H HG3  A GLU   B 1 26  ? 48.458 -26.111 -12.688 0.72 27.11 ?  26  GLU   B HG3  1 
ATOM   4458 H HG3  B GLU   B 1 26  ? 48.459 -26.114 -12.785 0.28 23.62 ?  26  GLU   B HG3  1 
ATOM   4459 N N    . ALA   B 1 27  ? 51.125 -21.866 -11.698 1.00 14.43 ?  27  ALA   B N    1 
ATOM   4460 C CA   . ALA   B 1 27  ? 51.083 -20.417 -11.552 1.00 14.66 ?  27  ALA   B CA   1 
ATOM   4461 C C    . ALA   B 1 27  ? 52.154 -19.754 -12.409 1.00 15.54 ?  27  ALA   B C    1 
ATOM   4462 O O    . ALA   B 1 27  ? 51.892 -18.761 -13.100 1.00 16.32 ?  27  ALA   B O    1 
ATOM   4463 C CB   . ALA   B 1 27  ? 51.236 -20.037 -10.078 1.00 14.75 ?  27  ALA   B CB   1 
ATOM   4464 H H    A ALA   B 1 27  ? 51.244 -22.300 -10.964 0.72 17.36 ?  27  ALA   B H    1 
ATOM   4465 H H    B ALA   B 1 27  ? 51.248 -22.300 -10.965 0.28 17.36 ?  27  ALA   B H    1 
ATOM   4466 H HA   . ALA   B 1 27  ? 50.223 -20.092 -11.851 1.00 17.63 ?  27  ALA   B HA   1 
ATOM   4467 H HB1  . ALA   B 1 27  ? 51.199 -19.074 -9.992  1.00 17.73 ?  27  ALA   B HB1  1 
ATOM   4468 H HB2  . ALA   B 1 27  ? 50.505 -20.440 -9.573  1.00 17.73 ?  27  ALA   B HB2  1 
ATOM   4469 H HB3  . ALA   B 1 27  ? 52.083 -20.371 -9.748  1.00 17.73 ?  27  ALA   B HB3  1 
ATOM   4470 N N    . LYS   B 1 28  ? 53.371 -20.301 -12.397 1.00 17.12 ?  28  LYS   B N    1 
ATOM   4471 C CA   . LYS   B 1 28  ? 54.445 -19.688 -13.169 1.00 19.50 ?  28  LYS   B CA   1 
ATOM   4472 C C    . LYS   B 1 28  ? 54.194 -19.782 -14.667 1.00 19.89 ?  28  LYS   B C    1 
ATOM   4473 O O    . LYS   B 1 28  ? 54.619 -18.893 -15.418 1.00 20.85 ?  28  LYS   B O    1 
ATOM   4474 C CB   . LYS   B 1 28  ? 55.802 -20.280 -12.768 1.00 23.13 ?  28  LYS   B CB   1 
ATOM   4475 C CG   . LYS   B 1 28  ? 56.189 -19.929 -11.334 1.00 26.88 ?  28  LYS   B CG   1 
ATOM   4476 C CD   . LYS   B 1 28  ? 57.620 -20.315 -10.983 1.00 31.65 ?  28  LYS   B CD   1 
ATOM   4477 C CE   . LYS   B 1 28  ? 57.737 -21.788 -10.670 1.00 35.34 ?  28  LYS   B CE   1 
ATOM   4478 N NZ   . LYS   B 1 28  ? 59.087 -22.127 -10.136 1.00 38.11 ?  28  LYS   B NZ   1 
ATOM   4479 H H    . LYS   B 1 28  ? 53.595 -21.013 -11.965 1.00 20.58 ?  28  LYS   B H    1 
ATOM   4480 H HA   . LYS   B 1 28  ? 54.474 -18.749 -12.955 1.00 23.44 ?  28  LYS   B HA   1 
ATOM   4481 H HB2  . LYS   B 1 28  ? 55.768 -21.246 -12.841 1.00 27.80 ?  28  LYS   B HB2  1 
ATOM   4482 H HB3  . LYS   B 1 28  ? 56.490 -19.927 -13.358 1.00 27.80 ?  28  LYS   B HB3  1 
ATOM   4483 H HG2  . LYS   B 1 28  ? 56.100 -18.970 -11.212 1.00 32.30 ?  28  LYS   B HG2  1 
ATOM   4484 H HG3  . LYS   B 1 28  ? 55.597 -20.396 -10.727 1.00 32.30 ?  28  LYS   B HG3  1 
ATOM   4485 H HD2  . LYS   B 1 28  ? 58.198 -20.114 -11.736 1.00 38.01 ?  28  LYS   B HD2  1 
ATOM   4486 H HD3  . LYS   B 1 28  ? 57.901 -19.812 -10.201 1.00 38.01 ?  28  LYS   B HD3  1 
ATOM   4487 H HE2  . LYS   B 1 28  ? 57.076 -22.026 -9.999  1.00 42.45 ?  28  LYS   B HE2  1 
ATOM   4488 H HE3  . LYS   B 1 28  ? 57.592 -22.301 -11.480 1.00 42.45 ?  28  LYS   B HE3  1 
ATOM   4489 H HZ1  . LYS   B 1 28  ? 59.134 -22.997 -9.958  1.00 45.77 ?  28  LYS   B HZ1  1 
ATOM   4490 H HZ2  . LYS   B 1 28  ? 59.711 -21.919 -10.736 1.00 45.77 ?  28  LYS   B HZ2  1 
ATOM   4491 H HZ3  . LYS   B 1 28  ? 59.242 -21.669 -9.388  1.00 45.77 ?  28  LYS   B HZ3  1 
ATOM   4492 N N    . LYS   B 1 29  ? 53.484 -20.817 -15.119 1.00 21.04 ?  29  LYS   B N    1 
ATOM   4493 C CA   . LYS   B 1 29  ? 53.215 -20.982 -16.544 1.00 23.84 ?  29  LYS   B CA   1 
ATOM   4494 C C    . LYS   B 1 29  ? 51.967 -20.232 -17.003 1.00 22.55 ?  29  LYS   B C    1 
ATOM   4495 O O    . LYS   B 1 29  ? 51.977 -19.621 -18.078 1.00 24.22 ?  29  LYS   B O    1 
ATOM   4496 C CB   . LYS   B 1 29  ? 53.082 -22.469 -16.884 1.00 29.03 ?  29  LYS   B CB   1 
ATOM   4497 C CG   . LYS   B 1 29  ? 52.910 -22.750 -18.367 1.00 33.81 ?  29  LYS   B CG   1 
ATOM   4498 C CD   . LYS   B 1 29  ? 53.095 -24.230 -18.678 1.00 37.56 ?  29  LYS   B CD   1 
ATOM   4499 C CE   . LYS   B 1 29  ? 51.948 -25.070 -18.139 1.00 40.13 ?  29  LYS   B CE   1 
ATOM   4500 N NZ   . LYS   B 1 29  ? 52.159 -26.523 -18.406 1.00 41.42 ?  29  LYS   B NZ   1 
ATOM   4501 H H    . LYS   B 1 29  ? 53.137 -21.437 -14.619 1.00 25.29 ?  29  LYS   B H    1 
ATOM   4502 H HA   . LYS   B 1 29  ? 53.967 -20.635 -17.040 1.00 28.64 ?  29  LYS   B HA   1 
ATOM   4503 H HB2  . LYS   B 1 29  ? 53.886 -22.927 -16.591 1.00 34.88 ?  29  LYS   B HB2  1 
ATOM   4504 H HB3  . LYS   B 1 29  ? 52.311 -22.829 -16.425 1.00 34.88 ?  29  LYS   B HB3  1 
ATOM   4505 H HG2  . LYS   B 1 29  ? 52.015 -22.491 -18.639 1.00 40.60 ?  29  LYS   B HG2  1 
ATOM   4506 H HG3  . LYS   B 1 29  ? 53.572 -22.247 -18.868 1.00 40.60 ?  29  LYS   B HG3  1 
ATOM   4507 H HD2  . LYS   B 1 29  ? 53.136 -24.352 -19.639 1.00 45.11 ?  29  LYS   B HD2  1 
ATOM   4508 H HD3  . LYS   B 1 29  ? 53.917 -24.542 -18.266 1.00 45.11 ?  29  LYS   B HD3  1 
ATOM   4509 H HE2  . LYS   B 1 29  ? 51.880 -24.946 -17.180 1.00 48.19 ?  29  LYS   B HE2  1 
ATOM   4510 H HE3  . LYS   B 1 29  ? 51.123 -24.798 -18.572 1.00 48.19 ?  29  LYS   B HE3  1 
ATOM   4511 H HZ1  . LYS   B 1 29  ? 51.476 -26.994 -18.084 1.00 49.74 ?  29  LYS   B HZ1  1 
ATOM   4512 H HZ2  . LYS   B 1 29  ? 52.220 -26.665 -19.283 1.00 49.74 ?  29  LYS   B HZ2  1 
ATOM   4513 H HZ3  . LYS   B 1 29  ? 52.910 -26.798 -18.016 1.00 49.74 ?  29  LYS   B HZ3  1 
ATOM   4514 N N    . VAL   B 1 30  ? 50.892 -20.279 -16.210 1.00 20.49 ?  30  VAL   B N    1 
ATOM   4515 C CA   . VAL   B 1 30  ? 49.606 -19.690 -16.590 1.00 20.49 ?  30  VAL   B CA   1 
ATOM   4516 C C    . VAL   B 1 30  ? 49.602 -18.180 -16.425 1.00 18.45 ?  30  VAL   B C    1 
ATOM   4517 O O    . VAL   B 1 30  ? 48.847 -17.473 -17.115 1.00 19.03 ?  30  VAL   B O    1 
ATOM   4518 C CB   . VAL   B 1 30  ? 48.501 -20.314 -15.715 1.00 22.41 ?  30  VAL   B CB   1 
ATOM   4519 C CG1  . VAL   B 1 30  ? 47.218 -19.501 -15.780 1.00 23.41 ?  30  VAL   B CG1  1 
ATOM   4520 C CG2  . VAL   B 1 30  ? 48.257 -21.763 -16.112 1.00 23.41 ?  30  VAL   B CG2  1 
ATOM   4521 H H    . VAL   B 1 30  ? 50.877 -20.676 -15.438 1.00 24.63 ?  30  VAL   B H    1 
ATOM   4522 H HA   . VAL   B 1 30  ? 49.416 -19.913 -17.514 1.00 24.63 ?  30  VAL   B HA   1 
ATOM   4523 H HB   . VAL   B 1 30  ? 48.796 -20.318 -14.791 1.00 26.94 ?  30  VAL   B HB   1 
ATOM   4524 H HG11 . VAL   B 1 30  ? 46.476 -20.081 -15.543 1.00 28.13 ?  30  VAL   B HG11 1 
ATOM   4525 H HG12 . VAL   B 1 30  ? 47.272 -18.768 -15.151 1.00 28.13 ?  30  VAL   B HG12 1 
ATOM   4526 H HG13 . VAL   B 1 30  ? 47.094 -19.174 -16.680 1.00 28.13 ?  30  VAL   B HG13 1 
ATOM   4527 H HG21 . VAL   B 1 30  ? 47.566 -22.141 -15.539 1.00 28.14 ?  30  VAL   B HG21 1 
ATOM   4528 H HG22 . VAL   B 1 30  ? 47.963 -21.795 -17.038 1.00 28.14 ?  30  VAL   B HG22 1 
ATOM   4529 H HG23 . VAL   B 1 30  ? 49.079 -22.265 -16.009 1.00 28.14 ?  30  VAL   B HG23 1 
ATOM   4530 N N    A LYS   B 1 31  ? 50.415 -17.661 -15.512 0.72 17.72 ?  31  LYS   B N    1 
ATOM   4531 N N    B LYS   B 1 31  ? 50.414 -17.670 -15.509 0.28 18.61 ?  31  LYS   B N    1 
ATOM   4532 C CA   A LYS   B 1 31  ? 50.423 -16.247 -15.158 0.72 18.24 ?  31  LYS   B CA   1 
ATOM   4533 C CA   B LYS   B 1 31  ? 50.422 -16.258 -15.150 0.28 19.10 ?  31  LYS   B CA   1 
ATOM   4534 C C    A LYS   B 1 31  ? 49.033 -15.743 -14.753 0.72 16.45 ?  31  LYS   B C    1 
ATOM   4535 C C    B LYS   B 1 31  ? 49.020 -15.772 -14.772 0.28 17.01 ?  31  LYS   B C    1 
ATOM   4536 O O    A LYS   B 1 31  ? 48.495 -14.817 -15.371 0.72 17.00 ?  31  LYS   B O    1 
ATOM   4537 O O    B LYS   B 1 31  ? 48.458 -14.895 -15.436 0.28 16.85 ?  31  LYS   B O    1 
ATOM   4538 C CB   A LYS   B 1 31  ? 51.029 -15.404 -16.273 0.72 21.28 ?  31  LYS   B CB   1 
ATOM   4539 C CB   B LYS   B 1 31  ? 51.026 -15.412 -16.263 0.28 21.83 ?  31  LYS   B CB   1 
ATOM   4540 C CG   A LYS   B 1 31  ? 52.479 -15.791 -16.571 0.72 24.79 ?  31  LYS   B CG   1 
ATOM   4541 C CG   B LYS   B 1 31  ? 52.456 -15.826 -16.586 0.28 24.50 ?  31  LYS   B CG   1 
ATOM   4542 C CD   A LYS   B 1 31  ? 53.078 -14.982 -17.703 0.72 28.45 ?  31  LYS   B CD   1 
ATOM   4543 C CD   B LYS   B 1 31  ? 53.048 -15.018 -17.719 0.28 26.90 ?  31  LYS   B CD   1 
ATOM   4544 C CE   A LYS   B 1 31  ? 54.561 -15.264 -17.841 0.72 31.16 ?  31  LYS   B CE   1 
ATOM   4545 C CE   B LYS   B 1 31  ? 54.547 -15.236 -17.813 0.28 28.65 ?  31  LYS   B CE   1 
ATOM   4546 N NZ   A LYS   B 1 31  ? 55.307 -14.902 -16.601 0.72 32.58 ?  31  LYS   B NZ   1 
ATOM   4547 N NZ   B LYS   B 1 31  ? 55.235 -14.827 -16.556 0.28 29.64 ?  31  LYS   B NZ   1 
ATOM   4548 H H    A LYS   B 1 31  ? 50.996 -18.132 -15.080 0.72 21.30 ?  31  LYS   B H    1 
ATOM   4549 H H    B LYS   B 1 31  ? 50.987 -18.140 -15.072 0.28 22.38 ?  31  LYS   B H    1 
ATOM   4550 H HA   A LYS   B 1 31  ? 50.990 -16.150 -14.387 0.72 21.93 ?  31  LYS   B HA   1 
ATOM   4551 H HA   B LYS   B 1 31  ? 50.986 -16.157 -14.377 0.28 22.96 ?  31  LYS   B HA   1 
ATOM   4552 H HB2  A LYS   B 1 31  ? 50.513 -15.527 -17.085 0.72 25.58 ?  31  LYS   B HB2  1 
ATOM   4553 H HB2  B LYS   B 1 31  ? 50.497 -15.508 -17.069 0.28 26.24 ?  31  LYS   B HB2  1 
ATOM   4554 H HB3  A LYS   B 1 31  ? 51.014 -14.476 -16.003 0.72 25.58 ?  31  LYS   B HB3  1 
ATOM   4555 H HB3  B LYS   B 1 31  ? 51.041 -14.484 -15.979 0.28 26.24 ?  31  LYS   B HB3  1 
ATOM   4556 H HG2  A LYS   B 1 31  ? 53.011 -15.643 -15.773 0.72 29.78 ?  31  LYS   B HG2  1 
ATOM   4557 H HG2  B LYS   B 1 31  ? 53.006 -15.698 -15.797 0.28 29.44 ?  31  LYS   B HG2  1 
ATOM   4558 H HG3  A LYS   B 1 31  ? 52.513 -16.730 -16.820 0.72 29.78 ?  31  LYS   B HG3  1 
ATOM   4559 H HG3  B LYS   B 1 31  ? 52.466 -16.761 -16.848 0.28 29.44 ?  31  LYS   B HG3  1 
ATOM   4560 H HD2  A LYS   B 1 31  ? 52.638 -15.224 -18.532 0.72 34.18 ?  31  LYS   B HD2  1 
ATOM   4561 H HD2  B LYS   B 1 31  ? 52.645 -15.297 -18.555 0.28 32.32 ?  31  LYS   B HD2  1 
ATOM   4562 H HD3  A LYS   B 1 31  ? 52.958 -14.040 -17.516 0.72 34.18 ?  31  LYS   B HD3  1 
ATOM   4563 H HD3  B LYS   B 1 31  ? 52.885 -14.077 -17.559 0.28 32.32 ?  31  LYS   B HD3  1 
ATOM   4564 H HE2  A LYS   B 1 31  ? 54.693 -16.212 -18.009 0.72 37.43 ?  31  LYS   B HE2  1 
ATOM   4565 H HE2  B LYS   B 1 31  ? 54.726 -16.178 -17.966 0.28 34.42 ?  31  LYS   B HE2  1 
ATOM   4566 H HE3  A LYS   B 1 31  ? 54.918 -14.741 -18.575 0.72 37.43 ?  31  LYS   B HE3  1 
ATOM   4567 H HE3  B LYS   B 1 31  ? 54.902 -14.704 -18.541 0.28 34.42 ?  31  LYS   B HE3  1 
ATOM   4568 H HZ1  A LYS   B 1 31  ? 56.183 -14.965 -16.743 0.72 39.13 ?  31  LYS   B HZ1  1 
ATOM   4569 H HZ1  B LYS   B 1 31  ? 56.114 -14.806 -16.683 0.28 35.60 ?  31  LYS   B HZ1  1 
ATOM   4570 H HZ2  A LYS   B 1 31  ? 55.111 -14.068 -16.361 0.72 39.13 ?  31  LYS   B HZ2  1 
ATOM   4571 H HZ2  B LYS   B 1 31  ? 54.958 -14.019 -16.307 0.28 35.60 ?  31  LYS   B HZ2  1 
ATOM   4572 H HZ3  A LYS   B 1 31  ? 55.083 -15.453 -15.937 0.72 39.13 ?  31  LYS   B HZ3  1 
ATOM   4573 H HZ3  B LYS   B 1 31  ? 55.051 -15.407 -15.905 0.28 35.60 ?  31  LYS   B HZ3  1 
ATOM   4574 N N    . PRO   B 1 32  ? 48.433 -16.325 -13.710 1.00 15.52 ?  32  PRO   B N    1 
ATOM   4575 C CA   . PRO   B 1 32  ? 47.061 -15.957 -13.339 1.00 14.72 ?  32  PRO   B CA   1 
ATOM   4576 C C    . PRO   B 1 32  ? 46.993 -14.612 -12.633 1.00 14.68 ?  32  PRO   B C    1 
ATOM   4577 O O    . PRO   B 1 32  ? 47.928 -14.191 -11.946 1.00 15.89 ?  32  PRO   B O    1 
ATOM   4578 C CB   . PRO   B 1 32  ? 46.668 -17.070 -12.359 1.00 14.87 ?  32  PRO   B CB   1 
ATOM   4579 C CG   . PRO   B 1 32  ? 47.980 -17.418 -11.696 1.00 15.17 ?  32  PRO   B CG   1 
ATOM   4580 C CD   . PRO   B 1 32  ? 49.030 -17.287 -12.758 1.00 15.23 ?  32  PRO   B CD   1 
ATOM   4581 H HA   . PRO   B 1 32  ? 46.469 -15.974 -14.118 1.00 17.71 ?  32  PRO   B HA   1 
ATOM   4582 H HB2  . PRO   B 1 32  ? 46.029 -16.728 -11.714 1.00 17.89 ?  32  PRO   B HB2  1 
ATOM   4583 H HB3  . PRO   B 1 32  ? 46.306 -17.831 -12.840 1.00 17.89 ?  32  PRO   B HB3  1 
ATOM   4584 H HG2  . PRO   B 1 32  ? 48.153 -16.800 -10.967 1.00 18.24 ?  32  PRO   B HG2  1 
ATOM   4585 H HG3  . PRO   B 1 32  ? 47.948 -18.331 -11.365 1.00 18.24 ?  32  PRO   B HG3  1 
ATOM   4586 H HD2  . PRO   B 1 32  ? 49.843 -16.913 -12.383 1.00 18.32 ?  32  PRO   B HD2  1 
ATOM   4587 H HD3  . PRO   B 1 32  ? 49.188 -18.138 -13.183 1.00 18.32 ?  32  PRO   B HD3  1 
ATOM   4588 N N    . THR   B 1 33  ? 45.840 -13.951 -12.787 1.00 14.23 ?  33  THR   B N    1 
ATOM   4589 C CA   . THR   B 1 33  ? 45.561 -12.774 -11.972 1.00 14.47 ?  33  THR   B CA   1 
ATOM   4590 C C    . THR   B 1 33  ? 45.524 -13.131 -10.490 1.00 13.87 ?  33  THR   B C    1 
ATOM   4591 O O    . THR   B 1 33  ? 46.008 -12.355 -9.649  1.00 14.83 ?  33  THR   B O    1 
ATOM   4592 C CB   . THR   B 1 33  ? 44.243 -12.125 -12.409 1.00 15.14 ?  33  THR   B CB   1 
ATOM   4593 O OG1  . THR   B 1 33  ? 44.262 -11.897 -13.817 1.00 15.29 ?  33  THR   B OG1  1 
ATOM   4594 C CG2  . THR   B 1 33  ? 44.031 -10.820 -11.681 1.00 16.55 ?  33  THR   B CG2  1 
ATOM   4595 H H    . THR   B 1 33  ? 45.219 -14.171 -13.346 1.00 17.12 ?  33  THR   B H    1 
ATOM   4596 H HA   . THR   B 1 33  ? 46.274 -12.135 -12.113 1.00 17.40 ?  33  THR   B HA   1 
ATOM   4597 H HB   . THR   B 1 33  ? 43.509 -12.728 -12.197 1.00 18.20 ?  33  THR   B HB   1 
ATOM   4598 H HG1  . THR   B 1 33  ? 43.543 -11.527 -14.063 1.00 18.38 ?  33  THR   B HG1  1 
ATOM   4599 H HG21 . THR   B 1 33  ? 43.275 -10.352 -12.056 1.00 19.89 ?  33  THR   B HG21 1 
ATOM   4600 H HG22 . THR   B 1 33  ? 43.869 -10.988 -10.739 1.00 19.89 ?  33  THR   B HG22 1 
ATOM   4601 H HG23 . THR   B 1 33  ? 44.824 -10.264 -11.768 1.00 19.89 ?  33  THR   B HG23 1 
ATOM   4602 N N    . VAL   B 1 34  ? 44.954 -14.295 -10.148 1.00 13.07 ?  34  VAL   B N    1 
ATOM   4603 C CA   . VAL   B 1 34  ? 44.749 -14.681 -8.756  1.00 12.87 ?  34  VAL   B CA   1 
ATOM   4604 C C    . VAL   B 1 34  ? 45.162 -16.131 -8.582  1.00 11.84 ?  34  VAL   B C    1 
ATOM   4605 O O    . VAL   B 1 34  ? 44.637 -17.015 -9.268  1.00 12.60 ?  34  VAL   B O    1 
ATOM   4606 C CB   . VAL   B 1 34  ? 43.276 -14.525 -8.320  1.00 13.84 ?  34  VAL   B CB   1 
ATOM   4607 C CG1  . VAL   B 1 34  ? 43.097 -14.963 -6.871  1.00 14.11 ?  34  VAL   B CG1  1 
ATOM   4608 C CG2  . VAL   B 1 34  ? 42.791 -13.098 -8.532  1.00 14.61 ?  34  VAL   B CG2  1 
ATOM   4609 H H    . VAL   B 1 34  ? 44.691 -14.890 -10.718 1.00 15.72 ?  34  VAL   B H    1 
ATOM   4610 H HA   . VAL   B 1 34  ? 45.303 -14.130 -8.181  1.00 15.48 ?  34  VAL   B HA   1 
ATOM   4611 H HB   . VAL   B 1 34  ? 42.730 -15.100 -8.880  1.00 16.65 ?  34  VAL   B HB   1 
ATOM   4612 H HG11 . VAL   B 1 34  ? 42.235 -14.642 -6.552  1.00 16.97 ?  34  VAL   B HG11 1 
ATOM   4613 H HG12 . VAL   B 1 34  ? 43.123 -15.929 -6.825  1.00 16.97 ?  34  VAL   B HG12 1 
ATOM   4614 H HG13 . VAL   B 1 34  ? 43.807 -14.580 -6.334  1.00 16.97 ?  34  VAL   B HG13 1 
ATOM   4615 H HG21 . VAL   B 1 34  ? 41.872 -13.028 -8.231  1.00 17.57 ?  34  VAL   B HG21 1 
ATOM   4616 H HG22 . VAL   B 1 34  ? 43.354 -12.492 -8.029  1.00 17.57 ?  34  VAL   B HG22 1 
ATOM   4617 H HG23 . VAL   B 1 34  ? 42.840 -12.880 -9.481  1.00 17.57 ?  34  VAL   B HG23 1 
ATOM   4618 N N    . VAL   B 1 35  ? 46.064 -16.385 -7.636  1.00 11.34 ?  35  VAL   B N    1 
ATOM   4619 C CA   . VAL   B 1 35  ? 46.290 -17.730 -7.117  1.00 11.22 ?  35  VAL   B CA   1 
ATOM   4620 C C    . VAL   B 1 35  ? 45.746 -17.781 -5.698  1.00 10.79 ?  35  VAL   B C    1 
ATOM   4621 O O    . VAL   B 1 35  ? 45.967 -16.859 -4.905  1.00 11.20 ?  35  VAL   B O    1 
ATOM   4622 C CB   . VAL   B 1 35  ? 47.771 -18.171 -7.192  1.00 12.13 ?  35  VAL   B CB   1 
ATOM   4623 C CG1  . VAL   B 1 35  ? 48.669 -17.340 -6.272  1.00 13.11 ?  35  VAL   B CG1  1 
ATOM   4624 C CG2  . VAL   B 1 35  ? 47.905 -19.667 -6.874  1.00 12.93 ?  35  VAL   B CG2  1 
ATOM   4625 H H    . VAL   B 1 35  ? 46.564 -15.785 -7.273  1.00 13.65 ?  35  VAL   B H    1 
ATOM   4626 H HA   . VAL   B 1 35  ? 45.771 -18.356 -7.645  1.00 13.51 ?  35  VAL   B HA   1 
ATOM   4627 H HB   . VAL   B 1 35  ? 48.082 -18.040 -8.102  1.00 14.59 ?  35  VAL   B HB   1 
ATOM   4628 H HG11 . VAL   B 1 35  ? 49.591 -17.569 -6.453  1.00 15.77 ?  35  VAL   B HG11 1 
ATOM   4629 H HG12 . VAL   B 1 35  ? 48.509 -16.406 -6.443  1.00 15.77 ?  35  VAL   B HG12 1 
ATOM   4630 H HG13 . VAL   B 1 35  ? 48.449 -17.557 -5.350  1.00 15.77 ?  35  VAL   B HG13 1 
ATOM   4631 H HG21 . VAL   B 1 35  ? 48.828 -19.940 -6.973  1.00 15.55 ?  35  VAL   B HG21 1 
ATOM   4632 H HG22 . VAL   B 1 35  ? 47.609 -19.833 -5.961  1.00 15.55 ?  35  VAL   B HG22 1 
ATOM   4633 H HG23 . VAL   B 1 35  ? 47.345 -20.181 -7.489  1.00 15.55 ?  35  VAL   B HG23 1 
ATOM   4634 N N    . VAL   B 1 36  ? 45.034 -18.860 -5.379  1.00 10.84 ?  36  VAL   B N    1 
ATOM   4635 C CA   . VAL   B 1 36  ? 44.485 -19.061 -4.047  1.00 10.73 ?  36  VAL   B CA   1 
ATOM   4636 C C    . VAL   B 1 36  ? 45.490 -19.821 -3.189  1.00 10.31 ?  36  VAL   B C    1 
ATOM   4637 O O    . VAL   B 1 36  ? 46.027 -20.857 -3.606  1.00 11.48 ?  36  VAL   B O    1 
ATOM   4638 C CB   . VAL   B 1 36  ? 43.149 -19.821 -4.123  1.00 10.99 ?  36  VAL   B CB   1 
ATOM   4639 C CG1  . VAL   B 1 36  ? 42.640 -20.192 -2.731  1.00 12.16 ?  36  VAL   B CG1  1 
ATOM   4640 C CG2  . VAL   B 1 36  ? 42.116 -19.002 -4.871  1.00 11.78 ?  36  VAL   B CG2  1 
ATOM   4641 H H    . VAL   B 1 36  ? 44.864 -19.504 -5.925  1.00 13.05 ?  36  VAL   B H    1 
ATOM   4642 H HA   . VAL   B 1 36  ? 44.319 -18.202 -3.633  1.00 12.92 ?  36  VAL   B HA   1 
ATOM   4643 H HB   . VAL   B 1 36  ? 43.283 -20.646 -4.617  1.00 13.23 ?  36  VAL   B HB   1 
ATOM   4644 H HG11 . VAL   B 1 36  ? 41.703 -20.427 -2.788  1.00 14.63 ?  36  VAL   B HG11 1 
ATOM   4645 H HG12 . VAL   B 1 36  ? 43.152 -20.941 -2.392  1.00 14.63 ?  36  VAL   B HG12 1 
ATOM   4646 H HG13 . VAL   B 1 36  ? 42.749 -19.423 -2.143  1.00 14.63 ?  36  VAL   B HG13 1 
ATOM   4647 H HG21 . VAL   B 1 36  ? 41.278 -19.488 -4.895  1.00 14.18 ?  36  VAL   B HG21 1 
ATOM   4648 H HG22 . VAL   B 1 36  ? 41.995 -18.153 -4.417  1.00 14.18 ?  36  VAL   B HG22 1 
ATOM   4649 H HG23 . VAL   B 1 36  ? 42.432 -18.846 -5.778  1.00 14.18 ?  36  VAL   B HG23 1 
ATOM   4650 N N    . ASN   B 1 37  ? 45.708 -19.334 -1.971  1.00 10.64 ?  37  ASN   B N    1 
ATOM   4651 C CA   . ASN   B 1 37  ? 46.455 -20.059 -0.958  1.00 11.19 ?  37  ASN   B CA   1 
ATOM   4652 C C    . ASN   B 1 37  ? 45.504 -20.722 0.027   1.00 11.40 ?  37  ASN   B C    1 
ATOM   4653 O O    . ASN   B 1 37  ? 44.494 -20.139 0.439   1.00 11.73 ?  37  ASN   B O    1 
ATOM   4654 C CB   . ASN   B 1 37  ? 47.381 -19.111 -0.202  1.00 11.04 ?  37  ASN   B CB   1 
ATOM   4655 C CG   . ASN   B 1 37  ? 48.230 -19.826 0.813   1.00 11.53 ?  37  ASN   B CG   1 
ATOM   4656 O OD1  . ASN   B 1 37  ? 48.567 -21.001 0.639   1.00 12.49 ?  37  ASN   B OD1  1 
ATOM   4657 N ND2  . ASN   B 1 37  ? 48.583 -19.128 1.884   1.00 11.69 ?  37  ASN   B ND2  1 
ATOM   4658 H H    . ASN   B 1 37  ? 45.429 -18.565 -1.705  1.00 12.81 ?  37  ASN   B H    1 
ATOM   4659 H HA   . ASN   B 1 37  ? 46.993 -20.749 -1.374  1.00 13.47 ?  37  ASN   B HA   1 
ATOM   4660 H HB2  . ASN   B 1 37  ? 47.977 -18.682 -0.834  1.00 13.29 ?  37  ASN   B HB2  1 
ATOM   4661 H HB3  . ASN   B 1 37  ? 46.853 -18.448 0.265   1.00 13.29 ?  37  ASN   B HB3  1 
ATOM   4662 H HD21 . ASN   B 1 37  ? 49.081 -19.487 2.489   1.00 14.07 ?  37  ASN   B HD21 1 
ATOM   4663 H HD22 . ASN   B 1 37  ? 48.343 -18.311 1.968   1.00 14.07 ?  37  ASN   B HD22 1 
ATOM   4664 N N    . ALA   B 1 38  ? 45.848 -21.953 0.402   1.00 11.72 ?  38  ALA   B N    1 
ATOM   4665 C CA   . ALA   B 1 38  ? 45.201 -22.697 1.484   1.00 12.09 ?  38  ALA   B CA   1 
ATOM   4666 C C    . ALA   B 1 38  ? 45.787 -22.210 2.809   1.00 11.72 ?  38  ALA   B C    1 
ATOM   4667 O O    . ALA   B 1 38  ? 46.688 -22.820 3.397   1.00 12.69 ?  38  ALA   B O    1 
ATOM   4668 C CB   . ALA   B 1 38  ? 45.424 -24.192 1.302   1.00 13.61 ?  38  ALA   B CB   1 
ATOM   4669 H H    . ALA   B 1 38  ? 46.492 -22.395 0.041   1.00 14.10 ?  38  ALA   B H    1 
ATOM   4670 H HA   . ALA   B 1 38  ? 44.249 -22.518 1.484   1.00 14.55 ?  38  ALA   B HA   1 
ATOM   4671 H HB1  . ALA   B 1 38  ? 44.983 -24.667 2.033   1.00 16.37 ?  38  ALA   B HB1  1 
ATOM   4672 H HB2  . ALA   B 1 38  ? 45.040 -24.466 0.458   1.00 16.37 ?  38  ALA   B HB2  1 
ATOM   4673 H HB3  . ALA   B 1 38  ? 46.372 -24.378 1.320   1.00 16.37 ?  38  ALA   B HB3  1 
ATOM   4674 N N    . ALA   B 1 39  ? 45.267 -21.070 3.271   1.00 11.62 ?  39  ALA   B N    1 
ATOM   4675 C CA   . ALA   B 1 39  ? 45.819 -20.333 4.399   1.00 12.03 ?  39  ALA   B CA   1 
ATOM   4676 C C    . ALA   B 1 39  ? 45.196 -20.779 5.721   1.00 11.90 ?  39  ALA   B C    1 
ATOM   4677 O O    . ALA   B 1 39  ? 44.165 -21.449 5.766   1.00 12.93 ?  39  ALA   B O    1 
ATOM   4678 C CB   . ALA   B 1 39  ? 45.575 -18.834 4.208   1.00 12.49 ?  39  ALA   B CB   1 
ATOM   4679 H H    . ALA   B 1 39  ? 44.573 -20.692 2.929   1.00 13.98 ?  39  ALA   B H    1 
ATOM   4680 H HA   . ALA   B 1 39  ? 46.774 -20.484 4.446   1.00 14.48 ?  39  ALA   B HA   1 
ATOM   4681 H HB1  . ALA   B 1 39  ? 45.945 -18.354 4.965   1.00 15.03 ?  39  ALA   B HB1  1 
ATOM   4682 H HB2  . ALA   B 1 39  ? 46.007 -18.545 3.388   1.00 15.03 ?  39  ALA   B HB2  1 
ATOM   4683 H HB3  . ALA   B 1 39  ? 44.619 -18.673 4.150   1.00 15.03 ?  39  ALA   B HB3  1 
ATOM   4684 N N    . ASN   B 1 40  ? 45.841 -20.369 6.810   1.00 12.65 ?  40  ASN   B N    1 
ATOM   4685 C CA   . ASN   B 1 40  ? 45.276 -20.411 8.150   1.00 13.47 ?  40  ASN   B CA   1 
ATOM   4686 C C    . ASN   B 1 40  ? 45.091 -18.981 8.666   1.00 13.04 ?  40  ASN   B C    1 
ATOM   4687 O O    . ASN   B 1 40  ? 45.495 -18.003 8.030   1.00 12.73 ?  40  ASN   B O    1 
ATOM   4688 C CB   . ASN   B 1 40  ? 46.127 -21.279 9.090   1.00 14.22 ?  40  ASN   B CB   1 
ATOM   4689 C CG   . ASN   B 1 40  ? 47.581 -20.864 9.121   1.00 15.33 ?  40  ASN   B CG   1 
ATOM   4690 O OD1  . ASN   B 1 40  ? 47.896 -19.680 9.204   1.00 17.38 ?  40  ASN   B OD1  1 
ATOM   4691 N ND2  . ASN   B 1 40  ? 48.477 -21.837 9.064   1.00 15.65 ?  40  ASN   B ND2  1 
ATOM   4692 H H    . ASN   B 1 40  ? 46.640 -20.050 6.788   1.00 15.21 ?  40  ASN   B H    1 
ATOM   4693 H HA   . ASN   B 1 40  ? 44.395 -20.809 8.099   1.00 16.20 ?  40  ASN   B HA   1 
ATOM   4694 H HB2  . ASN   B 1 40  ? 45.770 -21.208 9.988   1.00 17.10 ?  40  ASN   B HB2  1 
ATOM   4695 H HB3  . ASN   B 1 40  ? 46.081 -22.200 8.786   1.00 17.10 ?  40  ASN   B HB3  1 
ATOM   4696 H HD21 . ASN   B 1 40  ? 49.317 -21.652 9.082   1.00 18.82 ?  40  ASN   B HD21 1 
ATOM   4697 H HD22 . ASN   B 1 40  ? 48.219 -22.656 9.008   1.00 18.82 ?  40  ASN   B HD22 1 
ATOM   4698 N N    . VAL   B 1 41  ? 44.434 -18.850 9.820   1.00 13.40 ?  41  VAL   B N    1 
ATOM   4699 C CA   . VAL   B 1 41  ? 43.974 -17.528 10.263  1.00 13.96 ?  41  VAL   B CA   1 
ATOM   4700 C C    . VAL   B 1 41  ? 45.124 -16.569 10.551  1.00 13.94 ?  41  VAL   B C    1 
ATOM   4701 O O    . VAL   B 1 41  ? 44.943 -15.347 10.468  1.00 14.08 ?  41  VAL   B O    1 
ATOM   4702 C CB   . VAL   B 1 41  ? 43.007 -17.604 11.462  1.00 15.69 ?  41  VAL   B CB   1 
ATOM   4703 C CG1  . VAL   B 1 41  ? 41.694 -18.275 11.068  1.00 16.04 ?  41  VAL   B CG1  1 
ATOM   4704 C CG2  . VAL   B 1 41  ? 43.672 -18.286 12.654  1.00 16.84 ?  41  VAL   B CG2  1 
ATOM   4705 H H    . VAL   B 1 41  ? 44.243 -19.492 10.348  1.00 16.12 ?  41  VAL   B H    1 
ATOM   4706 H HA   . VAL   B 1 41  ? 43.470 -17.136 9.534   1.00 16.80 ?  41  VAL   B HA   1 
ATOM   4707 H HB   . VAL   B 1 41  ? 42.791 -16.699 11.737  1.00 18.87 ?  41  VAL   B HB   1 
ATOM   4708 H HG11 . VAL   B 1 41  ? 41.098 -18.280 11.835  1.00 19.29 ?  41  VAL   B HG11 1 
ATOM   4709 H HG12 . VAL   B 1 41  ? 41.291 -17.779 10.339  1.00 19.29 ?  41  VAL   B HG12 1 
ATOM   4710 H HG13 . VAL   B 1 41  ? 41.877 -19.186 10.788  1.00 19.29 ?  41  VAL   B HG13 1 
ATOM   4711 H HG21 . VAL   B 1 41  ? 43.042 -18.324 13.391  1.00 20.25 ?  41  VAL   B HG21 1 
ATOM   4712 H HG22 . VAL   B 1 41  ? 43.934 -19.187 12.400  1.00 20.25 ?  41  VAL   B HG22 1 
ATOM   4713 H HG23 . VAL   B 1 41  ? 44.455 -17.777 12.916  1.00 20.25 ?  41  VAL   B HG23 1 
ATOM   4714 N N    . TYR   B 1 42  ? 46.294 -17.082 10.933  1.00 14.01 ?  42  TYR   B N    1 
ATOM   4715 C CA   . TYR   B 1 42  ? 47.447 -16.236 11.201  1.00 14.46 ?  42  TYR   B CA   1 
ATOM   4716 C C    . TYR   B 1 42  ? 48.416 -16.173 10.024  1.00 13.92 ?  42  TYR   B C    1 
ATOM   4717 O O    . TYR   B 1 42  ? 49.505 -15.601 10.159  1.00 15.04 ?  42  TYR   B O    1 
ATOM   4718 C CB   . TYR   B 1 42  ? 48.134 -16.638 12.511  1.00 16.39 ?  42  TYR   B CB   1 
ATOM   4719 C CG   . TYR   B 1 42  ? 47.551 -15.929 13.731  1.00 16.45 ?  42  TYR   B CG   1 
ATOM   4720 C CD1  . TYR   B 1 42  ? 47.780 -14.571 13.935  1.00 15.77 ?  42  TYR   B CD1  1 
ATOM   4721 C CD2  . TYR   B 1 42  ? 46.783 -16.604 14.671  1.00 17.78 ?  42  TYR   B CD2  1 
ATOM   4722 C CE1  . TYR   B 1 42  ? 47.261 -13.906 15.025  1.00 16.65 ?  42  TYR   B CE1  1 
ATOM   4723 C CE2  . TYR   B 1 42  ? 46.258 -15.940 15.781  1.00 17.82 ?  42  TYR   B CE2  1 
ATOM   4724 C CZ   . TYR   B 1 42  ? 46.509 -14.583 15.951  1.00 17.89 ?  42  TYR   B CZ   1 
ATOM   4725 O OH   . TYR   B 1 42  ? 46.016 -13.884 17.042  1.00 20.30 ?  42  TYR   B OH   1 
ATOM   4726 H H    . TYR   B 1 42  ? 46.447 -17.927 11.029  1.00 16.85 ?  42  TYR   B H    1 
ATOM   4727 H HA   . TYR   B 1 42  ? 47.121 -15.334 11.327  1.00 17.39 ?  42  TYR   B HA   1 
ATOM   4728 H HB2  . TYR   B 1 42  ? 48.030 -17.593 12.639  1.00 19.71 ?  42  TYR   B HB2  1 
ATOM   4729 H HB3  . TYR   B 1 42  ? 49.077 -16.413 12.451  1.00 19.71 ?  42  TYR   B HB3  1 
ATOM   4730 H HD1  . TYR   B 1 42  ? 48.295 -14.099 13.311  1.00 18.97 ?  42  TYR   B HD1  1 
ATOM   4731 H HD2  . TYR   B 1 42  ? 46.614 -17.514 14.555  1.00 21.38 ?  42  TYR   B HD2  1 
ATOM   4732 H HE1  . TYR   B 1 42  ? 47.434 -13.001 15.136  1.00 20.02 ?  42  TYR   B HE1  1 
ATOM   4733 H HE2  . TYR   B 1 42  ? 45.744 -16.404 16.401  1.00 21.42 ?  42  TYR   B HE2  1 
ATOM   4734 H HH   . TYR   B 1 42  ? 46.253 -13.080 16.986  1.00 24.40 ?  42  TYR   B HH   1 
ATOM   4735 N N    . LEU   B 1 43  ? 48.019 -16.686 8.860   1.00 12.88 ?  43  LEU   B N    1 
ATOM   4736 C CA   . LEU   B 1 43  ? 48.843 -16.617 7.654   1.00 12.72 ?  43  LEU   B CA   1 
ATOM   4737 C C    . LEU   B 1 43  ? 50.255 -17.124 7.918   1.00 12.69 ?  43  LEU   B C    1 
ATOM   4738 O O    . LEU   B 1 43  ? 51.237 -16.529 7.472   1.00 13.71 ?  43  LEU   B O    1 
ATOM   4739 C CB   . LEU   B 1 43  ? 48.862 -15.212 7.042   1.00 12.70 ?  43  LEU   B CB   1 
ATOM   4740 C CG   . LEU   B 1 43  ? 47.505 -14.593 6.676   1.00 13.06 ?  43  LEU   B CG   1 
ATOM   4741 C CD1  . LEU   B 1 43  ? 47.708 -13.201 6.087   1.00 14.45 ?  43  LEU   B CD1  1 
ATOM   4742 C CD2  . LEU   B 1 43  ? 46.726 -15.485 5.720   1.00 13.45 ?  43  LEU   B CD2  1 
ATOM   4743 H H    . LEU   B 1 43  ? 47.272 -17.095 8.743   1.00 15.50 ?  43  LEU   B H    1 
ATOM   4744 H HA   . LEU   B 1 43  ? 48.445 -17.207 6.988   1.00 15.30 ?  43  LEU   B HA   1 
ATOM   4745 H HB2  . LEU   B 1 43  ? 49.291 -14.616 7.672   1.00 15.28 ?  43  LEU   B HB2  1 
ATOM   4746 H HB3  . LEU   B 1 43  ? 49.387 -15.249 6.225   1.00 15.28 ?  43  LEU   B HB3  1 
ATOM   4747 H HG   . LEU   B 1 43  ? 46.981 -14.498 7.485   1.00 15.71 ?  43  LEU   B HG   1 
ATOM   4748 H HD11 . LEU   B 1 43  ? 46.840 -12.824 5.865   1.00 17.37 ?  43  LEU   B HD11 1 
ATOM   4749 H HD12 . LEU   B 1 43  ? 48.149 -12.641 6.746   1.00 17.37 ?  43  LEU   B HD12 1 
ATOM   4750 H HD13 . LEU   B 1 43  ? 48.253 -13.268 5.290   1.00 17.37 ?  43  LEU   B HD13 1 
ATOM   4751 H HD21 . LEU   B 1 43  ? 45.926 -15.017 5.436   1.00 16.18 ?  43  LEU   B HD21 1 
ATOM   4752 H HD22 . LEU   B 1 43  ? 47.283 -15.689 4.954   1.00 16.18 ?  43  LEU   B HD22 1 
ATOM   4753 H HD23 . LEU   B 1 43  ? 46.484 -16.304 6.182   1.00 16.18 ?  43  LEU   B HD23 1 
ATOM   4754 N N    . LYS   B 1 44  ? 50.352 -18.247 8.630   1.00 12.94 ?  44  LYS   B N    1 
ATOM   4755 C CA   . LYS   B 1 44  ? 51.618 -18.924 8.883   1.00 13.87 ?  44  LYS   B CA   1 
ATOM   4756 C C    . LYS   B 1 44  ? 51.741 -20.047 7.864   1.00 13.27 ?  44  LYS   B C    1 
ATOM   4757 O O    . LYS   B 1 44  ? 51.044 -21.061 7.955   1.00 14.66 ?  44  LYS   B O    1 
ATOM   4758 C CB   . LYS   B 1 44  ? 51.660 -19.422 10.327  1.00 15.52 ?  44  LYS   B CB   1 
ATOM   4759 C CG   . LYS   B 1 44  ? 51.877 -18.297 11.327  1.00 18.70 ?  44  LYS   B CG   1 
ATOM   4760 C CD   . LYS   B 1 44  ? 53.080 -17.453 10.889  1.00 22.31 ?  44  LYS   B CD   1 
ATOM   4761 C CE   . LYS   B 1 44  ? 53.587 -16.520 11.954  1.00 25.56 ?  44  LYS   B CE   1 
ATOM   4762 N NZ   . LYS   B 1 44  ? 54.809 -15.785 11.537  1.00 27.18 ?  44  LYS   B NZ   1 
ATOM   4763 H H    . LYS   B 1 44  ? 49.675 -18.640 8.986   1.00 15.56 ?  44  LYS   B H    1 
ATOM   4764 H HA   . LYS   B 1 44  ? 52.349 -18.315 8.712   1.00 16.68 ?  44  LYS   B HA   1 
ATOM   4765 H HB2  . LYS   B 1 44  ? 50.806 -19.843 10.540  1.00 18.67 ?  44  LYS   B HB2  1 
ATOM   4766 H HB3  . LYS   B 1 44  ? 52.377 -20.056 10.426  1.00 18.67 ?  44  LYS   B HB3  1 
ATOM   4767 H HG2  . LYS   B 1 44  ? 51.093 -17.732 11.365  1.00 22.48 ?  44  LYS   B HG2  1 
ATOM   4768 H HG3  . LYS   B 1 44  ? 52.068 -18.678 12.204  1.00 22.48 ?  44  LYS   B HG3  1 
ATOM   4769 H HD2  . LYS   B 1 44  ? 53.801 -18.056 10.621  1.00 26.81 ?  44  LYS   B HD2  1 
ATOM   4770 H HD3  . LYS   B 1 44  ? 52.814 -16.908 10.132  1.00 26.81 ?  44  LYS   B HD3  1 
ATOM   4771 H HE2  . LYS   B 1 44  ? 52.896 -15.872 12.148  1.00 30.71 ?  44  LYS   B HE2  1 
ATOM   4772 H HE3  . LYS   B 1 44  ? 53.806 -17.037 12.736  1.00 30.71 ?  44  LYS   B HE3  1 
ATOM   4773 H HZ1  . LYS   B 1 44  ? 55.060 -15.228 12.184  1.00 32.65 ?  44  LYS   B HZ1  1 
ATOM   4774 H HZ2  . LYS   B 1 44  ? 55.471 -16.356 11.373  1.00 32.65 ?  44  LYS   B HZ2  1 
ATOM   4775 H HZ3  . LYS   B 1 44  ? 54.647 -15.312 10.798  1.00 32.65 ?  44  LYS   B HZ3  1 
ATOM   4776 N N    . HIS   B 1 45  ? 52.591 -19.833 6.863   1.00 12.87 ?  45  HIS   B N    1 
ATOM   4777 C CA   . HIS   B 1 45  ? 52.611 -20.665 5.660   1.00 13.36 ?  45  HIS   B CA   1 
ATOM   4778 C C    . HIS   B 1 45  ? 53.631 -21.786 5.821   1.00 15.26 ?  45  HIS   B C    1 
ATOM   4779 O O    . HIS   B 1 45  ? 54.696 -21.795 5.212   1.00 17.98 ?  45  HIS   B O    1 
ATOM   4780 C CB   . HIS   B 1 45  ? 52.927 -19.811 4.445   1.00 13.40 ?  45  HIS   B CB   1 
ATOM   4781 C CG   . HIS   B 1 45  ? 52.059 -18.606 4.333   1.00 13.23 ?  45  HIS   B CG   1 
ATOM   4782 N ND1  . HIS   B 1 45  ? 50.681 -18.685 4.289   1.00 13.21 ?  45  HIS   B ND1  1 
ATOM   4783 C CD2  . HIS   B 1 45  ? 52.377 -17.293 4.257   1.00 13.78 ?  45  HIS   B CD2  1 
ATOM   4784 C CE1  . HIS   B 1 45  ? 50.195 -17.461 4.181   1.00 12.84 ?  45  HIS   B CE1  1 
ATOM   4785 N NE2  . HIS   B 1 45  ? 51.198 -16.600 4.157   1.00 13.72 ?  45  HIS   B NE2  1 
ATOM   4786 H H    . HIS   B 1 45  ? 53.167 -19.191 6.852   1.00 15.49 ?  45  HIS   B H    1 
ATOM   4787 H HA   . HIS   B 1 45  ? 51.730 -21.060 5.531   1.00 16.07 ?  45  HIS   B HA   1 
ATOM   4788 H HB2  . HIS   B 1 45  ? 53.847 -19.516 4.497   1.00 16.12 ?  45  HIS   B HB2  1 
ATOM   4789 H HB3  . HIS   B 1 45  ? 52.800 -20.350 3.642   1.00 16.12 ?  45  HIS   B HB3  1 
ATOM   4790 H HD2  . HIS   B 1 45  ? 53.235 -16.929 4.263   1.00 16.58 ?  45  HIS   B HD2  1 
ATOM   4791 H HE1  . HIS   B 1 45  ? 49.295 -17.241 4.121   1.00 15.44 ?  45  HIS   B HE1  1 
ATOM   4792 H HE2  . HIS   B 1 45  ? 51.125 -15.745 4.099   1.00 16.51 ?  45  HIS   B HE2  1 
ATOM   4793 N N    A GLY   B 1 46  ? 53.264 -22.760 6.645   0.72 16.10 ?  46  GLY   B N    1 
ATOM   4794 N N    B GLY   B 1 46  ? 53.272 -22.746 6.664   0.28 16.28 ?  46  GLY   B N    1 
ATOM   4795 C CA   A GLY   B 1 46  ? 54.188 -23.811 7.026   0.72 18.10 ?  46  GLY   B CA   1 
ATOM   4796 C CA   B GLY   B 1 46  ? 54.190 -23.810 7.010   0.28 17.62 ?  46  GLY   B CA   1 
ATOM   4797 C C    A GLY   B 1 46  ? 54.234 -25.038 6.135   0.72 19.80 ?  46  GLY   B C    1 
ATOM   4798 C C    B GLY   B 1 46  ? 54.219 -24.963 6.027   0.28 18.83 ?  46  GLY   B C    1 
ATOM   4799 O O    A GLY   B 1 46  ? 55.313 -25.482 5.734   0.72 22.74 ?  46  GLY   B O    1 
ATOM   4800 O O    B GLY   B 1 46  ? 55.259 -25.254 5.428   0.28 19.71 ?  46  GLY   B O    1 
ATOM   4801 H H    A GLY   B 1 46  ? 52.488 -22.816 7.019   0.72 19.36 ?  46  GLY   B H    1 
ATOM   4802 H H    B GLY   B 1 46  ? 52.503 -22.793 7.055   0.28 19.58 ?  46  GLY   B H    1 
ATOM   4803 H HA2  A GLY   B 1 46  ? 55.082 -23.436 7.066   0.72 21.76 ?  46  GLY   B HA2  1 
ATOM   4804 H HA2  B GLY   B 1 46  ? 55.085 -23.441 7.070   0.28 21.19 ?  46  GLY   B HA2  1 
ATOM   4805 H HA3  A GLY   B 1 46  ? 53.956 -24.117 7.917   0.72 21.76 ?  46  GLY   B HA3  1 
ATOM   4806 H HA3  B GLY   B 1 46  ? 53.949 -24.157 7.883   0.28 21.19 ?  46  GLY   B HA3  1 
ATOM   4807 N N    . GLY   B 1 47  ? 53.078 -25.620 5.833   1.00 19.38 ?  47  GLY   B N    1 
ATOM   4808 C CA   . GLY   B 1 47  ? 53.023 -26.888 5.134   1.00 17.35 ?  47  GLY   B CA   1 
ATOM   4809 C C    . GLY   B 1 47  ? 52.105 -26.868 3.929   1.00 15.11 ?  47  GLY   B C    1 
ATOM   4810 O O    . GLY   B 1 47  ? 51.447 -25.869 3.641   1.00 15.10 ?  47  GLY   B O    1 
ATOM   4811 H H    A GLY   B 1 47  ? 52.304 -25.304 6.044   0.72 23.30 ?  47  GLY   B H    1 
ATOM   4812 H H    B GLY   B 1 47  ? 52.308 -25.339 6.102   0.28 23.30 ?  47  GLY   B H    1 
ATOM   4813 H HA2  . GLY   B 1 47  ? 53.910 -27.132 4.828   1.00 20.86 ?  47  GLY   B HA2  1 
ATOM   4814 H HA3  . GLY   B 1 47  ? 52.713 -27.573 5.745   1.00 20.86 ?  47  GLY   B HA3  1 
ATOM   4815 N N    . GLY   B 1 48  ? 52.054 -28.012 3.243   1.00 14.20 ?  48  GLY   B N    1 
ATOM   4816 C CA   . GLY   B 1 48  ? 51.126 -28.159 2.137   1.00 14.22 ?  48  GLY   B CA   1 
ATOM   4817 C C    . GLY   B 1 48  ? 51.265 -27.049 1.122   1.00 13.34 ?  48  GLY   B C    1 
ATOM   4818 O O    . GLY   B 1 48  ? 52.369 -26.580 0.815   1.00 13.87 ?  48  GLY   B O    1 
ATOM   4819 H H    . GLY   B 1 48  ? 52.542 -28.698 3.398   1.00 17.08 ?  48  GLY   B H    1 
ATOM   4820 H HA2  . GLY   B 1 48  ? 51.287 -29.008 1.692   1.00 17.10 ?  48  GLY   B HA2  1 
ATOM   4821 H HA3  . GLY   B 1 48  ? 50.216 -28.155 2.469   1.00 17.10 ?  48  GLY   B HA3  1 
ATOM   4822 N N    . VAL   B 1 49  ? 50.121 -26.620 0.587   1.00 12.93 ?  49  VAL   B N    1 
ATOM   4823 C CA   . VAL   B 1 49  ? 50.110 -25.595 -0.454  1.00 13.12 ?  49  VAL   B CA   1 
ATOM   4824 C C    . VAL   B 1 49  ? 50.768 -24.307 0.036   1.00 12.21 ?  49  VAL   B C    1 
ATOM   4825 O O    . VAL   B 1 49  ? 51.555 -23.686 -0.684  1.00 12.92 ?  49  VAL   B O    1 
ATOM   4826 C CB   . VAL   B 1 49  ? 48.669 -25.342 -0.943  1.00 14.27 ?  49  VAL   B CB   1 
ATOM   4827 C CG1  . VAL   B 1 49  ? 48.591 -24.082 -1.808  1.00 14.48 ?  49  VAL   B CG1  1 
ATOM   4828 C CG2  . VAL   B 1 49  ? 48.138 -26.552 -1.710  1.00 16.13 ?  49  VAL   B CG2  1 
ATOM   4829 H H    . VAL   B 1 49  ? 49.337 -26.900 0.808   1.00 15.55 ?  49  VAL   B H    1 
ATOM   4830 H HA   . VAL   B 1 49  ? 50.616 -25.914 -1.215  1.00 15.78 ?  49  VAL   B HA   1 
ATOM   4831 H HB   . VAL   B 1 49  ? 48.091 -25.205 -0.178  1.00 17.16 ?  49  VAL   B HB   1 
ATOM   4832 H HG11 . VAL   B 1 49  ? 47.758 -24.091 -2.311  1.00 17.42 ?  49  VAL   B HG11 1 
ATOM   4833 H HG12 . VAL   B 1 49  ? 48.612 -23.298 -1.234  1.00 17.42 ?  49  VAL   B HG12 1 
ATOM   4834 H HG13 . VAL   B 1 49  ? 49.342 -24.066 -2.419  1.00 17.42 ?  49  VAL   B HG13 1 
ATOM   4835 H HG21 . VAL   B 1 49  ? 47.232 -26.370 -2.006  1.00 19.40 ?  49  VAL   B HG21 1 
ATOM   4836 H HG22 . VAL   B 1 49  ? 48.709 -26.713 -2.479  1.00 19.40 ?  49  VAL   B HG22 1 
ATOM   4837 H HG23 . VAL   B 1 49  ? 48.147 -27.322 -1.124  1.00 19.40 ?  49  VAL   B HG23 1 
ATOM   4838 N N    . ALA   B 1 50  ? 50.421 -23.860 1.244   1.00 12.34 ?  50  ALA   B N    1 
ATOM   4839 C CA   . ALA   B 1 50  ? 50.946 -22.584 1.723   1.00 12.13 ?  50  ALA   B CA   1 
ATOM   4840 C C    . ALA   B 1 50  ? 52.466 -22.617 1.828   1.00 12.36 ?  50  ALA   B C    1 
ATOM   4841 O O    . ALA   B 1 50  ? 53.149 -21.647 1.460   1.00 12.14 ?  50  ALA   B O    1 
ATOM   4842 C CB   . ALA   B 1 50  ? 50.317 -22.232 3.068   1.00 12.22 ?  50  ALA   B CB   1 
ATOM   4843 H H    . ALA   B 1 50  ? 49.891 -24.263 1.789   1.00 14.85 ?  50  ALA   B H    1 
ATOM   4844 H HA   . ALA   B 1 50  ? 50.713 -21.889 1.094   1.00 14.59 ?  50  ALA   B HA   1 
ATOM   4845 H HB1  . ALA   B 1 50  ? 50.679 -21.383 3.374   1.00 14.70 ?  50  ALA   B HB1  1 
ATOM   4846 H HB2  . ALA   B 1 50  ? 49.357 -22.161 2.960   1.00 14.70 ?  50  ALA   B HB2  1 
ATOM   4847 H HB3  . ALA   B 1 50  ? 50.528 -22.929 3.710   1.00 14.70 ?  50  ALA   B HB3  1 
ATOM   4848 N N    . GLY   B 1 51  ? 53.016 -23.712 2.345   1.00 12.69 ?  51  GLY   B N    1 
ATOM   4849 C CA   . GLY   B 1 51  ? 54.462 -23.820 2.419   1.00 13.83 ?  51  GLY   B CA   1 
ATOM   4850 C C    . GLY   B 1 51  ? 55.112 -23.775 1.052   1.00 13.61 ?  51  GLY   B C    1 
ATOM   4851 O O    . GLY   B 1 51  ? 56.153 -23.137 0.870   1.00 14.22 ?  51  GLY   B O    1 
ATOM   4852 H H    . GLY   B 1 51  ? 52.587 -24.393 2.653   1.00 15.26 ?  51  GLY   B H    1 
ATOM   4853 H HA2  . GLY   B 1 51  ? 54.818 -23.089 2.949   1.00 16.64 ?  51  GLY   B HA2  1 
ATOM   4854 H HA3  . GLY   B 1 51  ? 54.710 -24.657 2.843   1.00 16.64 ?  51  GLY   B HA3  1 
ATOM   4855 N N    . ALA   B 1 52  ? 54.504 -24.436 0.068   1.00 13.04 ?  52  ALA   B N    1 
ATOM   4856 C CA   . ALA   B 1 52  ? 55.061 -24.444 -1.278  1.00 13.35 ?  52  ALA   B CA   1 
ATOM   4857 C C    . ALA   B 1 52  ? 54.986 -23.064 -1.925  1.00 12.88 ?  52  ALA   B C    1 
ATOM   4858 O O    . ALA   B 1 52  ? 55.962 -22.609 -2.542  1.00 13.80 ?  52  ALA   B O    1 
ATOM   4859 C CB   . ALA   B 1 52  ? 54.344 -25.482 -2.135  1.00 14.02 ?  52  ALA   B CB   1 
ATOM   4860 H H    . ALA   B 1 52  ? 53.766 -24.874 0.154   1.00 15.69 ?  52  ALA   B H    1 
ATOM   4861 H HA   . ALA   B 1 52  ? 55.994 -24.695 -1.222  1.00 16.06 ?  52  ALA   B HA   1 
ATOM   4862 H HB1  . ALA   B 1 52  ? 54.734 -25.475 -3.025  1.00 16.87 ?  52  ALA   B HB1  1 
ATOM   4863 H HB2  . ALA   B 1 52  ? 54.461 -26.356 -1.731  1.00 16.87 ?  52  ALA   B HB2  1 
ATOM   4864 H HB3  . ALA   B 1 52  ? 53.404 -25.259 -2.182  1.00 16.87 ?  52  ALA   B HB3  1 
ATOM   4865 N N    . LEU   B 1 53  ? 53.841 -22.384 -1.809  1.00 12.35 ?  53  LEU   B N    1 
ATOM   4866 C CA   . LEU   B 1 53  ? 53.735 -21.043 -2.382  1.00 12.58 ?  53  LEU   B CA   1 
ATOM   4867 C C    . LEU   B 1 53  ? 54.744 -20.101 -1.734  1.00 12.68 ?  53  LEU   B C    1 
ATOM   4868 O O    . LEU   B 1 53  ? 55.457 -19.355 -2.420  1.00 13.31 ?  53  LEU   B O    1 
ATOM   4869 C CB   . LEU   B 1 53  ? 52.314 -20.494 -2.219  1.00 13.06 ?  53  LEU   B CB   1 
ATOM   4870 C CG   . LEU   B 1 53  ? 51.175 -21.220 -2.940  1.00 13.41 ?  53  LEU   B CG   1 
ATOM   4871 C CD1  . LEU   B 1 53  ? 49.837 -20.607 -2.589  1.00 14.94 ?  53  LEU   B CD1  1 
ATOM   4872 C CD2  . LEU   B 1 53  ? 51.373 -21.226 -4.450  1.00 15.21 ?  53  LEU   B CD2  1 
ATOM   4873 H H    . LEU   B 1 53  ? 53.136 -22.664 -1.411  1.00 14.86 ?  53  LEU   B H    1 
ATOM   4874 H HA   . LEU   B 1 53  ? 53.939 -21.090 -3.334  1.00 15.14 ?  53  LEU   B HA   1 
ATOM   4875 H HB2  . LEU   B 1 53  ? 52.102 -20.501 -1.276  1.00 15.71 ?  53  LEU   B HB2  1 
ATOM   4876 H HB3  . LEU   B 1 53  ? 52.311 -19.580 -2.541  1.00 15.71 ?  53  LEU   B HB3  1 
ATOM   4877 H HG   . LEU   B 1 53  ? 51.156 -22.142 -2.641  1.00 16.13 ?  53  LEU   B HG   1 
ATOM   4878 H HD11 . LEU   B 1 53  ? 49.136 -21.093 -3.057  1.00 17.97 ?  53  LEU   B HD11 1 
ATOM   4879 H HD12 . LEU   B 1 53  ? 49.699 -20.679 -1.630  1.00 17.97 ?  53  LEU   B HD12 1 
ATOM   4880 H HD13 . LEU   B 1 53  ? 49.832 -19.679 -2.858  1.00 17.97 ?  53  LEU   B HD13 1 
ATOM   4881 H HD21 . LEU   B 1 53  ? 50.658 -21.738 -4.862  1.00 18.29 ?  53  LEU   B HD21 1 
ATOM   4882 H HD22 . LEU   B 1 53  ? 51.355 -20.314 -4.777  1.00 18.29 ?  53  LEU   B HD22 1 
ATOM   4883 H HD23 . LEU   B 1 53  ? 52.229 -21.636 -4.656  1.00 18.29 ?  53  LEU   B HD23 1 
ATOM   4884 N N    . ASN   B 1 54  ? 54.829 -20.124 -0.407  1.00 12.32 ?  54  ASN   B N    1 
ATOM   4885 C CA   . ASN   B 1 54  ? 55.748 -19.219 0.265   1.00 13.04 ?  54  ASN   B CA   1 
ATOM   4886 C C    . ASN   B 1 54  ? 57.194 -19.501 -0.135  1.00 13.31 ?  54  ASN   B C    1 
ATOM   4887 O O    . ASN   B 1 54  ? 57.975 -18.566 -0.364  1.00 14.02 ?  54  ASN   B O    1 
ATOM   4888 C CB   . ASN   B 1 54  ? 55.596 -19.304 1.774   1.00 13.81 ?  54  ASN   B CB   1 
ATOM   4889 C CG   . ASN   B 1 54  ? 56.567 -18.381 2.481   1.00 14.05 ?  54  ASN   B CG   1 
ATOM   4890 O OD1  . ASN   B 1 54  ? 56.579 -17.169 2.231   1.00 14.23 ?  54  ASN   B OD1  1 
ATOM   4891 N ND2  . ASN   B 1 54  ? 57.411 -18.943 3.343   1.00 15.36 ?  54  ASN   B ND2  1 
ATOM   4892 H H    . ASN   B 1 54  ? 54.381 -20.646 0.109   1.00 14.83 ?  54  ASN   B H    1 
ATOM   4893 H HA   . ASN   B 1 54  ? 55.540 -18.313 -0.006  1.00 15.68 ?  54  ASN   B HA   1 
ATOM   4894 H HB2  . ASN   B 1 54  ? 54.694 -19.040 2.020   1.00 16.61 ?  54  ASN   B HB2  1 
ATOM   4895 H HB3  . ASN   B 1 54  ? 55.771 -20.211 2.066   1.00 16.61 ?  54  ASN   B HB3  1 
ATOM   4896 H HD21 . ASN   B 1 54  ? 57.986 -18.462 3.765   1.00 18.47 ?  54  ASN   B HD21 1 
ATOM   4897 H HD22 . ASN   B 1 54  ? 57.384 -19.794 3.481   1.00 18.47 ?  54  ASN   B HD22 1 
ATOM   4898 N N    . LYS   B 1 55  ? 57.578 -20.780 -0.193  1.00 13.88 ?  55  LYS   B N    1 
ATOM   4899 C CA   . LYS   B 1 55  ? 58.932 -21.129 -0.616  1.00 14.92 ?  55  LYS   B CA   1 
ATOM   4900 C C    . LYS   B 1 55  ? 59.227 -20.586 -2.008  1.00 14.60 ?  55  LYS   B C    1 
ATOM   4901 O O    . LYS   B 1 55  ? 60.326 -20.083 -2.265  1.00 15.59 ?  55  LYS   B O    1 
ATOM   4902 C CB   . LYS   B 1 55  ? 59.112 -22.649 -0.576  1.00 16.64 ?  55  LYS   B CB   1 
ATOM   4903 C CG   . LYS   B 1 55  ? 60.487 -23.119 -1.017  1.00 20.92 ?  55  LYS   B CG   1 
ATOM   4904 C CD   . LYS   B 1 55  ? 60.656 -24.617 -0.837  1.00 24.63 ?  55  LYS   B CD   1 
ATOM   4905 C CE   . LYS   B 1 55  ? 60.700 -25.012 0.637   1.00 27.56 ?  55  LYS   B CE   1 
ATOM   4906 N NZ   . LYS   B 1 55  ? 61.033 -26.443 0.826   1.00 29.19 ?  55  LYS   B NZ   1 
ATOM   4907 H H    . LYS   B 1 55  ? 57.076 -21.451 0.000   1.00 16.69 ?  55  LYS   B H    1 
ATOM   4908 H HA   . LYS   B 1 55  ? 59.568 -20.736 -0.001  1.00 17.95 ?  55  LYS   B HA   1 
ATOM   4909 H HB2  . LYS   B 1 55  ? 58.967 -22.948 0.338   1.00 20.00 ?  55  LYS   B HB2  1 
ATOM   4910 H HB3  . LYS   B 1 55  ? 58.453 -23.058 -1.159  1.00 20.00 ?  55  LYS   B HB3  1 
ATOM   4911 H HG2  . LYS   B 1 55  ? 60.606 -22.912 -1.957  1.00 25.15 ?  55  LYS   B HG2  1 
ATOM   4912 H HG3  . LYS   B 1 55  ? 61.161 -22.669 -0.486  1.00 25.15 ?  55  LYS   B HG3  1 
ATOM   4913 H HD2  . LYS   B 1 55  ? 59.908 -25.081 -1.250  1.00 29.59 ?  55  LYS   B HD2  1 
ATOM   4914 H HD3  . LYS   B 1 55  ? 61.489 -24.899 -1.248  1.00 29.59 ?  55  LYS   B HD3  1 
ATOM   4915 H HE2  . LYS   B 1 55  ? 61.375 -24.473 1.084   1.00 33.11 ?  55  LYS   B HE2  1 
ATOM   4916 H HE3  . LYS   B 1 55  ? 59.829 -24.844 1.034   1.00 33.11 ?  55  LYS   B HE3  1 
ATOM   4917 H HZ1  . LYS   B 1 55  ? 61.022 -26.641 1.694   1.00 35.06 ?  55  LYS   B HZ1  1 
ATOM   4918 H HZ2  . LYS   B 1 55  ? 60.434 -26.949 0.406   1.00 35.06 ?  55  LYS   B HZ2  1 
ATOM   4919 H HZ3  . LYS   B 1 55  ? 61.840 -26.611 0.498   1.00 35.06 ?  55  LYS   B HZ3  1 
ATOM   4920 N N    . ALA   B 1 56  ? 58.256 -20.675 -2.922  1.00 14.23 ?  56  ALA   B N    1 
ATOM   4921 C CA   . ALA   B 1 56  ? 58.479 -20.177 -4.274  1.00 15.06 ?  56  ALA   B CA   1 
ATOM   4922 C C    . ALA   B 1 56  ? 58.759 -18.680 -4.274  1.00 14.79 ?  56  ALA   B C    1 
ATOM   4923 O O    . ALA   B 1 56  ? 59.500 -18.187 -5.136  1.00 15.86 ?  56  ALA   B O    1 
ATOM   4924 C CB   . ALA   B 1 56  ? 57.282 -20.505 -5.165  1.00 16.16 ?  56  ALA   B CB   1 
ATOM   4925 H H    . ALA   B 1 56  ? 57.469 -20.998 -2.783  1.00 17.12 ?  56  ALA   B H    1 
ATOM   4926 H HA   . ALA   B 1 56  ? 59.255 -20.617 -4.645  1.00 18.12 ?  56  ALA   B HA   1 
ATOM   4927 H HB1  . ALA   B 1 56  ? 57.452 -20.169 -6.062  1.00 19.43 ?  56  ALA   B HB1  1 
ATOM   4928 H HB2  . ALA   B 1 56  ? 57.164 -21.468 -5.193  1.00 19.43 ?  56  ALA   B HB2  1 
ATOM   4929 H HB3  . ALA   B 1 56  ? 56.487 -20.084 -4.802  1.00 19.43 ?  56  ALA   B HB3  1 
ATOM   4930 N N    . THR   B 1 57  ? 58.188 -17.943 -3.318  1.00 14.61 ?  57  THR   B N    1 
ATOM   4931 C CA   . THR   B 1 57  ? 58.430 -16.508 -3.198  1.00 14.62 ?  57  THR   B CA   1 
ATOM   4932 C C    . THR   B 1 57  ? 59.683 -16.181 -2.391  1.00 15.25 ?  57  THR   B C    1 
ATOM   4933 O O    . THR   B 1 57  ? 59.922 -15.006 -2.093  1.00 15.62 ?  57  THR   B O    1 
ATOM   4934 C CB   . THR   B 1 57  ? 57.228 -15.775 -2.571  1.00 13.64 ?  57  THR   B CB   1 
ATOM   4935 O OG1  . THR   B 1 57  ? 57.203 -15.977 -1.154  1.00 14.37 ?  57  THR   B OG1  1 
ATOM   4936 C CG2  . THR   B 1 57  ? 55.906 -16.207 -3.204  1.00 13.89 ?  57  THR   B CG2  1 
ATOM   4937 H H    . THR   B 1 57  ? 57.637 -18.251 -2.726  1.00 17.57 ?  57  THR   B H    1 
ATOM   4938 H HA   . THR   B 1 57  ? 58.551 -16.144 -4.087  1.00 17.58 ?  57  THR   B HA   1 
ATOM   4939 H HB   . THR   B 1 57  ? 57.327 -14.821 -2.744  1.00 16.41 ?  57  THR   B HB   1 
ATOM   4940 H HG1  . THR   B 1 57  ? 57.124 -16.795 -0.983  1.00 17.28 ?  57  THR   B HG1  1 
ATOM   4941 H HG21 . THR   B 1 57  ? 55.184 -15.640 -2.897  1.00 16.71 ?  57  THR   B HG21 1 
ATOM   4942 H HG22 . THR   B 1 57  ? 55.964 -16.150 -4.171  1.00 16.71 ?  57  THR   B HG22 1 
ATOM   4943 H HG23 . THR   B 1 57  ? 55.708 -17.126 -2.960  1.00 16.71 ?  57  THR   B HG23 1 
ATOM   4944 N N    . ASN   B 1 58  ? 60.478 -17.181 -2.023  1.00 16.19 ?  58  ASN   B N    1 
ATOM   4945 C CA   . ASN   B 1 58  ? 61.672 -16.964 -1.211  1.00 19.08 ?  58  ASN   B CA   1 
ATOM   4946 C C    . ASN   B 1 58  ? 61.331 -16.239 0.092   1.00 16.62 ?  58  ASN   B C    1 
ATOM   4947 O O    . ASN   B 1 58  ? 62.076 -15.368 0.555   1.00 17.41 ?  58  ASN   B O    1 
ATOM   4948 C CB   . ASN   B 1 58  ? 62.765 -16.222 -1.989  1.00 27.33 ?  58  ASN   B CB   1 
ATOM   4949 C CG   . ASN   B 1 58  ? 64.137 -16.380 -1.360  1.00 37.29 ?  58  ASN   B CG   1 
ATOM   4950 O OD1  . ASN   B 1 58  ? 64.443 -17.410 -0.760  1.00 40.07 ?  58  ASN   B OD1  1 
ATOM   4951 N ND2  . ASN   B 1 58  ? 64.972 -15.356 -1.496  1.00 44.42 ?  58  ASN   B ND2  1 
ATOM   4952 H H    . ASN   B 1 58  ? 60.344 -18.008 -2.224  1.00 19.47 ?  58  ASN   B H    1 
ATOM   4953 H HA   . ASN   B 1 58  ? 62.036 -17.835 -0.980  1.00 22.93 ?  58  ASN   B HA   1 
ATOM   4954 H HB2  . ASN   B 1 58  ? 62.808 -16.575 -2.892  1.00 32.84 ?  58  ASN   B HB2  1 
ATOM   4955 H HB3  . ASN   B 1 58  ? 62.555 -15.278 -2.010  1.00 32.84 ?  58  ASN   B HB3  1 
ATOM   4956 H HD21 . ASN   B 1 58  ? 65.762 -15.398 -1.158  1.00 53.34 ?  58  ASN   B HD21 1 
ATOM   4957 H HD22 . ASN   B 1 58  ? 64.722 -14.652 -1.921  1.00 53.34 ?  58  ASN   B HD22 1 
ATOM   4958 N N    . ASN   B 1 59  ? 60.206 -16.623 0.699   1.00 15.57 ?  59  ASN   B N    1 
ATOM   4959 C CA   . ASN   B 1 59  ? 59.734 -16.151 2.001   1.00 15.38 ?  59  ASN   B CA   1 
ATOM   4960 C C    . ASN   B 1 59  ? 59.135 -14.748 1.946   1.00 14.60 ?  59  ASN   B C    1 
ATOM   4961 O O    . ASN   B 1 59  ? 58.706 -14.241 2.989   1.00 15.11 ?  59  ASN   B O    1 
ATOM   4962 C CB   . ASN   B 1 59  ? 60.808 -16.210 3.102   1.00 16.55 ?  59  ASN   B CB   1 
ATOM   4963 C CG   . ASN   B 1 59  ? 60.218 -16.368 4.486   1.00 17.46 ?  59  ASN   B CG   1 
ATOM   4964 O OD1  . ASN   B 1 59  ? 59.390 -17.252 4.726   1.00 17.71 ?  59  ASN   B OD1  1 
ATOM   4965 N ND2  . ASN   B 1 59  ? 60.637 -15.512 5.408   1.00 18.11 ?  59  ASN   B ND2  1 
ATOM   4966 H H    . ASN   B 1 59  ? 59.668 -17.204 0.355   1.00 18.73 ?  59  ASN   B H    1 
ATOM   4967 H HA   . ASN   B 1 59  ? 59.026 -16.749 2.287   1.00 18.49 ?  59  ASN   B HA   1 
ATOM   4968 H HB2  . ASN   B 1 59  ? 61.393 -16.968 2.949   1.00 19.90 ?  59  ASN   B HB2  1 
ATOM   4969 H HB3  . ASN   B 1 59  ? 61.320 -15.387 3.096   1.00 19.90 ?  59  ASN   B HB3  1 
ATOM   4970 H HD21 . ASN   B 1 59  ? 60.328 -15.559 6.211   1.00 21.77 ?  59  ASN   B HD21 1 
ATOM   4971 H HD22 . ASN   B 1 59  ? 61.214 -14.907 5.205   1.00 21.77 ?  59  ASN   B HD22 1 
ATOM   4972 N N    . ALA   B 1 60  ? 59.074 -14.108 0.774   1.00 14.87 ?  60  ALA   B N    1 
ATOM   4973 C CA   . ALA   B 1 60  ? 58.481 -12.774 0.699   1.00 14.67 ?  60  ALA   B CA   1 
ATOM   4974 C C    . ALA   B 1 60  ? 57.009 -12.798 1.095   1.00 13.62 ?  60  ALA   B C    1 
ATOM   4975 O O    . ALA   B 1 60  ? 56.504 -11.846 1.706   1.00 14.32 ?  60  ALA   B O    1 
ATOM   4976 C CB   . ALA   B 1 60  ? 58.652 -12.201 -0.706  1.00 15.84 ?  60  ALA   B CB   1 
ATOM   4977 H H    . ALA   B 1 60  ? 59.371 -14.423 0.028   1.00 17.88 ?  60  ALA   B H    1 
ATOM   4978 H HA   . ALA   B 1 60  ? 58.946 -12.196 1.320   1.00 17.64 ?  60  ALA   B HA   1 
ATOM   4979 H HB1  . ALA   B 1 60  ? 58.254 -11.322 -0.733  1.00 19.04 ?  60  ALA   B HB1  1 
ATOM   4980 H HB2  . ALA   B 1 60  ? 59.601 -12.146 -0.910  1.00 19.04 ?  60  ALA   B HB2  1 
ATOM   4981 H HB3  . ALA   B 1 60  ? 58.214 -12.789 -1.341  1.00 19.04 ?  60  ALA   B HB3  1 
ATOM   4982 N N    . MET   B 1 61  ? 56.301 -13.873 0.743   1.00 13.03 ?  61  MET   B N    1 
ATOM   4983 C CA   . MET   B 1 61  ? 54.905 -13.996 1.134   1.00 12.74 ?  61  MET   B CA   1 
ATOM   4984 C C    . MET   B 1 61  ? 54.764 -13.997 2.653   1.00 12.76 ?  61  MET   B C    1 
ATOM   4985 O O    . MET   B 1 61  ? 53.863 -13.341 3.198   1.00 12.70 ?  61  MET   B O    1 
ATOM   4986 C CB   . MET   B 1 61  ? 54.327 -15.271 0.506   1.00 12.89 ?  61  MET   B CB   1 
ATOM   4987 C CG   . MET   B 1 61  ? 52.885 -15.572 0.918   1.00 12.58 ?  61  MET   B CG   1 
ATOM   4988 S SD   . MET   B 1 61  ? 52.243 -17.068 0.159   1.00 13.50 ?  61  MET   B SD   1 
ATOM   4989 C CE   . MET   B 1 61  ? 51.984 -16.502 -1.517  1.00 14.90 ?  61  MET   B CE   1 
ATOM   4990 H H    . MET   B 1 61  ? 56.606 -14.537 0.272   1.00 15.67 ?  61  MET   B H    1 
ATOM   4991 H HA   . MET   B 1 61  ? 54.414 -13.247 0.767   1.00 15.33 ?  61  MET   B HA   1 
ATOM   4992 H HB2  . MET   B 1 61  ? 54.343 -15.183 -0.463  1.00 15.51 ?  61  MET   B HB2  1 
ATOM   4993 H HB3  . MET   B 1 61  ? 54.876 -16.029 0.768   1.00 15.51 ?  61  MET   B HB3  1 
ATOM   4994 H HG2  . MET   B 1 61  ? 52.849 -15.695 1.881   1.00 15.13 ?  61  MET   B HG2  1 
ATOM   4995 H HG3  . MET   B 1 61  ? 52.319 -14.835 0.654   1.00 15.13 ?  61  MET   B HG3  1 
ATOM   4996 H HE1  . MET   B 1 61  ? 51.607 -17.227 -2.041  1.00 17.92 ?  61  MET   B HE1  1 
ATOM   4997 H HE2  . MET   B 1 61  ? 51.374 -15.748 -1.508  1.00 17.92 ?  61  MET   B HE2  1 
ATOM   4998 H HE3  . MET   B 1 61  ? 52.837 -16.232 -1.895  1.00 17.92 ?  61  MET   B HE3  1 
ATOM   4999 N N    . GLN   B 1 62  ? 55.640 -14.719 3.358   1.00 12.95 ?  62  GLN   B N    1 
ATOM   5000 C CA   . GLN   B 1 62  ? 55.538 -14.768 4.812   1.00 13.43 ?  62  GLN   B CA   1 
ATOM   5001 C C    . GLN   B 1 62  ? 55.820 -13.406 5.435   1.00 13.53 ?  62  GLN   B C    1 
ATOM   5002 O O    . GLN   B 1 62  ? 55.140 -13.000 6.382   1.00 14.01 ?  62  GLN   B O    1 
ATOM   5003 C CB   . GLN   B 1 62  ? 56.489 -15.820 5.389   1.00 13.89 ?  62  GLN   B CB   1 
ATOM   5004 C CG   . GLN   B 1 62  ? 56.260 -16.073 6.870   1.00 14.17 ?  62  GLN   B CG   1 
ATOM   5005 C CD   . GLN   B 1 62  ? 54.885 -16.668 7.111   1.00 13.59 ?  62  GLN   B CD   1 
ATOM   5006 O OE1  . GLN   B 1 62  ? 54.629 -17.818 6.747   1.00 14.20 ?  62  GLN   B OE1  1 
ATOM   5007 N NE2  . GLN   B 1 62  ? 53.972 -15.875 7.664   1.00 13.80 ?  62  GLN   B NE2  1 
ATOM   5008 H H    . GLN   B 1 62  ? 56.281 -15.188 3.021   1.00 15.58 ?  62  GLN   B H    1 
ATOM   5009 H HA   . GLN   B 1 62  ? 54.633 -15.021 5.050   1.00 16.16 ?  62  GLN   B HA   1 
ATOM   5010 H HB2  . GLN   B 1 62  ? 56.362 -16.659 4.918   1.00 16.71 ?  62  GLN   B HB2  1 
ATOM   5011 H HB3  . GLN   B 1 62  ? 57.405 -15.515 5.275   1.00 16.71 ?  62  GLN   B HB3  1 
ATOM   5012 H HG2  . GLN   B 1 62  ? 56.927 -16.703 7.191   1.00 17.04 ?  62  GLN   B HG2  1 
ATOM   5013 H HG3  . GLN   B 1 62  ? 56.324 -15.238 7.354   1.00 17.04 ?  62  GLN   B HG3  1 
ATOM   5014 H HE21 . GLN   B 1 62  ? 54.182 -15.075 7.893   1.00 16.59 ?  62  GLN   B HE21 1 
ATOM   5015 H HE22 . GLN   B 1 62  ? 53.181 -16.175 7.809   1.00 16.59 ?  62  GLN   B HE22 1 
ATOM   5016 N N    . VAL   B 1 63  ? 56.830 -12.691 4.936   1.00 14.04 ?  63  VAL   B N    1 
ATOM   5017 C CA   . VAL   B 1 63  ? 57.138 -11.372 5.489   1.00 15.02 ?  63  VAL   B CA   1 
ATOM   5018 C C    . VAL   B 1 63  ? 55.946 -10.436 5.306   1.00 13.99 ?  63  VAL   B C    1 
ATOM   5019 O O    . VAL   B 1 63  ? 55.530 -9.730  6.235   1.00 14.71 ?  63  VAL   B O    1 
ATOM   5020 C CB   . VAL   B 1 63  ? 58.432 -10.818 4.866   1.00 16.20 ?  63  VAL   B CB   1 
ATOM   5021 C CG1  . VAL   B 1 63  ? 58.664 -9.378  5.309   1.00 17.14 ?  63  VAL   B CG1  1 
ATOM   5022 C CG2  . VAL   B 1 63  ? 59.617 -11.690 5.261   1.00 16.76 ?  63  VAL   B CG2  1 
ATOM   5023 H H    . VAL   B 1 63  ? 57.340 -12.944 4.287   1.00 16.89 ?  63  VAL   B H    1 
ATOM   5024 H HA   . VAL   B 1 63  ? 57.293 -11.471 6.438   1.00 18.06 ?  63  VAL   B HA   1 
ATOM   5025 H HB   . VAL   B 1 63  ? 58.360 -10.835 3.898   1.00 19.48 ?  63  VAL   B HB   1 
ATOM   5026 H HG11 . VAL   B 1 63  ? 59.580 -9.134  5.114   1.00 20.60 ?  63  VAL   B HG11 1 
ATOM   5027 H HG12 . VAL   B 1 63  ? 58.055 -8.800  4.827   1.00 20.60 ?  63  VAL   B HG12 1 
ATOM   5028 H HG13 . VAL   B 1 63  ? 58.500 -9.317  6.263   1.00 20.60 ?  63  VAL   B HG13 1 
ATOM   5029 H HG21 . VAL   B 1 63  ? 60.427 -11.319 4.879   1.00 20.15 ?  63  VAL   B HG21 1 
ATOM   5030 H HG22 . VAL   B 1 63  ? 59.687 -11.704 6.231   1.00 20.15 ?  63  VAL   B HG22 1 
ATOM   5031 H HG23 . VAL   B 1 63  ? 59.476 -12.590 4.930   1.00 20.15 ?  63  VAL   B HG23 1 
ATOM   5032 N N    . GLU   B 1 64  ? 55.374 -10.429 4.103   1.00 13.77 ?  64  GLU   B N    1 
ATOM   5033 C CA   . GLU   B 1 64  ? 54.205 -9.599  3.827   1.00 13.51 ?  64  GLU   B CA   1 
ATOM   5034 C C    . GLU   B 1 64  ? 53.021 -9.999  4.702   1.00 13.29 ?  64  GLU   B C    1 
ATOM   5035 O O    . GLU   B 1 64  ? 52.271 -9.137  5.193   1.00 13.55 ?  64  GLU   B O    1 
ATOM   5036 C CB   . GLU   B 1 64  ? 53.846 -9.755  2.350   1.00 13.41 ?  64  GLU   B CB   1 
ATOM   5037 C CG   . GLU   B 1 64  ? 52.586 -9.020  1.915   1.00 13.97 ?  64  GLU   B CG   1 
ATOM   5038 C CD   . GLU   B 1 64  ? 52.063 -9.502  0.569   1.00 14.82 ?  64  GLU   B CD   1 
ATOM   5039 O OE1  . GLU   B 1 64  ? 52.248 -10.712 0.253   1.00 15.69 ?  64  GLU   B OE1  1 
ATOM   5040 O OE2  . GLU   B 1 64  ? 51.452 -8.680  -0.161  1.00 15.57 -1 64  GLU   B OE2  1 
ATOM   5041 H H    . GLU   B 1 64  ? 55.645 -10.901 3.429   1.00 16.57 ?  64  GLU   B H    1 
ATOM   5042 H HA   . GLU   B 1 64  ? 54.417 -8.675  3.998   1.00 16.26 ?  64  GLU   B HA   1 
ATOM   5043 H HB2  . GLU   B 1 64  ? 54.578 -9.406  1.812   1.00 16.13 ?  64  GLU   B HB2  1 
ATOM   5044 H HB3  . GLU   B 1 64  ? 53.721 -10.694 2.153   1.00 16.13 ?  64  GLU   B HB3  1 
ATOM   5045 H HG2  . GLU   B 1 64  ? 51.879 -9.168  2.567   1.00 16.80 ?  64  GLU   B HG2  1 
ATOM   5046 H HG3  . GLU   B 1 64  ? 52.776 -8.075  1.844   1.00 16.80 ?  64  GLU   B HG3  1 
ATOM   5047 N N    . SER   B 1 65  ? 52.837 -11.307 4.896   1.00 13.08 ?  65  SER   B N    1 
ATOM   5048 C CA   . SER   B 1 65  ? 51.730 -11.813 5.696   1.00 13.08 ?  65  SER   B CA   1 
ATOM   5049 C C    . SER   B 1 65  ? 51.861 -11.406 7.157   1.00 13.02 ?  65  SER   B C    1 
ATOM   5050 O O    . SER   B 1 65  ? 50.859 -11.031 7.789   1.00 13.51 ?  65  SER   B O    1 
ATOM   5051 C CB   . SER   B 1 65  ? 51.653 -13.337 5.568   1.00 13.26 ?  65  SER   B CB   1 
ATOM   5052 O OG   . SER   B 1 65  ? 51.303 -13.735 4.250   1.00 13.36 ?  65  SER   B OG   1 
ATOM   5053 H H    . SER   B 1 65  ? 53.347 -11.930 4.582   1.00 15.73 ?  65  SER   B H    1 
ATOM   5054 H HA   . SER   B 1 65  ? 50.898 -11.446 5.359   1.00 15.73 ?  65  SER   B HA   1 
ATOM   5055 H HB2  . SER   B 1 65  ? 52.515 -13.715 5.789   1.00 15.95 ?  65  SER   B HB2  1 
ATOM   5056 H HB3  . SER   B 1 65  ? 50.978 -13.670 6.185   1.00 15.95 ?  65  SER   B HB3  1 
ATOM   5057 H HG   . SER   B 1 65  ? 51.871 -13.442 3.699   1.00 16.07 ?  65  SER   B HG   1 
ATOM   5058 N N    . ASP   B 1 66  ? 53.070 -11.498 7.724   1.00 13.34 ?  66  ASP   B N    1 
ATOM   5059 C CA   . ASP   B 1 66  ? 53.250 -11.107 9.119   1.00 13.72 ?  66  ASP   B CA   1 
ATOM   5060 C C    . ASP   B 1 66  ? 52.938 -9.626  9.313   1.00 14.01 ?  66  ASP   B C    1 
ATOM   5061 O O    . ASP   B 1 66  ? 52.371 -9.226  10.337  1.00 14.45 ?  66  ASP   B O    1 
ATOM   5062 C CB   . ASP   B 1 66  ? 54.677 -11.421 9.578   1.00 15.06 ?  66  ASP   B CB   1 
ATOM   5063 C CG   . ASP   B 1 66  ? 54.937 -12.918 9.746   1.00 16.85 ?  66  ASP   B CG   1 
ATOM   5064 O OD1  . ASP   B 1 66  ? 53.980 -13.725 9.667   1.00 17.79 ?  66  ASP   B OD1  1 
ATOM   5065 O OD2  . ASP   B 1 66  ? 56.114 -13.290 9.964   1.00 19.42 -1 66  ASP   B OD2  1 
ATOM   5066 H H    . ASP   B 1 66  ? 53.776 -11.791 7.337   1.00 16.04 ?  66  ASP   B H    1 
ATOM   5067 H HA   . ASP   B 1 66  ? 52.643 -11.613 9.682   1.00 16.50 ?  66  ASP   B HA   1 
ATOM   5068 H HB2  . ASP   B 1 66  ? 55.305 -11.081 8.923   1.00 18.11 ?  66  ASP   B HB2  1 
ATOM   5069 H HB3  . ASP   B 1 66  ? 54.838 -10.995 10.439  1.00 18.11 ?  66  ASP   B HB3  1 
ATOM   5070 N N    . ASP   B 1 67  ? 53.310 -8.790  8.344   1.00 13.47 ?  67  ASP   B N    1 
ATOM   5071 C CA   . ASP   B 1 67  ? 52.967 -7.376  8.423   1.00 14.13 ?  67  ASP   B CA   1 
ATOM   5072 C C    . ASP   B 1 67  ? 51.456 -7.167  8.338   1.00 14.22 ?  67  ASP   B C    1 
ATOM   5073 O O    . ASP   B 1 67  ? 50.892 -6.356  9.084   1.00 14.99 ?  67  ASP   B O    1 
ATOM   5074 C CB   . ASP   B 1 67  ? 53.689 -6.610  7.322   1.00 15.54 ?  67  ASP   B CB   1 
ATOM   5075 C CG   . ASP   B 1 67  ? 53.259 -5.165  7.264   1.00 17.24 ?  67  ASP   B CG   1 
ATOM   5076 O OD1  . ASP   B 1 67  ? 53.760 -4.337  8.065   1.00 18.62 ?  67  ASP   B OD1  1 
ATOM   5077 O OD2  . ASP   B 1 67  ? 52.384 -4.879  6.435   1.00 18.26 -1 67  ASP   B OD2  1 
ATOM   5078 H H    . ASP   B 1 67  ? 53.762 -9.017  7.647   1.00 16.21 ?  67  ASP   B H    1 
ATOM   5079 H HA   . ASP   B 1 67  ? 53.268 -7.026  9.275   1.00 17.00 ?  67  ASP   B HA   1 
ATOM   5080 H HB2  . ASP   B 1 67  ? 54.647 -6.637  7.489   1.00 18.69 ?  67  ASP   B HB2  1 
ATOM   5081 H HB3  . ASP   B 1 67  ? 53.495 -7.027  6.464   1.00 18.69 ?  67  ASP   B HB3  1 
ATOM   5082 N N    . TYR   B 1 68  ? 50.777 -7.905  7.449   1.00 14.12 ?  68  TYR   B N    1 
ATOM   5083 C CA   . TYR   B 1 68  ? 49.320 -7.828  7.374   1.00 14.70 ?  68  TYR   B CA   1 
ATOM   5084 C C    . TYR   B 1 68  ? 48.683 -8.169  8.717   1.00 13.96 ?  68  TYR   B C    1 
ATOM   5085 O O    . TYR   B 1 68  ? 47.746 -7.488  9.162   1.00 14.97 ?  68  TYR   B O    1 
ATOM   5086 C CB   . TYR   B 1 68  ? 48.786 -8.756  6.274   1.00 15.33 ?  68  TYR   B CB   1 
ATOM   5087 C CG   . TYR   B 1 68  ? 47.279 -8.914  6.332   1.00 16.48 ?  68  TYR   B CG   1 
ATOM   5088 C CD1  . TYR   B 1 68  ? 46.695 -9.863  7.165   1.00 17.15 ?  68  TYR   B CD1  1 
ATOM   5089 C CD2  . TYR   B 1 68  ? 46.446 -8.087  5.598   1.00 17.37 ?  68  TYR   B CD2  1 
ATOM   5090 C CE1  . TYR   B 1 68  ? 45.334 -9.989  7.259   1.00 18.30 ?  68  TYR   B CE1  1 
ATOM   5091 C CE2  . TYR   B 1 68  ? 45.069 -8.217  5.678   1.00 17.94 ?  68  TYR   B CE2  1 
ATOM   5092 C CZ   . TYR   B 1 68  ? 44.531 -9.167  6.512   1.00 18.13 ?  68  TYR   B CZ   1 
ATOM   5093 O OH   . TYR   B 1 68  ? 43.163 -9.282  6.607   1.00 19.43 ?  68  TYR   B OH   1 
ATOM   5094 H H    . TYR   B 1 68  ? 51.137 -8.461  6.891   1.00 16.99 ?  68  TYR   B H    1 
ATOM   5095 H HA   . TYR   B 1 68  ? 49.072 -6.922  7.149   1.00 17.68 ?  68  TYR   B HA   1 
ATOM   5096 H HB2  . TYR   B 1 68  ? 49.013 -8.381  5.409   1.00 18.43 ?  68  TYR   B HB2  1 
ATOM   5097 H HB3  . TYR   B 1 68  ? 49.184 -9.632  6.375   1.00 18.43 ?  68  TYR   B HB3  1 
ATOM   5098 H HD1  . TYR   B 1 68  ? 47.243 -10.424 7.672   1.00 20.61 ?  68  TYR   B HD1  1 
ATOM   5099 H HD2  . TYR   B 1 68  ? 46.817 -7.436  5.050   1.00 20.89 ?  68  TYR   B HD2  1 
ATOM   5100 H HE1  . TYR   B 1 68  ? 44.956 -10.643 7.808   1.00 22.00 ?  68  TYR   B HE1  1 
ATOM   5101 H HE2  . TYR   B 1 68  ? 44.512 -7.657  5.187   1.00 21.57 ?  68  TYR   B HE2  1 
ATOM   5102 H HH   . TYR   B 1 68  ? 42.778 -8.732  6.090   1.00 23.36 ?  68  TYR   B HH   1 
ATOM   5103 N N    . ILE   B 1 69  ? 49.164 -9.239  9.364   1.00 13.95 ?  69  ILE   B N    1 
ATOM   5104 C CA   . ILE   B 1 69  ? 48.618 -9.656  10.654  1.00 14.50 ?  69  ILE   B CA   1 
ATOM   5105 C C    . ILE   B 1 69  ? 48.869 -8.600  11.723  1.00 14.13 ?  69  ILE   B C    1 
ATOM   5106 O O    . ILE   B 1 69  ? 47.995 -8.317  12.551  1.00 14.79 ?  69  ILE   B O    1 
ATOM   5107 C CB   . ILE   B 1 69  ? 49.194 -11.026 11.059  1.00 14.95 ?  69  ILE   B CB   1 
ATOM   5108 C CG1  . ILE   B 1 69  ? 48.673 -12.138 10.139  1.00 15.66 ?  69  ILE   B CG1  1 
ATOM   5109 C CG2  . ILE   B 1 69  ? 48.894 -11.330 12.520  1.00 16.24 ?  69  ILE   B CG2  1 
ATOM   5110 C CD1  . ILE   B 1 69  ? 47.199 -12.462 10.296  1.00 16.13 ?  69  ILE   B CD1  1 
ATOM   5111 H H    . ILE   B 1 69  ? 49.804 -9.737  9.075   1.00 16.78 ?  69  ILE   B H    1 
ATOM   5112 H HA   . ILE   B 1 69  ? 47.660 -9.756  10.561  1.00 17.44 ?  69  ILE   B HA   1 
ATOM   5113 H HB   . ILE   B 1 69  ? 50.159 -10.986 10.956  1.00 17.98 ?  69  ILE   B HB   1 
ATOM   5114 H HG12 . ILE   B 1 69  ? 48.820 -11.871 9.217   1.00 18.83 ?  69  ILE   B HG12 1 
ATOM   5115 H HG13 . ILE   B 1 69  ? 49.175 -12.950 10.322  1.00 18.83 ?  69  ILE   B HG13 1 
ATOM   5116 H HG21 . ILE   B 1 69  ? 49.036 -12.278 12.677  1.00 19.52 ?  69  ILE   B HG21 1 
ATOM   5117 H HG22 . ILE   B 1 69  ? 49.489 -10.813 13.083  1.00 19.52 ?  69  ILE   B HG22 1 
ATOM   5118 H HG23 . ILE   B 1 69  ? 47.971 -11.101 12.708  1.00 19.52 ?  69  ILE   B HG23 1 
ATOM   5119 H HD11 . ILE   B 1 69  ? 46.969 -13.169 9.673   1.00 19.39 ?  69  ILE   B HD11 1 
ATOM   5120 H HD12 . ILE   B 1 69  ? 47.036 -12.759 11.205  1.00 19.39 ?  69  ILE   B HD12 1 
ATOM   5121 H HD13 . ILE   B 1 69  ? 46.678 -11.670 10.104  1.00 19.39 ?  69  ILE   B HD13 1 
ATOM   5122 N N    . ALA   B 1 70  ? 50.063 -8.006  11.738  1.00 14.22 ?  70  ALA   B N    1 
ATOM   5123 C CA   . ALA   B 1 70  ? 50.338 -6.959  12.721  1.00 14.01 ?  70  ALA   B CA   1 
ATOM   5124 C C    . ALA   B 1 70  ? 49.323 -5.829  12.616  1.00 14.54 ?  70  ALA   B C    1 
ATOM   5125 O O    . ALA   B 1 70  ? 48.871 -5.292  13.634  1.00 15.13 ?  70  ALA   B O    1 
ATOM   5126 C CB   . ALA   B 1 70  ? 51.758 -6.425  12.540  1.00 14.60 ?  70  ALA   B CB   1 
ATOM   5127 H H    . ALA   B 1 70  ? 50.710 -8.184  11.204  1.00 17.10 ?  70  ALA   B H    1 
ATOM   5128 H HA   . ALA   B 1 70  ? 50.277 -7.339  13.611  1.00 16.85 ?  70  ALA   B HA   1 
ATOM   5129 H HB1  . ALA   B 1 70  ? 51.944 -5.772  13.236  1.00 17.56 ?  70  ALA   B HB1  1 
ATOM   5130 H HB2  . ALA   B 1 70  ? 52.389 -7.161  12.607  1.00 17.56 ?  70  ALA   B HB2  1 
ATOM   5131 H HB3  . ALA   B 1 70  ? 51.835 -6.007  11.667  1.00 17.56 ?  70  ALA   B HB3  1 
ATOM   5132 N N    . THR   B 1 71  ? 48.951 -5.462  11.393  1.00 15.09 ?  71  THR   B N    1 
ATOM   5133 C CA   . THR   B 1 71  ? 48.054 -4.331  11.184  1.00 16.26 ?  71  THR   B CA   1 
ATOM   5134 C C    . THR   B 1 71  ? 46.589 -4.704  11.391  1.00 16.82 ?  71  THR   B C    1 
ATOM   5135 O O    . THR   B 1 71  ? 45.805 -3.892  11.902  1.00 18.21 ?  71  THR   B O    1 
ATOM   5136 C CB   . THR   B 1 71  ? 48.262 -3.772  9.776   1.00 17.93 ?  71  THR   B CB   1 
ATOM   5137 O OG1  . THR   B 1 71  ? 49.580 -3.222  9.670   1.00 19.85 ?  71  THR   B OG1  1 
ATOM   5138 C CG2  . THR   B 1 71  ? 47.234 -2.700  9.450   1.00 18.91 ?  71  THR   B CG2  1 
ATOM   5139 H H    . THR   B 1 71  ? 49.204 -5.856  10.670  1.00 18.14 ?  71  THR   B H    1 
ATOM   5140 H HA   . THR   B 1 71  ? 48.279 -3.634  11.818  1.00 19.55 ?  71  THR   B HA   1 
ATOM   5141 H HB   . THR   B 1 71  ? 48.172 -4.486  9.127   1.00 21.55 ?  71  THR   B HB   1 
ATOM   5142 H HG1  . THR   B 1 71  ? 49.702 -2.897  8.899   1.00 23.86 ?  71  THR   B HG1  1 
ATOM   5143 H HG21 . THR   B 1 71  ? 47.535 -2.170  8.693   1.00 22.73 ?  71  THR   B HG21 1 
ATOM   5144 H HG22 . THR   B 1 71  ? 46.384 -3.106  9.229   1.00 22.73 ?  71  THR   B HG22 1 
ATOM   5145 H HG23 . THR   B 1 71  ? 47.117 -2.110  10.213  1.00 22.73 ?  71  THR   B HG23 1 
ATOM   5146 N N    . ASN   B 1 72  ? 46.200 -5.919  11.002  1.00 16.16 ?  72  ASN   B N    1 
ATOM   5147 C CA   . ASN   B 1 72  ? 44.799 -6.290  10.878  1.00 16.37 ?  72  ASN   B CA   1 
ATOM   5148 C C    . ASN   B 1 72  ? 44.336 -7.383  11.830  1.00 17.03 ?  72  ASN   B C    1 
ATOM   5149 O O    . ASN   B 1 72  ? 43.124 -7.553  11.993  1.00 18.26 ?  72  ASN   B O    1 
ATOM   5150 C CB   . ASN   B 1 72  ? 44.491 -6.728  9.437   1.00 17.12 ?  72  ASN   B CB   1 
ATOM   5151 C CG   . ASN   B 1 72  ? 44.776 -5.637  8.427   1.00 18.24 ?  72  ASN   B CG   1 
ATOM   5152 O OD1  . ASN   B 1 72  ? 45.798 -5.654  7.740   1.00 19.34 ?  72  ASN   B OD1  1 
ATOM   5153 N ND2  . ASN   B 1 72  ? 43.894 -4.662  8.357   1.00 19.97 ?  72  ASN   B ND2  1 
ATOM   5154 H H    . ASN   B 1 72  ? 46.747 -6.565  10.802  1.00 19.43 ?  72  ASN   B H    1 
ATOM   5155 H HA   . ASN   B 1 72  ? 44.266 -5.505  11.059  1.00 19.68 ?  72  ASN   B HA   1 
ATOM   5156 H HB2  . ASN   B 1 72  ? 45.046 -7.496  9.212   1.00 20.58 ?  72  ASN   B HB2  1 
ATOM   5157 H HB3  . ASN   B 1 72  ? 43.557 -6.960  9.368   1.00 20.58 ?  72  ASN   B HB3  1 
ATOM   5158 H HD21 . ASN   B 1 72  ? 44.007 -4.016  7.797   1.00 24.00 ?  72  ASN   B HD21 1 
ATOM   5159 H HD22 . ASN   B 1 72  ? 43.191 -4.681  8.851   1.00 24.00 ?  72  ASN   B HD22 1 
ATOM   5160 N N    . GLY   B 1 73  ? 45.242 -8.128  12.453  1.00 16.59 ?  73  GLY   B N    1 
ATOM   5161 C CA   . GLY   B 1 73  ? 44.852 -9.269  13.247  1.00 16.30 ?  73  GLY   B CA   1 
ATOM   5162 C C    . GLY   B 1 73  ? 44.499 -10.460 12.381  1.00 14.68 ?  73  GLY   B C    1 
ATOM   5163 O O    . GLY   B 1 73  ? 44.491 -10.381 11.151  1.00 14.81 ?  73  GLY   B O    1 
ATOM   5164 H H    . GLY   B 1 73  ? 46.092 -7.986  12.432  1.00 19.95 ?  73  GLY   B H    1 
ATOM   5165 H HA2  . GLY   B 1 73  ? 45.580 -9.515  13.840  1.00 19.60 ?  73  GLY   B HA2  1 
ATOM   5166 H HA3  . GLY   B 1 73  ? 44.079 -9.036  13.790  1.00 19.60 ?  73  GLY   B HA3  1 
ATOM   5167 N N    . PRO   B 1 74  ? 44.184 -11.583 13.024  1.00 15.17 ?  74  PRO   B N    1 
ATOM   5168 C CA   . PRO   B 1 74  ? 43.928 -12.819 12.284  1.00 14.60 ?  74  PRO   B CA   1 
ATOM   5169 C C    . PRO   B 1 74  ? 42.631 -12.764 11.493  1.00 13.88 ?  74  PRO   B C    1 
ATOM   5170 O O    . PRO   B 1 74  ? 41.695 -12.021 11.814  1.00 15.32 ?  74  PRO   B O    1 
ATOM   5171 C CB   . PRO   B 1 74  ? 43.844 -13.877 13.393  1.00 15.84 ?  74  PRO   B CB   1 
ATOM   5172 C CG   . PRO   B 1 74  ? 43.393 -13.117 14.593  1.00 17.45 ?  74  PRO   B CG   1 
ATOM   5173 C CD   . PRO   B 1 74  ? 44.066 -11.777 14.478  1.00 16.79 ?  74  PRO   B CD   1 
ATOM   5174 H HA   . PRO   B 1 74  ? 44.671 -13.020 11.689  1.00 17.55 ?  74  PRO   B HA   1 
ATOM   5175 H HB2  . PRO   B 1 74  ? 43.195 -14.554 13.144  1.00 19.04 ?  74  PRO   B HB2  1 
ATOM   5176 H HB3  . PRO   B 1 74  ? 44.718 -14.270 13.536  1.00 19.04 ?  74  PRO   B HB3  1 
ATOM   5177 H HG2  . PRO   B 1 74  ? 42.427 -13.019 14.574  1.00 20.98 ?  74  PRO   B HG2  1 
ATOM   5178 H HG3  . PRO   B 1 74  ? 43.676 -13.578 15.396  1.00 20.98 ?  74  PRO   B HG3  1 
ATOM   5179 H HD2  . PRO   B 1 74  ? 43.508 -11.085 14.875  1.00 20.19 ?  74  PRO   B HD2  1 
ATOM   5180 H HD3  . PRO   B 1 74  ? 44.943 -11.803 14.892  1.00 20.19 ?  74  PRO   B HD3  1 
ATOM   5181 N N    . LEU   B 1 75  ? 42.597 -13.570 10.439  1.00 13.42 ?  75  LEU   B N    1 
ATOM   5182 C CA   . LEU   B 1 75  ? 41.388 -13.778 9.667   1.00 13.46 ?  75  LEU   B CA   1 
ATOM   5183 C C    . LEU   B 1 75  ? 40.406 -14.628 10.468  1.00 13.75 ?  75  LEU   B C    1 
ATOM   5184 O O    . LEU   B 1 75  ? 40.748 -15.225 11.490  1.00 15.19 ?  75  LEU   B O    1 
ATOM   5185 C CB   . LEU   B 1 75  ? 41.717 -14.504 8.362   1.00 13.27 ?  75  LEU   B CB   1 
ATOM   5186 C CG   . LEU   B 1 75  ? 42.544 -13.739 7.324   1.00 14.98 ?  75  LEU   B CG   1 
ATOM   5187 C CD1  . LEU   B 1 75  ? 42.794 -14.585 6.077   1.00 16.75 ?  75  LEU   B CD1  1 
ATOM   5188 C CD2  . LEU   B 1 75  ? 41.900 -12.430 6.954   1.00 18.29 ?  75  LEU   B CD2  1 
ATOM   5189 H H    . LEU   B 1 75  ? 43.272 -14.019 10.151  1.00 16.15 ?  75  LEU   B H    1 
ATOM   5190 H HA   . LEU   B 1 75  ? 40.973 -12.929 9.458   1.00 16.19 ?  75  LEU   B HA   1 
ATOM   5191 H HB2  . LEU   B 1 75  ? 42.216 -15.312 8.581   1.00 15.97 ?  75  LEU   B HB2  1 
ATOM   5192 H HB3  . LEU   B 1 75  ? 40.885 -14.756 7.931   1.00 15.97 ?  75  LEU   B HB3  1 
ATOM   5193 H HG   . LEU   B 1 75  ? 43.411 -13.539 7.712   1.00 18.01 ?  75  LEU   B HG   1 
ATOM   5194 H HD11 . LEU   B 1 75  ? 43.327 -14.070 5.446   1.00 20.14 ?  75  LEU   B HD11 1 
ATOM   5195 H HD12 . LEU   B 1 75  ? 43.277 -15.390 6.329   1.00 20.14 ?  75  LEU   B HD12 1 
ATOM   5196 H HD13 . LEU   B 1 75  ? 41.946 -14.821 5.675   1.00 20.14 ?  75  LEU   B HD13 1 
ATOM   5197 H HD21 . LEU   B 1 75  ? 42.388 -12.036 6.215   1.00 21.99 ?  75  LEU   B HD21 1 
ATOM   5198 H HD22 . LEU   B 1 75  ? 40.981 -12.594 6.696   1.00 21.99 ?  75  LEU   B HD22 1 
ATOM   5199 H HD23 . LEU   B 1 75  ? 41.929 -11.837 7.722   1.00 21.99 ?  75  LEU   B HD23 1 
ATOM   5200 N N    . LYS   B 1 76  ? 39.171 -14.690 9.972   1.00 15.15 ?  76  LYS   B N    1 
ATOM   5201 C CA   . LYS   B 1 76  ? 38.182 -15.648 10.446  1.00 16.20 ?  76  LYS   B CA   1 
ATOM   5202 C C    . LYS   B 1 76  ? 38.291 -16.934 9.628   1.00 14.90 ?  76  LYS   B C    1 
ATOM   5203 O O    . LYS   B 1 76  ? 38.577 -16.896 8.433   1.00 14.74 ?  76  LYS   B O    1 
ATOM   5204 C CB   . LYS   B 1 76  ? 36.767 -15.087 10.245  1.00 18.33 ?  76  LYS   B CB   1 
ATOM   5205 C CG   . LYS   B 1 76  ? 36.484 -13.705 10.854  1.00 19.95 ?  76  LYS   B CG   1 
ATOM   5206 C CD   . LYS   B 1 76  ? 35.082 -13.195 10.478  1.00 21.12 ?  76  LYS   B CD   1 
ATOM   5207 C CE   . LYS   B 1 76  ? 34.800 -11.824 11.069  1.00 22.82 ?  76  LYS   B CE   1 
ATOM   5208 N NZ   . LYS   B 1 76  ? 33.526 -11.230 10.578  1.00 23.52 ?  76  LYS   B NZ   1 
ATOM   5209 H H    . LYS   B 1 76  ? 38.882 -14.187 9.335   1.00 18.21 ?  76  LYS   B H    1 
ATOM   5210 H HA   . LYS   B 1 76  ? 38.326 -15.852 11.382  1.00 19.47 ?  76  LYS   B HA   1 
ATOM   5211 H HB2  . LYS   B 1 76  ? 36.600 -15.021 9.291   1.00 22.04 ?  76  LYS   B HB2  1 
ATOM   5212 H HB3  . LYS   B 1 76  ? 36.136 -15.710 10.638  1.00 22.04 ?  76  LYS   B HB3  1 
ATOM   5213 H HG2  . LYS   B 1 76  ? 36.540 -13.766 11.821  1.00 23.98 ?  76  LYS   B HG2  1 
ATOM   5214 H HG3  . LYS   B 1 76  ? 37.141 -13.070 10.521  1.00 23.98 ?  76  LYS   B HG3  1 
ATOM   5215 H HD2  . LYS   B 1 76  ? 35.016 -13.130 9.512   1.00 25.38 ?  76  LYS   B HD2  1 
ATOM   5216 H HD3  . LYS   B 1 76  ? 34.418 -13.816 10.817  1.00 25.38 ?  76  LYS   B HD3  1 
ATOM   5217 H HE2  . LYS   B 1 76  ? 34.743 -11.905 12.033  1.00 27.42 ?  76  LYS   B HE2  1 
ATOM   5218 H HE3  . LYS   B 1 76  ? 35.524 -11.225 10.828  1.00 27.42 ?  76  LYS   B HE3  1 
ATOM   5219 H HZ1  . LYS   B 1 76  ? 33.401 -10.430 10.949  1.00 28.27 ?  76  LYS   B HZ1  1 
ATOM   5220 H HZ2  . LYS   B 1 76  ? 33.553 -11.136 9.693   1.00 28.27 ?  76  LYS   B HZ2  1 
ATOM   5221 H HZ3  . LYS   B 1 76  ? 32.841 -11.756 10.792  1.00 28.27 ?  76  LYS   B HZ3  1 
ATOM   5222 N N    . VAL   B 1 77  ? 38.046 -18.080 10.271  1.00 15.64 ?  77  VAL   B N    1 
ATOM   5223 C CA   . VAL   B 1 77  ? 37.843 -19.302 9.499   1.00 16.01 ?  77  VAL   B CA   1 
ATOM   5224 C C    . VAL   B 1 77  ? 36.653 -19.081 8.577   1.00 14.80 ?  77  VAL   B C    1 
ATOM   5225 O O    . VAL   B 1 77  ? 35.586 -18.634 9.015   1.00 15.03 ?  77  VAL   B O    1 
ATOM   5226 C CB   . VAL   B 1 77  ? 37.636 -20.511 10.423  1.00 17.83 ?  77  VAL   B CB   1 
ATOM   5227 C CG1  . VAL   B 1 77  ? 37.381 -21.761 9.586   1.00 18.16 ?  77  VAL   B CG1  1 
ATOM   5228 C CG2  . VAL   B 1 77  ? 38.848 -20.704 11.336  1.00 19.33 ?  77  VAL   B CG2  1 
ATOM   5229 H H    . VAL   B 1 77  ? 37.989 -18.168 11.117  1.00 18.80 ?  77  VAL   B H    1 
ATOM   5230 H HA   . VAL   B 1 77  ? 38.620 -19.463 8.946   1.00 19.25 ?  77  VAL   B HA   1 
ATOM   5231 H HB   . VAL   B 1 77  ? 36.855 -20.354 10.977  1.00 21.44 ?  77  VAL   B HB   1 
ATOM   5232 H HG11 . VAL   B 1 77  ? 37.417 -22.536 10.167  1.00 21.83 ?  77  VAL   B HG11 1 
ATOM   5233 H HG12 . VAL   B 1 77  ? 36.503 -21.698 9.175   1.00 21.83 ?  77  VAL   B HG12 1 
ATOM   5234 H HG13 . VAL   B 1 77  ? 38.063 -21.827 8.901   1.00 21.83 ?  77  VAL   B HG13 1 
ATOM   5235 H HG21 . VAL   B 1 77  ? 38.713 -21.503 11.863  1.00 23.23 ?  77  VAL   B HG21 1 
ATOM   5236 H HG22 . VAL   B 1 77  ? 39.639 -20.792 10.787  1.00 23.23 ?  77  VAL   B HG22 1 
ATOM   5237 H HG23 . VAL   B 1 77  ? 38.927 -19.929 11.915  1.00 23.23 ?  77  VAL   B HG23 1 
ATOM   5238 N N    . GLY   B 1 78  ? 36.837 -19.363 7.288   1.00 14.26 ?  78  GLY   B N    1 
ATOM   5239 C CA   . GLY   B 1 78  ? 35.862 -19.046 6.269   1.00 14.20 ?  78  GLY   B CA   1 
ATOM   5240 C C    . GLY   B 1 78  ? 36.112 -17.735 5.554   1.00 13.60 ?  78  GLY   B C    1 
ATOM   5241 O O    . GLY   B 1 78  ? 35.425 -17.453 4.565   1.00 14.13 ?  78  GLY   B O    1 
ATOM   5242 H H    . GLY   B 1 78  ? 37.538 -19.755 6.977   1.00 17.15 ?  78  GLY   B H    1 
ATOM   5243 H HA2  . GLY   B 1 78  ? 35.856 -19.744 5.603   1.00 17.08 ?  78  GLY   B HA2  1 
ATOM   5244 H HA3  . GLY   B 1 78  ? 34.983 -18.999 6.673   1.00 17.08 ?  78  GLY   B HA3  1 
ATOM   5245 N N    . GLY   B 1 79  ? 37.057 -16.923 6.041   1.00 13.45 ?  79  GLY   B N    1 
ATOM   5246 C CA   . GLY   B 1 79  ? 37.357 -15.631 5.459   1.00 12.90 ?  79  GLY   B CA   1 
ATOM   5247 C C    . GLY   B 1 79  ? 38.589 -15.659 4.565   1.00 12.74 ?  79  GLY   B C    1 
ATOM   5248 O O    . GLY   B 1 79  ? 39.198 -16.700 4.320   1.00 13.23 ?  79  GLY   B O    1 
ATOM   5249 H H    . GLY   B 1 79  ? 37.547 -17.105 6.722   1.00 16.18 ?  79  GLY   B H    1 
ATOM   5250 H HA2  . GLY   B 1 79  ? 36.604 -15.329 4.926   1.00 15.52 ?  79  GLY   B HA2  1 
ATOM   5251 H HA3  . GLY   B 1 79  ? 37.511 -14.982 6.164   1.00 15.52 ?  79  GLY   B HA3  1 
ATOM   5252 N N    . SER   B 1 80  ? 38.950 -14.469 4.074   1.00 12.55 ?  80  SER   B N    1 
ATOM   5253 C CA   . SER   B 1 80  ? 40.061 -14.341 3.142   1.00 12.53 ?  80  SER   B CA   1 
ATOM   5254 C C    . SER   B 1 80  ? 40.645 -12.936 3.195   1.00 12.25 ?  80  SER   B C    1 
ATOM   5255 O O    . SER   B 1 80  ? 40.033 -12.000 3.718   1.00 13.55 ?  80  SER   B O    1 
ATOM   5256 C CB   . SER   B 1 80  ? 39.628 -14.639 1.705   1.00 12.79 ?  80  SER   B CB   1 
ATOM   5257 O OG   . SER   B 1 80  ? 38.790 -13.622 1.201   1.00 13.90 ?  80  SER   B OG   1 
ATOM   5258 H H    . SER   B 1 80  ? 38.570 -13.723 4.268   1.00 15.10 ?  80  SER   B H    1 
ATOM   5259 H HA   . SER   B 1 80  ? 40.752 -14.970 3.393   1.00 15.07 ?  80  SER   B HA   1 
ATOM   5260 H HB2  . SER   B 1 80  ? 40.415 -14.696 1.140   1.00 15.39 ?  80  SER   B HB2  1 
ATOM   5261 H HB3  . SER   B 1 80  ? 39.146 -15.478 1.687   1.00 15.39 ?  80  SER   B HB3  1 
ATOM   5262 H HG   . SER   B 1 80  ? 38.094 -13.554 1.677   1.00 16.72 ?  80  SER   B HG   1 
ATOM   5263 N N    . CYS   B 1 81  ? 41.835 -12.794 2.613   1.00 11.99 ?  81  CYS   B N    1 
ATOM   5264 C CA   . CYS   B 1 81  ? 42.383 -11.481 2.299   1.00 12.31 ?  81  CYS   B CA   1 
ATOM   5265 C C    . CYS   B 1 81  ? 43.156 -11.571 0.992   1.00 11.36 ?  81  CYS   B C    1 
ATOM   5266 O O    . CYS   B 1 81  ? 43.651 -12.639 0.611   1.00 12.56 ?  81  CYS   B O    1 
ATOM   5267 C CB   . CYS   B 1 81  ? 43.274 -10.933 3.423   1.00 12.89 ?  81  CYS   B CB   1 
ATOM   5268 S SG   . CYS   B 1 81  ? 44.801 -11.873 3.657   1.00 13.58 ?  81  CYS   B SG   1 
ATOM   5269 H H    . CYS   B 1 81  ? 42.351 -13.446 2.381   1.00 14.43 ?  81  CYS   B H    1 
ATOM   5270 H HA   . CYS   B 1 81  ? 41.651 -10.856 2.170   1.00 14.81 ?  81  CYS   B HA   1 
ATOM   5271 H HB2  . CYS   B 1 81  ? 43.515 -10.016 3.218   1.00 15.50 ?  81  CYS   B HB2  1 
ATOM   5272 H HB3  . CYS   B 1 81  ? 42.771 -10.957 4.258   1.00 15.50 ?  81  CYS   B HB3  1 
ATOM   5273 H HG   . CYS   B 1 81  ? 45.428 -11.382 4.559   1.00 16.33 ?  81  CYS   B HG   1 
ATOM   5274 N N    . VAL   B 1 82  ? 43.275 -10.423 0.323   1.00 11.86 ?  82  VAL   B N    1 
ATOM   5275 C CA   . VAL   B 1 82  ? 44.032 -10.297 -0.919  1.00 12.23 ?  82  VAL   B CA   1 
ATOM   5276 C C    . VAL   B 1 82  ? 45.377 -9.658  -0.610  1.00 12.65 ?  82  VAL   B C    1 
ATOM   5277 O O    . VAL   B 1 82  ? 45.434 -8.536  -0.083  1.00 13.75 ?  82  VAL   B O    1 
ATOM   5278 C CB   . VAL   B 1 82  ? 43.278 -9.464  -1.966  1.00 13.18 ?  82  VAL   B CB   1 
ATOM   5279 C CG1  . VAL   B 1 82  ? 44.120 -9.335  -3.230  1.00 14.61 ?  82  VAL   B CG1  1 
ATOM   5280 C CG2  . VAL   B 1 82  ? 41.920 -10.076 -2.277  1.00 14.04 ?  82  VAL   B CG2  1 
ATOM   5281 H H    . VAL   B 1 82  ? 42.906 -9.678  0.571   1.00 14.27 ?  82  VAL   B H    1 
ATOM   5282 H HA   . VAL   B 1 82  ? 44.188 -11.176 -1.289  1.00 14.71 ?  82  VAL   B HA   1 
ATOM   5283 H HB   . VAL   B 1 82  ? 43.131 -8.571  -1.622  1.00 15.86 ?  82  VAL   B HB   1 
ATOM   5284 H HG11 . VAL   B 1 82  ? 43.558 -9.021  -3.958  1.00 17.58 ?  82  VAL   B HG11 1 
ATOM   5285 H HG12 . VAL   B 1 82  ? 44.836 -8.694  -3.076  1.00 17.58 ?  82  VAL   B HG12 1 
ATOM   5286 H HG13 . VAL   B 1 82  ? 44.495 -10.200 -3.456  1.00 17.58 ?  82  VAL   B HG13 1 
ATOM   5287 H HG21 . VAL   B 1 82  ? 41.485 -9.554  -2.971  1.00 16.89 ?  82  VAL   B HG21 1 
ATOM   5288 H HG22 . VAL   B 1 82  ? 42.046 -10.989 -2.584  1.00 16.89 ?  82  VAL   B HG22 1 
ATOM   5289 H HG23 . VAL   B 1 82  ? 41.381 -10.070 -1.472  1.00 16.89 ?  82  VAL   B HG23 1 
ATOM   5290 N N    . LEU   B 1 83  ? 46.453 -10.350 -0.978  1.00 12.36 ?  83  LEU   B N    1 
ATOM   5291 C CA   . LEU   B 1 83  ? 47.814 -9.837  -0.861  1.00 12.06 ?  83  LEU   B CA   1 
ATOM   5292 C C    . LEU   B 1 83  ? 48.510 -9.988  -2.212  1.00 11.87 ?  83  LEU   B C    1 
ATOM   5293 O O    . LEU   B 1 83  ? 47.901 -10.414 -3.198  1.00 12.08 ?  83  LEU   B O    1 
ATOM   5294 C CB   . LEU   B 1 83  ? 48.557 -10.516 0.296   1.00 12.67 ?  83  LEU   B CB   1 
ATOM   5295 C CG   . LEU   B 1 83  ? 48.058 -10.158 1.701   1.00 13.93 ?  83  LEU   B CG   1 
ATOM   5296 C CD1  . LEU   B 1 83  ? 48.695 -11.019 2.771   1.00 14.34 ?  83  LEU   B CD1  1 
ATOM   5297 C CD2  . LEU   B 1 83  ? 48.276 -8.672  2.011   1.00 14.97 ?  83  LEU   B CD2  1 
ATOM   5298 H H    . LEU   B 1 83  ? 46.413 -11.144 -1.312  1.00 14.87 ?  83  LEU   B H    1 
ATOM   5299 H HA   . LEU   B 1 83  ? 47.768 -8.894  -0.668  1.00 14.51 ?  83  LEU   B HA   1 
ATOM   5300 H HB2  . LEU   B 1 83  ? 48.477 -11.475 0.196   1.00 15.24 ?  83  LEU   B HB2  1 
ATOM   5301 H HB3  . LEU   B 1 83  ? 49.493 -10.262 0.245   1.00 15.24 ?  83  LEU   B HB3  1 
ATOM   5302 H HG   . LEU   B 1 83  ? 47.104 -10.314 1.730   1.00 16.75 ?  83  LEU   B HG   1 
ATOM   5303 H HD11 . LEU   B 1 83  ? 48.342 -10.762 3.639   1.00 17.25 ?  83  LEU   B HD11 1 
ATOM   5304 H HD12 . LEU   B 1 83  ? 48.477 -11.951 2.594   1.00 17.25 ?  83  LEU   B HD12 1 
ATOM   5305 H HD13 . LEU   B 1 83  ? 49.655 -10.898 2.754   1.00 17.25 ?  83  LEU   B HD13 1 
ATOM   5306 H HD21 . LEU   B 1 83  ? 48.076 -8.515  2.948   1.00 18.01 ?  83  LEU   B HD21 1 
ATOM   5307 H HD22 . LEU   B 1 83  ? 49.199 -8.442  1.827   1.00 18.01 ?  83  LEU   B HD22 1 
ATOM   5308 H HD23 . LEU   B 1 83  ? 47.684 -8.142  1.455   1.00 18.01 ?  83  LEU   B HD23 1 
ATOM   5309 N N    . SER   B 1 84  ? 49.789 -9.615  -2.274  1.00 13.05 ?  84  SER   B N    1 
ATOM   5310 C CA   . SER   B 1 84  ? 50.521 -9.752  -3.523  1.00 13.10 ?  84  SER   B CA   1 
ATOM   5311 C C    . SER   B 1 84  ? 50.676 -11.221 -3.904  1.00 12.40 ?  84  SER   B C    1 
ATOM   5312 O O    . SER   B 1 84  ? 50.799 -12.099 -3.050  1.00 12.43 ?  84  SER   B O    1 
ATOM   5313 C CB   . SER   B 1 84  ? 51.915 -9.145  -3.384  1.00 14.94 ?  84  SER   B CB   1 
ATOM   5314 O OG   . SER   B 1 84  ? 52.662 -9.367  -4.564  1.00 16.26 ?  84  SER   B OG   1 
ATOM   5315 H H    . SER   B 1 84  ? 50.239 -9.277  -1.623  1.00 15.70 ?  84  SER   B H    1 
ATOM   5316 H HA   . SER   B 1 84  ? 50.051 -9.297  -4.236  1.00 15.76 ?  84  SER   B HA   1 
ATOM   5317 H HB2  . SER   B 1 84  ? 51.832 -8.190  -3.229  1.00 17.97 ?  84  SER   B HB2  1 
ATOM   5318 H HB3  . SER   B 1 84  ? 52.373 -9.562  -2.635  1.00 17.97 ?  84  SER   B HB3  1 
ATOM   5319 H HG   . SER   B 1 84  ? 53.433 -9.023  -4.485  1.00 19.55 ?  84  SER   B HG   1 
ATOM   5320 N N    . GLY   B 1 85  ? 50.743 -11.471 -5.207  1.00 13.28 ?  85  GLY   B N    1 
ATOM   5321 C CA   . GLY   B 1 85  ? 51.105 -12.773 -5.714  1.00 14.13 ?  85  GLY   B CA   1 
ATOM   5322 C C    . GLY   B 1 85  ? 52.575 -12.957 -6.025  1.00 13.63 ?  85  GLY   B C    1 
ATOM   5323 O O    . GLY   B 1 85  ? 52.962 -14.036 -6.476  1.00 13.95 ?  85  GLY   B O    1 
ATOM   5324 H H    . GLY   B 1 85  ? 50.587 -10.899 -5.824  1.00 15.97 ?  85  GLY   B H    1 
ATOM   5325 H HA2  . GLY   B 1 85  ? 50.853 -13.451 -5.064  1.00 17.00 ?  85  GLY   B HA2  1 
ATOM   5326 H HA3  . GLY   B 1 85  ? 50.614 -12.949 -6.529  1.00 17.00 ?  85  GLY   B HA3  1 
ATOM   5327 N N    . HIS   B 1 86  ? 53.422 -11.949 -5.819  1.00 13.61 ?  86  HIS   B N    1 
ATOM   5328 C CA   . HIS   B 1 86  ? 54.885 -12.110 -5.911  1.00 13.67 ?  86  HIS   B CA   1 
ATOM   5329 C C    . HIS   B 1 86  ? 55.261 -12.633 -7.295  1.00 13.29 ?  86  HIS   B C    1 
ATOM   5330 O O    . HIS   B 1 86  ? 54.867 -12.030 -8.306  1.00 14.42 ?  86  HIS   B O    1 
ATOM   5331 C CB   . HIS   B 1 86  ? 55.391 -12.933 -4.725  1.00 14.15 ?  86  HIS   B CB   1 
ATOM   5332 C CG   . HIS   B 1 86  ? 55.066 -12.318 -3.404  1.00 14.39 ?  86  HIS   B CG   1 
ATOM   5333 N ND1  . HIS   B 1 86  ? 55.887 -11.401 -2.787  1.00 15.88 ?  86  HIS   B ND1  1 
ATOM   5334 C CD2  . HIS   B 1 86  ? 53.982 -12.455 -2.602  1.00 14.78 ?  86  HIS   B CD2  1 
ATOM   5335 C CE1  . HIS   B 1 86  ? 55.326 -11.006 -1.658  1.00 15.67 ?  86  HIS   B CE1  1 
ATOM   5336 N NE2  . HIS   B 1 86  ? 54.166 -11.622 -1.526  1.00 15.08 ?  86  HIS   B NE2  1 
ATOM   5337 H H    . HIS   B 1 86  ? 53.177 -11.154 -5.617  1.00 16.37 ?  86  HIS   B H    1 
ATOM   5338 H HA   . HIS   B 1 86  ? 55.289 -11.235 -5.825  1.00 16.44 ?  86  HIS   B HA   1 
ATOM   5339 H HB2  . HIS   B 1 86  ? 54.991 -13.815 -4.752  1.00 17.02 ?  86  HIS   B HB2  1 
ATOM   5340 H HB3  . HIS   B 1 86  ? 56.361 -13.012 -4.783  1.00 17.02 ?  86  HIS   B HB3  1 
ATOM   5341 H HD2  . HIS   B 1 86  ? 53.243 -12.997 -2.763  1.00 17.77 ?  86  HIS   B HD2  1 
ATOM   5342 H HE1  . HIS   B 1 86  ? 55.694 -10.404 -1.052  1.00 18.85 ?  86  HIS   B HE1  1 
ATOM   5343 H HE2  . HIS   B 1 86  ? 53.625 -11.537 -0.863  1.00 18.14 ?  86  HIS   B HE2  1 
ATOM   5344 N N    . ASN   B 1 87  ? 56.032 -13.717 -7.394  1.00 14.05 ?  87  ASN   B N    1 
ATOM   5345 C CA   . ASN   B 1 87  ? 56.423 -14.306 -8.667  1.00 14.94 ?  87  ASN   B CA   1 
ATOM   5346 C C    . ASN   B 1 87  ? 55.429 -15.335 -9.171  1.00 14.70 ?  87  ASN   B C    1 
ATOM   5347 O O    . ASN   B 1 87  ? 55.730 -16.032 -10.145 1.00 16.43 ?  87  ASN   B O    1 
ATOM   5348 C CB   . ASN   B 1 87  ? 57.810 -14.955 -8.555  1.00 16.78 ?  87  ASN   B CB   1 
ATOM   5349 C CG   . ASN   B 1 87  ? 57.862 -16.056 -7.502  1.00 17.29 ?  87  ASN   B CG   1 
ATOM   5350 O OD1  . ASN   B 1 87  ? 57.231 -15.955 -6.447  1.00 16.55 ?  87  ASN   B OD1  1 
ATOM   5351 N ND2  . ASN   B 1 87  ? 58.614 -17.126 -7.794  1.00 19.13 ?  87  ASN   B ND2  1 
ATOM   5352 H H    . ASN   B 1 87  ? 56.337 -14.150 -6.716  1.00 16.90 ?  87  ASN   B H    1 
ATOM   5353 H HA   . ASN   B 1 87  ? 56.476 -13.607 -9.328  1.00 17.97 ?  87  ASN   B HA   1 
ATOM   5354 H HB2  . ASN   B 1 87  ? 58.049 -15.347 -9.414  1.00 20.17 ?  87  ASN   B HB2  1 
ATOM   5355 H HB3  . ASN   B 1 87  ? 58.456 -14.278 -8.311  1.00 20.17 ?  87  ASN   B HB3  1 
ATOM   5356 H HD21 . ASN   B 1 87  ? 58.683 -17.773 -7.234  1.00 22.99 ?  87  ASN   B HD21 1 
ATOM   5357 H HD22 . ASN   B 1 87  ? 59.044 -17.164 -8.545  1.00 22.99 ?  87  ASN   B HD22 1 
ATOM   5358 N N    . LEU   B 1 88  ? 54.257 -15.436 -8.543  1.00 13.69 ?  88  LEU   B N    1 
ATOM   5359 C CA   . LEU   B 1 88  ? 53.273 -16.458 -8.875  1.00 14.04 ?  88  LEU   B CA   1 
ATOM   5360 C C    . LEU   B 1 88  ? 52.046 -15.932 -9.598  1.00 13.73 ?  88  LEU   B C    1 
ATOM   5361 O O    . LEU   B 1 88  ? 51.444 -16.673 -10.384 1.00 15.80 ?  88  LEU   B O    1 
ATOM   5362 C CB   . LEU   B 1 88  ? 52.791 -17.143 -7.595  1.00 15.08 ?  88  LEU   B CB   1 
ATOM   5363 C CG   . LEU   B 1 88  ? 53.904 -17.826 -6.816  1.00 17.15 ?  88  LEU   B CG   1 
ATOM   5364 C CD1  . LEU   B 1 88  ? 53.430 -18.166 -5.415  1.00 18.63 ?  88  LEU   B CD1  1 
ATOM   5365 C CD2  . LEU   B 1 88  ? 54.341 -19.075 -7.554  1.00 20.09 ?  88  LEU   B CD2  1 
ATOM   5366 H H    . LEU   B 1 88  ? 54.006 -14.921 -7.898  1.00 16.46 ?  88  LEU   B H    1 
ATOM   5367 H HA   . LEU   B 1 88  ? 53.682 -17.129 -9.437  1.00 16.88 ?  88  LEU   B HA   1 
ATOM   5368 H HB2  . LEU   B 1 88  ? 52.381 -16.483 -7.014  1.00 18.13 ?  88  LEU   B HB2  1 
ATOM   5369 H HB3  . LEU   B 1 88  ? 52.130 -17.822 -7.829  1.00 18.13 ?  88  LEU   B HB3  1 
ATOM   5370 H HG   . LEU   B 1 88  ? 54.661 -17.229 -6.748  1.00 20.62 ?  88  LEU   B HG   1 
ATOM   5371 H HD11 . LEU   B 1 88  ? 54.085 -18.742 -4.993  1.00 22.40 ?  88  LEU   B HD11 1 
ATOM   5372 H HD12 . LEU   B 1 88  ? 53.335 -17.344 -4.909  1.00 22.40 ?  88  LEU   B HD12 1 
ATOM   5373 H HD13 . LEU   B 1 88  ? 52.576 -18.619 -5.474  1.00 22.40 ?  88  LEU   B HD13 1 
ATOM   5374 H HD21 . LEU   B 1 88  ? 54.984 -19.553 -7.008  1.00 24.15 ?  88  LEU   B HD21 1 
ATOM   5375 H HD22 . LEU   B 1 88  ? 53.566 -19.633 -7.720  1.00 24.15 ?  88  LEU   B HD22 1 
ATOM   5376 H HD23 . LEU   B 1 88  ? 54.749 -18.817 -8.396  1.00 24.15 ?  88  LEU   B HD23 1 
ATOM   5377 N N    . ALA   B 1 89  ? 51.636 -14.700 -9.319  1.00 13.10 ?  89  ALA   B N    1 
ATOM   5378 C CA   . ALA   B 1 89  ? 50.353 -14.194 -9.776  1.00 12.57 ?  89  ALA   B CA   1 
ATOM   5379 C C    . ALA   B 1 89  ? 50.341 -12.707 -9.482  1.00 12.75 ?  89  ALA   B C    1 
ATOM   5380 O O    . ALA   B 1 89  ? 51.160 -12.210 -8.710  1.00 13.53 ?  89  ALA   B O    1 
ATOM   5381 C CB   . ALA   B 1 89  ? 49.206 -14.857 -9.025  1.00 12.89 ?  89  ALA   B CB   1 
ATOM   5382 H H    . ALA   B 1 89  ? 52.084 -14.129 -8.860  1.00 15.76 ?  89  ALA   B H    1 
ATOM   5383 H HA   . ALA   B 1 89  ? 50.244 -14.341 -10.735 1.00 15.12 ?  89  ALA   B HA   1 
ATOM   5384 H HB1  . ALA   B 1 89  ? 48.363 -14.511 -9.366  1.00 15.51 ?  89  ALA   B HB1  1 
ATOM   5385 H HB2  . ALA   B 1 89  ? 49.247 -15.817 -9.171  1.00 15.51 ?  89  ALA   B HB2  1 
ATOM   5386 H HB3  . ALA   B 1 89  ? 49.291 -14.659 -8.085  1.00 15.51 ?  89  ALA   B HB3  1 
ATOM   5387 N N    . LYS   B 1 90  ? 49.382 -11.998 -10.070 1.00 13.48 ?  90  LYS   B N    1 
ATOM   5388 C CA   . LYS   B 1 90  ? 49.200 -10.610 -9.660  1.00 13.57 ?  90  LYS   B CA   1 
ATOM   5389 C C    . LYS   B 1 90  ? 48.864 -10.534 -8.173  1.00 12.90 ?  90  LYS   B C    1 
ATOM   5390 O O    . LYS   B 1 90  ? 49.508 -9.795  -7.414  1.00 14.08 ?  90  LYS   B O    1 
ATOM   5391 C CB   . LYS   B 1 90  ? 48.140 -9.939  -10.532 1.00 15.00 ?  90  LYS   B CB   1 
ATOM   5392 C CG   . LYS   B 1 90  ? 47.798 -8.513  -10.124 1.00 15.03 ?  90  LYS   B CG   1 
ATOM   5393 C CD   . LYS   B 1 90  ? 48.979 -7.582  -10.193 1.00 16.67 ?  90  LYS   B CD   1 
ATOM   5394 C CE   . LYS   B 1 90  ? 48.491 -6.195  -9.849  1.00 18.64 ?  90  LYS   B CE   1 
ATOM   5395 N NZ   . LYS   B 1 90  ? 49.581 -5.203  -9.819  1.00 18.36 ?  90  LYS   B NZ   1 
ATOM   5396 H H    . LYS   B 1 90  ? 48.852 -12.284 -10.688 1.00 16.21 ?  90  LYS   B H    1 
ATOM   5397 H HA   . LYS   B 1 90  ? 50.032 -10.139 -9.801  1.00 16.32 ?  90  LYS   B HA   1 
ATOM   5398 H HB2  . LYS   B 1 90  ? 48.461 -9.906  -11.452 1.00 18.04 ?  90  LYS   B HB2  1 
ATOM   5399 H HB3  . LYS   B 1 90  ? 47.324 -10.461 -10.498 1.00 18.04 ?  90  LYS   B HB3  1 
ATOM   5400 H HG2  . LYS   B 1 90  ? 47.109 -8.169  -10.721 1.00 18.07 ?  90  LYS   B HG2  1 
ATOM   5401 H HG3  . LYS   B 1 90  ? 47.461 -8.512  -9.211  1.00 18.07 ?  90  LYS   B HG3  1 
ATOM   5402 H HD2  . LYS   B 1 90  ? 49.651 -7.846  -9.546  1.00 20.04 ?  90  LYS   B HD2  1 
ATOM   5403 H HD3  . LYS   B 1 90  ? 49.344 -7.573  -11.092 1.00 20.04 ?  90  LYS   B HD3  1 
ATOM   5404 H HE2  . LYS   B 1 90  ? 47.846 -5.904  -10.515 1.00 22.40 ?  90  LYS   B HE2  1 
ATOM   5405 H HE3  . LYS   B 1 90  ? 48.079 -6.204  -8.972  1.00 22.40 ?  90  LYS   B HE3  1 
ATOM   5406 H HZ1  . LYS   B 1 90  ? 49.258 -4.395  -9.616  1.00 22.07 ?  90  LYS   B HZ1  1 
ATOM   5407 H HZ2  . LYS   B 1 90  ? 50.187 -5.430  -9.211  1.00 22.07 ?  90  LYS   B HZ2  1 
ATOM   5408 H HZ3  . LYS   B 1 90  ? 49.975 -5.157  -10.618 1.00 22.07 ?  90  LYS   B HZ3  1 
ATOM   5409 N N    . HIS   B 1 91  ? 47.884 -11.336 -7.736  1.00 11.85 ?  91  HIS   B N    1 
ATOM   5410 C CA   . HIS   B 1 91  ? 47.410 -11.362 -6.365  1.00 12.04 ?  91  HIS   B CA   1 
ATOM   5411 C C    . HIS   B 1 91  ? 47.401 -12.790 -5.847  1.00 11.26 ?  91  HIS   B C    1 
ATOM   5412 O O    . HIS   B 1 91  ? 47.165 -13.741 -6.606  1.00 12.01 ?  91  HIS   B O    1 
ATOM   5413 C CB   . HIS   B 1 91  ? 45.959 -10.875 -6.262  1.00 13.73 ?  91  HIS   B CB   1 
ATOM   5414 C CG   . HIS   B 1 91  ? 45.764 -9.455  -6.670  1.00 16.85 ?  91  HIS   B CG   1 
ATOM   5415 N ND1  . HIS   B 1 91  ? 46.387 -8.396  -6.041  1.00 19.20 ?  91  HIS   B ND1  1 
ATOM   5416 C CD2  . HIS   B 1 91  ? 44.984 -8.913  -7.631  1.00 19.27 ?  91  HIS   B CD2  1 
ATOM   5417 C CE1  . HIS   B 1 91  ? 46.016 -7.263  -6.612  1.00 20.28 ?  91  HIS   B CE1  1 
ATOM   5418 N NE2  . HIS   B 1 91  ? 45.158 -7.550  -7.575  1.00 20.57 ?  91  HIS   B NE2  1 
ATOM   5419 H H    . HIS   B 1 91  ? 47.466 -11.892 -8.247  1.00 14.26 ?  91  HIS   B H    1 
ATOM   5420 H HA   . HIS   B 1 91  ? 47.980 -10.807 -5.801  1.00 14.49 ?  91  HIS   B HA   1 
ATOM   5421 H HB2  . HIS   B 1 91  ? 45.402 -11.424 -6.837  1.00 16.51 ?  91  HIS   B HB2  1 
ATOM   5422 H HB3  . HIS   B 1 91  ? 45.662 -10.960 -5.342  1.00 16.51 ?  91  HIS   B HB3  1 
ATOM   5423 H HD2  . HIS   B 1 91  ? 44.433 -9.365  -8.226  1.00 23.16 ?  91  HIS   B HD2  1 
ATOM   5424 H HE1  . HIS   B 1 91  ? 46.303 -6.411  -6.365  1.00 24.37 ?  91  HIS   B HE1  1 
ATOM   5425 H HE2  . HIS   B 1 91  ? 44.781 -6.967  -8.088  1.00 24.72 ?  91  HIS   B HE2  1 
ATOM   5426 N N    . CYS   B 1 92  ? 47.587 -12.928 -4.541  1.00 11.25 ?  92  CYS   B N    1 
ATOM   5427 C CA   . CYS   B 1 92  ? 47.274 -14.163 -3.831  1.00 10.89 ?  92  CYS   B CA   1 
ATOM   5428 C C    . CYS   B 1 92  ? 46.053 -13.921 -2.950  1.00 10.66 ?  92  CYS   B C    1 
ATOM   5429 O O    . CYS   B 1 92  ? 46.055 -13.010 -2.108  1.00 11.84 ?  92  CYS   B O    1 
ATOM   5430 C CB   . CYS   B 1 92  ? 48.451 -14.625 -2.978  1.00 11.21 ?  92  CYS   B CB   1 
ATOM   5431 S SG   . CYS   B 1 92  ? 48.087 -16.148 -2.070  1.00 12.13 ?  92  CYS   B SG   1 
ATOM   5432 H H    . CYS   B 1 92  ? 47.919 -12.310 -4.033  1.00 13.53 ?  92  CYS   B H    1 
ATOM   5433 H HA   . CYS   B 1 92  ? 47.069 -14.857 -4.476  1.00 13.11 ?  92  CYS   B HA   1 
ATOM   5434 H HB2  . CYS   B 1 92  ? 49.212 -14.785 -3.549  1.00 13.49 ?  92  CYS   B HB2  1 
ATOM   5435 H HB3  . CYS   B 1 92  ? 48.653 -13.934 -2.328  1.00 13.49 ?  92  CYS   B HB3  1 
ATOM   5436 H HG   . CYS   B 1 92  ? 49.065 -16.465 -1.448  1.00 14.60 ?  92  CYS   B HG   1 
ATOM   5437 N N    . LEU   B 1 93  ? 45.014 -14.722 -3.161  1.00 10.92 ?  93  LEU   B N    1 
ATOM   5438 C CA   . LEU   B 1 93  ? 43.839 -14.733 -2.300  1.00 10.91 ?  93  LEU   B CA   1 
ATOM   5439 C C    . LEU   B 1 93  ? 44.062 -15.796 -1.232  1.00 10.46 ?  93  LEU   B C    1 
ATOM   5440 O O    . LEU   B 1 93  ? 44.010 -17.001 -1.522  1.00 11.25 ?  93  LEU   B O    1 
ATOM   5441 C CB   . LEU   B 1 93  ? 42.579 -15.033 -3.107  1.00 11.61 ?  93  LEU   B CB   1 
ATOM   5442 C CG   . LEU   B 1 93  ? 41.277 -15.039 -2.304  1.00 12.26 ?  93  LEU   B CG   1 
ATOM   5443 C CD1  . LEU   B 1 93  ? 40.910 -13.646 -1.821  1.00 12.75 ?  93  LEU   B CD1  1 
ATOM   5444 C CD2  . LEU   B 1 93  ? 40.147 -15.639 -3.124  1.00 12.14 ?  93  LEU   B CD2  1 
ATOM   5445 H H    . LEU   B 1 93  ? 44.966 -15.288 -3.816  1.00 13.15 ?  93  LEU   B H    1 
ATOM   5446 H HA   . LEU   B 1 93  ? 43.739 -13.872 -1.874  1.00 13.13 ?  93  LEU   B HA   1 
ATOM   5447 H HB2  . LEU   B 1 93  ? 42.490 -14.356 -3.800  1.00 13.97 ?  93  LEU   B HB2  1 
ATOM   5448 H HB3  . LEU   B 1 93  ? 42.671 -15.905 -3.517  1.00 13.97 ?  93  LEU   B HB3  1 
ATOM   5449 H HG   . LEU   B 1 93  ? 41.394 -15.592 -1.521  1.00 14.75 ?  93  LEU   B HG   1 
ATOM   5450 H HD11 . LEU   B 1 93  ? 40.058 -13.682 -1.366  1.00 15.34 ?  93  LEU   B HD11 1 
ATOM   5451 H HD12 . LEU   B 1 93  ? 41.600 -13.330 -1.218  1.00 15.34 ?  93  LEU   B HD12 1 
ATOM   5452 H HD13 . LEU   B 1 93  ? 40.850 -13.052 -2.591  1.00 15.34 ?  93  LEU   B HD13 1 
ATOM   5453 H HD21 . LEU   B 1 93  ? 39.327 -15.623 -2.598  1.00 14.60 ?  93  LEU   B HD21 1 
ATOM   5454 H HD22 . LEU   B 1 93  ? 40.023 -15.118 -3.934  1.00 14.60 ?  93  LEU   B HD22 1 
ATOM   5455 H HD23 . LEU   B 1 93  ? 40.370 -16.555 -3.352  1.00 14.60 ?  93  LEU   B HD23 1 
ATOM   5456 N N    . HIS   B 1 94  ? 44.332 -15.360 -0.009  1.00 10.53 ?  94  HIS   B N    1 
ATOM   5457 C CA   . HIS   B 1 94  ? 44.550 -16.265 1.113   1.00 10.78 ?  94  HIS   B CA   1 
ATOM   5458 C C    . HIS   B 1 94  ? 43.184 -16.613 1.692   1.00 11.31 ?  94  HIS   B C    1 
ATOM   5459 O O    . HIS   B 1 94  ? 42.512 -15.737 2.239   1.00 12.70 ?  94  HIS   B O    1 
ATOM   5460 C CB   . HIS   B 1 94  ? 45.425 -15.594 2.171   1.00 11.30 ?  94  HIS   B CB   1 
ATOM   5461 C CG   . HIS   B 1 94  ? 46.806 -15.291 1.698   1.00 11.19 ?  94  HIS   B CG   1 
ATOM   5462 N ND1  . HIS   B 1 94  ? 47.835 -16.204 1.778   1.00 11.54 ?  94  HIS   B ND1  1 
ATOM   5463 C CD2  . HIS   B 1 94  ? 47.311 -14.182 1.103   1.00 11.56 ?  94  HIS   B CD2  1 
ATOM   5464 C CE1  . HIS   B 1 94  ? 48.924 -15.649 1.273   1.00 11.75 ?  94  HIS   B CE1  1 
ATOM   5465 N NE2  . HIS   B 1 94  ? 48.634 -14.428 0.852   1.00 11.70 ?  94  HIS   B NE2  1 
ATOM   5466 H H    . HIS   B 1 94  ? 44.393 -14.520 0.198   1.00 12.68 ?  94  HIS   B H    1 
ATOM   5467 H HA   . HIS   B 1 94  ? 44.979 -17.072 0.803   1.00 12.98 ?  94  HIS   B HA   1 
ATOM   5468 H HB2  . HIS   B 1 94  ? 45.014 -14.759 2.436   1.00 13.59 ?  94  HIS   B HB2  1 
ATOM   5469 H HB3  . HIS   B 1 94  ? 45.498 -16.187 2.932   1.00 13.59 ?  94  HIS   B HB3  1 
ATOM   5470 H HD2  . HIS   B 1 94  ? 46.849 -13.400 0.908   1.00 13.91 ?  94  HIS   B HD2  1 
ATOM   5471 H HE1  . HIS   B 1 94  ? 49.755 -16.064 1.206   1.00 14.14 ?  94  HIS   B HE1  1 
ATOM   5472 H HE2  . HIS   B 1 94  ? 49.186 -13.884 0.481   1.00 14.07 ?  94  HIS   B HE2  1 
ATOM   5473 N N    . VAL   B 1 95  ? 42.750 -17.868 1.540   1.00 11.10 ?  95  VAL   B N    1 
ATOM   5474 C CA   . VAL   B 1 95  ? 41.421 -18.306 1.968   1.00 10.89 ?  95  VAL   B CA   1 
ATOM   5475 C C    . VAL   B 1 95  ? 41.585 -19.337 3.072   1.00 11.29 ?  95  VAL   B C    1 
ATOM   5476 O O    . VAL   B 1 95  ? 42.351 -20.297 2.921   1.00 12.10 ?  95  VAL   B O    1 
ATOM   5477 C CB   . VAL   B 1 95  ? 40.611 -18.917 0.811   1.00 11.76 ?  95  VAL   B CB   1 
ATOM   5478 C CG1  . VAL   B 1 95  ? 39.241 -19.372 1.296   1.00 13.05 ?  95  VAL   B CG1  1 
ATOM   5479 C CG2  . VAL   B 1 95  ? 40.483 -17.927 -0.324  1.00 11.62 ?  95  VAL   B CG2  1 
ATOM   5480 H H    . VAL   B 1 95  ? 43.219 -18.493 1.177   1.00 13.36 ?  95  VAL   B H    1 
ATOM   5481 H HA   . VAL   B 1 95  ? 40.929 -17.551 2.323   1.00 13.10 ?  95  VAL   B HA   1 
ATOM   5482 H HB   . VAL   B 1 95  ? 41.081 -19.689 0.471   1.00 14.15 ?  95  VAL   B HB   1 
ATOM   5483 H HG11 . VAL   B 1 95  ? 38.677 -19.553 0.525   1.00 15.70 ?  95  VAL   B HG11 1 
ATOM   5484 H HG12 . VAL   B 1 95  ? 39.343 -20.179 1.823   1.00 15.70 ?  95  VAL   B HG12 1 
ATOM   5485 H HG13 . VAL   B 1 95  ? 38.843 -18.670 1.834   1.00 15.70 ?  95  VAL   B HG13 1 
ATOM   5486 H HG21 . VAL   B 1 95  ? 39.910 -18.306 -1.007  1.00 13.98 ?  95  VAL   B HG21 1 
ATOM   5487 H HG22 . VAL   B 1 95  ? 40.088 -17.106 0.019   1.00 13.98 ?  95  VAL   B HG22 1 
ATOM   5488 H HG23 . VAL   B 1 95  ? 41.361 -17.746 -0.685  1.00 13.98 ?  95  VAL   B HG23 1 
ATOM   5489 N N    . VAL   B 1 96  ? 40.853 -19.154 4.166   1.00 11.97 ?  96  VAL   B N    1 
ATOM   5490 C CA   . VAL   B 1 96  ? 40.933 -20.063 5.310   1.00 12.44 ?  96  VAL   B CA   1 
ATOM   5491 C C    . VAL   B 1 96  ? 39.748 -21.028 5.266   1.00 13.33 ?  96  VAL   B C    1 
ATOM   5492 O O    . VAL   B 1 96  ? 38.633 -20.676 5.659   1.00 13.64 ?  96  VAL   B O    1 
ATOM   5493 C CB   . VAL   B 1 96  ? 40.982 -19.317 6.647   1.00 13.32 ?  96  VAL   B CB   1 
ATOM   5494 C CG1  . VAL   B 1 96  ? 41.156 -20.313 7.791   1.00 14.12 ?  96  VAL   B CG1  1 
ATOM   5495 C CG2  . VAL   B 1 96  ? 42.096 -18.284 6.659   1.00 13.69 ?  96  VAL   B CG2  1 
ATOM   5496 H H    . VAL   B 1 96  ? 40.296 -18.509 4.278   1.00 14.40 ?  96  VAL   B H    1 
ATOM   5497 H HA   . VAL   B 1 96  ? 41.745 -20.590 5.240   1.00 14.96 ?  96  VAL   B HA   1 
ATOM   5498 H HB   . VAL   B 1 96  ? 40.140 -18.858 6.784   1.00 16.02 ?  96  VAL   B HB   1 
ATOM   5499 H HG11 . VAL   B 1 96  ? 41.350 -19.826 8.610   1.00 16.98 ?  96  VAL   B HG11 1 
ATOM   5500 H HG12 . VAL   B 1 96  ? 40.338 -20.824 7.902   1.00 16.98 ?  96  VAL   B HG12 1 
ATOM   5501 H HG13 . VAL   B 1 96  ? 41.894 -20.910 7.585   1.00 16.98 ?  96  VAL   B HG13 1 
ATOM   5502 H HG21 . VAL   B 1 96  ? 42.138 -17.870 7.539   1.00 16.46 ?  96  VAL   B HG21 1 
ATOM   5503 H HG22 . VAL   B 1 96  ? 42.937 -18.713 6.456   1.00 16.46 ?  96  VAL   B HG22 1 
ATOM   5504 H HG23 . VAL   B 1 96  ? 41.901 -17.602 5.991   1.00 16.46 ?  96  VAL   B HG23 1 
ATOM   5505 N N    . GLY   B 1 97  ? 39.985 -22.262 4.814   1.00 13.00 ?  97  GLY   B N    1 
ATOM   5506 C CA   . GLY   B 1 97  ? 39.021 -23.325 4.987   1.00 13.72 ?  97  GLY   B CA   1 
ATOM   5507 C C    . GLY   B 1 97  ? 39.156 -23.925 6.370   1.00 15.11 ?  97  GLY   B C    1 
ATOM   5508 O O    . GLY   B 1 97  ? 40.201 -23.795 7.021   1.00 15.60 ?  97  GLY   B O    1 
ATOM   5509 H H    . GLY   B 1 97  ? 40.703 -22.492 4.392   1.00 15.64 ?  97  GLY   B H    1 
ATOM   5510 H HA2  . GLY   B 1 97  ? 38.124 -22.963 4.868   1.00 16.51 ?  97  GLY   B HA2  1 
ATOM   5511 H HA3  . GLY   B 1 97  ? 39.168 -24.011 4.316   1.00 16.51 ?  97  GLY   B HA3  1 
ATOM   5512 N N    . PRO   B 1 98  ? 38.111 -24.598 6.848   1.00 16.18 ?  98  PRO   B N    1 
ATOM   5513 C CA   . PRO   B 1 98  ? 38.217 -25.289 8.137   1.00 17.21 ?  98  PRO   B CA   1 
ATOM   5514 C C    . PRO   B 1 98  ? 39.241 -26.416 8.087   1.00 16.79 ?  98  PRO   B C    1 
ATOM   5515 O O    . PRO   B 1 98  ? 39.335 -27.154 7.107   1.00 17.10 ?  98  PRO   B O    1 
ATOM   5516 C CB   . PRO   B 1 98  ? 36.800 -25.828 8.364   1.00 18.06 ?  98  PRO   B CB   1 
ATOM   5517 C CG   . PRO   B 1 98  ? 36.221 -25.966 7.000   1.00 17.53 ?  98  PRO   B CG   1 
ATOM   5518 C CD   . PRO   B 1 98  ? 36.791 -24.802 6.221   1.00 16.58 ?  98  PRO   B CD   1 
ATOM   5519 H HA   . PRO   B 1 98  ? 38.451 -24.662 8.834   1.00 20.69 ?  98  PRO   B HA   1 
ATOM   5520 H HB2  . PRO   B 1 98  ? 36.848 -26.690 8.806   1.00 21.71 ?  98  PRO   B HB2  1 
ATOM   5521 H HB3  . PRO   B 1 98  ? 36.292 -25.195 8.890   1.00 21.71 ?  98  PRO   B HB3  1 
ATOM   5522 H HG2  . PRO   B 1 98  ? 36.499 -26.812 6.610   1.00 21.07 ?  98  PRO   B HG2  1 
ATOM   5523 H HG3  . PRO   B 1 98  ? 35.255 -25.912 7.047   1.00 21.07 ?  98  PRO   B HG3  1 
ATOM   5524 H HD2  . PRO   B 1 98  ? 36.882 -25.039 5.279   1.00 19.94 ?  98  PRO   B HD2  1 
ATOM   5525 H HD3  . PRO   B 1 98  ? 36.238 -24.014 6.333   1.00 19.94 ?  98  PRO   B HD3  1 
ATOM   5526 N N    . ASN   B 1 99  ? 40.007 -26.542 9.167   1.00 18.07 ?  99  ASN   B N    1 
ATOM   5527 C CA   . ASN   B 1 99  ? 40.991 -27.612 9.324   1.00 19.51 ?  99  ASN   B CA   1 
ATOM   5528 C C    . ASN   B 1 99  ? 40.376 -28.692 10.213  1.00 22.68 ?  99  ASN   B C    1 
ATOM   5529 O O    . ASN   B 1 99  ? 40.326 -28.547 11.437  1.00 23.56 ?  99  ASN   B O    1 
ATOM   5530 C CB   . ASN   B 1 99  ? 42.270 -27.053 9.938   1.00 19.90 ?  99  ASN   B CB   1 
ATOM   5531 C CG   . ASN   B 1 99  ? 43.410 -28.057 9.941   1.00 20.47 ?  99  ASN   B CG   1 
ATOM   5532 O OD1  . ASN   B 1 99  ? 43.203 -29.246 10.145  1.00 21.23 ?  99  ASN   B OD1  1 
ATOM   5533 N ND2  . ASN   B 1 99  ? 44.617 -27.577 9.701   1.00 20.69 ?  99  ASN   B ND2  1 
ATOM   5534 H H    . ASN   B 1 99  ? 39.972 -26.007 9.835   1.00 21.72 ?  99  ASN   B H    1 
ATOM   5535 H HA   . ASN   B 1 99  ? 41.195 -28.006 8.461   1.00 23.45 ?  99  ASN   B HA   1 
ATOM   5536 H HB2  . ASN   B 1 99  ? 42.544 -26.281 9.432   1.00 23.92 ?  99  ASN   B HB2  1 
ATOM   5537 H HB3  . ASN   B 1 99  ? 42.088 -26.809 10.860  1.00 23.92 ?  99  ASN   B HB3  1 
ATOM   5538 H HD21 . ASN   B 1 99  ? 45.293 -28.101 9.684   1.00 24.87 ?  99  ASN   B HD21 1 
ATOM   5539 H HD22 . ASN   B 1 99  ? 44.716 -26.733 9.565   1.00 24.87 ?  99  ASN   B HD22 1 
ATOM   5540 N N    A VAL   B 1 100 ? 39.890 -29.770 9.590   0.72 24.64 ?  100 VAL   B N    1 
ATOM   5541 N N    B VAL   B 1 100 ? 39.914 -29.778 9.584   0.28 24.88 ?  100 VAL   B N    1 
ATOM   5542 C CA   A VAL   B 1 100 ? 39.278 -30.858 10.352  0.72 27.49 ?  100 VAL   B CA   1 
ATOM   5543 C CA   B VAL   B 1 100 ? 39.282 -30.869 10.323  0.28 27.22 ?  100 VAL   B CA   1 
ATOM   5544 C C    A VAL   B 1 100 ? 40.294 -31.526 11.270  0.72 28.09 ?  100 VAL   B C    1 
ATOM   5545 C C    B VAL   B 1 100 ? 40.285 -31.557 11.242  0.28 28.02 ?  100 VAL   B C    1 
ATOM   5546 O O    A VAL   B 1 100 ? 39.943 -32.004 12.356  0.72 28.89 ?  100 VAL   B O    1 
ATOM   5547 O O    B VAL   B 1 100 ? 39.913 -32.076 12.302  0.28 28.35 ?  100 VAL   B O    1 
ATOM   5548 C CB   A VAL   B 1 100 ? 38.601 -31.864 9.398   0.72 29.77 ?  100 VAL   B CB   1 
ATOM   5549 C CB   B VAL   B 1 100 ? 38.611 -31.852 9.343   0.28 28.66 ?  100 VAL   B CB   1 
ATOM   5550 C CG1  A VAL   B 1 100 ? 38.113 -33.085 10.163  0.72 30.70 ?  100 VAL   B CG1  1 
ATOM   5551 C CG1  B VAL   B 1 100 ? 38.106 -33.089 10.071  0.28 29.17 ?  100 VAL   B CG1  1 
ATOM   5552 C CG2  A VAL   B 1 100 ? 37.444 -31.197 8.668   0.72 30.18 ?  100 VAL   B CG2  1 
ATOM   5553 C CG2  B VAL   B 1 100 ? 37.466 -31.166 8.609   0.28 29.05 ?  100 VAL   B CG2  1 
ATOM   5554 H H    A VAL   B 1 100 ? 39.889 -29.886 8.736   0.72 29.61 ?  100 VAL   B H    1 
ATOM   5555 H H    B VAL   B 1 100 ? 39.956 -29.906 8.734   0.28 29.90 ?  100 VAL   B H    1 
ATOM   5556 H HA   A VAL   B 1 100 ? 38.577 -30.484 10.911  0.72 33.02 ?  100 VAL   B HA   1 
ATOM   5557 H HA   B VAL   B 1 100 ? 38.581 -30.499 10.880  0.28 32.70 ?  100 VAL   B HA   1 
ATOM   5558 H HB   A VAL   B 1 100 ? 39.244 -32.163 8.736   0.72 35.76 ?  100 VAL   B HB   1 
ATOM   5559 H HB   B VAL   B 1 100 ? 39.261 -32.140 8.682   0.28 34.43 ?  100 VAL   B HB   1 
ATOM   5560 H HG11 A VAL   B 1 100 ? 37.501 -33.587 9.600   0.72 36.87 ?  100 VAL   B HG11 1 
ATOM   5561 H HG11 B VAL   B 1 100 ? 37.506 -33.577 9.484   0.28 35.04 ?  100 VAL   B HG11 1 
ATOM   5562 H HG12 A VAL   B 1 100 ? 38.873 -33.640 10.397  0.72 36.87 ?  100 VAL   B HG12 1 
ATOM   5563 H HG12 B VAL   B 1 100 ? 38.861 -33.650 10.307  0.28 35.04 ?  100 VAL   B HG12 1 
ATOM   5564 H HG13 A VAL   B 1 100 ? 37.654 -32.792 10.966  0.72 36.87 ?  100 VAL   B HG13 1 
ATOM   5565 H HG13 B VAL   B 1 100 ? 37.632 -32.813 10.870  0.28 35.04 ?  100 VAL   B HG13 1 
ATOM   5566 H HG21 A VAL   B 1 100 ? 37.015 -31.849 8.092   0.72 36.26 ?  100 VAL   B HG21 1 
ATOM   5567 H HG21 B VAL   B 1 100 ? 37.043 -31.804 8.014   0.28 34.90 ?  100 VAL   B HG21 1 
ATOM   5568 H HG22 A VAL   B 1 100 ? 36.808 -30.867 9.323   0.72 36.26 ?  100 VAL   B HG22 1 
ATOM   5569 H HG22 B VAL   B 1 100 ? 36.823 -30.845 9.261   0.28 34.90 ?  100 VAL   B HG22 1 
ATOM   5570 H HG23 A VAL   B 1 100 ? 37.787 -30.462 8.139   0.72 36.26 ?  100 VAL   B HG23 1 
ATOM   5571 H HG23 B VAL   B 1 100 ? 37.820 -30.421 8.100   0.28 34.90 ?  100 VAL   B HG23 1 
ATOM   5572 N N    . ASN   B 1 101 ? 41.562 -31.586 10.855  1.00 28.39 ?  101 ASN   B N    1 
ATOM   5573 C CA   . ASN   B 1 101 ? 42.601 -32.128 11.730  1.00 30.22 ?  101 ASN   B CA   1 
ATOM   5574 C C    . ASN   B 1 101 ? 42.785 -31.292 12.992  1.00 33.52 ?  101 ASN   B C    1 
ATOM   5575 O O    . ASN   B 1 101 ? 43.402 -31.770 13.954  1.00 34.20 ?  101 ASN   B O    1 
ATOM   5576 C CB   . ASN   B 1 101 ? 43.920 -32.265 10.967  1.00 29.52 ?  101 ASN   B CB   1 
ATOM   5577 C CG   . ASN   B 1 101 ? 43.905 -33.425 9.987   1.00 28.56 ?  101 ASN   B CG   1 
ATOM   5578 O OD1  . ASN   B 1 101 ? 43.217 -34.418 10.204  1.00 29.37 ?  101 ASN   B OD1  1 
ATOM   5579 N ND2  . ASN   B 1 101 ? 44.655 -33.298 8.900   1.00 27.99 ?  101 ASN   B ND2  1 
ATOM   5580 H H    A ASN   B 1 101 ? 41.835 -31.341 10.078  0.72 34.10 ?  101 ASN   B H    1 
ATOM   5581 H H    B ASN   B 1 101 ? 41.843 -31.314 10.090  0.28 34.10 ?  101 ASN   B H    1 
ATOM   5582 H HA   . ASN   B 1 101 ? 42.333 -33.013 12.010  1.00 36.31 ?  101 ASN   B HA   1 
ATOM   5583 H HB2  . ASN   B 1 101 ? 44.088 -31.453 10.464  1.00 35.46 ?  101 ASN   B HB2  1 
ATOM   5584 H HB3  . ASN   B 1 101 ? 44.637 -32.419 11.600  1.00 35.46 ?  101 ASN   B HB3  1 
ATOM   5585 H HD21 . ASN   B 1 101 ? 44.674 -33.930 8.316   1.00 33.63 ?  101 ASN   B HD21 1 
ATOM   5586 H HD22 . ASN   B 1 101 ? 45.119 -32.585 8.778   1.00 33.63 ?  101 ASN   B HD22 1 
ATOM   5587 N N    A LYS   B 1 102 ? 42.274 -30.059 13.005  0.72 35.57 ?  102 LYS   B N    1 
ATOM   5588 N N    B LYS   B 1 102 ? 42.271 -30.062 13.010  0.28 35.58 ?  102 LYS   B N    1 
ATOM   5589 C CA   A LYS   B 1 102 ? 42.238 -29.221 14.196  0.72 38.05 ?  102 LYS   B CA   1 
ATOM   5590 C CA   B LYS   B 1 102 ? 42.242 -29.236 14.209  0.28 37.74 ?  102 LYS   B CA   1 
ATOM   5591 C C    A LYS   B 1 102 ? 40.858 -29.190 14.842  0.72 37.60 ?  102 LYS   B C    1 
ATOM   5592 C C    B LYS   B 1 102 ? 40.863 -29.202 14.855  0.28 37.64 ?  102 LYS   B C    1 
ATOM   5593 O O    A LYS   B 1 102 ? 40.627 -28.383 15.747  0.72 37.86 ?  102 LYS   B O    1 
ATOM   5594 O O    B LYS   B 1 102 ? 40.642 -28.417 15.782  0.28 37.94 ?  102 LYS   B O    1 
ATOM   5595 C CB   A LYS   B 1 102 ? 42.655 -27.789 13.858  0.72 41.12 ?  102 LYS   B CB   1 
ATOM   5596 C CB   B LYS   B 1 102 ? 42.698 -27.810 13.892  0.28 39.85 ?  102 LYS   B CB   1 
ATOM   5597 C CG   A LYS   B 1 102 ? 44.112 -27.598 13.483  0.72 44.09 ?  102 LYS   B CG   1 
ATOM   5598 C CG   B LYS   B 1 102 ? 44.164 -27.682 13.514  0.28 41.80 ?  102 LYS   B CG   1 
ATOM   5599 C CD   A LYS   B 1 102 ? 44.347 -26.150 13.081  0.72 46.65 ?  102 LYS   B CD   1 
ATOM   5600 C CD   B LYS   B 1 102 ? 44.493 -26.251 13.119  0.28 43.43 ?  102 LYS   B CD   1 
ATOM   5601 C CE   A LYS   B 1 102 ? 45.811 -25.849 12.823  0.72 48.56 ?  102 LYS   B CE   1 
ATOM   5602 C CE   B LYS   B 1 102 ? 45.980 -26.053 12.887  0.28 44.67 ?  102 LYS   B CE   1 
ATOM   5603 N NZ   A LYS   B 1 102 ? 46.001 -24.424 12.425  0.72 49.63 ?  102 LYS   B NZ   1 
ATOM   5604 N NZ   B LYS   B 1 102 ? 46.285 -24.647 12.493  0.28 45.38 ?  102 LYS   B NZ   1 
ATOM   5605 H H    A LYS   B 1 102 ? 41.929 -29.678 12.314  0.72 42.72 ?  102 LYS   B H    1 
ATOM   5606 H H    B LYS   B 1 102 ? 41.922 -29.676 12.323  0.28 42.74 ?  102 LYS   B H    1 
ATOM   5607 H HA   A LYS   B 1 102 ? 42.869 -29.569 14.844  0.72 45.70 ?  102 LYS   B HA   1 
ATOM   5608 H HA   B LYS   B 1 102 ? 42.862 -29.604 14.855  0.28 45.32 ?  102 LYS   B HA   1 
ATOM   5609 H HB2  A LYS   B 1 102 ? 42.120 -27.480 13.112  0.72 49.39 ?  102 LYS   B HB2  1 
ATOM   5610 H HB2  B LYS   B 1 102 ? 42.174 -27.472 13.151  0.28 47.86 ?  102 LYS   B HB2  1 
ATOM   5611 H HB3  A LYS   B 1 102 ? 42.482 -27.229 14.633  0.72 49.39 ?  102 LYS   B HB3  1 
ATOM   5612 H HB3  B LYS   B 1 102 ? 42.549 -27.256 14.675  0.28 47.86 ?  102 LYS   B HB3  1 
ATOM   5613 H HG2  A LYS   B 1 102 ? 44.677 -27.804 14.245  0.72 52.95 ?  102 LYS   B HG2  1 
ATOM   5614 H HG2  B LYS   B 1 102 ? 44.717 -27.924 14.274  0.28 50.19 ?  102 LYS   B HG2  1 
ATOM   5615 H HG3  A LYS   B 1 102 ? 44.333 -28.168 12.730  0.72 52.95 ?  102 LYS   B HG3  1 
ATOM   5616 H HG3  B LYS   B 1 102 ? 44.355 -28.259 12.759  0.28 50.19 ?  102 LYS   B HG3  1 
ATOM   5617 H HD2  A LYS   B 1 102 ? 43.853 -25.962 12.267  0.72 56.01 ?  102 LYS   B HD2  1 
ATOM   5618 H HD2  B LYS   B 1 102 ? 44.026 -26.032 12.297  0.28 52.15 ?  102 LYS   B HD2  1 
ATOM   5619 H HD3  A LYS   B 1 102 ? 44.041 -25.569 13.796  0.72 56.01 ?  102 LYS   B HD3  1 
ATOM   5620 H HD3  B LYS   B 1 102 ? 44.215 -25.652 13.830  0.28 52.15 ?  102 LYS   B HD3  1 
ATOM   5621 H HE2  A LYS   B 1 102 ? 46.320 -26.011 13.633  0.72 58.31 ?  102 LYS   B HE2  1 
ATOM   5622 H HE2  B LYS   B 1 102 ? 46.462 -26.251 13.706  0.28 53.64 ?  102 LYS   B HE2  1 
ATOM   5623 H HE3  A LYS   B 1 102 ? 46.133 -26.413 12.103  0.72 58.31 ?  102 LYS   B HE3  1 
ATOM   5624 H HE3  B LYS   B 1 102 ? 46.275 -26.640 12.173  0.28 53.64 ?  102 LYS   B HE3  1 
ATOM   5625 H HZ1  A LYS   B 1 102 ? 46.862 -24.261 12.277  0.72 59.59 ?  102 LYS   B HZ1  1 
ATOM   5626 H HZ1  B LYS   B 1 102 ? 47.159 -24.550 12.361  0.28 54.50 ?  102 LYS   B HZ1  1 
ATOM   5627 H HZ2  A LYS   B 1 102 ? 45.541 -24.252 11.682  0.72 59.59 ?  102 LYS   B HZ2  1 
ATOM   5628 H HZ2  B LYS   B 1 102 ? 45.854 -24.443 11.741  0.28 54.50 ?  102 LYS   B HZ2  1 
ATOM   5629 H HZ3  A LYS   B 1 102 ? 45.712 -23.886 13.073  0.72 59.59 ?  102 LYS   B HZ3  1 
ATOM   5630 H HZ3  B LYS   B 1 102 ? 46.024 -24.089 13.136  0.28 54.50 ?  102 LYS   B HZ3  1 
ATOM   5631 N N    . GLY   B 1 103 ? 39.930 -30.026 14.381  1.00 37.20 ?  103 GLY   B N    1 
ATOM   5632 C CA   . GLY   B 1 103 ? 38.602 -30.084 14.959  1.00 36.92 ?  103 GLY   B CA   1 
ATOM   5633 C C    . GLY   B 1 103 ? 37.652 -28.996 14.516  1.00 36.28 ?  103 GLY   B C    1 
ATOM   5634 O O    . GLY   B 1 103 ? 36.569 -28.870 15.098  1.00 36.57 ?  103 GLY   B O    1 
ATOM   5635 H H    A GLY   B 1 103 ? 40.048 -30.567 13.725  0.72 44.68 ?  103 GLY   B H    1 
ATOM   5636 H H    B GLY   B 1 103 ? 40.046 -30.561 13.720  0.28 44.68 ?  103 GLY   B H    1 
ATOM   5637 H HA2  . GLY   B 1 103 ? 38.204 -30.942 14.741  1.00 44.34 ?  103 GLY   B HA2  1 
ATOM   5638 H HA3  . GLY   B 1 103 ? 38.676 -30.027 15.924  1.00 44.34 ?  103 GLY   B HA3  1 
ATOM   5639 N N    A GLU   B 1 104 ? 38.025 -28.196 13.520  0.72 35.28 ?  104 GLU   B N    1 
ATOM   5640 N N    B GLU   B 1 104 ? 38.008 -28.215 13.501  0.28 35.78 ?  104 GLU   B N    1 
ATOM   5641 C CA   A GLU   B 1 104 ? 37.174 -27.106 13.072  0.72 34.29 ?  104 GLU   B CA   1 
ATOM   5642 C CA   B GLU   B 1 104 ? 37.144 -27.139 13.044  0.28 35.22 ?  104 GLU   B CA   1 
ATOM   5643 C C    A GLU   B 1 104 ? 35.987 -27.641 12.271  0.72 34.51 ?  104 GLU   B C    1 
ATOM   5644 C C    B GLU   B 1 104 ? 35.977 -27.688 12.225  0.28 35.29 ?  104 GLU   B C    1 
ATOM   5645 O O    A GLU   B 1 104 ? 36.019 -28.741 11.710  0.72 35.05 ?  104 GLU   B O    1 
ATOM   5646 O O    B GLU   B 1 104 ? 36.045 -28.772 11.638  0.28 35.49 ?  104 GLU   B O    1 
ATOM   5647 C CB   A GLU   B 1 104 ? 37.989 -26.104 12.251  0.72 33.25 ?  104 GLU   B CB   1 
ATOM   5648 C CB   B GLU   B 1 104 ? 37.951 -26.119 12.241  0.28 34.54 ?  104 GLU   B CB   1 
ATOM   5649 C CG   A GLU   B 1 104 ? 39.099 -25.449 13.065  0.72 32.21 ?  104 GLU   B CG   1 
ATOM   5650 C CG   B GLU   B 1 104 ? 39.060 -25.479 13.062  0.28 33.90 ?  104 GLU   B CG   1 
ATOM   5651 C CD   A GLU   B 1 104 ? 40.009 -24.551 12.252  0.72 31.04 ?  104 GLU   B CD   1 
ATOM   5652 C CD   B GLU   B 1 104 ? 39.957 -24.570 12.247  0.28 33.29 ?  104 GLU   B CD   1 
ATOM   5653 O OE1  A GLU   B 1 104 ? 39.998 -24.632 11.007  0.72 29.36 ?  104 GLU   B OE1  1 
ATOM   5654 O OE1  B GLU   B 1 104 ? 39.870 -24.596 11.002  0.28 32.85 ?  104 GLU   B OE1  1 
ATOM   5655 O OE2  A GLU   B 1 104 ? 40.750 -23.760 12.872  0.72 31.14 -1 104 GLU   B OE2  1 
ATOM   5656 O OE2  B GLU   B 1 104 ? 40.753 -23.826 12.857  0.28 33.17 -1 104 GLU   B OE2  1 
ATOM   5657 H H    A GLU   B 1 104 ? 38.770 -28.258 13.097  0.72 42.37 ?  104 GLU   B H    1 
ATOM   5658 H H    B GLU   B 1 104 ? 38.748 -28.282 13.068  0.28 42.98 ?  104 GLU   B H    1 
ATOM   5659 H HA   A GLU   B 1 104 ? 36.825 -26.641 13.848  0.72 41.18 ?  104 GLU   B HA   1 
ATOM   5660 H HA   B GLU   B 1 104 ? 36.775 -26.685 13.814  0.28 42.30 ?  104 GLU   B HA   1 
ATOM   5661 H HB2  A GLU   B 1 104 ? 38.396 -26.564 11.502  0.72 39.93 ?  104 GLU   B HB2  1 
ATOM   5662 H HB2  B GLU   B 1 104 ? 38.356 -26.561 11.480  0.28 41.48 ?  104 GLU   B HB2  1 
ATOM   5663 H HB3  A GLU   B 1 104 ? 37.398 -25.404 11.930  0.72 39.93 ?  104 GLU   B HB3  1 
ATOM   5664 H HB3  B GLU   B 1 104 ? 37.357 -25.413 11.938  0.28 41.48 ?  104 GLU   B HB3  1 
ATOM   5665 H HG2  A GLU   B 1 104 ? 38.699 -24.911 13.766  0.72 38.69 ?  104 GLU   B HG2  1 
ATOM   5666 H HG2  B GLU   B 1 104 ? 38.661 -24.951 13.772  0.28 40.72 ?  104 GLU   B HG2  1 
ATOM   5667 H HG3  A GLU   B 1 104 ? 39.654 -26.140 13.455  0.72 38.69 ?  104 GLU   B HG3  1 
ATOM   5668 H HG3  B GLU   B 1 104 ? 39.611 -26.180 13.446  0.28 40.72 ?  104 GLU   B HG3  1 
ATOM   5669 N N    A ASP   B 1 105 ? 34.926 -26.836 12.226  0.72 34.05 ?  105 ASP   B N    1 
ATOM   5670 N N    B ASP   B 1 105 ? 34.892 -26.915 12.195  0.28 35.12 ?  105 ASP   B N    1 
ATOM   5671 C CA   A ASP   B 1 105 ? 33.652 -27.277 11.671  0.72 34.21 ?  105 ASP   B CA   1 
ATOM   5672 C CA   B ASP   B 1 105 ? 33.638 -27.378 11.612  0.28 34.99 ?  105 ASP   B CA   1 
ATOM   5673 C C    A ASP   B 1 105 ? 33.722 -27.329 10.150  0.72 31.58 ?  105 ASP   B C    1 
ATOM   5674 C C    B ASP   B 1 105 ? 33.738 -27.393 10.091  0.28 33.56 ?  105 ASP   B C    1 
ATOM   5675 O O    A ASP   B 1 105 ? 33.899 -26.298 9.493   0.72 30.60 ?  105 ASP   B O    1 
ATOM   5676 O O    B ASP   B 1 105 ? 33.947 -26.350 9.462   0.28 33.32 ?  105 ASP   B O    1 
ATOM   5677 C CB   A ASP   B 1 105 ? 32.543 -26.323 12.112  0.72 37.40 ?  105 ASP   B CB   1 
ATOM   5678 C CB   B ASP   B 1 105 ? 32.495 -26.470 12.062  0.28 36.28 ?  105 ASP   B CB   1 
ATOM   5679 C CG   A ASP   B 1 105 ? 31.167 -26.796 11.691  0.72 40.13 ?  105 ASP   B CG   1 
ATOM   5680 C CG   B ASP   B 1 105 ? 31.131 -27.039 11.720  0.28 37.38 ?  105 ASP   B CG   1 
ATOM   5681 O OD1  A ASP   B 1 105 ? 31.064 -27.904 11.122  0.72 40.59 ?  105 ASP   B OD1  1 
ATOM   5682 O OD1  B ASP   B 1 105 ? 31.075 -28.095 11.054  0.28 37.66 ?  105 ASP   B OD1  1 
ATOM   5683 O OD2  A ASP   B 1 105 ? 30.185 -26.061 11.931  0.72 41.53 -1 105 ASP   B OD2  1 
ATOM   5684 O OD2  B ASP   B 1 105 ? 30.114 -26.436 12.123  0.28 37.84 -1 105 ASP   B OD2  1 
ATOM   5685 H H    A ASP   B 1 105 ? 34.921 -26.026 12.510  0.72 40.90 ?  105 ASP   B H    1 
ATOM   5686 H H    B ASP   B 1 105 ? 34.857 -26.115 12.505  0.28 42.18 ?  105 ASP   B H    1 
ATOM   5687 H HA   A ASP   B 1 105 ? 33.440 -28.163 12.002  0.72 41.09 ?  105 ASP   B HA   1 
ATOM   5688 H HA   B ASP   B 1 105 ? 33.448 -28.279 11.915  0.28 42.02 ?  105 ASP   B HA   1 
ATOM   5689 H HB2  A ASP   B 1 105 ? 32.556 -26.244 13.080  0.72 44.92 ?  105 ASP   B HB2  1 
ATOM   5690 H HB2  B ASP   B 1 105 ? 32.538 -26.357 13.026  0.28 43.58 ?  105 ASP   B HB2  1 
ATOM   5691 H HB3  A ASP   B 1 105 ? 32.690 -25.454 11.707  0.72 44.92 ?  105 ASP   B HB3  1 
ATOM   5692 H HB3  B ASP   B 1 105 ? 32.581 -25.607 11.625  0.28 43.58 ?  105 ASP   B HB3  1 
ATOM   5693 N N    A ILE   B 1 106 ? 33.546 -28.531 9.593   0.72 30.65 ?  106 ILE   B N    1 
ATOM   5694 N N    B ILE   B 1 106 ? 33.580 -28.581 9.503   0.28 32.47 ?  106 ILE   B N    1 
ATOM   5695 C CA   A ILE   B 1 106 ? 33.543 -28.713 8.147   0.72 29.61 ?  106 ILE   B CA   1 
ATOM   5696 C CA   B ILE   B 1 106 ? 33.588 -28.726 8.052   0.28 31.53 ?  106 ILE   B CA   1 
ATOM   5697 C C    A ILE   B 1 106 ? 32.459 -27.878 7.474   0.72 28.01 ?  106 ILE   B C    1 
ATOM   5698 C C    B ILE   B 1 106 ? 32.486 -27.904 7.394   0.28 30.55 ?  106 ILE   B C    1 
ATOM   5699 O O    A ILE   B 1 106 ? 32.571 -27.558 6.287   0.72 27.27 ?  106 ILE   B O    1 
ATOM   5700 O O    B ILE   B 1 106 ? 32.569 -27.602 6.198   0.28 30.39 ?  106 ILE   B O    1 
ATOM   5701 C CB   A ILE   B 1 106 ? 33.417 -30.219 7.814   0.72 30.36 ?  106 ILE   B CB   1 
ATOM   5702 C CB   B ILE   B 1 106 ? 33.496 -30.226 7.685   0.28 31.69 ?  106 ILE   B CB   1 
ATOM   5703 C CG1  A ILE   B 1 106 ? 33.652 -30.476 6.325   0.72 30.61 ?  106 ILE   B CG1  1 
ATOM   5704 C CG1  B ILE   B 1 106 ? 33.746 -30.444 6.191   0.28 31.69 ?  106 ILE   B CG1  1 
ATOM   5705 C CG2  A ILE   B 1 106 ? 32.050 -30.749 8.234   0.72 31.30 ?  106 ILE   B CG2  1 
ATOM   5706 C CG2  B ILE   B 1 106 ? 32.135 -30.785 8.075   0.28 31.99 ?  106 ILE   B CG2  1 
ATOM   5707 C CD1  A ILE   B 1 106 ? 35.000 -30.013 5.839   0.72 30.60 ?  106 ILE   B CD1  1 
ATOM   5708 C CD1  B ILE   B 1 106 ? 35.079 -29.919 5.716   0.28 31.68 ?  106 ILE   B CD1  1 
ATOM   5709 H H    A ILE   B 1 106 ? 33.420 -29.255 10.039  0.72 36.82 ?  106 ILE   B H    1 
ATOM   5710 H H    B ILE   B 1 106 ? 33.478 -29.321 9.927   0.28 39.00 ?  106 ILE   B H    1 
ATOM   5711 H HA   A ILE   B 1 106 ? 34.393 -28.408 7.809   0.72 35.57 ?  106 ILE   B HA   1 
ATOM   5712 H HA   B ILE   B 1 106 ? 34.430 -28.390 7.719   0.28 37.87 ?  106 ILE   B HA   1 
ATOM   5713 H HB   A ILE   B 1 106 ? 34.091 -30.701 8.317   0.72 36.46 ?  106 ILE   B HB   1 
ATOM   5714 H HB   B ILE   B 1 106 ? 34.178 -30.707 8.182   0.28 38.07 ?  106 ILE   B HB   1 
ATOM   5715 H HG12 A ILE   B 1 106 ? 33.592 -31.432 6.160   0.72 36.77 ?  106 ILE   B HG12 1 
ATOM   5716 H HG12 B ILE   B 1 106 ? 33.722 -31.398 6.006   0.28 38.06 ?  106 ILE   B HG12 1 
ATOM   5717 H HG13 A ILE   B 1 106 ? 32.973 -30.012 5.813   0.72 36.77 ?  106 ILE   B HG13 1 
ATOM   5718 H HG13 B ILE   B 1 106 ? 33.051 -29.996 5.686   0.28 38.06 ?  106 ILE   B HG13 1 
ATOM   5719 H HG21 A ILE   B 1 106 ? 32.044 -31.716 8.143   0.72 37.60 ?  106 ILE   B HG21 1 
ATOM   5720 H HG21 B ILE   B 1 106 ? 32.156 -31.751 7.992   0.28 38.43 ?  106 ILE   B HG21 1 
ATOM   5721 H HG22 A ILE   B 1 106 ? 31.886 -30.506 9.159   0.72 37.60 ?  106 ILE   B HG22 1 
ATOM   5722 H HG22 B ILE   B 1 106 ? 31.944 -30.536 8.993   0.28 38.43 ?  106 ILE   B HG22 1 
ATOM   5723 H HG23 A ILE   B 1 106 ? 31.368 -30.360 7.665   0.72 37.60 ?  106 ILE   B HG23 1 
ATOM   5724 H HG23 B ILE   B 1 106 ? 31.460 -30.417 7.484   0.28 38.43 ?  106 ILE   B HG23 1 
ATOM   5725 H HD11 A ILE   B 1 106 ? 35.183 -30.424 4.981   0.72 36.76 ?  106 ILE   B HD11 1 
ATOM   5726 H HD11 B ILE   B 1 106 ? 35.283 -30.313 4.855   0.28 38.06 ?  106 ILE   B HD11 1 
ATOM   5727 H HD12 A ILE   B 1 106 ? 34.988 -29.047 5.747   0.72 36.76 ?  106 ILE   B HD12 1 
ATOM   5728 H HD12 B ILE   B 1 106 ? 35.027 -28.954 5.636   0.28 38.06 ?  106 ILE   B HD12 1 
ATOM   5729 H HD13 A ILE   B 1 106 ? 35.676 -30.277 6.483   0.72 36.76 ?  106 ILE   B HD13 1 
ATOM   5730 H HD13 B ILE   B 1 106 ? 35.761 -30.164 6.362   0.28 38.06 ?  106 ILE   B HD13 1 
ATOM   5731 N N    A GLN   B 1 107 ? 31.411 -27.499 8.212   0.72 28.06 ?  107 GLN   B N    1 
ATOM   5732 N N    B GLN   B 1 107 ? 31.448 -27.534 8.148   0.28 29.96 ?  107 GLN   B N    1 
ATOM   5733 C CA   A GLN   B 1 107 ? 30.332 -26.708 7.627   0.72 27.94 ?  107 GLN   B CA   1 
ATOM   5734 C CA   B GLN   B 1 107 ? 30.359 -26.733 7.598   0.28 29.26 ?  107 GLN   B CA   1 
ATOM   5735 C C    A GLN   B 1 107 ? 30.814 -25.354 7.122   0.72 25.52 ?  107 GLN   B C    1 
ATOM   5736 C C    B GLN   B 1 107 ? 30.825 -25.364 7.110   0.28 26.38 ?  107 GLN   B C    1 
ATOM   5737 O O    A GLN   B 1 107 ? 30.163 -24.771 6.250   0.72 25.78 ?  107 GLN   B O    1 
ATOM   5738 O O    B GLN   B 1 107 ? 30.165 -24.773 6.249   0.28 26.51 ?  107 GLN   B O    1 
ATOM   5739 C CB   A GLN   B 1 107 ? 29.211 -26.511 8.652   0.72 31.75 ?  107 GLN   B CB   1 
ATOM   5740 C CB   B GLN   B 1 107 ? 29.257 -26.578 8.651   0.28 31.63 ?  107 GLN   B CB   1 
ATOM   5741 C CG   A GLN   B 1 107 ? 27.881 -26.037 8.066   0.72 35.48 ?  107 GLN   B CG   1 
ATOM   5742 C CG   B GLN   B 1 107 ? 27.919 -26.095 8.107   0.28 33.84 ?  107 GLN   B CG   1 
ATOM   5743 C CD   A GLN   B 1 107 ? 27.785 -24.524 7.954   0.72 38.30 ?  107 GLN   B CD   1 
ATOM   5744 C CD   B GLN   B 1 107 ? 27.810 -24.583 8.069   0.28 35.56 ?  107 GLN   B CD   1 
ATOM   5745 O OE1  A GLN   B 1 107 ? 28.604 -23.794 8.514   0.72 39.30 ?  107 GLN   B OE1  1 
ATOM   5746 O OE1  B GLN   B 1 107 ? 28.605 -23.874 8.687   0.28 36.10 ?  107 GLN   B OE1  1 
ATOM   5747 N NE2  A GLN   B 1 107 ? 26.776 -24.047 7.229   0.72 39.37 ?  107 GLN   B NE2  1 
ATOM   5748 N NE2  B GLN   B 1 107 ? 26.818 -24.080 7.344   0.28 36.24 ?  107 GLN   B NE2  1 
ATOM   5749 H H    A GLN   B 1 107 ? 31.309 -27.672 9.041   0.72 33.71 ?  107 GLN   B H    1 
ATOM   5750 H H    B GLN   B 1 107 ? 31.345 -27.747 8.972   0.28 35.99 ?  107 GLN   B H    1 
ATOM   5751 H HA   A GLN   B 1 107 ? 29.964 -27.192 6.870   0.72 33.57 ?  107 GLN   B HA   1 
ATOM   5752 H HA   B GLN   B 1 107 ? 29.975 -27.202 6.842   0.28 35.15 ?  107 GLN   B HA   1 
ATOM   5753 H HB2  A GLN   B 1 107 ? 29.050 -27.355 9.092   0.72 38.14 ?  107 GLN   B HB2  1 
ATOM   5754 H HB2  B GLN   B 1 107 ? 29.106 -27.439 9.067   0.28 38.00 ?  107 GLN   B HB2  1 
ATOM   5755 H HB3  A GLN   B 1 107 ? 29.500 -25.851 9.302   0.72 38.14 ?  107 GLN   B HB3  1 
ATOM   5756 H HB3  B GLN   B 1 107 ? 29.552 -25.941 9.320   0.28 38.00 ?  107 GLN   B HB3  1 
ATOM   5757 H HG2  A GLN   B 1 107 ? 27.773 -26.406 7.177   0.72 42.62 ?  107 GLN   B HG2  1 
ATOM   5758 H HG2  B GLN   B 1 107 ? 27.805 -26.425 7.202   0.28 40.65 ?  107 GLN   B HG2  1 
ATOM   5759 H HG3  A GLN   B 1 107 ? 27.158 -26.342 8.640   0.72 42.62 ?  107 GLN   B HG3  1 
ATOM   5760 H HG3  B GLN   B 1 107 ? 27.206 -26.436 8.675   0.28 40.65 ?  107 GLN   B HG3  1 
ATOM   5761 H HE21 A GLN   B 1 107 ? 26.222 -24.587 6.851   0.72 47.28 ?  107 GLN   B HE21 1 
ATOM   5762 H HE21 B GLN   B 1 107 ? 26.281 -24.606 6.925   0.28 43.52 ?  107 GLN   B HE21 1 
ATOM   5763 H HE22 A GLN   B 1 107 ? 26.673 -23.197 7.137   0.72 47.28 ?  107 GLN   B HE22 1 
ATOM   5764 H HE22 B GLN   B 1 107 ? 26.712 -23.229 7.294   0.28 43.52 ?  107 GLN   B HE22 1 
ATOM   5765 N N    . LEU   B 1 108 ? 31.943 -24.849 7.631   1.00 23.45 ?  108 LEU   B N    1 
ATOM   5766 C CA   . LEU   B 1 108 ? 32.471 -23.545 7.216   1.00 20.47 ?  108 LEU   B CA   1 
ATOM   5767 C C    . LEU   B 1 108 ? 33.117 -23.566 5.840   1.00 17.75 ?  108 LEU   B C    1 
ATOM   5768 O O    . LEU   B 1 108 ? 33.545 -22.507 5.352   1.00 16.96 ?  108 LEU   B O    1 
ATOM   5769 C CB   . LEU   B 1 108 ? 33.471 -23.030 8.252   1.00 21.23 ?  108 LEU   B CB   1 
ATOM   5770 C CG   . LEU   B 1 108 ? 32.852 -22.482 9.538   1.00 22.94 ?  108 LEU   B CG   1 
ATOM   5771 C CD1  . LEU   B 1 108 ? 33.855 -22.513 10.675  1.00 23.71 ?  108 LEU   B CD1  1 
ATOM   5772 C CD2  . LEU   B 1 108 ? 32.356 -21.061 9.312   1.00 23.53 ?  108 LEU   B CD2  1 
ATOM   5773 H H    A LEU   B 1 108 ? 32.413 -25.242 8.229   0.72 28.17 ?  108 LEU   B H    1 
ATOM   5774 H H    B LEU   B 1 108 ? 32.411 -25.237 8.234   0.28 28.17 ?  108 LEU   B H    1 
ATOM   5775 H HA   . LEU   B 1 108 ? 31.737 -22.917 7.183   1.00 24.60 ?  108 LEU   B HA   1 
ATOM   5776 H HB2  . LEU   B 1 108 ? 34.057 -23.758 8.505   1.00 25.51 ?  108 LEU   B HB2  1 
ATOM   5777 H HB3  . LEU   B 1 108 ? 33.987 -22.316 7.854   1.00 25.51 ?  108 LEU   B HB3  1 
ATOM   5778 H HG   . LEU   B 1 108 ? 32.090 -23.029 9.792   1.00 27.56 ?  108 LEU   B HG   1 
ATOM   5779 H HD11 . LEU   B 1 108 ? 33.429 -22.182 11.483  1.00 28.49 ?  108 LEU   B HD11 1 
ATOM   5780 H HD12 . LEU   B 1 108 ? 34.152 -23.426 10.809  1.00 28.49 ?  108 LEU   B HD12 1 
ATOM   5781 H HD13 . LEU   B 1 108 ? 34.608 -21.948 10.445  1.00 28.49 ?  108 LEU   B HD13 1 
ATOM   5782 H HD21 . LEU   B 1 108 ? 31.963 -20.727 10.134  1.00 28.28 ?  108 LEU   B HD21 1 
ATOM   5783 H HD22 . LEU   B 1 108 ? 33.107 -20.503 9.054   1.00 28.28 ?  108 LEU   B HD22 1 
ATOM   5784 H HD23 . LEU   B 1 108 ? 31.691 -21.067 8.606   1.00 28.28 ?  108 LEU   B HD23 1 
ATOM   5785 N N    . LEU   B 1 109 ? 33.181 -24.732 5.206   1.00 16.64 ?  109 LEU   B N    1 
ATOM   5786 C CA   . LEU   B 1 109 ? 33.812 -24.842 3.898   1.00 15.71 ?  109 LEU   B CA   1 
ATOM   5787 C C    . LEU   B 1 109 ? 33.041 -24.066 2.835   1.00 15.07 ?  109 LEU   B C    1 
ATOM   5788 O O    . LEU   B 1 109 ? 33.652 -23.481 1.934   1.00 14.62 ?  109 LEU   B O    1 
ATOM   5789 C CB   . LEU   B 1 109 ? 33.934 -26.320 3.529   1.00 15.84 ?  109 LEU   B CB   1 
ATOM   5790 C CG   . LEU   B 1 109 ? 34.706 -26.661 2.260   1.00 15.20 ?  109 LEU   B CG   1 
ATOM   5791 C CD1  . LEU   B 1 109 ? 36.072 -25.999 2.260   1.00 15.04 ?  109 LEU   B CD1  1 
ATOM   5792 C CD2  . LEU   B 1 109 ? 34.840 -28.177 2.134   1.00 15.93 ?  109 LEU   B CD2  1 
ATOM   5793 H H    . LEU   B 1 109 ? 32.884 -25.472 5.511   1.00 20.00 ?  109 LEU   B H    1 
ATOM   5794 H HA   . LEU   B 1 109 ? 34.709 -24.470 3.943   1.00 18.89 ?  109 LEU   B HA   1 
ATOM   5795 H HB2  . LEU   B 1 109 ? 34.378 -26.778 4.257   1.00 19.05 ?  109 LEU   B HB2  1 
ATOM   5796 H HB3  . LEU   B 1 109 ? 33.040 -26.679 3.422   1.00 19.05 ?  109 LEU   B HB3  1 
ATOM   5797 H HG   . LEU   B 1 109 ? 34.209 -26.349 1.485   1.00 18.28 ?  109 LEU   B HG   1 
ATOM   5798 H HD11 . LEU   B 1 109 ? 36.606 -26.375 1.540   1.00 18.08 ?  109 LEU   B HD11 1 
ATOM   5799 H HD12 . LEU   B 1 109 ? 35.960 -25.050 2.129   1.00 18.08 ?  109 LEU   B HD12 1 
ATOM   5800 H HD13 . LEU   B 1 109 ? 36.503 -26.174 3.112   1.00 18.08 ?  109 LEU   B HD13 1 
ATOM   5801 H HD21 . LEU   B 1 109 ? 35.391 -28.384 1.359   1.00 19.15 ?  109 LEU   B HD21 1 
ATOM   5802 H HD22 . LEU   B 1 109 ? 35.257 -28.527 2.936   1.00 19.15 ?  109 LEU   B HD22 1 
ATOM   5803 H HD23 . LEU   B 1 109 ? 33.958 -28.571 2.022   1.00 19.15 ?  109 LEU   B HD23 1 
ATOM   5804 N N    . LYS   B 1 110 ? 31.707 -24.037 2.917   1.00 14.75 ?  110 LYS   B N    1 
ATOM   5805 C CA   . LYS   B 1 110 ? 30.950 -23.276 1.927   1.00 14.84 ?  110 LYS   B CA   1 
ATOM   5806 C C    . LYS   B 1 110 ? 31.289 -21.788 2.015   1.00 14.29 ?  110 LYS   B C    1 
ATOM   5807 O O    . LYS   B 1 110 ? 31.540 -21.134 0.994   1.00 14.15 ?  110 LYS   B O    1 
ATOM   5808 C CB   . LYS   B 1 110 ? 29.444 -23.528 2.070   1.00 15.38 ?  110 LYS   B CB   1 
ATOM   5809 C CG   . LYS   B 1 110 ? 28.632 -22.911 0.924   1.00 15.44 ?  110 LYS   B CG   1 
ATOM   5810 C CD   . LYS   B 1 110 ? 27.170 -23.350 0.952   1.00 16.02 ?  110 LYS   B CD   1 
ATOM   5811 C CE   . LYS   B 1 110 ? 26.397 -22.809 -0.243  1.00 16.76 ?  110 LYS   B CE   1 
ATOM   5812 N NZ   . LYS   B 1 110 ? 26.730 -23.520 -1.503  1.00 17.13 ?  110 LYS   B NZ   1 
ATOM   5813 H H    . LYS   B 1 110 ? 31.238 -24.439 3.514   1.00 17.74 ?  110 LYS   B H    1 
ATOM   5814 H HA   . LYS   B 1 110 ? 31.210 -23.579 1.045   1.00 17.85 ?  110 LYS   B HA   1 
ATOM   5815 H HB2  . LYS   B 1 110 ? 29.282 -24.488 2.072   1.00 18.49 ?  110 LYS   B HB2  1 
ATOM   5816 H HB3  . LYS   B 1 110 ? 29.133 -23.141 2.903   1.00 18.49 ?  110 LYS   B HB3  1 
ATOM   5817 H HG2  . LYS   B 1 110 ? 28.658 -21.946 1.000   1.00 18.57 ?  110 LYS   B HG2  1 
ATOM   5818 H HG3  . LYS   B 1 110 ? 29.013 -23.192 0.078   1.00 18.57 ?  110 LYS   B HG3  1 
ATOM   5819 H HD2  . LYS   B 1 110 ? 27.124 -24.321 0.928   1.00 19.26 ?  110 LYS   B HD2  1 
ATOM   5820 H HD3  . LYS   B 1 110 ? 26.750 -23.018 1.763   1.00 19.26 ?  110 LYS   B HD3  1 
ATOM   5821 H HE2  . LYS   B 1 110 ? 25.446 -22.907 -0.083  1.00 20.15 ?  110 LYS   B HE2  1 
ATOM   5822 H HE3  . LYS   B 1 110 ? 26.617 -21.868 -0.362  1.00 20.15 ?  110 LYS   B HE3  1 
ATOM   5823 H HZ1  . LYS   B 1 110 ? 26.267 -23.178 -2.179  1.00 20.60 ?  110 LYS   B HZ1  1 
ATOM   5824 H HZ2  . LYS   B 1 110 ? 27.601 -23.437 -1.677  1.00 20.60 ?  110 LYS   B HZ2  1 
ATOM   5825 H HZ3  . LYS   B 1 110 ? 26.534 -24.384 -1.422  1.00 20.60 ?  110 LYS   B HZ3  1 
ATOM   5826 N N    . SER   B 1 111 ? 31.312 -21.238 3.235   1.00 14.48 ?  111 SER   B N    1 
ATOM   5827 C CA   . SER   B 1 111 ? 31.702 -19.841 3.408   1.00 14.59 ?  111 SER   B CA   1 
ATOM   5828 C C    . SER   B 1 111 ? 33.078 -19.582 2.804   1.00 13.79 ?  111 SER   B C    1 
ATOM   5829 O O    . SER   B 1 111 ? 33.300 -18.552 2.150   1.00 14.04 ?  111 SER   B O    1 
ATOM   5830 C CB   . SER   B 1 111 ? 31.709 -19.487 4.894   1.00 15.44 ?  111 SER   B CB   1 
ATOM   5831 O OG   . SER   B 1 111 ? 30.408 -19.478 5.436   1.00 16.81 ?  111 SER   B OG   1 
ATOM   5832 H H    . SER   B 1 111 ? 31.118 -21.656 3.966   1.00 17.42 ?  111 SER   B H    1 
ATOM   5833 H HA   . SER   B 1 111 ? 31.058 -19.274 2.962   1.00 17.54 ?  111 SER   B HA   1 
ATOM   5834 H HB2  . SER   B 1 111 ? 32.240 -20.145 5.374   1.00 18.57 ?  111 SER   B HB2  1 
ATOM   5835 H HB3  . SER   B 1 111 ? 32.091 -18.608 5.008   1.00 18.57 ?  111 SER   B HB3  1 
ATOM   5836 H HG   . SER   B 1 111 ? 30.434 -19.290 6.262   1.00 20.20 ?  111 SER   B HG   1 
ATOM   5837 N N    . ALA   B 1 112 ? 34.021 -20.497 3.030   1.00 13.82 ?  112 ALA   B N    1 
ATOM   5838 C CA   . ALA   B 1 112 ? 35.361 -20.328 2.479   1.00 13.32 ?  112 ALA   B CA   1 
ATOM   5839 C C    . ALA   B 1 112 ? 35.327 -20.239 0.953   1.00 12.76 ?  112 ALA   B C    1 
ATOM   5840 O O    . ALA   B 1 112 ? 35.945 -19.349 0.356   1.00 13.29 ?  112 ALA   B O    1 
ATOM   5841 C CB   . ALA   B 1 112 ? 36.264 -21.466 2.961   1.00 13.69 ?  112 ALA   B CB   1 
ATOM   5842 H H    . ALA   B 1 112 ? 33.908 -21.215 3.501   1.00 16.62 ?  112 ALA   B H    1 
ATOM   5843 H HA   . ALA   B 1 112 ? 35.727 -19.499 2.819   1.00 16.03 ?  112 ALA   B HA   1 
ATOM   5844 H HB1  . ALA   B 1 112 ? 37.155 -21.333 2.592   1.00 16.46 ?  112 ALA   B HB1  1 
ATOM   5845 H HB2  . ALA   B 1 112 ? 36.311 -21.447 3.933   1.00 16.46 ?  112 ALA   B HB2  1 
ATOM   5846 H HB3  . ALA   B 1 112 ? 35.905 -22.311 2.663   1.00 16.46 ?  112 ALA   B HB3  1 
ATOM   5847 N N    . TYR   B 1 113 ? 34.597 -21.146 0.300   1.00 12.75 ?  113 TYR   B N    1 
ATOM   5848 C CA   . TYR   B 1 113 ? 34.521 -21.100 -1.155  1.00 12.92 ?  113 TYR   B CA   1 
ATOM   5849 C C    . TYR   B 1 113 ? 33.813 -19.850 -1.671  1.00 12.63 ?  113 TYR   B C    1 
ATOM   5850 O O    . TYR   B 1 113 ? 34.085 -19.416 -2.794  1.00 12.74 ?  113 TYR   B O    1 
ATOM   5851 C CB   . TYR   B 1 113 ? 33.850 -22.362 -1.698  1.00 13.00 ?  113 TYR   B CB   1 
ATOM   5852 C CG   . TYR   B 1 113 ? 34.810 -23.506 -1.945  1.00 13.40 ?  113 TYR   B CG   1 
ATOM   5853 C CD1  . TYR   B 1 113 ? 35.807 -23.404 -2.908  1.00 13.83 ?  113 TYR   B CD1  1 
ATOM   5854 C CD2  . TYR   B 1 113 ? 34.712 -24.695 -1.235  1.00 13.69 ?  113 TYR   B CD2  1 
ATOM   5855 C CE1  . TYR   B 1 113 ? 36.689 -24.432 -3.148  1.00 13.73 ?  113 TYR   B CE1  1 
ATOM   5856 C CE2  . TYR   B 1 113 ? 35.587 -25.747 -1.471  1.00 13.83 ?  113 TYR   B CE2  1 
ATOM   5857 C CZ   . TYR   B 1 113 ? 36.566 -25.612 -2.435  1.00 13.90 ?  113 TYR   B CZ   1 
ATOM   5858 O OH   . TYR   B 1 113 ? 37.446 -26.627 -2.703  1.00 14.84 ?  113 TYR   B OH   1 
ATOM   5859 H H    . TYR   B 1 113 ? 34.136 -21.777 0.674   1.00 15.34 ?  113 TYR   B H    1 
ATOM   5860 H HA   . TYR   B 1 113 ? 35.419 -21.081 -1.493  1.00 15.55 ?  113 TYR   B HA   1 
ATOM   5861 H HB2  . TYR   B 1 113 ? 33.183 -22.672 -1.058  1.00 15.64 ?  113 TYR   B HB2  1 
ATOM   5862 H HB3  . TYR   B 1 113 ? 33.413 -22.149 -2.538  1.00 15.64 ?  113 TYR   B HB3  1 
ATOM   5863 H HD1  . TYR   B 1 113 ? 35.889 -22.614 -3.396  1.00 16.64 ?  113 TYR   B HD1  1 
ATOM   5864 H HD2  . TYR   B 1 113 ? 34.046 -24.786 -0.598  1.00 16.47 ?  113 TYR   B HD2  1 
ATOM   5865 H HE1  . TYR   B 1 113 ? 37.348 -24.347 -3.800  1.00 16.52 ?  113 TYR   B HE1  1 
ATOM   5866 H HE2  . TYR   B 1 113 ? 35.505 -26.538 -0.994  1.00 16.63 ?  113 TYR   B HE2  1 
ATOM   5867 H HH   . TYR   B 1 113 ? 37.272 -27.293 -2.216  1.00 17.85 ?  113 TYR   B HH   1 
ATOM   5868 N N    . GLU   B 1 114 ? 32.887 -19.275 -0.896  1.00 12.72 ?  114 GLU   B N    1 
ATOM   5869 C CA   . GLU   B 1 114 ? 32.206 -18.067 -1.351  1.00 12.67 ?  114 GLU   B CA   1 
ATOM   5870 C C    . GLU   B 1 114 ? 33.190 -16.944 -1.652  1.00 12.62 ?  114 GLU   B C    1 
ATOM   5871 O O    . GLU   B 1 114 ? 32.908 -16.083 -2.489  1.00 13.22 ?  114 GLU   B O    1 
ATOM   5872 C CB   . GLU   B 1 114 ? 31.149 -17.634 -0.329  1.00 13.52 ?  114 GLU   B CB   1 
ATOM   5873 C CG   . GLU   B 1 114 ? 29.929 -18.556 -0.388  1.00 13.78 ?  114 GLU   B CG   1 
ATOM   5874 C CD   . GLU   B 1 114 ? 28.902 -18.360 0.718   1.00 13.80 ?  114 GLU   B CD   1 
ATOM   5875 O OE1  . GLU   B 1 114 ? 29.194 -17.746 1.761   1.00 14.05 ?  114 GLU   B OE1  1 
ATOM   5876 O OE2  . GLU   B 1 114 ? 27.780 -18.899 0.557   1.00 14.72 -1 114 GLU   B OE2  1 
ATOM   5877 H H    . GLU   B 1 114 ? 32.627 -19.571 -0.124  1.00 15.30 ?  114 GLU   B H    1 
ATOM   5878 H HA   . GLU   B 1 114 ? 31.739 -18.269 -2.174  1.00 15.24 ?  114 GLU   B HA   1 
ATOM   5879 H HB2  . GLU   B 1 114 ? 31.522 -17.678 0.567   1.00 16.26 ?  114 GLU   B HB2  1 
ATOM   5880 H HB3  . GLU   B 1 114 ? 30.855 -16.732 -0.527  1.00 16.26 ?  114 GLU   B HB3  1 
ATOM   5881 H HG2  . GLU   B 1 114 ? 29.478 -18.415 -1.229  1.00 16.58 ?  114 GLU   B HG2  1 
ATOM   5882 H HG3  . GLU   B 1 114 ? 30.240 -19.476 -0.333  1.00 16.58 ?  114 GLU   B HG3  1 
ATOM   5883 N N    . ASN   B 1 115 ? 34.364 -16.944 -1.009  1.00 12.50 ?  115 ASN   B N    1 
ATOM   5884 C CA   . ASN   B 1 115 ? 35.348 -15.905 -1.307  1.00 12.22 ?  115 ASN   B CA   1 
ATOM   5885 C C    . ASN   B 1 115 ? 35.761 -15.929 -2.773  1.00 12.15 ?  115 ASN   B C    1 
ATOM   5886 O O    . ASN   B 1 115 ? 36.146 -14.889 -3.332  1.00 12.73 ?  115 ASN   B O    1 
ATOM   5887 C CB   . ASN   B 1 115 ? 36.584 -16.071 -0.417  1.00 12.98 ?  115 ASN   B CB   1 
ATOM   5888 C CG   . ASN   B 1 115 ? 36.308 -15.801 1.042   1.00 13.41 ?  115 ASN   B CG   1 
ATOM   5889 O OD1  . ASN   B 1 115 ? 36.300 -14.650 1.484   1.00 15.43 ?  115 ASN   B OD1  1 
ATOM   5890 N ND2  . ASN   B 1 115 ? 36.133 -16.869 1.820   1.00 13.64 ?  115 ASN   B ND2  1 
ATOM   5891 H H    . ASN   B 1 115 ? 34.606 -17.512 -0.404  1.00 15.03 ?  115 ASN   B H    1 
ATOM   5892 H HA   . ASN   B 1 115 ? 34.959 -15.038 -1.119  1.00 14.70 ?  115 ASN   B HA   1 
ATOM   5893 H HB2  . ASN   B 1 115 ? 36.915 -16.979 -0.502  1.00 15.62 ?  115 ASN   B HB2  1 
ATOM   5894 H HB3  . ASN   B 1 115 ? 37.266 -15.444 -0.708  1.00 15.62 ?  115 ASN   B HB3  1 
ATOM   5895 H HD21 . ASN   B 1 115 ? 35.982 -16.770 2.662   1.00 16.40 ?  115 ASN   B HD21 1 
ATOM   5896 H HD22 . ASN   B 1 115 ? 36.159 -17.661 1.482   1.00 16.40 ?  115 ASN   B HD22 1 
ATOM   5897 N N    . PHE   B 1 116 ? 35.741 -17.112 -3.402  1.00 12.03 ?  116 PHE   B N    1 
ATOM   5898 C CA   . PHE   B 1 116 ? 36.164 -17.202 -4.794  1.00 12.28 ?  116 PHE   B CA   1 
ATOM   5899 C C    . PHE   B 1 116 ? 35.262 -16.373 -5.704  1.00 11.95 ?  116 PHE   B C    1 
ATOM   5900 O O    . PHE   B 1 116 ? 35.692 -15.946 -6.779  1.00 12.63 ?  116 PHE   B O    1 
ATOM   5901 C CB   . PHE   B 1 116 ? 36.132 -18.651 -5.316  1.00 11.88 ?  116 PHE   B CB   1 
ATOM   5902 C CG   . PHE   B 1 116 ? 37.201 -19.606 -4.758  1.00 11.90 ?  116 PHE   B CG   1 
ATOM   5903 C CD1  . PHE   B 1 116 ? 37.847 -19.419 -3.546  1.00 12.74 ?  116 PHE   B CD1  1 
ATOM   5904 C CD2  . PHE   B 1 116 ? 37.506 -20.749 -5.491  1.00 12.29 ?  116 PHE   B CD2  1 
ATOM   5905 C CE1  . PHE   B 1 116 ? 38.773 -20.361 -3.092  1.00 12.95 ?  116 PHE   B CE1  1 
ATOM   5906 C CE2  . PHE   B 1 116 ? 38.423 -21.680 -5.043  1.00 12.32 ?  116 PHE   B CE2  1 
ATOM   5907 C CZ   . PHE   B 1 116 ? 39.049 -21.494 -3.850  1.00 12.30 ?  116 PHE   B CZ   1 
ATOM   5908 H H    . PHE   B 1 116 ? 35.488 -17.857 -3.054  1.00 14.47 ?  116 PHE   B H    1 
ATOM   5909 H HA   . PHE   B 1 116 ? 37.067 -16.870 -4.880  1.00 14.77 ?  116 PHE   B HA   1 
ATOM   5910 H HB2  . PHE   B 1 116 ? 35.259 -19.030 -5.108  1.00 14.29 ?  116 PHE   B HB2  1 
ATOM   5911 H HB3  . PHE   B 1 116 ? 36.240 -18.629 -6.282  1.00 14.29 ?  116 PHE   B HB3  1 
ATOM   5912 H HD1  . PHE   B 1 116 ? 37.645 -18.671 -3.028  1.00 15.33 ?  116 PHE   B HD1  1 
ATOM   5913 H HD2  . PHE   B 1 116 ? 37.069 -20.898 -6.302  1.00 14.78 ?  116 PHE   B HD2  1 
ATOM   5914 H HE1  . PHE   B 1 116 ? 39.204 -20.226 -2.278  1.00 15.57 ?  116 PHE   B HE1  1 
ATOM   5915 H HE2  . PHE   B 1 116 ? 38.611 -22.432 -5.556  1.00 14.82 ?  116 PHE   B HE2  1 
ATOM   5916 H HZ   . PHE   B 1 116 ? 39.679 -22.105 -3.550  1.00 14.80 ?  116 PHE   B HZ   1 
ATOM   5917 N N    . ASN   B 1 117 ? 33.991 -16.176 -5.321  1.00 12.84 ?  117 ASN   B N    1 
ATOM   5918 C CA   . ASN   B 1 117 ? 33.041 -15.462 -6.180  1.00 12.94 ?  117 ASN   B CA   1 
ATOM   5919 C C    . ASN   B 1 117 ? 33.359 -13.984 -6.329  1.00 13.24 ?  117 ASN   B C    1 
ATOM   5920 O O    . ASN   B 1 117 ? 32.755 -13.325 -7.180  1.00 14.44 ?  117 ASN   B O    1 
ATOM   5921 C CB   . ASN   B 1 117 ? 31.619 -15.688 -5.685  1.00 12.86 ?  117 ASN   B CB   1 
ATOM   5922 C CG   . ASN   B 1 117 ? 31.173 -17.100 -5.938  1.00 13.44 ?  117 ASN   B CG   1 
ATOM   5923 O OD1  . ASN   B 1 117 ? 31.533 -17.686 -6.959  1.00 14.12 ?  117 ASN   B OD1  1 
ATOM   5924 N ND2  . ASN   B 1 117 ? 30.438 -17.678 -5.002  1.00 13.32 ?  117 ASN   B ND2  1 
ATOM   5925 H H    . ASN   B 1 117 ? 33.664 -16.438 -4.568  1.00 15.44 ?  117 ASN   B H    1 
ATOM   5926 H HA   . ASN   B 1 117 ? 33.096 -15.857 -7.060  1.00 15.56 ?  117 ASN   B HA   1 
ATOM   5927 H HB2  . ASN   B 1 117 ? 31.578 -15.521 -4.727  1.00 15.47 ?  117 ASN   B HB2  1 
ATOM   5928 H HB3  . ASN   B 1 117 ? 31.019 -15.081 -6.152  1.00 15.47 ?  117 ASN   B HB3  1 
ATOM   5929 H HD21 . ASN   B 1 117 ? 30.162 -18.488 -5.108  1.00 16.03 ?  117 ASN   B HD21 1 
ATOM   5930 H HD22 . ASN   B 1 117 ? 30.211 -17.239 -4.297  1.00 16.03 ?  117 ASN   B HD22 1 
ATOM   5931 N N    . GLN   B 1 118 ? 34.295 -13.464 -5.553  1.00 12.71 ?  118 GLN   B N    1 
ATOM   5932 C CA   . GLN   B 1 118 ? 34.729 -12.078 -5.693  1.00 13.58 ?  118 GLN   B CA   1 
ATOM   5933 C C    . GLN   B 1 118 ? 35.803 -11.888 -6.761  1.00 14.00 ?  118 GLN   B C    1 
ATOM   5934 O O    . GLN   B 1 118 ? 36.284 -10.763 -6.936  1.00 15.22 ?  118 GLN   B O    1 
ATOM   5935 C CB   . GLN   B 1 118 ? 35.203 -11.547 -4.336  1.00 14.00 ?  118 GLN   B CB   1 
ATOM   5936 C CG   . GLN   B 1 118 ? 34.118 -11.587 -3.268  1.00 14.36 ?  118 GLN   B CG   1 
ATOM   5937 C CD   . GLN   B 1 118 ? 32.950 -10.676 -3.600  1.00 14.34 ?  118 GLN   B CD   1 
ATOM   5938 O OE1  . GLN   B 1 118 ? 33.143 -9.533  -4.031  1.00 15.30 ?  118 GLN   B OE1  1 
ATOM   5939 N NE2  . GLN   B 1 118 ? 31.734 -11.172 -3.408  1.00 14.77 ?  118 GLN   B NE2  1 
ATOM   5940 H H    . GLN   B 1 118 ? 34.706 -13.891 -4.930  1.00 15.29 ?  118 GLN   B H    1 
ATOM   5941 H HA   . GLN   B 1 118 ? 33.966 -11.546 -5.962  1.00 16.33 ?  118 GLN   B HA   1 
ATOM   5942 H HB2  . GLN   B 1 118 ? 35.949 -12.079 -4.027  1.00 16.84 ?  118 GLN   B HB2  1 
ATOM   5943 H HB3  . GLN   B 1 118 ? 35.479 -10.618 -4.439  1.00 16.84 ?  118 GLN   B HB3  1 
ATOM   5944 H HG2  . GLN   B 1 118 ? 33.782 -12.497 -3.192  1.00 17.27 ?  118 GLN   B HG2  1 
ATOM   5945 H HG3  . GLN   B 1 118 ? 34.493 -11.303 -2.420  1.00 17.27 ?  118 GLN   B HG3  1 
ATOM   5946 H HE21 . GLN   B 1 118 ? 31.641 -11.973 -3.101  1.00 17.76 ?  118 GLN   B HE21 1 
ATOM   5947 H HE22 . GLN   B 1 118 ? 31.048 -10.694 -3.583  1.00 17.76 ?  118 GLN   B HE22 1 
ATOM   5948 N N    . HIS   B 1 119 ? 36.157 -12.946 -7.499  1.00 13.00 ?  119 HIS   B N    1 
ATOM   5949 C CA   . HIS   B 1 119 ? 37.205 -12.893 -8.513  1.00 13.34 ?  119 HIS   B CA   1 
ATOM   5950 C C    . HIS   B 1 119 ? 36.723 -13.617 -9.758  1.00 13.37 ?  119 HIS   B C    1 
ATOM   5951 O O    . HIS   B 1 119 ? 36.209 -14.730 -9.664  1.00 14.02 ?  119 HIS   B O    1 
ATOM   5952 C CB   . HIS   B 1 119 ? 38.475 -13.537 -7.964  1.00 13.75 ?  119 HIS   B CB   1 
ATOM   5953 C CG   . HIS   B 1 119 ? 38.951 -12.855 -6.729  1.00 14.83 ?  119 HIS   B CG   1 
ATOM   5954 N ND1  . HIS   B 1 119 ? 39.755 -11.737 -6.768  1.00 16.30 ?  119 HIS   B ND1  1 
ATOM   5955 C CD2  . HIS   B 1 119 ? 38.645 -13.057 -5.427  1.00 15.80 ?  119 HIS   B CD2  1 
ATOM   5956 C CE1  . HIS   B 1 119 ? 39.964 -11.310 -5.536  1.00 17.49 ?  119 HIS   B CE1  1 
ATOM   5957 N NE2  . HIS   B 1 119 ? 39.292 -12.085 -4.705  1.00 17.17 ?  119 HIS   B NE2  1 
ATOM   5958 H H    . HIS   B 1 119 ? 35.781 -13.723 -7.433  1.00 15.64 ?  119 HIS   B H    1 
ATOM   5959 H HA   . HIS   B 1 119 ? 37.386 -11.962 -8.739  1.00 16.04 ?  119 HIS   B HA   1 
ATOM   5960 H HB2  . HIS   B 1 119 ? 38.295 -14.463 -7.752  1.00 16.53 ?  119 HIS   B HB2  1 
ATOM   5961 H HB3  . HIS   B 1 119 ? 39.173 -13.474 -8.637  1.00 16.53 ?  119 HIS   B HB3  1 
ATOM   5962 H HD2  . HIS   B 1 119 ? 38.111 -13.733 -5.085  1.00 18.99 ?  119 HIS   B HD2  1 
ATOM   5963 H HE1  . HIS   B 1 119 ? 40.501 -10.588 -5.291  1.00 21.02 ?  119 HIS   B HE1  1 
ATOM   5964 H HE2  . HIS   B 1 119 ? 39.296 -12.018 -3.845  1.00 20.64 ?  119 HIS   B HE2  1 
ATOM   5965 N N    . GLU   B 1 120 ? 36.874 -12.990 -10.923 1.00 14.01 ?  120 GLU   B N    1 
ATOM   5966 C CA   . GLU   B 1 120 ? 36.287 -13.568 -12.127 1.00 15.79 ?  120 GLU   B CA   1 
ATOM   5967 C C    . GLU   B 1 120 ? 36.961 -14.873 -12.539 1.00 14.32 ?  120 GLU   B C    1 
ATOM   5968 O O    . GLU   B 1 120 ? 36.301 -15.745 -13.113 1.00 14.60 ?  120 GLU   B O    1 
ATOM   5969 C CB   . GLU   B 1 120 ? 36.318 -12.556 -13.271 1.00 20.56 ?  120 GLU   B CB   1 
ATOM   5970 C CG   . GLU   B 1 120 ? 35.404 -11.361 -13.048 1.00 26.99 ?  120 GLU   B CG   1 
ATOM   5971 C CD   . GLU   B 1 120 ? 35.288 -10.470 -14.268 1.00 33.17 ?  120 GLU   B CD   1 
ATOM   5972 O OE1  . GLU   B 1 120 ? 36.271 -10.376 -15.036 1.00 35.56 ?  120 GLU   B OE1  1 
ATOM   5973 O OE2  . GLU   B 1 120 ? 34.214 -9.861  -14.457 1.00 36.18 -1 120 GLU   B OE2  1 
ATOM   5974 H H    . GLU   B 1 120 ? 37.299 -12.243 -11.042 1.00 16.85 ?  120 GLU   B H    1 
ATOM   5975 H HA   . GLU   B 1 120 ? 35.359 -13.767 -11.942 1.00 18.99 ?  120 GLU   B HA   1 
ATOM   5976 H HB2  . GLU   B 1 120 ? 37.219 -12.222 -13.377 1.00 24.71 ?  120 GLU   B HB2  1 
ATOM   5977 H HB3  . GLU   B 1 120 ? 36.030 -12.999 -14.087 1.00 24.71 ?  120 GLU   B HB3  1 
ATOM   5978 H HG2  . GLU   B 1 120 ? 34.513 -11.679 -12.820 1.00 32.43 ?  120 GLU   B HG2  1 
ATOM   5979 H HG3  . GLU   B 1 120 ? 35.756 -10.821 -12.326 1.00 32.43 ?  120 GLU   B HG3  1 
ATOM   5980 N N    . VAL   B 1 121 ? 38.258 -15.023 -12.273 1.00 13.87 ?  121 VAL   B N    1 
ATOM   5981 C CA   . VAL   B 1 121 ? 39.003 -16.231 -12.629 1.00 13.44 ?  121 VAL   B CA   1 
ATOM   5982 C C    . VAL   B 1 121 ? 40.119 -16.441 -11.615 1.00 13.14 ?  121 VAL   B C    1 
ATOM   5983 O O    . VAL   B 1 121 ? 40.801 -15.487 -11.226 1.00 13.74 ?  121 VAL   B O    1 
ATOM   5984 C CB   . VAL   B 1 121 ? 39.517 -16.175 -14.086 1.00 15.45 ?  121 VAL   B CB   1 
ATOM   5985 C CG1  . VAL   B 1 121 ? 40.376 -14.934 -14.334 1.00 16.76 ?  121 VAL   B CG1  1 
ATOM   5986 C CG2  . VAL   B 1 121 ? 40.269 -17.450 -14.445 1.00 17.08 ?  121 VAL   B CG2  1 
ATOM   5987 H H    . VAL   B 1 121 ? 38.745 -14.424 -11.887 1.00 16.68 ?  121 VAL   B H    1 
ATOM   5988 H HA   . VAL   B 1 121 ? 38.392 -16.984 -12.566 1.00 16.17 ?  121 VAL   B HA   1 
ATOM   5989 H HB   . VAL   B 1 121 ? 38.748 -16.119 -14.680 1.00 18.57 ?  121 VAL   B HB   1 
ATOM   5990 H HG11 . VAL   B 1 121 ? 40.688 -14.944 -15.252 1.00 20.16 ?  121 VAL   B HG11 1 
ATOM   5991 H HG12 . VAL   B 1 121 ? 39.838 -14.140 -14.177 1.00 20.16 ?  121 VAL   B HG12 1 
ATOM   5992 H HG13 . VAL   B 1 121 ? 41.131 -14.947 -13.727 1.00 20.16 ?  121 VAL   B HG13 1 
ATOM   5993 H HG21 . VAL   B 1 121 ? 40.467 -17.445 -15.396 1.00 20.53 ?  121 VAL   B HG21 1 
ATOM   5994 H HG22 . VAL   B 1 121 ? 41.097 -17.484 -13.939 1.00 20.53 ?  121 VAL   B HG22 1 
ATOM   5995 H HG23 . VAL   B 1 121 ? 39.718 -18.218 -14.228 1.00 20.53 ?  121 VAL   B HG23 1 
ATOM   5996 N N    . LEU   B 1 122 ? 40.298 -17.695 -11.183 1.00 12.47 ?  122 LEU   B N    1 
ATOM   5997 C CA   . LEU   B 1 122 ? 41.277 -18.048 -10.160 1.00 12.36 ?  122 LEU   B CA   1 
ATOM   5998 C C    . LEU   B 1 122 ? 41.924 -19.384 -10.480 1.00 12.40 ?  122 LEU   B C    1 
ATOM   5999 O O    . LEU   B 1 122 ? 41.258 -20.304 -10.976 1.00 13.26 ?  122 LEU   B O    1 
ATOM   6000 C CB   . LEU   B 1 122 ? 40.622 -18.280 -8.784  1.00 14.22 ?  122 LEU   B CB   1 
ATOM   6001 C CG   . LEU   B 1 122 ? 39.582 -17.269 -8.291  1.00 14.27 ?  122 LEU   B CG   1 
ATOM   6002 C CD1  . LEU   B 1 122 ? 38.186 -17.634 -8.775  1.00 14.90 ?  122 LEU   B CD1  1 
ATOM   6003 C CD2  . LEU   B 1 122 ? 39.621 -17.169 -6.777  1.00 13.74 ?  122 LEU   B CD2  1 
ATOM   6004 H H    . LEU   B 1 122 ? 39.853 -18.373 -11.472 1.00 15.00 ?  122 LEU   B H    1 
ATOM   6005 H HA   . LEU   B 1 122 ? 41.957 -17.359 -10.080 1.00 14.87 ?  122 LEU   B HA   1 
ATOM   6006 H HB2  . LEU   B 1 122 ? 40.183 -19.140 -8.805  1.00 17.10 ?  122 LEU   B HB2  1 
ATOM   6007 H HB3  . LEU   B 1 122 ? 41.326 -18.297 -8.117  1.00 17.10 ?  122 LEU   B HB3  1 
ATOM   6008 H HG   . LEU   B 1 122 ? 39.800 -16.392 -8.649  1.00 17.17 ?  122 LEU   B HG   1 
ATOM   6009 H HD11 . LEU   B 1 122 ? 37.550 -16.996 -8.412  1.00 17.92 ?  122 LEU   B HD11 1 
ATOM   6010 H HD12 . LEU   B 1 122 ? 38.170 -17.593 -9.747  1.00 17.92 ?  122 LEU   B HD12 1 
ATOM   6011 H HD13 . LEU   B 1 122 ? 37.971 -18.526 -8.476  1.00 17.92 ?  122 LEU   B HD13 1 
ATOM   6012 H HD21 . LEU   B 1 122 ? 38.934 -16.549 -6.479  1.00 16.53 ?  122 LEU   B HD21 1 
ATOM   6013 H HD22 . LEU   B 1 122 ? 39.459 -18.047 -6.397  1.00 16.53 ?  122 LEU   B HD22 1 
ATOM   6014 H HD23 . LEU   B 1 122 ? 40.495 -16.847 -6.502  1.00 16.53 ?  122 LEU   B HD23 1 
ATOM   6015 N N    . LEU   B 1 123 ? 43.210 -19.499 -10.122 1.00 11.81 ?  123 LEU   B N    1 
ATOM   6016 C CA   . LEU   B 1 123 ? 43.920 -20.772 -10.001 1.00 11.91 ?  123 LEU   B CA   1 
ATOM   6017 C C    . LEU   B 1 123 ? 43.890 -21.168 -8.528  1.00 11.67 ?  123 LEU   B C    1 
ATOM   6018 O O    . LEU   B 1 123 ? 44.249 -20.347 -7.675  1.00 12.13 ?  123 LEU   B O    1 
ATOM   6019 C CB   . LEU   B 1 123 ? 45.369 -20.594 -10.463 1.00 12.65 ?  123 LEU   B CB   1 
ATOM   6020 C CG   . LEU   B 1 123 ? 46.305 -21.781 -10.216 1.00 12.84 ?  123 LEU   B CG   1 
ATOM   6021 C CD1  . LEU   B 1 123 ? 45.875 -23.036 -10.985 1.00 13.74 ?  123 LEU   B CD1  1 
ATOM   6022 C CD2  . LEU   B 1 123 ? 47.723 -21.385 -10.592 1.00 13.56 ?  123 LEU   B CD2  1 
ATOM   6023 H H    . LEU   B 1 123 ? 43.707 -18.821 -9.926  1.00 14.21 ?  123 LEU   B H    1 
ATOM   6024 H HA   . LEU   B 1 123 ? 43.480 -21.455 -10.535 1.00 14.34 ?  123 LEU   B HA   1 
ATOM   6025 H HB2  . LEU   B 1 123 ? 45.362 -20.424 -11.418 1.00 15.21 ?  123 LEU   B HB2  1 
ATOM   6026 H HB3  . LEU   B 1 123 ? 45.741 -19.830 -10.000 1.00 15.21 ?  123 LEU   B HB3  1 
ATOM   6027 H HG   . LEU   B 1 123 ? 46.297 -21.998 -9.271  1.00 15.45 ?  123 LEU   B HG   1 
ATOM   6028 H HD11 . LEU   B 1 123 ? 46.507 -23.747 -10.801 1.00 16.53 ?  123 LEU   B HD11 1 
ATOM   6029 H HD12 . LEU   B 1 123 ? 44.987 -23.298 -10.690 1.00 16.53 ?  123 LEU   B HD12 1 
ATOM   6030 H HD13 . LEU   B 1 123 ? 45.863 -22.835 -11.932 1.00 16.53 ?  123 LEU   B HD13 1 
ATOM   6031 H HD21 . LEU   B 1 123 ? 48.312 -22.137 -10.438 1.00 16.31 ?  123 LEU   B HD21 1 
ATOM   6032 H HD22 . LEU   B 1 123 ? 47.741 -21.134 -11.530 1.00 16.31 ?  123 LEU   B HD22 1 
ATOM   6033 H HD23 . LEU   B 1 123 ? 47.993 -20.631 -10.045 1.00 16.31 ?  123 LEU   B HD23 1 
ATOM   6034 N N    . ALA   B 1 124 ? 43.454 -22.397 -8.217  1.00 11.41 ?  124 ALA   B N    1 
ATOM   6035 C CA   . ALA   B 1 124 ? 43.197 -22.711 -6.817  1.00 11.72 ?  124 ALA   B CA   1 
ATOM   6036 C C    . ALA   B 1 124 ? 43.474 -24.172 -6.495  1.00 11.18 ?  124 ALA   B C    1 
ATOM   6037 O O    . ALA   B 1 124 ? 43.333 -25.049 -7.360  1.00 12.02 ?  124 ALA   B O    1 
ATOM   6038 C CB   . ALA   B 1 124 ? 41.745 -22.404 -6.442  1.00 12.38 ?  124 ALA   B CB   1 
ATOM   6039 H H    . ALA   B 1 124 ? 43.280 -23.034 -8.783  1.00 13.73 ?  124 ALA   B H    1 
ATOM   6040 H HA   . ALA   B 1 124 ? 43.778 -22.162 -6.278  1.00 14.10 ?  124 ALA   B HA   1 
ATOM   6041 H HB1  . ALA   B 1 124 ? 41.604 -22.620 -5.508  1.00 14.90 ?  124 ALA   B HB1  1 
ATOM   6042 H HB2  . ALA   B 1 124 ? 41.577 -21.457 -6.590  1.00 14.90 ?  124 ALA   B HB2  1 
ATOM   6043 H HB3  . ALA   B 1 124 ? 41.151 -22.932 -6.999  1.00 14.90 ?  124 ALA   B HB3  1 
ATOM   6044 N N    . PRO   B 1 125 ? 43.778 -24.469 -5.233  1.00 11.62 ?  125 PRO   B N    1 
ATOM   6045 C CA   . PRO   B 1 125 ? 43.704 -25.833 -4.707  1.00 12.40 ?  125 PRO   B CA   1 
ATOM   6046 C C    . PRO   B 1 125 ? 42.303 -26.104 -4.156  1.00 12.84 ?  125 PRO   B C    1 
ATOM   6047 O O    . PRO   B 1 125 ? 41.507 -25.187 -3.955  1.00 13.22 ?  125 PRO   B O    1 
ATOM   6048 C CB   . PRO   B 1 125 ? 44.694 -25.761 -3.538  1.00 13.27 ?  125 PRO   B CB   1 
ATOM   6049 C CG   . PRO   B 1 125 ? 44.451 -24.377 -2.968  1.00 13.18 ?  125 PRO   B CG   1 
ATOM   6050 C CD   . PRO   B 1 125 ? 44.103 -23.500 -4.168  1.00 12.35 ?  125 PRO   B CD   1 
ATOM   6051 H HA   . PRO   B 1 125 ? 43.980 -26.504 -5.355  1.00 14.92 ?  125 PRO   B HA   1 
ATOM   6052 H HB2  . PRO   B 1 125 ? 44.487 -26.445 -2.880  1.00 15.96 ?  125 PRO   B HB2  1 
ATOM   6053 H HB3  . PRO   B 1 125 ? 45.605 -25.850 -3.858  1.00 15.96 ?  125 PRO   B HB3  1 
ATOM   6054 H HG2  . PRO   B 1 125 ? 43.709 -24.399 -2.342  1.00 15.85 ?  125 PRO   B HG2  1 
ATOM   6055 H HG3  . PRO   B 1 125 ? 45.256 -24.051 -2.529  1.00 15.85 ?  125 PRO   B HG3  1 
ATOM   6056 H HD2  . PRO   B 1 125 ? 43.337 -22.942 -3.975  1.00 14.86 ?  125 PRO   B HD2  1 
ATOM   6057 H HD3  . PRO   B 1 125 ? 44.876 -22.961 -4.425  1.00 14.86 ?  125 PRO   B HD3  1 
ATOM   6058 N N    . LEU   B 1 126 ? 42.037 -27.380 -3.855  1.00 13.27 ?  126 LEU   B N    1 
ATOM   6059 C CA   . LEU   B 1 126 ? 40.816 -27.742 -3.140  1.00 13.66 ?  126 LEU   B CA   1 
ATOM   6060 C C    . LEU   B 1 126 ? 40.938 -27.350 -1.675  1.00 13.99 ?  126 LEU   B C    1 
ATOM   6061 O O    . LEU   B 1 126 ? 41.833 -27.815 -0.966  1.00 16.07 ?  126 LEU   B O    1 
ATOM   6062 C CB   . LEU   B 1 126 ? 40.562 -29.237 -3.255  1.00 14.85 ?  126 LEU   B CB   1 
ATOM   6063 C CG   . LEU   B 1 126 ? 40.028 -29.731 -4.600  1.00 16.15 ?  126 LEU   B CG   1 
ATOM   6064 C CD1  . LEU   B 1 126 ? 40.052 -31.239 -4.661  1.00 18.17 ?  126 LEU   B CD1  1 
ATOM   6065 C CD2  . LEU   B 1 126 ? 38.618 -29.225 -4.862  1.00 16.50 ?  126 LEU   B CD2  1 
ATOM   6066 H H    . LEU   B 1 126 ? 42.553 -28.045 -4.039  1.00 15.96 ?  126 LEU   B H    1 
ATOM   6067 H HA   . LEU   B 1 126 ? 40.068 -27.262 -3.524  1.00 16.43 ?  126 LEU   B HA   1 
ATOM   6068 H HB2  . LEU   B 1 126 ? 41.397 -29.697 -3.086  1.00 17.86 ?  126 LEU   B HB2  1 
ATOM   6069 H HB3  . LEU   B 1 126 ? 39.914 -29.483 -2.578  1.00 17.86 ?  126 LEU   B HB3  1 
ATOM   6070 H HG   . LEU   B 1 126 ? 40.604 -29.390 -5.306  1.00 19.42 ?  126 LEU   B HG   1 
ATOM   6071 H HD11 . LEU   B 1 126 ? 39.712 -31.523 -5.523  1.00 21.85 ?  126 LEU   B HD11 1 
ATOM   6072 H HD12 . LEU   B 1 126 ? 40.963 -31.546 -4.544  1.00 21.85 ?  126 LEU   B HD12 1 
ATOM   6073 H HD13 . LEU   B 1 126 ? 39.490 -31.590 -3.951  1.00 21.85 ?  126 LEU   B HD13 1 
ATOM   6074 H HD21 . LEU   B 1 126 ? 38.282 -29.636 -5.673  1.00 19.84 ?  126 LEU   B HD21 1 
ATOM   6075 H HD22 . LEU   B 1 126 ? 38.053 -29.460 -4.111  1.00 19.84 ?  126 LEU   B HD22 1 
ATOM   6076 H HD23 . LEU   B 1 126 ? 38.639 -28.258 -4.968  1.00 19.84 ?  126 LEU   B HD23 1 
ATOM   6077 N N    . LEU   B 1 127 ? 40.012 -26.524 -1.209  1.00 13.71 ?  127 LEU   B N    1 
ATOM   6078 C CA   . LEU   B 1 127 ? 40.071 -26.027 0.154   1.00 14.34 ?  127 LEU   B CA   1 
ATOM   6079 C C    . LEU   B 1 127 ? 39.785 -27.144 1.153   1.00 14.09 ?  127 LEU   B C    1 
ATOM   6080 O O    . LEU   B 1 127 ? 38.960 -28.035 0.923   1.00 14.39 ?  127 LEU   B O    1 
ATOM   6081 C CB   . LEU   B 1 127 ? 39.060 -24.896 0.357   1.00 14.98 ?  127 LEU   B CB   1 
ATOM   6082 C CG   . LEU   B 1 127 ? 39.241 -23.632 -0.486  1.00 15.30 ?  127 LEU   B CG   1 
ATOM   6083 C CD1  . LEU   B 1 127 ? 38.115 -22.658 -0.166  1.00 15.56 ?  127 LEU   B CD1  1 
ATOM   6084 C CD2  . LEU   B 1 127 ? 40.608 -23.004 -0.260  1.00 16.05 ?  127 LEU   B CD2  1 
ATOM   6085 H H    . LEU   B 1 127 ? 39.339 -26.228 -1.666  1.00 16.49 ?  127 LEU   B H    1 
ATOM   6086 H HA   . LEU   B 1 127 ? 40.960 -25.671 0.327   1.00 17.24 ?  127 LEU   B HA   1 
ATOM   6087 H HB2  . LEU   B 1 127 ? 38.175 -25.251 0.159   1.00 18.02 ?  127 LEU   B HB2  1 
ATOM   6088 H HB3  . LEU   B 1 127 ? 39.091 -24.629 1.288   1.00 18.02 ?  127 LEU   B HB3  1 
ATOM   6089 H HG   . LEU   B 1 127 ? 39.163 -23.867 -1.421  1.00 18.39 ?  127 LEU   B HG   1 
ATOM   6090 H HD11 . LEU   B 1 127 ? 38.238 -21.850 -0.696  1.00 18.71 ?  127 LEU   B HD11 1 
ATOM   6091 H HD12 . LEU   B 1 127 ? 37.263 -23.064 -0.381  1.00 18.71 ?  127 LEU   B HD12 1 
ATOM   6092 H HD13 . LEU   B 1 127 ? 38.146 -22.433 0.779   1.00 18.71 ?  127 LEU   B HD13 1 
ATOM   6093 H HD21 . LEU   B 1 127 ? 40.645 -22.155 -0.722  1.00 19.30 ?  127 LEU   B HD21 1 
ATOM   6094 H HD22 . LEU   B 1 127 ? 40.741 -22.871 0.693   1.00 19.30 ?  127 LEU   B HD22 1 
ATOM   6095 H HD23 . LEU   B 1 127 ? 41.287 -23.603 -0.606  1.00 19.30 ?  127 LEU   B HD23 1 
ATOM   6096 N N    . SER   B 1 128 ? 40.460 -27.057 2.290   1.00 14.22 ?  128 SER   B N    1 
ATOM   6097 C CA   . SER   B 1 128 ? 40.335 -27.965 3.422   1.00 14.75 ?  128 SER   B CA   1 
ATOM   6098 C C    . SER   B 1 128 ? 40.822 -29.377 3.114   1.00 16.01 ?  128 SER   B C    1 
ATOM   6099 O O    . SER   B 1 128 ? 40.716 -30.249 3.977   1.00 17.51 ?  128 SER   B O    1 
ATOM   6100 C CB   . SER   B 1 128 ? 38.931 -27.958 4.046   1.00 14.84 ?  128 SER   B CB   1 
ATOM   6101 O OG   . SER   B 1 128 ? 38.636 -26.674 4.590   1.00 15.30 ?  128 SER   B OG   1 
ATOM   6102 H H    . SER   B 1 128 ? 41.035 -26.433 2.436   1.00 17.11 ?  128 SER   B H    1 
ATOM   6103 H HA   . SER   B 1 128 ? 40.927 -27.628 4.105   1.00 17.74 ?  128 SER   B HA   1 
ATOM   6104 H HB2  . SER   B 1 128 ? 38.275 -28.183 3.368   1.00 17.84 ?  128 SER   B HB2  1 
ATOM   6105 H HB3  . SER   B 1 128 ? 38.903 -28.627 4.760   1.00 17.84 ?  128 SER   B HB3  1 
ATOM   6106 H HG   . SER   B 1 128 ? 39.204 -26.483 5.182   1.00 18.40 ?  128 SER   B HG   1 
ATOM   6107 N N    . ALA   B 1 129 ? 41.396 -29.617 1.930   1.00 17.09 ?  129 ALA   B N    1 
ATOM   6108 C CA   . ALA   B 1 129 ? 41.938 -30.920 1.579   1.00 18.46 ?  129 ALA   B CA   1 
ATOM   6109 C C    . ALA   B 1 129 ? 43.342 -31.085 2.150   1.00 17.11 ?  129 ALA   B C    1 
ATOM   6110 O O    . ALA   B 1 129 ? 43.897 -30.182 2.792   1.00 17.04 ?  129 ALA   B O    1 
ATOM   6111 C CB   . ALA   B 1 129 ? 41.968 -31.095 0.062   1.00 20.40 ?  129 ALA   B CB   1 
ATOM   6112 H H    . ALA   B 1 129 ? 41.483 -29.032 1.301   1.00 20.54 ?  129 ALA   B H    1 
ATOM   6113 H HA   . ALA   B 1 129 ? 41.374 -31.613 1.950   1.00 22.19 ?  129 ALA   B HA   1 
ATOM   6114 H HB1  . ALA   B 1 129 ? 42.318 -31.977 -0.151  1.00 24.52 ?  129 ALA   B HB1  1 
ATOM   6115 H HB2  . ALA   B 1 129 ? 41.068 -31.006 -0.284  1.00 24.52 ?  129 ALA   B HB2  1 
ATOM   6116 H HB3  . ALA   B 1 129 ? 42.541 -30.413 -0.325  1.00 24.52 ?  129 ALA   B HB3  1 
ATOM   6117 N N    . GLY   B 1 130 ? 43.924 -32.254 1.891   1.00 17.01 ?  130 GLY   B N    1 
ATOM   6118 C CA   . GLY   B 1 130 ? 45.312 -32.481 2.245   1.00 17.55 ?  130 GLY   B CA   1 
ATOM   6119 C C    . GLY   B 1 130 ? 45.524 -32.394 3.737   1.00 17.47 ?  130 GLY   B C    1 
ATOM   6120 O O    . GLY   B 1 130 ? 44.823 -33.038 4.530   1.00 18.19 ?  130 GLY   B O    1 
ATOM   6121 H H    . GLY   B 1 130 ? 43.546 -32.922 1.500   1.00 20.45 ?  130 GLY   B H    1 
ATOM   6122 H HA2  . GLY   B 1 130 ? 45.590 -33.363 1.944   1.00 21.09 ?  130 GLY   B HA2  1 
ATOM   6123 H HA3  . GLY   B 1 130 ? 45.876 -31.819 1.811   1.00 21.09 ?  130 GLY   B HA3  1 
ATOM   6124 N N    . ILE   B 1 131 ? 46.511 -31.579 4.129   1.00 17.85 ?  131 ILE   B N    1 
ATOM   6125 C CA   . ILE   B 1 131 ? 46.881 -31.458 5.531   1.00 18.81 ?  131 ILE   B CA   1 
ATOM   6126 C C    . ILE   B 1 131 ? 45.773 -30.856 6.373   1.00 17.90 ?  131 ILE   B C    1 
ATOM   6127 O O    . ILE   B 1 131 ? 45.855 -30.916 7.603   1.00 19.57 ?  131 ILE   B O    1 
ATOM   6128 C CB   . ILE   B 1 131 ? 48.206 -30.680 5.717   1.00 20.58 ?  131 ILE   B CB   1 
ATOM   6129 C CG1  . ILE   B 1 131 ? 48.033 -29.191 5.377   1.00 21.40 ?  131 ILE   B CG1  1 
ATOM   6130 C CG2  . ILE   B 1 131 ? 49.318 -31.310 4.874   1.00 21.92 ?  131 ILE   B CG2  1 
ATOM   6131 C CD1  . ILE   B 1 131 ? 49.243 -28.338 5.701   1.00 22.75 ?  131 ILE   B CD1  1 
ATOM   6132 H H    . ILE   B 1 131 ? 46.971 -31.079 3.606   1.00 21.45 ?  131 ILE   B H    1 
ATOM   6133 H HA   . ILE   B 1 131 ? 47.030 -32.349 5.874   1.00 22.61 ?  131 ILE   B HA   1 
ATOM   6134 H HB   . ILE   B 1 131 ? 48.465 -30.746 6.647   1.00 24.74 ?  131 ILE   B HB   1 
ATOM   6135 H HG12 . ILE   B 1 131 ? 47.853 -29.109 4.428   1.00 25.72 ?  131 ILE   B HG12 1 
ATOM   6136 H HG13 . ILE   B 1 131 ? 47.283 -28.835 5.882   1.00 25.72 ?  131 ILE   B HG13 1 
ATOM   6137 H HG21 . ILE   B 1 131 ? 50.162 -30.901 5.112   1.00 26.34 ?  131 ILE   B HG21 1 
ATOM   6138 H HG22 . ILE   B 1 131 ? 49.343 -32.260 5.051   1.00 26.34 ?  131 ILE   B HG22 1 
ATOM   6139 H HG23 . ILE   B 1 131 ? 49.124 -31.151 3.935   1.00 26.34 ?  131 ILE   B HG23 1 
ATOM   6140 H HD11 . ILE   B 1 131 ? 49.019 -27.407 5.543   1.00 27.34 ?  131 ILE   B HD11 1 
ATOM   6141 H HD12 . ILE   B 1 131 ? 49.477 -28.468 6.633   1.00 27.34 ?  131 ILE   B HD12 1 
ATOM   6142 H HD13 . ILE   B 1 131 ? 49.978 -28.605 5.132   1.00 27.34 ?  131 ILE   B HD13 1 
ATOM   6143 N N    . PHE   B 1 132 ? 44.741 -30.279 5.748   1.00 16.83 ?  132 PHE   B N    1 
ATOM   6144 C CA   . PHE   B 1 132 ? 43.592 -29.767 6.486   1.00 17.27 ?  132 PHE   B CA   1 
ATOM   6145 C C    . PHE   B 1 132 ? 42.570 -30.851 6.825   1.00 18.90 ?  132 PHE   B C    1 
ATOM   6146 O O    . PHE   B 1 132 ? 41.676 -30.594 7.639   1.00 20.67 ?  132 PHE   B O    1 
ATOM   6147 C CB   . PHE   B 1 132 ? 42.900 -28.646 5.701   1.00 16.24 ?  132 PHE   B CB   1 
ATOM   6148 C CG   . PHE   B 1 132 ? 43.592 -27.300 5.791   1.00 16.12 ?  132 PHE   B CG   1 
ATOM   6149 C CD1  . PHE   B 1 132 ? 44.883 -27.122 5.321   1.00 17.56 ?  132 PHE   B CD1  1 
ATOM   6150 C CD2  . PHE   B 1 132 ? 42.913 -26.200 6.301   1.00 15.96 ?  132 PHE   B CD2  1 
ATOM   6151 C CE1  . PHE   B 1 132 ? 45.497 -25.879 5.395   1.00 17.73 ?  132 PHE   B CE1  1 
ATOM   6152 C CE2  . PHE   B 1 132 ? 43.518 -24.952 6.367   1.00 16.36 ?  132 PHE   B CE2  1 
ATOM   6153 C CZ   . PHE   B 1 132 ? 44.808 -24.798 5.917   1.00 17.31 ?  132 PHE   B CZ   1 
ATOM   6154 H H    . PHE   B 1 132 ? 44.680 -30.179 4.895   1.00 20.23 ?  132 PHE   B H    1 
ATOM   6155 H HA   . PHE   B 1 132 ? 43.908 -29.389 7.321   1.00 20.76 ?  132 PHE   B HA   1 
ATOM   6156 H HB2  . PHE   B 1 132 ? 42.874 -28.901 4.768   1.00 19.53 ?  132 PHE   B HB2  1 
ATOM   6157 H HB3  . PHE   B 1 132 ? 41.997 -28.544 6.041   1.00 19.53 ?  132 PHE   B HB3  1 
ATOM   6158 H HD1  . PHE   B 1 132 ? 45.350 -27.850 4.975   1.00 21.11 ?  132 PHE   B HD1  1 
ATOM   6159 H HD2  . PHE   B 1 132 ? 42.040 -26.305 6.611   1.00 19.19 ?  132 PHE   B HD2  1 
ATOM   6160 H HE1  . PHE   B 1 132 ? 46.368 -25.773 5.089   1.00 21.31 ?  132 PHE   B HE1  1 
ATOM   6161 H HE2  . PHE   B 1 132 ? 43.055 -24.228 6.725   1.00 19.67 ?  132 PHE   B HE2  1 
ATOM   6162 H HZ   . PHE   B 1 132 ? 45.220 -23.963 5.966   1.00 20.81 ?  132 PHE   B HZ   1 
ATOM   6163 N N    . GLY   B 1 133 ? 42.654 -32.041 6.214   1.00 18.26 ?  133 GLY   B N    1 
ATOM   6164 C CA   . GLY   B 1 133 ? 41.950 -33.211 6.714   1.00 19.43 ?  133 GLY   B CA   1 
ATOM   6165 C C    . GLY   B 1 133 ? 40.550 -33.478 6.189   1.00 20.02 ?  133 GLY   B C    1 
ATOM   6166 O O    . GLY   B 1 133 ? 39.973 -34.505 6.556   1.00 21.91 ?  133 GLY   B O    1 
ATOM   6167 H H    . GLY   B 1 133 ? 43.116 -32.184 5.499   1.00 21.95 ?  133 GLY   B H    1 
ATOM   6168 H HA2  . GLY   B 1 133 ? 42.491 -33.992 6.522   1.00 23.35 ?  133 GLY   B HA2  1 
ATOM   6169 H HA3  . GLY   B 1 133 ? 41.882 -33.130 7.676   1.00 23.35 ?  133 GLY   B HA3  1 
ATOM   6170 N N    . ALA   B 1 134 ? 39.975 -32.608 5.366   1.00 18.99 ?  134 ALA   B N    1 
ATOM   6171 C CA   . ALA   B 1 134 ? 38.654 -32.894 4.824   1.00 19.20 ?  134 ALA   B CA   1 
ATOM   6172 C C    . ALA   B 1 134 ? 38.756 -33.868 3.655   1.00 18.91 ?  134 ALA   B C    1 
ATOM   6173 O O    . ALA   B 1 134 ? 39.815 -34.040 3.045   1.00 19.88 ?  134 ALA   B O    1 
ATOM   6174 C CB   . ALA   B 1 134 ? 37.969 -31.609 4.364   1.00 19.46 ?  134 ALA   B CB   1 
ATOM   6175 H H    . ALA   B 1 134 ? 40.312 -31.853 5.128   1.00 22.83 ?  134 ALA   B H    1 
ATOM   6176 H HA   . ALA   B 1 134 ? 38.105 -33.300 5.513   1.00 23.07 ?  134 ALA   B HA   1 
ATOM   6177 H HB1  . ALA   B 1 134 ? 37.081 -31.826 4.036   1.00 23.39 ?  134 ALA   B HB1  1 
ATOM   6178 H HB2  . ALA   B 1 134 ? 37.903 -30.999 5.116   1.00 23.39 ?  134 ALA   B HB2  1 
ATOM   6179 H HB3  . ALA   B 1 134 ? 38.494 -31.206 3.656   1.00 23.39 ?  134 ALA   B HB3  1 
ATOM   6180 N N    . ASP   B 1 135 ? 37.630 -34.498 3.345   1.00 19.59 ?  135 ASP   B N    1 
ATOM   6181 C CA   . ASP   B 1 135 ? 37.550 -35.389 2.197   1.00 20.39 ?  135 ASP   B CA   1 
ATOM   6182 C C    . ASP   B 1 135 ? 37.631 -34.550 0.927   1.00 18.85 ?  135 ASP   B C    1 
ATOM   6183 O O    . ASP   B 1 135 ? 36.772 -33.679 0.714   1.00 18.99 ?  135 ASP   B O    1 
ATOM   6184 C CB   . ASP   B 1 135 ? 36.223 -36.140 2.252   1.00 22.03 ?  135 ASP   B CB   1 
ATOM   6185 C CG   . ASP   B 1 135 ? 36.062 -37.145 1.125   1.00 23.92 ?  135 ASP   B CG   1 
ATOM   6186 O OD1  . ASP   B 1 135 ? 36.920 -37.183 0.218   1.00 24.10 ?  135 ASP   B OD1  1 
ATOM   6187 O OD2  . ASP   B 1 135 ? 35.077 -37.921 1.158   1.00 27.11 -1 135 ASP   B OD2  1 
ATOM   6188 H H    . ASP   B 1 135 ? 36.897 -34.423 3.785   1.00 23.55 ?  135 ASP   B H    1 
ATOM   6189 H HA   . ASP   B 1 135 ? 38.281 -36.029 2.228   1.00 24.51 ?  135 ASP   B HA   1 
ATOM   6190 H HB2  . ASP   B 1 135 ? 36.173 -36.616 3.094   1.00 26.47 ?  135 ASP   B HB2  1 
ATOM   6191 H HB3  . ASP   B 1 135 ? 35.503 -35.497 2.186   1.00 26.47 ?  135 ASP   B HB3  1 
ATOM   6192 N N    . PRO   B 1 136 ? 38.633 -34.754 0.069   1.00 18.71 ?  136 PRO   B N    1 
ATOM   6193 C CA   . PRO   B 1 136 ? 38.717 -33.926 -1.146  1.00 18.16 ?  136 PRO   B CA   1 
ATOM   6194 C C    . PRO   B 1 136 ? 37.521 -34.086 -2.064  1.00 17.29 ?  136 PRO   B C    1 
ATOM   6195 O O    . PRO   B 1 136 ? 37.180 -33.144 -2.788  1.00 16.62 ?  136 PRO   B O    1 
ATOM   6196 C CB   . PRO   B 1 136 ? 40.025 -34.395 -1.801  1.00 18.73 ?  136 PRO   B CB   1 
ATOM   6197 C CG   . PRO   B 1 136 ? 40.221 -35.795 -1.270  1.00 20.05 ?  136 PRO   B CG   1 
ATOM   6198 C CD   . PRO   B 1 136 ? 39.726 -35.738 0.142   1.00 19.86 ?  136 PRO   B CD   1 
ATOM   6199 H HA   . PRO   B 1 136 ? 38.806 -32.992 -0.913  1.00 21.83 ?  136 PRO   B HA   1 
ATOM   6200 H HB2  . PRO   B 1 136 ? 39.933 -34.405 -2.768  1.00 22.52 ?  136 PRO   B HB2  1 
ATOM   6201 H HB3  . PRO   B 1 136 ? 40.757 -33.820 -1.530  1.00 22.52 ?  136 PRO   B HB3  1 
ATOM   6202 H HG2  . PRO   B 1 136 ? 39.693 -36.427 -1.789  1.00 24.10 ?  136 PRO   B HG2  1 
ATOM   6203 H HG3  . PRO   B 1 136 ? 41.161 -36.036 -1.294  1.00 24.10 ?  136 PRO   B HG3  1 
ATOM   6204 H HD2  . PRO   B 1 136 ? 39.385 -36.602 0.421   1.00 23.87 ?  136 PRO   B HD2  1 
ATOM   6205 H HD3  . PRO   B 1 136 ? 40.426 -35.421 0.738   1.00 23.87 ?  136 PRO   B HD3  1 
ATOM   6206 N N    . ILE   B 1 137 ? 36.868 -35.252 -2.060  1.00 17.84 ?  137 ILE   B N    1 
ATOM   6207 C CA   . ILE   B 1 137 ? 35.647 -35.428 -2.842  1.00 18.22 ?  137 ILE   B CA   1 
ATOM   6208 C C    . ILE   B 1 137 ? 34.571 -34.463 -2.360  1.00 17.75 ?  137 ILE   B C    1 
ATOM   6209 O O    . ILE   B 1 137 ? 33.845 -33.855 -3.161  1.00 17.11 ?  137 ILE   B O    1 
ATOM   6210 C CB   . ILE   B 1 137 ? 35.180 -36.898 -2.769  1.00 20.29 ?  137 ILE   B CB   1 
ATOM   6211 C CG1  . ILE   B 1 137 ? 36.168 -37.804 -3.506  1.00 22.62 ?  137 ILE   B CG1  1 
ATOM   6212 C CG2  . ILE   B 1 137 ? 33.777 -37.055 -3.338  1.00 20.86 ?  137 ILE   B CG2  1 
ATOM   6213 C CD1  . ILE   B 1 137 ? 35.890 -39.288 -3.333  1.00 24.99 ?  137 ILE   B CD1  1 
ATOM   6214 H H    . ILE   B 1 137 ? 37.116 -35.953 -1.628  1.00 21.44 ?  137 ILE   B H    1 
ATOM   6215 H HA   . ILE   B 1 137 ? 35.836 -35.228 -3.775  1.00 21.90 ?  137 ILE   B HA   1 
ATOM   6216 H HB   . ILE   B 1 137 ? 35.161 -37.167 -1.841  1.00 24.39 ?  137 ILE   B HB   1 
ATOM   6217 H HG12 . ILE   B 1 137 ? 36.131 -37.615 -4.457  1.00 27.18 ?  137 ILE   B HG12 1 
ATOM   6218 H HG13 . ILE   B 1 137 ? 37.062 -37.640 -3.172  1.00 27.18 ?  137 ILE   B HG13 1 
ATOM   6219 H HG21 . ILE   B 1 137 ? 33.541 -37.999 -3.369  1.00 25.07 ?  137 ILE   B HG21 1 
ATOM   6220 H HG22 . ILE   B 1 137 ? 33.146 -36.593 -2.767  1.00 25.07 ?  137 ILE   B HG22 1 
ATOM   6221 H HG23 . ILE   B 1 137 ? 33.753 -36.685 -4.232  1.00 25.07 ?  137 ILE   B HG23 1 
ATOM   6222 H HD11 . ILE   B 1 137 ? 36.535 -39.784 -3.859  1.00 30.02 ?  137 ILE   B HD11 1 
ATOM   6223 H HD12 . ILE   B 1 137 ? 35.975 -39.524 -2.395  1.00 30.02 ?  137 ILE   B HD12 1 
ATOM   6224 H HD13 . ILE   B 1 137 ? 34.996 -39.496 -3.646  1.00 30.02 ?  137 ILE   B HD13 1 
ATOM   6225 N N    . HIS   B 1 138 ? 34.447 -34.311 -1.043  1.00 17.83 ?  138 HIS   B N    1 
ATOM   6226 C CA   . HIS   B 1 138 ? 33.501 -33.342 -0.502  1.00 18.10 ?  138 HIS   B CA   1 
ATOM   6227 C C    . HIS   B 1 138 ? 33.909 -31.914 -0.833  1.00 17.30 ?  138 HIS   B C    1 
ATOM   6228 O O    . HIS   B 1 138 ? 33.055 -31.073 -1.134  1.00 18.11 ?  138 HIS   B O    1 
ATOM   6229 C CB   . HIS   B 1 138 ? 33.394 -33.516 1.006   1.00 19.52 ?  138 HIS   B CB   1 
ATOM   6230 C CG   . HIS   B 1 138 ? 32.463 -32.541 1.648   1.00 20.78 ?  138 HIS   B CG   1 
ATOM   6231 N ND1  . HIS   B 1 138 ? 31.124 -32.474 1.327   1.00 22.85 ?  138 HIS   B ND1  1 
ATOM   6232 C CD2  . HIS   B 1 138 ? 32.682 -31.569 2.564   1.00 21.42 ?  138 HIS   B CD2  1 
ATOM   6233 C CE1  . HIS   B 1 138 ? 30.554 -31.514 2.032   1.00 22.99 ?  138 HIS   B CE1  1 
ATOM   6234 N NE2  . HIS   B 1 138 ? 31.476 -30.951 2.793   1.00 22.16 ?  138 HIS   B NE2  1 
ATOM   6235 H H    . HIS   B 1 138 ? 34.899 -34.747 -0.455  1.00 21.43 ?  138 HIS   B H    1 
ATOM   6236 H HA   . HIS   B 1 138 ? 32.629 -33.511 -0.889  1.00 21.76 ?  138 HIS   B HA   1 
ATOM   6237 H HB2  . HIS   B 1 138 ? 33.065 -34.411 1.197   1.00 23.46 ?  138 HIS   B HB2  1 
ATOM   6238 H HB3  . HIS   B 1 138 ? 34.270 -33.397 1.400   1.00 23.46 ?  138 HIS   B HB3  1 
ATOM   6239 H HD1  . HIS   B 1 138 ? 30.723 -32.985 0.759   1.00 27.46 ?  138 HIS   B HD1  1 
ATOM   6240 H HD2  . HIS   B 1 138 ? 33.485 -31.370 2.979   1.00 25.75 ?  138 HIS   B HD2  1 
ATOM   6241 H HE1  . HIS   B 1 138 ? 29.650 -31.286 2.002   1.00 27.62 ?  138 HIS   B HE1  1 
ATOM   6242 N N    . SER   B 1 139 ? 35.202 -31.613 -0.768  1.00 16.35 ?  139 SER   B N    1 
ATOM   6243 C CA   . SER   B 1 139 ? 35.636 -30.263 -1.088  1.00 15.83 ?  139 SER   B CA   1 
ATOM   6244 C C    . SER   B 1 139 ? 35.293 -29.914 -2.526  1.00 14.93 ?  139 SER   B C    1 
ATOM   6245 O O    . SER   B 1 139 ? 34.839 -28.800 -2.805  1.00 15.04 ?  139 SER   B O    1 
ATOM   6246 C CB   . SER   B 1 139 ? 37.131 -30.122 -0.826  1.00 16.26 ?  139 SER   B CB   1 
ATOM   6247 O OG   . SER   B 1 139 ? 37.534 -28.786 -1.073  1.00 16.52 ?  139 SER   B OG   1 
ATOM   6248 H H    . SER   B 1 139 ? 35.832 -32.158 -0.560  1.00 19.66 ?  139 SER   B H    1 
ATOM   6249 H HA   . SER   B 1 139 ? 35.165 -29.639 -0.518  1.00 19.03 ?  139 SER   B HA   1 
ATOM   6250 H HB2  . SER   B 1 139 ? 37.309 -30.354 0.101   1.00 19.55 ?  139 SER   B HB2  1 
ATOM   6251 H HB3  . SER   B 1 139 ? 37.619 -30.709 -1.419  1.00 19.55 ?  139 SER   B HB3  1 
ATOM   6252 H HG   . SER   B 1 139 ? 38.358 -28.704 -0.903  1.00 19.86 ?  139 SER   B HG   1 
ATOM   6253 N N    . LEU   B 1 140 ? 35.475 -30.863 -3.451  1.00 14.67 ?  140 LEU   B N    1 
ATOM   6254 C CA   . LEU   B 1 140 ? 35.109 -30.614 -4.838  1.00 14.59 ?  140 LEU   B CA   1 
ATOM   6255 C C    . LEU   B 1 140 ? 33.605 -30.383 -4.967  1.00 15.09 ?  140 LEU   B C    1 
ATOM   6256 O O    . LEU   B 1 140 ? 33.167 -29.495 -5.703  1.00 15.05 ?  140 LEU   B O    1 
ATOM   6257 C CB   . LEU   B 1 140 ? 35.580 -31.775 -5.719  1.00 15.03 ?  140 LEU   B CB   1 
ATOM   6258 C CG   . LEU   B 1 140 ? 35.212 -31.665 -7.191  1.00 15.27 ?  140 LEU   B CG   1 
ATOM   6259 C CD1  . LEU   B 1 140 ? 35.775 -30.392 -7.796  1.00 16.29 ?  140 LEU   B CD1  1 
ATOM   6260 C CD2  . LEU   B 1 140 ? 35.687 -32.901 -7.933  1.00 16.28 ?  140 LEU   B CD2  1 
ATOM   6261 H H    . LEU   B 1 140 ? 35.797 -31.642 -3.304  1.00 17.64 ?  140 LEU   B H    1 
ATOM   6262 H HA   . LEU   B 1 140 ? 35.561 -29.813 -5.147  1.00 17.54 ?  140 LEU   B HA   1 
ATOM   6263 H HB2  . LEU   B 1 140 ? 36.549 -31.834 -5.667  1.00 18.07 ?  140 LEU   B HB2  1 
ATOM   6264 H HB3  . LEU   B 1 140 ? 35.188 -32.599 -5.387  1.00 18.07 ?  140 LEU   B HB3  1 
ATOM   6265 H HG   . LEU   B 1 140 ? 34.248 -31.622 -7.270  1.00 18.36 ?  140 LEU   B HG   1 
ATOM   6266 H HD11 . LEU   B 1 140 ? 35.650 -30.419 -8.756  1.00 19.58 ?  140 LEU   B HD11 1 
ATOM   6267 H HD12 . LEU   B 1 140 ? 35.302 -29.629 -7.423  1.00 19.58 ?  140 LEU   B HD12 1 
ATOM   6268 H HD13 . LEU   B 1 140 ? 36.718 -30.332 -7.584  1.00 19.58 ?  140 LEU   B HD13 1 
ATOM   6269 H HD21 . LEU   B 1 140 ? 35.442 -32.816 -8.869  1.00 19.57 ?  140 LEU   B HD21 1 
ATOM   6270 H HD22 . LEU   B 1 140 ? 36.644 -32.978 -7.843  1.00 19.57 ?  140 LEU   B HD22 1 
ATOM   6271 H HD23 . LEU   B 1 140 ? 35.249 -33.679 -7.549  1.00 19.57 ?  140 LEU   B HD23 1 
ATOM   6272 N N    . ARG   B 1 141 ? 32.802 -31.175 -4.249  1.00 15.28 ?  141 ARG   B N    1 
ATOM   6273 C CA   . ARG   B 1 141 ? 31.352 -30.998 -4.229  1.00 16.42 ?  141 ARG   B CA   1 
ATOM   6274 C C    . ARG   B 1 141 ? 30.977 -29.585 -3.806  1.00 15.92 ?  141 ARG   B C    1 
ATOM   6275 O O    . ARG   B 1 141 ? 30.170 -28.912 -4.464  1.00 16.29 ?  141 ARG   B O    1 
ATOM   6276 C CB   . ARG   B 1 141 ? 30.766 -32.020 -3.248  1.00 18.03 ?  141 ARG   B CB   1 
ATOM   6277 C CG   . ARG   B 1 141 ? 29.298 -31.896 -2.930  1.00 19.49 ?  141 ARG   B CG   1 
ATOM   6278 C CD   . ARG   B 1 141 ? 28.506 -32.539 -3.998  1.00 21.19 ?  141 ARG   B CD   1 
ATOM   6279 N NE   . ARG   B 1 141 ? 28.236 -31.627 -5.097  1.00 21.49 ?  141 ARG   B NE   1 
ATOM   6280 C CZ   . ARG   B 1 141 ? 28.223 -31.974 -6.377  1.00 21.27 ?  141 ARG   B CZ   1 
ATOM   6281 N NH1  . ARG   B 1 141 ? 28.669 -33.154 -6.782  1.00 21.21 ?  141 ARG   B NH1  1 
ATOM   6282 N NH2  . ARG   B 1 141 ? 27.744 -31.117 -7.274  1.00 22.19 ?  141 ARG   B NH2  1 
ATOM   6283 H H    . ARG   B 1 141 ? 33.083 -31.816 -3.756  1.00 18.37 ?  141 ARG   B H    1 
ATOM   6284 H HA   . ARG   B 1 141 ? 30.990 -31.157 -5.109  1.00 19.74 ?  141 ARG   B HA   1 
ATOM   6285 H HB2  . ARG   B 1 141 ? 30.921 -32.904 -3.609  1.00 21.68 ?  141 ARG   B HB2  1 
ATOM   6286 H HB3  . ARG   B 1 141 ? 31.243 -31.935 -2.408  1.00 21.68 ?  141 ARG   B HB3  1 
ATOM   6287 H HG2  . ARG   B 1 141 ? 29.114 -32.341 -2.091  1.00 23.43 ?  141 ARG   B HG2  1 
ATOM   6288 H HG3  . ARG   B 1 141 ? 29.040 -30.957 -2.874  1.00 23.43 ?  141 ARG   B HG3  1 
ATOM   6289 H HD2  . ARG   B 1 141 ? 28.998 -33.308 -4.338  1.00 25.46 ?  141 ARG   B HD2  1 
ATOM   6290 H HD3  . ARG   B 1 141 ? 27.665 -32.833 -3.628  1.00 25.46 ?  141 ARG   B HD3  1 
ATOM   6291 H HE   . ARG   B 1 141 ? 28.048 -30.811 -4.901  1.00 25.83 ?  141 ARG   B HE   1 
ATOM   6292 H HH11 . ARG   B 1 141 ? 28.970 -33.724 -6.215  1.00 25.49 ?  141 ARG   B HH11 1 
ATOM   6293 H HH12 . ARG   B 1 141 ? 28.660 -33.347 -7.617  1.00 25.49 ?  141 ARG   B HH12 1 
ATOM   6294 H HH21 . ARG   B 1 141 ? 27.461 -30.343 -7.023  1.00 26.67 ?  141 ARG   B HH21 1 
ATOM   6295 H HH22 . ARG   B 1 141 ? 27.754 -31.319 -8.110  1.00 26.67 ?  141 ARG   B HH22 1 
ATOM   6296 N N    . VAL   B 1 142 ? 31.527 -29.135 -2.682  1.00 15.73 ?  142 VAL   B N    1 
ATOM   6297 C CA   . VAL   B 1 142 ? 31.197 -27.802 -2.201  1.00 15.16 ?  142 VAL   B CA   1 
ATOM   6298 C C    . VAL   B 1 142 ? 31.674 -26.747 -3.194  1.00 15.21 ?  142 VAL   B C    1 
ATOM   6299 O O    . VAL   B 1 142 ? 30.974 -25.762 -3.456  1.00 15.83 ?  142 VAL   B O    1 
ATOM   6300 C CB   . VAL   B 1 142 ? 31.749 -27.570 -0.780  1.00 15.78 ?  142 VAL   B CB   1 
ATOM   6301 C CG1  . VAL   B 1 142 ? 31.429 -26.145 -0.304  1.00 15.67 ?  142 VAL   B CG1  1 
ATOM   6302 C CG2  . VAL   B 1 142 ? 31.185 -28.601 0.182   1.00 16.81 ?  142 VAL   B CG2  1 
ATOM   6303 H H    . VAL   B 1 142 ? 32.092 -29.563 -2.192  1.00 18.92 ?  142 VAL   B H    1 
ATOM   6304 H HA   . VAL   B 1 142 ? 30.236 -27.724 -2.143  1.00 18.23 ?  142 VAL   B HA   1 
ATOM   6305 H HB   . VAL   B 1 142 ? 32.715 -27.668 -0.792  1.00 18.97 ?  142 VAL   B HB   1 
ATOM   6306 H HG11 . VAL   B 1 142 ? 31.615 -26.079 0.645   1.00 18.84 ?  142 VAL   B HG11 1 
ATOM   6307 H HG12 . VAL   B 1 142 ? 31.984 -25.514 -0.792  1.00 18.84 ?  142 VAL   B HG12 1 
ATOM   6308 H HG13 . VAL   B 1 142 ? 30.492 -25.960 -0.471  1.00 18.84 ?  142 VAL   B HG13 1 
ATOM   6309 H HG21 . VAL   B 1 142 ? 31.503 -28.407 1.076   1.00 20.21 ?  142 VAL   B HG21 1 
ATOM   6310 H HG22 . VAL   B 1 142 ? 30.217 -28.558 0.155   1.00 20.21 ?  142 VAL   B HG22 1 
ATOM   6311 H HG23 . VAL   B 1 142 ? 31.485 -29.482 -0.093  1.00 20.21 ?  142 VAL   B HG23 1 
ATOM   6312 N N    . CYS   B 1 143 ? 32.861 -26.942 -3.774  1.00 14.51 ?  143 CYS   B N    1 
ATOM   6313 C CA   . CYS   B 1 143 ? 33.354 -26.008 -4.784  1.00 14.40 ?  143 CYS   B CA   1 
ATOM   6314 C C    . CYS   B 1 143 ? 32.348 -25.867 -5.922  1.00 14.27 ?  143 CYS   B C    1 
ATOM   6315 O O    . CYS   B 1 143 ? 31.939 -24.754 -6.279  1.00 14.77 ?  143 CYS   B O    1 
ATOM   6316 C CB   . CYS   B 1 143 ? 34.709 -26.488 -5.312  1.00 14.61 ?  143 CYS   B CB   1 
ATOM   6317 S SG   . CYS   B 1 143 ? 35.452 -25.392 -6.541  1.00 14.88 ?  143 CYS   B SG   1 
ATOM   6318 H H    . CYS   B 1 143 ? 33.394 -27.586 -3.594  1.00 17.45 ?  143 CYS   B H    1 
ATOM   6319 H HA   . CYS   B 1 143 ? 33.479 -25.132 -4.383  1.00 17.32 ?  143 CYS   B HA   1 
ATOM   6320 H HB2  . CYS   B 1 143 ? 35.332 -26.557 -4.569  1.00 17.57 ?  143 CYS   B HB2  1 
ATOM   6321 H HB3  . CYS   B 1 143 ? 34.596 -27.356 -5.720  1.00 17.57 ?  143 CYS   B HB3  1 
ATOM   6322 H HG   . CYS   B 1 143 ? 36.527 -25.818 -6.860  1.00 17.90 ?  143 CYS   B HG   1 
ATOM   6323 N N    . VAL   B 1 144 ? 31.935 -26.990 -6.506  1.00 15.21 ?  144 VAL   B N    1 
ATOM   6324 C CA   . VAL   B 1 144 ? 31.023 -26.930 -7.645  1.00 16.06 ?  144 VAL   B CA   1 
ATOM   6325 C C    . VAL   B 1 144 ? 29.679 -26.318 -7.271  1.00 16.32 ?  144 VAL   B C    1 
ATOM   6326 O O    . VAL   B 1 144 ? 29.067 -25.607 -8.078  1.00 17.60 ?  144 VAL   B O    1 
ATOM   6327 C CB   . VAL   B 1 144 ? 30.864 -28.341 -8.219  1.00 18.63 ?  144 VAL   B CB   1 
ATOM   6328 C CG1  . VAL   B 1 144 ? 29.588 -28.467 -9.047  1.00 21.57 ?  144 VAL   B CG1  1 
ATOM   6329 C CG2  . VAL   B 1 144 ? 32.104 -28.737 -9.010  1.00 18.56 ?  144 VAL   B CG2  1 
ATOM   6330 H H    . VAL   B 1 144 ? 32.167 -27.783 -6.273  1.00 18.30 ?  144 VAL   B H    1 
ATOM   6331 H HA   . VAL   B 1 144 ? 31.413 -26.375 -8.337  1.00 19.31 ?  144 VAL   B HA   1 
ATOM   6332 H HB   . VAL   B 1 144 ? 30.787 -28.964 -7.480  1.00 22.39 ?  144 VAL   B HB   1 
ATOM   6333 H HG11 . VAL   B 1 144 ? 29.665 -29.254 -9.616  1.00 25.92 ?  144 VAL   B HG11 1 
ATOM   6334 H HG12 . VAL   B 1 144 ? 28.833 -28.573 -8.450  1.00 25.92 ?  144 VAL   B HG12 1 
ATOM   6335 H HG13 . VAL   B 1 144 ? 29.483 -27.678 -9.594  1.00 25.92 ?  144 VAL   B HG13 1 
ATOM   6336 H HG21 . VAL   B 1 144 ? 31.985 -29.636 -9.357  1.00 22.31 ?  144 VAL   B HG21 1 
ATOM   6337 H HG22 . VAL   B 1 144 ? 32.220 -28.113 -9.746  1.00 22.31 ?  144 VAL   B HG22 1 
ATOM   6338 H HG23 . VAL   B 1 144 ? 32.874 -28.707 -8.425  1.00 22.31 ?  144 VAL   B HG23 1 
ATOM   6339 N N    . ASP   B 1 145 ? 29.216 -26.554 -6.051  1.00 16.11 ?  145 ASP   B N    1 
ATOM   6340 C CA   . ASP   B 1 145 ? 27.913 -26.081 -5.613  1.00 16.96 ?  145 ASP   B CA   1 
ATOM   6341 C C    . ASP   B 1 145 ? 27.947 -24.659 -5.073  1.00 16.67 ?  145 ASP   B C    1 
ATOM   6342 O O    . ASP   B 1 145 ? 26.887 -24.112 -4.743  1.00 18.48 ?  145 ASP   B O    1 
ATOM   6343 C CB   . ASP   B 1 145 ? 27.340 -26.993 -4.525  1.00 19.08 ?  145 ASP   B CB   1 
ATOM   6344 C CG   . ASP   B 1 145 ? 26.965 -28.368 -5.033  1.00 21.28 ?  145 ASP   B CG   1 
ATOM   6345 O OD1  . ASP   B 1 145 ? 26.847 -28.558 -6.263  1.00 21.26 ?  145 ASP   B OD1  1 
ATOM   6346 O OD2  . ASP   B 1 145 ? 26.775 -29.258 -4.181  1.00 23.32 -1 145 ASP   B OD2  1 
ATOM   6347 H H    . ASP   B 1 145 ? 29.654 -26.977 -5.448  1.00 19.37 ?  145 ASP   B H    1 
ATOM   6348 H HA   . ASP   B 1 145 ? 27.310 -26.079 -6.369  1.00 20.39 ?  145 ASP   B HA   1 
ATOM   6349 H HB2  . ASP   B 1 145 ? 28.000 -27.107 -3.832  1.00 22.93 ?  145 ASP   B HB2  1 
ATOM   6350 H HB3  . ASP   B 1 145 ? 26.541 -26.575 -4.163  1.00 22.93 ?  145 ASP   B HB3  1 
ATOM   6351 N N    . THR   B 1 146 ? 29.124 -24.043 -4.978  1.00 15.19 ?  146 THR   B N    1 
ATOM   6352 C CA   . THR   B 1 146 ? 29.266 -22.718 -4.384  1.00 14.80 ?  146 THR   B CA   1 
ATOM   6353 C C    . THR   B 1 146 ? 29.898 -21.700 -5.315  1.00 14.64 ?  146 THR   B C    1 
ATOM   6354 O O    . THR   B 1 146 ? 29.440 -20.537 -5.373  1.00 14.71 ?  146 THR   B O    1 
ATOM   6355 C CB   . THR   B 1 146 ? 30.096 -22.817 -3.102  1.00 15.10 ?  146 THR   B CB   1 
ATOM   6356 O OG1  . THR   B 1 146 ? 29.516 -23.805 -2.234  1.00 15.55 ?  146 THR   B OG1  1 
ATOM   6357 C CG2  . THR   B 1 146 ? 30.187 -21.466 -2.402  1.00 15.30 ?  146 THR   B CG2  1 
ATOM   6358 H H    . THR   B 1 146 ? 29.873 -24.370 -5.262  1.00 18.26 ?  146 THR   B H    1 
ATOM   6359 H HA   . THR   B 1 146 ? 28.395 -22.385 -4.141  1.00 17.80 ?  146 THR   B HA   1 
ATOM   6360 H HB   . THR   B 1 146 ? 31.005 -23.085 -3.330  1.00 18.16 ?  146 THR   B HB   1 
ATOM   6361 H HG1  . THR   B 1 146 ? 29.556 -24.565 -2.601  1.00 18.70 ?  146 THR   B HG1  1 
ATOM   6362 H HG21 . THR   B 1 146 ? 30.524 -21.579 -1.502  1.00 18.40 ?  146 THR   B HG21 1 
ATOM   6363 H HG22 . THR   B 1 146 ? 30.791 -20.878 -2.890  1.00 18.40 ?  146 THR   B HG22 1 
ATOM   6364 H HG23 . THR   B 1 146 ? 29.311 -21.056 -2.365  1.00 18.40 ?  146 THR   B HG23 1 
ATOM   6365 N N    . VAL   B 1 147 ? 30.964 -22.082 -6.017  1.00 14.05 ?  147 VAL   B N    1 
ATOM   6366 C CA   . VAL   B 1 147 ? 31.686 -21.135 -6.857  1.00 13.89 ?  147 VAL   B CA   1 
ATOM   6367 C C    . VAL   B 1 147 ? 30.952 -20.997 -8.179  1.00 14.44 ?  147 VAL   B C    1 
ATOM   6368 O O    . VAL   B 1 147 ? 30.577 -22.000 -8.806  1.00 15.32 ?  147 VAL   B O    1 
ATOM   6369 C CB   . VAL   B 1 147 ? 33.144 -21.581 -7.057  1.00 13.80 ?  147 VAL   B CB   1 
ATOM   6370 C CG1  . VAL   B 1 147 ? 33.899 -20.550 -7.874  1.00 13.84 ?  147 VAL   B CG1  1 
ATOM   6371 C CG2  . VAL   B 1 147 ? 33.820 -21.798 -5.709  1.00 13.88 ?  147 VAL   B CG2  1 
ATOM   6372 H H    . VAL   B 1 147 ? 31.290 -22.881 -6.026  1.00 16.90 ?  147 VAL   B H    1 
ATOM   6373 H HA   . VAL   B 1 147 ? 31.699 -20.271 -6.424  1.00 16.71 ?  147 VAL   B HA   1 
ATOM   6374 H HB   . VAL   B 1 147 ? 33.165 -22.422 -7.545  1.00 16.60 ?  147 VAL   B HB   1 
ATOM   6375 H HG11 . VAL   B 1 147 ? 34.846 -20.761 -7.864  1.00 16.64 ?  147 VAL   B HG11 1 
ATOM   6376 H HG12 . VAL   B 1 147 ? 33.570 -20.558 -8.787  1.00 16.64 ?  147 VAL   B HG12 1 
ATOM   6377 H HG13 . VAL   B 1 147 ? 33.757 -19.670 -7.482  1.00 16.64 ?  147 VAL   B HG13 1 
ATOM   6378 H HG21 . VAL   B 1 147 ? 34.763 -21.978 -5.850  1.00 16.70 ?  147 VAL   B HG21 1 
ATOM   6379 H HG22 . VAL   B 1 147 ? 33.714 -20.997 -5.172  1.00 16.70 ?  147 VAL   B HG22 1 
ATOM   6380 H HG23 . VAL   B 1 147 ? 33.404 -22.552 -5.263  1.00 16.70 ?  147 VAL   B HG23 1 
ATOM   6381 N N    . ARG   B 1 148 ? 30.749 -19.743 -8.598  1.00 14.17 ?  148 ARG   B N    1 
ATOM   6382 C CA   . ARG   B 1 148 ? 30.127 -19.419 -9.870  1.00 14.26 ?  148 ARG   B CA   1 
ATOM   6383 C C    . ARG   B 1 148 ? 31.077 -18.733 -10.840 1.00 14.34 ?  148 ARG   B C    1 
ATOM   6384 O O    . ARG   B 1 148 ? 30.793 -18.713 -12.042 1.00 15.81 ?  148 ARG   B O    1 
ATOM   6385 C CB   . ARG   B 1 148 ? 28.885 -18.541 -9.645  1.00 14.85 ?  148 ARG   B CB   1 
ATOM   6386 C CG   . ARG   B 1 148 ? 27.815 -19.248 -8.828  1.00 15.55 ?  148 ARG   B CG   1 
ATOM   6387 C CD   . ARG   B 1 148 ? 26.596 -18.372 -8.529  1.00 16.68 ?  148 ARG   B CD   1 
ATOM   6388 N NE   . ARG   B 1 148 ? 26.966 -17.166 -7.797  1.00 16.60 ?  148 ARG   B NE   1 
ATOM   6389 C CZ   . ARG   B 1 148 ? 27.278 -17.132 -6.508  1.00 15.69 ?  148 ARG   B CZ   1 
ATOM   6390 N NH1  . ARG   B 1 148 ? 27.226 -18.221 -5.751  1.00 15.60 ?  148 ARG   B NH1  1 
ATOM   6391 N NH2  . ARG   B 1 148 ? 27.672 -15.980 -5.967  1.00 15.85 ?  148 ARG   B NH2  1 
ATOM   6392 H H    . ARG   B 1 148 ? 30.980 -19.046 -8.144  1.00 17.04 ?  148 ARG   B H    1 
ATOM   6393 H HA   . ARG   B 1 148 ? 29.829 -20.241 -10.284 1.00 17.15 ?  148 ARG   B HA   1 
ATOM   6394 H HB2  . ARG   B 1 148 ? 29.145 -17.738 -9.165  1.00 17.86 ?  148 ARG   B HB2  1 
ATOM   6395 H HB3  . ARG   B 1 148 ? 28.502 -18.306 -10.504 1.00 17.86 ?  148 ARG   B HB3  1 
ATOM   6396 H HG2  . ARG   B 1 148 ? 27.506 -20.027 -9.323  1.00 18.70 ?  148 ARG   B HG2  1 
ATOM   6397 H HG3  . ARG   B 1 148 ? 28.195 -19.529 -7.982  1.00 18.70 ?  148 ARG   B HG3  1 
ATOM   6398 H HD2  . ARG   B 1 148 ? 26.184 -18.106 -9.364  1.00 20.06 ?  148 ARG   B HD2  1 
ATOM   6399 H HD3  . ARG   B 1 148 ? 25.966 -18.876 -7.989  1.00 20.06 ?  148 ARG   B HD3  1 
ATOM   6400 H HE   . ARG   B 1 148 ? 26.997 -16.429 -8.232  1.00 19.96 ?  148 ARG   B HE   1 
ATOM   6401 H HH11 . ARG   B 1 148 ? 26.976 -18.973 -6.086  1.00 18.76 ?  148 ARG   B HH11 1 
ATOM   6402 H HH12 . ARG   B 1 148 ? 27.432 -18.176 -4.914  1.00 18.76 ?  148 ARG   B HH12 1 
ATOM   6403 H HH21 . ARG   B 1 148 ? 27.717 -15.273 -6.450  1.00 19.05 ?  148 ARG   B HH21 1 
ATOM   6404 H HH22 . ARG   B 1 148 ? 27.879 -15.945 -5.132  1.00 19.05 ?  148 ARG   B HH22 1 
ATOM   6405 N N    . THR   B 1 149 ? 32.185 -18.180 -10.350 1.00 14.34 ?  149 THR   B N    1 
ATOM   6406 C CA   . THR   B 1 149 ? 33.226 -17.621 -11.197 1.00 14.15 ?  149 THR   B CA   1 
ATOM   6407 C C    . THR   B 1 149 ? 34.105 -18.760 -11.718 1.00 14.16 ?  149 THR   B C    1 
ATOM   6408 O O    . THR   B 1 149 ? 33.909 -19.932 -11.382 1.00 14.48 ?  149 THR   B O    1 
ATOM   6409 C CB   . THR   B 1 149 ? 34.001 -16.576 -10.408 1.00 14.42 ?  149 THR   B CB   1 
ATOM   6410 O OG1  . THR   B 1 149 ? 34.461 -17.184 -9.197  1.00 14.28 ?  149 THR   B OG1  1 
ATOM   6411 C CG2  . THR   B 1 149 ? 33.120 -15.366 -10.102 1.00 15.24 ?  149 THR   B CG2  1 
ATOM   6412 H H    . THR   B 1 149 ? 32.351 -18.113 -9.508  1.00 17.24 ?  149 THR   B H    1 
ATOM   6413 H HA   . THR   B 1 149 ? 32.811 -17.180 -11.956 1.00 17.02 ?  149 THR   B HA   1 
ATOM   6414 H HB   . THR   B 1 149 ? 34.762 -16.283 -10.923 1.00 17.34 ?  149 THR   B HB   1 
ATOM   6415 H HG1  . THR   B 1 149 ? 34.878 -16.619 -8.730  1.00 17.17 ?  149 THR   B HG1  1 
ATOM   6416 H HG21 . THR   B 1 149 ? 33.632 -14.699 -9.609  1.00 18.32 ?  149 THR   B HG21 1 
ATOM   6417 H HG22 . THR   B 1 149 ? 32.807 -14.963 -10.930 1.00 18.32 ?  149 THR   B HG22 1 
ATOM   6418 H HG23 . THR   B 1 149 ? 32.355 -15.627 -9.570  1.00 18.32 ?  149 THR   B HG23 1 
ATOM   6419 N N    . ASN   B 1 150 ? 35.068 -18.434 -12.569 1.00 13.97 ?  150 ASN   B N    1 
ATOM   6420 C CA   . ASN   B 1 150 ? 35.835 -19.455 -13.271 1.00 14.33 ?  150 ASN   B CA   1 
ATOM   6421 C C    . ASN   B 1 150 ? 36.999 -19.910 -12.398 1.00 13.90 ?  150 ASN   B C    1 
ATOM   6422 O O    . ASN   B 1 150 ? 37.943 -19.150 -12.161 1.00 14.51 ?  150 ASN   B O    1 
ATOM   6423 C CB   . ASN   B 1 150 ? 36.304 -18.924 -14.618 1.00 16.58 ?  150 ASN   B CB   1 
ATOM   6424 C CG   . ASN   B 1 150 ? 35.158 -18.717 -15.571 1.00 19.23 ?  150 ASN   B CG   1 
ATOM   6425 O OD1  . ASN   B 1 150 ? 34.258 -19.545 -15.648 1.00 20.31 ?  150 ASN   B OD1  1 
ATOM   6426 N ND2  . ASN   B 1 150 ? 35.160 -17.600 -16.277 1.00 21.21 ?  150 ASN   B ND2  1 
ATOM   6427 H H    . ASN   B 1 150 ? 35.303 -17.625 -12.752 1.00 16.80 ?  150 ASN   B H    1 
ATOM   6428 H HA   . ASN   B 1 150 ? 35.255 -20.221 -13.436 1.00 17.23 ?  150 ASN   B HA   1 
ATOM   6429 H HB2  . ASN   B 1 150 ? 36.742 -18.066 -14.484 1.00 19.93 ?  150 ASN   B HB2  1 
ATOM   6430 H HB3  . ASN   B 1 150 ? 36.917 -19.556 -15.015 1.00 19.93 ?  150 ASN   B HB3  1 
ATOM   6431 H HD21 . ASN   B 1 150 ? 34.522 -17.436 -16.834 1.00 25.49 ?  150 ASN   B HD21 1 
ATOM   6432 H HD22 . ASN   B 1 150 ? 35.804 -17.033 -16.191 1.00 25.49 ?  150 ASN   B HD22 1 
ATOM   6433 N N    . VAL   B 1 151 ? 36.944 -21.154 -11.930 1.00 13.39 ?  151 VAL   B N    1 
ATOM   6434 C CA   . VAL   B 1 151 ? 37.961 -21.694 -11.041 1.00 13.59 ?  151 VAL   B CA   1 
ATOM   6435 C C    . VAL   B 1 151 ? 38.661 -22.869 -11.715 1.00 13.36 ?  151 VAL   B C    1 
ATOM   6436 O O    . VAL   B 1 151 ? 38.015 -23.802 -12.218 1.00 14.71 ?  151 VAL   B O    1 
ATOM   6437 C CB   . VAL   B 1 151 ? 37.402 -22.030 -9.643  1.00 14.73 ?  151 VAL   B CB   1 
ATOM   6438 C CG1  . VAL   B 1 151 ? 36.225 -23.019 -9.720  1.00 15.82 ?  151 VAL   B CG1  1 
ATOM   6439 C CG2  . VAL   B 1 151 ? 38.510 -22.537 -8.732  1.00 14.80 ?  151 VAL   B CG2  1 
ATOM   6440 H H    . VAL   B 1 151 ? 36.313 -21.710 -12.122 1.00 16.11 ?  151 VAL   B H    1 
ATOM   6441 H HA   . VAL   B 1 151 ? 38.630 -21.000 -10.907 1.00 16.35 ?  151 VAL   B HA   1 
ATOM   6442 H HB   . VAL   B 1 151 ? 37.057 -21.211 -9.247  1.00 17.72 ?  151 VAL   B HB   1 
ATOM   6443 H HG11 . VAL   B 1 151 ? 35.907 -23.206 -8.821  1.00 19.03 ?  151 VAL   B HG11 1 
ATOM   6444 H HG12 . VAL   B 1 151 ? 35.508 -22.622 -10.244 1.00 19.03 ?  151 VAL   B HG12 1 
ATOM   6445 H HG13 . VAL   B 1 151 ? 36.525 -23.838 -10.141 1.00 19.03 ?  151 VAL   B HG13 1 
ATOM   6446 H HG21 . VAL   B 1 151 ? 38.162 -22.610 -7.827  1.00 17.79 ?  151 VAL   B HG21 1 
ATOM   6447 H HG22 . VAL   B 1 151 ? 38.802 -23.407 -9.042  1.00 17.79 ?  151 VAL   B HG22 1 
ATOM   6448 H HG23 . VAL   B 1 151 ? 39.247 -21.909 -8.751  1.00 17.79 ?  151 VAL   B HG23 1 
ATOM   6449 N N    . TYR   B 1 152 ? 39.992 -22.783 -11.738 1.00 13.02 ?  152 TYR   B N    1 
ATOM   6450 C CA   . TYR   B 1 152 ? 40.893 -23.766 -12.320 1.00 13.32 ?  152 TYR   B CA   1 
ATOM   6451 C C    . TYR   B 1 152 ? 41.615 -24.449 -11.164 1.00 12.81 ?  152 TYR   B C    1 
ATOM   6452 O O    . TYR   B 1 152 ? 42.470 -23.839 -10.517 1.00 13.24 ?  152 TYR   B O    1 
ATOM   6453 C CB   . TYR   B 1 152 ? 41.863 -23.061 -13.270 1.00 14.35 ?  152 TYR   B CB   1 
ATOM   6454 C CG   . TYR   B 1 152 ? 41.182 -22.585 -14.536 1.00 14.87 ?  152 TYR   B CG   1 
ATOM   6455 C CD1  . TYR   B 1 152 ? 40.537 -21.349 -14.595 1.00 15.27 ?  152 TYR   B CD1  1 
ATOM   6456 C CD2  . TYR   B 1 152 ? 41.165 -23.384 -15.667 1.00 16.17 ?  152 TYR   B CD2  1 
ATOM   6457 C CE1  . TYR   B 1 152 ? 39.899 -20.935 -15.750 1.00 16.98 ?  152 TYR   B CE1  1 
ATOM   6458 C CE2  . TYR   B 1 152 ? 40.528 -22.982 -16.820 1.00 17.14 ?  152 TYR   B CE2  1 
ATOM   6459 C CZ   . TYR   B 1 152 ? 39.905 -21.751 -16.861 1.00 17.58 ?  152 TYR   B CZ   1 
ATOM   6460 O OH   . TYR   B 1 152 ? 39.276 -21.346 -18.014 1.00 20.21 ?  152 TYR   B OH   1 
ATOM   6461 H H    . TYR   B 1 152 ? 40.424 -22.115 -11.391 1.00 15.66 ?  152 TYR   B H    1 
ATOM   6462 H HA   . TYR   B 1 152 ? 40.383 -24.427 -12.814 1.00 16.02 ?  152 TYR   B HA   1 
ATOM   6463 H HB2  . TYR   B 1 152 ? 42.235 -22.287 -12.818 1.00 17.25 ?  152 TYR   B HB2  1 
ATOM   6464 H HB3  . TYR   B 1 152 ? 42.571 -23.672 -13.515 1.00 17.25 ?  152 TYR   B HB3  1 
ATOM   6465 H HD1  . TYR   B 1 152 ? 40.529 -20.797 -13.845 1.00 18.36 ?  152 TYR   B HD1  1 
ATOM   6466 H HD2  . TYR   B 1 152 ? 41.580 -24.216 -15.642 1.00 19.44 ?  152 TYR   B HD2  1 
ATOM   6467 H HE1  . TYR   B 1 152 ? 39.476 -20.106 -15.783 1.00 20.42 ?  152 TYR   B HE1  1 
ATOM   6468 H HE2  . TYR   B 1 152 ? 40.533 -23.531 -17.572 1.00 20.61 ?  152 TYR   B HE2  1 
ATOM   6469 H HH   . TYR   B 1 152 ? 39.359 -21.933 -18.612 1.00 24.28 ?  152 TYR   B HH   1 
ATOM   6470 N N    . LEU   B 1 153 ? 41.247 -25.703 -10.893 1.00 13.04 ?  153 LEU   B N    1 
ATOM   6471 C CA   . LEU   B 1 153 ? 41.750 -26.457 -9.754  1.00 12.76 ?  153 LEU   B CA   1 
ATOM   6472 C C    . LEU   B 1 153 ? 42.976 -27.261 -10.156 1.00 13.14 ?  153 LEU   B C    1 
ATOM   6473 O O    . LEU   B 1 153 ? 42.949 -27.993 -11.151 1.00 14.34 ?  153 LEU   B O    1 
ATOM   6474 C CB   . LEU   B 1 153 ? 40.667 -27.409 -9.241  1.00 13.05 ?  153 LEU   B CB   1 
ATOM   6475 C CG   . LEU   B 1 153 ? 39.411 -26.752 -8.667  1.00 13.72 ?  153 LEU   B CG   1 
ATOM   6476 C CD1  . LEU   B 1 153 ? 38.309 -27.786 -8.509  1.00 14.89 ?  153 LEU   B CD1  1 
ATOM   6477 C CD2  . LEU   B 1 153 ? 39.727 -26.093 -7.325  1.00 13.98 ?  153 LEU   B CD2  1 
ATOM   6478 H H    . LEU   B 1 153 ? 40.676 -26.147 -11.372 1.00 15.69 ?  153 LEU   B H    1 
ATOM   6479 H HA   . LEU   B 1 153 ? 41.982 -25.844 -9.044  1.00 15.35 ?  153 LEU   B HA   1 
ATOM   6480 H HB2  . LEU   B 1 153 ? 40.383 -27.980 -9.969  1.00 15.70 ?  153 LEU   B HB2  1 
ATOM   6481 H HB3  . LEU   B 1 153 ? 41.050 -27.954 -8.533  1.00 15.70 ?  153 LEU   B HB3  1 
ATOM   6482 H HG   . LEU   B 1 153 ? 39.095 -26.062 -9.275  1.00 16.50 ?  153 LEU   B HG   1 
ATOM   6483 H HD11 . LEU   B 1 153 ? 37.504 -27.339 -8.195  1.00 17.91 ?  153 LEU   B HD11 1 
ATOM   6484 H HD12 . LEU   B 1 153 ? 38.144 -28.197 -9.368  1.00 17.91 ?  153 LEU   B HD12 1 
ATOM   6485 H HD13 . LEU   B 1 153 ? 38.593 -28.447 -7.865  1.00 17.91 ?  153 LEU   B HD13 1 
ATOM   6486 H HD21 . LEU   B 1 153 ? 38.916 -25.720 -6.948  1.00 16.81 ?  153 LEU   B HD21 1 
ATOM   6487 H HD22 . LEU   B 1 153 ? 40.093 -26.762 -6.723  1.00 16.81 ?  153 LEU   B HD22 1 
ATOM   6488 H HD23 . LEU   B 1 153 ? 40.381 -25.387 -7.464  1.00 16.81 ?  153 LEU   B HD23 1 
ATOM   6489 N N    . ALA   B 1 154 ? 44.036 -27.146 -9.362  1.00 13.03 ?  154 ALA   B N    1 
ATOM   6490 C CA   . ALA   B 1 154 ? 45.265 -27.905 -9.550  1.00 14.32 ?  154 ALA   B CA   1 
ATOM   6491 C C    . ALA   B 1 154 ? 45.333 -28.988 -8.479  1.00 15.00 ?  154 ALA   B C    1 
ATOM   6492 O O    . ALA   B 1 154 ? 45.277 -28.692 -7.277  1.00 16.81 ?  154 ALA   B O    1 
ATOM   6493 C CB   . ALA   B 1 154 ? 46.487 -26.991 -9.487  1.00 15.23 ?  154 ALA   B CB   1 
ATOM   6494 H H    . ALA   B 1 154 ? 44.059 -26.608 -8.686  1.00 15.67 ?  154 ALA   B H    1 
ATOM   6495 H HA   . ALA   B 1 154 ? 45.244 -28.329 -10.420 1.00 17.22 ?  154 ALA   B HA   1 
ATOM   6496 H HB1  . ALA   B 1 154 ? 47.286 -27.525 -9.615  1.00 18.31 ?  154 ALA   B HB1  1 
ATOM   6497 H HB2  . ALA   B 1 154 ? 46.422 -26.320 -10.188 1.00 18.31 ?  154 ALA   B HB2  1 
ATOM   6498 H HB3  . ALA   B 1 154 ? 46.516 -26.556 -8.619  1.00 18.31 ?  154 ALA   B HB3  1 
ATOM   6499 N N    . VAL   B 1 155 ? 45.435 -30.236 -8.915  1.00 14.39 ?  155 VAL   B N    1 
ATOM   6500 C CA   . VAL   B 1 155 ? 45.540 -31.383 -8.022  1.00 14.80 ?  155 VAL   B CA   1 
ATOM   6501 C C    . VAL   B 1 155 ? 46.872 -32.061 -8.308  1.00 14.67 ?  155 VAL   B C    1 
ATOM   6502 O O    . VAL   B 1 155 ? 47.098 -32.555 -9.420  1.00 16.63 ?  155 VAL   B O    1 
ATOM   6503 C CB   . VAL   B 1 155 ? 44.379 -32.372 -8.216  1.00 16.27 ?  155 VAL   B CB   1 
ATOM   6504 C CG1  . VAL   B 1 155 ? 44.549 -33.571 -7.298  1.00 16.42 ?  155 VAL   B CG1  1 
ATOM   6505 C CG2  . VAL   B 1 155 ? 43.044 -31.677 -7.966  1.00 17.16 ?  155 VAL   B CG2  1 
ATOM   6506 H H    . VAL   B 1 155 ? 45.450 -30.452 -9.751  1.00 17.31 ?  155 VAL   B H    1 
ATOM   6507 H HA   . VAL   B 1 155 ? 45.536 -31.083 -7.103  1.00 17.80 ?  155 VAL   B HA   1 
ATOM   6508 H HB   . VAL   B 1 155 ? 44.378 -32.688 -9.134  1.00 19.56 ?  155 VAL   B HB   1 
ATOM   6509 H HG11 . VAL   B 1 155 ? 43.718 -34.072 -7.272  1.00 19.75 ?  155 VAL   B HG11 1 
ATOM   6510 H HG12 . VAL   B 1 155 ? 45.261 -34.135 -7.639  1.00 19.75 ?  155 VAL   B HG12 1 
ATOM   6511 H HG13 . VAL   B 1 155 ? 44.771 -33.259 -6.407  1.00 19.75 ?  155 VAL   B HG13 1 
ATOM   6512 H HG21 . VAL   B 1 155 ? 42.326 -32.327 -8.049  1.00 20.63 ?  155 VAL   B HG21 1 
ATOM   6513 H HG22 . VAL   B 1 155 ? 43.044 -31.301 -7.072  1.00 20.63 ?  155 VAL   B HG22 1 
ATOM   6514 H HG23 . VAL   B 1 155 ? 42.922 -30.970 -8.621  1.00 20.63 ?  155 VAL   B HG23 1 
ATOM   6515 N N    . PHE   B 1 156 ? 47.745 -32.102 -7.301  1.00 15.02 ?  156 PHE   B N    1 
ATOM   6516 C CA   . PHE   B 1 156 ? 49.119 -32.563 -7.514  1.00 16.28 ?  156 PHE   B CA   1 
ATOM   6517 C C    . PHE   B 1 156 ? 49.209 -34.064 -7.794  1.00 17.84 ?  156 PHE   B C    1 
ATOM   6518 O O    . PHE   B 1 156 ? 49.922 -34.494 -8.712  1.00 19.69 ?  156 PHE   B O    1 
ATOM   6519 C CB   . PHE   B 1 156 ? 49.961 -32.193 -6.296  1.00 16.29 ?  156 PHE   B CB   1 
ATOM   6520 C CG   . PHE   B 1 156 ? 51.382 -32.660 -6.365  1.00 16.57 ?  156 PHE   B CG   1 
ATOM   6521 C CD1  . PHE   B 1 156 ? 52.253 -32.141 -7.302  1.00 18.11 ?  156 PHE   B CD1  1 
ATOM   6522 C CD2  . PHE   B 1 156 ? 51.850 -33.599 -5.472  1.00 17.19 ?  156 PHE   B CD2  1 
ATOM   6523 C CE1  . PHE   B 1 156 ? 53.575 -32.559 -7.351  1.00 18.83 ?  156 PHE   B CE1  1 
ATOM   6524 C CE2  . PHE   B 1 156 ? 53.167 -34.018 -5.517  1.00 18.28 ?  156 PHE   B CE2  1 
ATOM   6525 C CZ   . PHE   B 1 156 ? 54.022 -33.501 -6.462  1.00 18.64 ?  156 PHE   B CZ   1 
ATOM   6526 H H    . PHE   B 1 156 ? 47.566 -31.872 -6.493  1.00 18.06 ?  156 PHE   B H    1 
ATOM   6527 H HA   . PHE   B 1 156 ? 49.484 -32.099 -8.279  1.00 19.57 ?  156 PHE   B HA   1 
ATOM   6528 H HB2  . PHE   B 1 156 ? 49.971 -31.227 -6.211  1.00 19.58 ?  156 PHE   B HB2  1 
ATOM   6529 H HB3  . PHE   B 1 156 ? 49.559 -32.588 -5.507  1.00 19.58 ?  156 PHE   B HB3  1 
ATOM   6530 H HD1  . PHE   B 1 156 ? 51.952 -31.498 -7.908  1.00 21.77 ?  156 PHE   B HD1  1 
ATOM   6531 H HD2  . PHE   B 1 156 ? 51.273 -33.955 -4.835  1.00 20.67 ?  156 PHE   B HD2  1 
ATOM   6532 H HE1  . PHE   B 1 156 ? 54.150 -32.205 -7.990  1.00 22.64 ?  156 PHE   B HE1  1 
ATOM   6533 H HE2  . PHE   B 1 156 ? 53.469 -34.663 -4.916  1.00 21.97 ?  156 PHE   B HE2  1 
ATOM   6534 H HZ   . PHE   B 1 156 ? 54.905 -33.789 -6.493  1.00 22.40 ?  156 PHE   B HZ   1 
ATOM   6535 N N    . ASP   B 1 157 ? 48.548 -34.883 -6.985  1.00 18.14 ?  157 ASP   B N    1 
ATOM   6536 C CA   . ASP   B 1 157 ? 48.691 -36.331 -7.082  1.00 19.30 ?  157 ASP   B CA   1 
ATOM   6537 C C    . ASP   B 1 157 ? 47.771 -36.879 -8.169  1.00 19.14 ?  157 ASP   B C    1 
ATOM   6538 O O    . ASP   B 1 157 ? 46.546 -36.748 -8.071  1.00 18.64 ?  157 ASP   B O    1 
ATOM   6539 C CB   . ASP   B 1 157 ? 48.335 -36.941 -5.734  1.00 21.06 ?  157 ASP   B CB   1 
ATOM   6540 C CG   . ASP   B 1 157 ? 48.472 -38.447 -5.720  1.00 23.22 ?  157 ASP   B CG   1 
ATOM   6541 O OD1  . ASP   B 1 157 ? 48.805 -39.040 -6.772  1.00 23.67 ?  157 ASP   B OD1  1 
ATOM   6542 O OD2  . ASP   B 1 157 ? 48.248 -39.035 -4.645  1.00 25.66 -1 157 ASP   B OD2  1 
ATOM   6543 H H    . ASP   B 1 157 ? 48.009 -34.626 -6.370  1.00 21.81 ?  157 ASP   B H    1 
ATOM   6544 H HA   . ASP   B 1 157 ? 49.611 -36.561 -7.300  1.00 23.20 ?  157 ASP   B HA   1 
ATOM   6545 H HB2  . ASP   B 1 157 ? 48.912 -36.562 -5.053  1.00 25.32 ?  157 ASP   B HB2  1 
ATOM   6546 H HB3  . ASP   B 1 157 ? 47.410 -36.724 -5.532  1.00 25.32 ?  157 ASP   B HB3  1 
ATOM   6547 N N    A LYS   B 1 158 ? 48.362 -37.518 -9.188  0.72 20.05 ?  158 LYS   B N    1 
ATOM   6548 N N    B LYS   B 1 158 ? 48.364 -37.492 -9.200  0.28 19.84 ?  158 LYS   B N    1 
ATOM   6549 C CA   A LYS   B 1 158 ? 47.581 -38.137 -10.261 0.72 21.34 ?  158 LYS   B CA   1 
ATOM   6550 C CA   B LYS   B 1 158 ? 47.582 -38.053 -10.301 0.28 21.03 ?  158 LYS   B CA   1 
ATOM   6551 C C    A LYS   B 1 158 ? 46.519 -39.092 -9.719  0.72 21.52 ?  158 LYS   B C    1 
ATOM   6552 C C    B LYS   B 1 158 ? 46.521 -39.026 -9.799  0.28 20.94 ?  158 LYS   B C    1 
ATOM   6553 O O    A LYS   B 1 158 ? 45.404 -39.166 -10.253 0.72 21.80 ?  158 LYS   B O    1 
ATOM   6554 O O    B LYS   B 1 158 ? 45.422 -39.105 -10.363 0.28 20.89 ?  158 LYS   B O    1 
ATOM   6555 C CB   A LYS   B 1 158 ? 48.526 -38.872 -11.220 0.72 23.43 ?  158 LYS   B CB   1 
ATOM   6556 C CB   B LYS   B 1 158 ? 48.524 -38.738 -11.298 0.28 22.64 ?  158 LYS   B CB   1 
ATOM   6557 C CG   A LYS   B 1 158 ? 47.840 -39.782 -12.228 0.72 25.74 ?  158 LYS   B CG   1 
ATOM   6558 C CG   B LYS   B 1 158 ? 47.849 -39.657 -12.312 0.28 24.24 ?  158 LYS   B CG   1 
ATOM   6559 C CD   A LYS   B 1 158 ? 47.012 -39.002 -13.226 0.72 27.91 ?  158 LYS   B CD   1 
ATOM   6560 C CD   B LYS   B 1 158 ? 46.958 -38.892 -13.273 0.28 25.81 ?  158 LYS   B CD   1 
ATOM   6561 C CE   A LYS   B 1 158 ? 46.385 -39.932 -14.251 0.72 29.60 ?  158 LYS   B CE   1 
ATOM   6562 C CE   B LYS   B 1 158 ? 46.375 -39.816 -14.331 0.28 27.05 ?  158 LYS   B CE   1 
ATOM   6563 N NZ   A LYS   B 1 158 ? 45.346 -39.240 -15.062 0.72 30.05 ?  158 LYS   B NZ   1 
ATOM   6564 N NZ   B LYS   B 1 158 ? 45.346 -39.135 -15.167 0.28 27.56 ?  158 LYS   B NZ   1 
ATOM   6565 H H    A LYS   B 1 158 ? 49.216 -37.610 -9.276  0.72 24.10 ?  158 LYS   B H    1 
ATOM   6566 H H    B LYS   B 1 158 ? 49.215 -37.597 -9.285  0.28 23.84 ?  158 LYS   B H    1 
ATOM   6567 H HA   A LYS   B 1 158 ? 47.135 -37.441 -10.765 0.72 25.64 ?  158 LYS   B HA   1 
ATOM   6568 H HA   B LYS   B 1 158 ? 47.130 -37.334 -10.767 0.28 25.28 ?  158 LYS   B HA   1 
ATOM   6569 H HB2  A LYS   B 1 158 ? 49.033 -38.213 -11.725 0.72 28.16 ?  158 LYS   B HB2  1 
ATOM   6570 H HB2  B LYS   B 1 158 ? 48.994 -38.052 -11.801 0.28 27.21 ?  158 LYS   B HB2  1 
ATOM   6571 H HB3  A LYS   B 1 158 ? 49.136 -39.418 -10.701 0.72 28.16 ?  158 LYS   B HB3  1 
ATOM   6572 H HB3  B LYS   B 1 158 ? 49.165 -39.272 -10.804 0.28 27.21 ?  158 LYS   B HB3  1 
ATOM   6573 H HG2  A LYS   B 1 158 ? 48.518 -40.266 -12.722 0.72 30.93 ?  158 LYS   B HG2  1 
ATOM   6574 H HG2  B LYS   B 1 158 ? 48.536 -40.098 -12.833 0.28 29.13 ?  158 LYS   B HG2  1 
ATOM   6575 H HG3  A LYS   B 1 158 ? 47.260 -40.413 -11.771 0.72 30.93 ?  158 LYS   B HG3  1 
ATOM   6576 H HG3  B LYS   B 1 158 ? 47.311 -40.322 -11.854 0.28 29.13 ?  158 LYS   B HG3  1 
ATOM   6577 H HD2  A LYS   B 1 158 ? 46.300 -38.535 -12.761 0.72 33.53 ?  158 LYS   B HD2  1 
ATOM   6578 H HD2  B LYS   B 1 158 ? 46.226 -38.489 -12.782 0.28 31.01 ?  158 LYS   B HD2  1 
ATOM   6579 H HD3  A LYS   B 1 158 ? 47.581 -38.371 -13.694 0.72 33.53 ?  158 LYS   B HD3  1 
ATOM   6580 H HD3  B LYS   B 1 158 ? 47.482 -38.208 -13.720 0.28 31.01 ?  158 LYS   B HD3  1 
ATOM   6581 H HE2  A LYS   B 1 158 ? 47.073 -40.254 -14.852 0.72 35.55 ?  158 LYS   B HE2  1 
ATOM   6582 H HE2  B LYS   B 1 158 ? 47.087 -40.119 -14.917 0.28 32.49 ?  158 LYS   B HE2  1 
ATOM   6583 H HE3  A LYS   B 1 158 ? 45.966 -40.678 -13.793 0.72 35.55 ?  158 LYS   B HE3  1 
ATOM   6584 H HE3  B LYS   B 1 158 ? 45.956 -40.576 -13.896 0.28 32.49 ?  158 LYS   B HE3  1 
ATOM   6585 H HZ1  A LYS   B 1 158 ? 44.995 -39.804 -15.653 0.72 36.10 ?  158 LYS   B HZ1  1 
ATOM   6586 H HZ1  B LYS   B 1 158 ? 45.025 -39.700 -15.775 0.28 33.12 ?  158 LYS   B HZ1  1 
ATOM   6587 H HZ2  A LYS   B 1 158 ? 44.699 -38.935 -14.532 0.72 36.10 ?  158 LYS   B HZ2  1 
ATOM   6588 H HZ2  B LYS   B 1 158 ? 44.677 -38.851 -14.653 0.28 33.12 ?  158 LYS   B HZ2  1 
ATOM   6589 H HZ3  A LYS   B 1 158 ? 45.709 -38.553 -15.498 0.72 36.10 ?  158 LYS   B HZ3  1 
ATOM   6590 H HZ3  B LYS   B 1 158 ? 45.707 -38.436 -15.584 0.28 33.12 ?  158 LYS   B HZ3  1 
ATOM   6591 N N    A ASN   B 1 159 ? 46.848 -39.852 -8.673  0.72 21.63 ?  159 ASN   B N    1 
ATOM   6592 N N    B ASN   B 1 159 ? 46.829 -39.782 -8.744  0.28 21.12 ?  159 ASN   B N    1 
ATOM   6593 C CA   A ASN   B 1 159 ? 45.890 -40.825 -8.159  0.72 22.12 ?  159 ASN   B CA   1 
ATOM   6594 C CA   B ASN   B 1 159 ? 45.877 -40.771 -8.248  0.28 21.29 ?  159 ASN   B CA   1 
ATOM   6595 C C    A ASN   B 1 159 ? 44.697 -40.142 -7.492  0.72 21.07 ?  159 ASN   B C    1 
ATOM   6596 C C    B ASN   B 1 159 ? 44.687 -40.106 -7.557  0.28 20.70 ?  159 ASN   B C    1 
ATOM   6597 O O    A ASN   B 1 159 ? 43.565 -40.639 -7.576  0.72 21.51 ?  159 ASN   B O    1 
ATOM   6598 O O    B ASN   B 1 159 ? 43.552 -40.586 -7.670  0.28 20.83 ?  159 ASN   B O    1 
ATOM   6599 C CB   A ASN   B 1 159 ? 46.588 -41.795 -7.208  0.72 23.82 ?  159 ASN   B CB   1 
ATOM   6600 C CB   B ASN   B 1 159 ? 46.584 -41.763 -7.325  0.28 22.13 ?  159 ASN   B CB   1 
ATOM   6601 C CG   A ASN   B 1 159 ? 47.617 -42.657 -7.911  0.72 25.70 ?  159 ASN   B CG   1 
ATOM   6602 C CG   B ASN   B 1 159 ? 47.600 -42.618 -8.061  0.28 22.95 ?  159 ASN   B CG   1 
ATOM   6603 O OD1  A ASN   B 1 159 ? 47.377 -43.152 -9.018  0.72 26.97 ?  159 ASN   B OD1  1 
ATOM   6604 O OD1  B ASN   B 1 159 ? 47.361 -43.050 -9.190  0.28 23.38 ?  159 ASN   B OD1  1 
ATOM   6605 N ND2  A ASN   B 1 159 ? 48.772 -42.843 -7.273  0.72 26.54 ?  159 ASN   B ND2  1 
ATOM   6606 N ND2  B ASN   B 1 159 ? 48.744 -42.863 -7.425  0.28 23.50 ?  159 ASN   B ND2  1 
ATOM   6607 H H    A ASN   B 1 159 ? 47.591 -39.809 -8.249  0.72 25.99 ?  159 ASN   B H    1 
ATOM   6608 H H    B ASN   B 1 159 ? 47.569 -39.743 -8.309  0.28 25.38 ?  159 ASN   B H    1 
ATOM   6609 H HA   A ASN   B 1 159 ? 45.557 -41.345 -8.910  0.72 26.59 ?  159 ASN   B HA   1 
ATOM   6610 H HA   B ASN   B 1 159 ? 45.536 -41.276 -9.005  0.28 25.58 ?  159 ASN   B HA   1 
ATOM   6611 H HB2  A ASN   B 1 159 ? 47.044 -41.293 -6.517  0.72 28.62 ?  159 ASN   B HB2  1 
ATOM   6612 H HB2  B ASN   B 1 159 ? 47.052 -41.277 -6.630  0.28 26.60 ?  159 ASN   B HB2  1 
ATOM   6613 H HB3  A ASN   B 1 159 ? 45.928 -42.385 -6.817  0.72 28.62 ?  159 ASN   B HB3  1 
ATOM   6614 H HB3  B ASN   B 1 159 ? 45.926 -42.358 -6.932  0.28 26.60 ?  159 ASN   B HB3  1 
ATOM   6615 H HD21 A ASN   B 1 159 ? 49.391 -43.330 -7.625  0.72 31.88 ?  159 ASN   B HD21 1 
ATOM   6616 H HD21 B ASN   B 1 159 ? 49.353 -43.345 -7.799  0.28 28.24 ?  159 ASN   B HD21 1 
ATOM   6617 H HD22 A ASN   B 1 159 ? 48.896 -42.494 -6.496  0.72 31.88 ?  159 ASN   B HD22 1 
ATOM   6618 H HD22 B ASN   B 1 159 ? 48.874 -42.547 -6.636  0.28 28.24 ?  159 ASN   B HD22 1 
ATOM   6619 N N    . LEU   B 1 160 ? 44.917 -38.999 -6.843  1.00 20.26 ?  160 LEU   B N    1 
ATOM   6620 C CA   . LEU   B 1 160 ? 43.796 -38.256 -6.279  1.00 19.27 ?  160 LEU   B CA   1 
ATOM   6621 C C    . LEU   B 1 160 ? 42.998 -37.589 -7.386  1.00 18.72 ?  160 LEU   B C    1 
ATOM   6622 O O    . LEU   B 1 160 ? 41.760 -37.588 -7.352  1.00 18.55 ?  160 LEU   B O    1 
ATOM   6623 C CB   . LEU   B 1 160 ? 44.274 -37.228 -5.254  1.00 18.72 ?  160 LEU   B CB   1 
ATOM   6624 C CG   . LEU   B 1 160 ? 43.154 -36.318 -4.726  1.00 18.19 ?  160 LEU   B CG   1 
ATOM   6625 C CD1  . LEU   B 1 160 ? 42.031 -37.139 -4.106  1.00 19.11 ?  160 LEU   B CD1  1 
ATOM   6626 C CD2  . LEU   B 1 160 ? 43.691 -35.301 -3.728  1.00 18.41 ?  160 LEU   B CD2  1 
ATOM   6627 H H    A LEU   B 1 160 ? 45.691 -38.644 -6.724  0.72 24.35 ?  160 LEU   B H    1 
ATOM   6628 H H    B LEU   B 1 160 ? 45.694 -38.667 -6.687  0.28 24.35 ?  160 LEU   B H    1 
ATOM   6629 H HA   . LEU   B 1 160 ? 43.211 -38.882 -5.828  1.00 23.16 ?  160 LEU   B HA   1 
ATOM   6630 H HB2  . LEU   B 1 160 ? 44.664 -37.704 -4.500  1.00 22.50 ?  160 LEU   B HB2  1 
ATOM   6631 H HB3  . LEU   B 1 160 ? 44.953 -36.669 -5.669  1.00 22.50 ?  160 LEU   B HB3  1 
ATOM   6632 H HG   . LEU   B 1 160 ? 42.781 -35.826 -5.471  1.00 21.87 ?  160 LEU   B HG   1 
ATOM   6633 H HD11 . LEU   B 1 160 ? 41.413 -36.540 -3.667  1.00 22.96 ?  160 LEU   B HD11 1 
ATOM   6634 H HD12 . LEU   B 1 160 ? 41.573 -37.636 -4.804  1.00 22.96 ?  160 LEU   B HD12 1 
ATOM   6635 H HD13 . LEU   B 1 160 ? 42.410 -37.758 -3.458  1.00 22.96 ?  160 LEU   B HD13 1 
ATOM   6636 H HD21 . LEU   B 1 160 ? 42.965 -34.725 -3.449  1.00 22.12 ?  160 LEU   B HD21 1 
ATOM   6637 H HD22 . LEU   B 1 160 ? 44.059 -35.770 -2.964  1.00 22.12 ?  160 LEU   B HD22 1 
ATOM   6638 H HD23 . LEU   B 1 160 ? 44.385 -34.774 -4.158  1.00 22.12 ?  160 LEU   B HD23 1 
ATOM   6639 N N    A TYR   B 1 161 ? 43.691 -37.021 -8.378  0.72 18.67 ?  161 TYR   B N    1 
ATOM   6640 N N    B TYR   B 1 161 ? 43.686 -37.033 -8.389  0.28 18.40 ?  161 TYR   B N    1 
ATOM   6641 C CA   A TYR   B 1 161 ? 43.014 -36.460 -9.542  0.72 18.49 ?  161 TYR   B CA   1 
ATOM   6642 C CA   B TYR   B 1 161 ? 42.994 -36.457 -9.539  0.28 18.16 ?  161 TYR   B CA   1 
ATOM   6643 C C    A TYR   B 1 161 ? 42.059 -37.480 -10.151 0.72 18.35 ?  161 TYR   B C    1 
ATOM   6644 C C    B TYR   B 1 161 ? 42.057 -37.477 -10.174 0.28 18.17 ?  161 TYR   B C    1 
ATOM   6645 O O    A TYR   B 1 161 ? 40.886 -37.181 -10.396 0.72 18.01 ?  161 TYR   B O    1 
ATOM   6646 O O    B TYR   B 1 161 ? 40.897 -37.172 -10.472 0.28 17.80 ?  161 TYR   B O    1 
ATOM   6647 C CB   A TYR   B 1 161 ? 44.053 -36.001 -10.574 0.72 18.73 ?  161 TYR   B CB   1 
ATOM   6648 C CB   B TYR   B 1 161 ? 44.017 -35.950 -10.562 0.28 18.20 ?  161 TYR   B CB   1 
ATOM   6649 C CG   A TYR   B 1 161 ? 43.469 -35.523 -11.886 0.72 19.30 ?  161 TYR   B CG   1 
ATOM   6650 C CG   B TYR   B 1 161 ? 43.410 -35.481 -11.871 0.28 18.52 ?  161 TYR   B CG   1 
ATOM   6651 C CD1  A TYR   B 1 161 ? 43.085 -34.197 -12.049 0.72 19.08 ?  161 TYR   B CD1  1 
ATOM   6652 C CD1  B TYR   B 1 161 ? 42.992 -34.165 -12.032 0.28 18.52 ?  161 TYR   B CD1  1 
ATOM   6653 C CD2  A TYR   B 1 161 ? 43.293 -36.395 -12.958 0.72 20.01 ?  161 TYR   B CD2  1 
ATOM   6654 C CD2  B TYR   B 1 161 ? 43.257 -36.352 -12.944 0.28 18.83 ?  161 TYR   B CD2  1 
ATOM   6655 C CE1  A TYR   B 1 161 ? 42.550 -33.752 -13.237 0.72 20.13 ?  161 TYR   B CE1  1 
ATOM   6656 C CE1  B TYR   B 1 161 ? 42.437 -33.731 -13.221 0.28 19.01 ?  161 TYR   B CE1  1 
ATOM   6657 C CE2  A TYR   B 1 161 ? 42.753 -35.957 -14.150 0.72 21.01 ?  161 TYR   B CE2  1 
ATOM   6658 C CE2  B TYR   B 1 161 ? 42.701 -35.927 -14.137 0.28 19.32 ?  161 TYR   B CE2  1 
ATOM   6659 C CZ   A TYR   B 1 161 ? 42.383 -34.636 -14.284 0.72 21.08 ?  161 TYR   B CZ   1 
ATOM   6660 C CZ   B TYR   B 1 161 ? 42.294 -34.615 -14.270 0.28 19.47 ?  161 TYR   B CZ   1 
ATOM   6661 O OH   A TYR   B 1 161 ? 41.845 -34.189 -15.466 0.72 23.24 ?  161 TYR   B OH   1 
ATOM   6662 O OH   B TYR   B 1 161 ? 41.739 -34.187 -15.455 0.28 20.52 ?  161 TYR   B OH   1 
ATOM   6663 H H    A TYR   B 1 161 ? 44.545 -36.967 -8.407  0.72 22.44 ?  161 TYR   B H    1 
ATOM   6664 H H    B TYR   B 1 161 ? 44.542 -36.984 -8.428  0.28 22.11 ?  161 TYR   B H    1 
ATOM   6665 H HA   A TYR   B 1 161 ? 42.495 -35.690 -9.269  0.72 22.23 ?  161 TYR   B HA   1 
ATOM   6666 H HA   B TYR   B 1 161 ? 42.462 -35.703 -9.245  0.28 21.83 ?  161 TYR   B HA   1 
ATOM   6667 H HB2  A TYR   B 1 161 ? 44.561 -35.268 -10.194 0.72 22.51 ?  161 TYR   B HB2  1 
ATOM   6668 H HB2  B TYR   B 1 161 ? 44.497 -35.201 -10.176 0.28 21.88 ?  161 TYR   B HB2  1 
ATOM   6669 H HB3  A TYR   B 1 161 ? 44.645 -36.743 -10.771 0.72 22.51 ?  161 TYR   B HB3  1 
ATOM   6670 H HB3  B TYR   B 1 161 ? 44.636 -36.667 -10.766 0.28 21.88 ?  161 TYR   B HB3  1 
ATOM   6671 H HD1  A TYR   B 1 161 ? 43.195 -33.596 -11.346 0.72 22.93 ?  161 TYR   B HD1  1 
ATOM   6672 H HD1  B TYR   B 1 161 ? 43.086 -33.564 -11.327 0.28 22.27 ?  161 TYR   B HD1  1 
ATOM   6673 H HD2  A TYR   B 1 161 ? 43.535 -37.286 -12.871 0.72 24.06 ?  161 TYR   B HD2  1 
ATOM   6674 H HD2  B TYR   B 1 161 ? 43.528 -37.237 -12.859 0.28 22.64 ?  161 TYR   B HD2  1 
ATOM   6675 H HE1  A TYR   B 1 161 ? 42.298 -32.857 -13.328 0.72 24.19 ?  161 TYR   B HE1  1 
ATOM   6676 H HE1  B TYR   B 1 161 ? 42.161 -32.846 -13.313 0.28 22.86 ?  161 TYR   B HE1  1 
ATOM   6677 H HE2  A TYR   B 1 161 ? 42.635 -36.544 -14.860 0.72 25.24 ?  161 TYR   B HE2  1 
ATOM   6678 H HE2  B TYR   B 1 161 ? 42.603 -36.520 -14.846 0.28 23.22 ?  161 TYR   B HE2  1 
ATOM   6679 H HH   A TYR   B 1 161 ? 41.799 -34.818 -16.019 0.72 27.92 ?  161 TYR   B HH   1 
ATOM   6680 H HH   B TYR   B 1 161 ? 41.712 -34.821 -16.005 0.28 24.66 ?  161 TYR   B HH   1 
ATOM   6681 N N    . ASP   B 1 162 ? 42.544 -38.703 -10.382 1.00 18.73 ?  162 ASP   B N    1 
ATOM   6682 C CA   . ASP   B 1 162 ? 41.705 -39.738 -10.978 1.00 19.62 ?  162 ASP   B CA   1 
ATOM   6683 C C    . ASP   B 1 162 ? 40.510 -40.065 -10.091 1.00 19.10 ?  162 ASP   B C    1 
ATOM   6684 O O    . ASP   B 1 162 ? 39.398 -40.273 -10.591 1.00 19.52 ?  162 ASP   B O    1 
ATOM   6685 C CB   . ASP   B 1 162 ? 42.527 -41.004 -11.228 1.00 21.12 ?  162 ASP   B CB   1 
ATOM   6686 C CG   . ASP   B 1 162 ? 43.544 -40.848 -12.342 1.00 22.60 ?  162 ASP   B CG   1 
ATOM   6687 O OD1  . ASP   B 1 162 ? 43.426 -39.915 -13.158 1.00 22.93 ?  162 ASP   B OD1  1 
ATOM   6688 O OD2  . ASP   B 1 162 ? 44.452 -41.704 -12.424 1.00 24.10 -1 162 ASP   B OD2  1 
ATOM   6689 H H    A ASP   B 1 162 ? 43.346 -38.952 -10.206 0.72 22.52 ?  162 ASP   B H    1 
ATOM   6690 H H    B ASP   B 1 162 ? 43.342 -38.954 -10.191 0.28 22.52 ?  162 ASP   B H    1 
ATOM   6691 H HA   . ASP   B 1 162 ? 41.366 -39.422 -11.829 1.00 23.58 ?  162 ASP   B HA   1 
ATOM   6692 H HB2  . ASP   B 1 162 ? 43.013 -41.230 -10.423 1.00 25.38 ?  162 ASP   B HB2  1 
ATOM   6693 H HB3  . ASP   B 1 162 ? 41.927 -41.725 -11.473 1.00 25.38 ?  162 ASP   B HB3  1 
ATOM   6694 N N    . LYS   B 1 163 ? 40.719 -40.140 -8.774  1.00 18.27 ?  163 LYS   B N    1 
ATOM   6695 C CA   . LYS   B 1 163 ? 39.602 -40.414 -7.874  1.00 19.36 ?  163 LYS   B CA   1 
ATOM   6696 C C    . LYS   B 1 163 ? 38.561 -39.300 -7.928  1.00 17.70 ?  163 LYS   B C    1 
ATOM   6697 O O    . LYS   B 1 163 ? 37.348 -39.564 -7.912  1.00 18.26 ?  163 LYS   B O    1 
ATOM   6698 C CB   . LYS   B 1 163 ? 40.106 -40.601 -6.444  1.00 23.02 ?  163 LYS   B CB   1 
ATOM   6699 C CG   . LYS   B 1 163 ? 39.035 -41.107 -5.497  1.00 29.02 ?  163 LYS   B CG   1 
ATOM   6700 C CD   . LYS   B 1 163 ? 39.561 -41.306 -4.087  1.00 34.57 ?  163 LYS   B CD   1 
ATOM   6701 C CE   . LYS   B 1 163 ? 38.487 -41.919 -3.199  1.00 38.52 ?  163 LYS   B CE   1 
ATOM   6702 N NZ   . LYS   B 1 163 ? 38.768 -41.735 -1.749  1.00 42.02 ?  163 LYS   B NZ   1 
ATOM   6703 H H    . LYS   B 1 163 ? 41.484 -40.040 -8.387  1.00 21.96 ?  163 LYS   B H    1 
ATOM   6704 H HA   . LYS   B 1 163 ? 39.173 -41.234 -8.149  1.00 23.28 ?  163 LYS   B HA   1 
ATOM   6705 H HB2  . LYS   B 1 163 ? 40.830 -41.248 -6.447  1.00 27.66 ?  163 LYS   B HB2  1 
ATOM   6706 H HB3  . LYS   B 1 163 ? 40.424 -39.750 -6.105  1.00 27.66 ?  163 LYS   B HB3  1 
ATOM   6707 H HG2  . LYS   B 1 163 ? 38.312 -40.463 -5.459  1.00 34.86 ?  163 LYS   B HG2  1 
ATOM   6708 H HG3  . LYS   B 1 163 ? 38.704 -41.961 -5.819  1.00 34.86 ?  163 LYS   B HG3  1 
ATOM   6709 H HD2  . LYS   B 1 163 ? 40.322 -41.910 -4.109  1.00 41.52 ?  163 LYS   B HD2  1 
ATOM   6710 H HD3  . LYS   B 1 163 ? 39.819 -40.450 -3.714  1.00 41.52 ?  163 LYS   B HD3  1 
ATOM   6711 H HE2  . LYS   B 1 163 ? 37.633 -41.507 -3.399  1.00 46.26 ?  163 LYS   B HE2  1 
ATOM   6712 H HE3  . LYS   B 1 163 ? 38.440 -42.870 -3.376  1.00 46.26 ?  163 LYS   B HE3  1 
ATOM   6713 H HZ1  . LYS   B 1 163 ? 38.118 -42.104 -1.266  1.00 50.46 ?  163 LYS   B HZ1  1 
ATOM   6714 H HZ2  . LYS   B 1 163 ? 39.540 -42.122 -1.539  1.00 50.46 ?  163 LYS   B HZ2  1 
ATOM   6715 H HZ3  . LYS   B 1 163 ? 38.815 -40.868 -1.556  1.00 50.46 ?  163 LYS   B HZ3  1 
ATOM   6716 N N    . LEU   B 1 164 ? 39.021 -38.045 -7.988  1.00 16.50 ?  164 LEU   B N    1 
ATOM   6717 C CA   . LEU   B 1 164 ? 38.113 -36.906 -8.044  1.00 16.20 ?  164 LEU   B CA   1 
ATOM   6718 C C    . LEU   B 1 164 ? 37.317 -36.893 -9.346  1.00 16.87 ?  164 LEU   B C    1 
ATOM   6719 O O    . LEU   B 1 164 ? 36.092 -36.697 -9.336  1.00 17.94 ?  164 LEU   B O    1 
ATOM   6720 C CB   . LEU   B 1 164 ? 38.915 -35.613 -7.891  1.00 15.62 ?  164 LEU   B CB   1 
ATOM   6721 C CG   . LEU   B 1 164 ? 39.464 -35.341 -6.493  1.00 16.35 ?  164 LEU   B CG   1 
ATOM   6722 C CD1  . LEU   B 1 164 ? 40.544 -34.273 -6.557  1.00 16.51 ?  164 LEU   B CD1  1 
ATOM   6723 C CD2  . LEU   B 1 164 ? 38.357 -34.911 -5.550  1.00 17.83 ?  164 LEU   B CD2  1 
ATOM   6724 H H    . LEU   B 1 164 ? 39.859 -37.828 -8.000  1.00 19.84 ?  164 LEU   B H    1 
ATOM   6725 H HA   . LEU   B 1 164 ? 37.489 -36.959 -7.312  1.00 19.48 ?  164 LEU   B HA   1 
ATOM   6726 H HB2  . LEU   B 1 164 ? 39.677 -35.647 -8.499  1.00 18.78 ?  164 LEU   B HB2  1 
ATOM   6727 H HB3  . LEU   B 1 164 ? 38.350 -34.865 -8.130  1.00 18.78 ?  164 LEU   B HB3  1 
ATOM   6728 H HG   . LEU   B 1 164 ? 39.868 -36.151 -6.146  1.00 19.66 ?  164 LEU   B HG   1 
ATOM   6729 H HD11 . LEU   B 1 164 ? 40.880 -34.104 -5.660  1.00 19.85 ?  164 LEU   B HD11 1 
ATOM   6730 H HD12 . LEU   B 1 164 ? 41.273 -34.585 -7.123  1.00 19.85 ?  164 LEU   B HD12 1 
ATOM   6731 H HD13 . LEU   B 1 164 ? 40.169 -33.459 -6.926  1.00 19.85 ?  164 LEU   B HD13 1 
ATOM   6732 H HD21 . LEU   B 1 164 ? 38.742 -34.693 -4.689  1.00 21.43 ?  164 LEU   B HD21 1 
ATOM   6733 H HD22 . LEU   B 1 164 ? 37.909 -34.138 -5.922  1.00 21.43 ?  164 LEU   B HD22 1 
ATOM   6734 H HD23 . LEU   B 1 164 ? 37.727 -35.645 -5.455  1.00 21.43 ?  164 LEU   B HD23 1 
ATOM   6735 N N    . VAL   B 1 165 ? 37.998 -37.066 -10.480 1.00 18.76 ?  165 VAL   B N    1 
ATOM   6736 C CA   . VAL   B 1 165 ? 37.327 -37.003 -11.775 1.00 20.56 ?  165 VAL   B CA   1 
ATOM   6737 C C    . VAL   B 1 165 ? 36.396 -38.195 -11.945 1.00 22.59 ?  165 VAL   B C    1 
ATOM   6738 O O    . VAL   B 1 165 ? 35.225 -38.050 -12.322 1.00 23.94 ?  165 VAL   B O    1 
ATOM   6739 C CB   . VAL   B 1 165 ? 38.363 -36.936 -12.912 1.00 21.23 ?  165 VAL   B CB   1 
ATOM   6740 C CG1  . VAL   B 1 165 ? 37.687 -37.081 -14.252 1.00 22.46 ?  165 VAL   B CG1  1 
ATOM   6741 C CG2  . VAL   B 1 165 ? 39.148 -35.636 -12.847 1.00 20.66 ?  165 VAL   B CG2  1 
ATOM   6742 H H    . VAL   B 1 165 ? 38.849 -37.213 -10.527 1.00 22.55 ?  165 VAL   B H    1 
ATOM   6743 H HA   . VAL   B 1 165 ? 36.795 -36.196 -11.815 1.00 24.71 ?  165 VAL   B HA   1 
ATOM   6744 H HB   . VAL   B 1 165 ? 38.997 -37.664 -12.811 1.00 25.51 ?  165 VAL   B HB   1 
ATOM   6745 H HG11 . VAL   B 1 165 ? 38.278 -36.759 -14.944 1.00 26.99 ?  165 VAL   B HG11 1 
ATOM   6746 H HG12 . VAL   B 1 165 ? 37.495 -38.024 -14.399 1.00 26.99 ?  165 VAL   B HG12 1 
ATOM   6747 H HG13 . VAL   B 1 165 ? 36.863 -36.575 -14.247 1.00 26.99 ?  165 VAL   B HG13 1 
ATOM   6748 H HG21 . VAL   B 1 165 ? 39.766 -35.598 -13.597 1.00 24.83 ?  165 VAL   B HG21 1 
ATOM   6749 H HG22 . VAL   B 1 165 ? 38.529 -34.888 -12.897 1.00 24.83 ?  165 VAL   B HG22 1 
ATOM   6750 H HG23 . VAL   B 1 165 ? 39.641 -35.599 -12.013 1.00 24.83 ?  165 VAL   B HG23 1 
ATOM   6751 N N    . SER   B 1 166 ? 36.912 -39.397 -11.670 1.00 23.54 ?  166 SER   B N    1 
ATOM   6752 C CA   . SER   B 1 166 ? 36.155 -40.603 -11.959 1.00 25.08 ?  166 SER   B CA   1 
ATOM   6753 C C    . SER   B 1 166 ? 34.905 -40.691 -11.099 1.00 25.59 ?  166 SER   B C    1 
ATOM   6754 O O    . SER   B 1 166 ? 33.934 -41.321 -11.509 1.00 27.13 ?  166 SER   B O    1 
ATOM   6755 C CB   . SER   B 1 166 ? 37.026 -41.856 -11.806 1.00 25.95 ?  166 SER   B CB   1 
ATOM   6756 O OG   . SER   B 1 166 ? 37.399 -42.075 -10.456 1.00 26.10 ?  166 SER   B OG   1 
ATOM   6757 H H    . SER   B 1 166 ? 37.689 -39.534 -11.321 1.00 28.29 ?  166 SER   B H    1 
ATOM   6758 H HA   . SER   B 1 166 ? 35.870 -40.570 -12.885 1.00 30.13 ?  166 SER   B HA   1 
ATOM   6759 H HB2  . SER   B 1 166 ? 36.527 -42.627 -12.120 1.00 31.17 ?  166 SER   B HB2  1 
ATOM   6760 H HB3  . SER   B 1 166 ? 37.828 -41.748 -12.347 1.00 31.17 ?  166 SER   B HB3  1 
ATOM   6761 H HG   . SER   B 1 166 ? 37.853 -41.422 -10.178 1.00 31.36 ?  166 SER   B HG   1 
ATOM   6762 N N    . SER   B 1 167 ? 34.890 -40.066 -9.926  1.00 23.72 ?  167 SER   B N    1 
ATOM   6763 C CA   . SER   B 1 167 ? 33.740 -40.128 -9.033  1.00 23.13 ?  167 SER   B CA   1 
ATOM   6764 C C    . SER   B 1 167 ? 32.824 -38.904 -9.115  1.00 22.42 ?  167 SER   B C    1 
ATOM   6765 O O    . SER   B 1 167 ? 31.745 -38.916 -8.514  1.00 22.72 ?  167 SER   B O    1 
ATOM   6766 C CB   . SER   B 1 167 ? 34.200 -40.333 -7.583  1.00 22.79 ?  167 SER   B CB   1 
ATOM   6767 O OG   . SER   B 1 167 ? 34.870 -39.176 -7.094  1.00 22.83 ?  167 SER   B OG   1 
ATOM   6768 H H    . SER   B 1 167 ? 35.537 -39.600 -9.631  1.00 28.51 ?  167 SER   B H    1 
ATOM   6769 H HA   . SER   B 1 167 ? 33.205 -40.904 -9.281  1.00 27.79 ?  167 SER   B HA   1 
ATOM   6770 H HB2  . SER   B 1 167 ? 33.418 -40.518 -7.035  1.00 27.38 ?  167 SER   B HB2  1 
ATOM   6771 H HB3  . SER   B 1 167 ? 34.800 -41.103 -7.554  1.00 27.38 ?  167 SER   B HB3  1 
ATOM   6772 H HG   . SER   B 1 167 ? 35.545 -39.035 -7.561  1.00 27.44 ?  167 SER   B HG   1 
ATOM   6773 N N    . PHE   B 1 168 ? 33.207 -37.852 -9.843  1.00 22.00 ?  168 PHE   B N    1 
ATOM   6774 C CA   . PHE   B 1 168 ? 32.368 -36.652 -9.903  1.00 20.78 ?  168 PHE   B CA   1 
ATOM   6775 C C    . PHE   B 1 168 ? 31.068 -36.914 -10.659 1.00 17.88 ?  168 PHE   B C    1 
ATOM   6776 O O    . PHE   B 1 168 ? 30.012 -36.336 -10.327 1.00 18.05 ?  168 PHE   B O    1 
ATOM   6777 C CB   . PHE   B 1 168 ? 33.137 -35.504 -10.556 1.00 21.29 ?  168 PHE   B CB   1 
ATOM   6778 C CG   . PHE   B 1 168 ? 32.320 -34.266 -10.727 1.00 21.41 ?  168 PHE   B CG   1 
ATOM   6779 C CD1  . PHE   B 1 168 ? 31.941 -33.520 -9.621  1.00 22.21 ?  168 PHE   B CD1  1 
ATOM   6780 C CD2  . PHE   B 1 168 ? 31.910 -33.854 -11.980 1.00 20.83 ?  168 PHE   B CD2  1 
ATOM   6781 C CE1  . PHE   B 1 168 ? 31.172 -32.381 -9.760  1.00 22.14 ?  168 PHE   B CE1  1 
ATOM   6782 C CE2  . PHE   B 1 168 ? 31.150 -32.702 -12.132 1.00 21.85 ?  168 PHE   B CE2  1 
ATOM   6783 C CZ   . PHE   B 1 168 ? 30.772 -31.969 -11.018 1.00 21.74 ?  168 PHE   B CZ   1 
ATOM   6784 H H    . PHE   B 1 168 ? 33.934 -37.805 -10.299 1.00 26.44 ?  168 PHE   B H    1 
ATOM   6785 H HA   . PHE   B 1 168 ? 32.133 -36.387 -9.004  1.00 24.98 ?  168 PHE   B HA   1 
ATOM   6786 H HB2  . PHE   B 1 168 ? 33.896 -35.283 -10.000 1.00 25.58 ?  168 PHE   B HB2  1 
ATOM   6787 H HB3  . PHE   B 1 168 ? 33.435 -35.783 -11.435 1.00 25.58 ?  168 PHE   B HB3  1 
ATOM   6788 H HD1  . PHE   B 1 168 ? 32.201 -33.799 -8.775  1.00 26.69 ?  168 PHE   B HD1  1 
ATOM   6789 H HD2  . PHE   B 1 168 ? 32.155 -34.339 -12.732 1.00 25.04 ?  168 PHE   B HD2  1 
ATOM   6790 H HE1  . PHE   B 1 168 ? 30.925 -31.896 -9.009  1.00 26.60 ?  168 PHE   B HE1  1 
ATOM   6791 H HE2  . PHE   B 1 168 ? 30.877 -32.431 -12.982 1.00 26.26 ?  168 PHE   B HE2  1 
ATOM   6792 H HZ   . PHE   B 1 168 ? 30.256 -31.200 -11.118 1.00 26.13 ?  168 PHE   B HZ   1 
ATOM   6793 N N    . LEU   B 1 169 ? 31.126 -37.783 -11.667 1.00 18.52 ?  169 LEU   B N    1 
ATOM   6794 C CA   . LEU   B 1 169 ? 29.961 -38.122 -12.474 1.00 21.20 ?  169 LEU   B CA   1 
ATOM   6795 C C    . LEU   B 1 169 ? 29.964 -39.570 -12.946 1.00 24.26 ?  169 LEU   B C    1 
ATOM   6796 O O    . LEU   B 1 169 ? 29.074 -39.995 -13.687 1.00 26.58 ?  169 LEU   B O    1 
ATOM   6797 C CB   . LEU   B 1 169 ? 29.894 -37.212 -13.697 1.00 23.10 ?  169 LEU   B CB   1 
ATOM   6798 C CG   . LEU   B 1 169 ? 28.654 -36.327 -13.804 1.00 25.94 ?  169 LEU   B CG   1 
ATOM   6799 C CD1  . LEU   B 1 169 ? 28.585 -35.715 -15.184 1.00 26.72 ?  169 LEU   B CD1  1 
ATOM   6800 C CD2  . LEU   B 1 169 ? 27.388 -37.112 -13.499 1.00 26.09 ?  169 LEU   B CD2  1 
ATOM   6801 O OXT  . LEU   B 1 169 ? 30.852 -40.345 -12.610 1.00 25.36 -1 169 LEU   B OXT  1 
ATOM   6802 H H    . LEU   B 1 169 ? 31.842 -38.189 -11.914 1.00 22.26 ?  169 LEU   B H    1 
ATOM   6803 H HA   . LEU   B 1 169 ? 29.171 -37.981 -11.937 1.00 25.48 ?  169 LEU   B HA   1 
ATOM   6804 H HB2  . LEU   B 1 169 ? 30.664 -36.622 -13.690 1.00 27.76 ?  169 LEU   B HB2  1 
ATOM   6805 H HB3  . LEU   B 1 169 ? 29.917 -37.763 -14.496 1.00 27.76 ?  169 LEU   B HB3  1 
ATOM   6806 H HG   . LEU   B 1 169 ? 28.720 -35.603 -13.159 1.00 31.16 ?  169 LEU   B HG   1 
ATOM   6807 H HD11 . LEU   B 1 169 ? 27.812 -35.132 -15.233 1.00 32.10 ?  169 LEU   B HD11 1 
ATOM   6808 H HD12 . LEU   B 1 169 ? 29.395 -35.207 -15.341 1.00 32.10 ?  169 LEU   B HD12 1 
ATOM   6809 H HD13 . LEU   B 1 169 ? 28.507 -36.427 -15.837 1.00 32.10 ?  169 LEU   B HD13 1 
ATOM   6810 H HD21 . LEU   B 1 169 ? 26.640 -36.701 -13.954 1.00 31.35 ?  169 LEU   B HD21 1 
ATOM   6811 H HD22 . LEU   B 1 169 ? 27.505 -38.026 -13.810 1.00 31.35 ?  169 LEU   B HD22 1 
ATOM   6812 H HD23 . LEU   B 1 169 ? 27.238 -37.109 -12.541 1.00 31.35 ?  169 LEU   B HD23 1 
HETATM 6813 N N2   B A1BBN C 2 .   ? 15.532 3.580   6.169   0.28 15.92 ?  201 A1BBN A N2   1 
HETATM 6814 C C3   B A1BBN C 2 .   ? 15.207 1.324   3.462   0.28 18.93 ?  201 A1BBN A C3   1 
HETATM 6815 C C6   B A1BBN C 2 .   ? 15.679 4.526   5.172   0.28 14.54 ?  201 A1BBN A C6   1 
HETATM 6816 C C9   B A1BBN C 2 .   ? 13.771 -1.287  -0.290  0.28 23.96 ?  201 A1BBN A C9   1 
HETATM 6817 C C12  B A1BBN C 2 .   ? 12.128 0.553   1.443   0.28 24.13 ?  201 A1BBN A C12  1 
HETATM 6818 C C14  B A1BBN C 2 .   ? 12.100 0.984   -0.987  0.28 24.17 ?  201 A1BBN A C14  1 
HETATM 6819 C C1   B A1BBN C 2 .   ? 14.247 0.143   0.118   0.28 23.73 ?  201 A1BBN A C1   1 
HETATM 6820 C C10  B A1BBN C 2 .   ? 12.234 -1.410  -0.168  0.28 24.07 ?  201 A1BBN A C10  1 
HETATM 6821 C C11  B A1BBN C 2 .   ? 11.783 -0.944  1.236   0.28 24.01 ?  201 A1BBN A C11  1 
HETATM 6822 C C13  B A1BBN C 2 .   ? 12.996 1.068   0.273   0.28 24.09 ?  201 A1BBN A C13  1 
HETATM 6823 C C15  B A1BBN C 2 .   ? 11.592 -0.464  -1.203  0.28 24.05 ?  201 A1BBN A C15  1 
HETATM 6824 C C2   B A1BBN C 2 .   ? 15.132 0.050   1.371   0.28 22.45 ?  201 A1BBN A C2   1 
HETATM 6825 C C4   B A1BBN C 2 .   ? 15.383 2.513   4.209   0.28 17.17 ?  201 A1BBN A C4   1 
HETATM 6826 C C5   B A1BBN C 2 .   ? 15.605 3.908   3.950   0.28 16.02 ?  201 A1BBN A C5   1 
HETATM 6827 C C7   B A1BBN C 2 .   ? 15.341 2.335   5.612   0.28 16.73 ?  201 A1BBN A C7   1 
HETATM 6828 C C8   B A1BBN C 2 .   ? 15.009 0.123   5.436   0.28 18.18 ?  201 A1BBN A C8   1 
HETATM 6829 N N1   B A1BBN C 2 .   ? 15.222 1.321   2.070   0.28 20.75 ?  201 A1BBN A N1   1 
HETATM 6830 N N3   B A1BBN C 2 .   ? 15.150 1.158   6.257   0.28 17.19 ?  201 A1BBN A N3   1 
HETATM 6831 N N4   B A1BBN C 2 .   ? 15.023 0.148   4.112   0.28 18.51 ?  201 A1BBN A N4   1 
HETATM 6832 O O1   B A1BBN C 2 .   ? 15.136 0.659   -0.851  0.28 24.05 ?  201 A1BBN A O1   1 
HETATM 6833 H H7   B A1BBN C 2 .   ? 15.546 3.805   7.153   0.28 19.14 ?  201 A1BBN A H7   1 
HETATM 6834 H H6   B A1BBN C 2 .   ? 15.832 5.565   5.416   0.28 17.49 ?  201 A1BBN A H6   1 
HETATM 6835 H H10  B A1BBN C 2 .   ? 14.064 -1.520  -1.311  0.28 28.80 ?  201 A1BBN A H10  1 
HETATM 6836 H H9   B A1BBN C 2 .   ? 14.242 -2.064  0.317   0.28 28.80 ?  201 A1BBN A H9   1 
HETATM 6837 H H15  B A1BBN C 2 .   ? 11.217 1.147   1.551   0.28 29.00 ?  201 A1BBN A H15  1 
HETATM 6838 H H14  B A1BBN C 2 .   ? 12.672 0.672   2.377   0.28 29.00 ?  201 A1BBN A H14  1 
HETATM 6839 H H17  B A1BBN C 2 .   ? 11.248 1.652   -0.875  0.28 29.04 ?  201 A1BBN A H17  1 
HETATM 6840 H H18  B A1BBN C 2 .   ? 12.636 1.341   -1.863  0.28 29.04 ?  201 A1BBN A H18  1 
HETATM 6841 H H11  B A1BBN C 2 .   ? 11.919 -2.446  -0.345  0.28 28.93 ?  201 A1BBN A H11  1 
HETATM 6842 H H12  B A1BBN C 2 .   ? 12.262 -1.547  2.008   0.28 28.85 ?  201 A1BBN A H12  1 
HETATM 6843 H H13  B A1BBN C 2 .   ? 10.709 -1.098  1.351   0.28 28.85 ?  201 A1BBN A H13  1 
HETATM 6844 H H16  B A1BBN C 2 .   ? 13.290 2.110   0.445   0.28 28.94 ?  201 A1BBN A H16  1 
HETATM 6845 H H19  B A1BBN C 2 .   ? 11.828 -0.798  -2.212  0.28 28.90 ?  201 A1BBN A H19  1 
HETATM 6846 H H20  B A1BBN C 2 .   ? 10.504 -0.496  -1.113  0.28 28.90 ?  201 A1BBN A H20  1 
HETATM 6847 H H3   B A1BBN C 2 .   ? 16.140 -0.259  1.112   0.28 26.98 ?  201 A1BBN A H3   1 
HETATM 6848 H H2   B A1BBN C 2 .   ? 14.733 -0.722  2.028   0.28 26.98 ?  201 A1BBN A H2   1 
HETATM 6849 H H5   B A1BBN C 2 .   ? 15.676 4.365   2.978   0.28 19.27 ?  201 A1BBN A H5   1 
HETATM 6850 H H8   B A1BBN C 2 .   ? 14.848 -0.845  5.896   0.28 21.85 ?  201 A1BBN A H8   1 
HETATM 6851 H H4   B A1BBN C 2 .   ? 15.300 2.186   1.545   0.28 24.94 ?  201 A1BBN A H4   1 
HETATM 6852 H H1   B A1BBN C 2 .   ? 15.836 0.035   -0.980  0.28 28.89 ?  201 A1BBN A H1   1 
HETATM 6853 O O    . HOH   D 3 .   ? 14.691 -13.917 16.668  1.00 29.71 ?  301 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 14.632 -4.721  20.456  1.00 45.13 ?  302 HOH   A O    1 
HETATM 6855 O O    . HOH   D 3 .   ? -0.647 -8.489  2.195   1.00 43.08 ?  303 HOH   A O    1 
HETATM 6856 O O    . HOH   D 3 .   ? 17.112 -17.982 14.992  1.00 30.14 ?  304 HOH   A O    1 
HETATM 6857 O O    . HOH   D 3 .   ? 4.703  3.771   0.500   1.00 28.34 ?  305 HOH   A O    1 
HETATM 6858 O O    . HOH   D 3 .   ? 15.443 11.885  7.902   1.00 46.97 ?  306 HOH   A O    1 
HETATM 6859 O O    . HOH   D 3 .   ? 12.028 0.320   14.777  1.00 36.35 ?  307 HOH   A O    1 
HETATM 6860 O O    . HOH   D 3 .   ? -0.451 -3.067  2.983   1.00 41.01 ?  308 HOH   A O    1 
HETATM 6861 O O    . HOH   D 3 .   ? 9.113  -10.101 19.209  1.00 43.30 ?  309 HOH   A O    1 
HETATM 6862 O O    . HOH   D 3 .   ? 34.361 -1.879  12.526  1.00 39.52 ?  310 HOH   A O    1 
HETATM 6863 O O    . HOH   D 3 .   ? 15.115 -12.209 18.618  1.00 43.25 ?  311 HOH   A O    1 
HETATM 6864 O O    . HOH   D 3 .   ? 24.587 2.003   -6.991  1.00 20.88 ?  312 HOH   A O    1 
HETATM 6865 O O    . HOH   D 3 .   ? 26.884 11.449  1.603   1.00 18.45 ?  313 HOH   A O    1 
HETATM 6866 O O    . HOH   D 3 .   ? 11.757 -10.776 -10.083 1.00 53.01 ?  314 HOH   A O    1 
HETATM 6867 O O    . HOH   D 3 .   ? 18.940 -21.974 6.934   1.00 36.60 ?  315 HOH   A O    1 
HETATM 6868 O O    . HOH   D 3 .   ? 28.976 0.446   -9.748  1.00 23.02 ?  316 HOH   A O    1 
HETATM 6869 O O    . HOH   D 3 .   ? 9.865  -21.368 5.594   1.00 21.71 ?  317 HOH   A O    1 
HETATM 6870 O O    . HOH   D 3 .   ? 0.640  -4.557  0.146   1.00 32.52 ?  318 HOH   A O    1 
HETATM 6871 O O    . HOH   D 3 .   ? 17.536 -1.720  0.338   1.00 21.43 ?  319 HOH   A O    1 
HETATM 6872 O O    . HOH   D 3 .   ? 16.152 2.908   -1.500  1.00 17.96 ?  320 HOH   A O    1 
HETATM 6873 O O    . HOH   D 3 .   ? 3.561  -9.260  9.903   1.00 35.05 ?  321 HOH   A O    1 
HETATM 6874 O O    . HOH   D 3 .   ? 17.023 -19.294 4.854   1.00 17.20 ?  322 HOH   A O    1 
HETATM 6875 O O    . HOH   D 3 .   ? 28.669 -10.622 -14.077 1.00 43.66 ?  323 HOH   A O    1 
HETATM 6876 O O    . HOH   D 3 .   ? 30.923 6.180   -12.275 1.00 31.18 ?  324 HOH   A O    1 
HETATM 6877 O O    . HOH   D 3 .   ? 30.265 -13.295 -8.498  1.00 26.54 ?  325 HOH   A O    1 
HETATM 6878 O O    . HOH   D 3 .   ? 7.940  -12.585 -1.008  1.00 23.76 ?  326 HOH   A O    1 
HETATM 6879 O O    . HOH   D 3 .   ? 42.394 10.540  4.997   1.00 20.34 ?  327 HOH   A O    1 
HETATM 6880 O O    . HOH   D 3 .   ? 22.367 5.340   19.012  1.00 46.37 ?  328 HOH   A O    1 
HETATM 6881 O O    . HOH   D 3 .   ? 6.841  -8.112  11.764  1.00 22.51 ?  329 HOH   A O    1 
HETATM 6882 O O    . HOH   D 3 .   ? 14.197 -4.601  -11.921 1.00 32.08 ?  330 HOH   A O    1 
HETATM 6883 O O    . HOH   D 3 .   ? 14.043 -23.056 7.324   1.00 20.48 ?  331 HOH   A O    1 
HETATM 6884 O O    . HOH   D 3 .   ? 38.214 10.293  7.071   1.00 54.81 ?  332 HOH   A O    1 
HETATM 6885 O O    . HOH   D 3 .   ? 13.335 -1.452  -6.690  1.00 21.83 ?  333 HOH   A O    1 
HETATM 6886 O O    A HOH   D 3 .   ? 28.264 -0.200  -13.369 0.72 30.43 ?  334 HOH   A O    1 
HETATM 6887 O O    . HOH   D 3 .   ? 28.203 -6.295  19.589  1.00 43.91 ?  335 HOH   A O    1 
HETATM 6888 O O    . HOH   D 3 .   ? 19.963 -12.558 -8.915  1.00 27.84 ?  336 HOH   A O    1 
HETATM 6889 O O    . HOH   D 3 .   ? 37.517 2.823   10.274  1.00 27.10 ?  337 HOH   A O    1 
HETATM 6890 O O    . HOH   D 3 .   ? 43.357 7.702   2.702   1.00 44.21 ?  338 HOH   A O    1 
HETATM 6891 O O    . HOH   D 3 .   ? 26.528 -19.343 -1.793  1.00 16.01 ?  339 HOH   A O    1 
HETATM 6892 O O    . HOH   D 3 .   ? 34.053 -1.119  -8.905  1.00 28.37 ?  340 HOH   A O    1 
HETATM 6893 O O    . HOH   D 3 .   ? 14.612 -3.609  3.029   1.00 21.78 ?  341 HOH   A O    1 
HETATM 6894 O O    . HOH   D 3 .   ? 22.741 12.526  1.567   1.00 16.55 ?  342 HOH   A O    1 
HETATM 6895 O O    . HOH   D 3 .   ? 23.921 -15.737 -9.206  1.00 38.59 ?  343 HOH   A O    1 
HETATM 6896 O O    . HOH   D 3 .   ? 31.037 -18.122 7.766   1.00 19.71 ?  344 HOH   A O    1 
HETATM 6897 O O    . HOH   D 3 .   ? 14.587 -0.612  -12.239 1.00 27.46 ?  345 HOH   A O    1 
HETATM 6898 O O    . HOH   D 3 .   ? 27.313 13.798  2.828   1.00 32.15 ?  346 HOH   A O    1 
HETATM 6899 O O    . HOH   D 3 .   ? 36.262 -5.091  -0.469  1.00 33.50 ?  347 HOH   A O    1 
HETATM 6900 O O    . HOH   D 3 .   ? 18.672 -19.381 13.521  1.00 37.15 ?  348 HOH   A O    1 
HETATM 6901 O O    . HOH   D 3 .   ? 44.347 7.201   6.458   1.00 27.90 ?  349 HOH   A O    1 
HETATM 6902 O O    . HOH   D 3 .   ? 31.639 8.230   14.812  1.00 26.45 ?  350 HOH   A O    1 
HETATM 6903 O O    . HOH   D 3 .   ? 7.626  -6.305  -6.615  1.00 42.99 ?  351 HOH   A O    1 
HETATM 6904 O O    . HOH   D 3 .   ? 20.692 -19.781 -5.122  1.00 29.40 ?  352 HOH   A O    1 
HETATM 6905 O O    . HOH   D 3 .   ? 38.553 4.964   7.033   1.00 16.28 ?  353 HOH   A O    1 
HETATM 6906 O O    . HOH   D 3 .   ? 21.277 -2.375  -2.242  1.00 18.60 ?  354 HOH   A O    1 
HETATM 6907 O O    A HOH   D 3 .   ? 14.269 0.572   6.736   0.72 21.38 ?  355 HOH   A O    1 
HETATM 6908 O O    . HOH   D 3 .   ? 14.974 3.913   17.716  1.00 43.28 ?  356 HOH   A O    1 
HETATM 6909 O O    . HOH   D 3 .   ? 37.192 -2.755  9.729   1.00 45.90 ?  357 HOH   A O    1 
HETATM 6910 O O    . HOH   D 3 .   ? 18.512 9.493   8.955   1.00 23.55 ?  358 HOH   A O    1 
HETATM 6911 O O    . HOH   D 3 .   ? 8.083  -21.563 3.943   1.00 49.32 ?  359 HOH   A O    1 
HETATM 6912 O O    . HOH   D 3 .   ? 42.594 4.293   5.522   1.00 35.61 ?  360 HOH   A O    1 
HETATM 6913 O O    . HOH   D 3 .   ? 39.805 -1.041  -5.147  1.00 21.12 ?  361 HOH   A O    1 
HETATM 6914 O O    . HOH   D 3 .   ? 22.078 -19.348 11.351  1.00 39.10 ?  362 HOH   A O    1 
HETATM 6915 O O    . HOH   D 3 .   ? 14.388 -21.274 -4.311  1.00 30.79 ?  363 HOH   A O    1 
HETATM 6916 O O    . HOH   D 3 .   ? 35.782 -12.635 6.845   1.00 16.70 ?  364 HOH   A O    1 
HETATM 6917 O O    . HOH   D 3 .   ? 27.972 0.805   -7.178  1.00 15.31 ?  365 HOH   A O    1 
HETATM 6918 O O    . HOH   D 3 .   ? 22.570 -11.896 21.842  1.00 50.55 ?  366 HOH   A O    1 
HETATM 6919 O O    . HOH   D 3 .   ? 25.746 -0.783  -7.349  1.00 18.59 ?  367 HOH   A O    1 
HETATM 6920 O O    . HOH   D 3 .   ? 24.052 -2.117  -2.127  1.00 12.10 ?  368 HOH   A O    1 
HETATM 6921 O O    . HOH   D 3 .   ? 13.901 -4.966  17.416  1.00 28.72 ?  369 HOH   A O    1 
HETATM 6922 O O    . HOH   D 3 .   ? 31.121 -13.939 -2.466  1.00 15.53 ?  370 HOH   A O    1 
HETATM 6923 O O    . HOH   D 3 .   ? 17.158 -17.816 -5.169  1.00 28.62 ?  371 HOH   A O    1 
HETATM 6924 O O    . HOH   D 3 .   ? 31.918 -9.363  -6.694  1.00 25.15 ?  372 HOH   A O    1 
HETATM 6925 O O    . HOH   D 3 .   ? 30.797 3.093   8.272   1.00 13.52 ?  373 HOH   A O    1 
HETATM 6926 O O    . HOH   D 3 .   ? 21.838 -21.894 8.427   1.00 29.65 ?  374 HOH   A O    1 
HETATM 6927 O O    . HOH   D 3 .   ? 13.564 -15.257 -7.686  1.00 29.73 ?  375 HOH   A O    1 
HETATM 6928 O O    . HOH   D 3 .   ? 24.428 3.594   -1.834  1.00 17.27 ?  376 HOH   A O    1 
HETATM 6929 O O    . HOH   D 3 .   ? 10.399 -22.159 -1.350  1.00 52.39 ?  377 HOH   A O    1 
HETATM 6930 O O    . HOH   D 3 .   ? 19.337 -11.137 23.990  1.00 81.40 ?  378 HOH   A O    1 
HETATM 6931 O O    . HOH   D 3 .   ? 21.368 3.124   -0.342  1.00 14.45 ?  379 HOH   A O    1 
HETATM 6932 O O    . HOH   D 3 .   ? 37.254 11.998  4.915   1.00 28.24 ?  380 HOH   A O    1 
HETATM 6933 O O    . HOH   D 3 .   ? 27.418 -10.570 14.067  1.00 18.74 ?  381 HOH   A O    1 
HETATM 6934 O O    . HOH   D 3 .   ? 21.151 10.315  14.963  1.00 35.65 ?  382 HOH   A O    1 
HETATM 6935 O O    . HOH   D 3 .   ? 18.976 -0.705  -1.728  1.00 15.93 ?  383 HOH   A O    1 
HETATM 6936 O O    . HOH   D 3 .   ? 33.647 -7.149  4.343   1.00 17.36 ?  384 HOH   A O    1 
HETATM 6937 O O    . HOH   D 3 .   ? 24.173 -7.740  14.400  1.00 18.40 ?  385 HOH   A O    1 
HETATM 6938 O O    A HOH   D 3 .   ? 20.125 4.539   -7.596  0.72 19.54 ?  386 HOH   A O    1 
HETATM 6939 O O    . HOH   D 3 .   ? 24.666 -17.492 12.733  1.00 25.69 ?  387 HOH   A O    1 
HETATM 6940 O O    . HOH   D 3 .   ? 27.610 -6.163  -13.996 1.00 41.71 ?  388 HOH   A O    1 
HETATM 6941 O O    . HOH   D 3 .   ? 44.014 8.545   -2.999  1.00 30.07 ?  389 HOH   A O    1 
HETATM 6942 O O    . HOH   D 3 .   ? 16.488 -22.094 0.932   1.00 30.18 ?  390 HOH   A O    1 
HETATM 6943 O O    . HOH   D 3 .   ? 37.561 -2.101  5.886   1.00 26.70 ?  391 HOH   A O    1 
HETATM 6944 O O    . HOH   D 3 .   ? 14.453 -24.667 11.510  1.00 40.11 ?  392 HOH   A O    1 
HETATM 6945 O O    . HOH   D 3 .   ? 31.922 -7.270  -9.833  1.00 22.76 ?  393 HOH   A O    1 
HETATM 6946 O O    . HOH   D 3 .   ? 23.465 11.393  4.063   1.00 13.83 ?  394 HOH   A O    1 
HETATM 6947 O O    . HOH   D 3 .   ? 10.937 1.612   12.619  1.00 26.27 ?  395 HOH   A O    1 
HETATM 6948 O O    . HOH   D 3 .   ? 16.218 16.634  8.577   1.00 37.74 ?  396 HOH   A O    1 
HETATM 6949 O O    . HOH   D 3 .   ? 6.390  -5.585  11.007  1.00 21.93 ?  397 HOH   A O    1 
HETATM 6950 O O    . HOH   D 3 .   ? 15.218 -21.523 14.159  1.00 19.36 ?  398 HOH   A O    1 
HETATM 6951 O O    . HOH   D 3 .   ? 15.843 2.200   24.626  1.00 50.99 ?  399 HOH   A O    1 
HETATM 6952 O O    . HOH   D 3 .   ? 16.015 6.914   2.833   1.00 18.55 ?  400 HOH   A O    1 
HETATM 6953 O O    . HOH   D 3 .   ? 30.601 1.906   16.696  1.00 23.87 ?  401 HOH   A O    1 
HETATM 6954 O O    . HOH   D 3 .   ? 32.745 -9.288  5.904   1.00 21.59 ?  402 HOH   A O    1 
HETATM 6955 O O    . HOH   D 3 .   ? 26.952 4.184   -0.682  1.00 14.06 ?  403 HOH   A O    1 
HETATM 6956 O O    . HOH   D 3 .   ? 21.848 -13.861 -8.220  1.00 46.21 ?  404 HOH   A O    1 
HETATM 6957 O O    . HOH   D 3 .   ? 6.657  -3.370  12.763  1.00 32.29 ?  405 HOH   A O    1 
HETATM 6958 O O    . HOH   D 3 .   ? 38.119 -1.343  -1.884  1.00 20.14 ?  406 HOH   A O    1 
HETATM 6959 O O    . HOH   D 3 .   ? 20.564 -20.056 2.729   1.00 20.34 ?  407 HOH   A O    1 
HETATM 6960 O O    . HOH   D 3 .   ? 15.231 -8.057  -9.885  1.00 25.16 ?  408 HOH   A O    1 
HETATM 6961 O O    A HOH   D 3 .   ? 15.797 -0.947  5.210   0.72 25.27 ?  409 HOH   A O    1 
HETATM 6962 O O    . HOH   D 3 .   ? 23.965 -20.285 -1.364  1.00 19.02 ?  410 HOH   A O    1 
HETATM 6963 O O    . HOH   D 3 .   ? 40.969 -8.290  -6.715  1.00 36.21 ?  411 HOH   A O    1 
HETATM 6964 O O    . HOH   D 3 .   ? 30.289 -12.903 13.533  1.00 20.88 ?  412 HOH   A O    1 
HETATM 6965 O O    . HOH   D 3 .   ? 27.243 2.287   18.728  1.00 35.67 ?  413 HOH   A O    1 
HETATM 6966 O O    . HOH   D 3 .   ? 41.630 1.469   5.045   1.00 38.46 ?  414 HOH   A O    1 
HETATM 6967 O O    . HOH   D 3 .   ? 5.214  2.709   5.012   1.00 32.02 ?  415 HOH   A O    1 
HETATM 6968 O O    . HOH   D 3 .   ? 35.120 -5.248  -3.068  1.00 18.90 ?  416 HOH   A O    1 
HETATM 6969 O O    . HOH   D 3 .   ? 8.991  -12.130 17.190  1.00 42.20 ?  417 HOH   A O    1 
HETATM 6970 O O    . HOH   D 3 .   ? 11.623 -10.782 16.852  1.00 29.43 ?  418 HOH   A O    1 
HETATM 6971 O O    . HOH   D 3 .   ? 30.015 -10.070 13.041  1.00 25.37 ?  419 HOH   A O    1 
HETATM 6972 O O    A HOH   D 3 .   ? 11.072 -0.383  1.863   0.72 23.57 ?  420 HOH   A O    1 
HETATM 6973 O O    . HOH   D 3 .   ? 36.724 -4.936  5.402   1.00 23.85 ?  421 HOH   A O    1 
HETATM 6974 O O    . HOH   D 3 .   ? 32.751 -4.304  -9.896  1.00 29.45 ?  422 HOH   A O    1 
HETATM 6975 O O    . HOH   D 3 .   ? 10.408 -13.794 -1.823  1.00 19.87 ?  423 HOH   A O    1 
HETATM 6976 O O    A HOH   D 3 .   ? 18.621 -2.468  -16.391 0.72 36.36 ?  424 HOH   A O    1 
HETATM 6977 O O    . HOH   D 3 .   ? 45.016 -0.632  3.000   1.00 44.04 ?  425 HOH   A O    1 
HETATM 6978 O O    . HOH   D 3 .   ? 32.511 -10.651 3.265   1.00 32.86 ?  426 HOH   A O    1 
HETATM 6979 O O    . HOH   D 3 .   ? 18.386 -15.949 16.213  1.00 41.21 ?  427 HOH   A O    1 
HETATM 6980 O O    . HOH   D 3 .   ? 24.041 3.955   -4.866  1.00 23.05 ?  428 HOH   A O    1 
HETATM 6981 O O    . HOH   D 3 .   ? 22.569 8.166   18.345  1.00 43.57 ?  429 HOH   A O    1 
HETATM 6982 O O    . HOH   D 3 .   ? 21.295 -9.182  21.275  1.00 54.85 ?  430 HOH   A O    1 
HETATM 6983 O O    . HOH   D 3 .   ? 18.848 2.010   -0.776  1.00 15.19 ?  431 HOH   A O    1 
HETATM 6984 O O    . HOH   D 3 .   ? 37.751 -8.811  -3.413  1.00 23.61 ?  432 HOH   A O    1 
HETATM 6985 O O    . HOH   D 3 .   ? 23.447 -20.929 1.314   1.00 21.08 ?  433 HOH   A O    1 
HETATM 6986 O O    . HOH   D 3 .   ? 16.202 -14.267 20.132  1.00 53.55 ?  434 HOH   A O    1 
HETATM 6987 O O    . HOH   D 3 .   ? 27.035 -3.204  19.501  1.00 38.83 ?  435 HOH   A O    1 
HETATM 6988 O O    . HOH   D 3 .   ? 23.448 -8.031  17.050  1.00 23.58 ?  436 HOH   A O    1 
HETATM 6989 O O    A HOH   D 3 .   ? 18.479 4.838   -15.082 0.72 44.83 ?  437 HOH   A O    1 
HETATM 6990 O O    . HOH   D 3 .   ? 34.421 -8.081  -0.532  1.00 31.40 ?  438 HOH   A O    1 
HETATM 6991 O O    . HOH   D 3 .   ? 31.354 -12.782 0.006   1.00 21.93 ?  439 HOH   A O    1 
HETATM 6992 O O    . HOH   D 3 .   ? 20.536 -17.716 24.829  1.00 52.87 ?  440 HOH   A O    1 
HETATM 6993 O O    . HOH   D 3 .   ? -1.434 -4.914  7.572   1.00 44.44 ?  441 HOH   A O    1 
HETATM 6994 O O    . HOH   D 3 .   ? 23.228 7.533   -3.298  1.00 34.51 ?  442 HOH   A O    1 
HETATM 6995 O O    . HOH   D 3 .   ? 30.564 14.737  2.722   1.00 20.28 ?  443 HOH   A O    1 
HETATM 6996 O O    . HOH   D 3 .   ? 9.432  -16.267 -2.169  1.00 48.41 ?  444 HOH   A O    1 
HETATM 6997 O O    . HOH   D 3 .   ? 29.811 -1.949  -12.807 1.00 51.02 ?  445 HOH   A O    1 
HETATM 6998 O O    A HOH   D 3 .   ? 14.029 -0.341  3.398   0.72 18.59 ?  446 HOH   A O    1 
HETATM 6999 O O    . HOH   D 3 .   ? 21.486 -14.837 17.841  1.00 55.77 ?  447 HOH   A O    1 
HETATM 7000 O O    . HOH   D 3 .   ? 29.868 -16.083 10.792  1.00 34.54 ?  448 HOH   A O    1 
HETATM 7001 O O    . HOH   D 3 .   ? 32.418 -15.916 10.843  1.00 31.07 ?  449 HOH   A O    1 
HETATM 7002 O O    . HOH   D 3 .   ? 25.447 8.280   -4.840  1.00 33.57 ?  450 HOH   A O    1 
HETATM 7003 O O    . HOH   D 3 .   ? 27.808 7.021   -6.644  1.00 40.51 ?  451 HOH   A O    1 
HETATM 7004 O O    . HOH   D 3 .   ? 24.751 5.653   20.678  1.00 53.48 ?  452 HOH   A O    1 
HETATM 7005 O O    . HOH   D 3 .   ? 19.914 -17.370 -5.121  1.00 25.70 ?  453 HOH   A O    1 
HETATM 7006 O O    . HOH   D 3 .   ? 23.189 -22.372 -3.302  1.00 37.43 ?  454 HOH   A O    1 
HETATM 7007 O O    . HOH   D 3 .   ? 24.585 14.688  7.784   1.00 40.55 ?  455 HOH   A O    1 
HETATM 7008 O O    . HOH   D 3 .   ? 11.001 -14.978 -6.093  1.00 38.31 ?  456 HOH   A O    1 
HETATM 7009 O O    . HOH   D 3 .   ? 22.020 5.230   -6.063  1.00 32.46 ?  457 HOH   A O    1 
HETATM 7010 O O    . HOH   D 3 .   ? 18.777 10.962  11.227  1.00 34.33 ?  458 HOH   A O    1 
HETATM 7011 O O    . HOH   D 3 .   ? 26.950 11.663  -1.396  1.00 35.57 ?  459 HOH   A O    1 
HETATM 7012 O O    . HOH   D 3 .   ? 15.784 -21.549 3.639   1.00 24.96 ?  460 HOH   A O    1 
HETATM 7013 O O    . HOH   D 3 .   ? 23.409 13.710  5.509   1.00 19.45 ?  461 HOH   A O    1 
HETATM 7014 O O    . HOH   D 3 .   ? 39.727 -6.999  -3.444  1.00 45.08 ?  462 HOH   A O    1 
HETATM 7015 O O    . HOH   D 3 .   ? 27.447 -11.368 16.589  1.00 39.03 ?  463 HOH   A O    1 
HETATM 7016 O O    . HOH   D 3 .   ? 12.214 1.618   17.230  1.00 41.06 ?  464 HOH   A O    1 
HETATM 7017 O O    . HOH   D 3 .   ? 18.177 -16.170 -8.898  1.00 44.06 ?  465 HOH   A O    1 
HETATM 7018 O O    . HOH   D 3 .   ? 25.873 10.776  -3.775  1.00 28.44 ?  466 HOH   A O    1 
HETATM 7019 O O    . HOH   D 3 .   ? 12.021 -13.364 16.282  1.00 52.48 ?  467 HOH   A O    1 
HETATM 7020 O O    . HOH   D 3 .   ? 23.160 11.840  -4.105  1.00 22.04 ?  468 HOH   A O    1 
HETATM 7021 O O    . HOH   D 3 .   ? 16.846 -20.506 16.095  1.00 31.10 ?  469 HOH   A O    1 
HETATM 7022 O O    . HOH   D 3 .   ? 28.760 9.001   17.468  1.00 37.47 ?  470 HOH   A O    1 
HETATM 7023 O O    . HOH   D 3 .   ? 35.157 7.497   12.182  1.00 58.61 ?  471 HOH   A O    1 
HETATM 7024 O O    . HOH   D 3 .   ? 28.763 -4.775  -12.299 1.00 42.31 ?  472 HOH   A O    1 
HETATM 7025 O O    . HOH   D 3 .   ? 15.850 -17.192 -7.080  1.00 36.26 ?  473 HOH   A O    1 
HETATM 7026 O O    . HOH   D 3 .   ? 41.039 -3.941  -0.418  1.00 39.84 ?  474 HOH   A O    1 
HETATM 7027 O O    . HOH   D 3 .   ? 8.188  -3.147  -5.790  1.00 52.60 ?  475 HOH   A O    1 
HETATM 7028 O O    . HOH   D 3 .   ? 44.477 10.379  -1.673  1.00 36.08 ?  476 HOH   A O    1 
HETATM 7029 O O    . HOH   D 3 .   ? 30.771 0.734   19.157  1.00 40.80 ?  477 HOH   A O    1 
HETATM 7030 O O    . HOH   D 3 .   ? 16.198 -23.400 5.738   1.00 31.96 ?  478 HOH   A O    1 
HETATM 7031 O O    . HOH   D 3 .   ? 25.783 -18.875 -11.932 1.00 42.42 ?  479 HOH   A O    1 
HETATM 7032 O O    . HOH   D 3 .   ? 20.106 -22.372 4.200   1.00 32.54 ?  480 HOH   A O    1 
HETATM 7033 O O    . HOH   D 3 .   ? 17.377 -18.740 19.688  1.00 53.32 ?  481 HOH   A O    1 
HETATM 7034 O O    . HOH   D 3 .   ? 14.064 -10.308 -11.010 1.00 35.33 ?  482 HOH   A O    1 
HETATM 7035 O O    . HOH   D 3 .   ? 28.769 -7.958  -15.246 1.00 51.50 ?  483 HOH   A O    1 
HETATM 7036 O O    . HOH   D 3 .   ? 13.963 -25.251 8.825   1.00 35.04 ?  484 HOH   A O    1 
HETATM 7037 O O    . HOH   D 3 .   ? 16.120 -6.706  -11.944 1.00 43.57 ?  485 HOH   A O    1 
HETATM 7038 O O    . HOH   D 3 .   ? 41.770 9.436   -3.916  1.00 31.60 ?  486 HOH   A O    1 
HETATM 7039 O O    . HOH   D 3 .   ? 39.213 2.370   7.373   1.00 31.39 ?  487 HOH   A O    1 
HETATM 7040 O O    . HOH   D 3 .   ? 23.217 -12.901 19.249  1.00 58.17 ?  488 HOH   A O    1 
HETATM 7041 O O    . HOH   D 3 .   ? 18.453 -23.203 1.916   1.00 47.25 ?  489 HOH   A O    1 
HETATM 7042 O O    . HOH   D 3 .   ? 31.558 -0.592  -10.542 1.00 29.48 ?  490 HOH   A O    1 
HETATM 7043 O O    . HOH   D 3 .   ? 30.800 5.752   -14.742 1.00 36.03 ?  491 HOH   A O    1 
HETATM 7044 O O    . HOH   D 3 .   ? 40.598 -0.288  -7.808  1.00 33.54 ?  492 HOH   A O    1 
HETATM 7045 O O    B HOH   D 3 .   ? 14.610 8.009   5.060   0.28 25.18 ?  493 HOH   A O    1 
HETATM 7046 O O    . HOH   D 3 .   ? 37.400 -6.611  7.618   1.00 25.50 ?  494 HOH   A O    1 
HETATM 7047 O O    . HOH   D 3 .   ? 30.787 -5.859  -11.908 1.00 52.23 ?  495 HOH   A O    1 
HETATM 7048 O O    . HOH   D 3 .   ? 39.554 -0.069  6.596   1.00 34.50 ?  496 HOH   A O    1 
HETATM 7049 O O    . HOH   D 3 .   ? 28.965 14.483  0.864   1.00 51.57 ?  497 HOH   A O    1 
HETATM 7050 O O    . HOH   D 3 .   ? 20.606 -16.062 -7.449  1.00 30.20 ?  498 HOH   A O    1 
HETATM 7051 O O    . HOH   D 3 .   ? 37.970 13.979  6.661   1.00 35.64 ?  499 HOH   A O    1 
HETATM 7052 O O    . HOH   D 3 .   ? 22.058 -24.020 4.478   1.00 27.67 ?  500 HOH   A O    1 
HETATM 7053 O O    . HOH   D 3 .   ? 36.493 -6.535  10.246  1.00 48.58 ?  501 HOH   A O    1 
HETATM 7054 O O    A HOH   D 3 .   ? 14.847 8.649   4.825   0.72 35.11 ?  502 HOH   A O    1 
HETATM 7055 O O    . HOH   D 3 .   ? 17.238 -6.668  -14.225 1.00 45.84 ?  503 HOH   A O    1 
HETATM 7056 O O    . HOH   D 3 .   ? 24.159 9.163   -7.243  1.00 39.26 ?  504 HOH   A O    1 
HETATM 7057 O O    . HOH   D 3 .   ? 15.743 -12.229 27.335  1.00 45.90 ?  505 HOH   A O    1 
HETATM 7058 O O    . HOH   D 3 .   ? 16.331 -21.156 18.771  1.00 39.19 ?  506 HOH   A O    1 
HETATM 7059 O O    . HOH   D 3 .   ? 14.692 -22.718 19.819  1.00 37.54 ?  507 HOH   A O    1 
HETATM 7060 O O    . HOH   E 3 .   ? 29.879 -22.423 5.518   1.00 20.82 ?  201 HOH   B O    1 
HETATM 7061 O O    . HOH   E 3 .   ? 27.709 -29.162 -1.843  1.00 37.45 ?  202 HOH   B O    1 
HETATM 7062 O O    . HOH   E 3 .   ? 41.629 -36.044 -17.204 1.00 34.86 ?  203 HOH   B O    1 
HETATM 7063 O O    . HOH   E 3 .   ? 27.908 -41.746 -15.137 1.00 38.06 ?  204 HOH   B O    1 
HETATM 7064 O O    . HOH   E 3 .   ? 59.167 -18.685 6.857   1.00 37.79 ?  205 HOH   B O    1 
HETATM 7065 O O    . HOH   E 3 .   ? 31.048 -28.755 4.460   1.00 29.11 ?  206 HOH   B O    1 
HETATM 7066 O O    . HOH   E 3 .   ? 38.035 -39.491 -0.227  1.00 42.59 ?  207 HOH   B O    1 
HETATM 7067 O O    . HOH   E 3 .   ? 48.077 -6.938  15.512  1.00 29.31 ?  208 HOH   B O    1 
HETATM 7068 O O    . HOH   E 3 .   ? 41.383 -7.741  5.449   1.00 42.04 ?  209 HOH   B O    1 
HETATM 7069 O O    . HOH   E 3 .   ? 50.154 -3.427  7.118   1.00 33.39 ?  210 HOH   B O    1 
HETATM 7070 O O    . HOH   E 3 .   ? 49.479 -22.734 -19.754 1.00 49.65 ?  211 HOH   B O    1 
HETATM 7071 O O    . HOH   E 3 .   ? 30.218 -41.003 -8.038  1.00 18.79 ?  212 HOH   B O    1 
HETATM 7072 O O    . HOH   E 3 .   ? 30.010 -26.298 4.111   1.00 28.62 ?  213 HOH   B O    1 
HETATM 7073 O O    . HOH   E 3 .   ? 54.535 -9.438  -8.628  1.00 19.44 ?  214 HOH   B O    1 
HETATM 7074 O O    . HOH   E 3 .   ? 58.203 -12.963 8.395   1.00 30.23 ?  215 HOH   B O    1 
HETATM 7075 O O    . HOH   E 3 .   ? 56.694 -30.779 -7.773  1.00 29.61 ?  216 HOH   B O    1 
HETATM 7076 O O    . HOH   E 3 .   ? 53.029 -13.452 -20.380 1.00 37.82 ?  217 HOH   B O    1 
HETATM 7077 O O    . HOH   E 3 .   ? 56.406 -19.740 7.199   1.00 31.69 ?  218 HOH   B O    1 
HETATM 7078 O O    . HOH   E 3 .   ? 57.783 -24.429 5.058   1.00 40.35 ?  219 HOH   B O    1 
HETATM 7079 O O    . HOH   E 3 .   ? 34.558 -36.398 -7.152  1.00 20.87 ?  220 HOH   B O    1 
HETATM 7080 O O    . HOH   E 3 .   ? 47.432 -7.282  -3.831  1.00 43.88 ?  221 HOH   B O    1 
HETATM 7081 O O    . HOH   E 3 .   ? 48.595 -36.508 -15.541 1.00 44.75 ?  222 HOH   B O    1 
HETATM 7082 O O    . HOH   E 3 .   ? 37.163 -19.680 -18.158 1.00 43.90 ?  223 HOH   B O    1 
HETATM 7083 O O    . HOH   E 3 .   ? 41.506 -39.204 -14.930 1.00 23.19 ?  224 HOH   B O    1 
HETATM 7084 O O    . HOH   E 3 .   ? 50.815 -6.068  0.168   1.00 28.21 ?  225 HOH   B O    1 
HETATM 7085 O O    . HOH   E 3 .   ? 34.917 -24.635 13.808  1.00 34.98 ?  226 HOH   B O    1 
HETATM 7086 O O    . HOH   E 3 .   ? 45.134 -34.953 6.806   1.00 42.59 ?  227 HOH   B O    1 
HETATM 7087 O O    . HOH   E 3 .   ? 41.391 -9.624  13.053  1.00 23.01 ?  228 HOH   B O    1 
HETATM 7088 O O    . HOH   E 3 .   ? 57.411 -16.296 -12.264 1.00 18.63 ?  229 HOH   B O    1 
HETATM 7089 O O    . HOH   E 3 .   ? 35.127 -8.016  -2.954  1.00 18.88 ?  230 HOH   B O    1 
HETATM 7090 O O    . HOH   E 3 .   ? 25.420 -25.899 -1.285  1.00 34.06 ?  231 HOH   B O    1 
HETATM 7091 O O    . HOH   E 3 .   ? 57.207 -26.891 -7.607  1.00 37.44 ?  232 HOH   B O    1 
HETATM 7092 O O    . HOH   E 3 .   ? 44.450 -7.163  2.060   1.00 35.22 ?  233 HOH   B O    1 
HETATM 7093 O O    . HOH   E 3 .   ? 38.536 -11.057 -2.293  1.00 20.60 ?  234 HOH   B O    1 
HETATM 7094 O O    . HOH   E 3 .   ? 46.397 -1.562  13.195  1.00 28.16 ?  235 HOH   B O    1 
HETATM 7095 O O    . HOH   E 3 .   ? 32.782 -43.788 -11.288 1.00 25.30 ?  236 HOH   B O    1 
HETATM 7096 O O    . HOH   E 3 .   ? 51.691 -6.486  4.329   1.00 20.92 ?  237 HOH   B O    1 
HETATM 7097 O O    . HOH   E 3 .   ? 55.323 -16.496 -14.296 1.00 31.00 ?  238 HOH   B O    1 
HETATM 7098 O O    . HOH   E 3 .   ? 39.333 -10.864 6.112   1.00 26.85 ?  239 HOH   B O    1 
HETATM 7099 O O    . HOH   E 3 .   ? 43.033 -43.252 -8.211  1.00 31.49 ?  240 HOH   B O    1 
HETATM 7100 O O    . HOH   E 3 .   ? 44.902 -43.620 -10.512 1.00 28.61 ?  241 HOH   B O    1 
HETATM 7101 O O    . HOH   E 3 .   ? 40.621 -16.094 14.092  1.00 24.29 ?  242 HOH   B O    1 
HETATM 7102 O O    . HOH   E 3 .   ? 50.793 -12.988 -0.450  1.00 12.94 ?  243 HOH   B O    1 
HETATM 7103 O O    . HOH   E 3 .   ? 42.673 -22.855 3.879   1.00 12.94 ?  244 HOH   B O    1 
HETATM 7104 O O    . HOH   E 3 .   ? 42.915 -20.311 -20.672 1.00 38.62 ?  245 HOH   B O    1 
HETATM 7105 O O    . HOH   E 3 .   ? 34.327 -18.373 11.450  1.00 27.45 ?  246 HOH   B O    1 
HETATM 7106 O O    . HOH   E 3 .   ? 39.567 -11.142 0.284   1.00 17.57 ?  247 HOH   B O    1 
HETATM 7107 O O    . HOH   E 3 .   ? 29.816 -34.150 -0.427  1.00 37.36 ?  248 HOH   B O    1 
HETATM 7108 O O    . HOH   E 3 .   ? 42.606 -25.372 2.688   1.00 16.30 ?  249 HOH   B O    1 
HETATM 7109 O O    . HOH   E 3 .   ? 30.508 -42.230 -10.623 1.00 32.94 ?  250 HOH   B O    1 
HETATM 7110 O O    . HOH   E 3 .   ? 44.581 -27.761 -0.696  1.00 22.81 ?  251 HOH   B O    1 
HETATM 7111 O O    . HOH   E 3 .   ? 51.552 -13.806 10.987  1.00 29.90 ?  252 HOH   B O    1 
HETATM 7112 O O    . HOH   E 3 .   ? 57.675 -24.390 -3.790  1.00 21.36 ?  253 HOH   B O    1 
HETATM 7113 O O    . HOH   E 3 .   ? 50.986 -39.924 -8.240  1.00 38.53 ?  254 HOH   B O    1 
HETATM 7114 O O    . HOH   E 3 .   ? 41.912 -23.508 9.342   1.00 20.20 ?  255 HOH   B O    1 
HETATM 7115 O O    . HOH   E 3 .   ? 46.941 -29.564 9.775   1.00 31.71 ?  256 HOH   B O    1 
HETATM 7116 O O    . HOH   E 3 .   ? 29.731 -25.180 -10.744 1.00 18.48 ?  257 HOH   B O    1 
HETATM 7117 O O    . HOH   E 3 .   ? 28.430 -19.692 -13.134 1.00 24.94 ?  258 HOH   B O    1 
HETATM 7118 O O    . HOH   E 3 .   ? 40.399 -12.750 -11.532 1.00 16.39 ?  259 HOH   B O    1 
HETATM 7119 O O    . HOH   E 3 .   ? 43.138 -32.377 -17.138 1.00 25.57 ?  260 HOH   B O    1 
HETATM 7120 O O    . HOH   E 3 .   ? 27.120 -31.823 -9.894  1.00 23.47 ?  261 HOH   B O    1 
HETATM 7121 O O    . HOH   E 3 .   ? 58.260 -10.681 -4.055  1.00 21.27 ?  262 HOH   B O    1 
HETATM 7122 O O    . HOH   E 3 .   ? 28.470 -30.909 -14.739 1.00 33.19 ?  263 HOH   B O    1 
HETATM 7123 O O    . HOH   E 3 .   ? 33.543 -16.970 8.081   1.00 20.20 ?  264 HOH   B O    1 
HETATM 7124 O O    . HOH   E 3 .   ? 49.690 -0.484  10.230  1.00 31.32 ?  265 HOH   B O    1 
HETATM 7125 O O    . HOH   E 3 .   ? 30.894 -15.720 2.683   1.00 15.12 ?  266 HOH   B O    1 
HETATM 7126 O O    . HOH   E 3 .   ? 31.805 -17.907 -14.528 1.00 31.23 ?  267 HOH   B O    1 
HETATM 7127 O O    . HOH   E 3 .   ? 38.952 -11.909 12.406  1.00 37.42 ?  268 HOH   B O    1 
HETATM 7128 O O    . HOH   E 3 .   ? 56.194 -23.612 -14.743 1.00 29.84 ?  269 HOH   B O    1 
HETATM 7129 O O    . HOH   E 3 .   ? 48.089 -22.776 5.837   1.00 18.98 ?  270 HOH   B O    1 
HETATM 7130 O O    . HOH   E 3 .   ? 49.327 -28.735 -6.927  1.00 17.09 ?  271 HOH   B O    1 
HETATM 7131 O O    . HOH   E 3 .   ? 34.937 -33.269 -19.240 1.00 37.33 ?  272 HOH   B O    1 
HETATM 7132 O O    . HOH   E 3 .   ? 57.538 -9.241  1.385   1.00 20.84 ?  273 HOH   B O    1 
HETATM 7133 O O    . HOH   E 3 .   ? 43.436 -15.795 -12.191 1.00 15.38 ?  274 HOH   B O    1 
HETATM 7134 O O    . HOH   E 3 .   ? 42.455 -34.706 3.795   1.00 26.38 ?  275 HOH   B O    1 
HETATM 7135 O O    . HOH   E 3 .   ? 42.366 -9.929  9.343   1.00 21.50 ?  276 HOH   B O    1 
HETATM 7136 O O    . HOH   E 3 .   ? 46.633 -31.240 -4.849  1.00 26.76 ?  277 HOH   B O    1 
HETATM 7137 O O    . HOH   E 3 .   ? 36.043 -43.465 -8.392  1.00 41.30 ?  278 HOH   B O    1 
HETATM 7138 O O    . HOH   E 3 .   ? 41.175 -5.550  11.518  1.00 48.92 ?  279 HOH   B O    1 
HETATM 7139 O O    . HOH   E 3 .   ? 56.944 -8.595  8.417   1.00 20.35 ?  280 HOH   B O    1 
HETATM 7140 O O    . HOH   E 3 .   ? 57.125 -12.141 12.354  1.00 39.06 ?  281 HOH   B O    1 
HETATM 7141 O O    . HOH   E 3 .   ? 48.640 -12.135 -14.454 1.00 26.68 ?  282 HOH   B O    1 
HETATM 7142 O O    . HOH   E 3 .   ? 28.257 -34.335 -9.337  1.00 20.69 ?  283 HOH   B O    1 
HETATM 7143 O O    . HOH   E 3 .   ? 48.438 -25.058 3.141   1.00 14.76 ?  284 HOH   B O    1 
HETATM 7144 O O    . HOH   E 3 .   ? 47.908 -24.557 -17.831 1.00 34.07 ?  285 HOH   B O    1 
HETATM 7145 O O    . HOH   E 3 .   ? 34.494 -12.740 2.626   1.00 25.42 ?  286 HOH   B O    1 
HETATM 7146 O O    . HOH   E 3 .   ? 27.981 -22.886 -7.970  1.00 18.85 ?  287 HOH   B O    1 
HETATM 7147 O O    . HOH   E 3 .   ? 27.590 -26.658 -15.626 1.00 33.75 ?  288 HOH   B O    1 
HETATM 7148 O O    . HOH   E 3 .   ? 45.273 -33.389 -15.974 1.00 26.10 ?  289 HOH   B O    1 
HETATM 7149 O O    . HOH   E 3 .   ? 48.745 -20.008 5.952   1.00 15.18 ?  290 HOH   B O    1 
HETATM 7150 O O    . HOH   E 3 .   ? 47.101 -33.966 -4.665  1.00 19.43 ?  291 HOH   B O    1 
HETATM 7151 O O    . HOH   E 3 .   ? 42.758 -12.198 -18.453 1.00 28.33 ?  292 HOH   B O    1 
HETATM 7152 O O    . HOH   E 3 .   ? 33.571 -15.291 -13.965 1.00 22.85 ?  293 HOH   B O    1 
HETATM 7153 O O    . HOH   E 3 .   ? 59.804 -15.240 8.176   1.00 32.34 ?  294 HOH   B O    1 
HETATM 7154 O O    . HOH   E 3 .   ? 51.225 -37.595 -9.694  1.00 28.18 ?  295 HOH   B O    1 
HETATM 7155 O O    . HOH   E 3 .   ? 37.428 -17.964 13.109  1.00 33.52 ?  296 HOH   B O    1 
HETATM 7156 O O    . HOH   E 3 .   ? 36.834 -12.758 -1.469  1.00 26.85 ?  297 HOH   B O    1 
HETATM 7157 O O    . HOH   E 3 .   ? 52.481 -10.374 13.012  1.00 23.10 ?  298 HOH   B O    1 
HETATM 7158 O O    . HOH   E 3 .   ? 44.649 -27.476 2.016   1.00 17.09 ?  299 HOH   B O    1 
HETATM 7159 O O    . HOH   E 3 .   ? 53.020 -15.996 -12.745 1.00 28.18 ?  300 HOH   B O    1 
HETATM 7160 O O    . HOH   E 3 .   ? 35.143 -33.654 4.621   1.00 33.88 ?  301 HOH   B O    1 
HETATM 7161 O O    . HOH   E 3 .   ? 52.606 -35.645 -8.806  1.00 32.62 ?  302 HOH   B O    1 
HETATM 7162 O O    . HOH   E 3 .   ? 49.946 -24.664 5.842   1.00 35.28 ?  303 HOH   B O    1 
HETATM 7163 O O    . HOH   E 3 .   ? 48.183 -32.636 -16.651 1.00 45.73 ?  304 HOH   B O    1 
HETATM 7164 O O    . HOH   E 3 .   ? 53.463 -30.226 4.550   1.00 19.49 ?  305 HOH   B O    1 
HETATM 7165 O O    . HOH   E 3 .   ? 51.699 -6.020  -7.958  1.00 38.77 ?  306 HOH   B O    1 
HETATM 7166 O O    . HOH   E 3 .   ? 53.675 -12.577 -22.216 1.00 35.98 ?  307 HOH   B O    1 
HETATM 7167 O O    . HOH   E 3 .   ? 62.749 -13.584 4.734   1.00 28.36 ?  308 HOH   B O    1 
HETATM 7168 O O    . HOH   E 3 .   ? 40.311 -10.852 -9.522  1.00 18.57 ?  309 HOH   B O    1 
HETATM 7169 O O    . HOH   E 3 .   ? 25.973 -21.484 -3.500  1.00 18.52 ?  310 HOH   B O    1 
HETATM 7170 O O    . HOH   E 3 .   ? 44.064 -29.380 -4.673  1.00 24.90 ?  311 HOH   B O    1 
HETATM 7171 O O    . HOH   E 3 .   ? 45.858 -40.384 -3.548  1.00 31.50 ?  312 HOH   B O    1 
HETATM 7172 O O    . HOH   E 3 .   ? 37.003 -30.586 -21.003 1.00 32.48 ?  313 HOH   B O    1 
HETATM 7173 O O    . HOH   E 3 .   ? 43.249 -21.420 10.693  1.00 17.09 ?  314 HOH   B O    1 
HETATM 7174 O O    . HOH   E 3 .   ? 38.361 -12.680 7.950   1.00 19.48 ?  315 HOH   B O    1 
HETATM 7175 O O    . HOH   E 3 .   ? 32.857 -34.613 -5.853  1.00 18.72 ?  316 HOH   B O    1 
HETATM 7176 O O    . HOH   E 3 .   ? 52.505 -29.244 -13.122 1.00 26.73 ?  317 HOH   B O    1 
HETATM 7177 O O    . HOH   E 3 .   ? 38.433 -9.360  -13.275 1.00 29.82 ?  318 HOH   B O    1 
HETATM 7178 O O    . HOH   E 3 .   ? 37.903 -10.211 -10.729 1.00 18.75 ?  319 HOH   B O    1 
HETATM 7179 O O    . HOH   E 3 .   ? 41.805 -8.071  1.387   1.00 23.27 ?  320 HOH   B O    1 
HETATM 7180 O O    . HOH   E 3 .   ? 26.376 -21.048 -6.224  1.00 18.05 ?  321 HOH   B O    1 
HETATM 7181 O O    . HOH   E 3 .   ? 44.694 -24.588 9.573   1.00 22.04 ?  322 HOH   B O    1 
HETATM 7182 O O    . HOH   E 3 .   ? 37.301 -35.646 7.277   1.00 34.96 ?  323 HOH   B O    1 
HETATM 7183 O O    . HOH   E 3 .   ? 42.467 -9.735  -14.858 1.00 38.16 ?  324 HOH   B O    1 
HETATM 7184 O O    . HOH   E 3 .   ? 45.702 -36.302 -16.109 1.00 36.29 ?  325 HOH   B O    1 
HETATM 7185 O O    . HOH   E 3 .   ? 47.262 -24.447 8.187   1.00 25.50 ?  326 HOH   B O    1 
HETATM 7186 O O    . HOH   E 3 .   ? 44.157 -1.751  7.597   1.00 49.51 ?  327 HOH   B O    1 
HETATM 7187 O O    . HOH   E 3 .   ? 51.426 -33.071 -10.915 1.00 46.20 ?  328 HOH   B O    1 
HETATM 7188 O O    . HOH   E 3 .   ? 36.765 -12.389 4.289   1.00 18.64 ?  329 HOH   B O    1 
HETATM 7189 O O    . HOH   E 3 .   ? 62.927 -20.184 -0.720  1.00 40.08 ?  330 HOH   B O    1 
HETATM 7190 O O    . HOH   E 3 .   ? 43.176 -34.589 0.110   1.00 23.22 ?  331 HOH   B O    1 
HETATM 7191 O O    . HOH   E 3 .   ? 33.684 -31.185 11.064  1.00 37.16 ?  332 HOH   B O    1 
HETATM 7192 O O    . HOH   E 3 .   ? 57.604 -21.989 3.386   1.00 31.81 ?  333 HOH   B O    1 
HETATM 7193 O O    . HOH   E 3 .   ? 59.982 -17.287 -10.522 1.00 37.06 ?  334 HOH   B O    1 
HETATM 7194 O O    . HOH   E 3 .   ? 27.723 -14.750 -9.519  1.00 39.45 ?  335 HOH   B O    1 
HETATM 7195 O O    . HOH   E 3 .   ? 38.463 -12.156 -16.235 1.00 48.43 ?  336 HOH   B O    1 
HETATM 7196 O O    . HOH   E 3 .   ? 34.456 -10.363 7.758   1.00 22.64 ?  337 HOH   B O    1 
HETATM 7197 O O    . HOH   E 3 .   ? 43.535 -15.395 18.114  1.00 32.15 ?  338 HOH   B O    1 
HETATM 7198 O O    . HOH   E 3 .   ? 47.505 -27.449 2.025   1.00 16.08 ?  339 HOH   B O    1 
HETATM 7199 O O    . HOH   E 3 .   ? 37.078 -15.163 -16.568 1.00 41.94 ?  340 HOH   B O    1 
HETATM 7200 O O    . HOH   E 3 .   ? 42.855 -43.569 -14.370 1.00 43.59 ?  341 HOH   B O    1 
HETATM 7201 O O    . HOH   E 3 .   ? 28.877 -42.830 -12.358 1.00 48.52 ?  342 HOH   B O    1 
HETATM 7202 O O    . HOH   E 3 .   ? 46.844 -19.871 12.271  1.00 31.86 ?  343 HOH   B O    1 
HETATM 7203 O O    . HOH   E 3 .   ? 41.326 -24.510 15.897  1.00 45.98 ?  344 HOH   B O    1 
HETATM 7204 O O    . HOH   E 3 .   ? 37.081 -45.141 -9.687  1.00 36.10 ?  345 HOH   B O    1 
HETATM 7205 O O    . HOH   E 3 .   ? 39.635 -23.594 -20.366 1.00 38.86 ?  346 HOH   B O    1 
HETATM 7206 O O    . HOH   E 3 .   ? 33.035 -14.672 1.041   1.00 22.41 ?  347 HOH   B O    1 
HETATM 7207 O O    . HOH   E 3 .   ? 39.833 -44.173 -11.210 1.00 45.39 ?  348 HOH   B O    1 
HETATM 7208 O O    . HOH   E 3 .   ? 40.378 -43.472 -9.150  1.00 27.41 ?  349 HOH   B O    1 
HETATM 7209 O O    . HOH   E 3 .   ? 38.572 -22.364 15.046  1.00 45.48 ?  350 HOH   B O    1 
HETATM 7210 O O    . HOH   E 3 .   ? 44.238 -37.422 -17.864 1.00 37.23 ?  351 HOH   B O    1 
HETATM 7211 O O    . HOH   E 3 .   ? 62.541 -20.112 -4.826  1.00 46.25 ?  352 HOH   B O    1 
HETATM 7212 O O    . HOH   E 3 .   ? 33.755 -9.571  -8.862  1.00 31.33 ?  353 HOH   B O    1 
HETATM 7213 O O    . HOH   E 3 .   ? 27.815 -26.640 -0.493  1.00 32.76 ?  354 HOH   B O    1 
HETATM 7214 O O    . HOH   E 3 .   ? 55.716 -8.248  10.803  1.00 25.54 ?  355 HOH   B O    1 
HETATM 7215 O O    . HOH   E 3 .   ? 33.994 -7.863  11.488  1.00 40.31 ?  356 HOH   B O    1 
HETATM 7216 O O    . HOH   E 3 .   ? 56.618 -7.279  3.012   1.00 28.26 ?  357 HOH   B O    1 
HETATM 7217 O O    . HOH   E 3 .   ? 23.247 -23.669 6.786   1.00 36.30 ?  358 HOH   B O    1 
HETATM 7218 O O    . HOH   E 3 .   ? 36.145 -8.474  -9.748  1.00 36.02 ?  359 HOH   B O    1 
HETATM 7219 O O    . HOH   E 3 .   ? 61.548 -19.911 1.752   1.00 37.74 ?  360 HOH   B O    1 
HETATM 7220 O O    . HOH   E 3 .   ? 56.938 -21.620 -16.430 1.00 40.54 ?  361 HOH   B O    1 
HETATM 7221 O O    . HOH   E 3 .   ? 40.278 -8.824  9.891   1.00 38.50 ?  362 HOH   B O    1 
HETATM 7222 O O    . HOH   E 3 .   ? 27.169 -25.924 -11.377 1.00 35.80 ?  363 HOH   B O    1 
HETATM 7223 O O    . HOH   E 3 .   ? 40.399 -11.287 -13.910 1.00 34.57 ?  364 HOH   B O    1 
HETATM 7224 O O    . HOH   E 3 .   ? 43.198 -12.626 -21.165 1.00 37.22 ?  365 HOH   B O    1 
HETATM 7225 O O    . HOH   E 3 .   ? 48.317 -26.424 8.793   1.00 42.26 ?  366 HOH   B O    1 
HETATM 7226 O O    . HOH   E 3 .   ? 36.184 -8.639  8.985   1.00 34.72 ?  367 HOH   B O    1 
HETATM 7227 O O    . HOH   E 3 .   ? 54.267 -5.754  2.938   1.00 38.73 ?  368 HOH   B O    1 
HETATM 7228 O O    . HOH   E 3 .   ? 32.609 -23.595 14.073  1.00 40.90 ?  369 HOH   B O    1 
HETATM 7229 O O    . HOH   E 3 .   ? 59.009 -10.452 9.205   1.00 38.70 ?  370 HOH   B O    1 
HETATM 7230 O O    . HOH   E 3 .   ? 39.888 -7.014  7.793   1.00 37.38 ?  371 HOH   B O    1 
HETATM 7231 O O    . HOH   E 3 .   ? 52.079 -12.943 13.303  1.00 28.34 ?  372 HOH   B O    1 
HETATM 7232 O O    . HOH   E 3 .   ? 56.069 -7.807  -0.632  1.00 37.53 ?  373 HOH   B O    1 
HETATM 7233 O O    . HOH   E 3 .   ? 41.845 -10.026 -17.459 1.00 57.61 ?  374 HOH   B O    1 
HETATM 7234 O O    . HOH   E 3 .   ? 63.042 -12.375 7.022   1.00 36.97 ?  375 HOH   B O    1 
HETATM 7235 O O    . HOH   E 3 .   ? 36.535 -22.876 13.262  1.00 32.43 ?  376 HOH   B O    1 
HETATM 7236 O O    . HOH   E 3 .   ? 40.193 -7.709  3.197   1.00 37.35 ?  377 HOH   B O    1 
HETATM 7237 O O    . HOH   E 3 .   ? 42.721 -17.113 -23.143 1.00 43.83 ?  378 HOH   B O    1 
HETATM 7238 O O    . HOH   E 3 .   ? 38.034 -10.499 10.024  1.00 28.52 ?  379 HOH   B O    1 
HETATM 7239 O O    . HOH   E 3 .   ? 41.852 -6.739  -4.852  1.00 47.42 ?  380 HOH   B O    1 
HETATM 7240 O O    . HOH   E 3 .   ? 44.157 -5.602  -3.474  1.00 42.37 ?  381 HOH   B O    1 
HETATM 7241 O O    . HOH   E 3 .   ? 39.660 -14.121 15.635  1.00 51.70 ?  382 HOH   B O    1 
HETATM 7242 O O    . HOH   E 3 .   ? 52.905 -29.925 7.229   1.00 23.85 ?  383 HOH   B O    1 
HETATM 7243 O O    . HOH   E 3 .   ? 46.840 -5.408  2.898   1.00 40.58 ?  384 HOH   B O    1 
HETATM 7244 O O    . HOH   E 3 .   ? 60.520 -22.290 2.936   1.00 50.16 ?  385 HOH   B O    1 
HETATM 7245 O O    . HOH   E 3 .   ? 41.012 -9.749  15.797  1.00 49.38 ?  386 HOH   B O    1 
HETATM 7246 O O    . HOH   E 3 .   ? 23.959 -20.907 -7.656  1.00 29.99 ?  387 HOH   B O    1 
HETATM 7247 O O    . HOH   E 3 .   ? 35.446 -33.738 7.380   1.00 42.68 ?  388 HOH   B O    1 
HETATM 7248 O O    . HOH   E 3 .   ? 35.259 -20.371 13.340  1.00 34.32 ?  389 HOH   B O    1 
HETATM 7249 O O    . HOH   E 3 .   ? 40.784 -6.612  -0.829  1.00 26.47 ?  390 HOH   B O    1 
HETATM 7250 O O    . HOH   E 3 .   ? 23.175 -23.768 1.556   1.00 34.35 ?  391 HOH   B O    1 
HETATM 7251 O O    . HOH   E 3 .   ? 44.205 -31.761 -3.776  1.00 44.34 ?  392 HOH   B O    1 
HETATM 7252 O O    . HOH   E 3 .   ? 27.996 -27.086 2.303   1.00 30.89 ?  393 HOH   B O    1 
HETATM 7253 O O    . HOH   E 3 .   ? 26.623 -27.911 -13.460 1.00 41.30 ?  394 HOH   B O    1 
HETATM 7254 O O    . HOH   E 3 .   ? 50.683 -30.913 8.756   1.00 30.99 ?  395 HOH   B O    1 
HETATM 7255 O O    . HOH   E 3 .   ? 24.662 -20.626 -10.521 1.00 43.06 ?  396 HOH   B O    1 
HETATM 7256 O O    . HOH   E 3 .   ? 34.368 -33.523 9.611   1.00 37.58 ?  397 HOH   B O    1 
HETATM 7257 O O    . HOH   E 3 .   ? 26.830 -30.631 -12.607 1.00 30.38 ?  398 HOH   B O    1 
HETATM 7258 O O    . HOH   E 3 .   ? 45.673 -20.151 15.251  1.00 46.59 ?  399 HOH   B O    1 
HETATM 7259 O O    . HOH   E 3 .   ? 57.627 -6.443  -2.312  1.00 33.14 ?  400 HOH   B O    1 
HETATM 7260 O O    . HOH   E 3 .   ? 40.890 -11.792 -22.251 1.00 39.80 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.7871 0.7898 0.8739 -0.0018 -0.0328 0.0702  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7822 0.7824 0.8419 -0.0053 -0.0221 0.0481  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7828 0.7856 0.8628 -0.0028 -0.0320 0.0698  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7780 0.7788 0.8347 -0.0060 -0.0223 0.0497  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7608 0.7649 0.8338 -0.0089 -0.0298 0.0727  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.7584 0.7612 0.8147 -0.0106 -0.0241 0.0610  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7662 0.7693 0.8515 -0.0079 -0.0318 0.0760  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.7640 0.7655 0.8258 -0.0101 -0.0250 0.0615  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7961 0.7981 0.8698 0.0009  -0.0313 0.0673  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7898 0.7894 0.8408 -0.0031 -0.0199 0.0418  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.8010 0.8026 0.8717 0.0018  -0.0306 0.0666  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7941 0.7932 0.8426 -0.0023 -0.0188 0.0392  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.8001 0.8016 0.8724 0.0027  -0.0306 0.0669  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7933 0.7924 0.8429 -0.0020 -0.0189 0.0394  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.7297 0.7361 0.7715 -0.0168 -0.0234 0.0713  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.6683 0.6804 0.6593 -0.0327 -0.0160 0.0753  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.5899 0.6192 0.5818 -0.0497 0.0045  0.0511  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.5956 0.6235 0.5819 -0.0494 0.0006  0.0559  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.6842 0.6846 0.6153 -0.0332 -0.0275 0.1026  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.6979 0.6874 0.5744 -0.0346 -0.0365 0.1258  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.7035 0.6874 0.5563 -0.0349 -0.0399 0.1328  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.7021 0.6891 0.5624 -0.0348 -0.0385 0.1357  4   ASN   A ND2 
46   N N   A SER   A 5   ? 0.5418 0.5870 0.5392 -0.0666 0.0212  0.0367  5   SER   A N   
47   N N   B SER   A 5   ? 0.5518 0.5818 0.5464 -0.0510 0.0092  0.0369  5   SER   A N   
48   C CA  A SER   A 5   ? 0.4924 0.5512 0.4966 -0.0809 0.0385  0.0227  5   SER   A CA  
49   C CA  B SER   A 5   ? 0.5127 0.5422 0.5094 -0.0513 0.0150  0.0226  5   SER   A CA  
50   C C   A SER   A 5   ? 0.4374 0.5020 0.4301 -0.0933 0.0586  0.0205  5   SER   A C   
51   C C   B SER   A 5   ? 0.4683 0.4957 0.4525 -0.0516 0.0207  0.0148  5   SER   A C   
52   O O   A SER   A 5   ? 0.4410 0.5110 0.4251 -0.0891 0.0656  0.0105  5   SER   A O   
53   O O   B SER   A 5   ? 0.4697 0.4983 0.4497 -0.0505 0.0233  0.0109  5   SER   A O   
54   C CB  A SER   A 5   ? 0.4982 0.5626 0.5181 -0.0807 0.0375  0.0136  5   SER   A CB  
55   C CB  B SER   A 5   ? 0.5172 0.5475 0.5259 -0.0510 0.0155  0.0174  5   SER   A CB  
56   O OG  A SER   A 5   ? 0.5023 0.5716 0.5331 -0.0795 0.0379  0.0086  5   SER   A OG  
57   O OG  B SER   A 5   ? 0.5201 0.5509 0.5366 -0.0508 0.0156  0.0146  5   SER   A OG  
68   N N   A PHE   A 6   ? 0.3768 0.4421 0.3690 -0.1082 0.0729  0.0320  6   PHE   A N   
69   N N   B PHE   A 6   ? 0.4211 0.4459 0.4012 -0.0528 0.0234  0.0127  6   PHE   A N   
70   C CA  A PHE   A 6   ? 0.3193 0.3853 0.3099 -0.1161 0.0772  0.0462  6   PHE   A CA  
71   C CA  B PHE   A 6   ? 0.3744 0.3971 0.3534 -0.0536 0.0251  0.0124  6   PHE   A CA  
72   C C   A PHE   A 6   ? 0.3092 0.3791 0.3068 -0.1173 0.0882  0.0514  6   PHE   A C   
73   C C   B PHE   A 6   ? 0.3519 0.3764 0.3494 -0.0540 0.0291  0.0113  6   PHE   A C   
74   O O   A PHE   A 6   ? 0.3127 0.3852 0.3304 -0.1185 0.0823  0.0632  6   PHE   A O   
75   O O   B PHE   A 6   ? 0.3539 0.3796 0.3621 -0.0516 0.0270  0.0133  6   PHE   A O   
76   C CB  A PHE   A 6   ? 0.2872 0.3437 0.2713 -0.1104 0.0516  0.0500  6   PHE   A CB  
77   C CB  B PHE   A 6   ? 0.3531 0.3713 0.3145 -0.0529 0.0208  0.0124  6   PHE   A CB  
78   C CG  A PHE   A 6   ? 0.2615 0.3117 0.2459 -0.0984 0.0343  0.0535  6   PHE   A CG  
79   C CG  B PHE   A 6   ? 0.3339 0.3481 0.2849 -0.0519 0.0176  0.0136  6   PHE   A CG  
80   C CD1 A PHE   A 6   ? 0.2492 0.2977 0.2263 -0.0844 0.0252  0.0515  6   PHE   A CD1 
81   C CD1 B PHE   A 6   ? 0.3256 0.3378 0.2688 -0.0497 0.0158  0.0148  6   PHE   A CD1 
82   C CD2 A PHE   A 6   ? 0.2669 0.3021 0.2549 -0.0807 0.0247  0.0529  6   PHE   A CD2 
83   C CD2 B PHE   A 6   ? 0.3280 0.3388 0.2811 -0.0497 0.0166  0.0126  6   PHE   A CD2 
84   C CE1 A PHE   A 6   ? 0.2465 0.2890 0.2233 -0.0753 0.0250  0.0568  6   PHE   A CE1 
85   C CE1 B PHE   A 6   ? 0.3200 0.3307 0.2651 -0.0501 0.0144  0.0139  6   PHE   A CE1 
86   C CE2 A PHE   A 6   ? 0.2637 0.2960 0.2561 -0.0711 0.0263  0.0433  6   PHE   A CE2 
87   C CE2 B PHE   A 6   ? 0.3229 0.3308 0.2761 -0.0499 0.0179  0.0127  6   PHE   A CE2 
88   C CZ  A PHE   A 6   ? 0.2546 0.2869 0.2364 -0.0710 0.0245  0.0436  6   PHE   A CZ  
89   C CZ  B PHE   A 6   ? 0.3195 0.3280 0.2690 -0.0499 0.0160  0.0123  6   PHE   A CZ  
108  N N   A SER   A 7   ? 0.2957 0.3646 0.2944 -0.1137 0.0962  0.0396  7   SER   A N   
109  N N   B SER   A 7   ? 0.3279 0.3528 0.3345 -0.0566 0.0327  0.0072  7   SER   A N   
110  C CA  A SER   A 7   ? 0.2895 0.3551 0.3029 -0.0979 0.0942  0.0096  7   SER   A CA  
111  C CA  B SER   A 7   ? 0.3071 0.3317 0.3238 -0.0567 0.0356  0.0001  7   SER   A CA  
112  C C   A SER   A 7   ? 0.2696 0.3227 0.2923 -0.0914 0.1012  0.0117  7   SER   A C   
113  C C   B SER   A 7   ? 0.2875 0.3095 0.3001 -0.0548 0.0388  0.0020  7   SER   A C   
114  O O   A SER   A 7   ? 0.2791 0.3126 0.2930 -0.0963 0.1042  0.0204  7   SER   A O   
115  O O   B SER   A 7   ? 0.2880 0.3070 0.3008 -0.0556 0.0401  0.0011  7   SER   A O   
116  C CB  A SER   A 7   ? 0.3032 0.3744 0.3250 -0.0868 0.0853  -0.0016 7   SER   A CB  
117  C CB  B SER   A 7   ? 0.3077 0.3335 0.3401 -0.0552 0.0335  -0.0078 7   SER   A CB  
118  O OG  A SER   A 7   ? 0.3174 0.3883 0.3535 -0.0764 0.0796  -0.0049 7   SER   A OG  
119  O OG  B SER   A 7   ? 0.3091 0.3363 0.3535 -0.0526 0.0314  -0.0149 7   SER   A OG  
130  N N   A GLY   A 8   ? 0.2447 0.3003 0.2975 -0.0826 0.0912  0.0044  8   GLY   A N   
131  N N   B GLY   A 8   ? 0.2697 0.2909 0.2834 -0.0516 0.0384  -0.0020 8   GLY   A N   
132  C CA  A GLY   A 8   ? 0.2271 0.2799 0.3016 -0.0610 0.0812  0.0117  8   GLY   A CA  
133  C CA  B GLY   A 8   ? 0.2543 0.2734 0.2682 -0.0425 0.0394  -0.0016 8   GLY   A CA  
134  C C   A GLY   A 8   ? 0.2021 0.2610 0.2951 -0.0410 0.0680  0.0177  8   GLY   A C   
135  C C   B GLY   A 8   ? 0.2373 0.2556 0.2545 -0.0350 0.0350  -0.0035 8   GLY   A C   
136  O O   A GLY   A 8   ? 0.1988 0.2641 0.3173 -0.0242 0.0628  0.0001  8   GLY   A O   
137  O O   B GLY   A 8   ? 0.2372 0.2575 0.2622 -0.0317 0.0340  -0.0116 8   GLY   A O   
144  N N   A TYR   A 9   ? 0.1793 0.2410 0.2767 -0.0309 0.0587  0.0380  9   TYR   A N   
145  N N   B TYR   A 9   ? 0.2196 0.2358 0.2345 -0.0280 0.0311  0.0022  9   TYR   A N   
146  C CA  A TYR   A 9   ? 0.1653 0.2228 0.2594 -0.0270 0.0453  0.0510  9   TYR   A CA  
147  C CA  B TYR   A 9   ? 0.2044 0.2199 0.2161 -0.0205 0.0258  0.0097  9   TYR   A CA  
148  C C   A TYR   A 9   ? 0.1611 0.2031 0.2522 -0.0198 0.0507  0.0630  9   TYR   A C   
149  C C   B TYR   A 9   ? 0.2026 0.2114 0.2104 -0.0208 0.0299  0.0215  9   TYR   A C   
150  O O   A TYR   A 9   ? 0.1883 0.2170 0.2795 -0.0247 0.0381  0.0521  9   TYR   A O   
151  O O   B TYR   A 9   ? 0.2113 0.2129 0.2131 -0.0279 0.0289  0.0189  9   TYR   A O   
152  C CB  A TYR   A 9   ? 0.1642 0.2408 0.2596 -0.0228 0.0367  0.0433  9   TYR   A CB  
153  C CB  B TYR   A 9   ? 0.1932 0.2150 0.2108 -0.0118 0.0194  0.0058  9   TYR   A CB  
154  C CG  A TYR   A 9   ? 0.1692 0.2541 0.2475 -0.0131 0.0445  0.0366  9   TYR   A CG  
155  C CG  B TYR   A 9   ? 0.1848 0.2084 0.1962 0.0004  0.0174  0.0108  9   TYR   A CG  
156  C CD1 A TYR   A 9   ? 0.1738 0.2630 0.2523 -0.0262 0.0450  0.0280  9   TYR   A CD1 
157  C CD1 B TYR   A 9   ? 0.1799 0.2022 0.1918 0.0016  0.0186  0.0131  9   TYR   A CD1 
158  C CD2 A TYR   A 9   ? 0.1648 0.2513 0.2398 -0.0117 0.0348  0.0420  9   TYR   A CD2 
159  C CD2 B TYR   A 9   ? 0.1823 0.2035 0.1952 0.0006  0.0132  0.0124  9   TYR   A CD2 
160  C CE1 A TYR   A 9   ? 0.1790 0.2644 0.2539 -0.0275 0.0492  0.0231  9   TYR   A CE1 
161  C CE1 B TYR   A 9   ? 0.1820 0.2019 0.1931 0.0022  0.0136  0.0095  9   TYR   A CE1 
162  C CE2 A TYR   A 9   ? 0.1695 0.2543 0.2443 -0.0141 0.0364  0.0336  9   TYR   A CE2 
163  C CE2 B TYR   A 9   ? 0.1838 0.2035 0.1974 0.0009  0.0131  0.0087  9   TYR   A CE2 
164  C CZ  A TYR   A 9   ? 0.1653 0.2544 0.2581 -0.0307 0.0478  0.0297  9   TYR   A CZ  
165  C CZ  B TYR   A 9   ? 0.1858 0.2048 0.2059 -0.0047 0.0146  0.0078  9   TYR   A CZ  
166  O OH  A TYR   A 9   ? 0.1643 0.2552 0.2806 -0.0357 0.0476  0.0273  9   TYR   A OH  
167  O OH  B TYR   A 9   ? 0.2005 0.2089 0.2277 -0.0091 0.0115  0.0046  9   TYR   A OH  
186  N N   A LEU   A 10  ? 0.1605 0.1872 0.2498 -0.0154 0.0308  0.0578  10  LEU   A N   
187  N N   B LEU   A 10  ? 0.1986 0.2040 0.2096 -0.0173 0.0254  0.0221  10  LEU   A N   
188  C CA  A LEU   A 10  ? 0.1537 0.1853 0.2413 -0.0229 0.0138  0.0684  10  LEU   A CA  
189  C CA  B LEU   A 10  ? 0.1960 0.2041 0.2000 -0.0194 0.0269  0.0320  10  LEU   A CA  
190  C C   A LEU   A 10  ? 0.1553 0.1818 0.2150 -0.0352 -0.0058 0.0575  10  LEU   A C   
191  C C   B LEU   A 10  ? 0.1863 0.1863 0.1904 -0.0247 0.0303  0.0362  10  LEU   A C   
192  O O   A LEU   A 10  ? 0.1663 0.1732 0.1985 -0.0402 0.0116  0.0451  10  LEU   A O   
193  O O   B LEU   A 10  ? 0.1845 0.1834 0.1786 -0.0198 0.0336  0.0283  10  LEU   A O   
194  C CB  A LEU   A 10  ? 0.1622 0.1910 0.2735 -0.0230 -0.0054 0.0811  10  LEU   A CB  
195  C CB  B LEU   A 10  ? 0.2071 0.2260 0.2116 -0.0149 0.0155  0.0312  10  LEU   A CB  
196  C CG  A LEU   A 10  ? 0.1737 0.1944 0.3103 -0.0115 -0.0396 0.0746  10  LEU   A CG  
197  C CG  B LEU   A 10  ? 0.2178 0.2446 0.2163 -0.0099 0.0039  0.0241  10  LEU   A CG  
198  C CD1 A LEU   A 10  ? 0.1966 0.2035 0.3358 -0.0255 -0.0330 0.0635  10  LEU   A CD1 
199  C CD1 B LEU   A 10  ? 0.2170 0.2545 0.2215 -0.0108 0.0016  0.0137  10  LEU   A CD1 
200  C CD2 A LEU   A 10  ? 0.2031 0.2205 0.3254 -0.0132 -0.0240 0.0569  10  LEU   A CD2 
201  C CD2 B LEU   A 10  ? 0.2248 0.2508 0.2183 -0.0052 -0.0063 0.0231  10  LEU   A CD2 
224  N N   A LYS   A 11  ? 0.1601 0.1866 0.2137 -0.0404 -0.0077 0.0607  11  LYS   A N   
225  N N   B LYS   A 11  ? 0.1795 0.1738 0.1903 -0.0339 0.0321  0.0429  11  LYS   A N   
226  C CA  A LYS   A 11  ? 0.1595 0.1883 0.2102 -0.0403 -0.0182 0.0535  11  LYS   A CA  
227  C CA  B LYS   A 11  ? 0.1759 0.1658 0.1933 -0.0412 0.0220  0.0459  11  LYS   A CA  
228  C C   A LYS   A 11  ? 0.1541 0.1985 0.2012 -0.0429 -0.0158 0.0468  11  LYS   A C   
229  C C   B LYS   A 11  ? 0.1659 0.1675 0.1901 -0.0401 0.0283  0.0469  11  LYS   A C   
230  O O   A LYS   A 11  ? 0.1610 0.2270 0.2080 -0.0635 -0.0037 0.0601  11  LYS   A O   
231  O O   B LYS   A 11  ? 0.1678 0.1866 0.2030 -0.0397 0.0226  0.0671  11  LYS   A O   
232  C CB  A LYS   A 11  ? 0.1732 0.1757 0.2035 -0.0410 -0.0161 0.0309  11  LYS   A CB  
233  C CB  B LYS   A 11  ? 0.1856 0.1623 0.1890 -0.0464 0.0167  0.0435  11  LYS   A CB  
234  C CG  A LYS   A 11  ? 0.1868 0.1766 0.2009 -0.0329 -0.0060 0.0288  11  LYS   A CG  
235  C CG  B LYS   A 11  ? 0.1936 0.1564 0.1838 -0.0497 0.0168  0.0491  11  LYS   A CG  
236  C CD  A LYS   A 11  ? 0.1949 0.1766 0.1968 -0.0287 -0.0086 0.0282  11  LYS   A CD  
237  C CD  B LYS   A 11  ? 0.2072 0.1594 0.1895 -0.0439 0.0150  0.0520  11  LYS   A CD  
238  C CE  A LYS   A 11  ? 0.2064 0.1775 0.2068 -0.0101 -0.0024 0.0346  11  LYS   A CE  
239  C CE  B LYS   A 11  ? 0.2137 0.1569 0.1985 -0.0460 0.0149  0.0552  11  LYS   A CE  
240  N NZ  A LYS   A 11  ? 0.2003 0.1781 0.2190 0.0103  -0.0013 0.0360  11  LYS   A NZ  
241  N NZ  B LYS   A 11  ? 0.2145 0.1573 0.2092 -0.0434 0.0136  0.0482  11  LYS   A NZ  
268  N N   A LEU   A 12  ? 0.1511 0.1872 0.1936 -0.0337 -0.0140 0.0359  12  LEU   A N   
269  N N   B LEU   A 12  ? 0.1581 0.1550 0.1792 -0.0400 0.0329  0.0278  12  LEU   A N   
270  C CA  A LEU   A 12  ? 0.1518 0.2002 0.1871 -0.0250 -0.0058 0.0413  12  LEU   A CA  
271  C CA  B LEU   A 12  ? 0.1583 0.1512 0.1718 -0.0299 0.0247  0.0186  12  LEU   A CA  
272  C C   A LEU   A 12  ? 0.1577 0.1922 0.1812 -0.0370 0.0109  0.0366  12  LEU   A C   
273  C C   B LEU   A 12  ? 0.1563 0.1404 0.1671 -0.0305 0.0200  0.0034  12  LEU   A C   
274  O O   A LEU   A 12  ? 0.1679 0.2016 0.1882 -0.0356 0.0078  0.0260  12  LEU   A O   
275  O O   B LEU   A 12  ? 0.1557 0.1384 0.1675 -0.0287 0.0247  -0.0043 12  LEU   A O   
276  C CB  A LEU   A 12  ? 0.1602 0.2112 0.2065 -0.0219 -0.0070 0.0414  12  LEU   A CB  
277  C CB  B LEU   A 12  ? 0.1657 0.1494 0.1764 -0.0224 0.0213  0.0178  12  LEU   A CB  
278  C CG  A LEU   A 12  ? 0.1723 0.2102 0.2289 -0.0225 0.0046  0.0433  12  LEU   A CG  
279  C CG  B LEU   A 12  ? 0.1774 0.1507 0.1888 -0.0142 0.0268  0.0223  12  LEU   A CG  
280  C CD1 A LEU   A 12  ? 0.1867 0.2168 0.2389 -0.0116 0.0177  0.0455  12  LEU   A CD1 
281  C CD1 B LEU   A 12  ? 0.1871 0.1521 0.1893 -0.0096 0.0324  0.0292  12  LEU   A CD1 
282  C CD2 A LEU   A 12  ? 0.1711 0.2118 0.2494 -0.0230 -0.0062 0.0293  12  LEU   A CD2 
283  C CD2 B LEU   A 12  ? 0.1768 0.1540 0.2055 -0.0111 0.0203  0.0156  12  LEU   A CD2 
306  N N   A THR   A 13  ? 0.1543 0.1819 0.1797 -0.0289 0.0137  0.0163  13  THR   A N   
307  N N   B THR   A 13  ? 0.1550 0.1390 0.1703 -0.0261 0.0197  -0.0082 13  THR   A N   
308  C CA  A THR   A 13  ? 0.1630 0.1751 0.1806 -0.0342 0.0185  0.0117  13  THR   A CA  
309  C CA  B THR   A 13  ? 0.1600 0.1481 0.1658 -0.0192 0.0296  -0.0037 13  THR   A CA  
310  C C   A THR   A 13  ? 0.1651 0.1697 0.1837 -0.0334 0.0163  0.0222  13  THR   A C   
311  C C   B THR   A 13  ? 0.1579 0.1498 0.1654 -0.0137 0.0273  0.0006  13  THR   A C   
312  O O   A THR   A 13  ? 0.1721 0.1648 0.1818 -0.0308 0.0120  0.0209  13  THR   A O   
313  O O   B THR   A 13  ? 0.1584 0.1517 0.1595 -0.0040 0.0274  -0.0069 13  THR   A O   
314  C CB  A THR   A 13  ? 0.1716 0.1877 0.1909 -0.0349 0.0175  0.0193  13  THR   A CB  
315  C CB  B THR   A 13  ? 0.1710 0.1573 0.1694 -0.0171 0.0248  -0.0063 13  THR   A CB  
316  O OG1 A THR   A 13  ? 0.1669 0.1902 0.1920 -0.0375 0.0180  0.0278  13  THR   A OG1 
317  O OG1 B THR   A 13  ? 0.1768 0.1516 0.1817 -0.0148 0.0208  -0.0174 13  THR   A OG1 
318  C CG2 A THR   A 13  ? 0.1808 0.2017 0.2121 -0.0290 0.0207  0.0047  13  THR   A CG2 
319  C CG2 B THR   A 13  ? 0.1774 0.1703 0.1629 -0.0155 0.0342  -0.0044 13  THR   A CG2 
334  N N   A ASP   A 14  ? 0.1661 0.1690 0.2099 -0.0387 0.0141  0.0338  14  ASP   A N   
335  N N   B ASP   A 14  ? 0.1608 0.1566 0.1830 -0.0080 0.0202  -0.0006 14  ASP   A N   
336  C CA  A ASP   A 14  ? 0.1725 0.1780 0.2324 -0.0344 0.0031  0.0559  14  ASP   A CA  
337  C CA  B ASP   A 14  ? 0.1631 0.1653 0.1916 -0.0002 0.0182  0.0054  14  ASP   A CA  
338  C C   A ASP   A 14  ? 0.1705 0.1744 0.2100 -0.0288 -0.0010 0.0442  14  ASP   A C   
339  C C   B ASP   A 14  ? 0.1555 0.1519 0.1558 -0.0012 0.0236  0.0082  14  ASP   A C   
340  O O   A ASP   A 14  ? 0.1850 0.1831 0.2157 -0.0364 0.0059  0.0400  14  ASP   A O   
341  O O   B ASP   A 14  ? 0.1602 0.1552 0.1534 0.0011  0.0351  0.0114  14  ASP   A O   
342  C CB  A ASP   A 14  ? 0.1913 0.1998 0.3012 -0.0393 -0.0009 0.0745  14  ASP   A CB  
343  C CB  B ASP   A 14  ? 0.1808 0.1936 0.2408 0.0048  0.0110  0.0058  14  ASP   A CB  
344  C CG  A ASP   A 14  ? 0.2116 0.2539 0.3882 -0.0411 0.0003  0.0737  14  ASP   A CG  
345  C CG  B ASP   A 14  ? 0.1983 0.2231 0.2975 0.0027  0.0007  0.0023  14  ASP   A CG  
346  O OD1 A ASP   A 14  ? 0.2135 0.2647 0.4130 -0.0381 -0.0022 0.0939  14  ASP   A OD1 
347  O OD1 B ASP   A 14  ? 0.2081 0.2297 0.3132 0.0058  -0.0062 0.0109  14  ASP   A OD1 
348  O OD2 A ASP   A 14  ? 0.2292 0.2845 0.4304 -0.0342 -0.0090 0.0441  14  ASP   A OD2 
349  O OD2 B ASP   A 14  ? 0.2043 0.2404 0.3263 0.0051  -0.0046 -0.0068 14  ASP   A OD2 
358  N N   A ASN   A 15  ? 0.1656 0.1638 0.2130 -0.0326 0.0074  0.0454  15  ASN   A N   
359  N N   B ASN   A 15  ? 0.1434 0.1392 0.1366 -0.0125 0.0238  0.0046  15  ASN   A N   
360  C CA  A ASN   A 15  ? 0.1641 0.1644 0.2078 -0.0225 -0.0020 0.0328  15  ASN   A CA  
361  C CA  B ASN   A 15  ? 0.1366 0.1366 0.1516 -0.0144 0.0157  -0.0027 15  ASN   A CA  
362  C C   A ASN   A 15  ? 0.1639 0.1582 0.2097 -0.0232 -0.0027 0.0279  15  ASN   A C   
363  C C   B ASN   A 15  ? 0.1307 0.1331 0.1542 -0.0143 0.0161  -0.0028 15  ASN   A C   
364  O O   A ASN   A 15  ? 0.1707 0.1626 0.2254 -0.0260 -0.0085 0.0238  15  ASN   A O   
365  O O   B ASN   A 15  ? 0.1248 0.1307 0.1647 -0.0103 0.0097  -0.0043 15  ASN   A O   
366  C CB  A ASN   A 15  ? 0.1668 0.1708 0.2068 -0.0151 0.0025  0.0379  15  ASN   A CB  
367  C CB  B ASN   A 15  ? 0.1314 0.1393 0.1541 -0.0183 0.0156  -0.0072 15  ASN   A CB  
368  C CG  A ASN   A 15  ? 0.1633 0.1796 0.2147 -0.0133 0.0152  0.0309  15  ASN   A CG  
369  C CG  B ASN   A 15  ? 0.1248 0.1532 0.1642 -0.0198 0.0282  0.0029  15  ASN   A CG  
370  O OD1 A ASN   A 15  ? 0.1612 0.1813 0.2212 -0.0174 0.0339  0.0255  15  ASN   A OD1 
371  O OD1 B ASN   A 15  ? 0.1301 0.1616 0.1577 -0.0236 0.0328  -0.0022 15  ASN   A OD1 
372  N ND2 A ASN   A 15  ? 0.1724 0.1905 0.2209 -0.0190 0.0039  0.0391  15  ASN   A ND2 
373  N ND2 B ASN   A 15  ? 0.1267 0.1600 0.1714 -0.0217 0.0146  0.0087  15  ASN   A ND2 
386  N N   A VAL   A 16  ? 0.1650 0.1542 0.2096 -0.0220 -0.0019 0.0316  16  VAL   A N   
387  N N   B VAL   A 16  ? 0.1340 0.1358 0.1458 -0.0148 0.0185  -0.0019 16  VAL   A N   
388  C CA  A VAL   A 16  ? 0.1619 0.1587 0.1870 -0.0156 0.0094  0.0262  16  VAL   A CA  
389  C CA  B VAL   A 16  ? 0.1394 0.1359 0.1378 -0.0203 0.0169  -0.0100 16  VAL   A CA  
390  C C   A VAL   A 16  ? 0.1534 0.1619 0.1933 -0.0203 0.0100  0.0312  16  VAL   A C   
391  C C   B VAL   A 16  ? 0.1347 0.1337 0.1348 -0.0150 0.0231  -0.0059 16  VAL   A C   
392  O O   A VAL   A 16  ? 0.1523 0.1602 0.2065 -0.0269 0.0186  0.0223  16  VAL   A O   
393  O O   B VAL   A 16  ? 0.1293 0.1373 0.1459 -0.0220 0.0227  -0.0010 16  VAL   A O   
394  C CB  A VAL   A 16  ? 0.1786 0.1656 0.1638 -0.0051 0.0076  0.0261  16  VAL   A CB  
395  C CB  B VAL   A 16  ? 0.1525 0.1375 0.1338 -0.0247 0.0206  -0.0161 16  VAL   A CB  
396  C CG1 A VAL   A 16  ? 0.1838 0.1752 0.1631 0.0060  0.0048  0.0232  16  VAL   A CG1 
397  C CG1 B VAL   A 16  ? 0.1604 0.1424 0.1365 -0.0254 0.0109  -0.0236 16  VAL   A CG1 
398  C CG2 A VAL   A 16  ? 0.1872 0.1831 0.1806 0.0089  0.0297  0.0171  16  VAL   A CG2 
399  C CG2 B VAL   A 16  ? 0.1549 0.1379 0.1233 -0.0263 0.0330  -0.0196 16  VAL   A CG2 
418  N N   A TYR   A 17  ? 0.1588 0.1501 0.1956 -0.0187 0.0152  0.0365  17  TYR   A N   
419  N N   B TYR   A 17  ? 0.1420 0.1314 0.1456 -0.0053 0.0258  -0.0046 17  TYR   A N   
420  C CA  A TYR   A 17  ? 0.1623 0.1550 0.1912 -0.0264 0.0166  0.0408  17  TYR   A CA  
421  C CA  B TYR   A 17  ? 0.1507 0.1382 0.1613 -0.0026 0.0251  -0.0050 17  TYR   A CA  
422  C C   A TYR   A 17  ? 0.1506 0.1636 0.2118 -0.0221 0.0139  0.0490  17  TYR   A C   
423  C C   B TYR   A 17  ? 0.1531 0.1349 0.1775 -0.0044 0.0220  -0.0042 17  TYR   A C   
424  O O   A TYR   A 17  ? 0.1423 0.1723 0.2060 -0.0239 0.0149  0.0488  17  TYR   A O   
425  O O   B TYR   A 17  ? 0.1493 0.1201 0.1728 -0.0130 0.0218  -0.0144 17  TYR   A O   
426  C CB  A TYR   A 17  ? 0.1714 0.1528 0.1830 -0.0284 0.0068  0.0298  17  TYR   A CB  
427  C CB  B TYR   A 17  ? 0.1479 0.1493 0.1695 -0.0013 0.0195  0.0004  17  TYR   A CB  
428  C CG  A TYR   A 17  ? 0.1873 0.1579 0.1871 -0.0271 0.0069  0.0204  17  TYR   A CG  
429  C CG  B TYR   A 17  ? 0.1546 0.1670 0.1852 0.0059  0.0225  0.0037  17  TYR   A CG  
430  C CD1 A TYR   A 17  ? 0.1985 0.1752 0.1943 -0.0127 0.0153  0.0279  17  TYR   A CD1 
431  C CD1 B TYR   A 17  ? 0.1638 0.1784 0.2009 0.0131  0.0237  -0.0016 17  TYR   A CD1 
432  C CD2 A TYR   A 17  ? 0.2004 0.1570 0.1875 -0.0364 0.0104  0.0157  17  TYR   A CD2 
433  C CD2 B TYR   A 17  ? 0.1597 0.1707 0.1877 0.0050  0.0297  0.0086  17  TYR   A CD2 
434  C CE1 A TYR   A 17  ? 0.2023 0.1782 0.2084 -0.0148 0.0105  0.0319  17  TYR   A CE1 
435  C CE1 B TYR   A 17  ? 0.1732 0.1815 0.1967 0.0132  0.0306  -0.0002 17  TYR   A CE1 
436  C CE2 A TYR   A 17  ? 0.2112 0.1665 0.1907 -0.0293 0.0095  0.0080  17  TYR   A CE2 
437  C CE2 B TYR   A 17  ? 0.1667 0.1729 0.1939 0.0090  0.0299  0.0075  17  TYR   A CE2 
438  C CZ  A TYR   A 17  ? 0.2126 0.1749 0.1977 -0.0231 0.0088  0.0331  17  TYR   A CZ  
439  C CZ  B TYR   A 17  ? 0.1694 0.1787 0.1971 0.0151  0.0294  0.0070  17  TYR   A CZ  
440  O OH  A TYR   A 17  ? 0.2272 0.1772 0.2101 -0.0209 0.0203  0.0314  17  TYR   A OH  
441  O OH  B TYR   A 17  ? 0.1653 0.1835 0.2065 0.0190  0.0304  0.0097  17  TYR   A OH  
460  N N   A ILE   A 18  ? 0.1471 0.1675 0.2260 -0.0203 0.0211  0.0647  18  ILE   A N   
461  N N   B ILE   A 18  ? 0.1634 0.1578 0.1940 -0.0042 0.0216  0.0114  18  ILE   A N   
462  C CA  A ILE   A 18  ? 0.1503 0.1652 0.2405 -0.0115 0.0196  0.0593  18  ILE   A CA  
463  C CA  B ILE   A 18  ? 0.1700 0.1735 0.2050 -0.0123 0.0197  0.0171  18  ILE   A CA  
464  C C   A ILE   A 18  ? 0.1525 0.1741 0.2639 -0.0187 0.0230  0.0697  18  ILE   A C   
465  C C   B ILE   A 18  ? 0.1738 0.1789 0.2141 -0.0164 0.0192  0.0253  18  ILE   A C   
466  O O   A ILE   A 18  ? 0.1380 0.1904 0.2826 -0.0215 0.0297  0.0755  18  ILE   A O   
467  O O   B ILE   A 18  ? 0.1728 0.1855 0.2153 -0.0172 0.0234  0.0313  18  ILE   A O   
468  C CB  A ILE   A 18  ? 0.1625 0.1684 0.2346 -0.0017 0.0186  0.0765  18  ILE   A CB  
469  C CB  B ILE   A 18  ? 0.1767 0.1849 0.2101 -0.0146 0.0213  0.0227  18  ILE   A CB  
470  C CG1 A ILE   A 18  ? 0.1756 0.1847 0.2480 0.0003  0.0093  0.0809  18  ILE   A CG1 
471  C CG1 B ILE   A 18  ? 0.1810 0.1932 0.2158 -0.0171 0.0191  0.0224  18  ILE   A CG1 
472  C CG2 A ILE   A 18  ? 0.1677 0.1758 0.2518 -0.0041 0.0233  0.0705  18  ILE   A CG2 
473  C CG2 B ILE   A 18  ? 0.1818 0.1898 0.2161 -0.0192 0.0197  0.0284  18  ILE   A CG2 
474  C CD1 A ILE   A 18  ? 0.1905 0.2002 0.2650 0.0017  -0.0011 0.0775  18  ILE   A CD1 
475  C CD1 B ILE   A 18  ? 0.1869 0.2033 0.2241 -0.0180 0.0197  0.0285  18  ILE   A CD1 
498  N N   A LYS   A 19  ? 0.1590 0.1778 0.2584 -0.0093 0.0475  0.0586  19  LYS   A N   
499  N N   B LYS   A 19  ? 0.1776 0.1854 0.2253 -0.0183 0.0232  0.0235  19  LYS   A N   
500  C CA  A LYS   A 19  ? 0.1757 0.1923 0.2726 -0.0060 0.0536  0.0515  19  LYS   A CA  
501  C CA  B LYS   A 19  ? 0.1835 0.1953 0.2305 -0.0172 0.0246  0.0226  19  LYS   A CA  
502  C C   A LYS   A 19  ? 0.1695 0.1844 0.2905 0.0053  0.0557  0.0541  19  LYS   A C   
503  C C   B LYS   A 19  ? 0.1739 0.1917 0.2350 -0.0149 0.0290  0.0255  19  LYS   A C   
504  O O   A LYS   A 19  ? 0.1602 0.1800 0.3118 0.0084  0.0387  0.0651  19  LYS   A O   
505  O O   B LYS   A 19  ? 0.1684 0.1891 0.2398 -0.0186 0.0264  0.0255  19  LYS   A O   
506  C CB  A LYS   A 19  ? 0.1860 0.2074 0.2697 -0.0128 0.0583  0.0405  19  LYS   A CB  
507  C CB  B LYS   A 19  ? 0.1948 0.2098 0.2340 -0.0165 0.0230  0.0209  19  LYS   A CB  
508  C CG  A LYS   A 19  ? 0.2178 0.2291 0.2727 -0.0139 0.0537  0.0321  19  LYS   A CG  
509  C CG  B LYS   A 19  ? 0.2051 0.2223 0.2407 -0.0176 0.0183  0.0170  19  LYS   A CG  
510  C CD  A LYS   A 19  ? 0.2408 0.2498 0.2713 -0.0138 0.0545  0.0320  19  LYS   A CD  
511  C CD  B LYS   A 19  ? 0.2103 0.2334 0.2386 -0.0176 0.0128  0.0113  19  LYS   A CD  
512  C CE  A LYS   A 19  ? 0.2573 0.2612 0.2742 -0.0155 0.0414  0.0257  19  LYS   A CE  
513  C CE  B LYS   A 19  ? 0.2147 0.2404 0.2341 -0.0195 0.0077  0.0096  19  LYS   A CE  
514  N NZ  A LYS   A 19  ? 0.2622 0.2668 0.2769 -0.0233 0.0474  0.0202  19  LYS   A NZ  
515  N NZ  B LYS   A 19  ? 0.2144 0.2464 0.2265 -0.0160 0.0065  0.0069  19  LYS   A NZ  
542  N N   A ASN   A 20  ? 0.1821 0.1881 0.3136 0.0024  0.0574  0.0507  20  ASN   A N   
543  N N   B ASN   A 20  ? 0.1717 0.1930 0.2495 -0.0136 0.0292  0.0312  20  ASN   A N   
544  C CA  A ASN   A 20  ? 0.1933 0.2073 0.3252 0.0205  0.0577  0.0439  20  ASN   A CA  
545  C CA  B ASN   A 20  ? 0.1694 0.2000 0.2545 -0.0013 0.0326  0.0291  20  ASN   A CA  
546  C C   A ASN   A 20  ? 0.2082 0.2142 0.3178 0.0107  0.0702  0.0355  20  ASN   A C   
547  C C   B ASN   A 20  ? 0.1861 0.2071 0.2623 -0.0063 0.0443  0.0267  20  ASN   A C   
548  O O   A ASN   A 20  ? 0.2268 0.2362 0.3190 -0.0052 0.0658  0.0288  20  ASN   A O   
549  O O   B ASN   A 20  ? 0.1996 0.2210 0.2755 -0.0091 0.0431  0.0245  20  ASN   A O   
550  C CB  A ASN   A 20  ? 0.2072 0.2194 0.3436 0.0296  0.0622  0.0555  20  ASN   A CB  
551  C CB  B ASN   A 20  ? 0.1597 0.2012 0.2531 0.0045  0.0301  0.0339  20  ASN   A CB  
552  C CG  A ASN   A 20  ? 0.2268 0.2316 0.3718 0.0464  0.0670  0.0600  20  ASN   A CG  
553  C CG  B ASN   A 20  ? 0.1556 0.2030 0.2640 0.0172  0.0248  0.0378  20  ASN   A CG  
554  O OD1 A ASN   A 20  ? 0.2504 0.2406 0.4059 0.0550  0.0766  0.0420  20  ASN   A OD1 
555  O OD1 B ASN   A 20  ? 0.1567 0.1962 0.2768 0.0234  0.0298  0.0242  20  ASN   A OD1 
556  N ND2 A ASN   A 20  ? 0.2383 0.2367 0.3866 0.0525  0.0562  0.0756  20  ASN   A ND2 
557  N ND2 B ASN   A 20  ? 0.1647 0.2092 0.2759 0.0164  0.0200  0.0486  20  ASN   A ND2 
570  N N   A ALA   A 21  ? 0.2066 0.2061 0.3253 0.0088  0.0644  0.0250  21  ALA   A N   
571  N N   B ALA   A 21  ? 0.1881 0.2034 0.2659 -0.0107 0.0458  0.0202  21  ALA   A N   
572  C CA  A ALA   A 21  ? 0.2066 0.2067 0.3247 0.0044  0.0603  0.0386  21  ALA   A CA  
573  C CA  B ALA   A 21  ? 0.1931 0.2033 0.2675 -0.0140 0.0443  0.0188  21  ALA   A CA  
574  C C   A ALA   A 21  ? 0.2006 0.2072 0.3115 0.0052  0.0560  0.0343  21  ALA   A C   
575  C C   B ALA   A 21  ? 0.1832 0.1979 0.2522 -0.0178 0.0516  0.0162  21  ALA   A C   
576  O O   A ALA   A 21  ? 0.2066 0.2094 0.3081 0.0056  0.0482  0.0367  21  ALA   A O   
577  O O   B ALA   A 21  ? 0.1753 0.1912 0.2565 -0.0253 0.0450  0.0137  21  ALA   A O   
578  C CB  A ALA   A 21  ? 0.2175 0.2097 0.3366 -0.0036 0.0557  0.0577  21  ALA   A CB  
579  C CB  B ALA   A 21  ? 0.2026 0.2080 0.2790 -0.0117 0.0316  0.0163  21  ALA   A CB  
590  N N   A ASP   A 22  ? 0.2045 0.2048 0.3141 0.0021  0.0563  0.0365  22  ASP   A N   
591  N N   B ASP   A 22  ? 0.1893 0.1998 0.2461 -0.0121 0.0626  0.0138  22  ASP   A N   
592  C CA  A ASP   A 22  ? 0.2004 0.1937 0.3113 0.0072  0.0460  0.0382  22  ASP   A CA  
593  C CA  B ASP   A 22  ? 0.1945 0.1984 0.2464 -0.0069 0.0586  0.0091  22  ASP   A CA  
594  C C   A ASP   A 22  ? 0.1893 0.1950 0.2661 0.0012  0.0448  0.0402  22  ASP   A C   
595  C C   B ASP   A 22  ? 0.1855 0.1960 0.2187 -0.0179 0.0645  0.0120  22  ASP   A C   
596  O O   A ASP   A 22  ? 0.2047 0.2037 0.2699 -0.0075 0.0449  0.0375  22  ASP   A O   
597  O O   B ASP   A 22  ? 0.1930 0.1962 0.2147 -0.0248 0.0643  0.0017  22  ASP   A O   
598  C CB  A ASP   A 22  ? 0.2242 0.1989 0.3690 0.0094  0.0432  0.0244  22  ASP   A CB  
599  C CB  B ASP   A 22  ? 0.2118 0.2020 0.2769 0.0061  0.0510  0.0016  22  ASP   A CB  
600  C CG  A ASP   A 22  ? 0.2389 0.1990 0.4175 0.0060  0.0302  0.0307  22  ASP   A CG  
601  C CG  B ASP   A 22  ? 0.2239 0.2045 0.3101 0.0183  0.0397  0.0051  22  ASP   A CG  
602  O OD1 A ASP   A 22  ? 0.2338 0.1844 0.4246 -0.0119 0.0126  0.0520  22  ASP   A OD1 
603  O OD1 B ASP   A 22  ? 0.2285 0.2005 0.3131 0.0214  0.0349  0.0027  22  ASP   A OD1 
604  O OD2 A ASP   A 22  ? 0.2536 0.2115 0.4563 0.0278  0.0384  0.0171  22  ASP   A OD2 
605  O OD2 B ASP   A 22  ? 0.2290 0.2169 0.3335 0.0196  0.0305  0.0114  22  ASP   A OD2 
614  N N   A ILE   A 23  ? 0.1863 0.1918 0.2475 0.0047  0.0431  0.0346  23  ILE   A N   
615  N N   B ILE   A 23  ? 0.1761 0.1928 0.2079 -0.0135 0.0581  0.0164  23  ILE   A N   
616  C CA  A ILE   A 23  ? 0.1869 0.1879 0.2327 0.0026  0.0407  0.0354  23  ILE   A CA  
617  C CA  B ILE   A 23  ? 0.1764 0.1962 0.1955 -0.0133 0.0402  0.0181  23  ILE   A CA  
618  C C   A ILE   A 23  ? 0.1873 0.2005 0.2254 0.0011  0.0511  0.0335  23  ILE   A C   
619  C C   B ILE   A 23  ? 0.1850 0.2085 0.1990 -0.0232 0.0425  0.0144  23  ILE   A C   
620  O O   A ILE   A 23  ? 0.1946 0.2164 0.2287 0.0014  0.0412  0.0270  23  ILE   A O   
621  O O   B ILE   A 23  ? 0.1852 0.2059 0.1990 -0.0209 0.0420  0.0176  23  ILE   A O   
622  C CB  A ILE   A 23  ? 0.2009 0.1844 0.2101 0.0063  0.0371  0.0300  23  ILE   A CB  
623  C CB  B ILE   A 23  ? 0.1751 0.1885 0.1762 0.0014  0.0226  0.0185  23  ILE   A CB  
624  C CG1 A ILE   A 23  ? 0.2029 0.1797 0.2011 0.0115  0.0399  0.0259  23  ILE   A CG1 
625  C CG1 B ILE   A 23  ? 0.1732 0.1834 0.1680 0.0039  0.0113  0.0101  23  ILE   A CG1 
626  C CG2 A ILE   A 23  ? 0.2020 0.1873 0.2060 0.0090  0.0377  0.0422  23  ILE   A CG2 
627  C CG2 B ILE   A 23  ? 0.1785 0.1849 0.1680 0.0100  0.0134  0.0209  23  ILE   A CG2 
628  C CD1 A ILE   A 23  ? 0.2113 0.1816 0.2101 0.0111  0.0253  0.0226  23  ILE   A CD1 
629  C CD1 B ILE   A 23  ? 0.1712 0.1833 0.1708 0.0043  -0.0007 0.0080  23  ILE   A CD1 
652  N N   A VAL   A 24  ? 0.1975 0.2053 0.2357 -0.0113 0.0485  0.0248  24  VAL   A N   
653  N N   B VAL   A 24  ? 0.1988 0.2216 0.2149 -0.0344 0.0333  0.0098  24  VAL   A N   
654  C CA  A VAL   A 24  ? 0.2146 0.2166 0.2555 -0.0250 0.0474  0.0127  24  VAL   A CA  
655  C CA  B VAL   A 24  ? 0.2141 0.2325 0.2333 -0.0381 0.0276  0.0098  24  VAL   A CA  
656  C C   A VAL   A 24  ? 0.2167 0.2370 0.2570 -0.0345 0.0502  0.0080  24  VAL   A C   
657  C C   B VAL   A 24  ? 0.2267 0.2500 0.2430 -0.0316 0.0312  0.0056  24  VAL   A C   
658  O O   A VAL   A 24  ? 0.2292 0.2386 0.2597 -0.0269 0.0479  0.0041  24  VAL   A O   
659  O O   B VAL   A 24  ? 0.2322 0.2510 0.2453 -0.0267 0.0312  0.0048  24  VAL   A O   
660  C CB  A VAL   A 24  ? 0.2211 0.2160 0.2781 -0.0297 0.0491  0.0168  24  VAL   A CB  
661  C CB  B VAL   A 24  ? 0.2141 0.2312 0.2481 -0.0474 0.0175  0.0171  24  VAL   A CB  
662  C CG1 A VAL   A 24  ? 0.2289 0.2228 0.2807 -0.0215 0.0485  0.0080  24  VAL   A CG1 
663  C CG1 B VAL   A 24  ? 0.2209 0.2357 0.2584 -0.0450 0.0098  0.0188  24  VAL   A CG1 
664  C CG2 A VAL   A 24  ? 0.2348 0.2281 0.2867 -0.0259 0.0584  0.0286  24  VAL   A CG2 
665  C CG2 B VAL   A 24  ? 0.2127 0.2285 0.2459 -0.0561 0.0175  0.0153  24  VAL   A CG2 
684  N N   A GLU   A 25  ? 0.2191 0.2683 0.2651 -0.0419 0.0700  0.0047  25  GLU   A N   
685  N N   B GLU   A 25  ? 0.2369 0.2704 0.2564 -0.0280 0.0404  0.0010  25  GLU   A N   
686  C CA  A GLU   A 25  ? 0.2372 0.3020 0.2823 -0.0314 0.0801  0.0012  25  GLU   A CA  
687  C CA  B GLU   A 25  ? 0.2508 0.2912 0.2757 -0.0252 0.0417  0.0022  25  GLU   A CA  
688  C C   A GLU   A 25  ? 0.2231 0.3047 0.2499 -0.0427 0.0843  0.0027  25  GLU   A C   
689  C C   B GLU   A 25  ? 0.2427 0.2925 0.2587 -0.0308 0.0427  0.0033  25  GLU   A C   
690  O O   A GLU   A 25  ? 0.2258 0.3193 0.2573 -0.0436 0.0838  0.0028  25  GLU   A O   
691  O O   B GLU   A 25  ? 0.2449 0.2990 0.2661 -0.0281 0.0410  0.0016  25  GLU   A O   
692  C CB  A GLU   A 25  ? 0.2693 0.3327 0.3352 -0.0174 0.0859  0.0104  25  GLU   A CB  
693  C CB  B GLU   A 25  ? 0.2727 0.3095 0.3168 -0.0181 0.0419  0.0071  25  GLU   A CB  
694  C CG  A GLU   A 25  ? 0.3078 0.3616 0.4120 -0.0143 0.0719  0.0141  25  GLU   A CG  
695  C CG  B GLU   A 25  ? 0.2970 0.3265 0.3665 -0.0147 0.0373  0.0109  25  GLU   A CG  
696  C CD  A GLU   A 25  ? 0.3389 0.3860 0.4865 -0.0105 0.0558  0.0108  25  GLU   A CD  
697  C CD  B GLU   A 25  ? 0.3163 0.3401 0.4116 -0.0122 0.0309  0.0102  25  GLU   A CD  
698  O OE1 A GLU   A 25  ? 0.3489 0.3949 0.5056 -0.0074 0.0480  0.0042  25  GLU   A OE1 
699  O OE1 B GLU   A 25  ? 0.3234 0.3454 0.4269 -0.0104 0.0262  0.0095  25  GLU   A OE1 
700  O OE2 A GLU   A 25  ? 0.3523 0.3955 0.5252 -0.0109 0.0474  0.0040  25  GLU   A OE2 
701  O OE2 B GLU   A 25  ? 0.3234 0.3433 0.4323 -0.0127 0.0284  0.0064  25  GLU   A OE2 
714  N N   A GLU   A 26  ? 0.2176 0.2889 0.2481 -0.0565 0.0863  -0.0000 26  GLU   A N   
715  N N   B GLU   A 26  ? 0.2355 0.2847 0.2432 -0.0415 0.0504  0.0044  26  GLU   A N   
716  C CA  A GLU   A 26  ? 0.2339 0.2805 0.2463 -0.0692 0.0801  0.0026  26  GLU   A CA  
717  C CA  B GLU   A 26  ? 0.2346 0.2780 0.2294 -0.0510 0.0544  0.0074  26  GLU   A CA  
718  C C   A GLU   A 26  ? 0.2284 0.2674 0.2241 -0.0635 0.0625  0.0042  26  GLU   A C   
719  C C   B GLU   A 26  ? 0.2261 0.2648 0.2172 -0.0556 0.0556  0.0052  26  GLU   A C   
720  O O   A GLU   A 26  ? 0.2344 0.2620 0.2130 -0.0716 0.0526  0.0056  26  GLU   A O   
721  O O   B GLU   A 26  ? 0.2300 0.2629 0.2113 -0.0567 0.0542  -0.0013 26  GLU   A O   
722  C CB  A GLU   A 26  ? 0.2621 0.2837 0.2906 -0.0847 0.0719  0.0079  26  GLU   A CB  
723  C CB  B GLU   A 26  ? 0.2442 0.2826 0.2335 -0.0554 0.0446  0.0134  26  GLU   A CB  
724  C CG  A GLU   A 26  ? 0.2841 0.3007 0.3526 -0.0902 0.0767  -0.0044 26  GLU   A CG  
725  C CG  B GLU   A 26  ? 0.2548 0.2894 0.2518 -0.0553 0.0309  0.0116  26  GLU   A CG  
726  C CD  A GLU   A 26  ? 0.2920 0.3110 0.3781 -0.0970 0.1037  -0.0167 26  GLU   A CD  
727  C CD  B GLU   A 26  ? 0.2570 0.2918 0.2511 -0.0573 0.0270  0.0121  26  GLU   A CD  
728  O OE1 A GLU   A 26  ? 0.2827 0.3303 0.3687 -0.0878 0.1308  -0.0613 26  GLU   A OE1 
729  O OE1 B GLU   A 26  ? 0.2630 0.2910 0.2407 -0.0623 0.0276  0.0203  26  GLU   A OE1 
730  O OE2 A GLU   A 26  ? 0.3038 0.3131 0.3904 -0.0994 0.1132  0.0014  26  GLU   A OE2 
731  O OE2 B GLU   A 26  ? 0.2534 0.2945 0.2514 -0.0557 0.0207  0.0058  26  GLU   A OE2 
744  N N   . ALA   A 27  ? 0.2124 0.2520 0.2136 -0.0604 0.0579  0.0100  27  ALA   A N   
745  C CA  . ALA   A 27  ? 0.2188 0.2669 0.2055 -0.0522 0.0549  0.0054  27  ALA   A CA  
746  C C   . ALA   A 27  ? 0.2602 0.2977 0.2094 -0.0577 0.0600  -0.0178 27  ALA   A C   
747  O O   . ALA   A 27  ? 0.2584 0.2816 0.2187 -0.0687 0.0491  -0.0102 27  ALA   A O   
748  C CB  . ALA   A 27  ? 0.2065 0.2544 0.2067 -0.0507 0.0468  0.0055  27  ALA   A CB  
755  N N   A LYS   A 28  ? 0.2935 0.3244 0.2270 -0.0494 0.0573  -0.0445 28  LYS   A N   
756  N N   B LYS   A 28  ? 0.2967 0.3261 0.2454 -0.0452 0.0500  -0.0235 28  LYS   A N   
757  C CA  A LYS   A 28  ? 0.3273 0.3637 0.2616 -0.0358 0.0614  -0.0678 28  LYS   A CA  
758  C CA  B LYS   A 28  ? 0.3322 0.3587 0.2930 -0.0307 0.0390  -0.0303 28  LYS   A CA  
759  C C   A LYS   A 28  ? 0.3453 0.3936 0.2598 -0.0421 0.0822  -0.0578 28  LYS   A C   
760  C C   B LYS   A 28  ? 0.3507 0.3774 0.3073 -0.0277 0.0382  -0.0265 28  LYS   A C   
761  O O   A LYS   A 28  ? 0.3537 0.4012 0.2927 -0.0384 0.0643  -0.0581 28  LYS   A O   
762  O O   B LYS   A 28  ? 0.3539 0.3811 0.3170 -0.0258 0.0347  -0.0274 28  LYS   A O   
763  C CB  A LYS   A 28  ? 0.3478 0.3783 0.3173 -0.0185 0.0462  -0.0802 28  LYS   A CB  
764  C CB  B LYS   A 28  ? 0.3497 0.3732 0.3322 -0.0208 0.0286  -0.0349 28  LYS   A CB  
765  C CG  A LYS   A 28  ? 0.3660 0.3900 0.3742 -0.0066 0.0385  -0.0814 28  LYS   A CG  
766  C CG  B LYS   A 28  ? 0.3651 0.3845 0.3730 -0.0138 0.0226  -0.0358 28  LYS   A CG  
767  C CD  A LYS   A 28  ? 0.3802 0.4052 0.4362 0.0033  0.0293  -0.0862 28  LYS   A CD  
768  C CD  B LYS   A 28  ? 0.3780 0.3956 0.4132 -0.0084 0.0163  -0.0379 28  LYS   A CD  
769  C CE  A LYS   A 28  ? 0.3912 0.4161 0.4873 0.0092  0.0194  -0.0892 28  LYS   A CE  
770  C CE  B LYS   A 28  ? 0.3876 0.4036 0.4465 -0.0053 0.0104  -0.0399 28  LYS   A CE  
771  N NZ  A LYS   A 28  ? 0.4001 0.4222 0.5182 0.0133  0.0160  -0.0863 28  LYS   A NZ  
772  N NZ  B LYS   A 28  ? 0.3936 0.4083 0.4656 -0.0030 0.0080  -0.0403 28  LYS   A NZ  
799  N N   A LYS   A 29  ? 0.3526 0.4166 0.2474 -0.0564 0.1152  -0.0343 29  LYS   A N   
800  N N   B LYS   A 29  ? 0.3645 0.3912 0.3192 -0.0289 0.0402  -0.0182 29  LYS   A N   
801  C CA  A LYS   A 29  ? 0.3724 0.4400 0.2787 -0.0672 0.1253  -0.0140 29  LYS   A CA  
802  C CA  B LYS   A 29  ? 0.3796 0.4040 0.3385 -0.0299 0.0391  -0.0101 29  LYS   A CA  
803  C C   A LYS   A 29  ? 0.3731 0.4277 0.2666 -0.0823 0.1070  -0.0019 29  LYS   A C   
804  C C   B LYS   A 29  ? 0.3765 0.3947 0.3144 -0.0353 0.0313  -0.0039 29  LYS   A C   
805  O O   A LYS   A 29  ? 0.3819 0.4370 0.2992 -0.0758 0.0989  -0.0107 29  LYS   A O   
806  O O   B LYS   A 29  ? 0.3770 0.3976 0.3177 -0.0349 0.0315  -0.0041 29  LYS   A O   
807  C CB  A LYS   A 29  ? 0.3900 0.4723 0.3317 -0.0575 0.1403  -0.0097 29  LYS   A CB  
808  C CB  B LYS   A 29  ? 0.3958 0.4232 0.3868 -0.0245 0.0425  -0.0079 29  LYS   A CB  
809  C CG  A LYS   A 29  ? 0.4103 0.4997 0.4037 -0.0460 0.1427  -0.0085 29  LYS   A CG  
810  C CG  B LYS   A 29  ? 0.4107 0.4392 0.4348 -0.0188 0.0450  -0.0070 29  LYS   A CG  
811  C CD  A LYS   A 29  ? 0.4270 0.5227 0.4723 -0.0375 0.1398  -0.0059 29  LYS   A CD  
812  C CD  B LYS   A 29  ? 0.4228 0.4528 0.4776 -0.0147 0.0458  -0.0049 29  LYS   A CD  
813  C CE  A LYS   A 29  ? 0.4392 0.5378 0.5198 -0.0340 0.1349  -0.0004 29  LYS   A CE  
814  C CE  B LYS   A 29  ? 0.4317 0.4625 0.5083 -0.0131 0.0454  -0.0025 29  LYS   A CE  
815  N NZ  A LYS   A 29  ? 0.4445 0.5457 0.5471 -0.0319 0.1322  -0.0010 29  LYS   A NZ  
816  N NZ  B LYS   A 29  ? 0.4357 0.4671 0.5252 -0.0123 0.0451  -0.0019 29  LYS   A NZ  
843  N N   A VAL   A 30  ? 0.3622 0.4054 0.2351 -0.1027 0.0988  0.0139  30  VAL   A N   
844  N N   B VAL   A 30  ? 0.3722 0.3820 0.2896 -0.0416 0.0253  0.0020  30  VAL   A N   
845  C CA  A VAL   A 30  ? 0.3552 0.3834 0.2145 -0.1217 0.0707  0.0290  30  VAL   A CA  
846  C CA  B VAL   A 30  ? 0.3676 0.3692 0.2709 -0.0487 0.0142  0.0090  30  VAL   A CA  
847  C C   A VAL   A 30  ? 0.3542 0.3665 0.1735 -0.1246 0.0568  0.0339  30  VAL   A C   
848  C C   B VAL   A 30  ? 0.3661 0.3608 0.2518 -0.0524 0.0083  0.0097  30  VAL   A C   
849  O O   A VAL   A 30  ? 0.3589 0.3671 0.1793 -0.1234 0.0496  0.0362  30  VAL   A O   
850  O O   B VAL   A 30  ? 0.3670 0.3605 0.2471 -0.0514 0.0050  0.0101  30  VAL   A O   
851  C CB  A VAL   A 30  ? 0.3504 0.3767 0.2431 -0.1341 0.0538  0.0359  30  VAL   A CB  
852  C CB  B VAL   A 30  ? 0.3643 0.3640 0.2778 -0.0517 0.0107  0.0137  30  VAL   A CB  
853  C CG1 A VAL   A 30  ? 0.3585 0.3779 0.2587 -0.1322 0.0363  0.0363  30  VAL   A CG1 
854  C CG1 B VAL   A 30  ? 0.3657 0.3635 0.2811 -0.0516 0.0075  0.0149  30  VAL   A CG1 
855  C CG2 A VAL   A 30  ? 0.3439 0.3731 0.2665 -0.1425 0.0583  0.0389  30  VAL   A CG2 
856  C CG2 B VAL   A 30  ? 0.3622 0.3615 0.2831 -0.0535 0.0128  0.0174  30  VAL   A CG2 
875  N N   A LYS   A 31  ? 0.3497 0.3496 0.1643 -0.1239 0.0363  0.0318  31  LYS   A N   
876  N N   B LYS   A 31  ? 0.3631 0.3527 0.2487 -0.0577 0.0035  0.0112  31  LYS   A N   
877  C CA  A LYS   A 31  ? 0.3586 0.3468 0.1931 -0.1031 0.0055  0.0212  31  LYS   A CA  
878  C CA  B LYS   A 31  ? 0.3608 0.3477 0.2570 -0.0601 -0.0032 0.0141  31  LYS   A CA  
879  C C   A LYS   A 31  ? 0.3300 0.3244 0.1497 -0.0890 0.0008  0.0549  31  LYS   A C   
880  C C   B LYS   A 31  ? 0.3325 0.3250 0.1978 -0.0685 -0.0019 0.0360  31  LYS   A C   
881  O O   A LYS   A 31  ? 0.3293 0.3304 0.1651 -0.0873 -0.0117 0.0609  31  LYS   A O   
882  O O   B LYS   A 31  ? 0.3351 0.3276 0.2005 -0.0658 -0.0055 0.0394  31  LYS   A O   
883  C CB  A LYS   A 31  ? 0.3976 0.3717 0.3055 -0.0907 -0.0158 -0.0084 31  LYS   A CB  
884  C CB  B LYS   A 31  ? 0.3850 0.3662 0.3357 -0.0537 -0.0108 -0.0003 31  LYS   A CB  
885  C CG  A LYS   A 31  ? 0.4348 0.3959 0.4264 -0.0770 -0.0323 -0.0297 31  LYS   A CG  
886  C CG  B LYS   A 31  ? 0.4075 0.3846 0.4135 -0.0477 -0.0177 -0.0116 31  LYS   A CG  
887  C CD  A LYS   A 31  ? 0.4648 0.4134 0.5165 -0.0659 -0.0506 -0.0467 31  LYS   A CD  
888  C CD  B LYS   A 31  ? 0.4253 0.3990 0.4760 -0.0425 -0.0259 -0.0214 31  LYS   A CD  
889  C CE  A LYS   A 31  ? 0.4859 0.4263 0.5744 -0.0583 -0.0623 -0.0593 31  LYS   A CE  
890  C CE  B LYS   A 31  ? 0.4377 0.4087 0.5188 -0.0392 -0.0315 -0.0289 31  LYS   A CE  
891  N NZ  A LYS   A 31  ? 0.4985 0.4343 0.6010 -0.0537 -0.0659 -0.0639 31  LYS   A NZ  
892  N NZ  B LYS   A 31  ? 0.4454 0.4139 0.5397 -0.0373 -0.0335 -0.0322 31  LYS   A NZ  
919  N N   . PRO   A 32  ? 0.2989 0.2995 0.1537 -0.0827 0.0036  0.0467  32  PRO   A N   
920  C CA  . PRO   A 32  ? 0.2822 0.2785 0.1703 -0.0738 -0.0102 0.0640  32  PRO   A CA  
921  C C   . PRO   A 32  ? 0.2742 0.2719 0.1805 -0.0605 -0.0157 0.0722  32  PRO   A C   
922  O O   . PRO   A 32  ? 0.2715 0.2621 0.1830 -0.0595 -0.0329 0.0643  32  PRO   A O   
923  C CB  . PRO   A 32  ? 0.2709 0.2774 0.1806 -0.0738 -0.0136 0.0483  32  PRO   A CB  
924  C CG  . PRO   A 32  ? 0.2684 0.2856 0.1463 -0.0655 -0.0190 0.0320  32  PRO   A CG  
925  C CD  . PRO   A 32  ? 0.2748 0.2893 0.1388 -0.0752 -0.0102 0.0374  32  PRO   A CD  
933  N N   . THR   A 33  ? 0.2727 0.2687 0.1752 -0.0545 -0.0158 0.0694  33  THR   A N   
934  C CA  . THR   A 33  ? 0.2700 0.2682 0.1693 -0.0390 -0.0393 0.0633  33  THR   A CA  
935  C C   . THR   A 33  ? 0.2389 0.2468 0.1717 -0.0429 -0.0351 0.0549  33  THR   A C   
936  O O   . THR   A 33  ? 0.2316 0.2430 0.1777 -0.0416 -0.0475 0.0564  33  THR   A O   
937  C CB  . THR   A 33  ? 0.2947 0.2874 0.1997 -0.0283 -0.0493 0.0797  33  THR   A CB  
938  O OG1 . THR   A 33  ? 0.3176 0.3068 0.2289 -0.0175 -0.0419 0.0915  33  THR   A OG1 
939  C CG2 . THR   A 33  ? 0.2967 0.2929 0.2156 -0.0235 -0.0498 0.0725  33  THR   A CG2 
947  N N   . VAL   A 34  ? 0.2128 0.2269 0.1491 -0.0406 -0.0237 0.0463  34  VAL   A N   
948  C CA  . VAL   A 34  ? 0.1966 0.2023 0.1405 -0.0286 -0.0173 0.0440  34  VAL   A CA  
949  C C   . VAL   A 34  ? 0.1872 0.1917 0.1462 -0.0318 -0.0042 0.0374  34  VAL   A C   
950  O O   . VAL   A 34  ? 0.1866 0.1921 0.1759 -0.0369 0.0001  0.0436  34  VAL   A O   
951  C CB  . VAL   A 34  ? 0.1977 0.1932 0.1662 -0.0281 -0.0040 0.0338  34  VAL   A CB  
952  C CG1 . VAL   A 34  ? 0.2086 0.1938 0.1646 -0.0222 -0.0034 0.0172  34  VAL   A CG1 
953  C CG2 . VAL   A 34  ? 0.2051 0.2060 0.1975 -0.0194 -0.0132 0.0377  34  VAL   A CG2 
963  N N   . VAL   A 35  ? 0.1714 0.1781 0.1386 -0.0286 -0.0072 0.0303  35  VAL   A N   
964  C CA  . VAL   A 35  ? 0.1636 0.1737 0.1468 -0.0264 0.0029  0.0246  35  VAL   A CA  
965  C C   . VAL   A 35  ? 0.1531 0.1568 0.1484 -0.0191 0.0061  0.0231  35  VAL   A C   
966  O O   . VAL   A 35  ? 0.1492 0.1706 0.1658 -0.0229 0.0123  0.0205  35  VAL   A O   
967  C CB  . VAL   A 35  ? 0.1687 0.1782 0.1657 -0.0149 0.0144  0.0123  35  VAL   A CB  
968  C CG1 . VAL   A 35  ? 0.1788 0.1770 0.1777 -0.0039 0.0039  0.0105  35  VAL   A CG1 
969  C CG2 . VAL   A 35  ? 0.1645 0.1786 0.1935 -0.0121 0.0206  0.0112  35  VAL   A CG2 
979  N N   . VAL   A 36  ? 0.1401 0.1523 0.1449 -0.0185 0.0077  0.0270  36  VAL   A N   
980  C CA  . VAL   A 36  ? 0.1392 0.1445 0.1500 -0.0143 0.0111  0.0236  36  VAL   A CA  
981  C C   . VAL   A 36  ? 0.1350 0.1475 0.1655 -0.0195 0.0065  0.0237  36  VAL   A C   
982  O O   . VAL   A 36  ? 0.1378 0.1428 0.1813 -0.0102 0.0168  0.0198  36  VAL   A O   
983  C CB  . VAL   A 36  ? 0.1391 0.1361 0.1536 -0.0110 0.0078  0.0239  36  VAL   A CB  
984  C CG1 . VAL   A 36  ? 0.1423 0.1402 0.1735 -0.0165 0.0049  0.0080  36  VAL   A CG1 
985  C CG2 . VAL   A 36  ? 0.1489 0.1417 0.1742 -0.0092 -0.0063 0.0288  36  VAL   A CG2 
995  N N   . ASN   A 37  ? 0.1306 0.1348 0.1393 -0.0052 0.0012  0.0209  37  ASN   A N   
996  C CA  . ASN   A 37  ? 0.1342 0.1347 0.1300 -0.0019 0.0040  0.0216  37  ASN   A CA  
997  C C   . ASN   A 37  ? 0.1294 0.1282 0.1381 -0.0077 0.0147  0.0339  37  ASN   A C   
998  O O   . ASN   A 37  ? 0.1417 0.1400 0.1377 0.0020  0.0102  0.0139  37  ASN   A O   
999  C CB  . ASN   A 37  ? 0.1380 0.1335 0.1448 -0.0020 0.0022  0.0108  37  ASN   A CB  
1000 C CG  . ASN   A 37  ? 0.1357 0.1320 0.1675 0.0054  0.0078  0.0164  37  ASN   A CG  
1001 O OD1 . ASN   A 37  ? 0.1351 0.1353 0.1827 -0.0016 0.0064  0.0207  37  ASN   A OD1 
1002 N ND2 . ASN   A 37  ? 0.1353 0.1355 0.1689 -0.0025 0.0053  0.0311  37  ASN   A ND2 
1009 N N   A ALA   A 38  ? 0.1294 0.1420 0.1557 -0.0027 0.0121  0.0221  38  ALA   A N   
1010 N N   B ALA   A 38  ? 0.1335 0.1358 0.1428 -0.0118 0.0043  0.0280  38  ALA   A N   
1011 C CA  A ALA   A 38  ? 0.1341 0.1476 0.1518 -0.0059 -0.0007 0.0131  38  ALA   A CA  
1012 C CA  B ALA   A 38  ? 0.1395 0.1421 0.1434 -0.0184 -0.0080 0.0230  38  ALA   A CA  
1013 C C   A ALA   A 38  ? 0.1273 0.1448 0.1514 0.0025  -0.0028 0.0041  38  ALA   A C   
1014 C C   B ALA   A 38  ? 0.1364 0.1463 0.1492 -0.0060 -0.0141 0.0183  38  ALA   A C   
1015 O O   A ALA   A 38  ? 0.1239 0.1362 0.1592 -0.0011 -0.0084 0.0121  38  ALA   A O   
1016 O O   B ALA   A 38  ? 0.1304 0.1448 0.1661 -0.0053 -0.0228 0.0162  38  ALA   A O   
1017 C CB  A ALA   A 38  ? 0.1339 0.1582 0.1757 -0.0166 0.0007  0.0165  38  ALA   A CB  
1018 C CB  B ALA   A 38  ? 0.1458 0.1457 0.1522 -0.0273 -0.0157 0.0093  38  ALA   A CB  
1029 N N   A ALA   A 39  ? 0.1301 0.1387 0.1624 -0.0013 0.0013  0.0157  39  ALA   A N   
1030 N N   B ALA   A 39  ? 0.1425 0.1475 0.1489 -0.0045 -0.0056 0.0274  39  ALA   A N   
1031 C CA  A ALA   A 39  ? 0.1259 0.1262 0.1547 0.0017  0.0079  0.0097  39  ALA   A CA  
1032 C CA  B ALA   A 39  ? 0.1471 0.1526 0.1471 -0.0042 -0.0024 0.0204  39  ALA   A CA  
1033 C C   A ALA   A 39  ? 0.1243 0.1301 0.1556 -0.0021 -0.0034 0.0076  39  ALA   A C   
1034 C C   B ALA   A 39  ? 0.1416 0.1470 0.1460 -0.0082 0.0077  0.0204  39  ALA   A C   
1035 O O   A ALA   A 39  ? 0.1474 0.1371 0.1608 -0.0011 0.0003  0.0081  39  ALA   A O   
1036 O O   B ALA   A 39  ? 0.1482 0.1476 0.1419 -0.0160 0.0219  0.0187  39  ALA   A O   
1037 C CB  A ALA   A 39  ? 0.1206 0.1246 0.1705 0.0086  -0.0062 0.0034  39  ALA   A CB  
1038 C CB  B ALA   A 39  ? 0.1623 0.1607 0.1567 0.0046  -0.0087 0.0116  39  ALA   A CB  
1049 N N   A ASN   A 40  ? 0.1344 0.1369 0.1579 -0.0056 0.0092  0.0068  40  ASN   A N   
1050 N N   B ASN   A 40  ? 0.1397 0.1436 0.1397 -0.0011 0.0137  0.0245  40  ASN   A N   
1051 C CA  A ASN   A 40  ? 0.1459 0.1352 0.1572 -0.0044 0.0094  0.0068  40  ASN   A CA  
1052 C CA  B ASN   A 40  ? 0.1400 0.1378 0.1428 0.0071  0.0058  0.0245  40  ASN   A CA  
1053 C C   A ASN   A 40  ? 0.1485 0.1254 0.1423 -0.0095 0.0196  0.0225  40  ASN   A C   
1054 C C   B ASN   A 40  ? 0.1398 0.1337 0.1371 0.0075  0.0111  0.0258  40  ASN   A C   
1055 O O   A ASN   A 40  ? 0.1432 0.1293 0.1570 -0.0102 0.0083  0.0199  40  ASN   A O   
1056 O O   B ASN   A 40  ? 0.1316 0.1377 0.1432 0.0071  0.0055  0.0212  40  ASN   A O   
1057 C CB  A ASN   A 40  ? 0.1665 0.1478 0.1726 0.0044  -0.0054 0.0120  40  ASN   A CB  
1058 C CB  B ASN   A 40  ? 0.1470 0.1403 0.1482 0.0063  0.0082  0.0260  40  ASN   A CB  
1059 C CG  A ASN   A 40  ? 0.1778 0.1439 0.2017 0.0014  -0.0091 0.0120  40  ASN   A CG  
1060 C CG  B ASN   A 40  ? 0.1477 0.1396 0.1486 -0.0010 0.0179  0.0230  40  ASN   A CG  
1061 O OD1 A ASN   A 40  ? 0.1793 0.1446 0.2244 -0.0002 -0.0104 0.0085  40  ASN   A OD1 
1062 O OD1 B ASN   A 40  ? 0.1461 0.1408 0.1539 -0.0096 0.0299  0.0205  40  ASN   A OD1 
1063 N ND2 A ASN   A 40  ? 0.1834 0.1534 0.2229 0.0060  -0.0079 -0.0004 40  ASN   A ND2 
1064 N ND2 B ASN   A 40  ? 0.1499 0.1471 0.1671 0.0013  0.0193  0.0103  40  ASN   A ND2 
1077 N N   A VAL   A 41  ? 0.1510 0.1322 0.1531 -0.0068 0.0166  0.0200  41  VAL   A N   
1078 N N   B VAL   A 41  ? 0.1467 0.1335 0.1379 0.0084  0.0155  0.0264  41  VAL   A N   
1079 C CA  A VAL   A 41  ? 0.1541 0.1348 0.1710 -0.0049 0.0219  0.0175  41  VAL   A CA  
1080 C CA  B VAL   A 41  ? 0.1577 0.1350 0.1495 0.0081  0.0264  0.0210  41  VAL   A CA  
1081 C C   A VAL   A 41  ? 0.1514 0.1360 0.1698 -0.0011 0.0238  0.0213  41  VAL   A C   
1082 C C   B VAL   A 41  ? 0.1568 0.1322 0.1503 0.0062  0.0251  0.0232  41  VAL   A C   
1083 O O   A VAL   A 41  ? 0.1541 0.1321 0.1829 -0.0042 0.0183  0.0100  41  VAL   A O   
1084 O O   B VAL   A 41  ? 0.1620 0.1274 0.1562 0.0067  0.0233  0.0155  41  VAL   A O   
1085 C CB  A VAL   A 41  ? 0.1672 0.1506 0.1718 -0.0134 0.0365  0.0036  41  VAL   A CB  
1086 C CB  B VAL   A 41  ? 0.1718 0.1481 0.1613 0.0012  0.0366  0.0113  41  VAL   A CB  
1087 C CG1 A VAL   A 41  ? 0.1732 0.1578 0.1781 -0.0027 0.0301  -0.0032 41  VAL   A CG1 
1088 C CG1 B VAL   A 41  ? 0.1832 0.1546 0.1746 -0.0003 0.0462  0.0001  41  VAL   A CG1 
1089 C CG2 A VAL   A 41  ? 0.1931 0.1615 0.1712 -0.0193 0.0439  0.0117  41  VAL   A CG2 
1090 C CG2 B VAL   A 41  ? 0.1833 0.1519 0.1638 -0.0061 0.0370  0.0120  41  VAL   A CG2 
1109 N N   A TYR   A 42  ? 0.1415 0.1305 0.1918 -0.0011 0.0280  0.0286  42  TYR   A N   
1110 N N   B TYR   A 42  ? 0.1512 0.1303 0.1587 0.0056  0.0310  0.0306  42  TYR   A N   
1111 C CA  A TYR   A 42  ? 0.1438 0.1329 0.1907 -0.0074 0.0268  0.0263  42  TYR   A CA  
1112 C CA  B TYR   A 42  ? 0.1508 0.1334 0.1578 0.0041  0.0253  0.0320  42  TYR   A CA  
1113 C C   A TYR   A 42  ? 0.1382 0.1312 0.1787 -0.0072 0.0202  0.0255  42  TYR   A C   
1114 C C   B TYR   A 42  ? 0.1456 0.1343 0.1565 0.0013  0.0185  0.0267  42  TYR   A C   
1115 O O   A TYR   A 42  ? 0.1416 0.1346 0.2125 -0.0217 0.0222  0.0015  42  TYR   A O   
1116 O O   B TYR   A 42  ? 0.1453 0.1379 0.1736 -0.0013 0.0180  0.0187  42  TYR   A O   
1117 C CB  A TYR   A 42  ? 0.1617 0.1443 0.1792 -0.0088 0.0362  0.0286  42  TYR   A CB  
1118 C CB  B TYR   A 42  ? 0.1597 0.1372 0.1516 0.0059  0.0149  0.0393  42  TYR   A CB  
1119 C CG  A TYR   A 42  ? 0.1740 0.1541 0.1858 -0.0097 0.0373  0.0349  42  TYR   A CG  
1120 C CG  B TYR   A 42  ? 0.1675 0.1422 0.1545 0.0098  0.0017  0.0428  42  TYR   A CG  
1121 C CD1 A TYR   A 42  ? 0.1767 0.1625 0.1965 -0.0154 0.0359  0.0325  42  TYR   A CD1 
1122 C CD1 B TYR   A 42  ? 0.1688 0.1431 0.1517 0.0033  0.0069  0.0444  42  TYR   A CD1 
1123 C CD2 A TYR   A 42  ? 0.1862 0.1719 0.2027 -0.0071 0.0262  0.0260  42  TYR   A CD2 
1124 C CD2 B TYR   A 42  ? 0.1764 0.1534 0.1706 0.0119  -0.0030 0.0354  42  TYR   A CD2 
1125 C CE1 A TYR   A 42  ? 0.1808 0.1730 0.1934 -0.0097 0.0312  0.0254  42  TYR   A CE1 
1126 C CE1 B TYR   A 42  ? 0.1708 0.1481 0.1528 0.0024  0.0104  0.0441  42  TYR   A CE1 
1127 C CE2 A TYR   A 42  ? 0.1880 0.1827 0.2081 -0.0157 0.0192  0.0298  42  TYR   A CE2 
1128 C CE2 B TYR   A 42  ? 0.1807 0.1602 0.1722 0.0096  0.0006  0.0339  42  TYR   A CE2 
1129 C CZ  A TYR   A 42  ? 0.1877 0.1825 0.1874 -0.0173 0.0352  0.0252  42  TYR   A CZ  
1130 C CZ  B TYR   A 42  ? 0.1759 0.1567 0.1595 0.0006  0.0089  0.0330  42  TYR   A CZ  
1131 O OH  A TYR   A 42  ? 0.2003 0.2033 0.2192 -0.0172 0.0246  0.0099  42  TYR   A OH  
1132 O OH  B TYR   A 42  ? 0.1727 0.1670 0.1706 -0.0087 0.0066  0.0243  42  TYR   A OH  
1151 N N   . LEU   A 43  ? 0.1420 0.1324 0.1594 -0.0060 0.0135  0.0131  43  LEU   A N   
1152 C CA  . LEU   A 43  ? 0.1350 0.1324 0.1583 -0.0114 0.0127  0.0144  43  LEU   A CA  
1153 C C   . LEU   A 43  ? 0.1349 0.1383 0.1693 -0.0052 0.0077  0.0114  43  LEU   A C   
1154 O O   . LEU   A 43  ? 0.1499 0.1414 0.1886 0.0013  -0.0034 0.0110  43  LEU   A O   
1155 C CB  . LEU   A 43  ? 0.1395 0.1274 0.1809 -0.0091 0.0102  0.0129  43  LEU   A CB  
1156 C CG  . LEU   A 43  ? 0.1500 0.1369 0.1793 -0.0048 0.0020  0.0120  43  LEU   A CG  
1157 C CD1 . LEU   A 43  ? 0.1556 0.1390 0.1986 -0.0012 -0.0042 0.0153  43  LEU   A CD1 
1158 C CD2 . LEU   A 43  ? 0.1606 0.1397 0.1812 -0.0045 0.0077  0.0167  43  LEU   A CD2 
1171 N N   A LYS   A 44  ? 0.1387 0.1287 0.1507 -0.0007 0.0121  0.0135  44  LYS   A N   
1172 N N   B LYS   A 44  ? 0.1522 0.1564 0.1672 -0.0069 0.0049  0.0066  44  LYS   A N   
1173 C CA  A LYS   A 44  ? 0.1506 0.1295 0.1597 -0.0003 0.0275  0.0220  44  LYS   A CA  
1174 C CA  B LYS   A 44  ? 0.1748 0.1783 0.1821 -0.0093 0.0045  0.0057  44  LYS   A CA  
1175 C C   A LYS   A 44  ? 0.1365 0.1230 0.1513 0.0040  0.0091  0.0111  44  LYS   A C   
1176 C C   B LYS   A 44  ? 0.1712 0.1756 0.1620 -0.0069 -0.0008 0.0050  44  LYS   A C   
1177 O O   A LYS   A 44  ? 0.1406 0.1453 0.1780 0.0028  0.0072  -0.0020 44  LYS   A O   
1178 O O   B LYS   A 44  ? 0.1744 0.1807 0.1609 -0.0091 -0.0015 0.0035  44  LYS   A O   
1179 C CB  A LYS   A 44  ? 0.1833 0.1377 0.2025 0.0068  0.0412  0.0411  44  LYS   A CB  
1180 C CB  B LYS   A 44  ? 0.2011 0.2026 0.2255 -0.0110 0.0080  0.0053  44  LYS   A CB  
1181 C CG  A LYS   A 44  ? 0.2189 0.1707 0.2702 -0.0006 0.0656  0.0510  44  LYS   A CG  
1182 C CG  B LYS   A 44  ? 0.2254 0.2257 0.2761 -0.0125 0.0153  0.0055  44  LYS   A CG  
1183 C CD  A LYS   A 44  ? 0.2556 0.2335 0.3774 -0.0088 0.0465  0.0397  44  LYS   A CD  
1184 C CD  B LYS   A 44  ? 0.2459 0.2509 0.3288 -0.0157 0.0108  0.0033  44  LYS   A CD  
1185 C CE  A LYS   A 44  ? 0.2748 0.2744 0.4472 -0.0154 0.0353  0.0339  44  LYS   A CE  
1186 C CE  B LYS   A 44  ? 0.2560 0.2654 0.3630 -0.0186 0.0066  0.0022  44  LYS   A CE  
1187 N NZ  A LYS   A 44  ? 0.2844 0.2969 0.4804 -0.0235 0.0355  0.0364  44  LYS   A NZ  
1188 N NZ  B LYS   A 44  ? 0.2593 0.2688 0.3771 -0.0211 0.0044  0.0045  44  LYS   A NZ  
1215 N N   A HIS   A 45  ? 0.1214 0.1223 0.1562 0.0023  0.0081  0.0214  45  HIS   A N   
1216 N N   B HIS   A 45  ? 0.1652 0.1725 0.1626 -0.0042 -0.0025 0.0067  45  HIS   A N   
1217 C CA  A HIS   A 45  ? 0.1261 0.1254 0.1613 0.0034  0.0023  0.0199  45  HIS   A CA  
1218 C CA  B HIS   A 45  ? 0.1620 0.1680 0.1644 -0.0002 -0.0041 0.0045  45  HIS   A CA  
1219 C C   A HIS   A 45  ? 0.1320 0.1435 0.1748 0.0095  0.0070  0.0308  45  HIS   A C   
1220 C C   B HIS   A 45  ? 0.1644 0.1700 0.1738 0.0006  -0.0030 0.0050  45  HIS   A C   
1221 O O   A HIS   A 45  ? 0.1367 0.1418 0.2022 0.0085  0.0110  0.0141  45  HIS   A O   
1222 O O   B HIS   A 45  ? 0.1718 0.1684 0.1864 0.0055  0.0008  -0.0001 45  HIS   A O   
1223 C CB  A HIS   A 45  ? 0.1340 0.1215 0.1509 -0.0000 0.0071  0.0077  45  HIS   A CB  
1224 C CB  B HIS   A 45  ? 0.1545 0.1632 0.1524 0.0070  -0.0061 0.0020  45  HIS   A CB  
1225 C CG  A HIS   A 45  ? 0.1301 0.1226 0.1582 -0.0090 0.0070  0.0164  45  HIS   A CG  
1226 C CG  B HIS   A 45  ? 0.1428 0.1567 0.1432 0.0115  0.0005  0.0060  45  HIS   A CG  
1227 N ND1 A HIS   A 45  ? 0.1282 0.1297 0.1840 -0.0045 0.0103  0.0171  45  HIS   A ND1 
1228 N ND1 B HIS   A 45  ? 0.1365 0.1556 0.1478 0.0176  -0.0063 0.0172  45  HIS   A ND1 
1229 C CD2 A HIS   A 45  ? 0.1281 0.1298 0.1643 -0.0082 -0.0059 0.0211  45  HIS   A CD2 
1230 C CD2 B HIS   A 45  ? 0.1367 0.1498 0.1373 0.0114  0.0010  0.0013  45  HIS   A CD2 
1231 C CE1 A HIS   A 45  ? 0.1310 0.1345 0.1700 -0.0115 0.0084  0.0297  45  HIS   A CE1 
1232 C CE1 B HIS   A 45  ? 0.1329 0.1485 0.1311 0.0133  -0.0062 0.0078  45  HIS   A CE1 
1233 N NE2 A HIS   A 45  ? 0.1344 0.1378 0.1629 -0.0070 0.0032  0.0284  45  HIS   A NE2 
1234 N NE2 B HIS   A 45  ? 0.1325 0.1474 0.1281 0.0122  -0.0048 -0.0014 45  HIS   A NE2 
1249 N N   A GLY   A 46  ? 0.1480 0.1636 0.1945 0.0218  -0.0049 0.0395  46  GLY   A N   
1250 N N   B GLY   A 46  ? 0.1611 0.1711 0.1702 -0.0029 -0.0055 0.0080  46  GLY   A N   
1251 C CA  A GLY   A 46  ? 0.1558 0.1767 0.2135 0.0240  -0.0050 0.0451  46  GLY   A CA  
1252 C CA  B GLY   A 46  ? 0.1533 0.1736 0.1600 -0.0040 0.0044  0.0116  46  GLY   A CA  
1253 C C   A GLY   A 46  ? 0.1553 0.1656 0.2200 0.0326  -0.0095 0.0446  46  GLY   A C   
1254 C C   B GLY   A 46  ? 0.1523 0.1672 0.1430 -0.0012 0.0159  0.0229  46  GLY   A C   
1255 O O   A GLY   A 46  ? 0.1660 0.1625 0.2303 0.0289  -0.0215 0.0440  46  GLY   A O   
1256 O O   B GLY   A 46  ? 0.1569 0.1722 0.1388 -0.0026 0.0127  0.0188  46  GLY   A O   
1263 N N   A GLY   A 47  ? 0.1489 0.1653 0.2109 0.0302  -0.0105 0.0378  47  GLY   A N   
1264 N N   B GLY   A 47  ? 0.1552 0.1639 0.1438 0.0009  0.0178  0.0140  47  GLY   A N   
1265 C CA  A GLY   A 47  ? 0.1608 0.1676 0.1988 0.0257  -0.0123 0.0250  47  GLY   A CA  
1266 C CA  B GLY   A 47  ? 0.1525 0.1652 0.1467 0.0031  0.0104  0.0173  47  GLY   A CA  
1267 C C   A GLY   A 47  ? 0.1603 0.1608 0.1801 0.0227  -0.0161 0.0211  47  GLY   A C   
1268 C C   B GLY   A 47  ? 0.1412 0.1595 0.1309 0.0098  0.0076  0.0158  47  GLY   A C   
1269 O O   A GLY   A 47  ? 0.1610 0.1530 0.2013 0.0310  -0.0162 0.0215  47  GLY   A O   
1270 O O   B GLY   A 47  ? 0.1348 0.1567 0.1372 0.0096  -0.0026 0.0204  47  GLY   A O   
1277 N N   A GLY   A 48  ? 0.1577 0.1639 0.1615 0.0218  -0.0122 0.0140  48  GLY   A N   
1278 N N   B GLY   A 48  ? 0.1362 0.1599 0.1234 0.0167  0.0132  0.0105  48  GLY   A N   
1279 C CA  A GLY   A 48  ? 0.1596 0.1626 0.1610 0.0080  -0.0065 0.0030  48  GLY   A CA  
1280 C CA  B GLY   A 48  ? 0.1361 0.1536 0.1141 0.0136  0.0096  0.0054  48  GLY   A CA  
1281 C C   A GLY   A 48  ? 0.1480 0.1519 0.1516 -0.0008 -0.0043 0.0058  48  GLY   A C   
1282 C C   B GLY   A 48  ? 0.1430 0.1508 0.1155 0.0082  0.0077  0.0100  48  GLY   A C   
1283 O O   A GLY   A 48  ? 0.1612 0.1422 0.1585 0.0048  -0.0002 0.0092  48  GLY   A O   
1284 O O   B GLY   A 48  ? 0.1525 0.1528 0.1020 0.0098  0.0169  0.0072  48  GLY   A O   
1291 N N   A VAL   A 49  ? 0.1408 0.1477 0.1858 -0.0061 -0.0168 0.0047  49  VAL   A N   
1292 N N   B VAL   A 49  ? 0.1368 0.1453 0.1271 0.0062  -0.0015 0.0044  49  VAL   A N   
1293 C CA  A VAL   A 49  ? 0.1521 0.1442 0.1832 -0.0118 -0.0037 0.0138  49  VAL   A CA  
1294 C CA  B VAL   A 49  ? 0.1312 0.1506 0.1342 0.0075  -0.0025 0.0047  49  VAL   A CA  
1295 C C   A VAL   A 49  ? 0.1494 0.1342 0.1627 -0.0103 -0.0031 0.0247  49  VAL   A C   
1296 C C   B VAL   A 49  ? 0.1353 0.1427 0.1209 0.0126  0.0088  -0.0161 49  VAL   A C   
1297 O O   A VAL   A 49  ? 0.1531 0.1419 0.1683 -0.0149 -0.0008 0.0104  49  VAL   A O   
1298 O O   B VAL   A 49  ? 0.1395 0.1469 0.1123 0.0119  0.0287  -0.0141 49  VAL   A O   
1299 C CB  A VAL   A 49  ? 0.1623 0.1417 0.2129 -0.0133 -0.0109 0.0093  49  VAL   A CB  
1300 C CB  B VAL   A 49  ? 0.1258 0.1531 0.1630 0.0096  -0.0176 0.0176  49  VAL   A CB  
1301 C CG1 A VAL   A 49  ? 0.1719 0.1530 0.2231 -0.0002 -0.0009 0.0112  49  VAL   A CG1 
1302 C CG1 B VAL   A 49  ? 0.1140 0.1504 0.1672 0.0230  -0.0165 0.0247  49  VAL   A CG1 
1303 C CG2 A VAL   A 49  ? 0.1714 0.1461 0.2542 -0.0302 -0.0059 0.0043  49  VAL   A CG2 
1304 C CG2 B VAL   A 49  ? 0.1326 0.1610 0.1815 0.0020  -0.0192 0.0169  49  VAL   A CG2 
1323 N N   A ALA   A 50  ? 0.1374 0.1366 0.1472 -0.0096 -0.0152 0.0239  50  ALA   A N   
1324 N N   B ALA   A 50  ? 0.1364 0.1342 0.1128 0.0183  0.0065  -0.0199 50  ALA   A N   
1325 C CA  A ALA   A 50  ? 0.1339 0.1361 0.1499 -0.0186 -0.0066 0.0248  50  ALA   A CA  
1326 C CA  B ALA   A 50  ? 0.1395 0.1260 0.1196 0.0162  0.0064  -0.0144 50  ALA   A CA  
1327 C C   A ALA   A 50  ? 0.1286 0.1373 0.1615 -0.0152 -0.0043 0.0121  50  ALA   A C   
1328 C C   B ALA   A 50  ? 0.1429 0.1232 0.1131 0.0161  0.0033  -0.0117 50  ALA   A C   
1329 O O   A ALA   A 50  ? 0.1327 0.1388 0.1703 -0.0079 -0.0098 0.0070  50  ALA   A O   
1330 O O   B ALA   A 50  ? 0.1444 0.1219 0.1007 0.0166  0.0063  -0.0070 50  ALA   A O   
1331 C CB  A ALA   A 50  ? 0.1332 0.1418 0.1619 -0.0142 -0.0099 0.0137  50  ALA   A CB  
1332 C CB  B ALA   A 50  ? 0.1415 0.1172 0.1227 0.0200  0.0090  -0.0267 50  ALA   A CB  
1343 N N   A GLY   A 51  ? 0.1310 0.1261 0.1573 -0.0014 -0.0101 0.0080  51  GLY   A N   
1344 N N   B GLY   A 51  ? 0.1486 0.1231 0.1364 0.0211  -0.0042 -0.0178 51  GLY   A N   
1345 C CA  A GLY   A 51  ? 0.1429 0.1248 0.1779 0.0000  -0.0146 0.0077  51  GLY   A CA  
1346 C CA  B GLY   A 51  ? 0.1565 0.1267 0.1236 0.0185  -0.0092 -0.0215 51  GLY   A CA  
1347 C C   A GLY   A 51  ? 0.1248 0.1373 0.1609 -0.0007 -0.0022 -0.0033 51  GLY   A C   
1348 C C   B GLY   A 51  ? 0.1544 0.1363 0.1262 0.0148  -0.0013 -0.0270 51  GLY   A C   
1349 O O   A GLY   A 51  ? 0.1336 0.1522 0.1681 -0.0043 -0.0050 -0.0011 51  GLY   A O   
1350 O O   B GLY   A 51  ? 0.1571 0.1413 0.1241 0.0131  0.0016  -0.0296 51  GLY   A O   
1357 N N   A ALA   A 52  ? 0.1257 0.1479 0.1552 0.0008  -0.0033 0.0060  52  ALA   A N   
1358 N N   B ALA   A 52  ? 0.1573 0.1422 0.1289 0.0085  0.0043  -0.0312 52  ALA   A N   
1359 C CA  A ALA   A 52  ? 0.1341 0.1606 0.1690 -0.0031 -0.0000 0.0078  52  ALA   A CA  
1360 C CA  B ALA   A 52  ? 0.1557 0.1510 0.1419 0.0048  0.0083  -0.0230 52  ALA   A CA  
1361 C C   A ALA   A 52  ? 0.1321 0.1581 0.1554 -0.0093 0.0021  0.0067  52  ALA   A C   
1362 C C   B ALA   A 52  ? 0.1507 0.1509 0.1238 -0.0021 0.0115  -0.0230 52  ALA   A C   
1363 O O   A ALA   A 52  ? 0.1464 0.1630 0.1620 -0.0062 0.0009  0.0051  52  ALA   A O   
1364 O O   B ALA   A 52  ? 0.1557 0.1512 0.1395 -0.0024 0.0186  -0.0216 52  ALA   A O   
1365 C CB  A ALA   A 52  ? 0.1438 0.1839 0.1854 -0.0146 -0.0003 0.0112  52  ALA   A CB  
1366 C CB  B ALA   A 52  ? 0.1601 0.1628 0.1549 0.0027  0.0095  -0.0168 52  ALA   A CB  
1377 N N   A LEU   A 53  ? 0.1255 0.1512 0.1651 -0.0082 0.0013  0.0092  53  LEU   A N   
1378 N N   B LEU   A 53  ? 0.1442 0.1518 0.1147 -0.0048 0.0039  -0.0257 53  LEU   A N   
1379 C CA  A LEU   A 53  ? 0.1392 0.1562 0.1613 -0.0092 0.0030  0.0209  53  LEU   A CA  
1380 C CA  B LEU   A 53  ? 0.1474 0.1582 0.1119 -0.0062 -0.0073 -0.0222 53  LEU   A CA  
1381 C C   A LEU   A 53  ? 0.1353 0.1549 0.1299 0.0022  0.0038  0.0109  53  LEU   A C   
1382 C C   B LEU   A 53  ? 0.1519 0.1624 0.1178 0.0008  -0.0115 -0.0241 53  LEU   A C   
1383 O O   A LEU   A 53  ? 0.1582 0.1628 0.1384 -0.0131 0.0001  0.0008  53  LEU   A O   
1384 O O   B LEU   A 53  ? 0.1627 0.1686 0.1379 -0.0029 -0.0086 -0.0237 53  LEU   A O   
1385 C CB  A LEU   A 53  ? 0.1518 0.1558 0.1817 -0.0107 0.0049  0.0220  53  LEU   A CB  
1386 C CB  B LEU   A 53  ? 0.1490 0.1610 0.1084 -0.0118 -0.0154 -0.0143 53  LEU   A CB  
1387 C CG  A LEU   A 53  ? 0.1698 0.1535 0.1784 -0.0146 -0.0055 0.0225  53  LEU   A CG  
1388 C CG  B LEU   A 53  ? 0.1543 0.1638 0.1100 -0.0152 -0.0122 -0.0099 53  LEU   A CG  
1389 C CD1 A LEU   A 53  ? 0.1669 0.1602 0.1657 -0.0028 -0.0107 0.0173  53  LEU   A CD1 
1390 C CD1 B LEU   A 53  ? 0.1568 0.1685 0.1198 -0.0130 -0.0137 -0.0221 53  LEU   A CD1 
1391 C CD2 A LEU   A 53  ? 0.1973 0.1723 0.1998 -0.0228 0.0037  0.0231  53  LEU   A CD2 
1392 C CD2 B LEU   A 53  ? 0.1655 0.1701 0.1119 -0.0227 -0.0094 -0.0026 53  LEU   A CD2 
1415 N N   A ASN   A 54  ? 0.1309 0.1426 0.1376 -0.0055 -0.0038 0.0074  54  ASN   A N   
1416 N N   B ASN   A 54  ? 0.1525 0.1641 0.1336 0.0027  -0.0115 -0.0217 54  ASN   A N   
1417 C CA  A ASN   A 54  ? 0.1199 0.1347 0.1618 -0.0033 0.0051  -0.0000 54  ASN   A CA  
1418 C CA  B ASN   A 54  ? 0.1497 0.1648 0.1395 0.0038  -0.0124 -0.0188 54  ASN   A CA  
1419 C C   A ASN   A 54  ? 0.1304 0.1397 0.1673 -0.0077 0.0092  0.0036  54  ASN   A C   
1420 C C   B ASN   A 54  ? 0.1559 0.1612 0.1291 -0.0004 -0.0065 -0.0213 54  ASN   A C   
1421 O O   A ASN   A 54  ? 0.1354 0.1509 0.1740 -0.0025 -0.0025 -0.0047 54  ASN   A O   
1422 O O   B ASN   A 54  ? 0.1551 0.1591 0.1232 -0.0003 -0.0018 -0.0245 54  ASN   A O   
1423 C CB  A ASN   A 54  ? 0.1233 0.1306 0.1733 -0.0110 -0.0048 0.0002  54  ASN   A CB  
1424 C CB  B ASN   A 54  ? 0.1451 0.1647 0.1405 0.0153  -0.0057 -0.0131 54  ASN   A CB  
1425 C CG  A ASN   A 54  ? 0.1290 0.1360 0.1760 -0.0068 -0.0063 0.0034  54  ASN   A CG  
1426 C CG  B ASN   A 54  ? 0.1399 0.1581 0.1250 0.0204  0.0019  -0.0155 54  ASN   A CG  
1427 O OD1 A ASN   A 54  ? 0.1294 0.1317 0.1903 -0.0131 -0.0114 0.0173  54  ASN   A OD1 
1428 O OD1 B ASN   A 54  ? 0.1349 0.1576 0.1099 0.0139  0.0044  -0.0357 54  ASN   A OD1 
1429 N ND2 A ASN   A 54  ? 0.1327 0.1442 0.1802 -0.0086 -0.0131 0.0091  54  ASN   A ND2 
1430 N ND2 B ASN   A 54  ? 0.1419 0.1529 0.1271 0.0209  -0.0008 0.0000  54  ASN   A ND2 
1443 N N   A LYS   A 55  ? 0.1300 0.1439 0.1657 0.0008  0.0049  0.0032  55  LYS   A N   
1444 N N   B LYS   A 55  ? 0.1597 0.1595 0.1316 0.0013  -0.0078 -0.0242 55  LYS   A N   
1445 C CA  A LYS   A 55  ? 0.1368 0.1550 0.1732 0.0084  0.0005  -0.0146 55  LYS   A CA  
1446 C CA  B LYS   A 55  ? 0.1671 0.1675 0.1477 0.0091  -0.0081 -0.0242 55  LYS   A CA  
1447 C C   A LYS   A 55  ? 0.1356 0.1622 0.1701 0.0003  0.0042  -0.0198 55  LYS   A C   
1448 C C   B LYS   A 55  ? 0.1654 0.1735 0.1541 0.0052  -0.0087 -0.0187 55  LYS   A C   
1449 O O   A LYS   A 55  ? 0.1462 0.1757 0.1823 0.0032  -0.0008 -0.0272 55  LYS   A O   
1450 O O   B LYS   A 55  ? 0.1694 0.1772 0.1492 0.0058  -0.0054 -0.0172 55  LYS   A O   
1451 C CB  A LYS   A 55  ? 0.1444 0.1632 0.1771 0.0115  0.0051  -0.0238 55  LYS   A CB  
1452 C CB  B LYS   A 55  ? 0.1754 0.1762 0.1710 0.0111  -0.0087 -0.0142 55  LYS   A CB  
1453 C CG  A LYS   A 55  ? 0.1591 0.1895 0.1875 0.0250  -0.0048 -0.0187 55  LYS   A CG  
1454 C CG  B LYS   A 55  ? 0.1827 0.1864 0.1844 0.0156  -0.0084 -0.0003 55  LYS   A CG  
1455 C CD  A LYS   A 55  ? 0.1762 0.2138 0.1927 0.0378  0.0026  -0.0035 55  LYS   A CD  
1456 C CD  B LYS   A 55  ? 0.1964 0.2015 0.2169 0.0203  -0.0111 0.0098  55  LYS   A CD  
1457 C CE  A LYS   A 55  ? 0.1974 0.2396 0.2032 0.0505  -0.0044 0.0002  55  LYS   A CE  
1458 C CE  B LYS   A 55  ? 0.2062 0.2144 0.2457 0.0243  -0.0155 0.0189  55  LYS   A CE  
1459 N NZ  A LYS   A 55  ? 0.2052 0.2486 0.2110 0.0563  0.0000  0.0071  55  LYS   A NZ  
1460 N NZ  B LYS   A 55  ? 0.2130 0.2218 0.2638 0.0279  -0.0151 0.0234  55  LYS   A NZ  
1487 N N   A ALA   A 56  ? 0.1419 0.1715 0.1772 -0.0116 0.0087  -0.0174 56  ALA   A N   
1488 N N   B ALA   A 56  ? 0.1632 0.1791 0.1526 -0.0028 -0.0053 -0.0157 56  ALA   A N   
1489 C CA  A ALA   A 56  ? 0.1542 0.1907 0.1811 -0.0118 0.0179  -0.0185 56  ALA   A CA  
1490 C CA  B ALA   A 56  ? 0.1648 0.1885 0.1560 -0.0079 0.0031  -0.0089 56  ALA   A CA  
1491 C C   A ALA   A 56  ? 0.1650 0.1921 0.1564 -0.0091 0.0185  -0.0216 56  ALA   A C   
1492 C C   B ALA   A 56  ? 0.1641 0.1868 0.1360 -0.0105 0.0081  -0.0035 56  ALA   A C   
1493 O O   A ALA   A 56  ? 0.1730 0.1977 0.1667 0.0029  0.0171  -0.0137 56  ALA   A O   
1494 O O   B ALA   A 56  ? 0.1686 0.1896 0.1231 -0.0079 0.0159  0.0204  56  ALA   A O   
1495 C CB  A ALA   A 56  ? 0.1580 0.2113 0.1957 -0.0209 0.0157  -0.0107 56  ALA   A CB  
1496 C CB  B ALA   A 56  ? 0.1662 0.1975 0.1667 -0.0133 0.0030  -0.0064 56  ALA   A CB  
1507 N N   . THR   A 57  ? 0.1516 0.1823 0.1454 -0.0114 0.0076  -0.0189 57  THR   A N   
1508 C CA  . THR   A 57  ? 0.1561 0.1767 0.1607 -0.0117 0.0059  -0.0117 57  THR   A CA  
1509 C C   . THR   A 57  ? 0.1566 0.1802 0.1645 -0.0079 0.0025  -0.0184 57  THR   A C   
1510 O O   . THR   A 57  ? 0.1532 0.1830 0.1858 -0.0167 -0.0031 -0.0300 57  THR   A O   
1511 C CB  . THR   A 57  ? 0.1545 0.1727 0.1627 -0.0109 0.0059  -0.0027 57  THR   A CB  
1512 O OG1 . THR   A 57  ? 0.1423 0.1698 0.1571 -0.0064 -0.0002 -0.0063 57  THR   A OG1 
1513 C CG2 . THR   A 57  ? 0.1576 0.1800 0.1594 -0.0039 -0.0039 -0.0028 57  THR   A CG2 
1522 N N   . ASN   A 58  ? 0.1604 0.1772 0.1871 -0.0068 0.0104  -0.0271 58  ASN   A N   
1523 C CA  . ASN   A 58  ? 0.1762 0.1715 0.2119 -0.0132 0.0130  -0.0381 58  ASN   A CA  
1524 C C   . ASN   A 58  ? 0.1593 0.1595 0.1928 0.0001  0.0032  -0.0244 58  ASN   A C   
1525 O O   . ASN   A 58  ? 0.1605 0.1693 0.2104 -0.0102 -0.0014 -0.0269 58  ASN   A O   
1526 C CB  . ASN   A 58  ? 0.2171 0.1837 0.2298 -0.0174 0.0338  -0.0505 58  ASN   A CB  
1527 C CG  . ASN   A 58  ? 0.2528 0.2054 0.2882 -0.0148 0.0272  -0.0290 58  ASN   A CG  
1528 O OD1 . ASN   A 58  ? 0.2807 0.2051 0.3259 0.0241  0.0541  -0.0159 58  ASN   A OD1 
1529 N ND2 . ASN   A 58  ? 0.2591 0.2125 0.2998 -0.0172 0.0195  -0.0271 58  ASN   A ND2 
1536 N N   . ASN   A 59  ? 0.1447 0.1510 0.1743 -0.0029 -0.0033 -0.0114 59  ASN   A N   
1537 C CA  . ASN   A 59  ? 0.1462 0.1411 0.1697 -0.0018 -0.0067 -0.0065 59  ASN   A CA  
1538 C C   . ASN   A 59  ? 0.1417 0.1438 0.1655 -0.0058 -0.0095 -0.0005 59  ASN   A C   
1539 O O   . ASN   A 59  ? 0.1412 0.1473 0.1659 -0.0067 0.0020  0.0043  59  ASN   A O   
1540 C CB  . ASN   A 59  ? 0.1513 0.1379 0.1847 0.0077  -0.0142 -0.0133 59  ASN   A CB  
1541 C CG  . ASN   A 59  ? 0.1544 0.1403 0.1814 0.0003  -0.0275 0.0051  59  ASN   A CG  
1542 O OD1 . ASN   A 59  ? 0.1647 0.1498 0.1756 -0.0113 -0.0219 0.0015  59  ASN   A OD1 
1543 N ND2 . ASN   A 59  ? 0.1631 0.1478 0.1905 -0.0144 -0.0162 0.0044  59  ASN   A ND2 
1550 N N   . ALA   A 60  ? 0.1372 0.1473 0.1654 -0.0021 -0.0058 -0.0004 60  ALA   A N   
1551 C CA  . ALA   A 60  ? 0.1406 0.1504 0.1735 0.0003  -0.0073 0.0008  60  ALA   A CA  
1552 C C   . ALA   A 60  ? 0.1380 0.1467 0.1812 -0.0046 -0.0044 0.0024  60  ALA   A C   
1553 O O   . ALA   A 60  ? 0.1318 0.1483 0.1951 -0.0046 -0.0083 -0.0015 60  ALA   A O   
1554 C CB  . ALA   A 60  ? 0.1501 0.1626 0.1759 0.0010  -0.0171 -0.0137 60  ALA   A CB  
1560 N N   . MET   A 61  ? 0.1397 0.1394 0.1698 -0.0034 0.0019  -0.0017 61  MET   A N   
1561 C CA  . MET   A 61  ? 0.1404 0.1388 0.1703 -0.0081 0.0030  0.0069  61  MET   A CA  
1562 C C   . MET   A 61  ? 0.1307 0.1333 0.1743 -0.0079 -0.0041 0.0000  61  MET   A C   
1563 O O   . MET   A 61  ? 0.1335 0.1325 0.1774 -0.0006 0.0047  0.0054  61  MET   A O   
1564 C CB  . MET   A 61  ? 0.1446 0.1393 0.1567 -0.0077 0.0052  -0.0000 61  MET   A CB  
1565 C CG  . MET   A 61  ? 0.1477 0.1442 0.1731 -0.0025 0.0007  0.0019  61  MET   A CG  
1566 S SD  . MET   A 61  ? 0.1470 0.1505 0.2122 -0.0121 0.0020  -0.0133 61  MET   A SD  
1567 C CE  . MET   A 61  ? 0.1696 0.1605 0.2342 -0.0098 0.0247  -0.0074 61  MET   A CE  
1577 N N   . GLN   A 62  ? 0.1363 0.1288 0.1748 -0.0114 -0.0031 -0.0046 62  GLN   A N   
1578 C CA  . GLN   A 62  ? 0.1357 0.1298 0.1840 -0.0044 0.0027  0.0048  62  GLN   A CA  
1579 C C   . GLN   A 62  ? 0.1379 0.1206 0.1805 -0.0015 0.0023  0.0049  62  GLN   A C   
1580 O O   . GLN   A 62  ? 0.1381 0.1384 0.1733 0.0005  0.0032  0.0028  62  GLN   A O   
1581 C CB  . GLN   A 62  ? 0.1385 0.1282 0.1832 -0.0016 0.0072  0.0084  62  GLN   A CB  
1582 C CG  . GLN   A 62  ? 0.1421 0.1265 0.1822 -0.0047 -0.0056 0.0151  62  GLN   A CG  
1583 C CD  . GLN   A 62  ? 0.1499 0.1263 0.1757 -0.0055 0.0041  0.0122  62  GLN   A CD  
1584 O OE1 . GLN   A 62  ? 0.1533 0.1452 0.1917 -0.0054 -0.0054 0.0036  62  GLN   A OE1 
1585 N NE2 . GLN   A 62  ? 0.1546 0.1344 0.1893 0.0044  0.0063  -0.0074 62  GLN   A NE2 
1594 N N   . VAL   A 63  ? 0.1362 0.1336 0.1887 -0.0071 0.0019  -0.0135 63  VAL   A N   
1595 C CA  . VAL   A 63  ? 0.1393 0.1389 0.2072 -0.0140 0.0003  -0.0088 63  VAL   A CA  
1596 C C   . VAL   A 63  ? 0.1291 0.1424 0.2011 -0.0155 -0.0078 -0.0099 63  VAL   A C   
1597 O O   . VAL   A 63  ? 0.1284 0.1434 0.2240 -0.0128 -0.0013 -0.0028 63  VAL   A O   
1598 C CB  . VAL   A 63  ? 0.1507 0.1575 0.2381 -0.0126 -0.0092 -0.0345 63  VAL   A CB  
1599 C CG1 . VAL   A 63  ? 0.1623 0.1766 0.2741 -0.0097 -0.0193 -0.0526 63  VAL   A CG1 
1600 C CG2 . VAL   A 63  ? 0.1531 0.1559 0.2441 -0.0061 0.0122  -0.0224 63  VAL   A CG2 
1610 N N   . GLU   A 64  ? 0.1311 0.1479 0.1885 -0.0053 -0.0033 -0.0066 64  GLU   A N   
1611 C CA  . GLU   A 64  ? 0.1329 0.1436 0.1906 -0.0100 -0.0077 0.0027  64  GLU   A CA  
1612 C C   . GLU   A 64  ? 0.1300 0.1399 0.1861 -0.0069 0.0010  0.0057  64  GLU   A C   
1613 O O   . GLU   A 64  ? 0.1400 0.1489 0.1886 0.0009  -0.0009 0.0021  64  GLU   A O   
1614 C CB  . GLU   A 64  ? 0.1374 0.1604 0.2021 -0.0059 0.0002  -0.0016 64  GLU   A CB  
1615 C CG  . GLU   A 64  ? 0.1475 0.1606 0.2083 -0.0052 -0.0008 0.0016  64  GLU   A CG  
1616 C CD  . GLU   A 64  ? 0.1625 0.1688 0.2191 -0.0140 -0.0000 0.0001  64  GLU   A CD  
1617 O OE1 . GLU   A 64  ? 0.1610 0.1799 0.2372 -0.0217 0.0105  0.0070  64  GLU   A OE1 
1618 O OE2 . GLU   A 64  ? 0.1770 0.1711 0.2125 -0.0184 -0.0055 0.0080  64  GLU   A OE2 
1625 N N   . SER   A 65  ? 0.1255 0.1396 0.1801 0.0019  -0.0043 0.0060  65  SER   A N   
1626 C CA  . SER   A 65  ? 0.1307 0.1362 0.1833 -0.0018 -0.0071 -0.0017 65  SER   A CA  
1627 C C   . SER   A 65  ? 0.1316 0.1384 0.1892 -0.0076 -0.0031 0.0073  65  SER   A C   
1628 O O   . SER   A 65  ? 0.1379 0.1453 0.2008 0.0009  0.0151  -0.0005 65  SER   A O   
1629 C CB  . SER   A 65  ? 0.1324 0.1363 0.1822 -0.0098 0.0015  0.0109  65  SER   A CB  
1630 O OG  . SER   A 65  ? 0.1332 0.1464 0.1790 -0.0088 -0.0002 0.0149  65  SER   A OG  
1636 N N   . ASP   A 66  ? 0.1359 0.1381 0.1924 -0.0050 0.0125  0.0145  66  ASP   A N   
1637 C CA  . ASP   A 66  ? 0.1464 0.1475 0.2041 -0.0012 0.0116  0.0188  66  ASP   A CA  
1638 C C   . ASP   A 66  ? 0.1469 0.1469 0.1950 -0.0062 0.0079  0.0167  66  ASP   A C   
1639 O O   . ASP   A 66  ? 0.1523 0.1592 0.2097 -0.0050 0.0247  0.0224  66  ASP   A O   
1640 C CB  . ASP   A 66  ? 0.1579 0.1513 0.2351 0.0101  0.0173  0.0372  66  ASP   A CB  
1641 C CG  . ASP   A 66  ? 0.1849 0.1690 0.2619 0.0038  0.0106  0.0535  66  ASP   A CG  
1642 O OD1 . ASP   A 66  ? 0.1832 0.1975 0.2488 -0.0076 0.0025  0.0540  66  ASP   A OD1 
1643 O OD2 . ASP   A 66  ? 0.2030 0.1938 0.3429 0.0220  -0.0130 0.0278  66  ASP   A OD2 
1648 N N   . ASP   A 67  ? 0.1328 0.1497 0.2012 -0.0060 0.0093  0.0185  67  ASP   A N   
1649 C CA  . ASP   A 67  ? 0.1365 0.1639 0.2198 -0.0041 0.0087  0.0267  67  ASP   A CA  
1650 C C   . ASP   A 67  ? 0.1394 0.1654 0.2164 0.0009  0.0143  0.0246  67  ASP   A C   
1651 O O   . ASP   A 67  ? 0.1358 0.1739 0.2377 0.0015  0.0213  0.0299  67  ASP   A O   
1652 C CB  . ASP   A 67  ? 0.1446 0.1753 0.2475 -0.0073 -0.0129 0.0388  67  ASP   A CB  
1653 C CG  . ASP   A 67  ? 0.1467 0.1934 0.2785 -0.0077 -0.0225 0.0532  67  ASP   A CG  
1654 O OD1 . ASP   A 67  ? 0.1468 0.2126 0.3509 -0.0196 -0.0292 0.0636  67  ASP   A OD1 
1655 O OD2 . ASP   A 67  ? 0.1453 0.1952 0.2805 0.0017  -0.0124 0.0437  67  ASP   A OD2 
1660 N N   . TYR   A 68  ? 0.1454 0.1481 0.2123 0.0075  0.0196  0.0347  68  TYR   A N   
1661 C CA  . TYR   A 68  ? 0.1513 0.1504 0.2113 0.0071  0.0267  0.0316  68  TYR   A CA  
1662 C C   . TYR   A 68  ? 0.1422 0.1482 0.2156 0.0023  0.0248  0.0202  68  TYR   A C   
1663 O O   . TYR   A 68  ? 0.1530 0.1527 0.2250 0.0104  0.0308  0.0233  68  TYR   A O   
1664 C CB  . TYR   A 68  ? 0.1568 0.1485 0.2293 0.0136  0.0485  0.0408  68  TYR   A CB  
1665 C CG  . TYR   A 68  ? 0.1653 0.1653 0.2545 0.0105  0.0571  0.0368  68  TYR   A CG  
1666 C CD1 . TYR   A 68  ? 0.1714 0.1731 0.2929 -0.0191 0.0476  -0.0033 68  TYR   A CD1 
1667 C CD2 . TYR   A 68  ? 0.1835 0.1690 0.2977 0.0172  0.0642  0.0527  68  TYR   A CD2 
1668 C CE1 . TYR   A 68  ? 0.1769 0.1859 0.3311 -0.0163 0.0587  -0.0067 68  TYR   A CE1 
1669 C CE2 . TYR   A 68  ? 0.1832 0.1734 0.3283 0.0061  0.0675  0.0306  68  TYR   A CE2 
1670 C CZ  . TYR   A 68  ? 0.1788 0.1767 0.3449 -0.0134 0.0590  -0.0040 68  TYR   A CZ  
1671 O OH  . TYR   A 68  ? 0.2073 0.1755 0.3680 -0.0127 0.0378  -0.0348 68  TYR   A OH  
1681 N N   . ILE   A 69  ? 0.1384 0.1394 0.2052 0.0022  0.0201  0.0191  69  ILE   A N   
1682 C CA  . ILE   A 69  ? 0.1457 0.1431 0.1988 0.0078  0.0159  0.0062  69  ILE   A CA  
1683 C C   . ILE   A 69  ? 0.1465 0.1466 0.1920 0.0058  0.0176  0.0184  69  ILE   A C   
1684 O O   . ILE   A 69  ? 0.1544 0.1534 0.1976 0.0010  0.0222  0.0160  69  ILE   A O   
1685 C CB  . ILE   A 69  ? 0.1496 0.1637 0.2077 0.0047  0.0199  0.0006  69  ILE   A CB  
1686 C CG1 . ILE   A 69  ? 0.1524 0.1791 0.2160 0.0095  0.0142  -0.0198 69  ILE   A CG1 
1687 C CG2 . ILE   A 69  ? 0.1685 0.1911 0.2203 0.0163  0.0110  -0.0120 69  ILE   A CG2 
1688 C CD1 . ILE   A 69  ? 0.1566 0.1918 0.2312 -0.0046 0.0166  -0.0220 69  ILE   A CD1 
1700 N N   . ALA   A 70  ? 0.1522 0.1486 0.2173 -0.0062 0.0204  0.0236  70  ALA   A N   
1701 C CA  . ALA   A 70  ? 0.1571 0.1576 0.2313 -0.0147 0.0290  0.0315  70  ALA   A CA  
1702 C C   . ALA   A 70  ? 0.1594 0.1778 0.2205 -0.0117 0.0279  0.0325  70  ALA   A C   
1703 O O   . ALA   A 70  ? 0.1790 0.2136 0.2504 0.0117  0.0458  0.0476  70  ALA   A O   
1704 C CB  . ALA   A 70  ? 0.1593 0.1570 0.2583 -0.0208 0.0200  0.0253  70  ALA   A CB  
1710 N N   . THR   A 71  ? 0.1507 0.1739 0.2179 -0.0001 0.0189  0.0294  71  THR   A N   
1711 C CA  . THR   A 71  ? 0.1638 0.1930 0.2529 0.0143  0.0213  0.0309  71  THR   A CA  
1712 C C   . THR   A 71  ? 0.1498 0.1835 0.2777 0.0164  0.0336  0.0268  71  THR   A C   
1713 O O   . THR   A 71  ? 0.1540 0.2128 0.3294 0.0143  0.0512  0.0015  71  THR   A O   
1714 C CB  . THR   A 71  ? 0.1936 0.2274 0.2910 0.0179  -0.0185 0.0410  71  THR   A CB  
1715 O OG1 . THR   A 71  ? 0.2201 0.2432 0.3074 0.0062  -0.0399 0.0352  71  THR   A OG1 
1716 C CG2 . THR   A 71  ? 0.2081 0.2444 0.3232 0.0241  -0.0276 0.0559  71  THR   A CG2 
1724 N N   . ASN   A 72  ? 0.1507 0.1633 0.2466 0.0108  0.0303  0.0342  72  ASN   A N   
1725 C CA  . ASN   A 72  ? 0.1580 0.1716 0.2525 0.0206  0.0419  0.0310  72  ASN   A CA  
1726 C C   . ASN   A 72  ? 0.1684 0.1673 0.2455 0.0125  0.0473  0.0154  72  ASN   A C   
1727 O O   . ASN   A 72  ? 0.1889 0.1684 0.2641 0.0137  0.0515  0.0030  72  ASN   A O   
1728 C CB  . ASN   A 72  ? 0.1822 0.1795 0.2514 0.0198  0.0404  0.0409  72  ASN   A CB  
1729 C CG  . ASN   A 72  ? 0.2042 0.1933 0.2588 0.0283  0.0366  0.0418  72  ASN   A CG  
1730 O OD1 . ASN   A 72  ? 0.2226 0.2251 0.2810 0.0318  0.0415  0.0394  72  ASN   A OD1 
1731 N ND2 . ASN   A 72  ? 0.2205 0.1961 0.2663 0.0546  0.0253  0.0387  72  ASN   A ND2 
1738 N N   . GLY   A 73  ? 0.1660 0.1582 0.2337 0.0061  0.0459  0.0125  73  GLY   A N   
1739 C CA  . GLY   A 73  ? 0.1772 0.1561 0.2129 -0.0082 0.0517  0.0112  73  GLY   A CA  
1740 C C   . GLY   A 73  ? 0.1782 0.1501 0.1957 0.0026  0.0549  0.0219  73  GLY   A C   
1741 O O   . GLY   A 73  ? 0.1746 0.1593 0.2069 0.0139  0.0428  0.0275  73  GLY   A O   
1745 N N   . PRO   A 74  ? 0.1848 0.1558 0.1971 -0.0143 0.0525  0.0102  74  PRO   A N   
1746 C CA  . PRO   A 74  ? 0.1787 0.1485 0.2152 -0.0023 0.0444  0.0167  74  PRO   A CA  
1747 C C   . PRO   A 74  ? 0.1719 0.1307 0.2089 0.0011  0.0329  0.0140  74  PRO   A C   
1748 O O   . PRO   A 74  ? 0.1789 0.1410 0.2288 0.0033  0.0352  -0.0003 74  PRO   A O   
1749 C CB  . PRO   A 74  ? 0.1966 0.1759 0.2315 0.0015  0.0484  0.0275  74  PRO   A CB  
1750 C CG  . PRO   A 74  ? 0.2239 0.2159 0.2770 -0.0213 0.0373  0.0102  74  PRO   A CG  
1751 C CD  . PRO   A 74  ? 0.2008 0.1895 0.2276 -0.0285 0.0448  -0.0013 74  PRO   A CD  
1759 N N   . LEU   A 75  ? 0.1677 0.1322 0.1910 0.0012  0.0275  0.0068  75  LEU   A N   
1760 C CA  . LEU   A 75  ? 0.1649 0.1339 0.1787 0.0034  0.0146  0.0107  75  LEU   A CA  
1761 C C   . LEU   A 75  ? 0.1765 0.1437 0.1740 0.0065  0.0143  0.0157  75  LEU   A C   
1762 O O   . LEU   A 75  ? 0.2135 0.1615 0.1633 0.0157  0.0087  0.0128  75  LEU   A O   
1763 C CB  . LEU   A 75  ? 0.1714 0.1394 0.1718 -0.0050 0.0063  0.0206  75  LEU   A CB  
1764 C CG  . LEU   A 75  ? 0.1907 0.1729 0.1856 -0.0363 0.0029  0.0148  75  LEU   A CG  
1765 C CD1 . LEU   A 75  ? 0.2077 0.2256 0.1954 -0.0409 0.0008  0.0045  75  LEU   A CD1 
1766 C CD2 . LEU   A 75  ? 0.2234 0.2120 0.2346 -0.0137 0.0079  0.0255  75  LEU   A CD2 
1778 N N   . LYS   A 76  ? 0.1777 0.1416 0.1851 -0.0008 0.0077  0.0071  76  LYS   A N   
1779 C CA  . LYS   A 76  ? 0.1747 0.1623 0.1880 -0.0081 0.0083  -0.0035 76  LYS   A CA  
1780 C C   . LYS   A 76  ? 0.1717 0.1471 0.1586 0.0011  0.0103  0.0101  76  LYS   A C   
1781 O O   . LYS   A 76  ? 0.1809 0.1432 0.1654 0.0007  0.0187  0.0161  76  LYS   A O   
1782 C CB  . LYS   A 76  ? 0.1777 0.1786 0.2127 -0.0016 0.0028  -0.0259 76  LYS   A CB  
1783 C CG  . LYS   A 76  ? 0.1864 0.1781 0.2633 0.0088  -0.0007 -0.0180 76  LYS   A CG  
1784 C CD  . LYS   A 76  ? 0.1913 0.1786 0.3099 0.0143  -0.0065 -0.0201 76  LYS   A CD  
1785 C CE  . LYS   A 76  ? 0.2007 0.1941 0.3769 0.0050  -0.0028 -0.0296 76  LYS   A CE  
1786 N NZ  . LYS   A 76  ? 0.2041 0.1845 0.4219 -0.0044 -0.0057 -0.0379 76  LYS   A NZ  
1800 N N   . VAL   A 77  ? 0.1820 0.1586 0.1605 -0.0004 0.0184  0.0194  77  VAL   A N   
1801 C CA  . VAL   A 77  ? 0.1829 0.1541 0.1652 0.0015  0.0109  0.0146  77  VAL   A CA  
1802 C C   . VAL   A 77  ? 0.1783 0.1479 0.1693 0.0063  0.0114  0.0092  77  VAL   A C   
1803 O O   . VAL   A 77  ? 0.1835 0.1545 0.1742 0.0092  0.0265  0.0017  77  VAL   A O   
1804 C CB  . VAL   A 77  ? 0.1972 0.1742 0.1689 -0.0026 0.0011  0.0201  77  VAL   A CB  
1805 C CG1 . VAL   A 77  ? 0.1943 0.1813 0.1998 0.0107  -0.0024 0.0071  77  VAL   A CG1 
1806 C CG2 . VAL   A 77  ? 0.2172 0.1910 0.1873 -0.0055 -0.0098 0.0182  77  VAL   A CG2 
1816 N N   . GLY   A 78  ? 0.1675 0.1477 0.1542 0.0050  0.0168  0.0112  78  GLY   A N   
1817 C CA  . GLY   A 78  ? 0.1707 0.1474 0.1653 -0.0022 0.0189  0.0102  78  GLY   A CA  
1818 C C   . GLY   A 78  ? 0.1564 0.1394 0.1771 0.0037  0.0197  0.0119  78  GLY   A C   
1819 O O   . GLY   A 78  ? 0.1510 0.1443 0.2025 0.0011  0.0190  0.0323  78  GLY   A O   
1823 N N   . GLY   A 79  ? 0.1593 0.1357 0.1752 -0.0036 0.0121  0.0178  79  GLY   A N   
1824 C CA  . GLY   A 79  ? 0.1531 0.1426 0.1795 0.0007  0.0136  0.0234  79  GLY   A CA  
1825 C C   . GLY   A 79  ? 0.1417 0.1338 0.1731 0.0005  0.0127  0.0116  79  GLY   A C   
1826 O O   . GLY   A 79  ? 0.1484 0.1458 0.1857 0.0165  0.0141  0.0099  79  GLY   A O   
1830 N N   . SER   A 80  ? 0.1388 0.1510 0.1951 0.0009  0.0157  0.0011  80  SER   A N   
1831 C CA  . SER   A 80  ? 0.1381 0.1456 0.1820 -0.0012 0.0081  0.0055  80  SER   A CA  
1832 C C   . SER   A 80  ? 0.1412 0.1459 0.1773 -0.0009 0.0100  0.0154  80  SER   A C   
1833 O O   . SER   A 80  ? 0.1385 0.1703 0.2064 0.0086  0.0115  0.0018  80  SER   A O   
1834 C CB  . SER   A 80  ? 0.1508 0.1446 0.2067 -0.0080 0.0114  0.0074  80  SER   A CB  
1835 O OG  . SER   A 80  ? 0.1794 0.1427 0.2455 0.0032  0.0032  0.0234  80  SER   A OG  
1841 N N   . CYS   A 81  ? 0.1369 0.1382 0.1763 -0.0012 -0.0032 0.0168  81  CYS   A N   
1842 C CA  . CYS   A 81  ? 0.1359 0.1475 0.1712 -0.0037 -0.0019 0.0212  81  CYS   A CA  
1843 C C   . CYS   A 81  ? 0.1341 0.1446 0.1751 -0.0097 0.0016  0.0319  81  CYS   A C   
1844 O O   . CYS   A 81  ? 0.1354 0.1730 0.1954 0.0012  0.0020  0.0334  81  CYS   A O   
1845 C CB  . CYS   A 81  ? 0.1475 0.1584 0.1896 -0.0153 0.0020  0.0318  81  CYS   A CB  
1846 S SG  . CYS   A 81  ? 0.1535 0.1432 0.1986 -0.0150 0.0001  0.0204  81  CYS   A SG  
1852 N N   . VAL   A 82  ? 0.1391 0.1572 0.1747 -0.0016 -0.0142 0.0329  82  VAL   A N   
1853 C CA  . VAL   A 82  ? 0.1510 0.1581 0.1739 0.0005  -0.0122 0.0318  82  VAL   A CA  
1854 C C   . VAL   A 82  ? 0.1459 0.1575 0.1847 -0.0054 -0.0095 0.0308  82  VAL   A C   
1855 O O   . VAL   A 82  ? 0.1428 0.1665 0.2206 -0.0047 -0.0066 0.0082  82  VAL   A O   
1856 C CB  . VAL   A 82  ? 0.1801 0.1713 0.1885 0.0048  -0.0027 0.0343  82  VAL   A CB  
1857 C CG1 . VAL   A 82  ? 0.2027 0.1851 0.2176 0.0027  -0.0005 0.0316  82  VAL   A CG1 
1858 C CG2 . VAL   A 82  ? 0.1873 0.1726 0.2238 -0.0034 -0.0028 0.0350  82  VAL   A CG2 
1868 N N   . LEU   A 83  ? 0.1445 0.1554 0.1695 -0.0103 -0.0068 0.0198  83  LEU   A N   
1869 C CA  . LEU   A 83  ? 0.1489 0.1608 0.1640 -0.0105 -0.0087 0.0146  83  LEU   A CA  
1870 C C   . LEU   A 83  ? 0.1532 0.1621 0.1626 -0.0131 -0.0140 0.0198  83  LEU   A C   
1871 O O   . LEU   A 83  ? 0.1621 0.1659 0.1722 -0.0198 -0.0071 0.0281  83  LEU   A O   
1872 C CB  . LEU   A 83  ? 0.1526 0.1637 0.1800 -0.0103 -0.0158 0.0150  83  LEU   A CB  
1873 C CG  . LEU   A 83  ? 0.1666 0.1686 0.1870 -0.0111 0.0048  0.0144  83  LEU   A CG  
1874 C CD1 . LEU   A 83  ? 0.1807 0.1728 0.1986 -0.0228 -0.0054 0.0247  83  LEU   A CD1 
1875 C CD2 . LEU   A 83  ? 0.1678 0.1799 0.2029 -0.0155 0.0097  0.0160  83  LEU   A CD2 
1887 N N   . SER   A 84  ? 0.1702 0.1691 0.1704 -0.0135 -0.0108 0.0237  84  SER   A N   
1888 C CA  . SER   A 84  ? 0.1833 0.1727 0.1604 -0.0181 -0.0107 0.0179  84  SER   A CA  
1889 C C   . SER   A 84  ? 0.1823 0.1748 0.1568 -0.0254 0.0019  0.0145  84  SER   A C   
1890 O O   . SER   A 84  ? 0.1776 0.1888 0.1497 -0.0171 -0.0057 0.0224  84  SER   A O   
1891 C CB  . SER   A 84  ? 0.1952 0.1967 0.1714 -0.0162 -0.0091 0.0074  84  SER   A CB  
1892 O OG  . SER   A 84  ? 0.1965 0.2219 0.1836 -0.0129 -0.0225 -0.0032 84  SER   A OG  
1898 N N   . GLY   A 85  ? 0.1937 0.1905 0.1581 -0.0255 0.0144  0.0134  85  GLY   A N   
1899 C CA  . GLY   A 85  ? 0.1933 0.1988 0.1878 -0.0312 0.0166  0.0030  85  GLY   A CA  
1900 C C   . GLY   A 85  ? 0.1892 0.2102 0.1666 -0.0225 -0.0003 0.0005  85  GLY   A C   
1901 O O   . GLY   A 85  ? 0.1943 0.2253 0.1726 -0.0335 0.0116  -0.0098 85  GLY   A O   
1905 N N   . HIS   A 86  ? 0.1946 0.1986 0.1506 -0.0163 -0.0045 0.0110  86  HIS   A N   
1906 C CA  . HIS   A 86  ? 0.2142 0.2052 0.1378 -0.0182 -0.0053 0.0165  86  HIS   A CA  
1907 C C   . HIS   A 86  ? 0.2397 0.2208 0.1314 -0.0218 -0.0143 0.0110  86  HIS   A C   
1908 O O   . HIS   A 86  ? 0.2569 0.2433 0.1464 -0.0170 -0.0027 0.0044  86  HIS   A O   
1909 C CB  . HIS   A 86  ? 0.2139 0.2019 0.1518 -0.0185 -0.0064 0.0194  86  HIS   A CB  
1910 C CG  . HIS   A 86  ? 0.2058 0.1996 0.1643 -0.0137 0.0003  0.0267  86  HIS   A CG  
1911 N ND1 . HIS   A 86  ? 0.2081 0.2010 0.1983 -0.0179 -0.0068 0.0220  86  HIS   A ND1 
1912 C CD2 . HIS   A 86  ? 0.2063 0.1959 0.1624 0.0021  0.0119  0.0263  86  HIS   A CD2 
1913 C CE1 . HIS   A 86  ? 0.2025 0.2017 0.1940 -0.0111 0.0145  0.0319  86  HIS   A CE1 
1914 N NE2 . HIS   A 86  ? 0.2058 0.1962 0.1799 0.0039  0.0158  0.0384  86  HIS   A NE2 
1922 N N   . ASN   A 87  ? 0.2499 0.2265 0.1584 -0.0139 0.0075  -0.0076 87  ASN   A N   
1923 C CA  . ASN   A 87  ? 0.2711 0.2381 0.1614 -0.0147 0.0335  -0.0160 87  ASN   A CA  
1924 C C   . ASN   A 87  ? 0.2740 0.2555 0.1779 -0.0230 0.0561  0.0006  87  ASN   A C   
1925 O O   . ASN   A 87  ? 0.3026 0.2824 0.2181 -0.0374 0.0911  -0.0015 87  ASN   A O   
1926 C CB  . ASN   A 87  ? 0.2885 0.2432 0.1728 -0.0048 0.0393  -0.0123 87  ASN   A CB  
1927 C CG  . ASN   A 87  ? 0.2982 0.2498 0.1742 0.0038  0.0524  -0.0055 87  ASN   A CG  
1928 O OD1 . ASN   A 87  ? 0.3179 0.2492 0.1800 0.0156  0.0535  0.0056  87  ASN   A OD1 
1929 N ND2 . ASN   A 87  ? 0.2958 0.2719 0.1983 0.0028  0.0474  -0.0023 87  ASN   A ND2 
1936 N N   . LEU   A 88  ? 0.2448 0.2414 0.1706 -0.0231 0.0339  0.0059  88  LEU   A N   
1937 C CA  . LEU   A 88  ? 0.2207 0.2392 0.1930 -0.0284 0.0398  0.0253  88  LEU   A CA  
1938 C C   . LEU   A 88  ? 0.2078 0.2489 0.1932 -0.0274 0.0350  0.0343  88  LEU   A C   
1939 O O   . LEU   A 88  ? 0.2027 0.2520 0.2300 -0.0245 0.0417  0.0521  88  LEU   A O   
1940 C CB  . LEU   A 88  ? 0.2132 0.2424 0.2080 -0.0366 0.0092  0.0275  88  LEU   A CB  
1941 C CG  . LEU   A 88  ? 0.2287 0.2525 0.2329 -0.0361 -0.0073 0.0376  88  LEU   A CG  
1942 C CD1 . LEU   A 88  ? 0.2359 0.2615 0.2329 -0.0434 -0.0171 0.0233  88  LEU   A CD1 
1943 C CD2 . LEU   A 88  ? 0.2437 0.2647 0.2676 -0.0278 -0.0018 0.0329  88  LEU   A CD2 
1955 N N   . ALA   A 89  ? 0.2077 0.2426 0.1647 -0.0286 0.0167  0.0163  89  ALA   A N   
1956 C CA  . ALA   A 89  ? 0.2139 0.2426 0.1533 -0.0222 0.0110  0.0303  89  ALA   A CA  
1957 C C   . ALA   A 89  ? 0.2225 0.2427 0.1575 -0.0206 -0.0042 0.0330  89  ALA   A C   
1958 O O   . ALA   A 89  ? 0.2142 0.2389 0.1965 -0.0318 -0.0061 -0.0000 89  ALA   A O   
1959 C CB  . ALA   A 89  ? 0.2039 0.2444 0.1435 -0.0174 0.0020  0.0332  89  ALA   A CB  
1965 N N   . LYS   A 90  ? 0.2319 0.2535 0.1584 -0.0355 -0.0156 0.0361  90  LYS   A N   
1966 C CA  . LYS   A 90  ? 0.2497 0.2751 0.1631 -0.0300 -0.0252 0.0317  90  LYS   A CA  
1967 C C   . LYS   A 90  ? 0.2239 0.2455 0.1583 -0.0277 -0.0233 0.0157  90  LYS   A C   
1968 O O   . LYS   A 90  ? 0.2253 0.2549 0.1876 -0.0286 -0.0318 0.0088  90  LYS   A O   
1969 C CB  . LYS   A 90  ? 0.2869 0.3236 0.2069 -0.0328 -0.0333 0.0593  90  LYS   A CB  
1970 C CG  . LYS   A 90  ? 0.3391 0.3681 0.3167 -0.0374 -0.0292 0.0696  90  LYS   A CG  
1971 C CD  . LYS   A 90  ? 0.3916 0.4099 0.4342 -0.0439 -0.0085 0.0784  90  LYS   A CD  
1972 C CE  . LYS   A 90  ? 0.4316 0.4456 0.5306 -0.0479 0.0033  0.0761  90  LYS   A CE  
1973 N NZ  . LYS   A 90  ? 0.4565 0.4599 0.5880 -0.0508 0.0121  0.0713  90  LYS   A NZ  
1987 N N   . HIS   A 91  ? 0.2106 0.2130 0.1276 -0.0229 -0.0297 0.0244  91  HIS   A N   
1988 C CA  . HIS   A 91  ? 0.1916 0.1900 0.1422 -0.0162 -0.0278 0.0263  91  HIS   A CA  
1989 C C   . HIS   A 91  ? 0.1714 0.1820 0.1416 -0.0144 -0.0192 0.0284  91  HIS   A C   
1990 O O   . HIS   A 91  ? 0.1633 0.2029 0.1624 -0.0214 -0.0032 0.0302  91  HIS   A O   
1991 C CB  . HIS   A 91  ? 0.2067 0.2178 0.1906 0.0090  -0.0425 0.0315  91  HIS   A CB  
1992 C CG  . HIS   A 91  ? 0.2527 0.2693 0.2512 0.0195  -0.0653 0.0113  91  HIS   A CG  
1993 N ND1 . HIS   A 91  ? 0.2659 0.2969 0.2912 0.0234  -0.0787 -0.0147 91  HIS   A ND1 
1994 C CD2 . HIS   A 91  ? 0.2764 0.2928 0.2721 0.0253  -0.0816 0.0195  91  HIS   A CD2 
1995 C CE1 . HIS   A 91  ? 0.2787 0.3081 0.3085 0.0254  -0.0736 -0.0024 91  HIS   A CE1 
1996 N NE2 . HIS   A 91  ? 0.2877 0.3066 0.3020 0.0309  -0.0810 0.0116  91  HIS   A NE2 
2004 N N   . CYS   A 92  ? 0.1630 0.1727 0.1493 -0.0192 -0.0150 0.0282  92  CYS   A N   
2005 C CA  . CYS   A 92  ? 0.1528 0.1651 0.1596 -0.0108 0.0013  0.0257  92  CYS   A CA  
2006 C C   . CYS   A 92  ? 0.1431 0.1580 0.1583 -0.0141 0.0014  0.0295  92  CYS   A C   
2007 O O   . CYS   A 92  ? 0.1482 0.1678 0.1731 -0.0196 -0.0019 0.0163  92  CYS   A O   
2008 C CB  . CYS   A 92  ? 0.1594 0.1685 0.1655 -0.0075 -0.0088 0.0136  92  CYS   A CB  
2009 S SG  . CYS   A 92  ? 0.1540 0.1514 0.1714 -0.0123 -0.0029 0.0179  92  CYS   A SG  
2015 N N   . LEU   A 93  ? 0.1401 0.1438 0.1651 -0.0147 0.0084  0.0211  93  LEU   A N   
2016 C CA  . LEU   A 93  ? 0.1335 0.1430 0.1671 -0.0108 0.0054  0.0210  93  LEU   A CA  
2017 C C   . LEU   A 93  ? 0.1349 0.1345 0.1587 -0.0056 0.0095  0.0158  93  LEU   A C   
2018 O O   . LEU   A 93  ? 0.1284 0.1431 0.1640 -0.0050 0.0023  0.0157  93  LEU   A O   
2019 C CB  . LEU   A 93  ? 0.1387 0.1452 0.1763 -0.0043 -0.0035 0.0262  93  LEU   A CB  
2020 C CG  . LEU   A 93  ? 0.1455 0.1481 0.1754 -0.0047 0.0005  0.0227  93  LEU   A CG  
2021 C CD1 . LEU   A 93  ? 0.1568 0.1472 0.2010 -0.0045 0.0059  0.0124  93  LEU   A CD1 
2022 C CD2 . LEU   A 93  ? 0.1595 0.1486 0.1953 -0.0080 -0.0001 0.0215  93  LEU   A CD2 
2034 N N   . HIS   A 94  ? 0.1331 0.1272 0.1553 -0.0055 0.0033  0.0243  94  HIS   A N   
2035 C CA  . HIS   A 94  ? 0.1311 0.1327 0.1684 -0.0020 -0.0009 0.0180  94  HIS   A CA  
2036 C C   . HIS   A 94  ? 0.1271 0.1297 0.1653 -0.0083 -0.0023 0.0147  94  HIS   A C   
2037 O O   . HIS   A 94  ? 0.1279 0.1471 0.1958 0.0014  0.0018  -0.0081 94  HIS   A O   
2038 C CB  . HIS   A 94  ? 0.1281 0.1299 0.1643 -0.0052 -0.0084 0.0165  94  HIS   A CB  
2039 C CG  . HIS   A 94  ? 0.1375 0.1263 0.1560 -0.0070 -0.0064 0.0246  94  HIS   A CG  
2040 N ND1 . HIS   A 94  ? 0.1353 0.1306 0.1659 -0.0105 -0.0067 0.0191  94  HIS   A ND1 
2041 C CD2 . HIS   A 94  ? 0.1438 0.1385 0.1692 -0.0078 -0.0066 0.0178  94  HIS   A CD2 
2042 C CE1 . HIS   A 94  ? 0.1418 0.1336 0.1659 -0.0099 -0.0171 0.0176  94  HIS   A CE1 
2043 N NE2 . HIS   A 94  ? 0.1480 0.1347 0.1701 -0.0103 -0.0067 0.0115  94  HIS   A NE2 
2051 N N   . VAL   A 95  ? 0.1244 0.1260 0.1478 -0.0069 0.0031  0.0095  95  VAL   A N   
2052 C CA  . VAL   A 95  ? 0.1357 0.1282 0.1447 -0.0066 0.0058  0.0152  95  VAL   A CA  
2053 C C   . VAL   A 95  ? 0.1345 0.1315 0.1416 -0.0132 0.0020  0.0111  95  VAL   A C   
2054 O O   . VAL   A 95  ? 0.1352 0.1378 0.1630 0.0102  0.0025  0.0122  95  VAL   A O   
2055 C CB  . VAL   A 95  ? 0.1382 0.1375 0.1572 -0.0101 0.0091  0.0092  95  VAL   A CB  
2056 C CG1 . VAL   A 95  ? 0.1490 0.1404 0.1826 -0.0160 0.0045  0.0030  95  VAL   A CG1 
2057 C CG2 . VAL   A 95  ? 0.1379 0.1399 0.1671 -0.0148 0.0098  0.0259  95  VAL   A CG2 
2067 N N   . VAL   A 96  ? 0.1418 0.1300 0.1317 -0.0089 0.0026  0.0138  96  VAL   A N   
2068 C CA  . VAL   A 96  ? 0.1411 0.1374 0.1527 -0.0050 0.0024  0.0253  96  VAL   A CA  
2069 C C   . VAL   A 96  ? 0.1417 0.1446 0.1530 -0.0031 0.0072  0.0236  96  VAL   A C   
2070 O O   . VAL   A 96  ? 0.1514 0.1485 0.1736 -0.0046 0.0141  0.0044  96  VAL   A O   
2071 C CB  . VAL   A 96  ? 0.1463 0.1384 0.1580 -0.0066 0.0144  0.0198  96  VAL   A CB  
2072 C CG1 . VAL   A 96  ? 0.1566 0.1493 0.1456 -0.0070 0.0169  0.0092  96  VAL   A CG1 
2073 C CG2 . VAL   A 96  ? 0.1457 0.1464 0.1737 -0.0151 0.0164  0.0134  96  VAL   A CG2 
2083 N N   A GLY   A 97  ? 0.1400 0.1441 0.1688 -0.0112 0.0041  0.0121  97  GLY   A N   
2084 N N   B GLY   A 97  ? 0.1466 0.1473 0.1509 -0.0058 0.0059  0.0184  97  GLY   A N   
2085 C CA  A GLY   A 97  ? 0.1525 0.1567 0.1690 -0.0105 -0.0011 0.0164  97  GLY   A CA  
2086 C CA  B GLY   A 97  ? 0.1549 0.1520 0.1439 -0.0059 0.0048  0.0234  97  GLY   A CA  
2087 C C   A GLY   A 97  ? 0.1558 0.1666 0.1569 -0.0155 0.0014  0.0065  97  GLY   A C   
2088 C C   B GLY   A 97  ? 0.1595 0.1547 0.1460 -0.0079 0.0061  0.0278  97  GLY   A C   
2089 O O   A GLY   A 97  ? 0.1604 0.1644 0.1713 -0.0119 0.0028  0.0043  97  GLY   A O   
2090 O O   B GLY   A 97  ? 0.1596 0.1579 0.1622 -0.0122 0.0111  0.0305  97  GLY   A O   
2097 N N   A PRO   A 98  ? 0.1665 0.1663 0.1491 -0.0062 -0.0090 0.0088  98  PRO   A N   
2098 N N   B PRO   A 98  ? 0.1731 0.1520 0.1488 0.0020  0.0010  0.0373  98  PRO   A N   
2099 C CA  A PRO   A 98  ? 0.1729 0.1805 0.1548 -0.0106 -0.0042 0.0042  98  PRO   A CA  
2100 C CA  B PRO   A 98  ? 0.1823 0.1562 0.1587 0.0028  -0.0047 0.0217  98  PRO   A CA  
2101 C C   A PRO   A 98  ? 0.1769 0.1920 0.1385 -0.0164 -0.0063 0.0143  98  PRO   A C   
2102 C C   B PRO   A 98  ? 0.1923 0.1545 0.1544 0.0028  -0.0056 0.0222  98  PRO   A C   
2103 O O   A PRO   A 98  ? 0.1707 0.1767 0.1511 -0.0098 -0.0030 0.0087  98  PRO   A O   
2104 O O   B PRO   A 98  ? 0.1901 0.1493 0.1769 0.0061  -0.0041 0.0190  98  PRO   A O   
2105 C CB  A PRO   A 98  ? 0.1785 0.1891 0.1469 0.0040  -0.0082 -0.0032 98  PRO   A CB  
2106 C CB  B PRO   A 98  ? 0.1859 0.1548 0.1581 0.0071  -0.0038 0.0176  98  PRO   A CB  
2107 C CG  A PRO   A 98  ? 0.1814 0.1811 0.1578 0.0039  -0.0099 -0.0098 98  PRO   A CG  
2108 C CG  B PRO   A 98  ? 0.1879 0.1558 0.1640 0.0046  -0.0032 0.0265  98  PRO   A CG  
2109 C CD  A PRO   A 98  ? 0.1725 0.1678 0.1590 -0.0058 -0.0129 0.0005  98  PRO   A CD  
2110 C CD  B PRO   A 98  ? 0.1793 0.1484 0.1528 0.0037  -0.0039 0.0437  98  PRO   A CD  
2125 N N   A ASN   A 99  ? 0.1827 0.2184 0.1230 -0.0172 -0.0052 0.0340  99  ASN   A N   
2126 N N   B ASN   A 99  ? 0.2082 0.1558 0.1431 0.0093  -0.0064 0.0254  99  ASN   A N   
2127 C CA  A ASN   A 99  ? 0.2003 0.2364 0.1380 -0.0146 -0.0078 0.0375  99  ASN   A CA  
2128 C CA  B ASN   A 99  ? 0.2293 0.1635 0.1456 0.0148  -0.0057 0.0298  99  ASN   A CA  
2129 C C   A ASN   A 99  ? 0.2231 0.2689 0.1309 -0.0260 -0.0028 0.0490  99  ASN   A C   
2130 C C   B ASN   A 99  ? 0.2403 0.1739 0.1456 0.0179  -0.0110 0.0346  99  ASN   A C   
2131 O O   A ASN   A 99  ? 0.2330 0.2945 0.1476 -0.0165 -0.0083 0.0321  99  ASN   A O   
2132 O O   B ASN   A 99  ? 0.2408 0.1647 0.1341 0.0229  -0.0156 0.0302  99  ASN   A O   
2133 C CB  A ASN   A 99  ? 0.1952 0.2275 0.1535 -0.0130 -0.0176 0.0412  99  ASN   A CB  
2134 C CB  B ASN   A 99  ? 0.2401 0.1578 0.1624 0.0187  -0.0027 0.0299  99  ASN   A CB  
2135 C CG  A ASN   A 99  ? 0.1950 0.2210 0.1776 -0.0053 -0.0201 0.0392  99  ASN   A CG  
2136 C CG  B ASN   A 99  ? 0.2520 0.1591 0.1740 0.0206  -0.0024 0.0350  99  ASN   A CG  
2137 O OD1 A ASN   A 99  ? 0.2023 0.2252 0.1828 0.0031  -0.0166 0.0193  99  ASN   A OD1 
2138 O OD1 B ASN   A 99  ? 0.2501 0.1585 0.1620 0.0312  -0.0040 0.0451  99  ASN   A OD1 
2139 N ND2 A ASN   A 99  ? 0.1977 0.2153 0.2136 -0.0063 -0.0295 0.0517  99  ASN   A ND2 
2140 N ND2 B ASN   A 99  ? 0.2583 0.1632 0.2077 0.0183  -0.0070 0.0284  99  ASN   A ND2 
2153 N N   A VAL   A 100 ? 0.2418 0.2806 0.1273 -0.0443 -0.0222 0.0403  100 VAL   A N   
2154 N N   B VAL   A 100 ? 0.2545 0.2007 0.1764 0.0178  -0.0113 0.0416  100 VAL   A N   
2155 C CA  A VAL   A 100 ? 0.2689 0.3046 0.1474 -0.0456 -0.0329 0.0429  100 VAL   A CA  
2156 C CA  B VAL   A 100 ? 0.2743 0.2257 0.2218 0.0178  -0.0134 0.0305  100 VAL   A CA  
2157 C C   A VAL   A 100 ? 0.2872 0.3270 0.1486 -0.0478 -0.0505 0.0694  100 VAL   A C   
2158 C C   B VAL   A 100 ? 0.2838 0.2334 0.2237 0.0230  -0.0197 0.0261  100 VAL   A C   
2159 O O   A VAL   A 100 ? 0.2990 0.3361 0.1779 -0.0434 -0.0308 0.0622  100 VAL   A O   
2160 O O   B VAL   A 100 ? 0.2855 0.2335 0.2268 0.0211  -0.0278 0.0148  100 VAL   A O   
2161 C CB  A VAL   A 100 ? 0.2846 0.3063 0.1867 -0.0442 -0.0273 0.0258  100 VAL   A CB  
2162 C CB  B VAL   A 100 ? 0.2850 0.2457 0.2595 0.0119  -0.0055 0.0233  100 VAL   A CB  
2163 C CG1 A VAL   A 100 ? 0.2887 0.3142 0.2174 -0.0453 -0.0168 0.0187  100 VAL   A CG1 
2164 C CG1 B VAL   A 100 ? 0.2868 0.2511 0.2779 0.0131  -0.0048 0.0178  100 VAL   A CG1 
2165 C CG2 A VAL   A 100 ? 0.2947 0.3083 0.1813 -0.0448 -0.0279 0.0243  100 VAL   A CG2 
2166 C CG2 B VAL   A 100 ? 0.2894 0.2531 0.2772 0.0102  -0.0038 0.0246  100 VAL   A CG2 
2185 N N   A ASN   A 101 ? 0.2986 0.3393 0.1831 -0.0519 -0.0603 0.1019  101 ASN   A N   
2186 N N   B ASN   A 101 ? 0.2963 0.2473 0.2312 0.0251  -0.0166 0.0269  101 ASN   A N   
2187 C CA  A ASN   A 101 ? 0.3234 0.3524 0.2151 -0.0527 -0.0639 0.1210  101 ASN   A CA  
2188 C CA  B ASN   A 101 ? 0.3108 0.2680 0.2428 0.0293  -0.0119 0.0285  101 ASN   A CA  
2189 C C   A ASN   A 101 ? 0.3533 0.3848 0.2385 -0.0557 -0.0342 0.1475  101 ASN   A C   
2190 C C   B ASN   A 101 ? 0.3224 0.2838 0.2499 0.0277  -0.0065 0.0318  101 ASN   A C   
2191 O O   A ASN   A 101 ? 0.3629 0.3869 0.2808 -0.0491 -0.0292 0.1437  101 ASN   A O   
2192 O O   B ASN   A 101 ? 0.3242 0.2826 0.2412 0.0265  -0.0079 0.0371  101 ASN   A O   
2193 C CB  A ASN   A 101 ? 0.3219 0.3319 0.2130 -0.0515 -0.0907 0.1033  101 ASN   A CB  
2194 C CB  B ASN   A 101 ? 0.3163 0.2786 0.2596 0.0294  -0.0115 0.0262  101 ASN   A CB  
2195 C CG  A ASN   A 101 ? 0.3227 0.3120 0.2196 -0.0553 -0.0961 0.0755  101 ASN   A CG  
2196 C CG  B ASN   A 101 ? 0.3237 0.2933 0.2805 0.0253  -0.0117 0.0247  101 ASN   A CG  
2197 O OD1 A ASN   A 101 ? 0.3221 0.3194 0.2396 -0.0463 -0.0863 0.0397  101 ASN   A OD1 
2198 O OD1 B ASN   A 101 ? 0.3301 0.3010 0.2927 0.0218  -0.0133 0.0211  101 ASN   A OD1 
2199 N ND2 A ASN   A 101 ? 0.3280 0.3024 0.2372 -0.0609 -0.0984 0.0736  101 ASN   A ND2 
2200 N ND2 B ASN   A 101 ? 0.3274 0.2976 0.2889 0.0230  -0.0065 0.0235  101 ASN   A ND2 
2213 N N   A LYS   A 102 ? 0.3700 0.4177 0.2676 -0.0658 -0.0157 0.1476  102 LYS   A N   
2214 N N   B LYS   A 102 ? 0.3323 0.3005 0.2784 0.0284  -0.0009 0.0278  102 LYS   A N   
2215 C CA  A LYS   A 102 ? 0.3899 0.4492 0.2841 -0.0653 -0.0208 0.1348  102 LYS   A CA  
2216 C CA  B LYS   A 102 ? 0.3423 0.3184 0.2966 0.0249  0.0035  0.0234  102 LYS   A CA  
2217 C C   A LYS   A 102 ? 0.3943 0.4701 0.2688 -0.0507 -0.0202 0.1261  102 LYS   A C   
2218 C C   B LYS   A 102 ? 0.3391 0.3215 0.2878 0.0278  0.0068  0.0250  102 LYS   A C   
2219 O O   A LYS   A 102 ? 0.3994 0.4819 0.2721 -0.0437 -0.0246 0.1215  102 LYS   A O   
2220 O O   B LYS   A 102 ? 0.3418 0.3221 0.2910 0.0324  0.0091  0.0303  102 LYS   A O   
2221 C CB  A LYS   A 102 ? 0.4052 0.4574 0.3362 -0.0750 -0.0318 0.1110  102 LYS   A CB  
2222 C CB  B LYS   A 102 ? 0.3536 0.3313 0.3280 0.0206  -0.0017 0.0196  102 LYS   A CB  
2223 C CG  A LYS   A 102 ? 0.4191 0.4617 0.3842 -0.0825 -0.0397 0.0805  102 LYS   A CG  
2224 C CG  B LYS   A 102 ? 0.3639 0.3441 0.3623 0.0162  -0.0064 0.0160  102 LYS   A CG  
2225 C CD  A LYS   A 102 ? 0.4335 0.4670 0.4324 -0.0881 -0.0496 0.0517  102 LYS   A CD  
2226 C CD  B LYS   A 102 ? 0.3729 0.3567 0.3983 0.0121  -0.0106 0.0148  102 LYS   A CD  
2227 C CE  A LYS   A 102 ? 0.4451 0.4719 0.4708 -0.0921 -0.0570 0.0319  102 LYS   A CE  
2228 C CE  B LYS   A 102 ? 0.3799 0.3659 0.4258 0.0099  -0.0136 0.0154  102 LYS   A CE  
2229 N NZ  A LYS   A 102 ? 0.4505 0.4750 0.4915 -0.0977 -0.0570 0.0178  102 LYS   A NZ  
2230 N NZ  B LYS   A 102 ? 0.3838 0.3707 0.4441 0.0086  -0.0158 0.0144  102 LYS   A NZ  
2257 N N   A GLY   A 103 ? 0.3897 0.4792 0.2744 -0.0410 -0.0189 0.1066  103 GLY   A N   
2258 N N   B GLY   A 103 ? 0.3323 0.3247 0.2845 0.0299  0.0063  0.0149  103 GLY   A N   
2259 C CA  A GLY   A 103 ? 0.3852 0.4836 0.2736 -0.0339 -0.0131 0.0841  103 GLY   A CA  
2260 C CA  B GLY   A 103 ? 0.3250 0.3256 0.2943 0.0333  0.0035  0.0096  103 GLY   A CA  
2261 C C   A GLY   A 103 ? 0.3761 0.4867 0.2782 -0.0306 -0.0030 0.0571  103 GLY   A C   
2262 C C   B GLY   A 103 ? 0.3191 0.3254 0.2991 0.0347  -0.0013 0.0052  103 GLY   A C   
2263 O O   A GLY   A 103 ? 0.3851 0.4946 0.3049 -0.0226 -0.0006 0.0439  103 GLY   A O   
2264 O O   B GLY   A 103 ? 0.3204 0.3298 0.3177 0.0399  -0.0028 -0.0006 103 GLY   A O   
2271 N N   A GLU   A 104 ? 0.3527 0.4764 0.2327 -0.0402 0.0061  0.0421  104 GLU   A N   
2272 N N   B GLU   A 104 ? 0.3099 0.3177 0.2754 0.0303  -0.0083 0.0167  104 GLU   A N   
2273 C CA  A GLU   A 104 ? 0.3285 0.4609 0.2041 -0.0519 0.0114  0.0259  104 GLU   A CA  
2274 C CA  B GLU   A 104 ? 0.3014 0.3100 0.2495 0.0239  -0.0114 0.0192  104 GLU   A CA  
2275 C C   A GLU   A 104 ? 0.3293 0.4658 0.1982 -0.0492 0.0116  -0.0000 104 GLU   A C   
2276 C C   B GLU   A 104 ? 0.2947 0.3069 0.2327 0.0249  -0.0120 0.0080  104 GLU   A C   
2277 O O   A GLU   A 104 ? 0.3269 0.4662 0.2015 -0.0514 0.0120  -0.0091 104 GLU   A O   
2278 O O   B GLU   A 104 ? 0.2926 0.3045 0.2281 0.0256  -0.0115 0.0028  104 GLU   A O   
2279 C CB  A GLU   A 104 ? 0.2986 0.4377 0.1740 -0.0651 0.0187  0.0446  104 GLU   A CB  
2280 C CB  B GLU   A 104 ? 0.3009 0.3061 0.2432 0.0180  -0.0128 0.0335  104 GLU   A CB  
2281 C CG  A GLU   A 104 ? 0.2757 0.4171 0.1763 -0.0744 0.0025  0.0569  104 GLU   A CG  
2282 C CG  B GLU   A 104 ? 0.3016 0.3057 0.2411 0.0124  -0.0165 0.0434  104 GLU   A CG  
2283 C CD  A GLU   A 104 ? 0.2525 0.3965 0.1746 -0.0844 -0.0025 0.0714  104 GLU   A CD  
2284 C CD  B GLU   A 104 ? 0.3058 0.3071 0.2408 0.0073  -0.0217 0.0478  104 GLU   A CD  
2285 O OE1 A GLU   A 104 ? 0.2353 0.3831 0.1421 -0.0882 -0.0101 0.0751  104 GLU   A OE1 
2286 O OE1 B GLU   A 104 ? 0.3080 0.3109 0.2469 0.0079  -0.0217 0.0448  104 GLU   A OE1 
2287 O OE2 A GLU   A 104 ? 0.2608 0.3922 0.2071 -0.0887 0.0042  0.0828  104 GLU   A OE2 
2288 O OE2 B GLU   A 104 ? 0.3085 0.3062 0.2356 0.0023  -0.0217 0.0521  104 GLU   A OE2 
2301 N N   A ASP   A 105 ? 0.3318 0.4693 0.2139 -0.0435 0.0169  -0.0199 105 ASP   A N   
2302 N N   B ASP   A 105 ? 0.2939 0.3070 0.2380 0.0239  -0.0123 -0.0011 105 ASP   A N   
2303 C CA  A ASP   A 105 ? 0.3309 0.4709 0.2490 -0.0325 0.0258  -0.0502 105 ASP   A CA  
2304 C CA  B ASP   A 105 ? 0.2925 0.3059 0.2595 0.0265  -0.0035 -0.0197 105 ASP   A CA  
2305 C C   A ASP   A 105 ? 0.2991 0.4497 0.2171 -0.0389 0.0223  -0.0642 105 ASP   A C   
2306 C C   B ASP   A 105 ? 0.2924 0.2969 0.2377 0.0162  -0.0050 -0.0199 105 ASP   A C   
2307 O O   A ASP   A 105 ? 0.2850 0.4491 0.1771 -0.0379 0.0228  -0.0777 105 ASP   A O   
2308 O O   B ASP   A 105 ? 0.2867 0.2882 0.2062 0.0199  -0.0070 -0.0131 105 ASP   A O   
2309 C CB  A ASP   A 105 ? 0.3575 0.4895 0.3215 -0.0187 0.0284  -0.0643 105 ASP   A CB  
2310 C CB  B ASP   A 105 ? 0.2938 0.3126 0.3077 0.0371  0.0050  -0.0364 105 ASP   A CB  
2311 C CG  A ASP   A 105 ? 0.3786 0.5029 0.3815 -0.0070 0.0293  -0.0767 105 ASP   A CG  
2312 C CG  B ASP   A 105 ? 0.2973 0.3165 0.3505 0.0458  0.0137  -0.0531 105 ASP   A CG  
2313 O OD1 A ASP   A 105 ? 0.3866 0.5087 0.3886 -0.0084 0.0280  -0.0885 105 ASP   A OD1 
2314 O OD1 B ASP   A 105 ? 0.2986 0.3162 0.3570 0.0464  0.0109  -0.0615 105 ASP   A OD1 
2315 O OD2 A ASP   A 105 ? 0.3889 0.5086 0.4209 0.0001  0.0323  -0.0750 105 ASP   A OD2 
2316 O OD2 B ASP   A 105 ? 0.2966 0.3161 0.3694 0.0528  0.0253  -0.0580 105 ASP   A OD2 
2325 N N   A ILE   A 106 ? 0.2784 0.4257 0.2394 -0.0481 -0.0022 -0.0665 106 ILE   A N   
2326 N N   B ILE   A 106 ? 0.2971 0.3003 0.2550 0.0043  -0.0113 -0.0224 106 ILE   A N   
2327 C CA  A ILE   A 106 ? 0.2545 0.4008 0.2466 -0.0668 -0.0229 -0.0756 106 ILE   A CA  
2328 C CA  B ILE   A 106 ? 0.3010 0.3050 0.2721 -0.0131 -0.0153 -0.0270 106 ILE   A CA  
2329 C C   A ILE   A 106 ? 0.2386 0.3719 0.2409 -0.0899 -0.0155 -0.0940 106 ILE   A C   
2330 C C   B ILE   A 106 ? 0.3083 0.3084 0.2764 -0.0224 -0.0043 -0.0230 106 ILE   A C   
2331 O O   A ILE   A 106 ? 0.2155 0.3605 0.2499 -0.0920 0.0108  -0.0913 106 ILE   A O   
2332 O O   B ILE   A 106 ? 0.3090 0.3097 0.2772 -0.0220 -0.0000 -0.0187 106 ILE   A O   
2333 C CB  A ILE   A 106 ? 0.2615 0.4103 0.2920 -0.0546 -0.0447 -0.0497 106 ILE   A CB  
2334 C CB  B ILE   A 106 ? 0.3011 0.3111 0.2894 -0.0197 -0.0294 -0.0282 106 ILE   A CB  
2335 C CG1 A ILE   A 106 ? 0.2541 0.4126 0.3253 -0.0418 -0.0473 -0.0290 106 ILE   A CG1 
2336 C CG1 B ILE   A 106 ? 0.2973 0.3162 0.3046 -0.0203 -0.0334 -0.0262 106 ILE   A CG1 
2337 C CG2 A ILE   A 106 ? 0.2731 0.4145 0.3048 -0.0506 -0.0520 -0.0490 106 ILE   A CG2 
2338 C CG2 B ILE   A 106 ? 0.3043 0.3127 0.2931 -0.0218 -0.0326 -0.0292 106 ILE   A CG2 
2339 C CD1 A ILE   A 106 ? 0.2564 0.4116 0.3425 -0.0310 -0.0479 -0.0216 106 ILE   A CD1 
2340 C CD1 B ILE   A 106 ? 0.2951 0.3173 0.3141 -0.0202 -0.0341 -0.0295 106 ILE   A CD1 
2363 N N   A GLN   A 107 ? 0.2645 0.3569 0.2646 -0.0903 -0.0055 -0.1083 107 GLN   A N   
2364 N N   B GLN   A 107 ? 0.3148 0.3085 0.2909 -0.0303 0.0058  -0.0244 107 GLN   A N   
2365 C CA  A GLN   A 107 ? 0.2976 0.3423 0.3433 -0.0744 0.0173  -0.1004 107 GLN   A CA  
2366 C CA  B GLN   A 107 ? 0.3223 0.3117 0.3265 -0.0375 0.0156  -0.0260 107 GLN   A CA  
2367 C C   A GLN   A 107 ? 0.2681 0.2892 0.3265 -0.0617 0.0459  -0.0724 107 GLN   A C   
2368 C C   B GLN   A 107 ? 0.2873 0.2789 0.2994 -0.0470 0.0356  -0.0372 107 GLN   A C   
2369 O O   A GLN   A 107 ? 0.2674 0.2797 0.3817 -0.0532 0.0617  -0.0709 107 GLN   A O   
2370 O O   B GLN   A 107 ? 0.2918 0.2775 0.3202 -0.0504 0.0384  -0.0313 107 GLN   A O   
2371 C CB  A GLN   A 107 ? 0.3503 0.3793 0.4417 -0.0756 0.0048  -0.1081 107 GLN   A CB  
2372 C CB  B GLN   A 107 ? 0.3587 0.3445 0.3879 -0.0372 0.0025  -0.0184 107 GLN   A CB  
2373 C CG  A GLN   A 107 ? 0.3994 0.4152 0.5540 -0.0729 -0.0052 -0.1024 107 GLN   A CG  
2374 C CG  B GLN   A 107 ? 0.3893 0.3725 0.4525 -0.0359 -0.0101 -0.0093 107 GLN   A CG  
2375 C CD  A GLN   A 107 ? 0.4396 0.4439 0.6515 -0.0704 -0.0116 -0.0911 107 GLN   A CD  
2376 C CD  B GLN   A 107 ? 0.4131 0.3983 0.5087 -0.0341 -0.0192 0.0000  107 GLN   A CD  
2377 O OE1 A GLN   A 107 ? 0.4542 0.4556 0.6894 -0.0682 -0.0134 -0.0860 107 GLN   A OE1 
2378 O OE1 B GLN   A 107 ? 0.4232 0.4072 0.5287 -0.0335 -0.0228 0.0035  107 GLN   A OE1 
2379 N NE2 A GLN   A 107 ? 0.4530 0.4536 0.6866 -0.0716 -0.0146 -0.0900 107 GLN   A NE2 
2380 N NE2 B GLN   A 107 ? 0.4191 0.4073 0.5303 -0.0332 -0.0231 0.0027  107 GLN   A NE2 
2397 N N   . LEU   A 108 ? 0.2473 0.2486 0.2674 -0.0529 0.0442  -0.0513 108 LEU   A N   
2398 C CA  . LEU   A 108 ? 0.2124 0.2009 0.2192 -0.0206 0.0315  -0.0154 108 LEU   A CA  
2399 C C   . LEU   A 108 ? 0.1857 0.1671 0.2173 -0.0073 0.0166  0.0087  108 LEU   A C   
2400 O O   . LEU   A 108 ? 0.1823 0.1661 0.2301 0.0022  0.0260  0.0107  108 LEU   A O   
2401 C CB  . LEU   A 108 ? 0.2112 0.2121 0.2130 -0.0303 0.0302  -0.0138 108 LEU   A CB  
2402 C CG  . LEU   A 108 ? 0.2234 0.2345 0.2364 -0.0240 0.0376  -0.0146 108 LEU   A CG  
2403 C CD1 . LEU   A 108 ? 0.2356 0.2425 0.2535 -0.0309 0.0469  -0.0162 108 LEU   A CD1 
2404 C CD2 . LEU   A 108 ? 0.2241 0.2581 0.2784 -0.0146 0.0368  -0.0037 108 LEU   A CD2 
2417 N N   . LEU   A 109 ? 0.1694 0.1611 0.2097 0.0032  0.0178  0.0157  109 LEU   A N   
2418 C CA  . LEU   A 109 ? 0.1674 0.1564 0.2041 0.0078  0.0063  0.0159  109 LEU   A CA  
2419 C C   . LEU   A 109 ? 0.1517 0.1494 0.2105 -0.0047 0.0090  0.0106  109 LEU   A C   
2420 O O   . LEU   A 109 ? 0.1564 0.1435 0.2244 -0.0023 0.0029  0.0093  109 LEU   A O   
2421 C CB  . LEU   A 109 ? 0.1709 0.1634 0.2248 0.0051  0.0008  0.0287  109 LEU   A CB  
2422 C CG  . LEU   A 109 ? 0.1640 0.1714 0.2320 0.0077  0.0068  0.0356  109 LEU   A CG  
2423 C CD1 . LEU   A 109 ? 0.1667 0.1619 0.2359 -0.0019 0.0176  0.0192  109 LEU   A CD1 
2424 C CD2 . LEU   A 109 ? 0.1594 0.1958 0.2526 0.0048  0.0094  0.0419  109 LEU   A CD2 
2436 N N   . LYS   A 110 ? 0.1511 0.1482 0.2052 -0.0064 -0.0080 0.0043  110 LYS   A N   
2437 C CA  . LYS   A 110 ? 0.1523 0.1395 0.2152 -0.0113 -0.0075 0.0126  110 LYS   A CA  
2438 C C   . LYS   A 110 ? 0.1509 0.1353 0.1989 -0.0131 -0.0055 -0.0013 110 LYS   A C   
2439 O O   . LYS   A 110 ? 0.1471 0.1412 0.2088 -0.0043 0.0039  -0.0028 110 LYS   A O   
2440 C CB  . LYS   A 110 ? 0.1589 0.1455 0.2403 -0.0071 -0.0083 -0.0001 110 LYS   A CB  
2441 C CG  . LYS   A 110 ? 0.1632 0.1435 0.2504 -0.0035 -0.0122 -0.0013 110 LYS   A CG  
2442 C CD  . LYS   A 110 ? 0.1618 0.1543 0.2616 -0.0086 -0.0068 -0.0042 110 LYS   A CD  
2443 C CE  . LYS   A 110 ? 0.1694 0.1608 0.2822 -0.0066 0.0079  -0.0076 110 LYS   A CE  
2444 N NZ  . LYS   A 110 ? 0.1675 0.1575 0.2909 -0.0139 0.0119  0.0010  110 LYS   A NZ  
2458 N N   . SER   A 111 ? 0.1517 0.1384 0.2000 -0.0052 -0.0054 0.0027  111 SER   A N   
2459 C CA  . SER   A 111 ? 0.1435 0.1494 0.2027 -0.0034 0.0033  -0.0006 111 SER   A CA  
2460 C C   . SER   A 111 ? 0.1379 0.1397 0.1938 -0.0044 0.0091  0.0119  111 SER   A C   
2461 O O   . SER   A 111 ? 0.1537 0.1331 0.2117 -0.0061 0.0106  0.0094  111 SER   A O   
2462 C CB  . SER   A 111 ? 0.1629 0.1708 0.2073 -0.0045 0.0149  -0.0103 111 SER   A CB  
2463 O OG  . SER   A 111 ? 0.2064 0.1933 0.2199 0.0055  0.0194  -0.0168 111 SER   A OG  
2469 N N   . ALA   A 112 ? 0.1425 0.1321 0.2001 -0.0012 0.0129  0.0099  112 ALA   A N   
2470 C CA  . ALA   A 112 ? 0.1453 0.1274 0.1960 -0.0042 0.0188  0.0008  112 ALA   A CA  
2471 C C   . ALA   A 112 ? 0.1374 0.1235 0.2008 -0.0026 0.0060  0.0056  112 ALA   A C   
2472 O O   . ALA   A 112 ? 0.1424 0.1264 0.2108 -0.0140 0.0108  0.0149  112 ALA   A O   
2473 C CB  . ALA   A 112 ? 0.1567 0.1358 0.1910 -0.0047 0.0135  0.0124  112 ALA   A CB  
2479 N N   . TYR   A 113 ? 0.1305 0.1310 0.2114 -0.0055 0.0095  0.0155  113 TYR   A N   
2480 C CA  . TYR   A 113 ? 0.1339 0.1307 0.2012 -0.0071 0.0146  0.0212  113 TYR   A CA  
2481 C C   . TYR   A 113 ? 0.1277 0.1319 0.1900 -0.0104 0.0081  0.0064  113 TYR   A C   
2482 O O   . TYR   A 113 ? 0.1393 0.1351 0.2002 -0.0079 0.0161  0.0048  113 TYR   A O   
2483 C CB  . TYR   A 113 ? 0.1355 0.1357 0.1947 -0.0076 0.0039  0.0248  113 TYR   A CB  
2484 C CG  . TYR   A 113 ? 0.1355 0.1441 0.1973 -0.0137 0.0135  0.0244  113 TYR   A CG  
2485 C CD1 . TYR   A 113 ? 0.1390 0.1598 0.1993 -0.0015 0.0144  0.0187  113 TYR   A CD1 
2486 C CD2 . TYR   A 113 ? 0.1412 0.1543 0.1967 -0.0153 0.0085  0.0244  113 TYR   A CD2 
2487 C CE1 . TYR   A 113 ? 0.1465 0.1719 0.2000 -0.0020 0.0090  0.0273  113 TYR   A CE1 
2488 C CE2 . TYR   A 113 ? 0.1407 0.1642 0.2000 -0.0087 0.0051  0.0295  113 TYR   A CE2 
2489 C CZ  . TYR   A 113 ? 0.1419 0.1637 0.1992 0.0036  0.0115  0.0329  113 TYR   A CZ  
2490 O OH  . TYR   A 113 ? 0.1408 0.1746 0.2344 0.0108  0.0052  0.0281  113 TYR   A OH  
2500 N N   . GLU   A 114 ? 0.1323 0.1272 0.2026 -0.0088 0.0131  0.0184  114 GLU   A N   
2501 C CA  . GLU   A 114 ? 0.1392 0.1222 0.2224 0.0014  0.0109  0.0214  114 GLU   A CA  
2502 C C   . GLU   A 114 ? 0.1291 0.1281 0.2129 -0.0037 0.0102  0.0147  114 GLU   A C   
2503 O O   . GLU   A 114 ? 0.1485 0.1309 0.2052 -0.0015 0.0025  0.0170  114 GLU   A O   
2504 C CB  . GLU   A 114 ? 0.1338 0.1269 0.2161 -0.0090 0.0101  0.0198  114 GLU   A CB  
2505 C CG  . GLU   A 114 ? 0.1416 0.1358 0.2363 0.0013  0.0146  0.0120  114 GLU   A CG  
2506 C CD  . GLU   A 114 ? 0.1552 0.1364 0.2399 -0.0049 0.0008  0.0094  114 GLU   A CD  
2507 O OE1 . GLU   A 114 ? 0.1565 0.1330 0.2386 -0.0141 0.0133  -0.0027 114 GLU   A OE1 
2508 O OE2 . GLU   A 114 ? 0.1747 0.1423 0.2556 -0.0096 0.0044  -0.0035 114 GLU   A OE2 
2515 N N   . ASN   A 115 ? 0.1386 0.1314 0.2027 -0.0081 0.0095  0.0146  115 ASN   A N   
2516 C CA  . ASN   A 115 ? 0.1379 0.1401 0.2098 -0.0083 0.0097  0.0126  115 ASN   A CA  
2517 C C   . ASN   A 115 ? 0.1394 0.1307 0.1970 -0.0098 0.0080  0.0170  115 ASN   A C   
2518 O O   . ASN   A 115 ? 0.1449 0.1470 0.1962 -0.0096 0.0098  0.0208  115 ASN   A O   
2519 C CB  . ASN   A 115 ? 0.1473 0.1401 0.2017 -0.0148 0.0162  0.0231  115 ASN   A CB  
2520 C CG  . ASN   A 115 ? 0.1441 0.1555 0.2129 -0.0173 0.0156  0.0141  115 ASN   A CG  
2521 O OD1 . ASN   A 115 ? 0.1472 0.2511 0.2319 -0.0162 0.0265  0.0298  115 ASN   A OD1 
2522 N ND2 . ASN   A 115 ? 0.1496 0.1368 0.2161 -0.0154 0.0246  0.0228  115 ASN   A ND2 
2529 N N   . PHE   A 116 ? 0.1352 0.1380 0.2056 -0.0020 0.0167  0.0277  116 PHE   A N   
2530 C CA  . PHE   A 116 ? 0.1341 0.1427 0.1977 0.0009  0.0177  0.0199  116 PHE   A CA  
2531 C C   . PHE   A 116 ? 0.1344 0.1454 0.2033 -0.0071 0.0119  0.0321  116 PHE   A C   
2532 O O   . PHE   A 116 ? 0.1426 0.1547 0.2102 0.0004  0.0122  0.0353  116 PHE   A O   
2533 C CB  . PHE   A 116 ? 0.1355 0.1317 0.2131 -0.0042 0.0218  0.0216  116 PHE   A CB  
2534 C CG  . PHE   A 116 ? 0.1379 0.1330 0.1991 -0.0052 0.0150  0.0189  116 PHE   A CG  
2535 C CD1 . PHE   A 116 ? 0.1416 0.1352 0.2035 -0.0061 0.0133  0.0200  116 PHE   A CD1 
2536 C CD2 . PHE   A 116 ? 0.1384 0.1401 0.2135 -0.0062 0.0174  0.0244  116 PHE   A CD2 
2537 C CE1 . PHE   A 116 ? 0.1427 0.1317 0.2160 -0.0170 0.0090  0.0112  116 PHE   A CE1 
2538 C CE2 . PHE   A 116 ? 0.1380 0.1379 0.2208 -0.0046 0.0157  0.0138  116 PHE   A CE2 
2539 C CZ  . PHE   A 116 ? 0.1440 0.1245 0.2127 -0.0044 0.0092  0.0132  116 PHE   A CZ  
2549 N N   . ASN   A 117 ? 0.1377 0.1367 0.2148 -0.0072 0.0169  0.0284  117 ASN   A N   
2550 C CA  . ASN   A 117 ? 0.1405 0.1367 0.2280 -0.0043 0.0167  0.0271  117 ASN   A CA  
2551 C C   . ASN   A 117 ? 0.1406 0.1442 0.2316 -0.0061 0.0159  0.0281  117 ASN   A C   
2552 O O   . ASN   A 117 ? 0.1524 0.1520 0.2469 -0.0067 -0.0020 0.0422  117 ASN   A O   
2553 C CB  . ASN   A 117 ? 0.1371 0.1403 0.2295 -0.0024 0.0122  0.0343  117 ASN   A CB  
2554 C CG  . ASN   A 117 ? 0.1367 0.1438 0.2266 -0.0104 0.0159  0.0339  117 ASN   A CG  
2555 O OD1 . ASN   A 117 ? 0.1413 0.1644 0.2412 -0.0168 0.0113  0.0251  117 ASN   A OD1 
2556 N ND2 . ASN   A 117 ? 0.1330 0.1443 0.2276 -0.0033 0.0086  0.0320  117 ASN   A ND2 
2563 N N   . GLN   A 118 ? 0.1355 0.1439 0.2270 -0.0084 0.0042  0.0331  118 GLN   A N   
2564 C CA  . GLN   A 118 ? 0.1439 0.1572 0.2354 -0.0123 -0.0001 0.0237  118 GLN   A CA  
2565 C C   . GLN   A 118 ? 0.1461 0.1703 0.2240 -0.0155 -0.0011 0.0348  118 GLN   A C   
2566 O O   . GLN   A 118 ? 0.1443 0.1953 0.2458 -0.0056 -0.0062 0.0093  118 GLN   A O   
2567 C CB  . GLN   A 118 ? 0.1376 0.1606 0.2517 -0.0051 0.0109  0.0275  118 GLN   A CB  
2568 C CG  . GLN   A 118 ? 0.1406 0.1635 0.2400 -0.0019 0.0082  0.0327  118 GLN   A CG  
2569 C CD  . GLN   A 118 ? 0.1387 0.1651 0.2524 -0.0010 0.0090  0.0316  118 GLN   A CD  
2570 O OE1 . GLN   A 118 ? 0.1413 0.1741 0.2658 0.0089  0.0031  0.0257  118 GLN   A OE1 
2571 N NE2 . GLN   A 118 ? 0.1539 0.1667 0.2458 0.0017  0.0050  0.0389  118 GLN   A NE2 
2580 N N   . HIS   A 119 ? 0.1468 0.1630 0.2188 -0.0088 0.0024  0.0399  119 HIS   A N   
2581 C CA  . HIS   A 119 ? 0.1545 0.1730 0.2052 -0.0079 0.0025  0.0430  119 HIS   A CA  
2582 C C   . HIS   A 119 ? 0.1647 0.1817 0.1967 -0.0089 0.0064  0.0463  119 HIS   A C   
2583 O O   . HIS   A 119 ? 0.1694 0.1875 0.2142 -0.0245 -0.0054 0.0458  119 HIS   A O   
2584 C CB  . HIS   A 119 ? 0.1581 0.1695 0.2185 -0.0079 0.0160  0.0407  119 HIS   A CB  
2585 C CG  . HIS   A 119 ? 0.1622 0.1744 0.2585 0.0001  0.0114  0.0493  119 HIS   A CG  
2586 N ND1 . HIS   A 119 ? 0.1762 0.1903 0.3185 -0.0107 0.0102  0.0322  119 HIS   A ND1 
2587 C CD2 . HIS   A 119 ? 0.1785 0.1859 0.2767 0.0128  0.0381  0.0634  119 HIS   A CD2 
2588 C CE1 . HIS   A 119 ? 0.1741 0.1860 0.3215 -0.0118 0.0313  0.0547  119 HIS   A CE1 
2589 N NE2 . HIS   A 119 ? 0.1892 0.1828 0.3109 0.0066  0.0508  0.0718  119 HIS   A NE2 
2597 N N   . GLU   A 120 ? 0.1705 0.2099 0.1998 -0.0070 -0.0037 0.0714  120 GLU   A N   
2598 C CA  . GLU   A 120 ? 0.1981 0.2417 0.2370 -0.0052 -0.0037 0.1134  120 GLU   A CA  
2599 C C   . GLU   A 120 ? 0.1761 0.2257 0.2233 -0.0134 0.0058  0.1006  120 GLU   A C   
2600 O O   . GLU   A 120 ? 0.1775 0.2201 0.2400 -0.0177 -0.0009 0.0979  120 GLU   A O   
2601 C CB  . GLU   A 120 ? 0.2719 0.3054 0.3092 0.0027  0.0008  0.1585  120 GLU   A CB  
2602 C CG  . GLU   A 120 ? 0.3621 0.3788 0.4296 0.0137  0.0037  0.1607  120 GLU   A CG  
2603 C CD  . GLU   A 120 ? 0.4342 0.4398 0.5475 0.0224  0.0127  0.1485  120 GLU   A CD  
2604 O OE1 . GLU   A 120 ? 0.4567 0.4654 0.5746 0.0248  0.0186  0.1462  120 GLU   A OE1 
2605 O OE2 . GLU   A 120 ? 0.4890 0.4890 0.6011 0.0239  0.0147  0.1411  120 GLU   A OE2 
2612 N N   . VAL   A 121 ? 0.1755 0.2207 0.1982 -0.0122 0.0143  0.0785  121 VAL   A N   
2613 C CA  . VAL   A 121 ? 0.1881 0.2271 0.1848 -0.0124 0.0236  0.0757  121 VAL   A CA  
2614 C C   . VAL   A 121 ? 0.1795 0.2065 0.1644 -0.0229 0.0134  0.0601  121 VAL   A C   
2615 O O   . VAL   A 121 ? 0.1773 0.2079 0.1860 -0.0314 -0.0066 0.0523  121 VAL   A O   
2616 C CB  . VAL   A 121 ? 0.2257 0.2629 0.2221 -0.0024 0.0371  0.0789  121 VAL   A CB  
2617 C CG1 . VAL   A 121 ? 0.2270 0.2818 0.2131 0.0041  0.0454  0.0776  121 VAL   A CG1 
2618 C CG2 . VAL   A 121 ? 0.2518 0.2797 0.2684 -0.0117 0.0329  0.0673  121 VAL   A CG2 
2628 N N   . LEU   A 122 ? 0.1644 0.1821 0.1740 -0.0184 0.0125  0.0483  122 LEU   A N   
2629 C CA  . LEU   A 122 ? 0.1698 0.1678 0.1738 -0.0195 0.0241  0.0448  122 LEU   A CA  
2630 C C   . LEU   A 122 ? 0.1617 0.1685 0.1888 -0.0216 0.0095  0.0396  122 LEU   A C   
2631 O O   . LEU   A 122 ? 0.1571 0.1772 0.2235 -0.0272 0.0111  0.0446  122 LEU   A O   
2632 C CB  . LEU   A 122 ? 0.1860 0.1661 0.2143 -0.0140 0.0108  0.0545  122 LEU   A CB  
2633 C CG  . LEU   A 122 ? 0.1813 0.1706 0.2127 -0.0139 0.0196  0.0347  122 LEU   A CG  
2634 C CD1 . LEU   A 122 ? 0.1978 0.1735 0.2271 -0.0133 0.0253  0.0384  122 LEU   A CD1 
2635 C CD2 . LEU   A 122 ? 0.1783 0.1650 0.2004 -0.0135 0.0295  0.0276  122 LEU   A CD2 
2647 N N   A LEU   A 123 ? 0.1609 0.1611 0.1770 -0.0205 0.0053  0.0324  123 LEU   A N   
2648 N N   B LEU   A 123 ? 0.1640 0.1664 0.1768 -0.0183 0.0056  0.0320  123 LEU   A N   
2649 C CA  A LEU   A 123 ? 0.1601 0.1599 0.1671 -0.0214 0.0102  0.0379  123 LEU   A CA  
2650 C CA  B LEU   A 123 ? 0.1643 0.1674 0.1724 -0.0173 0.0035  0.0290  123 LEU   A CA  
2651 C C   A LEU   A 123 ? 0.1482 0.1582 0.1654 -0.0140 0.0012  0.0401  123 LEU   A C   
2652 C C   B LEU   A 123 ? 0.1554 0.1589 0.1614 -0.0164 0.0105  0.0313  123 LEU   A C   
2653 O O   A LEU   A 123 ? 0.1423 0.1583 0.1761 -0.0210 -0.0023 0.0350  123 LEU   A O   
2654 O O   B LEU   A 123 ? 0.1530 0.1523 0.1581 -0.0157 0.0174  0.0230  123 LEU   A O   
2655 C CB  A LEU   A 123 ? 0.1688 0.1724 0.1690 -0.0266 0.0283  0.0428  123 LEU   A CB  
2656 C CB  B LEU   A 123 ? 0.1725 0.1796 0.1851 -0.0165 -0.0014 0.0250  123 LEU   A CB  
2657 C CG  A LEU   A 123 ? 0.1758 0.1891 0.1864 -0.0193 0.0298  0.0283  123 LEU   A CG  
2658 C CG  B LEU   A 123 ? 0.1778 0.1907 0.1875 -0.0127 -0.0023 0.0238  123 LEU   A CG  
2659 C CD1 A LEU   A 123 ? 0.1801 0.2002 0.2054 -0.0092 0.0292  0.0203  123 LEU   A CD1 
2660 C CD1 B LEU   A 123 ? 0.1795 0.1954 0.1949 -0.0081 -0.0008 0.0228  123 LEU   A CD1 
2661 C CD2 A LEU   A 123 ? 0.1869 0.1928 0.1920 -0.0176 0.0262  0.0282  123 LEU   A CD2 
2662 C CD2 B LEU   A 123 ? 0.1834 0.1972 0.1954 -0.0105 -0.0059 0.0186  123 LEU   A CD2 
2685 N N   . ALA   A 124 ? 0.1515 0.1557 0.1619 -0.0156 0.0091  0.0318  124 ALA   A N   
2686 C CA  . ALA   A 124 ? 0.1430 0.1497 0.1693 -0.0110 0.0036  0.0298  124 ALA   A CA  
2687 C C   . ALA   A 124 ? 0.1407 0.1518 0.1719 -0.0130 0.0140  0.0331  124 ALA   A C   
2688 O O   . ALA   A 124 ? 0.1386 0.1628 0.1891 -0.0116 0.0151  0.0388  124 ALA   A O   
2689 C CB  . ALA   A 124 ? 0.1471 0.1454 0.1990 -0.0095 0.0041  0.0324  124 ALA   A CB  
2696 N N   A PRO   A 125 ? 0.1334 0.1469 0.1736 -0.0089 0.0086  0.0441  125 PRO   A N   
2697 N N   B PRO   A 125 ? 0.1561 0.1638 0.1665 -0.0089 0.0100  0.0313  125 PRO   A N   
2698 C CA  A PRO   A 125 ? 0.1413 0.1437 0.1836 -0.0040 0.0067  0.0334  125 PRO   A CA  
2699 C CA  B PRO   A 125 ? 0.1688 0.1735 0.1691 -0.0043 0.0078  0.0233  125 PRO   A CA  
2700 C C   A PRO   A 125 ? 0.1293 0.1445 0.1820 -0.0073 0.0073  0.0332  125 PRO   A C   
2701 C C   B PRO   A 125 ? 0.1729 0.1819 0.1742 -0.0023 0.0076  0.0188  125 PRO   A C   
2702 O O   A PRO   A 125 ? 0.1299 0.1414 0.2003 -0.0006 0.0048  0.0339  125 PRO   A O   
2703 O O   B PRO   A 125 ? 0.1731 0.1825 0.1858 0.0004  0.0091  0.0173  125 PRO   A O   
2704 C CB  A PRO   A 125 ? 0.1548 0.1423 0.1854 -0.0102 0.0168  0.0245  125 PRO   A CB  
2705 C CB  B PRO   A 125 ? 0.1749 0.1724 0.1686 -0.0042 0.0133  0.0230  125 PRO   A CB  
2706 C CG  A PRO   A 125 ? 0.1483 0.1409 0.1880 -0.0123 0.0127  0.0283  125 PRO   A CG  
2707 C CG  B PRO   A 125 ? 0.1754 0.1697 0.1699 -0.0075 0.0102  0.0281  125 PRO   A CG  
2708 C CD  A PRO   A 125 ? 0.1403 0.1505 0.1827 -0.0176 0.0085  0.0442  125 PRO   A CD  
2709 C CD  B PRO   A 125 ? 0.1659 0.1695 0.1666 -0.0107 0.0109  0.0315  125 PRO   A CD  
2724 N N   A LEU   A 126 ? 0.1275 0.1542 0.1821 -0.0019 0.0121  0.0345  126 LEU   A N   
2725 N N   B LEU   A 126 ? 0.1826 0.1895 0.1811 -0.0010 -0.0008 0.0184  126 LEU   A N   
2726 C CA  A LEU   A 126 ? 0.1283 0.1589 0.1868 -0.0047 0.0039  0.0325  126 LEU   A CA  
2727 C CA  B LEU   A 126 ? 0.1843 0.1952 0.1965 -0.0018 -0.0035 0.0233  126 LEU   A CA  
2728 C C   A LEU   A 126 ? 0.1338 0.1533 0.1948 0.0057  0.0017  0.0224  126 LEU   A C   
2729 C C   B LEU   A 126 ? 0.1769 0.1848 0.1842 0.0058  -0.0018 0.0176  126 LEU   A C   
2730 O O   A LEU   A 126 ? 0.1420 0.1471 0.2271 0.0152  0.0175  0.0424  126 LEU   A O   
2731 O O   B LEU   A 126 ? 0.1837 0.1828 0.1924 0.0061  -0.0027 0.0231  126 LEU   A O   
2732 C CB  A LEU   A 126 ? 0.1304 0.1716 0.1794 -0.0097 0.0053  0.0241  126 LEU   A CB  
2733 C CB  B LEU   A 126 ? 0.1944 0.2158 0.2426 -0.0055 -0.0138 0.0262  126 LEU   A CB  
2734 C CG  A LEU   A 126 ? 0.1363 0.2047 0.1986 -0.0147 0.0132  0.0278  126 LEU   A CG  
2735 C CG  B LEU   A 126 ? 0.2015 0.2285 0.2839 -0.0076 -0.0218 0.0243  126 LEU   A CG  
2736 C CD1 A LEU   A 126 ? 0.1417 0.2206 0.2212 -0.0132 0.0005  0.0247  126 LEU   A CD1 
2737 C CD1 B LEU   A 126 ? 0.2009 0.2305 0.2943 -0.0079 -0.0252 0.0224  126 LEU   A CD1 
2738 C CD2 A LEU   A 126 ? 0.1532 0.1986 0.1991 -0.0288 0.0131  0.0447  126 LEU   A CD2 
2739 C CD2 B LEU   A 126 ? 0.2012 0.2311 0.2930 -0.0089 -0.0275 0.0268  126 LEU   A CD2 
2762 N N   A LEU   A 127 ? 0.1377 0.1515 0.1844 0.0077  0.0102  0.0274  127 LEU   A N   
2763 N N   B LEU   A 127 ? 0.1690 0.1799 0.1712 0.0098  -0.0010 0.0209  127 LEU   A N   
2764 C CA  A LEU   A 127 ? 0.1367 0.1551 0.1681 0.0025  -0.0021 0.0211  127 LEU   A CA  
2765 C CA  B LEU   A 127 ? 0.1622 0.1793 0.1690 0.0117  -0.0069 0.0212  127 LEU   A CA  
2766 C C   A LEU   A 127 ? 0.1403 0.1451 0.1706 -0.0021 0.0022  0.0192  127 LEU   A C   
2767 C C   B LEU   A 127 ? 0.1627 0.1777 0.1781 0.0060  -0.0123 0.0151  127 LEU   A C   
2768 O O   A LEU   A 127 ? 0.1459 0.1453 0.1838 -0.0150 0.0056  0.0235  127 LEU   A O   
2769 O O   B LEU   A 127 ? 0.1668 0.1787 0.1751 0.0000  -0.0117 0.0209  127 LEU   A O   
2770 C CB  A LEU   A 127 ? 0.1528 0.1657 0.1814 0.0106  0.0076  0.0110  127 LEU   A CB  
2771 C CB  B LEU   A 127 ? 0.1604 0.1884 0.1726 0.0187  -0.0062 0.0158  127 LEU   A CB  
2772 C CG  A LEU   A 127 ? 0.1561 0.1633 0.1860 0.0151  -0.0020 0.0254  127 LEU   A CG  
2773 C CG  B LEU   A 127 ? 0.1546 0.1980 0.1679 0.0207  -0.0102 0.0235  127 LEU   A CG  
2774 C CD1 A LEU   A 127 ? 0.1579 0.1532 0.2028 0.0055  0.0010  0.0226  127 LEU   A CD1 
2775 C CD1 B LEU   A 127 ? 0.1568 0.2031 0.1805 0.0227  -0.0019 0.0262  127 LEU   A CD1 
2776 C CD2 A LEU   A 127 ? 0.1688 0.1662 0.2018 0.0218  -0.0099 0.0285  127 LEU   A CD2 
2777 C CD2 B LEU   A 127 ? 0.1562 0.2037 0.1623 0.0217  -0.0244 0.0182  127 LEU   A CD2 
2800 N N   A SER   A 128 ? 0.1492 0.1442 0.1743 -0.0054 -0.0012 0.0194  128 SER   A N   
2801 N N   B SER   A 128 ? 0.1622 0.1778 0.1835 -0.0013 -0.0119 0.0109  128 SER   A N   
2802 C CA  A SER   A 128 ? 0.1611 0.1463 0.1556 -0.0021 -0.0063 0.0185  128 SER   A CA  
2803 C CA  B SER   A 128 ? 0.1613 0.1769 0.1759 -0.0030 -0.0092 0.0075  128 SER   A CA  
2804 C C   A SER   A 128 ? 0.1676 0.1508 0.1461 -0.0009 -0.0113 0.0205  128 SER   A C   
2805 C C   B SER   A 128 ? 0.1682 0.1805 0.1742 -0.0020 -0.0211 0.0068  128 SER   A C   
2806 O O   A SER   A 128 ? 0.1817 0.1625 0.1508 0.0014  -0.0050 0.0103  128 SER   A O   
2807 O O   B SER   A 128 ? 0.1667 0.1764 0.1735 -0.0007 -0.0181 0.0013  128 SER   A O   
2808 C CB  A SER   A 128 ? 0.1655 0.1507 0.1656 -0.0048 -0.0070 0.0253  128 SER   A CB  
2809 C CB  B SER   A 128 ? 0.1548 0.1745 0.1782 -0.0061 -0.0045 0.0117  128 SER   A CB  
2810 O OG  A SER   A 128 ? 0.1621 0.1587 0.1774 -0.0036 -0.0074 0.0132  128 SER   A OG  
2811 O OG  B SER   A 128 ? 0.1438 0.1710 0.1785 -0.0053 0.0053  0.0219  128 SER   A OG  
2822 N N   A ALA   A 129 ? 0.1597 0.1545 0.1660 -0.0011 -0.0164 0.0257  129 ALA   A N   
2823 N N   B ALA   A 129 ? 0.1779 0.1913 0.1810 -0.0010 -0.0326 0.0039  129 ALA   A N   
2824 C CA  A ALA   A 129 ? 0.1529 0.1521 0.1953 0.0012  -0.0131 0.0225  129 ALA   A CA  
2825 C CA  B ALA   A 129 ? 0.1927 0.2016 0.1981 -0.0020 -0.0306 0.0018  129 ALA   A CA  
2826 C C   A ALA   A 129 ? 0.1510 0.1406 0.2056 -0.0085 -0.0187 0.0035  129 ALA   A C   
2827 C C   B ALA   A 129 ? 0.2114 0.2127 0.2051 -0.0052 -0.0316 0.0022  129 ALA   A C   
2828 O O   A ALA   A 129 ? 0.1526 0.1472 0.2000 -0.0135 -0.0174 0.0192  129 ALA   A O   
2829 O O   B ALA   A 129 ? 0.2144 0.2162 0.1970 -0.0045 -0.0383 0.0100  129 ALA   A O   
2830 C CB  A ALA   A 129 ? 0.1554 0.1662 0.2116 0.0138  0.0022  0.0379  129 ALA   A CB  
2831 C CB  B ALA   A 129 ? 0.1945 0.2085 0.2170 -0.0012 -0.0191 0.0083  129 ALA   A CB  
2842 N N   A GLY   A 130 ? 0.1619 0.1338 0.2485 -0.0049 -0.0144 -0.0039 130 GLY   A N   
2843 N N   B GLY   A 130 ? 0.2240 0.2156 0.2105 -0.0110 -0.0260 0.0022  130 GLY   A N   
2844 C CA  A GLY   A 130 ? 0.1754 0.1461 0.2730 -0.0057 -0.0227 0.0041  130 GLY   A CA  
2845 C CA  B GLY   A 130 ? 0.2343 0.2210 0.2093 -0.0151 -0.0227 0.0040  130 GLY   A CA  
2846 C C   A GLY   A 130 ? 0.1730 0.1418 0.2695 0.0050  -0.0472 0.0060  130 GLY   A C   
2847 C C   B GLY   A 130 ? 0.2427 0.2277 0.2108 -0.0168 -0.0195 0.0092  130 GLY   A C   
2848 O O   A GLY   A 130 ? 0.1828 0.1463 0.2897 0.0137  -0.0655 -0.0019 130 GLY   A O   
2849 O O   B GLY   A 130 ? 0.2440 0.2279 0.2070 -0.0213 -0.0274 0.0103  130 GLY   A O   
2856 N N   A ILE   A 131 ? 0.1779 0.1428 0.2409 -0.0101 -0.0439 0.0145  131 ILE   A N   
2857 N N   B ILE   A 131 ? 0.2501 0.2315 0.2204 -0.0130 -0.0135 0.0114  131 ILE   A N   
2858 C CA  A ILE   A 131 ? 0.1962 0.1390 0.2138 -0.0109 -0.0554 0.0131  131 ILE   A CA  
2859 C CA  B ILE   A 131 ? 0.2533 0.2339 0.2232 -0.0111 -0.0173 0.0089  131 ILE   A CA  
2860 C C   A ILE   A 131 ? 0.1904 0.1448 0.2010 -0.0071 -0.0406 0.0246  131 ILE   A C   
2861 C C   B ILE   A 131 ? 0.2487 0.2289 0.2168 -0.0090 -0.0170 0.0231  131 ILE   A C   
2862 O O   A ILE   A 131 ? 0.2028 0.1502 0.2083 -0.0032 -0.0358 0.0252  131 ILE   A O   
2863 O O   B ILE   A 131 ? 0.2500 0.2249 0.2191 -0.0075 -0.0184 0.0281  131 ILE   A O   
2864 C CB  A ILE   A 131 ? 0.2213 0.1590 0.2081 -0.0255 -0.0531 0.0034  131 ILE   A CB  
2865 C CB  B ILE   A 131 ? 0.2600 0.2416 0.2374 -0.0084 -0.0228 -0.0046 131 ILE   A CB  
2866 C CG1 A ILE   A 131 ? 0.2237 0.1927 0.2140 -0.0375 -0.0519 0.0033  131 ILE   A CG1 
2867 C CG1 B ILE   A 131 ? 0.2650 0.2505 0.2459 -0.0093 -0.0244 -0.0111 131 ILE   A CG1 
2868 C CG2 A ILE   A 131 ? 0.2403 0.1455 0.2197 -0.0265 -0.0274 0.0005  131 ILE   A CG2 
2869 C CG2 B ILE   A 131 ? 0.2607 0.2405 0.2468 -0.0059 -0.0275 -0.0097 131 ILE   A CG2 
2870 C CD1 A ILE   A 131 ? 0.2288 0.2069 0.2406 -0.0427 -0.0424 -0.0028 131 ILE   A CD1 
2871 C CD1 B ILE   A 131 ? 0.2676 0.2551 0.2570 -0.0081 -0.0248 -0.0134 131 ILE   A CD1 
2894 N N   A PHE   A 132 ? 0.1739 0.1467 0.1996 0.0012  -0.0433 0.0236  132 PHE   A N   
2895 N N   B PHE   A 132 ? 0.2419 0.2279 0.2132 -0.0092 -0.0134 0.0292  132 PHE   A N   
2896 C CA  A PHE   A 132 ? 0.1849 0.1525 0.2031 -0.0074 -0.0300 0.0156  132 PHE   A CA  
2897 C CA  B PHE   A 132 ? 0.2367 0.2273 0.2073 -0.0106 -0.0138 0.0280  132 PHE   A CA  
2898 C C   A PHE   A 132 ? 0.2010 0.1627 0.2038 -0.0174 -0.0333 0.0178  132 PHE   A C   
2899 C C   B PHE   A 132 ? 0.2399 0.2264 0.2109 -0.0157 -0.0166 0.0457  132 PHE   A C   
2900 O O   A PHE   A 132 ? 0.2101 0.1689 0.2009 -0.0208 -0.0438 0.0243  132 PHE   A O   
2901 O O   B PHE   A 132 ? 0.2464 0.2316 0.2193 -0.0208 -0.0102 0.0603  132 PHE   A O   
2902 C CB  A PHE   A 132 ? 0.1737 0.1517 0.1679 -0.0066 -0.0246 0.0243  132 PHE   A CB  
2903 C CB  B PHE   A 132 ? 0.2280 0.2251 0.1919 -0.0075 -0.0114 0.0122  132 PHE   A CB  
2904 C CG  A PHE   A 132 ? 0.1707 0.1497 0.1670 0.0035  -0.0223 0.0232  132 PHE   A CG  
2905 C CG  B PHE   A 132 ? 0.2191 0.2231 0.1871 -0.0048 -0.0031 -0.0027 132 PHE   A CG  
2906 C CD1 A PHE   A 132 ? 0.1683 0.1636 0.1875 0.0085  -0.0188 0.0152  132 PHE   A CD1 
2907 C CD1 B PHE   A 132 ? 0.2170 0.2259 0.1885 -0.0056 0.0019  -0.0135 132 PHE   A CD1 
2908 C CD2 A PHE   A 132 ? 0.1711 0.1613 0.1759 0.0114  -0.0317 0.0112  132 PHE   A CD2 
2909 C CD2 B PHE   A 132 ? 0.2156 0.2216 0.1895 -0.0034 0.0025  -0.0150 132 PHE   A CD2 
2910 C CE1 A PHE   A 132 ? 0.1703 0.1764 0.1964 0.0110  -0.0276 0.0039  132 PHE   A CE1 
2911 C CE1 B PHE   A 132 ? 0.2151 0.2292 0.1925 -0.0040 0.0053  -0.0196 132 PHE   A CE1 
2912 C CE2 A PHE   A 132 ? 0.1646 0.1761 0.1943 0.0167  -0.0328 0.0107  132 PHE   A CE2 
2913 C CE2 B PHE   A 132 ? 0.2144 0.2255 0.1982 -0.0006 0.0069  -0.0191 132 PHE   A CE2 
2914 C CZ  A PHE   A 132 ? 0.1637 0.1750 0.1879 0.0060  -0.0370 0.0077  132 PHE   A CZ  
2915 C CZ  B PHE   A 132 ? 0.2128 0.2258 0.1909 -0.0028 0.0072  -0.0225 132 PHE   A CZ  
2934 N N   A GLY   A 133 ? 0.2049 0.1783 0.1939 -0.0128 -0.0507 0.0219  133 GLY   A N   
2935 N N   B GLY   A 133 ? 0.2334 0.2205 0.2008 -0.0134 -0.0320 0.0437  133 GLY   A N   
2936 C CA  A GLY   A 133 ? 0.2129 0.1863 0.1855 -0.0178 -0.0507 0.0152  133 GLY   A CA  
2937 C CA  B GLY   A 133 ? 0.2279 0.2154 0.1974 -0.0148 -0.0429 0.0341  133 GLY   A CA  
2938 C C   A GLY   A 133 ? 0.2126 0.1960 0.1881 -0.0150 -0.0604 0.0067  133 GLY   A C   
2939 C C   B GLY   A 133 ? 0.2234 0.2140 0.1988 -0.0169 -0.0505 0.0234  133 GLY   A C   
2940 O O   A GLY   A 133 ? 0.2361 0.2143 0.1992 -0.0183 -0.0645 -0.0085 133 GLY   A O   
2941 O O   B GLY   A 133 ? 0.2294 0.2165 0.1999 -0.0169 -0.0534 0.0211  133 GLY   A O   
2948 N N   A ALA   A 134 ? 0.2032 0.1871 0.1851 -0.0125 -0.0521 0.0072  134 ALA   A N   
2949 N N   B ALA   A 134 ? 0.2173 0.2113 0.1967 -0.0193 -0.0501 0.0155  134 ALA   A N   
2950 C CA  A ALA   A 134 ? 0.1954 0.1943 0.1897 -0.0103 -0.0378 0.0154  134 ALA   A CA  
2951 C CA  B ALA   A 134 ? 0.2122 0.2121 0.2035 -0.0163 -0.0517 0.0150  134 ALA   A CA  
2952 C C   A ALA   A 134 ? 0.1956 0.2049 0.1904 -0.0090 -0.0257 0.0257  134 ALA   A C   
2953 C C   B ALA   A 134 ? 0.2098 0.2142 0.2129 -0.0128 -0.0476 0.0194  134 ALA   A C   
2954 O O   A ALA   A 134 ? 0.2132 0.2133 0.2208 0.0006  0.0010  0.0342  134 ALA   A O   
2955 O O   B ALA   A 134 ? 0.2142 0.2172 0.2204 -0.0122 -0.0401 0.0214  134 ALA   A O   
2956 C CB  A ALA   A 134 ? 0.1995 0.1888 0.2050 -0.0094 -0.0355 0.0079  134 ALA   A CB  
2957 C CB  B ALA   A 134 ? 0.2130 0.2096 0.2090 -0.0149 -0.0565 0.0109  134 ALA   A CB  
2968 N N   A ASP   A 135 ? 0.2015 0.2179 0.2079 -0.0196 -0.0303 0.0390  135 ASP   A N   
2969 N N   B ASP   A 135 ? 0.2105 0.2172 0.2214 -0.0111 -0.0471 0.0259  135 ASP   A N   
2970 C CA  A ASP   A 135 ? 0.2033 0.2387 0.2370 -0.0351 -0.0464 0.0513  135 ASP   A CA  
2971 C CA  B ASP   A 135 ? 0.2101 0.2233 0.2328 -0.0138 -0.0443 0.0326  135 ASP   A CA  
2972 C C   A ASP   A 135 ? 0.1852 0.2328 0.2362 -0.0222 -0.0358 0.0630  135 ASP   A C   
2973 C C   B ASP   A 135 ? 0.2034 0.2173 0.2245 -0.0031 -0.0326 0.0414  135 ASP   A C   
2974 O O   A ASP   A 135 ? 0.1792 0.2227 0.2346 -0.0264 -0.0330 0.0644  135 ASP   A O   
2975 O O   B ASP   A 135 ? 0.2020 0.2092 0.2214 -0.0044 -0.0255 0.0505  135 ASP   A O   
2976 C CB  A ASP   A 135 ? 0.2268 0.2689 0.2875 -0.0504 -0.0681 0.0461  135 ASP   A CB  
2977 C CB  B ASP   A 135 ? 0.2158 0.2375 0.2590 -0.0243 -0.0556 0.0319  135 ASP   A CB  
2978 C CG  A ASP   A 135 ? 0.2447 0.2919 0.3397 -0.0594 -0.0687 0.0489  135 ASP   A CG  
2979 C CG  B ASP   A 135 ? 0.2206 0.2507 0.2829 -0.0331 -0.0612 0.0348  135 ASP   A CG  
2980 O OD1 A ASP   A 135 ? 0.2415 0.3039 0.3307 -0.0658 -0.0784 0.0701  135 ASP   A OD1 
2981 O OD1 B ASP   A 135 ? 0.2220 0.2554 0.2994 -0.0319 -0.0533 0.0378  135 ASP   A OD1 
2982 O OD2 A ASP   A 135 ? 0.2706 0.3074 0.3976 -0.0544 -0.0445 0.0437  135 ASP   A OD2 
2983 O OD2 B ASP   A 135 ? 0.2235 0.2564 0.2927 -0.0425 -0.0661 0.0398  135 ASP   A OD2 
2992 N N   A PRO   A 136 ? 0.1705 0.2356 0.2435 -0.0028 -0.0210 0.0744  136 PRO   A N   
2993 N N   B PRO   A 136 ? 0.1973 0.2202 0.2285 0.0064  -0.0241 0.0422  136 PRO   A N   
2994 C CA  A PRO   A 136 ? 0.1640 0.2328 0.2534 -0.0041 -0.0137 0.0573  136 PRO   A CA  
2995 C CA  B PRO   A 136 ? 0.1932 0.2200 0.2313 0.0091  -0.0205 0.0364  136 PRO   A CA  
2996 C C   A PRO   A 136 ? 0.1431 0.2260 0.2349 -0.0063 -0.0015 0.0502  136 PRO   A C   
2997 C C   B PRO   A 136 ? 0.1864 0.2207 0.2275 0.0111  -0.0198 0.0331  136 PRO   A C   
2998 O O   A PRO   A 136 ? 0.1302 0.2234 0.2242 -0.0076 0.0095  0.0469  136 PRO   A O   
2999 O O   B PRO   A 136 ? 0.1849 0.2219 0.2236 0.0125  -0.0232 0.0399  136 PRO   A O   
3000 C CB  A PRO   A 136 ? 0.1838 0.2349 0.2666 0.0053  -0.0157 0.0572  136 PRO   A CB  
3001 C CB  B PRO   A 136 ? 0.1995 0.2185 0.2371 0.0118  -0.0165 0.0399  136 PRO   A CB  
3002 C CG  A PRO   A 136 ? 0.2037 0.2454 0.2910 0.0119  -0.0156 0.0537  136 PRO   A CG  
3003 C CG  B PRO   A 136 ? 0.2025 0.2217 0.2416 0.0112  -0.0185 0.0383  136 PRO   A CG  
3004 C CD  A PRO   A 136 ? 0.1845 0.2417 0.2682 0.0120  -0.0115 0.0760  136 PRO   A CD  
3005 C CD  B PRO   A 136 ? 0.2014 0.2220 0.2356 0.0119  -0.0175 0.0408  136 PRO   A CD  
3020 N N   A ILE   A 137 ? 0.1448 0.2260 0.2477 -0.0109 -0.0119 0.0527  137 ILE   A N   
3021 N N   B ILE   A 137 ? 0.1851 0.2235 0.2303 0.0062  -0.0185 0.0249  137 ILE   A N   
3022 C CA  A ILE   A 137 ? 0.1472 0.2418 0.2546 -0.0189 -0.0149 0.0518  137 ILE   A CA  
3023 C CA  B ILE   A 137 ? 0.1869 0.2313 0.2334 -0.0023 -0.0180 0.0190  137 ILE   A CA  
3024 C C   A ILE   A 137 ? 0.1455 0.2322 0.2429 -0.0198 -0.0206 0.0501  137 ILE   A C   
3025 C C   B ILE   A 137 ? 0.1815 0.2259 0.2325 -0.0070 -0.0138 0.0171  137 ILE   A C   
3026 O O   A ILE   A 137 ? 0.1510 0.2233 0.2544 -0.0285 -0.0183 0.0436  137 ILE   A O   
3027 O O   B ILE   A 137 ? 0.1839 0.2208 0.2398 -0.0099 -0.0125 0.0097  137 ILE   A O   
3028 C CB  A ILE   A 137 ? 0.1599 0.2667 0.2751 -0.0217 -0.0362 0.0506  137 ILE   A CB  
3029 C CB  B ILE   A 137 ? 0.1965 0.2445 0.2436 -0.0063 -0.0260 0.0129  137 ILE   A CB  
3030 C CG1 A ILE   A 137 ? 0.1739 0.2944 0.3066 -0.0049 -0.0354 0.0508  137 ILE   A CG1 
3031 C CG1 B ILE   A 137 ? 0.2017 0.2563 0.2520 -0.0010 -0.0287 0.0090  137 ILE   A CG1 
3032 C CG2 A ILE   A 137 ? 0.1754 0.2710 0.2755 -0.0335 -0.0539 0.0333  137 ILE   A CG2 
3033 C CG2 B ILE   A 137 ? 0.2037 0.2470 0.2441 -0.0120 -0.0269 0.0045  137 ILE   A CG2 
3034 C CD1 A ILE   A 137 ? 0.1930 0.3080 0.3272 0.0045  -0.0268 0.0508  137 ILE   A CD1 
3035 C CD1 B ILE   A 137 ? 0.2083 0.2624 0.2621 0.0030  -0.0283 0.0033  137 ILE   A CD1 
3058 N N   A HIS   A 138 ? 0.1492 0.2440 0.2451 -0.0208 -0.0067 0.0427  138 HIS   A N   
3059 N N   B HIS   A 138 ? 0.1766 0.2297 0.2327 -0.0110 -0.0086 0.0166  138 HIS   A N   
3060 C CA  A HIS   A 138 ? 0.1596 0.2444 0.2337 -0.0211 -0.0074 0.0422  138 HIS   A CA  
3061 C CA  B HIS   A 138 ? 0.1716 0.2279 0.2276 -0.0171 -0.0097 0.0255  138 HIS   A CA  
3062 C C   A HIS   A 138 ? 0.1531 0.2241 0.2304 -0.0142 -0.0096 0.0461  138 HIS   A C   
3063 C C   B HIS   A 138 ? 0.1579 0.2169 0.2230 -0.0132 -0.0123 0.0362  138 HIS   A C   
3064 O O   A HIS   A 138 ? 0.1669 0.2217 0.2259 -0.0119 0.0008  0.0420  138 HIS   A O   
3065 O O   B HIS   A 138 ? 0.1598 0.2168 0.2161 -0.0121 -0.0099 0.0336  138 HIS   A O   
3066 C CB  A HIS   A 138 ? 0.1751 0.2656 0.2267 -0.0248 -0.0173 0.0272  138 HIS   A CB  
3067 C CB  B HIS   A 138 ? 0.1846 0.2397 0.2316 -0.0255 -0.0179 0.0209  138 HIS   A CB  
3068 C CG  A HIS   A 138 ? 0.1952 0.2787 0.2368 -0.0274 -0.0140 0.0093  138 HIS   A CG  
3069 C CG  B HIS   A 138 ? 0.1953 0.2469 0.2379 -0.0324 -0.0150 0.0140  138 HIS   A CG  
3070 N ND1 A HIS   A 138 ? 0.2092 0.2905 0.2518 -0.0267 -0.0097 -0.0084 138 HIS   A ND1 
3071 N ND1 B HIS   A 138 ? 0.2019 0.2533 0.2460 -0.0325 -0.0111 0.0055  138 HIS   A ND1 
3072 C CD2 A HIS   A 138 ? 0.1965 0.2872 0.2350 -0.0220 -0.0139 0.0130  138 HIS   A CD2 
3073 C CD2 B HIS   A 138 ? 0.1999 0.2524 0.2397 -0.0332 -0.0175 0.0158  138 HIS   A CD2 
3074 C CE1 A HIS   A 138 ? 0.2138 0.2976 0.2562 -0.0187 -0.0073 -0.0006 138 HIS   A CE1 
3075 C CE1 B HIS   A 138 ? 0.2062 0.2580 0.2486 -0.0300 -0.0121 0.0098  138 HIS   A CE1 
3076 N NE2 A HIS   A 138 ? 0.2087 0.2968 0.2414 -0.0177 -0.0049 0.0066  138 HIS   A NE2 
3077 N NE2 B HIS   A 138 ? 0.2059 0.2577 0.2448 -0.0304 -0.0157 0.0139  138 HIS   A NE2 
3092 N N   . SER   A 139 ? 0.1459 0.2068 0.2268 -0.0113 -0.0082 0.0465  139 SER   A N   
3093 C CA  . SER   A 139 ? 0.1486 0.2009 0.2241 -0.0140 -0.0091 0.0500  139 SER   A CA  
3094 C C   . SER   A 139 ? 0.1395 0.1896 0.2273 -0.0119 0.0028  0.0415  139 SER   A C   
3095 O O   . SER   A 139 ? 0.1338 0.1787 0.2399 -0.0133 -0.0046 0.0363  139 SER   A O   
3096 C CB  . SER   A 139 ? 0.1440 0.1944 0.2276 -0.0167 -0.0096 0.0497  139 SER   A CB  
3097 O OG  . SER   A 139 ? 0.1465 0.1922 0.2382 -0.0196 -0.0137 0.0572  139 SER   A OG  
3104 N N   . LEU   A 140 ? 0.1368 0.1986 0.2203 -0.0059 0.0066  0.0508  140 LEU   A N   
3105 C CA  . LEU   A 140 ? 0.1314 0.1921 0.2286 -0.0078 0.0024  0.0445  140 LEU   A CA  
3106 C C   . LEU   A 140 ? 0.1306 0.1948 0.2203 -0.0147 0.0015  0.0435  140 LEU   A C   
3107 O O   . LEU   A 140 ? 0.1379 0.1890 0.2420 -0.0090 0.0022  0.0414  140 LEU   A O   
3108 C CB  . LEU   A 140 ? 0.1384 0.1966 0.2382 -0.0132 0.0039  0.0464  140 LEU   A CB  
3109 C CG  . LEU   A 140 ? 0.1385 0.2059 0.2424 -0.0261 0.0058  0.0554  140 LEU   A CG  
3110 C CD1 . LEU   A 140 ? 0.1449 0.2115 0.2545 -0.0168 0.0052  0.0559  140 LEU   A CD1 
3111 C CD2 . LEU   A 140 ? 0.1472 0.2203 0.2497 -0.0236 0.0067  0.0581  140 LEU   A CD2 
3123 N N   . ARG   A 141 ? 0.1366 0.1978 0.2289 -0.0126 -0.0078 0.0346  141 ARG   A N   
3124 C CA  . ARG   A 141 ? 0.1559 0.2113 0.2537 -0.0263 -0.0112 0.0191  141 ARG   A CA  
3125 C C   . ARG   A 141 ? 0.1539 0.1906 0.2405 -0.0192 -0.0093 0.0209  141 ARG   A C   
3126 O O   . ARG   A 141 ? 0.1509 0.1857 0.2510 -0.0247 -0.0004 0.0205  141 ARG   A O   
3127 C CB  . ARG   A 141 ? 0.1791 0.2416 0.2768 -0.0363 -0.0285 -0.0038 141 ARG   A CB  
3128 C CG  . ARG   A 141 ? 0.2205 0.2790 0.3160 -0.0458 -0.0230 -0.0104 141 ARG   A CG  
3129 C CD  . ARG   A 141 ? 0.2522 0.3075 0.3454 -0.0591 -0.0224 -0.0072 141 ARG   A CD  
3130 N NE  . ARG   A 141 ? 0.2464 0.3311 0.3572 -0.0647 -0.0265 -0.0019 141 ARG   A NE  
3131 C CZ  . ARG   A 141 ? 0.2482 0.3537 0.3608 -0.0833 -0.0150 0.0009  141 ARG   A CZ  
3132 N NH1 . ARG   A 141 ? 0.2331 0.3542 0.3590 -0.0937 0.0001  -0.0179 141 ARG   A NH1 
3133 N NH2 . ARG   A 141 ? 0.2609 0.3720 0.3745 -0.0748 -0.0311 0.0039  141 ARG   A NH2 
3147 N N   . VAL   A 142 ? 0.1409 0.1854 0.2355 -0.0103 -0.0072 0.0107  142 VAL   A N   
3148 C CA  . VAL   A 142 ? 0.1422 0.1758 0.2308 -0.0126 0.0076  0.0093  142 VAL   A CA  
3149 C C   . VAL   A 142 ? 0.1320 0.1735 0.2252 -0.0151 0.0040  0.0189  142 VAL   A C   
3150 O O   . VAL   A 142 ? 0.1405 0.1712 0.2330 -0.0034 0.0095  0.0190  142 VAL   A O   
3151 C CB  . VAL   A 142 ? 0.1524 0.1850 0.2294 -0.0147 0.0069  0.0224  142 VAL   A CB  
3152 C CG1 . VAL   A 142 ? 0.1509 0.1787 0.2267 -0.0142 0.0119  0.0139  142 VAL   A CG1 
3153 C CG2 . VAL   A 142 ? 0.1704 0.2009 0.2468 -0.0054 0.0114  0.0197  142 VAL   A CG2 
3163 N N   . CYS   A 143 ? 0.1407 0.1700 0.2106 -0.0169 0.0038  0.0215  143 CYS   A N   
3164 C CA  . CYS   A 143 ? 0.1403 0.1706 0.2178 -0.0132 0.0072  0.0321  143 CYS   A CA  
3165 C C   . CYS   A 143 ? 0.1384 0.1655 0.2246 -0.0132 0.0029  0.0395  143 CYS   A C   
3166 O O   . CYS   A 143 ? 0.1401 0.1647 0.2223 -0.0114 0.0060  0.0325  143 CYS   A O   
3167 C CB  . CYS   A 143 ? 0.1485 0.1700 0.2299 -0.0065 0.0161  0.0351  143 CYS   A CB  
3168 S SG  . CYS   A 143 ? 0.1683 0.1776 0.2129 0.0040  0.0131  0.0274  143 CYS   A SG  
3174 N N   . VAL   A 144 ? 0.1392 0.1734 0.2493 -0.0141 0.0021  0.0437  144 VAL   A N   
3175 C CA  . VAL   A 144 ? 0.1491 0.1835 0.2779 -0.0156 0.0172  0.0477  144 VAL   A CA  
3176 C C   . VAL   A 144 ? 0.1457 0.1726 0.2687 -0.0231 -0.0078 0.0427  144 VAL   A C   
3177 O O   . VAL   A 144 ? 0.1696 0.1695 0.2803 -0.0106 -0.0050 0.0373  144 VAL   A O   
3178 C CB  . VAL   A 144 ? 0.1738 0.2020 0.3315 -0.0049 0.0309  0.0436  144 VAL   A CB  
3179 C CG1 . VAL   A 144 ? 0.1838 0.2193 0.3668 -0.0188 0.0133  0.0305  144 VAL   A CG1 
3180 C CG2 . VAL   A 144 ? 0.1604 0.2084 0.3314 -0.0092 0.0334  0.0632  144 VAL   A CG2 
3190 N N   . ASP   A 145 ? 0.1558 0.1693 0.2839 -0.0257 -0.0001 0.0255  145 ASP   A N   
3191 C CA  . ASP   A 145 ? 0.1652 0.1773 0.2872 -0.0242 -0.0025 0.0108  145 ASP   A CA  
3192 C C   . ASP   A 145 ? 0.1659 0.1659 0.2832 -0.0185 -0.0012 0.0018  145 ASP   A C   
3193 O O   . ASP   A 145 ? 0.1833 0.1697 0.3296 -0.0190 -0.0069 -0.0250 145 ASP   A O   
3194 C CB  . ASP   A 145 ? 0.1820 0.2091 0.3091 -0.0342 -0.0179 0.0079  145 ASP   A CB  
3195 C CG  . ASP   A 145 ? 0.2043 0.2486 0.3384 -0.0521 -0.0284 0.0142  145 ASP   A CG  
3196 O OD1 . ASP   A 145 ? 0.2005 0.2585 0.3517 -0.0668 -0.0233 0.0142  145 ASP   A OD1 
3197 O OD2 . ASP   A 145 ? 0.2199 0.2739 0.3500 -0.0623 -0.0414 0.0147  145 ASP   A OD2 
3202 N N   . THR   A 146 ? 0.1540 0.1496 0.2505 -0.0177 0.0013  0.0147  146 THR   A N   
3203 C CA  . THR   A 146 ? 0.1472 0.1498 0.2353 -0.0098 0.0011  0.0135  146 THR   A CA  
3204 C C   . THR   A 146 ? 0.1355 0.1483 0.2422 -0.0008 0.0067  0.0153  146 THR   A C   
3205 O O   . THR   A 146 ? 0.1488 0.1562 0.2608 -0.0013 0.0039  0.0153  146 THR   A O   
3206 C CB  . THR   A 146 ? 0.1442 0.1580 0.2343 -0.0030 0.0057  0.0176  146 THR   A CB  
3207 O OG1 . THR   A 146 ? 0.1451 0.1711 0.2450 -0.0017 0.0016  0.0118  146 THR   A OG1 
3208 C CG2 . THR   A 146 ? 0.1437 0.1566 0.2470 -0.0084 0.0036  0.0177  146 THR   A CG2 
3216 N N   . VAL   A 147 ? 0.1356 0.1515 0.2298 -0.0028 0.0126  0.0198  147 VAL   A N   
3217 C CA  . VAL   A 147 ? 0.1405 0.1520 0.2330 -0.0087 0.0237  0.0307  147 VAL   A CA  
3218 C C   . VAL   A 147 ? 0.1428 0.1503 0.2441 -0.0143 0.0190  0.0406  147 VAL   A C   
3219 O O   . VAL   A 147 ? 0.1469 0.1554 0.2571 -0.0169 0.0085  0.0389  147 VAL   A O   
3220 C CB  . VAL   A 147 ? 0.1495 0.1490 0.2305 -0.0145 0.0184  0.0354  147 VAL   A CB  
3221 C CG1 . VAL   A 147 ? 0.1793 0.1620 0.2203 -0.0053 0.0131  0.0418  147 VAL   A CG1 
3222 C CG2 . VAL   A 147 ? 0.1539 0.1520 0.2382 -0.0103 0.0137  0.0282  147 VAL   A CG2 
3232 N N   . ARG   A 148 ? 0.1440 0.1546 0.2460 -0.0146 0.0176  0.0540  148 ARG   A N   
3233 C CA  . ARG   A 148 ? 0.1520 0.1576 0.2396 -0.0166 0.0031  0.0553  148 ARG   A CA  
3234 C C   . ARG   A 148 ? 0.1614 0.1624 0.2400 -0.0174 0.0053  0.0661  148 ARG   A C   
3235 O O   . ARG   A 148 ? 0.1893 0.1697 0.2627 -0.0221 0.0220  0.0612  148 ARG   A O   
3236 C CB  . ARG   A 148 ? 0.1622 0.1551 0.2646 -0.0092 0.0180  0.0451  148 ARG   A CB  
3237 C CG  . ARG   A 148 ? 0.1794 0.1536 0.2953 -0.0158 0.0380  0.0318  148 ARG   A CG  
3238 C CD  . ARG   A 148 ? 0.1979 0.1552 0.3142 -0.0066 0.0533  0.0543  148 ARG   A CD  
3239 N NE  . ARG   A 148 ? 0.1868 0.1642 0.3103 0.0090  0.0554  0.0676  148 ARG   A NE  
3240 C CZ  . ARG   A 148 ? 0.1817 0.1544 0.2930 0.0071  0.0440  0.0619  148 ARG   A CZ  
3241 N NH1 . ARG   A 148 ? 0.1912 0.1507 0.2948 -0.0047 0.0479  0.0310  148 ARG   A NH1 
3242 N NH2 . ARG   A 148 ? 0.1712 0.1684 0.3011 0.0117  0.0457  0.0630  148 ARG   A NH2 
3256 N N   . THR   A 149 ? 0.1580 0.1702 0.2291 -0.0171 0.0001  0.0615  149 THR   A N   
3257 C CA  . THR   A 149 ? 0.1625 0.1713 0.2269 -0.0160 -0.0011 0.0572  149 THR   A CA  
3258 C C   . THR   A 149 ? 0.1556 0.1722 0.2268 -0.0206 0.0109  0.0590  149 THR   A C   
3259 O O   . THR   A 149 ? 0.1525 0.1799 0.2400 -0.0214 0.0078  0.0585  149 THR   A O   
3260 C CB  . THR   A 149 ? 0.1630 0.1799 0.2393 -0.0178 0.0027  0.0478  149 THR   A CB  
3261 O OG1 . THR   A 149 ? 0.1665 0.1662 0.2538 -0.0247 0.0033  0.0442  149 THR   A OG1 
3262 C CG2 . THR   A 149 ? 0.1603 0.1886 0.2445 -0.0109 -0.0026 0.0416  149 THR   A CG2 
3270 N N   . ASN   A 150 ? 0.1608 0.1751 0.2446 -0.0122 0.0018  0.0703  150 ASN   A N   
3271 C CA  . ASN   A 150 ? 0.1765 0.1822 0.2340 -0.0180 0.0055  0.0593  150 ASN   A CA  
3272 C C   . ASN   A 150 ? 0.1546 0.1718 0.2277 -0.0180 0.0072  0.0543  150 ASN   A C   
3273 O O   . ASN   A 150 ? 0.1633 0.1832 0.2552 -0.0190 -0.0017 0.0573  150 ASN   A O   
3274 C CB  . ASN   A 150 ? 0.2161 0.2084 0.2576 -0.0247 0.0182  0.0737  150 ASN   A CB  
3275 C CG  . ASN   A 150 ? 0.2717 0.2352 0.3098 -0.0233 0.0012  0.0784  150 ASN   A CG  
3276 O OD1 . ASN   A 150 ? 0.2981 0.2411 0.3205 -0.0304 0.0023  0.0916  150 ASN   A OD1 
3277 N ND2 . ASN   A 150 ? 0.3014 0.2600 0.3481 -0.0177 -0.0059 0.0735  150 ASN   A ND2 
3284 N N   . VAL   A 151 ? 0.1541 0.1615 0.2243 -0.0194 0.0072  0.0480  151 VAL   A N   
3285 C CA  . VAL   A 151 ? 0.1626 0.1668 0.2237 -0.0208 0.0115  0.0530  151 VAL   A CA  
3286 C C   . VAL   A 151 ? 0.1567 0.1653 0.2297 -0.0254 0.0163  0.0561  151 VAL   A C   
3287 O O   . VAL   A 151 ? 0.1625 0.1737 0.2665 -0.0223 0.0145  0.0500  151 VAL   A O   
3288 C CB  . VAL   A 151 ? 0.1871 0.1874 0.2289 -0.0072 0.0077  0.0464  151 VAL   A CB  
3289 C CG1 . VAL   A 151 ? 0.1797 0.2075 0.2534 -0.0159 0.0022  0.0320  151 VAL   A CG1 
3290 C CG2 . VAL   A 151 ? 0.1936 0.1879 0.2287 -0.0026 0.0256  0.0423  151 VAL   A CG2 
3300 N N   A TYR   A 152 ? 0.1540 0.1602 0.2381 -0.0240 0.0088  0.0492  152 TYR   A N   
3301 N N   B TYR   A 152 ? 0.1643 0.1741 0.2183 -0.0161 0.0116  0.0473  152 TYR   A N   
3302 C CA  A TYR   A 152 ? 0.1539 0.1642 0.2109 -0.0233 0.0130  0.0511  152 TYR   A CA  
3303 C CA  B TYR   A 152 ? 0.1729 0.1829 0.1951 -0.0083 0.0106  0.0447  152 TYR   A CA  
3304 C C   A TYR   A 152 ? 0.1462 0.1569 0.2154 -0.0224 0.0248  0.0508  152 TYR   A C   
3305 C C   B TYR   A 152 ? 0.1699 0.1848 0.1850 -0.0044 0.0118  0.0485  152 TYR   A C   
3306 O O   A TYR   A 152 ? 0.1546 0.1479 0.2244 -0.0242 0.0267  0.0416  152 TYR   A O   
3307 O O   B TYR   A 152 ? 0.1755 0.1833 0.1903 -0.0043 0.0061  0.0493  152 TYR   A O   
3308 C CB  A TYR   A 152 ? 0.1680 0.1796 0.2169 -0.0208 0.0279  0.0632  152 TYR   A CB  
3309 C CB  B TYR   A 152 ? 0.1867 0.1908 0.1990 -0.0051 0.0181  0.0414  152 TYR   A CB  
3310 C CG  A TYR   A 152 ? 0.1759 0.2007 0.2112 -0.0250 0.0348  0.0634  152 TYR   A CG  
3311 C CG  B TYR   A 152 ? 0.1984 0.2004 0.2005 -0.0049 0.0207  0.0396  152 TYR   A CG  
3312 C CD1 A TYR   A 152 ? 0.1878 0.2261 0.2310 -0.0079 0.0372  0.0659  152 TYR   A CD1 
3313 C CD1 B TYR   A 152 ? 0.2020 0.2094 0.2094 -0.0048 0.0269  0.0442  152 TYR   A CD1 
3314 C CD2 A TYR   A 152 ? 0.1760 0.2079 0.2049 -0.0337 0.0286  0.0490  152 TYR   A CD2 
3315 C CD2 B TYR   A 152 ? 0.2026 0.2027 0.1973 -0.0059 0.0193  0.0357  152 TYR   A CD2 
3316 C CE1 A TYR   A 152 ? 0.2038 0.2360 0.2368 -0.0007 0.0275  0.0747  152 TYR   A CE1 
3317 C CE1 B TYR   A 152 ? 0.2074 0.2158 0.2176 -0.0044 0.0229  0.0459  152 TYR   A CE1 
3318 C CE2 A TYR   A 152 ? 0.1923 0.2217 0.2180 -0.0250 0.0310  0.0613  152 TYR   A CE2 
3319 C CE2 B TYR   A 152 ? 0.2088 0.2110 0.2090 -0.0067 0.0173  0.0408  152 TYR   A CE2 
3320 C CZ  A TYR   A 152 ? 0.2109 0.2272 0.2289 -0.0093 0.0316  0.0858  152 TYR   A CZ  
3321 C CZ  B TYR   A 152 ? 0.2125 0.2172 0.2167 -0.0069 0.0193  0.0504  152 TYR   A CZ  
3322 O OH  A TYR   A 152 ? 0.2318 0.2431 0.2597 0.0070  0.0412  0.0948  152 TYR   A OH  
3323 O OH  B TYR   A 152 ? 0.2226 0.2311 0.2329 -0.0078 0.0220  0.0588  152 TYR   A OH  
3342 N N   A LEU   A 153 ? 0.1445 0.1536 0.2316 -0.0249 0.0193  0.0550  153 LEU   A N   
3343 N N   B LEU   A 153 ? 0.1677 0.1868 0.1795 -0.0009 0.0125  0.0484  153 LEU   A N   
3344 C CA  A LEU   A 153 ? 0.1392 0.1523 0.2370 -0.0154 0.0177  0.0519  153 LEU   A CA  
3345 C CA  B LEU   A 153 ? 0.1640 0.1874 0.1729 0.0070  0.0134  0.0471  153 LEU   A CA  
3346 C C   A LEU   A 153 ? 0.1429 0.1563 0.2447 -0.0141 0.0321  0.0482  153 LEU   A C   
3347 C C   B LEU   A 153 ? 0.1636 0.1916 0.1703 0.0099  0.0162  0.0458  153 LEU   A C   
3348 O O   A LEU   A 153 ? 0.1570 0.1662 0.2569 -0.0207 0.0388  0.0393  153 LEU   A O   
3349 O O   B LEU   A 153 ? 0.1648 0.1978 0.1675 0.0110  0.0144  0.0397  153 LEU   A O   
3350 C CB  A LEU   A 153 ? 0.1369 0.1555 0.2335 -0.0167 0.0073  0.0425  153 LEU   A CB  
3351 C CB  B LEU   A 153 ? 0.1627 0.1899 0.1746 0.0095  0.0111  0.0474  153 LEU   A CB  
3352 C CG  A LEU   A 153 ? 0.1393 0.1644 0.2218 -0.0192 0.0051  0.0395  153 LEU   A CG  
3353 C CG  B LEU   A 153 ? 0.1657 0.1916 0.1746 0.0130  0.0101  0.0498  153 LEU   A CG  
3354 C CD1 A LEU   A 153 ? 0.1493 0.1609 0.2157 -0.0161 -0.0039 0.0459  153 LEU   A CD1 
3355 C CD1 B LEU   A 153 ? 0.1709 0.1904 0.1860 0.0160  0.0120  0.0472  153 LEU   A CD1 
3356 C CD2 A LEU   A 153 ? 0.1455 0.1646 0.2158 -0.0176 0.0080  0.0146  153 LEU   A CD2 
3357 C CD2 B LEU   A 153 ? 0.1676 0.1932 0.1745 0.0121  0.0095  0.0447  153 LEU   A CD2 
3380 N N   A ALA   A 154 ? 0.1370 0.1564 0.2533 -0.0056 0.0376  0.0479  154 ALA   A N   
3381 N N   B ALA   A 154 ? 0.1642 0.1904 0.1824 0.0065  0.0264  0.0462  154 ALA   A N   
3382 C CA  A ALA   A 154 ? 0.1544 0.1616 0.2613 -0.0041 0.0398  0.0507  154 ALA   A CA  
3383 C CA  B ALA   A 154 ? 0.1744 0.1897 0.1955 0.0032  0.0236  0.0434  154 ALA   A CA  
3384 C C   A ALA   A 154 ? 0.1529 0.1601 0.2715 0.0010  0.0361  0.0597  154 ALA   A C   
3385 C C   B ALA   A 154 ? 0.1791 0.1893 0.2054 0.0023  0.0225  0.0420  154 ALA   A C   
3386 O O   A ALA   A 154 ? 0.1578 0.1661 0.2745 0.0018  0.0356  0.0580  154 ALA   A O   
3387 O O   B ALA   A 154 ? 0.1806 0.1869 0.2032 -0.0001 0.0213  0.0366  154 ALA   A O   
3388 C CB  A ALA   A 154 ? 0.1669 0.1614 0.2686 0.0033  0.0311  0.0428  154 ALA   A CB  
3389 C CB  B ALA   A 154 ? 0.1768 0.1866 0.2003 0.0041  0.0191  0.0403  154 ALA   A CB  
3400 N N   A VAL   A 155 ? 0.1595 0.1654 0.2754 0.0071  0.0364  0.0766  155 VAL   A N   
3401 N N   B VAL   A 155 ? 0.1843 0.1920 0.2185 0.0029  0.0257  0.0437  155 VAL   A N   
3402 C CA  A VAL   A 155 ? 0.1697 0.1818 0.2773 0.0131  0.0368  0.0798  155 VAL   A CA  
3403 C CA  B VAL   A 155 ? 0.1902 0.1992 0.2322 0.0052  0.0266  0.0406  155 VAL   A CA  
3404 C C   A VAL   A 155 ? 0.1771 0.1907 0.2923 0.0277  0.0299  0.0856  155 VAL   A C   
3405 C C   B VAL   A 155 ? 0.2033 0.2084 0.2484 0.0049  0.0319  0.0427  155 VAL   A C   
3406 O O   A VAL   A 155 ? 0.1787 0.1960 0.3026 0.0332  0.0265  0.0697  155 VAL   A O   
3407 O O   B VAL   A 155 ? 0.2003 0.2049 0.2514 0.0049  0.0422  0.0425  155 VAL   A O   
3408 C CB  A VAL   A 155 ? 0.1806 0.1900 0.2556 0.0189  0.0274  0.0681  155 VAL   A CB  
3409 C CB  B VAL   A 155 ? 0.1853 0.1988 0.2226 0.0118  0.0174  0.0350  155 VAL   A CB  
3410 C CG1 A VAL   A 155 ? 0.2022 0.2000 0.2614 0.0268  0.0158  0.0622  155 VAL   A CG1 
3411 C CG1 B VAL   A 155 ? 0.1828 0.2004 0.2200 0.0198  0.0151  0.0327  155 VAL   A CG1 
3412 C CG2 A VAL   A 155 ? 0.1898 0.1979 0.2579 0.0307  0.0067  0.0637  155 VAL   A CG2 
3413 C CG2 B VAL   A 155 ? 0.1903 0.2015 0.2258 0.0166  0.0080  0.0334  155 VAL   A CG2 
3432 N N   A PHE   A 156 ? 0.1877 0.1950 0.3117 0.0342  0.0401  0.0986  156 PHE   A N   
3433 N N   B PHE   A 156 ? 0.2234 0.2234 0.2760 0.0036  0.0244  0.0423  156 PHE   A N   
3434 C CA  A PHE   A 156 ? 0.2155 0.1948 0.3458 0.0441  0.0343  0.0983  156 PHE   A CA  
3435 C CA  B PHE   A 156 ? 0.2463 0.2378 0.3028 0.0043  0.0151  0.0330  156 PHE   A CA  
3436 C C   A PHE   A 156 ? 0.2164 0.1989 0.3505 0.0501  0.0442  0.1056  156 PHE   A C   
3437 C C   B PHE   A 156 ? 0.2545 0.2454 0.3130 0.0062  0.0124  0.0330  156 PHE   A C   
3438 O O   A PHE   A 156 ? 0.2146 0.2039 0.3628 0.0470  0.0468  0.0797  156 PHE   A O   
3439 O O   B PHE   A 156 ? 0.2638 0.2498 0.3316 0.0051  0.0046  0.0306  156 PHE   A O   
3440 C CB  A PHE   A 156 ? 0.2450 0.1983 0.3479 0.0432  0.0179  0.1060  156 PHE   A CB  
3441 C CB  B PHE   A 156 ? 0.2591 0.2450 0.3124 0.0028  0.0120  0.0247  156 PHE   A CB  
3442 C CG  A PHE   A 156 ? 0.2819 0.2068 0.3599 0.0460  0.0018  0.1004  156 PHE   A CG  
3443 C CG  B PHE   A 156 ? 0.2687 0.2536 0.3230 0.0013  0.0082  0.0110  156 PHE   A CG  
3444 C CD1 A PHE   A 156 ? 0.3016 0.2203 0.3743 0.0451  0.0011  0.0872  156 PHE   A CD1 
3445 C CD1 B PHE   A 156 ? 0.2718 0.2565 0.3279 -0.0001 0.0066  0.0099  156 PHE   A CD1 
3446 C CD2 A PHE   A 156 ? 0.2962 0.2130 0.3637 0.0546  -0.0009 0.1120  156 PHE   A CD2 
3447 C CD2 B PHE   A 156 ? 0.2725 0.2583 0.3283 -0.0013 0.0065  0.0054  156 PHE   A CD2 
3448 C CE1 A PHE   A 156 ? 0.3138 0.2271 0.3911 0.0452  0.0036  0.0856  156 PHE   A CE1 
3449 C CE1 B PHE   A 156 ? 0.2756 0.2595 0.3313 -0.0020 0.0034  0.0069  156 PHE   A CE1 
3450 C CE2 A PHE   A 156 ? 0.3104 0.2221 0.3768 0.0569  -0.0019 0.0960  156 PHE   A CE2 
3451 C CE2 B PHE   A 156 ? 0.2753 0.2599 0.3299 -0.0027 0.0050  0.0040  156 PHE   A CE2 
3452 C CZ  A PHE   A 156 ? 0.3161 0.2264 0.3894 0.0556  0.0008  0.0805  156 PHE   A CZ  
3453 C CZ  B PHE   A 156 ? 0.2771 0.2608 0.3328 -0.0019 0.0024  0.0030  156 PHE   A CZ  
3472 N N   A ASP   A 157 ? 0.2182 0.2070 0.3481 0.0494  0.0447  0.1258  157 ASP   A N   
3473 N N   B ASP   A 157 ? 0.2482 0.2480 0.3042 0.0069  0.0132  0.0435  157 ASP   A N   
3474 C CA  A ASP   A 157 ? 0.2323 0.2316 0.3655 0.0547  0.0324  0.1361  157 ASP   A CA  
3475 C CA  B ASP   A 157 ? 0.2380 0.2511 0.2914 0.0073  0.0144  0.0507  157 ASP   A CA  
3476 C C   A ASP   A 157 ? 0.2104 0.2543 0.3660 0.0635  0.0431  0.1477  157 ASP   A C   
3477 C C   B ASP   A 157 ? 0.2337 0.2535 0.2845 0.0080  0.0099  0.0527  157 ASP   A C   
3478 O O   A ASP   A 157 ? 0.2018 0.2533 0.3683 0.0562  0.0549  0.1517  157 ASP   A O   
3479 O O   B ASP   A 157 ? 0.2288 0.2518 0.2886 0.0084  0.0085  0.0495  157 ASP   A O   
3480 C CB  A ASP   A 157 ? 0.2573 0.2412 0.3910 0.0638  0.0132  0.1227  157 ASP   A CB  
3481 C CB  B ASP   A 157 ? 0.2251 0.2525 0.2888 0.0090  0.0233  0.0602  157 ASP   A CB  
3482 C CG  A ASP   A 157 ? 0.2858 0.2531 0.4288 0.0638  -0.0112 0.1122  157 ASP   A CG  
3483 C CG  B ASP   A 157 ? 0.2140 0.2545 0.2906 0.0108  0.0228  0.0698  157 ASP   A CG  
3484 O OD1 A ASP   A 157 ? 0.3112 0.2599 0.4569 0.0547  -0.0328 0.0933  157 ASP   A OD1 
3485 O OD1 B ASP   A 157 ? 0.2154 0.2571 0.3060 0.0095  0.0241  0.0788  157 ASP   A OD1 
3486 O OD2 A ASP   A 157 ? 0.2851 0.2587 0.4521 0.0589  -0.0126 0.1219  157 ASP   A OD2 
3487 O OD2 B ASP   A 157 ? 0.1969 0.2510 0.2819 0.0117  0.0191  0.0703  157 ASP   A OD2 
3496 N N   A LYS   A 158 ? 0.2160 0.2856 0.3823 0.0681  0.0499  0.1278  158 LYS   A N   
3497 N N   B LYS   A 158 ? 0.2377 0.2623 0.2767 0.0072  0.0079  0.0518  158 LYS   A N   
3498 C CA  A LYS   A 158 ? 0.2164 0.3119 0.3959 0.0746  0.0581  0.1175  158 LYS   A CA  
3499 C CA  B LYS   A 158 ? 0.2440 0.2727 0.2693 0.0062  0.0092  0.0518  158 LYS   A CA  
3500 C C   A LYS   A 158 ? 0.2012 0.3140 0.3920 0.0712  0.0531  0.1349  158 LYS   A C   
3501 C C   B LYS   A 158 ? 0.2345 0.2762 0.2634 0.0037  0.0146  0.0580  158 LYS   A C   
3502 O O   A LYS   A 158 ? 0.1987 0.3206 0.3957 0.0661  0.0643  0.1354  158 LYS   A O   
3503 O O   B LYS   A 158 ? 0.2278 0.2784 0.2593 0.0015  0.0189  0.0642  158 LYS   A O   
3504 C CB  A LYS   A 158 ? 0.2350 0.3290 0.4093 0.0797  0.0802  0.1058  158 LYS   A CB  
3505 C CB  B LYS   A 158 ? 0.2571 0.2816 0.2773 0.0066  0.0053  0.0469  158 LYS   A CB  
3506 C CG  A LYS   A 158 ? 0.2560 0.3456 0.4309 0.0797  0.0962  0.0940  158 LYS   A CG  
3507 C CG  B LYS   A 158 ? 0.2697 0.2889 0.2927 0.0056  0.0012  0.0438  158 LYS   A CG  
3508 C CD  A LYS   A 158 ? 0.2681 0.3567 0.4401 0.0737  0.1211  0.0962  158 LYS   A CD  
3509 C CD  B LYS   A 158 ? 0.2763 0.2924 0.3110 0.0016  0.0010  0.0427  158 LYS   A CD  
3510 C CE  A LYS   A 158 ? 0.2750 0.3624 0.4456 0.0656  0.1356  0.1051  158 LYS   A CE  
3511 C CE  B LYS   A 158 ? 0.2801 0.2960 0.3291 -0.0012 0.0032  0.0423  158 LYS   A CE  
3512 N NZ  A LYS   A 158 ? 0.2769 0.3638 0.4513 0.0577  0.1416  0.1183  158 LYS   A NZ  
3513 N NZ  B LYS   A 158 ? 0.2828 0.2968 0.3420 -0.0030 0.0065  0.0417  158 LYS   A NZ  
3540 N N   A ASN   A 159 ? 0.1909 0.3107 0.4040 0.0683  0.0327  0.1367  159 ASN   A N   
3541 N N   B ASN   A 159 ? 0.2338 0.2798 0.2756 0.0019  0.0132  0.0523  159 ASN   A N   
3542 C CA  A ASN   A 159 ? 0.1968 0.3052 0.4048 0.0551  0.0085  0.1468  159 ASN   A CA  
3543 C CA  B ASN   A 159 ? 0.2340 0.2803 0.2897 -0.0019 0.0093  0.0505  159 ASN   A CA  
3544 C C   A ASN   A 159 ? 0.1830 0.3038 0.3660 0.0347  0.0125  0.1180  159 ASN   A C   
3545 C C   B ASN   A 159 ? 0.2154 0.2661 0.2535 -0.0143 0.0036  0.0498  159 ASN   A C   
3546 O O   A ASN   A 159 ? 0.1629 0.3010 0.3514 0.0315  -0.0144 0.0837  159 ASN   A O   
3547 O O   B ASN   A 159 ? 0.2131 0.2722 0.2437 -0.0157 -0.0059 0.0498  159 ASN   A O   
3548 C CB  A ASN   A 159 ? 0.2180 0.3077 0.4666 0.0577  -0.0018 0.1636  159 ASN   A CB  
3549 C CB  B ASN   A 159 ? 0.2543 0.2942 0.3475 0.0029  0.0115  0.0477  159 ASN   A CB  
3550 C CG  A ASN   A 159 ? 0.2514 0.3240 0.5442 0.0517  0.0053  0.1595  159 ASN   A CG  
3551 C CG  B ASN   A 159 ? 0.2741 0.3098 0.4021 0.0044  0.0167  0.0427  159 ASN   A CG  
3552 O OD1 A ASN   A 159 ? 0.2575 0.3431 0.5800 0.0454  0.0171  0.1499  159 ASN   A OD1 
3553 O OD1 B ASN   A 159 ? 0.2838 0.3173 0.4270 0.0027  0.0161  0.0367  159 ASN   A OD1 
3554 N ND2 A ASN   A 159 ? 0.2667 0.3283 0.5767 0.0528  0.0033  0.1543  159 ASN   A ND2 
3555 N ND2 B ASN   A 159 ? 0.2781 0.3136 0.4176 0.0057  0.0200  0.0434  159 ASN   A ND2 
3568 N N   A LEU   A 160 ? 0.1752 0.2950 0.3425 0.0284  0.0087  0.1268  160 LEU   A N   
3569 N N   B LEU   A 160 ? 0.2002 0.2474 0.2413 -0.0213 -0.0001 0.0581  160 LEU   A N   
3570 C CA  A LEU   A 160 ? 0.1700 0.2884 0.3234 0.0163  0.0209  0.1269  160 LEU   A CA  
3571 C CA  B LEU   A 160 ? 0.1982 0.2384 0.2360 -0.0239 0.0072  0.0585  160 LEU   A CA  
3572 C C   A LEU   A 160 ? 0.1586 0.2933 0.3119 0.0089  0.0288  0.1184  160 LEU   A C   
3573 C C   B LEU   A 160 ? 0.1911 0.2372 0.2286 -0.0116 0.0087  0.0504  160 LEU   A C   
3574 O O   A LEU   A 160 ? 0.1557 0.3048 0.3302 0.0053  0.0263  0.1153  160 LEU   A O   
3575 O O   B LEU   A 160 ? 0.1869 0.2357 0.2351 -0.0131 0.0089  0.0426  160 LEU   A O   
3576 C CB  A LEU   A 160 ? 0.1791 0.2814 0.3082 0.0117  0.0263  0.1209  160 LEU   A CB  
3577 C CB  B LEU   A 160 ? 0.2093 0.2362 0.2411 -0.0314 0.0131  0.0578  160 LEU   A CB  
3578 C CG  A LEU   A 160 ? 0.1869 0.2785 0.3002 0.0014  0.0242  0.1046  160 LEU   A CG  
3579 C CG  B LEU   A 160 ? 0.2280 0.2433 0.2549 -0.0336 0.0102  0.0435  160 LEU   A CG  
3580 C CD1 A LEU   A 160 ? 0.2016 0.2767 0.3216 -0.0103 0.0316  0.0940  160 LEU   A CD1 
3581 C CD1 B LEU   A 160 ? 0.2292 0.2430 0.2544 -0.0357 0.0107  0.0380  160 LEU   A CD1 
3582 C CD2 A LEU   A 160 ? 0.1901 0.2775 0.2907 -0.0006 0.0259  0.0953  160 LEU   A CD2 
3583 C CD2 B LEU   A 160 ? 0.2354 0.2466 0.2616 -0.0348 0.0099  0.0416  160 LEU   A CD2 
3606 N N   A TYR   A 161 ? 0.1588 0.2833 0.2971 0.0103  0.0301  0.1170  161 TYR   A N   
3607 N N   B TYR   A 161 ? 0.1904 0.2415 0.2217 0.0013  0.0124  0.0561  161 TYR   A N   
3608 C CA  A TYR   A 161 ? 0.1584 0.2775 0.2938 0.0083  0.0333  0.1144  161 TYR   A CA  
3609 C CA  B TYR   A 161 ? 0.1903 0.2467 0.2235 0.0088  0.0147  0.0634  161 TYR   A CA  
3610 C C   A TYR   A 161 ? 0.1540 0.2923 0.3134 0.0043  0.0277  0.1179  161 TYR   A C   
3611 C C   B TYR   A 161 ? 0.1934 0.2616 0.2327 0.0074  0.0078  0.0632  161 TYR   A C   
3612 O O   A TYR   A 161 ? 0.1378 0.2903 0.3148 -0.0090 0.0246  0.1099  161 TYR   A O   
3613 O O   B TYR   A 161 ? 0.1851 0.2615 0.2192 0.0030  -0.0035 0.0654  161 TYR   A O   
3614 C CB  A TYR   A 161 ? 0.1785 0.2696 0.3001 0.0123  0.0319  0.1001  161 TYR   A CB  
3615 C CB  B TYR   A 161 ? 0.1891 0.2396 0.2249 0.0162  0.0225  0.0649  161 TYR   A CB  
3616 C CG  A TYR   A 161 ? 0.1826 0.2570 0.2976 0.0136  0.0272  0.0860  161 TYR   A CG  
3617 C CG  B TYR   A 161 ? 0.1872 0.2339 0.2281 0.0193  0.0271  0.0613  161 TYR   A CG  
3618 C CD1 A TYR   A 161 ? 0.1750 0.2445 0.3010 0.0088  0.0196  0.0780  161 TYR   A CD1 
3619 C CD1 B TYR   A 161 ? 0.1850 0.2314 0.2383 0.0195  0.0219  0.0550  161 TYR   A CD1 
3620 C CD2 A TYR   A 161 ? 0.1822 0.2582 0.2985 0.0186  0.0220  0.0775  161 TYR   A CD2 
3621 C CD2 B TYR   A 161 ? 0.1857 0.2336 0.2312 0.0223  0.0283  0.0609  161 TYR   A CD2 
3622 C CE1 A TYR   A 161 ? 0.1806 0.2409 0.2946 0.0034  0.0183  0.0832  161 TYR   A CE1 
3623 C CE1 B TYR   A 161 ? 0.1885 0.2326 0.2407 0.0195  0.0185  0.0562  161 TYR   A CE1 
3624 C CE2 A TYR   A 161 ? 0.1844 0.2484 0.2976 0.0108  0.0211  0.0821  161 TYR   A CE2 
3625 C CE2 B TYR   A 161 ? 0.1877 0.2329 0.2368 0.0193  0.0253  0.0618  161 TYR   A CE2 
3626 C CZ  A TYR   A 161 ? 0.1906 0.2393 0.3001 0.0017  0.0201  0.0832  161 TYR   A CZ  
3627 C CZ  B TYR   A 161 ? 0.1937 0.2350 0.2481 0.0174  0.0201  0.0565  161 TYR   A CZ  
3628 O OH  A TYR   A 161 ? 0.2027 0.2300 0.3055 -0.0002 0.0136  0.0885  161 TYR   A OH  
3629 O OH  B TYR   A 161 ? 0.2050 0.2395 0.2676 0.0156  0.0170  0.0534  161 TYR   A OH  
3648 N N   A ASP   A 162 ? 0.1487 0.3113 0.3332 0.0153  0.0366  0.1294  162 ASP   A N   
3649 N N   B ASP   A 162 ? 0.2021 0.2781 0.2619 0.0089  0.0151  0.0610  162 ASP   A N   
3650 C CA  A ASP   A 162 ? 0.1489 0.3409 0.3409 0.0102  0.0390  0.1306  162 ASP   A CA  
3651 C CA  B ASP   A 162 ? 0.2111 0.2980 0.2826 0.0016  0.0199  0.0602  162 ASP   A CA  
3652 C C   A ASP   A 162 ? 0.1324 0.3560 0.3345 0.0012  0.0352  0.1350  162 ASP   A C   
3653 C C   B ASP   A 162 ? 0.2192 0.3078 0.2836 -0.0063 0.0136  0.0598  162 ASP   A C   
3654 O O   A ASP   A 162 ? 0.1360 0.3617 0.3575 -0.0028 0.0384  0.1249  162 ASP   A O   
3655 O O   B ASP   A 162 ? 0.2217 0.3106 0.2869 -0.0089 0.0112  0.0581  162 ASP   A O   
3656 C CB  A ASP   A 162 ? 0.1578 0.3544 0.3575 0.0191  0.0403  0.1241  162 ASP   A CB  
3657 C CB  B ASP   A 162 ? 0.2117 0.3090 0.3049 0.0022  0.0288  0.0580  162 ASP   A CB  
3658 C CG  A ASP   A 162 ? 0.1752 0.3703 0.3729 0.0242  0.0483  0.1123  162 ASP   A CG  
3659 C CG  B ASP   A 162 ? 0.2151 0.3197 0.3220 -0.0011 0.0389  0.0596  162 ASP   A CG  
3660 O OD1 A ASP   A 162 ? 0.1923 0.3859 0.3820 0.0235  0.0498  0.0970  162 ASP   A OD1 
3661 O OD1 B ASP   A 162 ? 0.2157 0.3251 0.3316 0.0024  0.0382  0.0585  162 ASP   A OD1 
3662 O OD2 A ASP   A 162 ? 0.1825 0.3680 0.3918 0.0268  0.0557  0.1034  162 ASP   A OD2 
3663 O OD2 B ASP   A 162 ? 0.2185 0.3227 0.3283 -0.0064 0.0475  0.0610  162 ASP   A OD2 
3672 N N   A LYS   A 163 ? 0.1492 0.3720 0.3369 0.0047  0.0056  0.1316  163 LYS   A N   
3673 N N   B LYS   A 163 ? 0.2294 0.3157 0.2924 -0.0105 0.0098  0.0543  163 LYS   A N   
3674 C CA  A LYS   A 163 ? 0.1626 0.3837 0.3242 -0.0002 -0.0063 0.1249  163 LYS   A CA  
3675 C CA  B LYS   A 163 ? 0.2405 0.3219 0.2970 -0.0151 0.0094  0.0474  163 LYS   A CA  
3676 C C   A LYS   A 163 ? 0.1549 0.3686 0.3178 -0.0084 0.0088  0.1158  163 LYS   A C   
3677 C C   B LYS   A 163 ? 0.2344 0.3151 0.2831 -0.0170 0.0153  0.0448  163 LYS   A C   
3678 O O   A LYS   A 163 ? 0.1533 0.3835 0.3280 -0.0150 0.0130  0.1088  163 LYS   A O   
3679 O O   B LYS   A 163 ? 0.2350 0.3207 0.2897 -0.0114 0.0165  0.0390  163 LYS   A O   
3680 C CB  A LYS   A 163 ? 0.2048 0.4128 0.3593 0.0160  -0.0268 0.1191  163 LYS   A CB  
3681 C CB  B LYS   A 163 ? 0.2599 0.3344 0.3243 -0.0138 0.0024  0.0422  163 LYS   A CB  
3682 C CG  A LYS   A 163 ? 0.2503 0.4405 0.4139 0.0211  -0.0237 0.1078  163 LYS   A CG  
3683 C CG  B LYS   A 163 ? 0.2751 0.3450 0.3559 -0.0157 0.0022  0.0374  163 LYS   A CG  
3684 C CD  A LYS   A 163 ? 0.2940 0.4617 0.4688 0.0250  -0.0221 0.1003  163 LYS   A CD  
3685 C CD  B LYS   A 163 ? 0.2881 0.3534 0.3852 -0.0174 -0.0000 0.0361  163 LYS   A CD  
3686 C CE  A LYS   A 163 ? 0.3281 0.4756 0.5180 0.0248  -0.0191 0.0936  163 LYS   A CE  
3687 C CE  B LYS   A 163 ? 0.2971 0.3582 0.4069 -0.0191 -0.0019 0.0368  163 LYS   A CE  
3688 N NZ  A LYS   A 163 ? 0.3398 0.4835 0.5444 0.0229  -0.0185 0.0917  163 LYS   A NZ  
3689 N NZ  B LYS   A 163 ? 0.3007 0.3594 0.4185 -0.0188 -0.0036 0.0373  163 LYS   A NZ  
3716 N N   A LEU   A 164 ? 0.1363 0.3353 0.3010 -0.0159 0.0059  0.1108  164 LEU   A N   
3717 N N   B LEU   A 164 ? 0.2253 0.2999 0.2605 -0.0222 0.0140  0.0464  164 LEU   A N   
3718 C CA  A LEU   A 164 ? 0.1438 0.3081 0.2898 -0.0257 0.0184  0.1020  164 LEU   A CA  
3719 C CA  B LEU   A 164 ? 0.2229 0.2893 0.2459 -0.0253 0.0185  0.0436  164 LEU   A CA  
3720 C C   A LEU   A 164 ? 0.1476 0.3033 0.2953 -0.0297 0.0229  0.0927  164 LEU   A C   
3721 C C   B LEU   A 164 ? 0.2260 0.2894 0.2437 -0.0200 0.0190  0.0421  164 LEU   A C   
3722 O O   A LEU   A 164 ? 0.1554 0.3064 0.2949 -0.0348 0.0449  0.0791  164 LEU   A O   
3723 O O   B LEU   A 164 ? 0.2226 0.2914 0.2429 -0.0185 0.0299  0.0397  164 LEU   A O   
3724 C CB  A LEU   A 164 ? 0.1504 0.2914 0.2658 -0.0252 0.0238  0.1003  164 LEU   A CB  
3725 C CB  B LEU   A 164 ? 0.2160 0.2801 0.2298 -0.0306 0.0207  0.0448  164 LEU   A CB  
3726 C CG  A LEU   A 164 ? 0.1592 0.2788 0.2637 -0.0137 0.0212  0.0798  164 LEU   A CG  
3727 C CG  B LEU   A 164 ? 0.2092 0.2705 0.2076 -0.0332 0.0239  0.0436  164 LEU   A CG  
3728 C CD1 A LEU   A 164 ? 0.1562 0.2711 0.2479 -0.0016 0.0254  0.0726  164 LEU   A CD1 
3729 C CD1 B LEU   A 164 ? 0.2043 0.2657 0.1871 -0.0330 0.0251  0.0422  164 LEU   A CD1 
3730 C CD2 A LEU   A 164 ? 0.1659 0.2762 0.2636 -0.0212 0.0228  0.0684  164 LEU   A CD2 
3731 C CD2 B LEU   A 164 ? 0.2107 0.2697 0.2062 -0.0343 0.0218  0.0406  164 LEU   A CD2 
3754 N N   A VAL   A 165 ? 0.1452 0.2937 0.2913 -0.0270 0.0211  0.0995  165 VAL   A N   
3755 N N   B VAL   A 165 ? 0.2325 0.2868 0.2376 -0.0172 0.0160  0.0452  165 VAL   A N   
3756 C CA  A VAL   A 165 ? 0.1557 0.2868 0.2763 -0.0278 0.0300  0.1003  165 VAL   A CA  
3757 C CA  B VAL   A 165 ? 0.2417 0.2837 0.2300 -0.0138 0.0142  0.0448  165 VAL   A CA  
3758 C C   A VAL   A 165 ? 0.1447 0.2999 0.2877 -0.0219 0.0314  0.0972  165 VAL   A C   
3759 C C   B VAL   A 165 ? 0.2493 0.2862 0.2358 -0.0101 0.0180  0.0335  165 VAL   A C   
3760 O O   A VAL   A 165 ? 0.1423 0.3000 0.2952 -0.0188 0.0348  0.0972  165 VAL   A O   
3761 O O   B VAL   A 165 ? 0.2454 0.2829 0.2338 -0.0073 0.0183  0.0326  165 VAL   A O   
3762 C CB  A VAL   A 165 ? 0.1753 0.2741 0.2831 -0.0260 0.0401  0.0876  165 VAL   A CB  
3763 C CB  B VAL   A 165 ? 0.2443 0.2800 0.2285 -0.0148 0.0146  0.0483  165 VAL   A CB  
3764 C CG1 A VAL   A 165 ? 0.1845 0.2756 0.2960 -0.0255 0.0393  0.0735  165 VAL   A CG1 
3765 C CG1 B VAL   A 165 ? 0.2470 0.2814 0.2295 -0.0158 0.0145  0.0457  165 VAL   A CG1 
3766 C CG2 A VAL   A 165 ? 0.1894 0.2725 0.2795 -0.0239 0.0352  0.0934  165 VAL   A CG2 
3767 C CG2 B VAL   A 165 ? 0.2454 0.2787 0.2298 -0.0133 0.0082  0.0481  165 VAL   A CG2 
3786 N N   A SER   A 166 ? 0.1371 0.3110 0.2954 -0.0201 0.0233  0.0949  166 SER   A N   
3787 N N   B SER   A 166 ? 0.2603 0.2932 0.2548 -0.0091 0.0227  0.0211  166 SER   A N   
3788 C CA  A SER   A 166 ? 0.1490 0.3331 0.3127 -0.0208 0.0145  0.0854  166 SER   A CA  
3789 C CA  B SER   A 166 ? 0.2753 0.3012 0.2728 -0.0085 0.0279  0.0088  166 SER   A CA  
3790 C C   A SER   A 166 ? 0.1464 0.3550 0.3212 -0.0248 -0.0029 0.0738  166 SER   A C   
3791 C C   B SER   A 166 ? 0.2797 0.3080 0.2726 -0.0092 0.0318  0.0030  166 SER   A C   
3792 O O   A SER   A 166 ? 0.1680 0.3674 0.3557 -0.0348 0.0087  0.0470  166 SER   A O   
3793 O O   B SER   A 166 ? 0.2765 0.3103 0.2744 -0.0091 0.0415  -0.0043 166 SER   A O   
3794 C CB  A SER   A 166 ? 0.1728 0.3405 0.3430 -0.0135 0.0112  0.0731  166 SER   A CB  
3795 C CB  B SER   A 166 ? 0.2846 0.3045 0.2991 -0.0026 0.0256  -0.0004 166 SER   A CB  
3796 O OG  A SER   A 166 ? 0.2143 0.3457 0.3768 -0.0169 0.0091  0.0690  166 SER   A OG  
3797 O OG  B SER   A 166 ? 0.2941 0.3077 0.3224 -0.0021 0.0248  -0.0080 166 SER   A OG  
3808 N N   A SER   A 167 ? 0.1465 0.3615 0.2954 -0.0070 -0.0122 0.0767  167 SER   A N   
3809 N N   B SER   A 167 ? 0.2903 0.3159 0.2800 -0.0100 0.0245  0.0059  167 SER   A N   
3810 C CA  A SER   A 167 ? 0.1760 0.3648 0.2909 0.0049  -0.0200 0.0615  167 SER   A CA  
3811 C CA  B SER   A 167 ? 0.2989 0.3240 0.2922 -0.0124 0.0181  0.0101  167 SER   A CA  
3812 C C   A SER   A 167 ? 0.1823 0.3621 0.2845 0.0099  -0.0078 0.0500  167 SER   A C   
3813 C C   B SER   A 167 ? 0.3079 0.3307 0.3019 -0.0140 0.0123  0.0069  167 SER   A C   
3814 O O   A SER   A 167 ? 0.2009 0.3635 0.2813 0.0160  -0.0200 0.0421  167 SER   A O   
3815 O O   B SER   A 167 ? 0.3058 0.3297 0.2956 -0.0142 0.0082  0.0088  167 SER   A O   
3816 C CB  A SER   A 167 ? 0.1900 0.3697 0.2925 0.0151  -0.0151 0.0620  167 SER   A CB  
3817 C CB  B SER   A 167 ? 0.3015 0.3281 0.2986 -0.0117 0.0166  0.0185  167 SER   A CB  
3818 O OG  A SER   A 167 ? 0.1944 0.3734 0.2932 0.0187  -0.0041 0.0642  167 SER   A OG  
3819 O OG  B SER   A 167 ? 0.3034 0.3317 0.3075 -0.0095 0.0152  0.0213  167 SER   A OG  
3830 N N   A PHE   A 168 ? 0.1772 0.3563 0.2772 0.0141  0.0004  0.0457  168 PHE   A N   
3831 N N   B PHE   A 168 ? 0.3206 0.3392 0.3251 -0.0138 0.0095  0.0012  168 PHE   A N   
3832 C CA  A PHE   A 168 ? 0.1737 0.3514 0.2854 0.0068  0.0099  0.0351  168 PHE   A CA  
3833 C CA  B PHE   A 168 ? 0.3374 0.3469 0.3481 -0.0130 0.0038  -0.0049 168 PHE   A CA  
3834 C C   A PHE   A 168 ? 0.1929 0.3694 0.3216 -0.0094 0.0392  0.0190  168 PHE   A C   
3835 C C   B PHE   A 168 ? 0.3618 0.3667 0.3929 -0.0072 -0.0005 -0.0059 168 PHE   A C   
3836 O O   A PHE   A 168 ? 0.2087 0.3685 0.3566 -0.0220 0.0389  0.0338  168 PHE   A O   
3837 O O   B PHE   A 168 ? 0.3662 0.3669 0.4055 -0.0083 -0.0017 -0.0084 168 PHE   A O   
3838 C CB  A PHE   A 168 ? 0.1675 0.3328 0.2673 0.0061  -0.0103 0.0375  168 PHE   A CB  
3839 C CB  B PHE   A 168 ? 0.3267 0.3340 0.3246 -0.0162 0.0049  -0.0085 168 PHE   A CB  
3840 C CG  A PHE   A 168 ? 0.1600 0.3160 0.2443 -0.0079 -0.0117 0.0419  168 PHE   A CG  
3841 C CG  B PHE   A 168 ? 0.3176 0.3211 0.3017 -0.0193 0.0045  -0.0112 168 PHE   A CG  
3842 C CD1 A PHE   A 168 ? 0.1572 0.3135 0.2464 -0.0149 -0.0155 0.0556  168 PHE   A CD1 
3843 C CD1 B PHE   A 168 ? 0.3124 0.3173 0.2932 -0.0203 0.0024  -0.0110 168 PHE   A CD1 
3844 C CD2 A PHE   A 168 ? 0.1509 0.3061 0.2302 -0.0065 0.0093  0.0350  168 PHE   A CD2 
3845 C CD2 B PHE   A 168 ? 0.3146 0.3139 0.2871 -0.0211 0.0045  -0.0153 168 PHE   A CD2 
3846 C CE1 A PHE   A 168 ? 0.1480 0.3086 0.2393 -0.0239 -0.0128 0.0662  168 PHE   A CE1 
3847 C CE1 B PHE   A 168 ? 0.3104 0.3134 0.2863 -0.0217 0.0022  -0.0123 168 PHE   A CE1 
3848 C CE2 A PHE   A 168 ? 0.1588 0.3010 0.2342 -0.0125 0.0056  0.0466  168 PHE   A CE2 
3849 C CE2 B PHE   A 168 ? 0.3125 0.3110 0.2815 -0.0236 0.0027  -0.0148 168 PHE   A CE2 
3850 C CZ  A PHE   A 168 ? 0.1549 0.3037 0.2385 -0.0212 -0.0028 0.0617  168 PHE   A CZ  
3851 C CZ  B PHE   A 168 ? 0.3105 0.3117 0.2799 -0.0229 0.0021  -0.0136 168 PHE   A CZ  
3870 N N   A LEU   A 169 ? 0.2235 0.3901 0.3666 -0.0146 0.0422  -0.0187 169 LEU   A N   
3871 N N   B LEU   A 169 ? 0.3789 0.3849 0.4202 -0.0011 -0.0023 -0.0068 169 LEU   A N   
3872 C CA  A LEU   A 169 ? 0.2849 0.4157 0.4424 -0.0147 0.0155  -0.0423 169 LEU   A CA  
3873 C CA  B LEU   A 169 ? 0.3931 0.4013 0.4388 0.0059  -0.0036 -0.0086 169 LEU   A CA  
3874 C C   A LEU   A 169 ? 0.3095 0.4215 0.4904 -0.0185 0.0098  -0.0422 169 LEU   A C   
3875 C C   B LEU   A 169 ? 0.3981 0.4072 0.4454 0.0067  0.0024  -0.0064 169 LEU   A C   
3876 O O   A LEU   A 169 ? 0.3151 0.4212 0.5090 -0.0213 0.0159  -0.0473 169 LEU   A O   
3877 O O   B LEU   A 169 ? 0.4017 0.4104 0.4511 0.0080  0.0057  -0.0044 169 LEU   A O   
3878 C CB  A LEU   A 169 ? 0.3206 0.4319 0.4573 -0.0159 -0.0040 -0.0598 169 LEU   A CB  
3879 C CB  B LEU   A 169 ? 0.4020 0.4099 0.4468 0.0127  -0.0118 -0.0128 169 LEU   A CB  
3880 C CG  A LEU   A 169 ? 0.3535 0.4446 0.4657 -0.0179 -0.0172 -0.0806 169 LEU   A CG  
3881 C CG  B LEU   A 169 ? 0.4094 0.4163 0.4521 0.0180  -0.0181 -0.0164 169 LEU   A CG  
3882 C CD1 A LEU   A 169 ? 0.3672 0.4498 0.4730 -0.0157 -0.0235 -0.0870 169 LEU   A CD1 
3883 C CD1 B LEU   A 169 ? 0.4124 0.4181 0.4535 0.0204  -0.0202 -0.0172 169 LEU   A CD1 
3884 C CD2 A LEU   A 169 ? 0.3637 0.4489 0.4653 -0.0217 -0.0202 -0.0889 169 LEU   A CD2 
3885 C CD2 B LEU   A 169 ? 0.4123 0.4186 0.4530 0.0201  -0.0198 -0.0187 169 LEU   A CD2 
3886 O OXT A LEU   A 169 ? 0.3107 0.4249 0.5007 -0.0174 0.0056  -0.0432 169 LEU   A OXT 
3887 O OXT B LEU   A 169 ? 0.3979 0.4082 0.4457 0.0068  0.0031  -0.0043 169 LEU   A OXT 
3910 N N   A SER   B 1   ? 0.3597 0.3243 0.3451 -0.1093 -0.0787 0.0198  1   SER   B N   
3911 N N   B SER   B 1   ? 0.3436 0.3383 0.3372 -0.0610 -0.0420 0.0137  1   SER   B N   
3912 C CA  A SER   B 1   ? 0.3486 0.3295 0.3504 -0.1171 -0.0926 0.0131  1   SER   B CA  
3913 C CA  B SER   B 1   ? 0.3385 0.3405 0.3388 -0.0632 -0.0447 0.0148  1   SER   B CA  
3914 C C   A SER   B 1   ? 0.3226 0.3321 0.3447 -0.1176 -0.1059 0.0346  1   SER   B C   
3915 C C   B SER   B 1   ? 0.3271 0.3410 0.3342 -0.0630 -0.0539 0.0305  1   SER   B C   
3916 O O   A SER   B 1   ? 0.3358 0.3359 0.3342 -0.1012 -0.0982 0.0375  1   SER   B O   
3917 O O   B SER   B 1   ? 0.3309 0.3417 0.3257 -0.0598 -0.0517 0.0273  1   SER   B O   
3918 C CB  A SER   B 1   ? 0.3621 0.3312 0.3742 -0.1189 -0.0810 -0.0135 1   SER   B CB  
3919 C CB  B SER   B 1   ? 0.3430 0.3418 0.3531 -0.0636 -0.0363 0.0008  1   SER   B CB  
3920 O OG  A SER   B 1   ? 0.3783 0.3422 0.4164 -0.1155 -0.0614 -0.0266 1   SER   B OG  
3921 O OG  B SER   B 1   ? 0.3478 0.3465 0.3702 -0.0637 -0.0320 -0.0082 1   SER   B OG  
3936 N N   A MET   B 2   ? 0.2975 0.3342 0.3532 -0.1215 -0.0997 0.0773  2   MET   B N   
3937 N N   B MET   B 2   ? 0.3142 0.3412 0.3364 -0.0639 -0.0614 0.0579  2   MET   B N   
3938 C CA  A MET   B 2   ? 0.2837 0.3448 0.3718 -0.1028 -0.0933 0.1037  2   MET   B CA  
3939 C CA  B MET   B 2   ? 0.3002 0.3421 0.3427 -0.0618 -0.0696 0.0833  2   MET   B CA  
3940 C C   A MET   B 2   ? 0.2531 0.3326 0.3415 -0.0806 -0.1011 0.1347  2   MET   B C   
3941 C C   B MET   B 2   ? 0.2681 0.3276 0.3227 -0.0691 -0.0803 0.1153  2   MET   B C   
3942 O O   A MET   B 2   ? 0.2482 0.3443 0.3456 -0.0624 -0.1203 0.1414  2   MET   B O   
3943 O O   B MET   B 2   ? 0.2705 0.3338 0.3234 -0.0639 -0.0830 0.1150  2   MET   B O   
3944 C CB  A MET   B 2   ? 0.3149 0.3768 0.4541 -0.0875 -0.0638 0.0781  2   MET   B CB  
3945 C CB  B MET   B 2   ? 0.3191 0.3591 0.3799 -0.0485 -0.0621 0.0726  2   MET   B CB  
3946 C CG  A MET   B 2   ? 0.3469 0.4033 0.5309 -0.0683 -0.0364 0.0628  2   MET   B CG  
3947 C CG  B MET   B 2   ? 0.3347 0.3731 0.4093 -0.0356 -0.0578 0.0676  2   MET   B CG  
3948 S SD  A MET   B 2   ? 0.3776 0.4339 0.6037 -0.0485 -0.0150 0.0476  2   MET   B SD  
3949 S SD  B MET   B 2   ? 0.3474 0.3861 0.4354 -0.0231 -0.0576 0.0611  2   MET   B SD  
3950 C CE  A MET   B 2   ? 0.3794 0.4420 0.6126 -0.0505 -0.0025 0.0431  2   MET   B CE  
3951 C CE  B MET   B 2   ? 0.3493 0.3880 0.4422 -0.0244 -0.0514 0.0571  2   MET   B CE  
3970 N N   . VAL   B 3   ? 0.2340 0.3028 0.3049 -0.0829 -0.0873 0.1421  3   VAL   B N   
3971 C CA  . VAL   B 3   ? 0.2200 0.2695 0.2991 -0.0829 -0.0818 0.1185  3   VAL   B CA  
3972 C C   . VAL   B 3   ? 0.2073 0.2566 0.2624 -0.0730 -0.0711 0.1039  3   VAL   B C   
3973 O O   . VAL   B 3   ? 0.2045 0.2810 0.2696 -0.0687 -0.0704 0.1081  3   VAL   B O   
3974 C CB  . VAL   B 3   ? 0.2358 0.2648 0.3610 -0.0831 -0.0737 0.0911  3   VAL   B CB  
3975 C CG1 . VAL   B 3   ? 0.2488 0.2595 0.3877 -0.0820 -0.0702 0.0881  3   VAL   B CG1 
3976 C CG2 . VAL   B 3   ? 0.2365 0.2661 0.3835 -0.0811 -0.0558 0.0958  3   VAL   B CG2 
3987 N N   . ASN   B 4   ? 0.2021 0.2261 0.2300 -0.0715 -0.0664 0.0772  4   ASN   B N   
3988 C CA  . ASN   B 4   ? 0.2018 0.2277 0.1939 -0.0676 -0.0610 0.0501  4   ASN   B CA  
3989 C C   . ASN   B 4   ? 0.1982 0.2408 0.1996 -0.0664 -0.0518 0.0387  4   ASN   B C   
3990 O O   . ASN   B 4   ? 0.1988 0.2509 0.2193 -0.0604 -0.0430 0.0233  4   ASN   B O   
3991 C CB  . ASN   B 4   ? 0.2051 0.2221 0.1840 -0.0599 -0.0641 0.0435  4   ASN   B CB  
3992 C CG  . ASN   B 4   ? 0.2037 0.2025 0.1736 -0.0563 -0.0573 0.0395  4   ASN   B CG  
3993 O OD1 . ASN   B 4   ? 0.2088 0.1923 0.1788 -0.0531 -0.0546 0.0376  4   ASN   B OD1 
3994 N ND2 . ASN   B 4   ? 0.2281 0.2076 0.1839 -0.0339 -0.0394 0.0299  4   ASN   B ND2 
4001 N N   . SER   B 5   ? 0.2082 0.2514 0.2124 -0.0656 -0.0449 0.0308  5   SER   B N   
4002 C CA  . SER   B 5   ? 0.2265 0.2877 0.2302 -0.0586 -0.0255 0.0238  5   SER   B CA  
4003 C C   . SER   B 5   ? 0.2497 0.2990 0.2650 -0.0789 0.0071  0.0258  5   SER   B C   
4004 O O   . SER   B 5   ? 0.2669 0.2979 0.3445 -0.0668 0.0519  0.0233  5   SER   B O   
4005 C CB  . SER   B 5   ? 0.2396 0.3077 0.2479 -0.0407 -0.0129 0.0368  5   SER   B CB  
4006 O OG  . SER   B 5   ? 0.2744 0.3413 0.3124 -0.0260 -0.0138 0.0478  5   SER   B OG  
4012 N N   . PHE   B 6   ? 0.2785 0.3238 0.2458 -0.0900 0.0293  0.0407  6   PHE   B N   
4013 C CA  . PHE   B 6   ? 0.2975 0.3305 0.2087 -0.1090 0.0376  0.0266  6   PHE   B CA  
4014 C C   . PHE   B 6   ? 0.3530 0.3599 0.2776 -0.1118 0.0629  -0.0084 6   PHE   B C   
4015 O O   . PHE   B 6   ? 0.3662 0.3849 0.3066 -0.1017 0.0500  -0.0130 6   PHE   B O   
4016 C CB  . PHE   B 6   ? 0.2705 0.3107 0.1919 -0.1014 0.0049  0.0207  6   PHE   B CB  
4017 C CG  . PHE   B 6   ? 0.2421 0.2836 0.1926 -0.0915 -0.0139 0.0147  6   PHE   B CG  
4018 C CD1 . PHE   B 6   ? 0.2410 0.2559 0.1766 -0.0845 -0.0281 0.0157  6   PHE   B CD1 
4019 C CD2 . PHE   B 6   ? 0.2181 0.2797 0.1877 -0.0791 -0.0129 0.0477  6   PHE   B CD2 
4020 C CE1 . PHE   B 6   ? 0.2377 0.2348 0.1793 -0.0697 -0.0294 0.0260  6   PHE   B CE1 
4021 C CE2 . PHE   B 6   ? 0.2197 0.2649 0.2101 -0.0662 -0.0061 0.0520  6   PHE   B CE2 
4022 C CZ  . PHE   B 6   ? 0.2215 0.2427 0.1900 -0.0621 -0.0213 0.0401  6   PHE   B CZ  
4032 N N   A SER   B 7   ? 0.3868 0.3513 0.2967 -0.1265 0.0972  -0.0351 7   SER   B N   
4033 N N   B SER   B 7   ? 0.3630 0.3555 0.3034 -0.1136 0.0667  -0.0191 7   SER   B N   
4034 C CA  A SER   B 7   ? 0.4211 0.3606 0.3469 -0.1227 0.1241  -0.0432 7   SER   B CA  
4035 C CA  B SER   B 7   ? 0.3731 0.3573 0.3415 -0.1081 0.0684  -0.0227 7   SER   B CA  
4036 C C   A SER   B 7   ? 0.4242 0.3486 0.3309 -0.1253 0.1434  -0.0622 7   SER   B C   
4037 C C   B SER   B 7   ? 0.3675 0.3488 0.3399 -0.1052 0.0707  -0.0300 7   SER   B C   
4038 O O   A SER   B 7   ? 0.4370 0.3505 0.3477 -0.1305 0.1447  -0.0643 7   SER   B O   
4039 O O   B SER   B 7   ? 0.3733 0.3479 0.3473 -0.1095 0.0694  -0.0335 7   SER   B O   
4040 C CB  A SER   B 7   ? 0.4421 0.3780 0.4137 -0.1155 0.1345  -0.0386 7   SER   B CB  
4041 C CB  B SER   B 7   ? 0.3835 0.3646 0.3787 -0.1057 0.0698  -0.0207 7   SER   B CB  
4042 O OG  A SER   B 7   ? 0.4568 0.3947 0.4650 -0.1097 0.1404  -0.0374 7   SER   B OG  
4043 O OG  B SER   B 7   ? 0.3899 0.3696 0.4029 -0.1043 0.0706  -0.0193 7   SER   B OG  
4054 N N   A GLY   B 8   ? 0.4179 0.3379 0.3256 -0.1124 0.1491  -0.0750 8   GLY   B N   
4055 N N   B GLY   B 8   ? 0.3575 0.3415 0.3346 -0.0937 0.0686  -0.0333 8   GLY   B N   
4056 C CA  A GLY   B 8   ? 0.4028 0.3184 0.3161 -0.1090 0.1556  -0.0727 8   GLY   B CA  
4057 C CA  B GLY   B 8   ? 0.3453 0.3314 0.3257 -0.0852 0.0673  -0.0307 8   GLY   B CA  
4058 C C   A GLY   B 8   ? 0.3884 0.2912 0.3066 -0.1080 0.1526  -0.0724 8   GLY   B C   
4059 C C   B GLY   B 8   ? 0.3345 0.3194 0.3156 -0.0776 0.0645  -0.0298 8   GLY   B C   
4060 O O   A GLY   B 8   ? 0.4015 0.3006 0.3448 -0.0959 0.1512  -0.0817 8   GLY   B O   
4061 O O   B GLY   B 8   ? 0.3417 0.3231 0.3316 -0.0716 0.0651  -0.0326 8   GLY   B O   
4068 N N   A TYR   B 9   ? 0.3727 0.2622 0.2724 -0.1042 0.1191  -0.0792 9   TYR   B N   
4069 N N   B TYR   B 9   ? 0.3186 0.3048 0.2892 -0.0750 0.0519  -0.0328 9   TYR   B N   
4070 C CA  A TYR   B 9   ? 0.3546 0.2329 0.2411 -0.0966 0.0858  -0.0651 9   TYR   B CA  
4071 C CA  B TYR   B 9   ? 0.3023 0.2908 0.2615 -0.0723 0.0385  -0.0329 9   TYR   B CA  
4072 C C   A TYR   B 9   ? 0.3474 0.2284 0.2323 -0.0943 0.0502  -0.0528 9   TYR   B C   
4073 C C   B TYR   B 9   ? 0.3030 0.2892 0.2549 -0.0674 0.0231  -0.0316 9   TYR   B C   
4074 O O   A TYR   B 9   ? 0.3520 0.2400 0.2617 -0.0932 0.0516  -0.0434 9   TYR   B O   
4075 O O   B TYR   B 9   ? 0.3031 0.2923 0.2664 -0.0655 0.0250  -0.0324 9   TYR   B O   
4076 C CB  A TYR   B 9   ? 0.3494 0.2105 0.2402 -0.0909 0.0787  -0.0663 9   TYR   B CB  
4077 C CB  B TYR   B 9   ? 0.2871 0.2799 0.2488 -0.0739 0.0369  -0.0352 9   TYR   B CB  
4078 C CG  A TYR   B 9   ? 0.3430 0.1980 0.2392 -0.0993 0.0721  -0.0669 9   TYR   B CG  
4079 C CG  B TYR   B 9   ? 0.2723 0.2713 0.2390 -0.0795 0.0339  -0.0355 9   TYR   B CG  
4080 C CD1 A TYR   B 9   ? 0.3425 0.1979 0.2499 -0.1116 0.0752  -0.0576 9   TYR   B CD1 
4081 C CD1 B TYR   B 9   ? 0.2661 0.2690 0.2396 -0.0840 0.0362  -0.0345 9   TYR   B CD1 
4082 C CD2 A TYR   B 9   ? 0.3335 0.1991 0.2260 -0.0925 0.0661  -0.0708 9   TYR   B CD2 
4083 C CD2 B TYR   B 9   ? 0.2624 0.2680 0.2273 -0.0819 0.0302  -0.0387 9   TYR   B CD2 
4084 C CE1 A TYR   B 9   ? 0.3386 0.2094 0.2518 -0.1077 0.0761  -0.0675 9   TYR   B CE1 
4085 C CE1 B TYR   B 9   ? 0.2590 0.2700 0.2403 -0.0859 0.0343  -0.0365 9   TYR   B CE1 
4086 C CE2 A TYR   B 9   ? 0.3332 0.1991 0.2346 -0.0932 0.0664  -0.0651 9   TYR   B CE2 
4087 C CE2 B TYR   B 9   ? 0.2572 0.2669 0.2274 -0.0837 0.0286  -0.0377 9   TYR   B CE2 
4088 C CZ  A TYR   B 9   ? 0.3353 0.2097 0.2453 -0.0982 0.0685  -0.0772 9   TYR   B CZ  
4089 C CZ  B TYR   B 9   ? 0.2555 0.2699 0.2330 -0.0858 0.0278  -0.0401 9   TYR   B CZ  
4090 O OH  A TYR   B 9   ? 0.3324 0.2148 0.2607 -0.1031 0.0692  -0.0855 9   TYR   B OH  
4091 O OH  B TYR   B 9   ? 0.2513 0.2738 0.2406 -0.0888 0.0240  -0.0396 9   TYR   B OH  
4110 N N   A LEU   B 10  ? 0.3355 0.2070 0.2179 -0.1018 0.0222  -0.0497 10  LEU   B N   
4111 N N   B LEU   B 10  ? 0.3034 0.2848 0.2490 -0.0671 0.0101  -0.0286 10  LEU   B N   
4112 C CA  A LEU   B 10  ? 0.3365 0.2088 0.2113 -0.1092 -0.0159 -0.0398 10  LEU   B CA  
4113 C CA  B LEU   B 10  ? 0.3084 0.2850 0.2499 -0.0692 -0.0052 -0.0220 10  LEU   B CA  
4114 C C   A LEU   B 10  ? 0.3175 0.2156 0.2086 -0.1047 -0.0326 -0.0332 10  LEU   B C   
4115 C C   B LEU   B 10  ? 0.3028 0.2846 0.2482 -0.0672 -0.0139 -0.0221 10  LEU   B C   
4116 O O   A LEU   B 10  ? 0.2956 0.2197 0.2105 -0.0972 -0.0253 -0.0218 10  LEU   B O   
4117 O O   B LEU   B 10  ? 0.2936 0.2862 0.2412 -0.0648 -0.0124 -0.0209 10  LEU   B O   
4118 C CB  A LEU   B 10  ? 0.3605 0.2033 0.2339 -0.1097 -0.0309 -0.0212 10  LEU   B CB  
4119 C CB  B LEU   B 10  ? 0.3208 0.2867 0.2633 -0.0697 -0.0085 -0.0119 10  LEU   B CB  
4120 C CG  A LEU   B 10  ? 0.3807 0.2061 0.2681 -0.1081 -0.0604 -0.0125 10  LEU   B CG  
4121 C CG  B LEU   B 10  ? 0.3311 0.2893 0.2801 -0.0693 -0.0150 -0.0048 10  LEU   B CG  
4122 C CD1 A LEU   B 10  ? 0.3950 0.2151 0.2879 -0.0989 -0.0606 -0.0091 10  LEU   B CD1 
4123 C CD1 B LEU   B 10  ? 0.3348 0.2910 0.2898 -0.0669 -0.0142 -0.0038 10  LEU   B CD1 
4124 C CD2 A LEU   B 10  ? 0.3869 0.2111 0.2933 -0.1085 -0.0535 0.0129  10  LEU   B CD2 
4125 C CD2 B LEU   B 10  ? 0.3345 0.2910 0.2880 -0.0702 -0.0137 0.0013  10  LEU   B CD2 
4148 N N   A LYS   B 11  ? 0.3321 0.2398 0.2172 -0.0939 -0.0375 -0.0237 11  LYS   B N   
4149 N N   B LYS   B 11  ? 0.3100 0.2870 0.2605 -0.0646 -0.0204 -0.0217 11  LYS   B N   
4150 C CA  A LYS   B 11  ? 0.3468 0.2656 0.2621 -0.0805 -0.0417 -0.0259 11  LYS   B CA  
4151 C CA  B LYS   B 11  ? 0.3184 0.2896 0.2860 -0.0612 -0.0266 -0.0241 11  LYS   B CA  
4152 C C   A LYS   B 11  ? 0.3191 0.2441 0.2623 -0.0961 -0.0425 -0.0365 11  LYS   B C   
4153 C C   B LYS   B 11  ? 0.2996 0.2630 0.2658 -0.0745 -0.0348 -0.0305 11  LYS   B C   
4154 O O   A LYS   B 11  ? 0.3348 0.2550 0.2865 -0.1079 -0.0519 -0.0695 11  LYS   B O   
4155 O O   B LYS   B 11  ? 0.3015 0.2715 0.2599 -0.0733 -0.0458 -0.0414 11  LYS   B O   
4156 C CB  A LYS   B 11  ? 0.3844 0.3121 0.3332 -0.0540 -0.0460 -0.0348 11  LYS   B CB  
4157 C CB  B LYS   B 11  ? 0.3437 0.3174 0.3405 -0.0452 -0.0266 -0.0254 11  LYS   B CB  
4158 C CG  A LYS   B 11  ? 0.4172 0.3457 0.4081 -0.0351 -0.0482 -0.0393 11  LYS   B CG  
4159 C CG  B LYS   B 11  ? 0.3654 0.3386 0.3973 -0.0333 -0.0266 -0.0254 11  LYS   B CG  
4160 C CD  A LYS   B 11  ? 0.4422 0.3686 0.4668 -0.0219 -0.0481 -0.0430 11  LYS   B CD  
4161 C CD  B LYS   B 11  ? 0.3824 0.3536 0.4441 -0.0247 -0.0264 -0.0250 11  LYS   B CD  
4162 C CE  A LYS   B 11  ? 0.4592 0.3843 0.5109 -0.0138 -0.0445 -0.0455 11  LYS   B CE  
4163 C CE  B LYS   B 11  ? 0.3937 0.3641 0.4791 -0.0198 -0.0252 -0.0245 11  LYS   B CE  
4164 N NZ  A LYS   B 11  ? 0.4687 0.3936 0.5348 -0.0092 -0.0443 -0.0446 11  LYS   B NZ  
4165 N NZ  B LYS   B 11  ? 0.3993 0.3700 0.4979 -0.0171 -0.0248 -0.0233 11  LYS   B NZ  
4192 N N   . LEU   B 12  ? 0.2769 0.2313 0.2609 -0.0843 -0.0391 -0.0338 12  LEU   B N   
4193 C CA  . LEU   B 12  ? 0.2484 0.2038 0.2713 -0.0685 -0.0266 -0.0336 12  LEU   B CA  
4194 C C   . LEU   B 12  ? 0.2335 0.2071 0.2865 -0.0651 -0.0410 -0.0262 12  LEU   B C   
4195 O O   . LEU   B 12  ? 0.2285 0.2046 0.3152 -0.0680 -0.0610 -0.0248 12  LEU   B O   
4196 C CB  . LEU   B 12  ? 0.2488 0.1797 0.2679 -0.0516 -0.0162 -0.0277 12  LEU   B CB  
4197 C CG  . LEU   B 12  ? 0.2576 0.1715 0.2703 -0.0496 -0.0104 -0.0210 12  LEU   B CG  
4198 C CD1 . LEU   B 12  ? 0.2712 0.1715 0.2659 -0.0342 -0.0172 0.0052  12  LEU   B CD1 
4199 C CD2 . LEU   B 12  ? 0.2622 0.1817 0.2804 -0.0451 -0.0072 -0.0316 12  LEU   B CD2 
4212 N N   . THR   B 13  ? 0.2311 0.2128 0.2830 -0.0668 -0.0436 -0.0397 13  THR   B N   
4213 C CA  . THR   B 13  ? 0.2341 0.2221 0.2785 -0.0716 -0.0651 -0.0195 13  THR   B CA  
4214 C C   . THR   B 13  ? 0.2852 0.2448 0.2987 -0.0836 -0.0834 -0.0135 13  THR   B C   
4215 O O   . THR   B 13  ? 0.3074 0.2470 0.3101 -0.0803 -0.0550 -0.0181 13  THR   B O   
4216 C CB  . THR   B 13  ? 0.2140 0.2128 0.2801 -0.0629 -0.0590 -0.0108 13  THR   B CB  
4217 O OG1 . THR   B 13  ? 0.2063 0.1964 0.2834 -0.0496 -0.0421 -0.0106 13  THR   B OG1 
4218 C CG2 . THR   B 13  ? 0.2218 0.2251 0.2796 -0.0554 -0.0501 0.0012  13  THR   B CG2 
4226 N N   A ASP   B 14  ? 0.3000 0.2583 0.3047 -0.0977 -0.1209 0.0004  14  ASP   B N   
4227 N N   B ASP   B 14  ? 0.2964 0.2569 0.3103 -0.0855 -0.0907 -0.0030 14  ASP   B N   
4228 C CA  A ASP   B 14  ? 0.3158 0.2765 0.3297 -0.0935 -0.1290 0.0180  14  ASP   B CA  
4229 C CA  B ASP   B 14  ? 0.3064 0.2688 0.3281 -0.0814 -0.0926 0.0072  14  ASP   B CA  
4230 C C   A ASP   B 14  ? 0.3018 0.2573 0.2870 -0.0950 -0.1153 0.0233  14  ASP   B C   
4231 C C   B ASP   B 14  ? 0.2901 0.2492 0.2889 -0.0820 -0.1006 0.0158  14  ASP   B C   
4232 O O   A ASP   B 14  ? 0.3303 0.2771 0.2937 -0.0951 -0.0978 0.0362  14  ASP   B O   
4233 O O   B ASP   B 14  ? 0.3038 0.2537 0.2861 -0.0819 -0.0948 0.0202  14  ASP   B O   
4234 C CB  A ASP   B 14  ? 0.3412 0.3200 0.4139 -0.0865 -0.1366 0.0207  14  ASP   B CB  
4235 C CB  B ASP   B 14  ? 0.3296 0.3005 0.3895 -0.0754 -0.0837 0.0079  14  ASP   B CB  
4236 C CG  A ASP   B 14  ? 0.3683 0.3570 0.4976 -0.0816 -0.1287 0.0108  14  ASP   B CG  
4237 C CG  B ASP   B 14  ? 0.3493 0.3244 0.4440 -0.0692 -0.0742 0.0036  14  ASP   B CG  
4238 O OD1 A ASP   B 14  ? 0.3827 0.3735 0.5190 -0.0810 -0.1280 -0.0030 14  ASP   B OD1 
4239 O OD1 B ASP   B 14  ? 0.3559 0.3326 0.4598 -0.0666 -0.0712 -0.0015 14  ASP   B OD1 
4240 O OD2 A ASP   B 14  ? 0.3747 0.3707 0.5386 -0.0815 -0.1239 0.0118  14  ASP   B OD2 
4241 O OD2 B ASP   B 14  ? 0.3565 0.3334 0.4678 -0.0690 -0.0713 0.0030  14  ASP   B OD2 
4250 N N   . ASN   B 15  ? 0.2607 0.2262 0.2656 -0.0746 -0.1088 0.0228  15  ASN   B N   
4251 C CA  . ASN   B 15  ? 0.2139 0.1873 0.2512 -0.0481 -0.0732 0.0110  15  ASN   B CA  
4252 C C   . ASN   B 15  ? 0.1907 0.1696 0.2392 -0.0318 -0.0542 0.0014  15  ASN   B C   
4253 O O   . ASN   B 15  ? 0.1864 0.1582 0.2538 -0.0321 -0.0531 -0.0110 15  ASN   B O   
4254 C CB  . ASN   B 15  ? 0.2002 0.1797 0.2631 -0.0216 -0.0696 0.0148  15  ASN   B CB  
4255 C CG  . ASN   B 15  ? 0.1803 0.1772 0.2779 -0.0269 -0.0453 0.0142  15  ASN   B CG  
4256 O OD1 . ASN   B 15  ? 0.1869 0.2120 0.3089 -0.0470 -0.0434 0.0168  15  ASN   B OD1 
4257 N ND2 . ASN   B 15  ? 0.1834 0.1571 0.2634 -0.0149 -0.0176 -0.0073 15  ASN   B ND2 
4265 N N   . VAL   B 16  ? 0.1890 0.1620 0.2390 -0.0382 -0.0629 -0.0025 16  VAL   B N   
4266 C CA  . VAL   B 16  ? 0.1856 0.1639 0.2375 -0.0313 -0.0446 -0.0209 16  VAL   B CA  
4267 C C   . VAL   B 16  ? 0.1806 0.1813 0.2246 -0.0418 -0.0433 -0.0035 16  VAL   B C   
4268 O O   . VAL   B 16  ? 0.1828 0.1949 0.2453 -0.0369 -0.0400 -0.0283 16  VAL   B O   
4269 C CB  . VAL   B 16  ? 0.1904 0.1610 0.2468 -0.0161 -0.0276 -0.0173 16  VAL   B CB  
4270 C CG1 . VAL   B 16  ? 0.1994 0.1602 0.2422 -0.0051 -0.0208 -0.0176 16  VAL   B CG1 
4271 C CG2 . VAL   B 16  ? 0.1936 0.1665 0.2718 -0.0093 -0.0206 -0.0170 16  VAL   B CG2 
4281 N N   . TYR   B 17  ? 0.1895 0.1910 0.2250 -0.0358 -0.0318 -0.0112 17  TYR   B N   
4282 C CA  . TYR   B 17  ? 0.1997 0.2050 0.2180 -0.0405 -0.0372 0.0054  17  TYR   B CA  
4283 C C   . TYR   B 17  ? 0.1937 0.1730 0.2057 -0.0397 -0.0212 -0.0105 17  TYR   B C   
4284 O O   . TYR   B 17  ? 0.1938 0.1821 0.2219 -0.0354 -0.0292 -0.0390 17  TYR   B O   
4285 C CB  . TYR   B 17  ? 0.2443 0.2618 0.2564 -0.0243 -0.0417 0.0399  17  TYR   B CB  
4286 C CG  . TYR   B 17  ? 0.2834 0.3240 0.3105 -0.0114 -0.0584 0.0520  17  TYR   B CG  
4287 C CD1 . TYR   B 17  ? 0.3062 0.3468 0.3420 -0.0094 -0.0708 0.0585  17  TYR   B CD1 
4288 C CD2 . TYR   B 17  ? 0.3079 0.3535 0.3432 0.0017  -0.0673 0.0569  17  TYR   B CD2 
4289 C CE1 . TYR   B 17  ? 0.3272 0.3712 0.3670 -0.0004 -0.0839 0.0632  17  TYR   B CE1 
4290 C CE2 . TYR   B 17  ? 0.3271 0.3723 0.3677 0.0140  -0.0889 0.0684  17  TYR   B CE2 
4291 C CZ  . TYR   B 17  ? 0.3403 0.3849 0.3805 0.0138  -0.0936 0.0708  17  TYR   B CZ  
4292 O OH  . TYR   B 17  ? 0.3564 0.4053 0.3982 0.0206  -0.1015 0.0719  17  TYR   B OH  
4302 N N   . ILE   B 18  ? 0.1969 0.1800 0.2009 -0.0388 -0.0141 -0.0238 18  ILE   B N   
4303 C CA  . ILE   B 18  ? 0.2031 0.1729 0.2103 -0.0434 0.0017  -0.0275 18  ILE   B CA  
4304 C C   . ILE   B 18  ? 0.2153 0.1804 0.2084 -0.0541 -0.0025 -0.0392 18  ILE   B C   
4305 O O   . ILE   B 18  ? 0.2364 0.1949 0.2152 -0.0493 0.0061  -0.0462 18  ILE   B O   
4306 C CB  . ILE   B 18  ? 0.2133 0.1762 0.2188 -0.0466 -0.0109 -0.0251 18  ILE   B CB  
4307 C CG1 . ILE   B 18  ? 0.2162 0.1767 0.2207 -0.0439 0.0037  -0.0166 18  ILE   B CG1 
4308 C CG2 . ILE   B 18  ? 0.2122 0.1850 0.2240 -0.0498 -0.0216 -0.0190 18  ILE   B CG2 
4309 C CD1 . ILE   B 18  ? 0.2167 0.2043 0.2336 -0.0436 -0.0207 0.0137  18  ILE   B CD1 
4321 N N   . LYS   B 19  ? 0.2180 0.1770 0.2203 -0.0328 0.0355  -0.0472 19  LYS   B N   
4322 C CA  . LYS   B 19  ? 0.2246 0.1745 0.2478 -0.0339 0.0282  -0.0553 19  LYS   B CA  
4323 C C   . LYS   B 19  ? 0.2047 0.1758 0.2600 -0.0277 0.0348  -0.0702 19  LYS   B C   
4324 O O   . LYS   B 19  ? 0.2061 0.1833 0.2473 -0.0253 0.0311  -0.0607 19  LYS   B O   
4325 C CB  . LYS   B 19  ? 0.2646 0.1980 0.2692 -0.0409 0.0446  -0.0462 19  LYS   B CB  
4326 C CG  . LYS   B 19  ? 0.2993 0.2243 0.3028 -0.0534 0.0626  -0.0530 19  LYS   B CG  
4327 C CD  . LYS   B 19  ? 0.3321 0.2562 0.3229 -0.0599 0.0864  -0.0444 19  LYS   B CD  
4328 C CE  . LYS   B 19  ? 0.3608 0.2827 0.3484 -0.0614 0.0894  -0.0419 19  LYS   B CE  
4329 N NZ  . LYS   B 19  ? 0.3824 0.2973 0.3615 -0.0669 0.0940  -0.0422 19  LYS   B NZ  
4343 N N   . ASN   B 20  ? 0.2072 0.1954 0.2966 -0.0194 0.0396  -0.0773 20  ASN   B N   
4344 C CA  . ASN   B 20  ? 0.2139 0.2050 0.3216 -0.0166 0.0422  -0.0932 20  ASN   B CA  
4345 C C   . ASN   B 20  ? 0.2138 0.2284 0.3138 -0.0210 0.0580  -0.1052 20  ASN   B C   
4346 O O   . ASN   B 20  ? 0.2386 0.2682 0.3342 -0.0317 0.0534  -0.0998 20  ASN   B O   
4347 C CB  . ASN   B 20  ? 0.2466 0.2122 0.3602 0.0129  0.0292  -0.1014 20  ASN   B CB  
4348 C CG  . ASN   B 20  ? 0.2769 0.2247 0.3845 0.0426  0.0273  -0.1115 20  ASN   B CG  
4349 O OD1 . ASN   B 20  ? 0.3083 0.2495 0.4077 0.0542  0.0214  -0.1098 20  ASN   B OD1 
4350 N ND2 . ASN   B 20  ? 0.2711 0.2273 0.3824 0.0444  0.0125  -0.1095 20  ASN   B ND2 
4357 N N   . ALA   B 21  ? 0.2158 0.2153 0.3088 -0.0293 0.0608  -0.0937 21  ALA   B N   
4358 C CA  . ALA   B 21  ? 0.2264 0.2212 0.3210 -0.0391 0.0490  -0.0729 21  ALA   B CA  
4359 C C   . ALA   B 21  ? 0.2213 0.1994 0.3021 -0.0318 0.0476  -0.0583 21  ALA   B C   
4360 O O   . ALA   B 21  ? 0.2261 0.1917 0.2916 -0.0380 0.0435  -0.0516 21  ALA   B O   
4361 C CB  . ALA   B 21  ? 0.2428 0.2497 0.3406 -0.0544 0.0415  -0.0495 21  ALA   B CB  
4367 N N   . ASP   B 22  ? 0.2127 0.1818 0.2824 -0.0260 0.0416  -0.0422 22  ASP   B N   
4368 C CA  . ASP   B 22  ? 0.2059 0.1765 0.2758 -0.0124 0.0308  -0.0314 22  ASP   B CA  
4369 C C   . ASP   B 22  ? 0.2003 0.1674 0.2325 -0.0165 0.0234  -0.0175 22  ASP   B C   
4370 O O   . ASP   B 22  ? 0.2031 0.1791 0.2337 -0.0106 0.0123  -0.0162 22  ASP   B O   
4371 C CB  . ASP   B 22  ? 0.2115 0.1815 0.3220 -0.0062 0.0302  -0.0180 22  ASP   B CB  
4372 C CG  . ASP   B 22  ? 0.2017 0.2021 0.3719 0.0044  0.0070  -0.0095 22  ASP   B CG  
4373 O OD1 . ASP   B 22  ? 0.2132 0.1894 0.3630 0.0036  -0.0079 0.0024  22  ASP   B OD1 
4374 O OD2 . ASP   B 22  ? 0.2072 0.2298 0.4314 0.0097  -0.0151 -0.0216 22  ASP   B OD2 
4379 N N   . ILE   B 23  ? 0.1975 0.1529 0.2144 -0.0109 0.0065  0.0114  23  ILE   B N   
4380 C CA  . ILE   B 23  ? 0.1886 0.1582 0.1918 -0.0133 0.0016  0.0050  23  ILE   B CA  
4381 C C   . ILE   B 23  ? 0.1795 0.1669 0.1811 -0.0049 -0.0112 0.0055  23  ILE   B C   
4382 O O   . ILE   B 23  ? 0.1712 0.1637 0.1733 -0.0089 -0.0122 0.0057  23  ILE   B O   
4383 C CB  . ILE   B 23  ? 0.1795 0.1599 0.2046 -0.0204 -0.0010 0.0200  23  ILE   B CB  
4384 C CG1 . ILE   B 23  ? 0.1791 0.1705 0.2249 -0.0111 0.0011  0.0300  23  ILE   B CG1 
4385 C CG2 . ILE   B 23  ? 0.1875 0.1800 0.2137 -0.0148 -0.0027 0.0140  23  ILE   B CG2 
4386 C CD1 . ILE   B 23  ? 0.1911 0.1836 0.2301 -0.0077 0.0038  0.0335  23  ILE   B CD1 
4398 N N   . VAL   B 24  ? 0.1751 0.1605 0.1984 -0.0111 -0.0082 -0.0021 24  VAL   B N   
4399 C CA  . VAL   B 24  ? 0.1772 0.1634 0.2208 -0.0061 -0.0178 -0.0036 24  VAL   B CA  
4400 C C   . VAL   B 24  ? 0.1775 0.1679 0.2252 -0.0079 -0.0109 -0.0019 24  VAL   B C   
4401 O O   . VAL   B 24  ? 0.1773 0.1769 0.2365 -0.0145 -0.0040 0.0069  24  VAL   B O   
4402 C CB  . VAL   B 24  ? 0.1834 0.1730 0.2347 0.0037  -0.0234 -0.0046 24  VAL   B CB  
4403 C CG1 . VAL   B 24  ? 0.1799 0.1784 0.2674 -0.0002 -0.0195 -0.0157 24  VAL   B CG1 
4404 C CG2 . VAL   B 24  ? 0.1964 0.1972 0.2309 0.0103  -0.0273 -0.0125 24  VAL   B CG2 
4414 N N   . GLU   B 25  ? 0.1961 0.1793 0.2293 -0.0079 -0.0024 -0.0049 25  GLU   B N   
4415 C CA  . GLU   B 25  ? 0.2113 0.2124 0.2510 0.0030  0.0104  -0.0106 25  GLU   B CA  
4416 C C   . GLU   B 25  ? 0.2037 0.2086 0.2114 -0.0146 0.0181  -0.0018 25  GLU   B C   
4417 O O   . GLU   B 25  ? 0.2086 0.2231 0.2271 -0.0133 0.0244  0.0007  25  GLU   B O   
4418 C CB  . GLU   B 25  ? 0.2524 0.2605 0.3353 0.0347  0.0304  -0.0205 25  GLU   B CB  
4419 C CG  . GLU   B 25  ? 0.3001 0.3250 0.4539 0.0440  0.0246  -0.0236 25  GLU   B CG  
4420 C CD  . GLU   B 25  ? 0.3492 0.3852 0.5489 0.0423  0.0259  -0.0265 25  GLU   B CD  
4421 O OE1 . GLU   B 25  ? 0.3684 0.4071 0.5823 0.0466  0.0315  -0.0269 25  GLU   B OE1 
4422 O OE2 . GLU   B 25  ? 0.3655 0.4069 0.5831 0.0405  0.0252  -0.0317 25  GLU   B OE2 
4429 N N   A GLU   B 26  ? 0.2000 0.1944 0.1919 -0.0291 0.0216  -0.0039 26  GLU   B N   
4430 N N   B GLU   B 26  ? 0.2022 0.2014 0.2046 -0.0262 0.0144  -0.0017 26  GLU   B N   
4431 C CA  A GLU   B 26  ? 0.2042 0.2128 0.2072 -0.0369 0.0040  0.0013  26  GLU   B CA  
4432 C CA  B GLU   B 26  ? 0.2028 0.2038 0.2120 -0.0335 0.0030  0.0021  26  GLU   B CA  
4433 C C   A GLU   B 26  ? 0.1892 0.2031 0.1943 -0.0289 0.0071  0.0109  26  GLU   B C   
4434 C C   B GLU   B 26  ? 0.1888 0.1968 0.1957 -0.0285 0.0060  0.0121  26  GLU   B C   
4435 O O   A GLU   B 26  ? 0.2077 0.2179 0.2060 -0.0287 0.0069  0.0193  26  GLU   B O   
4436 O O   B GLU   B 26  ? 0.1977 0.2059 0.1967 -0.0281 0.0045  0.0149  26  GLU   B O   
4437 C CB  A GLU   B 26  ? 0.2378 0.2356 0.2399 -0.0466 0.0152  0.0210  26  GLU   B CB  
4438 C CB  B GLU   B 26  ? 0.2217 0.2111 0.2402 -0.0438 0.0016  0.0040  26  GLU   B CB  
4439 C CG  A GLU   B 26  ? 0.2817 0.2741 0.3013 -0.0471 0.0359  0.0126  26  GLU   B CG  
4440 C CG  B GLU   B 26  ? 0.2441 0.2238 0.2788 -0.0529 0.0041  -0.0096 26  GLU   B CG  
4441 C CD  A GLU   B 26  ? 0.3104 0.3000 0.3307 -0.0585 0.0682  -0.0001 26  GLU   B CD  
4442 C CD  B GLU   B 26  ? 0.2576 0.2254 0.2966 -0.0705 0.0068  -0.0336 26  GLU   B CD  
4443 O OE1 A GLU   B 26  ? 0.3325 0.2965 0.3445 -0.0681 0.1023  0.0131  26  GLU   B OE1 
4444 O OE1 B GLU   B 26  ? 0.2671 0.2160 0.3120 -0.0863 0.0181  -0.0495 26  GLU   B OE1 
4445 O OE2 A GLU   B 26  ? 0.3138 0.3216 0.3617 -0.0537 0.0674  0.0040  26  GLU   B OE2 
4446 O OE2 B GLU   B 26  ? 0.2619 0.2351 0.3113 -0.0656 0.0056  -0.0251 26  GLU   B OE2 
4459 N N   . ALA   B 27  ? 0.1712 0.1831 0.1941 -0.0259 0.0088  0.0193  27  ALA   B N   
4460 C CA  . ALA   B 27  ? 0.1709 0.1807 0.2055 -0.0161 0.0005  0.0359  27  ALA   B CA  
4461 C C   . ALA   B 27  ? 0.1717 0.1919 0.2269 -0.0151 0.0114  0.0428  27  ALA   B C   
4462 O O   . ALA   B 27  ? 0.1825 0.1983 0.2394 -0.0038 0.0069  0.0470  27  ALA   B O   
4463 C CB  . ALA   B 27  ? 0.1807 0.1702 0.2094 -0.0188 0.0037  0.0307  27  ALA   B CB  
4470 N N   . LYS   B 28  ? 0.1679 0.2159 0.2666 -0.0249 0.0139  0.0621  28  LYS   B N   
4471 C CA  . LYS   B 28  ? 0.1930 0.2577 0.2904 -0.0108 0.0496  0.0939  28  LYS   B CA  
4472 C C   . LYS   B 28  ? 0.2183 0.2681 0.2693 -0.0008 0.0610  0.0814  28  LYS   B C   
4473 O O   . LYS   B 28  ? 0.2410 0.2732 0.2780 -0.0004 0.0642  0.0700  28  LYS   B O   
4474 C CB  . LYS   B 28  ? 0.2231 0.3043 0.3515 -0.0010 0.0769  0.1190  28  LYS   B CB  
4475 C CG  . LYS   B 28  ? 0.2550 0.3604 0.4061 0.0124  0.0945  0.1288  28  LYS   B CG  
4476 C CD  . LYS   B 28  ? 0.3065 0.4215 0.4744 0.0226  0.1083  0.1299  28  LYS   B CD  
4477 C CE  . LYS   B 28  ? 0.3533 0.4633 0.5263 0.0306  0.1129  0.1345  28  LYS   B CE  
4478 N NZ  . LYS   B 28  ? 0.4027 0.4880 0.5573 0.0358  0.1121  0.1367  28  LYS   B NZ  
4492 N N   . LYS   B 29  ? 0.2339 0.2916 0.2740 0.0152  0.0553  0.0684  29  LYS   B N   
4493 C CA  . LYS   B 29  ? 0.2782 0.3266 0.3010 0.0133  0.0545  0.0650  29  LYS   B CA  
4494 C C   . LYS   B 29  ? 0.2709 0.3201 0.2657 0.0081  0.0376  0.0677  29  LYS   B C   
4495 O O   . LYS   B 29  ? 0.2954 0.3420 0.2827 0.0148  0.0388  0.0693  29  LYS   B O   
4496 C CB  . LYS   B 29  ? 0.3382 0.3689 0.3960 0.0135  0.0544  0.0581  29  LYS   B CB  
4497 C CG  . LYS   B 29  ? 0.3886 0.4062 0.4896 0.0120  0.0546  0.0560  29  LYS   B CG  
4498 C CD  . LYS   B 29  ? 0.4290 0.4330 0.5652 0.0083  0.0611  0.0521  29  LYS   B CD  
4499 C CE  . LYS   B 29  ? 0.4578 0.4500 0.6169 0.0048  0.0690  0.0505  29  LYS   B CE  
4500 N NZ  . LYS   B 29  ? 0.4704 0.4608 0.6426 0.0037  0.0734  0.0479  29  LYS   B NZ  
4514 N N   . VAL   B 30  ? 0.2369 0.2919 0.2498 -0.0118 0.0228  0.0568  30  VAL   B N   
4515 C CA  . VAL   B 30  ? 0.2247 0.2711 0.2828 -0.0300 -0.0158 0.0579  30  VAL   B CA  
4516 C C   . VAL   B 30  ? 0.1998 0.2516 0.2495 -0.0307 -0.0181 0.0646  30  VAL   B C   
4517 O O   . VAL   B 30  ? 0.2108 0.2624 0.2497 -0.0226 -0.0145 0.0720  30  VAL   B O   
4518 C CB  . VAL   B 30  ? 0.2364 0.2714 0.3439 -0.0475 -0.0417 0.0711  30  VAL   B CB  
4519 C CG1 . VAL   B 30  ? 0.2465 0.2894 0.3534 -0.0424 -0.0358 0.0666  30  VAL   B CG1 
4520 C CG2 . VAL   B 30  ? 0.2528 0.2706 0.3662 -0.0568 -0.0474 0.0636  30  VAL   B CG2 
4530 N N   A LYS   B 31  ? 0.1843 0.2229 0.2662 -0.0374 -0.0110 0.0727  31  LYS   B N   
4531 N N   B LYS   B 31  ? 0.2080 0.2435 0.2558 -0.0308 -0.0201 0.0584  31  LYS   B N   
4532 C CA  A LYS   B 31  ? 0.1686 0.2285 0.2961 -0.0459 -0.0110 0.0750  31  LYS   B CA  
4533 C CA  B LYS   B 31  ? 0.2151 0.2437 0.2670 -0.0325 -0.0246 0.0513  31  LYS   B CA  
4534 C C   A LYS   B 31  ? 0.1675 0.1909 0.2665 -0.0477 -0.0271 0.0663  31  LYS   B C   
4535 C C   B LYS   B 31  ? 0.2023 0.2075 0.2363 -0.0373 -0.0366 0.0462  31  LYS   B C   
4536 O O   A LYS   B 31  ? 0.1654 0.1977 0.2827 -0.0364 -0.0286 0.0785  31  LYS   B O   
4537 O O   B LYS   B 31  ? 0.2054 0.2102 0.2247 -0.0343 -0.0425 0.0444  31  LYS   B O   
4538 C CB  A LYS   B 31  ? 0.1776 0.2780 0.3531 -0.0364 0.0159  0.0992  31  LYS   B CB  
4539 C CB  B LYS   B 31  ? 0.2382 0.2788 0.3126 -0.0262 -0.0151 0.0525  31  LYS   B CB  
4540 C CG  A LYS   B 31  ? 0.2073 0.3206 0.4139 -0.0338 0.0302  0.1033  31  LYS   B CG  
4541 C CG  B LYS   B 31  ? 0.2639 0.3075 0.3595 -0.0242 -0.0081 0.0475  31  LYS   B CG  
4542 C CD  A LYS   B 31  ? 0.2398 0.3663 0.4749 -0.0308 0.0255  0.1007  31  LYS   B CD  
4543 C CD  B LYS   B 31  ? 0.2847 0.3338 0.4038 -0.0224 -0.0058 0.0427  31  LYS   B CD  
4544 C CE  A LYS   B 31  ? 0.2613 0.3983 0.5242 -0.0289 0.0187  0.0928  31  LYS   B CE  
4545 C CE  B LYS   B 31  ? 0.2980 0.3521 0.4385 -0.0205 -0.0047 0.0369  31  LYS   B CE  
4546 N NZ  A LYS   B 31  ? 0.2766 0.4140 0.5471 -0.0213 0.0110  0.0821  31  LYS   B NZ  
4547 N NZ  B LYS   B 31  ? 0.3080 0.3631 0.4549 -0.0168 -0.0063 0.0314  31  LYS   B NZ  
4574 N N   . PRO   B 32  ? 0.1882 0.1754 0.2259 -0.0426 -0.0418 0.0492  32  PRO   B N   
4575 C CA  . PRO   B 32  ? 0.1992 0.1694 0.1908 -0.0390 -0.0449 0.0308  32  PRO   B CA  
4576 C C   . PRO   B 32  ? 0.2088 0.1583 0.1907 -0.0426 -0.0560 0.0289  32  PRO   B C   
4577 O O   . PRO   B 32  ? 0.2142 0.1621 0.2275 -0.0424 -0.0700 0.0370  32  PRO   B O   
4578 C CB  . PRO   B 32  ? 0.2142 0.1625 0.1884 -0.0451 -0.0346 0.0166  32  PRO   B CB  
4579 C CG  . PRO   B 32  ? 0.2283 0.1526 0.1955 -0.0342 -0.0537 0.0293  32  PRO   B CG  
4580 C CD  . PRO   B 32  ? 0.2136 0.1550 0.2102 -0.0280 -0.0566 0.0339  32  PRO   B CD  
4588 N N   . THR   B 33  ? 0.2092 0.1486 0.1831 -0.0373 -0.0456 0.0229  33  THR   B N   
4589 C CA  . THR   B 33  ? 0.2131 0.1583 0.1784 -0.0418 -0.0480 0.0352  33  THR   B CA  
4590 C C   . THR   B 33  ? 0.2107 0.1496 0.1665 -0.0357 -0.0461 0.0206  33  THR   B C   
4591 O O   . THR   B 33  ? 0.2268 0.1538 0.1830 -0.0473 -0.0495 0.0187  33  THR   B O   
4592 C CB  . THR   B 33  ? 0.2232 0.1669 0.1851 -0.0262 -0.0590 0.0424  33  THR   B CB  
4593 O OG1 . THR   B 33  ? 0.2072 0.1783 0.1954 -0.0318 -0.0480 0.0429  33  THR   B OG1 
4594 C CG2 . THR   B 33  ? 0.2530 0.1752 0.2005 -0.0205 -0.0585 0.0341  33  THR   B CG2 
4602 N N   . VAL   B 34  ? 0.1924 0.1451 0.1590 -0.0386 -0.0427 0.0206  34  VAL   B N   
4603 C CA  . VAL   B 34  ? 0.1817 0.1419 0.1653 -0.0311 -0.0362 0.0115  34  VAL   B CA  
4604 C C   . VAL   B 34  ? 0.1640 0.1425 0.1433 -0.0342 -0.0214 0.0127  34  VAL   B C   
4605 O O   . VAL   B 34  ? 0.1840 0.1454 0.1494 -0.0320 -0.0381 0.0094  34  VAL   B O   
4606 C CB  . VAL   B 34  ? 0.1889 0.1493 0.1878 -0.0133 -0.0308 0.0132  34  VAL   B CB  
4607 C CG1 . VAL   B 34  ? 0.1806 0.1641 0.1914 -0.0096 -0.0124 0.0029  34  VAL   B CG1 
4608 C CG2 . VAL   B 34  ? 0.1907 0.1585 0.2059 -0.0183 -0.0288 0.0159  34  VAL   B CG2 
4618 N N   . VAL   B 35  ? 0.1571 0.1361 0.1378 -0.0281 -0.0169 0.0089  35  VAL   B N   
4619 C CA  . VAL   B 35  ? 0.1523 0.1371 0.1371 -0.0218 -0.0168 0.0140  35  VAL   B CA  
4620 C C   . VAL   B 35  ? 0.1465 0.1281 0.1354 -0.0206 -0.0231 0.0129  35  VAL   B C   
4621 O O   . VAL   B 35  ? 0.1513 0.1319 0.1425 -0.0254 -0.0051 -0.0032 35  VAL   B O   
4622 C CB  . VAL   B 35  ? 0.1535 0.1483 0.1589 -0.0208 -0.0004 0.0042  35  VAL   B CB  
4623 C CG1 . VAL   B 35  ? 0.1495 0.1634 0.1851 -0.0272 -0.0006 0.0007  35  VAL   B CG1 
4624 C CG2 . VAL   B 35  ? 0.1575 0.1545 0.1792 -0.0164 -0.0065 0.0025  35  VAL   B CG2 
4634 N N   . VAL   B 36  ? 0.1433 0.1290 0.1396 -0.0194 -0.0194 0.0080  36  VAL   B N   
4635 C CA  . VAL   B 36  ? 0.1436 0.1268 0.1374 -0.0145 -0.0089 0.0031  36  VAL   B CA  
4636 C C   . VAL   B 36  ? 0.1361 0.1283 0.1273 -0.0103 -0.0056 0.0099  36  VAL   B C   
4637 O O   . VAL   B 36  ? 0.1452 0.1436 0.1474 -0.0118 -0.0092 -0.0017 36  VAL   B O   
4638 C CB  . VAL   B 36  ? 0.1447 0.1328 0.1402 -0.0169 -0.0037 0.0028  36  VAL   B CB  
4639 C CG1 . VAL   B 36  ? 0.1419 0.1448 0.1754 -0.0175 -0.0027 0.0001  36  VAL   B CG1 
4640 C CG2 . VAL   B 36  ? 0.1465 0.1419 0.1593 -0.0164 -0.0169 0.0104  36  VAL   B CG2 
4650 N N   . ASN   B 37  ? 0.1413 0.1332 0.1299 -0.0014 -0.0097 0.0073  37  ASN   B N   
4651 C CA  . ASN   B 37  ? 0.1432 0.1339 0.1483 -0.0013 -0.0165 0.0097  37  ASN   B CA  
4652 C C   . ASN   B 37  ? 0.1423 0.1349 0.1560 0.0040  -0.0124 0.0037  37  ASN   B C   
4653 O O   . ASN   B 37  ? 0.1537 0.1393 0.1525 0.0017  0.0001  0.0069  37  ASN   B O   
4654 C CB  . ASN   B 37  ? 0.1430 0.1366 0.1399 -0.0008 -0.0141 0.0035  37  ASN   B CB  
4655 C CG  . ASN   B 37  ? 0.1469 0.1377 0.1533 -0.0020 -0.0129 0.0012  37  ASN   B CG  
4656 O OD1 . ASN   B 37  ? 0.1591 0.1390 0.1765 0.0106  -0.0184 0.0003  37  ASN   B OD1 
4657 N ND2 . ASN   B 37  ? 0.1538 0.1360 0.1544 -0.0005 -0.0154 0.0074  37  ASN   B ND2 
4664 N N   . ALA   B 38  ? 0.1512 0.1351 0.1590 0.0076  -0.0020 0.0091  38  ALA   B N   
4665 C CA  . ALA   B 38  ? 0.1606 0.1377 0.1612 -0.0004 -0.0020 0.0118  38  ALA   B CA  
4666 C C   . ALA   B 38  ? 0.1553 0.1323 0.1578 -0.0032 0.0028  0.0100  38  ALA   B C   
4667 O O   . ALA   B 38  ? 0.1698 0.1459 0.1664 0.0084  -0.0011 0.0163  38  ALA   B O   
4668 C CB  . ALA   B 38  ? 0.1903 0.1452 0.1815 -0.0072 0.0064  0.0098  38  ALA   B CB  
4674 N N   . ALA   B 39  ? 0.1634 0.1341 0.1440 0.0034  -0.0061 0.0092  39  ALA   B N   
4675 C CA  . ALA   B 39  ? 0.1655 0.1400 0.1517 0.0045  -0.0084 0.0094  39  ALA   B CA  
4676 C C   . ALA   B 39  ? 0.1735 0.1417 0.1369 0.0041  -0.0056 0.0005  39  ALA   B C   
4677 O O   . ALA   B 39  ? 0.1806 0.1517 0.1588 -0.0022 -0.0033 0.0094  39  ALA   B O   
4678 C CB  . ALA   B 39  ? 0.1576 0.1508 0.1663 -0.0080 -0.0044 0.0032  39  ALA   B CB  
4684 N N   . ASN   B 40  ? 0.1752 0.1689 0.1363 -0.0026 0.0012  -0.0083 40  ASN   B N   
4685 C CA  . ASN   B 40  ? 0.1815 0.1709 0.1592 0.0055  -0.0020 -0.0024 40  ASN   B CA  
4686 C C   . ASN   B 40  ? 0.1871 0.1677 0.1407 0.0096  -0.0082 0.0065  40  ASN   B C   
4687 O O   . ASN   B 40  ? 0.1813 0.1585 0.1438 0.0091  -0.0113 0.0032  40  ASN   B O   
4688 C CB  . ASN   B 40  ? 0.1918 0.1693 0.1790 0.0153  -0.0158 0.0130  40  ASN   B CB  
4689 C CG  . ASN   B 40  ? 0.1991 0.1765 0.2068 0.0095  -0.0257 0.0160  40  ASN   B CG  
4690 O OD1 . ASN   B 40  ? 0.1973 0.1747 0.2886 0.0078  -0.0429 0.0180  40  ASN   B OD1 
4691 N ND2 . ASN   B 40  ? 0.2079 0.1797 0.2071 0.0066  -0.0247 0.0187  40  ASN   B ND2 
4698 N N   . VAL   B 41  ? 0.1919 0.1735 0.1439 0.0158  0.0061  0.0076  41  VAL   B N   
4699 C CA  . VAL   B 41  ? 0.1997 0.1855 0.1455 0.0102  0.0044  -0.0063 41  VAL   B CA  
4700 C C   . VAL   B 41  ? 0.1961 0.1875 0.1460 0.0176  -0.0044 -0.0070 41  VAL   B C   
4701 O O   . VAL   B 41  ? 0.1920 0.1862 0.1569 0.0196  -0.0131 -0.0137 41  VAL   B O   
4702 C CB  . VAL   B 41  ? 0.2211 0.2019 0.1732 -0.0025 0.0237  -0.0217 41  VAL   B CB  
4703 C CG1 . VAL   B 41  ? 0.2211 0.2049 0.1835 -0.0073 0.0355  -0.0309 41  VAL   B CG1 
4704 C CG2 . VAL   B 41  ? 0.2372 0.2204 0.1822 -0.0105 0.0266  -0.0085 41  VAL   B CG2 
4714 N N   . TYR   B 42  ? 0.2102 0.1850 0.1372 0.0191  -0.0167 0.0016  42  TYR   B N   
4715 C CA  . TYR   B 42  ? 0.2129 0.1858 0.1507 0.0200  -0.0322 -0.0074 42  TYR   B CA  
4716 C C   . TYR   B 42  ? 0.1933 0.1723 0.1632 0.0246  -0.0299 -0.0114 42  TYR   B C   
4717 O O   . TYR   B 42  ? 0.1929 0.1830 0.1957 0.0159  -0.0329 -0.0176 42  TYR   B O   
4718 C CB  . TYR   B 42  ? 0.2370 0.2154 0.1703 0.0192  -0.0309 0.0040  42  TYR   B CB  
4719 C CG  . TYR   B 42  ? 0.2355 0.2324 0.1571 0.0048  -0.0322 0.0190  42  TYR   B CG  
4720 C CD1 . TYR   B 42  ? 0.2216 0.2335 0.1441 -0.0059 -0.0213 0.0095  42  TYR   B CD1 
4721 C CD2 . TYR   B 42  ? 0.2456 0.2414 0.1886 0.0100  -0.0226 0.0231  42  TYR   B CD2 
4722 C CE1 . TYR   B 42  ? 0.2289 0.2478 0.1559 -0.0027 -0.0211 0.0155  42  TYR   B CE1 
4723 C CE2 . TYR   B 42  ? 0.2428 0.2535 0.1807 0.0113  0.0079  0.0443  42  TYR   B CE2 
4724 C CZ  . TYR   B 42  ? 0.2441 0.2604 0.1753 0.0178  0.0074  0.0187  42  TYR   B CZ  
4725 O OH  . TYR   B 42  ? 0.2722 0.2791 0.2200 0.0269  0.0100  0.0175  42  TYR   B OH  
4735 N N   . LEU   B 43  ? 0.1798 0.1576 0.1521 0.0100  -0.0149 -0.0083 43  LEU   B N   
4736 C CA  . LEU   B 43  ? 0.1726 0.1623 0.1484 0.0071  -0.0172 -0.0024 43  LEU   B CA  
4737 C C   . LEU   B 43  ? 0.1770 0.1627 0.1425 0.0066  -0.0154 -0.0010 43  LEU   B C   
4738 O O   . LEU   B 43  ? 0.1764 0.1718 0.1727 0.0058  -0.0243 0.0068  43  LEU   B O   
4739 C CB  . LEU   B 43  ? 0.1714 0.1536 0.1576 0.0011  -0.0193 -0.0073 43  LEU   B CB  
4740 C CG  . LEU   B 43  ? 0.1748 0.1468 0.1747 -0.0004 -0.0261 -0.0033 43  LEU   B CG  
4741 C CD1 . LEU   B 43  ? 0.1823 0.1564 0.2102 -0.0032 -0.0430 -0.0049 43  LEU   B CD1 
4742 C CD2 . LEU   B 43  ? 0.1762 0.1531 0.1818 -0.0064 -0.0289 -0.0041 43  LEU   B CD2 
4754 N N   . LYS   B 44  ? 0.1809 0.1589 0.1518 0.0083  -0.0149 -0.0072 44  LYS   B N   
4755 C CA  . LYS   B 44  ? 0.1956 0.1703 0.1610 0.0130  -0.0182 -0.0003 44  LYS   B CA  
4756 C C   . LYS   B 44  ? 0.1841 0.1656 0.1544 0.0201  -0.0162 -0.0016 44  LYS   B C   
4757 O O   . LYS   B 44  ? 0.2042 0.1624 0.1905 0.0073  -0.0116 0.0006  44  LYS   B O   
4758 C CB  . LYS   B 44  ? 0.2228 0.1904 0.1766 0.0240  -0.0359 -0.0002 44  LYS   B CB  
4759 C CG  . LYS   B 44  ? 0.2644 0.2198 0.2264 0.0213  -0.0602 0.0087  44  LYS   B CG  
4760 C CD  . LYS   B 44  ? 0.3015 0.2425 0.3037 -0.0001 -0.0717 0.0128  44  LYS   B CD  
4761 C CE  . LYS   B 44  ? 0.3372 0.2702 0.3637 -0.0120 -0.0796 0.0208  44  LYS   B CE  
4762 N NZ  . LYS   B 44  ? 0.3556 0.2834 0.3936 -0.0102 -0.0821 0.0376  44  LYS   B NZ  
4776 N N   . HIS   B 45  ? 0.1740 0.1711 0.1441 0.0059  -0.0128 0.0105  45  HIS   B N   
4777 C CA  . HIS   B 45  ? 0.1797 0.1698 0.1582 0.0082  -0.0097 -0.0001 45  HIS   B CA  
4778 C C   . HIS   B 45  ? 0.2015 0.1853 0.1931 0.0181  -0.0172 -0.0019 45  HIS   B C   
4779 O O   . HIS   B 45  ? 0.2178 0.2181 0.2474 0.0439  0.0079  -0.0015 45  HIS   B O   
4780 C CB  . HIS   B 45  ? 0.1727 0.1712 0.1652 0.0007  -0.0121 -0.0021 45  HIS   B CB  
4781 C CG  . HIS   B 45  ? 0.1740 0.1631 0.1655 -0.0074 -0.0136 -0.0006 45  HIS   B CG  
4782 N ND1 . HIS   B 45  ? 0.1759 0.1557 0.1705 -0.0001 -0.0226 -0.0071 45  HIS   B ND1 
4783 C CD2 . HIS   B 45  ? 0.1831 0.1620 0.1786 -0.0127 -0.0272 0.0020  45  HIS   B CD2 
4784 C CE1 . HIS   B 45  ? 0.1849 0.1415 0.1613 -0.0043 -0.0325 -0.0056 45  HIS   B CE1 
4785 N NE2 . HIS   B 45  ? 0.1953 0.1543 0.1718 -0.0040 -0.0296 -0.0030 45  HIS   B NE2 
4793 N N   A GLY   B 46  ? 0.2101 0.1732 0.2286 0.0181  -0.0348 0.0080  46  GLY   B N   
4794 N N   B GLY   B 46  ? 0.2111 0.1902 0.2174 0.0172  -0.0283 0.0053  46  GLY   B N   
4795 C CA  A GLY   B 46  ? 0.2249 0.1841 0.2787 0.0122  -0.0420 0.0025  46  GLY   B CA  
4796 C CA  B GLY   B 46  ? 0.2219 0.2004 0.2473 0.0126  -0.0363 0.0082  46  GLY   B CA  
4797 C C   A GLY   B 46  ? 0.2297 0.2004 0.3223 0.0164  -0.0378 0.0022  46  GLY   B C   
4798 C C   B GLY   B 46  ? 0.2273 0.2119 0.2763 0.0114  -0.0366 0.0114  46  GLY   B C   
4799 O O   A GLY   B 46  ? 0.2408 0.2120 0.4110 0.0219  -0.0090 -0.0226 46  GLY   B O   
4800 O O   B GLY   B 46  ? 0.2315 0.2218 0.2954 0.0160  -0.0311 0.0184  46  GLY   B O   
4807 N N   . GLY   B 47  ? 0.2292 0.2161 0.2911 -0.0019 -0.0304 0.0019  47  GLY   B N   
4808 C CA  . GLY   B 47  ? 0.2167 0.1928 0.2498 -0.0054 -0.0232 0.0043  47  GLY   B CA  
4809 C C   . GLY   B 47  ? 0.1947 0.1696 0.2097 -0.0018 -0.0050 0.0092  47  GLY   B C   
4810 O O   . GLY   B 47  ? 0.2078 0.1570 0.2090 0.0062  -0.0127 0.0125  47  GLY   B O   
4815 N N   . GLY   B 48  ? 0.1695 0.1573 0.2128 0.0037  -0.0151 0.0156  48  GLY   B N   
4816 C CA  . GLY   B 48  ? 0.1682 0.1565 0.2155 -0.0039 -0.0142 0.0103  48  GLY   B CA  
4817 C C   . GLY   B 48  ? 0.1636 0.1510 0.1921 0.0009  0.0004  0.0116  48  GLY   B C   
4818 O O   . GLY   B 48  ? 0.1561 0.1513 0.2195 0.0054  -0.0116 0.0059  48  GLY   B O   
4822 N N   . VAL   B 49  ? 0.1642 0.1562 0.1709 0.0135  -0.0098 0.0067  49  VAL   B N   
4823 C CA  . VAL   B 49  ? 0.1622 0.1634 0.1729 0.0127  -0.0212 -0.0082 49  VAL   B CA  
4824 C C   . VAL   B 49  ? 0.1493 0.1557 0.1590 0.0121  -0.0118 -0.0052 49  VAL   B C   
4825 O O   . VAL   B 49  ? 0.1627 0.1594 0.1689 0.0034  -0.0097 -0.0043 49  VAL   B O   
4826 C CB  . VAL   B 49  ? 0.1625 0.1798 0.1999 0.0015  -0.0305 -0.0056 49  VAL   B CB  
4827 C CG1 . VAL   B 49  ? 0.1612 0.1885 0.2006 0.0076  -0.0367 -0.0092 49  VAL   B CG1 
4828 C CG2 . VAL   B 49  ? 0.1878 0.1968 0.2283 -0.0073 -0.0477 -0.0064 49  VAL   B CG2 
4838 N N   . ALA   B 50  ? 0.1511 0.1469 0.1709 0.0024  -0.0064 0.0046  50  ALA   B N   
4839 C CA  . ALA   B 50  ? 0.1476 0.1393 0.1738 0.0086  -0.0097 -0.0011 50  ALA   B CA  
4840 C C   . ALA   B 50  ? 0.1554 0.1503 0.1640 0.0032  -0.0086 0.0014  50  ALA   B C   
4841 O O   . ALA   B 50  ? 0.1571 0.1469 0.1571 0.0043  -0.0022 -0.0015 50  ALA   B O   
4842 C CB  . ALA   B 50  ? 0.1556 0.1434 0.1652 -0.0016 -0.0058 0.0059  50  ALA   B CB  
4848 N N   . GLY   B 51  ? 0.1571 0.1541 0.1708 0.0132  -0.0152 0.0102  51  GLY   B N   
4849 C CA  . GLY   B 51  ? 0.1635 0.1615 0.2005 0.0156  -0.0169 0.0103  51  GLY   B CA  
4850 C C   . GLY   B 51  ? 0.1615 0.1566 0.1990 0.0173  -0.0086 0.0016  51  GLY   B C   
4851 O O   . GLY   B 51  ? 0.1613 0.1684 0.2107 0.0093  -0.0123 -0.0024 51  GLY   B O   
4855 N N   . ALA   B 52  ? 0.1578 0.1503 0.1874 0.0150  -0.0111 0.0048  52  ALA   B N   
4856 C CA  . ALA   B 52  ? 0.1613 0.1604 0.1856 0.0143  -0.0035 -0.0078 52  ALA   B CA  
4857 C C   . ALA   B 52  ? 0.1548 0.1529 0.1818 0.0067  -0.0059 -0.0044 52  ALA   B C   
4858 O O   . ALA   B 52  ? 0.1533 0.1600 0.2111 0.0097  -0.0034 0.0010  52  ALA   B O   
4859 C CB  . ALA   B 52  ? 0.1772 0.1605 0.1951 0.0036  0.0083  -0.0083 52  ALA   B CB  
4865 N N   . LEU   B 53  ? 0.1456 0.1519 0.1717 0.0143  -0.0035 0.0025  53  LEU   B N   
4866 C CA  . LEU   B 53  ? 0.1476 0.1658 0.1646 0.0108  -0.0084 -0.0033 53  LEU   B CA  
4867 C C   . LEU   B 53  ? 0.1547 0.1562 0.1709 0.0089  0.0027  0.0019  53  LEU   B C   
4868 O O   . LEU   B 53  ? 0.1579 0.1674 0.1803 -0.0005 0.0043  0.0103  53  LEU   B O   
4869 C CB  . LEU   B 53  ? 0.1479 0.1703 0.1779 0.0098  -0.0081 0.0103  53  LEU   B CB  
4870 C CG  . LEU   B 53  ? 0.1505 0.1783 0.1807 0.0047  -0.0025 0.0256  53  LEU   B CG  
4871 C CD1 . LEU   B 53  ? 0.1613 0.1957 0.2108 0.0173  -0.0061 0.0047  53  LEU   B CD1 
4872 C CD2 . LEU   B 53  ? 0.1662 0.2099 0.2017 -0.0062 -0.0052 -0.0110 53  LEU   B CD2 
4884 N N   . ASN   B 54  ? 0.1562 0.1479 0.1641 0.0013  -0.0047 0.0018  54  ASN   B N   
4885 C CA  . ASN   B 54  ? 0.1607 0.1622 0.1725 0.0017  -0.0053 -0.0086 54  ASN   B CA  
4886 C C   . ASN   B 54  ? 0.1532 0.1624 0.1902 0.0021  -0.0022 -0.0063 54  ASN   B C   
4887 O O   . ASN   B 54  ? 0.1523 0.1679 0.2125 -0.0040 0.0032  -0.0095 54  ASN   B O   
4888 C CB  . ASN   B 54  ? 0.1630 0.1702 0.1915 0.0069  -0.0006 0.0008  54  ASN   B CB  
4889 C CG  . ASN   B 54  ? 0.1685 0.1805 0.1848 0.0029  -0.0083 0.0036  54  ASN   B CG  
4890 O OD1 . ASN   B 54  ? 0.1587 0.1777 0.2043 0.0012  -0.0137 -0.0146 54  ASN   B OD1 
4891 N ND2 . ASN   B 54  ? 0.1774 0.1958 0.2106 -0.0014 -0.0278 0.0125  54  ASN   B ND2 
4898 N N   . LYS   B 55  ? 0.1504 0.1642 0.2126 0.0103  -0.0036 -0.0005 55  LYS   B N   
4899 C CA  . LYS   B 55  ? 0.1627 0.1803 0.2240 0.0158  -0.0037 -0.0039 55  LYS   B CA  
4900 C C   . LYS   B 55  ? 0.1569 0.1744 0.2234 0.0083  0.0037  -0.0078 55  LYS   B C   
4901 O O   . LYS   B 55  ? 0.1565 0.1982 0.2378 0.0073  0.0019  -0.0089 55  LYS   B O   
4902 C CB  . LYS   B 55  ? 0.1777 0.1902 0.2642 0.0310  0.0110  0.0088  55  LYS   B CB  
4903 C CG  . LYS   B 55  ? 0.2202 0.2239 0.3508 0.0382  0.0246  0.0169  55  LYS   B CG  
4904 C CD  . LYS   B 55  ? 0.2574 0.2526 0.4258 0.0512  0.0366  0.0358  55  LYS   B CD  
4905 C CE  . LYS   B 55  ? 0.2828 0.2755 0.4888 0.0543  0.0541  0.0463  55  LYS   B CE  
4906 N NZ  . LYS   B 55  ? 0.2934 0.2922 0.5235 0.0521  0.0438  0.0577  55  LYS   B NZ  
4920 N N   . ALA   B 56  ? 0.1522 0.1758 0.2128 0.0091  0.0029  -0.0118 56  ALA   B N   
4921 C CA  . ALA   B 56  ? 0.1678 0.1974 0.2072 0.0053  0.0025  -0.0109 56  ALA   B CA  
4922 C C   . ALA   B 56  ? 0.1697 0.1928 0.1996 0.0038  0.0170  -0.0035 56  ALA   B C   
4923 O O   . ALA   B 56  ? 0.1795 0.2026 0.2203 0.0042  0.0323  -0.0014 56  ALA   B O   
4924 C CB  . ALA   B 56  ? 0.1813 0.2210 0.2118 -0.0086 -0.0055 -0.0130 56  ALA   B CB  
4930 N N   . THR   B 57  ? 0.1581 0.1811 0.2158 0.0002  0.0220  -0.0034 57  THR   B N   
4931 C CA  . THR   B 57  ? 0.1657 0.1842 0.2055 -0.0008 0.0243  -0.0031 57  THR   B CA  
4932 C C   . THR   B 57  ? 0.1665 0.1931 0.2198 -0.0004 0.0229  -0.0057 57  THR   B C   
4933 O O   . THR   B 57  ? 0.1715 0.1908 0.2311 -0.0188 0.0129  -0.0039 57  THR   B O   
4934 C CB  . THR   B 57  ? 0.1752 0.1670 0.1761 -0.0050 0.0147  0.0067  57  THR   B CB  
4935 O OG1 . THR   B 57  ? 0.1742 0.1644 0.2074 -0.0052 0.0127  0.0009  57  THR   B OG1 
4936 C CG2 . THR   B 57  ? 0.1706 0.1744 0.1828 -0.0060 0.0210  0.0024  57  THR   B CG2 
4944 N N   . ASN   B 58  ? 0.1609 0.2164 0.2380 -0.0116 0.0056  -0.0225 58  ASN   B N   
4945 C CA  . ASN   B 58  ? 0.1813 0.2610 0.2826 -0.0311 0.0347  -0.0137 58  ASN   B CA  
4946 C C   . ASN   B 58  ? 0.1567 0.2359 0.2390 -0.0201 -0.0022 -0.0122 58  ASN   B C   
4947 O O   . ASN   B 58  ? 0.1581 0.2481 0.2555 -0.0189 -0.0006 -0.0225 58  ASN   B O   
4948 C CB  . ASN   B 58  ? 0.2794 0.3441 0.4151 -0.0557 0.0861  -0.0030 58  ASN   B CB  
4949 C CG  . ASN   B 58  ? 0.4042 0.4365 0.5762 -0.0608 0.1142  0.0193  58  ASN   B CG  
4950 O OD1 . ASN   B 58  ? 0.4242 0.4620 0.6362 -0.0609 0.1204  0.0268  58  ASN   B OD1 
4951 N ND2 . ASN   B 58  ? 0.5282 0.5282 0.6315 -0.0660 0.1266  0.0266  58  ASN   B ND2 
4958 N N   . ASN   B 59  ? 0.1595 0.2162 0.2160 -0.0111 -0.0035 -0.0002 59  ASN   B N   
4959 C CA  . ASN   B 59  ? 0.1575 0.2159 0.2109 -0.0159 -0.0159 0.0006  59  ASN   B CA  
4960 C C   . ASN   B 59  ? 0.1507 0.2061 0.1980 -0.0173 -0.0149 -0.0130 59  ASN   B C   
4961 O O   . ASN   B 59  ? 0.1616 0.2035 0.2091 -0.0144 -0.0056 -0.0095 59  ASN   B O   
4962 C CB  . ASN   B 59  ? 0.1694 0.2334 0.2261 -0.0078 -0.0257 0.0066  59  ASN   B CB  
4963 C CG  . ASN   B 59  ? 0.1834 0.2449 0.2350 -0.0002 -0.0351 0.0155  59  ASN   B CG  
4964 O OD1 . ASN   B 59  ? 0.1855 0.2499 0.2376 0.0004  -0.0268 0.0285  59  ASN   B OD1 
4965 N ND2 . ASN   B 59  ? 0.1884 0.2544 0.2452 -0.0040 -0.0393 0.0059  59  ASN   B ND2 
4972 N N   . ALA   B 60  ? 0.1587 0.1969 0.2095 -0.0185 0.0002  -0.0102 60  ALA   B N   
4973 C CA  . ALA   B 60  ? 0.1710 0.1884 0.1979 -0.0192 -0.0062 -0.0047 60  ALA   B CA  
4974 C C   . ALA   B 60  ? 0.1646 0.1730 0.1801 -0.0171 -0.0122 0.0039  60  ALA   B C   
4975 O O   . ALA   B 60  ? 0.1753 0.1743 0.1944 -0.0180 -0.0015 -0.0072 60  ALA   B O   
4976 C CB  . ALA   B 60  ? 0.1892 0.1885 0.2240 -0.0166 0.0045  -0.0003 60  ALA   B CB  
4982 N N   . MET   B 61  ? 0.1566 0.1663 0.1721 -0.0124 -0.0023 0.0040  61  MET   B N   
4983 C CA  . MET   B 61  ? 0.1576 0.1578 0.1688 -0.0112 -0.0159 0.0056  61  MET   B CA  
4984 C C   . MET   B 61  ? 0.1613 0.1501 0.1735 -0.0120 -0.0173 0.0081  61  MET   B C   
4985 O O   . MET   B 61  ? 0.1643 0.1495 0.1689 -0.0024 -0.0093 -0.0109 61  MET   B O   
4986 C CB  . MET   B 61  ? 0.1568 0.1595 0.1736 -0.0017 -0.0093 0.0015  61  MET   B CB  
4987 C CG  . MET   B 61  ? 0.1488 0.1556 0.1736 -0.0056 -0.0127 0.0052  61  MET   B CG  
4988 S SD  . MET   B 61  ? 0.1550 0.1583 0.1997 -0.0043 -0.0090 -0.0110 61  MET   B SD  
4989 C CE  . MET   B 61  ? 0.1637 0.1825 0.2200 -0.0048 -0.0107 -0.0254 61  MET   B CE  
4999 N N   . GLN   B 62  ? 0.1614 0.1619 0.1689 -0.0077 -0.0263 0.0046  62  GLN   B N   
5000 C CA  . GLN   B 62  ? 0.1673 0.1679 0.1752 -0.0002 -0.0313 0.0011  62  GLN   B CA  
5001 C C   . GLN   B 62  ? 0.1634 0.1694 0.1811 -0.0026 -0.0326 -0.0080 62  GLN   B C   
5002 O O   . GLN   B 62  ? 0.1729 0.1702 0.1892 -0.0004 -0.0304 -0.0180 62  GLN   B O   
5003 C CB  . GLN   B 62  ? 0.1758 0.1714 0.1806 -0.0017 -0.0227 0.0007  62  GLN   B CB  
5004 C CG  . GLN   B 62  ? 0.1771 0.1727 0.1886 -0.0003 -0.0329 -0.0071 62  GLN   B CG  
5005 C CD  . GLN   B 62  ? 0.1750 0.1708 0.1706 0.0024  -0.0332 0.0036  62  GLN   B CD  
5006 O OE1 . GLN   B 62  ? 0.1771 0.1705 0.1920 0.0045  -0.0367 -0.0083 62  GLN   B OE1 
5007 N NE2 . GLN   B 62  ? 0.1786 0.1754 0.1703 0.0068  -0.0248 -0.0083 62  GLN   B NE2 
5016 N N   . VAL   B 63  ? 0.1635 0.1724 0.1977 -0.0074 -0.0350 -0.0151 63  VAL   B N   
5017 C CA  . VAL   B 63  ? 0.1776 0.1730 0.2199 -0.0077 -0.0316 -0.0081 63  VAL   B CA  
5018 C C   . VAL   B 63  ? 0.1824 0.1615 0.1876 -0.0176 -0.0335 -0.0256 63  VAL   B C   
5019 O O   . VAL   B 63  ? 0.1925 0.1630 0.2034 -0.0123 -0.0430 -0.0230 63  VAL   B O   
5020 C CB  . VAL   B 63  ? 0.1728 0.1923 0.2506 -0.0196 -0.0286 -0.0180 63  VAL   B CB  
5021 C CG1 . VAL   B 63  ? 0.1792 0.2011 0.2709 -0.0333 -0.0168 -0.0153 63  VAL   B CG1 
5022 C CG2 . VAL   B 63  ? 0.1695 0.2092 0.2582 -0.0137 -0.0304 -0.0225 63  VAL   B CG2 
5032 N N   . GLU   B 64  ? 0.1778 0.1623 0.1833 -0.0126 -0.0340 -0.0196 64  GLU   B N   
5033 C CA  . GLU   B 64  ? 0.1694 0.1534 0.1906 -0.0140 -0.0315 -0.0057 64  GLU   B CA  
5034 C C   . GLU   B 64  ? 0.1675 0.1529 0.1847 -0.0056 -0.0349 -0.0156 64  GLU   B C   
5035 O O   . GLU   B 64  ? 0.1776 0.1616 0.1759 -0.0098 -0.0309 -0.0126 64  GLU   B O   
5036 C CB  . GLU   B 64  ? 0.1644 0.1667 0.1785 -0.0192 -0.0199 -0.0004 64  GLU   B CB  
5037 C CG  . GLU   B 64  ? 0.1762 0.1663 0.1884 -0.0254 -0.0262 -0.0081 64  GLU   B CG  
5038 C CD  . GLU   B 64  ? 0.1833 0.1785 0.2014 -0.0314 -0.0339 0.0005  64  GLU   B CD  
5039 O OE1 . GLU   B 64  ? 0.1867 0.1994 0.2099 -0.0332 -0.0228 -0.0288 64  GLU   B OE1 
5040 O OE2 . GLU   B 64  ? 0.1951 0.1868 0.2095 -0.0310 -0.0353 -0.0097 64  GLU   B OE2 
5047 N N   . SER   B 65  ? 0.1686 0.1500 0.1785 -0.0075 -0.0220 -0.0155 65  SER   B N   
5048 C CA  . SER   B 65  ? 0.1672 0.1509 0.1788 -0.0023 -0.0243 -0.0136 65  SER   B CA  
5049 C C   . SER   B 65  ? 0.1698 0.1541 0.1708 0.0031  -0.0296 -0.0155 65  SER   B C   
5050 O O   . SER   B 65  ? 0.1744 0.1620 0.1767 -0.0004 -0.0270 -0.0199 65  SER   B O   
5051 C CB  . SER   B 65  ? 0.1684 0.1594 0.1760 -0.0106 -0.0191 -0.0088 65  SER   B CB  
5052 O OG  . SER   B 65  ? 0.1727 0.1579 0.1772 -0.0076 -0.0193 -0.0221 65  SER   B OG  
5058 N N   . ASP   B 66  ? 0.1795 0.1612 0.1661 0.0015  -0.0395 -0.0177 66  ASP   B N   
5059 C CA  . ASP   B 66  ? 0.1844 0.1703 0.1665 0.0045  -0.0397 -0.0137 66  ASP   B CA  
5060 C C   . ASP   B 66  ? 0.1930 0.1773 0.1620 -0.0067 -0.0268 -0.0174 66  ASP   B C   
5061 O O   . ASP   B 66  ? 0.1973 0.1803 0.1716 0.0045  -0.0294 -0.0217 66  ASP   B O   
5062 C CB  . ASP   B 66  ? 0.2037 0.1805 0.1879 0.0099  -0.0455 -0.0147 66  ASP   B CB  
5063 C CG  . ASP   B 66  ? 0.2276 0.1929 0.2198 0.0191  -0.0561 -0.0026 66  ASP   B CG  
5064 O OD1 . ASP   B 66  ? 0.2536 0.1888 0.2336 0.0148  -0.0535 0.0066  66  ASP   B OD1 
5065 O OD2 . ASP   B 66  ? 0.2425 0.2175 0.2778 0.0413  -0.0571 -0.0103 66  ASP   B OD2 
5070 N N   . ASP   B 67  ? 0.1849 0.1664 0.1607 -0.0079 -0.0276 -0.0178 67  ASP   B N   
5071 C CA  . ASP   B 67  ? 0.1977 0.1636 0.1757 -0.0106 -0.0243 -0.0090 67  ASP   B CA  
5072 C C   . ASP   B 67  ? 0.1914 0.1613 0.1874 -0.0003 -0.0231 -0.0089 67  ASP   B C   
5073 O O   . ASP   B 67  ? 0.1963 0.1654 0.2076 -0.0027 -0.0146 -0.0221 67  ASP   B O   
5074 C CB  . ASP   B 67  ? 0.2176 0.1756 0.1972 -0.0184 -0.0445 -0.0094 67  ASP   B CB  
5075 C CG  . ASP   B 67  ? 0.2543 0.1848 0.2159 -0.0125 -0.0717 -0.0135 67  ASP   B CG  
5076 O OD1 . ASP   B 67  ? 0.2785 0.1917 0.2373 -0.0136 -0.0709 -0.0099 67  ASP   B OD1 
5077 O OD2 . ASP   B 67  ? 0.2664 0.1912 0.2362 0.0040  -0.0685 -0.0126 67  ASP   B OD2 
5082 N N   . TYR   B 68  ? 0.1864 0.1619 0.1884 -0.0014 -0.0424 -0.0196 68  TYR   B N   
5083 C CA  . TYR   B 68  ? 0.1846 0.1775 0.1964 0.0060  -0.0421 -0.0299 68  TYR   B CA  
5084 C C   . TYR   B 68  ? 0.1769 0.1673 0.1863 0.0061  -0.0358 -0.0343 68  TYR   B C   
5085 O O   . TYR   B 68  ? 0.1837 0.1809 0.2043 0.0091  -0.0365 -0.0466 68  TYR   B O   
5086 C CB  . TYR   B 68  ? 0.1874 0.1968 0.1982 0.0076  -0.0507 -0.0353 68  TYR   B CB  
5087 C CG  . TYR   B 68  ? 0.2017 0.2101 0.2144 0.0137  -0.0397 -0.0610 68  TYR   B CG  
5088 C CD1 . TYR   B 68  ? 0.2008 0.2181 0.2327 -0.0039 -0.0350 -0.0724 68  TYR   B CD1 
5089 C CD2 . TYR   B 68  ? 0.2024 0.2324 0.2253 0.0197  -0.0520 -0.0497 68  TYR   B CD2 
5090 C CE1 . TYR   B 68  ? 0.2049 0.2348 0.2557 0.0018  -0.0199 -0.0665 68  TYR   B CE1 
5091 C CE2 . TYR   B 68  ? 0.2015 0.2373 0.2429 0.0143  -0.0368 -0.0671 68  TYR   B CE2 
5092 C CZ  . TYR   B 68  ? 0.1967 0.2322 0.2599 0.0044  -0.0251 -0.0680 68  TYR   B CZ  
5093 O OH  . TYR   B 68  ? 0.1945 0.2479 0.2959 -0.0031 -0.0197 -0.0355 68  TYR   B OH  
5103 N N   . ILE   B 69  ? 0.1776 0.1599 0.1926 0.0061  -0.0352 -0.0336 69  ILE   B N   
5104 C CA  . ILE   B 69  ? 0.1809 0.1690 0.2011 -0.0052 -0.0264 -0.0344 69  ILE   B CA  
5105 C C   . ILE   B 69  ? 0.1822 0.1684 0.1862 0.0070  -0.0368 -0.0241 69  ILE   B C   
5106 O O   . ILE   B 69  ? 0.1942 0.1831 0.1847 0.0054  -0.0208 -0.0307 69  ILE   B O   
5107 C CB  . ILE   B 69  ? 0.1865 0.1742 0.2074 -0.0035 -0.0033 -0.0330 69  ILE   B CB  
5108 C CG1 . ILE   B 69  ? 0.1917 0.1795 0.2237 -0.0046 0.0072  -0.0325 69  ILE   B CG1 
5109 C CG2 . ILE   B 69  ? 0.2037 0.1900 0.2232 0.0000  -0.0083 -0.0219 69  ILE   B CG2 
5110 C CD1 . ILE   B 69  ? 0.1904 0.1882 0.2343 -0.0201 0.0029  -0.0386 69  ILE   B CD1 
5122 N N   . ALA   B 70  ? 0.1795 0.1683 0.1923 0.0072  -0.0391 -0.0257 70  ALA   B N   
5123 C CA  . ALA   B 70  ? 0.1839 0.1722 0.1763 0.0036  -0.0445 -0.0273 70  ALA   B CA  
5124 C C   . ALA   B 70  ? 0.1903 0.1700 0.1921 -0.0007 -0.0405 -0.0374 70  ALA   B C   
5125 O O   . ALA   B 70  ? 0.2032 0.1718 0.1996 0.0054  -0.0368 -0.0358 70  ALA   B O   
5126 C CB  . ALA   B 70  ? 0.1906 0.1873 0.1769 -0.0004 -0.0406 -0.0319 70  ALA   B CB  
5132 N N   . THR   B 71  ? 0.1979 0.1731 0.2023 0.0029  -0.0591 -0.0363 71  THR   B N   
5133 C CA  . THR   B 71  ? 0.2128 0.1799 0.2250 0.0102  -0.0627 -0.0366 71  THR   B CA  
5134 C C   . THR   B 71  ? 0.2039 0.1783 0.2567 0.0254  -0.0618 -0.0500 71  THR   B C   
5135 O O   . THR   B 71  ? 0.2135 0.1818 0.2968 0.0267  -0.0565 -0.0616 71  THR   B O   
5136 C CB  . THR   B 71  ? 0.2378 0.2018 0.2417 0.0035  -0.0721 -0.0147 71  THR   B CB  
5137 O OG1 . THR   B 71  ? 0.2522 0.2289 0.2730 -0.0165 -0.0683 0.0067  71  THR   B OG1 
5138 C CG2 . THR   B 71  ? 0.2576 0.2015 0.2596 0.0066  -0.0578 -0.0060 71  THR   B CG2 
5146 N N   . ASN   B 72  ? 0.1917 0.1837 0.2386 0.0143  -0.0597 -0.0680 72  ASN   B N   
5147 C CA  . ASN   B 72  ? 0.1889 0.1951 0.2381 0.0202  -0.0460 -0.0702 72  ASN   B CA  
5148 C C   . ASN   B 72  ? 0.1888 0.2039 0.2542 0.0030  -0.0233 -0.0680 72  ASN   B C   
5149 O O   . ASN   B 72  ? 0.1955 0.2194 0.2787 0.0079  -0.0110 -0.0681 72  ASN   B O   
5150 C CB  . ASN   B 72  ? 0.1962 0.2044 0.2499 0.0158  -0.0599 -0.0566 72  ASN   B CB  
5151 C CG  . ASN   B 72  ? 0.2148 0.2206 0.2576 0.0296  -0.0644 -0.0318 72  ASN   B CG  
5152 O OD1 . ASN   B 72  ? 0.2359 0.2424 0.2563 0.0170  -0.0450 -0.0423 72  ASN   B OD1 
5153 N ND2 . ASN   B 72  ? 0.2236 0.2271 0.3080 0.0400  -0.0555 -0.0020 72  ASN   B ND2 
5160 N N   . GLY   B 73  ? 0.1916 0.2038 0.2351 -0.0024 -0.0237 -0.0678 73  GLY   B N   
5161 C CA  . GLY   B 73  ? 0.1936 0.2154 0.2103 -0.0043 -0.0104 -0.0588 73  GLY   B CA  
5162 C C   . GLY   B 73  ? 0.1892 0.2066 0.1620 0.0041  -0.0218 -0.0508 73  GLY   B C   
5163 O O   . GLY   B 73  ? 0.1851 0.1929 0.1848 0.0068  -0.0187 -0.0369 73  GLY   B O   
5167 N N   . PRO   B 74  ? 0.1930 0.2210 0.1625 0.0019  -0.0301 -0.0381 74  PRO   B N   
5168 C CA  . PRO   B 74  ? 0.1850 0.2177 0.1518 0.0058  -0.0239 -0.0242 74  PRO   B CA  
5169 C C   . PRO   B 74  ? 0.1719 0.1966 0.1590 0.0040  -0.0210 -0.0211 74  PRO   B C   
5170 O O   . PRO   B 74  ? 0.1767 0.2022 0.2033 0.0095  -0.0111 -0.0327 74  PRO   B O   
5171 C CB  . PRO   B 74  ? 0.1999 0.2394 0.1624 0.0043  -0.0204 -0.0176 74  PRO   B CB  
5172 C CG  . PRO   B 74  ? 0.2205 0.2524 0.1900 0.0050  -0.0103 -0.0151 74  PRO   B CG  
5173 C CD  . PRO   B 74  ? 0.2147 0.2423 0.1810 0.0093  -0.0158 -0.0259 74  PRO   B CD  
5181 N N   . LEU   B 75  ? 0.1714 0.1862 0.1524 0.0074  -0.0218 -0.0212 75  LEU   B N   
5182 C CA  . LEU   B 75  ? 0.1743 0.1863 0.1507 0.0005  -0.0167 -0.0067 75  LEU   B CA  
5183 C C   . LEU   B 75  ? 0.1804 0.1977 0.1446 0.0074  -0.0125 -0.0028 75  LEU   B C   
5184 O O   . LEU   B 75  ? 0.1987 0.2168 0.1616 -0.0053 -0.0124 0.0059  75  LEU   B O   
5185 C CB  . LEU   B 75  ? 0.1732 0.1868 0.1444 -0.0104 -0.0200 0.0103  75  LEU   B CB  
5186 C CG  . LEU   B 75  ? 0.2069 0.2007 0.1615 -0.0326 -0.0155 0.0054  75  LEU   B CG  
5187 C CD1 . LEU   B 75  ? 0.2431 0.2210 0.1724 -0.0418 0.0113  0.0051  75  LEU   B CD1 
5188 C CD2 . LEU   B 75  ? 0.2464 0.2219 0.2268 -0.0205 0.0040  0.0138  75  LEU   B CD2 
5200 N N   . LYS   B 76  ? 0.1788 0.2202 0.1765 0.0040  0.0041  0.0112  76  LYS   B N   
5201 C CA  . LYS   B 76  ? 0.1899 0.2240 0.2014 -0.0039 0.0243  0.0108  76  LYS   B CA  
5202 C C   . LYS   B 76  ? 0.1840 0.2094 0.1729 -0.0023 0.0181  0.0371  76  LYS   B C   
5203 O O   . LYS   B 76  ? 0.1916 0.1880 0.1803 -0.0070 0.0104  0.0305  76  LYS   B O   
5204 C CB  . LYS   B 76  ? 0.2011 0.2279 0.2676 -0.0083 0.0386  -0.0122 76  LYS   B CB  
5205 C CG  . LYS   B 76  ? 0.2097 0.2439 0.3044 -0.0005 0.0281  -0.0219 76  LYS   B CG  
5206 C CD  . LYS   B 76  ? 0.2151 0.2471 0.3404 0.0028  0.0183  -0.0360 76  LYS   B CD  
5207 C CE  . LYS   B 76  ? 0.2263 0.2613 0.3795 0.0100  0.0048  -0.0416 76  LYS   B CE  
5208 N NZ  . LYS   B 76  ? 0.2273 0.2657 0.4008 0.0047  -0.0211 -0.0560 76  LYS   B NZ  
5222 N N   . VAL   B 77  ? 0.1935 0.2219 0.1787 0.0046  0.0185  0.0351  77  VAL   B N   
5223 C CA  . VAL   B 77  ? 0.1980 0.2167 0.1937 0.0083  0.0207  0.0594  77  VAL   B CA  
5224 C C   . VAL   B 77  ? 0.1840 0.1905 0.1877 0.0103  0.0314  0.0439  77  VAL   B C   
5225 O O   . VAL   B 77  ? 0.1882 0.1870 0.1961 0.0224  0.0349  0.0333  77  VAL   B O   
5226 C CB  . VAL   B 77  ? 0.2116 0.2253 0.2406 0.0073  0.0319  0.0731  77  VAL   B CB  
5227 C CG1 . VAL   B 77  ? 0.2111 0.2179 0.2609 -0.0003 0.0337  0.0868  77  VAL   B CG1 
5228 C CG2 . VAL   B 77  ? 0.2281 0.2422 0.2641 0.0061  0.0192  0.0785  77  VAL   B CG2 
5238 N N   . GLY   B 78  ? 0.1798 0.1785 0.1833 0.0059  0.0181  0.0328  78  GLY   B N   
5239 C CA  . GLY   B 78  ? 0.1816 0.1728 0.1851 0.0083  0.0258  0.0225  78  GLY   B CA  
5240 C C   . GLY   B 78  ? 0.1723 0.1651 0.1793 0.0103  0.0232  0.0325  78  GLY   B C   
5241 O O   . GLY   B 78  ? 0.1727 0.1615 0.2025 0.0186  0.0241  0.0314  78  GLY   B O   
5245 N N   . GLY   B 79  ? 0.1636 0.1672 0.1802 0.0075  0.0180  0.0206  79  GLY   B N   
5246 C CA  . GLY   B 79  ? 0.1663 0.1605 0.1632 0.0103  0.0117  0.0182  79  GLY   B CA  
5247 C C   . GLY   B 79  ? 0.1576 0.1562 0.1704 0.0135  0.0090  0.0098  79  GLY   B C   
5248 O O   . GLY   B 79  ? 0.1621 0.1541 0.1866 0.0082  0.0174  0.0198  79  GLY   B O   
5252 N N   . SER   B 80  ? 0.1562 0.1476 0.1732 0.0075  0.0202  0.0133  80  SER   B N   
5253 C CA  . SER   B 80  ? 0.1499 0.1491 0.1770 0.0001  0.0051  0.0122  80  SER   B CA  
5254 C C   . SER   B 80  ? 0.1482 0.1412 0.1759 0.0061  -0.0053 0.0124  80  SER   B C   
5255 O O   . SER   B 80  ? 0.1617 0.1429 0.2102 0.0068  0.0025  0.0061  80  SER   B O   
5256 C CB  . SER   B 80  ? 0.1554 0.1526 0.1780 -0.0024 0.0031  0.0160  80  SER   B CB  
5257 O OG  . SER   B 80  ? 0.1558 0.1708 0.2015 -0.0058 -0.0099 0.0142  80  SER   B OG  
5263 N N   . CYS   B 81  ? 0.1436 0.1370 0.1752 0.0011  -0.0094 -0.0009 81  CYS   B N   
5264 C CA  . CYS   B 81  ? 0.1517 0.1367 0.1795 0.0038  -0.0133 0.0052  81  CYS   B CA  
5265 C C   . CYS   B 81  ? 0.1482 0.1368 0.1465 0.0001  -0.0123 0.0060  81  CYS   B C   
5266 O O   . CYS   B 81  ? 0.1742 0.1357 0.1671 0.0072  -0.0015 0.0002  81  CYS   B O   
5267 C CB  . CYS   B 81  ? 0.1663 0.1478 0.1756 -0.0091 -0.0104 0.0033  81  CYS   B CB  
5268 S SG  . CYS   B 81  ? 0.1715 0.1645 0.1798 -0.0040 -0.0258 -0.0071 81  CYS   B SG  
5274 N N   . VAL   B 82  ? 0.1551 0.1358 0.1596 0.0027  -0.0130 0.0036  82  VAL   B N   
5275 C CA  . VAL   B 82  ? 0.1632 0.1355 0.1659 -0.0054 -0.0102 0.0062  82  VAL   B CA  
5276 C C   . VAL   B 82  ? 0.1717 0.1303 0.1786 -0.0031 -0.0113 0.0017  82  VAL   B C   
5277 O O   . VAL   B 82  ? 0.1758 0.1315 0.2152 -0.0055 -0.0067 -0.0151 82  VAL   B O   
5278 C CB  . VAL   B 82  ? 0.1708 0.1558 0.1742 -0.0006 -0.0150 0.0090  82  VAL   B CB  
5279 C CG1 . VAL   B 82  ? 0.1913 0.1808 0.1832 0.0043  -0.0239 0.0248  82  VAL   B CG1 
5280 C CG2 . VAL   B 82  ? 0.1773 0.1696 0.1868 -0.0051 -0.0266 0.0138  82  VAL   B CG2 
5290 N N   . LEU   B 83  ? 0.1599 0.1304 0.1792 -0.0127 -0.0251 -0.0113 83  LEU   B N   
5291 C CA  . LEU   B 83  ? 0.1565 0.1378 0.1639 -0.0155 -0.0193 0.0014  83  LEU   B CA  
5292 C C   . LEU   B 83  ? 0.1565 0.1323 0.1623 -0.0188 -0.0179 0.0035  83  LEU   B C   
5293 O O   . LEU   B 83  ? 0.1588 0.1432 0.1571 -0.0231 -0.0165 0.0048  83  LEU   B O   
5294 C CB  . LEU   B 83  ? 0.1634 0.1505 0.1674 -0.0124 -0.0245 -0.0138 83  LEU   B CB  
5295 C CG  . LEU   B 83  ? 0.1822 0.1765 0.1704 -0.0129 -0.0107 -0.0107 83  LEU   B CG  
5296 C CD1 . LEU   B 83  ? 0.1991 0.1732 0.1725 -0.0160 -0.0207 -0.0005 83  LEU   B CD1 
5297 C CD2 . LEU   B 83  ? 0.2020 0.1748 0.1920 -0.0098 -0.0204 -0.0284 83  LEU   B CD2 
5309 N N   . SER   B 84  ? 0.1645 0.1440 0.1875 -0.0242 -0.0210 0.0028  84  SER   B N   
5310 C CA  . SER   B 84  ? 0.1630 0.1673 0.1674 -0.0296 -0.0165 0.0149  84  SER   B CA  
5311 C C   . SER   B 84  ? 0.1580 0.1827 0.1303 -0.0236 -0.0213 0.0151  84  SER   B C   
5312 O O   . SER   B 84  ? 0.1677 0.1702 0.1343 -0.0206 -0.0150 0.0027  84  SER   B O   
5313 C CB  . SER   B 84  ? 0.1832 0.1713 0.2132 -0.0286 0.0070  0.0145  84  SER   B CB  
5314 O OG  . SER   B 84  ? 0.1838 0.1888 0.2453 -0.0454 0.0059  0.0221  84  SER   B OG  
5320 N N   . GLY   B 85  ? 0.1591 0.2006 0.1448 -0.0260 -0.0137 0.0213  85  GLY   B N   
5321 C CA  . GLY   B 85  ? 0.1610 0.2075 0.1686 -0.0367 0.0021  -0.0089 85  GLY   B CA  
5322 C C   . GLY   B 85  ? 0.1540 0.1980 0.1657 -0.0404 -0.0035 0.0055  85  GLY   B C   
5323 O O   . GLY   B 85  ? 0.1705 0.1955 0.1639 -0.0514 0.0149  -0.0117 85  GLY   B O   
5327 N N   . HIS   B 86  ? 0.1538 0.1818 0.1814 -0.0330 -0.0101 0.0118  86  HIS   B N   
5328 C CA  . HIS   B 86  ? 0.1620 0.1795 0.1780 -0.0368 -0.0188 0.0183  86  HIS   B CA  
5329 C C   . HIS   B 86  ? 0.1615 0.1897 0.1537 -0.0432 -0.0068 0.0328  86  HIS   B C   
5330 O O   . HIS   B 86  ? 0.1727 0.2029 0.1722 -0.0363 0.0026  0.0257  86  HIS   B O   
5331 C CB  . HIS   B 86  ? 0.1742 0.1853 0.1781 -0.0236 -0.0311 0.0112  86  HIS   B CB  
5332 C CG  . HIS   B 86  ? 0.1742 0.1956 0.1767 -0.0137 -0.0259 0.0151  86  HIS   B CG  
5333 N ND1 . HIS   B 86  ? 0.1836 0.2192 0.2006 -0.0255 -0.0254 -0.0097 86  HIS   B ND1 
5334 C CD2 . HIS   B 86  ? 0.1783 0.1972 0.1858 -0.0069 -0.0239 0.0090  86  HIS   B CD2 
5335 C CE1 . HIS   B 86  ? 0.1935 0.2118 0.1903 -0.0134 -0.0074 -0.0233 86  HIS   B CE1 
5336 N NE2 . HIS   B 86  ? 0.1892 0.2008 0.1831 0.0002  -0.0088 -0.0002 86  HIS   B NE2 
5344 N N   . ASN   B 87  ? 0.1637 0.1915 0.1786 -0.0305 0.0021  0.0221  87  ASN   B N   
5345 C CA  . ASN   B 87  ? 0.1738 0.2097 0.1843 -0.0326 0.0296  0.0147  87  ASN   B CA  
5346 C C   . ASN   B 87  ? 0.1940 0.1964 0.1683 -0.0314 0.0387  0.0102  87  ASN   B C   
5347 O O   . ASN   B 87  ? 0.2229 0.2043 0.1970 -0.0270 0.0571  0.0020  87  ASN   B O   
5348 C CB  . ASN   B 87  ? 0.1765 0.2417 0.2192 -0.0255 0.0305  0.0101  87  ASN   B CB  
5349 C CG  . ASN   B 87  ? 0.1816 0.2573 0.2179 0.0040  0.0404  0.0342  87  ASN   B CG  
5350 O OD1 . ASN   B 87  ? 0.1763 0.2503 0.2023 0.0155  0.0482  0.0469  87  ASN   B OD1 
5351 N ND2 . ASN   B 87  ? 0.2193 0.2611 0.2463 0.0099  0.0551  0.0264  87  ASN   B ND2 
5358 N N   . LEU   B 88  ? 0.1791 0.1856 0.1553 -0.0345 0.0164  0.0132  88  LEU   B N   
5359 C CA  . LEU   B 88  ? 0.1928 0.1792 0.1614 -0.0371 0.0040  -0.0032 88  LEU   B CA  
5360 C C   . LEU   B 88  ? 0.1871 0.1706 0.1640 -0.0434 -0.0007 -0.0055 88  LEU   B C   
5361 O O   . LEU   B 88  ? 0.2160 0.1805 0.2037 -0.0215 -0.0256 -0.0116 88  LEU   B O   
5362 C CB  . LEU   B 88  ? 0.2061 0.1857 0.1812 -0.0478 -0.0135 0.0117  88  LEU   B CB  
5363 C CG  . LEU   B 88  ? 0.2422 0.2098 0.1998 -0.0419 -0.0284 0.0326  88  LEU   B CG  
5364 C CD1 . LEU   B 88  ? 0.2588 0.2365 0.2127 -0.0565 -0.0160 0.0526  88  LEU   B CD1 
5365 C CD2 . LEU   B 88  ? 0.2727 0.2322 0.2584 -0.0020 -0.0485 0.0068  88  LEU   B CD2 
5377 N N   . ALA   B 89  ? 0.1679 0.1697 0.1602 -0.0443 0.0157  -0.0020 89  ALA   B N   
5378 C CA  . ALA   B 89  ? 0.1714 0.1644 0.1418 -0.0439 0.0015  0.0107  89  ALA   B CA  
5379 C C   . ALA   B 89  ? 0.1792 0.1658 0.1394 -0.0491 0.0134  0.0082  89  ALA   B C   
5380 O O   . ALA   B 89  ? 0.1583 0.1731 0.1829 -0.0451 0.0130  -0.0237 89  ALA   B O   
5381 C CB  . ALA   B 89  ? 0.1606 0.1634 0.1658 -0.0385 -0.0003 0.0155  89  ALA   B CB  
5387 N N   . LYS   B 90  ? 0.2151 0.1532 0.1439 -0.0527 -0.0098 0.0173  90  LYS   B N   
5388 C CA  . LYS   B 90  ? 0.2185 0.1512 0.1458 -0.0489 -0.0121 0.0215  90  LYS   B CA  
5389 C C   . LYS   B 90  ? 0.1939 0.1440 0.1522 -0.0413 -0.0161 0.0052  90  LYS   B C   
5390 O O   . LYS   B 90  ? 0.2009 0.1581 0.1760 -0.0508 -0.0051 0.0031  90  LYS   B O   
5391 C CB  . LYS   B 90  ? 0.2311 0.1573 0.1815 -0.0424 -0.0105 0.0202  90  LYS   B CB  
5392 C CG  . LYS   B 90  ? 0.2254 0.1710 0.1746 -0.0268 0.0146  0.0106  90  LYS   B CG  
5393 C CD  . LYS   B 90  ? 0.2424 0.1826 0.2083 -0.0141 0.0363  0.0015  90  LYS   B CD  
5394 C CE  . LYS   B 90  ? 0.2436 0.2040 0.2604 -0.0145 0.0449  -0.0082 90  LYS   B CE  
5395 N NZ  . LYS   B 90  ? 0.2490 0.1925 0.2563 -0.0248 0.0659  -0.0154 90  LYS   B NZ  
5409 N N   . HIS   B 91  ? 0.1754 0.1400 0.1350 -0.0312 -0.0148 0.0088  91  HIS   B N   
5410 C CA  . HIS   B 91  ? 0.1651 0.1345 0.1578 -0.0240 -0.0211 0.0081  91  HIS   B CA  
5411 C C   . HIS   B 91  ? 0.1558 0.1421 0.1298 -0.0265 -0.0065 0.0047  91  HIS   B C   
5412 O O   . HIS   B 91  ? 0.1756 0.1443 0.1364 -0.0290 -0.0193 0.0027  91  HIS   B O   
5413 C CB  . HIS   B 91  ? 0.1822 0.1371 0.2022 -0.0137 -0.0125 0.0128  91  HIS   B CB  
5414 C CG  . HIS   B 91  ? 0.2217 0.1591 0.2593 -0.0016 0.0197  0.0269  91  HIS   B CG  
5415 N ND1 . HIS   B 91  ? 0.2482 0.1641 0.3170 0.0003  0.0295  0.0100  91  HIS   B ND1 
5416 C CD2 . HIS   B 91  ? 0.2355 0.1903 0.3063 0.0187  0.0058  0.0607  91  HIS   B CD2 
5417 C CE1 . HIS   B 91  ? 0.2528 0.1820 0.3355 0.0168  0.0261  0.0124  91  HIS   B CE1 
5418 N NE2 . HIS   B 91  ? 0.2482 0.1967 0.3366 0.0306  0.0187  0.0626  91  HIS   B NE2 
5426 N N   . CYS   B 92  ? 0.1538 0.1401 0.1334 -0.0298 -0.0125 -0.0043 92  CYS   B N   
5427 C CA  . CYS   B 92  ? 0.1494 0.1355 0.1290 -0.0246 -0.0092 -0.0024 92  CYS   B CA  
5428 C C   . CYS   B 92  ? 0.1489 0.1319 0.1244 -0.0146 -0.0065 0.0011  92  CYS   B C   
5429 O O   . CYS   B 92  ? 0.1571 0.1370 0.1556 -0.0153 -0.0072 0.0039  92  CYS   B O   
5430 C CB  . CYS   B 92  ? 0.1501 0.1402 0.1358 -0.0130 -0.0069 0.0052  92  CYS   B CB  
5431 S SG  . CYS   B 92  ? 0.1514 0.1450 0.1646 -0.0120 -0.0124 0.0066  92  CYS   B SG  
5437 N N   . LEU   B 93  ? 0.1362 0.1346 0.1441 -0.0172 -0.0081 -0.0017 93  LEU   B N   
5438 C CA  . LEU   B 93  ? 0.1399 0.1372 0.1375 -0.0078 -0.0147 0.0048  93  LEU   B CA  
5439 C C   . LEU   B 93  ? 0.1366 0.1347 0.1261 -0.0036 -0.0124 0.0150  93  LEU   B C   
5440 O O   . LEU   B 93  ? 0.1467 0.1292 0.1516 -0.0091 -0.0126 0.0039  93  LEU   B O   
5441 C CB  . LEU   B 93  ? 0.1429 0.1367 0.1615 -0.0036 -0.0089 0.0128  93  LEU   B CB  
5442 C CG  . LEU   B 93  ? 0.1401 0.1456 0.1800 -0.0059 -0.0082 0.0161  93  LEU   B CG  
5443 C CD1 . LEU   B 93  ? 0.1492 0.1548 0.1806 0.0077  -0.0030 0.0012  93  LEU   B CD1 
5444 C CD2 . LEU   B 93  ? 0.1416 0.1455 0.1740 -0.0044 -0.0128 0.0023  93  LEU   B CD2 
5456 N N   . HIS   B 94  ? 0.1404 0.1329 0.1270 -0.0079 -0.0135 0.0104  94  HIS   B N   
5457 C CA  . HIS   B 94  ? 0.1504 0.1296 0.1297 -0.0033 -0.0091 0.0111  94  HIS   B CA  
5458 C C   . HIS   B 94  ? 0.1405 0.1317 0.1573 -0.0040 -0.0115 0.0166  94  HIS   B C   
5459 O O   . HIS   B 94  ? 0.1401 0.1443 0.1980 -0.0071 0.0110  -0.0047 94  HIS   B O   
5460 C CB  . HIS   B 94  ? 0.1440 0.1390 0.1462 -0.0029 -0.0141 0.0085  94  HIS   B CB  
5461 C CG  . HIS   B 94  ? 0.1502 0.1302 0.1447 -0.0096 -0.0251 0.0048  94  HIS   B CG  
5462 N ND1 . HIS   B 94  ? 0.1524 0.1376 0.1484 -0.0063 -0.0223 0.0028  94  HIS   B ND1 
5463 C CD2 . HIS   B 94  ? 0.1455 0.1377 0.1559 -0.0041 -0.0148 -0.0006 94  HIS   B CD2 
5464 C CE1 . HIS   B 94  ? 0.1508 0.1391 0.1567 -0.0118 -0.0234 -0.0024 94  HIS   B CE1 
5465 N NE2 . HIS   B 94  ? 0.1422 0.1428 0.1594 -0.0129 -0.0149 -0.0033 94  HIS   B NE2 
5473 N N   . VAL   B 95  ? 0.1392 0.1297 0.1528 -0.0014 -0.0079 0.0104  95  VAL   B N   
5474 C CA  . VAL   B 95  ? 0.1357 0.1366 0.1414 -0.0020 0.0011  0.0173  95  VAL   B CA  
5475 C C   . VAL   B 95  ? 0.1432 0.1340 0.1518 -0.0008 0.0111  0.0119  95  VAL   B C   
5476 O O   . VAL   B 95  ? 0.1527 0.1319 0.1750 0.0057  0.0013  0.0176  95  VAL   B O   
5477 C CB  . VAL   B 95  ? 0.1429 0.1401 0.1638 -0.0075 -0.0109 0.0138  95  VAL   B CB  
5478 C CG1 . VAL   B 95  ? 0.1600 0.1537 0.1821 -0.0098 -0.0011 0.0195  95  VAL   B CG1 
5479 C CG2 . VAL   B 95  ? 0.1491 0.1414 0.1509 0.0009  -0.0120 0.0081  95  VAL   B CG2 
5489 N N   . VAL   B 96  ? 0.1530 0.1411 0.1606 0.0081  0.0058  0.0167  96  VAL   B N   
5490 C CA  . VAL   B 96  ? 0.1679 0.1535 0.1511 0.0061  0.0086  0.0192  96  VAL   B CA  
5491 C C   . VAL   B 96  ? 0.1762 0.1515 0.1786 0.0062  0.0114  0.0225  96  VAL   B C   
5492 O O   . VAL   B 96  ? 0.1731 0.1600 0.1850 -0.0029 0.0217  0.0072  96  VAL   B O   
5493 C CB  . VAL   B 96  ? 0.1736 0.1761 0.1564 0.0070  0.0018  0.0154  96  VAL   B CB  
5494 C CG1 . VAL   B 96  ? 0.1795 0.1926 0.1644 0.0133  0.0134  0.0136  96  VAL   B CG1 
5495 C CG2 . VAL   B 96  ? 0.1833 0.1745 0.1623 0.0027  0.0128  0.0157  96  VAL   B CG2 
5505 N N   . GLY   B 97  ? 0.1778 0.1538 0.1623 0.0053  0.0050  0.0266  97  GLY   B N   
5506 C CA  . GLY   B 97  ? 0.1948 0.1530 0.1737 0.0054  0.0085  0.0255  97  GLY   B CA  
5507 C C   . GLY   B 97  ? 0.2226 0.1693 0.1823 0.0101  0.0135  0.0263  97  GLY   B C   
5508 O O   . GLY   B 97  ? 0.2392 0.1756 0.1779 0.0040  0.0047  0.0207  97  GLY   B O   
5512 N N   . PRO   B 98  ? 0.2398 0.1780 0.1971 0.0152  0.0467  0.0409  98  PRO   B N   
5513 C CA  . PRO   B 98  ? 0.2580 0.1976 0.1983 0.0312  0.0668  0.0404  98  PRO   B CA  
5514 C C   . PRO   B 98  ? 0.2729 0.1943 0.1706 0.0502  0.0655  0.0592  98  PRO   B C   
5515 O O   . PRO   B 98  ? 0.2611 0.1888 0.1998 0.0373  0.0635  0.0515  98  PRO   B O   
5516 C CB  . PRO   B 98  ? 0.2489 0.2086 0.2288 0.0280  0.0788  0.0448  98  PRO   B CB  
5517 C CG  . PRO   B 98  ? 0.2360 0.1968 0.2331 0.0218  0.0685  0.0584  98  PRO   B CG  
5518 C CD  . PRO   B 98  ? 0.2222 0.1834 0.2246 0.0244  0.0588  0.0495  98  PRO   B CD  
5526 N N   . ASN   B 99  ? 0.2913 0.2185 0.1766 0.0753  0.0720  0.0459  99  ASN   B N   
5527 C CA  . ASN   B 99  ? 0.3115 0.2337 0.1961 0.0902  0.0636  0.0710  99  ASN   B CA  
5528 C C   . ASN   B 99  ? 0.3397 0.2741 0.2480 0.0843  0.0805  0.1061  99  ASN   B C   
5529 O O   . ASN   B 99  ? 0.3491 0.2830 0.2629 0.0917  0.0755  0.1046  99  ASN   B O   
5530 C CB  . ASN   B 99  ? 0.3207 0.2313 0.2041 0.0846  0.0472  0.0571  99  ASN   B CB  
5531 C CG  . ASN   B 99  ? 0.3251 0.2336 0.2191 0.0749  0.0362  0.0504  99  ASN   B CG  
5532 O OD1 . ASN   B 99  ? 0.3238 0.2319 0.2511 0.0851  0.0439  0.0503  99  ASN   B OD1 
5533 N ND2 . ASN   B 99  ? 0.3240 0.2351 0.2272 0.0711  0.0124  0.0489  99  ASN   B ND2 
5540 N N   A VAL   B 100 ? 0.3542 0.2883 0.2937 0.0639  0.0954  0.1317  100 VAL   B N   
5541 N N   B VAL   B 100 ? 0.3606 0.2898 0.2952 0.0686  0.0686  0.1134  100 VAL   B N   
5542 C CA  A VAL   B 100 ? 0.3791 0.3118 0.3536 0.0468  0.0807  0.1481  100 VAL   B CA  
5543 C CA  B VAL   B 100 ? 0.3844 0.3101 0.3397 0.0538  0.0504  0.1203  100 VAL   B CA  
5544 C C   A VAL   B 100 ? 0.4012 0.3243 0.3417 0.0519  0.0689  0.1633  100 VAL   B C   
5545 C C   B VAL   B 100 ? 0.4028 0.3214 0.3406 0.0535  0.0458  0.1433  100 VAL   B C   
5546 O O   A VAL   B 100 ? 0.4067 0.3392 0.3519 0.0491  0.0823  0.1499  100 VAL   B O   
5547 O O   B VAL   B 100 ? 0.4050 0.3264 0.3457 0.0489  0.0486  0.1355  100 VAL   B O   
5548 C CB  A VAL   B 100 ? 0.3836 0.3241 0.4234 0.0184  0.0738  0.1554  100 VAL   B CB  
5549 C CB  B VAL   B 100 ? 0.3890 0.3194 0.3806 0.0382  0.0377  0.1103  100 VAL   B CB  
5550 C CG1 A VAL   B 100 ? 0.3867 0.3310 0.4486 0.0086  0.0698  0.1517  100 VAL   B CG1 
5551 C CG1 B VAL   B 100 ? 0.3909 0.3235 0.3938 0.0327  0.0334  0.1059  100 VAL   B CG1 
5552 C CG2 A VAL   B 100 ? 0.3823 0.3268 0.4377 0.0088  0.0760  0.1675  100 VAL   B CG2 
5553 C CG2 B VAL   B 100 ? 0.3896 0.3221 0.3923 0.0331  0.0338  0.1091  100 VAL   B CG2 
5572 N N   . ASN   B 101 ? 0.4173 0.3274 0.3338 0.0592  0.0417  0.1632  101 ASN   B N   
5573 C CA  . ASN   B 101 ? 0.4557 0.3463 0.3464 0.0584  0.0129  0.1696  101 ASN   B CA  
5574 C C   . ASN   B 101 ? 0.5101 0.3996 0.3641 0.0489  -0.0021 0.1635  101 ASN   B C   
5575 O O   . ASN   B 101 ? 0.5119 0.4075 0.3801 0.0556  0.0002  0.1398  101 ASN   B O   
5576 C CB  . ASN   B 101 ? 0.4437 0.3256 0.3521 0.0532  0.0139  0.1446  101 ASN   B CB  
5577 C CG  . ASN   B 101 ? 0.4291 0.3044 0.3517 0.0497  0.0114  0.1372  101 ASN   B CG  
5578 O OD1 . ASN   B 101 ? 0.4300 0.3038 0.3823 0.0406  0.0264  0.1265  101 ASN   B OD1 
5579 N ND2 . ASN   B 101 ? 0.4179 0.2955 0.3501 0.0492  0.0038  0.1193  101 ASN   B ND2 
5587 N N   A LYS   B 102 ? 0.5394 0.4281 0.3840 0.0361  -0.0009 0.1557  102 LYS   B N   
5588 N N   B LYS   B 102 ? 0.5325 0.4280 0.3916 0.0397  -0.0031 0.1465  102 LYS   B N   
5589 C CA  A LYS   B 102 ? 0.5669 0.4627 0.4161 0.0221  0.0037  0.1310  102 LYS   B CA  
5590 C CA  B LYS   B 102 ? 0.5523 0.4569 0.4246 0.0299  -0.0006 0.1239  102 LYS   B CA  
5591 C C   A LYS   B 102 ? 0.5658 0.4637 0.3989 0.0259  0.0048  0.1369  102 LYS   B C   
5592 C C   B LYS   B 102 ? 0.5567 0.4612 0.4123 0.0287  0.0057  0.1312  102 LYS   B C   
5593 O O   A LYS   B 102 ? 0.5736 0.4669 0.3981 0.0256  -0.0055 0.1418  102 LYS   B O   
5594 O O   B LYS   B 102 ? 0.5610 0.4650 0.4156 0.0265  0.0002  0.1342  102 LYS   B O   
5595 C CB  A LYS   B 102 ? 0.5922 0.4947 0.4756 0.0066  0.0165  0.0889  102 LYS   B CB  
5596 C CB  B LYS   B 102 ? 0.5647 0.4789 0.4706 0.0218  0.0000  0.0876  102 LYS   B CB  
5597 C CG  A LYS   B 102 ? 0.6134 0.5208 0.5411 -0.0057 0.0286  0.0448  102 LYS   B CG  
5598 C CG  B LYS   B 102 ? 0.5742 0.4967 0.5172 0.0152  0.0017  0.0534  102 LYS   B CG  
5599 C CD  A LYS   B 102 ? 0.6301 0.5414 0.6008 -0.0158 0.0404  0.0089  102 LYS   B CD  
5600 C CD  B LYS   B 102 ? 0.5818 0.5106 0.5576 0.0103  0.0043  0.0252  102 LYS   B CD  
5601 C CE  A LYS   B 102 ? 0.6406 0.5563 0.6481 -0.0238 0.0511  -0.0159 102 LYS   B CE  
5602 C CE  B LYS   B 102 ? 0.5870 0.5206 0.5897 0.0072  0.0072  0.0047  102 LYS   B CE  
5603 N NZ  A LYS   B 102 ? 0.6461 0.5649 0.6745 -0.0273 0.0562  -0.0314 102 LYS   B NZ  
5604 N NZ  B LYS   B 102 ? 0.5902 0.5266 0.6075 0.0058  0.0084  -0.0063 102 LYS   B NZ  
5631 N N   . GLY   B 103 ? 0.5541 0.4589 0.4005 0.0295  0.0199  0.1295  103 GLY   B N   
5632 C CA  . GLY   B 103 ? 0.5380 0.4534 0.4113 0.0341  0.0507  0.1100  103 GLY   B CA  
5633 C C   . GLY   B 103 ? 0.5176 0.4460 0.4148 0.0347  0.0770  0.0857  103 GLY   B C   
5634 O O   . GLY   B 103 ? 0.5237 0.4510 0.4149 0.0317  0.0857  0.0871  103 GLY   B O   
5639 N N   A GLU   B 104 ? 0.5028 0.4350 0.4025 0.0424  0.1004  0.0710  104 GLU   B N   
5640 N N   B GLU   B 104 ? 0.5032 0.4415 0.4149 0.0303  0.0691  0.0674  104 GLU   B N   
5641 C CA  A GLU   B 104 ? 0.4879 0.4216 0.3933 0.0537  0.1150  0.0565  104 GLU   B CA  
5642 C CA  B GLU   B 104 ? 0.4884 0.4352 0.4146 0.0267  0.0585  0.0468  104 GLU   B CA  
5643 C C   A GLU   B 104 ? 0.4872 0.4234 0.4008 0.0360  0.1595  0.0651  104 GLU   B C   
5644 C C   B GLU   B 104 ? 0.4817 0.4350 0.4244 0.0198  0.0695  0.0411  104 GLU   B C   
5645 O O   A GLU   B 104 ? 0.4854 0.4227 0.4234 0.0328  0.1681  0.0676  104 GLU   B O   
5646 O O   B GLU   B 104 ? 0.4807 0.4345 0.4335 0.0188  0.0721  0.0405  104 GLU   B O   
5647 C CB  A GLU   B 104 ? 0.4769 0.4040 0.3823 0.0837  0.0758  0.0224  104 GLU   B CB  
5648 C CB  B GLU   B 104 ? 0.4817 0.4280 0.4026 0.0298  0.0352  0.0280  104 GLU   B CB  
5649 C CG  A GLU   B 104 ? 0.4653 0.3896 0.3690 0.1112  0.0287  -0.0128 104 GLU   B CG  
5650 C CG  B GLU   B 104 ? 0.4751 0.4216 0.3915 0.0320  0.0098  0.0090  104 GLU   B CG  
5651 C CD  A GLU   B 104 ? 0.4537 0.3771 0.3487 0.1328  -0.0068 -0.0396 104 GLU   B CD  
5652 C CD  B GLU   B 104 ? 0.4692 0.4157 0.3802 0.0327  -0.0095 -0.0066 104 GLU   B CD  
5653 O OE1 A GLU   B 104 ? 0.4415 0.3643 0.3096 0.1462  -0.0055 -0.0543 104 GLU   B OE1 
5654 O OE1 B GLU   B 104 ? 0.4655 0.4123 0.3702 0.0317  -0.0131 -0.0119 104 GLU   B OE1 
5655 O OE2 A GLU   B 104 ? 0.4537 0.3792 0.3502 0.1357  -0.0319 -0.0495 104 GLU   B OE2 
5656 O OE2 B GLU   B 104 ? 0.4679 0.4143 0.3781 0.0333  -0.0205 -0.0137 104 GLU   B OE2 
5669 N N   A ASP   B 105 ? 0.4833 0.4243 0.3864 0.0237  0.1960  0.0677  105 ASP   B N   
5670 N N   B ASP   B 105 ? 0.4747 0.4345 0.4251 0.0144  0.0779  0.0355  105 ASP   B N   
5671 C CA  A ASP   B 105 ? 0.4801 0.4216 0.3983 0.0125  0.2223  0.0548  105 ASP   B CA  
5672 C CA  B ASP   B 105 ? 0.4677 0.4319 0.4297 0.0093  0.0846  0.0273  105 ASP   B CA  
5673 C C   A ASP   B 105 ? 0.4554 0.3853 0.3592 -0.0069 0.2301  0.0524  105 ASP   B C   
5674 C C   B ASP   B 105 ? 0.4536 0.4167 0.4047 0.0019  0.0875  0.0211  105 ASP   B C   
5675 O O   A ASP   B 105 ? 0.4389 0.3796 0.3441 -0.0038 0.2224  0.0526  105 ASP   B O   
5676 O O   B ASP   B 105 ? 0.4533 0.4167 0.3962 0.0031  0.0905  0.0224  105 ASP   B O   
5677 C CB  A ASP   B 105 ? 0.4967 0.4481 0.4763 0.0245  0.2270  0.0372  105 ASP   B CB  
5678 C CB  B ASP   B 105 ? 0.4720 0.4416 0.4650 0.0130  0.0860  0.0240  105 ASP   B CB  
5679 C CG  A ASP   B 105 ? 0.5062 0.4664 0.5522 0.0311  0.2349  0.0264  105 ASP   B CG  
5680 C CG  B ASP   B 105 ? 0.4745 0.4478 0.4981 0.0151  0.0876  0.0228  105 ASP   B CG  
5681 O OD1 A ASP   B 105 ? 0.5063 0.4718 0.5643 0.0278  0.2519  0.0315  105 ASP   B OD1 
5682 O OD1 B ASP   B 105 ? 0.4743 0.4490 0.5076 0.0139  0.0900  0.0244  105 ASP   B OD1 
5683 O OD2 A ASP   B 105 ? 0.5096 0.4733 0.5949 0.0380  0.2309  0.0154  105 ASP   B OD2 
5684 O OD2 B ASP   B 105 ? 0.4745 0.4509 0.5123 0.0166  0.0888  0.0224  105 ASP   B OD2 
5693 N N   A ILE   B 106 ? 0.4418 0.3540 0.3687 -0.0217 0.2126  0.0484  106 ILE   B N   
5694 N N   B ILE   B 106 ? 0.4392 0.4006 0.3940 -0.0038 0.0827  0.0152  106 ILE   B N   
5695 C CA  A ILE   B 106 ? 0.4230 0.3220 0.3802 -0.0394 0.2118  0.0407  106 ILE   B CA  
5696 C CA  B ILE   B 106 ? 0.4243 0.3865 0.3870 -0.0086 0.0816  0.0083  106 ILE   B CA  
5697 C C   A ILE   B 106 ? 0.3867 0.3089 0.3686 -0.0379 0.2136  0.0312  106 ILE   B C   
5698 C C   B ILE   B 106 ? 0.4038 0.3763 0.3804 -0.0057 0.0828  0.0037  106 ILE   B C   
5699 O O   A ILE   B 106 ? 0.3771 0.2846 0.3747 -0.0446 0.2085  0.0319  106 ILE   B O   
5700 O O   B ILE   B 106 ? 0.4025 0.3732 0.3788 -0.0076 0.0805  0.0014  106 ILE   B O   
5701 C CB  A ILE   B 106 ? 0.4443 0.3120 0.3971 -0.0537 0.2006  0.0394  106 ILE   B CB  
5702 C CB  B ILE   B 106 ? 0.4302 0.3852 0.3888 -0.0151 0.0782  0.0061  106 ILE   B CB  
5703 C CG1 A ILE   B 106 ? 0.4544 0.3107 0.3978 -0.0526 0.1872  0.0291  106 ILE   B CG1 
5704 C CG1 B ILE   B 106 ? 0.4334 0.3844 0.3861 -0.0168 0.0740  0.0043  106 ILE   B CG1 
5705 C CG2 A ILE   B 106 ? 0.4516 0.3155 0.4223 -0.0586 0.1997  0.0391  106 ILE   B CG2 
5706 C CG2 B ILE   B 106 ? 0.4319 0.3872 0.3964 -0.0167 0.0786  0.0051  106 ILE   B CG2 
5707 C CD1 A ILE   B 106 ? 0.4598 0.3149 0.3880 -0.0480 0.1831  0.0249  106 ILE   B CD1 
5708 C CD1 B ILE   B 106 ? 0.4352 0.3850 0.3836 -0.0164 0.0716  0.0032  106 ILE   B CD1 
5731 N N   A GLN   B 107 ? 0.3662 0.3244 0.3756 -0.0339 0.1997  0.0301  107 GLN   B N   
5732 N N   B GLN   B 107 ? 0.3854 0.3696 0.3835 -0.0030 0.0840  0.0042  107 GLN   B N   
5733 C CA  A GLN   B 107 ? 0.3408 0.3360 0.3848 -0.0325 0.1775  0.0298  107 GLN   B CA  
5734 C CA  B GLN   B 107 ? 0.3643 0.3600 0.3874 -0.0013 0.0827  0.0085  107 GLN   B CA  
5735 C C   A GLN   B 107 ? 0.3079 0.3096 0.3519 -0.0187 0.1419  0.0164  107 GLN   B C   
5736 C C   B GLN   B 107 ? 0.3257 0.3272 0.3496 0.0033  0.0955  0.0092  107 GLN   B C   
5737 O O   A GLN   B 107 ? 0.2949 0.3069 0.3776 -0.0138 0.1128  -0.0105 107 GLN   B O   
5738 O O   B GLN   B 107 ? 0.3239 0.3283 0.3549 0.0054  0.0838  -0.0000 107 GLN   B O   
5739 C CB  A GLN   B 107 ? 0.3679 0.3786 0.4598 -0.0350 0.1533  0.0340  107 GLN   B CB  
5740 C CB  B GLN   B 107 ? 0.3836 0.3825 0.4358 -0.0030 0.0677  0.0110  107 GLN   B CB  
5741 C CG  A GLN   B 107 ? 0.3991 0.4162 0.5328 -0.0312 0.1123  0.0337  107 GLN   B CG  
5742 C CG  B GLN   B 107 ? 0.4016 0.4022 0.4821 -0.0029 0.0507  0.0132  107 GLN   B CG  
5743 C CD  A GLN   B 107 ? 0.4239 0.4448 0.5864 -0.0283 0.0836  0.0381  107 GLN   B CD  
5744 C CD  B GLN   B 107 ? 0.4158 0.4170 0.5184 -0.0024 0.0381  0.0165  107 GLN   B CD  
5745 O OE1 A GLN   B 107 ? 0.4321 0.4558 0.6054 -0.0219 0.0777  0.0370  107 GLN   B OE1 
5746 O OE1 B GLN   B 107 ? 0.4198 0.4223 0.5295 -0.0002 0.0357  0.0173  107 GLN   B OE1 
5747 N NE2 A GLN   B 107 ? 0.4360 0.4542 0.6056 -0.0275 0.0701  0.0417  107 GLN   B NE2 
5748 N NE2 B GLN   B 107 ? 0.4222 0.4220 0.5327 -0.0021 0.0325  0.0181  107 GLN   B NE2 
5765 N N   . LEU   B 108 ? 0.2865 0.2926 0.3117 0.0102  0.1176  0.0175  108 LEU   B N   
5766 C CA  . LEU   B 108 ? 0.2530 0.2580 0.2666 0.0286  0.0854  0.0315  108 LEU   B CA  
5767 C C   . LEU   B 108 ? 0.2112 0.2059 0.2574 0.0233  0.0489  0.0293  108 LEU   B C   
5768 O O   . LEU   B 108 ? 0.2022 0.1938 0.2483 0.0237  0.0380  0.0262  108 LEU   B O   
5769 C CB  . LEU   B 108 ? 0.2700 0.2857 0.2508 0.0326  0.0882  0.0468  108 LEU   B CB  
5770 C CG  . LEU   B 108 ? 0.2865 0.3195 0.2655 0.0373  0.0812  0.0289  108 LEU   B CG  
5771 C CD1 . LEU   B 108 ? 0.3033 0.3396 0.2579 0.0291  0.0790  0.0330  108 LEU   B CD1 
5772 C CD2 . LEU   B 108 ? 0.2927 0.3271 0.2743 0.0448  0.0641  0.0123  108 LEU   B CD2 
5785 N N   . LEU   B 109 ? 0.1899 0.1821 0.2601 0.0059  0.0452  0.0284  109 LEU   B N   
5786 C CA  . LEU   B 109 ? 0.1699 0.1599 0.2670 0.0035  0.0428  0.0330  109 LEU   B CA  
5787 C C   . LEU   B 109 ? 0.1585 0.1458 0.2683 -0.0016 0.0393  0.0202  109 LEU   B C   
5788 O O   . LEU   B 109 ? 0.1562 0.1416 0.2579 0.0034  0.0390  0.0296  109 LEU   B O   
5789 C CB  . LEU   B 109 ? 0.1839 0.1469 0.2712 0.0033  0.0292  0.0389  109 LEU   B CB  
5790 C CG  . LEU   B 109 ? 0.1782 0.1432 0.2562 0.0052  0.0246  0.0277  109 LEU   B CG  
5791 C CD1 . LEU   B 109 ? 0.1687 0.1559 0.2468 0.0101  0.0263  0.0239  109 LEU   B CD1 
5792 C CD2 . LEU   B 109 ? 0.1872 0.1575 0.2606 0.0048  0.0174  0.0260  109 LEU   B CD2 
5804 N N   . LYS   B 110 ? 0.1579 0.1420 0.2606 -0.0057 0.0326  0.0223  110 LYS   B N   
5805 C CA  . LYS   B 110 ? 0.1526 0.1434 0.2681 -0.0059 0.0292  0.0194  110 LYS   B CA  
5806 C C   . LYS   B 110 ? 0.1511 0.1467 0.2451 -0.0050 0.0359  0.0170  110 LYS   B C   
5807 O O   . LYS   B 110 ? 0.1498 0.1467 0.2410 -0.0080 0.0266  0.0095  110 LYS   B O   
5808 C CB  . LYS   B 110 ? 0.1578 0.1430 0.2835 -0.0034 0.0299  0.0199  110 LYS   B CB  
5809 C CG  . LYS   B 110 ? 0.1548 0.1412 0.2908 -0.0087 0.0223  0.0219  110 LYS   B CG  
5810 C CD  . LYS   B 110 ? 0.1654 0.1470 0.2963 -0.0103 0.0165  0.0238  110 LYS   B CD  
5811 C CE  . LYS   B 110 ? 0.1614 0.1593 0.3161 -0.0024 0.0183  0.0127  110 LYS   B CE  
5812 N NZ  . LYS   B 110 ? 0.1622 0.1777 0.3111 0.0021  0.0099  0.0107  110 LYS   B NZ  
5826 N N   . SER   B 111 ? 0.1522 0.1466 0.2515 -0.0073 0.0245  0.0173  111 SER   B N   
5827 C CA  . SER   B 111 ? 0.1634 0.1464 0.2445 -0.0046 0.0178  0.0227  111 SER   B CA  
5828 C C   . SER   B 111 ? 0.1574 0.1380 0.2286 -0.0040 0.0140  0.0096  111 SER   B C   
5829 O O   . SER   B 111 ? 0.1526 0.1423 0.2387 -0.0036 0.0086  0.0043  111 SER   B O   
5830 C CB  . SER   B 111 ? 0.1738 0.1662 0.2467 0.0028  0.0343  0.0300  111 SER   B CB  
5831 O OG  . SER   B 111 ? 0.1915 0.1963 0.2507 0.0073  0.0375  0.0341  111 SER   B OG  
5837 N N   . ALA   B 112 ? 0.1475 0.1458 0.2317 0.0066  0.0262  0.0179  112 ALA   B N   
5838 C CA  . ALA   B 112 ? 0.1430 0.1520 0.2113 -0.0009 0.0135  0.0059  112 ALA   B CA  
5839 C C   . ALA   B 112 ? 0.1285 0.1460 0.2103 -0.0002 0.0063  0.0091  112 ALA   B C   
5840 O O   . ALA   B 112 ? 0.1378 0.1451 0.2220 -0.0082 0.0078  0.0019  112 ALA   B O   
5841 C CB  . ALA   B 112 ? 0.1499 0.1490 0.2211 0.0021  0.0086  0.0157  112 ALA   B CB  
5847 N N   . TYR   B 113 ? 0.1344 0.1330 0.2171 -0.0014 0.0082  0.0070  113 TYR   B N   
5848 C CA  . TYR   B 113 ? 0.1349 0.1357 0.2204 -0.0025 0.0173  0.0015  113 TYR   B CA  
5849 C C   . TYR   B 113 ? 0.1342 0.1274 0.2184 -0.0056 0.0102  0.0017  113 TYR   B C   
5850 O O   . TYR   B 113 ? 0.1408 0.1340 0.2093 -0.0069 0.0012  -0.0004 113 TYR   B O   
5851 C CB  . TYR   B 113 ? 0.1424 0.1230 0.2285 -0.0044 0.0164  0.0084  113 TYR   B CB  
5852 C CG  . TYR   B 113 ? 0.1472 0.1276 0.2344 -0.0093 0.0114  0.0160  113 TYR   B CG  
5853 C CD1 . TYR   B 113 ? 0.1449 0.1352 0.2454 -0.0081 0.0077  0.0234  113 TYR   B CD1 
5854 C CD2 . TYR   B 113 ? 0.1540 0.1253 0.2410 -0.0096 0.0049  0.0088  113 TYR   B CD2 
5855 C CE1 . TYR   B 113 ? 0.1532 0.1391 0.2296 -0.0006 0.0190  0.0088  113 TYR   B CE1 
5856 C CE2 . TYR   B 113 ? 0.1569 0.1254 0.2430 -0.0050 0.0085  0.0137  113 TYR   B CE2 
5857 C CZ  . TYR   B 113 ? 0.1500 0.1359 0.2423 0.0035  0.0076  0.0141  113 TYR   B CZ  
5858 O OH  . TYR   B 113 ? 0.1583 0.1306 0.2752 0.0116  0.0161  0.0050  113 TYR   B OH  
5868 N N   . GLU   B 114 ? 0.1358 0.1245 0.2228 -0.0041 0.0129  -0.0005 114 GLU   B N   
5869 C CA  . GLU   B 114 ? 0.1354 0.1232 0.2227 0.0037  0.0083  0.0018  114 GLU   B CA  
5870 C C   . GLU   B 114 ? 0.1364 0.1216 0.2216 -0.0047 0.0079  0.0017  114 GLU   B C   
5871 O O   . GLU   B 114 ? 0.1358 0.1250 0.2416 0.0010  -0.0009 0.0133  114 GLU   B O   
5872 C CB  . GLU   B 114 ? 0.1402 0.1337 0.2398 -0.0037 0.0168  0.0075  114 GLU   B CB  
5873 C CG  . GLU   B 114 ? 0.1440 0.1320 0.2476 -0.0073 0.0138  0.0029  114 GLU   B CG  
5874 C CD  . GLU   B 114 ? 0.1456 0.1278 0.2511 -0.0147 0.0139  0.0099  114 GLU   B CD  
5875 O OE1 . GLU   B 114 ? 0.1364 0.1503 0.2472 -0.0058 0.0168  0.0094  114 GLU   B OE1 
5876 O OE2 . GLU   B 114 ? 0.1461 0.1510 0.2621 -0.0152 0.0121  0.0080  114 GLU   B OE2 
5883 N N   . ASN   B 115 ? 0.1376 0.1253 0.2119 -0.0074 -0.0041 0.0099  115 ASN   B N   
5884 C CA  . ASN   B 115 ? 0.1361 0.1328 0.1954 -0.0088 0.0024  0.0093  115 ASN   B CA  
5885 C C   . ASN   B 115 ? 0.1329 0.1279 0.2007 -0.0112 -0.0068 -0.0011 115 ASN   B C   
5886 O O   . ASN   B 115 ? 0.1495 0.1323 0.2018 -0.0123 0.0009  0.0019  115 ASN   B O   
5887 C CB  . ASN   B 115 ? 0.1472 0.1453 0.2008 -0.0130 0.0022  0.0100  115 ASN   B CB  
5888 C CG  . ASN   B 115 ? 0.1641 0.1494 0.1962 0.0011  0.0063  0.0085  115 ASN   B CG  
5889 O OD1 . ASN   B 115 ? 0.2089 0.1624 0.2151 -0.0053 0.0143  -0.0047 115 ASN   B OD1 
5890 N ND2 . ASN   B 115 ? 0.1545 0.1612 0.2024 -0.0034 0.0021  0.0135  115 ASN   B ND2 
5897 N N   . PHE   B 116 ? 0.1347 0.1316 0.1908 -0.0077 -0.0032 0.0047  116 PHE   B N   
5898 C CA  . PHE   B 116 ? 0.1400 0.1357 0.1907 -0.0106 -0.0048 0.0026  116 PHE   B CA  
5899 C C   . PHE   B 116 ? 0.1427 0.1155 0.1960 -0.0130 -0.0028 0.0057  116 PHE   B C   
5900 O O   . PHE   B 116 ? 0.1420 0.1335 0.2044 -0.0056 -0.0106 0.0095  116 PHE   B O   
5901 C CB  . PHE   B 116 ? 0.1367 0.1216 0.1930 -0.0074 -0.0080 0.0066  116 PHE   B CB  
5902 C CG  . PHE   B 116 ? 0.1287 0.1300 0.1936 -0.0089 -0.0056 0.0048  116 PHE   B CG  
5903 C CD1 . PHE   B 116 ? 0.1385 0.1357 0.2098 -0.0049 -0.0011 0.0015  116 PHE   B CD1 
5904 C CD2 . PHE   B 116 ? 0.1368 0.1346 0.1954 -0.0064 0.0007  -0.0036 116 PHE   B CD2 
5905 C CE1 . PHE   B 116 ? 0.1453 0.1394 0.2072 -0.0027 -0.0171 0.0103  116 PHE   B CE1 
5906 C CE2 . PHE   B 116 ? 0.1351 0.1371 0.1958 -0.0004 -0.0007 -0.0011 116 PHE   B CE2 
5907 C CZ  . PHE   B 116 ? 0.1307 0.1401 0.1966 -0.0026 -0.0126 0.0098  116 PHE   B CZ  
5917 N N   . ASN   B 117 ? 0.1401 0.1271 0.2205 -0.0058 -0.0143 0.0108  117 ASN   B N   
5918 C CA  . ASN   B 117 ? 0.1477 0.1288 0.2150 -0.0014 -0.0132 0.0079  117 ASN   B CA  
5919 C C   . ASN   B 117 ? 0.1476 0.1304 0.2251 -0.0026 -0.0117 0.0080  117 ASN   B C   
5920 O O   . ASN   B 117 ? 0.1556 0.1355 0.2576 -0.0059 -0.0370 0.0173  117 ASN   B O   
5921 C CB  . ASN   B 117 ? 0.1411 0.1306 0.2171 0.0005  -0.0071 -0.0006 117 ASN   B CB  
5922 C CG  . ASN   B 117 ? 0.1429 0.1349 0.2329 -0.0008 0.0069  -0.0036 117 ASN   B CG  
5923 O OD1 . ASN   B 117 ? 0.1618 0.1372 0.2373 -0.0135 -0.0015 -0.0007 117 ASN   B OD1 
5924 N ND2 . ASN   B 117 ? 0.1433 0.1401 0.2227 -0.0059 -0.0056 -0.0020 117 ASN   B ND2 
5931 N N   . GLN   B 118 ? 0.1437 0.1273 0.2121 -0.0084 -0.0192 0.0013  118 GLN   B N   
5932 C CA  . GLN   B 118 ? 0.1541 0.1316 0.2302 0.0017  -0.0192 -0.0015 118 GLN   B CA  
5933 C C   . GLN   B 118 ? 0.1553 0.1299 0.2466 -0.0032 -0.0141 -0.0035 118 GLN   B C   
5934 O O   . GLN   B 118 ? 0.1748 0.1294 0.2741 -0.0107 -0.0106 0.0084  118 GLN   B O   
5935 C CB  . GLN   B 118 ? 0.1581 0.1366 0.2373 -0.0010 -0.0223 0.0046  118 GLN   B CB  
5936 C CG  . GLN   B 118 ? 0.1684 0.1419 0.2353 0.0037  -0.0140 -0.0039 118 GLN   B CG  
5937 C CD  . GLN   B 118 ? 0.1740 0.1307 0.2402 0.0047  -0.0150 -0.0079 118 GLN   B CD  
5938 O OE1 . GLN   B 118 ? 0.1761 0.1322 0.2729 0.0032  -0.0031 0.0065  118 GLN   B OE1 
5939 N NE2 . GLN   B 118 ? 0.1847 0.1315 0.2450 0.0015  -0.0221 0.0045  118 GLN   B NE2 
5948 N N   . HIS   B 119 ? 0.1594 0.1322 0.2025 -0.0108 -0.0159 0.0094  119 HIS   B N   
5949 C CA  . HIS   B 119 ? 0.1676 0.1456 0.1936 -0.0079 -0.0197 0.0112  119 HIS   B CA  
5950 C C   . HIS   B 119 ? 0.1727 0.1457 0.1895 -0.0111 -0.0341 0.0171  119 HIS   B C   
5951 O O   . HIS   B 119 ? 0.1790 0.1498 0.2038 -0.0318 -0.0293 0.0145  119 HIS   B O   
5952 C CB  . HIS   B 119 ? 0.1703 0.1559 0.1961 -0.0025 -0.0262 0.0087  119 HIS   B CB  
5953 C CG  . HIS   B 119 ? 0.1725 0.1798 0.2112 0.0042  -0.0426 -0.0056 119 HIS   B CG  
5954 N ND1 . HIS   B 119 ? 0.1890 0.1947 0.2357 -0.0013 -0.0496 -0.0284 119 HIS   B ND1 
5955 C CD2 . HIS   B 119 ? 0.1915 0.2025 0.2062 0.0342  -0.0521 -0.0129 119 HIS   B CD2 
5956 C CE1 . HIS   B 119 ? 0.2137 0.2137 0.2370 0.0139  -0.0553 -0.0375 119 HIS   B CE1 
5957 N NE2 . HIS   B 119 ? 0.2110 0.2237 0.2176 0.0316  -0.0525 -0.0352 119 HIS   B NE2 
5965 N N   . GLU   B 120 ? 0.1952 0.1503 0.1867 -0.0180 -0.0421 0.0274  120 GLU   B N   
5966 C CA  . GLU   B 120 ? 0.2267 0.1715 0.2019 -0.0106 -0.0552 0.0363  120 GLU   B CA  
5967 C C   . GLU   B 120 ? 0.1997 0.1564 0.1879 -0.0210 -0.0408 0.0312  120 GLU   B C   
5968 O O   . GLU   B 120 ? 0.1915 0.1700 0.1934 -0.0193 -0.0452 0.0195  120 GLU   B O   
5969 C CB  . GLU   B 120 ? 0.2934 0.2204 0.2673 0.0136  -0.0798 0.0692  120 GLU   B CB  
5970 C CG  . GLU   B 120 ? 0.3530 0.2961 0.3764 0.0302  -0.1045 0.0914  120 GLU   B CG  
5971 C CD  . GLU   B 120 ? 0.4034 0.3637 0.4930 0.0360  -0.1063 0.1078  120 GLU   B CD  
5972 O OE1 . GLU   B 120 ? 0.4260 0.3926 0.5325 0.0322  -0.0998 0.1204  120 GLU   B OE1 
5973 O OE2 . GLU   B 120 ? 0.4249 0.3998 0.5502 0.0361  -0.1047 0.1037  120 GLU   B OE2 
5980 N N   . VAL   B 121 ? 0.1876 0.1500 0.1894 -0.0260 -0.0331 0.0242  121 VAL   B N   
5981 C CA  . VAL   B 121 ? 0.1795 0.1624 0.1688 -0.0219 -0.0333 0.0232  121 VAL   B CA  
5982 C C   . VAL   B 121 ? 0.1731 0.1546 0.1716 -0.0271 -0.0299 0.0208  121 VAL   B C   
5983 O O   . VAL   B 121 ? 0.1828 0.1505 0.1887 -0.0360 -0.0394 0.0187  121 VAL   B O   
5984 C CB  . VAL   B 121 ? 0.2068 0.2030 0.1770 -0.0129 -0.0373 0.0231  121 VAL   B CB  
5985 C CG1 . VAL   B 121 ? 0.2097 0.2102 0.2170 -0.0232 -0.0120 0.0158  121 VAL   B CG1 
5986 C CG2 . VAL   B 121 ? 0.2323 0.2311 0.1855 -0.0047 -0.0373 0.0104  121 VAL   B CG2 
5996 N N   . LEU   B 122 ? 0.1638 0.1471 0.1630 -0.0188 -0.0294 0.0108  122 LEU   B N   
5997 C CA  . LEU   B 122 ? 0.1508 0.1580 0.1608 -0.0210 -0.0208 0.0144  122 LEU   B CA  
5998 C C   . LEU   B 122 ? 0.1531 0.1451 0.1728 -0.0304 -0.0200 0.0164  122 LEU   B C   
5999 O O   . LEU   B 122 ? 0.1652 0.1488 0.1897 -0.0386 -0.0295 0.0081  122 LEU   B O   
6000 C CB  . LEU   B 122 ? 0.1755 0.1685 0.1964 -0.0085 -0.0228 0.0156  122 LEU   B CB  
6001 C CG  . LEU   B 122 ? 0.1605 0.1831 0.1987 -0.0188 -0.0079 0.0159  122 LEU   B CG  
6002 C CD1 . LEU   B 122 ? 0.1686 0.2057 0.1917 -0.0259 -0.0190 0.0136  122 LEU   B CD1 
6003 C CD2 . LEU   B 122 ? 0.1567 0.1840 0.1813 -0.0107 -0.0003 0.0057  122 LEU   B CD2 
6015 N N   . LEU   B 123 ? 0.1550 0.1375 0.1563 -0.0240 -0.0166 0.0118  123 LEU   B N   
6016 C CA  . LEU   B 123 ? 0.1575 0.1392 0.1560 -0.0264 -0.0223 0.0028  123 LEU   B CA  
6017 C C   . LEU   B 123 ? 0.1523 0.1377 0.1536 -0.0286 -0.0212 0.0057  123 LEU   B C   
6018 O O   . LEU   B 123 ? 0.1667 0.1387 0.1554 -0.0355 -0.0206 0.0002  123 LEU   B O   
6019 C CB  . LEU   B 123 ? 0.1656 0.1438 0.1711 -0.0287 -0.0176 0.0009  123 LEU   B CB  
6020 C CG  . LEU   B 123 ? 0.1643 0.1444 0.1792 -0.0216 -0.0113 0.0075  123 LEU   B CG  
6021 C CD1 . LEU   B 123 ? 0.1762 0.1496 0.1963 -0.0198 -0.0019 -0.0167 123 LEU   B CD1 
6022 C CD2 . LEU   B 123 ? 0.1764 0.1475 0.1912 -0.0202 -0.0002 0.0146  123 LEU   B CD2 
6034 N N   . ALA   B 124 ? 0.1507 0.1317 0.1513 -0.0203 -0.0140 -0.0008 124 ALA   B N   
6035 C CA  . ALA   B 124 ? 0.1444 0.1319 0.1688 -0.0150 -0.0123 -0.0051 124 ALA   B CA  
6036 C C   . ALA   B 124 ? 0.1386 0.1334 0.1530 -0.0192 -0.0172 0.0006  124 ALA   B C   
6037 O O   . ALA   B 124 ? 0.1543 0.1366 0.1656 -0.0198 -0.0142 0.0034  124 ALA   B O   
6038 C CB  . ALA   B 124 ? 0.1486 0.1364 0.1856 -0.0079 -0.0039 -0.0020 124 ALA   B CB  
6044 N N   . PRO   B 125 ? 0.1552 0.1346 0.1517 -0.0162 -0.0181 0.0121  125 PRO   B N   
6045 C CA  . PRO   B 125 ? 0.1605 0.1388 0.1718 -0.0139 -0.0182 0.0231  125 PRO   B CA  
6046 C C   . PRO   B 125 ? 0.1523 0.1332 0.2024 -0.0165 -0.0134 0.0114  125 PRO   B C   
6047 O O   . PRO   B 125 ? 0.1490 0.1317 0.2214 -0.0089 -0.0042 0.0146  125 PRO   B O   
6048 C CB  . PRO   B 125 ? 0.1598 0.1578 0.1864 -0.0209 -0.0220 0.0341  125 PRO   B CB  
6049 C CG  . PRO   B 125 ? 0.1693 0.1604 0.1709 -0.0272 -0.0284 0.0219  125 PRO   B CG  
6050 C CD  . PRO   B 125 ? 0.1641 0.1452 0.1601 -0.0279 -0.0212 -0.0021 125 PRO   B CD  
6058 N N   . LEU   B 126 ? 0.1601 0.1285 0.2154 -0.0188 0.0081  0.0183  126 LEU   B N   
6059 C CA  . LEU   B 126 ? 0.1644 0.1368 0.2178 -0.0139 0.0129  0.0150  126 LEU   B CA  
6060 C C   . LEU   B 126 ? 0.1636 0.1494 0.2184 0.0048  0.0128  0.0234  126 LEU   B C   
6061 O O   . LEU   B 126 ? 0.1859 0.1773 0.2475 0.0224  -0.0063 -0.0023 126 LEU   B O   
6062 C CB  . LEU   B 126 ? 0.1824 0.1379 0.2439 -0.0201 0.0132  0.0170  126 LEU   B CB  
6063 C CG  . LEU   B 126 ? 0.2031 0.1515 0.2590 -0.0266 0.0194  -0.0067 126 LEU   B CG  
6064 C CD1 . LEU   B 126 ? 0.2181 0.1562 0.3163 -0.0236 0.0233  -0.0045 126 LEU   B CD1 
6065 C CD2 . LEU   B 126 ? 0.2058 0.1649 0.2563 -0.0357 0.0142  -0.0046 126 LEU   B CD2 
6077 N N   . LEU   B 127 ? 0.1560 0.1355 0.2294 0.0031  0.0177  0.0125  127 LEU   B N   
6078 C CA  . LEU   B 127 ? 0.1592 0.1500 0.2356 -0.0066 0.0272  0.0228  127 LEU   B CA  
6079 C C   . LEU   B 127 ? 0.1556 0.1402 0.2396 -0.0058 0.0182  0.0279  127 LEU   B C   
6080 O O   . LEU   B 127 ? 0.1582 0.1459 0.2428 -0.0178 0.0147  0.0151  127 LEU   B O   
6081 C CB  . LEU   B 127 ? 0.1785 0.1422 0.2487 -0.0022 0.0249  0.0199  127 LEU   B CB  
6082 C CG  . LEU   B 127 ? 0.1890 0.1388 0.2535 -0.0024 0.0268  0.0216  127 LEU   B CG  
6083 C CD1 . LEU   B 127 ? 0.1961 0.1382 0.2569 0.0044  0.0221  0.0041  127 LEU   B CD1 
6084 C CD2 . LEU   B 127 ? 0.1948 0.1505 0.2647 -0.0176 0.0314  0.0298  127 LEU   B CD2 
6096 N N   . SER   B 128 ? 0.1625 0.1382 0.2398 0.0009  0.0023  0.0163  128 SER   B N   
6097 C CA  . SER   B 128 ? 0.1761 0.1511 0.2335 0.0046  -0.0065 0.0200  128 SER   B CA  
6098 C C   . SER   B 128 ? 0.1851 0.1533 0.2698 0.0084  -0.0318 0.0156  128 SER   B C   
6099 O O   . SER   B 128 ? 0.2021 0.1551 0.3081 0.0013  -0.0357 0.0299  128 SER   B O   
6100 C CB  . SER   B 128 ? 0.1813 0.1534 0.2291 0.0035  0.0001  0.0342  128 SER   B CB  
6101 O OG  . SER   B 128 ? 0.1862 0.1639 0.2313 0.0110  0.0085  0.0347  128 SER   B OG  
6107 N N   . ALA   B 129 ? 0.1954 0.1612 0.2926 0.0262  -0.0171 0.0039  129 ALA   B N   
6108 C CA  . ALA   B 129 ? 0.2165 0.1699 0.3149 0.0286  -0.0192 -0.0044 129 ALA   B CA  
6109 C C   . ALA   B 129 ? 0.1974 0.1594 0.2932 0.0209  0.0046  0.0107  129 ALA   B C   
6110 O O   . ALA   B 129 ? 0.1914 0.1618 0.2944 0.0155  -0.0028 0.0071  129 ALA   B O   
6111 C CB  . ALA   B 129 ? 0.2480 0.1844 0.3427 0.0281  -0.0029 -0.0041 129 ALA   B CB  
6117 N N   . GLY   B 130 ? 0.1995 0.1574 0.2894 0.0234  0.0094  -0.0005 130 GLY   B N   
6118 C CA  . GLY   B 130 ? 0.2021 0.1668 0.2978 0.0240  0.0300  -0.0026 130 GLY   B CA  
6119 C C   . GLY   B 130 ? 0.2063 0.1684 0.2890 0.0172  0.0245  0.0064  130 GLY   B C   
6120 O O   . GLY   B 130 ? 0.2176 0.1798 0.2937 0.0179  0.0125  0.0143  130 GLY   B O   
6124 N N   . ILE   B 131 ? 0.2019 0.1798 0.2964 0.0298  0.0158  0.0099  131 ILE   B N   
6125 C CA  . ILE   B 131 ? 0.2264 0.1988 0.2896 0.0232  0.0017  0.0222  131 ILE   B CA  
6126 C C   . ILE   B 131 ? 0.2335 0.1888 0.2578 0.0210  0.0046  0.0205  131 ILE   B C   
6127 O O   . ILE   B 131 ? 0.2599 0.2096 0.2742 0.0231  -0.0120 0.0209  131 ILE   B O   
6128 C CB  . ILE   B 131 ? 0.2290 0.2292 0.3240 0.0163  -0.0073 0.0301  131 ILE   B CB  
6129 C CG1 . ILE   B 131 ? 0.2348 0.2462 0.3322 -0.0102 -0.0064 0.0371  131 ILE   B CG1 
6130 C CG2 . ILE   B 131 ? 0.2312 0.2524 0.3492 0.0228  -0.0041 0.0224  131 ILE   B CG2 
6131 C CD1 . ILE   B 131 ? 0.2472 0.2641 0.3531 -0.0270 -0.0161 0.0359  131 ILE   B CD1 
6143 N N   . PHE   B 132 ? 0.2202 0.1748 0.2443 0.0135  0.0236  0.0160  132 PHE   B N   
6144 C CA  . PHE   B 132 ? 0.2340 0.1780 0.2441 0.0063  0.0409  0.0137  132 PHE   B CA  
6145 C C   . PHE   B 132 ? 0.2533 0.1940 0.2707 0.0101  0.0553  0.0123  132 PHE   B C   
6146 O O   . PHE   B 132 ? 0.2685 0.2214 0.2953 0.0070  0.0729  0.0132  132 PHE   B O   
6147 C CB  . PHE   B 132 ? 0.2162 0.1746 0.2263 0.0081  0.0420  0.0191  132 PHE   B CB  
6148 C CG  . PHE   B 132 ? 0.2096 0.1791 0.2238 0.0192  0.0303  0.0192  132 PHE   B CG  
6149 C CD1 . PHE   B 132 ? 0.2278 0.1793 0.2600 0.0143  0.0239  0.0186  132 PHE   B CD1 
6150 C CD2 . PHE   B 132 ? 0.2089 0.1871 0.2105 0.0254  0.0192  0.0339  132 PHE   B CD2 
6151 C CE1 . PHE   B 132 ? 0.2308 0.1838 0.2589 0.0103  0.0150  0.0242  132 PHE   B CE1 
6152 C CE2 . PHE   B 132 ? 0.2179 0.1931 0.2107 0.0214  0.0109  0.0316  132 PHE   B CE2 
6153 C CZ  . PHE   B 132 ? 0.2270 0.1914 0.2392 0.0144  0.0029  0.0414  132 PHE   B CZ  
6163 N N   . GLY   B 133 ? 0.2483 0.1798 0.2657 0.0014  0.0426  0.0362  133 GLY   B N   
6164 C CA  . GLY   B 133 ? 0.2601 0.1951 0.2831 -0.0205 0.0382  0.0421  133 GLY   B CA  
6165 C C   . GLY   B 133 ? 0.2658 0.2046 0.2903 -0.0388 0.0464  0.0485  133 GLY   B C   
6166 O O   . GLY   B 133 ? 0.2827 0.2242 0.3255 -0.0524 0.0489  0.0581  133 GLY   B O   
6170 N N   . ALA   B 134 ? 0.2471 0.2020 0.2725 -0.0348 0.0455  0.0309  134 ALA   B N   
6171 C CA  . ALA   B 134 ? 0.2437 0.1973 0.2884 -0.0291 0.0501  0.0142  134 ALA   B CA  
6172 C C   . ALA   B 134 ? 0.2507 0.1819 0.2858 -0.0220 0.0474  0.0314  134 ALA   B C   
6173 O O   . ALA   B 134 ? 0.2538 0.2053 0.2963 -0.0067 0.0390  0.0251  134 ALA   B O   
6174 C CB  . ALA   B 134 ? 0.2383 0.2023 0.2988 -0.0240 0.0410  0.0023  134 ALA   B CB  
6180 N N   . ASP   B 135 ? 0.2705 0.1770 0.2969 -0.0221 0.0221  0.0333  135 ASP   B N   
6181 C CA  . ASP   B 135 ? 0.2916 0.1714 0.3118 -0.0168 0.0045  0.0380  135 ASP   B CA  
6182 C C   . ASP   B 135 ? 0.2701 0.1572 0.2890 -0.0071 0.0026  0.0418  135 ASP   B C   
6183 O O   . ASP   B 135 ? 0.2576 0.1518 0.3120 -0.0107 -0.0017 0.0341  135 ASP   B O   
6184 C CB  . ASP   B 135 ? 0.3252 0.1795 0.3323 -0.0329 0.0028  0.0366  135 ASP   B CB  
6185 C CG  . ASP   B 135 ? 0.3491 0.1849 0.3747 -0.0545 0.0017  0.0340  135 ASP   B CG  
6186 O OD1 . ASP   B 135 ? 0.3591 0.1746 0.3820 -0.0380 -0.0117 0.0342  135 ASP   B OD1 
6187 O OD2 . ASP   B 135 ? 0.3668 0.2262 0.4371 -0.0664 0.0066  0.0221  135 ASP   B OD2 
6192 N N   . PRO   B 136 ? 0.2548 0.1619 0.2943 0.0145  -0.0160 0.0283  136 PRO   B N   
6193 C CA  . PRO   B 136 ? 0.2270 0.1591 0.3039 0.0175  -0.0167 0.0175  136 PRO   B CA  
6194 C C   . PRO   B 136 ? 0.1978 0.1465 0.3125 0.0104  -0.0115 0.0084  136 PRO   B C   
6195 O O   . PRO   B 136 ? 0.1756 0.1424 0.3134 0.0055  -0.0117 0.0171  136 PRO   B O   
6196 C CB  . PRO   B 136 ? 0.2318 0.1800 0.2999 0.0343  -0.0203 0.0043  136 PRO   B CB  
6197 C CG  . PRO   B 136 ? 0.2531 0.1922 0.3165 0.0335  -0.0139 0.0011  136 PRO   B CG  
6198 C CD  . PRO   B 136 ? 0.2612 0.1811 0.3121 0.0397  -0.0106 0.0081  136 PRO   B CD  
6206 N N   . ILE   B 137 ? 0.2093 0.1390 0.3295 0.0083  -0.0099 0.0043  137 ILE   B N   
6207 C CA  . ILE   B 137 ? 0.2174 0.1359 0.3389 -0.0050 -0.0045 -0.0005 137 ILE   B CA  
6208 C C   . ILE   B 137 ? 0.2117 0.1387 0.3241 -0.0094 0.0038  0.0114  137 ILE   B C   
6209 O O   . ILE   B 137 ? 0.1958 0.1471 0.3073 -0.0147 0.0072  0.0126  137 ILE   B O   
6210 C CB  . ILE   B 137 ? 0.2441 0.1416 0.3853 -0.0031 -0.0106 0.0053  137 ILE   B CB  
6211 C CG1 . ILE   B 137 ? 0.2619 0.1647 0.4328 0.0083  -0.0096 -0.0038 137 ILE   B CG1 
6212 C CG2 . ILE   B 137 ? 0.2522 0.1481 0.3923 -0.0322 -0.0159 0.0176  137 ILE   B CG2 
6213 C CD1 . ILE   B 137 ? 0.2778 0.2035 0.4682 0.0190  -0.0167 -0.0025 137 ILE   B CD1 
6225 N N   . HIS   B 138 ? 0.2185 0.1402 0.3187 -0.0037 0.0156  0.0194  138 HIS   B N   
6226 C CA  . HIS   B 138 ? 0.2304 0.1439 0.3133 -0.0043 0.0312  0.0211  138 HIS   B CA  
6227 C C   . HIS   B 138 ? 0.2106 0.1410 0.3060 -0.0038 0.0313  0.0303  138 HIS   B C   
6228 O O   . HIS   B 138 ? 0.2011 0.1520 0.3350 -0.0035 0.0320  0.0360  138 HIS   B O   
6229 C CB  . HIS   B 138 ? 0.2631 0.1589 0.3195 -0.0193 0.0603  0.0173  138 HIS   B CB  
6230 C CG  . HIS   B 138 ? 0.2880 0.1800 0.3216 -0.0229 0.0889  0.0362  138 HIS   B CG  
6231 N ND1 . HIS   B 138 ? 0.3008 0.2096 0.3577 -0.0157 0.0950  0.0286  138 HIS   B ND1 
6232 C CD2 . HIS   B 138 ? 0.3047 0.1903 0.3190 -0.0182 0.0913  0.0252  138 HIS   B CD2 
6233 C CE1 . HIS   B 138 ? 0.3061 0.2145 0.3527 -0.0156 0.0948  0.0275  138 HIS   B CE1 
6234 N NE2 . HIS   B 138 ? 0.3123 0.1948 0.3347 -0.0098 0.0933  0.0257  138 HIS   B NE2 
6242 N N   . SER   B 139 ? 0.2017 0.1317 0.2880 -0.0027 0.0278  0.0192  139 SER   B N   
6243 C CA  . SER   B 139 ? 0.1954 0.1333 0.2726 -0.0058 0.0228  0.0030  139 SER   B CA  
6244 C C   . SER   B 139 ? 0.1691 0.1293 0.2688 -0.0036 0.0179  0.0055  139 SER   B C   
6245 O O   . SER   B 139 ? 0.1659 0.1369 0.2686 0.0003  0.0030  0.0089  139 SER   B O   
6246 C CB  . SER   B 139 ? 0.2001 0.1347 0.2830 -0.0027 0.0065  0.0009  139 SER   B CB  
6247 O OG  . SER   B 139 ? 0.1977 0.1392 0.2907 -0.0036 -0.0125 0.0130  139 SER   B OG  
6253 N N   . LEU   B 140 ? 0.1695 0.1227 0.2650 -0.0030 0.0212  -0.0014 140 LEU   B N   
6254 C CA  . LEU   B 140 ? 0.1635 0.1250 0.2657 -0.0038 0.0131  0.0033  140 LEU   B CA  
6255 C C   . LEU   B 140 ? 0.1579 0.1295 0.2861 -0.0060 0.0007  -0.0012 140 LEU   B C   
6256 O O   . LEU   B 140 ? 0.1550 0.1365 0.2804 -0.0038 -0.0024 0.0081  140 LEU   B O   
6257 C CB  . LEU   B 140 ? 0.1679 0.1272 0.2758 -0.0062 0.0190  0.0093  140 LEU   B CB  
6258 C CG  . LEU   B 140 ? 0.1701 0.1296 0.2804 -0.0116 0.0048  0.0093  140 LEU   B CG  
6259 C CD1 . LEU   B 140 ? 0.1779 0.1401 0.3009 -0.0157 0.0104  0.0044  140 LEU   B CD1 
6260 C CD2 . LEU   B 140 ? 0.1886 0.1415 0.2885 -0.0082 -0.0015 -0.0086 140 LEU   B CD2 
6272 N N   . ARG   B 141 ? 0.1496 0.1344 0.2966 -0.0108 0.0077  -0.0011 141 ARG   B N   
6273 C CA  . ARG   B 141 ? 0.1518 0.1354 0.3366 -0.0193 0.0205  -0.0002 141 ARG   B CA  
6274 C C   . ARG   B 141 ? 0.1479 0.1315 0.3255 -0.0179 0.0050  -0.0000 141 ARG   B C   
6275 O O   . ARG   B 141 ? 0.1612 0.1406 0.3172 -0.0137 -0.0032 -0.0082 141 ARG   B O   
6276 C CB  . ARG   B 141 ? 0.1748 0.1499 0.3605 -0.0260 0.0282  -0.0068 141 ARG   B CB  
6277 C CG  . ARG   B 141 ? 0.2070 0.1735 0.3601 -0.0280 0.0334  0.0012  141 ARG   B CG  
6278 C CD  . ARG   B 141 ? 0.2490 0.1955 0.3605 -0.0211 0.0199  -0.0092 141 ARG   B CD  
6279 N NE  . ARG   B 141 ? 0.2688 0.1946 0.3531 -0.0348 0.0217  -0.0149 141 ARG   B NE  
6280 C CZ  . ARG   B 141 ? 0.2887 0.1824 0.3370 -0.0346 0.0235  -0.0335 141 ARG   B CZ  
6281 N NH1 . ARG   B 141 ? 0.3034 0.1700 0.3326 -0.0366 0.0207  -0.0300 141 ARG   B NH1 
6282 N NH2 . ARG   B 141 ? 0.2988 0.2021 0.3423 -0.0201 0.0140  -0.0203 141 ARG   B NH2 
6296 N N   . VAL   B 142 ? 0.1546 0.1319 0.3112 -0.0125 0.0113  -0.0005 142 VAL   B N   
6297 C CA  . VAL   B 142 ? 0.1464 0.1326 0.2971 -0.0062 0.0176  -0.0036 142 VAL   B CA  
6298 C C   . VAL   B 142 ? 0.1456 0.1327 0.2997 -0.0088 0.0075  -0.0043 142 VAL   B C   
6299 O O   . VAL   B 142 ? 0.1563 0.1312 0.3141 -0.0026 0.0153  0.0058  142 VAL   B O   
6300 C CB  . VAL   B 142 ? 0.1601 0.1456 0.2938 -0.0040 0.0230  0.0072  142 VAL   B CB  
6301 C CG1 . VAL   B 142 ? 0.1601 0.1408 0.2943 0.0050  0.0217  0.0042  142 VAL   B CG1 
6302 C CG2 . VAL   B 142 ? 0.1853 0.1509 0.3026 -0.0015 0.0179  0.0122  142 VAL   B CG2 
6312 N N   . CYS   B 143 ? 0.1418 0.1374 0.2720 -0.0065 0.0042  0.0037  143 CYS   B N   
6313 C CA  . CYS   B 143 ? 0.1418 0.1371 0.2684 -0.0091 0.0060  0.0090  143 CYS   B CA  
6314 C C   . CYS   B 143 ? 0.1398 0.1390 0.2636 -0.0088 0.0030  0.0030  143 CYS   B C   
6315 O O   . CYS   B 143 ? 0.1429 0.1420 0.2764 -0.0054 -0.0086 0.0009  143 CYS   B O   
6316 C CB  . CYS   B 143 ? 0.1477 0.1383 0.2690 -0.0046 -0.0046 0.0019  143 CYS   B CB  
6317 S SG  . CYS   B 143 ? 0.1550 0.1577 0.2528 -0.0065 0.0022  0.0064  143 CYS   B SG  
6323 N N   . VAL   B 144 ? 0.1451 0.1383 0.2946 -0.0104 -0.0027 -0.0121 144 VAL   B N   
6324 C CA  . VAL   B 144 ? 0.1537 0.1424 0.3140 -0.0197 -0.0169 -0.0114 144 VAL   B CA  
6325 C C   . VAL   B 144 ? 0.1512 0.1455 0.3234 -0.0115 -0.0164 0.0050  144 VAL   B C   
6326 O O   . VAL   B 144 ? 0.1593 0.1656 0.3438 -0.0055 -0.0153 0.0259  144 VAL   B O   
6327 C CB  . VAL   B 144 ? 0.1760 0.1609 0.3708 -0.0170 -0.0248 -0.0308 144 VAL   B CB  
6328 C CG1 . VAL   B 144 ? 0.2028 0.2110 0.4056 -0.0122 -0.0317 -0.0350 144 VAL   B CG1 
6329 C CG2 . VAL   B 144 ? 0.1946 0.1591 0.3515 -0.0030 -0.0441 -0.0394 144 VAL   B CG2 
6339 N N   . ASP   B 145 ? 0.1512 0.1304 0.3305 -0.0133 -0.0133 -0.0049 145 ASP   B N   
6340 C CA  . ASP   B 145 ? 0.1506 0.1396 0.3543 -0.0119 0.0014  0.0018  145 ASP   B CA  
6341 C C   . ASP   B 145 ? 0.1511 0.1456 0.3367 -0.0143 0.0009  0.0007  145 ASP   B C   
6342 O O   . ASP   B 145 ? 0.1492 0.1641 0.3888 -0.0137 0.0101  -0.0173 145 ASP   B O   
6343 C CB  . ASP   B 145 ? 0.1651 0.1541 0.4055 -0.0148 0.0136  0.0171  145 ASP   B CB  
6344 C CG  . ASP   B 145 ? 0.1841 0.1624 0.4619 -0.0247 0.0261  0.0034  145 ASP   B CG  
6345 O OD1 . ASP   B 145 ? 0.1856 0.1600 0.4624 -0.0313 -0.0142 -0.0124 145 ASP   B OD1 
6346 O OD2 . ASP   B 145 ? 0.2075 0.1694 0.5090 -0.0326 0.0509  0.0032  145 ASP   B OD2 
6351 N N   . THR   B 146 ? 0.1481 0.1348 0.2942 -0.0141 -0.0016 0.0068  146 THR   B N   
6352 C CA  . THR   B 146 ? 0.1475 0.1384 0.2764 -0.0109 0.0067  0.0022  146 THR   B CA  
6353 C C   . THR   B 146 ? 0.1435 0.1440 0.2687 -0.0064 -0.0004 0.0040  146 THR   B C   
6354 O O   . THR   B 146 ? 0.1465 0.1373 0.2752 -0.0040 -0.0039 0.0053  146 THR   B O   
6355 C CB  . THR   B 146 ? 0.1477 0.1417 0.2843 -0.0058 0.0187  0.0046  146 THR   B CB  
6356 O OG1 . THR   B 146 ? 0.1524 0.1401 0.2983 -0.0069 0.0183  0.0167  146 THR   B OG1 
6357 C CG2 . THR   B 146 ? 0.1601 0.1377 0.2834 -0.0057 0.0097  -0.0119 146 THR   B CG2 
6365 N N   . VAL   B 147 ? 0.1496 0.1392 0.2452 -0.0030 0.0074  0.0041  147 VAL   B N   
6366 C CA  . VAL   B 147 ? 0.1500 0.1334 0.2444 -0.0166 -0.0075 0.0060  147 VAL   B CA  
6367 C C   . VAL   B 147 ? 0.1503 0.1358 0.2624 -0.0248 -0.0187 -0.0037 147 VAL   B C   
6368 O O   . VAL   B 147 ? 0.1622 0.1482 0.2718 -0.0197 -0.0371 -0.0019 147 VAL   B O   
6369 C CB  . VAL   B 147 ? 0.1487 0.1447 0.2309 -0.0091 -0.0145 0.0010  147 VAL   B CB  
6370 C CG1 . VAL   B 147 ? 0.1485 0.1617 0.2156 -0.0138 -0.0133 0.0067  147 VAL   B CG1 
6371 C CG2 . VAL   B 147 ? 0.1555 0.1422 0.2298 -0.0084 -0.0044 0.0039  147 VAL   B CG2 
6381 N N   . ARG   B 148 ? 0.1480 0.1418 0.2486 -0.0120 -0.0289 -0.0067 148 ARG   B N   
6382 C CA  . ARG   B 148 ? 0.1530 0.1487 0.2401 -0.0087 -0.0341 -0.0117 148 ARG   B CA  
6383 C C   . ARG   B 148 ? 0.1627 0.1552 0.2270 -0.0163 -0.0340 0.0005  148 ARG   B C   
6384 O O   . ARG   B 148 ? 0.1776 0.1817 0.2414 -0.0297 -0.0415 0.0101  148 ARG   B O   
6385 C CB  . ARG   B 148 ? 0.1610 0.1563 0.2471 -0.0048 -0.0366 -0.0155 148 ARG   B CB  
6386 C CG  . ARG   B 148 ? 0.1604 0.1713 0.2593 -0.0100 -0.0338 -0.0359 148 ARG   B CG  
6387 C CD  . ARG   B 148 ? 0.1659 0.1919 0.2761 0.0058  -0.0349 -0.0396 148 ARG   B CD  
6388 N NE  . ARG   B 148 ? 0.1761 0.1849 0.2696 0.0193  -0.0397 -0.0347 148 ARG   B NE  
6389 C CZ  . ARG   B 148 ? 0.1639 0.1769 0.2553 0.0157  -0.0362 -0.0299 148 ARG   B CZ  
6390 N NH1 . ARG   B 148 ? 0.1566 0.1856 0.2504 0.0059  -0.0181 -0.0286 148 ARG   B NH1 
6391 N NH2 . ARG   B 148 ? 0.1819 0.1645 0.2558 0.0127  -0.0260 -0.0194 148 ARG   B NH2 
6405 N N   . THR   B 149 ? 0.1663 0.1439 0.2345 -0.0176 -0.0377 0.0060  149 THR   B N   
6406 C CA  . THR   B 149 ? 0.1726 0.1470 0.2182 -0.0192 -0.0370 0.0113  149 THR   B CA  
6407 C C   . THR   B 149 ? 0.1768 0.1493 0.2120 -0.0168 -0.0410 0.0084  149 THR   B C   
6408 O O   . THR   B 149 ? 0.1821 0.1454 0.2226 -0.0203 -0.0249 0.0103  149 THR   B O   
6409 C CB  . THR   B 149 ? 0.1755 0.1454 0.2271 -0.0220 -0.0416 0.0033  149 THR   B CB  
6410 O OG1 . THR   B 149 ? 0.1736 0.1565 0.2123 -0.0257 -0.0408 0.0034  149 THR   B OG1 
6411 C CG2 . THR   B 149 ? 0.1831 0.1566 0.2393 -0.0119 -0.0300 0.0020  149 THR   B CG2 
6419 N N   . ASN   B 150 ? 0.1766 0.1489 0.2053 -0.0207 -0.0394 0.0028  150 ASN   B N   
6420 C CA  . ASN   B 150 ? 0.1846 0.1656 0.1942 -0.0243 -0.0395 0.0038  150 ASN   B CA  
6421 C C   . ASN   B 150 ? 0.1710 0.1613 0.1959 -0.0186 -0.0285 0.0003  150 ASN   B C   
6422 O O   . ASN   B 150 ? 0.1774 0.1567 0.2174 -0.0296 -0.0493 0.0056  150 ASN   B O   
6423 C CB  . ASN   B 150 ? 0.2141 0.2068 0.2091 -0.0272 -0.0524 0.0184  150 ASN   B CB  
6424 C CG  . ASN   B 150 ? 0.2412 0.2461 0.2433 -0.0242 -0.0513 0.0276  150 ASN   B CG  
6425 O OD1 . ASN   B 150 ? 0.2486 0.2665 0.2565 -0.0337 -0.0619 0.0244  150 ASN   B OD1 
6426 N ND2 . ASN   B 150 ? 0.2556 0.2626 0.2877 -0.0149 -0.0551 0.0650  150 ASN   B ND2 
6433 N N   . VAL   B 151 ? 0.1643 0.1575 0.1870 -0.0207 -0.0361 -0.0011 151 VAL   B N   
6434 C CA  . VAL   B 151 ? 0.1630 0.1562 0.1971 -0.0294 -0.0311 0.0020  151 VAL   B CA  
6435 C C   . VAL   B 151 ? 0.1689 0.1492 0.1895 -0.0319 -0.0343 0.0043  151 VAL   B C   
6436 O O   . VAL   B 151 ? 0.1799 0.1616 0.2173 -0.0325 -0.0230 -0.0126 151 VAL   B O   
6437 C CB  . VAL   B 151 ? 0.1861 0.1661 0.2075 -0.0100 -0.0227 0.0028  151 VAL   B CB  
6438 C CG1 . VAL   B 151 ? 0.1938 0.1691 0.2383 -0.0179 -0.0149 -0.0011 151 VAL   B CG1 
6439 C CG2 . VAL   B 151 ? 0.1951 0.1871 0.1800 -0.0007 -0.0269 0.0126  151 VAL   B CG2 
6449 N N   . TYR   B 152 ? 0.1626 0.1438 0.1884 -0.0255 -0.0262 0.0011  152 TYR   B N   
6450 C CA  . TYR   B 152 ? 0.1683 0.1627 0.1751 -0.0315 -0.0189 -0.0068 152 TYR   B CA  
6451 C C   . TYR   B 152 ? 0.1618 0.1463 0.1785 -0.0243 -0.0164 -0.0051 152 TYR   B C   
6452 O O   . TYR   B 152 ? 0.1682 0.1476 0.1871 -0.0296 -0.0155 0.0010  152 TYR   B O   
6453 C CB  . TYR   B 152 ? 0.1882 0.1808 0.1761 -0.0369 -0.0180 0.0032  152 TYR   B CB  
6454 C CG  . TYR   B 152 ? 0.2052 0.1913 0.1683 -0.0510 -0.0176 -0.0031 152 TYR   B CG  
6455 C CD1 . TYR   B 152 ? 0.2185 0.2006 0.1610 -0.0445 -0.0251 0.0115  152 TYR   B CD1 
6456 C CD2 . TYR   B 152 ? 0.2288 0.2123 0.1733 -0.0497 -0.0124 -0.0004 152 TYR   B CD2 
6457 C CE1 . TYR   B 152 ? 0.2363 0.2230 0.1860 -0.0434 -0.0336 0.0198  152 TYR   B CE1 
6458 C CE2 . TYR   B 152 ? 0.2394 0.2351 0.1767 -0.0483 -0.0241 -0.0049 152 TYR   B CE2 
6459 C CZ  . TYR   B 152 ? 0.2438 0.2468 0.1775 -0.0426 -0.0482 0.0196  152 TYR   B CZ  
6460 O OH  . TYR   B 152 ? 0.2664 0.2866 0.2147 -0.0287 -0.0494 0.0243  152 TYR   B OH  
6470 N N   . LEU   B 153 ? 0.1653 0.1432 0.1871 -0.0319 -0.0154 -0.0047 153 LEU   B N   
6471 C CA  . LEU   B 153 ? 0.1689 0.1391 0.1767 -0.0240 -0.0071 -0.0126 153 LEU   B CA  
6472 C C   . LEU   B 153 ? 0.1713 0.1370 0.1911 -0.0289 -0.0087 -0.0167 153 LEU   B C   
6473 O O   . LEU   B 153 ? 0.1773 0.1661 0.2013 -0.0227 -0.0110 -0.0337 153 LEU   B O   
6474 C CB  . LEU   B 153 ? 0.1701 0.1391 0.1865 -0.0270 -0.0095 -0.0101 153 LEU   B CB  
6475 C CG  . LEU   B 153 ? 0.1635 0.1464 0.2115 -0.0277 -0.0087 -0.0066 153 LEU   B CG  
6476 C CD1 . LEU   B 153 ? 0.1748 0.1556 0.2354 -0.0334 0.0027  0.0116  153 LEU   B CD1 
6477 C CD2 . LEU   B 153 ? 0.1655 0.1593 0.2062 -0.0303 0.0065  0.0024  153 LEU   B CD2 
6489 N N   . ALA   B 154 ? 0.1624 0.1396 0.1929 -0.0070 -0.0123 -0.0187 154 ALA   B N   
6490 C CA  . ALA   B 154 ? 0.1767 0.1466 0.2208 -0.0022 -0.0169 -0.0242 154 ALA   B CA  
6491 C C   . ALA   B 154 ? 0.1912 0.1513 0.2274 0.0029  -0.0256 -0.0317 154 ALA   B C   
6492 O O   . ALA   B 154 ? 0.2269 0.1553 0.2565 0.0085  -0.0135 -0.0138 154 ALA   B O   
6493 C CB  . ALA   B 154 ? 0.1728 0.1675 0.2384 -0.0027 -0.0104 -0.0297 154 ALA   B CB  
6499 N N   . VAL   B 155 ? 0.1546 0.1430 0.2493 -0.0075 0.0006  -0.0213 155 VAL   B N   
6500 C CA  . VAL   B 155 ? 0.1513 0.1413 0.2697 -0.0044 -0.0127 -0.0142 155 VAL   B CA  
6501 C C   . VAL   B 155 ? 0.1512 0.1490 0.2572 -0.0022 -0.0118 -0.0293 155 VAL   B C   
6502 O O   . VAL   B 155 ? 0.1783 0.1640 0.2898 0.0070  -0.0141 -0.0451 155 VAL   B O   
6503 C CB  . VAL   B 155 ? 0.1586 0.1582 0.3013 -0.0006 -0.0191 0.0001  155 VAL   B CB  
6504 C CG1 . VAL   B 155 ? 0.1676 0.1548 0.3016 -0.0098 -0.0257 0.0038  155 VAL   B CG1 
6505 C CG2 . VAL   B 155 ? 0.1558 0.1728 0.3235 -0.0033 -0.0243 0.0303  155 VAL   B CG2 
6515 N N   . PHE   B 156 ? 0.1412 0.1559 0.2736 0.0051  -0.0091 -0.0276 156 PHE   B N   
6516 C CA  . PHE   B 156 ? 0.1509 0.1599 0.3078 0.0068  -0.0081 -0.0293 156 PHE   B CA  
6517 C C   . PHE   B 156 ? 0.1532 0.1761 0.3486 0.0146  -0.0131 -0.0429 156 PHE   B C   
6518 O O   . PHE   B 156 ? 0.1833 0.1924 0.3723 0.0290  -0.0044 -0.0545 156 PHE   B O   
6519 C CB  . PHE   B 156 ? 0.1615 0.1555 0.3018 0.0025  -0.0137 -0.0236 156 PHE   B CB  
6520 C CG  . PHE   B 156 ? 0.1578 0.1703 0.3014 0.0024  -0.0113 -0.0091 156 PHE   B CG  
6521 C CD1 . PHE   B 156 ? 0.1675 0.1907 0.3298 0.0112  0.0091  0.0276  156 PHE   B CD1 
6522 C CD2 . PHE   B 156 ? 0.1672 0.1848 0.3012 0.0129  -0.0165 -0.0026 156 PHE   B CD2 
6523 C CE1 . PHE   B 156 ? 0.1697 0.2046 0.3412 0.0110  0.0118  0.0265  156 PHE   B CE1 
6524 C CE2 . PHE   B 156 ? 0.1760 0.2014 0.3171 0.0196  -0.0119 0.0044  156 PHE   B CE2 
6525 C CZ  . PHE   B 156 ? 0.1675 0.2038 0.3367 0.0203  -0.0107 0.0095  156 PHE   B CZ  
6535 N N   . ASP   B 157 ? 0.1542 0.1634 0.3717 0.0194  -0.0296 -0.0345 157 ASP   B N   
6536 C CA  . ASP   B 157 ? 0.1727 0.1726 0.3881 0.0168  -0.0293 -0.0452 157 ASP   B CA  
6537 C C   . ASP   B 157 ? 0.1701 0.1746 0.3827 0.0145  -0.0240 -0.0667 157 ASP   B C   
6538 O O   . ASP   B 157 ? 0.1524 0.1669 0.3889 0.0079  -0.0249 -0.0504 157 ASP   B O   
6539 C CB  . ASP   B 157 ? 0.2063 0.1963 0.3978 0.0097  -0.0589 -0.0292 157 ASP   B CB  
6540 C CG  . ASP   B 157 ? 0.2510 0.2076 0.4239 0.0061  -0.0597 -0.0253 157 ASP   B CG  
6541 O OD1 . ASP   B 157 ? 0.2589 0.2031 0.4375 0.0131  -0.0475 -0.0090 157 ASP   B OD1 
6542 O OD2 . ASP   B 157 ? 0.2906 0.2336 0.4508 0.0097  -0.0396 -0.0228 157 ASP   B OD2 
6547 N N   A LYS   B 158 ? 0.1688 0.2007 0.3924 0.0101  -0.0102 -0.0941 158 LYS   B N   
6548 N N   B LYS   B 158 ? 0.1950 0.2039 0.3548 0.0142  -0.0178 -0.0740 158 LYS   B N   
6549 C CA  A LYS   B 158 ? 0.1827 0.2221 0.4059 0.0054  0.0024  -0.1182 158 LYS   B CA  
6550 C CA  B LYS   B 158 ? 0.2255 0.2307 0.3429 0.0144  -0.0129 -0.0788 158 LYS   B CA  
6551 C C   A LYS   B 158 ? 0.1809 0.2014 0.4354 0.0035  -0.0109 -0.1039 158 LYS   B C   
6552 C C   B LYS   B 158 ? 0.2300 0.2285 0.3372 0.0160  -0.0193 -0.0718 158 LYS   B C   
6553 O O   A LYS   B 158 ? 0.1850 0.1937 0.4497 -0.0033 -0.0159 -0.1103 158 LYS   B O   
6554 O O   B LYS   B 158 ? 0.2338 0.2302 0.3296 0.0157  -0.0181 -0.0717 158 LYS   B O   
6555 C CB  A LYS   B 158 ? 0.2118 0.2736 0.4049 0.0083  0.0102  -0.1364 158 LYS   B CB  
6556 C CB  B LYS   B 158 ? 0.2517 0.2590 0.3497 0.0146  -0.0072 -0.0860 158 LYS   B CB  
6557 C CG  A LYS   B 158 ? 0.2509 0.3232 0.4040 0.0112  0.0142  -0.1436 158 LYS   B CG  
6558 C CG  B LYS   B 158 ? 0.2764 0.2836 0.3611 0.0148  -0.0019 -0.0916 158 LYS   B CG  
6559 C CD  A LYS   B 158 ? 0.2790 0.3694 0.4122 0.0111  0.0149  -0.1375 158 LYS   B CD  
6560 C CD  B LYS   B 158 ? 0.2962 0.3069 0.3776 0.0136  0.0011  -0.0887 158 LYS   B CD  
6561 C CE  A LYS   B 158 ? 0.3003 0.4000 0.4242 0.0101  0.0081  -0.1290 158 LYS   B CE  
6562 C CE  B LYS   B 158 ? 0.3107 0.3237 0.3932 0.0131  0.0009  -0.0854 158 LYS   B CE  
6563 N NZ  A LYS   B 158 ? 0.3024 0.4139 0.4256 0.0062  0.0031  -0.1221 158 LYS   B NZ  
6564 N NZ  B LYS   B 158 ? 0.3156 0.3318 0.3999 0.0112  0.0003  -0.0833 158 LYS   B NZ  
6591 N N   A ASN   B 159 ? 0.1791 0.1850 0.4577 0.0102  -0.0284 -0.0836 159 ASN   B N   
6592 N N   B ASN   B 159 ? 0.2282 0.2224 0.3518 0.0165  -0.0306 -0.0621 159 ASN   B N   
6593 C CA  A ASN   B 159 ? 0.2009 0.1724 0.4673 0.0244  -0.0524 -0.0706 159 ASN   B CA  
6594 C CA  B ASN   B 159 ? 0.2276 0.2126 0.3687 0.0197  -0.0427 -0.0578 159 ASN   B CA  
6595 C C   A ASN   B 159 ? 0.1901 0.1563 0.4541 0.0185  -0.0693 -0.0597 159 ASN   B C   
6596 C C   B ASN   B 159 ? 0.2061 0.1865 0.3938 0.0177  -0.0509 -0.0572 159 ASN   B C   
6597 O O   A ASN   B 159 ? 0.1932 0.1428 0.4812 -0.0047 -0.0769 -0.0383 159 ASN   B O   
6598 O O   B ASN   B 159 ? 0.2092 0.1852 0.3969 0.0142  -0.0517 -0.0507 159 ASN   B O   
6599 C CB  A ASN   B 159 ? 0.2265 0.1873 0.4913 0.0365  -0.0624 -0.0665 159 ASN   B CB  
6600 C CB  B ASN   B 159 ? 0.2442 0.2276 0.3692 0.0245  -0.0472 -0.0520 159 ASN   B CB  
6601 C CG  A ASN   B 159 ? 0.2591 0.2113 0.5061 0.0396  -0.0727 -0.0718 159 ASN   B CG  
6602 C CG  B ASN   B 159 ? 0.2593 0.2424 0.3705 0.0282  -0.0525 -0.0488 159 ASN   B CG  
6603 O OD1 A ASN   B 159 ? 0.2841 0.2220 0.5188 0.0472  -0.0684 -0.0775 159 ASN   B OD1 
6604 O OD1 B ASN   B 159 ? 0.2666 0.2476 0.3743 0.0328  -0.0526 -0.0485 159 ASN   B OD1 
6605 N ND2 A ASN   B 159 ? 0.2603 0.2256 0.5223 0.0338  -0.0804 -0.0613 159 ASN   B ND2 
6606 N ND2 B ASN   B 159 ? 0.2624 0.2502 0.3802 0.0274  -0.0537 -0.0424 159 ASN   B ND2 
6619 N N   . LEU   B 160 ? 0.1846 0.1648 0.4204 0.0154  -0.0553 -0.0532 160 LEU   B N   
6620 C CA  . LEU   B 160 ? 0.1767 0.1614 0.3941 0.0082  -0.0418 -0.0265 160 LEU   B CA  
6621 C C   . LEU   B 160 ? 0.1700 0.1558 0.3856 -0.0051 -0.0269 -0.0380 160 LEU   B C   
6622 O O   . LEU   B 160 ? 0.1529 0.1578 0.3943 -0.0050 -0.0364 -0.0164 160 LEU   B O   
6623 C CB  . LEU   B 160 ? 0.1715 0.1727 0.3671 -0.0035 -0.0458 -0.0079 160 LEU   B CB  
6624 C CG  . LEU   B 160 ? 0.1696 0.1848 0.3367 0.0051  -0.0406 -0.0020 160 LEU   B CG  
6625 C CD1 . LEU   B 160 ? 0.1903 0.2064 0.3292 -0.0005 -0.0226 -0.0026 160 LEU   B CD1 
6626 C CD2 . LEU   B 160 ? 0.1707 0.1881 0.3405 0.0173  -0.0331 -0.0139 160 LEU   B CD2 
6639 N N   A TYR   B 161 ? 0.1688 0.1553 0.3852 -0.0067 -0.0049 -0.0528 161 TYR   B N   
6640 N N   B TYR   B 161 ? 0.1769 0.1627 0.3594 -0.0066 -0.0113 -0.0457 161 TYR   B N   
6641 C CA  A TYR   B 161 ? 0.1784 0.1596 0.3647 -0.0230 0.0140  -0.0487 161 TYR   B CA  
6642 C CA  B TYR   B 161 ? 0.1877 0.1710 0.3313 -0.0106 0.0040  -0.0469 161 TYR   B CA  
6643 C C   A TYR   B 161 ? 0.1792 0.1628 0.3551 -0.0135 0.0198  -0.0397 161 TYR   B C   
6644 C C   B TYR   B 161 ? 0.1854 0.1688 0.3361 -0.0086 0.0099  -0.0479 161 TYR   B C   
6645 O O   A TYR   B 161 ? 0.1762 0.1643 0.3438 -0.0216 0.0156  -0.0367 161 TYR   B O   
6646 O O   B TYR   B 161 ? 0.1845 0.1707 0.3212 -0.0102 0.0073  -0.0506 161 TYR   B O   
6647 C CB  A TYR   B 161 ? 0.1927 0.1700 0.3489 -0.0350 0.0310  -0.0608 161 TYR   B CB  
6648 C CB  B TYR   B 161 ? 0.2029 0.1846 0.3042 -0.0117 0.0147  -0.0478 161 TYR   B CB  
6649 C CG  A TYR   B 161 ? 0.2233 0.1791 0.3307 -0.0396 0.0452  -0.0697 161 TYR   B CG  
6650 C CG  B TYR   B 161 ? 0.2236 0.1973 0.2829 -0.0133 0.0218  -0.0453 161 TYR   B CG  
6651 C CD1 A TYR   B 161 ? 0.2288 0.1750 0.3211 -0.0506 0.0420  -0.0749 161 TYR   B CD1 
6652 C CD1 B TYR   B 161 ? 0.2295 0.2009 0.2733 -0.0161 0.0230  -0.0449 161 TYR   B CD1 
6653 C CD2 A TYR   B 161 ? 0.2492 0.1910 0.3202 -0.0380 0.0403  -0.0687 161 TYR   B CD2 
6654 C CD2 B TYR   B 161 ? 0.2368 0.2052 0.2736 -0.0137 0.0208  -0.0411 161 TYR   B CD2 
6655 C CE1 A TYR   B 161 ? 0.2503 0.1933 0.3213 -0.0536 0.0391  -0.0707 161 TYR   B CE1 
6656 C CE1 B TYR   B 161 ? 0.2404 0.2107 0.2714 -0.0185 0.0233  -0.0403 161 TYR   B CE1 
6657 C CE2 A TYR   B 161 ? 0.2698 0.2077 0.3207 -0.0457 0.0384  -0.0611 161 TYR   B CE2 
6658 C CE2 B TYR   B 161 ? 0.2479 0.2142 0.2719 -0.0176 0.0212  -0.0365 161 TYR   B CE2 
6659 C CZ  A TYR   B 161 ? 0.2703 0.2074 0.3232 -0.0592 0.0313  -0.0570 161 TYR   B CZ  
6660 C CZ  B TYR   B 161 ? 0.2498 0.2165 0.2736 -0.0217 0.0195  -0.0337 161 TYR   B CZ  
6661 O OH  A TYR   B 161 ? 0.2992 0.2345 0.3492 -0.0593 0.0338  -0.0542 161 TYR   B OH  
6662 O OH  B TYR   B 161 ? 0.2644 0.2282 0.2869 -0.0244 0.0221  -0.0317 161 TYR   B OH  
6681 N N   . ASP   B 162 ? 0.1832 0.1655 0.3631 -0.0099 0.0054  -0.0577 162 ASP   B N   
6682 C CA  . ASP   B 162 ? 0.1965 0.1652 0.3837 -0.0112 -0.0046 -0.0578 162 ASP   B CA  
6683 C C   . ASP   B 162 ? 0.1921 0.1563 0.3773 -0.0140 -0.0098 -0.0483 162 ASP   B C   
6684 O O   . ASP   B 162 ? 0.1932 0.1635 0.3851 -0.0217 -0.0294 -0.0433 162 ASP   B O   
6685 C CB  . ASP   B 162 ? 0.2161 0.1718 0.4144 -0.0056 -0.0119 -0.0817 162 ASP   B CB  
6686 C CG  . ASP   B 162 ? 0.2172 0.2019 0.4397 0.0003  -0.0120 -0.0879 162 ASP   B CG  
6687 O OD1 . ASP   B 162 ? 0.2170 0.2219 0.4323 -0.0034 0.0046  -0.0872 162 ASP   B OD1 
6688 O OD2 . ASP   B 162 ? 0.2302 0.2220 0.4633 0.0166  -0.0105 -0.0827 162 ASP   B OD2 
6694 N N   . LYS   B 163 ? 0.1889 0.1416 0.3636 -0.0135 -0.0287 -0.0295 163 LYS   B N   
6695 C CA  . LYS   B 163 ? 0.2039 0.1605 0.3714 -0.0219 -0.0203 -0.0172 163 LYS   B CA  
6696 C C   . LYS   B 163 ? 0.1696 0.1502 0.3526 -0.0171 -0.0209 -0.0055 163 LYS   B C   
6697 O O   . LYS   B 163 ? 0.1680 0.1599 0.3660 -0.0230 -0.0282 -0.0010 163 LYS   B O   
6698 C CB  . LYS   B 163 ? 0.2593 0.2063 0.4091 -0.0234 -0.0261 -0.0071 163 LYS   B CB  
6699 C CG  . LYS   B 163 ? 0.3398 0.2918 0.4710 -0.0267 -0.0155 -0.0008 163 LYS   B CG  
6700 C CD  . LYS   B 163 ? 0.4084 0.3687 0.5364 -0.0409 -0.0172 0.0000  163 LYS   B CD  
6701 C CE  . LYS   B 163 ? 0.4563 0.4215 0.5858 -0.0504 -0.0182 0.0045  163 LYS   B CE  
6702 N NZ  . LYS   B 163 ? 0.5010 0.4812 0.6142 -0.0542 -0.0178 0.0058  163 LYS   B NZ  
6716 N N   . LEU   B 164 ? 0.1577 0.1425 0.3269 -0.0128 -0.0259 -0.0042 164 LEU   B N   
6717 C CA  . LEU   B 164 ? 0.1576 0.1443 0.3138 -0.0139 -0.0280 -0.0026 164 LEU   B CA  
6718 C C   . LEU   B 164 ? 0.1701 0.1473 0.3237 -0.0191 -0.0411 -0.0029 164 LEU   B C   
6719 O O   . LEU   B 164 ? 0.1693 0.1715 0.3409 -0.0237 -0.0381 -0.0006 164 LEU   B O   
6720 C CB  . LEU   B 164 ? 0.1544 0.1419 0.2971 -0.0123 -0.0212 -0.0008 164 LEU   B CB  
6721 C CG  . LEU   B 164 ? 0.1668 0.1601 0.2943 -0.0160 -0.0127 0.0077  164 LEU   B CG  
6722 C CD1 . LEU   B 164 ? 0.1809 0.1617 0.2846 -0.0151 -0.0326 -0.0076 164 LEU   B CD1 
6723 C CD2 . LEU   B 164 ? 0.1834 0.1923 0.3016 -0.0146 0.0076  -0.0132 164 LEU   B CD2 
6735 N N   . VAL   B 165 ? 0.2113 0.1589 0.3426 -0.0288 -0.0529 -0.0009 165 VAL   B N   
6736 C CA  . VAL   B 165 ? 0.2540 0.1727 0.3546 -0.0388 -0.0728 -0.0043 165 VAL   B CA  
6737 C C   . VAL   B 165 ? 0.2822 0.1813 0.3948 -0.0466 -0.1085 -0.0021 165 VAL   B C   
6738 O O   . VAL   B 165 ? 0.3033 0.2009 0.4053 -0.0567 -0.1108 0.0046  165 VAL   B O   
6739 C CB  . VAL   B 165 ? 0.2757 0.1931 0.3377 -0.0219 -0.0424 -0.0229 165 VAL   B CB  
6740 C CG1 . VAL   B 165 ? 0.2943 0.2024 0.3568 -0.0222 -0.0276 -0.0255 165 VAL   B CG1 
6741 C CG2 . VAL   B 165 ? 0.2706 0.1920 0.3223 -0.0222 -0.0351 -0.0219 165 VAL   B CG2 
6751 N N   . SER   B 166 ? 0.2924 0.1640 0.4381 -0.0478 -0.1312 -0.0193 166 SER   B N   
6752 C CA  . SER   B 166 ? 0.2873 0.1706 0.4950 -0.0449 -0.1153 -0.0276 166 SER   B CA  
6753 C C   . SER   B 166 ? 0.2669 0.1861 0.5191 -0.0532 -0.1062 0.0056  166 SER   B C   
6754 O O   . SER   B 166 ? 0.2651 0.2095 0.5561 -0.0648 -0.1194 -0.0142 166 SER   B O   
6755 C CB  . SER   B 166 ? 0.2854 0.1735 0.5269 -0.0365 -0.1039 -0.0400 166 SER   B CB  
6756 O OG  . SER   B 166 ? 0.2705 0.1764 0.5449 -0.0204 -0.1023 -0.0179 166 SER   B OG  
6762 N N   . SER   B 167 ? 0.2415 0.1828 0.4771 -0.0501 -0.1083 0.0394  167 SER   B N   
6763 C CA  . SER   B 167 ? 0.2303 0.1888 0.4597 -0.0450 -0.0728 0.0439  167 SER   B CA  
6764 C C   . SER   B 167 ? 0.2210 0.2046 0.4263 -0.0579 -0.0662 0.0647  167 SER   B C   
6765 O O   . SER   B 167 ? 0.2195 0.2235 0.4203 -0.0653 -0.0722 0.0630  167 SER   B O   
6766 C CB  . SER   B 167 ? 0.2123 0.1885 0.4651 -0.0365 -0.0415 0.0431  167 SER   B CB  
6767 O OG  . SER   B 167 ? 0.2048 0.2041 0.4587 -0.0228 -0.0192 0.0476  167 SER   B OG  
6773 N N   . PHE   B 168 ? 0.2186 0.2035 0.4139 -0.0550 -0.0453 0.0697  168 PHE   B N   
6774 C CA  . PHE   B 168 ? 0.2185 0.1966 0.3746 -0.0522 -0.0393 0.0366  168 PHE   B CA  
6775 C C   . PHE   B 168 ? 0.1923 0.1786 0.3083 -0.0330 -0.0258 0.0157  168 PHE   B C   
6776 O O   . PHE   B 168 ? 0.2233 0.1697 0.2929 -0.0039 -0.0199 -0.0023 168 PHE   B O   
6777 C CB  . PHE   B 168 ? 0.2318 0.1987 0.3782 -0.0664 -0.0501 0.0519  168 PHE   B CB  
6778 C CG  . PHE   B 168 ? 0.2618 0.1883 0.3633 -0.0688 -0.0545 0.0359  168 PHE   B CG  
6779 C CD1 . PHE   B 168 ? 0.2885 0.1918 0.3636 -0.0654 -0.0552 0.0304  168 PHE   B CD1 
6780 C CD2 . PHE   B 168 ? 0.2538 0.1837 0.3541 -0.0695 -0.0566 0.0445  168 PHE   B CD2 
6781 C CE1 . PHE   B 168 ? 0.3022 0.1930 0.3459 -0.0536 -0.0421 0.0425  168 PHE   B CE1 
6782 C CE2 . PHE   B 168 ? 0.2870 0.1916 0.3516 -0.0492 -0.0528 0.0329  168 PHE   B CE2 
6783 C CZ  . PHE   B 168 ? 0.2977 0.1845 0.3438 -0.0385 -0.0506 0.0483  168 PHE   B CZ  
6793 N N   . LEU   B 169 ? 0.2084 0.1913 0.3038 -0.0062 -0.0064 0.0085  169 LEU   B N   
6794 C CA  . LEU   B 169 ? 0.2482 0.2193 0.3381 -0.0061 0.0016  -0.0245 169 LEU   B CA  
6795 C C   . LEU   B 169 ? 0.2828 0.2411 0.3979 0.0093  0.0034  -0.0544 169 LEU   B C   
6796 O O   . LEU   B 169 ? 0.3059 0.2637 0.4402 0.0123  0.0062  -0.0721 169 LEU   B O   
6797 C CB  . LEU   B 169 ? 0.2755 0.2587 0.3437 -0.0128 -0.0060 -0.0005 169 LEU   B CB  
6798 C CG  . LEU   B 169 ? 0.3146 0.2945 0.3764 -0.0057 -0.0023 0.0023  169 LEU   B CG  
6799 C CD1 . LEU   B 169 ? 0.3269 0.3079 0.3804 -0.0093 -0.0045 0.0125  169 LEU   B CD1 
6800 C CD2 . LEU   B 169 ? 0.3135 0.3003 0.3776 0.0087  0.0126  -0.0080 169 LEU   B CD2 
6801 O OXT . LEU   B 169 ? 0.2997 0.2537 0.4101 0.0313  0.0144  -0.0568 169 LEU   B OXT 
6813 N N2  B A1BBN C .   ? 0.1470 0.2446 0.2134 -0.0240 0.0036  0.0135  201 A1BBN A N2  
6814 C C3  B A1BBN C .   ? 0.1902 0.2748 0.2544 -0.0277 0.0282  -0.0091 201 A1BBN A C3  
6815 C C6  B A1BBN C .   ? 0.1207 0.2375 0.1942 -0.0437 0.0179  0.0155  201 A1BBN A C6  
6816 C C9  B A1BBN C .   ? 0.2739 0.3356 0.3010 -0.0672 0.0341  -0.0316 201 A1BBN A C9  
6817 C C12 B A1BBN C .   ? 0.2819 0.3385 0.2965 -0.0712 0.0318  -0.0355 201 A1BBN A C12 
6818 C C14 B A1BBN C .   ? 0.2836 0.3399 0.2948 -0.0697 0.0274  -0.0342 201 A1BBN A C14 
6819 C C1  B A1BBN C .   ? 0.2671 0.3316 0.3028 -0.0614 0.0356  -0.0286 201 A1BBN A C1  
6820 C C10 B A1BBN C .   ? 0.2807 0.3383 0.2957 -0.0702 0.0322  -0.0358 201 A1BBN A C10 
6821 C C11 B A1BBN C .   ? 0.2810 0.3376 0.2936 -0.0733 0.0338  -0.0389 201 A1BBN A C11 
6822 C C13 B A1BBN C .   ? 0.2793 0.3379 0.2980 -0.0674 0.0303  -0.0329 201 A1BBN A C13 
6823 C C15 B A1BBN C .   ? 0.2840 0.3391 0.2907 -0.0704 0.0288  -0.0343 201 A1BBN A C15 
6824 C C2  B A1BBN C .   ? 0.2400 0.3187 0.2943 -0.0488 0.0363  -0.0239 201 A1BBN A C2  
6825 C C4  B A1BBN C .   ? 0.1642 0.2582 0.2300 -0.0281 0.0254  0.0000  201 A1BBN A C4  
6826 C C5  B A1BBN C .   ? 0.1435 0.2506 0.2147 -0.0335 0.0274  0.0113  201 A1BBN A C5  
6827 C C7  B A1BBN C .   ? 0.1606 0.2524 0.2227 -0.0270 0.0198  0.0058  201 A1BBN A C7  
6828 C C8  B A1BBN C .   ? 0.1812 0.2672 0.2423 -0.0220 0.0258  -0.0048 201 A1BBN A C8  
6829 N N1  B A1BBN C .   ? 0.2144 0.2974 0.2767 -0.0381 0.0309  -0.0149 201 A1BBN A N1  
6830 N N3  B A1BBN C .   ? 0.1708 0.2575 0.2249 -0.0288 0.0315  0.0049  201 A1BBN A N3  
6831 N N4  B A1BBN C .   ? 0.1835 0.2710 0.2490 -0.0253 0.0322  -0.0109 201 A1BBN A N4  
6832 O O1  B A1BBN C .   ? 0.2700 0.3331 0.3105 -0.0574 0.0378  -0.0282 201 A1BBN A O1  
6853 O O   . HOH   D .   ? 0.3701 0.3553 0.4036 -0.1322 -0.0143 0.1359  301 HOH   A O   
6854 O O   . HOH   D .   ? 0.4362 0.7465 0.5319 -0.1188 0.0878  0.0352  302 HOH   A O   
6855 O O   . HOH   D .   ? 0.5632 0.4645 0.6091 0.0705  -0.0825 0.0726  303 HOH   A O   
6856 O O   . HOH   D .   ? 0.3164 0.2762 0.5527 -0.0574 -0.1534 0.1563  304 HOH   A O   
6857 O O   . HOH   D .   ? 0.3231 0.2492 0.5042 -0.0214 -0.0757 0.0102  305 HOH   A O   
6858 O O   . HOH   D .   ? 0.5367 0.5628 0.6851 0.1546  -0.1017 0.1104  306 HOH   A O   
6859 O O   . HOH   D .   ? 0.4324 0.3643 0.5844 0.0167  0.1703  0.0391  307 HOH   A O   
6860 O O   . HOH   D .   ? 0.3169 0.6558 0.5855 0.1146  0.0985  0.1671  308 HOH   A O   
6861 O O   . HOH   D .   ? 0.5971 0.4679 0.5802 -0.1235 0.1147  0.1748  309 HOH   A O   
6862 O O   . HOH   D .   ? 0.6518 0.5137 0.3362 0.2235  -0.1127 0.0489  310 HOH   A O   
6863 O O   . HOH   D .   ? 0.5954 0.4361 0.6119 -0.0450 0.2060  0.1751  311 HOH   A O   
6864 O O   . HOH   D .   ? 0.2261 0.2293 0.3379 0.0039  -0.0579 0.0410  312 HOH   A O   
6865 O O   . HOH   D .   ? 0.2358 0.1852 0.2800 0.0364  -0.0471 -0.0065 313 HOH   A O   
6866 O O   . HOH   D .   ? 0.6868 0.7050 0.6223 -0.0863 -0.1280 -0.1185 314 HOH   A O   
6867 O O   . HOH   D .   ? 0.5254 0.2370 0.6281 0.0791  -0.0088 -0.0213 315 HOH   A O   
6868 O O   . HOH   D .   ? 0.3333 0.3490 0.1923 -0.0611 0.0558  0.0255  316 HOH   A O   
6869 O O   . HOH   D .   ? 0.3135 0.2342 0.2771 -0.0444 0.0104  -0.0059 317 HOH   A O   
6870 O O   . HOH   D .   ? 0.2756 0.5496 0.4106 0.0156  -0.0170 0.1101  318 HOH   A O   
6871 O O   . HOH   D .   ? 0.3750 0.1982 0.2410 0.0275  0.0361  0.0239  319 HOH   A O   
6872 O O   . HOH   D .   ? 0.2214 0.1705 0.2905 0.0081  -0.0571 -0.0154 320 HOH   A O   
6873 O O   . HOH   D .   ? 0.2716 0.4702 0.5899 -0.0035 0.1024  0.2513  321 HOH   A O   
6874 O O   . HOH   D .   ? 0.1838 0.1946 0.2750 -0.0268 0.0237  0.0359  322 HOH   A O   
6875 O O   . HOH   D .   ? 0.5375 0.7030 0.4186 0.2401  -0.0507 -0.0716 323 HOH   A O   
6876 O O   . HOH   D .   ? 0.5428 0.2838 0.3579 -0.1240 0.0711  0.0465  324 HOH   A O   
6877 O O   . HOH   D .   ? 0.1937 0.4561 0.3587 0.0851  -0.0009 0.0612  325 HOH   A O   
6878 O O   . HOH   D .   ? 0.1790 0.4120 0.3118 -0.0208 0.0252  0.1038  326 HOH   A O   
6879 O O   . HOH   D .   ? 0.2244 0.1942 0.3543 -0.0452 0.0098  -0.0240 327 HOH   A O   
6880 O O   . HOH   D .   ? 0.6057 0.6483 0.5077 0.0295  0.2777  -0.0938 328 HOH   A O   
6881 O O   . HOH   D .   ? 0.2672 0.2775 0.3106 -0.0059 0.0554  0.0759  329 HOH   A O   
6882 O O   . HOH   D .   ? 0.4911 0.3808 0.3469 -0.1162 -0.1293 0.0425  330 HOH   A O   
6883 O O   . HOH   D .   ? 0.2801 0.2133 0.2846 -0.0163 0.0107  0.0249  331 HOH   A O   
6884 O O   . HOH   D .   ? 0.7535 0.8042 0.5249 0.1319  -0.0514 -0.0734 332 HOH   A O   
6885 O O   . HOH   D .   ? 0.2388 0.2079 0.3827 0.0052  -0.1000 -0.0420 333 HOH   A O   
6886 O O   A HOH   D .   ? 0.4086 0.4967 0.2509 -0.0781 0.0769  0.0663  334 HOH   A O   
6887 O O   . HOH   D .   ? 0.6574 0.6106 0.4002 -0.0464 0.0086  0.1187  335 HOH   A O   
6888 O O   . HOH   D .   ? 0.2132 0.3964 0.4483 -0.0474 0.0376  -0.1178 336 HOH   A O   
6889 O O   . HOH   D .   ? 0.2350 0.3434 0.4514 -0.0502 -0.0783 0.1586  337 HOH   A O   
6890 O O   . HOH   D .   ? 0.5473 0.6572 0.4755 0.0762  -0.0697 0.2240  338 HOH   A O   
6891 O O   . HOH   D .   ? 0.1666 0.1702 0.2714 -0.0272 0.0045  0.0119  339 HOH   A O   
6892 O O   . HOH   D .   ? 0.3426 0.4630 0.2725 -0.0113 0.0645  0.0308  340 HOH   A O   
6893 O O   . HOH   D .   ? 0.1919 0.3585 0.2771 0.0825  0.0546  0.1020  341 HOH   A O   
6894 O O   . HOH   D .   ? 0.1889 0.1918 0.2479 0.0145  -0.0237 0.0338  342 HOH   A O   
6895 O O   . HOH   D .   ? 0.5562 0.3516 0.5585 0.1504  -0.0271 -0.0067 343 HOH   A O   
6896 O O   . HOH   D .   ? 0.2355 0.2169 0.2964 0.0331  0.0285  0.0491  344 HOH   A O   
6897 O O   . HOH   D .   ? 0.4033 0.3477 0.2923 -0.0497 -0.1204 0.0612  345 HOH   A O   
6898 O O   . HOH   D .   ? 0.5770 0.2162 0.4285 0.0583  -0.0761 0.0360  346 HOH   A O   
6899 O O   . HOH   D .   ? 0.3558 0.4570 0.4601 -0.0367 0.1649  0.0783  347 HOH   A O   
6900 O O   . HOH   D .   ? 0.5190 0.3774 0.5151 -0.1717 -0.0524 0.2045  348 HOH   A O   
6901 O O   . HOH   D .   ? 0.2647 0.4265 0.3690 0.1100  -0.0805 -0.0455 349 HOH   A O   
6902 O O   . HOH   D .   ? 0.3452 0.4207 0.2390 -0.1425 -0.0112 -0.0630 350 HOH   A O   
6903 O O   . HOH   D .   ? 0.3230 0.7394 0.5709 -0.0488 -0.0917 0.2471  351 HOH   A O   
6904 O O   . HOH   D .   ? 0.3102 0.4187 0.3880 -0.1330 -0.1056 -0.0034 352 HOH   A O   
6905 O O   . HOH   D .   ? 0.1567 0.2122 0.2497 -0.0007 -0.0052 0.0567  353 HOH   A O   
6906 O O   . HOH   D .   ? 0.1702 0.2071 0.3296 0.0101  -0.0408 -0.0568 354 HOH   A O   
6907 O O   A HOH   D .   ? 0.2048 0.3753 0.2322 0.0315  0.0192  0.0346  355 HOH   A O   
6908 O O   . HOH   D .   ? 0.5072 0.5431 0.5943 0.1870  0.0588  -0.0618 356 HOH   A O   
6909 O O   . HOH   D .   ? 0.4466 0.7163 0.5809 -0.0844 -0.1368 0.0405  357 HOH   A O   
6910 O O   . HOH   D .   ? 0.2177 0.2660 0.4110 0.0244  0.0922  -0.0600 358 HOH   A O   
6911 O O   . HOH   D .   ? 0.7538 0.4425 0.6777 0.0432  -0.1296 0.0415  359 HOH   A O   
6912 O O   . HOH   D .   ? 0.3793 0.4882 0.4855 0.2042  0.0748  0.0568  360 HOH   A O   
6913 O O   . HOH   D .   ? 0.2099 0.2086 0.3839 0.0284  0.0883  0.0122  361 HOH   A O   
6914 O O   . HOH   D .   ? 0.7515 0.4166 0.3173 0.0334  0.0506  0.1260  362 HOH   A O   
6915 O O   . HOH   D .   ? 0.3209 0.3834 0.4657 -0.0846 -0.0905 -0.0699 363 HOH   A O   
6916 O O   . HOH   D .   ? 0.1607 0.1949 0.2789 0.0055  0.0013  0.0231  364 HOH   A O   
6917 O O   . HOH   D .   ? 0.2124 0.1747 0.1947 -0.0011 0.0203  0.0216  365 HOH   A O   
6918 O O   . HOH   D .   ? 0.5772 0.5738 0.7698 -0.0961 -0.0644 0.1049  366 HOH   A O   
6919 O O   . HOH   D .   ? 0.1994 0.2555 0.2513 -0.0310 -0.0062 0.0858  367 HOH   A O   
6920 O O   . HOH   D .   ? 0.1456 0.1368 0.1774 -0.0017 0.0087  0.0100  368 HOH   A O   
6921 O O   . HOH   D .   ? 0.3170 0.3473 0.4269 -0.1313 0.0801  0.0013  369 HOH   A O   
6922 O O   . HOH   D .   ? 0.1720 0.1494 0.2685 -0.0116 0.0206  -0.0031 370 HOH   A O   
6923 O O   . HOH   D .   ? 0.2665 0.4503 0.3706 -0.0428 0.0382  0.0024  371 HOH   A O   
6924 O O   . HOH   D .   ? 0.4220 0.2361 0.2975 0.1178  0.0397  0.0190  372 HOH   A O   
6925 O O   . HOH   D .   ? 0.1606 0.1684 0.1847 -0.0081 -0.0133 -0.0013 373 HOH   A O   
6926 O O   . HOH   D .   ? 0.4293 0.2414 0.4560 -0.1101 0.0799  0.0240  374 HOH   A O   
6927 O O   . HOH   D .   ? 0.4121 0.3439 0.3737 -0.1171 -0.0259 -0.0206 375 HOH   A O   
6928 O O   . HOH   D .   ? 0.2256 0.2069 0.2238 -0.0007 0.0245  0.0201  376 HOH   A O   
6929 O O   . HOH   D .   ? 0.6534 0.6995 0.6377 -0.1335 0.0507  0.0200  377 HOH   A O   
6930 O O   . HOH   D .   ? 1.1406 1.0830 0.8693 -0.0294 -0.0699 -0.0951 378 HOH   A O   
6931 O O   . HOH   D .   ? 0.1593 0.1792 0.2107 0.0121  -0.0198 -0.0205 379 HOH   A O   
6932 O O   . HOH   D .   ? 0.4482 0.2497 0.3753 -0.1319 0.1583  -0.0447 380 HOH   A O   
6933 O O   . HOH   D .   ? 0.2228 0.2396 0.2495 -0.0335 -0.0438 0.0517  381 HOH   A O   
6934 O O   . HOH   D .   ? 0.3383 0.6939 0.3223 0.1424  0.0624  -0.0526 382 HOH   A O   
6935 O O   . HOH   D .   ? 0.1802 0.1895 0.2357 0.0028  -0.0237 0.0119  383 HOH   A O   
6936 O O   . HOH   D .   ? 0.1799 0.2168 0.2628 -0.0266 0.0090  0.0346  384 HOH   A O   
6937 O O   . HOH   D .   ? 0.2661 0.2266 0.2063 -0.0629 0.0153  0.0398  385 HOH   A O   
6938 O O   A HOH   D .   ? 0.2460 0.2350 0.2617 0.0163  -0.0026 0.0691  386 HOH   A O   
6939 O O   . HOH   D .   ? 0.3337 0.2849 0.3574 -0.0154 -0.0369 0.0936  387 HOH   A O   
6940 O O   . HOH   D .   ? 0.3979 0.7387 0.4483 -0.0764 -0.0248 0.2189  388 HOH   A O   
6941 O O   . HOH   D .   ? 0.2826 0.4983 0.3616 0.0661  0.0771  0.2187  389 HOH   A O   
6942 O O   . HOH   D .   ? 0.3928 0.2732 0.4808 -0.0959 0.0224  -0.0075 390 HOH   A O   
6943 O O   . HOH   D .   ? 0.2794 0.3576 0.3773 -0.0104 0.0997  -0.0545 391 HOH   A O   
6944 O O   . HOH   D .   ? 0.4713 0.4350 0.6176 0.1518  0.1467  -0.0960 392 HOH   A O   
6945 O O   . HOH   D .   ? 0.3228 0.3072 0.2348 0.0097  0.0572  0.0024  393 HOH   A O   
6946 O O   . HOH   D .   ? 0.1466 0.1571 0.2218 0.0005  -0.0211 0.0085  394 HOH   A O   
6947 O O   . HOH   D .   ? 0.2756 0.3566 0.3658 -0.0253 0.0943  -0.0312 395 HOH   A O   
6948 O O   . HOH   D .   ? 0.4759 0.5018 0.4561 0.1429  -0.1069 -0.1619 396 HOH   A O   
6949 O O   . HOH   D .   ? 0.1863 0.2974 0.3494 -0.0208 0.0689  0.0781  397 HOH   A O   
6950 O O   . HOH   D .   ? 0.2139 0.2365 0.2853 -0.0140 -0.0260 0.0824  398 HOH   A O   
6951 O O   . HOH   D .   ? 0.6593 0.6866 0.5916 0.0951  0.0504  0.0022  399 HOH   A O   
6952 O O   . HOH   D .   ? 0.1930 0.1841 0.3275 0.0205  -0.0353 0.0311  400 HOH   A O   
6953 O O   . HOH   D .   ? 0.3417 0.2884 0.2770 -0.0715 -0.1053 0.0437  401 HOH   A O   
6954 O O   . HOH   D .   ? 0.1946 0.2027 0.4228 0.0402  0.1114  0.1052  402 HOH   A O   
6955 O O   . HOH   D .   ? 0.1896 0.1523 0.1922 -0.0251 0.0206  0.0001  403 HOH   A O   
6956 O O   . HOH   D .   ? 0.5569 0.6351 0.5639 0.2254  0.1395  0.0561  404 HOH   A O   
6957 O O   . HOH   D .   ? 0.3018 0.3739 0.5511 -0.0411 0.0952  0.0235  405 HOH   A O   
6958 O O   . HOH   D .   ? 0.2582 0.2369 0.2699 -0.0588 0.0007  0.0621  406 HOH   A O   
6959 O O   . HOH   D .   ? 0.2433 0.1842 0.3454 -0.0016 -0.0383 0.0166  407 HOH   A O   
6960 O O   . HOH   D .   ? 0.2808 0.3030 0.3722 -0.0097 -0.0261 -0.0660 408 HOH   A O   
6961 O O   A HOH   D .   ? 0.2881 0.2067 0.4654 0.0049  0.1341  0.0323  409 HOH   A O   
6962 O O   . HOH   D .   ? 0.1717 0.1788 0.3721 0.0001  -0.0136 0.0130  410 HOH   A O   
6963 O O   . HOH   D .   ? 0.2613 0.3744 0.7403 -0.0226 0.0464  -0.0383 411 HOH   A O   
6964 O O   . HOH   D .   ? 0.2257 0.2878 0.2798 -0.0191 -0.0513 0.0682  412 HOH   A O   
6965 O O   . HOH   D .   ? 0.5402 0.5693 0.2456 0.0291  0.0984  0.0944  413 HOH   A O   
6966 O O   . HOH   D .   ? 0.4630 0.6375 0.3607 -0.0829 -0.0116 0.1468  414 HOH   A O   
6967 O O   . HOH   D .   ? 0.3734 0.3273 0.5161 0.0951  0.0790  0.0389  415 HOH   A O   
6968 O O   . HOH   D .   ? 0.3371 0.1378 0.2432 -0.0060 -0.0599 0.0192  416 HOH   A O   
6969 O O   . HOH   D .   ? 0.6542 0.4280 0.5213 -0.1550 0.0412  0.0859  417 HOH   A O   
6970 O O   . HOH   D .   ? 0.4897 0.3458 0.2827 -0.0685 -0.0098 0.0193  418 HOH   A O   
6971 O O   . HOH   D .   ? 0.2107 0.2746 0.4786 -0.0308 -0.0172 0.0298  419 HOH   A O   
6972 O O   A HOH   D .   ? 0.3056 0.2502 0.3399 0.0792  0.1147  0.0854  420 HOH   A O   
6973 O O   . HOH   D .   ? 0.2429 0.3794 0.2837 0.1332  -0.0048 0.0247  421 HOH   A O   
6974 O O   . HOH   D .   ? 0.2853 0.6344 0.1994 -0.0091 0.0509  0.0019  422 HOH   A O   
6975 O O   . HOH   D .   ? 0.1824 0.2498 0.3226 -0.0277 -0.0039 0.0702  423 HOH   A O   
6976 O O   A HOH   D .   ? 0.5850 0.4872 0.3091 -0.1234 0.0041  0.1228  424 HOH   A O   
6977 O O   . HOH   D .   ? 0.6975 0.4259 0.5500 0.1833  -0.0806 0.1542  425 HOH   A O   
6978 O O   . HOH   D .   ? 0.4441 0.2422 0.5622 -0.0971 -0.2495 0.1179  426 HOH   A O   
6979 O O   . HOH   D .   ? 0.5510 0.4734 0.5414 -0.0904 -0.1141 -0.1359 427 HOH   A O   
6980 O O   . HOH   D .   ? 0.2105 0.2562 0.4089 0.0126  -0.0482 -0.0076 428 HOH   A O   
6981 O O   . HOH   D .   ? 0.5285 0.7393 0.3877 0.0516  0.2284  -0.0705 429 HOH   A O   
6982 O O   . HOH   D .   ? 0.6327 0.7153 0.7362 -0.1417 0.0667  -0.1309 430 HOH   A O   
6983 O O   . HOH   D .   ? 0.2105 0.1670 0.1998 0.0043  -0.0166 -0.0163 431 HOH   A O   
6984 O O   . HOH   D .   ? 0.2093 0.2336 0.4541 -0.0236 -0.0829 0.0698  432 HOH   A O   
6985 O O   . HOH   D .   ? 0.2886 0.1949 0.3174 0.0182  0.0106  0.0240  433 HOH   A O   
6986 O O   . HOH   D .   ? 0.5901 0.7280 0.7167 0.0656  -0.0165 -0.0610 434 HOH   A O   
6987 O O   . HOH   D .   ? 0.5727 0.4928 0.4097 -0.0256 -0.1471 -0.0121 435 HOH   A O   
6988 O O   . HOH   D .   ? 0.3955 0.2944 0.2062 -0.1019 0.0193  0.0543  436 HOH   A O   
6989 O O   A HOH   D .   ? 0.6082 0.6832 0.4120 0.1515  -0.1037 0.1817  437 HOH   A O   
6990 O O   . HOH   D .   ? 0.4579 0.4053 0.3297 0.2543  -0.0603 -0.0424 438 HOH   A O   
6991 O O   . HOH   D .   ? 0.2476 0.3100 0.2754 0.0062  -0.0023 -0.0550 439 HOH   A O   
6992 O O   . HOH   D .   ? 0.6847 0.6075 0.7168 0.0519  -0.1005 -0.0290 440 HOH   A O   
6993 O O   . HOH   D .   ? 0.5774 0.5666 0.5443 -0.0037 0.0708  0.2621  441 HOH   A O   
6994 O O   . HOH   D .   ? 0.3178 0.3607 0.6327 0.0010  0.1365  -0.1407 442 HOH   A O   
6995 O O   . HOH   D .   ? 0.2405 0.2083 0.3217 0.0122  0.0192  0.0241  443 HOH   A O   
6996 O O   . HOH   D .   ? 0.7322 0.3817 0.7253 0.1627  0.0584  -0.0894 444 HOH   A O   
6997 O O   . HOH   D .   ? 0.6652 0.7420 0.5312 -0.1008 0.1874  0.1319  445 HOH   A O   
6998 O O   A HOH   D .   ? 0.1680 0.2077 0.3308 0.0086  0.0202  0.0641  446 HOH   A O   
6999 O O   . HOH   D .   ? 0.7450 0.5887 0.7852 0.0195  -0.1224 0.1942  447 HOH   A O   
7000 O O   . HOH   D .   ? 0.4317 0.4633 0.4173 0.0370  0.0880  0.0568  448 HOH   A O   
7001 O O   . HOH   D .   ? 0.4449 0.3155 0.4203 0.0389  0.0526  0.0097  449 HOH   A O   
7002 O O   . HOH   D .   ? 0.4070 0.4531 0.4153 0.2114  -0.0496 0.0716  450 HOH   A O   
7003 O O   . HOH   D .   ? 0.5061 0.5679 0.4652 -0.0344 -0.0482 0.1439  451 HOH   A O   
7004 O O   . HOH   D .   ? 0.7557 0.7844 0.4918 0.0292  -0.0927 -0.0587 452 HOH   A O   
7005 O O   . HOH   D .   ? 0.3046 0.2921 0.3798 -0.0478 0.0141  -0.0562 453 HOH   A O   
7006 O O   . HOH   D .   ? 0.3702 0.5512 0.5008 -0.1683 0.1058  -0.1082 454 HOH   A O   
7007 O O   . HOH   D .   ? 0.3875 0.5965 0.5566 0.0508  -0.0290 0.2271  455 HOH   A O   
7008 O O   . HOH   D .   ? 0.4566 0.5774 0.4214 0.0431  -0.0918 -0.0787 456 HOH   A O   
7009 O O   . HOH   D .   ? 0.3241 0.3242 0.5849 -0.0117 -0.0971 -0.0756 457 HOH   A O   
7010 O O   . HOH   D .   ? 0.2983 0.4637 0.5425 0.0447  0.0229  -0.1634 458 HOH   A O   
7011 O O   . HOH   D .   ? 0.4397 0.4540 0.4577 -0.1289 0.0299  -0.0203 459 HOH   A O   
7012 O O   . HOH   D .   ? 0.2858 0.2932 0.3694 -0.0985 0.0396  -0.0343 460 HOH   A O   
7013 O O   . HOH   D .   ? 0.2633 0.1829 0.2927 0.0216  -0.0791 -0.0232 461 HOH   A O   
7014 O O   . HOH   D .   ? 0.6115 0.3806 0.7207 0.0641  -0.0133 0.2396  462 HOH   A O   
7015 O O   . HOH   D .   ? 0.3982 0.6806 0.4043 -0.0854 -0.1025 0.2197  463 HOH   A O   
7016 O O   . HOH   D .   ? 0.6075 0.4494 0.5033 0.0443  0.1557  0.0529  464 HOH   A O   
7017 O O   . HOH   D .   ? 0.5795 0.6152 0.4793 0.1640  -0.0132 -0.0003 465 HOH   A O   
7018 O O   . HOH   D .   ? 0.3933 0.2804 0.4068 0.0154  0.1148  0.0160  466 HOH   A O   
7019 O O   . HOH   D .   ? 0.7784 0.6262 0.5894 0.0282  0.1340  0.2651  467 HOH   A O   
7020 O O   . HOH   D .   ? 0.2752 0.2909 0.2712 0.0441  -0.0055 -0.0025 468 HOH   A O   
7021 O O   . HOH   D .   ? 0.5088 0.3084 0.3643 -0.0916 -0.1423 0.0600  469 HOH   A O   
7022 O O   . HOH   D .   ? 0.4392 0.5461 0.4384 -0.1951 -0.0463 -0.0070 470 HOH   A O   
7023 O O   . HOH   D .   ? 0.6871 0.7504 0.7896 -0.1516 -0.1335 0.0286  471 HOH   A O   
7024 O O   . HOH   D .   ? 0.7143 0.4065 0.4866 -0.0603 0.1486  -0.0071 472 HOH   A O   
7025 O O   . HOH   D .   ? 0.4562 0.6006 0.3212 -0.0063 -0.0085 0.0530  473 HOH   A O   
7026 O O   . HOH   D .   ? 0.6009 0.4428 0.4700 -0.0205 -0.0203 -0.1213 474 HOH   A O   
7027 O O   . HOH   D .   ? 0.6580 0.7987 0.5420 0.2731  -0.1507 0.0026  475 HOH   A O   
7028 O O   . HOH   D .   ? 0.4027 0.4733 0.4949 0.0408  0.1975  0.1161  476 HOH   A O   
7029 O O   . HOH   D .   ? 0.8137 0.3803 0.3563 -0.0202 -0.1433 0.0262  477 HOH   A O   
7030 O O   . HOH   D .   ? 0.3056 0.2911 0.6176 -0.0123 0.1370  -0.0680 478 HOH   A O   
7031 O O   . HOH   D .   ? 0.5500 0.5700 0.4918 0.0604  -0.0759 -0.0386 479 HOH   A O   
7032 O O   . HOH   D .   ? 0.3307 0.2224 0.6831 0.0039  0.0920  0.0865  480 HOH   A O   
7033 O O   . HOH   D .   ? 0.7364 0.5722 0.7173 -0.1021 0.0723  -0.0988 481 HOH   A O   
7034 O O   . HOH   D .   ? 0.5033 0.4991 0.3400 -0.0471 -0.0675 0.0121  482 HOH   A O   
7035 O O   . HOH   D .   ? 0.6755 0.5634 0.7179 0.0787  0.2495  -0.1150 483 HOH   A O   
7036 O O   . HOH   D .   ? 0.4218 0.3778 0.5318 -0.0843 0.0511  0.0269  484 HOH   A O   
7037 O O   . HOH   D .   ? 0.6281 0.4889 0.5383 -0.1097 -0.0587 -0.0539 485 HOH   A O   
7038 O O   . HOH   D .   ? 0.2501 0.5326 0.4178 0.0912  0.0929  0.2655  486 HOH   A O   
7039 O O   . HOH   D .   ? 0.2897 0.2464 0.6565 -0.0007 -0.1318 0.0272  487 HOH   A O   
7040 O O   . HOH   D .   ? 0.8303 0.8221 0.5577 -0.0936 0.1460  0.1903  488 HOH   A O   
7041 O O   . HOH   D .   ? 0.5704 0.5979 0.6269 0.1107  -0.1117 0.0901  489 HOH   A O   
7042 O O   . HOH   D .   ? 0.4322 0.4082 0.2798 -0.1022 0.1268  -0.0569 490 HOH   A O   
7043 O O   . HOH   D .   ? 0.6349 0.2905 0.4435 -0.0516 0.0984  0.0637  491 HOH   A O   
7044 O O   . HOH   D .   ? 0.4783 0.3355 0.4608 -0.0082 0.2311  0.0316  492 HOH   A O   
7045 O O   B HOH   D .   ? 0.2960 0.3593 0.3014 0.0473  0.0352  0.0344  493 HOH   A O   
7046 O O   . HOH   D .   ? 0.2371 0.3659 0.3658 0.0583  -0.0574 0.0562  494 HOH   A O   
7047 O O   . HOH   D .   ? 0.4183 0.9434 0.6228 -0.1078 -0.0554 0.2319  495 HOH   A O   
7048 O O   . HOH   D .   ? 0.3292 0.4676 0.5142 0.0653  -0.0736 0.0321  496 HOH   A O   
7049 O O   . HOH   D .   ? 0.5581 0.8189 0.5825 0.1263  -0.0543 0.0872  497 HOH   A O   
7050 O O   . HOH   D .   ? 0.3074 0.4905 0.3495 -0.0266 -0.0468 -0.0592 498 HOH   A O   
7051 O O   . HOH   D .   ? 0.5541 0.2966 0.5034 0.0691  -0.1160 0.0795  499 HOH   A O   
7052 O O   . HOH   D .   ? 0.3182 0.2610 0.4721 0.0026  0.0075  0.0603  500 HOH   A O   
7053 O O   . HOH   D .   ? 0.5516 0.7059 0.5883 0.3292  -0.0319 0.1384  501 HOH   A O   
7054 O O   A HOH   D .   ? 0.3102 0.7413 0.2826 0.0645  0.0512  0.1436  502 HOH   A O   
7055 O O   . HOH   D .   ? 0.7055 0.5631 0.4730 -0.0873 -0.0844 -0.1223 503 HOH   A O   
7056 O O   . HOH   D .   ? 0.3099 0.7109 0.4707 0.0481  0.0506  -0.1008 504 HOH   A O   
7057 O O   . HOH   D .   ? 0.4957 0.6920 0.5562 -0.0547 -0.0772 0.0771  505 HOH   A O   
7058 O O   . HOH   D .   ? 0.4902 0.5390 0.4598 0.1619  0.0327  0.1427  506 HOH   A O   
7059 O O   . HOH   D .   ? 0.2975 0.5081 0.6206 -0.0195 -0.0711 0.3164  507 HOH   A O   
7060 O O   . HOH   E .   ? 0.2338 0.2287 0.3284 0.0168  0.0770  0.0211  201 HOH   B O   
7061 O O   . HOH   E .   ? 0.3620 0.3395 0.7214 -0.0208 0.0436  -0.0645 202 HOH   B O   
7062 O O   . HOH   E .   ? 0.5290 0.3832 0.4122 -0.0082 0.0078  -0.1650 203 HOH   B O   
7063 O O   . HOH   E .   ? 0.3598 0.5910 0.4955 -0.0080 0.1827  -0.1791 204 HOH   B O   
7064 O O   . HOH   E .   ? 0.3087 0.6927 0.4343 0.1055  0.0388  0.2703  205 HOH   B O   
7065 O O   . HOH   E .   ? 0.3365 0.2288 0.5408 -0.0068 0.1951  0.0235  206 HOH   B O   
7066 O O   . HOH   E .   ? 0.7512 0.3998 0.4673 0.0012  0.1459  -0.0108 207 HOH   B O   
7067 O O   . HOH   E .   ? 0.3585 0.4638 0.2914 -0.0302 -0.0416 -0.1175 208 HOH   B O   
7068 O O   . HOH   E .   ? 0.5436 0.6175 0.4363 0.3246  -0.1141 -0.0305 209 HOH   B O   
7069 O O   . HOH   E .   ? 0.4078 0.4540 0.4069 0.1860  0.0058  0.0747  210 HOH   B O   
7070 O O   . HOH   E .   ? 0.6397 0.6768 0.5701 0.2008  0.0418  -0.0406 211 HOH   B O   
7071 O O   . HOH   E .   ? 0.1760 0.2040 0.3341 -0.0253 -0.0194 0.0140  212 HOH   B O   
7072 O O   . HOH   E .   ? 0.3167 0.2055 0.5652 -0.0058 0.1852  0.0620  213 HOH   B O   
7073 O O   . HOH   E .   ? 0.1998 0.2383 0.3005 -0.0050 0.0289  -0.0311 214 HOH   B O   
7074 O O   . HOH   E .   ? 0.3854 0.4006 0.3625 -0.0119 -0.1243 0.0554  215 HOH   B O   
7075 O O   . HOH   E .   ? 0.3932 0.2969 0.4347 0.0441  -0.0873 -0.0074 216 HOH   B O   
7076 O O   . HOH   E .   ? 0.3988 0.4502 0.5880 -0.0979 -0.0172 -0.1413 217 HOH   B O   
7077 O O   . HOH   E .   ? 0.2737 0.2835 0.6467 0.0621  -0.1106 0.0347  218 HOH   B O   
7078 O O   . HOH   E .   ? 0.3761 0.5470 0.6102 0.2307  0.0566  -0.0764 219 HOH   B O   
7079 O O   . HOH   E .   ? 0.1864 0.2340 0.3725 -0.0201 0.0312  -0.0188 220 HOH   B O   
7080 O O   . HOH   E .   ? 0.5450 0.4645 0.6578 0.0414  -0.0837 0.3035  221 HOH   B O   
7081 O O   . HOH   E .   ? 0.7231 0.5375 0.4396 0.1705  -0.0350 -0.1321 222 HOH   B O   
7082 O O   . HOH   E .   ? 0.5261 0.7400 0.4018 0.2512  0.0616  0.0946  223 HOH   B O   
7083 O O   . HOH   E .   ? 0.2361 0.2651 0.3799 -0.0272 0.0176  -0.0607 224 HOH   B O   
7084 O O   . HOH   E .   ? 0.5319 0.2296 0.3104 -0.0129 -0.0796 0.0163  225 HOH   B O   
7085 O O   . HOH   E .   ? 0.6077 0.4368 0.2847 -0.0625 0.0920  -0.0365 226 HOH   B O   
7086 O O   . HOH   E .   ? 0.6227 0.6196 0.3759 0.0507  0.0241  0.0912  227 HOH   B O   
7087 O O   . HOH   E .   ? 0.2742 0.2765 0.3237 0.0204  0.0361  -0.0921 228 HOH   B O   
7088 O O   . HOH   E .   ? 0.2452 0.1851 0.2776 -0.0288 0.0796  -0.0025 229 HOH   B O   
7089 O O   . HOH   E .   ? 0.2194 0.1492 0.3487 0.0132  -0.0550 -0.0082 230 HOH   B O   
7090 O O   . HOH   E .   ? 0.5579 0.3377 0.3984 -0.2418 0.0195  0.0218  231 HOH   B O   
7091 O O   . HOH   E .   ? 0.4268 0.3781 0.6179 -0.0030 -0.1638 -0.0848 232 HOH   B O   
7092 O O   . HOH   E .   ? 0.4811 0.4432 0.4138 0.0184  0.1014  -0.1491 233 HOH   B O   
7093 O O   . HOH   E .   ? 0.2660 0.2343 0.2824 0.0890  -0.0923 -0.0675 234 HOH   B O   
7094 O O   . HOH   E .   ? 0.3847 0.2446 0.4408 0.0344  -0.1106 -0.1166 235 HOH   B O   
7095 O O   . HOH   E .   ? 0.2864 0.3106 0.3642 -0.0975 0.0598  -0.0633 236 HOH   B O   
7096 O O   . HOH   E .   ? 0.3720 0.2116 0.2114 0.0218  -0.0774 -0.0106 237 HOH   B O   
7097 O O   . HOH   E .   ? 0.4948 0.3101 0.3732 -0.1427 -0.0248 0.0014  238 HOH   B O   
7098 O O   . HOH   E .   ? 0.2945 0.3721 0.3536 -0.0858 0.0429  -0.0682 239 HOH   B O   
7099 O O   . HOH   E .   ? 0.3231 0.1929 0.6804 -0.0079 -0.1247 -0.0312 240 HOH   B O   
7100 O O   . HOH   E .   ? 0.4080 0.2615 0.4177 0.0810  -0.0541 -0.0658 241 HOH   B O   
7101 O O   . HOH   E .   ? 0.3699 0.3103 0.2428 0.0275  0.0563  0.0409  242 HOH   B O   
7102 O O   . HOH   E .   ? 0.1639 0.1588 0.1690 -0.0114 -0.0056 -0.0033 243 HOH   B O   
7103 O O   . HOH   E .   ? 0.1571 0.1450 0.1897 -0.0023 -0.0132 0.0074  244 HOH   B O   
7104 O O   . HOH   E .   ? 0.4494 0.7220 0.2959 -0.1447 -0.1117 0.0251  245 HOH   B O   
7105 O O   . HOH   E .   ? 0.3729 0.4082 0.2618 0.0168  0.1004  0.0090  246 HOH   B O   
7106 O O   . HOH   E .   ? 0.2287 0.2084 0.2304 -0.0310 -0.0458 0.0241  247 HOH   B O   
7107 O O   . HOH   E .   ? 0.4206 0.4114 0.5877 -0.1686 -0.0313 0.1308  248 HOH   B O   
7108 O O   . HOH   E .   ? 0.1656 0.1622 0.2917 -0.0050 0.0038  -0.0094 249 HOH   B O   
7109 O O   . HOH   E .   ? 0.4538 0.4768 0.3211 0.0418  -0.0075 -0.0738 250 HOH   B O   
7110 O O   . HOH   E .   ? 0.2115 0.4036 0.2514 -0.0351 -0.0078 0.0385  251 HOH   B O   
7111 O O   . HOH   E .   ? 0.3137 0.5022 0.3203 -0.1334 -0.0373 -0.0776 252 HOH   B O   
7112 O O   . HOH   E .   ? 0.2810 0.2309 0.2996 0.0627  0.0658  -0.0066 253 HOH   B O   
7113 O O   . HOH   E .   ? 0.2916 0.5944 0.5782 0.1704  -0.0916 -0.0884 254 HOH   B O   
7114 O O   . HOH   E .   ? 0.3071 0.2306 0.2300 0.0289  -0.0259 -0.0071 255 HOH   B O   
7115 O O   . HOH   E .   ? 0.3538 0.3702 0.4808 0.1254  -0.0398 -0.0862 256 HOH   B O   
7116 O O   . HOH   E .   ? 0.1731 0.1837 0.3453 -0.0233 -0.0132 0.0070  257 HOH   B O   
7117 O O   . HOH   E .   ? 0.2316 0.3862 0.3300 -0.0498 -0.0772 -0.0445 258 HOH   B O   
7118 O O   . HOH   E .   ? 0.2252 0.1618 0.2357 -0.0332 -0.0443 0.0229  259 HOH   B O   
7119 O O   . HOH   E .   ? 0.3565 0.2890 0.3262 -0.0437 0.0211  -0.0601 260 HOH   B O   
7120 O O   . HOH   E .   ? 0.2243 0.2103 0.4571 -0.0012 -0.0579 -0.0524 261 HOH   B O   
7121 O O   . HOH   E .   ? 0.2547 0.3284 0.2252 -0.0600 0.0260  0.0440  262 HOH   B O   
7122 O O   . HOH   E .   ? 0.2298 0.5127 0.5185 -0.0531 -0.0173 -0.1472 263 HOH   B O   
7123 O O   . HOH   E .   ? 0.2030 0.2754 0.2891 0.0324  0.0452  0.0913  264 HOH   B O   
7124 O O   . HOH   E .   ? 0.4252 0.2908 0.4742 -0.0178 -0.1287 -0.0487 265 HOH   B O   
7125 O O   . HOH   E .   ? 0.1512 0.1757 0.2476 -0.0094 0.0055  0.0163  266 HOH   B O   
7126 O O   . HOH   E .   ? 0.3459 0.5002 0.3405 -0.0208 -0.0971 0.0882  267 HOH   B O   
7127 O O   . HOH   E .   ? 0.3103 0.4905 0.6209 -0.0534 -0.0507 -0.1353 268 HOH   B O   
7128 O O   . HOH   E .   ? 0.3000 0.3861 0.4477 0.0345  0.1584  0.0354  269 HOH   B O   
7129 O O   . HOH   E .   ? 0.2487 0.2349 0.2374 0.0000  0.0030  -0.0002 270 HOH   B O   
7130 O O   . HOH   E .   ? 0.2299 0.1675 0.2521 -0.0305 -0.0170 0.0162  271 HOH   B O   
7131 O O   . HOH   E .   ? 0.5840 0.3930 0.4413 0.0177  0.0703  0.0353  272 HOH   B O   
7132 O O   . HOH   E .   ? 0.2685 0.2092 0.3140 -0.0561 0.0215  -0.0027 273 HOH   B O   
7133 O O   . HOH   E .   ? 0.2014 0.1974 0.1854 -0.0533 -0.0499 0.0170  274 HOH   B O   
7134 O O   . HOH   E .   ? 0.3136 0.2242 0.4644 0.0215  0.0402  0.0516  275 HOH   B O   
7135 O O   . HOH   E .   ? 0.2637 0.2883 0.2649 -0.0466 -0.0760 0.0258  276 HOH   B O   
7136 O O   . HOH   E .   ? 0.2933 0.4907 0.2329 0.1705  -0.0375 -0.0397 277 HOH   B O   
7137 O O   . HOH   E .   ? 0.4436 0.4380 0.6875 0.0380  0.0826  -0.0396 278 HOH   B O   
7138 O O   . HOH   E .   ? 0.3390 0.7789 0.7407 0.0362  -0.0848 -0.0949 279 HOH   B O   
7139 O O   . HOH   E .   ? 0.2451 0.2816 0.2466 -0.0357 -0.0580 -0.0404 280 HOH   B O   
7140 O O   . HOH   E .   ? 0.4760 0.4889 0.5191 -0.0029 -0.1578 0.0134  281 HOH   B O   
7141 O O   . HOH   E .   ? 0.2372 0.2347 0.5418 -0.0495 0.0092  0.1401  282 HOH   B O   
7142 O O   . HOH   E .   ? 0.1939 0.1496 0.4428 -0.0087 -0.0302 -0.0036 283 HOH   B O   
7143 O O   . HOH   E .   ? 0.1805 0.1618 0.2184 -0.0004 0.0074  -0.0001 284 HOH   B O   
7144 O O   . HOH   E .   ? 0.4477 0.3942 0.4525 -0.1040 0.0827  -0.1118 285 HOH   B O   
7145 O O   . HOH   E .   ? 0.2469 0.3557 0.3635 -0.0588 0.0403  -0.1247 286 HOH   B O   
7146 O O   . HOH   E .   ? 0.1770 0.1685 0.3708 -0.0195 -0.0009 -0.0011 287 HOH   B O   
7147 O O   . HOH   E .   ? 0.3007 0.4841 0.4974 -0.0981 -0.1166 0.0877  288 HOH   B O   
7148 O O   . HOH   E .   ? 0.3610 0.3267 0.3041 -0.0551 0.0328  -0.1305 289 HOH   B O   
7149 O O   . HOH   E .   ? 0.1790 0.2166 0.1813 -0.0137 -0.0193 0.0137  290 HOH   B O   
7150 O O   . HOH   E .   ? 0.1822 0.2207 0.3353 0.0142  -0.0050 -0.0088 291 HOH   B O   
7151 O O   . HOH   E .   ? 0.4402 0.3780 0.2582 0.0928  -0.0832 0.0521  292 HOH   B O   
7152 O O   . HOH   E .   ? 0.2769 0.2844 0.3069 0.0056  -0.0956 0.0259  293 HOH   B O   
7153 O O   . HOH   E .   ? 0.2633 0.6935 0.2719 0.1073  -0.0421 -0.0654 294 HOH   B O   
7154 O O   . HOH   E .   ? 0.1961 0.3887 0.4859 0.0477  -0.0296 -0.1468 295 HOH   B O   
7155 O O   . HOH   E .   ? 0.4451 0.5487 0.2797 0.0286  0.1023  0.1234  296 HOH   B O   
7156 O O   . HOH   E .   ? 0.3802 0.2221 0.4178 -0.0852 -0.1748 0.0744  297 HOH   B O   
7157 O O   . HOH   E .   ? 0.3768 0.2600 0.2407 0.0133  -0.0828 0.0017  298 HOH   B O   
7158 O O   . HOH   E .   ? 0.2070 0.1734 0.2688 0.0104  -0.0087 0.0162  299 HOH   B O   
7159 O O   . HOH   E .   ? 0.5011 0.3099 0.2595 -0.1962 0.0845  -0.0376 300 HOH   B O   
7160 O O   . HOH   E .   ? 0.3884 0.5105 0.3885 -0.2155 0.1123  -0.0362 301 HOH   B O   
7161 O O   . HOH   E .   ? 0.2268 0.3759 0.6365 0.0881  -0.0641 -0.1604 302 HOH   B O   
7162 O O   . HOH   E .   ? 0.6127 0.3717 0.3561 0.2561  0.1460  0.0852  303 HOH   B O   
7163 O O   . HOH   E .   ? 0.7170 0.4758 0.5448 0.1647  0.1866  0.0304  304 HOH   B O   
7164 O O   . HOH   E .   ? 0.2141 0.1727 0.3537 0.0333  -0.0872 0.0051  305 HOH   B O   
7165 O O   . HOH   E .   ? 0.5351 0.4475 0.4905 0.1904  0.0144  0.0810  306 HOH   B O   
7166 O O   . HOH   E .   ? 0.2369 0.5423 0.5879 -0.0893 -0.0021 0.0501  307 HOH   B O   
7167 O O   . HOH   E .   ? 0.2314 0.3204 0.5260 -0.0151 -0.0857 -0.0219 308 HOH   B O   
7168 O O   . HOH   E .   ? 0.2257 0.1865 0.2935 -0.0298 -0.0203 -0.0059 309 HOH   B O   
7169 O O   . HOH   E .   ? 0.1746 0.1598 0.3692 0.0061  -0.0015 -0.0007 310 HOH   B O   
7170 O O   . HOH   E .   ? 0.3615 0.2036 0.3809 0.0665  0.1172  0.0250  311 HOH   B O   
7171 O O   . HOH   E .   ? 0.4017 0.2849 0.5104 -0.0280 -0.0568 0.1062  312 HOH   B O   
7172 O O   . HOH   E .   ? 0.5412 0.3951 0.2977 -0.0220 -0.0353 -0.0414 313 HOH   B O   
7173 O O   . HOH   E .   ? 0.2374 0.2027 0.2091 -0.0108 0.0137  0.0161  314 HOH   B O   
7174 O O   . HOH   E .   ? 0.1785 0.2884 0.2731 -0.0151 -0.0185 0.0820  315 HOH   B O   
7175 O O   . HOH   E .   ? 0.1749 0.2037 0.3326 -0.0318 -0.0049 0.0138  316 HOH   B O   
7176 O O   . HOH   E .   ? 0.3117 0.3155 0.3885 -0.0342 0.1180  -0.0914 317 HOH   B O   
7177 O O   . HOH   E .   ? 0.4816 0.2733 0.3781 0.0577  0.0044  0.0583  318 HOH   B O   
7178 O O   . HOH   E .   ? 0.2784 0.1612 0.2729 -0.0238 -0.0320 0.0272  319 HOH   B O   
7179 O O   . HOH   E .   ? 0.3820 0.2160 0.2861 0.1141  0.0857  0.0212  320 HOH   B O   
7180 O O   . HOH   E .   ? 0.1786 0.1754 0.3316 -0.0170 -0.0191 -0.0124 321 HOH   B O   
7181 O O   . HOH   E .   ? 0.3445 0.2398 0.2533 0.0278  -0.0339 0.0231  322 HOH   B O   
7182 O O   . HOH   E .   ? 0.4974 0.3778 0.4532 -0.1014 0.0121  0.0970  323 HOH   B O   
7183 O O   . HOH   E .   ? 0.3925 0.6836 0.3739 0.0941  -0.0597 0.0615  324 HOH   B O   
7184 O O   . HOH   E .   ? 0.5078 0.4107 0.4603 -0.0405 0.1301  -0.1487 325 HOH   B O   
7185 O O   . HOH   E .   ? 0.2791 0.2086 0.4814 0.0138  -0.0093 0.0448  326 HOH   B O   
7186 O O   . HOH   E .   ? 0.6464 0.5325 0.7022 0.1508  -0.0613 0.2533  327 HOH   B O   
7187 O O   . HOH   E .   ? 0.4317 0.4740 0.8496 -0.0164 -0.1168 0.2649  328 HOH   B O   
7188 O O   . HOH   E .   ? 0.1992 0.2055 0.3036 0.0280  0.0394  0.0241  329 HOH   B O   
7189 O O   . HOH   E .   ? 0.4880 0.4602 0.5746 0.0595  -0.0494 0.0205  330 HOH   B O   
7190 O O   . HOH   E .   ? 0.2154 0.3177 0.3491 0.0689  -0.0222 -0.0811 331 HOH   B O   
7191 O O   . HOH   E .   ? 0.5921 0.4000 0.4199 0.0907  0.1691  0.1794  332 HOH   B O   
7192 O O   . HOH   E .   ? 0.2984 0.3551 0.5551 -0.0745 -0.1802 0.1786  333 HOH   B O   
7193 O O   . HOH   E .   ? 0.4974 0.3345 0.5761 0.1452  0.2525  0.1966  334 HOH   B O   
7194 O O   . HOH   E .   ? 0.8844 0.2443 0.3703 0.0731  -0.1228 0.0018  335 HOH   B O   
7195 O O   . HOH   E .   ? 0.7503 0.7147 0.3753 0.0264  -0.0516 0.1464  336 HOH   B O   
7196 O O   . HOH   E .   ? 0.2774 0.1938 0.3889 0.0223  -0.0814 -0.0291 337 HOH   B O   
7197 O O   . HOH   E .   ? 0.5263 0.4460 0.2491 0.1776  -0.1300 -0.0595 338 HOH   B O   
7198 O O   . HOH   E .   ? 0.1870 0.1619 0.2621 -0.0004 -0.0253 0.0153  339 HOH   B O   
7199 O O   . HOH   E .   ? 0.4575 0.7405 0.3958 -0.0658 -0.0964 0.1957  340 HOH   B O   
7200 O O   . HOH   E .   ? 0.5658 0.4636 0.6266 -0.0776 -0.0801 -0.1331 341 HOH   B O   
7201 O O   . HOH   E .   ? 0.4946 0.6210 0.7280 -0.0313 0.0034  -0.0163 342 HOH   B O   
7202 O O   . HOH   E .   ? 0.5058 0.3607 0.3441 0.0279  -0.1319 -0.0696 343 HOH   B O   
7203 O O   . HOH   E .   ? 0.5876 0.5947 0.5648 -0.0962 -0.0477 0.1714  344 HOH   B O   
7204 O O   . HOH   E .   ? 0.4018 0.5379 0.4321 -0.1143 -0.0770 -0.0506 345 HOH   B O   
7205 O O   . HOH   E .   ? 0.5524 0.5589 0.3651 0.0098  -0.1234 0.0448  346 HOH   B O   
7206 O O   . HOH   E .   ? 0.2305 0.2084 0.4127 -0.0147 0.0911  -0.0177 347 HOH   B O   
7207 O O   . HOH   E .   ? 0.4489 0.6642 0.6116 0.0503  -0.1153 0.0239  348 HOH   B O   
7208 O O   . HOH   E .   ? 0.3572 0.2247 0.4596 -0.0476 -0.0801 -0.0362 349 HOH   B O   
7209 O O   . HOH   E .   ? 0.5120 0.6242 0.5918 -0.1268 0.0026  0.1230  350 HOH   B O   
7210 O O   . HOH   E .   ? 0.3970 0.4436 0.5740 -0.1597 -0.0195 0.0049  351 HOH   B O   
7211 O O   . HOH   E .   ? 0.4223 0.6537 0.6812 0.0726  0.0581  0.0019  352 HOH   B O   
7212 O O   . HOH   E .   ? 0.2404 0.6378 0.3121 0.1550  -0.0559 -0.1455 353 HOH   B O   
7213 O O   . HOH   E .   ? 0.2509 0.4839 0.5098 0.0056  0.0061  0.0115  354 HOH   B O   
7214 O O   . HOH   E .   ? 0.4144 0.2333 0.3228 -0.0788 0.0194  -0.0707 355 HOH   B O   
7215 O O   . HOH   E .   ? 0.5257 0.5545 0.4513 0.2175  -0.0996 0.1089  356 HOH   B O   
7216 O O   . HOH   E .   ? 0.3902 0.2732 0.4103 -0.0816 -0.0304 -0.0497 357 HOH   B O   
7217 O O   . HOH   E .   ? 0.4800 0.3135 0.5857 -0.0873 0.1343  0.0746  358 HOH   B O   
7218 O O   . HOH   E .   ? 0.5304 0.3835 0.4548 0.0332  0.1498  -0.0696 359 HOH   B O   
7219 O O   . HOH   E .   ? 0.5619 0.3590 0.5130 -0.0194 -0.1434 -0.0526 360 HOH   B O   
7220 O O   . HOH   E .   ? 0.5155 0.4351 0.5896 0.0515  0.1071  0.1370  361 HOH   B O   
7221 O O   . HOH   E .   ? 0.4503 0.7050 0.3076 0.2115  -0.0210 0.0443  362 HOH   B O   
7222 O O   . HOH   E .   ? 0.2369 0.3975 0.7258 -0.0905 -0.0493 -0.0724 363 HOH   B O   
7223 O O   . HOH   E .   ? 0.6450 0.2503 0.4180 -0.0256 0.0038  0.0903  364 HOH   B O   
7224 O O   . HOH   E .   ? 0.4953 0.4125 0.5063 0.0067  0.0206  -0.0164 365 HOH   B O   
7225 O O   . HOH   E .   ? 0.5340 0.5750 0.4966 -0.0655 -0.0366 -0.1159 366 HOH   B O   
7226 O O   . HOH   E .   ? 0.4667 0.3326 0.5198 0.0165  -0.1676 0.0373  367 HOH   B O   
7227 O O   . HOH   E .   ? 0.5802 0.3154 0.5761 -0.1414 -0.0462 0.0381  368 HOH   B O   
7228 O O   . HOH   E .   ? 0.6689 0.4398 0.4453 0.1058  0.0586  0.0447  369 HOH   B O   
7229 O O   . HOH   E .   ? 0.5661 0.5643 0.3401 0.1470  -0.1321 0.0768  370 HOH   B O   
7230 O O   . HOH   E .   ? 0.3928 0.5064 0.5210 0.2079  0.0882  0.1389  371 HOH   B O   
7231 O O   . HOH   E .   ? 0.4133 0.3104 0.3531 0.0705  -0.0963 -0.0366 372 HOH   B O   
7232 O O   . HOH   E .   ? 0.7345 0.3825 0.3089 -0.0476 -0.1228 -0.0663 373 HOH   B O   
7233 O O   . HOH   E .   ? 0.8274 0.7751 0.5863 0.2644  -0.1169 0.0671  374 HOH   B O   
7234 O O   . HOH   E .   ? 0.4524 0.4897 0.4626 -0.0492 -0.0450 -0.0009 375 HOH   B O   
7235 O O   . HOH   E .   ? 0.4681 0.5413 0.2227 -0.0434 0.0499  0.0206  376 HOH   B O   
7236 O O   . HOH   E .   ? 0.3474 0.5386 0.5330 0.1125  -0.0241 0.0031  377 HOH   B O   
7237 O O   . HOH   E .   ? 0.4857 0.7727 0.4069 -0.1394 -0.0249 -0.1490 378 HOH   B O   
7238 O O   . HOH   E .   ? 0.2315 0.3749 0.4774 0.0204  -0.0631 -0.0593 379 HOH   B O   
7239 O O   . HOH   E .   ? 0.4832 0.7024 0.6160 0.1432  0.0337  0.2681  380 HOH   B O   
7240 O O   . HOH   E .   ? 0.7305 0.3781 0.5013 -0.1053 -0.0209 -0.0092 381 HOH   B O   
7241 O O   . HOH   E .   ? 0.5753 0.7088 0.6801 0.0099  0.1916  0.1334  382 HOH   B O   
7242 O O   . HOH   E .   ? 0.2930 0.2783 0.3351 0.0110  0.0156  0.0174  383 HOH   B O   
7243 O O   . HOH   E .   ? 0.6842 0.4210 0.4367 0.0561  0.1638  -0.0299 384 HOH   B O   
7244 O O   . HOH   E .   ? 0.4792 0.8668 0.5600 0.1211  0.1308  0.0653  385 HOH   B O   
7245 O O   . HOH   E .   ? 0.8174 0.5928 0.4660 0.2524  0.0492  0.0534  386 HOH   B O   
7246 O O   . HOH   E .   ? 0.2729 0.4366 0.4300 -0.0750 -0.1271 -0.0374 387 HOH   B O   
7247 O O   . HOH   E .   ? 0.6522 0.4271 0.5424 -0.0951 0.0744  -0.0293 388 HOH   B O   
7248 O O   . HOH   E .   ? 0.5389 0.4208 0.3443 -0.0492 0.1044  -0.0135 389 HOH   B O   
7249 O O   . HOH   E .   ? 0.4203 0.2430 0.3426 0.0767  -0.0310 0.0215  390 HOH   B O   
7250 O O   . HOH   E .   ? 0.4757 0.3504 0.4792 -0.1739 -0.0049 0.0741  391 HOH   B O   
7251 O O   . HOH   E .   ? 0.6163 0.5120 0.5565 0.1037  0.0588  0.0268  392 HOH   B O   
7252 O O   . HOH   E .   ? 0.4128 0.2456 0.5152 -0.0403 0.0020  0.0868  393 HOH   B O   
7253 O O   . HOH   E .   ? 0.2877 0.5562 0.7253 -0.1689 -0.0634 -0.0831 394 HOH   B O   
7254 O O   . HOH   E .   ? 0.3192 0.4434 0.4149 0.0110  0.0249  -0.1018 395 HOH   B O   
7255 O O   . HOH   E .   ? 0.4964 0.6761 0.4637 0.1212  0.0569  -0.1083 396 HOH   B O   
7256 O O   . HOH   E .   ? 0.4987 0.4591 0.4700 0.0996  0.1495  0.1099  397 HOH   B O   
7257 O O   . HOH   E .   ? 0.2214 0.2836 0.6495 -0.0571 -0.0872 0.0069  398 HOH   B O   
7258 O O   . HOH   E .   ? 0.5410 0.6145 0.6148 -0.0319 -0.1459 0.2803  399 HOH   B O   
7259 O O   . HOH   E .   ? 0.5263 0.4111 0.3218 -0.2029 -0.0420 0.0906  400 HOH   B O   
7260 O O   . HOH   E .   ? 0.5787 0.5536 0.3798 0.1663  -0.0540 -0.0419 401 HOH   B O   
# 
