data_7HFB
# 
_entry.id   7HFB 
# 
_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   7HFB         pdb_00007hfb 10.2210/pdb7hfb/pdb 
WWPDB D_1001407401 ?            ?                   
# 
_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                        7HFB 
_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,4r)-4-methyl-1-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}cyclohexan-1-ol' 274.361   1   ? ? 
? ?                                                                                    
3 water       nat water                                                                                         18.015    424 ? ? 
? ?                                                                                    
# 
_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,4r)-4-methyl-1-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}cyclohexan-1-ol' A1BAX 
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 
A1BAX non-polymer         . '(1r,4r)-4-methyl-1-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}cyclohexan-1-ol' ? 
'C15 H22 N4 O'   274.361 
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 A1BAX 1   201 201  A1BAX LA1 A . 
D 3 HOH   1   301 229  HOH   HOH A . 
D 3 HOH   2   302 292  HOH   HOH A . 
D 3 HOH   3   303 625  HOH   HOH A . 
D 3 HOH   4   304 1301 HOH   HOH A . 
D 3 HOH   5   305 199  HOH   HOH A . 
D 3 HOH   6   306 109  HOH   HOH A . 
D 3 HOH   7   307 196  HOH   HOH A . 
D 3 HOH   8   308 26   HOH   HOH A . 
D 3 HOH   9   309 247  HOH   HOH A . 
D 3 HOH   10  310 18   HOH   HOH A . 
D 3 HOH   11  311 105  HOH   HOH A . 
D 3 HOH   12  312 337  HOH   HOH A . 
D 3 HOH   13  313 192  HOH   HOH A . 
D 3 HOH   14  314 1295 HOH   HOH A . 
D 3 HOH   15  315 209  HOH   HOH A . 
D 3 HOH   16  316 153  HOH   HOH A . 
D 3 HOH   17  317 1290 HOH   HOH A . 
D 3 HOH   18  318 136  HOH   HOH A . 
D 3 HOH   19  319 76   HOH   HOH A . 
D 3 HOH   20  320 8    HOH   HOH A . 
D 3 HOH   21  321 17   HOH   HOH A . 
D 3 HOH   22  322 661  HOH   HOH A . 
D 3 HOH   23  323 93   HOH   HOH A . 
D 3 HOH   24  324 393  HOH   HOH A . 
D 3 HOH   25  325 49   HOH   HOH A . 
D 3 HOH   26  326 155  HOH   HOH A . 
D 3 HOH   27  327 1283 HOH   HOH A . 
D 3 HOH   28  328 139  HOH   HOH A . 
D 3 HOH   29  329 57   HOH   HOH A . 
D 3 HOH   30  330 15   HOH   HOH A . 
D 3 HOH   31  331 124  HOH   HOH A . 
D 3 HOH   32  332 1    HOH   HOH A . 
D 3 HOH   33  333 225  HOH   HOH A . 
D 3 HOH   34  334 102  HOH   HOH A . 
D 3 HOH   35  335 964  HOH   HOH A . 
D 3 HOH   36  336 33   HOH   HOH A . 
D 3 HOH   37  337 354  HOH   HOH A . 
D 3 HOH   38  338 164  HOH   HOH A . 
D 3 HOH   39  339 140  HOH   HOH A . 
D 3 HOH   40  340 469  HOH   HOH A . 
D 3 HOH   41  341 39   HOH   HOH A . 
D 3 HOH   42  342 461  HOH   HOH A . 
D 3 HOH   43  343 92   HOH   HOH A . 
D 3 HOH   44  344 409  HOH   HOH A . 
D 3 HOH   45  345 1310 HOH   HOH A . 
D 3 HOH   46  346 151  HOH   HOH A . 
D 3 HOH   47  347 366  HOH   HOH A . 
D 3 HOH   48  348 66   HOH   HOH A . 
D 3 HOH   49  349 320  HOH   HOH A . 
D 3 HOH   50  350 1309 HOH   HOH A . 
D 3 HOH   51  351 162  HOH   HOH A . 
D 3 HOH   52  352 27   HOH   HOH A . 
D 3 HOH   53  353 165  HOH   HOH A . 
D 3 HOH   54  354 21   HOH   HOH A . 
D 3 HOH   55  355 56   HOH   HOH A . 
D 3 HOH   56  356 2    HOH   HOH A . 
D 3 HOH   57  357 19   HOH   HOH A . 
D 3 HOH   58  358 42   HOH   HOH A . 
D 3 HOH   59  359 396  HOH   HOH A . 
D 3 HOH   60  360 381  HOH   HOH A . 
D 3 HOH   61  361 939  HOH   HOH A . 
D 3 HOH   62  362 46   HOH   HOH A . 
D 3 HOH   63  363 86   HOH   HOH A . 
D 3 HOH   64  364 34   HOH   HOH A . 
D 3 HOH   65  365 81   HOH   HOH A . 
D 3 HOH   66  366 4    HOH   HOH A . 
D 3 HOH   67  367 116  HOH   HOH A . 
D 3 HOH   68  368 169  HOH   HOH A . 
D 3 HOH   69  369 74   HOH   HOH A . 
D 3 HOH   70  370 241  HOH   HOH A . 
D 3 HOH   71  371 5    HOH   HOH A . 
D 3 HOH   72  372 236  HOH   HOH A . 
D 3 HOH   73  373 2    HOH   HOH A . 
D 3 HOH   74  374 630  HOH   HOH A . 
D 3 HOH   75  375 1300 HOH   HOH A . 
D 3 HOH   76  376 159  HOH   HOH A . 
D 3 HOH   77  377 62   HOH   HOH A . 
D 3 HOH   78  378 1308 HOH   HOH A . 
D 3 HOH   79  379 45   HOH   HOH A . 
D 3 HOH   80  380 85   HOH   HOH A . 
D 3 HOH   81  381 662  HOH   HOH A . 
D 3 HOH   82  382 186  HOH   HOH A . 
D 3 HOH   83  383 6    HOH   HOH A . 
D 3 HOH   84  384 218  HOH   HOH A . 
D 3 HOH   85  385 12   HOH   HOH A . 
D 3 HOH   86  386 138  HOH   HOH A . 
D 3 HOH   87  387 134  HOH   HOH A . 
D 3 HOH   88  388 35   HOH   HOH A . 
D 3 HOH   89  389 281  HOH   HOH A . 
D 3 HOH   90  390 132  HOH   HOH A . 
D 3 HOH   91  391 148  HOH   HOH A . 
D 3 HOH   92  392 36   HOH   HOH A . 
D 3 HOH   93  393 58   HOH   HOH A . 
D 3 HOH   94  394 83   HOH   HOH A . 
D 3 HOH   95  395 68   HOH   HOH A . 
D 3 HOH   96  396 67   HOH   HOH A . 
D 3 HOH   97  397 1315 HOH   HOH A . 
D 3 HOH   98  398 3    HOH   HOH A . 
D 3 HOH   99  399 9    HOH   HOH A . 
D 3 HOH   100 400 1134 HOH   HOH A . 
D 3 HOH   101 401 3    HOH   HOH A . 
D 3 HOH   102 402 351  HOH   HOH A . 
D 3 HOH   103 403 121  HOH   HOH A . 
D 3 HOH   104 404 405  HOH   HOH A . 
D 3 HOH   105 405 122  HOH   HOH A . 
D 3 HOH   106 406 25   HOH   HOH A . 
D 3 HOH   107 407 1222 HOH   HOH A . 
D 3 HOH   108 408 125  HOH   HOH A . 
D 3 HOH   109 409 303  HOH   HOH A . 
D 3 HOH   110 410 24   HOH   HOH A . 
D 3 HOH   111 411 195  HOH   HOH A . 
D 3 HOH   112 412 278  HOH   HOH A . 
D 3 HOH   113 413 1289 HOH   HOH A . 
D 3 HOH   114 414 1068 HOH   HOH A . 
D 3 HOH   115 415 96   HOH   HOH A . 
D 3 HOH   116 416 1279 HOH   HOH A . 
D 3 HOH   117 417 123  HOH   HOH A . 
D 3 HOH   118 418 78   HOH   HOH A . 
D 3 HOH   119 419 154  HOH   HOH A . 
D 3 HOH   120 420 333  HOH   HOH A . 
D 3 HOH   121 421 156  HOH   HOH A . 
D 3 HOH   122 422 115  HOH   HOH A . 
D 3 HOH   123 423 8    HOH   HOH A . 
D 3 HOH   124 424 53   HOH   HOH A . 
D 3 HOH   125 425 95   HOH   HOH A . 
D 3 HOH   126 426 493  HOH   HOH A . 
D 3 HOH   127 427 7    HOH   HOH A . 
D 3 HOH   128 428 51   HOH   HOH A . 
D 3 HOH   129 429 397  HOH   HOH A . 
D 3 HOH   130 430 188  HOH   HOH A . 
D 3 HOH   131 431 1286 HOH   HOH A . 
D 3 HOH   132 432 16   HOH   HOH A . 
D 3 HOH   133 433 1275 HOH   HOH A . 
D 3 HOH   134 434 1238 HOH   HOH A . 
D 3 HOH   135 435 1296 HOH   HOH A . 
D 3 HOH   136 436 212  HOH   HOH A . 
D 3 HOH   137 437 80   HOH   HOH A . 
D 3 HOH   138 438 40   HOH   HOH A . 
D 3 HOH   139 439 70   HOH   HOH A . 
D 3 HOH   140 440 1313 HOH   HOH A . 
D 3 HOH   141 441 71   HOH   HOH A . 
D 3 HOH   142 442 582  HOH   HOH A . 
D 3 HOH   143 443 5    HOH   HOH A . 
D 3 HOH   144 444 296  HOH   HOH A . 
D 3 HOH   145 445 104  HOH   HOH A . 
D 3 HOH   146 446 952  HOH   HOH A . 
D 3 HOH   147 447 12   HOH   HOH A . 
D 3 HOH   148 448 4    HOH   HOH A . 
D 3 HOH   149 449 97   HOH   HOH A . 
D 3 HOH   150 450 94   HOH   HOH A . 
D 3 HOH   151 451 576  HOH   HOH A . 
D 3 HOH   152 452 73   HOH   HOH A . 
D 3 HOH   153 453 1189 HOH   HOH A . 
D 3 HOH   154 454 944  HOH   HOH A . 
D 3 HOH   155 455 79   HOH   HOH A . 
D 3 HOH   156 456 1094 HOH   HOH A . 
D 3 HOH   157 457 16   HOH   HOH A . 
D 3 HOH   158 458 330  HOH   HOH A . 
D 3 HOH   159 459 107  HOH   HOH A . 
D 3 HOH   160 460 1119 HOH   HOH A . 
D 3 HOH   161 461 509  HOH   HOH A . 
D 3 HOH   162 462 726  HOH   HOH A . 
D 3 HOH   163 463 163  HOH   HOH A . 
D 3 HOH   164 464 408  HOH   HOH A . 
D 3 HOH   165 465 756  HOH   HOH A . 
D 3 HOH   166 466 319  HOH   HOH A . 
D 3 HOH   167 467 126  HOH   HOH A . 
D 3 HOH   168 468 6    HOH   HOH A . 
D 3 HOH   169 469 342  HOH   HOH A . 
D 3 HOH   170 470 1307 HOH   HOH A . 
D 3 HOH   171 471 14   HOH   HOH A . 
D 3 HOH   172 472 801  HOH   HOH A . 
D 3 HOH   173 473 556  HOH   HOH A . 
D 3 HOH   174 474 280  HOH   HOH A . 
D 3 HOH   175 475 250  HOH   HOH A . 
D 3 HOH   176 476 361  HOH   HOH A . 
D 3 HOH   177 477 135  HOH   HOH A . 
D 3 HOH   178 478 224  HOH   HOH A . 
D 3 HOH   179 479 63   HOH   HOH A . 
D 3 HOH   180 480 267  HOH   HOH A . 
D 3 HOH   181 481 521  HOH   HOH A . 
D 3 HOH   182 482 370  HOH   HOH A . 
D 3 HOH   183 483 1276 HOH   HOH A . 
D 3 HOH   184 484 1287 HOH   HOH A . 
D 3 HOH   185 485 202  HOH   HOH A . 
D 3 HOH   186 486 695  HOH   HOH A . 
D 3 HOH   187 487 1314 HOH   HOH A . 
D 3 HOH   188 488 674  HOH   HOH A . 
D 3 HOH   189 489 919  HOH   HOH A . 
D 3 HOH   190 490 1306 HOH   HOH A . 
D 3 HOH   191 491 1299 HOH   HOH A . 
D 3 HOH   192 492 331  HOH   HOH A . 
D 3 HOH   193 493 941  HOH   HOH A . 
D 3 HOH   194 494 309  HOH   HOH A . 
D 3 HOH   195 495 318  HOH   HOH A . 
D 3 HOH   196 496 981  HOH   HOH A . 
D 3 HOH   197 497 152  HOH   HOH A . 
D 3 HOH   198 498 326  HOH   HOH A . 
D 3 HOH   199 499 208  HOH   HOH A . 
D 3 HOH   200 500 805  HOH   HOH A . 
D 3 HOH   201 501 315  HOH   HOH A . 
D 3 HOH   202 502 263  HOH   HOH A . 
D 3 HOH   203 503 7    HOH   HOH A . 
D 3 HOH   204 504 711  HOH   HOH A . 
D 3 HOH   205 505 1284 HOH   HOH A . 
D 3 HOH   206 506 180  HOH   HOH A . 
D 3 HOH   207 507 1071 HOH   HOH A . 
D 3 HOH   208 508 356  HOH   HOH A . 
D 3 HOH   209 509 363  HOH   HOH A . 
D 3 HOH   210 510 313  HOH   HOH A . 
D 3 HOH   211 511 350  HOH   HOH A . 
D 3 HOH   212 512 10   HOH   HOH A . 
D 3 HOH   213 513 371  HOH   HOH A . 
D 3 HOH   214 514 772  HOH   HOH A . 
D 3 HOH   215 515 185  HOH   HOH A . 
D 3 HOH   216 516 429  HOH   HOH A . 
D 3 HOH   217 517 11   HOH   HOH A . 
D 3 HOH   218 518 17   HOH   HOH A . 
D 3 HOH   219 519 376  HOH   HOH A . 
D 3 HOH   220 520 1074 HOH   HOH A . 
D 3 HOH   221 521 13   HOH   HOH A . 
D 3 HOH   222 522 1292 HOH   HOH A . 
D 3 HOH   223 523 346  HOH   HOH A . 
D 3 HOH   224 524 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 531  HOH   HOH B . 
E 3 HOH   3   203 900  HOH   HOH B . 
E 3 HOH   4   204 758  HOH   HOH B . 
E 3 HOH   5   205 654  HOH   HOH B . 
E 3 HOH   6   206 549  HOH   HOH B . 
E 3 HOH   7   207 120  HOH   HOH B . 
E 3 HOH   8   208 364  HOH   HOH B . 
E 3 HOH   9   209 353  HOH   HOH B . 
E 3 HOH   10  210 358  HOH   HOH B . 
E 3 HOH   11  211 82   HOH   HOH B . 
E 3 HOH   12  212 743  HOH   HOH B . 
E 3 HOH   13  213 343  HOH   HOH B . 
E 3 HOH   14  214 1249 HOH   HOH B . 
E 3 HOH   15  215 264  HOH   HOH B . 
E 3 HOH   16  216 1278 HOH   HOH B . 
E 3 HOH   17  217 50   HOH   HOH B . 
E 3 HOH   18  218 398  HOH   HOH B . 
E 3 HOH   19  219 723  HOH   HOH B . 
E 3 HOH   20  220 131  HOH   HOH B . 
E 3 HOH   21  221 69   HOH   HOH B . 
E 3 HOH   22  222 452  HOH   HOH B . 
E 3 HOH   23  223 15   HOH   HOH B . 
E 3 HOH   24  224 221  HOH   HOH B . 
E 3 HOH   25  225 282  HOH   HOH B . 
E 3 HOH   26  226 444  HOH   HOH B . 
E 3 HOH   27  227 75   HOH   HOH B . 
E 3 HOH   28  228 240  HOH   HOH B . 
E 3 HOH   29  229 110  HOH   HOH B . 
E 3 HOH   30  230 181  HOH   HOH B . 
E 3 HOH   31  231 347  HOH   HOH B . 
E 3 HOH   32  232 1    HOH   HOH B . 
E 3 HOH   33  233 133  HOH   HOH B . 
E 3 HOH   34  234 144  HOH   HOH B . 
E 3 HOH   35  235 332  HOH   HOH B . 
E 3 HOH   36  236 205  HOH   HOH B . 
E 3 HOH   37  237 232  HOH   HOH B . 
E 3 HOH   38  238 1140 HOH   HOH B . 
E 3 HOH   39  239 272  HOH   HOH B . 
E 3 HOH   40  240 60   HOH   HOH B . 
E 3 HOH   41  241 172  HOH   HOH B . 
E 3 HOH   42  242 47   HOH   HOH B . 
E 3 HOH   43  243 52   HOH   HOH B . 
E 3 HOH   44  244 14   HOH   HOH B . 
E 3 HOH   45  245 54   HOH   HOH B . 
E 3 HOH   46  246 129  HOH   HOH B . 
E 3 HOH   47  247 127  HOH   HOH B . 
E 3 HOH   48  248 72   HOH   HOH B . 
E 3 HOH   49  249 30   HOH   HOH B . 
E 3 HOH   50  250 31   HOH   HOH B . 
E 3 HOH   51  251 391  HOH   HOH B . 
E 3 HOH   52  252 220  HOH   HOH B . 
E 3 HOH   53  253 9    HOH   HOH B . 
E 3 HOH   54  254 252  HOH   HOH B . 
E 3 HOH   55  255 143  HOH   HOH B . 
E 3 HOH   56  256 10   HOH   HOH B . 
E 3 HOH   57  257 325  HOH   HOH B . 
E 3 HOH   58  258 128  HOH   HOH B . 
E 3 HOH   59  259 166  HOH   HOH B . 
E 3 HOH   60  260 231  HOH   HOH B . 
E 3 HOH   61  261 41   HOH   HOH B . 
E 3 HOH   62  262 150  HOH   HOH B . 
E 3 HOH   63  263 59   HOH   HOH B . 
E 3 HOH   64  264 103  HOH   HOH B . 
E 3 HOH   65  265 11   HOH   HOH B . 
E 3 HOH   66  266 1277 HOH   HOH B . 
E 3 HOH   67  267 300  HOH   HOH B . 
E 3 HOH   68  268 216  HOH   HOH B . 
E 3 HOH   69  269 114  HOH   HOH B . 
E 3 HOH   70  270 77   HOH   HOH B . 
E 3 HOH   71  271 302  HOH   HOH B . 
E 3 HOH   72  272 242  HOH   HOH B . 
E 3 HOH   73  273 1312 HOH   HOH B . 
E 3 HOH   74  274 89   HOH   HOH B . 
E 3 HOH   75  275 182  HOH   HOH B . 
E 3 HOH   76  276 61   HOH   HOH B . 
E 3 HOH   77  277 175  HOH   HOH B . 
E 3 HOH   78  278 88   HOH   HOH B . 
E 3 HOH   79  279 117  HOH   HOH B . 
E 3 HOH   80  280 341  HOH   HOH B . 
E 3 HOH   81  281 1285 HOH   HOH B . 
E 3 HOH   82  282 299  HOH   HOH B . 
E 3 HOH   83  283 147  HOH   HOH B . 
E 3 HOH   84  284 84   HOH   HOH B . 
E 3 HOH   85  285 243  HOH   HOH B . 
E 3 HOH   86  286 276  HOH   HOH B . 
E 3 HOH   87  287 106  HOH   HOH B . 
E 3 HOH   88  288 20   HOH   HOH B . 
E 3 HOH   89  289 635  HOH   HOH B . 
E 3 HOH   90  290 287  HOH   HOH B . 
E 3 HOH   91  291 416  HOH   HOH B . 
E 3 HOH   92  292 311  HOH   HOH B . 
E 3 HOH   93  293 13   HOH   HOH B . 
E 3 HOH   94  294 234  HOH   HOH B . 
E 3 HOH   95  295 1305 HOH   HOH B . 
E 3 HOH   96  296 22   HOH   HOH B . 
E 3 HOH   97  297 235  HOH   HOH B . 
E 3 HOH   98  298 271  HOH   HOH B . 
E 3 HOH   99  299 43   HOH   HOH B . 
E 3 HOH   100 300 197  HOH   HOH B . 
E 3 HOH   101 301 1066 HOH   HOH B . 
E 3 HOH   102 302 99   HOH   HOH B . 
E 3 HOH   103 303 38   HOH   HOH B . 
E 3 HOH   104 304 137  HOH   HOH B . 
E 3 HOH   105 305 316  HOH   HOH B . 
E 3 HOH   106 306 142  HOH   HOH B . 
E 3 HOH   107 307 1126 HOH   HOH B . 
E 3 HOH   108 308 160  HOH   HOH B . 
E 3 HOH   109 309 387  HOH   HOH B . 
E 3 HOH   110 310 170  HOH   HOH B . 
E 3 HOH   111 311 141  HOH   HOH B . 
E 3 HOH   112 312 1274 HOH   HOH B . 
E 3 HOH   113 313 101  HOH   HOH B . 
E 3 HOH   114 314 112  HOH   HOH B . 
E 3 HOH   115 315 1294 HOH   HOH B . 
E 3 HOH   116 316 23   HOH   HOH B . 
E 3 HOH   117 317 1106 HOH   HOH B . 
E 3 HOH   118 318 100  HOH   HOH B . 
E 3 HOH   119 319 37   HOH   HOH B . 
E 3 HOH   120 320 48   HOH   HOH B . 
E 3 HOH   121 321 1291 HOH   HOH B . 
E 3 HOH   122 322 334  HOH   HOH B . 
E 3 HOH   123 323 297  HOH   HOH B . 
E 3 HOH   124 324 91   HOH   HOH B . 
E 3 HOH   125 325 118  HOH   HOH B . 
E 3 HOH   126 326 32   HOH   HOH B . 
E 3 HOH   127 327 177  HOH   HOH B . 
E 3 HOH   128 328 161  HOH   HOH B . 
E 3 HOH   129 329 215  HOH   HOH B . 
E 3 HOH   130 330 28   HOH   HOH B . 
E 3 HOH   131 331 717  HOH   HOH B . 
E 3 HOH   132 332 44   HOH   HOH B . 
E 3 HOH   133 333 704  HOH   HOH B . 
E 3 HOH   134 334 29   HOH   HOH B . 
E 3 HOH   135 335 55   HOH   HOH B . 
E 3 HOH   136 336 98   HOH   HOH B . 
E 3 HOH   137 337 339  HOH   HOH B . 
E 3 HOH   138 338 207  HOH   HOH B . 
E 3 HOH   139 339 1293 HOH   HOH B . 
E 3 HOH   140 340 65   HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 362  HOH   HOH B . 
E 3 HOH   143 343 178  HOH   HOH B . 
E 3 HOH   144 344 445  HOH   HOH B . 
E 3 HOH   145 345 90   HOH   HOH B . 
E 3 HOH   146 346 623  HOH   HOH B . 
E 3 HOH   147 347 463  HOH   HOH B . 
E 3 HOH   148 348 960  HOH   HOH B . 
E 3 HOH   149 349 1304 HOH   HOH B . 
E 3 HOH   150 350 191  HOH   HOH B . 
E 3 HOH   151 351 1046 HOH   HOH B . 
E 3 HOH   152 352 87   HOH   HOH B . 
E 3 HOH   153 353 541  HOH   HOH B . 
E 3 HOH   154 354 304  HOH   HOH B . 
E 3 HOH   155 355 335  HOH   HOH B . 
E 3 HOH   156 356 203  HOH   HOH B . 
E 3 HOH   157 357 290  HOH   HOH B . 
E 3 HOH   158 358 1077 HOH   HOH B . 
E 3 HOH   159 359 1280 HOH   HOH B . 
E 3 HOH   160 360 479  HOH   HOH B . 
E 3 HOH   161 361 389  HOH   HOH B . 
E 3 HOH   162 362 1072 HOH   HOH B . 
E 3 HOH   163 363 718  HOH   HOH B . 
E 3 HOH   164 364 283  HOH   HOH B . 
E 3 HOH   165 365 615  HOH   HOH B . 
E 3 HOH   166 366 1316 HOH   HOH B . 
E 3 HOH   167 367 291  HOH   HOH B . 
E 3 HOH   168 368 898  HOH   HOH B . 
E 3 HOH   169 369 1303 HOH   HOH B . 
E 3 HOH   170 370 667  HOH   HOH B . 
E 3 HOH   171 371 431  HOH   HOH B . 
E 3 HOH   172 372 190  HOH   HOH B . 
E 3 HOH   173 373 373  HOH   HOH B . 
E 3 HOH   174 374 340  HOH   HOH B . 
E 3 HOH   175 375 310  HOH   HOH B . 
E 3 HOH   176 376 1000 HOH   HOH B . 
E 3 HOH   177 377 1163 HOH   HOH B . 
E 3 HOH   178 378 149  HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 1311 HOH   HOH B . 
E 3 HOH   181 381 176  HOH   HOH B . 
E 3 HOH   182 382 418  HOH   HOH B . 
E 3 HOH   183 383 1173 HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 265  HOH   HOH B . 
E 3 HOH   186 386 1298 HOH   HOH B . 
E 3 HOH   187 387 491  HOH   HOH B . 
E 3 HOH   188 388 470  HOH   HOH B . 
E 3 HOH   189 389 248  HOH   HOH B . 
E 3 HOH   190 390 184  HOH   HOH B . 
E 3 HOH   191 391 360  HOH   HOH B . 
E 3 HOH   192 392 355  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 274  HOH   HOH B . 
E 3 HOH   195 395 566  HOH   HOH B . 
E 3 HOH   196 396 314  HOH   HOH B . 
E 3 HOH   197 397 157  HOH   HOH B . 
E 3 HOH   198 398 792  HOH   HOH B . 
E 3 HOH   199 399 321  HOH   HOH B . 
E 3 HOH   200 400 558  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           7HFB 
_cell.length_a           88.804 
_cell.length_b           88.804 
_cell.length_c           39.608 
_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                         7HFB 
_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          7HFB 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.83 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-08-11 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HFB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.120 
_reflns.number_obs                   118321 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.063 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.200 
_reflns.B_iso_Wilson_estimate        14.810 
_reflns.pdbx_redundancy              6.600 
_reflns.pdbx_Rrim_I_all              0.069 
_reflns.pdbx_Rpim_I_all              0.027 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     783147 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.120 1.140  ? 37041 5670 ? 3.062 ? ? ? 6.500 ? 0.600  ? ? ? ? ? ? 96.700 3.325 1.283 0.304 
1 2 6.130 44.400 ? 5524  794  ? 0.033 ? ? ? 7.000 ? 51.900 ? ? ? ? ? ? 99.800 0.036 0.014 0.997 
# 
_refine.entry_id                                 7HFB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.1200 
_refine.ls_d_res_low                             39.7100 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.4400 
_refine.ls_number_reflns_obs                     118125 
_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                          0.1566 
_refine.ls_R_factor_R_work                       0.1555 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1791 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  5666 
_refine.ls_number_reflns_R_work                  112459 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               22.6108 
_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                            0.1700 
_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                                91.860 
_refine.B_iso_min                                11.090 
_refine.pdbx_overall_phase_error                 22.0300 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.1200 
_refine_hist.d_res_low                        39.7100 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             424 
_refine_hist.number_atoms_total               3008 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.06 
_refine_hist.pdbx_B_iso_mean_solvent          34.82 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.1200 1.1300  30 94.0000  3602 . 0.4770 0.4779 . 144 0.0000 3746 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 3675 . 0.4120 0.4434 . 179 0.0000 3854 . 'X-RAY DIFFRACTION' 
1.1500 1.1600  30 100.0000 3788 . 0.3794 0.3726 . 186 0.0000 3974 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 3702 . 0.3278 0.3572 . 194 0.0000 3896 . 'X-RAY DIFFRACTION' 
1.1800 1.1900  30 100.0000 3741 . 0.3150 0.3402 . 202 0.0000 3943 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 3746 . 0.2852 0.3314 . 187 0.0000 3933 . 'X-RAY DIFFRACTION' 
1.2100 1.2200  30 100.0000 3719 . 0.2579 0.2922 . 202 0.0000 3921 . 'X-RAY DIFFRACTION' 
1.2200 1.2400  30 100.0000 3773 . 0.2476 0.2748 . 173 0.0000 3946 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 99.0000  3678 . 0.2381 0.2276 . 168 0.0000 3846 . 'X-RAY DIFFRACTION' 
1.2600 1.2800  30 97.0000  3634 . 0.2213 0.2532 . 198 0.0000 3832 . 'X-RAY DIFFRACTION' 
1.2800 1.3000  30 99.0000  3737 . 0.2101 0.2426 . 168 0.0000 3905 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 3741 . 0.2007 0.2254 . 222 0.0000 3963 . 'X-RAY DIFFRACTION' 
1.3300 1.3500  30 100.0000 3717 . 0.1990 0.2359 . 196 0.0000 3913 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 3722 . 0.1948 0.2531 . 201 0.0000 3923 . 'X-RAY DIFFRACTION' 
1.3800 1.4100  30 100.0000 3844 . 0.1793 0.2501 . 152 0.0000 3996 . 'X-RAY DIFFRACTION' 
1.4100 1.4400  30 100.0000 3708 . 0.1590 0.1935 . 208 0.0000 3916 . 'X-RAY DIFFRACTION' 
1.4400 1.4800  30 100.0000 3762 . 0.1441 0.1685 . 183 0.0000 3945 . 'X-RAY DIFFRACTION' 
1.4800 1.5200  30 100.0000 3776 . 0.1276 0.1511 . 176 0.0000 3952 . 'X-RAY DIFFRACTION' 
1.5200 1.5700  30 99.0000  3703 . 0.1221 0.1550 . 210 0.0000 3913 . 'X-RAY DIFFRACTION' 
1.5700 1.6200  30 99.0000  3714 . 0.1182 0.1544 . 185 0.0000 3899 . 'X-RAY DIFFRACTION' 
1.6200 1.6700  30 100.0000 3769 . 0.1277 0.1600 . 191 0.0000 3960 . 'X-RAY DIFFRACTION' 
1.6700 1.7400  30 100.0000 3807 . 0.1319 0.1692 . 154 0.0000 3961 . 'X-RAY DIFFRACTION' 
1.7400 1.8200  30 100.0000 3738 . 0.1287 0.1491 . 206 0.0000 3944 . 'X-RAY DIFFRACTION' 
1.8200 1.9200  30 100.0000 3768 . 0.1303 0.1564 . 211 0.0000 3979 . 'X-RAY DIFFRACTION' 
1.9200 2.0400  30 100.0000 3779 . 0.1357 0.1494 . 191 0.0000 3970 . 'X-RAY DIFFRACTION' 
2.0400 2.1900  30 100.0000 3764 . 0.1332 0.1530 . 220 0.0000 3984 . 'X-RAY DIFFRACTION' 
2.1900 2.4100  30 100.0000 3766 . 0.1340 0.1410 . 181 0.0000 3947 . 'X-RAY DIFFRACTION' 
2.4100 2.7600  30 100.0000 3809 . 0.1425 0.1583 . 198 0.0000 4007 . 'X-RAY DIFFRACTION' 
2.7600 3.4800  30 100.0000 3845 . 0.1493 0.1924 . 177 0.0000 4022 . 'X-RAY DIFFRACTION' 
3.4800 39.7100 30 100.0000 3932 . 0.1496 0.1686 . 203 0.0000 4135 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFB 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004331' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFB 
_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 7HFB A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFB 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 7HFB SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFB MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFB SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFB 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 LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HFB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    303 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.55 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
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  ? ? 56.43  -133.10 
2 1 PHE A 156 ? B -97.44 36.74   
3 1 HIS B 86  ? ? 57.42  -128.28 
# 
_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 B A HOH 521 ? 5.84 . 
2 1 O ? A HOH 522 ? 5.88 . 
3 1 O ? A HOH 523 ? 6.09 . 
4 1 O ? A HOH 524 ? 7.52 . 
5 1 O ? B HOH 400 ? 6.29 . 
# 
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 
A1BAX N2   N Y N 1   
A1BAX C3   C Y N 2   
A1BAX C6   C Y N 3   
A1BAX C9   C N N 4   
A1BAX C12  C N N 5   
A1BAX C14  C N N 6   
A1BAX C1   C N N 7   
A1BAX C10  C N N 8   
A1BAX C11  C N N 9   
A1BAX C13  C N N 10  
A1BAX C15  C Y N 11  
A1BAX C2   C Y N 12  
A1BAX C4   C Y N 13  
A1BAX C5   C Y N 14  
A1BAX C7   C N N 15  
A1BAX C8   C N N 16  
A1BAX N1   N Y N 17  
A1BAX N3   N Y N 18  
A1BAX N4   N N N 19  
A1BAX O1   O N N 20  
A1BAX H5   H N N 21  
A1BAX H12  H N N 22  
A1BAX H11  H N N 23  
A1BAX H15  H N N 24  
A1BAX H16  H N N 25  
A1BAX H20  H N N 26  
A1BAX H21  H N N 27  
A1BAX H19  H N N 28  
A1BAX H2   H N N 29  
A1BAX H3   H N N 30  
A1BAX H4   H N N 31  
A1BAX H14  H N N 32  
A1BAX H13  H N N 33  
A1BAX H1   H N N 34  
A1BAX H18  H N N 35  
A1BAX H17  H N N 36  
A1BAX H7   H N N 37  
A1BAX H9   H N N 38  
A1BAX H10  H N N 39  
A1BAX H6   H N N 40  
A1BAX H8   H N N 41  
A1BAX H22  H N N 42  
ALA   N    N N N 43  
ALA   CA   C N S 44  
ALA   C    C N N 45  
ALA   O    O N N 46  
ALA   CB   C N N 47  
ALA   OXT  O N N 48  
ALA   H    H N N 49  
ALA   H2   H N N 50  
ALA   HA   H N N 51  
ALA   HB1  H N N 52  
ALA   HB2  H N N 53  
ALA   HB3  H N N 54  
ALA   HXT  H N N 55  
ARG   N    N N N 56  
ARG   CA   C N S 57  
ARG   C    C N N 58  
ARG   O    O N N 59  
ARG   CB   C N N 60  
ARG   CG   C N N 61  
ARG   CD   C N N 62  
ARG   NE   N N N 63  
ARG   CZ   C N N 64  
ARG   NH1  N N N 65  
ARG   NH2  N N N 66  
ARG   OXT  O N N 67  
ARG   H    H N N 68  
ARG   H2   H N N 69  
ARG   HA   H N N 70  
ARG   HB2  H N N 71  
ARG   HB3  H N N 72  
ARG   HG2  H N N 73  
ARG   HG3  H N N 74  
ARG   HD2  H N N 75  
ARG   HD3  H N N 76  
ARG   HE   H N N 77  
ARG   HH11 H N N 78  
ARG   HH12 H N N 79  
ARG   HH21 H N N 80  
ARG   HH22 H N N 81  
ARG   HXT  H N N 82  
ASN   N    N N N 83  
ASN   CA   C N S 84  
ASN   C    C N N 85  
ASN   O    O N N 86  
ASN   CB   C N N 87  
ASN   CG   C N N 88  
ASN   OD1  O N N 89  
ASN   ND2  N N N 90  
ASN   OXT  O N N 91  
ASN   H    H N N 92  
ASN   H2   H N N 93  
ASN   HA   H N N 94  
ASN   HB2  H N N 95  
ASN   HB3  H N N 96  
ASN   HD21 H N N 97  
ASN   HD22 H N N 98  
ASN   HXT  H N N 99  
ASP   N    N N N 100 
ASP   CA   C N S 101 
ASP   C    C N N 102 
ASP   O    O N N 103 
ASP   CB   C N N 104 
ASP   CG   C N N 105 
ASP   OD1  O N N 106 
ASP   OD2  O N N 107 
ASP   OXT  O N N 108 
ASP   H    H N N 109 
ASP   H2   H N N 110 
ASP   HA   H N N 111 
ASP   HB2  H N N 112 
ASP   HB3  H N N 113 
ASP   HD2  H N N 114 
ASP   HXT  H N N 115 
CYS   N    N N N 116 
CYS   CA   C N R 117 
CYS   C    C N N 118 
CYS   O    O N N 119 
CYS   CB   C N N 120 
CYS   SG   S N N 121 
CYS   OXT  O N N 122 
CYS   H    H N N 123 
CYS   H2   H N N 124 
CYS   HA   H N N 125 
CYS   HB2  H N N 126 
CYS   HB3  H N N 127 
CYS   HG   H N N 128 
CYS   HXT  H N N 129 
GLN   N    N N N 130 
GLN   CA   C N S 131 
GLN   C    C N N 132 
GLN   O    O N N 133 
GLN   CB   C N N 134 
GLN   CG   C N N 135 
GLN   CD   C N N 136 
GLN   OE1  O N N 137 
GLN   NE2  N N N 138 
GLN   OXT  O N N 139 
GLN   H    H N N 140 
GLN   H2   H N N 141 
GLN   HA   H N N 142 
GLN   HB2  H N N 143 
GLN   HB3  H N N 144 
GLN   HG2  H N N 145 
GLN   HG3  H N N 146 
GLN   HE21 H N N 147 
GLN   HE22 H N N 148 
GLN   HXT  H N N 149 
GLU   N    N N N 150 
GLU   CA   C N S 151 
GLU   C    C N N 152 
GLU   O    O N N 153 
GLU   CB   C N N 154 
GLU   CG   C N N 155 
GLU   CD   C N N 156 
GLU   OE1  O N N 157 
GLU   OE2  O N N 158 
GLU   OXT  O N N 159 
GLU   H    H N N 160 
GLU   H2   H N N 161 
GLU   HA   H N N 162 
GLU   HB2  H N N 163 
GLU   HB3  H N N 164 
GLU   HG2  H N N 165 
GLU   HG3  H N N 166 
GLU   HE2  H N N 167 
GLU   HXT  H N N 168 
GLY   N    N N N 169 
GLY   CA   C N N 170 
GLY   C    C N N 171 
GLY   O    O N N 172 
GLY   OXT  O N N 173 
GLY   H    H N N 174 
GLY   H2   H N N 175 
GLY   HA2  H N N 176 
GLY   HA3  H N N 177 
GLY   HXT  H N N 178 
HIS   N    N N N 179 
HIS   CA   C N S 180 
HIS   C    C N N 181 
HIS   O    O N N 182 
HIS   CB   C N N 183 
HIS   CG   C Y N 184 
HIS   ND1  N Y N 185 
HIS   CD2  C Y N 186 
HIS   CE1  C Y N 187 
HIS   NE2  N Y N 188 
HIS   OXT  O N N 189 
HIS   H    H N N 190 
HIS   H2   H N N 191 
HIS   HA   H N N 192 
HIS   HB2  H N N 193 
HIS   HB3  H N N 194 
HIS   HD1  H N N 195 
HIS   HD2  H N N 196 
HIS   HE1  H N N 197 
HIS   HE2  H N N 198 
HIS   HXT  H N N 199 
HOH   O    O N N 200 
HOH   H1   H N N 201 
HOH   H2   H N N 202 
ILE   N    N N N 203 
ILE   CA   C N S 204 
ILE   C    C N N 205 
ILE   O    O N N 206 
ILE   CB   C N S 207 
ILE   CG1  C N N 208 
ILE   CG2  C N N 209 
ILE   CD1  C N N 210 
ILE   OXT  O N N 211 
ILE   H    H N N 212 
ILE   H2   H N N 213 
ILE   HA   H N N 214 
ILE   HB   H N N 215 
ILE   HG12 H N N 216 
ILE   HG13 H N N 217 
ILE   HG21 H N N 218 
ILE   HG22 H N N 219 
ILE   HG23 H N N 220 
ILE   HD11 H N N 221 
ILE   HD12 H N N 222 
ILE   HD13 H N N 223 
ILE   HXT  H N N 224 
LEU   N    N N N 225 
LEU   CA   C N S 226 
LEU   C    C N N 227 
LEU   O    O N N 228 
LEU   CB   C N N 229 
LEU   CG   C N N 230 
LEU   CD1  C N N 231 
LEU   CD2  C N N 232 
LEU   OXT  O N N 233 
LEU   H    H N N 234 
LEU   H2   H N N 235 
LEU   HA   H N N 236 
LEU   HB2  H N N 237 
LEU   HB3  H N N 238 
LEU   HG   H N N 239 
LEU   HD11 H N N 240 
LEU   HD12 H N N 241 
LEU   HD13 H N N 242 
LEU   HD21 H N N 243 
LEU   HD22 H N N 244 
LEU   HD23 H N N 245 
LEU   HXT  H N N 246 
LYS   N    N N N 247 
LYS   CA   C N S 248 
LYS   C    C N N 249 
LYS   O    O N N 250 
LYS   CB   C N N 251 
LYS   CG   C N N 252 
LYS   CD   C N N 253 
LYS   CE   C N N 254 
LYS   NZ   N N N 255 
LYS   OXT  O N N 256 
LYS   H    H N N 257 
LYS   H2   H N N 258 
LYS   HA   H N N 259 
LYS   HB2  H N N 260 
LYS   HB3  H N N 261 
LYS   HG2  H N N 262 
LYS   HG3  H N N 263 
LYS   HD2  H N N 264 
LYS   HD3  H N N 265 
LYS   HE2  H N N 266 
LYS   HE3  H N N 267 
LYS   HZ1  H N N 268 
LYS   HZ2  H N N 269 
LYS   HZ3  H N N 270 
LYS   HXT  H N N 271 
MET   N    N N N 272 
MET   CA   C N S 273 
MET   C    C N N 274 
MET   O    O N N 275 
MET   CB   C N N 276 
MET   CG   C N N 277 
MET   SD   S N N 278 
MET   CE   C N N 279 
MET   OXT  O N N 280 
MET   H    H N N 281 
MET   H2   H N N 282 
MET   HA   H N N 283 
MET   HB2  H N N 284 
MET   HB3  H N N 285 
MET   HG2  H N N 286 
MET   HG3  H N N 287 
MET   HE1  H N N 288 
MET   HE2  H N N 289 
MET   HE3  H N N 290 
MET   HXT  H N N 291 
PHE   N    N N N 292 
PHE   CA   C N S 293 
PHE   C    C N N 294 
PHE   O    O N N 295 
PHE   CB   C N N 296 
PHE   CG   C Y N 297 
PHE   CD1  C Y N 298 
PHE   CD2  C Y N 299 
PHE   CE1  C Y N 300 
PHE   CE2  C Y N 301 
PHE   CZ   C Y N 302 
PHE   OXT  O N N 303 
PHE   H    H N N 304 
PHE   H2   H N N 305 
PHE   HA   H N N 306 
PHE   HB2  H N N 307 
PHE   HB3  H N N 308 
PHE   HD1  H N N 309 
PHE   HD2  H N N 310 
PHE   HE1  H N N 311 
PHE   HE2  H N N 312 
PHE   HZ   H N N 313 
PHE   HXT  H N N 314 
PRO   N    N N N 315 
PRO   CA   C N S 316 
PRO   C    C N N 317 
PRO   O    O N N 318 
PRO   CB   C N N 319 
PRO   CG   C N N 320 
PRO   CD   C N N 321 
PRO   OXT  O N N 322 
PRO   H    H N N 323 
PRO   HA   H N N 324 
PRO   HB2  H N N 325 
PRO   HB3  H N N 326 
PRO   HG2  H N N 327 
PRO   HG3  H N N 328 
PRO   HD2  H N N 329 
PRO   HD3  H N N 330 
PRO   HXT  H N N 331 
SER   N    N N N 332 
SER   CA   C N S 333 
SER   C    C N N 334 
SER   O    O N N 335 
SER   CB   C N N 336 
SER   OG   O N N 337 
SER   OXT  O N N 338 
SER   H    H N N 339 
SER   H2   H N N 340 
SER   HA   H N N 341 
SER   HB2  H N N 342 
SER   HB3  H N N 343 
SER   HG   H N N 344 
SER   HXT  H N N 345 
THR   N    N N N 346 
THR   CA   C N S 347 
THR   C    C N N 348 
THR   O    O N N 349 
THR   CB   C N R 350 
THR   OG1  O N N 351 
THR   CG2  C N N 352 
THR   OXT  O N N 353 
THR   H    H N N 354 
THR   H2   H N N 355 
THR   HA   H N N 356 
THR   HB   H N N 357 
THR   HG1  H N N 358 
THR   HG21 H N N 359 
THR   HG22 H N N 360 
THR   HG23 H N N 361 
THR   HXT  H N N 362 
TYR   N    N N N 363 
TYR   CA   C N S 364 
TYR   C    C N N 365 
TYR   O    O N N 366 
TYR   CB   C N N 367 
TYR   CG   C Y N 368 
TYR   CD1  C Y N 369 
TYR   CD2  C Y N 370 
TYR   CE1  C Y N 371 
TYR   CE2  C Y N 372 
TYR   CZ   C Y N 373 
TYR   OH   O N N 374 
TYR   OXT  O N N 375 
TYR   H    H N N 376 
TYR   H2   H N N 377 
TYR   HA   H N N 378 
TYR   HB2  H N N 379 
TYR   HB3  H N N 380 
TYR   HD1  H N N 381 
TYR   HD2  H N N 382 
TYR   HE1  H N N 383 
TYR   HE2  H N N 384 
TYR   HH   H N N 385 
TYR   HXT  H N N 386 
VAL   N    N N N 387 
VAL   CA   C N S 388 
VAL   C    C N N 389 
VAL   O    O N N 390 
VAL   CB   C N N 391 
VAL   CG1  C N N 392 
VAL   CG2  C N N 393 
VAL   OXT  O N N 394 
VAL   H    H N N 395 
VAL   H2   H N N 396 
VAL   HA   H N N 397 
VAL   HB   H N N 398 
VAL   HG11 H N N 399 
VAL   HG12 H N N 400 
VAL   HG13 H N N 401 
VAL   HG21 H N N 402 
VAL   HG22 H N N 403 
VAL   HG23 H N N 404 
VAL   HXT  H N N 405 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BAX C14 C11  sing N N 1   
A1BAX C11 C10  sing N N 2   
A1BAX C11 C12  sing N N 3   
A1BAX C10 C9   sing N N 4   
A1BAX C12 C13  sing N N 5   
A1BAX C9  C8   sing N N 6   
A1BAX C13 C8   sing N N 7   
A1BAX C7  C8   sing N N 8   
A1BAX C7  N4   sing N N 9   
A1BAX C8  O1   sing N N 10  
A1BAX N4  C6   sing N N 11  
A1BAX C1  C2   sing N N 12  
A1BAX C6  N3   doub Y N 13  
A1BAX C6  C15  sing Y N 14  
A1BAX C2  C15  sing Y N 15  
A1BAX C2  C3   doub Y N 16  
A1BAX N3  C5   sing Y N 17  
A1BAX C15 C4   doub Y N 18  
A1BAX C3  N1   sing Y N 19  
A1BAX C5  N2   doub Y N 20  
A1BAX C4  N1   sing Y N 21  
A1BAX C4  N2   sing Y N 22  
A1BAX C3  H5   sing N N 23  
A1BAX C9  H12  sing N N 24  
A1BAX C9  H11  sing N N 25  
A1BAX C12 H15  sing N N 26  
A1BAX C12 H16  sing N N 27  
A1BAX C14 H20  sing N N 28  
A1BAX C14 H21  sing N N 29  
A1BAX C14 H19  sing N N 30  
A1BAX C1  H2   sing N N 31  
A1BAX C1  H3   sing N N 32  
A1BAX C1  H4   sing N N 33  
A1BAX C10 H14  sing N N 34  
A1BAX C10 H13  sing N N 35  
A1BAX C11 H1   sing N N 36  
A1BAX C13 H18  sing N N 37  
A1BAX C13 H17  sing N N 38  
A1BAX C5  H7   sing N N 39  
A1BAX C7  H9   sing N N 40  
A1BAX C7  H10  sing N N 41  
A1BAX N1  H6   sing N N 42  
A1BAX N4  H8   sing N N 43  
A1BAX O1  H22  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TYR   N   CA   sing N N 350 
TYR   N   H    sing N N 351 
TYR   N   H2   sing N N 352 
TYR   CA  C    sing N N 353 
TYR   CA  CB   sing N N 354 
TYR   CA  HA   sing N N 355 
TYR   C   O    doub N N 356 
TYR   C   OXT  sing N N 357 
TYR   CB  CG   sing N N 358 
TYR   CB  HB2  sing N N 359 
TYR   CB  HB3  sing N N 360 
TYR   CG  CD1  doub Y N 361 
TYR   CG  CD2  sing Y N 362 
TYR   CD1 CE1  sing Y N 363 
TYR   CD1 HD1  sing N N 364 
TYR   CD2 CE2  doub Y N 365 
TYR   CD2 HD2  sing N N 366 
TYR   CE1 CZ   doub Y N 367 
TYR   CE1 HE1  sing N N 368 
TYR   CE2 CZ   sing Y N 369 
TYR   CE2 HE2  sing N N 370 
TYR   CZ  OH   sing N N 371 
TYR   OH  HH   sing N N 372 
TYR   OXT HXT  sing N N 373 
VAL   N   CA   sing N N 374 
VAL   N   H    sing N N 375 
VAL   N   H2   sing N N 376 
VAL   CA  C    sing N N 377 
VAL   CA  CB   sing N N 378 
VAL   CA  HA   sing N N 379 
VAL   C   O    doub N N 380 
VAL   C   OXT  sing N N 381 
VAL   CB  CG1  sing N N 382 
VAL   CB  CG2  sing N N 383 
VAL   CB  HB   sing N N 384 
VAL   CG1 HG11 sing N N 385 
VAL   CG1 HG12 sing N N 386 
VAL   CG1 HG13 sing N N 387 
VAL   CG2 HG21 sing N N 388 
VAL   CG2 HG22 sing N N 389 
VAL   CG2 HG23 sing N N 390 
VAL   OXT HXT  sing N N 391 
# 
_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                    7HFB 
_atom_sites.fract_transf_matrix[1][1]   0.011261 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011261 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.025247 
_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   ? 19.581 -16.013 22.229  0.46 68.66 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.522 -15.955 22.372  0.54 68.90 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.605 -14.946 22.413  0.46 68.27 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.535 -14.893 22.523  0.54 68.47 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.244 -13.593 22.118  0.46 66.64 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.173 -13.537 22.238  0.54 66.78 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.373 -13.328 22.533  0.46 67.17 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.237 -13.221 22.771  0.54 67.38 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.991 -14.986 23.829  0.46 69.13 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.885 -14.925 23.921  0.54 69.33 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.948 -13.889 23.994  0.46 69.40 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.813 -13.849 24.037  0.54 69.60 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.380 -16.353 24.108  0.46 69.39 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.300 -16.301 24.206  0.54 69.59 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.884 -15.074 21.781  0.46 81.94 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.830 -15.027 21.875  0.54 82.18 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.691 -14.833 24.483  0.46 82.97 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.563 -14.745 24.591  0.54 83.22 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.466 -14.035 24.823  0.46 83.29 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.313 -13.990 24.856  0.54 83.54 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.394 -13.028 24.019  0.46 83.29 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.239 -12.978 24.056  0.54 83.54 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.333 -13.924 23.245  0.46 83.29 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.219 -13.912 23.273  0.54 83.54 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.934 -16.330 24.969  0.46 83.28 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.818 -16.271 25.047  0.54 83.52 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.740 -16.561 23.409  0.46 83.28 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.696 -16.541 23.486  0.54 83.52 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.086 -17.018 24.119  0.46 83.28 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.022 -16.947 24.261  0.54 83.52 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.521 -12.742 21.390  1.00 63.96 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 18.977 -11.393 21.064  1.00 58.11 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 17.852 -10.393 21.335  1.00 52.55 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.739 -10.764 21.721  1.00 52.48 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.536 -11.298 19.636  1.00 57.41 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.537 -11.714 18.583  1.00 56.52 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.387 -11.276 18.593  1.00 56.05 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 18.975 -12.567 17.662  1.00 56.34 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.745 -12.931 21.069  0.46 76.77 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.797 -12.970 20.984  0.54 76.77 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.705 -11.172 21.654  1.00 69.75 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 19.797 -10.379 19.459  1.00 68.91 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.309 -11.879 19.560  1.00 68.91 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.450 -12.833 17.035  1.00 67.62 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.787 -12.853 17.691  1.00 67.62 ?  4   ASN   A HD22 1 
ATOM   46   N N    A SER   A 1 5   ? 18.152 -9.110  21.129  0.46 49.61 ?  5   SER   A N    1 
ATOM   47   N N    B SER   A 1 5   ? 18.153 -9.111  21.119  0.54 49.49 ?  5   SER   A N    1 
ATOM   48   C CA   A SER   A 1 5   ? 17.257 -8.023  21.505  0.46 46.68 ?  5   SER   A CA   1 
ATOM   49   C CA   B SER   A 1 5   ? 17.274 -8.012  21.496  0.54 46.49 ?  5   SER   A CA   1 
ATOM   50   C C    A SER   A 1 5   ? 16.401 -7.516  20.348  0.46 42.81 ?  5   SER   A C    1 
ATOM   51   C C    B SER   A 1 5   ? 16.416 -7.505  20.341  0.54 42.68 ?  5   SER   A C    1 
ATOM   52   O O    A SER   A 1 5   ? 15.748 -6.476  20.487  0.46 42.57 ?  5   SER   A O    1 
ATOM   53   O O    B SER   A 1 5   ? 15.777 -6.456  20.474  0.54 42.34 ?  5   SER   A O    1 
ATOM   54   C CB   A SER   A 1 5   ? 18.055 -6.865  22.109  0.46 47.54 ?  5   SER   A CB   1 
ATOM   55   C CB   B SER   A 1 5   ? 18.092 -6.858  22.081  0.54 47.27 ?  5   SER   A CB   1 
ATOM   56   O OG   A SER   A 1 5   ? 19.028 -6.385  21.197  0.46 48.02 ?  5   SER   A OG   1 
ATOM   57   O OG   B SER   A 1 5   ? 18.947 -6.296  21.101  0.54 47.66 ?  5   SER   A OG   1 
ATOM   58   H H    A SER   A 1 5   ? 18.883 -8.845  20.764  0.46 59.54 ?  5   SER   A H    1 
ATOM   59   H H    B SER   A 1 5   ? 18.879 -8.852  20.739  0.54 59.40 ?  5   SER   A H    1 
ATOM   60   H HA   A SER   A 1 5   ? 16.657 -8.347  22.193  0.46 56.03 ?  5   SER   A HA   1 
ATOM   61   H HA   B SER   A 1 5   ? 16.675 -8.321  22.192  0.54 55.80 ?  5   SER   A HA   1 
ATOM   62   H HB2  A SER   A 1 5   ? 17.446 -6.141  22.324  0.46 57.06 ?  5   SER   A HB2  1 
ATOM   63   H HB2  B SER   A 1 5   ? 17.488 -6.170  22.402  0.54 56.74 ?  5   SER   A HB2  1 
ATOM   64   H HB3  A SER   A 1 5   ? 18.497 -7.174  22.916  0.46 57.06 ?  5   SER   A HB3  1 
ATOM   65   H HB3  B SER   A 1 5   ? 18.631 -7.193  22.818  0.54 56.74 ?  5   SER   A HB3  1 
ATOM   66   H HG   A SER   A 1 5   ? 19.461 -5.755  21.547  0.46 57.64 ?  5   SER   A HG   1 
ATOM   67   H HG   B SER   A 1 5   ? 19.394 -5.666  21.436  0.54 57.21 ?  5   SER   A HG   1 
ATOM   68   N N    . PHE   A 1 6   ? 16.388 -8.213  19.215  1.00 38.97 ?  6   PHE   A N    1 
ATOM   69   C CA   . PHE   A 1 6   ? 15.501 -7.834  18.122  1.00 32.17 ?  6   PHE   A CA   1 
ATOM   70   C C    . PHE   A 1 6   ? 14.063 -8.176  18.506  1.00 30.68 ?  6   PHE   A C    1 
ATOM   71   O O    . PHE   A 1 6   ? 13.788 -9.277  18.992  1.00 32.73 ?  6   PHE   A O    1 
ATOM   72   C CB   . PHE   A 1 6   ? 15.900 -8.574  16.849  1.00 28.56 ?  6   PHE   A CB   1 
ATOM   73   C CG   . PHE   A 1 6   ? 17.192 -8.089  16.240  1.00 25.59 ?  6   PHE   A CG   1 
ATOM   74   C CD1  . PHE   A 1 6   ? 17.226 -6.924  15.490  1.00 24.94 ?  6   PHE   A CD1  1 
ATOM   75   C CD2  . PHE   A 1 6   ? 18.365 -8.802  16.411  1.00 25.99 ?  6   PHE   A CD2  1 
ATOM   76   C CE1  . PHE   A 1 6   ? 18.410 -6.475  14.925  1.00 24.30 ?  6   PHE   A CE1  1 
ATOM   77   C CE2  . PHE   A 1 6   ? 19.550 -8.359  15.851  1.00 25.75 ?  6   PHE   A CE2  1 
ATOM   78   C CZ   . PHE   A 1 6   ? 19.572 -7.192  15.109  1.00 24.67 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 16.882 -8.899  19.057  0.46 46.78 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 16.867 -8.911  19.064  0.54 46.78 ?  6   PHE   A H    1 
ATOM   81   H HA   . PHE   A 1 6   ? 15.564 -6.881  17.968  1.00 38.61 ?  6   PHE   A HA   1 
ATOM   82   H HB2  . PHE   A 1 6   ? 16.007 -9.516  17.058  1.00 34.29 ?  6   PHE   A HB2  1 
ATOM   83   H HB3  . PHE   A 1 6   ? 15.200 -8.461  16.192  1.00 34.29 ?  6   PHE   A HB3  1 
ATOM   84   H HD1  . PHE   A 1 6   ? 16.445 -6.434  15.369  1.00 29.95 ?  6   PHE   A HD1  1 
ATOM   85   H HD2  . PHE   A 1 6   ? 18.358 -9.587  16.913  1.00 31.20 ?  6   PHE   A HD2  1 
ATOM   86   H HE1  . PHE   A 1 6   ? 18.423 -5.689  14.426  1.00 29.18 ?  6   PHE   A HE1  1 
ATOM   87   H HE2  . PHE   A 1 6   ? 20.337 -8.844  15.971  1.00 30.91 ?  6   PHE   A HE2  1 
ATOM   88   H HZ   . PHE   A 1 6   ? 20.366 -6.894  14.728  1.00 29.62 ?  6   PHE   A HZ   1 
ATOM   89   N N    A SER   A 1 7   ? 13.140 -7.246  18.262  0.46 28.74 ?  7   SER   A N    1 
ATOM   90   N N    B SER   A 1 7   ? 13.149 -7.227  18.291  0.54 29.24 ?  7   SER   A N    1 
ATOM   91   C CA   A SER   A 1 7   ? 11.757 -7.403  18.695  0.46 28.37 ?  7   SER   A CA   1 
ATOM   92   C CA   B SER   A 1 7   ? 11.801 -7.280  18.847  0.54 29.67 ?  7   SER   A CA   1 
ATOM   93   C C    A SER   A 1 7   ? 10.795 -7.143  17.546  0.46 26.40 ?  7   SER   A C    1 
ATOM   94   C C    B SER   A 1 7   ? 10.761 -7.130  17.747  0.54 27.76 ?  7   SER   A C    1 
ATOM   95   O O    A SER   A 1 7   ? 11.036 -6.282  16.696  0.46 26.17 ?  7   SER   A O    1 
ATOM   96   O O    B SER   A 1 7   ? 10.880 -6.256  16.884  0.54 27.28 ?  7   SER   A O    1 
ATOM   97   C CB   A SER   A 1 7   ? 11.432 -6.464  19.868  0.46 29.13 ?  7   SER   A CB   1 
ATOM   98   C CB   B SER   A 1 7   ? 11.612 -6.165  19.885  0.54 30.91 ?  7   SER   A CB   1 
ATOM   99   O OG   A SER   A 1 7   ? 10.139 -6.724  20.385  0.46 30.04 ?  7   SER   A OG   1 
ATOM   100  O OG   B SER   A 1 7   ? 10.273 -5.700  19.906  0.54 32.04 ?  7   SER   A OG   1 
ATOM   101  H H    A SER   A 1 7   ? 13.301 -6.516  17.835  0.46 34.50 ?  7   SER   A H    1 
ATOM   102  H H    B SER   A 1 7   ? 13.298 -6.531  17.810  0.54 35.10 ?  7   SER   A H    1 
ATOM   103  H HA   A SER   A 1 7   ? 11.624 -8.311  18.990  0.46 34.06 ?  7   SER   A HA   1 
ATOM   104  H HA   B SER   A 1 7   ? 11.663 -8.131  19.288  0.54 35.62 ?  7   SER   A HA   1 
ATOM   105  H HB2  A SER   A 1 7   ? 12.094 -6.595  20.568  0.46 34.97 ?  7   SER   A HB2  1 
ATOM   106  H HB2  B SER   A 1 7   ? 11.814 -6.514  20.765  0.54 37.11 ?  7   SER   A HB2  1 
ATOM   107  H HB3  A SER   A 1 7   ? 11.460 -5.546  19.558  0.46 34.97 ?  7   SER   A HB3  1 
ATOM   108  H HB3  B SER   A 1 7   ? 12.219 -5.433  19.673  0.54 37.11 ?  7   SER   A HB3  1 
ATOM   109  H HG   A SER   A 1 7   ? 9.983  -6.217  21.037  0.46 36.07 ?  7   SER   A HG   1 
ATOM   110  H HG   B SER   A 1 7   ? 10.200 -5.062  20.447  0.54 38.46 ?  7   SER   A HG   1 
ATOM   111  N N    A GLY   A 1 8   ? 9.701  -7.902  17.531  0.46 25.11 ?  8   GLY   A N    1 
ATOM   112  N N    B GLY   A 1 8   ? 9.740  -7.982  17.786  0.54 27.17 ?  8   GLY   A N    1 
ATOM   113  C CA   A GLY   A 1 8   ? 8.639  -7.685  16.570  0.46 23.94 ?  8   GLY   A CA   1 
ATOM   114  C CA   B GLY   A 1 8   ? 8.594  -7.814  16.919  0.54 26.41 ?  8   GLY   A CA   1 
ATOM   115  C C    A GLY   A 1 8   ? 8.885  -8.229  15.179  0.46 22.37 ?  8   GLY   A C    1 
ATOM   116  C C    B GLY   A 1 8   ? 8.803  -8.210  15.481  0.54 24.88 ?  8   GLY   A C    1 
ATOM   117  O O    A GLY   A 1 8   ? 8.229  -7.785  14.231  0.46 22.15 ?  8   GLY   A O    1 
ATOM   118  O O    B GLY   A 1 8   ? 8.002  -7.823  14.625  0.54 24.91 ?  8   GLY   A O    1 
ATOM   119  H H    A GLY   A 1 8   ? 9.561  -8.546  18.083  0.46 30.15 ?  8   GLY   A H    1 
ATOM   120  H H    B GLY   A 1 8   ? 9.699  -8.667  18.300  0.54 32.62 ?  8   GLY   A H    1 
ATOM   121  H HA2  A GLY   A 1 8   ? 7.831  -8.098  16.916  0.46 28.74 ?  8   GLY   A HA2  1 
ATOM   122  H HA2  B GLY   A 1 8   ? 7.860  -8.341  17.265  0.54 31.71 ?  8   GLY   A HA2  1 
ATOM   123  H HA3  A GLY   A 1 8   ? 8.477  -6.731  16.504  0.46 28.74 ?  8   GLY   A HA3  1 
ATOM   124  H HA3  B GLY   A 1 8   ? 8.331  -6.885  16.920  0.54 31.71 ?  8   GLY   A HA3  1 
ATOM   125  N N    A TYR   A 1 9   ? 9.803  -9.181  15.022  0.46 20.79 ?  9   TYR   A N    1 
ATOM   126  N N    B TYR   A 1 9   ? 9.853  -8.967  15.181  0.54 23.08 ?  9   TYR   A N    1 
ATOM   127  C CA   A TYR   A 1 9   ? 10.108 -9.760  13.719  0.46 19.46 ?  9   TYR   A CA   1 
ATOM   128  C CA   B TYR   A 1 9   ? 10.100 -9.380  13.810  0.54 21.38 ?  9   TYR   A CA   1 
ATOM   129  C C    A TYR   A 1 9   ? 9.234  -10.976 13.439  0.46 18.69 ?  9   TYR   A C    1 
ATOM   130  C C    B TYR   A 1 9   ? 9.275  -10.615 13.467  0.54 20.51 ?  9   TYR   A C    1 
ATOM   131  O O    A TYR   A 1 9   ? 8.820  -11.696 14.352  0.46 19.29 ?  9   TYR   A O    1 
ATOM   132  O O    B TYR   A 1 9   ? 9.164  -11.547 14.267  0.54 21.26 ?  9   TYR   A O    1 
ATOM   133  C CB   A TYR   A 1 9   ? 11.583 -10.174 13.627  0.46 19.11 ?  9   TYR   A CB   1 
ATOM   134  C CB   B TYR   A 1 9   ? 11.589 -9.658  13.604  0.54 20.23 ?  9   TYR   A CB   1 
ATOM   135  C CG   A TYR   A 1 9   ? 12.517 -9.003  13.432  0.46 18.63 ?  9   TYR   A CG   1 
ATOM   136  C CG   B TYR   A 1 9   ? 12.428 -8.406  13.422  0.54 19.92 ?  9   TYR   A CG   1 
ATOM   137  C CD1  A TYR   A 1 9   ? 12.880 -8.208  14.504  0.46 18.75 ?  9   TYR   A CD1  1 
ATOM   138  C CD1  B TYR   A 1 9   ? 12.635 -7.519  14.475  0.54 20.47 ?  9   TYR   A CD1  1 
ATOM   139  C CD2  A TYR   A 1 9   ? 13.013 -8.682  12.175  0.46 18.24 ?  9   TYR   A CD2  1 
ATOM   140  C CD2  B TYR   A 1 9   ? 13.001 -8.106  12.194  0.54 19.17 ?  9   TYR   A CD2  1 
ATOM   141  C CE1  A TYR   A 1 9   ? 13.714 -7.122  14.339  0.46 18.93 ?  9   TYR   A CE1  1 
ATOM   142  C CE1  B TYR   A 1 9   ? 13.394 -6.374  14.308  0.54 20.00 ?  9   TYR   A CE1  1 
ATOM   143  C CE2  A TYR   A 1 9   ? 13.853 -7.593  11.997  0.46 18.37 ?  9   TYR   A CE2  1 
ATOM   144  C CE2  B TYR   A 1 9   ? 13.761 -6.968  12.018  0.54 19.56 ?  9   TYR   A CE2  1 
ATOM   145  C CZ   A TYR   A 1 9   ? 14.199 -6.820  13.087  0.46 18.89 ?  9   TYR   A CZ   1 
ATOM   146  C CZ   B TYR   A 1 9   ? 13.952 -6.109  13.077  0.54 19.77 ?  9   TYR   A CZ   1 
ATOM   147  O OH   A TYR   A 1 9   ? 15.024 -5.731  12.931  0.46 20.09 ?  9   TYR   A OH   1 
ATOM   148  O OH   B TYR   A 1 9   ? 14.693 -4.973  12.894  0.54 18.91 ?  9   TYR   A OH   1 
ATOM   149  H H    A TYR   A 1 9   ? 10.269 -9.503  15.666  0.46 24.96 ?  9   TYR   A H    1 
ATOM   150  H H    B TYR   A 1 9   ? 10.438 -9.259  15.749  0.54 27.71 ?  9   TYR   A H    1 
ATOM   151  H HA   A TYR   A 1 9   ? 9.937  -9.101  13.031  0.46 23.37 ?  9   TYR   A HA   1 
ATOM   152  H HA   B TYR   A 1 9   ? 9.853  -8.664  13.208  0.54 25.67 ?  9   TYR   A HA   1 
ATOM   153  H HB2  A TYR   A 1 9   ? 11.836 -10.631 14.446  0.46 22.95 ?  9   TYR   A HB2  1 
ATOM   154  H HB2  B TYR   A 1 9   ? 11.946 -10.173 14.351  0.54 24.29 ?  9   TYR   A HB2  1 
ATOM   155  H HB3  A TYR   A 1 9   ? 11.689 -10.774 12.871  0.46 22.95 ?  9   TYR   A HB3  1 
ATOM   156  H HB3  B TYR   A 1 9   ? 11.657 -10.161 12.785  0.54 24.29 ?  9   TYR   A HB3  1 
ATOM   157  H HD1  A TYR   A 1 9   ? 12.545 -8.407  15.352  0.46 22.52 ?  9   TYR   A HD1  1 
ATOM   158  H HD1  B TYR   A 1 9   ? 12.259 -7.703  15.306  0.54 24.57 ?  9   TYR   A HD1  1 
ATOM   159  H HD2  A TYR   A 1 9   ? 12.780 -9.208  11.442  0.46 21.90 ?  9   TYR   A HD2  1 
ATOM   160  H HD2  B TYR   A 1 9   ? 12.877 -8.686  11.479  0.54 23.02 ?  9   TYR   A HD2  1 
ATOM   161  H HE1  A TYR   A 1 9   ? 13.945 -6.599  15.070  0.46 22.73 ?  9   TYR   A HE1  1 
ATOM   162  H HE1  B TYR   A 1 9   ? 13.526 -5.787  15.020  0.54 24.01 ?  9   TYR   A HE1  1 
ATOM   163  H HE2  A TYR   A 1 9   ? 14.188 -7.390  11.152  0.46 22.06 ?  9   TYR   A HE2  1 
ATOM   164  H HE2  B TYR   A 1 9   ? 14.139 -6.779  11.188  0.54 23.49 ?  9   TYR   A HE2  1 
ATOM   165  H HH   A TYR   A 1 9   ? 15.150 -5.358  13.672  0.46 24.12 ?  9   TYR   A HH   1 
ATOM   166  H HH   B TYR   A 1 9   ? 14.736 -4.530  13.608  0.54 22.71 ?  9   TYR   A HH   1 
ATOM   167  N N    A LEU   A 1 10  ? 8.963  -11.191 12.155  0.46 17.56 ?  10  LEU   A N    1 
ATOM   168  N N    B LEU   A 1 10  ? 8.679  -10.603 12.275  0.54 18.57 ?  10  LEU   A N    1 
ATOM   169  C CA   A LEU   A 1 10  ? 8.308  -12.394 11.660  0.46 16.51 ?  10  LEU   A CA   1 
ATOM   170  C CA   B LEU   A 1 10  ? 7.930  -11.749 11.780  0.54 18.38 ?  10  LEU   A CA   1 
ATOM   171  C C    A LEU   A 1 10  ? 9.384  -13.352 11.161  0.46 15.04 ?  10  LEU   A C    1 
ATOM   172  C C    B LEU   A 1 10  ? 8.900  -12.792 11.238  0.54 18.22 ?  10  LEU   A C    1 
ATOM   173  O O    A LEU   A 1 10  ? 10.296 -12.943 10.436  0.46 13.73 ?  10  LEU   A O    1 
ATOM   174  O O    B LEU   A 1 10  ? 9.802  -12.473 10.457  0.54 18.13 ?  10  LEU   A O    1 
ATOM   175  C CB   A LEU   A 1 10  ? 7.354  -12.039 10.518  0.46 16.87 ?  10  LEU   A CB   1 
ATOM   176  C CB   B LEU   A 1 10  ? 6.978  -11.309 10.668  0.54 18.56 ?  10  LEU   A CB   1 
ATOM   177  C CG   A LEU   A 1 10  ? 6.639  -13.200 9.823   0.46 18.80 ?  10  LEU   A CG   1 
ATOM   178  C CG   B LEU   A 1 10  ? 5.818  -12.247 10.331  0.54 19.06 ?  10  LEU   A CG   1 
ATOM   179  C CD1  A LEU   A 1 10  ? 5.565  -13.792 10.723  0.46 20.29 ?  10  LEU   A CD1  1 
ATOM   180  C CD1  B LEU   A 1 10  ? 4.712  -12.129 11.369  0.54 18.18 ?  10  LEU   A CD1  1 
ATOM   181  C CD2  A LEU   A 1 10  ? 6.063  -12.770 8.482   0.46 20.51 ?  10  LEU   A CD2  1 
ATOM   182  C CD2  B LEU   A 1 10  ? 5.278  -11.942 8.949   0.54 18.75 ?  10  LEU   A CD2  1 
ATOM   183  H H    A LEU   A 1 10  ? 9.172  -10.641 11.527  0.46 21.09 ?  10  LEU   A H    1 
ATOM   184  H H    B LEU   A 1 10  ? 8.698  -9.933  11.731  0.54 22.30 ?  10  LEU   A H    1 
ATOM   185  H HA   A LEU   A 1 10  ? 7.804  -12.817 12.374  0.46 19.83 ?  10  LEU   A HA   1 
ATOM   186  H HA   B LEU   A 1 10  ? 7.412  -12.137 12.506  0.54 22.07 ?  10  LEU   A HA   1 
ATOM   187  H HB2  A LEU   A 1 10  ? 6.666  -11.449 10.871  0.46 20.26 ?  10  LEU   A HB2  1 
ATOM   188  H HB2  B LEU   A 1 10  ? 6.594  -10.457 10.922  0.54 22.29 ?  10  LEU   A HB2  1 
ATOM   189  H HB3  A LEU   A 1 10  ? 7.858  -11.567 9.839   0.46 20.26 ?  10  LEU   A HB3  1 
ATOM   190  H HB3  B LEU   A 1 10  ? 7.500  -11.199 9.860   0.54 22.29 ?  10  LEU   A HB3  1 
ATOM   191  H HG   A LEU   A 1 10  ? 7.283  -13.899 9.648   0.46 22.57 ?  10  LEU   A HG   1 
ATOM   192  H HG   B LEU   A 1 10  ? 6.139  -13.161 10.337  0.54 22.88 ?  10  LEU   A HG   1 
ATOM   193  H HD11 A LEU   A 1 10  ? 5.133  -14.526 10.258  0.46 24.36 ?  10  LEU   A HD11 1 
ATOM   194  H HD11 B LEU   A 1 10  ? 3.999  -12.749 11.144  0.54 21.83 ?  10  LEU   A HD11 1 
ATOM   195  H HD12 A LEU   A 1 10  ? 5.979  -14.117 11.539  0.46 24.36 ?  10  LEU   A HD12 1 
ATOM   196  H HD12 B LEU   A 1 10  ? 5.070  -12.345 12.245  0.54 21.83 ?  10  LEU   A HD12 1 
ATOM   197  H HD13 A LEU   A 1 10  ? 4.913  -13.106 10.936  0.46 24.36 ?  10  LEU   A HD13 1 
ATOM   198  H HD13 B LEU   A 1 10  ? 4.369  -11.221 11.369  0.54 21.83 ?  10  LEU   A HD13 1 
ATOM   199  H HD21 A LEU   A 1 10  ? 5.616  -13.528 8.076   0.46 24.63 ?  10  LEU   A HD21 1 
ATOM   200  H HD21 B LEU   A 1 10  ? 4.536  -12.536 8.764   0.54 22.52 ?  10  LEU   A HD21 1 
ATOM   201  H HD22 A LEU   A 1 10  ? 5.432  -12.049 8.627   0.46 24.63 ?  10  LEU   A HD22 1 
ATOM   202  H HD22 B LEU   A 1 10  ? 4.982  -11.019 8.923   0.54 22.52 ?  10  LEU   A HD22 1 
ATOM   203  H HD23 A LEU   A 1 10  ? 6.788  -12.468 7.914   0.46 24.63 ?  10  LEU   A HD23 1 
ATOM   204  H HD23 B LEU   A 1 10  ? 5.985  -12.081 8.299   0.54 22.52 ?  10  LEU   A HD23 1 
ATOM   205  N N    A LYS   A 1 11  ? 9.288  -14.614 11.566  0.46 14.53 ?  11  LYS   A N    1 
ATOM   206  N N    B LYS   A 1 11  ? 8.713  -14.040 11.652  0.54 18.43 ?  11  LYS   A N    1 
ATOM   207  C CA   A LYS   A 1 11  ? 10.272 -15.627 11.205  0.46 14.73 ?  11  LYS   A CA   1 
ATOM   208  C CA   B LYS   A 1 11  ? 9.609  -15.118 11.254  0.54 17.09 ?  11  LYS   A CA   1 
ATOM   209  C C    A LYS   A 1 11  ? 9.891  -16.226 9.854   0.46 14.67 ?  11  LYS   A C    1 
ATOM   210  C C    B LYS   A 1 11  ? 9.283  -15.579 9.839   0.54 17.29 ?  11  LYS   A C    1 
ATOM   211  O O    A LYS   A 1 11  ? 8.828  -16.836 9.721   0.46 15.84 ?  11  LYS   A O    1 
ATOM   212  O O    B LYS   A 1 11  ? 8.163  -16.031 9.573   0.54 17.63 ?  11  LYS   A O    1 
ATOM   213  C CB   A LYS   A 1 11  ? 10.321 -16.693 12.302  0.46 13.43 ?  11  LYS   A CB   1 
ATOM   214  C CB   B LYS   A 1 11  ? 9.466  -16.291 12.216  0.54 17.75 ?  11  LYS   A CB   1 
ATOM   215  C CG   A LYS   A 1 11  ? 11.315 -17.828 12.096  0.46 13.97 ?  11  LYS   A CG   1 
ATOM   216  C CG   B LYS   A 1 11  ? 10.485 -17.382 11.982  0.54 17.36 ?  11  LYS   A CG   1 
ATOM   217  C CD   A LYS   A 1 11  ? 11.344 -18.714 13.341  0.46 14.68 ?  11  LYS   A CD   1 
ATOM   218  C CD   B LYS   A 1 11  ? 10.365 -18.472 13.030  0.54 17.48 ?  11  LYS   A CD   1 
ATOM   219  C CE   A LYS   A 1 11  ? 12.348 -19.856 13.231  0.46 15.35 ?  11  LYS   A CE   1 
ATOM   220  C CE   B LYS   A 1 11  ? 11.442 -19.521 12.849  0.54 18.51 ?  11  LYS   A CE   1 
ATOM   221  N NZ   A LYS   A 1 11  ? 13.718 -19.386 12.924  0.46 14.02 ?  11  LYS   A NZ   1 
ATOM   222  N NZ   B LYS   A 1 11  ? 12.815 -18.955 12.982  0.54 19.08 ?  11  LYS   A NZ   1 
ATOM   223  H H    A LYS   A 1 11  ? 8.642  -14.909 12.069  0.46 17.45 ?  11  LYS   A H    1 
ATOM   224  H H    B LYS   A 1 11  ? 8.071  -14.291 12.170  0.54 22.13 ?  11  LYS   A H    1 
ATOM   225  H HA   A LYS   A 1 11  ? 11.142 -15.211 11.133  0.46 17.69 ?  11  LYS   A HA   1 
ATOM   226  H HA   B LYS   A 1 11  ? 10.527 -14.805 11.276  0.54 20.52 ?  11  LYS   A HA   1 
ATOM   227  H HB2  A LYS   A 1 11  ? 10.542 -16.259 13.142  0.46 16.13 ?  11  LYS   A HB2  1 
ATOM   228  H HB2  B LYS   A 1 11  ? 9.573  -15.972 13.122  0.54 21.32 ?  11  LYS   A HB2  1 
ATOM   229  H HB3  A LYS   A 1 11  ? 9.436  -17.092 12.376  0.46 16.13 ?  11  LYS   A HB3  1 
ATOM   230  H HB3  B LYS   A 1 11  ? 8.583  -16.682 12.103  0.54 21.32 ?  11  LYS   A HB3  1 
ATOM   231  H HG2  A LYS   A 1 11  ? 11.042 -18.364 11.335  0.46 16.77 ?  11  LYS   A HG2  1 
ATOM   232  H HG2  B LYS   A 1 11  ? 10.337 -17.781 11.109  0.54 20.85 ?  11  LYS   A HG2  1 
ATOM   233  H HG3  A LYS   A 1 11  ? 12.200 -17.458 11.955  0.46 16.77 ?  11  LYS   A HG3  1 
ATOM   234  H HG3  B LYS   A 1 11  ? 11.375 -17.003 12.032  0.54 20.85 ?  11  LYS   A HG3  1 
ATOM   235  H HD2  A LYS   A 1 11  ? 11.584 -18.173 14.109  0.46 17.64 ?  11  LYS   A HD2  1 
ATOM   236  H HD2  B LYS   A 1 11  ? 10.462 -18.080 13.912  0.54 20.99 ?  11  LYS   A HD2  1 
ATOM   237  H HD3  A LYS   A 1 11  ? 10.460 -19.099 13.473  0.46 17.64 ?  11  LYS   A HD3  1 
ATOM   238  H HD3  B LYS   A 1 11  ? 9.499  -18.903 12.947  0.54 20.99 ?  11  LYS   A HD3  1 
ATOM   239  H HE2  A LYS   A 1 11  ? 12.373 -20.333 14.075  0.46 18.43 ?  11  LYS   A HE2  1 
ATOM   240  H HE2  B LYS   A 1 11  ? 11.332 -20.207 13.525  0.54 22.22 ?  11  LYS   A HE2  1 
ATOM   241  H HE3  A LYS   A 1 11  ? 12.065 -20.455 12.521  0.46 18.43 ?  11  LYS   A HE3  1 
ATOM   242  H HE3  B LYS   A 1 11  ? 11.360 -19.908 11.964  0.54 22.22 ?  11  LYS   A HE3  1 
ATOM   243  H HZ1  A LYS   A 1 11  ? 14.276 -20.079 12.895  0.46 16.84 ?  11  LYS   A HZ1  1 
ATOM   244  H HZ1  B LYS   A 1 11  ? 13.418 -19.605 12.933  0.54 22.91 ?  11  LYS   A HZ1  1 
ATOM   245  H HZ2  A LYS   A 1 11  ? 13.728 -18.976 12.133  0.46 16.84 ?  11  LYS   A HZ2  1 
ATOM   246  H HZ2  B LYS   A 1 11  ? 12.968 -18.368 12.329  0.54 22.91 ?  11  LYS   A HZ2  1 
ATOM   247  H HZ3  A LYS   A 1 11  ? 13.992 -18.818 13.549  0.46 16.84 ?  11  LYS   A HZ3  1 
ATOM   248  H HZ3  B LYS   A 1 11  ? 12.899 -18.540 13.766  0.54 22.91 ?  11  LYS   A HZ3  1 
ATOM   249  N N    A LEU   A 1 12  ? 10.749 -16.050 8.848   0.46 13.37 ?  12  LEU   A N    1 
ATOM   250  N N    B LEU   A 1 12  ? 10.265 -15.489 8.938   0.54 17.82 ?  12  LEU   A N    1 
ATOM   251  C CA   A LEU   A 1 12  ? 10.494 -16.614 7.525   0.46 13.58 ?  12  LEU   A CA   1 
ATOM   252  C CA   B LEU   A 1 12  ? 10.109 -15.981 7.573   0.54 17.98 ?  12  LEU   A CA   1 
ATOM   253  C C    A LEU   A 1 12  ? 11.106 -18.002 7.359   0.46 13.55 ?  12  LEU   A C    1 
ATOM   254  C C    B LEU   A 1 12  ? 10.670 -17.387 7.392   0.54 18.16 ?  12  LEU   A C    1 
ATOM   255  O O    A LEU   A 1 12  ? 10.481 -18.886 6.761   0.46 14.51 ?  12  LEU   A O    1 
ATOM   256  O O    B LEU   A 1 12  ? 10.011 -18.249 6.802   0.54 18.90 ?  12  LEU   A O    1 
ATOM   257  C CB   A LEU   A 1 12  ? 11.039 -15.694 6.429   0.46 13.80 ?  12  LEU   A CB   1 
ATOM   258  C CB   B LEU   A 1 12  ? 10.766 -15.021 6.571   0.54 19.23 ?  12  LEU   A CB   1 
ATOM   259  C CG   A LEU   A 1 12  ? 10.399 -14.312 6.245   0.46 14.12 ?  12  LEU   A CG   1 
ATOM   260  C CG   B LEU   A 1 12  ? 10.235 -13.586 6.568   0.54 19.97 ?  12  LEU   A CG   1 
ATOM   261  C CD1  A LEU   A 1 12  ? 11.172 -13.533 5.193   0.46 14.19 ?  12  LEU   A CD1  1 
ATOM   262  C CD1  B LEU   A 1 12  ? 10.848 -12.790 5.425   0.54 20.65 ?  12  LEU   A CD1  1 
ATOM   263  C CD2  A LEU   A 1 12  ? 8.923  -14.410 5.857   0.46 15.57 ?  12  LEU   A CD2  1 
ATOM   264  C CD2  B LEU   A 1 12  ? 8.712  -13.573 6.484   0.54 20.97 ?  12  LEU   A CD2  1 
ATOM   265  H H    A LEU   A 1 12  ? 11.486 -15.617 8.917   0.46 16.06 ?  12  LEU   A H    1 
ATOM   266  H H    B LEU   A 1 12  ? 11.036 -15.138 9.099   0.54 21.40 ?  12  LEU   A H    1 
ATOM   267  H HA   A LEU   A 1 12  ? 9.533  -16.695 7.402   0.46 16.31 ?  12  LEU   A HA   1 
ATOM   268  H HA   B LEU   A 1 12  ? 9.163  -16.018 7.367   0.54 21.59 ?  12  LEU   A HA   1 
ATOM   269  H HB2  A LEU   A 1 12  ? 11.977 -15.545 6.612   0.46 16.57 ?  12  LEU   A HB2  1 
ATOM   270  H HB2  B LEU   A 1 12  ? 11.715 -14.979 6.766   0.54 23.09 ?  12  LEU   A HB2  1 
ATOM   271  H HB3  A LEU   A 1 12  ? 10.946 -16.159 5.587   0.46 16.57 ?  12  LEU   A HB3  1 
ATOM   272  H HB3  B LEU   A 1 12  ? 10.635 -15.378 5.679   0.54 23.09 ?  12  LEU   A HB3  1 
ATOM   273  H HG   A LEU   A 1 12  ? 10.457 -13.822 7.079   0.46 16.96 ?  12  LEU   A HG   1 
ATOM   274  H HG   B LEU   A 1 12  ? 10.492 -13.158 7.402   0.54 23.98 ?  12  LEU   A HG   1 
ATOM   275  H HD11 A LEU   A 1 12  ? 10.763 -12.663 5.079   0.46 17.04 ?  12  LEU   A HD11 1 
ATOM   276  H HD11 B LEU   A 1 12  ? 10.497 -11.886 5.448   0.54 24.79 ?  12  LEU   A HD11 1 
ATOM   277  H HD12 A LEU   A 1 12  ? 12.091 -13.432 5.489   0.46 17.04 ?  12  LEU   A HD12 1 
ATOM   278  H HD12 B LEU   A 1 12  ? 11.812 -12.773 5.533   0.54 24.79 ?  12  LEU   A HD12 1 
ATOM   279  H HD13 A LEU   A 1 12  ? 11.147 -14.024 4.356   0.46 17.04 ?  12  LEU   A HD13 1 
ATOM   280  H HD13 B LEU   A 1 12  ? 10.615 -13.215 4.586   0.54 24.79 ?  12  LEU   A HD13 1 
ATOM   281  H HD21 A LEU   A 1 12  ? 8.573  -13.514 5.716   0.46 18.70 ?  12  LEU   A HD21 1 
ATOM   282  H HD21 B LEU   A 1 12  ? 8.416  -12.671 6.293   0.54 25.18 ?  12  LEU   A HD21 1 
ATOM   283  H HD22 A LEU   A 1 12  ? 8.842  -14.927 5.041   0.46 18.70 ?  12  LEU   A HD22 1 
ATOM   284  H HD22 B LEU   A 1 12  ? 8.432  -14.173 5.776   0.54 25.18 ?  12  LEU   A HD22 1 
ATOM   285  H HD23 A LEU   A 1 12  ? 8.434  -14.843 6.574   0.46 18.70 ?  12  LEU   A HD23 1 
ATOM   286  H HD23 B LEU   A 1 12  ? 8.346  -13.870 7.333   0.54 25.18 ?  12  LEU   A HD23 1 
ATOM   287  N N    A THR   A 1 13  ? 12.313 -18.217 7.874   0.46 13.86 ?  13  THR   A N    1 
ATOM   288  N N    B THR   A 1 13  ? 11.879 -17.630 7.887   0.54 18.70 ?  13  THR   A N    1 
ATOM   289  C CA   A THR   A 1 13  ? 13.000 -19.501 7.780   0.46 14.53 ?  13  THR   A CA   1 
ATOM   290  C CA   B THR   A 1 13  ? 12.524 -18.930 7.801   0.54 18.68 ?  13  THR   A CA   1 
ATOM   291  C C    A THR   A 1 13  ? 13.767 -19.722 9.075   0.46 14.81 ?  13  THR   A C    1 
ATOM   292  C C    B THR   A 1 13  ? 13.218 -19.195 9.129   0.54 18.63 ?  13  THR   A C    1 
ATOM   293  O O    A THR   A 1 13  ? 13.694 -18.924 10.015  0.46 14.47 ?  13  THR   A O    1 
ATOM   294  O O    B THR   A 1 13  ? 13.024 -18.475 10.115  0.54 19.03 ?  13  THR   A O    1 
ATOM   295  C CB   A THR   A 1 13  ? 13.967 -19.574 6.586   0.46 15.98 ?  13  THR   A CB   1 
ATOM   296  C CB   B THR   A 1 13  ? 13.557 -18.980 6.666   0.54 18.01 ?  13  THR   A CB   1 
ATOM   297  O OG1  A THR   A 1 13  ? 15.052 -18.663 6.791   0.46 16.09 ?  13  THR   A OG1  1 
ATOM   298  O OG1  B THR   A 1 13  ? 14.648 -18.109 6.988   0.54 18.96 ?  13  THR   A OG1  1 
ATOM   299  C CG2  A THR   A 1 13  ? 13.280 -19.243 5.269   0.46 16.49 ?  13  THR   A CG2  1 
ATOM   300  C CG2  B THR   A 1 13  ? 12.946 -18.586 5.323   0.54 17.65 ?  13  THR   A CG2  1 
ATOM   301  H H    A THR   A 1 13  ? 12.772 -17.614 8.284   0.46 16.65 ?  13  THR   A H    1 
ATOM   302  H H    B THR   A 1 13  ? 12.359 -17.035 8.282   0.54 22.46 ?  13  THR   A H    1 
ATOM   303  H HA   A THR   A 1 13  ? 12.346 -20.208 7.679   0.46 17.45 ?  13  THR   A HA   1 
ATOM   304  H HA   B THR   A 1 13  ? 11.860 -19.617 7.639   0.54 22.43 ?  13  THR   A HA   1 
ATOM   305  H HB   A THR   A 1 13  ? 14.328 -20.474 6.521   0.46 19.19 ?  13  THR   A HB   1 
ATOM   306  H HB   B THR   A 1 13  ? 13.900 -19.879 6.578   0.54 21.63 ?  13  THR   A HB   1 
ATOM   307  H HG1  A THR   A 1 13  ? 15.592 -18.696 6.139   0.46 19.33 ?  13  THR   A HG1  1 
ATOM   308  H HG1  B THR   A 1 13  ? 15.217 -18.107 6.367   0.54 22.77 ?  13  THR   A HG1  1 
ATOM   309  H HG21 A THR   A 1 13  ? 13.905 -19.369 4.531   0.46 19.80 ?  13  THR   A HG21 1 
ATOM   310  H HG21 B THR   A 1 13  ? 13.612 -18.670 4.619   0.54 21.20 ?  13  THR   A HG21 1 
ATOM   311  H HG22 A THR   A 1 13  ? 12.522 -19.829 5.138   0.46 19.80 ?  13  THR   A HG22 1 
ATOM   312  H HG22 B THR   A 1 13  ? 12.199 -19.169 5.117   0.54 21.20 ?  13  THR   A HG22 1 
ATOM   313  H HG23 A THR   A 1 13  ? 12.981 -18.324 5.272   0.46 19.80 ?  13  THR   A HG23 1 
ATOM   314  H HG23 B THR   A 1 13  ? 12.635 -17.670 5.352   0.54 21.20 ?  13  THR   A HG23 1 
ATOM   315  N N    A ASP   A 1 14  ? 14.548 -20.801 9.100   0.46 15.14 ?  14  ASP   A N    1 
ATOM   316  N N    B ASP   A 1 14  ? 14.072 -20.217 9.133   0.54 19.10 ?  14  ASP   A N    1 
ATOM   317  C CA   A ASP   A 1 14  ? 15.391 -21.080 10.253  0.46 16.31 ?  14  ASP   A CA   1 
ATOM   318  C CA   B ASP   A 1 14  ? 14.811 -20.553 10.342  0.54 20.44 ?  14  ASP   A CA   1 
ATOM   319  C C    A ASP   A 1 14  ? 16.273 -19.896 10.616  0.46 15.18 ?  14  ASP   A C    1 
ATOM   320  C C    B ASP   A 1 14  ? 15.683 -19.390 10.805  0.54 18.98 ?  14  ASP   A C    1 
ATOM   321  O O    A ASP   A 1 14  ? 16.545 -19.677 11.803  0.46 15.03 ?  14  ASP   A O    1 
ATOM   322  O O    B ASP   A 1 14  ? 15.827 -19.159 12.011  0.54 20.10 ?  14  ASP   A O    1 
ATOM   323  C CB   A ASP   A 1 14  ? 16.283 -22.286 9.980   0.46 19.05 ?  14  ASP   A CB   1 
ATOM   324  C CB   B ASP   A 1 14  ? 15.670 -21.788 10.089  0.54 23.62 ?  14  ASP   A CB   1 
ATOM   325  C CG   A ASP   A 1 14  ? 17.285 -22.514 11.083  0.46 21.39 ?  14  ASP   A CG   1 
ATOM   326  C CG   B ASP   A 1 14  ? 16.534 -22.154 11.283  0.54 27.03 ?  14  ASP   A CG   1 
ATOM   327  O OD1  A ASP   A 1 14  ? 16.870 -22.950 12.178  0.46 21.95 ?  14  ASP   A OD1  1 
ATOM   328  O OD1  B ASP   A 1 14  ? 16.032 -22.100 12.426  0.54 28.66 ?  14  ASP   A OD1  1 
ATOM   329  O OD2  A ASP   A 1 14  ? 18.485 -22.237 10.856  0.46 22.86 -1 14  ASP   A OD2  1 
ATOM   330  O OD2  B ASP   A 1 14  ? 17.706 -22.528 11.079  0.54 28.30 -1 14  ASP   A OD2  1 
ATOM   331  H H    A ASP   A 1 14  ? 14.622 -21.372 8.462   0.46 18.18 ?  14  ASP   A H    1 
ATOM   332  H H    B ASP   A 1 14  ? 14.246 -20.715 8.453   0.54 22.93 ?  14  ASP   A H    1 
ATOM   333  H HA   A ASP   A 1 14  ? 14.831 -21.279 11.018  0.46 19.58 ?  14  ASP   A HA   1 
ATOM   334  H HA   B ASP   A 1 14  ? 14.175 -20.758 11.044  0.54 24.54 ?  14  ASP   A HA   1 
ATOM   335  H HB2  A ASP   A 1 14  ? 15.725 -23.080 9.907   0.46 22.88 ?  14  ASP   A HB2  1 
ATOM   336  H HB2  B ASP   A 1 14  ? 15.086 -22.539 9.899   0.54 28.36 ?  14  ASP   A HB2  1 
ATOM   337  H HB3  A ASP   A 1 14  ? 16.772 -22.146 9.160   0.46 22.88 ?  14  ASP   A HB3  1 
ATOM   338  H HB3  B ASP   A 1 14  ? 16.247 -21.615 9.329   0.54 28.36 ?  14  ASP   A HB3  1 
ATOM   339  N N    A ASN   A 1 15  ? 16.733 -19.124 9.623   0.46 14.96 ?  15  ASN   A N    1 
ATOM   340  N N    B ASN   A 1 15  ? 16.273 -18.645 9.868   0.54 17.21 ?  15  ASN   A N    1 
ATOM   341  C CA   A ASN   A 1 15  ? 17.720 -18.078 9.876   0.46 14.54 ?  15  ASN   A CA   1 
ATOM   342  C CA   B ASN   A 1 15  ? 17.269 -17.633 10.210  0.54 17.05 ?  15  ASN   A CA   1 
ATOM   343  C C    A ASN   A 1 15  ? 17.359 -16.689 9.360   0.46 15.02 ?  15  ASN   A C    1 
ATOM   344  C C    B ASN   A 1 15  ? 16.943 -16.232 9.711   0.54 16.37 ?  15  ASN   A C    1 
ATOM   345  O O    A ASN   A 1 15  ? 18.150 -15.763 9.562   0.46 15.98 ?  15  ASN   A O    1 
ATOM   346  O O    B ASN   A 1 15  ? 17.726 -15.312 9.972   0.54 16.54 ?  15  ASN   A O    1 
ATOM   347  C CB   A ASN   A 1 15  ? 19.091 -18.468 9.300   0.46 14.09 ?  15  ASN   A CB   1 
ATOM   348  C CB   B ASN   A 1 15  ? 18.658 -18.036 9.692   0.54 17.52 ?  15  ASN   A CB   1 
ATOM   349  C CG   A ASN   A 1 15  ? 19.090 -18.524 7.784   0.46 14.92 ?  15  ASN   A CG   1 
ATOM   350  C CG   B ASN   A 1 15  ? 18.700 -18.193 8.182   0.54 18.13 ?  15  ASN   A CG   1 
ATOM   351  O OD1  A ASN   A 1 15  ? 18.413 -19.361 7.181   0.46 16.16 ?  15  ASN   A OD1  1 
ATOM   352  O OD1  B ASN   A 1 15  ? 17.964 -18.999 7.607   0.54 17.81 ?  15  ASN   A OD1  1 
ATOM   353  N ND2  A ASN   A 1 15  ? 19.860 -17.635 7.159   0.46 14.79 ?  15  ASN   A ND2  1 
ATOM   354  N ND2  B ASN   A 1 15  ? 19.565 -17.416 7.529   0.54 18.22 ?  15  ASN   A ND2  1 
ATOM   355  H H    A ASN   A 1 15  ? 16.500 -19.196 8.799   0.46 17.96 ?  15  ASN   A H    1 
ATOM   356  H H    B ASN   A 1 15  ? 16.108 -18.702 9.029   0.54 20.66 ?  15  ASN   A H    1 
ATOM   357  H HA   A ASN   A 1 15  ? 17.842 -18.007 10.834  0.46 17.46 ?  15  ASN   A HA   1 
ATOM   358  H HA   B ASN   A 1 15  ? 17.333 -17.588 11.177  0.54 20.47 ?  15  ASN   A HA   1 
ATOM   359  H HB2  A ASN   A 1 15  ? 19.754 -17.806 9.578   0.46 16.92 ?  15  ASN   A HB2  1 
ATOM   360  H HB2  B ASN   A 1 15  ? 19.298 -17.349 9.943   0.54 21.04 ?  15  ASN   A HB2  1 
ATOM   361  H HB3  A ASN   A 1 15  ? 19.347 -19.342 9.636   0.46 16.92 ?  15  ASN   A HB3  1 
ATOM   362  H HB3  B ASN   A 1 15  ? 18.913 -18.883 10.092  0.54 21.04 ?  15  ASN   A HB3  1 
ATOM   363  H HD21 A ASN   A 1 15  ? 19.898 -17.630 6.301   0.46 17.76 ?  15  ASN   A HD21 1 
ATOM   364  H HD21 B ASN   A 1 15  ? 19.633 -17.467 6.672   0.54 21.88 ?  15  ASN   A HD21 1 
ATOM   365  H HD22 A ASN   A 1 15  ? 20.322 -17.064 7.611   0.46 17.76 ?  15  ASN   A HD22 1 
ATOM   366  H HD22 B ASN   A 1 15  ? 20.062 -16.858 7.962   0.54 21.88 ?  15  ASN   A HD22 1 
ATOM   367  N N    A VAL   A 1 16  ? 16.213 -16.508 8.706   0.46 14.33 ?  16  VAL   A N    1 
ATOM   368  N N    B VAL   A 1 16  ? 15.826 -16.033 9.018   0.54 16.20 ?  16  VAL   A N    1 
ATOM   369  C CA   A VAL   A 1 16  ? 15.823 -15.224 8.132   0.46 14.42 ?  16  VAL   A CA   1 
ATOM   370  C CA   B VAL   A 1 16  ? 15.473 -14.740 8.441   0.54 16.16 ?  16  VAL   A CA   1 
ATOM   371  C C    A VAL   A 1 16  ? 14.566 -14.710 8.823   0.46 13.77 ?  16  VAL   A C    1 
ATOM   372  C C    B VAL   A 1 16  ? 14.188 -14.230 9.086   0.54 16.43 ?  16  VAL   A C    1 
ATOM   373  O O    A VAL   A 1 16  ? 13.559 -15.426 8.915   0.46 13.32 ?  16  VAL   A O    1 
ATOM   374  O O    B VAL   A 1 16  ? 13.153 -14.910 9.057   0.54 16.65 ?  16  VAL   A O    1 
ATOM   375  C CB   A VAL   A 1 16  ? 15.624 -15.308 6.608   0.46 15.17 ?  16  VAL   A CB   1 
ATOM   376  C CB   B VAL   A 1 16  ? 15.331 -14.811 6.914   0.54 16.23 ?  16  VAL   A CB   1 
ATOM   377  C CG1  A VAL   A 1 16  ? 15.232 -13.946 6.044   0.46 15.49 ?  16  VAL   A CG1  1 
ATOM   378  C CG1  B VAL   A 1 16  ? 15.050 -13.426 6.355   0.54 16.62 ?  16  VAL   A CG1  1 
ATOM   379  C CG2  A VAL   A 1 16  ? 16.894 -15.825 5.939   0.46 15.96 ?  16  VAL   A CG2  1 
ATOM   380  C CG2  B VAL   A 1 16  ? 16.587 -15.397 6.279   0.54 17.10 ?  16  VAL   A CG2  1 
ATOM   381  H H    A VAL   A 1 16  ? 15.644 -17.138 8.565   0.46 17.21 ?  16  VAL   A H    1 
ATOM   382  H H    B VAL   A 1 16  ? 15.246 -16.648 8.863   0.54 19.45 ?  16  VAL   A H    1 
ATOM   383  H HA   A VAL   A 1 16  ? 16.532 -14.585 8.299   0.46 17.32 ?  16  VAL   A HA   1 
ATOM   384  H HA   B VAL   A 1 16  ? 16.177 -14.103 8.641   0.54 19.41 ?  16  VAL   A HA   1 
ATOM   385  H HB   A VAL   A 1 16  ? 14.910 -15.933 6.419   0.46 18.21 ?  16  VAL   A HB   1 
ATOM   386  H HB   B VAL   A 1 16  ? 14.585 -15.387 6.689   0.54 19.50 ?  16  VAL   A HB   1 
ATOM   387  H HG11 A VAL   A 1 16  ? 15.282 -13.983 5.076   0.46 18.60 ?  16  VAL   A HG11 1 
ATOM   388  H HG11 B VAL   A 1 16  ? 15.121 -13.455 5.389   0.54 19.96 ?  16  VAL   A HG11 1 
ATOM   389  H HG12 A VAL   A 1 16  ? 14.327 -13.736 6.320   0.46 18.60 ?  16  VAL   A HG12 1 
ATOM   390  H HG12 B VAL   A 1 16  ? 14.156 -13.156 6.613   0.54 19.96 ?  16  VAL   A HG12 1 
ATOM   391  H HG13 A VAL   A 1 16  ? 15.847 -13.275 6.380   0.46 18.60 ?  16  VAL   A HG13 1 
ATOM   392  H HG13 B VAL   A 1 16  ? 15.702 -12.803 6.715   0.54 19.96 ?  16  VAL   A HG13 1 
ATOM   393  H HG21 A VAL   A 1 16  ? 16.806 -15.726 4.979   0.46 19.17 ?  16  VAL   A HG21 1 
ATOM   394  H HG21 B VAL   A 1 16  ? 16.591 -15.192 5.330   0.54 20.53 ?  16  VAL   A HG21 1 
ATOM   395  H HG22 A VAL   A 1 16  ? 17.653 -15.309 6.256   0.46 19.17 ?  16  VAL   A HG22 1 
ATOM   396  H HG22 B VAL   A 1 16  ? 17.367 -15.012 6.704   0.54 20.53 ?  16  VAL   A HG22 1 
ATOM   397  H HG23 A VAL   A 1 16  ? 17.016 -16.761 6.166   0.46 19.17 ?  16  VAL   A HG23 1 
ATOM   398  H HG23 B VAL   A 1 16  ? 16.586 -16.359 6.408   0.54 20.53 ?  16  VAL   A HG23 1 
ATOM   399  N N    A TYR   A 1 17  ? 14.630 -13.453 9.278   0.46 13.25 ?  17  TYR   A N    1 
ATOM   400  N N    B TYR   A 1 17  ? 14.257 -13.019 9.639   0.54 16.54 ?  17  TYR   A N    1 
ATOM   401  C CA   A TYR   A 1 17  ? 13.552 -12.754 9.964   0.46 13.28 ?  17  TYR   A CA   1 
ATOM   402  C CA   B TYR   A 1 17  ? 13.146 -12.331 10.283  0.54 16.86 ?  17  TYR   A CA   1 
ATOM   403  C C    A TYR   A 1 17  ? 13.276 -11.447 9.233   0.46 14.28 ?  17  TYR   A C    1 
ATOM   404  C C    B TYR   A 1 17  ? 12.967 -10.970 9.628   0.54 15.65 ?  17  TYR   A C    1 
ATOM   405  O O    A TYR   A 1 17  ? 14.166 -10.894 8.587   0.46 14.08 ?  17  TYR   A O    1 
ATOM   406  O O    B TYR   A 1 17  ? 13.922 -10.400 9.097   0.54 15.66 ?  17  TYR   A O    1 
ATOM   407  C CB   A TYR   A 1 17  ? 13.952 -12.458 11.429  0.46 13.10 ?  17  TYR   A CB   1 
ATOM   408  C CB   B TYR   A 1 17  ? 13.426 -12.145 11.781  0.54 18.39 ?  17  TYR   A CB   1 
ATOM   409  C CG   A TYR   A 1 17  ? 14.119 -13.721 12.251  0.46 13.11 ?  17  TYR   A CG   1 
ATOM   410  C CG   B TYR   A 1 17  ? 13.212 -13.399 12.606  0.54 20.08 ?  17  TYR   A CG   1 
ATOM   411  C CD1  A TYR   A 1 17  ? 15.289 -14.470 12.179  0.46 14.50 ?  17  TYR   A CD1  1 
ATOM   412  C CD1  B TYR   A 1 17  ? 14.126 -14.438 12.579  0.54 21.00 ?  17  TYR   A CD1  1 
ATOM   413  C CD2  A TYR   A 1 17  ? 13.094 -14.181 13.079  0.46 13.81 ?  17  TYR   A CD2  1 
ATOM   414  C CD2  B TYR   A 1 17  ? 12.093 -13.534 13.418  0.54 20.16 ?  17  TYR   A CD2  1 
ATOM   415  C CE1  A TYR   A 1 17  ? 15.441 -15.643 12.913  0.46 14.61 ?  17  TYR   A CE1  1 
ATOM   416  C CE1  B TYR   A 1 17  ? 13.924 -15.586 13.332  0.54 21.09 ?  17  TYR   A CE1  1 
ATOM   417  C CE2  A TYR   A 1 17  ? 13.239 -15.355 13.814  0.46 14.97 ?  17  TYR   A CE2  1 
ATOM   418  C CE2  B TYR   A 1 17  ? 11.888 -14.675 14.175  0.54 19.98 ?  17  TYR   A CE2  1 
ATOM   419  C CZ   A TYR   A 1 17  ? 14.413 -16.082 13.730  0.46 14.98 ?  17  TYR   A CZ   1 
ATOM   420  C CZ   B TYR   A 1 17  ? 12.806 -15.698 14.128  0.54 20.41 ?  17  TYR   A CZ   1 
ATOM   421  O OH   A TYR   A 1 17  ? 14.548 -17.237 14.469  0.46 15.68 ?  17  TYR   A OH   1 
ATOM   422  O OH   B TYR   A 1 17  ? 12.602 -16.837 14.880  0.54 20.78 ?  17  TYR   A OH   1 
ATOM   423  H H    A TYR   A 1 17  ? 15.337 -12.959 9.190   0.46 15.91 ?  17  TYR   A H    1 
ATOM   424  H H    B TYR   A 1 17  ? 14.981 -12.551 9.647   0.54 19.86 ?  17  TYR   A H    1 
ATOM   425  H HA   A TYR   A 1 17  ? 12.752 -13.297 9.958   0.46 15.95 ?  17  TYR   A HA   1 
ATOM   426  H HA   B TYR   A 1 17  ? 12.329 -12.836 10.175  0.54 20.25 ?  17  TYR   A HA   1 
ATOM   427  H HB2  A TYR   A 1 17  ? 14.795 -11.977 11.437  0.46 15.74 ?  17  TYR   A HB2  1 
ATOM   428  H HB2  B TYR   A 1 17  ? 14.345 -11.858 11.896  0.54 22.08 ?  17  TYR   A HB2  1 
ATOM   429  H HB3  A TYR   A 1 17  ? 13.259 -11.915 11.838  0.46 15.74 ?  17  TYR   A HB3  1 
ATOM   430  H HB3  B TYR   A 1 17  ? 12.837 -11.462 12.118  0.54 22.08 ?  17  TYR   A HB3  1 
ATOM   431  H HD1  A TYR   A 1 17  ? 15.978 -14.181 11.629  0.46 17.41 ?  17  TYR   A HD1  1 
ATOM   432  H HD1  B TYR   A 1 17  ? 14.884 -14.369 12.042  0.54 25.22 ?  17  TYR   A HD1  1 
ATOM   433  H HD2  A TYR   A 1 17  ? 12.297 -13.697 13.138  0.46 16.59 ?  17  TYR   A HD2  1 
ATOM   434  H HD2  B TYR   A 1 17  ? 11.468 -12.843 13.449  0.54 24.20 ?  17  TYR   A HD2  1 
ATOM   435  H HE1  A TYR   A 1 17  ? 16.231 -16.134 12.857  0.46 17.55 ?  17  TYR   A HE1  1 
ATOM   436  H HE1  B TYR   A 1 17  ? 14.544 -16.275 13.306  0.54 25.32 ?  17  TYR   A HE1  1 
ATOM   437  H HE2  A TYR   A 1 17  ? 12.549 -15.645 14.364  0.46 17.98 ?  17  TYR   A HE2  1 
ATOM   438  H HE2  B TYR   A 1 17  ? 11.131 -14.748 14.710  0.54 23.99 ?  17  TYR   A HE2  1 
ATOM   439  H HH   A TYR   A 1 17  ? 15.310 -17.568 14.341  0.46 18.83 ?  17  TYR   A HH   1 
ATOM   440  H HH   B TYR   A 1 17  ? 11.884 -16.761 15.314  0.54 24.95 ?  17  TYR   A HH   1 
ATOM   441  N N    A ILE   A 1 18  ? 12.044 -10.937 9.337   0.46 15.04 ?  18  ILE   A N    1 
ATOM   442  N N    B ILE   A 1 18  ? 11.744 -10.432 9.674   0.54 14.39 ?  18  ILE   A N    1 
ATOM   443  C CA   A ILE   A 1 18  ? 11.654 -9.738  8.598   0.46 15.33 ?  18  ILE   A CA   1 
ATOM   444  C CA   B ILE   A 1 18  ? 11.425 -9.227  8.914   0.54 14.82 ?  18  ILE   A CA   1 
ATOM   445  C C    A ILE   A 1 18  ? 10.685 -8.901  9.426   0.46 16.07 ?  18  ILE   A C    1 
ATOM   446  C C    B ILE   A 1 18  ? 10.487 -8.321  9.704   0.54 15.53 ?  18  ILE   A C    1 
ATOM   447  O O    A ILE   A 1 18  ? 9.892  -9.431  10.209  0.46 15.95 ?  18  ILE   A O    1 
ATOM   448  O O    B ILE   A 1 18  ? 9.633  -8.789  10.461  0.54 16.21 ?  18  ILE   A O    1 
ATOM   449  C CB   A ILE   A 1 18  ? 11.061 -10.100 7.215   0.46 14.84 ?  18  ILE   A CB   1 
ATOM   450  C CB   B ILE   A 1 18  ? 10.860 -9.599  7.524   0.54 15.65 ?  18  ILE   A CB   1 
ATOM   451  C CG1  A ILE   A 1 18  ? 10.945 -8.858  6.329   0.46 16.37 ?  18  ILE   A CG1  1 
ATOM   452  C CG1  B ILE   A 1 18  ? 10.888 -8.401  6.579   0.54 17.29 ?  18  ILE   A CG1  1 
ATOM   453  C CG2  A ILE   A 1 18  ? 9.708  -10.805 7.368   0.46 14.58 ?  18  ILE   A CG2  1 
ATOM   454  C CG2  B ILE   A 1 18  ? 9.441  -10.143 7.640   0.54 16.99 ?  18  ILE   A CG2  1 
ATOM   455  C CD1  A ILE   A 1 18  ? 10.596 -9.170  4.888   0.46 17.80 ?  18  ILE   A CD1  1 
ATOM   456  C CD1  B ILE   A 1 18  ? 10.883 -8.804  5.119   0.54 18.04 ?  18  ILE   A CD1  1 
ATOM   457  H H    A ILE   A 1 18  ? 11.425 -11.267 9.831   0.46 18.07 ?  18  ILE   A H    1 
ATOM   458  H H    B ILE   A 1 18  ? 11.091 -10.743 10.141  0.54 17.29 ?  18  ILE   A H    1 
ATOM   459  H HA   A ILE   A 1 18  ? 12.445 -9.197  8.446   0.46 18.42 ?  18  ILE   A HA   1 
ATOM   460  H HA   B ILE   A 1 18  ? 12.240 -8.729  8.771   0.54 17.80 ?  18  ILE   A HA   1 
ATOM   461  H HB   A ILE   A 1 18  ? 11.673 -10.716 6.786   0.46 17.83 ?  18  ILE   A HB   1 
ATOM   462  H HB   B ILE   A 1 18  ? 11.421 -10.295 7.154   0.54 18.80 ?  18  ILE   A HB   1 
ATOM   463  H HG12 A ILE   A 1 18  ? 10.256 -8.279  6.684   0.46 19.66 ?  18  ILE   A HG12 1 
ATOM   464  H HG12 B ILE   A 1 18  ? 10.107 -7.852  6.741   0.54 20.77 ?  18  ILE   A HG12 1 
ATOM   465  H HG13 A ILE   A 1 18  ? 11.800 -8.391  6.331   0.46 19.66 ?  18  ILE   A HG13 1 
ATOM   466  H HG13 B ILE   A 1 18  ? 11.695 -7.889  6.744   0.54 20.77 ?  18  ILE   A HG13 1 
ATOM   467  H HG21 A ILE   A 1 18  ? 9.456  -11.187 6.511   0.46 17.51 ?  18  ILE   A HG21 1 
ATOM   468  H HG21 B ILE   A 1 18  ? 9.179  -10.512 6.782   0.54 20.40 ?  18  ILE   A HG21 1 
ATOM   469  H HG22 A ILE   A 1 18  ? 9.793  -11.509 8.029   0.46 17.51 ?  18  ILE   A HG22 1 
ATOM   470  H HG22 B ILE   A 1 18  ? 9.423  -10.834 8.318   0.54 20.40 ?  18  ILE   A HG22 1 
ATOM   471  H HG23 A ILE   A 1 18  ? 9.043  -10.161 7.651   0.46 17.51 ?  18  ILE   A HG23 1 
ATOM   472  H HG23 B ILE   A 1 18  ? 8.842  -9.421  7.885   0.54 20.40 ?  18  ILE   A HG23 1 
ATOM   473  H HD11 A ILE   A 1 18  ? 10.602 -8.345  4.376   0.46 21.38 ?  18  ILE   A HD11 1 
ATOM   474  H HD11 B ILE   A 1 18  ? 10.905 -8.007  4.570   0.54 21.66 ?  18  ILE   A HD11 1 
ATOM   475  H HD12 A ILE   A 1 18  ? 11.255 -9.785  4.528   0.46 21.38 ?  18  ILE   A HD12 1 
ATOM   476  H HD12 B ILE   A 1 18  ? 11.664 -9.353  4.939   0.54 21.66 ?  18  ILE   A HD12 1 
ATOM   477  H HD13 A ILE   A 1 18  ? 9.715  -9.572  4.857   0.46 21.38 ?  18  ILE   A HD13 1 
ATOM   478  H HD13 B ILE   A 1 18  ? 10.076 -9.313  4.934   0.54 21.66 ?  18  ILE   A HD13 1 
ATOM   479  N N    A LYS   A 1 19  ? 10.749 -7.577  9.236   0.46 17.16 ?  19  LYS   A N    1 
ATOM   480  N N    B LYS   A 1 19  ? 10.654 -7.007  9.518   0.54 15.08 ?  19  LYS   A N    1 
ATOM   481  C CA   A LYS   A 1 19  ? 9.957  -6.622  10.006  0.46 17.89 ?  19  LYS   A CA   1 
ATOM   482  C CA   B LYS   A 1 19  ? 9.865  -6.007  10.230  0.54 15.03 ?  19  LYS   A CA   1 
ATOM   483  C C    A LYS   A 1 19  ? 9.760  -5.352  9.184   0.46 18.27 ?  19  LYS   A C    1 
ATOM   484  C C    B LYS   A 1 19  ? 9.648  -4.794  9.332   0.54 15.55 ?  19  LYS   A C    1 
ATOM   485  O O    A LYS   A 1 19  ? 10.617 -4.982  8.377   0.46 18.53 ?  19  LYS   A O    1 
ATOM   486  O O    B LYS   A 1 19  ? 10.537 -4.414  8.566   0.54 15.67 ?  19  LYS   A O    1 
ATOM   487  C CB   A LYS   A 1 19  ? 10.662 -6.298  11.336  0.46 18.49 ?  19  LYS   A CB   1 
ATOM   488  C CB   B LYS   A 1 19  ? 10.581 -5.581  11.520  0.54 14.91 ?  19  LYS   A CB   1 
ATOM   489  C CG   A LYS   A 1 19  ? 9.998  -5.251  12.237  0.46 19.13 ?  19  LYS   A CG   1 
ATOM   490  C CG   B LYS   A 1 19  ? 9.774  -4.661  12.419  0.54 17.03 ?  19  LYS   A CG   1 
ATOM   491  C CD   A LYS   A 1 19  ? 10.825 -5.047  13.512  0.46 19.85 ?  19  LYS   A CD   1 
ATOM   492  C CD   B LYS   A 1 19  ? 10.556 -4.317  13.674  0.54 18.44 ?  19  LYS   A CD   1 
ATOM   493  C CE   A LYS   A 1 19  ? 10.218 -4.025  14.470  0.46 20.49 ?  19  LYS   A CE   1 
ATOM   494  C CE   B LYS   A 1 19  ? 9.783  -3.353  14.565  0.54 19.93 ?  19  LYS   A CE   1 
ATOM   495  N NZ   A LYS   A 1 19  ? 11.043 -3.889  15.710  0.46 20.50 ?  19  LYS   A NZ   1 
ATOM   496  N NZ   B LYS   A 1 19  ? 10.528 -3.017  15.811  0.54 21.23 ?  19  LYS   A NZ   1 
ATOM   497  H H    A LYS   A 1 19  ? 11.263 -7.203  8.658   0.46 20.61 ?  19  LYS   A H    1 
ATOM   498  H H    B LYS   A 1 19  ? 11.235 -6.657  8.977   0.54 18.11 ?  19  LYS   A H    1 
ATOM   499  H HA   A LYS   A 1 19  ? 9.089  -6.996  10.202  0.46 21.49 ?  19  LYS   A HA   1 
ATOM   500  H HA   B LYS   A 1 19  ? 9.003  -6.371  10.464  0.54 18.05 ?  19  LYS   A HA   1 
ATOM   501  H HB2  A LYS   A 1 19  ? 10.720 -7.116  11.852  0.46 22.20 ?  19  LYS   A HB2  1 
ATOM   502  H HB2  B LYS   A 1 19  ? 10.794 -6.376  12.036  0.54 17.91 ?  19  LYS   A HB2  1 
ATOM   503  H HB3  A LYS   A 1 19  ? 11.556 -5.977  11.141  0.46 22.20 ?  19  LYS   A HB3  1 
ATOM   504  H HB3  B LYS   A 1 19  ? 11.402 -5.115  11.290  0.54 17.91 ?  19  LYS   A HB3  1 
ATOM   505  H HG2  A LYS   A 1 19  ? 9.944  -4.401  11.773  0.46 22.97 ?  19  LYS   A HG2  1 
ATOM   506  H HG2  B LYS   A 1 19  ? 9.577  -3.838  11.947  0.54 20.45 ?  19  LYS   A HG2  1 
ATOM   507  H HG3  A LYS   A 1 19  ? 9.113  -5.553  12.496  0.46 22.97 ?  19  LYS   A HG3  1 
ATOM   508  H HG3  B LYS   A 1 19  ? 8.953  -5.106  12.682  0.54 20.45 ?  19  LYS   A HG3  1 
ATOM   509  H HD2  A LYS   A 1 19  ? 10.893 -5.891  13.984  0.46 23.84 ?  19  LYS   A HD2  1 
ATOM   510  H HD2  B LYS   A 1 19  ? 10.725 -5.128  14.180  0.54 22.14 ?  19  LYS   A HD2  1 
ATOM   511  H HD3  A LYS   A 1 19  ? 11.711 -4.734  13.267  0.46 23.84 ?  19  LYS   A HD3  1 
ATOM   512  H HD3  B LYS   A 1 19  ? 11.395 -3.896  13.425  0.54 22.14 ?  19  LYS   A HD3  1 
ATOM   513  H HE2  A LYS   A 1 19  ? 10.182 -3.157  14.036  0.46 24.60 ?  19  LYS   A HE2  1 
ATOM   514  H HE2  B LYS   A 1 19  ? 9.626  -2.529  14.075  0.54 23.93 ?  19  LYS   A HE2  1 
ATOM   515  H HE3  A LYS   A 1 19  ? 9.330  -4.311  14.728  0.46 24.60 ?  19  LYS   A HE3  1 
ATOM   516  H HE3  B LYS   A 1 19  ? 8.940  -3.758  14.814  0.54 23.93 ?  19  LYS   A HE3  1 
ATOM   517  H HZ1  A LYS   A 1 19  ? 10.684 -3.282  16.251  0.46 24.62 ?  19  LYS   A HZ1  1 
ATOM   518  H HZ1  B LYS   A 1 19  ? 10.046 -2.454  16.307  0.54 25.49 ?  19  LYS   A HZ1  1 
ATOM   519  H HZ2  A LYS   A 1 19  ? 11.081 -4.670  16.136  0.46 24.62 ?  19  LYS   A HZ2  1 
ATOM   520  H HZ2  B LYS   A 1 19  ? 10.680 -3.756  16.281  0.54 25.49 ?  19  LYS   A HZ2  1 
ATOM   521  H HZ3  A LYS   A 1 19  ? 11.870 -3.636  15.499  0.46 24.62 ?  19  LYS   A HZ3  1 
ATOM   522  H HZ3  B LYS   A 1 19  ? 11.303 -2.633  15.609  0.54 25.49 ?  19  LYS   A HZ3  1 
ATOM   523  N N    A ASN   A 1 20  ? 8.615  -4.694  9.384   0.46 19.84 ?  20  ASN   A N    1 
ATOM   524  N N    B ASN   A 1 20  ? 8.459  -4.190  9.428   0.54 15.49 ?  20  ASN   A N    1 
ATOM   525  C CA   A ASN   A 1 20  ? 8.376  -3.365  8.821   0.46 20.59 ?  20  ASN   A CA   1 
ATOM   526  C CA   B ASN   A 1 20  ? 8.168  -2.917  8.763   0.54 16.81 ?  20  ASN   A CA   1 
ATOM   527  C C    A ASN   A 1 20  ? 9.005  -2.339  9.757   0.46 20.50 ?  20  ASN   A C    1 
ATOM   528  C C    B ASN   A 1 20  ? 8.724  -1.809  9.643   0.54 18.20 ?  20  ASN   A C    1 
ATOM   529  O O    A ASN   A 1 20  ? 8.495  -2.100  10.858  0.46 20.66 ?  20  ASN   A O    1 
ATOM   530  O O    B ASN   A 1 20  ? 8.068  -1.365  10.591  0.54 18.51 ?  20  ASN   A O    1 
ATOM   531  C CB   A ASN   A 1 20  ? 6.875  -3.126  8.655   0.46 21.30 ?  20  ASN   A CB   1 
ATOM   532  C CB   B ASN   A 1 20  ? 6.663  -2.753  8.569   0.54 17.38 ?  20  ASN   A CB   1 
ATOM   533  C CG   A ASN   A 1 20  ? 6.538  -1.690  8.269   0.46 21.79 ?  20  ASN   A CG   1 
ATOM   534  C CG   B ASN   A 1 20  ? 6.281  -1.471  7.837   0.54 17.73 ?  20  ASN   A CG   1 
ATOM   535  O OD1  A ASN   A 1 20  ? 5.609  -1.092  8.824   0.46 22.67 ?  20  ASN   A OD1  1 
ATOM   536  O OD1  B ASN   A 1 20  ? 5.106  -1.112  7.823   0.54 17.78 ?  20  ASN   A OD1  1 
ATOM   537  N ND2  A ASN   A 1 20  ? 7.277  -1.134  7.311   0.46 22.34 ?  20  ASN   A ND2  1 
ATOM   538  N ND2  B ASN   A 1 20  ? 7.243  -0.792  7.224   0.54 18.22 ?  20  ASN   A ND2  1 
ATOM   539  H H    A ASN   A 1 20  ? 7.953  -5.001  9.841   0.46 23.83 ?  20  ASN   A H    1 
ATOM   540  H H    B ASN   A 1 20  ? 7.797  -4.505  9.868   0.54 18.60 ?  20  ASN   A H    1 
ATOM   541  H HA   A ASN   A 1 20  ? 8.795  -3.294  7.952   0.46 24.72 ?  20  ASN   A HA   1 
ATOM   542  H HA   B ASN   A 1 20  ? 8.606  -2.886  7.900   0.54 20.18 ?  20  ASN   A HA   1 
ATOM   543  H HB2  A ASN   A 1 20  ? 6.534  -3.707  7.957   0.46 25.58 ?  20  ASN   A HB2  1 
ATOM   544  H HB2  B ASN   A 1 20  ? 6.326  -3.504  8.056   0.54 20.87 ?  20  ASN   A HB2  1 
ATOM   545  H HB3  A ASN   A 1 20  ? 6.426  -3.318  9.493   0.46 25.58 ?  20  ASN   A HB3  1 
ATOM   546  H HB3  B ASN   A 1 20  ? 6.232  -2.735  9.436   0.54 20.87 ?  20  ASN   A HB3  1 
ATOM   547  H HD21 A ASN   A 1 20  ? 7.123  -0.324  7.059   0.46 26.82 ?  20  ASN   A HD21 1 
ATOM   548  H HD21 B ASN   A 1 20  ? 7.049  -0.067  6.801   0.54 21.87 ?  20  ASN   A HD21 1 
ATOM   549  H HD22 A ASN   A 1 20  ? 7.915  -1.580  6.946   0.46 26.82 ?  20  ASN   A HD22 1 
ATOM   550  H HD22 B ASN   A 1 20  ? 8.055  -1.062  7.247   0.54 21.87 ?  20  ASN   A HD22 1 
ATOM   551  N N    A ALA   A 1 21  ? 10.123 -1.739  9.338   0.46 20.20 ?  21  ALA   A N    1 
ATOM   552  N N    B ALA   A 1 21  ? 9.941  -1.362  9.335   0.54 20.25 ?  21  ALA   A N    1 
ATOM   553  C CA   A ALA   A 1 21  ? 10.811 -0.806  10.218  0.46 19.25 ?  21  ALA   A CA   1 
ATOM   554  C CA   B ALA   A 1 21  ? 10.619 -0.408  10.197  0.54 21.16 ?  21  ALA   A CA   1 
ATOM   555  C C    A ALA   A 1 21  ? 11.736 0.102   9.423   0.46 18.96 ?  21  ALA   A C    1 
ATOM   556  C C    B ALA   A 1 21  ? 11.723 0.290   9.424   0.54 20.49 ?  21  ALA   A C    1 
ATOM   557  O O    A ALA   A 1 21  ? 12.214 -0.260  8.344   0.46 19.13 ?  21  ALA   A O    1 
ATOM   558  O O    B ALA   A 1 21  ? 12.174 -0.178  8.375   0.54 20.47 ?  21  ALA   A O    1 
ATOM   559  C CB   A ALA   A 1 21  ? 11.599 -1.550  11.300  0.46 19.83 ?  21  ALA   A CB   1 
ATOM   560  C CB   B ALA   A 1 21  ? 11.201 -1.093  11.437  0.54 22.65 ?  21  ALA   A CB   1 
ATOM   561  H H    A ALA   A 1 21  ? 10.484 -1.849  8.565   0.46 24.25 ?  21  ALA   A H    1 
ATOM   562  H H    B ALA   A 1 21  ? 10.386 -1.609  8.644   0.54 24.31 ?  21  ALA   A H    1 
ATOM   563  H HA   A ALA   A 1 21  ? 10.150 -0.247  10.658  0.46 23.12 ?  21  ALA   A HA   1 
ATOM   564  H HA   B ALA   A 1 21  ? 9.981  0.259   10.492  0.54 25.41 ?  21  ALA   A HA   1 
ATOM   565  H HB1  A ALA   A 1 21  ? 12.015 -0.897  11.881  0.46 23.81 ?  21  ALA   A HB1  1 
ATOM   566  H HB1  B ALA   A 1 21  ? 11.646 -0.428  11.983  0.54 27.19 ?  21  ALA   A HB1  1 
ATOM   567  H HB2  A ALA   A 1 21  ? 10.984 -2.102  11.809  0.46 23.81 ?  21  ALA   A HB2  1 
ATOM   568  H HB2  B ALA   A 1 21  ? 10.482 -1.509  11.939  0.54 27.19 ?  21  ALA   A HB2  1 
ATOM   569  H HB3  A ALA   A 1 21  ? 12.270 -2.102  10.876  0.46 23.81 ?  21  ALA   A HB3  1 
ATOM   570  H HB3  B ALA   A 1 21  ? 11.839 -1.770  11.154  0.54 27.19 ?  21  ALA   A HB3  1 
ATOM   571  N N    A ASP   A 1 22  ? 11.969 1.292   9.979   0.46 18.64 ?  22  ASP   A N    1 
ATOM   572  N N    B ASP   A 1 22  ? 12.137 1.430   9.967   0.54 20.34 ?  22  ASP   A N    1 
ATOM   573  C CA   A ASP   A 1 22  ? 12.999 2.213   9.505   0.46 17.84 ?  22  ASP   A CA   1 
ATOM   574  C CA   B ASP   A 1 22  ? 13.316 2.150   9.507   0.54 19.66 ?  22  ASP   A CA   1 
ATOM   575  C C    A ASP   A 1 22  ? 14.333 1.750   10.074  0.46 16.64 ?  22  ASP   A C    1 
ATOM   576  C C    B ASP   A 1 22  ? 14.559 1.479   10.082  0.54 17.61 ?  22  ASP   A C    1 
ATOM   577  O O    A ASP   A 1 22  ? 14.555 1.814   11.288  0.46 16.29 ?  22  ASP   A O    1 
ATOM   578  O O    B ASP   A 1 22  ? 14.681 1.329   11.303  0.54 18.53 ?  22  ASP   A O    1 
ATOM   579  C CB   A ASP   A 1 22  ? 12.668 3.626   9.979   0.46 18.50 ?  22  ASP   A CB   1 
ATOM   580  C CB   B ASP   A 1 22  ? 13.221 3.589   10.012  0.54 20.55 ?  22  ASP   A CB   1 
ATOM   581  C CG   A ASP   A 1 22  ? 13.709 4.657   9.573   0.46 19.03 ?  22  ASP   A CG   1 
ATOM   582  C CG   B ASP   A 1 22  ? 14.280 4.502   9.422   0.54 21.63 ?  22  ASP   A CG   1 
ATOM   583  O OD1  A ASP   A 1 22  ? 14.806 4.292   9.111   0.46 18.40 ?  22  ASP   A OD1  1 
ATOM   584  O OD1  B ASP   A 1 22  ? 15.336 4.004   8.983   0.54 21.94 ?  22  ASP   A OD1  1 
ATOM   585  O OD2  A ASP   A 1 22  ? 13.414 5.862   9.719   0.46 20.78 -1 22  ASP   A OD2  1 
ATOM   586  O OD2  B ASP   A 1 22  ? 14.059 5.734   9.408   0.54 23.50 -1 22  ASP   A OD2  1 
ATOM   587  H H    A ASP   A 1 22  ? 11.520 1.602   10.646  0.46 22.38 ?  22  ASP   A H    1 
ATOM   588  H H    B ASP   A 1 22  ? 11.717 1.824   10.605  0.54 24.42 ?  22  ASP   A H    1 
ATOM   589  H HA   A ASP   A 1 22  ? 13.042 2.203   8.533   0.46 21.42 ?  22  ASP   A HA   1 
ATOM   590  H HA   B ASP   A 1 22  ? 13.355 2.144   8.532   0.54 23.61 ?  22  ASP   A HA   1 
ATOM   591  H HB2  A ASP   A 1 22  ? 11.822 3.903   9.597   0.46 22.22 ?  22  ASP   A HB2  1 
ATOM   592  H HB2  B ASP   A 1 22  ? 12.351 3.949   9.790   0.54 24.67 ?  22  ASP   A HB2  1 
ATOM   593  H HB3  A ASP   A 1 22  ? 12.614 3.631   10.946  0.46 22.22 ?  22  ASP   A HB3  1 
ATOM   594  H HB3  B ASP   A 1 22  ? 13.347 3.588   10.973  0.54 24.67 ?  22  ASP   A HB3  1 
ATOM   595  N N    A ILE   A 1 23  ? 15.228 1.299   9.194   0.46 16.47 ?  23  ILE   A N    1 
ATOM   596  N N    B ILE   A 1 23  ? 15.487 1.083   9.209   0.54 16.46 ?  23  ILE   A N    1 
ATOM   597  C CA   A ILE   A 1 23  ? 16.478 0.684   9.635   0.46 16.20 ?  23  ILE   A CA   1 
ATOM   598  C CA   B ILE   A 1 23  ? 16.728 0.468   9.675   0.54 16.52 ?  23  ILE   A CA   1 
ATOM   599  C C    A ILE   A 1 23  ? 17.303 1.632   10.500  0.46 15.95 ?  23  ILE   A C    1 
ATOM   600  C C    B ILE   A 1 23  ? 17.486 1.406   10.609  0.54 16.51 ?  23  ILE   A C    1 
ATOM   601  O O    A ILE   A 1 23  ? 18.023 1.184   11.401  0.46 16.95 ?  23  ILE   A O    1 
ATOM   602  O O    B ILE   A 1 23  ? 18.138 0.951   11.559  0.54 16.57 ?  23  ILE   A O    1 
ATOM   603  C CB   A ILE   A 1 23  ? 17.264 0.130   8.426   0.46 15.39 ?  23  ILE   A CB   1 
ATOM   604  C CB   B ILE   A 1 23  ? 17.588 -0.016  8.485   0.54 15.53 ?  23  ILE   A CB   1 
ATOM   605  C CG1  A ILE   A 1 23  ? 18.395 -0.793  8.894   0.46 16.65 ?  23  ILE   A CG1  1 
ATOM   606  C CG1  B ILE   A 1 23  ? 18.626 -1.042  8.966   0.54 14.84 ?  23  ILE   A CG1  1 
ATOM   607  C CG2  A ILE   A 1 23  ? 17.804 1.268   7.562   0.46 15.34 ?  23  ILE   A CG2  1 
ATOM   608  C CG2  B ILE   A 1 23  ? 18.254 1.161   7.764   0.54 16.67 ?  23  ILE   A CG2  1 
ATOM   609  C CD1  A ILE   A 1 23  ? 19.103 -1.519  7.766   0.46 16.91 ?  23  ILE   A CD1  1 
ATOM   610  C CD1  B ILE   A 1 23  ? 19.493 -1.623  7.863   0.54 14.75 ?  23  ILE   A CD1  1 
ATOM   611  H H    A ILE   A 1 23  ? 15.130 1.338   8.343   0.46 19.78 ?  23  ILE   A H    1 
ATOM   612  H H    B ILE   A 1 23  ? 15.417 1.155   8.361   0.54 19.76 ?  23  ILE   A H    1 
ATOM   613  H HA   A ILE   A 1 23  ? 16.253 -0.072  10.194  0.46 19.46 ?  23  ILE   A HA   1 
ATOM   614  H HA   B ILE   A 1 23  ? 16.489 -0.311  10.190  0.54 19.84 ?  23  ILE   A HA   1 
ATOM   615  H HB   A ILE   A 1 23  ? 16.650 -0.393  7.887   0.46 18.49 ?  23  ILE   A HB   1 
ATOM   616  H HB   B ILE   A 1 23  ? 16.999 -0.458  7.854   0.54 18.65 ?  23  ILE   A HB   1 
ATOM   617  H HG12 A ILE   A 1 23  ? 19.052 -0.265  9.367   0.46 19.99 ?  23  ILE   A HG12 1 
ATOM   618  H HG12 B ILE   A 1 23  ? 19.206 -0.616  9.612   0.54 17.82 ?  23  ILE   A HG12 1 
ATOM   619  H HG13 A ILE   A 1 23  ? 18.021 -1.465  9.487   0.46 19.99 ?  23  ILE   A HG13 1 
ATOM   620  H HG13 B ILE   A 1 23  ? 18.152 -1.780  9.389   0.54 17.82 ?  23  ILE   A HG13 1 
ATOM   621  H HG21 A ILE   A 1 23  ? 18.139 0.897   6.729   0.46 18.42 ?  23  ILE   A HG21 1 
ATOM   622  H HG21 B ILE   A 1 23  ? 18.609 0.847   6.914   0.54 20.01 ?  23  ILE   A HG21 1 
ATOM   623  H HG22 A ILE   A 1 23  ? 17.087 1.893   7.379   0.46 18.42 ?  23  ILE   A HG22 1 
ATOM   624  H HG22 B ILE   A 1 23  ? 17.594 1.852   7.609   0.54 20.01 ?  23  ILE   A HG22 1 
ATOM   625  H HG23 A ILE   A 1 23  ? 18.521 1.713   8.038   0.46 18.42 ?  23  ILE   A HG23 1 
ATOM   626  H HG23 B ILE   A 1 23  ? 18.974 1.504   8.314   0.54 20.01 ?  23  ILE   A HG23 1 
ATOM   627  H HD11 A ILE   A 1 23  ? 19.745 -2.139  8.144   0.46 20.30 ?  23  ILE   A HD11 1 
ATOM   628  H HD11 B ILE   A 1 23  ? 20.048 -2.324  8.237   0.54 17.71 ?  23  ILE   A HD11 1 
ATOM   629  H HD12 A ILE   A 1 23  ? 18.447 -2.001  7.238   0.46 20.30 ?  23  ILE   A HD12 1 
ATOM   630  H HD12 B ILE   A 1 23  ? 18.921 -1.986  7.170   0.54 17.71 ?  23  ILE   A HD12 1 
ATOM   631  H HD13 A ILE   A 1 23  ? 19.560 -0.867  7.210   0.46 20.30 ?  23  ILE   A HD13 1 
ATOM   632  H HD13 B ILE   A 1 23  ? 20.050 -0.918  7.498   0.54 17.71 ?  23  ILE   A HD13 1 
ATOM   633  N N    A VAL   A 1 24  ? 17.204 2.946   10.266  0.46 16.37 ?  24  VAL   A N    1 
ATOM   634  N N    B VAL   A 1 24  ? 17.390 2.721   10.378  0.54 17.38 ?  24  VAL   A N    1 
ATOM   635  C CA   A VAL   A 1 24  ? 17.915 3.904   11.114  0.46 17.54 ?  24  VAL   A CA   1 
ATOM   636  C CA   B VAL   A 1 24  ? 18.044 3.694   11.253  0.54 18.75 ?  24  VAL   A CA   1 
ATOM   637  C C    A VAL   A 1 24  ? 17.405 3.823   12.549  0.46 18.59 ?  24  VAL   A C    1 
ATOM   638  C C    B VAL   A 1 24  ? 17.467 3.609   12.662  0.54 19.73 ?  24  VAL   A C    1 
ATOM   639  O O    A VAL   A 1 24  ? 18.187 3.804   13.507  0.46 18.60 ?  24  VAL   A O    1 
ATOM   640  O O    B VAL   A 1 24  ? 18.201 3.495   13.652  0.54 20.05 ?  24  VAL   A O    1 
ATOM   641  C CB   A VAL   A 1 24  ? 17.790 5.330   10.544  0.46 18.40 ?  24  VAL   A CB   1 
ATOM   642  C CB   B VAL   A 1 24  ? 17.907 5.115   10.671  0.54 20.23 ?  24  VAL   A CB   1 
ATOM   643  C CG1  A VAL   A 1 24  ? 18.304 6.365   11.548  0.46 19.49 ?  24  VAL   A CG1  1 
ATOM   644  C CG1  B VAL   A 1 24  ? 18.469 6.155   11.640  0.54 21.78 ?  24  VAL   A CG1  1 
ATOM   645  C CG2  A VAL   A 1 24  ? 18.542 5.448   9.226   0.46 19.57 ?  24  VAL   A CG2  1 
ATOM   646  C CG2  B VAL   A 1 24  ? 18.591 5.210   9.311   0.54 21.59 ?  24  VAL   A CG2  1 
ATOM   647  H H    A VAL   A 1 24  ? 16.743 3.303   9.634   0.46 19.66 ?  24  VAL   A H    1 
ATOM   648  H H    B VAL   A 1 24  ? 16.951 3.075   9.727   0.54 20.87 ?  24  VAL   A H    1 
ATOM   649  H HA   A VAL   A 1 24  ? 18.857 3.677   11.122  0.46 21.06 ?  24  VAL   A HA   1 
ATOM   650  H HA   B VAL   A 1 24  ? 18.991 3.490   11.299  0.54 22.52 ?  24  VAL   A HA   1 
ATOM   651  H HB   A VAL   A 1 24  ? 16.856 5.524   10.370  0.46 22.10 ?  24  VAL   A HB   1 
ATOM   652  H HB   B VAL   A 1 24  ? 16.967 5.313   10.537  0.54 24.29 ?  24  VAL   A HB   1 
ATOM   653  H HG11 A VAL   A 1 24  ? 18.461 7.202   11.085  0.46 23.41 ?  24  VAL   A HG11 1 
ATOM   654  H HG11 B VAL   A 1 24  ? 18.585 6.995   11.168  0.54 26.15 ?  24  VAL   A HG11 1 
ATOM   655  H HG12 A VAL   A 1 24  ? 17.638 6.492   12.241  0.46 23.41 ?  24  VAL   A HG12 1 
ATOM   656  H HG12 B VAL   A 1 24  ? 17.844 6.273   12.372  0.54 26.15 ?  24  VAL   A HG12 1 
ATOM   657  H HG13 A VAL   A 1 24  ? 19.132 6.041   11.936  0.46 23.41 ?  24  VAL   A HG13 1 
ATOM   658  H HG13 B VAL   A 1 24  ? 19.323 5.843   11.975  0.54 26.15 ?  24  VAL   A HG13 1 
ATOM   659  H HG21 A VAL   A 1 24  ? 18.218 6.226   8.744   0.46 23.50 ?  24  VAL   A HG21 1 
ATOM   660  H HG21 B VAL   A 1 24  ? 18.512 6.120   8.977   0.54 25.92 ?  24  VAL   A HG21 1 
ATOM   661  H HG22 A VAL   A 1 24  ? 19.490 5.550   9.411   0.46 23.50 ?  24  VAL   A HG22 1 
ATOM   662  H HG22 B VAL   A 1 24  ? 19.528 4.978   9.411   0.54 25.92 ?  24  VAL   A HG22 1 
ATOM   663  H HG23 A VAL   A 1 24  ? 18.390 4.648   8.699   0.46 23.50 ?  24  VAL   A HG23 1 
ATOM   664  H HG23 B VAL   A 1 24  ? 18.162 4.596   8.695   0.54 25.92 ?  24  VAL   A HG23 1 
ATOM   665  N N    A GLU   A 1 25  ? 16.081 3.774   12.717  0.46 19.47 ?  25  GLU   A N    1 
ATOM   666  N N    B GLU   A 1 25  ? 16.138 3.675   12.771  0.54 20.19 ?  25  GLU   A N    1 
ATOM   667  C CA   A GLU   A 1 25  ? 15.518 3.731   14.062  0.46 20.66 ?  25  GLU   A CA   1 
ATOM   668  C CA   B GLU   A 1 25  ? 15.500 3.608   14.081  0.54 21.37 ?  25  GLU   A CA   1 
ATOM   669  C C    A GLU   A 1 25  ? 15.726 2.374   14.721  0.46 20.52 ?  25  GLU   A C    1 
ATOM   670  C C    B GLU   A 1 25  ? 15.746 2.260   14.743  0.54 20.88 ?  25  GLU   A C    1 
ATOM   671  O O    A GLU   A 1 25  ? 15.919 2.306   15.940  0.46 21.25 ?  25  GLU   A O    1 
ATOM   672  O O    B GLU   A 1 25  ? 15.980 2.188   15.956  0.54 21.95 ?  25  GLU   A O    1 
ATOM   673  C CB   A GLU   A 1 25  ? 14.035 4.100   14.024  0.46 23.14 ?  25  GLU   A CB   1 
ATOM   674  C CB   B GLU   A 1 25  ? 14.002 3.890   13.943  0.54 23.65 ?  25  GLU   A CB   1 
ATOM   675  C CG   A GLU   A 1 25  ? 13.783 5.539   13.595  0.46 26.13 ?  25  GLU   A CG   1 
ATOM   676  C CG   B GLU   A 1 25  ? 13.685 5.349   13.651  0.54 26.97 ?  25  GLU   A CG   1 
ATOM   677  C CD   A GLU   A 1 25  ? 14.582 6.552   14.403  0.46 28.40 ?  25  GLU   A CD   1 
ATOM   678  C CD   B GLU   A 1 25  ? 14.292 6.294   14.673  0.54 29.80 ?  25  GLU   A CD   1 
ATOM   679  O OE1  A GLU   A 1 25  ? 14.740 6.363   15.629  0.46 28.72 ?  25  GLU   A OE1  1 
ATOM   680  O OE1  B GLU   A 1 25  ? 14.196 5.999   15.884  0.54 30.66 ?  25  GLU   A OE1  1 
ATOM   681  O OE2  A GLU   A 1 25  ? 15.078 7.530   13.802  0.46 29.66 -1 25  GLU   A OE2  1 
ATOM   682  O OE2  B GLU   A 1 25  ? 14.878 7.320   14.268  0.54 31.28 -1 25  GLU   A OE2  1 
ATOM   683  H H    A GLU   A 1 25  ? 15.504 3.764   12.082  0.46 23.38 ?  25  GLU   A H    1 
ATOM   684  H H    B GLU   A 1 25  ? 15.598 3.767   12.110  0.54 24.24 ?  25  GLU   A H    1 
ATOM   685  H HA   A GLU   A 1 25  ? 15.973 4.389   14.609  0.46 24.81 ?  25  GLU   A HA   1 
ATOM   686  H HA   B GLU   A 1 25  ? 15.888 4.288   14.653  0.54 25.66 ?  25  GLU   A HA   1 
ATOM   687  H HB2  A GLU   A 1 25  ? 13.581 3.518   13.391  0.46 27.79 ?  25  GLU   A HB2  1 
ATOM   688  H HB2  B GLU   A 1 25  ? 13.645 3.360   13.211  0.54 28.39 ?  25  GLU   A HB2  1 
ATOM   689  H HB3  A GLU   A 1 25  ? 13.655 3.981   14.909  0.46 27.79 ?  25  GLU   A HB3  1 
ATOM   690  H HB3  B GLU   A 1 25  ? 13.557 3.652   14.769  0.54 28.39 ?  25  GLU   A HB3  1 
ATOM   691  H HG2  A GLU   A 1 25  ? 14.058 5.645   12.675  0.46 31.38 ?  25  GLU   A HG2  1 
ATOM   692  H HG2  B GLU   A 1 25  ? 14.025 5.578   12.771  0.54 32.38 ?  25  GLU   A HG2  1 
ATOM   693  H HG3  A GLU   A 1 25  ? 12.834 5.730   13.686  0.46 31.38 ?  25  GLU   A HG3  1 
ATOM   694  H HG3  B GLU   A 1 25  ? 12.725 5.480   13.683  0.54 32.38 ?  25  GLU   A HG3  1 
ATOM   695  N N    A GLU   A 1 26  ? 15.698 1.290   13.939  0.46 20.29 ?  26  GLU   A N    1 
ATOM   696  N N    B GLU   A 1 26  ? 15.720 1.180   13.961  0.54 20.19 ?  26  GLU   A N    1 
ATOM   697  C CA   A GLU   A 1 26  ? 16.021 -0.025  14.487  0.46 20.51 ?  26  GLU   A CA   1 
ATOM   698  C CA   B GLU   A 1 26  ? 16.041 -0.131  14.511  0.54 20.16 ?  26  GLU   A CA   1 
ATOM   699  C C    A GLU   A 1 26  ? 17.439 -0.051  15.041  0.46 19.46 ?  26  GLU   A C    1 
ATOM   700  C C    B GLU   A 1 26  ? 17.482 -0.186  14.997  0.54 19.57 ?  26  GLU   A C    1 
ATOM   701  O O    A GLU   A 1 26  ? 17.667 -0.490  16.173  0.46 18.98 ?  26  GLU   A O    1 
ATOM   702  O O    B GLU   A 1 26  ? 17.770 -0.768  16.048  0.54 19.61 ?  26  GLU   A O    1 
ATOM   703  C CB   A GLU   A 1 26  ? 15.859 -1.104  13.413  0.46 22.12 ?  26  GLU   A CB   1 
ATOM   704  C CB   B GLU   A 1 26  ? 15.791 -1.214  13.465  0.54 20.95 ?  26  GLU   A CB   1 
ATOM   705  C CG   A GLU   A 1 26  ? 14.446 -1.611  13.217  0.46 24.08 ?  26  GLU   A CG   1 
ATOM   706  C CG   B GLU   A 1 26  ? 14.327 -1.485  13.192  0.54 22.85 ?  26  GLU   A CG   1 
ATOM   707  C CD   A GLU   A 1 26  ? 13.966 -2.464  14.378  0.46 24.54 ?  26  GLU   A CD   1 
ATOM   708  C CD   B GLU   A 1 26  ? 13.589 -2.033  14.385  0.54 22.75 ?  26  GLU   A CD   1 
ATOM   709  O OE1  A GLU   A 1 26  ? 14.463 -3.596  14.556  0.46 24.02 ?  26  GLU   A OE1  1 
ATOM   710  O OE1  B GLU   A 1 26  ? 14.079 -2.995  15.006  0.54 22.17 ?  26  GLU   A OE1  1 
ATOM   711  O OE2  A GLU   A 1 26  ? 13.094 -1.990  15.126  0.46 25.54 -1 26  GLU   A OE2  1 
ATOM   712  O OE2  B GLU   A 1 26  ? 12.518 -1.483  14.700  0.54 23.90 -1 26  GLU   A OE2  1 
ATOM   713  H H    A GLU   A 1 26  ? 15.493 1.295   13.106  0.46 24.37 ?  26  GLU   A H    1 
ATOM   714  H H    B GLU   A 1 26  ? 15.518 1.184   13.127  0.54 24.25 ?  26  GLU   A H    1 
ATOM   715  H HA   A GLU   A 1 26  ? 15.409 -0.224  15.210  0.46 24.63 ?  26  GLU   A HA   1 
ATOM   716  H HA   B GLU   A 1 26  ? 15.464 -0.303  15.269  0.54 24.21 ?  26  GLU   A HA   1 
ATOM   717  H HB2  A GLU   A 1 26  ? 16.160 -0.745  12.565  0.46 26.56 ?  26  GLU   A HB2  1 
ATOM   718  H HB2  B GLU   A 1 26  ? 16.201 -0.933  12.626  0.54 25.16 ?  26  GLU   A HB2  1 
ATOM   719  H HB3  A GLU   A 1 26  ? 16.411 -1.864  13.658  0.46 26.56 ?  26  GLU   A HB3  1 
ATOM   720  H HB3  B GLU   A 1 26  ? 16.205 -2.037  13.766  0.54 25.16 ?  26  GLU   A HB3  1 
ATOM   721  H HG2  A GLU   A 1 26  ? 13.849 -0.853  13.133  0.46 28.91 ?  26  GLU   A HG2  1 
ATOM   722  H HG2  B GLU   A 1 26  ? 13.889 -0.660  12.959  0.54 27.43 ?  26  GLU   A HG2  1 
ATOM   723  H HG3  A GLU   A 1 26  ? 14.411 -2.149  12.408  0.46 28.91 ?  26  GLU   A HG3  1 
ATOM   724  H HG3  B GLU   A 1 26  ? 14.254 -2.129  12.475  0.54 27.43 ?  26  GLU   A HG3  1 
ATOM   725  N N    . ALA   A 1 27  ? 18.406 0.423   14.253  1.00 18.81 ?  27  ALA   A N    1 
ATOM   726  C CA   . ALA   A 1 27  ? 19.799 0.413   14.694  1.00 18.60 ?  27  ALA   A CA   1 
ATOM   727  C C    . ALA   A 1 27  ? 19.975 1.225   15.969  1.00 21.32 ?  27  ALA   A C    1 
ATOM   728  O O    . ALA   A 1 27  ? 20.640 0.778   16.910  1.00 21.46 ?  27  ALA   A O    1 
ATOM   729  C CB   . ALA   A 1 27  ? 20.721 0.921   13.580  1.00 18.29 ?  27  ALA   A CB   1 
ATOM   730  H H    A ALA   A 1 27  ? 18.281 0.767   13.477  0.46 22.59 ?  27  ALA   A H    1 
ATOM   731  H H    B ALA   A 1 27  ? 18.258 0.845   13.519  0.54 22.59 ?  27  ALA   A H    1 
ATOM   732  H HA   . ALA   A 1 27  ? 20.053 -0.497  14.892  1.00 22.33 ?  27  ALA   A HA   1 
ATOM   733  H HB1  . ALA   A 1 27  ? 21.641 0.901   13.895  1.00 21.97 ?  27  ALA   A HB1  1 
ATOM   734  H HB2  . ALA   A 1 27  ? 20.630 0.343   12.805  1.00 21.97 ?  27  ALA   A HB2  1 
ATOM   735  H HB3  . ALA   A 1 27  ? 20.474 1.829   13.346  1.00 21.97 ?  27  ALA   A HB3  1 
ATOM   736  N N    A LYS   A 1 28  ? 19.381 2.420   16.027  0.46 23.07 ?  28  LYS   A N    1 
ATOM   737  N N    B LYS   A 1 28  ? 19.372 2.417   16.024  0.54 22.58 ?  28  LYS   A N    1 
ATOM   738  C CA   A LYS   A 1 28  ? 19.536 3.251   17.219  0.46 25.76 ?  28  LYS   A CA   1 
ATOM   739  C CA   B LYS   A 1 28  ? 19.494 3.251   17.216  0.54 25.00 ?  28  LYS   A CA   1 
ATOM   740  C C    A LYS   A 1 28  ? 18.962 2.564   18.452  0.46 26.27 ?  28  LYS   A C    1 
ATOM   741  C C    B LYS   A 1 28  ? 18.934 2.545   18.443  0.54 25.49 ?  28  LYS   A C    1 
ATOM   742  O O    A LYS   A 1 28  ? 19.503 2.703   19.556  0.46 27.33 ?  28  LYS   A O    1 
ATOM   743  O O    B LYS   A 1 28  ? 19.473 2.683   19.548  0.54 26.92 ?  28  LYS   A O    1 
ATOM   744  C CB   A LYS   A 1 28  ? 18.901 4.624   17.003  0.46 28.19 ?  28  LYS   A CB   1 
ATOM   745  C CB   B LYS   A 1 28  ? 18.805 4.599   16.996  0.54 27.29 ?  28  LYS   A CB   1 
ATOM   746  C CG   A LYS   A 1 28  ? 19.736 5.520   16.108  0.46 30.47 ?  28  LYS   A CG   1 
ATOM   747  C CG   B LYS   A 1 28  ? 19.602 5.539   16.112  0.54 29.56 ?  28  LYS   A CG   1 
ATOM   748  C CD   A LYS   A 1 28  ? 19.276 6.962   16.147  0.46 32.94 ?  28  LYS   A CD   1 
ATOM   749  C CD   B LYS   A 1 28  ? 19.148 6.981   16.250  0.54 32.45 ?  28  LYS   A CD   1 
ATOM   750  C CE   A LYS   A 1 28  ? 17.954 7.139   15.439  0.46 34.34 ?  28  LYS   A CE   1 
ATOM   751  C CE   B LYS   A 1 28  ? 17.852 7.229   15.513  0.54 34.11 ?  28  LYS   A CE   1 
ATOM   752  N NZ   A LYS   A 1 28  ? 17.576 8.575   15.359  0.46 35.25 ?  28  LYS   A NZ   1 
ATOM   753  N NZ   B LYS   A 1 28  ? 17.531 8.682   15.461  0.54 35.15 ?  28  LYS   A NZ   1 
ATOM   754  H H    A LYS   A 1 28  ? 18.900 2.767   15.408  0.46 27.70 ?  28  LYS   A H    1 
ATOM   755  H H    B LYS   A 1 28  ? 18.900 2.760   15.395  0.54 27.11 ?  28  LYS   A H    1 
ATOM   756  H HA   A LYS   A 1 28  ? 20.480 3.392   17.384  0.46 30.92 ?  28  LYS   A HA   1 
ATOM   757  H HA   B LYS   A 1 28  ? 20.430 3.427   17.388  0.54 30.02 ?  28  LYS   A HA   1 
ATOM   758  H HB2  A LYS   A 1 28  ? 18.032 4.513   16.588  0.46 33.85 ?  28  LYS   A HB2  1 
ATOM   759  H HB2  B LYS   A 1 28  ? 17.947 4.455   16.571  0.54 32.76 ?  28  LYS   A HB2  1 
ATOM   760  H HB3  A LYS   A 1 28  ? 18.803 5.071   17.861  0.46 33.85 ?  28  LYS   A HB3  1 
ATOM   761  H HB3  B LYS   A 1 28  ? 18.679 5.038   17.854  0.54 32.76 ?  28  LYS   A HB3  1 
ATOM   762  H HG2  A LYS   A 1 28  ? 20.660 5.491   16.401  0.46 36.57 ?  28  LYS   A HG2  1 
ATOM   763  H HG2  B LYS   A 1 28  ? 20.539 5.495   16.362  0.54 35.49 ?  28  LYS   A HG2  1 
ATOM   764  H HG3  A LYS   A 1 28  ? 19.666 5.207   15.193  0.46 36.57 ?  28  LYS   A HG3  1 
ATOM   765  H HG3  B LYS   A 1 28  ? 19.491 5.277   15.185  0.54 35.49 ?  28  LYS   A HG3  1 
ATOM   766  H HD2  A LYS   A 1 28  ? 19.167 7.239   17.071  0.46 39.54 ?  28  LYS   A HD2  1 
ATOM   767  H HD2  B LYS   A 1 28  ? 19.009 7.185   17.189  0.54 38.95 ?  28  LYS   A HD2  1 
ATOM   768  H HD3  A LYS   A 1 28  ? 19.936 7.521   15.706  0.46 39.54 ?  28  LYS   A HD3  1 
ATOM   769  H HD3  B LYS   A 1 28  ? 19.826 7.567   15.878  0.54 38.95 ?  28  LYS   A HD3  1 
ATOM   770  H HE2  A LYS   A 1 28  ? 18.026 6.790   14.536  0.46 41.22 ?  28  LYS   A HE2  1 
ATOM   771  H HE2  B LYS   A 1 28  ? 17.934 6.901   14.603  0.54 40.95 ?  28  LYS   A HE2  1 
ATOM   772  H HE3  A LYS   A 1 28  ? 17.263 6.667   15.929  0.46 41.22 ?  28  LYS   A HE3  1 
ATOM   773  H HE3  B LYS   A 1 28  ? 17.130 6.772   15.972  0.54 40.95 ?  28  LYS   A HE3  1 
ATOM   774  H HZ1  A LYS   A 1 28  ? 16.797 8.661   14.939  0.46 42.31 ?  28  LYS   A HZ1  1 
ATOM   775  H HZ1  B LYS   A 1 28  ? 16.767 8.809   15.024  0.54 42.19 ?  28  LYS   A HZ1  1 
ATOM   776  H HZ2  A LYS   A 1 28  ? 17.504 8.916   16.178  0.46 42.31 ?  28  LYS   A HZ2  1 
ATOM   777  H HZ2  B LYS   A 1 28  ? 17.450 9.005   16.286  0.54 42.19 ?  28  LYS   A HZ2  1 
ATOM   778  H HZ3  A LYS   A 1 28  ? 18.198 9.028   14.911  0.46 42.31 ?  28  LYS   A HZ3  1 
ATOM   779  H HZ3  B LYS   A 1 28  ? 18.182 9.122   15.041  0.54 42.19 ?  28  LYS   A HZ3  1 
ATOM   780  N N    A LYS   A 1 29  ? 17.871 1.815   18.284  0.46 26.63 ?  29  LYS   A N    1 
ATOM   781  N N    B LYS   A 1 29  ? 17.855 1.780   18.268  0.54 25.69 ?  29  LYS   A N    1 
ATOM   782  C CA   A LYS   A 1 29  ? 17.262 1.116   19.411  0.46 28.24 ?  29  LYS   A CA   1 
ATOM   783  C CA   B LYS   A 1 29  ? 17.219 1.095   19.389  0.54 27.48 ?  29  LYS   A CA   1 
ATOM   784  C C    A LYS   A 1 29  ? 18.093 -0.093  19.822  0.46 27.32 ?  29  LYS   A C    1 
ATOM   785  C C    B LYS   A 1 29  ? 18.019 -0.127  19.821  0.54 26.79 ?  29  LYS   A C    1 
ATOM   786  O O    A LYS   A 1 29  ? 18.401 -0.273  21.006  0.46 28.47 ?  29  LYS   A O    1 
ATOM   787  O O    B LYS   A 1 29  ? 18.225 -0.353  21.019  0.54 27.94 ?  29  LYS   A O    1 
ATOM   788  C CB   A LYS   A 1 29  ? 15.842 0.679   19.040  0.46 31.13 ?  29  LYS   A CB   1 
ATOM   789  C CB   B LYS   A 1 29  ? 15.804 0.668   18.993  0.54 30.39 ?  29  LYS   A CB   1 
ATOM   790  C CG   A LYS   A 1 29  ? 15.111 -0.081  20.141  0.46 34.15 ?  29  LYS   A CG   1 
ATOM   791  C CG   B LYS   A 1 29  ? 15.018 -0.031  20.097  0.54 33.66 ?  29  LYS   A CG   1 
ATOM   792  C CD   A LYS   A 1 29  ? 14.770 0.833   21.306  0.46 36.84 ?  29  LYS   A CD   1 
ATOM   793  C CD   B LYS   A 1 29  ? 14.613 0.943   21.192  0.54 36.50 ?  29  LYS   A CD   1 
ATOM   794  C CE   A LYS   A 1 29  ? 13.898 0.127   22.334  0.46 38.52 ?  29  LYS   A CE   1 
ATOM   795  C CE   B LYS   A 1 29  ? 13.718 0.277   22.229  0.54 38.21 ?  29  LYS   A CE   1 
ATOM   796  N NZ   A LYS   A 1 29  ? 13.463 1.053   23.416  0.46 39.54 ?  29  LYS   A NZ   1 
ATOM   797  N NZ   B LYS   A 1 29  ? 13.381 1.207   23.343  0.54 39.37 ?  29  LYS   A NZ   1 
ATOM   798  H H    A LYS   A 1 29  ? 17.463 1.703   17.536  0.46 31.97 ?  29  LYS   A H    1 
ATOM   799  H H    B LYS   A 1 29  ? 17.467 1.646   17.510  0.54 30.84 ?  29  LYS   A H    1 
ATOM   800  H HA   A LYS   A 1 29  ? 17.202 1.715   20.171  0.46 33.90 ?  29  LYS   A HA   1 
ATOM   801  H HA   B LYS   A 1 29  ? 17.153 1.700   20.144  0.54 32.99 ?  29  LYS   A HA   1 
ATOM   802  H HB2  A LYS   A 1 29  ? 15.315 1.467   18.833  0.46 37.37 ?  29  LYS   A HB2  1 
ATOM   803  H HB2  B LYS   A 1 29  ? 15.302 1.455   18.735  0.54 36.48 ?  29  LYS   A HB2  1 
ATOM   804  H HB3  A LYS   A 1 29  ? 15.884 0.100   18.263  0.46 37.37 ?  29  LYS   A HB3  1 
ATOM   805  H HB3  B LYS   A 1 29  ? 15.861 0.055   18.245  0.54 36.48 ?  29  LYS   A HB3  1 
ATOM   806  H HG2  A LYS   A 1 29  ? 14.283 -0.439  19.785  0.46 41.00 ?  29  LYS   A HG2  1 
ATOM   807  H HG2  B LYS   A 1 29  ? 14.210 -0.414  19.720  0.54 40.41 ?  29  LYS   A HG2  1 
ATOM   808  H HG3  A LYS   A 1 29  ? 15.669 -0.804  20.471  0.46 41.00 ?  29  LYS   A HG3  1 
ATOM   809  H HG3  B LYS   A 1 29  ? 15.560 -0.731  20.497  0.54 40.41 ?  29  LYS   A HG3  1 
ATOM   810  H HD2  A LYS   A 1 29  ? 15.589 1.114   21.743  0.46 44.22 ?  29  LYS   A HD2  1 
ATOM   811  H HD2  B LYS   A 1 29  ? 15.408 1.269   21.641  0.54 43.82 ?  29  LYS   A HD2  1 
ATOM   812  H HD3  A LYS   A 1 29  ? 14.284 1.605   20.974  0.46 44.22 ?  29  LYS   A HD3  1 
ATOM   813  H HD3  B LYS   A 1 29  ? 14.123 1.682   20.797  0.54 43.82 ?  29  LYS   A HD3  1 
ATOM   814  H HE2  A LYS   A 1 29  ? 13.106 -0.222  21.895  0.46 46.23 ?  29  LYS   A HE2  1 
ATOM   815  H HE2  B LYS   A 1 29  ? 12.891 -0.003  21.806  0.54 45.87 ?  29  LYS   A HE2  1 
ATOM   816  H HE3  A LYS   A 1 29  ? 14.403 -0.597  22.737  0.46 46.23 ?  29  LYS   A HE3  1 
ATOM   817  H HE3  B LYS   A 1 29  ? 14.179 -0.491  22.603  0.54 45.87 ?  29  LYS   A HE3  1 
ATOM   818  H HZ1  A LYS   A 1 29  ? 12.956 0.617   24.003  0.46 47.46 ?  29  LYS   A HZ1  1 
ATOM   819  H HZ1  B LYS   A 1 29  ? 12.859 0.795   23.935  0.54 47.26 ?  29  LYS   A HZ1  1 
ATOM   820  H HZ2  A LYS   A 1 29  ? 14.174 1.384   23.837  0.46 47.46 ?  29  LYS   A HZ2  1 
ATOM   821  H HZ2  B LYS   A 1 29  ? 14.125 1.474   23.751  0.54 47.26 ?  29  LYS   A HZ2  1 
ATOM   822  H HZ3  A LYS   A 1 29  ? 12.993 1.725   23.070  0.46 47.46 ?  29  LYS   A HZ3  1 
ATOM   823  H HZ3  B LYS   A 1 29  ? 12.953 1.919   23.025  0.54 47.26 ?  29  LYS   A HZ3  1 
ATOM   824  N N    . VAL   A 1 30  ? 18.458 -0.935  18.858  1.00 26.58 ?  30  VAL   A N    1 
ATOM   825  C CA   . VAL   A 1 30  ? 19.083 -2.215  19.169  1.00 25.55 ?  30  VAL   A CA   1 
ATOM   826  C C    . VAL   A 1 30  ? 20.594 -2.116  19.342  1.00 24.69 ?  30  VAL   A C    1 
ATOM   827  O O    . VAL   A 1 30  ? 21.183 -2.895  20.097  1.00 24.47 ?  30  VAL   A O    1 
ATOM   828  C CB   . VAL   A 1 30  ? 18.732 -3.212  18.050  1.00 26.26 ?  30  VAL   A CB   1 
ATOM   829  C CG1  . VAL   A 1 30  ? 19.470 -4.530  18.237  1.00 27.67 ?  30  VAL   A CG1  1 
ATOM   830  C CG2  . VAL   A 1 30  ? 17.226 -3.442  17.998  1.00 27.35 ?  30  VAL   A CG2  1 
ATOM   831  H H    A VAL   A 1 30  ? 18.351 -0.790  18.015  0.46 31.91 ?  30  VAL   A H    1 
ATOM   832  H H    B VAL   A 1 30  ? 18.392 -0.772  18.014  0.54 31.91 ?  30  VAL   A H    1 
ATOM   833  H HA   . VAL   A 1 30  ? 18.704 -2.557  19.994  1.00 30.67 ?  30  VAL   A HA   1 
ATOM   834  H HB   . VAL   A 1 30  ? 19.005 -2.842  17.197  1.00 31.52 ?  30  VAL   A HB   1 
ATOM   835  H HG11 . VAL   A 1 30  ? 19.046 -5.210  17.684  1.00 33.22 ?  30  VAL   A HG11 1 
ATOM   836  H HG12 . VAL   A 1 30  ? 20.394 -4.421  17.970  1.00 33.22 ?  30  VAL   A HG12 1 
ATOM   837  H HG13 . VAL   A 1 30  ? 19.419 -4.792  19.169  1.00 33.22 ?  30  VAL   A HG13 1 
ATOM   838  H HG21 . VAL   A 1 30  ? 17.029 -4.114  17.325  1.00 32.83 ?  30  VAL   A HG21 1 
ATOM   839  H HG22 . VAL   A 1 30  ? 16.922 -3.750  18.867  1.00 32.83 ?  30  VAL   A HG22 1 
ATOM   840  H HG23 . VAL   A 1 30  ? 16.786 -2.609  17.770  1.00 32.83 ?  30  VAL   A HG23 1 
ATOM   841  N N    A LYS   A 1 31  ? 21.239 -1.181  18.654  0.46 24.19 ?  31  LYS   A N    1 
ATOM   842  N N    B LYS   A 1 31  ? 21.235 -1.177  18.656  0.54 23.77 ?  31  LYS   A N    1 
ATOM   843  C CA   A LYS   A 1 31  ? 22.693 -1.099  18.602  0.46 25.05 ?  31  LYS   A CA   1 
ATOM   844  C CA   B LYS   A 1 31  ? 22.689 -1.094  18.592  0.54 24.59 ?  31  LYS   A CA   1 
ATOM   845  C C    A LYS   A 1 31  ? 23.292 -2.471  18.280  0.46 22.99 ?  31  LYS   A C    1 
ATOM   846  C C    B LYS   A 1 31  ? 23.290 -2.467  18.279  0.54 22.57 ?  31  LYS   A C    1 
ATOM   847  O O    A LYS   A 1 31  ? 24.071 -3.018  19.069  0.46 23.62 ?  31  LYS   A O    1 
ATOM   848  O O    B LYS   A 1 31  ? 24.068 -3.009  19.072  0.54 23.13 ?  31  LYS   A O    1 
ATOM   849  C CB   A LYS   A 1 31  ? 23.272 -0.541  19.894  0.46 29.34 ?  31  LYS   A CB   1 
ATOM   850  C CB   B LYS   A 1 31  ? 23.278 -0.514  19.870  0.54 29.11 ?  31  LYS   A CB   1 
ATOM   851  C CG   A LYS   A 1 31  ? 22.577 0.717   20.392  0.46 34.23 ?  31  LYS   A CG   1 
ATOM   852  C CG   B LYS   A 1 31  ? 22.579 0.751   20.342  0.54 34.28 ?  31  LYS   A CG   1 
ATOM   853  C CD   A LYS   A 1 31  ? 23.578 1.783   20.809  0.46 38.06 ?  31  LYS   A CD   1 
ATOM   854  C CD   B LYS   A 1 31  ? 23.558 1.753   20.933  0.54 38.37 ?  31  LYS   A CD   1 
ATOM   855  C CE   A LYS   A 1 31  ? 22.939 2.821   21.720  0.46 40.68 ?  31  LYS   A CE   1 
ATOM   856  C CE   B LYS   A 1 31  ? 22.860 2.720   21.879  0.54 41.20 ?  31  LYS   A CE   1 
ATOM   857  N NZ   A LYS   A 1 31  ? 21.741 3.457   21.110  0.46 42.01 ?  31  LYS   A NZ   1 
ATOM   858  N NZ   B LYS   A 1 31  ? 21.686 3.398   21.270  0.54 42.59 ?  31  LYS   A NZ   1 
ATOM   859  H H    A LYS   A 1 31  ? 20.844 -0.568  18.198  0.46 29.04 ?  31  LYS   A H    1 
ATOM   860  H H    B LYS   A 1 31  ? 20.836 -0.562  18.207  0.54 28.54 ?  31  LYS   A H    1 
ATOM   861  H HA   A LYS   A 1 31  ? 22.936 -0.493  17.887  0.46 30.07 ?  31  LYS   A HA   1 
ATOM   862  H HA   B LYS   A 1 31  ? 22.924 -0.497  17.867  0.54 29.53 ?  31  LYS   A HA   1 
ATOM   863  H HB2  A LYS   A 1 31  ? 23.199 -1.215  20.585  0.46 35.23 ?  31  LYS   A HB2  1 
ATOM   864  H HB2  B LYS   A 1 31  ? 23.206 -1.175  20.571  0.54 34.95 ?  31  LYS   A HB2  1 
ATOM   865  H HB3  A LYS   A 1 31  ? 24.206 -0.323  19.743  0.46 35.23 ?  31  LYS   A HB3  1 
ATOM   866  H HB3  B LYS   A 1 31  ? 24.212 -0.300  19.712  0.54 34.95 ?  31  LYS   A HB3  1 
ATOM   867  H HG2  A LYS   A 1 31  ? 22.024 1.080   19.683  0.46 41.09 ?  31  LYS   A HG2  1 
ATOM   868  H HG2  B LYS   A 1 31  ? 22.134 1.169   19.589  0.54 41.15 ?  31  LYS   A HG2  1 
ATOM   869  H HG3  A LYS   A 1 31  ? 22.032 0.494   21.163  0.46 41.09 ?  31  LYS   A HG3  1 
ATOM   870  H HG3  B LYS   A 1 31  ? 21.932 0.518   21.027  0.54 41.15 ?  31  LYS   A HG3  1 
ATOM   871  H HD2  A LYS   A 1 31  ? 24.311 1.366   21.289  0.46 45.69 ?  31  LYS   A HD2  1 
ATOM   872  H HD2  B LYS   A 1 31  ? 24.242 1.277   21.431  0.54 46.06 ?  31  LYS   A HD2  1 
ATOM   873  H HD3  A LYS   A 1 31  ? 23.911 2.236   20.017  0.46 45.69 ?  31  LYS   A HD3  1 
ATOM   874  H HD3  B LYS   A 1 31  ? 23.962 2.267   20.216  0.54 46.06 ?  31  LYS   A HD3  1 
ATOM   875  H HE2  A LYS   A 1 31  ? 22.664 2.390   22.545  0.46 48.83 ?  31  LYS   A HE2  1 
ATOM   876  H HE2  B LYS   A 1 31  ? 22.534 2.222   22.638  0.54 49.45 ?  31  LYS   A HE2  1 
ATOM   877  H HE3  A LYS   A 1 31  ? 23.586 3.518   21.909  0.46 48.83 ?  31  LYS   A HE3  1 
ATOM   878  H HE3  B LYS   A 1 31  ? 23.491 3.398   22.171  0.54 49.45 ?  31  LYS   A HE3  1 
ATOM   879  H HZ1  A LYS   A 1 31  ? 21.406 4.068   21.663  0.46 50.42 ?  31  LYS   A HZ1  1 
ATOM   880  H HZ1  B LYS   A 1 31  ? 21.326 3.966   21.854  0.54 51.13 ?  31  LYS   A HZ1  1 
ATOM   881  H HZ2  A LYS   A 1 31  ? 21.962 3.849   20.343  0.46 50.42 ?  31  LYS   A HZ2  1 
ATOM   882  H HZ2  B LYS   A 1 31  ? 21.936 3.847   20.545  0.54 51.13 ?  31  LYS   A HZ2  1 
ATOM   883  H HZ3  A LYS   A 1 31  ? 21.117 2.841   20.950  0.46 50.42 ?  31  LYS   A HZ3  1 
ATOM   884  H HZ3  B LYS   A 1 31  ? 21.072 2.794   21.040  0.54 51.13 ?  31  LYS   A HZ3  1 
ATOM   885  N N    . PRO   A 1 32  ? 22.957 -3.045  17.128  1.00 20.97 ?  32  PRO   A N    1 
ATOM   886  C CA   . PRO   A 1 32  ? 23.437 -4.389  16.802  1.00 20.94 ?  32  PRO   A CA   1 
ATOM   887  C C    . PRO   A 1 32  ? 24.937 -4.388  16.566  1.00 20.83 ?  32  PRO   A C    1 
ATOM   888  O O    . PRO   A 1 32  ? 25.575 -3.353  16.369  1.00 20.25 ?  32  PRO   A O    1 
ATOM   889  C CB   . PRO   A 1 32  ? 22.691 -4.709  15.504  1.00 20.29 ?  32  PRO   A CB   1 
ATOM   890  C CG   . PRO   A 1 32  ? 22.531 -3.370  14.850  1.00 20.11 ?  32  PRO   A CG   1 
ATOM   891  C CD   . PRO   A 1 32  ? 22.244 -2.432  15.996  1.00 19.55 ?  32  PRO   A CD   1 
ATOM   892  H HA   . PRO   A 1 32  ? 23.199 -5.023  17.497  1.00 25.14 ?  32  PRO   A HA   1 
ATOM   893  H HB2  . PRO   A 1 32  ? 23.224 -5.308  14.954  1.00 24.37 ?  32  PRO   A HB2  1 
ATOM   894  H HB3  . PRO   A 1 32  ? 21.826 -5.107  15.706  1.00 24.37 ?  32  PRO   A HB3  1 
ATOM   895  H HG2  . PRO   A 1 32  ? 23.355 -3.129  14.400  1.00 24.14 ?  32  PRO   A HG2  1 
ATOM   896  H HG3  . PRO   A 1 32  ? 21.790 -3.398  14.227  1.00 24.14 ?  32  PRO   A HG3  1 
ATOM   897  H HD2  . PRO   A 1 32  ? 22.601 -1.554  15.791  1.00 23.47 ?  32  PRO   A HD2  1 
ATOM   898  H HD3  . PRO   A 1 32  ? 21.292 -2.403  16.164  1.00 23.47 ?  32  PRO   A HD3  1 
ATOM   899  N N    . THR   A 1 33  ? 25.494 -5.599  16.561  1.00 20.54 ?  33  THR   A N    1 
ATOM   900  C CA   . THR   A 1 33  ? 26.907 -5.758  16.240  1.00 20.83 ?  33  THR   A CA   1 
ATOM   901  C C    . THR   A 1 33  ? 27.199 -5.319  14.812  1.00 19.23 ?  33  THR   A C    1 
ATOM   902  O O    . THR   A 1 33  ? 28.236 -4.697  14.549  1.00 19.10 ?  33  THR   A O    1 
ATOM   903  C CB   . THR   A 1 33  ? 27.319 -7.215  16.454  1.00 22.60 ?  33  THR   A CB   1 
ATOM   904  O OG1  . THR   A 1 33  ? 27.025 -7.590  17.800  1.00 24.55 ?  33  THR   A OG1  1 
ATOM   905  C CG2  . THR   A 1 33  ? 28.810 -7.409  16.193  1.00 24.08 ?  33  THR   A CG2  1 
ATOM   906  H H    . THR   A 1 33  ? 25.081 -6.333  16.726  1.00 24.66 ?  33  THR   A H    1 
ATOM   907  H HA   . THR   A 1 33  ? 27.432 -5.200  16.828  1.00 25.01 ?  33  THR   A HA   1 
ATOM   908  H HB   . THR   A 1 33  ? 26.827 -7.784  15.840  1.00 27.13 ?  33  THR   A HB   1 
ATOM   909  H HG1  . THR   A 1 33  ? 27.248 -8.387  17.931  1.00 29.47 ?  33  THR   A HG1  1 
ATOM   910  H HG21 . THR   A 1 33  ? 29.082 -8.295  16.472  1.00 28.91 ?  33  THR   A HG21 1 
ATOM   911  H HG22 . THR   A 1 33  ? 29.002 -7.306  15.244  1.00 28.91 ?  33  THR   A HG22 1 
ATOM   912  H HG23 . THR   A 1 33  ? 29.322 -6.750  16.688  1.00 28.91 ?  33  THR   A HG23 1 
ATOM   913  N N    . VAL   A 1 34  ? 26.301 -5.637  13.874  1.00 17.82 ?  34  VAL   A N    1 
ATOM   914  C CA   . VAL   A 1 34  ? 26.486 -5.313  12.462  1.00 16.03 ?  34  VAL   A CA   1 
ATOM   915  C C    . VAL   A 1 34  ? 25.187 -4.756  11.896  1.00 15.71 ?  34  VAL   A C    1 
ATOM   916  O O    . VAL   A 1 34  ? 24.146 -5.420  11.956  1.00 16.49 ?  34  VAL   A O    1 
ATOM   917  C CB   . VAL   A 1 34  ? 26.935 -6.520  11.618  1.00 16.79 ?  34  VAL   A CB   1 
ATOM   918  C CG1  . VAL   A 1 34  ? 27.091 -6.129  10.149  1.00 16.71 ?  34  VAL   A CG1  1 
ATOM   919  C CG2  . VAL   A 1 34  ? 28.221 -7.132  12.167  1.00 18.88 ?  34  VAL   A CG2  1 
ATOM   920  H H    . VAL   A 1 34  ? 25.558 -6.048  14.033  1.00 21.40 ?  34  VAL   A H    1 
ATOM   921  H HA   . VAL   A 1 34  ? 27.162 -4.623  12.373  1.00 19.25 ?  34  VAL   A HA   1 
ATOM   922  H HB   . VAL   A 1 34  ? 26.244 -7.203  11.667  1.00 20.17 ?  34  VAL   A HB   1 
ATOM   923  H HG11 . VAL   A 1 34  ? 27.592 -6.827  9.690   1.00 20.06 ?  34  VAL   A HG11 1 
ATOM   924  H HG12 . VAL   A 1 34  ? 26.216 -6.036  9.745   1.00 20.06 ?  34  VAL   A HG12 1 
ATOM   925  H HG13 . VAL   A 1 34  ? 27.577 -5.292  10.095  1.00 20.06 ?  34  VAL   A HG13 1 
ATOM   926  H HG21 . VAL   A 1 34  ? 28.484 -7.876  11.602  1.00 22.68 ?  34  VAL   A HG21 1 
ATOM   927  H HG22 . VAL   A 1 34  ? 28.914 -6.457  12.173  1.00 22.68 ?  34  VAL   A HG22 1 
ATOM   928  H HG23 . VAL   A 1 34  ? 28.059 -7.448  13.072  1.00 22.68 ?  34  VAL   A HG23 1 
ATOM   929  N N    . VAL   A 1 35  ? 25.243 -3.542  11.355  1.00 14.81 ?  35  VAL   A N    1 
ATOM   930  C CA   . VAL   A 1 35  ? 24.210 -3.015  10.469  1.00 14.18 ?  35  VAL   A CA   1 
ATOM   931  C C    . VAL   A 1 35  ? 24.763 -3.028  9.046   1.00 14.06 ?  35  VAL   A C    1 
ATOM   932  O O    . VAL   A 1 35  ? 25.916 -2.646  8.818   1.00 14.07 ?  35  VAL   A O    1 
ATOM   933  C CB   . VAL   A 1 35  ? 23.710 -1.614  10.880  1.00 15.19 ?  35  VAL   A CB   1 
ATOM   934  C CG1  . VAL   A 1 35  ? 24.804 -0.525  10.743  1.00 16.21 ?  35  VAL   A CG1  1 
ATOM   935  C CG2  . VAL   A 1 35  ? 22.477 -1.245  10.053  1.00 16.31 ?  35  VAL   A CG2  1 
ATOM   936  H H    . VAL   A 1 35  ? 25.878 -2.984  11.493  1.00 17.78 ?  35  VAL   A H    1 
ATOM   937  H HA   . VAL   A 1 35  ? 23.442 -3.611  10.486  1.00 17.03 ?  35  VAL   A HA   1 
ATOM   938  H HB   . VAL   A 1 35  ? 23.436 -1.643  11.809  1.00 18.25 ?  35  VAL   A HB   1 
ATOM   939  H HG11 . VAL   A 1 35  ? 24.473 0.310   11.108  1.00 19.47 ?  35  VAL   A HG11 1 
ATOM   940  H HG12 . VAL   A 1 35  ? 25.595 -0.808  11.228  1.00 19.47 ?  35  VAL   A HG12 1 
ATOM   941  H HG13 . VAL   A 1 35  ? 25.023 -0.408  9.802   1.00 19.47 ?  35  VAL   A HG13 1 
ATOM   942  H HG21 . VAL   A 1 35  ? 22.130 -0.397  10.368  1.00 19.59 ?  35  VAL   A HG21 1 
ATOM   943  H HG22 . VAL   A 1 35  ? 22.735 -1.170  9.120   1.00 19.59 ?  35  VAL   A HG22 1 
ATOM   944  H HG23 . VAL   A 1 35  ? 21.809 -1.938  10.157  1.00 19.59 ?  35  VAL   A HG23 1 
ATOM   945  N N    . VAL   A 1 36  ? 23.941 -3.490  8.092   1.00 13.27 ?  36  VAL   A N    1 
ATOM   946  C CA   . VAL   A 1 36  ? 24.324 -3.530  6.684   1.00 12.48 ?  36  VAL   A CA   1 
ATOM   947  C C    . VAL   A 1 36  ? 23.880 -2.239  6.009   1.00 13.35 ?  36  VAL   A C    1 
ATOM   948  O O    . VAL   A 1 36  ? 22.730 -1.805  6.169   1.00 13.64 ?  36  VAL   A O    1 
ATOM   949  C CB   . VAL   A 1 36  ? 23.708 -4.747  5.976   1.00 13.02 ?  36  VAL   A CB   1 
ATOM   950  C CG1  . VAL   A 1 36  ? 23.983 -4.681  4.490   1.00 13.39 ?  36  VAL   A CG1  1 
ATOM   951  C CG2  . VAL   A 1 36  ? 24.245 -6.030  6.583   1.00 14.26 ?  36  VAL   A CG2  1 
ATOM   952  H H    . VAL   A 1 36  ? 23.143 -3.771  8.240   1.00 15.94 ?  36  VAL   A H    1 
ATOM   953  H HA   . VAL   A 1 36  ? 25.291 -3.600  6.615   1.00 14.99 ?  36  VAL   A HA   1 
ATOM   954  H HB   . VAL   A 1 36  ? 22.743 -4.732  6.107   1.00 15.64 ?  36  VAL   A HB   1 
ATOM   955  H HG11 . VAL   A 1 36  ? 23.847 -5.565  4.109   1.00 16.08 ?  36  VAL   A HG11 1 
ATOM   956  H HG12 . VAL   A 1 36  ? 23.378 -4.049  4.078   1.00 16.08 ?  36  VAL   A HG12 1 
ATOM   957  H HG13 . VAL   A 1 36  ? 24.903 -4.405  4.355   1.00 16.08 ?  36  VAL   A HG13 1 
ATOM   958  H HG21 . VAL   A 1 36  ? 23.852 -6.787  6.117   1.00 17.13 ?  36  VAL   A HG21 1 
ATOM   959  H HG22 . VAL   A 1 36  ? 25.207 -6.045  6.487   1.00 17.13 ?  36  VAL   A HG22 1 
ATOM   960  H HG23 . VAL   A 1 36  ? 24.003 -6.065  7.524   1.00 17.13 ?  36  VAL   A HG23 1 
ATOM   961  N N    . ASN   A 1 37  ? 24.794 -1.627  5.256   1.00 12.45 ?  37  ASN   A N    1 
ATOM   962  C CA   . ASN   A 1 37  ? 24.478 -0.510  4.381   1.00 12.30 ?  37  ASN   A CA   1 
ATOM   963  C C    . ASN   A 1 37  ? 24.330 -0.981  2.940   1.00 12.20 ?  37  ASN   A C    1 
ATOM   964  O O    . ASN   A 1 37  ? 25.108 -1.816  2.459   1.00 12.94 ?  37  ASN   A O    1 
ATOM   965  C CB   . ASN   A 1 37  ? 25.564 0.568   4.459   1.00 12.37 ?  37  ASN   A CB   1 
ATOM   966  C CG   . ASN   A 1 37  ? 25.244 1.772   3.607   1.00 13.14 ?  37  ASN   A CG   1 
ATOM   967  O OD1  . ASN   A 1 37  ? 24.076 2.109   3.411   1.00 13.47 ?  37  ASN   A OD1  1 
ATOM   968  N ND2  . ASN   A 1 37  ? 26.276 2.435   3.105   1.00 13.35 ?  37  ASN   A ND2  1 
ATOM   969  H H    . ASN   A 1 37  ? 25.630 -1.851  5.240   1.00 14.96 ?  37  ASN   A H    1 
ATOM   970  H HA   . ASN   A 1 37  ? 23.644 -0.109  4.665   1.00 14.77 ?  37  ASN   A HA   1 
ATOM   971  H HB2  . ASN   A 1 37  ? 25.653 0.869   5.378   1.00 14.85 ?  37  ASN   A HB2  1 
ATOM   972  H HB3  . ASN   A 1 37  ? 26.409 0.193   4.153   1.00 14.85 ?  37  ASN   A HB3  1 
ATOM   973  H HD21 . ASN   A 1 37  ? 26.149 3.132   2.613   1.00 16.04 ?  37  ASN   A HD21 1 
ATOM   974  H HD22 . ASN   A 1 37  ? 27.081 2.182   3.266   1.00 16.04 ?  37  ASN   A HD22 1 
ATOM   975  N N    A ALA   A 1 38  ? 23.316 -0.430  2.268   0.46 12.05 ?  38  ALA   A N    1 
ATOM   976  N N    B ALA   A 1 38  ? 23.328 -0.446  2.241   0.54 12.86 ?  38  ALA   A N    1 
ATOM   977  C CA   A ALA   A 1 38  ? 23.128 -0.535  0.823   0.46 11.76 ?  38  ALA   A CA   1 
ATOM   978  C CA   B ALA   A 1 38  ? 23.153 -0.711  0.810   0.54 13.62 ?  38  ALA   A CA   1 
ATOM   979  C C    A ALA   A 1 38  ? 24.077 0.456   0.155   0.46 12.10 ?  38  ALA   A C    1 
ATOM   980  C C    B ALA   A 1 38  ? 23.967 0.315   0.023   0.54 14.03 ?  38  ALA   A C    1 
ATOM   981  O O    A ALA   A 1 38  ? 23.708 1.574   -0.217  0.46 11.47 ?  38  ALA   A O    1 
ATOM   982  O O    B ALA   A 1 38  ? 23.466 1.348   -0.433  0.54 13.79 ?  38  ALA   A O    1 
ATOM   983  C CB   A ALA   A 1 38  ? 21.675 -0.249  0.464   0.46 12.29 ?  38  ALA   A CB   1 
ATOM   984  C CB   B ALA   A 1 38  ? 21.678 -0.688  0.434   0.54 14.09 ?  38  ALA   A CB   1 
ATOM   985  H H    A ALA   A 1 38  ? 22.698 0.033   2.653   0.46 14.47 ?  38  ALA   A H    1 
ATOM   986  H H    B ALA   A 1 38  ? 22.730 0.075   2.581   0.54 15.45 ?  38  ALA   A H    1 
ATOM   987  H HA   A ALA   A 1 38  ? 23.354 -1.428  0.529   0.46 14.12 ?  38  ALA   A HA   1 
ATOM   988  H HA   B ALA   A 1 38  ? 23.501 -1.595  0.610   0.54 16.36 ?  38  ALA   A HA   1 
ATOM   989  H HB1  A ALA   A 1 38  ? 21.564 -0.331  -0.496  0.46 14.76 ?  38  ALA   A HB1  1 
ATOM   990  H HB1  B ALA   A 1 38  ? 21.600 -0.801  -0.526  0.54 16.92 ?  38  ALA   A HB1  1 
ATOM   991  H HB2  A ALA   A 1 38  ? 21.106 -0.893  0.918   0.46 14.76 ?  38  ALA   A HB2  1 
ATOM   992  H HB2  B ALA   A 1 38  ? 21.217 -1.408  0.891   0.54 16.92 ?  38  ALA   A HB2  1 
ATOM   993  H HB3  A ALA   A 1 38  ? 21.447 0.649   0.749   0.46 14.76 ?  38  ALA   A HB3  1 
ATOM   994  H HB3  B ALA   A 1 38  ? 21.300 0.168   0.694   0.54 16.92 ?  38  ALA   A HB3  1 
ATOM   995  N N    A ALA   A 1 39  ? 25.328 0.027   0.011   0.46 11.09 ?  39  ALA   A N    1 
ATOM   996  N N    B ALA   A 1 39  ? 25.249 0.006   -0.148  0.54 14.08 ?  39  ALA   A N    1 
ATOM   997  C CA   A ALA   A 1 39  ? 26.414 0.870   -0.469  0.46 11.92 ?  39  ALA   A CA   1 
ATOM   998  C CA   B ALA   A 1 39  ? 26.224 0.972   -0.636  0.54 13.26 ?  39  ALA   A CA   1 
ATOM   999  C C    A ALA   A 1 39  ? 26.530 0.821   -1.990  0.46 11.79 ?  39  ALA   A C    1 
ATOM   1000 C C    B ALA   A 1 39  ? 26.389 0.896   -2.151  0.54 12.72 ?  39  ALA   A C    1 
ATOM   1001 O O    A ALA   A 1 39  ? 26.070 -0.116  -2.646  0.46 12.41 ?  39  ALA   A O    1 
ATOM   1002 O O    B ALA   A 1 39  ? 25.918 -0.027  -2.820  0.54 13.49 ?  39  ALA   A O    1 
ATOM   1003 C CB   A ALA   A 1 39  ? 27.730 0.383   0.141   0.46 12.55 ?  39  ALA   A CB   1 
ATOM   1004 C CB   B ALA   A 1 39  ? 27.575 0.735   0.043   0.54 13.91 ?  39  ALA   A CB   1 
ATOM   1005 H H    A ALA   A 1 39  ? 25.578 -0.774  0.187   0.46 13.32 ?  39  ALA   A H    1 
ATOM   1006 H H    B ALA   A 1 39  ? 25.583 -0.772  0.005   0.54 16.91 ?  39  ALA   A H    1 
ATOM   1007 H HA   A ALA   A 1 39  ? 26.267 1.788   -0.193  0.46 14.32 ?  39  ALA   A HA   1 
ATOM   1008 H HA   B ALA   A 1 39  ? 25.930 1.865   -0.408  0.54 15.93 ?  39  ALA   A HA   1 
ATOM   1009 H HB1  A ALA   A 1 39  ? 28.456 0.941   -0.179  0.46 15.07 ?  39  ALA   A HB1  1 
ATOM   1010 H HB1  B ALA   A 1 39  ? 28.220 1.382   -0.289  0.54 16.71 ?  39  ALA   A HB1  1 
ATOM   1011 H HB2  A ALA   A 1 39  ? 27.672 0.440   1.108   0.46 15.07 ?  39  ALA   A HB2  1 
ATOM   1012 H HB2  B ALA   A 1 39  ? 27.473 0.840   1.004   0.54 16.71 ?  39  ALA   A HB2  1 
ATOM   1013 H HB3  A ALA   A 1 39  ? 27.881 -0.539  -0.126  0.46 15.07 ?  39  ALA   A HB3  1 
ATOM   1014 H HB3  B ALA   A 1 39  ? 27.882 -0.165  -0.156  0.54 16.71 ?  39  ALA   A HB3  1 
ATOM   1015 N N    A ASN   A 1 40  ? 27.180 1.843   -2.549  0.46 13.07 ?  40  ASN   A N    1 
ATOM   1016 N N    B ASN   A 1 40  ? 27.069 1.901   -2.697  0.54 12.86 ?  40  ASN   A N    1 
ATOM   1017 C CA   A ASN   A 1 40  ? 27.688 1.796   -3.916  0.46 13.64 ?  40  ASN   A CA   1 
ATOM   1018 C CA   B ASN   A 1 40  ? 27.645 1.833   -4.033  0.54 13.25 ?  40  ASN   A CA   1 
ATOM   1019 C C    A ASN   A 1 40  ? 29.210 1.672   -3.887  0.46 13.11 ?  40  ASN   A C    1 
ATOM   1020 C C    B ASN   A 1 40  ? 29.164 1.690   -3.918  0.54 12.65 ?  40  ASN   A C    1 
ATOM   1021 O O    A ASN   A 1 40  ? 29.840 1.781   -2.831  0.46 13.30 ?  40  ASN   A O    1 
ATOM   1022 O O    B ASN   A 1 40  ? 29.741 1.797   -2.831  0.54 12.46 ?  40  ASN   A O    1 
ATOM   1023 C CB   A ASN   A 1 40  ? 27.216 2.999   -4.751  0.46 13.48 ?  40  ASN   A CB   1 
ATOM   1024 C CB   B ASN   A 1 40  ? 27.235 3.044   -4.888  0.54 12.96 ?  40  ASN   A CB   1 
ATOM   1025 C CG   A ASN   A 1 40  ? 27.579 4.338   -4.129  0.46 15.34 ?  40  ASN   A CG   1 
ATOM   1026 C CG   B ASN   A 1 40  ? 27.629 4.371   -4.263  0.54 14.55 ?  40  ASN   A CG   1 
ATOM   1027 O OD1  A ASN   A 1 40  ? 28.724 4.581   -3.753  0.46 15.88 ?  40  ASN   A OD1  1 
ATOM   1028 O OD1  B ASN   A 1 40  ? 28.810 4.659   -4.071  0.54 14.64 ?  40  ASN   A OD1  1 
ATOM   1029 N ND2  A ASN   A 1 40  ? 26.592 5.224   -4.028  0.46 15.87 ?  40  ASN   A ND2  1 
ATOM   1030 N ND2  B ASN   A 1 40  ? 26.631 5.201   -3.964  0.54 15.08 ?  40  ASN   A ND2  1 
ATOM   1031 H H    A ASN   A 1 40  ? 27.345 2.589   -2.147  0.46 15.70 ?  40  ASN   A H    1 
ATOM   1032 H H    B ASN   A 1 40  ? 27.209 2.653   -2.302  0.54 15.45 ?  40  ASN   A H    1 
ATOM   1033 H HA   A ASN   A 1 40  ? 27.341 1.001   -4.342  0.46 16.38 ?  40  ASN   A HA   1 
ATOM   1034 H HA   B ASN   A 1 40  ? 27.306 1.037   -4.476  0.54 15.91 ?  40  ASN   A HA   1 
ATOM   1035 H HB2  A ASN   A 1 40  ? 27.630 2.948   -5.636  0.46 16.19 ?  40  ASN   A HB2  1 
ATOM   1036 H HB2  B ASN   A 1 40  ? 27.671 2.979   -5.755  0.54 15.57 ?  40  ASN   A HB2  1 
ATOM   1037 H HB3  A ASN   A 1 40  ? 26.254 2.965   -4.844  0.46 16.19 ?  40  ASN   A HB3  1 
ATOM   1038 H HB3  B ASN   A 1 40  ? 26.272 3.041   -5.005  0.54 15.57 ?  40  ASN   A HB3  1 
ATOM   1039 H HD21 A ASN   A 1 40  ? 26.742 6.002   -3.694  0.46 19.06 ?  40  ASN   A HD21 1 
ATOM   1040 H HD21 B ASN   A 1 40  ? 26.799 5.968   -3.612  0.54 18.11 ?  40  ASN   A HD21 1 
ATOM   1041 H HD22 A ASN   A 1 40  ? 25.800 5.015   -4.292  0.46 19.06 ?  40  ASN   A HD22 1 
ATOM   1042 H HD22 B ASN   A 1 40  ? 25.816 4.970   -4.119  0.54 18.11 ?  40  ASN   A HD22 1 
ATOM   1043 N N    . VAL   A 1 41  ? 29.801 1.398   -5.056  1.00 13.36 ?  41  VAL   A N    1 
ATOM   1044 C CA   . VAL   A 1 41  ? 31.235 1.101   -5.085  1.00 14.01 ?  41  VAL   A CA   1 
ATOM   1045 C C    . VAL   A 1 41  ? 32.101 2.249   -4.598  1.00 14.06 ?  41  VAL   A C    1 
ATOM   1046 O O    . VAL   A 1 41  ? 33.237 2.018   -4.171  1.00 14.55 ?  41  VAL   A O    1 
ATOM   1047 C CB   . VAL   A 1 41  ? 31.729 0.597   -6.462  1.00 14.53 ?  41  VAL   A CB   1 
ATOM   1048 C CG1  . VAL   A 1 41  ? 31.054 -0.726  -6.857  1.00 15.46 ?  41  VAL   A CG1  1 
ATOM   1049 C CG2  . VAL   A 1 41  ? 31.584 1.664   -7.545  1.00 16.13 ?  41  VAL   A CG2  1 
ATOM   1050 H H    A VAL   A 1 41  ? 29.400 1.363   -5.816  0.46 16.05 ?  41  VAL   A H    1 
ATOM   1051 H H    B VAL   A 1 41  ? 29.414 1.337   -5.822  0.54 16.05 ?  41  VAL   A H    1 
ATOM   1052 H HA   . VAL   A 1 41  ? 31.391 0.371   -4.471  1.00 16.82 ?  41  VAL   A HA   1 
ATOM   1053 H HB   . VAL   A 1 41  ? 32.680 0.409   -6.388  1.00 17.46 ?  41  VAL   A HB   1 
ATOM   1054 H HG11 . VAL   A 1 41  ? 31.409 -1.029  -7.712  1.00 18.57 ?  41  VAL   A HG11 1 
ATOM   1055 H HG12 . VAL   A 1 41  ? 31.237 -1.394  -6.175  1.00 18.57 ?  41  VAL   A HG12 1 
ATOM   1056 H HG13 . VAL   A 1 41  ? 30.097 -0.587  -6.933  1.00 18.57 ?  41  VAL   A HG13 1 
ATOM   1057 H HG21 . VAL   A 1 41  ? 31.833 1.282   -8.410  1.00 19.37 ?  41  VAL   A HG21 1 
ATOM   1058 H HG22 . VAL   A 1 41  ? 30.671 1.973   -7.576  1.00 19.37 ?  41  VAL   A HG22 1 
ATOM   1059 H HG23 . VAL   A 1 41  ? 32.181 2.408   -7.345  1.00 19.37 ?  41  VAL   A HG23 1 
ATOM   1060 N N    . TYR   A 1 42  ? 31.607 3.486   -4.667  1.00 14.01 ?  42  TYR   A N    1 
ATOM   1061 C CA   . TYR   A 1 42  ? 32.369 4.664   -4.253  1.00 13.48 ?  42  TYR   A CA   1 
ATOM   1062 C C    . TYR   A 1 42  ? 32.120 5.043   -2.802  1.00 12.72 ?  42  TYR   A C    1 
ATOM   1063 O O    . TYR   A 1 42  ? 32.687 6.025   -2.317  1.00 13.45 ?  42  TYR   A O    1 
ATOM   1064 C CB   . TYR   A 1 42  ? 32.034 5.855   -5.163  1.00 14.56 ?  42  TYR   A CB   1 
ATOM   1065 C CG   . TYR   A 1 42  ? 32.212 5.542   -6.633  1.00 14.75 ?  42  TYR   A CG   1 
ATOM   1066 C CD1  . TYR   A 1 42  ? 33.469 5.322   -7.164  1.00 16.12 ?  42  TYR   A CD1  1 
ATOM   1067 C CD2  . TYR   A 1 42  ? 31.118 5.421   -7.482  1.00 16.39 ?  42  TYR   A CD2  1 
ATOM   1068 C CE1  . TYR   A 1 42  ? 33.637 4.997   -8.505  1.00 17.71 ?  42  TYR   A CE1  1 
ATOM   1069 C CE2  . TYR   A 1 42  ? 31.281 5.109   -8.827  1.00 17.15 ?  42  TYR   A CE2  1 
ATOM   1070 C CZ   . TYR   A 1 42  ? 32.549 4.893   -9.327  1.00 17.84 ?  42  TYR   A CZ   1 
ATOM   1071 O OH   . TYR   A 1 42  ? 32.728 4.594   -10.658 1.00 19.37 ?  42  TYR   A OH   1 
ATOM   1072 H H    . TYR   A 1 42  ? 30.815 3.666   -4.958  1.00 16.83 ?  42  TYR   A H    1 
ATOM   1073 H HA   . TYR   A 1 42  ? 33.311 4.478   -4.363  1.00 16.19 ?  42  TYR   A HA   1 
ATOM   1074 H HB2  . TYR   A 1 42  ? 31.104 6.113   -5.025  1.00 17.49 ?  42  TYR   A HB2  1 
ATOM   1075 H HB3  . TYR   A 1 42  ? 32.615 6.600   -4.945  1.00 17.49 ?  42  TYR   A HB3  1 
ATOM   1076 H HD1  . TYR   A 1 42  ? 34.217 5.383   -6.610  1.00 19.36 ?  42  TYR   A HD1  1 
ATOM   1077 H HD2  . TYR   A 1 42  ? 30.262 5.566   -7.146  1.00 19.68 ?  42  TYR   A HD2  1 
ATOM   1078 H HE1  . TYR   A 1 42  ? 34.490 4.859   -8.844  1.00 21.27 ?  42  TYR   A HE1  1 
ATOM   1079 H HE2  . TYR   A 1 42  ? 30.539 5.041   -9.388  1.00 20.60 ?  42  TYR   A HE2  1 
ATOM   1080 H HH   . TYR   A 1 42  ? 33.553 4.483   -10.818 1.00 23.26 ?  42  TYR   A HH   1 
ATOM   1081 N N    . LEU   A 1 43  ? 31.257 4.305   -2.115  1.00 12.88 ?  43  LEU   A N    1 
ATOM   1082 C CA   . LEU   A 1 43  ? 30.808 4.649   -0.771  1.00 12.62 ?  43  LEU   A CA   1 
ATOM   1083 C C    . LEU   A 1 43  ? 30.334 6.096   -0.674  1.00 12.84 ?  43  LEU   A C    1 
ATOM   1084 O O    . LEU   A 1 43  ? 30.598 6.792   0.309   1.00 14.13 ?  43  LEU   A O    1 
ATOM   1085 C CB   . LEU   A 1 43  ? 31.853 4.323   0.292   1.00 14.11 ?  43  LEU   A CB   1 
ATOM   1086 C CG   . LEU   A 1 43  ? 32.333 2.857   0.385   1.00 13.83 ?  43  LEU   A CG   1 
ATOM   1087 C CD1  . LEU   A 1 43  ? 33.408 2.743   1.442   1.00 14.97 ?  43  LEU   A CD1  1 
ATOM   1088 C CD2  . LEU   A 1 43  ? 31.189 1.906   0.705   1.00 13.90 ?  43  LEU   A CD2  1 
ATOM   1089 H H    . LEU   A 1 43  ? 30.900 3.577   -2.421  1.00 15.47 ?  43  LEU   A H    1 
ATOM   1090 H HA   . LEU   A 1 43  ? 30.033 4.096   -0.576  1.00 15.16 ?  43  LEU   A HA   1 
ATOM   1091 H HB2  . LEU   A 1 43  ? 32.632 4.871   0.131   1.00 16.94 ?  43  LEU   A HB2  1 
ATOM   1092 H HB3  . LEU   A 1 43  ? 31.476 4.548   1.160   1.00 16.94 ?  43  LEU   A HB3  1 
ATOM   1093 H HG   . LEU   A 1 43  ? 32.722 2.594   -0.465  1.00 16.61 ?  43  LEU   A HG   1 
ATOM   1094 H HD11 . LEU   A 1 43  ? 33.709 1.819   1.489   1.00 17.97 ?  43  LEU   A HD11 1 
ATOM   1095 H HD12 . LEU   A 1 43  ? 34.153 3.317   1.202   1.00 17.97 ?  43  LEU   A HD12 1 
ATOM   1096 H HD13 . LEU   A 1 43  ? 33.043 3.014   2.297   1.00 17.97 ?  43  LEU   A HD13 1 
ATOM   1097 H HD21 . LEU   A 1 43  ? 31.548 1.008   0.823   1.00 16.69 ?  43  LEU   A HD21 1 
ATOM   1098 H HD22 . LEU   A 1 43  ? 30.763 2.193   1.531   1.00 16.69 ?  43  LEU   A HD22 1 
ATOM   1099 H HD23 . LEU   A 1 43  ? 30.554 1.917   -0.020  1.00 16.69 ?  43  LEU   A HD23 1 
ATOM   1100 N N    A LYS   A 1 44  ? 29.611 6.542   -1.701  0.46 13.35 ?  44  LYS   A N    1 
ATOM   1101 N N    B LYS   A 1 44  ? 29.609 6.544   -1.697  0.54 13.21 ?  44  LYS   A N    1 
ATOM   1102 C CA   A LYS   A 1 44  ? 28.967 7.853   -1.697  0.46 14.23 ?  44  LYS   A CA   1 
ATOM   1103 C CA   B LYS   A 1 44  ? 28.988 7.863   -1.692  0.54 14.11 ?  44  LYS   A CA   1 
ATOM   1104 C C    A LYS   A 1 44  ? 27.545 7.646   -1.200  0.46 13.45 ?  44  LYS   A C    1 
ATOM   1105 C C    B LYS   A 1 44  ? 27.563 7.711   -1.181  0.54 13.27 ?  44  LYS   A C    1 
ATOM   1106 O O    A LYS   A 1 44  ? 26.691 7.134   -1.927  0.46 14.31 ?  44  LYS   A O    1 
ATOM   1107 O O    B LYS   A 1 44  ? 26.689 7.221   -1.901  0.54 14.75 ?  44  LYS   A O    1 
ATOM   1108 C CB   A LYS   A 1 44  ? 28.988 8.465   -3.093  0.46 16.29 ?  44  LYS   A CB   1 
ATOM   1109 C CB   B LYS   A 1 44  ? 29.010 8.464   -3.095  0.54 16.31 ?  44  LYS   A CB   1 
ATOM   1110 C CG   A LYS   A 1 44  ? 30.358 8.937   -3.548  0.46 19.87 ?  44  LYS   A CG   1 
ATOM   1111 C CG   B LYS   A 1 44  ? 30.377 8.968   -3.531  0.54 20.25 ?  44  LYS   A CG   1 
ATOM   1112 C CD   A LYS   A 1 44  ? 31.021 9.846   -2.521  0.46 24.05 ?  44  LYS   A CD   1 
ATOM   1113 C CD   B LYS   A 1 44  ? 31.044 9.814   -2.451  0.54 24.90 ?  44  LYS   A CD   1 
ATOM   1114 C CE   A LYS   A 1 44  ? 32.341 10.382  -3.036  0.46 26.60 ?  44  LYS   A CE   1 
ATOM   1115 C CE   B LYS   A 1 44  ? 32.421 10.269  -2.879  0.54 27.50 ?  44  LYS   A CE   1 
ATOM   1116 N NZ   A LYS   A 1 44  ? 33.158 10.977  -1.948  0.46 27.35 ?  44  LYS   A NZ   1 
ATOM   1117 N NZ   B LYS   A 1 44  ? 33.233 10.724  -1.721  0.54 27.73 ?  44  LYS   A NZ   1 
ATOM   1118 H H    A LYS   A 1 44  ? 29.468 6.094   -2.424  0.46 16.03 ?  44  LYS   A H    1 
ATOM   1119 H H    B LYS   A 1 44  ? 29.461 6.095   -2.420  0.54 15.87 ?  44  LYS   A H    1 
ATOM   1120 H HA   A LYS   A 1 44  ? 29.409 8.441   -1.072  0.46 17.09 ?  44  LYS   A HA   1 
ATOM   1121 H HA   B LYS   A 1 44  ? 29.443 8.442   -1.066  0.54 16.95 ?  44  LYS   A HA   1 
ATOM   1122 H HB2  A LYS   A 1 44  ? 28.678 7.804   -3.730  0.46 19.56 ?  44  LYS   A HB2  1 
ATOM   1123 H HB2  B LYS   A 1 44  ? 28.725 7.789   -3.730  0.54 19.59 ?  44  LYS   A HB2  1 
ATOM   1124 H HB3  A LYS   A 1 44  ? 28.393 9.235   -3.107  0.46 19.56 ?  44  LYS   A HB3  1 
ATOM   1125 H HB3  B LYS   A 1 44  ? 28.395 9.218   -3.122  0.54 19.59 ?  44  LYS   A HB3  1 
ATOM   1126 H HG2  A LYS   A 1 44  ? 30.929 8.167   -3.684  0.46 23.86 ?  44  LYS   A HG2  1 
ATOM   1127 H HG2  B LYS   A 1 44  ? 30.948 8.209   -3.719  0.54 24.31 ?  44  LYS   A HG2  1 
ATOM   1128 H HG3  A LYS   A 1 44  ? 30.264 9.437   -4.375  0.46 23.86 ?  44  LYS   A HG3  1 
ATOM   1129 H HG3  B LYS   A 1 44  ? 30.274 9.518   -4.325  0.54 24.31 ?  44  LYS   A HG3  1 
ATOM   1130 H HD2  A LYS   A 1 44  ? 30.431 10.593  -2.325  0.46 28.88 ?  44  LYS   A HD2  1 
ATOM   1131 H HD2  B LYS   A 1 44  ? 30.486 10.590  -2.263  0.54 29.90 ?  44  LYS   A HD2  1 
ATOM   1132 H HD3  A LYS   A 1 44  ? 31.202 9.340   -1.712  0.46 28.88 ?  44  LYS   A HD3  1 
ATOM   1133 H HD3  B LYS   A 1 44  ? 31.162 9.284   -1.646  0.54 29.90 ?  44  LYS   A HD3  1 
ATOM   1134 H HE2  A LYS   A 1 44  ? 32.846 9.652   -3.430  0.46 31.93 ?  44  LYS   A HE2  1 
ATOM   1135 H HE2  B LYS   A 1 44  ? 32.881 9.526   -3.299  0.54 33.01 ?  44  LYS   A HE2  1 
ATOM   1136 H HE3  A LYS   A 1 44  ? 32.168 11.067  -3.697  0.46 31.93 ?  44  LYS   A HE3  1 
ATOM   1137 H HE3  B LYS   A 1 44  ? 32.331 11.005  -3.499  0.54 33.01 ?  44  LYS   A HE3  1 
ATOM   1138 H HZ1  A LYS   A 1 44  ? 33.924 11.282  -2.276  0.46 32.83 ?  44  LYS   A HZ1  1 
ATOM   1139 H HZ1  B LYS   A 1 44  ? 34.034 10.986  -1.999  0.54 33.29 ?  44  LYS   A HZ1  1 
ATOM   1140 H HZ2  A LYS   A 1 44  ? 32.714 11.650  -1.570  0.46 32.83 ?  44  LYS   A HZ2  1 
ATOM   1141 H HZ2  B LYS   A 1 44  ? 32.827 11.409  -1.318  0.54 33.29 ?  44  LYS   A HZ2  1 
ATOM   1142 H HZ3  A LYS   A 1 44  ? 33.331 10.362  -1.327  0.46 32.83 ?  44  LYS   A HZ3  1 
ATOM   1143 H HZ3  B LYS   A 1 44  ? 33.328 10.062  -1.136  0.54 33.29 ?  44  LYS   A HZ3  1 
ATOM   1144 N N    A HIS   A 1 45  ? 27.292 8.035   0.049   0.46 13.28 ?  45  HIS   A N    1 
ATOM   1145 N N    B HIS   A 1 45  ? 27.332 8.130   0.063   0.54 13.45 ?  45  HIS   A N    1 
ATOM   1146 C CA   A HIS   A 1 45  ? 26.053 7.677   0.738   0.46 12.97 ?  45  HIS   A CA   1 
ATOM   1147 C CA   B HIS   A 1 45  ? 26.093 7.833   0.775   0.54 13.62 ?  45  HIS   A CA   1 
ATOM   1148 C C    A HIS   A 1 45  ? 25.027 8.800   0.569   0.46 13.26 ?  45  HIS   A C    1 
ATOM   1149 C C    B HIS   A 1 45  ? 25.140 9.014   0.614   0.54 15.10 ?  45  HIS   A C    1 
ATOM   1150 O O    A HIS   A 1 45  ? 24.659 9.508   1.508   0.46 14.40 ?  45  HIS   A O    1 
ATOM   1151 O O    B HIS   A 1 45  ? 24.975 9.842   1.511   0.54 17.23 ?  45  HIS   A O    1 
ATOM   1152 C CB   A HIS   A 1 45  ? 26.339 7.388   2.207   0.46 12.91 ?  45  HIS   A CB   1 
ATOM   1153 C CB   B HIS   A 1 45  ? 26.390 7.574   2.246   0.54 12.66 ?  45  HIS   A CB   1 
ATOM   1154 C CG   A HIS   A 1 45  ? 27.469 6.429   2.427   0.46 12.53 ?  45  HIS   A CG   1 
ATOM   1155 C CG   B HIS   A 1 45  ? 27.483 6.582   2.482   0.54 12.61 ?  45  HIS   A CG   1 
ATOM   1156 N ND1  A HIS   A 1 45  ? 27.477 5.144   1.923   0.46 12.33 ?  45  HIS   A ND1  1 
ATOM   1157 N ND1  B HIS   A 1 45  ? 27.463 5.304   1.966   0.54 12.98 ?  45  HIS   A ND1  1 
ATOM   1158 C CD2  A HIS   A 1 45  ? 28.641 6.582   3.091   0.46 12.93 ?  45  HIS   A CD2  1 
ATOM   1159 C CD2  B HIS   A 1 45  ? 28.640 6.692   3.177   0.54 13.31 ?  45  HIS   A CD2  1 
ATOM   1160 C CE1  A HIS   A 1 45  ? 28.603 4.547   2.276   0.46 12.61 ?  45  HIS   A CE1  1 
ATOM   1161 C CE1  B HIS   A 1 45  ? 28.560 4.667   2.340   0.54 13.06 ?  45  HIS   A CE1  1 
ATOM   1162 N NE2  A HIS   A 1 45  ? 29.328 5.398   2.981   0.46 12.92 ?  45  HIS   A NE2  1 
ATOM   1163 N NE2  B HIS   A 1 45  ? 29.295 5.490   3.069   0.54 13.41 ?  45  HIS   A NE2  1 
ATOM   1164 H H    A HIS   A 1 45  ? 27.824 8.517   0.528   0.46 15.96 ?  45  HIS   A H    1 
ATOM   1165 H H    B HIS   A 1 45  ? 27.887 8.602   0.523   0.54 16.15 ?  45  HIS   A H    1 
ATOM   1166 H HA   A HIS   A 1 45  ? 25.688 6.870   0.342   0.46 15.58 ?  45  HIS   A HA   1 
ATOM   1167 H HA   B HIS   A 1 45  ? 25.682 7.036   0.397   0.54 16.36 ?  45  HIS   A HA   1 
ATOM   1168 H HB2  A HIS   A 1 45  ? 26.565 8.220   2.653   0.46 15.51 ?  45  HIS   A HB2  1 
ATOM   1169 H HB2  B HIS   A 1 45  ? 26.653 8.407   2.664   0.54 15.20 ?  45  HIS   A HB2  1 
ATOM   1170 H HB3  A HIS   A 1 45  ? 25.547 7.003   2.614   0.46 15.51 ?  45  HIS   A HB3  1 
ATOM   1171 H HB3  B HIS   A 1 45  ? 25.589 7.230   2.673   0.54 15.20 ?  45  HIS   A HB3  1 
ATOM   1172 H HD2  A HIS   A 1 45  ? 28.931 7.346   3.539   0.46 15.54 ?  45  HIS   A HD2  1 
ATOM   1173 H HD2  B HIS   A 1 45  ? 28.941 7.444   3.637   0.54 15.99 ?  45  HIS   A HD2  1 
ATOM   1174 H HE1  A HIS   A 1 45  ? 28.849 3.675   2.064   0.46 15.15 ?  45  HIS   A HE1  1 
ATOM   1175 H HE1  B HIS   A 1 45  ? 28.784 3.790   2.122   0.54 15.68 ?  45  HIS   A HE1  1 
ATOM   1176 H HE2  A HIS   A 1 45  ? 30.105 5.234   3.323   0.46 15.52 ?  45  HIS   A HE2  1 
ATOM   1177 H HE2  B HIS   A 1 45  ? 30.056 5.298   3.428   0.54 16.11 ?  45  HIS   A HE2  1 
ATOM   1178 N N    A GLY   A 1 46  ? 24.539 8.936   -0.664  0.46 14.04 ?  46  GLY   A N    1 
ATOM   1179 N N    B GLY   A 1 46  ? 24.479 9.076   -0.541  0.54 15.72 ?  46  GLY   A N    1 
ATOM   1180 C CA   A GLY   A 1 46  ? 23.748 10.096  -1.035  0.46 14.73 ?  46  GLY   A CA   1 
ATOM   1181 C CA   B GLY   A 1 46  ? 23.657 10.234  -0.844  0.54 15.79 ?  46  GLY   A CA   1 
ATOM   1182 C C    A GLY   A 1 46  ? 22.254 9.975   -0.821  0.46 15.17 ?  46  GLY   A C    1 
ATOM   1183 C C    B GLY   A 1 46  ? 22.195 10.088  -0.483  0.54 15.24 ?  46  GLY   A C    1 
ATOM   1184 O O    A GLY   A 1 46  ? 21.571 10.975  -0.568  0.46 15.19 ?  46  GLY   A O    1 
ATOM   1185 O O    B GLY   A 1 46  ? 21.589 10.996  0.098   0.54 16.05 ?  46  GLY   A O    1 
ATOM   1186 H H    A GLY   A 1 46  ? 24.659 8.367   -1.299  0.46 16.86 ?  46  GLY   A H    1 
ATOM   1187 H H    B GLY   A 1 46  ? 24.496 8.465   -1.156  0.54 18.88 ?  46  GLY   A H    1 
ATOM   1188 H HA2  A GLY   A 1 46  ? 24.060 10.858  -0.524  0.46 17.69 ?  46  GLY   A HA2  1 
ATOM   1189 H HA2  B GLY   A 1 46  ? 24.012 10.998  -0.363  0.54 18.96 ?  46  GLY   A HA2  1 
ATOM   1190 H HA3  A GLY   A 1 46  ? 23.894 10.282  -1.972  0.46 17.69 ?  46  GLY   A HA3  1 
ATOM   1191 H HA3  B GLY   A 1 46  ? 23.719 10.417  -1.791  0.54 18.96 ?  46  GLY   A HA3  1 
ATOM   1192 N N    A GLY   A 1 47  ? 21.730 8.763   -0.943  0.46 15.89 ?  47  GLY   A N    1 
ATOM   1193 N N    B GLY   A 1 47  ? 21.610 8.959   -0.850  0.54 15.15 ?  47  GLY   A N    1 
ATOM   1194 C CA   A GLY   A 1 47  ? 20.297 8.572   -0.882  0.46 15.19 ?  47  GLY   A CA   1 
ATOM   1195 C CA   B GLY   A 1 47  ? 20.200 8.740   -0.617  0.54 14.94 ?  47  GLY   A CA   1 
ATOM   1196 C C    A GLY   A 1 47  ? 19.957 7.138   -0.545  0.46 14.72 ?  47  GLY   A C    1 
ATOM   1197 C C    B GLY   A 1 47  ? 19.915 7.308   -0.220  0.54 14.99 ?  47  GLY   A C    1 
ATOM   1198 O O    A GLY   A 1 47  ? 20.833 6.292   -0.349  0.46 14.31 ?  47  GLY   A O    1 
ATOM   1199 O O    B GLY   A 1 47  ? 20.835 6.516   0.015   0.54 15.28 ?  47  GLY   A O    1 
ATOM   1200 H H    A GLY   A 1 47  ? 22.180 8.036   -1.056  0.46 19.09 ?  47  GLY   A H    1 
ATOM   1201 H H    B GLY   A 1 47  ? 22.012 8.297   -1.234  0.54 18.19 ?  47  GLY   A H    1 
ATOM   1202 H HA2  A GLY   A 1 47  ? 19.911 9.157   -0.210  0.46 18.25 ?  47  GLY   A HA2  1 
ATOM   1203 H HA2  B GLY   A 1 47  ? 19.889 9.326   0.094   0.54 17.95 ?  47  GLY   A HA2  1 
ATOM   1204 H HA3  A GLY   A 1 47  ? 19.902 8.781   -1.742  0.46 18.25 ?  47  GLY   A HA3  1 
ATOM   1205 H HA3  B GLY   A 1 47  ? 19.702 8.952   -1.426  0.54 17.95 ?  47  GLY   A HA3  1 
ATOM   1206 N N    A GLY   A 1 48  ? 18.657 6.871   -0.481  0.46 14.28 ?  48  GLY   A N    1 
ATOM   1207 N N    B GLY   A 1 48  ? 18.639 6.958   -0.139  0.54 14.49 ?  48  GLY   A N    1 
ATOM   1208 C CA   A GLY   A 1 48  ? 18.204 5.553   -0.097  0.46 14.68 ?  48  GLY   A CA   1 
ATOM   1209 C CA   B GLY   A 1 48  ? 18.272 5.616   0.260   0.54 14.17 ?  48  GLY   A CA   1 
ATOM   1210 C C    A GLY   A 1 48  ? 18.610 5.227   1.327   0.46 14.28 ?  48  GLY   A C    1 
ATOM   1211 C C    B GLY   A 1 48  ? 18.786 5.295   1.660   0.54 14.05 ?  48  GLY   A C    1 
ATOM   1212 O O    A GLY   A 1 48  ? 18.739 6.104   2.190   0.46 14.36 ?  48  GLY   A O    1 
ATOM   1213 O O    B GLY   A 1 48  ? 19.019 6.172   2.500   0.54 14.47 ?  48  GLY   A O    1 
ATOM   1214 H H    A GLY   A 1 48  ? 18.025 7.434   -0.648  0.46 17.15 ?  48  GLY   A H    1 
ATOM   1215 H H    B GLY   A 1 48  ? 17.976 7.477   -0.309  0.54 17.40 ?  48  GLY   A H    1 
ATOM   1216 H HA2  A GLY   A 1 48  ? 17.239 5.501   -0.168  0.46 17.63 ?  48  GLY   A HA2  1 
ATOM   1217 H HA2  B GLY   A 1 48  ? 17.304 5.525   0.241   0.54 17.02 ?  48  GLY   A HA2  1 
ATOM   1218 H HA3  A GLY   A 1 48  ? 18.597 4.891   -0.687  0.46 17.63 ?  48  GLY   A HA3  1 
ATOM   1219 H HA3  B GLY   A 1 48  ? 18.651 4.973   -0.367  0.54 17.02 ?  48  GLY   A HA3  1 
ATOM   1220 N N    A VAL   A 1 49  ? 18.814 3.934   1.577   0.46 14.14 ?  49  VAL   A N    1 
ATOM   1221 N N    B VAL   A 1 49  ? 18.950 3.992   1.899   0.54 13.25 ?  49  VAL   A N    1 
ATOM   1222 C CA   A VAL   A 1 49  ? 19.252 3.489   2.898   0.46 14.40 ?  49  VAL   A CA   1 
ATOM   1223 C CA   B VAL   A 1 49  ? 19.505 3.520   3.166   0.54 12.81 ?  49  VAL   A CA   1 
ATOM   1224 C C    A VAL   A 1 49  ? 20.568 4.154   3.278   0.46 12.82 ?  49  VAL   A C    1 
ATOM   1225 C C    B VAL   A 1 49  ? 20.835 4.197   3.473   0.54 12.23 ?  49  VAL   A C    1 
ATOM   1226 O O    A VAL   A 1 49  ? 20.741 4.626   4.406   0.46 12.75 ?  49  VAL   A O    1 
ATOM   1227 O O    B VAL   A 1 49  ? 21.097 4.583   4.619   0.54 12.48 ?  49  VAL   A O    1 
ATOM   1228 C CB   A VAL   A 1 49  ? 19.382 1.956   2.923   0.46 16.87 ?  49  VAL   A CB   1 
ATOM   1229 C CB   B VAL   A 1 49  ? 19.658 1.987   3.134   0.54 13.49 ?  49  VAL   A CB   1 
ATOM   1230 C CG1  A VAL   A 1 49  ? 20.093 1.504   4.188   0.46 17.14 ?  49  VAL   A CG1  1 
ATOM   1231 C CG1  B VAL   A 1 49  ? 20.552 1.517   4.268   0.54 12.91 ?  49  VAL   A CG1  1 
ATOM   1232 C CG2  A VAL   A 1 49  ? 18.012 1.302   2.814   0.46 18.17 ?  49  VAL   A CG2  1 
ATOM   1233 C CG2  B VAL   A 1 49  ? 18.296 1.294   3.205   0.54 14.53 ?  49  VAL   A CG2  1 
ATOM   1234 H H    A VAL   A 1 49  ? 18.714 3.299   1.005   0.46 16.98 ?  49  VAL   A H    1 
ATOM   1235 H H    B VAL   A 1 49  ? 18.750 3.368   1.345   0.54 15.92 ?  49  VAL   A H    1 
ATOM   1236 H HA   A VAL   A 1 49  ? 18.583 3.741   3.556   0.46 17.30 ?  49  VAL   A HA   1 
ATOM   1237 H HA   B VAL   A 1 49  ? 18.889 3.741   3.881   0.54 15.39 ?  49  VAL   A HA   1 
ATOM   1238 H HB   A VAL   A 1 49  ? 19.914 1.671   2.163   0.46 20.26 ?  49  VAL   A HB   1 
ATOM   1239 H HB   B VAL   A 1 49  ? 20.075 1.730   2.295   0.54 16.21 ?  49  VAL   A HB   1 
ATOM   1240 H HG11 A VAL   A 1 49  ? 19.907 0.562   4.332   0.46 20.58 ?  49  VAL   A HG11 1 
ATOM   1241 H HG11 B VAL   A 1 49  ? 20.397 0.572   4.416   0.54 15.50 ?  49  VAL   A HG11 1 
ATOM   1242 H HG12 A VAL   A 1 49  ? 21.048 1.638   4.084   0.46 20.58 ?  49  VAL   A HG12 1 
ATOM   1243 H HG12 B VAL   A 1 49  ? 21.480 1.664   4.022   0.54 15.50 ?  49  VAL   A HG12 1 
ATOM   1244 H HG13 A VAL   A 1 49  ? 19.762 2.021   4.938   0.46 20.58 ?  49  VAL   A HG13 1 
ATOM   1245 H HG13 B VAL   A 1 49  ? 20.334 2.017   5.069   0.54 15.50 ?  49  VAL   A HG13 1 
ATOM   1246 H HG21 A VAL   A 1 49  ? 18.122 0.339   2.827   0.46 21.82 ?  49  VAL   A HG21 1 
ATOM   1247 H HG21 B VAL   A 1 49  ? 18.427 0.333   3.165   0.54 17.45 ?  49  VAL   A HG21 1 
ATOM   1248 H HG22 A VAL   A 1 49  ? 17.470 1.585   3.567   0.46 21.82 ?  49  VAL   A HG22 1 
ATOM   1249 H HG22 B VAL   A 1 49  ? 17.864 1.533   4.040   0.54 17.45 ?  49  VAL   A HG22 1 
ATOM   1250 H HG23 A VAL   A 1 49  ? 17.598 1.579   1.983   0.46 21.82 ?  49  VAL   A HG23 1 
ATOM   1251 H HG23 B VAL   A 1 49  ? 17.752 1.584   2.456   0.54 17.45 ?  49  VAL   A HG23 1 
ATOM   1252 N N    A ALA   A 1 50  ? 21.526 4.173   2.347   0.46 11.77 ?  50  ALA   A N    1 
ATOM   1253 N N    B ALA   A 1 50  ? 21.710 4.318   2.468   0.54 13.30 ?  50  ALA   A N    1 
ATOM   1254 C CA   A ALA   A 1 50  ? 22.843 4.732   2.644   0.46 11.98 ?  50  ALA   A CA   1 
ATOM   1255 C CA   B ALA   A 1 50  ? 23.042 4.868   2.713   0.54 13.02 ?  50  ALA   A CA   1 
ATOM   1256 C C    A ALA   A 1 50  ? 22.756 6.204   3.026   0.46 12.01 ?  50  ALA   A C    1 
ATOM   1257 C C    B ALA   A 1 50  ? 22.963 6.315   3.187   0.54 13.21 ?  50  ALA   A C    1 
ATOM   1258 O O    A ALA   A 1 50  ? 23.405 6.642   3.983   0.46 12.27 ?  50  ALA   A O    1 
ATOM   1259 O O    B ALA   A 1 50  ? 23.571 6.682   4.200   0.54 13.52 ?  50  ALA   A O    1 
ATOM   1260 C CB   A ALA   A 1 50  ? 23.758 4.552   1.437   0.46 12.56 ?  50  ALA   A CB   1 
ATOM   1261 C CB   B ALA   A 1 50  ? 23.900 4.763   1.452   0.54 13.51 ?  50  ALA   A CB   1 
ATOM   1262 H H    A ALA   A 1 50  ? 21.435 3.880   1.550   0.46 14.14 ?  50  ALA   A H    1 
ATOM   1263 H H    B ALA   A 1 50  ? 21.552 4.108   1.648   0.54 15.97 ?  50  ALA   A H    1 
ATOM   1264 H HA   A ALA   A 1 50  ? 23.226 4.261   3.396   0.46 14.39 ?  50  ALA   A HA   1 
ATOM   1265 H HA   B ALA   A 1 50  ? 23.469 4.355   3.410   0.54 15.63 ?  50  ALA   A HA   1 
ATOM   1266 H HB1  A ALA   A 1 50  ? 24.627 4.930   1.642   0.46 15.08 ?  50  ALA   A HB1  1 
ATOM   1267 H HB1  B ALA   A 1 50  ? 24.780 5.132   1.637   0.54 16.22 ?  50  ALA   A HB1  1 
ATOM   1268 H HB2  A ALA   A 1 50  ? 23.842 3.605   1.249   0.46 15.08 ?  50  ALA   A HB2  1 
ATOM   1269 H HB2  B ALA   A 1 50  ? 23.983 3.829   1.202   0.54 16.22 ?  50  ALA   A HB2  1 
ATOM   1270 H HB3  A ALA   A 1 50  ? 23.369 5.010   0.675   0.46 15.08 ?  50  ALA   A HB3  1 
ATOM   1271 H HB3  B ALA   A 1 50  ? 23.479 5.262   0.735   0.54 16.22 ?  50  ALA   A HB3  1 
ATOM   1272 N N    A GLY   A 1 51  ? 21.963 6.983   2.292   0.46 11.76 ?  51  GLY   A N    1 
ATOM   1273 N N    B GLY   A 1 51  ? 22.208 7.152   2.472   0.54 12.95 ?  51  GLY   A N    1 
ATOM   1274 C CA   A GLY   A 1 51  ? 21.823 8.390   2.625   0.46 13.13 ?  51  GLY   A CA   1 
ATOM   1275 C CA   B GLY   A 1 51  ? 22.044 8.524   2.914   0.54 12.74 ?  51  GLY   A CA   1 
ATOM   1276 C C    A GLY   A 1 51  ? 21.241 8.602   4.009   0.46 12.96 ?  51  GLY   A C    1 
ATOM   1277 C C    B GLY   A 1 51  ? 21.375 8.609   4.270   0.54 13.06 ?  51  GLY   A C    1 
ATOM   1278 O O    A GLY   A 1 51  ? 21.677 9.490   4.744   0.46 13.51 ?  51  GLY   A O    1 
ATOM   1279 O O    B GLY   A 1 51  ? 21.711 9.474   5.082   0.54 13.35 ?  51  GLY   A O    1 
ATOM   1280 H H    A GLY   A 1 51  ? 21.509 6.728   1.612   0.46 14.13 ?  51  GLY   A H    1 
ATOM   1281 H H    B GLY   A 1 51  ? 21.793 6.946   1.745   0.54 15.55 ?  51  GLY   A H    1 
ATOM   1282 H HA2  A GLY   A 1 51  ? 22.687 8.823   2.597   0.46 15.77 ?  51  GLY   A HA2  1 
ATOM   1283 H HA2  B GLY   A 1 51  ? 22.911 8.951   2.965   0.54 15.30 ?  51  GLY   A HA2  1 
ATOM   1284 H HA3  A GLY   A 1 51  ? 21.240 8.823   1.978   0.46 15.77 ?  51  GLY   A HA3  1 
ATOM   1285 H HA3  B GLY   A 1 51  ? 21.502 9.005   2.262   0.54 15.30 ?  51  GLY   A HA3  1 
ATOM   1286 N N    A ALA   A 1 52  ? 20.260 7.778   4.389   0.46 13.32 ?  52  ALA   A N    1 
ATOM   1287 N N    B ALA   A 1 52  ? 20.453 7.687   4.548   0.54 13.37 ?  52  ALA   A N    1 
ATOM   1288 C CA   A ALA   A 1 52  ? 19.640 7.920   5.702   0.46 13.43 ?  52  ALA   A CA   1 
ATOM   1289 C CA   B ALA   A 1 52  ? 19.748 7.684   5.824   0.54 13.36 ?  52  ALA   A CA   1 
ATOM   1290 C C    A ALA   A 1 52  ? 20.582 7.482   6.819   0.46 13.36 ?  52  ALA   A C    1 
ATOM   1291 C C    B ALA   A 1 52  ? 20.676 7.294   6.970   0.54 12.53 ?  52  ALA   A C    1 
ATOM   1292 O O    A ALA   A 1 52  ? 20.675 8.150   7.856   0.46 14.20 ?  52  ALA   A O    1 
ATOM   1293 O O    B ALA   A 1 52  ? 20.715 7.968   8.009   0.54 13.68 ?  52  ALA   A O    1 
ATOM   1294 C CB   A ALA   A 1 52  ? 18.324 7.138   5.748   0.46 13.57 ?  52  ALA   A CB   1 
ATOM   1295 C CB   B ALA   A 1 52  ? 18.542 6.744   5.744   0.54 14.83 ?  52  ALA   A CB   1 
ATOM   1296 H H    A ALA   A 1 52  ? 19.946 7.131   3.911   0.46 16.00 ?  52  ALA   A H    1 
ATOM   1297 H H    B ALA   A 1 52  ? 20.229 7.044   4.013   0.54 16.06 ?  52  ALA   A H    1 
ATOM   1298 H HA   A ALA   A 1 52  ? 19.425 8.851   5.844   0.46 16.13 ?  52  ALA   A HA   1 
ATOM   1299 H HA   B ALA   A 1 52  ? 19.417 8.576   5.994   0.54 16.05 ?  52  ALA   A HA   1 
ATOM   1300 H HB1  A ALA   A 1 52  ? 17.918 7.242   6.624   0.46 16.30 ?  52  ALA   A HB1  1 
ATOM   1301 H HB1  B ALA   A 1 52  ? 18.076 6.753   6.596   0.54 17.82 ?  52  ALA   A HB1  1 
ATOM   1302 H HB2  A ALA   A 1 52  ? 17.721 7.483   5.066   0.46 16.30 ?  52  ALA   A HB2  1 
ATOM   1303 H HB2  B ALA   A 1 52  ? 17.942 7.052   5.042   0.54 17.82 ?  52  ALA   A HB2  1 
ATOM   1304 H HB3  A ALA   A 1 52  ? 18.501 6.197   5.579   0.46 16.30 ?  52  ALA   A HB3  1 
ATOM   1305 H HB3  B ALA   A 1 52  ? 18.846 5.845   5.544   0.54 17.82 ?  52  ALA   A HB3  1 
ATOM   1306 N N    A LEU   A 1 53  ? 21.295 6.367   6.632   0.46 13.25 ?  53  LEU   A N    1 
ATOM   1307 N N    B LEU   A 1 53  ? 21.432 6.206   6.807   0.54 12.13 ?  53  LEU   A N    1 
ATOM   1308 C CA   A LEU   A 1 53  ? 22.228 5.913   7.659   0.46 13.58 ?  53  LEU   A CA   1 
ATOM   1309 C CA   B LEU   A 1 53  ? 22.409 5.846   7.830   0.54 12.16 ?  53  LEU   A CA   1 
ATOM   1310 C C    A LEU   A 1 53  ? 23.335 6.933   7.883   0.46 14.60 ?  53  LEU   A C    1 
ATOM   1311 C C    B LEU   A 1 53  ? 23.422 6.967   8.016   0.54 12.30 ?  53  LEU   A C    1 
ATOM   1312 O O    A LEU   A 1 53  ? 23.716 7.214   9.025   0.46 16.07 ?  53  LEU   A O    1 
ATOM   1313 O O    B LEU   A 1 53  ? 23.696 7.402   9.141   0.54 12.69 ?  53  LEU   A O    1 
ATOM   1314 C CB   A LEU   A 1 53  ? 22.828 4.562   7.263   0.46 13.76 ?  53  LEU   A CB   1 
ATOM   1315 C CB   B LEU   A 1 53  ? 23.121 4.543   7.450   0.54 12.64 ?  53  LEU   A CB   1 
ATOM   1316 C CG   A LEU   A 1 53  ? 21.888 3.357   7.330   0.46 13.57 ?  53  LEU   A CG   1 
ATOM   1317 C CG   B LEU   A 1 53  ? 22.330 3.239   7.533   0.54 12.70 ?  53  LEU   A CG   1 
ATOM   1318 C CD1  A LEU   A 1 53  ? 22.587 2.128   6.774   0.46 13.25 ?  53  LEU   A CD1  1 
ATOM   1319 C CD1  B LEU   A 1 53  ? 23.134 2.133   6.889   0.54 13.05 ?  53  LEU   A CD1  1 
ATOM   1320 C CD2  A LEU   A 1 53  ? 21.423 3.112   8.761   0.46 14.08 ?  53  LEU   A CD2  1 
ATOM   1321 C CD2  B LEU   A 1 53  ? 21.999 2.898   8.972   0.54 12.98 ?  53  LEU   A CD2  1 
ATOM   1322 H H    A LEU   A 1 53  ? 21.259 5.868   5.934   0.46 15.91 ?  53  LEU   A H    1 
ATOM   1323 H H    B LEU   A 1 53  ? 21.390 5.665   6.134   0.54 14.57 ?  53  LEU   A H    1 
ATOM   1324 H HA   A LEU   A 1 53  ? 21.754 5.799   8.498   0.46 16.31 ?  53  LEU   A HA   1 
ATOM   1325 H HA   B LEU   A 1 53  ? 21.951 5.703   8.673   0.54 14.61 ?  53  LEU   A HA   1 
ATOM   1326 H HB2  A LEU   A 1 53  ? 23.148 4.630   6.348   0.46 16.53 ?  53  LEU   A HB2  1 
ATOM   1327 H HB2  B LEU   A 1 53  ? 23.430 4.630   6.534   0.54 15.18 ?  53  LEU   A HB2  1 
ATOM   1328 H HB3  A LEU   A 1 53  ? 23.578 4.376   7.850   0.46 16.53 ?  53  LEU   A HB3  1 
ATOM   1329 H HB3  B LEU   A 1 53  ? 23.889 4.445   8.034   0.54 15.18 ?  53  LEU   A HB3  1 
ATOM   1330 H HG   A LEU   A 1 53  ? 21.105 3.537   6.783   0.46 16.30 ?  53  LEU   A HG   1 
ATOM   1331 H HG   B LEU   A 1 53  ? 21.499 3.337   7.041   0.54 15.25 ?  53  LEU   A HG   1 
ATOM   1332 H HD11 A LEU   A 1 53  ? 21.982 1.374   6.822   0.46 15.92 ?  53  LEU   A HD11 1 
ATOM   1333 H HD11 B LEU   A 1 53  ? 22.634 1.305   6.954   0.54 15.67 ?  53  LEU   A HD11 1 
ATOM   1334 H HD12 A LEU   A 1 53  ? 22.837 2.297   5.853   0.46 15.92 ?  53  LEU   A HD12 1 
ATOM   1335 H HD12 B LEU   A 1 53  ? 23.288 2.356   5.959   0.54 15.67 ?  53  LEU   A HD12 1 
ATOM   1336 H HD13 A LEU   A 1 53  ? 23.380 1.953   7.306   0.46 15.92 ?  53  LEU   A HD13 1 
ATOM   1337 H HD13 B LEU   A 1 53  ? 23.979 2.048   7.356   0.54 15.67 ?  53  LEU   A HD13 1 
ATOM   1338 H HD21 A LEU   A 1 53  ? 20.939 2.276   8.797   0.46 16.91 ?  53  LEU   A HD21 1 
ATOM   1339 H HD21 B LEU   A 1 53  ? 21.544 2.040   8.997   0.54 15.59 ?  53  LEU   A HD21 1 
ATOM   1340 H HD22 A LEU   A 1 53  ? 22.202 3.071   9.341   0.46 16.91 ?  53  LEU   A HD22 1 
ATOM   1341 H HD22 B LEU   A 1 53  ? 22.820 2.852   9.484   0.54 15.59 ?  53  LEU   A HD22 1 
ATOM   1342 H HD23 A LEU   A 1 53  ? 20.846 3.841   9.040   0.46 16.91 ?  53  LEU   A HD23 1 
ATOM   1343 H HD23 B LEU   A 1 53  ? 21.419 3.587   9.337   0.54 15.59 ?  53  LEU   A HD23 1 
ATOM   1344 N N    A ASN   A 1 54  ? 23.875 7.495   6.804   0.46 14.06 ?  54  ASN   A N    1 
ATOM   1345 N N    B ASN   A 1 54  ? 23.976 7.464   6.914   0.54 12.60 ?  54  ASN   A N    1 
ATOM   1346 C CA   A ASN   A 1 54  ? 24.948 8.467   6.960   0.46 14.05 ?  54  ASN   A CA   1 
ATOM   1347 C CA   B ASN   A 1 54  ? 25.004 8.488   7.031   0.54 12.73 ?  54  ASN   A CA   1 
ATOM   1348 C C    A ASN   A 1 54  ? 24.461 9.708   7.704   0.46 14.14 ?  54  ASN   A C    1 
ATOM   1349 C C    B ASN   A 1 54  ? 24.469 9.737   7.731   0.54 13.26 ?  54  ASN   A C    1 
ATOM   1350 O O    A ASN   A 1 54  ? 25.165 10.241  8.572   0.46 14.91 ?  54  ASN   A O    1 
ATOM   1351 O O    B ASN   A 1 54  ? 25.150 10.315  8.589   0.54 13.75 ?  54  ASN   A O    1 
ATOM   1352 C CB   A ASN   A 1 54  ? 25.508 8.842   5.594   0.46 14.56 ?  54  ASN   A CB   1 
ATOM   1353 C CB   B ASN   A 1 54  ? 25.572 8.837   5.665   0.54 13.13 ?  54  ASN   A CB   1 
ATOM   1354 C CG   A ASN   A 1 54  ? 26.550 9.920   5.691   0.46 15.21 ?  54  ASN   A CG   1 
ATOM   1355 C CG   B ASN   A 1 54  ? 26.571 9.955   5.754   0.54 13.61 ?  54  ASN   A CG   1 
ATOM   1356 O OD1  A ASN   A 1 54  ? 27.564 9.745   6.366   0.46 15.68 ?  54  ASN   A OD1  1 
ATOM   1357 O OD1  B ASN   A 1 54  ? 27.568 9.844   6.474   0.54 12.90 ?  54  ASN   A OD1  1 
ATOM   1358 N ND2  A ASN   A 1 54  ? 26.308 11.049  5.037   0.46 16.10 ?  54  ASN   A ND2  1 
ATOM   1359 N ND2  B ASN   A 1 54  ? 26.304 11.055  5.065   0.54 14.85 ?  54  ASN   A ND2  1 
ATOM   1360 H H    A ASN   A 1 54  ? 23.639 7.337   5.994   0.46 16.88 ?  54  ASN   A H    1 
ATOM   1361 H H    B ASN   A 1 54  ? 23.778 7.231   6.108   0.54 15.14 ?  54  ASN   A H    1 
ATOM   1362 H HA   A ASN   A 1 54  ? 25.664 8.070   7.480   0.46 16.88 ?  54  ASN   A HA   1 
ATOM   1363 H HA   B ASN   A 1 54  ? 25.727 8.137   7.571   0.54 15.30 ?  54  ASN   A HA   1 
ATOM   1364 H HB2  A ASN   A 1 54  ? 25.920 8.060   5.195   0.46 17.49 ?  54  ASN   A HB2  1 
ATOM   1365 H HB2  B ASN   A 1 54  ? 26.021 8.057   5.298   0.54 15.77 ?  54  ASN   A HB2  1 
ATOM   1366 H HB3  A ASN   A 1 54  ? 24.787 9.165   5.033   0.46 17.49 ?  54  ASN   A HB3  1 
ATOM   1367 H HB3  B ASN   A 1 54  ? 24.851 9.114   5.079   0.54 15.77 ?  54  ASN   A HB3  1 
ATOM   1368 H HD21 A ASN   A 1 54  ? 26.875 11.696  5.065   0.46 19.34 ?  54  ASN   A HD21 1 
ATOM   1369 H HD21 B ASN   A 1 54  ? 26.845 11.723  5.091   0.54 17.83 ?  54  ASN   A HD21 1 
ATOM   1370 H HD22 A ASN   A 1 54  ? 25.585 11.134  4.576   0.46 19.34 ?  54  ASN   A HD22 1 
ATOM   1371 H HD22 B ASN   A 1 54  ? 25.593 11.099  4.581   0.54 17.83 ?  54  ASN   A HD22 1 
ATOM   1372 N N    . LYS   A 1 55  ? 23.260 10.185  7.367   1.00 14.25 ?  55  LYS   A N    1 
ATOM   1373 C CA   . LYS   A 1 55  ? 22.685 11.352  8.029   1.00 14.31 ?  55  LYS   A CA   1 
ATOM   1374 C C    . LYS   A 1 55  ? 22.581 11.118  9.530   1.00 14.01 ?  55  LYS   A C    1 
ATOM   1375 O O    . LYS   A 1 55  ? 22.869 12.017  10.334  1.00 14.84 ?  55  LYS   A O    1 
ATOM   1376 C CB   . LYS   A 1 55  ? 21.321 11.656  7.398   1.00 15.34 ?  55  LYS   A CB   1 
ATOM   1377 C CG   . LYS   A 1 55  ? 20.548 12.814  8.021   1.00 17.72 ?  55  LYS   A CG   1 
ATOM   1378 C CD   . LYS   A 1 55  ? 19.213 13.028  7.282   1.00 19.98 ?  55  LYS   A CD   1 
ATOM   1379 C CE   . LYS   A 1 55  ? 18.414 14.199  7.836   1.00 21.71 ?  55  LYS   A CE   1 
ATOM   1380 N NZ   . LYS   A 1 55  ? 17.083 14.309  7.166   1.00 22.96 ?  55  LYS   A NZ   1 
ATOM   1381 H H    A LYS   A 1 55  ? 22.755 9.835   6.761   0.46 17.12 ?  55  LYS   A H    1 
ATOM   1382 H H    B LYS   A 1 55  ? 22.761 9.823   6.763   0.54 17.12 ?  55  LYS   A H    1 
ATOM   1383 H HA   . LYS   A 1 55  ? 23.261 12.112  7.882   1.00 17.19 ?  55  LYS   A HA   1 
ATOM   1384 H HB2  . LYS   A 1 55  ? 21.457 11.868  6.460   1.00 18.42 ?  55  LYS   A HB2  1 
ATOM   1385 H HB3  . LYS   A 1 55  ? 20.764 10.861  7.468   1.00 18.42 ?  55  LYS   A HB3  1 
ATOM   1386 H HG2  . LYS   A 1 55  ? 20.353 12.611  8.952   1.00 21.28 ?  55  LYS   A HG2  1 
ATOM   1387 H HG3  . LYS   A 1 55  ? 21.072 13.627  7.954   1.00 21.28 ?  55  LYS   A HG3  1 
ATOM   1388 H HD2  . LYS   A 1 55  ? 19.400 13.201  6.346   1.00 24.00 ?  55  LYS   A HD2  1 
ATOM   1389 H HD3  . LYS   A 1 55  ? 18.675 12.224  7.369   1.00 24.00 ?  55  LYS   A HD3  1 
ATOM   1390 H HE2  . LYS   A 1 55  ? 18.272 14.068  8.789   1.00 26.07 ?  55  LYS   A HE2  1 
ATOM   1391 H HE3  . LYS   A 1 55  ? 18.907 15.023  7.684   1.00 26.07 ?  55  LYS   A HE3  1 
ATOM   1392 H HZ1  . LYS   A 1 55  ? 16.627 14.996  7.507   1.00 27.57 ?  55  LYS   A HZ1  1 
ATOM   1393 H HZ2  . LYS   A 1 55  ? 17.191 14.441  6.294   1.00 27.57 ?  55  LYS   A HZ2  1 
ATOM   1394 H HZ3  . LYS   A 1 55  ? 16.616 13.563  7.292   1.00 27.57 ?  55  LYS   A HZ3  1 
ATOM   1395 N N    . ALA   A 1 56  ? 22.189 9.904   9.927   1.00 15.41 ?  56  ALA   A N    1 
ATOM   1396 C CA   . ALA   A 1 56  ? 22.077 9.580   11.342  1.00 15.81 ?  56  ALA   A CA   1 
ATOM   1397 C C    . ALA   A 1 56  ? 23.420 9.609   12.065  1.00 15.55 ?  56  ALA   A C    1 
ATOM   1398 O O    . ALA   A 1 56  ? 23.436 9.772   13.288  1.00 16.72 ?  56  ALA   A O    1 
ATOM   1399 C CB   . ALA   A 1 56  ? 21.378 8.229   11.521  1.00 16.67 ?  56  ALA   A CB   1 
ATOM   1400 H H    . ALA   A 1 56  ? 21.977 9.259   9.399   1.00 18.50 ?  56  ALA   A H    1 
ATOM   1401 H HA   . ALA   A 1 56  ? 21.521 10.241  11.766  1.00 18.99 ?  56  ALA   A HA   1 
ATOM   1402 H HB1  . ALA   A 1 56  ? 21.309 8.029   12.473  1.00 20.02 ?  56  ALA   A HB1  1 
ATOM   1403 H HB2  . ALA   A 1 56  ? 20.490 8.279   11.134  1.00 20.02 ?  56  ALA   A HB2  1 
ATOM   1404 H HB3  . ALA   A 1 56  ? 21.893 7.536   11.080  1.00 20.02 ?  56  ALA   A HB3  1 
ATOM   1405 N N    . THR   A 1 57  ? 24.531 9.426   11.350  1.00 15.04 ?  57  THR   A N    1 
ATOM   1406 C CA   . THR   A 1 57  ? 25.865 9.548   11.938  1.00 14.86 ?  57  THR   A CA   1 
ATOM   1407 C C    . THR   A 1 57  ? 26.422 10.960  11.849  1.00 14.83 ?  57  THR   A C    1 
ATOM   1408 O O    . THR   A 1 57  ? 27.609 11.165  12.134  1.00 15.23 ?  57  THR   A O    1 
ATOM   1409 C CB   . THR   A 1 57  ? 26.876 8.588   11.287  1.00 14.13 ?  57  THR   A CB   1 
ATOM   1410 O OG1  . THR   A 1 57  ? 27.261 9.063   9.987   1.00 14.39 ?  57  THR   A OG1  1 
ATOM   1411 C CG2  . THR   A 1 57  ? 26.329 7.179   11.209  1.00 14.57 ?  57  THR   A CG2  1 
ATOM   1412 H H    . THR   A 1 57  ? 24.546 9.207   10.513  1.00 18.07 ?  57  THR   A H    1 
ATOM   1413 H HA   . THR   A 1 57  ? 25.812 9.303   12.877  1.00 17.84 ?  57  THR   A HA   1 
ATOM   1414 H HB   . THR   A 1 57  ? 27.673 8.552   11.844  1.00 16.97 ?  57  THR   A HB   1 
ATOM   1415 H HG1  . THR   A 1 57  ? 26.576 9.121   9.492   1.00 17.29 ?  57  THR   A HG1  1 
ATOM   1416 H HG21 . THR   A 1 57  ? 27.017 6.566   10.902  1.00 17.50 ?  57  THR   A HG21 1 
ATOM   1417 H HG22 . THR   A 1 57  ? 26.027 6.890   12.089  1.00 17.50 ?  57  THR   A HG22 1 
ATOM   1418 H HG23 . THR   A 1 57  ? 25.580 7.143   10.597  1.00 17.50 ?  57  THR   A HG23 1 
ATOM   1419 N N    . ASN   A 1 58  ? 25.610 11.933  11.449  1.00 15.27 ?  58  ASN   A N    1 
ATOM   1420 C CA   . ASN   A 1 58  ? 26.084 13.310  11.363  1.00 15.90 ?  58  ASN   A CA   1 
ATOM   1421 C C    . ASN   A 1 58  ? 27.241 13.426  10.365  1.00 15.05 ?  58  ASN   A C    1 
ATOM   1422 O O    . ASN   A 1 58  ? 28.148 14.243  10.527  1.00 15.45 ?  58  ASN   A O    1 
ATOM   1423 C CB   . ASN   A 1 58  ? 26.461 13.820  12.766  1.00 19.09 ?  58  ASN   A CB   1 
ATOM   1424 C CG   . ASN   A 1 58  ? 26.870 15.268  12.797  1.00 23.54 ?  58  ASN   A CG   1 
ATOM   1425 O OD1  . ASN   A 1 58  ? 26.250 16.108  12.158  1.00 25.33 ?  58  ASN   A OD1  1 
ATOM   1426 N ND2  . ASN   A 1 58  ? 27.917 15.573  13.573  1.00 25.01 ?  58  ASN   A ND2  1 
ATOM   1427 H H    . ASN   A 1 58  ? 24.795 11.818  11.206  1.00 18.33 ?  58  ASN   A H    1 
ATOM   1428 H HA   . ASN   A 1 58  ? 25.357 13.861  11.040  1.00 19.09 ?  58  ASN   A HA   1 
ATOM   1429 H HB2  . ASN   A 1 58  ? 25.690 13.713  13.356  1.00 22.92 ?  58  ASN   A HB2  1 
ATOM   1430 H HB3  . ASN   A 1 58  ? 27.202 13.301  13.110  1.00 22.92 ?  58  ASN   A HB3  1 
ATOM   1431 H HD21 . ASN   A 1 58  ? 28.190 16.387  13.637  1.00 30.03 ?  58  ASN   A HD21 1 
ATOM   1432 H HD22 . ASN   A 1 58  ? 28.321 14.950  14.008  1.00 30.03 ?  58  ASN   A HD22 1 
ATOM   1433 N N    . ASN   A 1 59  ? 27.212 12.611  9.310   1.00 14.28 ?  59  ASN   A N    1 
ATOM   1434 C CA   . ASN   A 1 59  ? 28.184 12.581  8.213   1.00 14.17 ?  59  ASN   A CA   1 
ATOM   1435 C C    . ASN   A 1 59  ? 29.500 11.889  8.607   1.00 13.96 ?  59  ASN   A C    1 
ATOM   1436 O O    . ASN   A 1 59  ? 30.420 11.843  7.787   1.00 14.11 ?  59  ASN   A O    1 
ATOM   1437 C CB   . ASN   A 1 59  ? 28.473 13.969  7.604   1.00 14.16 ?  59  ASN   A CB   1 
ATOM   1438 C CG   . ASN   A 1 59  ? 28.833 13.897  6.134   1.00 14.83 ?  59  ASN   A CG   1 
ATOM   1439 O OD1  . ASN   A 1 59  ? 28.125 13.278  5.340   1.00 14.78 ?  59  ASN   A OD1  1 
ATOM   1440 N ND2  . ASN   A 1 59  ? 29.920 14.548  5.758   1.00 15.74 ?  59  ASN   A ND2  1 
ATOM   1441 H H    . ASN   A 1 59  ? 26.593 12.024  9.207   1.00 17.15 ?  59  ASN   A H    1 
ATOM   1442 H HA   . ASN   A 1 59  ? 27.789 12.047  7.507   1.00 17.02 ?  59  ASN   A HA   1 
ATOM   1443 H HB2  . ASN   A 1 59  ? 27.686 14.523  7.689   1.00 17.01 ?  59  ASN   A HB2  1 
ATOM   1444 H HB3  . ASN   A 1 59  ? 29.220 14.366  8.071   1.00 17.01 ?  59  ASN   A HB3  1 
ATOM   1445 H HD21 . ASN   A 1 59  ? 30.162 14.544  4.932   1.00 18.90 ?  59  ASN   A HD21 1 
ATOM   1446 H HD22 . ASN   A 1 59  ? 30.387 14.975  6.340   1.00 18.90 ?  59  ASN   A HD22 1 
ATOM   1447 N N    . ALA   A 1 60  ? 29.619 11.333  9.812   1.00 13.92 ?  60  ALA   A N    1 
ATOM   1448 C CA   . ALA   A 1 60  ? 30.856 10.648  10.161  1.00 13.76 ?  60  ALA   A CA   1 
ATOM   1449 C C    . ALA   A 1 60  ? 31.072 9.419   9.284   1.00 13.55 ?  60  ALA   A C    1 
ATOM   1450 O O    . ALA   A 1 60  ? 32.214 9.083   8.945   1.00 14.17 ?  60  ALA   A O    1 
ATOM   1451 C CB   . ALA   A 1 60  ? 30.865 10.280  11.641  1.00 14.40 ?  60  ALA   A CB   1 
ATOM   1452 H H    . ALA   A 1 60  ? 29.023 11.343  10.432  1.00 16.72 ?  60  ALA   A H    1 
ATOM   1453 H HA   . ALA   A 1 60  ? 31.600 11.254  10.007  1.00 16.53 ?  60  ALA   A HA   1 
ATOM   1454 H HB1  . ALA   A 1 60  ? 31.696 9.828   11.851  1.00 17.30 ?  60  ALA   A HB1  1 
ATOM   1455 H HB2  . ALA   A 1 60  ? 30.790 11.093  12.169  1.00 17.30 ?  60  ALA   A HB2  1 
ATOM   1456 H HB3  . ALA   A 1 60  ? 30.113 9.697   11.826  1.00 17.30 ?  60  ALA   A HB3  1 
ATOM   1457 N N    . MET   A 1 61  ? 29.995 8.723   8.919   1.00 13.60 ?  61  MET   A N    1 
ATOM   1458 C CA   . MET   A 1 61  ? 30.118 7.593   8.007   1.00 13.18 ?  61  MET   A CA   1 
ATOM   1459 C C    . MET   A 1 61  ? 30.762 8.016   6.687   1.00 13.43 ?  61  MET   A C    1 
ATOM   1460 O O    . MET   A 1 61  ? 31.648 7.325   6.168   1.00 13.48 ?  61  MET   A O    1 
ATOM   1461 C CB   . MET   A 1 61  ? 28.753 6.935   7.799   1.00 13.64 ?  61  MET   A CB   1 
ATOM   1462 C CG   . MET   A 1 61  ? 28.768 5.773   6.823   1.00 13.82 ?  61  MET   A CG   1 
ATOM   1463 S SD   . MET   A 1 61  ? 27.137 5.023   6.611   1.00 14.74 ?  61  MET   A SD   1 
ATOM   1464 C CE   . MET   A 1 61  ? 27.003 4.133   8.164   1.00 16.83 ?  61  MET   A CE   1 
ATOM   1465 H H    . MET   A 1 61  ? 29.196 8.887   9.182   1.00 16.33 ?  61  MET   A H    1 
ATOM   1466 H HA   . MET   A 1 61  ? 30.696 6.932   8.419   1.00 15.83 ?  61  MET   A HA   1 
ATOM   1467 H HB2  . MET   A 1 61  ? 28.438 6.600   8.654   1.00 16.39 ?  61  MET   A HB2  1 
ATOM   1468 H HB3  . MET   A 1 61  ? 28.134 7.600   7.461   1.00 16.39 ?  61  MET   A HB3  1 
ATOM   1469 H HG2  . MET   A 1 61  ? 29.056 6.086   5.951   1.00 16.60 ?  61  MET   A HG2  1 
ATOM   1470 H HG3  . MET   A 1 61  ? 29.371 5.088   7.148   1.00 16.60 ?  61  MET   A HG3  1 
ATOM   1471 H HE1  . MET   A 1 61  ? 26.157 3.648   8.179   1.00 20.20 ?  61  MET   A HE1  1 
ATOM   1472 H HE2  . MET   A 1 61  ? 27.738 3.505   8.233   1.00 20.20 ?  61  MET   A HE2  1 
ATOM   1473 H HE3  . MET   A 1 61  ? 27.031 4.762   8.900   1.00 20.20 ?  61  MET   A HE3  1 
ATOM   1474 N N    . GLN   A 1 62  ? 30.324 9.144   6.120   1.00 13.28 ?  62  GLN   A N    1 
ATOM   1475 C CA   . GLN   A 1 62  ? 30.899 9.611   4.858   1.00 13.46 ?  62  GLN   A CA   1 
ATOM   1476 C C    . GLN   A 1 62  ? 32.374 9.982   5.008   1.00 13.46 ?  62  GLN   A C    1 
ATOM   1477 O O    . GLN   A 1 62  ? 33.193 9.650   4.137   1.00 13.69 ?  62  GLN   A O    1 
ATOM   1478 C CB   . GLN   A 1 62  ? 30.111 10.802  4.313   1.00 13.49 ?  62  GLN   A CB   1 
ATOM   1479 C CG   . GLN   A 1 62  ? 30.505 11.148  2.887   1.00 13.34 ?  62  GLN   A CG   1 
ATOM   1480 C CD   . GLN   A 1 62  ? 30.151 10.021  1.935   1.00 13.09 ?  62  GLN   A CD   1 
ATOM   1481 O OE1  . GLN   A 1 62  ? 28.963 9.727   1.738   1.00 13.97 ?  62  GLN   A OE1  1 
ATOM   1482 N NE2  . GLN   A 1 62  ? 31.165 9.338   1.392   1.00 14.01 ?  62  GLN   A NE2  1 
ATOM   1483 H H    . GLN   A 1 62  ? 29.700 9.644   6.440   1.00 15.95 ?  62  GLN   A H    1 
ATOM   1484 H HA   . GLN   A 1 62  ? 30.843 8.889   4.212   1.00 16.17 ?  62  GLN   A HA   1 
ATOM   1485 H HB2  . GLN   A 1 62  ? 29.164 10.587  4.322   1.00 16.20 ?  62  GLN   A HB2  1 
ATOM   1486 H HB3  . GLN   A 1 62  ? 30.282 11.577  4.870   1.00 16.20 ?  62  GLN   A HB3  1 
ATOM   1487 H HG2  . GLN   A 1 62  ? 30.025 11.938  2.603   1.00 16.02 ?  62  GLN   A HG2  1 
ATOM   1488 H HG3  . GLN   A 1 62  ? 31.462 11.299  2.841   1.00 16.02 ?  62  GLN   A HG3  1 
ATOM   1489 H HE21 . GLN   A 1 62  ? 31.982 9.561   1.567   1.00 16.83 ?  62  GLN   A HE21 1 
ATOM   1490 H HE22 . GLN   A 1 62  ? 31.014 8.682   0.854   1.00 16.83 ?  62  GLN   A HE22 1 
ATOM   1491 N N    . VAL   A 1 63  ? 32.731 10.668  6.096   1.00 13.94 ?  63  VAL   A N    1 
ATOM   1492 C CA   . VAL   A 1 63  ? 34.125 11.059  6.320   1.00 14.31 ?  63  VAL   A CA   1 
ATOM   1493 C C    . VAL   A 1 63  ? 35.015 9.825   6.385   1.00 14.38 ?  63  VAL   A C    1 
ATOM   1494 O O    . VAL   A 1 63  ? 36.053 9.749   5.717   1.00 14.44 ?  63  VAL   A O    1 
ATOM   1495 C CB   . VAL   A 1 63  ? 34.237 11.918  7.592   1.00 16.08 ?  63  VAL   A CB   1 
ATOM   1496 C CG1  . VAL   A 1 63  ? 35.707 12.159  7.953   1.00 17.97 ?  63  VAL   A CG1  1 
ATOM   1497 C CG2  . VAL   A 1 63  ? 33.494 13.241  7.407   1.00 17.01 ?  63  VAL   A CG2  1 
ATOM   1498 H H    . VAL   A 1 63  ? 32.184 10.925  6.714   1.00 16.74 ?  63  VAL   A H    1 
ATOM   1499 H HA   . VAL   A 1 63  ? 34.420 11.594  5.572   1.00 17.19 ?  63  VAL   A HA   1 
ATOM   1500 H HB   . VAL   A 1 63  ? 33.825 11.445  8.332   1.00 19.31 ?  63  VAL   A HB   1 
ATOM   1501 H HG11 . VAL   A 1 63  ? 35.763 12.903  8.574   1.00 21.58 ?  63  VAL   A HG11 1 
ATOM   1502 H HG12 . VAL   A 1 63  ? 36.072 11.360  8.364   1.00 21.58 ?  63  VAL   A HG12 1 
ATOM   1503 H HG13 . VAL   A 1 63  ? 36.199 12.370  7.143   1.00 21.58 ?  63  VAL   A HG13 1 
ATOM   1504 H HG21 . VAL   A 1 63  ? 33.589 13.773  8.212   1.00 20.43 ?  63  VAL   A HG21 1 
ATOM   1505 H HG22 . VAL   A 1 63  ? 33.872 13.712  6.650   1.00 20.43 ?  63  VAL   A HG22 1 
ATOM   1506 H HG23 . VAL   A 1 63  ? 32.554 13.053  7.244   1.00 20.43 ?  63  VAL   A HG23 1 
ATOM   1507 N N    . GLU   A 1 64  ? 34.593 8.816   7.155   1.00 13.96 ?  64  GLU   A N    1 
ATOM   1508 C CA   . GLU   A 1 64  ? 35.349 7.573   7.240   1.00 13.83 ?  64  GLU   A CA   1 
ATOM   1509 C C    . GLU   A 1 64  ? 35.427 6.887   5.884   1.00 13.51 ?  64  GLU   A C    1 
ATOM   1510 O O    . GLU   A 1 64  ? 36.474 6.334   5.510   1.00 13.95 ?  64  GLU   A O    1 
ATOM   1511 C CB   . GLU   A 1 64  ? 34.659 6.660   8.254   1.00 14.20 ?  64  GLU   A CB   1 
ATOM   1512 C CG   . GLU   A 1 64  ? 35.293 5.302   8.393   1.00 14.11 ?  64  GLU   A CG   1 
ATOM   1513 C CD   . GLU   A 1 64  ? 34.420 4.323   9.149   1.00 15.33 ?  64  GLU   A CD   1 
ATOM   1514 O OE1  . GLU   A 1 64  ? 33.182 4.414   9.017   1.00 15.87 ?  64  GLU   A OE1  1 
ATOM   1515 O OE2  . GLU   A 1 64  ? 34.964 3.421   9.839   1.00 15.46 -1 64  GLU   A OE2  1 
ATOM   1516 H H    . GLU   A 1 64  ? 33.870 8.825   7.634   1.00 16.76 ?  64  GLU   A H    1 
ATOM   1517 H HA   . GLU   A 1 64  ? 36.246 7.761   7.555   1.00 16.62 ?  64  GLU   A HA   1 
ATOM   1518 H HB2  . GLU   A 1 64  ? 34.680 7.088   9.127   1.00 17.06 ?  64  GLU   A HB2  1 
ATOM   1519 H HB3  . GLU   A 1 64  ? 33.734 6.537   7.978   1.00 17.06 ?  64  GLU   A HB3  1 
ATOM   1520 H HG2  . GLU   A 1 64  ? 35.456 4.929   7.509   1.00 16.95 ?  64  GLU   A HG2  1 
ATOM   1521 H HG3  . GLU   A 1 64  ? 36.125 5.395   8.872   1.00 16.95 ?  64  GLU   A HG3  1 
ATOM   1522 N N    . SER   A 1 65  ? 34.310 6.875   5.156   1.00 13.27 ?  65  SER   A N    1 
ATOM   1523 C CA   . SER   A 1 65  ? 34.257 6.217   3.855   1.00 13.04 ?  65  SER   A CA   1 
ATOM   1524 C C    . SER   A 1 65  ? 35.192 6.875   2.852   1.00 13.44 ?  65  SER   A C    1 
ATOM   1525 O O    . SER   A 1 65  ? 35.851 6.187   2.062   1.00 14.65 ?  65  SER   A O    1 
ATOM   1526 C CB   . SER   A 1 65  ? 32.824 6.237   3.320   1.00 13.31 ?  65  SER   A CB   1 
ATOM   1527 O OG   . SER   A 1 65  ? 31.957 5.433   4.116   1.00 13.50 ?  65  SER   A OG   1 
ATOM   1528 H H    . SER   A 1 65  ? 33.569 7.255   5.387   1.00 15.94 ?  65  SER   A H    1 
ATOM   1529 H HA   . SER   A 1 65  ? 34.528 5.291   3.958   1.00 15.67 ?  65  SER   A HA   1 
ATOM   1530 H HB2  . SER   A 1 65  ? 32.498 7.149   3.325   1.00 15.99 ?  65  SER   A HB2  1 
ATOM   1531 H HB3  . SER   A 1 65  ? 32.820 5.888   2.417   1.00 15.99 ?  65  SER   A HB3  1 
ATOM   1532 H HG   . SER   A 1 65  ? 31.946 5.727   4.913   1.00 16.22 ?  65  SER   A HG   1 
ATOM   1533 N N    . ASP   A 1 66  ? 35.263 8.210   2.860   1.00 13.10 ?  66  ASP   A N    1 
ATOM   1534 C CA   . ASP   A 1 66  ? 36.131 8.900   1.915   1.00 14.21 ?  66  ASP   A CA   1 
ATOM   1535 C C    . ASP   A 1 66  ? 37.587 8.529   2.143   1.00 13.73 ?  66  ASP   A C    1 
ATOM   1536 O O    . ASP   A 1 66  ? 38.348 8.347   1.185   1.00 15.22 ?  66  ASP   A O    1 
ATOM   1537 C CB   . ASP   A 1 66  ? 35.951 10.416  2.024   1.00 15.75 ?  66  ASP   A CB   1 
ATOM   1538 C CG   . ASP   A 1 66  ? 34.632 10.903  1.426   1.00 17.61 ?  66  ASP   A CG   1 
ATOM   1539 O OD1  . ASP   A 1 66  ? 33.894 10.109  0.796   1.00 18.11 ?  66  ASP   A OD1  1 
ATOM   1540 O OD2  . ASP   A 1 66  ? 34.326 12.105  1.566   1.00 20.37 -1 66  ASP   A OD2  1 
ATOM   1541 H H    . ASP   A 1 66  ? 34.813 8.725   3.385   1.00 15.74 ?  66  ASP   A H    1 
ATOM   1542 H HA   . ASP   A 1 66  ? 35.892 8.634   1.014   1.00 17.07 ?  66  ASP   A HA   1 
ATOM   1543 H HB2  . ASP   A 1 66  ? 35.968 10.671  2.959   1.00 18.91 ?  66  ASP   A HB2  1 
ATOM   1544 H HB3  . ASP   A 1 66  ? 36.678 10.853  1.549   1.00 18.91 ?  66  ASP   A HB3  1 
ATOM   1545 N N    . ASP   A 1 67  ? 37.993 8.411   3.406   1.00 14.42 ?  67  ASP   A N    1 
ATOM   1546 C CA   . ASP   A 1 67  ? 39.346 7.956   3.696   1.00 16.14 ?  67  ASP   A CA   1 
ATOM   1547 C C    . ASP   A 1 67  ? 39.549 6.518   3.232   1.00 15.16 ?  67  ASP   A C    1 
ATOM   1548 O O    . ASP   A 1 67  ? 40.602 6.186   2.675   1.00 15.79 ?  67  ASP   A O    1 
ATOM   1549 C CB   . ASP   A 1 67  ? 39.640 8.101   5.187   1.00 17.02 ?  67  ASP   A CB   1 
ATOM   1550 C CG   . ASP   A 1 67  ? 40.928 7.421   5.593   1.00 17.81 ?  67  ASP   A CG   1 
ATOM   1551 O OD1  . ASP   A 1 67  ? 41.997 8.035   5.425   1.00 20.68 ?  67  ASP   A OD1  1 
ATOM   1552 O OD2  . ASP   A 1 67  ? 40.877 6.268   6.083   1.00 17.41 -1 67  ASP   A OD2  1 
ATOM   1553 H H    . ASP   A 1 67  ? 37.517 8.598   4.098   1.00 17.32 ?  67  ASP   A H    1 
ATOM   1554 H HA   . ASP   A 1 67  ? 39.978 8.509   3.216   1.00 19.38 ?  67  ASP   A HA   1 
ATOM   1555 H HB2  . ASP   A 1 67  ? 39.723 9.035   5.405   1.00 20.44 ?  67  ASP   A HB2  1 
ATOM   1556 H HB3  . ASP   A 1 67  ? 38.922 7.692   5.695   1.00 20.44 ?  67  ASP   A HB3  1 
ATOM   1557 N N    . TYR   A 1 68  ? 38.551 5.646   3.440   1.00 14.75 ?  68  TYR   A N    1 
ATOM   1558 C CA   . TYR   A 1 68  ? 38.667 4.262   2.970   1.00 14.88 ?  68  TYR   A CA   1 
ATOM   1559 C C    . TYR   A 1 68  ? 38.908 4.215   1.461   1.00 14.00 ?  68  TYR   A C    1 
ATOM   1560 O O    . TYR   A 1 68  ? 39.773 3.470   0.982   1.00 15.36 ?  68  TYR   A O    1 
ATOM   1561 C CB   . TYR   A 1 68  ? 37.410 3.449   3.343   1.00 15.05 ?  68  TYR   A CB   1 
ATOM   1562 C CG   . TYR   A 1 68  ? 37.435 2.053   2.720   1.00 15.66 ?  68  TYR   A CG   1 
ATOM   1563 C CD1  . TYR   A 1 68  ? 36.992 1.854   1.413   1.00 17.76 ?  68  TYR   A CD1  1 
ATOM   1564 C CD2  . TYR   A 1 68  ? 37.973 0.981   3.394   1.00 17.50 ?  68  TYR   A CD2  1 
ATOM   1565 C CE1  . TYR   A 1 68  ? 37.054 0.635   0.803   1.00 19.90 ?  68  TYR   A CE1  1 
ATOM   1566 C CE2  . TYR   A 1 68  ? 38.031 -0.279  2.784   1.00 18.60 ?  68  TYR   A CE2  1 
ATOM   1567 C CZ   . TYR   A 1 68  ? 37.580 -0.429  1.487   1.00 19.57 ?  68  TYR   A CZ   1 
ATOM   1568 O OH   . TYR   A 1 68  ? 37.651 -1.649  0.855   1.00 22.01 ?  68  TYR   A OH   1 
ATOM   1569 H H    . TYR   A 1 68  ? 37.810 5.825   3.842   1.00 17.71 ?  68  TYR   A H    1 
ATOM   1570 H HA   . TYR   A 1 68  ? 39.423 3.846   3.403   1.00 17.87 ?  68  TYR   A HA   1 
ATOM   1571 H HB2  . TYR   A 1 68  ? 37.368 3.346   4.309   1.00 18.08 ?  68  TYR   A HB2  1 
ATOM   1572 H HB3  . TYR   A 1 68  ? 36.617 3.911   3.024   1.00 18.08 ?  68  TYR   A HB3  1 
ATOM   1573 H HD1  . TYR   A 1 68  ? 36.646 2.587   0.942   1.00 21.33 ?  68  TYR   A HD1  1 
ATOM   1574 H HD2  . TYR   A 1 68  ? 38.291 1.086   4.259   1.00 21.01 ?  68  TYR   A HD2  1 
ATOM   1575 H HE1  . TYR   A 1 68  ? 36.746 0.532   -0.070  1.00 23.89 ?  68  TYR   A HE1  1 
ATOM   1576 H HE2  . TYR   A 1 68  ? 38.393 -1.010  3.229   1.00 22.34 ?  68  TYR   A HE2  1 
ATOM   1577 H HH   . TYR   A 1 68  ? 37.983 -2.217  1.372   1.00 26.43 ?  68  TYR   A HH   1 
ATOM   1578 N N    . ILE   A 1 69  ? 38.134 4.984   0.689   1.00 13.78 ?  69  ILE   A N    1 
ATOM   1579 C CA   . ILE   A 1 69  ? 38.264 4.965   -0.768  1.00 14.41 ?  69  ILE   A CA   1 
ATOM   1580 C C    . ILE   A 1 69  ? 39.598 5.564   -1.202  1.00 14.53 ?  69  ILE   A C    1 
ATOM   1581 O O    . ILE   A 1 69  ? 40.239 5.069   -2.136  1.00 14.57 ?  69  ILE   A O    1 
ATOM   1582 C CB   . ILE   A 1 69  ? 37.072 5.680   -1.440  1.00 14.90 ?  69  ILE   A CB   1 
ATOM   1583 C CG1  . ILE   A 1 69  ? 35.749 4.968   -1.148  1.00 15.72 ?  69  ILE   A CG1  1 
ATOM   1584 C CG2  . ILE   A 1 69  ? 37.324 5.857   -2.958  1.00 16.61 ?  69  ILE   A CG2  1 
ATOM   1585 C CD1  . ILE   A 1 69  ? 35.561 3.687   -1.915  1.00 16.67 ?  69  ILE   A CD1  1 
ATOM   1586 H H    . ILE   A 1 69  ? 37.523 5.516   0.982   1.00 16.55 ?  69  ILE   A H    1 
ATOM   1587 H HA   . ILE   A 1 69  ? 38.251 4.040   -1.065  1.00 17.30 ?  69  ILE   A HA   1 
ATOM   1588 H HB   . ILE   A 1 69  ? 37.017 6.566   -1.053  1.00 17.90 ?  69  ILE   A HB   1 
ATOM   1589 H HG12 . ILE   A 1 69  ? 35.712 4.761   -0.198  1.00 18.88 ?  69  ILE   A HG12 1 
ATOM   1590 H HG13 . ILE   A 1 69  ? 35.019 5.569   -1.374  1.00 18.88 ?  69  ILE   A HG13 1 
ATOM   1591 H HG21 . ILE   A 1 69  ? 36.483 6.069   -3.394  1.00 19.95 ?  69  ILE   A HG21 1 
ATOM   1592 H HG22 . ILE   A 1 69  ? 37.954 6.588   -3.093  1.00 19.95 ?  69  ILE   A HG22 1 
ATOM   1593 H HG23 . ILE   A 1 69  ? 37.687 5.036   -3.319  1.00 19.95 ?  69  ILE   A HG23 1 
ATOM   1594 H HD11 . ILE   A 1 69  ? 34.761 3.246   -1.589  1.00 20.02 ?  69  ILE   A HD11 1 
ATOM   1595 H HD12 . ILE   A 1 69  ? 35.460 3.898   -2.856  1.00 20.02 ?  69  ILE   A HD12 1 
ATOM   1596 H HD13 . ILE   A 1 69  ? 36.332 3.121   -1.778  1.00 20.02 ?  69  ILE   A HD13 1 
ATOM   1597 N N    . ALA   A 1 70  ? 40.026 6.645   -0.552  1.00 15.36 ?  70  ALA   A N    1 
ATOM   1598 C CA   . ALA   A 1 70  ? 41.315 7.239   -0.891  1.00 16.03 ?  70  ALA   A CA   1 
ATOM   1599 C C    . ALA   A 1 70  ? 42.450 6.237   -0.735  1.00 16.95 ?  70  ALA   A C    1 
ATOM   1600 O O    . ALA   A 1 70  ? 43.419 6.270   -1.498  1.00 18.98 ?  70  ALA   A O    1 
ATOM   1601 C CB   . ALA   A 1 70  ? 41.582 8.472   -0.025  1.00 16.76 ?  70  ALA   A CB   1 
ATOM   1602 H H    . ALA   A 1 70  ? 39.593 7.051   0.067   1.00 18.45 ?  70  ALA   A H    1 
ATOM   1603 H HA   . ALA   A 1 70  ? 41.297 7.528   -1.821  1.00 19.25 ?  70  ALA   A HA   1 
ATOM   1604 H HB1  . ALA   A 1 70  ? 42.447 8.843   -0.268  1.00 20.13 ?  70  ALA   A HB1  1 
ATOM   1605 H HB2  . ALA   A 1 70  ? 40.886 9.123   -0.178  1.00 20.13 ?  70  ALA   A HB2  1 
ATOM   1606 H HB3  . ALA   A 1 70  ? 41.592 8.201   0.906   1.00 20.13 ?  70  ALA   A HB3  1 
ATOM   1607 N N    . THR   A 1 71  ? 42.359 5.357   0.266   1.00 15.33 ?  71  THR   A N    1 
ATOM   1608 C CA   . THR   A 1 71  ? 43.401 4.359   0.500   1.00 17.35 ?  71  THR   A CA   1 
ATOM   1609 C C    . THR   A 1 71  ? 43.250 3.141   -0.401  1.00 17.59 ?  71  THR   A C    1 
ATOM   1610 O O    . THR   A 1 71  ? 44.241 2.640   -0.944  1.00 19.77 ?  71  THR   A O    1 
ATOM   1611 C CB   . THR   A 1 71  ? 43.358 3.923   1.963   1.00 19.52 ?  71  THR   A CB   1 
ATOM   1612 O OG1  . THR   A 1 71  ? 43.646 5.048   2.800   1.00 21.31 ?  71  THR   A OG1  1 
ATOM   1613 C CG2  . THR   A 1 71  ? 44.356 2.809   2.234   1.00 21.33 ?  71  THR   A CG2  1 
ATOM   1614 H H    . THR   A 1 71  ? 41.697 5.317   0.815   1.00 18.41 ?  71  THR   A H    1 
ATOM   1615 H HA   . THR   A 1 71  ? 44.265 4.757   0.323   1.00 20.84 ?  71  THR   A HA   1 
ATOM   1616 H HB   . THR   A 1 71  ? 42.467 3.593   2.168   1.00 23.43 ?  71  THR   A HB   1 
ATOM   1617 H HG1  . THR   A 1 71  ? 43.075 5.654   2.667   1.00 25.59 ?  71  THR   A HG1  1 
ATOM   1618 H HG21 . THR   A 1 71  ? 44.509 2.728   3.188   1.00 25.61 ?  71  THR   A HG21 1 
ATOM   1619 H HG22 . THR   A 1 71  ? 44.017 1.962   1.899   1.00 25.61 ?  71  THR   A HG22 1 
ATOM   1620 H HG23 . THR   A 1 71  ? 45.201 3.004   1.797   1.00 25.61 ?  71  THR   A HG23 1 
ATOM   1621 N N    . ASN   A 1 72  ? 42.029 2.642   -0.570  1.00 16.53 ?  72  ASN   A N    1 
ATOM   1622 C CA   . ASN   A 1 72  ? 41.811 1.318   -1.141  1.00 16.53 ?  72  ASN   A CA   1 
ATOM   1623 C C    . ASN   A 1 72  ? 41.178 1.312   -2.521  1.00 16.83 ?  72  ASN   A C    1 
ATOM   1624 O O    . ASN   A 1 72  ? 41.188 0.266   -3.174  1.00 17.59 ?  72  ASN   A O    1 
ATOM   1625 C CB   . ASN   A 1 72  ? 40.928 0.498   -0.199  1.00 17.25 ?  72  ASN   A CB   1 
ATOM   1626 C CG   . ASN   A 1 72  ? 41.546 0.346   1.162   1.00 18.56 ?  72  ASN   A CG   1 
ATOM   1627 O OD1  . ASN   A 1 72  ? 41.102 0.948   2.140   1.00 20.70 ?  72  ASN   A OD1  1 
ATOM   1628 N ND2  . ASN   A 1 72  ? 42.599 -0.434  1.228   1.00 18.83 ?  72  ASN   A ND2  1 
ATOM   1629 H H    . ASN   A 1 72  ? 41.303 3.056   -0.371  1.00 19.86 ?  72  ASN   A H    1 
ATOM   1630 H HA   . ASN   A 1 72  ? 42.661 0.863   -1.214  1.00 19.85 ?  72  ASN   A HA   1 
ATOM   1631 H HB2  . ASN   A 1 72  ? 40.072 0.940   -0.095  1.00 20.72 ?  72  ASN   A HB2  1 
ATOM   1632 H HB3  . ASN   A 1 72  ? 40.802 -0.390  -0.569  1.00 20.72 ?  72  ASN   A HB3  1 
ATOM   1633 H HD21 . ASN   A 1 72  ? 42.996 -0.554  1.984   1.00 22.61 ?  72  ASN   A HD21 1 
ATOM   1634 H HD22 . ASN   A 1 72  ? 42.883 -0.839  0.526   1.00 22.61 ?  72  ASN   A HD22 1 
ATOM   1635 N N    . GLY   A 1 73  ? 40.618 2.421   -2.984  1.00 15.40 ?  73  GLY   A N    1 
ATOM   1636 C CA   . GLY   A 1 73  ? 39.896 2.420   -4.232  1.00 15.50 ?  73  GLY   A CA   1 
ATOM   1637 C C    . GLY   A 1 73  ? 38.503 1.863   -4.061  1.00 15.15 ?  73  GLY   A C    1 
ATOM   1638 O O    . GLY   A 1 73  ? 38.129 1.399   -2.979  1.00 15.72 ?  73  GLY   A O    1 
ATOM   1639 H H    . GLY   A 1 73  ? 40.641 3.189   -2.589  1.00 18.50 ?  73  GLY   A H    1 
ATOM   1640 H HA2  . GLY   A 1 73  ? 39.829 3.332   -4.566  1.00 18.62 ?  73  GLY   A HA2  1 
ATOM   1641 H HA3  . GLY   A 1 73  ? 40.371 1.887   -4.886  1.00 18.62 ?  73  GLY   A HA3  1 
ATOM   1642 N N    . PRO   A 1 74  ? 37.717 1.880   -5.140  1.00 15.52 ?  74  PRO   A N    1 
ATOM   1643 C CA   . PRO   A 1 74  ? 36.313 1.459   -5.056  1.00 15.52 ?  74  PRO   A CA   1 
ATOM   1644 C C    . PRO   A 1 74  ? 36.151 -0.021  -4.732  1.00 15.03 ?  74  PRO   A C    1 
ATOM   1645 O O    . PRO   A 1 74  ? 37.023 -0.857  -5.008  1.00 15.93 ?  74  PRO   A O    1 
ATOM   1646 C CB   . PRO   A 1 74  ? 35.773 1.756   -6.460  1.00 17.61 ?  74  PRO   A CB   1 
ATOM   1647 C CG   . PRO   A 1 74  ? 36.730 2.710   -7.080  1.00 21.27 ?  74  PRO   A CG   1 
ATOM   1648 C CD   . PRO   A 1 74  ? 38.064 2.398   -6.475  1.00 17.84 ?  74  PRO   A CD   1 
ATOM   1649 H HA   . PRO   A 1 74  ? 35.837 1.997   -4.401  1.00 18.64 ?  74  PRO   A HA   1 
ATOM   1650 H HB2  . PRO   A 1 74  ? 35.730 0.927   -6.969  1.00 21.14 ?  74  PRO   A HB2  1 
ATOM   1651 H HB3  . PRO   A 1 74  ? 34.887 2.150   -6.388  1.00 21.14 ?  74  PRO   A HB3  1 
ATOM   1652 H HG2  . PRO   A 1 74  ? 36.751 2.576   -8.039  1.00 25.53 ?  74  PRO   A HG2  1 
ATOM   1653 H HG3  . PRO   A 1 74  ? 36.466 3.619   -6.868  1.00 25.53 ?  74  PRO   A HG3  1 
ATOM   1654 H HD2  . PRO   A 1 74  ? 38.527 1.722   -6.998  1.00 21.42 ?  74  PRO   A HD2  1 
ATOM   1655 H HD3  . PRO   A 1 74  ? 38.597 3.210   -6.403  1.00 21.42 ?  74  PRO   A HD3  1 
ATOM   1656 N N    . LEU   A 1 75  ? 34.994 -0.341  -4.149  1.00 14.58 ?  75  LEU   A N    1 
ATOM   1657 C CA   . LEU   A 1 75  ? 34.602 -1.734  -3.997  1.00 14.10 ?  75  LEU   A CA   1 
ATOM   1658 C C    . LEU   A 1 75  ? 34.231 -2.328  -5.353  1.00 14.58 ?  75  LEU   A C    1 
ATOM   1659 O O    . LEU   A 1 75  ? 34.087 -1.620  -6.352  1.00 15.96 ?  75  LEU   A O    1 
ATOM   1660 C CB   . LEU   A 1 75  ? 33.410 -1.873  -3.046  1.00 14.22 ?  75  LEU   A CB   1 
ATOM   1661 C CG   . LEU   A 1 75  ? 33.615 -1.397  -1.615  1.00 15.84 ?  75  LEU   A CG   1 
ATOM   1662 C CD1  . LEU   A 1 75  ? 32.345 -1.576  -0.796  1.00 18.01 ?  75  LEU   A CD1  1 
ATOM   1663 C CD2  . LEU   A 1 75  ? 34.760 -2.075  -0.934  1.00 19.98 ?  75  LEU   A CD2  1 
ATOM   1664 H H    . LEU   A 1 75  ? 34.414 0.231   -3.852  1.00 17.51 ?  75  LEU   A H    1 
ATOM   1665 H HA   . LEU   A 1 75  ? 35.346 -2.236  -3.642  1.00 16.94 ?  75  LEU   A HA   1 
ATOM   1666 H HB2  . LEU   A 1 75  ? 32.668 -1.368  -3.417  1.00 17.08 ?  75  LEU   A HB2  1 
ATOM   1667 H HB3  . LEU   A 1 75  ? 33.169 -2.811  -3.006  1.00 17.08 ?  75  LEU   A HB3  1 
ATOM   1668 H HG   . LEU   A 1 75  ? 33.819 -0.443  -1.638  1.00 19.02 ?  75  LEU   A HG   1 
ATOM   1669 H HD11 . LEU   A 1 75  ? 32.501 -1.253  0.107   1.00 21.63 ?  75  LEU   A HD11 1 
ATOM   1670 H HD12 . LEU   A 1 75  ? 31.629 -1.063  -1.207  1.00 21.63 ?  75  LEU   A HD12 1 
ATOM   1671 H HD13 . LEU   A 1 75  ? 32.112 -2.515  -0.777  1.00 21.63 ?  75  LEU   A HD13 1 
ATOM   1672 H HD21 . LEU   A 1 75  ? 34.798 -1.780  -0.011  1.00 23.99 ?  75  LEU   A HD21 1 
ATOM   1673 H HD22 . LEU   A 1 75  ? 34.627 -3.032  -0.974  1.00 23.99 ?  75  LEU   A HD22 1 
ATOM   1674 H HD23 . LEU   A 1 75  ? 35.587 -1.836  -1.388  1.00 23.99 ?  75  LEU   A HD23 1 
ATOM   1675 N N    . LYS   A 1 76  ? 34.063 -3.652  -5.371  1.00 15.09 ?  76  LYS   A N    1 
ATOM   1676 C CA   . LYS   A 1 76  ? 33.465 -4.370  -6.489  1.00 15.49 ?  76  LYS   A CA   1 
ATOM   1677 C C    . LYS   A 1 76  ? 31.954 -4.437  -6.303  1.00 13.64 ?  76  LYS   A C    1 
ATOM   1678 O O    . LYS   A 1 76  ? 31.454 -4.531  -5.179  1.00 13.85 ?  76  LYS   A O    1 
ATOM   1679 C CB   . LYS   A 1 76  ? 33.993 -5.814  -6.544  1.00 17.58 ?  76  LYS   A CB   1 
ATOM   1680 C CG   . LYS   A 1 76  ? 35.506 -5.942  -6.692  1.00 19.55 ?  76  LYS   A CG   1 
ATOM   1681 C CD   . LYS   A 1 76  ? 35.985 -7.375  -6.537  1.00 21.26 ?  76  LYS   A CD   1 
ATOM   1682 C CE   . LYS   A 1 76  ? 37.490 -7.433  -6.698  1.00 24.34 ?  76  LYS   A CE   1 
ATOM   1683 N NZ   . LYS   A 1 76  ? 38.018 -8.780  -6.477  1.00 25.69 ?  76  LYS   A NZ   1 
ATOM   1684 H H    . LYS   A 1 76  ? 34.303 -4.172  -4.725  1.00 18.13 ?  76  LYS   A H    1 
ATOM   1685 H HA   . LYS   A 1 76  ? 33.665 -3.920  -7.326  1.00 18.60 ?  76  LYS   A HA   1 
ATOM   1686 H HB2  . LYS   A 1 76  ? 33.737 -6.265  -5.724  1.00 21.11 ?  76  LYS   A HB2  1 
ATOM   1687 H HB3  . LYS   A 1 76  ? 33.584 -6.262  -7.302  1.00 21.11 ?  76  LYS   A HB3  1 
ATOM   1688 H HG2  . LYS   A 1 76  ? 35.767 -5.631  -7.572  1.00 23.48 ?  76  LYS   A HG2  1 
ATOM   1689 H HG3  . LYS   A 1 76  ? 35.939 -5.407  -6.007  1.00 23.48 ?  76  LYS   A HG3  1 
ATOM   1690 H HD2  . LYS   A 1 76  ? 35.751 -7.707  -5.653  1.00 25.53 ?  76  LYS   A HD2  1 
ATOM   1691 H HD3  . LYS   A 1 76  ? 35.577 -7.933  -7.223  1.00 25.53 ?  76  LYS   A HD3  1 
ATOM   1692 H HE2  . LYS   A 1 76  ? 37.720 -7.155  -7.597  1.00 29.22 ?  76  LYS   A HE2  1 
ATOM   1693 H HE3  . LYS   A 1 76  ? 37.896 -6.836  -6.048  1.00 29.22 ?  76  LYS   A HE3  1 
ATOM   1694 H HZ1  . LYS   A 1 76  ? 38.901 -8.787  -6.578  1.00 30.84 ?  76  LYS   A HZ1  1 
ATOM   1695 H HZ2  . LYS   A 1 76  ? 37.819 -9.062  -5.655  1.00 30.84 ?  76  LYS   A HZ2  1 
ATOM   1696 H HZ3  . LYS   A 1 76  ? 37.659 -9.352  -7.065  1.00 30.84 ?  76  LYS   A HZ3  1 
ATOM   1697 N N    . VAL   A 1 77  ? 31.218 -4.412  -7.422  1.00 14.44 ?  77  VAL   A N    1 
ATOM   1698 C CA   . VAL   A 1 77  ? 29.806 -4.789  -7.355  1.00 14.08 ?  77  VAL   A CA   1 
ATOM   1699 C C    . VAL   A 1 77  ? 29.725 -6.234  -6.891  1.00 14.38 ?  77  VAL   A C    1 
ATOM   1700 O O    . VAL   A 1 77  ? 30.371 -7.116  -7.463  1.00 14.71 ?  77  VAL   A O    1 
ATOM   1701 C CB   . VAL   A 1 77  ? 29.107 -4.588  -8.710  1.00 15.96 ?  77  VAL   A CB   1 
ATOM   1702 C CG1  . VAL   A 1 77  ? 27.631 -4.973  -8.617  1.00 17.80 ?  77  VAL   A CG1  1 
ATOM   1703 C CG2  . VAL   A 1 77  ? 29.217 -3.142  -9.161  1.00 18.09 ?  77  VAL   A CG2  1 
ATOM   1704 H H    . VAL   A 1 77  ? 31.496 -4.180  -8.198  1.00 17.34 ?  77  VAL   A H    1 
ATOM   1705 H HA   . VAL   A 1 77  ? 29.353 -4.231  -6.697  1.00 16.91 ?  77  VAL   A HA   1 
ATOM   1706 H HB   . VAL   A 1 77  ? 29.529 -5.155  -9.375  1.00 19.17 ?  77  VAL   A HB   1 
ATOM   1707 H HG11 . VAL   A 1 77  ? 27.190 -4.722  -9.441  1.00 21.38 ?  77  VAL   A HG11 1 
ATOM   1708 H HG12 . VAL   A 1 77  ? 27.559 -5.930  -8.479  1.00 21.38 ?  77  VAL   A HG12 1 
ATOM   1709 H HG13 . VAL   A 1 77  ? 27.232 -4.500  -7.869  1.00 21.38 ?  77  VAL   A HG13 1 
ATOM   1710 H HG21 . VAL   A 1 77  ? 28.720 -3.035  -9.987  1.00 21.72 ?  77  VAL   A HG21 1 
ATOM   1711 H HG22 . VAL   A 1 77  ? 28.848 -2.571  -8.472  1.00 21.72 ?  77  VAL   A HG22 1 
ATOM   1712 H HG23 . VAL   A 1 77  ? 30.151 -2.930  -9.306  1.00 21.72 ?  77  VAL   A HG23 1 
ATOM   1713 N N    . GLY   A 1 78  ? 28.922 -6.484  -5.858  1.00 13.65 ?  78  GLY   A N    1 
ATOM   1714 C CA   . GLY   A 1 78  ? 28.882 -7.763  -5.183  1.00 14.26 ?  78  GLY   A CA   1 
ATOM   1715 C C    . GLY   A 1 78  ? 29.804 -7.850  -3.985  1.00 13.67 ?  78  GLY   A C    1 
ATOM   1716 O O    . GLY   A 1 78  ? 29.741 -8.839  -3.240  1.00 14.54 ?  78  GLY   A O    1 
ATOM   1717 H H    . GLY   A 1 78  ? 28.367 -5.905  -5.532  1.00 16.39 ?  78  GLY   A H    1 
ATOM   1718 H HA2  . GLY   A 1 78  ? 27.972 -7.938  -4.885  1.00 17.13 ?  78  GLY   A HA2  1 
ATOM   1719 H HA3  . GLY   A 1 78  ? 29.128 -8.461  -5.813  1.00 17.13 ?  78  GLY   A HA3  1 
ATOM   1720 N N    . GLY   A 1 79  ? 30.673 -6.855  -3.782  1.00 13.90 ?  79  GLY   A N    1 
ATOM   1721 C CA   . GLY   A 1 79  ? 31.636 -6.870  -2.705  1.00 13.95 ?  79  GLY   A CA   1 
ATOM   1722 C C    . GLY   A 1 79  ? 31.179 -6.093  -1.485  1.00 12.92 ?  79  GLY   A C    1 
ATOM   1723 O O    . GLY   A 1 79  ? 30.056 -5.585  -1.414  1.00 14.01 ?  79  GLY   A O    1 
ATOM   1724 H H    . GLY   A 1 79  ? 30.718 -6.146  -4.273  1.00 16.69 ?  79  GLY   A H    1 
ATOM   1725 H HA2  . GLY   A 1 79  ? 31.802 -7.790  -2.440  1.00 16.76 ?  79  GLY   A HA2  1 
ATOM   1726 H HA3  . GLY   A 1 79  ? 32.471 -6.490  -3.019  1.00 16.76 ?  79  GLY   A HA3  1 
ATOM   1727 N N    . SER   A 1 80  ? 32.084 -5.984  -0.512  1.00 13.53 ?  80  SER   A N    1 
ATOM   1728 C CA   . SER   A 1 80  ? 31.762 -5.354  0.758   1.00 12.97 ?  80  SER   A CA   1 
ATOM   1729 C C    . SER   A 1 80  ? 33.033 -4.904  1.460   1.00 13.46 ?  80  SER   A C    1 
ATOM   1730 O O    . SER   A 1 80  ? 34.149 -5.336  1.130   1.00 15.11 ?  80  SER   A O    1 
ATOM   1731 C CB   . SER   A 1 80  ? 30.989 -6.313  1.674   1.00 13.91 ?  80  SER   A CB   1 
ATOM   1732 O OG   . SER   A 1 80  ? 31.834 -7.350  2.153   1.00 16.11 ?  80  SER   A OG   1 
ATOM   1733 H H    . SER   A 1 80  ? 32.899 -6.274  -0.560  1.00 16.25 ?  80  SER   A H    1 
ATOM   1734 H HA   . SER   A 1 80  ? 31.208 -4.581  0.588   1.00 15.58 ?  80  SER   A HA   1 
ATOM   1735 H HB2  . SER   A 1 80  ? 30.638 -5.821  2.437   1.00 16.71 ?  80  SER   A HB2  1 
ATOM   1736 H HB3  . SER   A 1 80  ? 30.252 -6.710  1.177   1.00 16.71 ?  80  SER   A HB3  1 
ATOM   1737 H HG   . SER   A 1 80  ? 32.142 -7.786  1.498   1.00 19.35 ?  80  SER   A HG   1 
ATOM   1738 N N    . CYS   A 1 81  ? 32.841 -4.055  2.467   1.00 13.11 ?  81  CYS   A N    1 
ATOM   1739 C CA   . CYS   A 1 81  ? 33.894 -3.776  3.428   1.00 13.68 ?  81  CYS   A CA   1 
ATOM   1740 C C    . CYS   A 1 81  ? 33.265 -3.537  4.790   1.00 13.01 ?  81  CYS   A C    1 
ATOM   1741 O O    . CYS   A 1 81  ? 32.106 -3.119  4.883   1.00 14.36 ?  81  CYS   A O    1 
ATOM   1742 C CB   . CYS   A 1 81  ? 34.766 -2.581  3.009   1.00 14.99 ?  81  CYS   A CB   1 
ATOM   1743 S SG   . CYS   A 1 81  ? 33.907 -0.998  3.035   1.00 14.49 ?  81  CYS   A SG   1 
ATOM   1744 H H    . CYS   A 1 81  ? 32.106 -3.628  2.625   1.00 15.75 ?  81  CYS   A H    1 
ATOM   1745 H HA   . CYS   A 1 81  ? 34.472 -4.557  3.500   1.00 16.44 ?  81  CYS   A HA   1 
ATOM   1746 H HB2  . CYS   A 1 81  ? 35.522 -2.519  3.616   1.00 18.01 ?  81  CYS   A HB2  1 
ATOM   1747 H HB3  . CYS   A 1 81  ? 35.084 -2.735  2.106   1.00 18.01 ?  81  CYS   A HB3  1 
ATOM   1748 H HG   . CYS   A 1 81  ? 34.660 -0.137  2.691   1.00 17.40 ?  81  CYS   A HG   1 
ATOM   1749 N N    . VAL   A 1 82  ? 34.035 -3.802  5.844   1.00 13.29 ?  82  VAL   A N    1 
ATOM   1750 C CA   . VAL   A 1 82  ? 33.617 -3.554  7.216   1.00 13.52 ?  82  VAL   A CA   1 
ATOM   1751 C C    . VAL   A 1 82  ? 34.215 -2.237  7.679   1.00 14.61 ?  82  VAL   A C    1 
ATOM   1752 O O    . VAL   A 1 82  ? 35.438 -2.075  7.675   1.00 15.41 ?  82  VAL   A O    1 
ATOM   1753 C CB   . VAL   A 1 82  ? 34.044 -4.694  8.152   1.00 15.70 ?  82  VAL   A CB   1 
ATOM   1754 C CG1  . VAL   A 1 82  ? 33.587 -4.413  9.574   1.00 17.64 ?  82  VAL   A CG1  1 
ATOM   1755 C CG2  . VAL   A 1 82  ? 33.479 -6.023  7.662   1.00 16.37 ?  82  VAL   A CG2  1 
ATOM   1756 H H    . VAL   A 1 82  ? 34.830 -4.141  5.792   1.00 15.96 ?  82  VAL   A H    1 
ATOM   1757 H HA   . VAL   A 1 82  ? 32.645 -3.480  7.248   1.00 16.24 ?  82  VAL   A HA   1 
ATOM   1758 H HB   . VAL   A 1 82  ? 35.009 -4.754  8.157   1.00 18.85 ?  82  VAL   A HB   1 
ATOM   1759 H HG11 . VAL   A 1 82  ? 33.689 -5.217  10.101  1.00 21.18 ?  82  VAL   A HG11 1 
ATOM   1760 H HG12 . VAL   A 1 82  ? 34.129 -3.699  9.948   1.00 21.18 ?  82  VAL   A HG12 1 
ATOM   1761 H HG13 . VAL   A 1 82  ? 32.653 -4.143  9.558   1.00 21.18 ?  82  VAL   A HG13 1 
ATOM   1762 H HG21 . VAL   A 1 82  ? 33.705 -6.716  8.299   1.00 19.66 ?  82  VAL   A HG21 1 
ATOM   1763 H HG22 . VAL   A 1 82  ? 32.513 -5.945  7.585   1.00 19.66 ?  82  VAL   A HG22 1 
ATOM   1764 H HG23 . VAL   A 1 82  ? 33.863 -6.227  6.796   1.00 19.66 ?  82  VAL   A HG23 1 
ATOM   1765 N N    . LEU   A 1 83  ? 33.361 -1.306  8.097   1.00 13.55 ?  83  LEU   A N    1 
ATOM   1766 C CA   . LEU   A 1 83  ? 33.803 -0.049  8.686   1.00 13.69 ?  83  LEU   A CA   1 
ATOM   1767 C C    . LEU   A 1 83  ? 33.097 0.142   10.024  1.00 13.90 ?  83  LEU   A C    1 
ATOM   1768 O O    . LEU   A 1 83  ? 32.372 -0.747  10.494  1.00 14.72 ?  83  LEU   A O    1 
ATOM   1769 C CB   . LEU   A 1 83  ? 33.561 1.115   7.715   1.00 14.15 ?  83  LEU   A CB   1 
ATOM   1770 C CG   . LEU   A 1 83  ? 34.459 1.123   6.472   1.00 14.59 ?  83  LEU   A CG   1 
ATOM   1771 C CD1  . LEU   A 1 83  ? 34.050 2.212   5.498   1.00 15.47 ?  83  LEU   A CD1  1 
ATOM   1772 C CD2  . LEU   A 1 83  ? 35.934 1.276   6.856   1.00 16.21 ?  83  LEU   A CD2  1 
ATOM   1773 H H    . LEU   A 1 83  ? 32.500 -1.389  8.064   1.00 16.27 ?  83  LEU   A H    1 
ATOM   1774 H HA   . LEU   A 1 83  ? 34.759 -0.096  8.856   1.00 16.44 ?  83  LEU   A HA   1 
ATOM   1775 H HB2  . LEU   A 1 83  ? 32.642 1.075   7.403   1.00 17.00 ?  83  LEU   A HB2  1 
ATOM   1776 H HB3  . LEU   A 1 83  ? 33.708 1.951   8.182   1.00 17.00 ?  83  LEU   A HB3  1 
ATOM   1777 H HG   . LEU   A 1 83  ? 34.367 0.271   6.016   1.00 17.52 ?  83  LEU   A HG   1 
ATOM   1778 H HD11 . LEU   A 1 83  ? 34.641 2.183   4.724   1.00 18.58 ?  83  LEU   A HD11 1 
ATOM   1779 H HD12 . LEU   A 1 83  ? 33.136 2.061   5.221   1.00 18.58 ?  83  LEU   A HD12 1 
ATOM   1780 H HD13 . LEU   A 1 83  ? 34.130 3.074   5.936   1.00 18.58 ?  83  LEU   A HD13 1 
ATOM   1781 H HD21 . LEU   A 1 83  ? 36.460 1.456   6.057   1.00 19.46 ?  83  LEU   A HD21 1 
ATOM   1782 H HD22 . LEU   A 1 83  ? 36.031 2.012   7.481   1.00 19.46 ?  83  LEU   A HD22 1 
ATOM   1783 H HD23 . LEU   A 1 83  ? 36.250 0.453   7.270   1.00 19.46 ?  83  LEU   A HD23 1 
ATOM   1784 N N    . SER   A 1 84  ? 33.294 1.296   10.653  1.00 14.57 ?  84  SER   A N    1 
ATOM   1785 C CA   . SER   A 1 84  ? 32.651 1.546   11.930  1.00 14.59 ?  84  SER   A CA   1 
ATOM   1786 C C    . SER   A 1 84  ? 31.131 1.664   11.785  1.00 14.96 ?  84  SER   A C    1 
ATOM   1787 O O    . SER   A 1 84  ? 30.607 2.133   10.766  1.00 15.11 ?  84  SER   A O    1 
ATOM   1788 C CB   . SER   A 1 84  ? 33.183 2.842   12.525  1.00 15.65 ?  84  SER   A CB   1 
ATOM   1789 O OG   . SER   A 1 84  ? 32.532 3.161   13.740  1.00 16.92 ?  84  SER   A OG   1 
ATOM   1790 H H    . SER   A 1 84  ? 33.790 1.941   10.361  1.00 17.50 ?  84  SER   A H    1 
ATOM   1791 H HA   . SER   A 1 84  ? 32.861 0.815   12.537  1.00 17.52 ?  84  SER   A HA   1 
ATOM   1792 H HB2  . SER   A 1 84  ? 34.136 2.740   12.704  1.00 18.79 ?  84  SER   A HB2  1 
ATOM   1793 H HB3  . SER   A 1 84  ? 33.052 3.558   11.882  1.00 18.79 ?  84  SER   A HB3  1 
ATOM   1794 H HG   . SER   A 1 84  ? 32.833 3.893   14.038  1.00 20.32 ?  84  SER   A HG   1 
ATOM   1795 N N    . GLY   A 1 85  ? 30.427 1.276   12.844  1.00 15.24 ?  85  GLY   A N    1 
ATOM   1796 C CA   . GLY   A 1 85  ? 29.005 1.521   12.937  1.00 16.64 ?  85  GLY   A CA   1 
ATOM   1797 C C    . GLY   A 1 85  ? 28.651 2.844   13.580  1.00 15.76 ?  85  GLY   A C    1 
ATOM   1798 O O    . GLY   A 1 85  ? 27.467 3.176   13.683  1.00 16.78 ?  85  GLY   A O    1 
ATOM   1799 H H    . GLY   A 1 85  ? 30.759 0.862   13.526  1.00 18.30 ?  85  GLY   A H    1 
ATOM   1800 H HA2  . GLY   A 1 85  ? 28.628 1.505   12.045  1.00 19.98 ?  85  GLY   A HA2  1 
ATOM   1801 H HA3  . GLY   A 1 85  ? 28.596 0.818   13.455  1.00 19.98 ?  85  GLY   A HA3  1 
ATOM   1802 N N    . HIS   A 1 86  ? 29.643 3.608   14.033  1.00 15.08 ?  86  HIS   A N    1 
ATOM   1803 C CA   . HIS   A 1 86  ? 29.432 4.956   14.589  1.00 15.83 ?  86  HIS   A CA   1 
ATOM   1804 C C    . HIS   A 1 86  ? 28.440 4.840   15.740  1.00 16.49 ?  86  HIS   A C    1 
ATOM   1805 O O    . HIS   A 1 86  ? 28.601 3.946   16.585  1.00 17.58 ?  86  HIS   A O    1 
ATOM   1806 C CB   . HIS   A 1 86  ? 29.064 5.925   13.474  1.00 15.38 ?  86  HIS   A CB   1 
ATOM   1807 C CG   . HIS   A 1 86  ? 30.125 6.015   12.441  1.00 15.64 ?  86  HIS   A CG   1 
ATOM   1808 N ND1  . HIS   A 1 86  ? 31.229 6.830   12.584  1.00 17.71 ?  86  HIS   A ND1  1 
ATOM   1809 C CD2  . HIS   A 1 86  ? 30.310 5.315   11.300  1.00 15.46 ?  86  HIS   A CD2  1 
ATOM   1810 C CE1  . HIS   A 1 86  ? 32.030 6.652   11.548  1.00 17.18 ?  86  HIS   A CE1  1 
ATOM   1811 N NE2  . HIS   A 1 86  ? 31.502 5.731   10.762  1.00 16.22 ?  86  HIS   A NE2  1 
ATOM   1812 H H    . HIS   A 1 86  ? 30.469 3.369   14.048  1.00 18.11 ?  86  HIS   A H    1 
ATOM   1813 H HA   . HIS   A 1 86  ? 30.269 5.271   14.960  1.00 19.01 ?  86  HIS   A HA   1 
ATOM   1814 H HB2  . HIS   A 1 86  ? 28.243 5.628   13.045  1.00 18.47 ?  86  HIS   A HB2  1 
ATOM   1815 H HB3  . HIS   A 1 86  ? 28.930 6.816   13.848  1.00 18.47 ?  86  HIS   A HB3  1 
ATOM   1816 H HD2  . HIS   A 1 86  ? 29.737 4.669   10.946  1.00 18.57 ?  86  HIS   A HD2  1 
ATOM   1817 H HE1  . HIS   A 1 86  ? 32.831 7.095   11.394  1.00 20.63 ?  86  HIS   A HE1  1 
ATOM   1818 H HE2  . HIS   A 1 86  ? 31.837 5.451   10.016  1.00 19.48 ?  86  HIS   A HE2  1 
ATOM   1819 N N    . ASN   A 1 87  ? 27.427 5.695   15.808  1.00 17.90 ?  87  ASN   A N    1 
ATOM   1820 C CA   . ASN   A 1 87  ? 26.453 5.692   16.883  1.00 19.52 ?  87  ASN   A CA   1 
ATOM   1821 C C    . ASN   A 1 87  ? 25.317 4.711   16.650  1.00 20.85 ?  87  ASN   A C    1 
ATOM   1822 O O    . ASN   A 1 87  ? 24.391 4.656   17.464  1.00 24.93 ?  87  ASN   A O    1 
ATOM   1823 C CB   . ASN   A 1 87  ? 25.863 7.099   17.041  1.00 21.19 ?  87  ASN   A CB   1 
ATOM   1824 C CG   . ASN   A 1 87  ? 25.354 7.669   15.727  1.00 21.74 ?  87  ASN   A CG   1 
ATOM   1825 O OD1  . ASN   A 1 87  ? 26.009 7.550   14.691  1.00 22.54 ?  87  ASN   A OD1  1 
ATOM   1826 N ND2  . ASN   A 1 87  ? 24.189 8.298   15.766  1.00 22.18 ?  87  ASN   A ND2  1 
ATOM   1827 H H    . ASN   A 1 87  ? 27.278 6.305   15.216  1.00 21.49 ?  87  ASN   A H    1 
ATOM   1828 H HA   . ASN   A 1 87  ? 26.892 5.455   17.717  1.00 23.43 ?  87  ASN   A HA   1 
ATOM   1829 H HB2  . ASN   A 1 87  ? 25.120 7.062   17.667  1.00 25.44 ?  87  ASN   A HB2  1 
ATOM   1830 H HB3  . ASN   A 1 87  ? 26.549 7.696   17.379  1.00 25.44 ?  87  ASN   A HB3  1 
ATOM   1831 H HD21 . ASN   A 1 87  ? 23.856 8.630   15.046  1.00 26.62 ?  87  ASN   A HD21 1 
ATOM   1832 H HD22 . ASN   A 1 87  ? 23.759 8.365   16.509  1.00 26.62 ?  87  ASN   A HD22 1 
ATOM   1833 N N    A LEU   A 1 88  ? 25.365 3.933   15.569  0.46 19.68 ?  88  LEU   A N    1 
ATOM   1834 N N    B LEU   A 1 88  ? 25.369 3.920   15.582  0.54 19.68 ?  88  LEU   A N    1 
ATOM   1835 C CA   A LEU   A 1 88  ? 24.255 3.070   15.177  0.46 19.59 ?  88  LEU   A CA   1 
ATOM   1836 C CA   B LEU   A 1 88  ? 24.250 3.069   15.201  0.54 19.74 ?  88  LEU   A CA   1 
ATOM   1837 C C    A LEU   A 1 88  ? 24.477 1.602   15.509  0.46 19.51 ?  88  LEU   A C    1 
ATOM   1838 C C    B LEU   A 1 88  ? 24.474 1.591   15.474  0.54 19.63 ?  88  LEU   A C    1 
ATOM   1839 O O    A LEU   A 1 88  ? 23.506 0.881   15.766  0.46 20.35 ?  88  LEU   A O    1 
ATOM   1840 O O    B LEU   A 1 88  ? 23.502 0.853   15.648  0.54 20.51 ?  88  LEU   A O    1 
ATOM   1841 C CB   A LEU   A 1 88  ? 24.015 3.186   13.669  0.46 19.19 ?  88  LEU   A CB   1 
ATOM   1842 C CB   B LEU   A 1 88  ? 23.955 3.240   13.708  0.54 19.44 ?  88  LEU   A CB   1 
ATOM   1843 C CG   A LEU   A 1 88  ? 23.716 4.573   13.102  0.46 20.46 ?  88  LEU   A CG   1 
ATOM   1844 C CG   B LEU   A 1 88  ? 23.652 4.663   13.237  0.54 20.78 ?  88  LEU   A CG   1 
ATOM   1845 C CD1  A LEU   A 1 88  ? 23.610 4.497   11.587  0.46 21.19 ?  88  LEU   A CD1  1 
ATOM   1846 C CD1  B LEU   A 1 88  ? 23.487 4.696   11.726  0.54 21.55 ?  88  LEU   A CD1  1 
ATOM   1847 C CD2  A LEU   A 1 88  ? 22.446 5.153   13.708  0.46 21.69 ?  88  LEU   A CD2  1 
ATOM   1848 C CD2  B LEU   A 1 88  ? 22.412 5.212   13.925  0.54 21.94 ?  88  LEU   A CD2  1 
ATOM   1849 H H    A LEU   A 1 88  ? 26.047 3.882   15.045  0.46 23.64 ?  88  LEU   A H    1 
ATOM   1850 H H    B LEU   A 1 88  ? 26.057 3.851   15.069  0.54 23.64 ?  88  LEU   A H    1 
ATOM   1851 H HA   A LEU   A 1 88  ? 23.452 3.365   15.632  0.46 23.52 ?  88  LEU   A HA   1 
ATOM   1852 H HA   B LEU   A 1 88  ? 23.465 3.351   15.696  0.54 23.70 ?  88  LEU   A HA   1 
ATOM   1853 H HB2  A LEU   A 1 88  ? 24.802 2.860   13.211  0.46 23.04 ?  88  LEU   A HB2  1 
ATOM   1854 H HB2  B LEU   A 1 88  ? 24.723 2.928   13.211  0.54 23.34 ?  88  LEU   A HB2  1 
ATOM   1855 H HB3  A LEU   A 1 88  ? 23.257 2.624   13.444  0.46 23.04 ?  88  LEU   A HB3  1 
ATOM   1856 H HB3  B LEU   A 1 88  ? 23.184 2.693   13.493  0.54 23.34 ?  88  LEU   A HB3  1 
ATOM   1857 H HG   A LEU   A 1 88  ? 24.448 5.169   13.317  0.46 24.57 ?  88  LEU   A HG   1 
ATOM   1858 H HG   B LEU   A 1 88  ? 24.397 5.238   13.467  0.54 24.95 ?  88  LEU   A HG   1 
ATOM   1859 H HD11 A LEU   A 1 88  ? 23.430 5.384   11.236  0.46 25.45 ?  88  LEU   A HD11 1 
ATOM   1860 H HD11 B LEU   A 1 88  ? 23.303 5.607   11.448  0.54 25.88 ?  88  LEU   A HD11 1 
ATOM   1861 H HD12 A LEU   A 1 88  ? 24.446 4.162   11.227  0.46 25.45 ?  88  LEU   A HD12 1 
ATOM   1862 H HD12 B LEU   A 1 88  ? 24.306 4.382   11.312  0.54 25.88 ?  88  LEU   A HD12 1 
ATOM   1863 H HD13 A LEU   A 1 88  ? 22.885 3.896   11.351  0.46 25.45 ?  88  LEU   A HD13 1 
ATOM   1864 H HD13 B LEU   A 1 88  ? 22.747 4.119   11.475  0.54 25.88 ?  88  LEU   A HD13 1 
ATOM   1865 H HD21 A LEU   A 1 88  ? 22.252 6.004   13.284  0.46 26.04 ?  88  LEU   A HD21 1 
ATOM   1866 H HD21 B LEU   A 1 88  ? 22.191 6.073   13.536  0.54 26.34 ?  88  LEU   A HD21 1 
ATOM   1867 H HD22 A LEU   A 1 88  ? 21.713 4.535   13.558  0.46 26.04 ?  88  LEU   A HD22 1 
ATOM   1868 H HD22 B LEU   A 1 88  ? 21.677 4.591   13.789  0.54 26.34 ?  88  LEU   A HD22 1 
ATOM   1869 H HD23 A LEU   A 1 88  ? 22.581 5.280   14.660  0.46 26.04 ?  88  LEU   A HD23 1 
ATOM   1870 H HD23 B LEU   A 1 88  ? 22.592 5.310   14.871  0.54 26.34 ?  88  LEU   A HD23 1 
ATOM   1871 N N    . ALA   A 1 89  ? 25.724 1.146   15.500  1.00 18.30 ?  89  ALA   A N    1 
ATOM   1872 C CA   . ALA   A 1 89  ? 26.060 -0.262  15.638  1.00 18.37 ?  89  ALA   A CA   1 
ATOM   1873 C C    . ALA   A 1 89  ? 27.549 -0.335  15.930  1.00 18.67 ?  89  ALA   A C    1 
ATOM   1874 O O    . ALA   A 1 89  ? 28.273 0.654   15.784  1.00 19.15 ?  89  ALA   A O    1 
ATOM   1875 C CB   . ALA   A 1 89  ? 25.764 -1.007  14.338  1.00 17.81 ?  89  ALA   A CB   1 
ATOM   1876 H H    A ALA   A 1 89  ? 26.415 1.652   15.415  0.46 21.98 ?  89  ALA   A H    1 
ATOM   1877 H H    B ALA   A 1 89  ? 26.413 1.654   15.418  0.54 21.98 ?  89  ALA   A H    1 
ATOM   1878 H HA   . ALA   A 1 89  ? 25.554 -0.660  16.369  1.00 22.06 ?  89  ALA   A HA   1 
ATOM   1879 H HB1  . ALA   A 1 89  ? 26.014 -1.939  14.448  1.00 21.39 ?  89  ALA   A HB1  1 
ATOM   1880 H HB2  . ALA   A 1 89  ? 24.816 -0.942  14.142  1.00 21.39 ?  89  ALA   A HB2  1 
ATOM   1881 H HB3  . ALA   A 1 89  ? 26.281 -0.609  13.624  1.00 21.39 ?  89  ALA   A HB3  1 
ATOM   1882 N N    . LYS   A 1 90  ? 28.020 -1.516  16.321  1.00 18.98 ?  90  LYS   A N    1 
ATOM   1883 C CA   . LYS   A 1 90  ? 29.464 -1.684  16.451  1.00 19.80 ?  90  LYS   A CA   1 
ATOM   1884 C C    . LYS   A 1 90  ? 30.148 -1.483  15.103  1.00 17.80 ?  90  LYS   A C    1 
ATOM   1885 O O    . LYS   A 1 90  ? 31.077 -0.667  14.973  1.00 18.79 ?  90  LYS   A O    1 
ATOM   1886 C CB   . LYS   A 1 90  ? 29.794 -3.061  17.030  1.00 22.16 ?  90  LYS   A CB   1 
ATOM   1887 C CG   . LYS   A 1 90  ? 31.265 -3.224  17.396  1.00 27.79 ?  90  LYS   A CG   1 
ATOM   1888 C CD   . LYS   A 1 90  ? 31.469 -4.439  18.290  1.00 33.36 ?  90  LYS   A CD   1 
ATOM   1889 C CE   . LYS   A 1 90  ? 32.882 -4.505  18.852  1.00 37.53 ?  90  LYS   A CE   1 
ATOM   1890 N NZ   . LYS   A 1 90  ? 33.863 -5.004  17.853  1.00 40.02 ?  90  LYS   A NZ   1 
ATOM   1891 H H    . LYS   A 1 90  ? 27.542 -2.202  16.519  1.00 22.79 ?  90  LYS   A H    1 
ATOM   1892 H HA   . LYS   A 1 90  ? 29.805 -1.017  17.061  1.00 23.78 ?  90  LYS   A HA   1 
ATOM   1893 H HB2  . LYS   A 1 90  ? 29.267 -3.199  17.836  1.00 26.61 ?  90  LYS   A HB2  1 
ATOM   1894 H HB3  . LYS   A 1 90  ? 29.571 -3.743  16.375  1.00 26.61 ?  90  LYS   A HB3  1 
ATOM   1895 H HG2  . LYS   A 1 90  ? 31.788 -3.345  16.589  1.00 33.36 ?  90  LYS   A HG2  1 
ATOM   1896 H HG3  . LYS   A 1 90  ? 31.566 -2.436  17.878  1.00 33.36 ?  90  LYS   A HG3  1 
ATOM   1897 H HD2  . LYS   A 1 90  ? 30.850 -4.395  19.036  1.00 40.05 ?  90  LYS   A HD2  1 
ATOM   1898 H HD3  . LYS   A 1 90  ? 31.312 -5.245  17.773  1.00 40.05 ?  90  LYS   A HD3  1 
ATOM   1899 H HE2  . LYS   A 1 90  ? 33.158 -3.616  19.126  1.00 45.06 ?  90  LYS   A HE2  1 
ATOM   1900 H HE3  . LYS   A 1 90  ? 32.895 -5.106  19.614  1.00 45.06 ?  90  LYS   A HE3  1 
ATOM   1901 H HZ1  . LYS   A 1 90  ? 34.673 -5.053  18.220  1.00 48.03 ?  90  LYS   A HZ1  1 
ATOM   1902 H HZ2  . LYS   A 1 90  ? 33.624 -5.815  17.573  1.00 48.03 ?  90  LYS   A HZ2  1 
ATOM   1903 H HZ3  . LYS   A 1 90  ? 33.893 -4.454  17.156  1.00 48.03 ?  90  LYS   A HZ3  1 
ATOM   1904 N N    . HIS   A 1 91  ? 29.693 -2.215  14.085  1.00 15.70 ?  91  HIS   A N    1 
ATOM   1905 C CA   . HIS   A 1 91  ? 30.261 -2.201  12.751  1.00 15.76 ?  91  HIS   A CA   1 
ATOM   1906 C C    . HIS   A 1 91  ? 29.174 -1.937  11.724  1.00 14.29 ?  91  HIS   A C    1 
ATOM   1907 O O    . HIS   A 1 91  ? 28.000 -2.283  11.923  1.00 15.25 ?  91  HIS   A O    1 
ATOM   1908 C CB   . HIS   A 1 91  ? 30.865 -3.557  12.380  1.00 19.47 ?  91  HIS   A CB   1 
ATOM   1909 C CG   . HIS   A 1 91  ? 31.892 -4.053  13.344  1.00 24.57 ?  91  HIS   A CG   1 
ATOM   1910 N ND1  . HIS   A 1 91  ? 33.170 -3.541  13.396  1.00 26.96 ?  91  HIS   A ND1  1 
ATOM   1911 C CD2  . HIS   A 1 91  ? 31.836 -5.024  14.284  1.00 26.85 ?  91  HIS   A CD2  1 
ATOM   1912 C CE1  . HIS   A 1 91  ? 33.856 -4.174  14.331  1.00 28.41 ?  91  HIS   A CE1  1 
ATOM   1913 N NE2  . HIS   A 1 91  ? 33.070 -5.081  14.883  1.00 28.56 ?  91  HIS   A NE2  1 
ATOM   1914 H H    . HIS   A 1 91  ? 29.025 -2.757  14.153  1.00 18.85 ?  91  HIS   A H    1 
ATOM   1915 H HA   . HIS   A 1 91  ? 30.949 -1.516  12.679  1.00 18.92 ?  91  HIS   A HA   1 
ATOM   1916 H HB2  . HIS   A 1 91  ? 30.152 -4.212  12.346  1.00 23.38 ?  91  HIS   A HB2  1 
ATOM   1917 H HB3  . HIS   A 1 91  ? 31.286 -3.483  11.509  1.00 23.38 ?  91  HIS   A HB3  1 
ATOM   1918 H HD1  . HIS   A 1 91  ? 33.473 -2.907  12.894  1.00 32.37 ?  91  HIS   A HD1  1 
ATOM   1919 H HD2  . HIS   A 1 91  ? 31.103 -5.552  14.487  1.00 32.24 ?  91  HIS   A HD2  1 
ATOM   1920 H HE1  . HIS   A 1 91  ? 34.747 -4.006  14.556  1.00 34.10 ?  91  HIS   A HE1  1 
ATOM   1921 N N    . CYS   A 1 92  ? 29.575 -1.365  10.598  1.00 14.18 ?  92  CYS   A N    1 
ATOM   1922 C CA   . CYS   A 1 92  ? 28.728 -1.293  9.414   1.00 14.20 ?  92  CYS   A CA   1 
ATOM   1923 C C    . CYS   A 1 92  ? 29.376 -2.119  8.313   1.00 13.94 ?  92  CYS   A C    1 
ATOM   1924 O O    . CYS   A 1 92  ? 30.527 -1.864  7.940   1.00 14.16 ?  92  CYS   A O    1 
ATOM   1925 C CB   . CYS   A 1 92  ? 28.525 0.147   8.939   1.00 14.33 ?  92  CYS   A CB   1 
ATOM   1926 S SG   . CYS   A 1 92  ? 27.503 0.257   7.440   1.00 14.02 ?  92  CYS   A SG   1 
ATOM   1927 H H    . CYS   A 1 92  ? 30.348 -1.000  10.486  1.00 17.03 ?  92  CYS   A H    1 
ATOM   1928 H HA   . CYS   A 1 92  ? 27.855 -1.669  9.618   1.00 17.05 ?  92  CYS   A HA   1 
ATOM   1929 H HB2  . CYS   A 1 92  ? 28.090 0.658   9.643   1.00 17.22 ?  92  CYS   A HB2  1 
ATOM   1930 H HB3  . CYS   A 1 92  ? 29.395 0.538   8.742   1.00 17.22 ?  92  CYS   A HB3  1 
ATOM   1931 H HG   . CYS   A 1 92  ? 27.381 1.406   7.132   1.00 16.84 ?  92  CYS   A HG   1 
ATOM   1932 N N    . LEU   A 1 93  ? 28.634 -3.096  7.798   1.00 13.43 ?  93  LEU   A N    1 
ATOM   1933 C CA   . LEU   A 1 93  ? 29.035 -3.861  6.624   1.00 12.38 ?  93  LEU   A CA   1 
ATOM   1934 C C    . LEU   A 1 93  ? 28.442 -3.178  5.398   1.00 12.54 ?  93  LEU   A C    1 
ATOM   1935 O O    . LEU   A 1 93  ? 27.231 -3.231  5.179   1.00 12.91 ?  93  LEU   A O    1 
ATOM   1936 C CB   . LEU   A 1 93  ? 28.564 -5.312  6.737   1.00 13.76 ?  93  LEU   A CB   1 
ATOM   1937 C CG   . LEU   A 1 93  ? 28.922 -6.230  5.566   1.00 13.58 ?  93  LEU   A CG   1 
ATOM   1938 C CD1  . LEU   A 1 93  ? 30.430 -6.493  5.530   1.00 14.85 ?  93  LEU   A CD1  1 
ATOM   1939 C CD2  . LEU   A 1 93  ? 28.138 -7.546  5.618   1.00 14.55 ?  93  LEU   A CD2  1 
ATOM   1940 H H    . LEU   A 1 93  ? 27.875 -3.346  8.126   1.00 16.13 ?  93  LEU   A H    1 
ATOM   1941 H HA   . LEU   A 1 93  ? 29.999 -3.848  6.544   1.00 14.87 ?  93  LEU   A HA   1 
ATOM   1942 H HB2  . LEU   A 1 93  ? 28.964 -5.695  7.538   1.00 16.53 ?  93  LEU   A HB2  1 
ATOM   1943 H HB3  . LEU   A 1 93  ? 27.602 -5.317  6.825   1.00 16.53 ?  93  LEU   A HB3  1 
ATOM   1944 H HG   . LEU   A 1 93  ? 28.693 -5.775  4.743   1.00 16.31 ?  93  LEU   A HG   1 
ATOM   1945 H HD11 . LEU   A 1 93  ? 30.630 -7.094  4.799   1.00 17.84 ?  93  LEU   A HD11 1 
ATOM   1946 H HD12 . LEU   A 1 93  ? 30.901 -5.649  5.401   1.00 17.84 ?  93  LEU   A HD12 1 
ATOM   1947 H HD13 . LEU   A 1 93  ? 30.705 -6.890  6.373   1.00 17.84 ?  93  LEU   A HD13 1 
ATOM   1948 H HD21 . LEU   A 1 93  ? 28.399 -8.093  4.858   1.00 17.47 ?  93  LEU   A HD21 1 
ATOM   1949 H HD22 . LEU   A 1 93  ? 28.348 -8.006  6.444   1.00 17.47 ?  93  LEU   A HD22 1 
ATOM   1950 H HD23 . LEU   A 1 93  ? 27.192 -7.349  5.575   1.00 17.47 ?  93  LEU   A HD23 1 
ATOM   1951 N N    . HIS   A 1 94  ? 29.283 -2.498  4.619   1.00 12.65 ?  94  HIS   A N    1 
ATOM   1952 C CA   . HIS   A 1 94  ? 28.845 -1.812  3.409   1.00 12.59 ?  94  HIS   A CA   1 
ATOM   1953 C C    . HIS   A 1 94  ? 28.865 -2.842  2.295   1.00 12.47 ?  94  HIS   A C    1 
ATOM   1954 O O    . HIS   A 1 94  ? 29.925 -3.378  1.964   1.00 13.99 ?  94  HIS   A O    1 
ATOM   1955 C CB   . HIS   A 1 94  ? 29.815 -0.677  3.080   1.00 12.30 ?  94  HIS   A CB   1 
ATOM   1956 C CG   . HIS   A 1 94  ? 29.822 0.410   4.100   1.00 12.23 ?  94  HIS   A CG   1 
ATOM   1957 N ND1  . HIS   A 1 94  ? 28.972 1.494   4.034   1.00 12.64 ?  94  HIS   A ND1  1 
ATOM   1958 C CD2  . HIS   A 1 94  ? 30.567 0.572   5.217   1.00 12.85 ?  94  HIS   A CD2  1 
ATOM   1959 C CE1  . HIS   A 1 94  ? 29.195 2.271   5.080   1.00 12.93 ?  94  HIS   A CE1  1 
ATOM   1960 N NE2  . HIS   A 1 94  ? 30.145 1.724   5.818   1.00 12.95 ?  94  HIS   A NE2  1 
ATOM   1961 H H    . HIS   A 1 94  ? 30.127 -2.433  4.766   1.00 15.20 ?  94  HIS   A H    1 
ATOM   1962 H HA   . HIS   A 1 94  ? 27.943 -1.463  3.524   1.00 15.12 ?  94  HIS   A HA   1 
ATOM   1963 H HB2  . HIS   A 1 94  ? 30.707 -1.032  3.021   1.00 14.77 ?  94  HIS   A HB2  1 
ATOM   1964 H HB3  . HIS   A 1 94  ? 29.552 -0.279  2.233   1.00 14.77 ?  94  HIS   A HB3  1 
ATOM   1965 H HD2  . HIS   A 1 94  ? 31.218 -0.009  5.537   1.00 15.44 ?  94  HIS   A HD2  1 
ATOM   1966 H HE1  . HIS   A 1 94  ? 28.749 3.070   5.270   1.00 15.53 ?  94  HIS   A HE1  1 
ATOM   1967 H HE2  . HIS   A 1 94  ? 30.466 2.060   6.546   1.00 15.55 ?  94  HIS   A HE2  1 
ATOM   1968 N N    . VAL   A 1 95  ? 27.694 -3.169  1.751   1.00 12.12 ?  95  VAL   A N    1 
ATOM   1969 C CA   . VAL   A 1 95  ? 27.550 -4.207  0.737   1.00 12.42 ?  95  VAL   A CA   1 
ATOM   1970 C C    . VAL   A 1 95  ? 27.000 -3.574  -0.528  1.00 12.34 ?  95  VAL   A C    1 
ATOM   1971 O O    . VAL   A 1 95  ? 26.011 -2.836  -0.476  1.00 12.73 ?  95  VAL   A O    1 
ATOM   1972 C CB   . VAL   A 1 95  ? 26.628 -5.355  1.198   1.00 12.86 ?  95  VAL   A CB   1 
ATOM   1973 C CG1  . VAL   A 1 95  ? 26.518 -6.397  0.093   1.00 13.37 ?  95  VAL   A CG1  1 
ATOM   1974 C CG2  . VAL   A 1 95  ? 27.142 -5.977  2.482   1.00 12.63 ?  95  VAL   A CG2  1 
ATOM   1975 H H    . VAL   A 1 95  ? 26.945 -2.787  1.948   1.00 14.55 ?  95  VAL   A H    1 
ATOM   1976 H HA   . VAL   A 1 95  ? 28.420 -4.585  0.533   1.00 14.92 ?  95  VAL   A HA   1 
ATOM   1977 H HB   . VAL   A 1 95  ? 25.739 -5.005  1.365   1.00 15.45 ?  95  VAL   A HB   1 
ATOM   1978 H HG11 . VAL   A 1 95  ? 26.144 -7.212  0.458   1.00 16.06 ?  95  VAL   A HG11 1 
ATOM   1979 H HG12 . VAL   A 1 95  ? 25.945 -6.058  -0.614  1.00 16.06 ?  95  VAL   A HG12 1 
ATOM   1980 H HG13 . VAL   A 1 95  ? 27.407 -6.576  -0.263  1.00 16.06 ?  95  VAL   A HG13 1 
ATOM   1981 H HG21 . VAL   A 1 95  ? 26.588 -6.742  2.709   1.00 15.17 ?  95  VAL   A HG21 1 
ATOM   1982 H HG22 . VAL   A 1 95  ? 28.060 -6.263  2.351   1.00 15.17 ?  95  VAL   A HG22 1 
ATOM   1983 H HG23 . VAL   A 1 95  ? 27.098 -5.317  3.190   1.00 15.17 ?  95  VAL   A HG23 1 
ATOM   1984 N N    . VAL   A 1 96  ? 27.632 -3.871  -1.662  1.00 11.96 ?  96  VAL   A N    1 
ATOM   1985 C CA   . VAL   A 1 96  ? 27.237 -3.339  -2.960  1.00 12.15 ?  96  VAL   A CA   1 
ATOM   1986 C C    . VAL   A 1 96  ? 26.442 -4.390  -3.726  1.00 13.15 ?  96  VAL   A C    1 
ATOM   1987 O O    . VAL   A 1 96  ? 27.010 -5.336  -4.280  1.00 13.52 ?  96  VAL   A O    1 
ATOM   1988 C CB   . VAL   A 1 96  ? 28.443 -2.887  -3.785  1.00 12.50 ?  96  VAL   A CB   1 
ATOM   1989 C CG1  . VAL   A 1 96  ? 27.955 -2.246  -5.079  1.00 13.01 ?  96  VAL   A CG1  1 
ATOM   1990 C CG2  . VAL   A 1 96  ? 29.298 -1.925  -2.973  1.00 13.55 ?  96  VAL   A CG2  1 
ATOM   1991 H H    . VAL   A 1 96  ? 28.320 -4.394  -1.706  1.00 14.37 ?  96  VAL   A H    1 
ATOM   1992 H HA   . VAL   A 1 96  ? 26.666 -2.567  -2.823  1.00 14.60 ?  96  VAL   A HA   1 
ATOM   1993 H HB   . VAL   A 1 96  ? 28.985 -3.657  -4.013  1.00 15.01 ?  96  VAL   A HB   1 
ATOM   1994 H HG11 . VAL   A 1 96  ? 28.687 -1.774  -5.499  1.00 15.63 ?  96  VAL   A HG11 1 
ATOM   1995 H HG12 . VAL   A 1 96  ? 27.621 -2.937  -5.674  1.00 15.63 ?  96  VAL   A HG12 1 
ATOM   1996 H HG13 . VAL   A 1 96  ? 27.237 -1.619  -4.871  1.00 15.63 ?  96  VAL   A HG13 1 
ATOM   1997 H HG21 . VAL   A 1 96  ? 29.998 -1.565  -3.542  1.00 16.27 ?  96  VAL   A HG21 1 
ATOM   1998 H HG22 . VAL   A 1 96  ? 28.739 -1.204  -2.642  1.00 16.27 ?  96  VAL   A HG22 1 
ATOM   1999 H HG23 . VAL   A 1 96  ? 29.695 -2.403  -2.227  1.00 16.27 ?  96  VAL   A HG23 1 
ATOM   2000 N N    A GLY   A 1 97  ? 25.125 -4.218  -3.770  0.46 13.38 ?  97  GLY   A N    1 
ATOM   2001 N N    B GLY   A 1 97  ? 25.129 -4.212  -3.810  0.54 12.87 ?  97  GLY   A N    1 
ATOM   2002 C CA   A GLY   A 1 97  ? 24.300 -4.986  -4.665  0.46 14.03 ?  97  GLY   A CA   1 
ATOM   2003 C CA   B GLY   A 1 97  ? 24.342 -4.994  -4.728  0.54 13.30 ?  97  GLY   A CA   1 
ATOM   2004 C C    A GLY   A 1 97  ? 24.227 -4.304  -6.016  0.46 13.91 ?  97  GLY   A C    1 
ATOM   2005 C C    B GLY   A 1 97  ? 24.440 -4.412  -6.126  0.54 12.77 ?  97  GLY   A C    1 
ATOM   2006 O O    A GLY   A 1 97  ? 24.475 -3.099  -6.133  0.46 14.56 ?  97  GLY   A O    1 
ATOM   2007 O O    B GLY   A 1 97  ? 24.797 -3.242  -6.303  0.54 14.17 ?  97  GLY   A O    1 
ATOM   2008 H H    A GLY   A 1 97  ? 24.688 -3.652  -3.285  0.46 16.07 ?  97  GLY   A H    1 
ATOM   2009 H H    B GLY   A 1 97  ? 24.675 -3.642  -3.345  0.54 15.46 ?  97  GLY   A H    1 
ATOM   2010 H HA2  A GLY   A 1 97  ? 24.678 -5.868  -4.779  0.46 16.86 ?  97  GLY   A HA2  1 
ATOM   2011 H HA2  B GLY   A 1 97  ? 24.666 -5.907  -4.736  0.54 15.98 ?  97  GLY   A HA2  1 
ATOM   2012 H HA3  A GLY   A 1 97  ? 23.404 -5.070  -4.298  0.46 16.86 ?  97  GLY   A HA3  1 
ATOM   2013 H HA3  B GLY   A 1 97  ? 23.411 -4.995  -4.448  0.54 15.98 ?  97  GLY   A HA3  1 
ATOM   2014 N N    A PRO   A 1 98  ? 23.877 -5.049  -7.062  0.46 13.51 ?  98  PRO   A N    1 
ATOM   2015 N N    B PRO   A 1 98  ? 24.119 -5.204  -7.148  0.54 13.28 ?  98  PRO   A N    1 
ATOM   2016 C CA   A PRO   A 1 98  ? 23.760 -4.435  -8.390  0.46 13.38 ?  98  PRO   A CA   1 
ATOM   2017 C CA   B PRO   A 1 98  ? 24.103 -4.670  -8.514  0.54 13.87 ?  98  PRO   A CA   1 
ATOM   2018 C C    A PRO   A 1 98  ? 22.655 -3.391  -8.434  0.46 13.60 ?  98  PRO   A C    1 
ATOM   2019 C C    B PRO   A 1 98  ? 23.040 -3.598  -8.697  0.54 15.13 ?  98  PRO   A C    1 
ATOM   2020 O O    A PRO   A 1 98  ? 21.562 -3.587  -7.901  0.46 13.67 ?  98  PRO   A O    1 
ATOM   2021 O O    B PRO   A 1 98  ? 21.951 -3.659  -8.120  0.54 16.68 ?  98  PRO   A O    1 
ATOM   2022 C CB   A PRO   A 1 98  ? 23.442 -5.623  -9.305  0.46 13.78 ?  98  PRO   A CB   1 
ATOM   2023 C CB   B PRO   A 1 98  ? 23.790 -5.902  -9.374  0.54 14.35 ?  98  PRO   A CB   1 
ATOM   2024 C CG   A PRO   A 1 98  ? 22.834 -6.647  -8.401  0.46 14.07 ?  98  PRO   A CG   1 
ATOM   2025 C CG   B PRO   A 1 98  ? 23.071 -6.831  -8.443  0.54 14.29 ?  98  PRO   A CG   1 
ATOM   2026 C CD   A PRO   A 1 98  ? 23.565 -6.488  -7.092  0.46 13.82 ?  98  PRO   A CD   1 
ATOM   2027 C CD   B PRO   A 1 98  ? 23.778 -6.638  -7.123  0.54 13.49 ?  98  PRO   A CD   1 
ATOM   2028 H HA   A PRO   A 1 98  ? 24.600 -4.033  -8.649  0.46 16.07 ?  98  PRO   A HA   1 
ATOM   2029 H HA   B PRO   A 1 98  ? 24.970 -4.311  -8.748  0.54 16.66 ?  98  PRO   A HA   1 
ATOM   2030 H HB2  A PRO   A 1 98  ? 22.813 -5.349  -9.992  0.46 16.55 ?  98  PRO   A HB2  1 
ATOM   2031 H HB2  B PRO   A 1 98  ? 23.222 -5.642  -10.120 0.54 17.23 ?  98  PRO   A HB2  1 
ATOM   2032 H HB3  A PRO   A 1 98  ? 24.262 -5.955  -9.703  0.46 16.55 ?  98  PRO   A HB3  1 
ATOM   2033 H HB3  B PRO   A 1 98  ? 24.616 -6.295  -9.692  0.54 17.23 ?  98  PRO   A HB3  1 
ATOM   2034 H HG2  A PRO   A 1 98  ? 21.887 -6.463  -8.293  0.46 16.90 ?  98  PRO   A HG2  1 
ATOM   2035 H HG2  B PRO   A 1 98  ? 22.137 -6.572  -8.382  0.54 17.17 ?  98  PRO   A HG2  1 
ATOM   2036 H HG3  A PRO   A 1 98  ? 22.973 -7.531  -8.771  0.46 16.90 ?  98  PRO   A HG3  1 
ATOM   2037 H HG3  B PRO   A 1 98  ? 23.158 -7.741  -8.762  0.54 17.17 ?  98  PRO   A HG3  1 
ATOM   2038 H HD2  A PRO   A 1 98  ? 22.989 -6.738  -6.351  0.46 16.59 ?  98  PRO   A HD2  1 
ATOM   2039 H HD2  B PRO   A 1 98  ? 23.179 -6.845  -6.389  0.54 16.20 ?  98  PRO   A HD2  1 
ATOM   2040 H HD3  A PRO   A 1 98  ? 24.386 -7.004  -7.097  0.46 16.59 ?  98  PRO   A HD3  1 
ATOM   2041 H HD3  B PRO   A 1 98  ? 24.585 -7.177  -7.091  0.54 16.20 ?  98  PRO   A HD3  1 
ATOM   2042 N N    A ASN   A 1 99  ? 22.958 -2.267  -9.073  0.46 13.89 ?  99  ASN   A N    1 
ATOM   2043 N N    B ASN   A 1 99  ? 23.366 -2.614  -9.527  0.54 16.00 ?  99  ASN   A N    1 
ATOM   2044 C CA   A ASN   A 1 99  ? 21.987 -1.209  -9.311  0.46 14.72 ?  99  ASN   A CA   1 
ATOM   2045 C CA   B ASN   A 1 99  ? 22.425 -1.577  -9.933  0.54 17.83 ?  99  ASN   A CA   1 
ATOM   2046 C C    A ASN   A 1 99  ? 21.436 -1.392  -10.721 0.46 17.17 ?  99  ASN   A C    1 
ATOM   2047 C C    B ASN   A 1 99  ? 21.866 -2.006  -11.284 0.54 18.20 ?  99  ASN   A C    1 
ATOM   2048 O O    A ASN   A 1 99  ? 22.123 -1.102  -11.707 0.46 18.74 ?  99  ASN   A O    1 
ATOM   2049 O O    B ASN   A 1 99  ? 22.488 -1.787  -12.325 0.54 17.57 ?  99  ASN   A O    1 
ATOM   2050 C CB   A ASN   A 1 99  ? 22.646 0.157   -9.150  0.46 14.08 ?  99  ASN   A CB   1 
ATOM   2051 C CB   B ASN   A 1 99  ? 23.126 -0.227  -10.027 0.54 18.52 ?  99  ASN   A CB   1 
ATOM   2052 C CG   A ASN   A 1 99  ? 21.643 1.293   -9.168  0.46 14.63 ?  99  ASN   A CG   1 
ATOM   2053 C CG   B ASN   A 1 99  ? 22.168 0.903   -10.361 0.54 19.58 ?  99  ASN   A CG   1 
ATOM   2054 O OD1  A ASN   A 1 99  ? 20.670 1.265   -9.919  0.46 15.95 ?  99  ASN   A OD1  1 
ATOM   2055 O OD1  B ASN   A 1 99  ? 21.042 0.671   -10.790 0.54 19.31 ?  99  ASN   A OD1  1 
ATOM   2056 N ND2  A ASN   A 1 99  ? 21.872 2.293   -8.334  0.46 15.92 ?  99  ASN   A ND2  1 
ATOM   2057 N ND2  B ASN   A 1 99  ? 22.617 2.138   -10.166 0.54 22.55 ?  99  ASN   A ND2  1 
ATOM   2058 H H    A ASN   A 1 99  ? 23.743 -2.085  -9.375  0.46 16.68 ?  99  ASN   A H    1 
ATOM   2059 H H    B ASN   A 1 99  ? 24.148 -2.523  -9.874  0.54 19.22 ?  99  ASN   A H    1 
ATOM   2060 H HA   A ASN   A 1 99  ? 21.257 -1.280  -8.678  0.46 17.68 ?  99  ASN   A HA   1 
ATOM   2061 H HA   B ASN   A 1 99  ? 21.699 -1.513  -9.291  0.54 21.41 ?  99  ASN   A HA   1 
ATOM   2062 H HB2  A ASN   A 1 99  ? 23.119 0.189   -8.307  0.46 16.91 ?  99  ASN   A HB2  1 
ATOM   2063 H HB2  B ASN   A 1 99  ? 23.538 -0.024  -9.175  0.54 22.24 ?  99  ASN   A HB2  1 
ATOM   2064 H HB3  A ASN   A 1 99  ? 23.267 0.299   -9.885  0.46 16.91 ?  99  ASN   A HB3  1 
ATOM   2065 H HB3  B ASN   A 1 99  ? 23.802 -0.270  -10.722 0.54 22.24 ?  99  ASN   A HB3  1 
ATOM   2066 H HD21 A ASN   A 1 99  ? 21.330 2.958   -8.302  0.46 19.11 ?  99  ASN   A HD21 1 
ATOM   2067 H HD21 B ASN   A 1 99  ? 22.113 2.811   -10.345 0.54 27.08 ?  99  ASN   A HD21 1 
ATOM   2068 H HD22 A ASN   A 1 99  ? 22.562 2.272   -7.821  0.46 19.11 ?  99  ASN   A HD22 1 
ATOM   2069 H HD22 B ASN   A 1 99  ? 23.411 2.263   -9.872  0.54 27.08 ?  99  ASN   A HD22 1 
ATOM   2070 N N    A VAL   A 1 100 ? 20.199 -1.888  -10.806 0.46 17.29 ?  100 VAL   A N    1 
ATOM   2071 N N    B VAL   A 1 100 ? 20.687 -2.630  -11.266 0.54 20.86 ?  100 VAL   A N    1 
ATOM   2072 C CA   A VAL   A 1 100 ? 19.557 -2.122  -12.098 0.46 18.72 ?  100 VAL   A CA   1 
ATOM   2073 C CA   B VAL   A 1 100 ? 20.128 -3.154  -12.509 0.54 23.87 ?  100 VAL   A CA   1 
ATOM   2074 C C    A VAL   A 1 100 ? 19.471 -0.833  -12.904 0.46 20.00 ?  100 VAL   A C    1 
ATOM   2075 C C    B VAL   A 1 100 ? 19.606 -2.037  -13.405 0.54 25.54 ?  100 VAL   A C    1 
ATOM   2076 O O    A VAL   A 1 100 ? 19.537 -0.854  -14.140 0.46 20.80 ?  100 VAL   A O    1 
ATOM   2077 O O    B VAL   A 1 100 ? 19.459 -2.237  -14.616 0.54 26.82 ?  100 VAL   A O    1 
ATOM   2078 C CB   A VAL   A 1 100 ? 18.170 -2.765  -11.883 0.46 19.66 ?  100 VAL   A CB   1 
ATOM   2079 C CB   B VAL   A 1 100 ? 19.076 -4.253  -12.255 0.54 26.20 ?  100 VAL   A CB   1 
ATOM   2080 C CG1  A VAL   A 1 100 ? 17.461 -2.977  -13.215 0.46 20.62 ?  100 VAL   A CG1  1 
ATOM   2081 C CG1  B VAL   A 1 100 ? 19.309 -4.923  -10.907 0.54 27.38 ?  100 VAL   A CG1  1 
ATOM   2082 C CG2  A VAL   A 1 100 ? 18.311 -4.080  -11.139 0.46 19.80 ?  100 VAL   A CG2  1 
ATOM   2083 C CG2  B VAL   A 1 100 ? 17.661 -3.704  -12.367 0.54 27.74 ?  100 VAL   A CG2  1 
ATOM   2084 H H    A VAL   A 1 100 ? 19.713 -2.093  -10.126 0.46 20.76 ?  100 VAL   A H    1 
ATOM   2085 H H    B VAL   A 1 100 ? 20.213 -2.755  -10.561 0.54 25.05 ?  100 VAL   A H    1 
ATOM   2086 H HA   A VAL   A 1 100 ? 20.095 -2.754  -12.598 0.46 22.48 ?  100 VAL   A HA   1 
ATOM   2087 H HA   B VAL   A 1 100 ? 20.850 -3.581  -12.991 0.54 28.66 ?  100 VAL   A HA   1 
ATOM   2088 H HB   A VAL   A 1 100 ? 17.624 -2.171  -11.344 0.46 23.61 ?  100 VAL   A HB   1 
ATOM   2089 H HB   B VAL   A 1 100 ? 19.178 -4.938  -12.937 0.54 31.46 ?  100 VAL   A HB   1 
ATOM   2090 H HG11 A VAL   A 1 100 ? 16.677 -3.532  -13.071 0.46 24.76 ?  100 VAL   A HG11 1 
ATOM   2091 H HG11 B VAL   A 1 100 ? 18.802 -5.745  -10.874 0.54 32.87 ?  100 VAL   A HG11 1 
ATOM   2092 H HG12 A VAL   A 1 100 ? 17.193 -2.118  -13.575 0.46 24.76 ?  100 VAL   A HG12 1 
ATOM   2093 H HG12 B VAL   A 1 100 ? 20.256 -5.113  -10.805 0.54 32.87 ?  100 VAL   A HG12 1 
ATOM   2094 H HG13 A VAL   A 1 100 ? 18.068 -3.420  -13.829 0.46 24.76 ?  100 VAL   A HG13 1 
ATOM   2095 H HG13 B VAL   A 1 100 ? 19.013 -4.326  -10.200 0.54 32.87 ?  100 VAL   A HG13 1 
ATOM   2096 H HG21 A VAL   A 1 100 ? 17.446 -4.517  -11.102 0.46 23.78 ?  100 VAL   A HG21 1 
ATOM   2097 H HG21 B VAL   A 1 100 ? 17.044 -4.359  -12.007 0.54 33.30 ?  100 VAL   A HG21 1 
ATOM   2098 H HG22 A VAL   A 1 100 ? 18.946 -4.642  -11.609 0.46 23.78 ?  100 VAL   A HG22 1 
ATOM   2099 H HG22 B VAL   A 1 100 ? 17.601 -2.880  -11.863 0.54 33.30 ?  100 VAL   A HG22 1 
ATOM   2100 H HG23 A VAL   A 1 100 ? 18.630 -3.903  -10.239 0.46 23.78 ?  100 VAL   A HG23 1 
ATOM   2101 H HG23 B VAL   A 1 100 ? 17.457 -3.542  -13.303 0.54 33.30 ?  100 VAL   A HG23 1 
ATOM   2102 N N    A ASN   A 1 101 ? 19.301 0.304   -12.231 0.46 20.79 ?  101 ASN   A N    1 
ATOM   2103 N N    B ASN   A 1 101 ? 19.314 -0.862  -12.849 0.54 26.20 ?  101 ASN   A N    1 
ATOM   2104 C CA   A ASN   A 1 101 ? 19.247 1.590   -12.916 0.46 22.39 ?  101 ASN   A CA   1 
ATOM   2105 C CA   B ASN   A 1 101 ? 19.017 0.285   -13.700 0.54 26.84 ?  101 ASN   A CA   1 
ATOM   2106 C C    A ASN   A 1 101 ? 20.602 2.042   -13.445 0.46 24.04 ?  101 ASN   A C    1 
ATOM   2107 C C    B ASN   A 1 101 ? 20.263 0.821   -14.396 0.54 28.30 ?  101 ASN   A C    1 
ATOM   2108 O O    A ASN   A 1 101 ? 20.669 3.106   -14.070 0.46 25.60 ?  101 ASN   A O    1 
ATOM   2109 O O    B ASN   A 1 101 ? 20.139 1.681   -15.278 0.54 29.30 ?  101 ASN   A O    1 
ATOM   2110 C CB   A ASN   A 1 101 ? 18.650 2.644   -11.986 0.46 21.76 ?  101 ASN   A CB   1 
ATOM   2111 C CB   B ASN   A 1 101 ? 18.340 1.398   -12.892 0.54 27.04 ?  101 ASN   A CB   1 
ATOM   2112 C CG   A ASN   A 1 101 ? 17.278 2.249   -11.472 0.46 21.55 ?  101 ASN   A CG   1 
ATOM   2113 C CG   B ASN   A 1 101 ? 16.958 1.003   -12.389 0.54 27.56 ?  101 ASN   A CG   1 
ATOM   2114 O OD1  A ASN   A 1 101 ? 16.423 1.781   -12.234 0.46 21.26 ?  101 ASN   A OD1  1 
ATOM   2115 O OD1  B ASN   A 1 101 ? 16.289 0.153   -12.974 0.54 28.61 ?  101 ASN   A OD1  1 
ATOM   2116 N ND2  A ASN   A 1 101 ? 17.066 2.414   -10.172 0.46 21.27 ?  101 ASN   A ND2  1 
ATOM   2117 N ND2  B ASN   A 1 101 ? 16.524 1.627   -11.301 0.54 27.40 ?  101 ASN   A ND2  1 
ATOM   2118 H H    A ASN   A 1 101 ? 19.195 0.352   -11.383 0.46 24.96 ?  101 ASN   A H    1 
ATOM   2119 H H    B ASN   A 1 101 ? 19.273 -0.708  -12.006 0.54 31.46 ?  101 ASN   A H    1 
ATOM   2120 H HA   A ASN   A 1 101 ? 18.654 1.504   -13.678 0.46 26.88 ?  101 ASN   A HA   1 
ATOM   2121 H HA   B ASN   A 1 101 ? 18.395 0.001   -14.388 0.54 32.22 ?  101 ASN   A HA   1 
ATOM   2122 H HB2  A ASN   A 1 101 ? 19.242 2.766   -11.227 0.46 26.12 ?  101 ASN   A HB2  1 
ATOM   2123 H HB2  B ASN   A 1 101 ? 18.892 1.612   -12.126 0.54 32.47 ?  101 ASN   A HB2  1 
ATOM   2124 H HB3  A ASN   A 1 101 ? 18.561 3.477   -12.475 0.46 26.12 ?  101 ASN   A HB3  1 
ATOM   2125 H HB3  B ASN   A 1 101 ? 18.240 2.179   -13.460 0.54 32.47 ?  101 ASN   A HB3  1 
ATOM   2126 H HD21 A ASN   A 1 101 ? 16.307 2.200   -9.832  0.46 25.54 ?  101 ASN   A HD21 1 
ATOM   2127 H HD21 B ASN   A 1 101 ? 15.750 1.438   -10.979 0.54 32.89 ?  101 ASN   A HD21 1 
ATOM   2128 H HD22 A ASN   A 1 101 ? 17.686 2.741   -9.672  0.46 25.54 ?  101 ASN   A HD22 1 
ATOM   2129 H HD22 B ASN   A 1 101 ? 17.016 2.221   -10.923 0.54 32.89 ?  101 ASN   A HD22 1 
ATOM   2130 N N    A LYS   A 1 102 ? 21.667 1.271   -13.214 0.46 24.93 ?  102 LYS   A N    1 
ATOM   2131 N N    B LYS   A 1 102 ? 21.447 0.332   -14.012 0.54 29.70 ?  102 LYS   A N    1 
ATOM   2132 C CA   A LYS   A 1 102 ? 22.954 1.477   -13.868 0.46 25.49 ?  102 LYS   A CA   1 
ATOM   2133 C CA   B LYS   A 1 102 ? 22.721 0.644   -14.648 0.54 30.59 ?  102 LYS   A CA   1 
ATOM   2134 C C    A LYS   A 1 102 ? 23.269 0.397   -14.892 0.46 26.96 ?  102 LYS   A C    1 
ATOM   2135 C C    B LYS   A 1 102 ? 23.231 -0.493  -15.531 0.54 29.10 ?  102 LYS   A C    1 
ATOM   2136 O O    A LYS   A 1 102 ? 24.341 0.441   -15.502 0.46 28.23 ?  102 LYS   A O    1 
ATOM   2137 O O    B LYS   A 1 102 ? 24.380 -0.449  -15.981 0.54 29.90 ?  102 LYS   A O    1 
ATOM   2138 C CB   A LYS   A 1 102 ? 24.087 1.520   -12.833 0.46 25.90 ?  102 LYS   A CB   1 
ATOM   2139 C CB   B LYS   A 1 102 ? 23.787 0.923   -13.587 0.54 33.92 ?  102 LYS   A CB   1 
ATOM   2140 C CG   A LYS   A 1 102 ? 23.977 2.626   -11.803 0.46 26.06 ?  102 LYS   A CG   1 
ATOM   2141 C CG   B LYS   A 1 102 ? 23.965 2.370   -13.178 0.54 36.48 ?  102 LYS   A CG   1 
ATOM   2142 C CD   A LYS   A 1 102 ? 25.142 2.549   -10.827 0.46 26.89 ?  102 LYS   A CD   1 
ATOM   2143 C CD   B LYS   A 1 102 ? 25.385 2.591   -12.653 0.54 38.56 ?  102 LYS   A CD   1 
ATOM   2144 C CE   A LYS   A 1 102 ? 25.109 3.670   -9.801  0.46 27.43 ?  102 LYS   A CE   1 
ATOM   2145 C CE   B LYS   A 1 102 ? 25.413 3.380   -11.352 0.54 40.01 ?  102 LYS   A CE   1 
ATOM   2146 N NZ   A LYS   A 1 102 ? 26.228 3.541   -8.815  0.46 27.44 ?  102 LYS   A NZ   1 
ATOM   2147 N NZ   B LYS   A 1 102 ? 25.645 2.493   -10.174 0.54 41.00 ?  102 LYS   A NZ   1 
ATOM   2148 H H    A LYS   A 1 102 ? 21.672 0.606   -12.669 0.46 29.93 ?  102 LYS   A H    1 
ATOM   2149 H H    B LYS   A 1 102 ? 21.540 -0.204  -13.349 0.54 35.66 ?  102 LYS   A H    1 
ATOM   2150 H HA   A LYS   A 1 102 ? 22.948 2.320   -14.337 0.46 30.61 ?  102 LYS   A HA   1 
ATOM   2151 H HA   B LYS   A 1 102 ? 22.619 1.448   -15.173 0.54 36.73 ?  102 LYS   A HA   1 
ATOM   2152 H HB2  A LYS   A 1 102 ? 24.104 0.676   -12.355 0.46 31.09 ?  102 LYS   A HB2  1 
ATOM   2153 H HB2  B LYS   A 1 102 ? 23.557 0.426   -12.790 0.54 40.72 ?  102 LYS   A HB2  1 
ATOM   2154 H HB3  A LYS   A 1 102 ? 24.930 1.641   -13.301 0.46 31.09 ?  102 LYS   A HB3  1 
ATOM   2155 H HB3  B LYS   A 1 102 ? 24.642 0.612   -13.924 0.54 40.72 ?  102 LYS   A HB3  1 
ATOM   2156 H HG2  A LYS   A 1 102 ? 24.002 3.487   -12.248 0.46 31.29 ?  102 LYS   A HG2  1 
ATOM   2157 H HG2  B LYS   A 1 102 ? 23.833 2.946   -13.946 0.54 43.79 ?  102 LYS   A HG2  1 
ATOM   2158 H HG3  A LYS   A 1 102 ? 23.149 2.523   -11.307 0.46 31.29 ?  102 LYS   A HG3  1 
ATOM   2159 H HG3  B LYS   A 1 102 ? 23.331 2.591   -12.479 0.54 43.79 ?  102 LYS   A HG3  1 
ATOM   2160 H HD2  A LYS   A 1 102 ? 25.103 1.704   -10.351 0.46 32.29 ?  102 LYS   A HD2  1 
ATOM   2161 H HD2  B LYS   A 1 102 ? 25.804 1.730   -12.487 0.54 46.29 ?  102 LYS   A HD2  1 
ATOM   2162 H HD3  A LYS   A 1 102 ? 25.975 2.615   -11.320 0.46 32.29 ?  102 LYS   A HD3  1 
ATOM   2163 H HD3  B LYS   A 1 102 ? 25.894 3.083   -13.316 0.54 46.29 ?  102 LYS   A HD3  1 
ATOM   2164 H HE2  A LYS   A 1 102 ? 25.199 4.522   -10.256 0.46 32.92 ?  102 LYS   A HE2  1 
ATOM   2165 H HE2  B LYS   A 1 102 ? 26.137 4.023   -11.390 0.54 48.02 ?  102 LYS   A HE2  1 
ATOM   2166 H HE3  A LYS   A 1 102 ? 24.269 3.636   -9.316  0.46 32.92 ?  102 LYS   A HE3  1 
ATOM   2167 H HE3  B LYS   A 1 102 ? 24.567 3.836   -11.229 0.54 48.02 ?  102 LYS   A HE3  1 
ATOM   2168 H HZ1  A LYS   A 1 102 ? 26.191 4.205   -8.225  0.46 32.94 ?  102 LYS   A HZ1  1 
ATOM   2169 H HZ1  B LYS   A 1 102 ? 25.384 2.904   -9.428  0.54 49.21 ?  102 LYS   A HZ1  1 
ATOM   2170 H HZ2  A LYS   A 1 102 ? 26.164 2.765   -8.384  0.46 32.94 ?  102 LYS   A HZ2  1 
ATOM   2171 H HZ2  B LYS   A 1 102 ? 25.182 1.738   -10.264 0.54 49.21 ?  102 LYS   A HZ2  1 
ATOM   2172 H HZ3  A LYS   A 1 102 ? 27.010 3.572   -9.239  0.46 32.94 ?  102 LYS   A HZ3  1 
ATOM   2173 H HZ3  B LYS   A 1 102 ? 26.509 2.293   -10.109 0.54 49.21 ?  102 LYS   A HZ3  1 
ATOM   2174 N N    A GLY   A 1 103 ? 22.376 -0.571  -15.091 0.46 27.42 ?  103 GLY   A N    1 
ATOM   2175 N N    B GLY   A 1 103 ? 22.430 -1.532  -15.748 0.54 27.29 ?  103 GLY   A N    1 
ATOM   2176 C CA   A GLY   A 1 103 ? 22.636 -1.666  -16.004 0.46 28.17 ?  103 GLY   A CA   1 
ATOM   2177 C CA   B GLY   A 1 103 ? 22.854 -2.662  -16.549 0.54 26.28 ?  103 GLY   A CA   1 
ATOM   2178 C C    A GLY   A 1 103 ? 23.483 -2.779  -15.435 0.46 28.55 ?  103 GLY   A C    1 
ATOM   2179 C C    B GLY   A 1 103 ? 23.671 -3.710  -15.821 0.54 24.51 ?  103 GLY   A C    1 
ATOM   2180 O O    A GLY   A 1 103 ? 24.051 -3.562  -16.203 0.46 29.65 ?  103 GLY   A O    1 
ATOM   2181 O O    B GLY   A 1 103 ? 24.116 -4.672  -16.458 0.54 24.89 ?  103 GLY   A O    1 
ATOM   2182 H H    A GLY   A 1 103 ? 21.611 -0.615  -14.707 0.46 32.92 ?  103 GLY   A H    1 
ATOM   2183 H H    B GLY   A 1 103 ? 21.634 -1.597  -15.440 0.54 32.77 ?  103 GLY   A H    1 
ATOM   2184 H HA2  A GLY   A 1 103 ? 21.789 -2.043  -16.299 0.46 33.82 ?  103 GLY   A HA2  1 
ATOM   2185 H HA2  B GLY   A 1 103 ? 22.069 -3.098  -16.913 0.54 31.55 ?  103 GLY   A HA2  1 
ATOM   2186 H HA3  A GLY   A 1 103 ? 23.099 -1.329  -16.784 0.46 33.82 ?  103 GLY   A HA3  1 
ATOM   2187 H HA3  B GLY   A 1 103 ? 23.384 -2.335  -17.294 0.54 31.55 ?  103 GLY   A HA3  1 
ATOM   2188 N N    A GLU   A 1 104 ? 23.589 -2.879  -14.113 0.46 26.94 ?  104 GLU   A N    1 
ATOM   2189 N N    B GLU   A 1 104 ? 23.883 -3.565  -14.518 0.54 22.36 ?  104 GLU   A N    1 
ATOM   2190 C CA   A GLU   A 1 104 ? 24.442 -3.877  -13.487 0.46 25.37 ?  104 GLU   A CA   1 
ATOM   2191 C CA   B GLU   A 1 104 ? 24.718 -4.513  -13.795 0.54 20.40 ?  104 GLU   A CA   1 
ATOM   2192 C C    A GLU   A 1 104 ? 23.735 -5.227  -13.387 0.46 25.46 ?  104 GLU   A C    1 
ATOM   2193 C C    B GLU   A 1 104 ? 23.986 -5.841  -13.616 0.54 19.80 ?  104 GLU   A C    1 
ATOM   2194 O O    A GLU   A 1 104 ? 22.517 -5.308  -13.195 0.46 25.76 ?  104 GLU   A O    1 
ATOM   2195 O O    B GLU   A 1 104 ? 22.756 -5.895  -13.525 0.54 21.18 ?  104 GLU   A O    1 
ATOM   2196 C CB   A GLU   A 1 104 ? 24.917 -3.379  -12.118 0.46 23.65 ?  104 GLU   A CB   1 
ATOM   2197 C CB   B GLU   A 1 104 ? 25.168 -3.916  -12.457 0.54 19.77 ?  104 GLU   A CB   1 
ATOM   2198 C CG   A GLU   A 1 104 ? 25.909 -2.215  -12.258 0.46 22.99 ?  104 GLU   A CG   1 
ATOM   2199 C CG   B GLU   A 1 104 ? 25.977 -2.634  -12.669 0.54 20.57 ?  104 GLU   A CG   1 
ATOM   2200 C CD   A GLU   A 1 104 ? 26.160 -1.427  -10.974 0.46 21.95 ?  104 GLU   A CD   1 
ATOM   2201 C CD   B GLU   A 1 104 ? 26.459 -1.946  -11.400 0.54 20.48 ?  104 GLU   A CD   1 
ATOM   2202 O OE1  A GLU   A 1 104 ? 25.550 -1.744  -9.931  0.46 21.14 ?  104 GLU   A OE1  1 
ATOM   2203 O OE1  B GLU   A 1 104 ? 25.967 -2.251  -10.294 0.54 20.17 ?  104 GLU   A OE1  1 
ATOM   2204 O OE2  A GLU   A 1 104 ? 26.975 -0.471  -11.022 0.46 21.86 -1 104 GLU   A OE2  1 
ATOM   2205 O OE2  B GLU   A 1 104 ? 27.339 -1.060  -11.530 0.54 21.36 -1 104 GLU   A OE2  1 
ATOM   2206 H H    A GLU   A 1 104 ? 23.177 -2.375  -13.555 0.46 32.35 ?  104 GLU   A H    1 
ATOM   2207 H H    B GLU   A 1 104 ? 23.552 -2.941  -14.035 0.54 26.85 ?  104 GLU   A H    1 
ATOM   2208 H HA   A GLU   A 1 104 ? 25.222 -4.007  -14.040 0.46 30.46 ?  104 GLU   A HA   1 
ATOM   2209 H HA   B GLU   A 1 104 ? 25.511 -4.693  -14.319 0.54 24.49 ?  104 GLU   A HA   1 
ATOM   2210 H HB2  A GLU   A 1 104 ? 24.150 -3.072  -11.608 0.46 28.40 ?  104 GLU   A HB2  1 
ATOM   2211 H HB2  B GLU   A 1 104 ? 24.389 -3.705  -11.923 0.54 23.73 ?  104 GLU   A HB2  1 
ATOM   2212 H HB3  A GLU   A 1 104 ? 25.358 -4.107  -11.649 0.46 28.40 ?  104 GLU   A HB3  1 
ATOM   2213 H HB3  B GLU   A 1 104 ? 25.729 -4.561  -11.995 0.54 23.73 ?  104 GLU   A HB3  1 
ATOM   2214 H HG2  A GLU   A 1 104 ? 26.756 -2.573  -12.568 0.46 27.61 ?  104 GLU   A HG2  1 
ATOM   2215 H HG2  B GLU   A 1 104 ? 26.752 -2.848  -13.211 0.54 24.69 ?  104 GLU   A HG2  1 
ATOM   2216 H HG3  A GLU   A 1 104 ? 25.560 -1.595  -12.919 0.46 27.61 ?  104 GLU   A HG3  1 
ATOM   2217 H HG3  B GLU   A 1 104 ? 25.418 -1.994  -13.132 0.54 24.69 ?  104 GLU   A HG3  1 
ATOM   2218 N N    A ASP   A 1 105 ? 24.526 -6.292  -13.531 0.46 26.21 ?  105 ASP   A N    1 
ATOM   2219 N N    B ASP   A 1 105 ? 24.773 -6.920  -13.582 0.54 20.59 ?  105 ASP   A N    1 
ATOM   2220 C CA   A ASP   A 1 105 ? 24.007 -7.651  -13.642 0.46 26.88 ?  105 ASP   A CA   1 
ATOM   2221 C CA   B ASP   A 1 105 ? 24.262 -8.288  -13.643 0.54 22.05 ?  105 ASP   A CA   1 
ATOM   2222 C C    A ASP   A 1 105 ? 23.312 -8.064  -12.347 0.46 24.89 ?  105 ASP   A C    1 
ATOM   2223 C C    B ASP   A 1 105 ? 23.488 -8.642  -12.376 0.54 20.81 ?  105 ASP   A C    1 
ATOM   2224 O O    A ASP   A 1 105 ? 23.939 -8.106  -11.285 0.46 24.33 ?  105 ASP   A O    1 
ATOM   2225 O O    B ASP   A 1 105 ? 24.040 -8.608  -11.272 0.54 19.11 ?  105 ASP   A O    1 
ATOM   2226 C CB   A ASP   A 1 105 ? 25.169 -8.595  -13.946 0.46 29.30 ?  105 ASP   A CB   1 
ATOM   2227 C CB   B ASP   A 1 105 ? 25.457 -9.224  -13.815 0.54 24.05 ?  105 ASP   A CB   1 
ATOM   2228 C CG   A ASP   A 1 105 ? 24.708 -9.992  -14.282 0.46 31.68 ?  105 ASP   A CG   1 
ATOM   2229 C CG   B ASP   A 1 105 ? 25.063 -10.680 -13.927 0.54 25.96 ?  105 ASP   A CG   1 
ATOM   2230 O OD1  A ASP   A 1 105 ? 23.479 -10.214 -14.340 0.46 32.05 ?  105 ASP   A OD1  1 
ATOM   2231 O OD1  B ASP   A 1 105 ? 23.853 -10.982 -14.017 0.54 25.63 ?  105 ASP   A OD1  1 
ATOM   2232 O OD2  A ASP   A 1 105 ? 25.575 -10.866 -14.496 0.46 33.23 -1 105 ASP   A OD2  1 
ATOM   2233 O OD2  B ASP   A 1 105 ? 25.988 -11.526 -13.920 0.54 27.64 -1 105 ASP   A OD2  1 
ATOM   2234 H H    A ASP   A 1 105 ? 25.386 -6.260  -13.568 0.46 31.47 ?  105 ASP   A H    1 
ATOM   2235 H H    B ASP   A 1 105 ? 25.634 -6.883  -13.534 0.54 24.73 ?  105 ASP   A H    1 
ATOM   2236 H HA   A ASP   A 1 105 ? 23.372 -7.718  -14.372 0.46 32.27 ?  105 ASP   A HA   1 
ATOM   2237 H HA   B ASP   A 1 105 ? 23.675 -8.389  -14.408 0.54 26.48 ?  105 ASP   A HA   1 
ATOM   2238 H HB2  A ASP   A 1 105 ? 25.663 -8.267  -14.717 0.46 35.17 ?  105 ASP   A HB2  1 
ATOM   2239 H HB2  B ASP   A 1 105 ? 25.944 -8.972  -14.618 0.54 28.88 ?  105 ASP   A HB2  1 
ATOM   2240 H HB3  A ASP   A 1 105 ? 25.766 -8.635  -13.175 0.46 35.17 ?  105 ASP   A HB3  1 
ATOM   2241 H HB3  B ASP   A 1 105 ? 26.037 -9.145  -13.042 0.54 28.88 ?  105 ASP   A HB3  1 
ATOM   2242 N N    A ILE   A 1 106 ? 22.018 -8.390  -12.439 0.46 23.99 ?  106 ILE   A N    1 
ATOM   2243 N N    B ILE   A 1 106 ? 22.219 -9.028  -12.541 0.54 22.06 ?  106 ILE   A N    1 
ATOM   2244 C CA   A ILE   A 1 106 ? 21.254 -8.810  -11.268 0.46 22.80 ?  106 ILE   A CA   1 
ATOM   2245 C CA   B ILE   A 1 106 ? 21.383 -9.395  -11.400 0.54 23.40 ?  106 ILE   A CA   1 
ATOM   2246 C C    A ILE   A 1 106 ? 21.773 -10.120 -10.689 0.46 22.06 ?  106 ILE   A C    1 
ATOM   2247 C C    B ILE   A 1 106 ? 21.978 -10.577 -10.648 0.54 22.88 ?  106 ILE   A C    1 
ATOM   2248 O O    A ILE   A 1 106 ? 21.538 -10.409 -9.512  0.46 21.74 ?  106 ILE   A O    1 
ATOM   2249 O O    B ILE   A 1 106 ? 21.818 -10.688 -9.426  0.54 22.61 ?  106 ILE   A O    1 
ATOM   2250 C CB   A ILE   A 1 106 ? 19.744 -8.887  -11.595 0.46 23.43 ?  106 ILE   A CB   1 
ATOM   2251 C CB   B ILE   A 1 106 ? 19.936 -9.670  -11.863 0.54 25.09 ?  106 ILE   A CB   1 
ATOM   2252 C CG1  A ILE   A 1 106 ? 18.919 -8.989  -10.310 0.46 24.28 ?  106 ILE   A CG1  1 
ATOM   2253 C CG1  B ILE   A 1 106 ? 18.989 -9.793  -10.667 0.54 25.79 ?  106 ILE   A CG1  1 
ATOM   2254 C CG2  A ILE   A 1 106 ? 19.447 -10.078 -12.500 0.46 23.92 ?  106 ILE   A CG2  1 
ATOM   2255 C CG2  B ILE   A 1 106 ? 19.866 -10.945 -12.682 0.54 25.92 ?  106 ILE   A CG2  1 
ATOM   2256 C CD1  A ILE   A 1 106 ? 19.127 -7.829  -9.358  0.46 24.92 ?  106 ILE   A CD1  1 
ATOM   2257 C CD1  B ILE   A 1 106 ? 18.725 -8.493  -9.961  0.54 26.20 ?  106 ILE   A CD1  1 
ATOM   2258 H H    A ILE   A 1 106 ? 21.567 -8.368  -13.166 0.46 28.80 ?  106 ILE   A H    1 
ATOM   2259 H H    B ILE   A 1 106 ? 21.827 -9.084  -13.300 0.54 26.48 ?  106 ILE   A H    1 
ATOM   2260 H HA   A ILE   A 1 106 ? 21.373 -8.138  -10.588 0.46 27.37 ?  106 ILE   A HA   1 
ATOM   2261 H HA   B ILE   A 1 106 ? 21.360 -8.650  -10.785 0.54 28.09 ?  106 ILE   A HA   1 
ATOM   2262 H HB   A ILE   A 1 106 ? 19.488 -8.078  -12.062 0.46 28.13 ?  106 ILE   A HB   1 
ATOM   2263 H HB   B ILE   A 1 106 ? 19.642 -8.930  -12.419 0.54 30.13 ?  106 ILE   A HB   1 
ATOM   2264 H HG12 A ILE   A 1 106 ? 17.976 -9.012  -10.544 0.46 29.15 ?  106 ILE   A HG12 1 
ATOM   2265 H HG12 B ILE   A 1 106 ? 18.138 -10.137 -10.981 0.54 30.96 ?  106 ILE   A HG12 1 
ATOM   2266 H HG13 A ILE   A 1 106 ? 19.158 -9.805  -9.843  0.46 29.15 ?  106 ILE   A HG13 1 
ATOM   2267 H HG13 B ILE   A 1 106 ? 19.372 -10.408 -10.024 0.54 30.96 ?  106 ILE   A HG13 1 
ATOM   2268 H HG21 A ILE   A 1 106 ? 18.550 -9.988  -12.856 0.46 28.72 ?  106 ILE   A HG21 1 
ATOM   2269 H HG21 B ILE   A 1 106 ? 19.005 -10.988 -13.125 0.54 31.12 ?  106 ILE   A HG21 1 
ATOM   2270 H HG22 A ILE   A 1 106 ? 20.092 -10.089 -13.226 0.46 28.72 ?  106 ILE   A HG22 1 
ATOM   2271 H HG22 B ILE   A 1 106 ? 20.577 -10.936 -13.340 0.54 31.12 ?  106 ILE   A HG22 1 
ATOM   2272 H HG23 A ILE   A 1 106 ? 19.519 -10.896 -11.983 0.46 28.72 ?  106 ILE   A HG23 1 
ATOM   2273 H HG23 B ILE   A 1 106 ? 19.972 -11.707 -12.090 0.54 31.12 ?  106 ILE   A HG23 1 
ATOM   2274 H HD11 A ILE   A 1 106 ? 18.386 -7.795  -8.736  0.46 29.91 ?  106 ILE   A HD11 1 
ATOM   2275 H HD11 B ILE   A 1 106 ? 18.126 -8.659  -9.218  0.54 31.45 ?  106 ILE   A HD11 1 
ATOM   2276 H HD12 A ILE   A 1 106 ? 19.959 -7.961  -8.875  0.46 29.91 ?  106 ILE   A HD12 1 
ATOM   2277 H HD12 B ILE   A 1 106 ? 19.562 -8.129  -9.639  0.54 31.45 ?  106 ILE   A HD12 1 
ATOM   2278 H HD13 A ILE   A 1 106 ? 19.168 -7.005  -9.870  0.46 29.91 ?  106 ILE   A HD13 1 
ATOM   2279 H HD13 B ILE   A 1 106 ? 18.312 -7.879  -10.588 0.54 31.45 ?  106 ILE   A HD13 1 
ATOM   2280 N N    A GLN   A 1 107 ? 22.478 -10.924 -11.494 0.46 22.90 ?  107 GLN   A N    1 
ATOM   2281 N N    B GLN   A 1 107 ? 22.684 -11.468 -11.352 0.54 23.10 ?  107 GLN   A N    1 
ATOM   2282 C CA   A GLN   A 1 107 ? 23.081 -12.154 -10.989 0.46 24.83 ?  107 GLN   A CA   1 
ATOM   2283 C CA   B GLN   A 1 107 ? 23.321 -12.602 -10.692 0.54 25.39 ?  107 GLN   A CA   1 
ATOM   2284 C C    A GLN   A 1 107 ? 24.056 -11.887 -9.850  0.46 22.91 ?  107 GLN   A C    1 
ATOM   2285 C C    B GLN   A 1 107 ? 24.290 -12.155 -9.608  0.54 23.20 ?  107 GLN   A C    1 
ATOM   2286 O O    A GLN   A 1 107 ? 24.276 -12.764 -9.008  0.46 24.55 ?  107 GLN   A O    1 
ATOM   2287 O O    B GLN   A 1 107 ? 24.564 -12.920 -8.676  0.54 23.79 ?  107 GLN   A O    1 
ATOM   2288 C CB   A GLN   A 1 107 ? 23.792 -12.896 -12.126 0.46 28.84 ?  107 GLN   A CB   1 
ATOM   2289 C CB   B GLN   A 1 107 ? 24.043 -13.469 -11.726 0.54 29.61 ?  107 GLN   A CB   1 
ATOM   2290 C CG   A GLN   A 1 107 ? 22.906 -13.203 -13.322 0.46 33.20 ?  107 GLN   A CG   1 
ATOM   2291 C CG   B GLN   A 1 107 ? 23.118 -14.098 -12.757 0.54 33.94 ?  107 GLN   A CG   1 
ATOM   2292 C CD   A GLN   A 1 107 ? 21.660 -13.977 -12.940 0.46 36.63 ?  107 GLN   A CD   1 
ATOM   2293 C CD   B GLN   A 1 107 ? 22.164 -15.107 -12.145 0.54 37.82 ?  107 GLN   A CD   1 
ATOM   2294 O OE1  A GLN   A 1 107 ? 21.736 -15.029 -12.306 0.46 38.36 ?  107 GLN   A OE1  1 
ATOM   2295 O OE1  B GLN   A 1 107 ? 22.566 -15.952 -11.343 0.54 38.97 ?  107 GLN   A OE1  1 
ATOM   2296 N NE2  A GLN   A 1 107 ? 20.502 -13.452 -13.318 0.46 37.68 ?  107 GLN   A NE2  1 
ATOM   2297 N NE2  B GLN   A 1 107 ? 20.891 -15.019 -12.518 0.54 38.92 ?  107 GLN   A NE2  1 
ATOM   2298 H H    A GLN   A 1 107 ? 22.618 -10.781 -12.322 0.46 27.50 ?  107 GLN   A H    1 
ATOM   2299 H H    B GLN   A 1 107 ? 22.812 -11.432 -12.200 0.54 27.73 ?  107 GLN   A H    1 
ATOM   2300 H HA   A GLN   A 1 107 ? 22.390 -12.736 -10.642 0.46 29.81 ?  107 GLN   A HA   1 
ATOM   2301 H HA   B GLN   A 1 107 ? 22.637 -13.148 -10.277 0.54 30.48 ?  107 GLN   A HA   1 
ATOM   2302 H HB2  A GLN   A 1 107 ? 24.533 -12.353 -12.441 0.46 34.62 ?  107 GLN   A HB2  1 
ATOM   2303 H HB2  B GLN   A 1 107 ? 24.685 -12.920 -12.202 0.54 35.55 ?  107 GLN   A HB2  1 
ATOM   2304 H HB3  A GLN   A 1 107 ? 24.131 -13.741 -11.788 0.46 34.62 ?  107 GLN   A HB3  1 
ATOM   2305 H HB3  B GLN   A 1 107 ? 24.504 -14.188 -11.266 0.54 35.55 ?  107 GLN   A HB3  1 
ATOM   2306 H HG2  A GLN   A 1 107 ? 22.628 -12.372 -13.734 0.46 39.86 ?  107 GLN   A HG2  1 
ATOM   2307 H HG2  B GLN   A 1 107 ? 22.590 -13.400 -13.177 0.54 40.75 ?  107 GLN   A HG2  1 
ATOM   2308 H HG3  A GLN   A 1 107 ? 23.409 -13.737 -13.960 0.46 39.86 ?  107 GLN   A HG3  1 
ATOM   2309 H HG3  B GLN   A 1 107 ? 23.653 -14.556 -13.425 0.54 40.75 ?  107 GLN   A HG3  1 
ATOM   2310 H HE21 A GLN   A 1 107 ? 20.488 -12.714 -13.758 0.46 45.23 ?  107 GLN   A HE21 1 
ATOM   2311 H HE21 B GLN   A 1 107 ? 20.648 -14.413 -13.078 0.54 46.72 ?  107 GLN   A HE21 1 
ATOM   2312 H HE22 A GLN   A 1 107 ? 19.767 -13.854 -13.125 0.46 45.23 ?  107 GLN   A HE22 1 
ATOM   2313 H HE22 B GLN   A 1 107 ? 20.311 -15.568 -12.200 0.54 46.72 ?  107 GLN   A HE22 1 
ATOM   2314 N N    A LEU   A 1 108 ? 24.642 -10.687 -9.795  0.46 19.24 ?  108 LEU   A N    1 
ATOM   2315 N N    B LEU   A 1 108 ? 24.795 -10.924 -9.692  0.54 20.55 ?  108 LEU   A N    1 
ATOM   2316 C CA   A LEU   A 1 108 ? 25.597 -10.363 -8.740  0.46 17.25 ?  108 LEU   A CA   1 
ATOM   2317 C CA   B LEU   A 1 108 ? 25.669 -10.407 -8.653  0.54 18.62 ?  108 LEU   A CA   1 
ATOM   2318 C C    A LEU   A 1 108 ? 24.935 -10.214 -7.378  0.46 16.23 ?  108 LEU   A C    1 
ATOM   2319 C C    B LEU   A 1 108 ? 24.939 -10.176 -7.339  0.54 17.09 ?  108 LEU   A C    1 
ATOM   2320 O O    A LEU   A 1 108 ? 25.640 -10.098 -6.374  0.46 15.62 ?  108 LEU   A O    1 
ATOM   2321 O O    B LEU   A 1 108 ? 25.600 -9.950  -6.323  0.54 17.30 ?  108 LEU   A O    1 
ATOM   2322 C CB   A LEU   A 1 108 ? 26.378 -9.093  -9.099  0.46 17.22 ?  108 LEU   A CB   1 
ATOM   2323 C CB   B LEU   A 1 108 ? 26.366 -9.124  -9.119  0.54 18.81 ?  108 LEU   A CB   1 
ATOM   2324 C CG   A LEU   A 1 108 ? 27.368 -9.252  -10.256 0.46 18.98 ?  108 LEU   A CG   1 
ATOM   2325 C CG   B LEU   A 1 108 ? 27.389 -9.330  -10.241 0.54 20.67 ?  108 LEU   A CG   1 
ATOM   2326 C CD1  A LEU   A 1 108 ? 27.756 -7.897  -10.838 0.46 19.85 ?  108 LEU   A CD1  1 
ATOM   2327 C CD1  B LEU   A 1 108 ? 27.901 -7.996  -10.777 0.54 21.25 ?  108 LEU   A CD1  1 
ATOM   2328 C CD2  A LEU   A 1 108 ? 28.606 -10.012 -9.802  0.46 20.95 ?  108 LEU   A CD2  1 
ATOM   2329 C CD2  B LEU   A 1 108 ? 28.548 -10.196 -9.766  0.54 22.74 ?  108 LEU   A CD2  1 
ATOM   2330 H H    A LEU   A 1 108 ? 24.495 -10.049 -10.346 0.46 23.10 ?  108 LEU   A H    1 
ATOM   2331 H H    B LEU   A 1 108 ? 24.644 -10.380 -10.334 0.54 24.68 ?  108 LEU   A H    1 
ATOM   2332 H HA   A LEU   A 1 108 ? 26.235 -11.088 -8.667  0.46 20.72 ?  108 LEU   A HA   1 
ATOM   2333 H HA   B LEU   A 1 108 ? 26.355 -11.068 -8.481  0.54 22.36 ?  108 LEU   A HA   1 
ATOM   2334 H HB2  A LEU   A 1 108 ? 25.746 -8.402  -9.349  0.46 20.68 ?  108 LEU   A HB2  1 
ATOM   2335 H HB2  B LEU   A 1 108 ? 25.693 -8.505  -9.442  0.54 22.59 ?  108 LEU   A HB2  1 
ATOM   2336 H HB3  A LEU   A 1 108 ? 26.880 -8.809  -8.320  0.46 20.68 ?  108 LEU   A HB3  1 
ATOM   2337 H HB3  B LEU   A 1 108 ? 26.832 -8.734  -8.363  0.54 22.59 ?  108 LEU   A HB3  1 
ATOM   2338 H HG   A LEU   A 1 108 ? 26.948 -9.768  -10.960 0.46 22.79 ?  108 LEU   A HG   1 
ATOM   2339 H HG   B LEU   A 1 108 ? 26.956 -9.795  -10.973 0.54 24.82 ?  108 LEU   A HG   1 
ATOM   2340 H HD11 A LEU   A 1 108 ? 28.350 -8.035  -11.593 0.46 23.83 ?  108 LEU   A HD11 1 
ATOM   2341 H HD11 B LEU   A 1 108 ? 28.532 -8.164  -11.493 0.54 25.52 ?  108 LEU   A HD11 1 
ATOM   2342 H HD12 A LEU   A 1 108 ? 26.954 -7.437  -11.128 0.46 23.83 ?  108 LEU   A HD12 1 
ATOM   2343 H HD12 B LEU   A 1 108 ? 27.149 -7.482  -11.113 0.54 25.52 ?  108 LEU   A HD12 1 
ATOM   2344 H HD13 A LEU   A 1 108 ? 28.207 -7.376  -10.154 0.46 23.83 ?  108 LEU   A HD13 1 
ATOM   2345 H HD13 B LEU   A 1 108 ? 28.336 -7.512  -10.058 0.54 25.52 ?  108 LEU   A HD13 1 
ATOM   2346 H HD21 A LEU   A 1 108 ? 29.235 -10.060 -10.540 0.46 25.16 ?  108 LEU   A HD21 1 
ATOM   2347 H HD21 B LEU   A 1 108 ? 29.266 -10.145 -10.415 0.54 27.30 ?  108 LEU   A HD21 1 
ATOM   2348 H HD22 A LEU   A 1 108 ? 29.009 -9.544  -9.054  0.46 25.16 ?  108 LEU   A HD22 1 
ATOM   2349 H HD22 B LEU   A 1 108 ? 28.855 -9.867  -8.906  0.54 27.30 ?  108 LEU   A HD22 1 
ATOM   2350 H HD23 A LEU   A 1 108 ? 28.347 -10.907 -9.530  0.46 25.16 ?  108 LEU   A HD23 1 
ATOM   2351 H HD23 B LEU   A 1 108 ? 28.245 -11.113 -9.679  0.54 27.30 ?  108 LEU   A HD23 1 
ATOM   2352 N N    . LEU   A 1 109 ? 23.603 -10.239 -7.319  1.00 15.88 ?  109 LEU   A N    1 
ATOM   2353 C CA   . LEU   A 1 109 ? 22.905 -10.093 -6.049  1.00 15.27 ?  109 LEU   A CA   1 
ATOM   2354 C C    . LEU   A 1 109 ? 23.239 -11.243 -5.108  1.00 14.61 ?  109 LEU   A C    1 
ATOM   2355 O O    . LEU   A 1 109 ? 23.378 -11.047 -3.898  1.00 14.63 ?  109 LEU   A O    1 
ATOM   2356 C CB   . LEU   A 1 109 ? 21.401 -9.991  -6.305  1.00 16.77 ?  109 LEU   A CB   1 
ATOM   2357 C CG   . LEU   A 1 109 ? 20.518 -9.662  -5.104  1.00 17.30 ?  109 LEU   A CG   1 
ATOM   2358 C CD1  . LEU   A 1 109 ? 20.942 -8.364  -4.440  1.00 16.81 ?  109 LEU   A CD1  1 
ATOM   2359 C CD2  . LEU   A 1 109 ? 19.056 -9.580  -5.538  1.00 18.35 ?  109 LEU   A CD2  1 
ATOM   2360 H H    A LEU   A 1 109 ? 23.082 -10.340 -7.998  0.46 19.07 ?  109 LEU   A H    1 
ATOM   2361 H H    B LEU   A 1 109 ? 23.095 -10.352 -8.006  0.54 19.07 ?  109 LEU   A H    1 
ATOM   2362 H HA   . LEU   A 1 109 ? 23.197 -9.268  -5.629  1.00 18.34 ?  109 LEU   A HA   1 
ATOM   2363 H HB2  . LEU   A 1 109 ? 21.252 -9.290  -6.961  1.00 20.14 ?  109 LEU   A HB2  1 
ATOM   2364 H HB3  . LEU   A 1 109 ? 21.094 -10.834 -6.661  1.00 20.14 ?  109 LEU   A HB3  1 
ATOM   2365 H HG   . LEU   A 1 109 ? 20.594 -10.372 -4.445  1.00 20.78 ?  109 LEU   A HG   1 
ATOM   2366 H HD11 . LEU   A 1 109 ? 20.263 -8.096  -3.799  1.00 20.19 ?  109 LEU   A HD11 1 
ATOM   2367 H HD12 . LEU   A 1 109 ? 21.789 -8.493  -3.995  1.00 20.19 ?  109 LEU   A HD12 1 
ATOM   2368 H HD13 . LEU   A 1 109 ? 21.028 -7.676  -5.126  1.00 20.19 ?  109 LEU   A HD13 1 
ATOM   2369 H HD21 . LEU   A 1 109 ? 18.525 -9.193  -4.819  1.00 22.04 ?  109 LEU   A HD21 1 
ATOM   2370 H HD22 . LEU   A 1 109 ? 18.985 -9.025  -6.330  1.00 22.04 ?  109 LEU   A HD22 1 
ATOM   2371 H HD23 . LEU   A 1 109 ? 18.727 -10.476 -5.737  1.00 22.04 ?  109 LEU   A HD23 1 
ATOM   2372 N N    . LYS   A 1 110 ? 23.392 -12.450 -5.647  1.00 14.67 ?  110 LYS   A N    1 
ATOM   2373 C CA   . LYS   A 1 110 ? 23.753 -13.568 -4.782  1.00 14.31 ?  110 LYS   A CA   1 
ATOM   2374 C C    . LYS   A 1 110 ? 25.138 -13.364 -4.181  1.00 14.03 ?  110 LYS   A C    1 
ATOM   2375 O O    . LYS   A 1 110 ? 25.339 -13.578 -2.979  1.00 14.41 ?  110 LYS   A O    1 
ATOM   2376 C CB   . LYS   A 1 110 ? 23.646 -14.893 -5.538  1.00 16.04 ?  110 LYS   A CB   1 
ATOM   2377 C CG   . LYS   A 1 110 ? 23.858 -16.104 -4.633  1.00 16.86 ?  110 LYS   A CG   1 
ATOM   2378 C CD   . LYS   A 1 110 ? 23.567 -17.426 -5.335  1.00 17.17 ?  110 LYS   A CD   1 
ATOM   2379 C CE   . LYS   A 1 110 ? 23.722 -18.609 -4.392  1.00 17.60 ?  110 LYS   A CE   1 
ATOM   2380 N NZ   . LYS   A 1 110 ? 22.563 -18.758 -3.466  1.00 18.62 ?  110 LYS   A NZ   1 
ATOM   2381 H H    . LYS   A 1 110 ? 23.284 -12.648 -6.479  1.00 17.62 ?  110 LYS   A H    1 
ATOM   2382 H HA   . LYS   A 1 110 ? 23.121 -13.610 -4.049  1.00 17.19 ?  110 LYS   A HA   1 
ATOM   2383 H HB2  . LYS   A 1 110 ? 22.760 -14.966 -5.935  1.00 19.27 ?  110 LYS   A HB2  1 
ATOM   2384 H HB3  . LYS   A 1 110 ? 24.320 -14.919 -6.237  1.00 19.27 ?  110 LYS   A HB3  1 
ATOM   2385 H HG2  . LYS   A 1 110 ? 24.781 -16.125 -4.338  1.00 20.25 ?  110 LYS   A HG2  1 
ATOM   2386 H HG3  . LYS   A 1 110 ? 23.265 -16.038 -3.869  1.00 20.25 ?  110 LYS   A HG3  1 
ATOM   2387 H HD2  . LYS   A 1 110 ? 22.651 -17.417 -5.663  1.00 20.61 ?  110 LYS   A HD2  1 
ATOM   2388 H HD3  . LYS   A 1 110 ? 24.184 -17.536 -6.075  1.00 20.61 ?  110 LYS   A HD3  1 
ATOM   2389 H HE2  . LYS   A 1 110 ? 23.801 -19.424 -4.915  1.00 21.14 ?  110 LYS   A HE2  1 
ATOM   2390 H HE3  . LYS   A 1 110 ? 24.526 -18.483 -3.857  1.00 21.14 ?  110 LYS   A HE3  1 
ATOM   2391 H HZ1  . LYS   A 1 110 ? 22.688 -19.455 -2.929  1.00 22.36 ?  110 LYS   A HZ1  1 
ATOM   2392 H HZ2  . LYS   A 1 110 ? 22.476 -18.022 -2.970  1.00 22.36 ?  110 LYS   A HZ2  1 
ATOM   2393 H HZ3  . LYS   A 1 110 ? 21.816 -18.880 -3.933  1.00 22.36 ?  110 LYS   A HZ3  1 
ATOM   2394 N N    . SER   A 1 111 ? 26.097 -12.933 -4.999  1.00 14.63 ?  111 SER   A N    1 
ATOM   2395 C CA   . SER   A 1 111 ? 27.424 -12.616 -4.481  1.00 14.02 ?  111 SER   A CA   1 
ATOM   2396 C C    . SER   A 1 111 ? 27.363 -11.570 -3.375  1.00 13.95 ?  111 SER   A C    1 
ATOM   2397 O O    . SER   A 1 111 ? 28.042 -11.690 -2.353  1.00 14.40 ?  111 SER   A O    1 
ATOM   2398 C CB   . SER   A 1 111 ? 28.316 -12.131 -5.623  1.00 15.23 ?  111 SER   A CB   1 
ATOM   2399 O OG   . SER   A 1 111 ? 28.402 -13.136 -6.627  1.00 17.24 ?  111 SER   A OG   1 
ATOM   2400 H H    . SER   A 1 111 ? 26.005 -12.815 -5.852  1.00 17.57 ?  111 SER   A H    1 
ATOM   2401 H HA   . SER   A 1 111 ? 27.825 -13.421 -4.122  1.00 16.84 ?  111 SER   A HA   1 
ATOM   2402 H HB2  . SER   A 1 111 ? 27.932 -11.336 -6.023  1.00 18.29 ?  111 SER   A HB2  1 
ATOM   2403 H HB3  . SER   A 1 111 ? 29.205 -11.943 -5.287  1.00 18.29 ?  111 SER   A HB3  1 
ATOM   2404 H HG   . SER   A 1 111 ? 28.907 -12.873 -7.259  1.00 20.71 ?  111 SER   A HG   1 
ATOM   2405 N N    . ALA   A 1 112 ? 26.543 -10.538 -3.558  1.00 13.75 ?  112 ALA   A N    1 
ATOM   2406 C CA   . ALA   A 1 112 ? 26.402 -9.513  -2.526  1.00 14.05 ?  112 ALA   A CA   1 
ATOM   2407 C C    . ALA   A 1 112 ? 25.910 -10.117 -1.207  1.00 13.18 ?  112 ALA   A C    1 
ATOM   2408 O O    . ALA   A 1 112 ? 26.459 -9.824  -0.139  1.00 13.44 ?  112 ALA   A O    1 
ATOM   2409 C CB   . ALA   A 1 112 ? 25.457 -8.413  -3.018  1.00 14.76 ?  112 ALA   A CB   1 
ATOM   2410 H H    . ALA   A 1 112 ? 26.053 -10.411 -4.252  1.00 16.51 ?  112 ALA   A H    1 
ATOM   2411 H HA   . ALA   A 1 112 ? 27.270 -9.106  -2.363  1.00 16.88 ?  112 ALA   A HA   1 
ATOM   2412 H HB1  . ALA   A 1 112 ? 25.397 -7.716  -2.339  1.00 17.72 ?  112 ALA   A HB1  1 
ATOM   2413 H HB2  . ALA   A 1 112 ? 25.811 -8.033  -3.839  1.00 17.72 ?  112 ALA   A HB2  1 
ATOM   2414 H HB3  . ALA   A 1 112 ? 24.581 -8.792  -3.179  1.00 17.72 ?  112 ALA   A HB3  1 
ATOM   2415 N N    . TYR   A 1 113 ? 24.865 -10.953 -1.257  1.00 13.68 ?  113 TYR   A N    1 
ATOM   2416 C CA   . TYR   A 1 113 ? 24.346 -11.554 -0.027  1.00 13.22 ?  113 TYR   A CA   1 
ATOM   2417 C C    . TYR   A 1 113 ? 25.337 -12.519 0.626   1.00 13.00 ?  113 TYR   A C    1 
ATOM   2418 O O    . TYR   A 1 113 ? 25.298 -12.712 1.846   1.00 13.31 ?  113 TYR   A O    1 
ATOM   2419 C CB   . TYR   A 1 113 ? 23.021 -12.267 -0.299  1.00 14.52 ?  113 TYR   A CB   1 
ATOM   2420 C CG   . TYR   A 1 113 ? 21.806 -11.360 -0.240  1.00 13.63 ?  113 TYR   A CG   1 
ATOM   2421 C CD1  . TYR   A 1 113 ? 21.435 -10.754 0.954   1.00 14.78 ?  113 TYR   A CD1  1 
ATOM   2422 C CD2  . TYR   A 1 113 ? 21.030 -11.117 -1.365  1.00 14.76 ?  113 TYR   A CD2  1 
ATOM   2423 C CE1  . TYR   A 1 113 ? 20.328 -9.948  1.026   1.00 14.83 ?  113 TYR   A CE1  1 
ATOM   2424 C CE2  . TYR   A 1 113 ? 19.898 -10.308 -1.300  1.00 15.45 ?  113 TYR   A CE2  1 
ATOM   2425 C CZ   . TYR   A 1 113 ? 19.569 -9.720  -0.100  1.00 14.92 ?  113 TYR   A CZ   1 
ATOM   2426 O OH   . TYR   A 1 113 ? 18.454 -8.907  0.004   1.00 16.11 ?  113 TYR   A OH   1 
ATOM   2427 H H    . TYR   A 1 113 ? 24.455 -11.180 -1.976  1.00 16.43 ?  113 TYR   A H    1 
ATOM   2428 H HA   . TYR   A 1 113 ? 24.171 -10.848 0.611   1.00 15.87 ?  113 TYR   A HA   1 
ATOM   2429 H HB2  . TYR   A 1 113 ? 23.052 -12.658 -1.190  1.00 17.44 ?  113 TYR   A HB2  1 
ATOM   2430 H HB3  . TYR   A 1 113 ? 22.901 -12.971 0.358   1.00 17.44 ?  113 TYR   A HB3  1 
ATOM   2431 H HD1  . TYR   A 1 113 ? 21.949 -10.914 1.718   1.00 17.75 ?  113 TYR   A HD1  1 
ATOM   2432 H HD2  . TYR   A 1 113 ? 21.252 -11.524 -2.173  1.00 17.72 ?  113 TYR   A HD2  1 
ATOM   2433 H HE1  . TYR   A 1 113 ? 20.093 -9.550  1.835   1.00 17.80 ?  113 TYR   A HE1  1 
ATOM   2434 H HE2  . TYR   A 1 113 ? 19.383 -10.153 -2.059  1.00 18.56 ?  113 TYR   A HE2  1 
ATOM   2435 H HH   . TYR   A 1 113 ? 18.040 -8.895  -0.731  1.00 19.34 ?  113 TYR   A HH   1 
ATOM   2436 N N    . GLU   A 1 114 ? 26.227 -13.135 -0.157  1.00 12.90 ?  114 GLU   A N    1 
ATOM   2437 C CA   . GLU   A 1 114 ? 27.230 -14.018 0.443   1.00 13.05 ?  114 GLU   A CA   1 
ATOM   2438 C C    . GLU   A 1 114 ? 28.085 -13.305 1.490   1.00 12.94 ?  114 GLU   A C    1 
ATOM   2439 O O    . GLU   A 1 114 ? 28.558 -13.942 2.445   1.00 13.63 ?  114 GLU   A O    1 
ATOM   2440 C CB   . GLU   A 1 114 ? 28.092 -14.681 -0.638  1.00 13.34 ?  114 GLU   A CB   1 
ATOM   2441 C CG   . GLU   A 1 114 ? 27.318 -15.713 -1.435  1.00 14.53 ?  114 GLU   A CG   1 
ATOM   2442 C CD   . GLU   A 1 114 ? 28.033 -16.258 -2.666  1.00 14.68 ?  114 GLU   A CD   1 
ATOM   2443 O OE1  . GLU   A 1 114 ? 28.996 -15.649 -3.166  1.00 14.77 ?  114 GLU   A OE1  1 
ATOM   2444 O OE2  . GLU   A 1 114 ? 27.591 -17.324 -3.153  1.00 16.77 -1 114 GLU   A OE2  1 
ATOM   2445 H H    . GLU   A 1 114 ? 26.276 -13.047 -1.018  1.00 15.49 ?  114 GLU   A H    1 
ATOM   2446 H HA   . GLU   A 1 114 ? 26.754 -14.725 0.898   1.00 15.67 ?  114 GLU   A HA   1 
ATOM   2447 H HB2  . GLU   A 1 114 ? 28.409 -14.001 -1.254  1.00 16.02 ?  114 GLU   A HB2  1 
ATOM   2448 H HB3  . GLU   A 1 114 ? 28.842 -15.124 -0.214  1.00 16.02 ?  114 GLU   A HB3  1 
ATOM   2449 H HG2  . GLU   A 1 114 ? 27.132 -16.476 -0.860  1.00 17.45 ?  114 GLU   A HG2  1 
ATOM   2450 H HG3  . GLU   A 1 114 ? 26.477 -15.323 -1.726  1.00 17.45 ?  114 GLU   A HG3  1 
ATOM   2451 N N    . ASN   A 1 115 ? 28.277 -11.992 1.354   1.00 13.28 ?  115 ASN   A N    1 
ATOM   2452 C CA   . ASN   A 1 115 ? 29.033 -11.260 2.363   1.00 13.50 ?  115 ASN   A CA   1 
ATOM   2453 C C    . ASN   A 1 115 ? 28.405 -11.385 3.743   1.00 13.76 ?  115 ASN   A C    1 
ATOM   2454 O O    . ASN   A 1 115 ? 29.111 -11.311 4.755   1.00 13.96 ?  115 ASN   A O    1 
ATOM   2455 C CB   . ASN   A 1 115 ? 29.158 -9.785  1.975   1.00 13.58 ?  115 ASN   A CB   1 
ATOM   2456 C CG   . ASN   A 1 115 ? 29.959 -9.592  0.711   1.00 14.10 ?  115 ASN   A CG   1 
ATOM   2457 O OD1  . ASN   A 1 115 ? 31.182 -9.757  0.718   1.00 17.91 ?  115 ASN   A OD1  1 
ATOM   2458 N ND2  . ASN   A 1 115 ? 29.288 -9.255  -0.379  1.00 14.63 ?  115 ASN   A ND2  1 
ATOM   2459 H H    . ASN   A 1 115 ? 27.992 -11.507 0.702   1.00 15.95 ?  115 ASN   A H    1 
ATOM   2460 H HA   . ASN   A 1 115 ? 29.927 -11.631 2.416   1.00 16.21 ?  115 ASN   A HA   1 
ATOM   2461 H HB2  . ASN   A 1 115 ? 28.274 -9.417  1.845   1.00 16.31 ?  115 ASN   A HB2  1 
ATOM   2462 H HB3  . ASN   A 1 115 ? 29.617 -9.311  2.689   1.00 16.31 ?  115 ASN   A HB3  1 
ATOM   2463 H HD21 . ASN   A 1 115 ? 29.692 -9.138  -1.124  1.00 17.57 ?  115 ASN   A HD21 1 
ATOM   2464 H HD22 . ASN   A 1 115 ? 28.424 -9.157  -0.343  1.00 17.57 ?  115 ASN   A HD22 1 
ATOM   2465 N N    . PHE   A 1 116 ? 27.079 -11.547 3.813   1.00 14.15 ?  116 PHE   A N    1 
ATOM   2466 C CA   . PHE   A 1 116 ? 26.425 -11.639 5.116   1.00 14.29 ?  116 PHE   A CA   1 
ATOM   2467 C C    . PHE   A 1 116 ? 26.895 -12.867 5.891   1.00 14.05 ?  116 PHE   A C    1 
ATOM   2468 O O    . PHE   A 1 116 ? 26.828 -12.891 7.123   1.00 14.66 ?  116 PHE   A O    1 
ATOM   2469 C CB   . PHE   A 1 116 ? 24.896 -11.766 4.969   1.00 14.06 ?  116 PHE   A CB   1 
ATOM   2470 C CG   . PHE   A 1 116 ? 24.157 -10.526 4.504   1.00 13.59 ?  116 PHE   A CG   1 
ATOM   2471 C CD1  . PHE   A 1 116 ? 24.750 -9.513  3.750   1.00 13.60 ?  116 PHE   A CD1  1 
ATOM   2472 C CD2  . PHE   A 1 116 ? 22.809 -10.394 4.840   1.00 15.00 ?  116 PHE   A CD2  1 
ATOM   2473 C CE1  . PHE   A 1 116 ? 23.986 -8.406  3.341   1.00 13.46 ?  116 PHE   A CE1  1 
ATOM   2474 C CE2  . PHE   A 1 116 ? 22.066 -9.309  4.441   1.00 15.42 ?  116 PHE   A CE2  1 
ATOM   2475 C CZ   . PHE   A 1 116 ? 22.641 -8.317  3.690   1.00 14.43 ?  116 PHE   A CZ   1 
ATOM   2476 H H    . PHE   A 1 116 ? 26.552 -11.600 3.133   1.00 17.00 ?  116 PHE   A H    1 
ATOM   2477 H HA   . PHE   A 1 116 ? 26.619 -10.851 5.638   1.00 17.17 ?  116 PHE   A HA   1 
ATOM   2478 H HB2  . PHE   A 1 116 ? 24.701 -12.468 4.329   1.00 16.88 ?  116 PHE   A HB2  1 
ATOM   2479 H HB3  . PHE   A 1 116 ? 24.525 -12.013 5.835   1.00 16.88 ?  116 PHE   A HB3  1 
ATOM   2480 H HD1  . PHE   A 1 116 ? 25.643 -9.570  3.509   1.00 16.34 ?  116 PHE   A HD1  1 
ATOM   2481 H HD2  . PHE   A 1 116 ? 22.402 -11.069 5.341   1.00 18.01 ?  116 PHE   A HD2  1 
ATOM   2482 H HE1  . PHE   A 1 116 ? 24.381 -7.721  2.837   1.00 16.17 ?  116 PHE   A HE1  1 
ATOM   2483 H HE2  . PHE   A 1 116 ? 21.166 -9.255  4.681   1.00 18.52 ?  116 PHE   A HE2  1 
ATOM   2484 H HZ   . PHE   A 1 116 ? 22.140 -7.575  3.430   1.00 17.33 ?  116 PHE   A HZ   1 
ATOM   2485 N N    . ASN   A 1 117 ? 27.340 -13.908 5.186   1.00 13.72 ?  117 ASN   A N    1 
ATOM   2486 C CA   . ASN   A 1 117 ? 27.698 -15.148 5.862   1.00 14.59 ?  117 ASN   A CA   1 
ATOM   2487 C C    . ASN   A 1 117 ? 28.958 -15.033 6.701   1.00 15.07 ?  117 ASN   A C    1 
ATOM   2488 O O    . ASN   A 1 117 ? 29.254 -15.958 7.468   1.00 16.36 ?  117 ASN   A O    1 
ATOM   2489 C CB   . ASN   A 1 117 ? 27.807 -16.284 4.845   1.00 14.74 ?  117 ASN   A CB   1 
ATOM   2490 C CG   . ASN   A 1 117 ? 26.460 -16.685 4.310   1.00 15.27 ?  117 ASN   A CG   1 
ATOM   2491 O OD1  . ASN   A 1 117 ? 25.487 -16.715 5.052   1.00 15.70 ?  117 ASN   A OD1  1 
ATOM   2492 N ND2  . ASN   A 1 117 ? 26.386 -16.978 3.026   1.00 15.05 ?  117 ASN   A ND2  1 
ATOM   2493 H H    . ASN   A 1 117 ? 27.424 -13.927 4.326   1.00 16.48 ?  117 ASN   A H    1 
ATOM   2494 H HA   . ASN   A 1 117 ? 26.973 -15.380 6.463   1.00 17.52 ?  117 ASN   A HA   1 
ATOM   2495 H HB2  . ASN   A 1 117 ? 28.352 -15.990 4.095   1.00 17.70 ?  117 ASN   A HB2  1 
ATOM   2496 H HB3  . ASN   A 1 117 ? 28.211 -17.054 5.270   1.00 17.70 ?  117 ASN   A HB3  1 
ATOM   2497 H HD21 . ASN   A 1 117 ? 25.632 -17.221 2.688   1.00 18.08 ?  117 ASN   A HD21 1 
ATOM   2498 H HD22 . ASN   A 1 117 ? 27.091 -16.963 2.541   1.00 18.08 ?  117 ASN   A HD22 1 
ATOM   2499 N N    . GLN   A 1 118 ? 29.694 -13.933 6.586   1.00 15.63 ?  118 GLN   A N    1 
ATOM   2500 C CA   . GLN   A 1 118 ? 30.866 -13.708 7.417   1.00 16.01 ?  118 GLN   A CA   1 
ATOM   2501 C C    . GLN   A 1 118 ? 30.518 -13.131 8.783   1.00 16.11 ?  118 GLN   A C    1 
ATOM   2502 O O    . GLN   A 1 118 ? 31.430 -12.828 9.559   1.00 17.69 ?  118 GLN   A O    1 
ATOM   2503 C CB   . GLN   A 1 118 ? 31.874 -12.821 6.673   1.00 16.07 ?  118 GLN   A CB   1 
ATOM   2504 C CG   . GLN   A 1 118 ? 32.329 -13.402 5.346   1.00 15.80 ?  118 GLN   A CG   1 
ATOM   2505 C CD   . GLN   A 1 118 ? 33.162 -14.663 5.525   1.00 16.08 ?  118 GLN   A CD   1 
ATOM   2506 O OE1  . GLN   A 1 118 ? 34.012 -14.737 6.413   1.00 17.10 ?  118 GLN   A OE1  1 
ATOM   2507 N NE2  . GLN   A 1 118 ? 32.900 -15.670 4.693   1.00 15.73 ?  118 GLN   A NE2  1 
ATOM   2508 H H    . GLN   A 1 118 ? 29.534 -13.292 6.025   1.00 18.77 ?  118 GLN   A H    1 
ATOM   2509 H HA   . GLN   A 1 118 ? 31.293 -14.560 7.572   1.00 19.22 ?  118 GLN   A HA   1 
ATOM   2510 H HB2  . GLN   A 1 118 ? 31.465 -11.956 6.496   1.00 19.30 ?  118 GLN   A HB2  1 
ATOM   2511 H HB3  . GLN   A 1 118 ? 32.660 -12.701 7.230   1.00 19.30 ?  118 GLN   A HB3  1 
ATOM   2512 H HG2  . GLN   A 1 118 ? 31.548 -13.617 4.808   1.00 18.98 ?  118 GLN   A HG2  1 
ATOM   2513 H HG3  . GLN   A 1 118 ? 32.877 -12.748 4.883   1.00 18.98 ?  118 GLN   A HG3  1 
ATOM   2514 H HE21 . GLN   A 1 118 ? 32.285 -15.578 4.085   1.00 18.89 ?  118 GLN   A HE21 1 
ATOM   2515 H HE22 . GLN   A 1 118 ? 33.328 -16.403 4.756   1.00 18.89 ?  118 GLN   A HE22 1 
ATOM   2516 N N    . HIS   A 1 119 ? 29.230 -12.968 9.095   1.00 15.46 ?  119 HIS   A N    1 
ATOM   2517 C CA   . HIS   A 1 119 ? 28.778 -12.342 10.334  1.00 16.18 ?  119 HIS   A CA   1 
ATOM   2518 C C    . HIS   A 1 119 ? 27.644 -13.162 10.923  1.00 16.01 ?  119 HIS   A C    1 
ATOM   2519 O O    . HIS   A 1 119 ? 26.707 -13.514 10.208  1.00 16.59 ?  119 HIS   A O    1 
ATOM   2520 C CB   . HIS   A 1 119 ? 28.334 -10.907 10.041  1.00 16.51 ?  119 HIS   A CB   1 
ATOM   2521 C CG   . HIS   A 1 119 ? 29.432 -10.106 9.436   1.00 17.68 ?  119 HIS   A CG   1 
ATOM   2522 N ND1  . HIS   A 1 119 ? 30.407 -9.509  10.202  1.00 19.86 ?  119 HIS   A ND1  1 
ATOM   2523 C CD2  . HIS   A 1 119 ? 29.794 -9.918  8.147   1.00 18.32 ?  119 HIS   A CD2  1 
ATOM   2524 C CE1  . HIS   A 1 119 ? 31.294 -8.939  9.408   1.00 20.08 ?  119 HIS   A CE1  1 
ATOM   2525 N NE2  . HIS   A 1 119 ? 30.950 -9.180  8.156   1.00 20.20 ?  119 HIS   A NE2  1 
ATOM   2526 H H    . HIS   A 1 119 ? 28.578 -13.230 8.593   1.00 18.56 ?  119 HIS   A H    1 
ATOM   2527 H HA   . HIS   A 1 119 ? 29.503 -12.319 10.970  1.00 19.43 ?  119 HIS   A HA   1 
ATOM   2528 H HB2  . HIS   A 1 119 ? 27.585 -10.921 9.422   1.00 19.83 ?  119 HIS   A HB2  1 
ATOM   2529 H HB3  . HIS   A 1 119 ? 28.066 -10.482 10.874  1.00 19.83 ?  119 HIS   A HB3  1 
ATOM   2530 H HD2  . HIS   A 1 119 ? 29.338 -10.223 7.394   1.00 21.99 ?  119 HIS   A HD2  1 
ATOM   2531 H HE1  . HIS   A 1 119 ? 32.035 -8.446  9.683   1.00 24.11 ?  119 HIS   A HE1  1 
ATOM   2532 H HE2  . HIS   A 1 119 ? 31.369 -8.895  7.460   1.00 24.25 ?  119 HIS   A HE2  1 
ATOM   2533 N N    . GLU   A 1 120 ? 27.724 -13.452 12.224  1.00 17.70 ?  120 GLU   A N    1 
ATOM   2534 C CA   . GLU   A 1 120 ? 26.757 -14.366 12.832  1.00 20.72 ?  120 GLU   A CA   1 
ATOM   2535 C C    . GLU   A 1 120 ? 25.351 -13.780 12.879  1.00 19.49 ?  120 GLU   A C    1 
ATOM   2536 O O    . GLU   A 1 120 ? 24.363 -14.524 12.764  1.00 20.06 ?  120 GLU   A O    1 
ATOM   2537 C CB   . GLU   A 1 120 ? 27.212 -14.757 14.238  1.00 26.23 ?  120 GLU   A CB   1 
ATOM   2538 C CG   . GLU   A 1 120 ? 28.399 -15.697 14.254  1.00 34.36 ?  120 GLU   A CG   1 
ATOM   2539 C CD   . GLU   A 1 120 ? 28.501 -16.481 15.543  1.00 41.20 ?  120 GLU   A CD   1 
ATOM   2540 O OE1  . GLU   A 1 120 ? 27.916 -16.041 16.556  1.00 43.54 ?  120 GLU   A OE1  1 
ATOM   2541 O OE2  . GLU   A 1 120 ? 29.159 -17.543 15.540  1.00 45.29 -1 120 GLU   A OE2  1 
ATOM   2542 H H    . GLU   A 1 120 ? 28.324 -13.143 12.761  1.00 21.26 ?  120 GLU   A H    1 
ATOM   2543 H HA   . GLU   A 1 120 ? 26.715 -15.170 12.302  1.00 24.88 ?  120 GLU   A HA   1 
ATOM   2544 H HB2  . GLU   A 1 120 ? 27.462 -13.956 14.726  1.00 31.49 ?  120 GLU   A HB2  1 
ATOM   2545 H HB3  . GLU   A 1 120 ? 26.477 -15.200 14.692  1.00 31.49 ?  120 GLU   A HB3  1 
ATOM   2546 H HG2  . GLU   A 1 120 ? 28.312 -16.332 13.528  1.00 41.25 ?  120 GLU   A HG2  1 
ATOM   2547 H HG3  . GLU   A 1 120 ? 29.213 -15.182 14.156  1.00 41.25 ?  120 GLU   A HG3  1 
ATOM   2548 N N    . VAL   A 1 121 ? 25.237 -12.470 13.097  1.00 18.51 ?  121 VAL   A N    1 
ATOM   2549 C CA   . VAL   A 1 121 ? 23.950 -11.790 13.212  1.00 18.94 ?  121 VAL   A CA   1 
ATOM   2550 C C    . VAL   A 1 121 ? 24.073 -10.434 12.539  1.00 17.43 ?  121 VAL   A C    1 
ATOM   2551 O O    . VAL   A 1 121 ? 25.057 -9.721  12.753  1.00 17.44 ?  121 VAL   A O    1 
ATOM   2552 C CB   . VAL   A 1 121 ? 23.536 -11.588 14.688  1.00 22.07 ?  121 VAL   A CB   1 
ATOM   2553 C CG1  . VAL   A 1 121 ? 22.178 -10.891 14.779  1.00 22.74 ?  121 VAL   A CG1  1 
ATOM   2554 C CG2  . VAL   A 1 121 ? 23.500 -12.902 15.441  1.00 24.60 ?  121 VAL   A CG2  1 
ATOM   2555 H H    . VAL   A 1 121 ? 25.911 -11.936 13.198  1.00 22.22 ?  121 VAL   A H    1 
ATOM   2556 H HA   . VAL   A 1 121 ? 23.267 -12.306 12.766  1.00 22.74 ?  121 VAL   A HA   1 
ATOM   2557 H HB   . VAL   A 1 121 ? 24.183 -11.013 15.126  1.00 26.50 ?  121 VAL   A HB   1 
ATOM   2558 H HG11 . VAL   A 1 121 ? 21.856 -10.936 15.694  1.00 27.31 ?  121 VAL   A HG11 1 
ATOM   2559 H HG12 . VAL   A 1 121 ? 22.275 -9.962  14.512  1.00 27.31 ?  121 VAL   A HG12 1 
ATOM   2560 H HG13 . VAL   A 1 121 ? 21.551 -11.340 14.189  1.00 27.31 ?  121 VAL   A HG13 1 
ATOM   2561 H HG21 . VAL   A 1 121 ? 23.178 -12.741 16.346  1.00 29.54 ?  121 VAL   A HG21 1 
ATOM   2562 H HG22 . VAL   A 1 121 ? 22.895 -13.510 14.985  1.00 29.54 ?  121 VAL   A HG22 1 
ATOM   2563 H HG23 . VAL   A 1 121 ? 24.390 -13.274 15.470  1.00 29.54 ?  121 VAL   A HG23 1 
ATOM   2564 N N    . LEU   A 1 122 ? 23.058 -10.053 11.762  1.00 16.24 ?  122 LEU   A N    1 
ATOM   2565 C CA   . LEU   A 1 122 ? 23.064 -8.763  11.084  1.00 15.88 ?  122 LEU   A CA   1 
ATOM   2566 C C    . LEU   A 1 122 ? 21.671 -8.157  11.028  1.00 15.08 ?  122 LEU   A C    1 
ATOM   2567 O O    . LEU   A 1 122 ? 20.679 -8.872  10.866  1.00 16.44 ?  122 LEU   A O    1 
ATOM   2568 C CB   . LEU   A 1 122 ? 23.497 -8.882  9.621   1.00 17.48 ?  122 LEU   A CB   1 
ATOM   2569 C CG   . LEU   A 1 122 ? 24.699 -9.740  9.256   1.00 17.44 ?  122 LEU   A CG   1 
ATOM   2570 C CD1  . LEU   A 1 122 ? 24.246 -11.166 9.024   1.00 17.77 ?  122 LEU   A CD1  1 
ATOM   2571 C CD2  . LEU   A 1 122 ? 25.399 -9.182  8.025   1.00 16.48 ?  122 LEU   A CD2  1 
ATOM   2572 H H    . LEU   A 1 122 ? 22.352 -10.523 11.609  1.00 19.51 ?  122 LEU   A H    1 
ATOM   2573 H HA   . LEU   A 1 122 ? 23.667 -8.146  11.543  1.00 19.08 ?  122 LEU   A HA   1 
ATOM   2574 H HB2  . LEU   A 1 122 ? 22.752 -9.239  9.124   1.00 20.98 ?  122 LEU   A HB2  1 
ATOM   2575 H HB3  . LEU   A 1 122 ? 23.696 -7.989  9.299   1.00 20.98 ?  122 LEU   A HB3  1 
ATOM   2576 H HG   . LEU   A 1 122 ? 25.341 -9.737  9.988   1.00 20.94 ?  122 LEU   A HG   1 
ATOM   2577 H HD11 . LEU   A 1 122 ? 25.009 -11.712 8.789   1.00 21.34 ?  122 LEU   A HD11 1 
ATOM   2578 H HD12 . LEU   A 1 122 ? 23.834 -11.503 9.836   1.00 21.34 ?  122 LEU   A HD12 1 
ATOM   2579 H HD13 . LEU   A 1 122 ? 23.596 -11.176 8.300   1.00 21.34 ?  122 LEU   A HD13 1 
ATOM   2580 H HD21 . LEU   A 1 122 ? 26.144 -9.759  7.785   1.00 19.80 ?  122 LEU   A HD21 1 
ATOM   2581 H HD22 . LEU   A 1 122 ? 24.767 -9.144  7.288   1.00 19.80 ?  122 LEU   A HD22 1 
ATOM   2582 H HD23 . LEU   A 1 122 ? 25.730 -8.287  8.217   1.00 19.80 ?  122 LEU   A HD23 1 
ATOM   2583 N N    A LEU   A 1 123 ? 21.611 -6.835  11.168  0.46 15.19 ?  123 LEU   A N    1 
ATOM   2584 N N    B LEU   A 1 123 ? 21.620 -6.829  11.149  0.54 15.43 ?  123 LEU   A N    1 
ATOM   2585 C CA   A LEU   A 1 123 ? 20.472 -6.041  10.724  0.46 15.21 ?  123 LEU   A CA   1 
ATOM   2586 C CA   B LEU   A 1 123 ? 20.447 -6.021  10.829  0.54 15.33 ?  123 LEU   A CA   1 
ATOM   2587 C C    A LEU   A 1 123 ? 20.763 -5.561  9.310   0.46 14.88 ?  123 LEU   A C    1 
ATOM   2588 C C    B LEU   A 1 123 ? 20.655 -5.437  9.434   0.54 13.93 ?  123 LEU   A C    1 
ATOM   2589 O O    A LEU   A 1 123 ? 21.885 -5.141  9.015   0.46 14.93 ?  123 LEU   A O    1 
ATOM   2590 O O    B LEU   A 1 123 ? 21.644 -4.731  9.207   0.54 14.10 ?  123 LEU   A O    1 
ATOM   2591 C CB   A LEU   A 1 123 ? 20.302 -4.827  11.637  0.46 14.81 ?  123 LEU   A CB   1 
ATOM   2592 C CB   B LEU   A 1 123 ? 20.295 -4.898  11.860  0.54 15.84 ?  123 LEU   A CB   1 
ATOM   2593 C CG   A LEU   A 1 123 ? 19.233 -3.778  11.320  0.46 15.90 ?  123 LEU   A CG   1 
ATOM   2594 C CG   B LEU   A 1 123 ? 19.307 -3.778  11.506  0.54 16.72 ?  123 LEU   A CG   1 
ATOM   2595 C CD1  A LEU   A 1 123 ? 17.844 -4.396  11.342  0.46 17.01 ?  123 LEU   A CD1  1 
ATOM   2596 C CD1  B LEU   A 1 123 ? 17.869 -4.298  11.412  0.54 17.57 ?  123 LEU   A CD1  1 
ATOM   2597 C CD2  A LEU   A 1 123 ? 19.317 -2.615  12.313  0.46 16.00 ?  123 LEU   A CD2  1 
ATOM   2598 C CD2  B LEU   A 1 123 ? 19.398 -2.626  12.498  0.54 17.38 ?  123 LEU   A CD2  1 
ATOM   2599 H H    A LEU   A 1 123 ? 22.242 -6.366  11.528  0.46 18.24 ?  123 LEU   A H    1 
ATOM   2600 H H    B LEU   A 1 123 ? 22.290 -6.354  11.422  0.54 18.54 ?  123 LEU   A H    1 
ATOM   2601 H HA   A LEU   A 1 123 ? 19.669 -6.583  10.727  0.46 18.27 ?  123 LEU   A HA   1 
ATOM   2602 H HA   B LEU   A 1 123 ? 19.653 -6.567  10.830  0.54 18.41 ?  123 LEU   A HA   1 
ATOM   2603 H HB2  A LEU   A 1 123 ? 20.103 -5.162  12.520  0.46 17.78 ?  123 LEU   A HB2  1 
ATOM   2604 H HB2  B LEU   A 1 123 ? 19.994 -5.293  12.698  0.54 19.02 ?  123 LEU   A HB2  1 
ATOM   2605 H HB3  A LEU   A 1 123 ? 21.147 -4.362  11.653  0.46 17.78 ?  123 LEU   A HB3  1 
ATOM   2606 H HB3  B LEU   A 1 123 ? 21.162 -4.485  12.000  0.54 19.02 ?  123 LEU   A HB3  1 
ATOM   2607 H HG   A LEU   A 1 123 ? 19.387 -3.418  10.432  0.46 19.09 ?  123 LEU   A HG   1 
ATOM   2608 H HG   B LEU   A 1 123 ? 19.542 -3.419  10.640  0.54 20.08 ?  123 LEU   A HG   1 
ATOM   2609 H HD11 A LEU   A 1 123 ? 17.185 -3.703  11.183  0.46 20.43 ?  123 LEU   A HD11 1 
ATOM   2610 H HD11 B LEU   A 1 123 ? 17.279 -3.558  11.194  0.54 21.09 ?  123 LEU   A HD11 1 
ATOM   2611 H HD12 A LEU   A 1 123 ? 17.790 -5.070  10.646  0.46 20.43 ?  123 LEU   A HD12 1 
ATOM   2612 H HD12 B LEU   A 1 123 ? 17.819 -4.973  10.715  0.54 21.09 ?  123 LEU   A HD12 1 
ATOM   2613 H HD13 A LEU   A 1 123 ? 17.694 -4.804  12.210  0.46 20.43 ?  123 LEU   A HD13 1 
ATOM   2614 H HD13 B LEU   A 1 123 ? 17.611 -4.684  12.264  0.54 21.09 ?  123 LEU   A HD13 1 
ATOM   2615 H HD21 A LEU   A 1 123 ? 18.634 -1.961  12.100  0.46 19.22 ?  123 LEU   A HD21 1 
ATOM   2616 H HD21 B LEU   A 1 123 ? 18.762 -1.941  12.242  0.54 20.87 ?  123 LEU   A HD21 1 
ATOM   2617 H HD22 A LEU   A 1 123 ? 19.176 -2.957  13.213  0.46 19.22 ?  123 LEU   A HD22 1 
ATOM   2618 H HD22 B LEU   A 1 123 ? 19.190 -2.957  13.386  0.54 20.87 ?  123 LEU   A HD22 1 
ATOM   2619 H HD23 A LEU   A 1 123 ? 20.196 -2.208  12.253  0.46 19.22 ?  123 LEU   A HD23 1 
ATOM   2620 H HD23 B LEU   A 1 123 ? 20.298 -2.266  12.481  0.54 20.87 ?  123 LEU   A HD23 1 
ATOM   2621 N N    A ALA   A 1 124 ? 19.757 -5.609  8.433   0.46 14.45 ?  124 ALA   A N    1 
ATOM   2622 N N    B ALA   A 1 124 ? 19.745 -5.721  8.503   0.54 13.30 ?  124 ALA   A N    1 
ATOM   2623 C CA   A ALA   A 1 124 ? 20.064 -5.416  7.023   0.46 14.66 ?  124 ALA   A CA   1 
ATOM   2624 C CA   B ALA   A 1 124 ? 19.990 -5.384  7.108   0.54 13.38 ?  124 ALA   A CA   1 
ATOM   2625 C C    A ALA   A 1 124 ? 18.824 -5.005  6.242   0.46 13.99 ?  124 ALA   A C    1 
ATOM   2626 C C    B ALA   A 1 124 ? 18.745 -4.888  6.389   0.54 13.54 ?  124 ALA   A C    1 
ATOM   2627 O O    A ALA   A 1 124 ? 17.705 -5.394  6.595   0.46 14.09 ?  124 ALA   A O    1 
ATOM   2628 O O    B ALA   A 1 124 ? 17.615 -5.191  6.788   0.54 14.45 ?  124 ALA   A O    1 
ATOM   2629 C CB   A ALA   A 1 124 ? 20.649 -6.696  6.416   0.46 15.29 ?  124 ALA   A CB   1 
ATOM   2630 C CB   B ALA   A 1 124 ? 20.552 -6.578  6.324   0.54 13.01 ?  124 ALA   A CB   1 
ATOM   2631 H H    A ALA   A 1 124 ? 18.934 -5.729  8.626   0.46 17.36 ?  124 ALA   A H    1 
ATOM   2632 H H    B ALA   A 1 124 ? 18.999 -6.112  8.653   0.54 15.97 ?  124 ALA   A H    1 
ATOM   2633 H HA   A ALA   A 1 124 ? 20.740 -4.717  6.958   0.46 17.60 ?  124 ALA   A HA   1 
ATOM   2634 H HA   B ALA   A 1 124 ? 20.658 -4.686  7.080   0.54 16.07 ?  124 ALA   A HA   1 
ATOM   2635 H HB1  A ALA   A 1 124 ? 20.845 -6.538  5.480   0.46 18.37 ?  124 ALA   A HB1  1 
ATOM   2636 H HB1  B ALA   A 1 124 ? 20.700 -6.312  5.400   0.54 15.62 ?  124 ALA   A HB1  1 
ATOM   2637 H HB2  A ALA   A 1 124 ? 21.463 -6.932  6.890   0.46 18.37 ?  124 ALA   A HB2  1 
ATOM   2638 H HB2  B ALA   A 1 124 ? 21.396 -6.855  6.721   0.54 15.62 ?  124 ALA   A HB2  1 
ATOM   2639 H HB3  A ALA   A 1 124 ? 19.997 -7.408  6.504   0.46 18.37 ?  124 ALA   A HB3  1 
ATOM   2640 H HB3  B ALA   A 1 124 ? 19.918 -7.311  6.357   0.54 15.62 ?  124 ALA   A HB3  1 
ATOM   2641 N N    A PRO   A 1 125 ? 19.001 -4.266  5.154   0.46 13.45 ?  125 PRO   A N    1 
ATOM   2642 N N    B PRO   A 1 125 ? 18.931 -4.148  5.299   0.54 13.97 ?  125 PRO   A N    1 
ATOM   2643 C CA   A PRO   A 1 125 ? 17.931 -4.040  4.185   0.46 13.76 ?  125 PRO   A CA   1 
ATOM   2644 C CA   B PRO   A 1 125 ? 17.844 -3.864  4.361   0.54 14.84 ?  125 PRO   A CA   1 
ATOM   2645 C C    A PRO   A 1 125 ? 17.996 -5.115  3.107   0.46 13.35 ?  125 PRO   A C    1 
ATOM   2646 C C    B PRO   A 1 125 ? 17.896 -4.878  3.222   0.54 14.46 ?  125 PRO   A C    1 
ATOM   2647 O O    A PRO   A 1 125 ? 18.971 -5.854  2.988   0.46 14.48 ?  125 PRO   A O    1 
ATOM   2648 O O    B PRO   A 1 125 ? 18.840 -5.659  3.103   0.54 14.60 ?  125 PRO   A O    1 
ATOM   2649 C CB   A PRO   A 1 125 ? 18.354 -2.704  3.571   0.46 13.76 ?  125 PRO   A CB   1 
ATOM   2650 C CB   B PRO   A 1 125 ? 18.238 -2.477  3.838   0.54 15.38 ?  125 PRO   A CB   1 
ATOM   2651 C CG   A PRO   A 1 125 ? 19.866 -2.865  3.475   0.46 13.27 ?  125 PRO   A CG   1 
ATOM   2652 C CG   B PRO   A 1 125 ? 19.752 -2.576  3.754   0.54 15.22 ?  125 PRO   A CG   1 
ATOM   2653 C CD   A PRO   A 1 125 ? 20.261 -3.625  4.733   0.46 13.02 ?  125 PRO   A CD   1 
ATOM   2654 C CD   B PRO   A 1 125 ? 20.185 -3.480  4.894   0.54 14.50 ?  125 PRO   A CD   1 
ATOM   2655 H HA   A PRO   A 1 125 ? 17.049 -3.992  4.605   0.46 16.53 ?  125 PRO   A HA   1 
ATOM   2656 H HA   B PRO   A 1 125 ? 16.984 -3.847  4.799   0.54 17.82 ?  125 PRO   A HA   1 
ATOM   2657 H HB2  A PRO   A 1 125 ? 17.950 -2.603  2.696   0.46 16.53 ?  125 PRO   A HB2  1 
ATOM   2658 H HB2  B PRO   A 1 125 ? 17.843 -2.323  2.965   0.54 18.47 ?  125 PRO   A HB2  1 
ATOM   2659 H HB3  A PRO   A 1 125 ? 18.110 -1.974  4.161   0.46 16.53 ?  125 PRO   A HB3  1 
ATOM   2660 H HB3  B PRO   A 1 125 ? 17.963 -1.792  4.472   0.54 18.47 ?  125 PRO   A HB3  1 
ATOM   2661 H HG2  A PRO   A 1 125 ? 20.094 -3.377  2.681   0.46 15.94 ?  125 PRO   A HG2  1 
ATOM   2662 H HG2  B PRO   A 1 125 ? 20.001 -2.963  2.900   0.54 18.27 ?  125 PRO   A HG2  1 
ATOM   2663 H HG3  A PRO   A 1 125 ? 20.287 -1.993  3.454   0.46 15.94 ?  125 PRO   A HG3  1 
ATOM   2664 H HG3  B PRO   A 1 125 ? 20.139 -1.692  3.852   0.54 18.27 ?  125 PRO   A HG3  1 
ATOM   2665 H HD2  A PRO   A 1 125 ? 20.932 -4.297  4.532   0.46 15.64 ?  125 PRO   A HD2  1 
ATOM   2666 H HD2  B PRO   A 1 125 ? 20.842 -4.124  4.578   0.54 17.41 ?  125 PRO   A HD2  1 
ATOM   2667 H HD3  A PRO   A 1 125 ? 20.574 -3.008  5.418   0.46 15.64 ?  125 PRO   A HD3  1 
ATOM   2668 H HD3  B PRO   A 1 125 ? 20.540 -2.946  5.625   0.54 17.41 ?  125 PRO   A HD3  1 
ATOM   2669 N N    A LEU   A 1 126 ? 16.939 -5.180  2.306   0.46 13.29 ?  126 LEU   A N    1 
ATOM   2670 N N    B LEU   A 1 126 ? 16.864 -4.858  2.381   0.54 15.27 ?  126 LEU   A N    1 
ATOM   2671 C CA   A LEU   A 1 126 ? 16.958 -6.030  1.124   0.46 13.50 ?  126 LEU   A CA   1 
ATOM   2672 C CA   B LEU   A 1 126 ? 16.921 -5.631  1.147   0.54 14.62 ?  126 LEU   A CA   1 
ATOM   2673 C C    A LEU   A 1 126 ? 17.870 -5.426  0.065   0.46 13.71 ?  126 LEU   A C    1 
ATOM   2674 C C    B LEU   A 1 126 ? 17.924 -4.991  0.190   0.54 15.78 ?  126 LEU   A C    1 
ATOM   2675 O O    A LEU   A 1 126 ? 17.632 -4.314  -0.422  0.46 14.25 ?  126 LEU   A O    1 
ATOM   2676 O O    B LEU   A 1 126 ? 17.893 -3.782  -0.044  0.54 17.58 ?  126 LEU   A O    1 
ATOM   2677 C CB   A LEU   A 1 126 ? 15.550 -6.209  0.576   0.46 14.04 ?  126 LEU   A CB   1 
ATOM   2678 C CB   B LEU   A 1 126 ? 15.539 -5.699  0.496   0.54 15.29 ?  126 LEU   A CB   1 
ATOM   2679 C CG   A LEU   A 1 126 ? 14.672 -7.162  1.384   0.46 14.71 ?  126 LEU   A CG   1 
ATOM   2680 C CG   B LEU   A 1 126 ? 14.497 -6.578  1.199   0.54 16.39 ?  126 LEU   A CG   1 
ATOM   2681 C CD1  A LEU   A 1 126 ? 13.225 -7.036  0.961   0.46 15.38 ?  126 LEU   A CD1  1 
ATOM   2682 C CD1  B LEU   A 1 126 ? 13.139 -6.438  0.532   0.54 17.37 ?  126 LEU   A CD1  1 
ATOM   2683 C CD2  A LEU   A 1 126 ? 15.169 -8.602  1.228   0.46 14.95 ?  126 LEU   A CD2  1 
ATOM   2684 C CD2  B LEU   A 1 126 ? 14.922 -8.035  1.214   0.54 17.82 ?  126 LEU   A CD2  1 
ATOM   2685 H H    A LEU   A 1 126 ? 16.212 -4.741  2.421   0.46 15.96 ?  126 LEU   A H    1 
ATOM   2686 H H    B LEU   A 1 126 ? 16.119 -4.428  2.490   0.54 18.33 ?  126 LEU   A H    1 
ATOM   2687 H HA   A LEU   A 1 126 ? 17.312 -6.901  1.361   0.46 16.21 ?  126 LEU   A HA   1 
ATOM   2688 H HA   B LEU   A 1 126 ? 17.214 -6.540  1.344   0.54 17.55 ?  126 LEU   A HA   1 
ATOM   2689 H HB2  A LEU   A 1 126 ? 15.113 -5.345  0.562   0.46 16.86 ?  126 LEU   A HB2  1 
ATOM   2690 H HB2  B LEU   A 1 126 ? 15.178 -4.800  0.456   0.54 18.36 ?  126 LEU   A HB2  1 
ATOM   2691 H HB3  A LEU   A 1 126 ? 15.614 -6.558  -0.328  0.46 16.86 ?  126 LEU   A HB3  1 
ATOM   2692 H HB3  B LEU   A 1 126 ? 15.642 -6.044  -0.406  0.54 18.36 ?  126 LEU   A HB3  1 
ATOM   2693 H HG   A LEU   A 1 126 ? 14.734 -6.927  2.322   0.46 17.66 ?  126 LEU   A HG   1 
ATOM   2694 H HG   B LEU   A 1 126 ? 14.404 -6.281  2.118   0.54 19.68 ?  126 LEU   A HG   1 
ATOM   2695 H HD11 A LEU   A 1 126 ? 12.690 -7.653  1.485   0.46 18.47 ?  126 LEU   A HD11 1 
ATOM   2696 H HD11 B LEU   A 1 126 ? 12.496 -6.998  0.998   0.54 20.86 ?  126 LEU   A HD11 1 
ATOM   2697 H HD12 A LEU   A 1 126 ? 12.931 -6.126  1.117   0.46 18.47 ?  126 LEU   A HD12 1 
ATOM   2698 H HD12 B LEU   A 1 126 ? 12.857 -5.511  0.571   0.54 20.86 ?  126 LEU   A HD12 1 
ATOM   2699 H HD13 A LEU   A 1 126 ? 13.152 -7.253  0.018   0.46 18.47 ?  126 LEU   A HD13 1 
ATOM   2700 H HD13 B LEU   A 1 126 ? 13.210 -6.722  -0.395  0.54 20.86 ?  126 LEU   A HD13 1 
ATOM   2701 H HD21 A LEU   A 1 126 ? 14.517 -9.204  1.616   0.46 17.95 ?  126 LEU   A HD21 1 
ATOM   2702 H HD21 B LEU   A 1 126 ? 14.184 -8.575  1.533   0.54 21.40 ?  126 LEU   A HD21 1 
ATOM   2703 H HD22 A LEU   A 1 126 ? 15.284 -8.797  0.286   0.46 17.95 ?  126 LEU   A HD22 1 
ATOM   2704 H HD22 B LEU   A 1 126 ? 15.164 -8.300  0.313   0.54 21.40 ?  126 LEU   A HD22 1 
ATOM   2705 H HD23 A LEU   A 1 126 ? 16.020 -8.696  1.689   0.46 17.95 ?  126 LEU   A HD23 1 
ATOM   2706 H HD23 B LEU   A 1 126 ? 15.685 -8.132  1.804   0.54 21.40 ?  126 LEU   A HD23 1 
ATOM   2707 N N    A LEU   A 1 127 ? 18.907 -6.173  -0.301  0.46 13.51 ?  127 LEU   A N    1 
ATOM   2708 N N    B LEU   A 1 127 ? 18.830 -5.794  -0.352  0.54 14.73 ?  127 LEU   A N    1 
ATOM   2709 C CA   A LEU   A 1 127 ? 19.898 -5.669  -1.236  0.46 13.32 ?  127 LEU   A CA   1 
ATOM   2710 C CA   B LEU   A 1 127 ? 19.830 -5.267  -1.268  0.54 15.08 ?  127 LEU   A CA   1 
ATOM   2711 C C    A LEU   A 1 127 ? 19.275 -5.457  -2.609  0.46 13.00 ?  127 LEU   A C    1 
ATOM   2712 C C    B LEU   A 1 127 ? 19.257 -5.091  -2.673  0.54 15.02 ?  127 LEU   A C    1 
ATOM   2713 O O    A LEU   A 1 127 ? 18.464 -6.263  -3.082  0.46 13.88 ?  127 LEU   A O    1 
ATOM   2714 O O    B LEU   A 1 127 ? 18.353 -5.814  -3.108  0.54 15.33 ?  127 LEU   A O    1 
ATOM   2715 C CB   A LEU   A 1 127 ? 21.064 -6.652  -1.341  0.46 13.88 ?  127 LEU   A CB   1 
ATOM   2716 C CB   B LEU   A 1 127 ? 21.062 -6.176  -1.311  0.54 15.64 ?  127 LEU   A CB   1 
ATOM   2717 C CG   A LEU   A 1 127 ? 21.866 -6.927  -0.067  0.46 14.30 ?  127 LEU   A CG   1 
ATOM   2718 C CG   B LEU   A 1 127 ? 21.830 -6.314  0.010   0.54 16.36 ?  127 LEU   A CG   1 
ATOM   2719 C CD1  A LEU   A 1 127 ? 22.937 -7.959  -0.361  0.46 14.51 ?  127 LEU   A CD1  1 
ATOM   2720 C CD1  B LEU   A 1 127 ? 23.021 -7.263  -0.133  0.54 17.50 ?  127 LEU   A CD1  1 
ATOM   2721 C CD2  A LEU   A 1 127 ? 22.502 -5.653  0.464   0.46 14.18 ?  127 LEU   A CD2  1 
ATOM   2722 C CD2  B LEU   A 1 127 ? 22.292 -4.961  0.535   0.54 17.22 ?  127 LEU   A CD2  1 
ATOM   2723 H H    A LEU   A 1 127 ? 19.051 -6.980  -0.031  0.46 16.23 ?  127 LEU   A H    1 
ATOM   2724 H H    B LEU   A 1 127 ? 18.896 -6.637  -0.193  0.54 17.70 ?  127 LEU   A H    1 
ATOM   2725 H HA   A LEU   A 1 127 ? 20.239 -4.822  -0.923  0.46 15.99 ?  127 LEU   A HA   1 
ATOM   2726 H HA   B LEU   A 1 127 ? 20.117 -4.394  -0.946  0.54 18.11 ?  127 LEU   A HA   1 
ATOM   2727 H HB2  A LEU   A 1 127 ? 20.718 -7.507  -1.643  0.46 16.66 ?  127 LEU   A HB2  1 
ATOM   2728 H HB2  B LEU   A 1 127 ? 20.778 -7.066  -1.574  0.54 18.78 ?  127 LEU   A HB2  1 
ATOM   2729 H HB3  A LEU   A 1 127 ? 21.693 -6.314  -1.997  0.46 16.66 ?  127 LEU   A HB3  1 
ATOM   2730 H HB3  B LEU   A 1 127 ? 21.680 -5.825  -1.971  0.54 18.78 ?  127 LEU   A HB3  1 
ATOM   2731 H HG   A LEU   A 1 127 ? 21.276 -7.289  0.617   0.46 17.18 ?  127 LEU   A HG   1 
ATOM   2732 H HG   B LEU   A 1 127 ? 21.236 -6.696  0.672   0.54 19.65 ?  127 LEU   A HG   1 
ATOM   2733 H HD11 A LEU   A 1 127 ? 23.356 -8.230  0.472   0.46 17.43 ?  127 LEU   A HD11 1 
ATOM   2734 H HD11 B LEU   A 1 127 ? 23.483 -7.320  0.721   0.54 21.02 ?  127 LEU   A HD11 1 
ATOM   2735 H HD12 A LEU   A 1 127 ? 22.529 -8.728  -0.790  0.46 17.43 ?  127 LEU   A HD12 1 
ATOM   2736 H HD12 B LEU   A 1 127 ? 22.699 -8.139  -0.392  0.54 21.02 ?  127 LEU   A HD12 1 
ATOM   2737 H HD13 A LEU   A 1 127 ? 23.598 -7.566  -0.951  0.46 17.43 ?  127 LEU   A HD13 1 
ATOM   2738 H HD13 B LEU   A 1 127 ? 23.624 -6.917  -0.809  0.54 21.02 ?  127 LEU   A HD13 1 
ATOM   2739 H HD21 A LEU   A 1 127 ? 23.072 -5.873  1.217   0.46 17.04 ?  127 LEU   A HD21 1 
ATOM   2740 H HD21 B LEU   A 1 127 ? 22.903 -5.099  1.274   0.54 20.68 ?  127 LEU   A HD21 1 
ATOM   2741 H HD22 A LEU   A 1 127 ? 23.031 -5.248  -0.243  0.46 17.04 ?  127 LEU   A HD22 1 
ATOM   2742 H HD22 B LEU   A 1 127 ? 22.739 -4.480  -0.179  0.54 20.68 ?  127 LEU   A HD22 1 
ATOM   2743 H HD23 A LEU   A 1 127 ? 21.803 -5.044  0.743   0.46 17.04 ?  127 LEU   A HD23 1 
ATOM   2744 H HD23 B LEU   A 1 127 ? 21.517 -4.459  0.836   0.54 20.68 ?  127 LEU   A HD23 1 
ATOM   2745 N N    A SER   A 1 128 ? 19.675 -4.367  -3.257  0.46 12.57 ?  128 SER   A N    1 
ATOM   2746 N N    B SER   A 1 128 ? 19.798 -4.101  -3.380  0.54 16.16 ?  128 SER   A N    1 
ATOM   2747 C CA   A SER   A 1 128 ? 19.258 -3.974  -4.597  0.46 12.68 ?  128 SER   A CA   1 
ATOM   2748 C CA   B SER   A 1 128 ? 19.502 -3.785  -4.774  0.54 17.25 ?  128 SER   A CA   1 
ATOM   2749 C C    A SER   A 1 128 ? 17.805 -3.519  -4.668  0.46 12.32 ?  128 SER   A C    1 
ATOM   2750 C C    B SER   A 1 128 ? 18.096 -3.249  -4.998  0.54 19.68 ?  128 SER   A C    1 
ATOM   2751 O O    A SER   A 1 128 ? 17.328 -3.204  -5.756  0.46 13.11 ?  128 SER   A O    1 
ATOM   2752 O O    B SER   A 1 128 ? 17.696 -3.065  -6.151  0.54 20.45 ?  128 SER   A O    1 
ATOM   2753 C CB   A SER   A 1 128 ? 19.556 -5.046  -5.660  0.46 13.64 ?  128 SER   A CB   1 
ATOM   2754 C CB   B SER   A 1 128 ? 19.799 -4.944  -5.733  0.54 16.51 ?  128 SER   A CB   1 
ATOM   2755 O OG   A SER   A 1 128 ? 20.957 -5.282  -5.754  0.46 14.79 ?  128 SER   A OG   1 
ATOM   2756 O OG   B SER   A 1 128 ? 21.199 -5.160  -5.856  0.54 15.27 ?  128 SER   A OG   1 
ATOM   2757 H H    A SER   A 1 128 ? 20.244 -3.818  -2.920  0.46 15.09 ?  128 SER   A H    1 
ATOM   2758 H H    B SER   A 1 128 ? 20.386 -3.572  -3.047  0.54 19.40 ?  128 SER   A H    1 
ATOM   2759 H HA   A SER   A 1 128 ? 19.790 -3.216  -4.841  0.46 15.23 ?  128 SER   A HA   1 
ATOM   2760 H HA   B SER   A 1 128 ? 20.091 -3.069  -5.025  0.54 20.72 ?  128 SER   A HA   1 
ATOM   2761 H HB2  A SER   A 1 128 ? 19.120 -5.880  -5.427  0.46 16.39 ?  128 SER   A HB2  1 
ATOM   2762 H HB2  B SER   A 1 128 ? 19.372 -5.747  -5.399  0.54 19.82 ?  128 SER   A HB2  1 
ATOM   2763 H HB3  A SER   A 1 128 ? 19.239 -4.738  -6.525  0.46 16.39 ?  128 SER   A HB3  1 
ATOM   2764 H HB3  B SER   A 1 128 ? 19.442 -4.719  -6.608  0.54 19.82 ?  128 SER   A HB3  1 
ATOM   2765 H HG   A SER   A 1 128 ? 21.363 -4.581  -5.973  0.46 17.76 ?  128 SER   A HG   1 
ATOM   2766 H HG   B SER   A 1 128 ? 21.567 -4.457  -6.120  0.54 18.34 ?  128 SER   A HG   1 
ATOM   2767 N N    A ALA   A 1 129 ? 17.093 -3.455  -3.548  0.46 12.36 ?  129 ALA   A N    1 
ATOM   2768 N N    B ALA   A 1 129 ? 17.349 -2.963  -3.937  0.54 21.68 ?  129 ALA   A N    1 
ATOM   2769 C CA   A ALA   A 1 129 ? 15.732 -2.939  -3.554  0.46 12.18 ?  129 ALA   A CA   1 
ATOM   2770 C CA   B ALA   A 1 129 ? 16.069 -2.295  -4.091  0.54 23.91 ?  129 ALA   A CA   1 
ATOM   2771 C C    A ALA   A 1 129 ? 15.738 -1.407  -3.500  0.46 12.63 ?  129 ALA   A C    1 
ATOM   2772 C C    B ALA   A 1 129 ? 16.284 -0.784  -4.203  0.54 24.51 ?  129 ALA   A C    1 
ATOM   2773 O O    A ALA   A 1 129 ? 16.783 -0.755  -3.529  0.46 13.53 ?  129 ALA   A O    1 
ATOM   2774 O O    B ALA   A 1 129 ? 17.410 -0.283  -4.169  0.54 26.12 ?  129 ALA   A O    1 
ATOM   2775 C CB   A ALA   A 1 129 ? 14.928 -3.549  -2.407  0.46 13.53 ?  129 ALA   A CB   1 
ATOM   2776 C CB   B ALA   A 1 129 ? 15.145 -2.645  -2.929  0.54 24.55 ?  129 ALA   A CB   1 
ATOM   2777 H H    A ALA   A 1 129 ? 17.370 -3.714  -2.773  0.46 14.85 ?  129 ALA   A H    1 
ATOM   2778 H H    B ALA   A 1 129 ? 17.555 -3.145  -3.119  0.54 26.04 ?  129 ALA   A H    1 
ATOM   2779 H HA   A ALA   A 1 129 ? 15.301 -3.199  -4.380  0.46 14.63 ?  129 ALA   A HA   1 
ATOM   2780 H HA   B ALA   A 1 129 ? 15.649 -2.609  -4.907  0.54 28.71 ?  129 ALA   A HA   1 
ATOM   2781 H HB1  A ALA   A 1 129 ? 14.022 -3.199  -2.431  0.46 16.25 ?  129 ALA   A HB1  1 
ATOM   2782 H HB1  B ALA   A 1 129 ? 14.261 -2.295  -3.123  0.54 29.47 ?  129 ALA   A HB1  1 
ATOM   2783 H HB2  A ALA   A 1 129 ? 14.906 -4.517  -2.512  0.46 16.25 ?  129 ALA   A HB2  1 
ATOM   2784 H HB2  B ALA   A 1 129 ? 15.106 -3.608  -2.839  0.54 29.47 ?  129 ALA   A HB2  1 
ATOM   2785 H HB3  A ALA   A 1 129 ? 15.348 -3.322  -1.563  0.46 16.25 ?  129 ALA   A HB3  1 
ATOM   2786 H HB3  B ALA   A 1 129 ? 15.493 -2.249  -2.115  0.54 29.47 ?  129 ALA   A HB3  1 
ATOM   2787 N N    A GLY   A 1 130 ? 14.553 -0.815  -3.432  0.46 13.62 ?  130 GLY   A N    1 
ATOM   2788 N N    B GLY   A 1 130 ? 15.189 -0.043  -4.342  0.54 24.16 ?  130 GLY   A N    1 
ATOM   2789 C CA   A GLY   A 1 130 ? 14.485 0.635   -3.374  0.46 13.81 ?  130 GLY   A CA   1 
ATOM   2790 C CA   B GLY   A 1 130 ? 15.298 1.404   -4.434  0.54 23.96 ?  130 GLY   A CA   1 
ATOM   2791 C C    A GLY   A 1 130 ? 15.073 1.258   -4.621  0.46 12.87 ?  130 GLY   A C    1 
ATOM   2792 C C    B GLY   A 1 130 ? 15.849 1.848   -5.776  0.54 23.22 ?  130 GLY   A C    1 
ATOM   2793 O O    A GLY   A 1 130 ? 14.823 0.801   -5.742  0.46 12.86 ?  130 GLY   A O    1 
ATOM   2794 O O    B GLY   A 1 130 ? 15.475 1.323   -6.828  0.54 22.35 ?  130 GLY   A O    1 
ATOM   2795 H H    A GLY   A 1 130 ? 13.797 -1.220  -3.436  0.46 16.36 ?  130 GLY   A H    1 
ATOM   2796 H H    B GLY   A 1 130 ? 14.392 -0.349  -4.374  0.54 29.00 ?  130 GLY   A H    1 
ATOM   2797 H HA2  A GLY   A 1 130 ? 13.564 0.914   -3.297  0.46 16.59 ?  130 GLY   A HA2  1 
ATOM   2798 H HA2  B GLY   A 1 130 ? 14.422 1.801   -4.315  0.54 28.76 ?  130 GLY   A HA2  1 
ATOM   2799 H HA3  A GLY   A 1 130 ? 14.982 0.953   -2.608  0.46 16.59 ?  130 GLY   A HA3  1 
ATOM   2800 H HA3  B GLY   A 1 130 ? 15.887 1.732   -3.743  0.54 28.76 ?  130 GLY   A HA3  1 
ATOM   2801 N N    A ILE   A 1 131 ? 15.880 2.312   -4.427  0.46 13.28 ?  131 ILE   A N    1 
ATOM   2802 N N    B ILE   A 1 131 ? 16.752 2.836   -5.748  0.54 24.00 ?  131 ILE   A N    1 
ATOM   2803 C CA   A ILE   A 1 131 ? 16.446 3.052   -5.554  0.46 13.76 ?  131 ILE   A CA   1 
ATOM   2804 C CA   B ILE   A 1 131 ? 17.290 3.371   -6.998  0.54 25.38 ?  131 ILE   A CA   1 
ATOM   2805 C C    A ILE   A 1 131 ? 17.470 2.262   -6.359  0.46 12.87 ?  131 ILE   A C    1 
ATOM   2806 C C    B ILE   A 1 131 ? 18.026 2.304   -7.796  0.54 24.44 ?  131 ILE   A C    1 
ATOM   2807 O O    A ILE   A 1 131 ? 17.905 2.740   -7.415  0.46 13.30 ?  131 ILE   A O    1 
ATOM   2808 O O    B ILE   A 1 131 ? 18.193 2.449   -9.011  0.54 25.19 ?  131 ILE   A O    1 
ATOM   2809 C CB   A ILE   A 1 131 ? 17.015 4.429   -5.143  0.46 15.28 ?  131 ILE   A CB   1 
ATOM   2810 C CB   B ILE   A 1 131 ? 18.157 4.641   -6.795  0.54 27.98 ?  131 ILE   A CB   1 
ATOM   2811 C CG1  A ILE   A 1 131 ? 18.313 4.286   -4.337  0.46 16.46 ?  131 ILE   A CG1  1 
ATOM   2812 C CG1  B ILE   A 1 131 ? 19.564 4.287   -6.300  0.54 29.57 ?  131 ILE   A CG1  1 
ATOM   2813 C CG2  A ILE   A 1 131 ? 15.975 5.212   -4.360  0.46 15.51 ?  131 ILE   A CG2  1 
ATOM   2814 C CG2  B ILE   A 1 131 ? 17.463 5.622   -5.846  0.54 28.55 ?  131 ILE   A CG2  1 
ATOM   2815 C CD1  A ILE   A 1 131 ? 18.942 5.623   -3.936  0.46 17.07 ?  131 ILE   A CD1  1 
ATOM   2816 C CD1  B ILE   A 1 131 ? 20.594 5.338   -6.619  0.54 30.61 ?  131 ILE   A CD1  1 
ATOM   2817 H H    A ILE   A 1 131 ? 16.104 2.617   -3.655  0.46 15.95 ?  131 ILE   A H    1 
ATOM   2818 H H    B ILE   A 1 131 ? 17.049 3.209   -5.034  0.54 28.82 ?  131 ILE   A H    1 
ATOM   2819 H HA   A ILE   A 1 131 ? 15.721 3.239   -6.162  0.46 16.53 ?  131 ILE   A HA   1 
ATOM   2820 H HA   B ILE   A 1 131 ? 16.543 3.649   -7.546  0.54 30.47 ?  131 ILE   A HA   1 
ATOM   2821 H HB   A ILE   A 1 131 ? 17.216 4.926   -5.953  0.46 18.35 ?  131 ILE   A HB   1 
ATOM   2822 H HB   B ILE   A 1 131 ? 18.243 5.088   -7.652  0.54 33.58 ?  131 ILE   A HB   1 
ATOM   2823 H HG12 A ILE   A 1 131 ? 18.124 3.794   -3.524  0.46 19.77 ?  131 ILE   A HG12 1 
ATOM   2824 H HG12 B ILE   A 1 131 ? 19.531 4.182   -5.341  0.54 35.50 ?  131 ILE   A HG12 1 
ATOM   2825 H HG13 A ILE   A 1 131 ? 18.968 3.808   -4.868  0.46 19.77 ?  131 ILE   A HG13 1 
ATOM   2826 H HG13 B ILE   A 1 131 ? 19.870 3.464   -6.708  0.54 35.50 ?  131 ILE   A HG13 1 
ATOM   2827 H HG21 A ILE   A 1 131 ? 16.271 6.131   -4.275  0.46 18.63 ?  131 ILE   A HG21 1 
ATOM   2828 H HG21 B ILE   A 1 131 ? 17.986 6.438   -5.800  0.54 34.27 ?  131 ILE   A HG21 1 
ATOM   2829 H HG22 A ILE   A 1 131 ? 15.134 5.177   -4.838  0.46 18.63 ?  131 ILE   A HG22 1 
ATOM   2830 H HG22 B ILE   A 1 131 ? 16.576 5.818   -6.187  0.54 34.27 ?  131 ILE   A HG22 1 
ATOM   2831 H HG23 A ILE   A 1 131 ? 15.877 4.810   -3.483  0.46 18.63 ?  131 ILE   A HG23 1 
ATOM   2832 H HG23 B ILE   A 1 131 ? 17.399 5.225   -4.966  0.54 34.27 ?  131 ILE   A HG23 1 
ATOM   2833 H HD11 A ILE   A 1 131 ? 19.816 5.456   -3.542  0.46 20.50 ?  131 ILE   A HD11 1 
ATOM   2834 H HD11 B ILE   A 1 131 ? 21.446 5.057   -6.254  0.54 36.74 ?  131 ILE   A HD11 1 
ATOM   2835 H HD12 A ILE   A 1 131 ? 19.043 6.178   -4.727  0.46 20.50 ?  131 ILE   A HD12 1 
ATOM   2836 H HD12 B ILE   A 1 131 ? 20.660 5.433   -7.583  0.54 36.74 ?  131 ILE   A HD12 1 
ATOM   2837 H HD13 A ILE   A 1 131 ? 18.371 6.067   -3.292  0.46 20.50 ?  131 ILE   A HD13 1 
ATOM   2838 H HD13 B ILE   A 1 131 ? 20.317 6.174   -6.220  0.54 36.74 ?  131 ILE   A HD13 1 
ATOM   2839 N N    A PHE   A 1 132 ? 17.881 1.078   -5.901  0.46 12.10 ?  132 PHE   A N    1 
ATOM   2840 N N    B PHE   A 1 132 ? 18.496 1.239   -7.141  0.54 22.95 ?  132 PHE   A N    1 
ATOM   2841 C CA   A PHE   A 1 132 ? 18.747 0.234   -6.716  0.46 12.64 ?  132 PHE   A CA   1 
ATOM   2842 C CA   B PHE   A 1 132 ? 19.133 0.152   -7.878  0.54 22.53 ?  132 PHE   A CA   1 
ATOM   2843 C C    A PHE   A 1 132 ? 17.996 -0.508  -7.816  0.46 13.73 ?  132 PHE   A C    1 
ATOM   2844 C C    B PHE   A 1 132 ? 18.132 -0.696  -8.654  0.54 21.21 ?  132 PHE   A C    1 
ATOM   2845 O O    A PHE   A 1 132 ? 18.646 -1.127  -8.666  0.46 14.61 ?  132 PHE   A O    1 
ATOM   2846 O O    B PHE   A 1 132 ? 18.536 -1.413  -9.576  0.54 20.90 ?  132 PHE   A O    1 
ATOM   2847 C CB   A PHE   A 1 132 ? 19.529 -0.754  -5.852  0.46 11.93 ?  132 PHE   A CB   1 
ATOM   2848 C CB   B PHE   A 1 132 ? 20.003 -0.703  -6.951  0.54 23.58 ?  132 PHE   A CB   1 
ATOM   2849 C CG   A PHE   A 1 132 ? 20.744 -0.163  -5.196  0.46 12.03 ?  132 PHE   A CG   1 
ATOM   2850 C CG   B PHE   A 1 132 ? 21.359 -0.099  -6.663  0.54 25.45 ?  132 PHE   A CG   1 
ATOM   2851 C CD1  A PHE   A 1 132 ? 20.626 0.880   -4.294  0.46 12.85 ?  132 PHE   A CD1  1 
ATOM   2852 C CD1  B PHE   A 1 132 ? 21.699 1.163   -7.146  0.54 26.47 ?  132 PHE   A CD1  1 
ATOM   2853 C CD2  A PHE   A 1 132 ? 22.002 -0.677  -5.457  0.46 12.91 ?  132 PHE   A CD2  1 
ATOM   2854 C CD2  B PHE   A 1 132 ? 22.297 -0.800  -5.924  0.54 25.84 ?  132 PHE   A CD2  1 
ATOM   2855 C CE1  A PHE   A 1 132 ? 21.744 1.402   -3.668  0.46 13.04 ?  132 PHE   A CE1  1 
ATOM   2856 C CE1  B PHE   A 1 132 ? 22.938 1.711   -6.891  0.54 26.75 ?  132 PHE   A CE1  1 
ATOM   2857 C CE2  A PHE   A 1 132 ? 23.120 -0.160  -4.836  0.46 12.22 ?  132 PHE   A CE2  1 
ATOM   2858 C CE2  B PHE   A 1 132 ? 23.541 -0.254  -5.663  0.54 26.69 ?  132 PHE   A CE2  1 
ATOM   2859 C CZ   A PHE   A 1 132 ? 22.993 0.891   -3.945  0.46 12.09 ?  132 PHE   A CZ   1 
ATOM   2860 C CZ   B PHE   A 1 132 ? 23.863 1.002   -6.148  0.54 26.65 ?  132 PHE   A CZ   1 
ATOM   2861 H H    A PHE   A 1 132 ? 17.685 0.754   -5.129  0.46 14.53 ?  132 PHE   A H    1 
ATOM   2862 H H    B PHE   A 1 132 ? 18.464 1.135   -6.287  0.54 27.56 ?  132 PHE   A H    1 
ATOM   2863 H HA   A PHE   A 1 132 ? 19.400 0.802   -7.150  0.46 15.18 ?  132 PHE   A HA   1 
ATOM   2864 H HA   B PHE   A 1 132 ? 19.708 0.541   -8.551  0.54 27.05 ?  132 PHE   A HA   1 
ATOM   2865 H HB2  A PHE   A 1 132 ? 18.944 -1.086  -5.151  0.46 14.34 ?  132 PHE   A HB2  1 
ATOM   2866 H HB2  B PHE   A 1 132 ? 19.547 -0.818  -6.102  0.54 28.31 ?  132 PHE   A HB2  1 
ATOM   2867 H HB3  A PHE   A 1 132 ? 19.822 -1.494  -6.408  0.46 14.34 ?  132 PHE   A HB3  1 
ATOM   2868 H HB3  B PHE   A 1 132 ? 20.146 -1.567  -7.367  0.54 28.31 ?  132 PHE   A HB3  1 
ATOM   2869 H HD1  A PHE   A 1 132 ? 19.787 1.225   -4.096  0.46 15.43 ?  132 PHE   A HD1  1 
ATOM   2870 H HD1  B PHE   A 1 132 ? 21.080 1.644   -7.649  0.54 31.78 ?  132 PHE   A HD1  1 
ATOM   2871 H HD2  A PHE   A 1 132 ? 22.095 -1.386  -6.051  0.46 15.50 ?  132 PHE   A HD2  1 
ATOM   2872 H HD2  B PHE   A 1 132 ? 22.086 -1.647  -5.594  0.54 31.02 ?  132 PHE   A HD2  1 
ATOM   2873 H HE1  A PHE   A 1 132 ? 21.654 2.108   -3.065  0.46 15.66 ?  132 PHE   A HE1  1 
ATOM   2874 H HE1  B PHE   A 1 132 ? 23.149 2.557   -7.221  0.54 32.11 ?  132 PHE   A HE1  1 
ATOM   2875 H HE2  A PHE   A 1 132 ? 23.961 -0.509  -5.025  0.46 14.68 ?  132 PHE   A HE2  1 
ATOM   2876 H HE2  B PHE   A 1 132 ? 24.162 -0.732  -5.162  0.54 32.05 ?  132 PHE   A HE2  1 
ATOM   2877 H HZ   A PHE   A 1 132 ? 23.746 1.245   -3.528  0.46 14.53 ?  132 PHE   A HZ   1 
ATOM   2878 H HZ   B PHE   A 1 132 ? 24.698 1.369   -5.972  0.54 31.99 ?  132 PHE   A HZ   1 
ATOM   2879 N N    A GLY   A 1 133 ? 16.662 -0.487  -7.809  0.46 14.11 ?  133 GLY   A N    1 
ATOM   2880 N N    B GLY   A 1 133 ? 16.850 -0.640  -8.300  0.54 20.07 ?  133 GLY   A N    1 
ATOM   2881 C CA   A GLY   A 1 133 ? 15.886 -0.835  -8.984  0.46 15.07 ?  133 GLY   A CA   1 
ATOM   2882 C CA   B GLY   A 1 133 ? 15.796 -1.054  -9.200  0.54 19.72 ?  133 GLY   A CA   1 
ATOM   2883 C C    A GLY   A 1 133 ? 15.561 -2.296  -9.204  0.46 16.52 ?  133 GLY   A C    1 
ATOM   2884 C C    B GLY   A 1 133 ? 15.411 -2.521  -9.203  0.54 19.62 ?  133 GLY   A C    1 
ATOM   2885 O O    A GLY   A 1 133 ? 14.979 -2.616  -10.246 0.46 17.91 ?  133 GLY   A O    1 
ATOM   2886 O O    B GLY   A 1 133 ? 14.525 -2.898  -9.980  0.54 20.92 ?  133 GLY   A O    1 
ATOM   2887 H H    A GLY   A 1 133 ? 16.180 -0.263  -7.128  0.46 16.94 ?  133 GLY   A H    1 
ATOM   2888 H H    B GLY   A 1 133 ? 16.573 -0.358  -7.533  0.54 24.10 ?  133 GLY   A H    1 
ATOM   2889 H HA2  A GLY   A 1 133 ? 15.034 -0.368  -8.942  0.46 18.09 ?  133 GLY   A HA2  1 
ATOM   2890 H HA2  B GLY   A 1 133 ? 15.001 -0.543  -8.986  0.54 23.68 ?  133 GLY   A HA2  1 
ATOM   2891 H HA3  A GLY   A 1 133 ? 16.353 -0.514  -9.771  0.46 18.09 ?  133 GLY   A HA3  1 
ATOM   2892 H HA3  B GLY   A 1 133 ? 16.063 -0.817  -10.102 0.54 23.68 ?  133 GLY   A HA3  1 
ATOM   2893 N N    A ALA   A 1 134 ? 15.887 -3.189  -8.272  0.46 16.15 ?  134 ALA   A N    1 
ATOM   2894 N N    B ALA   A 1 134 ? 16.023 -3.362  -8.373  0.54 18.20 ?  134 ALA   A N    1 
ATOM   2895 C CA   A ALA   A 1 134 ? 15.545 -4.594  -8.449  0.46 17.42 ?  134 ALA   A CA   1 
ATOM   2896 C CA   B ALA   A 1 134 ? 15.645 -4.771  -8.373  0.54 18.38 ?  134 ALA   A CA   1 
ATOM   2897 C C    A ALA   A 1 134 ? 14.186 -4.910  -7.823  0.46 17.50 ?  134 ALA   A C    1 
ATOM   2898 C C    B ALA   A 1 134 ? 14.286 -4.966  -7.713  0.54 18.87 ?  134 ALA   A C    1 
ATOM   2899 O O    A ALA   A 1 134 ? 13.607 -4.110  -7.085  0.46 18.71 ?  134 ALA   A O    1 
ATOM   2900 O O    B ALA   A 1 134 ? 13.891 -4.216  -6.815  0.54 19.96 ?  134 ALA   A O    1 
ATOM   2901 C CB   A ALA   A 1 134 ? 16.623 -5.498  -7.855  0.46 18.71 ?  134 ALA   A CB   1 
ATOM   2902 C CB   B ALA   A 1 134 ? 16.678 -5.618  -7.636  0.54 19.37 ?  134 ALA   A CB   1 
ATOM   2903 H H    A ALA   A 1 134 ? 16.293 -3.003  -7.535  0.46 19.40 ?  134 ALA   A H    1 
ATOM   2904 H H    B ALA   A 1 134 ? 16.642 -3.149  -7.812  0.54 21.86 ?  134 ALA   A H    1 
ATOM   2905 H HA   A ALA   A 1 134 ? 15.489 -4.785  -9.398  0.46 20.92 ?  134 ALA   A HA   1 
ATOM   2906 H HA   B ALA   A 1 134 ? 15.587 -5.081  -9.291  0.54 22.07 ?  134 ALA   A HA   1 
ATOM   2907 H HB1  A ALA   A 1 134 ? 16.376 -6.423  -8.010  0.46 22.47 ?  134 ALA   A HB1  1 
ATOM   2908 H HB1  B ALA   A 1 134 ? 16.396 -6.546  -7.662  0.54 23.26 ?  134 ALA   A HB1  1 
ATOM   2909 H HB2  A ALA   A 1 134 ? 17.471 -5.306  -8.287  0.46 22.47 ?  134 ALA   A HB2  1 
ATOM   2910 H HB2  B ALA   A 1 134 ? 17.535 -5.518  -8.077  0.54 23.26 ?  134 ALA   A HB2  1 
ATOM   2911 H HB3  A ALA   A 1 134 ? 16.691 -5.327  -6.904  0.46 22.47 ?  134 ALA   A HB3  1 
ATOM   2912 H HB3  B ALA   A 1 134 ? 16.737 -5.313  -6.719  0.54 23.26 ?  134 ALA   A HB3  1 
ATOM   2913 N N    A ASP   A 1 135 ? 13.677 -6.095  -8.137  0.46 17.98 ?  135 ASP   A N    1 
ATOM   2914 N N    B ASP   A 1 135 ? 13.577 -5.999  -8.161  0.54 19.36 ?  135 ASP   A N    1 
ATOM   2915 C CA   A ASP   A 1 135 ? 12.430 -6.596  -7.569  0.46 18.00 ?  135 ASP   A CA   1 
ATOM   2916 C CA   B ASP   A 1 135 ? 12.284 -6.345  -7.589  0.54 19.96 ?  135 ASP   A CA   1 
ATOM   2917 C C    A ASP   A 1 135 ? 12.669 -7.020  -6.127  0.46 17.53 ?  135 ASP   A C    1 
ATOM   2918 C C    B ASP   A 1 135 ? 12.485 -6.794  -6.146  0.54 19.10 ?  135 ASP   A C    1 
ATOM   2919 O O    A ASP   A 1 135 ? 13.396 -7.995  -5.898  0.46 18.36 ?  135 ASP   A O    1 
ATOM   2920 O O    B ASP   A 1 135 ? 13.269 -7.719  -5.899  0.54 19.54 ?  135 ASP   A O    1 
ATOM   2921 C CB   A ASP   A 1 135 ? 11.948 -7.794  -8.391  0.46 20.02 ?  135 ASP   A CB   1 
ATOM   2922 C CB   B ASP   A 1 135 ? 11.660 -7.469  -8.417  0.54 22.58 ?  135 ASP   A CB   1 
ATOM   2923 C CG   A ASP   A 1 135 ? 10.690 -8.450  -7.823  0.46 22.05 ?  135 ASP   A CG   1 
ATOM   2924 C CG   B ASP   A 1 135 ? 10.189 -7.701  -8.093  0.54 25.81 ?  135 ASP   A CG   1 
ATOM   2925 O OD1  A ASP   A 1 135 ? 10.091 -7.913  -6.870  0.46 20.60 ?  135 ASP   A OD1  1 
ATOM   2926 O OD1  B ASP   A 1 135 ? 9.649  -7.029  -7.189  0.54 27.86 ?  135 ASP   A OD1  1 
ATOM   2927 O OD2  A ASP   A 1 135 ? 10.305 -9.525  -8.335  0.46 25.27 -1 135 ASP   A OD2  1 
ATOM   2928 O OD2  B ASP   A 1 135 ? 9.570  -8.563  -8.751  0.54 26.71 -1 135 ASP   A OD2  1 
ATOM   2929 H H    A ASP   A 1 135 ? 14.043 -6.641  -8.689  0.46 21.59 ?  135 ASP   A H    1 
ATOM   2930 H H    B ASP   A 1 135 ? 13.826 -6.527  -8.795  0.54 23.25 ?  135 ASP   A H    1 
ATOM   2931 H HA   A ASP   A 1 135 ? 11.756 -5.906  -7.601  0.46 21.61 ?  135 ASP   A HA   1 
ATOM   2932 H HA   B ASP   A 1 135 ? 11.696 -5.573  -7.628  0.54 23.96 ?  135 ASP   A HA   1 
ATOM   2933 H HB2  A ASP   A 1 135 ? 11.763 -7.499  -9.295  0.46 24.04 ?  135 ASP   A HB2  1 
ATOM   2934 H HB2  B ASP   A 1 135 ? 11.745 -7.253  -9.363  0.54 27.11 ?  135 ASP   A HB2  1 
ATOM   2935 H HB3  A ASP   A 1 135 ? 12.634 -8.475  -8.394  0.46 24.04 ?  135 ASP   A HB3  1 
ATOM   2936 H HB3  B ASP   A 1 135 ? 12.120 -8.300  -8.228  0.54 27.11 ?  135 ASP   A HB3  1 
ATOM   2937 N N    A PRO   A 1 136 ? 12.103 -6.332  -5.133  0.46 17.16 ?  136 PRO   A N    1 
ATOM   2938 N N    B PRO   A 1 136 ? 11.821 -6.173  -5.169  0.54 19.56 ?  136 PRO   A N    1 
ATOM   2939 C CA   A PRO   A 1 136 ? 12.345 -6.743  -3.738  0.46 17.28 ?  136 PRO   A CA   1 
ATOM   2940 C CA   B PRO   A 1 136 ? 12.033 -6.572  -3.765  0.54 20.05 ?  136 PRO   A CA   1 
ATOM   2941 C C    A PRO   A 1 136 ? 11.880 -8.153  -3.421  0.46 16.48 ?  136 PRO   A C    1 
ATOM   2942 C C    B PRO   A 1 136 ? 11.745 -8.035  -3.474  0.54 19.78 ?  136 PRO   A C    1 
ATOM   2943 O O    A PRO   A 1 136 ? 12.478 -8.802  -2.554  0.46 15.23 ?  136 PRO   A O    1 
ATOM   2944 O O    B PRO   A 1 136 ? 12.437 -8.631  -2.640  0.54 18.43 ?  136 PRO   A O    1 
ATOM   2945 C CB   A PRO   A 1 136 ? 11.598 -5.681  -2.918  0.46 18.19 ?  136 PRO   A CB   1 
ATOM   2946 C CB   B PRO   A 1 136 ? 11.095 -5.631  -2.994  0.54 21.18 ?  136 PRO   A CB   1 
ATOM   2947 C CG   A PRO   A 1 136 ? 10.665 -5.033  -3.882  0.46 19.47 ?  136 PRO   A CG   1 
ATOM   2948 C CG   B PRO   A 1 136 ? 10.122 -5.131  -4.030  0.54 22.71 ?  136 PRO   A CG   1 
ATOM   2949 C CD   A PRO   A 1 136 ? 11.309 -5.098  -5.219  0.46 18.87 ?  136 PRO   A CD   1 
ATOM   2950 C CD   B PRO   A 1 136 ? 10.910 -5.027  -5.278  0.54 21.36 ?  136 PRO   A CD   1 
ATOM   2951 H HA   A PRO   A 1 136 ? 13.295 -6.676  -3.532  0.46 20.76 ?  136 PRO   A HA   1 
ATOM   2952 H HA   B PRO   A 1 136 ? 12.949 -6.385  -3.501  0.54 24.08 ?  136 PRO   A HA   1 
ATOM   2953 H HB2  A PRO   A 1 136 ? 11.107 -6.110  -2.202  0.46 21.84 ?  136 PRO   A HB2  1 
ATOM   2954 H HB2  B PRO   A 1 136 ? 10.635 -6.124  -2.298  0.54 25.43 ?  136 PRO   A HB2  1 
ATOM   2955 H HB3  A PRO   A 1 136 ? 12.228 -5.034  -2.567  0.46 21.84 ?  136 PRO   A HB3  1 
ATOM   2956 H HB3  B PRO   A 1 136 ? 11.608 -4.897  -2.618  0.54 25.43 ?  136 PRO   A HB3  1 
ATOM   2957 H HG2  A PRO   A 1 136 ? 9.821  -5.516  -3.894  0.46 23.37 ?  136 PRO   A HG2  1 
ATOM   2958 H HG2  B PRO   A 1 136 ? 9.402  -5.770  -4.138  0.54 27.27 ?  136 PRO   A HG2  1 
ATOM   2959 H HG3  A PRO   A 1 136 ? 10.519 -4.109  -3.627  0.46 23.37 ?  136 PRO   A HG3  1 
ATOM   2960 H HG3  B PRO   A 1 136 ? 9.785  -4.263  -3.773  0.54 27.27 ?  136 PRO   A HG3  1 
ATOM   2961 H HD2  A PRO   A 1 136 ? 10.638 -5.182  -5.919  0.46 22.66 ?  136 PRO   A HD2  1 
ATOM   2962 H HD2  B PRO   A 1 136 ? 10.339 -5.117  -6.054  0.54 25.64 ?  136 PRO   A HD2  1 
ATOM   2963 H HD3  A PRO   A 1 136 ? 11.883 -4.330  -5.369  0.46 22.66 ?  136 PRO   A HD3  1 
ATOM   2964 H HD3  B PRO   A 1 136 ? 11.420 -4.199  -5.304  0.54 25.64 ?  136 PRO   A HD3  1 
ATOM   2965 N N    A ILE   A 1 137 ? 10.832 -8.648  -4.086  0.46 16.69 ?  137 ILE   A N    1 
ATOM   2966 N N    B ILE   A 1 137 ? 10.737 -8.630  -4.120  0.54 20.36 ?  137 ILE   A N    1 
ATOM   2967 C CA   A ILE   A 1 137 ? 10.441 -10.043 -3.903  0.46 16.93 ?  137 ILE   A CA   1 
ATOM   2968 C CA   B ILE   A 1 137 ? 10.438 -10.038 -3.867  0.54 20.91 ?  137 ILE   A CA   1 
ATOM   2969 C C    A ILE   A 1 137 ? 11.581 -10.967 -4.308  0.46 16.75 ?  137 ILE   A C    1 
ATOM   2970 C C    B ILE   A 1 137 ? 11.615 -10.900 -4.295  0.54 19.53 ?  137 ILE   A C    1 
ATOM   2971 O O    A ILE   A 1 137 ? 11.881 -11.949 -3.618  0.46 16.29 ?  137 ILE   A O    1 
ATOM   2972 O O    B ILE   A 1 137 ? 11.983 -11.864 -3.613  0.54 19.13 ?  137 ILE   A O    1 
ATOM   2973 C CB   A ILE   A 1 137 ? 9.147  -10.354 -4.678  0.46 18.70 ?  137 ILE   A CB   1 
ATOM   2974 C CB   B ILE   A 1 137 ? 9.138  -10.478 -4.569  0.54 23.82 ?  137 ILE   A CB   1 
ATOM   2975 C CG1  A ILE   A 1 137 ? 7.969  -9.603  -4.055  0.46 20.62 ?  137 ILE   A CG1  1 
ATOM   2976 C CG1  B ILE   A 1 137 ? 8.084  -9.369  -4.563  0.54 25.85 ?  137 ILE   A CG1  1 
ATOM   2977 C CG2  A ILE   A 1 137 ? 8.902  -11.865 -4.714  0.46 17.84 ?  137 ILE   A CG2  1 
ATOM   2978 C CG2  B ILE   A 1 137 ? 8.591  -11.731 -3.896  0.54 24.69 ?  137 ILE   A CG2  1 
ATOM   2979 C CD1  A ILE   A 1 137 ? 6.674  -9.766  -4.806  0.46 22.85 ?  137 ILE   A CD1  1 
ATOM   2980 C CD1  B ILE   A 1 137 ? 6.829  -9.743  -5.315  0.54 27.28 ?  137 ILE   A CD1  1 
ATOM   2981 H H    A ILE   A 1 137 ? 10.345 -8.199  -4.636  0.46 20.05 ?  137 ILE   A H    1 
ATOM   2982 H H    B ILE   A 1 137 ? 10.244 -8.246  -4.708  0.54 24.44 ?  137 ILE   A H    1 
ATOM   2983 H HA   A ILE   A 1 137 ? 10.266 -10.188 -2.963  0.46 20.33 ?  137 ILE   A HA   1 
ATOM   2984 H HA   B ILE   A 1 137 ? 10.314 -10.166 -2.916  0.54 25.10 ?  137 ILE   A HA   1 
ATOM   2985 H HB   A ILE   A 1 137 ? 9.256  -10.039 -5.588  0.46 22.45 ?  137 ILE   A HB   1 
ATOM   2986 H HB   B ILE   A 1 137 ? 9.343  -10.699 -5.489  0.54 28.60 ?  137 ILE   A HB   1 
ATOM   2987 H HG12 A ILE   A 1 137 ? 7.832  -9.924  -3.152  0.46 24.76 ?  137 ILE   A HG12 1 
ATOM   2988 H HG12 B ILE   A 1 137 ? 7.848  -9.164  -3.645  0.54 31.03 ?  137 ILE   A HG12 1 
ATOM   2989 H HG13 A ILE   A 1 137 ? 8.179  -8.651  -4.034  0.46 24.76 ?  137 ILE   A HG13 1 
ATOM   2990 H HG13 B ILE   A 1 137 ? 8.440  -8.578  -4.997  0.54 31.03 ?  137 ILE   A HG13 1 
ATOM   2991 H HG21 A ILE   A 1 137 ? 8.035  -12.040 -5.113  0.46 21.42 ?  137 ILE   A HG21 1 
ATOM   2992 H HG21 B ILE   A 1 137 ? 7.901  -12.119 -4.457  0.54 29.64 ?  137 ILE   A HG21 1 
ATOM   2993 H HG22 A ILE   A 1 137 ? 9.587  -12.286 -5.249  0.46 21.42 ?  137 ILE   A HG22 1 
ATOM   2994 H HG22 B ILE   A 1 137 ? 9.314  -12.365 -3.774  0.54 29.64 ?  137 ILE   A HG22 1 
ATOM   2995 H HG23 A ILE   A 1 137 ? 8.922  -12.207 -3.809  0.46 21.42 ?  137 ILE   A HG23 1 
ATOM   2996 H HG23 B ILE   A 1 137 ? 8.217  -11.487 -3.034  0.54 29.64 ?  137 ILE   A HG23 1 
ATOM   2997 H HD11 A ILE   A 1 137 ? 5.987  -9.286  -4.327  0.46 27.43 ?  137 ILE   A HD11 1 
ATOM   2998 H HD11 B ILE   A 1 137 ? 6.274  -8.955  -5.413  0.54 32.75 ?  137 ILE   A HD11 1 
ATOM   2999 H HD12 A ILE   A 1 137 ? 6.774  -9.404  -5.703  0.46 27.43 ?  137 ILE   A HD12 1 
ATOM   3000 H HD12 B ILE   A 1 137 ? 7.076  -10.085 -6.190  0.54 32.75 ?  137 ILE   A HD12 1 
ATOM   3001 H HD13 A ILE   A 1 137 ? 6.438  -10.705 -4.853  0.46 27.43 ?  137 ILE   A HD13 1 
ATOM   3002 H HD13 B ILE   A 1 137 ? 6.353  -10.425 -4.817  0.54 32.75 ?  137 ILE   A HD13 1 
ATOM   3003 N N    A HIS   A 1 138 ? 12.230 -10.670 -5.435  0.46 17.07 ?  138 HIS   A N    1 
ATOM   3004 N N    B HIS   A 1 138 ? 12.220 -10.566 -5.435  0.54 18.69 ?  138 HIS   A N    1 
ATOM   3005 C CA   A HIS   A 1 138 ? 13.369 -11.475 -5.858  0.46 16.72 ?  138 HIS   A CA   1 
ATOM   3006 C CA   B HIS   A 1 138 ? 13.406 -11.285 -5.881  0.54 17.40 ?  138 HIS   A CA   1 
ATOM   3007 C C    A HIS   A 1 138 ? 14.511 -11.373 -4.859  0.46 16.13 ?  138 HIS   A C    1 
ATOM   3008 C C    B HIS   A 1 138 ? 14.539 -11.133 -4.872  0.54 16.23 ?  138 HIS   A C    1 
ATOM   3009 O O    A HIS   A 1 138 ? 15.168 -12.374 -4.547  0.46 16.91 ?  138 HIS   A O    1 
ATOM   3010 O O    B HIS   A 1 138 ? 15.182 -12.115 -4.484  0.54 16.15 ?  138 HIS   A O    1 
ATOM   3011 C CB   A HIS   A 1 138 ? 13.841 -11.037 -7.241  0.46 17.85 ?  138 HIS   A CB   1 
ATOM   3012 C CB   B HIS   A 1 138 ? 13.827 -10.770 -7.257  0.54 18.97 ?  138 HIS   A CB   1 
ATOM   3013 C CG   A HIS   A 1 138 ? 15.090 -11.728 -7.688  0.46 18.38 ?  138 HIS   A CG   1 
ATOM   3014 C CG   B HIS   A 1 138 ? 15.066 -11.419 -7.785  0.54 20.30 ?  138 HIS   A CG   1 
ATOM   3015 N ND1  A HIS   A 1 138 ? 15.159 -13.091 -7.877  0.46 19.49 ?  138 HIS   A ND1  1 
ATOM   3016 N ND1  B HIS   A 1 138 ? 15.121 -12.753 -8.123  0.54 21.44 ?  138 HIS   A ND1  1 
ATOM   3017 C CD2  A HIS   A 1 138 ? 16.325 -11.247 -7.965  0.46 18.33 ?  138 HIS   A CD2  1 
ATOM   3018 C CD2  B HIS   A 1 138 ? 16.303 -10.922 -8.016  0.54 21.10 ?  138 HIS   A CD2  1 
ATOM   3019 C CE1  A HIS   A 1 138 ? 16.379 -13.420 -8.261  0.46 19.19 ?  138 HIS   A CE1  1 
ATOM   3020 C CE1  B HIS   A 1 138 ? 16.337 -13.049 -8.546  0.54 21.36 ?  138 HIS   A CE1  1 
ATOM   3021 N NE2  A HIS   A 1 138 ? 17.108 -12.320 -8.318  0.46 18.81 ?  138 HIS   A NE2  1 
ATOM   3022 N NE2  B HIS   A 1 138 ? 17.074 -11.954 -8.491  0.54 21.50 ?  138 HIS   A NE2  1 
ATOM   3023 H H    A HIS   A 1 138 ? 12.038 -10.016 -5.961  0.46 20.50 ?  138 HIS   A H    1 
ATOM   3024 H H    B HIS   A 1 138 ? 11.967 -9.932  -5.960  0.54 22.45 ?  138 HIS   A H    1 
ATOM   3025 H HA   A HIS   A 1 138 ? 13.103 -12.401 -5.909  0.46 20.08 ?  138 HIS   A HA   1 
ATOM   3026 H HA   B HIS   A 1 138 ? 13.193 -12.227 -5.964  0.54 20.89 ?  138 HIS   A HA   1 
ATOM   3027 H HB2  A HIS   A 1 138 ? 13.144 -11.233 -7.884  0.46 21.44 ?  138 HIS   A HB2  1 
ATOM   3028 H HB2  B HIS   A 1 138 ? 13.109 -10.941 -7.889  0.54 22.77 ?  138 HIS   A HB2  1 
ATOM   3029 H HB3  A HIS   A 1 138 ? 14.018 -10.081 -7.226  0.46 21.44 ?  138 HIS   A HB3  1 
ATOM   3030 H HB3  B HIS   A 1 138 ? 13.994 -9.817  -7.199  0.54 22.77 ?  138 HIS   A HB3  1 
ATOM   3031 H HD1  A HIS   A 1 138 ? 14.506 -13.639 -7.769  0.46 23.41 ?  138 HIS   A HD1  1 
ATOM   3032 H HD2  A HIS   A 1 138 ? 16.593 -10.355 -7.924  0.46 22.01 ?  138 HIS   A HD2  1 
ATOM   3033 H HD2  B HIS   A 1 138 ? 16.576 -10.045 -7.880  0.54 25.34 ?  138 HIS   A HD2  1 
ATOM   3034 H HE1  A HIS   A 1 138 ? 16.674 -14.278 -8.458  0.46 23.05 ?  138 HIS   A HE1  1 
ATOM   3035 H HE1  B HIS   A 1 138 ? 16.625 -13.887 -8.833  0.54 25.64 ?  138 HIS   A HE1  1 
ATOM   3036 H HE2  B HIS   A 1 138 ? 17.901 -11.898 -8.717  0.54 25.82 ?  138 HIS   A HE2  1 
ATOM   3037 N N    A SER   A 1 139 ? 14.766 -10.168 -4.347  0.46 16.01 ?  139 SER   A N    1 
ATOM   3038 N N    B SER   A 1 139 ? 14.789 -9.902  -4.424  0.54 16.13 ?  139 SER   A N    1 
ATOM   3039 C CA   A SER   A 1 139 ? 15.870 -9.989  -3.411  0.46 16.07 ?  139 SER   A CA   1 
ATOM   3040 C CA   B SER   A 1 139 ? 15.859 -9.673  -3.457  0.54 15.77 ?  139 SER   A CA   1 
ATOM   3041 C C    A SER   A 1 139 ? 15.671 -10.835 -2.160  0.46 16.30 ?  139 SER   A C    1 
ATOM   3042 C C    B SER   A 1 139 ? 15.628 -10.466 -2.176  0.54 14.89 ?  139 SER   A C    1 
ATOM   3043 O O    A SER   A 1 139 ? 16.631 -11.398 -1.622  0.46 16.38 ?  139 SER   A O    1 
ATOM   3044 O O    B SER   A 1 139 ? 16.556 -11.096 -1.654  0.54 14.68 ?  139 SER   A O    1 
ATOM   3045 C CB   A SER   A 1 139 ? 16.023 -8.513  -3.048  0.46 15.21 ?  139 SER   A CB   1 
ATOM   3046 C CB   B SER   A 1 139 ? 15.990 -8.180  -3.159  0.54 14.88 ?  139 SER   A CB   1 
ATOM   3047 O OG   A SER   A 1 139 ? 17.137 -8.354  -2.186  0.46 15.30 ?  139 SER   A OG   1 
ATOM   3048 O OG   B SER   A 1 139 ? 17.069 -7.917  -2.277  0.54 15.94 ?  139 SER   A OG   1 
ATOM   3049 H H    A SER   A 1 139 ? 14.321 -9.451  -4.507  0.46 19.23 ?  139 SER   A H    1 
ATOM   3050 H H    B SER   A 1 139 ? 14.362 -9.198  -4.657  0.54 19.37 ?  139 SER   A H    1 
ATOM   3051 H HA   A SER   A 1 139 ? 16.698 -10.270 -3.829  0.46 19.30 ?  139 SER   A HA   1 
ATOM   3052 H HA   B SER   A 1 139 ? 16.695 -9.978  -3.834  0.54 18.93 ?  139 SER   A HA   1 
ATOM   3053 H HB2  A SER   A 1 139 ? 16.156 -7.993  -3.860  0.46 18.26 ?  139 SER   A HB2  1 
ATOM   3054 H HB2  B SER   A 1 139 ? 16.175 -7.714  -3.983  0.54 17.87 ?  139 SER   A HB2  1 
ATOM   3055 H HB3  A SER   A 1 139 ? 15.222 -8.205  -2.591  0.46 18.26 ?  139 SER   A HB3  1 
ATOM   3056 H HB3  B SER   A 1 139 ? 15.153 -7.863  -2.777  0.54 17.87 ?  139 SER   A HB3  1 
ATOM   3057 H HG   A SER   A 1 139 ? 17.850 -8.504  -2.600  0.46 18.38 ?  139 SER   A HG   1 
ATOM   3058 H HG   B SER   A 1 139 ? 17.093 -7.095  -2.083  0.54 19.14 ?  139 SER   A HG   1 
ATOM   3059 N N    A LEU   A 1 140 ? 14.427 -10.941 -1.684  0.46 15.46 ?  140 LEU   A N    1 
ATOM   3060 N N    B LEU   A 1 140 ? 14.394 -10.467 -1.660  0.54 14.84 ?  140 LEU   A N    1 
ATOM   3061 C CA   A LEU   A 1 140 ? 14.148 -11.775 -0.518  0.46 14.34 ?  140 LEU   A CA   1 
ATOM   3062 C CA   B LEU   A 1 140 ? 14.101 -11.250 -0.462  0.54 14.86 ?  140 LEU   A CA   1 
ATOM   3063 C C    A LEU   A 1 140 ? 14.413 -13.241 -0.825  0.46 14.21 ?  140 LEU   A C    1 
ATOM   3064 C C    B LEU   A 1 140 ? 14.355 -12.736 -0.698  0.54 15.11 ?  140 LEU   A C    1 
ATOM   3065 O O    A LEU   A 1 140 ? 14.964 -13.969 0.010   0.46 14.22 ?  140 LEU   A O    1 
ATOM   3066 O O    B LEU   A 1 140 ? 14.899 -13.427 0.173   0.54 15.34 ?  140 LEU   A O    1 
ATOM   3067 C CB   A LEU   A 1 140 ? 12.702 -11.582 -0.059  0.46 14.63 ?  140 LEU   A CB   1 
ATOM   3068 C CB   B LEU   A 1 140 ? 12.660 -11.002 -0.008  0.54 14.87 ?  140 LEU   A CB   1 
ATOM   3069 C CG   A LEU   A 1 140 ? 12.303 -12.449 1.140   0.46 14.77 ?  140 LEU   A CG   1 
ATOM   3070 C CG   B LEU   A 1 140 ? 12.170 -11.818 1.192   0.54 15.30 ?  140 LEU   A CG   1 
ATOM   3071 C CD1  A LEU   A 1 140 ? 13.238 -12.228 2.327   0.46 15.31 ?  140 LEU   A CD1  1 
ATOM   3072 C CD1  B LEU   A 1 140 ? 13.092 -11.646 2.383   0.54 15.58 ?  140 LEU   A CD1  1 
ATOM   3073 C CD2  A LEU   A 1 140 ? 10.856 -12.182 1.521   0.46 14.64 ?  140 LEU   A CD2  1 
ATOM   3074 C CD2  B LEU   A 1 140 ? 10.747 -11.430 1.556   0.54 15.81 ?  140 LEU   A CD2  1 
ATOM   3075 H H    A LEU   A 1 140 ? 13.745 -10.539 -2.008  0.46 18.57 ?  140 LEU   A H    1 
ATOM   3076 H H    B LEU   A 1 140 ? 13.722 -10.033 -1.974  0.54 17.82 ?  140 LEU   A H    1 
ATOM   3077 H HA   A LEU   A 1 140 ? 14.734 -11.508 0.210   0.46 17.23 ?  140 LEU   A HA   1 
ATOM   3078 H HA   B LEU   A 1 140 ? 14.687 -10.958 0.257   0.54 17.84 ?  140 LEU   A HA   1 
ATOM   3079 H HB2  A LEU   A 1 140 ? 12.577 -10.654 0.191   0.46 17.57 ?  140 LEU   A HB2  1 
ATOM   3080 H HB2  B LEU   A 1 140 ? 12.572 -10.061 0.231   0.54 17.86 ?  140 LEU   A HB2  1 
ATOM   3081 H HB3  A LEU   A 1 140 ? 12.113 -11.806 -0.796  0.46 17.57 ?  140 LEU   A HB3  1 
ATOM   3082 H HB3  B LEU   A 1 140 ? 12.067 -11.197 -0.748  0.54 17.86 ?  140 LEU   A HB3  1 
ATOM   3083 H HG   A LEU   A 1 140 ? 12.368 -13.382 0.884   0.46 17.73 ?  140 LEU   A HG   1 
ATOM   3084 H HG   B LEU   A 1 140 ? 12.168 -12.754 0.953   0.54 18.37 ?  140 LEU   A HG   1 
ATOM   3085 H HD11 A LEU   A 1 140 ? 12.866 -12.664 3.108   0.46 18.38 ?  140 LEU   A HD11 1 
ATOM   3086 H HD11 B LEU   A 1 140 ? 12.695 -12.080 3.154   0.54 18.71 ?  140 LEU   A HD11 1 
ATOM   3087 H HD12 A LEU   A 1 140 ? 14.110 -12.606 2.121   0.46 18.38 ?  140 LEU   A HD12 1 
ATOM   3088 H HD12 B LEU   A 1 140 ? 13.949 -12.054 2.180   0.54 18.71 ?  140 LEU   A HD12 1 
ATOM   3089 H HD13 A LEU   A 1 140 ? 13.324 -11.274 2.490   0.46 18.38 ?  140 LEU   A HD13 1 
ATOM   3090 H HD13 B LEU   A 1 140 ? 13.209 -10.699 2.560   0.54 18.71 ?  140 LEU   A HD13 1 
ATOM   3091 H HD21 A LEU   A 1 140 ? 10.620 -12.740 2.279   0.46 17.59 ?  140 LEU   A HD21 1 
ATOM   3092 H HD21 B LEU   A 1 140 ? 10.459 -11.961 2.316   0.54 18.99 ?  140 LEU   A HD21 1 
ATOM   3093 H HD22 A LEU   A 1 140 ? 10.755 -11.246 1.756   0.46 17.59 ?  140 LEU   A HD22 1 
ATOM   3094 H HD22 B LEU   A 1 140 ? 10.721 -10.487 1.784   0.54 18.99 ?  140 LEU   A HD22 1 
ATOM   3095 H HD23 A LEU   A 1 140 ? 10.283 -12.395 0.765   0.46 17.59 ?  140 LEU   A HD23 1 
ATOM   3096 H HD23 B LEU   A 1 140 ? 10.168 -11.602 0.796   0.54 18.99 ?  140 LEU   A HD23 1 
ATOM   3097 N N    A ARG   A 1 141 ? 14.023 -13.690 -2.016  0.46 14.64 ?  141 ARG   A N    1 
ATOM   3098 N N    B ARG   A 1 141 ? 13.979 -13.240 -1.876  0.54 15.81 ?  141 ARG   A N    1 
ATOM   3099 C CA   A ARG   A 1 141 ? 14.291 -15.065 -2.418  0.46 15.91 ?  141 ARG   A CA   1 
ATOM   3100 C CA   B ARG   A 1 141 ? 14.162 -14.658 -2.175  0.54 17.62 ?  141 ARG   A CA   1 
ATOM   3101 C C    A ARG   A 1 141 ? 15.786 -15.347 -2.388  0.46 15.65 ?  141 ARG   A C    1 
ATOM   3102 C C    B ARG   A 1 141 ? 15.642 -15.021 -2.277  0.54 17.03 ?  141 ARG   A C    1 
ATOM   3103 O O    A ARG   A 1 141 ? 16.235 -16.339 -1.802  0.46 16.11 ?  141 ARG   A O    1 
ATOM   3104 O O    B ARG   A 1 141 ? 16.068 -16.054 -1.747  0.54 17.36 ?  141 ARG   A O    1 
ATOM   3105 C CB   A ARG   A 1 141 ? 13.735 -15.287 -3.824  0.46 17.89 ?  141 ARG   A CB   1 
ATOM   3106 C CB   B ARG   A 1 141 ? 13.401 -15.027 -3.453  0.54 19.96 ?  141 ARG   A CB   1 
ATOM   3107 C CG   A ARG   A 1 141 ? 13.697 -16.726 -4.266  0.46 18.97 ?  141 ARG   A CG   1 
ATOM   3108 C CG   B ARG   A 1 141 ? 12.004 -15.584 -3.216  0.54 23.68 ?  141 ARG   A CG   1 
ATOM   3109 C CD   A ARG   A 1 141 ? 12.664 -17.472 -3.483  0.46 20.40 ?  141 ARG   A CD   1 
ATOM   3110 C CD   B ARG   A 1 141 ? 11.091 -15.362 -4.420  0.54 26.21 ?  141 ARG   A CD   1 
ATOM   3111 N NE   A ARG   A 1 141 ? 13.250 -18.319 -2.456  0.46 21.31 ?  141 ARG   A NE   1 
ATOM   3112 N NE   B ARG   A 1 141 ? 9.682  -15.520 -4.074  0.54 28.33 ?  141 ARG   A NE   1 
ATOM   3113 C CZ   A ARG   A 1 141 ? 12.575 -18.805 -1.424  0.46 21.12 ?  141 ARG   A CZ   1 
ATOM   3114 C CZ   B ARG   A 1 141 ? 8.671  -15.217 -4.878  0.54 30.18 ?  141 ARG   A CZ   1 
ATOM   3115 N NH1  A ARG   A 1 141 ? 11.331 -18.426 -1.172  0.46 20.96 ?  141 ARG   A NH1  1 
ATOM   3116 N NH1  B ARG   A 1 141 ? 8.874  -14.752 -6.101  0.54 30.94 ?  141 ARG   A NH1  1 
ATOM   3117 N NH2  A ARG   A 1 141 ? 13.160 -19.697 -0.628  0.46 20.83 ?  141 ARG   A NH2  1 
ATOM   3118 N NH2  B ARG   A 1 141 ? 7.423  -15.377 -4.442  0.54 30.82 ?  141 ARG   A NH2  1 
ATOM   3119 H H    A ARG   A 1 141 ? 13.607 -13.225 -2.604  0.46 17.58 ?  141 ARG   A H    1 
ATOM   3120 H H    B ARG   A 1 141 ? 13.626 -12.781 -2.507  0.54 18.99 ?  141 ARG   A H    1 
ATOM   3121 H HA   A ARG   A 1 141 ? 13.852 -15.677 -1.806  0.46 19.11 ?  141 ARG   A HA   1 
ATOM   3122 H HA   B ARG   A 1 141 ? 13.789 -15.179 -1.452  0.54 21.16 ?  141 ARG   A HA   1 
ATOM   3123 H HB2  A ARG   A 1 141 ? 12.831 -14.943 -3.858  0.46 21.48 ?  141 ARG   A HB2  1 
ATOM   3124 H HB2  B ARG   A 1 141 ? 13.310 -14.230 -4.004  0.54 23.97 ?  141 ARG   A HB2  1 
ATOM   3125 H HB3  A ARG   A 1 141 ? 14.292 -14.805 -4.453  0.46 21.48 ?  141 ARG   A HB3  1 
ATOM   3126 H HB3  B ARG   A 1 141 ? 13.905 -15.698 -3.936  0.54 23.97 ?  141 ARG   A HB3  1 
ATOM   3127 H HG2  A ARG   A 1 141 ? 13.466 -16.771 -5.207  0.46 22.77 ?  141 ARG   A HG2  1 
ATOM   3128 H HG2  B ARG   A 1 141 ? 12.071 -16.541 -3.071  0.54 28.42 ?  141 ARG   A HG2  1 
ATOM   3129 H HG3  A ARG   A 1 141 ? 14.564 -17.139 -4.110  0.46 22.77 ?  141 ARG   A HG3  1 
ATOM   3130 H HG3  B ARG   A 1 141 ? 11.616 -15.165 -2.439  0.54 28.42 ?  141 ARG   A HG3  1 
ATOM   3131 H HD2  A ARG   A 1 141 ? 12.077 -16.835 -3.046  0.46 24.50 ?  141 ARG   A HD2  1 
ATOM   3132 H HD2  B ARG   A 1 141 ? 11.218 -14.463 -4.759  0.54 31.46 ?  141 ARG   A HD2  1 
ATOM   3133 H HD3  A ARG   A 1 141 ? 12.153 -18.036 -4.084  0.46 24.50 ?  141 ARG   A HD3  1 
ATOM   3134 H HD3  B ARG   A 1 141 ? 11.309 -16.012 -5.108  0.54 31.46 ?  141 ARG   A HD3  1 
ATOM   3135 H HE   A ARG   A 1 141 ? 14.052 -18.606 -2.581  0.46 25.58 ?  141 ARG   A HE   1 
ATOM   3136 H HE   B ARG   A 1 141 ? 9.494  -15.755 -3.269  0.54 34.02 ?  141 ARG   A HE   1 
ATOM   3137 H HH11 A ARG   A 1 141 ? 10.942 -17.853 -1.683  0.46 25.16 ?  141 ARG   A HH11 1 
ATOM   3138 H HH11 B ARG   A 1 141 ? 9.676  -14.646 -6.395  0.54 37.14 ?  141 ARG   A HH11 1 
ATOM   3139 H HH12 A ARG   A 1 141 ? 10.915 -18.748 -0.495  0.46 25.16 ?  141 ARG   A HH12 1 
ATOM   3140 H HH12 B ARG   A 1 141 ? 8.204  -14.563 -6.604  0.54 37.14 ?  141 ARG   A HH12 1 
ATOM   3141 H HH21 A ARG   A 1 141 ? 13.967 -19.949 -0.783  0.46 25.00 ?  141 ARG   A HH21 1 
ATOM   3142 H HH21 B ARG   A 1 141 ? 7.280  -15.676 -3.650  0.54 37.00 ?  141 ARG   A HH21 1 
ATOM   3143 H HH22 A ARG   A 1 141 ? 12.735 -20.012 0.050   0.46 25.00 ?  141 ARG   A HH22 1 
ATOM   3144 H HH22 B ARG   A 1 141 ? 6.761  -15.182 -4.955  0.54 37.00 ?  141 ARG   A HH22 1 
ATOM   3145 N N    A VAL   A 1 142 ? 16.577 -14.470 -3.009  0.46 14.90 ?  142 VAL   A N    1 
ATOM   3146 N N    B VAL   A 1 142 ? 16.449 -14.181 -2.936  0.54 16.19 ?  142 VAL   A N    1 
ATOM   3147 C CA   A VAL   A 1 142 ? 18.026 -14.643 -2.987  0.46 15.27 ?  142 VAL   A CA   1 
ATOM   3148 C CA   B VAL   A 1 142 ? 17.884 -14.455 -3.021  0.54 15.79 ?  142 VAL   A CA   1 
ATOM   3149 C C    A VAL   A 1 142 ? 18.562 -14.564 -1.560  0.46 15.18 ?  142 VAL   A C    1 
ATOM   3150 C C    B VAL   A 1 142 ? 18.488 -14.529 -1.624  0.54 15.61 ?  142 VAL   A C    1 
ATOM   3151 O O    A VAL   A 1 142 ? 19.432 -15.353 -1.171  0.46 15.09 ?  142 VAL   A O    1 
ATOM   3152 O O    B VAL   A 1 142 ? 19.324 -15.390 -1.328  0.54 16.46 ?  142 VAL   A O    1 
ATOM   3153 C CB   A VAL   A 1 142 ? 18.726 -13.654 -3.938  0.46 15.57 ?  142 VAL   A CB   1 
ATOM   3154 C CB   B VAL   A 1 142 ? 18.589 -13.399 -3.895  0.54 16.31 ?  142 VAL   A CB   1 
ATOM   3155 C CG1  A VAL   A 1 142 ? 20.226 -13.904 -3.934  0.46 15.25 ?  142 VAL   A CG1  1 
ATOM   3156 C CG1  B VAL   A 1 142 ? 20.098 -13.600 -3.874  0.54 16.47 ?  142 VAL   A CG1  1 
ATOM   3157 C CG2  A VAL   A 1 142 ? 18.191 -13.796 -5.356  0.46 16.78 ?  142 VAL   A CG2  1 
ATOM   3158 C CG2  B VAL   A 1 142 ? 18.077 -13.455 -5.325  0.54 16.68 ?  142 VAL   A CG2  1 
ATOM   3159 H H    A VAL   A 1 142 ? 16.302 -13.792 -3.458  0.46 17.90 ?  142 VAL   A H    1 
ATOM   3160 H H    B VAL   A 1 142 ? 16.199 -13.451 -3.327  0.54 19.44 ?  142 VAL   A H    1 
ATOM   3161 H HA   A VAL   A 1 142 ? 18.231 -15.529 -3.320  0.46 18.34 ?  142 VAL   A HA   1 
ATOM   3162 H HA   B VAL   A 1 142 ? 18.015 -15.313 -3.446  0.54 18.96 ?  142 VAL   A HA   1 
ATOM   3163 H HB   A VAL   A 1 142 ? 18.569 -12.741 -3.643  0.46 18.70 ?  142 VAL   A HB   1 
ATOM   3164 H HB   B VAL   A 1 142 ? 18.405 -12.511 -3.545  0.54 19.58 ?  142 VAL   A HB   1 
ATOM   3165 H HG11 A VAL   A 1 142 ? 20.635 -13.402 -4.660  0.46 18.31 ?  142 VAL   A HG11 1 
ATOM   3166 H HG11 B VAL   A 1 142 ? 20.500 -13.057 -4.575  0.54 19.78 ?  142 VAL   A HG11 1 
ATOM   3167 H HG12 A VAL   A 1 142 ? 20.596 -13.613 -3.087  0.46 18.31 ?  142 VAL   A HG12 1 
ATOM   3168 H HG12 B VAL   A 1 142 ? 20.448 -13.326 -3.011  0.54 19.78 ?  142 VAL   A HG12 1 
ATOM   3169 H HG13 A VAL   A 1 142 ? 20.388 -14.852 -4.062  0.46 18.31 ?  142 VAL   A HG13 1 
ATOM   3170 H HG13 B VAL   A 1 142 ? 20.295 -14.534 -4.032  0.54 19.78 ?  142 VAL   A HG13 1 
ATOM   3171 H HG21 A VAL   A 1 142 ? 18.695 -13.208 -5.946  0.46 20.15 ?  142 VAL   A HG21 1 
ATOM   3172 H HG21 B VAL   A 1 142 ? 18.538 -12.783 -5.854  0.54 20.04 ?  142 VAL   A HG21 1 
ATOM   3173 H HG22 A VAL   A 1 142 ? 18.299 -14.716 -5.642  0.46 20.15 ?  142 VAL   A HG22 1 
ATOM   3174 H HG22 B VAL   A 1 142 ? 18.256 -14.337 -5.686  0.54 20.04 ?  142 VAL   A HG22 1 
ATOM   3175 H HG23 A VAL   A 1 142 ? 17.256 -13.549 -5.368  0.46 20.15 ?  142 VAL   A HG23 1 
ATOM   3176 H HG23 B VAL   A 1 142 ? 17.126 -13.281 -5.326  0.54 20.04 ?  142 VAL   A HG23 1 
ATOM   3177 N N    . CYS   A 1 143 ? 18.070 -13.617 -0.752  1.00 15.45 ?  143 CYS   A N    1 
ATOM   3178 C CA   . CYS   A 1 143 ? 18.542 -13.563 0.630   1.00 15.52 ?  143 CYS   A CA   1 
ATOM   3179 C C    . CYS   A 1 143 ? 18.285 -14.886 1.346   1.00 16.74 ?  143 CYS   A C    1 
ATOM   3180 O O    . CYS   A 1 143 ? 19.189 -15.472 1.948   1.00 16.09 ?  143 CYS   A O    1 
ATOM   3181 C CB   . CYS   A 1 143 ? 17.825 -12.428 1.361   1.00 16.78 ?  143 CYS   A CB   1 
ATOM   3182 S SG   . CYS   A 1 143 ? 18.285 -12.230 3.099   1.00 16.97 ?  143 CYS   A SG   1 
ATOM   3183 H H    A CYS   A 1 143 ? 17.490 -13.025 -0.969  0.46 18.55 ?  143 CYS   A H    1 
ATOM   3184 H H    B CYS   A 1 143 ? 17.497 -13.009 -0.940  0.54 18.55 ?  143 CYS   A H    1 
ATOM   3185 H HA   . CYS   A 1 143 ? 19.497 -13.387 0.643   1.00 18.63 ?  143 CYS   A HA   1 
ATOM   3186 H HB2  . CYS   A 1 143 ? 18.019 -11.596 0.901   1.00 20.15 ?  143 CYS   A HB2  1 
ATOM   3187 H HB3  . CYS   A 1 143 ? 16.873 -12.599 1.324   1.00 20.15 ?  143 CYS   A HB3  1 
ATOM   3188 H HG   . CYS   A 1 143 ? 19.456 -12.006 3.163   1.00 20.38 ?  143 CYS   A HG   1 
ATOM   3189 N N    . VAL   A 1 144 ? 17.048 -15.379 1.279   1.00 17.37 ?  144 VAL   A N    1 
ATOM   3190 C CA   . VAL   A 1 144 ? 16.682 -16.605 1.983   1.00 19.12 ?  144 VAL   A CA   1 
ATOM   3191 C C    . VAL   A 1 144 ? 17.488 -17.784 1.470   1.00 18.07 ?  144 VAL   A C    1 
ATOM   3192 O O    . VAL   A 1 144 ? 17.865 -18.681 2.240   1.00 19.08 ?  144 VAL   A O    1 
ATOM   3193 C CB   . VAL   A 1 144 ? 15.164 -16.837 1.850   1.00 21.76 ?  144 VAL   A CB   1 
ATOM   3194 C CG1  . VAL   A 1 144 ? 14.797 -18.299 2.079   1.00 24.19 ?  144 VAL   A CG1  1 
ATOM   3195 C CG2  . VAL   A 1 144 ? 14.433 -15.905 2.803   1.00 22.79 ?  144 VAL   A CG2  1 
ATOM   3196 H H    . VAL   A 1 144 ? 16.406 -15.024 0.831   1.00 20.85 ?  144 VAL   A H    1 
ATOM   3197 H HA   . VAL   A 1 144 ? 16.885 -16.502 2.922   1.00 22.96 ?  144 VAL   A HA   1 
ATOM   3198 H HB   . VAL   A 1 144 ? 14.892 -16.602 0.947   1.00 26.13 ?  144 VAL   A HB   1 
ATOM   3199 H HG11 . VAL   A 1 144 ? 13.846 -18.360 2.249   1.00 29.04 ?  144 VAL   A HG11 1 
ATOM   3200 H HG12 . VAL   A 1 144 ? 15.024 -18.811 1.286   1.00 29.04 ?  144 VAL   A HG12 1 
ATOM   3201 H HG13 . VAL   A 1 144 ? 15.292 -18.631 2.844   1.00 29.04 ?  144 VAL   A HG13 1 
ATOM   3202 H HG21 . VAL   A 1 144 ? 13.482 -16.085 2.753   1.00 27.37 ?  144 VAL   A HG21 1 
ATOM   3203 H HG22 . VAL   A 1 144 ? 14.753 -16.064 3.705   1.00 27.37 ?  144 VAL   A HG22 1 
ATOM   3204 H HG23 . VAL   A 1 144 ? 14.610 -14.987 2.546   1.00 27.37 ?  144 VAL   A HG23 1 
ATOM   3205 N N    . ASP   A 1 145 ? 17.777 -17.801 0.171   1.00 18.94 ?  145 ASP   A N    1 
ATOM   3206 C CA   . ASP   A 1 145 ? 18.477 -18.913 -0.463  1.00 19.58 ?  145 ASP   A CA   1 
ATOM   3207 C C    . ASP   A 1 145 ? 19.993 -18.786 -0.400  1.00 18.80 ?  145 ASP   A C    1 
ATOM   3208 O O    . ASP   A 1 145 ? 20.694 -19.682 -0.880  1.00 20.13 ?  145 ASP   A O    1 
ATOM   3209 C CB   . ASP   A 1 145 ? 18.050 -19.040 -1.931  1.00 21.47 ?  145 ASP   A CB   1 
ATOM   3210 C CG   . ASP   A 1 145 ? 16.602 -19.478 -2.086  1.00 23.41 ?  145 ASP   A CG   1 
ATOM   3211 O OD1  . ASP   A 1 145 ? 16.021 -20.027 -1.123  1.00 24.05 ?  145 ASP   A OD1  1 
ATOM   3212 O OD2  . ASP   A 1 145 ? 16.049 -19.251 -3.179  1.00 24.45 -1 145 ASP   A OD2  1 
ATOM   3213 H H    . ASP   A 1 145 ? 17.554 -17.175 -0.378  1.00 22.75 ?  145 ASP   A H    1 
ATOM   3214 H HA   . ASP   A 1 145 ? 18.225 -19.733 -0.015  1.00 23.52 ?  145 ASP   A HA   1 
ATOM   3215 H HB2  . ASP   A 1 145 ? 18.151 -18.177 -2.370  1.00 25.78 ?  145 ASP   A HB2  1 
ATOM   3216 H HB3  . ASP   A 1 145 ? 18.613 -19.697 -2.370  1.00 25.78 ?  145 ASP   A HB3  1 
ATOM   3217 N N    . THR   A 1 146 ? 20.527 -17.709 0.164   1.00 17.12 ?  146 THR   A N    1 
ATOM   3218 C CA   . THR   A 1 146 ? 21.969 -17.476 0.172   1.00 15.92 ?  146 THR   A CA   1 
ATOM   3219 C C    . THR   A 1 146 ? 22.528 -17.289 1.567   1.00 15.96 ?  146 THR   A C    1 
ATOM   3220 O O    . THR   A 1 146 ? 23.591 -17.831 1.876   1.00 17.17 ?  146 THR   A O    1 
ATOM   3221 C CB   . THR   A 1 146 ? 22.303 -16.233 -0.667  1.00 15.31 ?  146 THR   A CB   1 
ATOM   3222 O OG1  . THR   A 1 146 ? 21.789 -16.389 -1.994  1.00 16.41 ?  146 THR   A OG1  1 
ATOM   3223 C CG2  . THR   A 1 146 ? 23.807 -16.004 -0.731  1.00 16.00 ?  146 THR   A CG2  1 
ATOM   3224 H H    . THR   A 1 146 ? 20.076 -17.091 0.560   1.00 20.55 ?  146 THR   A H    1 
ATOM   3225 H HA   . THR   A 1 146 ? 22.422 -18.234 -0.221  1.00 19.12 ?  146 THR   A HA   1 
ATOM   3226 H HB   . THR   A 1 146 ? 21.907 -15.450 -0.257  1.00 18.39 ?  146 THR   A HB   1 
ATOM   3227 H HG1  . THR   A 1 146 ? 20.954 -16.462 -1.964  1.00 19.71 ?  146 THR   A HG1  1 
ATOM   3228 H HG21 . THR   A 1 146 ? 24.010 -15.352 -1.425  1.00 19.22 ?  146 THR   A HG21 1 
ATOM   3229 H HG22 . THR   A 1 146 ? 24.132 -15.663 0.117   1.00 19.22 ?  146 THR   A HG22 1 
ATOM   3230 H HG23 . THR   A 1 146 ? 24.261 -16.832 -0.939  1.00 19.22 ?  146 THR   A HG23 1 
ATOM   3231 N N    . VAL   A 1 147 ? 21.856 -16.513 2.405   1.00 15.02 ?  147 VAL   A N    1 
ATOM   3232 C CA   . VAL   A 1 147 ? 22.349 -16.208 3.742   1.00 15.34 ?  147 VAL   A CA   1 
ATOM   3233 C C    . VAL   A 1 147 ? 22.010 -17.372 4.668   1.00 16.40 ?  147 VAL   A C    1 
ATOM   3234 O O    . VAL   A 1 147 ? 20.862 -17.828 4.723   1.00 17.13 ?  147 VAL   A O    1 
ATOM   3235 C CB   . VAL   A 1 147 ? 21.744 -14.888 4.248   1.00 15.44 ?  147 VAL   A CB   1 
ATOM   3236 C CG1  . VAL   A 1 147 ? 22.278 -14.547 5.630   1.00 17.06 ?  147 VAL   A CG1  1 
ATOM   3237 C CG2  . VAL   A 1 147 ? 22.009 -13.761 3.251   1.00 15.94 ?  147 VAL   A CG2  1 
ATOM   3238 H H    . VAL   A 1 147 ? 21.096 -16.157 2.228   1.00 18.04 ?  147 VAL   A H    1 
ATOM   3239 H HA   . VAL   A 1 147 ? 23.313 -16.114 3.718   1.00 18.42 ?  147 VAL   A HA   1 
ATOM   3240 H HB   . VAL   A 1 147 ? 20.784 -14.997 4.323   1.00 18.54 ?  147 VAL   A HB   1 
ATOM   3241 H HG11 . VAL   A 1 147 ? 21.998 -13.649 5.863   1.00 20.48 ?  147 VAL   A HG11 1 
ATOM   3242 H HG12 . VAL   A 1 147 ? 21.916 -15.179 6.276   1.00 20.48 ?  147 VAL   A HG12 1 
ATOM   3243 H HG13 . VAL   A 1 147 ? 23.244 -14.602 5.621   1.00 20.48 ?  147 VAL   A HG13 1 
ATOM   3244 H HG21 . VAL   A 1 147 ? 21.703 -12.924 3.634   1.00 19.14 ?  147 VAL   A HG21 1 
ATOM   3245 H HG22 . VAL   A 1 147 ? 22.961 -13.715 3.072   1.00 19.14 ?  147 VAL   A HG22 1 
ATOM   3246 H HG23 . VAL   A 1 147 ? 21.526 -13.945 2.430   1.00 19.14 ?  147 VAL   A HG23 1 
ATOM   3247 N N    . ARG   A 1 148 ? 23.014 -17.848 5.402   1.00 16.26 ?  148 ARG   A N    1 
ATOM   3248 C CA   . ARG   A 1 148 ? 22.866 -18.910 6.379   1.00 17.20 ?  148 ARG   A CA   1 
ATOM   3249 C C    . ARG   A 1 148 ? 23.000 -18.420 7.810   1.00 17.89 ?  148 ARG   A C    1 
ATOM   3250 O O    . ARG   A 1 148 ? 22.604 -19.142 8.734   1.00 19.40 ?  148 ARG   A O    1 
ATOM   3251 C CB   . ARG   A 1 148 ? 23.901 -20.016 6.116   1.00 17.80 ?  148 ARG   A CB   1 
ATOM   3252 C CG   . ARG   A 1 148 ? 23.770 -20.653 4.745   1.00 18.31 ?  148 ARG   A CG   1 
ATOM   3253 C CD   . ARG   A 1 148 ? 24.861 -21.683 4.475   1.00 18.87 ?  148 ARG   A CD   1 
ATOM   3254 N NE   . ARG   A 1 148 ? 26.199 -21.105 4.499   1.00 19.10 ?  148 ARG   A NE   1 
ATOM   3255 C CZ   . ARG   A 1 148 ? 26.717 -20.389 3.509   1.00 17.62 ?  148 ARG   A CZ   1 
ATOM   3256 N NH1  . ARG   A 1 148 ? 26.043 -20.168 2.391   1.00 17.63 ?  148 ARG   A NH1  1 
ATOM   3257 N NH2  . ARG   A 1 148 ? 27.931 -19.847 3.656   1.00 18.21 ?  148 ARG   A NH2  1 
ATOM   3258 H H    . ARG   A 1 148 ? 23.812 -17.549 5.349   1.00 19.53 ?  148 ARG   A H    1 
ATOM   3259 H HA   . ARG   A 1 148 ? 21.982 -19.305 6.288   1.00 20.65 ?  148 ARG   A HA   1 
ATOM   3260 H HB2  . ARG   A 1 148 ? 24.786 -19.647 6.189   1.00 21.37 ?  148 ARG   A HB2  1 
ATOM   3261 H HB3  . ARG   A 1 148 ? 23.778 -20.724 6.775   1.00 21.37 ?  148 ARG   A HB3  1 
ATOM   3262 H HG2  . ARG   A 1 148 ? 22.909 -21.095 4.680   1.00 21.99 ?  148 ARG   A HG2  1 
ATOM   3263 H HG3  . ARG   A 1 148 ? 23.835 -19.955 4.072   1.00 21.99 ?  148 ARG   A HG3  1 
ATOM   3264 H HD2  . ARG   A 1 148 ? 24.822 -22.371 5.154   1.00 22.66 ?  148 ARG   A HD2  1 
ATOM   3265 H HD3  . ARG   A 1 148 ? 24.719 -22.073 3.597   1.00 22.66 ?  148 ARG   A HD3  1 
ATOM   3266 H HE   . ARG   A 1 148 ? 26.682 -21.227 5.200   1.00 22.93 ?  148 ARG   A HE   1 
ATOM   3267 H HH11 . ARG   A 1 148 ? 25.259 -20.496 2.289   1.00 21.17 ?  148 ARG   A HH11 1 
ATOM   3268 H HH12 . ARG   A 1 148 ? 26.395 -19.691 1.764   1.00 21.17 ?  148 ARG   A HH12 1 
ATOM   3269 H HH21 . ARG   A 1 148 ? 28.380 -19.978 4.379   1.00 21.87 ?  148 ARG   A HH21 1 
ATOM   3270 H HH22 . ARG   A 1 148 ? 28.280 -19.376 3.021   1.00 21.87 ?  148 ARG   A HH22 1 
ATOM   3271 N N    . THR   A 1 149 ? 23.551 -17.224 8.016   1.00 17.78 ?  149 THR   A N    1 
ATOM   3272 C CA   . THR   A 1 149 ? 23.615 -16.618 9.335   1.00 17.27 ?  149 THR   A CA   1 
ATOM   3273 C C    . THR   A 1 149 ? 22.289 -15.922 9.634   1.00 17.18 ?  149 THR   A C    1 
ATOM   3274 O O    . THR   A 1 149 ? 21.369 -15.894 8.805   1.00 17.91 ?  149 THR   A O    1 
ATOM   3275 C CB   . THR   A 1 149 ? 24.812 -15.680 9.404   1.00 18.11 ?  149 THR   A CB   1 
ATOM   3276 O OG1  . THR   A 1 149 ? 24.720 -14.764 8.312   1.00 18.23 ?  149 THR   A OG1  1 
ATOM   3277 C CG2  . THR   A 1 149 ? 26.109 -16.479 9.300   1.00 19.34 ?  149 THR   A CG2  1 
ATOM   3278 H H    . THR   A 1 149 ? 23.912 -16.747 7.399   1.00 21.35 ?  149 THR   A H    1 
ATOM   3279 H HA   . THR   A 1 149 ? 23.736 -17.323 9.999   1.00 20.74 ?  149 THR   A HA   1 
ATOM   3280 H HB   . THR   A 1 149 ? 24.800 -15.210 10.258  1.00 21.75 ?  149 THR   A HB   1 
ATOM   3281 H HG1  . THR   A 1 149 ? 25.368 -14.229 8.344   1.00 21.89 ?  149 THR   A HG1  1 
ATOM   3282 H HG21 . THR   A 1 149 ? 26.868 -15.881 9.371   1.00 23.22 ?  149 THR   A HG21 1 
ATOM   3283 H HG22 . THR   A 1 149 ? 26.159 -17.138 10.010  1.00 23.22 ?  149 THR   A HG22 1 
ATOM   3284 H HG23 . THR   A 1 149 ? 26.147 -16.936 8.445   1.00 23.22 ?  149 THR   A HG23 1 
ATOM   3285 N N    . ASN   A 1 150 ? 22.171 -15.364 10.838  1.00 17.70 ?  150 ASN   A N    1 
ATOM   3286 C CA   . ASN   A 1 150 ? 20.898 -14.833 11.320  1.00 18.37 ?  150 ASN   A CA   1 
ATOM   3287 C C    . ASN   A 1 150 ? 20.741 -13.398 10.839  1.00 18.31 ?  150 ASN   A C    1 
ATOM   3288 O O    . ASN   A 1 150 ? 21.500 -12.509 11.241  1.00 19.14 ?  150 ASN   A O    1 
ATOM   3289 C CB   . ASN   A 1 150 ? 20.833 -14.922 12.838  1.00 21.43 ?  150 ASN   A CB   1 
ATOM   3290 C CG   . ASN   A 1 150 ? 20.805 -16.340 13.316  1.00 26.55 ?  150 ASN   A CG   1 
ATOM   3291 O OD1  . ASN   A 1 150 ? 20.158 -17.178 12.702  1.00 28.18 ?  150 ASN   A OD1  1 
ATOM   3292 N ND2  . ASN   A 1 150 ? 21.530 -16.632 14.390  1.00 29.59 ?  150 ASN   A ND2  1 
ATOM   3293 H H    . ASN   A 1 150 ? 22.816 -15.278 11.399  1.00 21.26 ?  150 ASN   A H    1 
ATOM   3294 H HA   . ASN   A 1 150 ? 20.170 -15.366 10.952  1.00 22.06 ?  150 ASN   A HA   1 
ATOM   3295 H HB2  . ASN   A 1 150 ? 21.610 -14.495 13.219  1.00 25.74 ?  150 ASN   A HB2  1 
ATOM   3296 H HB3  . ASN   A 1 150 ? 20.021 -14.488 13.149  1.00 25.74 ?  150 ASN   A HB3  1 
ATOM   3297 H HD21 . ASN   A 1 150 ? 21.549 -17.438 14.704  1.00 35.52 ?  150 ASN   A HD21 1 
ATOM   3298 H HD22 . ASN   A 1 150 ? 21.976 -16.014 14.787  1.00 35.52 ?  150 ASN   A HD22 1 
ATOM   3299 N N    . VAL   A 1 151 ? 19.763 -13.168 9.980   1.00 17.60 ?  151 VAL   A N    1 
ATOM   3300 C CA   . VAL   A 1 151 ? 19.566 -11.866 9.370   1.00 17.91 ?  151 VAL   A CA   1 
ATOM   3301 C C    . VAL   A 1 151 ? 18.192 -11.332 9.751   1.00 16.88 ?  151 VAL   A C    1 
ATOM   3302 O O    . VAL   A 1 151 ? 17.183 -12.041 9.635   1.00 19.09 ?  151 VAL   A O    1 
ATOM   3303 C CB   . VAL   A 1 151 ? 19.813 -11.902 7.847   1.00 18.75 ?  151 VAL   A CB   1 
ATOM   3304 C CG1  . VAL   A 1 151 ? 18.939 -12.924 7.160   1.00 20.76 ?  151 VAL   A CG1  1 
ATOM   3305 C CG2  . VAL   A 1 151 ? 19.627 -10.511 7.238   1.00 19.62 ?  151 VAL   A CG2  1 
ATOM   3306 H H    . VAL   A 1 151 ? 19.193 -13.763 9.726   1.00 21.14 ?  151 VAL   A H    1 
ATOM   3307 H HA   . VAL   A 1 151 ? 20.220 -11.253 9.743   1.00 21.51 ?  151 VAL   A HA   1 
ATOM   3308 H HB   . VAL   A 1 151 ? 20.737 -12.163 7.695   1.00 22.51 ?  151 VAL   A HB   1 
ATOM   3309 H HG11 . VAL   A 1 151 ? 19.104 -12.893 6.206   1.00 24.93 ?  151 VAL   A HG11 1 
ATOM   3310 H HG12 . VAL   A 1 151 ? 19.157 -13.808 7.503   1.00 24.93 ?  151 VAL   A HG12 1 
ATOM   3311 H HG13 . VAL   A 1 151 ? 18.009 -12.721 7.343   1.00 24.93 ?  151 VAL   A HG13 1 
ATOM   3312 H HG21 . VAL   A 1 151 ? 19.918 -10.533 6.308   1.00 23.56 ?  151 VAL   A HG21 1 
ATOM   3313 H HG22 . VAL   A 1 151 ? 18.690 -10.266 7.279   1.00 23.56 ?  151 VAL   A HG22 1 
ATOM   3314 H HG23 . VAL   A 1 151 ? 20.163 -9.872  7.730   1.00 23.56 ?  151 VAL   A HG23 1 
ATOM   3315 N N    . TYR   A 1 152 ? 18.177 -10.085 10.223  1.00 17.04 ?  152 TYR   A N    1 
ATOM   3316 C CA   . TYR   A 1 152 ? 16.976 -9.350  10.603  1.00 16.76 ?  152 TYR   A CA   1 
ATOM   3317 C C    . TYR   A 1 152 ? 16.786 -8.239  9.579   1.00 15.62 ?  152 TYR   A C    1 
ATOM   3318 O O    . TYR   A 1 152 ? 17.565 -7.281  9.544   1.00 16.44 ?  152 TYR   A O    1 
ATOM   3319 C CB   . TYR   A 1 152 ? 17.140 -8.809  12.019  1.00 17.95 ?  152 TYR   A CB   1 
ATOM   3320 C CG   . TYR   A 1 152 ? 17.101 -9.918  13.030  1.00 19.71 ?  152 TYR   A CG   1 
ATOM   3321 C CD1  . TYR   A 1 152 ? 18.234 -10.673 13.301  1.00 21.77 ?  152 TYR   A CD1  1 
ATOM   3322 C CD2  . TYR   A 1 152 ? 15.918 -10.250 13.679  1.00 19.91 ?  152 TYR   A CD2  1 
ATOM   3323 C CE1  . TYR   A 1 152 ? 18.205 -11.712 14.202  1.00 23.34 ?  152 TYR   A CE1  1 
ATOM   3324 C CE2  . TYR   A 1 152 ? 15.875 -11.295 14.591  1.00 22.63 ?  152 TYR   A CE2  1 
ATOM   3325 C CZ   . TYR   A 1 152 ? 17.027 -12.022 14.850  1.00 23.65 ?  152 TYR   A CZ   1 
ATOM   3326 O OH   . TYR   A 1 152 ? 17.002 -13.066 15.753  1.00 27.71 ?  152 TYR   A OH   1 
ATOM   3327 H H    . TYR   A 1 152 ? 18.896 -9.615  10.319  1.00 20.46 ?  152 TYR   A H    1 
ATOM   3328 H HA   . TYR   A 1 152 ? 16.211 -9.939  10.573  1.00 20.12 ?  152 TYR   A HA   1 
ATOM   3329 H HB2  . TYR   A 1 152 ? 17.998 -8.364  12.090  1.00 21.55 ?  152 TYR   A HB2  1 
ATOM   3330 H HB3  . TYR   A 1 152 ? 16.426 -8.188  12.212  1.00 21.55 ?  152 TYR   A HB3  1 
ATOM   3331 H HD1  . TYR   A 1 152 ? 19.031 -10.472 12.866  1.00 26.14 ?  152 TYR   A HD1  1 
ATOM   3332 H HD2  . TYR   A 1 152 ? 15.140 -9.759  13.506  1.00 23.91 ?  152 TYR   A HD2  1 
ATOM   3333 H HE1  . TYR   A 1 152 ? 18.973 -12.206 14.382  1.00 28.03 ?  152 TYR   A HE1  1 
ATOM   3334 H HE2  . TYR   A 1 152 ? 15.078 -11.502 15.031  1.00 27.17 ?  152 TYR   A HE2  1 
ATOM   3335 H HH   . TYR   A 1 152 ? 16.231 -13.147 16.079  1.00 33.27 ?  152 TYR   A HH   1 
ATOM   3336 N N    A LEU   A 1 153 ? 15.816 -8.446  8.687   0.46 15.30 ?  153 LEU   A N    1 
ATOM   3337 N N    B LEU   A 1 153 ? 15.713 -8.323  8.791   0.54 15.41 ?  153 LEU   A N    1 
ATOM   3338 C CA   A LEU   A 1 153 ? 15.582 -7.590  7.534   0.46 14.88 ?  153 LEU   A CA   1 
ATOM   3339 C CA   B LEU   A 1 153 ? 15.453 -7.379  7.711   0.54 14.36 ?  153 LEU   A CA   1 
ATOM   3340 C C    A LEU   A 1 153 ? 14.559 -6.518  7.885   0.46 15.41 ?  153 LEU   A C    1 
ATOM   3341 C C    B LEU   A 1 153 ? 14.500 -6.277  8.159   0.54 15.56 ?  153 LEU   A C    1 
ATOM   3342 O O    A LEU   A 1 153 ? 13.417 -6.830  8.249   0.46 15.99 ?  153 LEU   A O    1 
ATOM   3343 O O    B LEU   A 1 153 ? 13.456 -6.555  8.763   0.54 15.28 ?  153 LEU   A O    1 
ATOM   3344 C CB   A LEU   A 1 153 ? 15.069 -8.423  6.359   0.46 15.18 ?  153 LEU   A CB   1 
ATOM   3345 C CB   B LEU   A 1 153 ? 14.869 -8.088  6.489   0.54 13.56 ?  153 LEU   A CB   1 
ATOM   3346 C CG   A LEU   A 1 153 ? 16.015 -9.480  5.777   0.46 15.49 ?  153 LEU   A CG   1 
ATOM   3347 C CG   B LEU   A 1 153 ? 15.777 -9.099  5.779   0.54 14.07 ?  153 LEU   A CG   1 
ATOM   3348 C CD1  A LEU   A 1 153 ? 15.267 -10.360 4.790   0.46 15.29 ?  153 LEU   A CD1  1 
ATOM   3349 C CD1  B LEU   A 1 153 ? 14.959 -9.964  4.838   0.54 14.46 ?  153 LEU   A CD1  1 
ATOM   3350 C CD2  A LEU   A 1 153 ? 17.204 -8.839  5.100   0.46 15.77 ?  153 LEU   A CD2  1 
ATOM   3351 C CD2  B LEU   A 1 153 ? 16.889 -8.403  5.021   0.54 14.36 ?  153 LEU   A CD2  1 
ATOM   3352 H H    A LEU   A 1 153 ? 15.269 -9.116  8.726   0.46 18.38 ?  153 LEU   A H    1 
ATOM   3353 H H    B LEU   A 1 153 ? 15.099 -8.927  8.870   0.54 18.50 ?  153 LEU   A H    1 
ATOM   3354 H HA   A LEU   A 1 153 ? 16.412 -7.166  7.275   0.46 17.87 ?  153 LEU   A HA   1 
ATOM   3355 H HA   B LEU   A 1 153 ? 16.279 -6.962  7.453   0.54 17.25 ?  153 LEU   A HA   1 
ATOM   3356 H HB2  A LEU   A 1 153 ? 14.266 -8.885  6.643   0.46 18.23 ?  153 LEU   A HB2  1 
ATOM   3357 H HB2  B LEU   A 1 153 ? 14.069 -8.559  6.764   0.54 16.28 ?  153 LEU   A HB2  1 
ATOM   3358 H HB3  A LEU   A 1 153 ? 14.849 -7.815  5.635   0.46 18.23 ?  153 LEU   A HB3  1 
ATOM   3359 H HB3  B LEU   A 1 153 ? 14.630 -7.410  5.833   0.54 16.28 ?  153 LEU   A HB3  1 
ATOM   3360 H HG   A LEU   A 1 153 ? 16.341 -10.046 6.498   0.46 18.60 ?  153 LEU   A HG   1 
ATOM   3361 H HG   B LEU   A 1 153 ? 16.179 -9.677  6.447   0.54 16.90 ?  153 LEU   A HG   1 
ATOM   3362 H HD11 A LEU   A 1 153 ? 15.877 -11.021 4.432   0.46 18.36 ?  153 LEU   A HD11 1 
ATOM   3363 H HD11 B LEU   A 1 153 ? 15.551 -10.593 4.399   0.54 17.36 ?  153 LEU   A HD11 1 
ATOM   3364 H HD12 A LEU   A 1 153 ? 14.534 -10.799 5.251   0.46 18.36 ?  153 LEU   A HD12 1 
ATOM   3365 H HD12 B LEU   A 1 153 ? 14.289 -10.443 5.351   0.54 17.36 ?  153 LEU   A HD12 1 
ATOM   3366 H HD13 A LEU   A 1 153 ? 14.921 -9.803  4.075   0.46 18.36 ?  153 LEU   A HD13 1 
ATOM   3367 H HD13 B LEU   A 1 153 ? 14.530 -9.396  4.182   0.54 17.36 ?  153 LEU   A HD13 1 
ATOM   3368 H HD21 A LEU   A 1 153 ? 17.761 -9.536  4.715   0.46 18.94 ?  153 LEU   A HD21 1 
ATOM   3369 H HD21 B LEU   A 1 153 ? 17.427 -9.073  4.576   0.54 17.25 ?  153 LEU   A HD21 1 
ATOM   3370 H HD22 A LEU   A 1 153 ? 16.887 -8.247  4.402   0.46 18.94 ?  153 LEU   A HD22 1 
ATOM   3371 H HD22 B LEU   A 1 153 ? 16.495 -7.804  4.369   0.54 17.25 ?  153 LEU   A HD22 1 
ATOM   3372 H HD23 A LEU   A 1 153 ? 17.711 -8.339  5.758   0.46 18.94 ?  153 LEU   A HD23 1 
ATOM   3373 H HD23 B LEU   A 1 153 ? 17.430 -7.902  5.649   0.54 17.25 ?  153 LEU   A HD23 1 
ATOM   3374 N N    A ALA   A 1 154 ? 14.963 -5.259  7.754   0.46 15.55 ?  154 ALA   A N    1 
ATOM   3375 N N    B ALA   A 1 154 ? 14.849 -5.033  7.827   0.54 15.72 ?  154 ALA   A N    1 
ATOM   3376 C CA   A ALA   A 1 154 ? 14.096 -4.115  7.999   0.46 15.45 ?  154 ALA   A CA   1 
ATOM   3377 C CA   B ALA   A 1 154 ? 14.010 -3.866  8.070   0.54 16.43 ?  154 ALA   A CA   1 
ATOM   3378 C C    A ALA   A 1 154 ? 13.582 -3.588  6.665   0.46 15.06 ?  154 ALA   A C    1 
ATOM   3379 C C    B ALA   A 1 154 ? 13.560 -3.309  6.726   0.54 16.49 ?  154 ALA   A C    1 
ATOM   3380 O O    A ALA   A 1 154 ? 14.376 -3.254  5.775   0.46 15.11 ?  154 ALA   A O    1 
ATOM   3381 O O    B ALA   A 1 154 ? 14.392 -2.864  5.926   0.54 16.45 ?  154 ALA   A O    1 
ATOM   3382 C CB   A ALA   A 1 154 ? 14.867 -3.019  8.732   0.46 16.11 ?  154 ALA   A CB   1 
ATOM   3383 C CB   B ALA   A 1 154 ? 14.789 -2.801  8.842   0.54 17.35 ?  154 ALA   A CB   1 
ATOM   3384 H H    A ALA   A 1 154 ? 15.760 -5.045  7.519   0.46 18.67 ?  154 ALA   A H    1 
ATOM   3385 H H    B ALA   A 1 154 ? 15.595 -4.833  7.441   0.54 18.88 ?  154 ALA   A H    1 
ATOM   3386 H HA   A ALA   A 1 154 ? 13.341 -4.390  8.545   0.46 18.55 ?  154 ALA   A HA   1 
ATOM   3387 H HA   B ALA   A 1 154 ? 13.228 -4.116  8.584   0.54 19.72 ?  154 ALA   A HA   1 
ATOM   3388 H HB1  A ALA   A 1 154 ? 14.271 -2.269  8.880   0.46 19.35 ?  154 ALA   A HB1  1 
ATOM   3389 H HB1  B ALA   A 1 154 ? 14.213 -2.035  8.994   0.54 20.84 ?  154 ALA   A HB1  1 
ATOM   3390 H HB2  A ALA   A 1 154 ? 15.184 -3.366  9.579   0.46 19.35 ?  154 ALA   A HB2  1 
ATOM   3391 H HB2  B ALA   A 1 154 ? 15.075 -3.173  9.689   0.54 20.84 ?  154 ALA   A HB2  1 
ATOM   3392 H HB3  A ALA   A 1 154 ? 15.617 -2.745  8.182   0.46 19.35 ?  154 ALA   A HB3  1 
ATOM   3393 H HB3  B ALA   A 1 154 ? 15.562 -2.534  8.319   0.54 20.84 ?  154 ALA   A HB3  1 
ATOM   3394 N N    A VAL   A 1 155 ? 12.262 -3.513  6.530   0.46 15.38 ?  155 VAL   A N    1 
ATOM   3395 N N    B VAL   A 1 155 ? 12.252 -3.340  6.477   0.54 17.76 ?  155 VAL   A N    1 
ATOM   3396 C CA   A VAL   A 1 155 ? 11.611 -3.012  5.324   0.46 16.25 ?  155 VAL   A CA   1 
ATOM   3397 C CA   B VAL   A 1 155 ? 11.667 -2.848  5.233   0.54 18.64 ?  155 VAL   A CA   1 
ATOM   3398 C C    A VAL   A 1 155 ? 10.882 -1.721  5.685   0.46 17.67 ?  155 VAL   A C    1 
ATOM   3399 C C    B VAL   A 1 155 ? 10.857 -1.598  5.548   0.54 20.49 ?  155 VAL   A C    1 
ATOM   3400 O O    A VAL   A 1 155 ? 9.980  -1.724  6.533   0.46 17.31 ?  155 VAL   A O    1 
ATOM   3401 O O    B VAL   A 1 155 ? 9.851  -1.668  6.264   0.54 20.27 ?  155 VAL   A O    1 
ATOM   3402 C CB   A VAL   A 1 155 ? 10.655 -4.060  4.729   0.46 16.53 ?  155 VAL   A CB   1 
ATOM   3403 C CB   B VAL   A 1 155 ? 10.797 -3.923  4.564   0.54 18.36 ?  155 VAL   A CB   1 
ATOM   3404 C CG1  A VAL   A 1 155 ? 9.957  -3.508  3.496   0.46 17.44 ?  155 VAL   A CG1  1 
ATOM   3405 C CG1  B VAL   A 1 155 ? 10.117 -3.362  3.322   0.54 19.30 ?  155 VAL   A CG1  1 
ATOM   3406 C CG2  A VAL   A 1 155 ? 11.413 -5.354  4.399   0.46 17.77 ?  155 VAL   A CG2  1 
ATOM   3407 C CG2  B VAL   A 1 155 ? 11.647 -5.149  4.226   0.54 19.33 ?  155 VAL   A CG2  1 
ATOM   3408 H H    A VAL   A 1 155 ? 11.713 -3.755  7.142   0.46 18.48 ?  155 VAL   A H    1 
ATOM   3409 H H    B VAL   A 1 155 ? 11.671 -3.660  7.027   0.54 21.32 ?  155 VAL   A H    1 
ATOM   3410 H HA   A VAL   A 1 155 ? 12.285 -2.811  4.655   0.46 19.52 ?  155 VAL   A HA   1 
ATOM   3411 H HA   B VAL   A 1 155 ? 12.378 -2.604  4.620   0.54 22.38 ?  155 VAL   A HA   1 
ATOM   3412 H HB   A VAL   A 1 155 ? 9.976  -4.280  5.387   0.46 19.86 ?  155 VAL   A HB   1 
ATOM   3413 H HB   B VAL   A 1 155 ? 10.105 -4.198  5.187   0.54 22.04 ?  155 VAL   A HB   1 
ATOM   3414 H HG11 A VAL   A 1 155 ? 9.505  -4.232  3.038   0.46 20.95 ?  155 VAL   A HG11 1 
ATOM   3415 H HG11 B VAL   A 1 155 ? 9.740  -4.095  2.815   0.54 23.17 ?  155 VAL   A HG11 1 
ATOM   3416 H HG12 A VAL   A 1 155 ? 9.313  -2.838  3.772   0.46 20.95 ?  155 VAL   A HG12 1 
ATOM   3417 H HG12 B VAL   A 1 155 ? 9.412  -2.752  3.595   0.54 23.17 ?  155 VAL   A HG12 1 
ATOM   3418 H HG13 A VAL   A 1 155 ? 10.621 -3.110  2.912   0.46 20.95 ?  155 VAL   A HG13 1 
ATOM   3419 H HG13 B VAL   A 1 155 ? 10.776 -2.892  2.789   0.54 23.17 ?  155 VAL   A HG13 1 
ATOM   3420 H HG21 A VAL   A 1 155 ? 10.804 -5.980  3.976   0.46 21.34 ?  155 VAL   A HG21 1 
ATOM   3421 H HG21 B VAL   A 1 155 ? 11.095 -5.795  3.760   0.54 23.21 ?  155 VAL   A HG21 1 
ATOM   3422 H HG22 A VAL   A 1 155 ? 12.143 -5.145  3.794   0.46 21.34 ?  155 VAL   A HG22 1 
ATOM   3423 H HG22 B VAL   A 1 155 ? 12.386 -4.875  3.661   0.54 23.21 ?  155 VAL   A HG22 1 
ATOM   3424 H HG23 A VAL   A 1 155 ? 11.763 -5.736  5.219   0.46 21.34 ?  155 VAL   A HG23 1 
ATOM   3425 H HG23 B VAL   A 1 155 ? 11.986 -5.536  5.049   0.54 23.21 ?  155 VAL   A HG23 1 
ATOM   3426 N N    A PHE   A 1 156 ? 11.279 -0.616  5.045   0.46 18.66 ?  156 PHE   A N    1 
ATOM   3427 N N    B PHE   A 1 156 ? 11.282 -0.458  5.003   0.54 22.37 ?  156 PHE   A N    1 
ATOM   3428 C CA   A PHE   A 1 156 ? 10.756 0.700   5.414   0.46 19.29 ?  156 PHE   A CA   1 
ATOM   3429 C CA   B PHE   A 1 156 ? 10.721 0.846   5.357   0.54 24.64 ?  156 PHE   A CA   1 
ATOM   3430 C C    A PHE   A 1 156 ? 9.305  0.883   4.982   0.46 19.53 ?  156 PHE   A C    1 
ATOM   3431 C C    B PHE   A 1 156 ? 9.663  1.324   4.373   0.54 26.20 ?  156 PHE   A C    1 
ATOM   3432 O O    A PHE   A 1 156 ? 8.504  1.479   5.713   0.46 18.84 ?  156 PHE   A O    1 
ATOM   3433 O O    B PHE   A 1 156 ? 9.574  2.518   4.073   0.54 28.32 ?  156 PHE   A O    1 
ATOM   3434 C CB   A PHE   A 1 156 ? 11.633 1.782   4.783   0.46 20.13 ?  156 PHE   A CB   1 
ATOM   3435 C CB   B PHE   A 1 156 ? 11.835 1.880   5.483   0.54 25.83 ?  156 PHE   A CB   1 
ATOM   3436 C CG   A PHE   A 1 156 ? 11.168 3.183   5.066   0.46 21.64 ?  156 PHE   A CG   1 
ATOM   3437 C CG   B PHE   A 1 156 ? 11.440 3.112   6.246   0.54 28.04 ?  156 PHE   A CG   1 
ATOM   3438 C CD1  A PHE   A 1 156 ? 11.216 3.693   6.353   0.46 22.84 ?  156 PHE   A CD1  1 
ATOM   3439 C CD1  B PHE   A 1 156 ? 10.491 3.051   7.253   0.54 29.17 ?  156 PHE   A CD1  1 
ATOM   3440 C CD2  A PHE   A 1 156 ? 10.687 3.993   4.048   0.46 22.22 ?  156 PHE   A CD2  1 
ATOM   3441 C CD2  B PHE   A 1 156 ? 12.024 4.332   5.958   0.54 28.05 ?  156 PHE   A CD2  1 
ATOM   3442 C CE1  A PHE   A 1 156 ? 10.792 4.979   6.623   0.46 23.78 ?  156 PHE   A CE1  1 
ATOM   3443 C CE1  B PHE   A 1 156 ? 10.133 4.181   7.955   0.54 29.59 ?  156 PHE   A CE1  1 
ATOM   3444 C CE2  A PHE   A 1 156 ? 10.259 5.288   4.311   0.46 22.97 ?  156 PHE   A CE2  1 
ATOM   3445 C CE2  B PHE   A 1 156 ? 11.669 5.467   6.655   0.54 28.89 ?  156 PHE   A CE2  1 
ATOM   3446 C CZ   A PHE   A 1 156 ? 10.315 5.782   5.600   0.46 22.92 ?  156 PHE   A CZ   1 
ATOM   3447 C CZ   B PHE   A 1 156 ? 10.723 5.391   7.657   0.54 29.54 ?  156 PHE   A CZ   1 
ATOM   3448 H H    A PHE   A 1 156 ? 11.848 -0.612  4.401   0.46 22.41 ?  156 PHE   A H    1 
ATOM   3449 H H    B PHE   A 1 156 ? 11.903 -0.419  4.415   0.54 26.86 ?  156 PHE   A H    1 
ATOM   3450 H HA   A PHE   A 1 156 ? 10.810 0.792   6.380   0.46 23.16 ?  156 PHE   A HA   1 
ATOM   3451 H HA   B PHE   A 1 156 ? 10.293 0.744   6.214   0.54 29.58 ?  156 PHE   A HA   1 
ATOM   3452 H HB2  A PHE   A 1 156 ? 12.537 1.692   5.122   0.46 24.16 ?  156 PHE   A HB2  1 
ATOM   3453 H HB2  B PHE   A 1 156 ? 12.574 1.476   5.956   0.54 31.01 ?  156 PHE   A HB2  1 
ATOM   3454 H HB3  A PHE   A 1 156 ? 11.632 1.656   3.819   0.46 24.16 ?  156 PHE   A HB3  1 
ATOM   3455 H HB3  B PHE   A 1 156 ? 12.121 2.155   4.593   0.54 31.01 ?  156 PHE   A HB3  1 
ATOM   3456 H HD1  A PHE   A 1 156 ? 11.534 3.159   7.046   0.46 27.43 ?  156 PHE   A HD1  1 
ATOM   3457 H HD1  B PHE   A 1 156 ? 10.092 2.233   7.459   0.54 35.02 ?  156 PHE   A HD1  1 
ATOM   3458 H HD2  A PHE   A 1 156 ? 10.651 3.664   3.177   0.46 26.68 ?  156 PHE   A HD2  1 
ATOM   3459 H HD2  B PHE   A 1 156 ? 12.666 4.387   5.285   0.54 33.67 ?  156 PHE   A HD2  1 
ATOM   3460 H HE1  A PHE   A 1 156 ? 10.828 5.308   7.492   0.46 28.55 ?  156 PHE   A HE1  1 
ATOM   3461 H HE1  B PHE   A 1 156 ? 9.493  4.122   8.628   0.54 35.53 ?  156 PHE   A HE1  1 
ATOM   3462 H HE2  A PHE   A 1 156 ? 9.942  5.822   3.619   0.46 27.58 ?  156 PHE   A HE2  1 
ATOM   3463 H HE2  B PHE   A 1 156 ? 12.069 6.279   6.452   0.54 34.68 ?  156 PHE   A HE2  1 
ATOM   3464 H HZ   A PHE   A 1 156 ? 10.030 6.647   5.780   0.46 27.52 ?  156 PHE   A HZ   1 
ATOM   3465 H HZ   B PHE   A 1 156 ? 10.481 6.152   8.128   0.54 35.46 ?  156 PHE   A HZ   1 
ATOM   3466 N N    A ASP   A 1 157 ? 8.954  0.391   3.799   0.46 19.80 ?  157 ASP   A N    1 
ATOM   3467 N N    B ASP   A 1 157 ? 8.851  0.413   3.850   0.54 24.57 ?  157 ASP   A N    1 
ATOM   3468 C CA   A ASP   A 1 157 ? 7.630  0.599   3.224   0.46 21.29 ?  157 ASP   A CA   1 
ATOM   3469 C CA   B ASP   A 1 157 ? 7.710  0.768   3.014   0.54 23.53 ?  157 ASP   A CA   1 
ATOM   3470 C C    A ASP   A 1 157 ? 6.668  -0.458  3.756   0.46 21.12 ?  157 ASP   A C    1 
ATOM   3471 C C    B ASP   A 1 157 ? 6.569  -0.145  3.435   0.54 22.84 ?  157 ASP   A C    1 
ATOM   3472 O O    A ASP   A 1 157 ? 6.867  -1.656  3.530   0.46 20.50 ?  157 ASP   A O    1 
ATOM   3473 O O    B ASP   A 1 157 ? 6.640  -1.361  3.230   0.54 22.45 ?  157 ASP   A O    1 
ATOM   3474 C CB   A ASP   A 1 157 ? 7.736  0.508   1.704   0.46 22.62 ?  157 ASP   A CB   1 
ATOM   3475 C CB   B ASP   A 1 157 ? 8.041  0.598   1.531   0.54 22.91 ?  157 ASP   A CB   1 
ATOM   3476 C CG   A ASP   A 1 157 ? 6.523  1.068   0.994   0.46 24.73 ?  157 ASP   A CG   1 
ATOM   3477 C CG   B ASP   A 1 157 ? 6.897  1.013   0.627   0.54 22.42 ?  157 ASP   A CG   1 
ATOM   3478 O OD1  A ASP   A 1 157 ? 6.440  2.305   0.833   0.46 26.20 ?  157 ASP   A OD1  1 
ATOM   3479 O OD1  B ASP   A 1 157 ? 5.844  0.342   0.658   0.54 23.64 ?  157 ASP   A OD1  1 
ATOM   3480 O OD2  A ASP   A 1 157 ? 5.649  0.268   0.596   0.46 25.60 -1 157 ASP   A OD2  1 
ATOM   3481 O OD2  B ASP   A 1 157 ? 7.042  2.018   -0.103  0.54 22.81 -1 157 ASP   A OD2  1 
ATOM   3482 H H    A ASP   A 1 157 ? 9.476  -0.083  3.310   0.46 23.77 ?  157 ASP   A H    1 
ATOM   3483 H H    B ASP   A 1 157 ? 8.944  -0.435  3.968   0.54 29.50 ?  157 ASP   A H    1 
ATOM   3484 H HA   A ASP   A 1 157 ? 7.304  1.475   3.473   0.46 25.57 ?  157 ASP   A HA   1 
ATOM   3485 H HA   B ASP   A 1 157 ? 7.454  1.690   3.175   0.54 28.25 ?  157 ASP   A HA   1 
ATOM   3486 H HB2  A ASP   A 1 157 ? 8.526  0.997   1.418   0.46 27.16 ?  157 ASP   A HB2  1 
ATOM   3487 H HB2  B ASP   A 1 157 ? 8.816  1.141   1.316   0.54 27.51 ?  157 ASP   A HB2  1 
ATOM   3488 H HB3  A ASP   A 1 157 ? 7.818  -0.422  1.451   0.46 27.16 ?  157 ASP   A HB3  1 
ATOM   3489 H HB3  B ASP   A 1 157 ? 8.244  -0.335  1.356   0.54 27.51 ?  157 ASP   A HB3  1 
ATOM   3490 N N    A LYS   A 1 158 ? 5.621  -0.015  4.458   0.46 22.11 ?  158 LYS   A N    1 
ATOM   3491 N N    B LYS   A 1 158 ? 5.528  0.439   4.033   0.54 23.63 ?  158 LYS   A N    1 
ATOM   3492 C CA   A LYS   A 1 158 ? 4.672  -0.957  5.044   0.46 23.31 ?  158 LYS   A CA   1 
ATOM   3493 C CA   B LYS   A 1 158 ? 4.464  -0.371  4.618   0.54 24.46 ?  158 LYS   A CA   1 
ATOM   3494 C C    A LYS   A 1 158 ? 3.948  -1.755  3.964   0.46 23.24 ?  158 LYS   A C    1 
ATOM   3495 C C    B LYS   A 1 158 ? 3.817  -1.266  3.571   0.54 23.52 ?  158 LYS   A C    1 
ATOM   3496 O O    A LYS   A 1 158 ? 3.752  -2.968  4.102   0.46 22.89 ?  158 LYS   A O    1 
ATOM   3497 O O    B LYS   A 1 158 ? 3.659  -2.475  3.779   0.54 22.24 ?  158 LYS   A O    1 
ATOM   3498 C CB   A LYS   A 1 158 ? 3.679  -0.207  5.936   0.46 24.88 ?  158 LYS   A CB   1 
ATOM   3499 C CB   B LYS   A 1 158 ? 3.409  0.527   5.271   0.54 26.87 ?  158 LYS   A CB   1 
ATOM   3500 C CG   A LYS   A 1 158 ? 2.455  -1.016  6.365   0.46 26.28 ?  158 LYS   A CG   1 
ATOM   3501 C CG   B LYS   A 1 158 ? 2.103  -0.207  5.597   0.54 29.80 ?  158 LYS   A CG   1 
ATOM   3502 C CD   A LYS   A 1 158 ? 2.818  -2.257  7.184   0.46 27.68 ?  158 LYS   A CD   1 
ATOM   3503 C CD   B LYS   A 1 158 ? 0.963  0.747   5.910   0.54 33.08 ?  158 LYS   A CD   1 
ATOM   3504 C CE   A LYS   A 1 158 ? 1.554  -2.946  7.694   0.46 28.40 ?  158 LYS   A CE   1 
ATOM   3505 C CE   B LYS   A 1 158 ? 1.106  1.367   7.287   0.54 35.23 ?  158 LYS   A CE   1 
ATOM   3506 N NZ   A LYS   A 1 158 ? 1.817  -4.296  8.265   0.46 28.16 ?  158 LYS   A NZ   1 
ATOM   3507 N NZ   B LYS   A 1 158 ? -0.084 2.189   7.646   0.54 36.19 ?  158 LYS   A NZ   1 
ATOM   3508 H H    A LYS   A 1 158 ? 5.448  0.811   4.606   0.46 26.55 ?  158 LYS   A H    1 
ATOM   3509 H H    B LYS   A 1 158 ? 5.416  1.288   4.100   0.54 28.37 ?  158 LYS   A H    1 
ATOM   3510 H HA   A LYS   A 1 158 ? 5.155  -1.585  5.602   0.46 27.98 ?  158 LYS   A HA   1 
ATOM   3511 H HA   B LYS   A 1 158 ? 4.837  -0.937  5.309   0.54 29.37 ?  158 LYS   A HA   1 
ATOM   3512 H HB2  A LYS   A 1 158 ? 4.142  0.073   6.744   0.46 29.87 ?  158 LYS   A HB2  1 
ATOM   3513 H HB2  B LYS   A 1 158 ? 3.767  0.878   6.106   0.54 32.26 ?  158 LYS   A HB2  1 
ATOM   3514 H HB3  A LYS   A 1 158 ? 3.362  0.575   5.459   0.46 29.87 ?  158 LYS   A HB3  1 
ATOM   3515 H HB3  B LYS   A 1 158 ? 3.200  1.259   4.671   0.54 32.26 ?  158 LYS   A HB3  1 
ATOM   3516 H HG2  A LYS   A 1 158 ? 1.891  -0.454  6.917   0.46 31.55 ?  158 LYS   A HG2  1 
ATOM   3517 H HG2  B LYS   A 1 158 ? 1.815  -0.741  4.842   0.54 35.78 ?  158 LYS   A HG2  1 
ATOM   3518 H HG3  A LYS   A 1 158 ? 1.963  -1.303  5.580   0.46 31.55 ?  158 LYS   A HG3  1 
ATOM   3519 H HG3  B LYS   A 1 158 ? 2.251  -0.773  6.367   0.54 35.78 ?  158 LYS   A HG3  1 
ATOM   3520 H HD2  A LYS   A 1 158 ? 3.306  -2.882  6.626   0.46 33.24 ?  158 LYS   A HD2  1 
ATOM   3521 H HD2  B LYS   A 1 158 ? 0.953  1.461   5.251   0.54 39.71 ?  158 LYS   A HD2  1 
ATOM   3522 H HD3  A LYS   A 1 158 ? 3.357  -1.992  7.947   0.46 33.24 ?  158 LYS   A HD3  1 
ATOM   3523 H HD3  B LYS   A 1 158 ? 0.126  0.255   5.880   0.54 39.71 ?  158 LYS   A HD3  1 
ATOM   3524 H HE2  A LYS   A 1 158 ? 1.147  -2.398  8.383   0.46 34.09 ?  158 LYS   A HE2  1 
ATOM   3525 H HE2  B LYS   A 1 158 ? 1.198  0.661   7.946   0.54 42.29 ?  158 LYS   A HE2  1 
ATOM   3526 H HE3  A LYS   A 1 158 ? 0.940  -3.052  6.956   0.46 34.09 ?  158 LYS   A HE3  1 
ATOM   3527 H HE3  B LYS   A 1 158 ? 1.887  1.941   7.298   0.54 42.29 ?  158 LYS   A HE3  1 
ATOM   3528 H HZ1  A LYS   A 1 158 ? 1.058  -4.659  8.550   0.46 33.81 ?  158 LYS   A HZ1  1 
ATOM   3529 H HZ1  B LYS   A 1 158 ? 0.022  2.541   8.456   0.54 43.45 ?  158 LYS   A HZ1  1 
ATOM   3530 H HZ2  A LYS   A 1 158 ? 2.175  -4.823  7.641   0.46 33.81 ?  158 LYS   A HZ2  1 
ATOM   3531 H HZ2  B LYS   A 1 158 ? -0.189 2.847   7.056   0.54 43.45 ?  158 LYS   A HZ2  1 
ATOM   3532 H HZ3  A LYS   A 1 158 ? 2.385  -4.234  8.948   0.46 33.81 ?  158 LYS   A HZ3  1 
ATOM   3533 H HZ3  B LYS   A 1 158 ? -0.816 1.682   7.646   0.54 43.45 ?  158 LYS   A HZ3  1 
ATOM   3534 N N    A ASN   A 1 159 ? 3.546  -1.092  2.878   0.46 23.30 ?  159 ASN   A N    1 
ATOM   3535 N N    B ASN   A 1 159 ? 3.400  -0.684  2.446   0.54 23.95 ?  159 ASN   A N    1 
ATOM   3536 C CA   A ASN   A 1 159 ? 2.867  -1.801  1.798   0.46 23.36 ?  159 ASN   A CA   1 
ATOM   3537 C CA   B ASN   A 1 159 ? 2.706  -1.481  1.443   0.54 24.86 ?  159 ASN   A CA   1 
ATOM   3538 C C    A ASN   A 1 159 ? 3.764  -2.877  1.194   0.46 22.17 ?  159 ASN   A C    1 
ATOM   3539 C C    B ASN   A 1 159 ? 3.617  -2.542  0.854   0.54 23.26 ?  159 ASN   A C    1 
ATOM   3540 O O    A ASN   A 1 159 ? 3.303  -3.986  0.896   0.46 20.87 ?  159 ASN   A O    1 
ATOM   3541 O O    B ASN   A 1 159 ? 3.155  -3.637  0.515   0.54 22.44 ?  159 ASN   A O    1 
ATOM   3542 C CB   A ASN   A 1 159 ? 2.390  -0.803  0.740   0.46 25.22 ?  159 ASN   A CB   1 
ATOM   3543 C CB   B ASN   A 1 159 ? 2.130  -0.585  0.350   0.54 27.80 ?  159 ASN   A CB   1 
ATOM   3544 C CG   A ASN   A 1 159 ? 1.206  0.022   1.213   0.46 27.21 ?  159 ASN   A CG   1 
ATOM   3545 C CG   B ASN   A 1 159 ? 0.959  0.244   0.839   0.54 30.59 ?  159 ASN   A CG   1 
ATOM   3546 O OD1  A ASN   A 1 159 ? 0.368  -0.466  1.970   0.46 27.67 ?  159 ASN   A OD1  1 
ATOM   3547 O OD1  B ASN   A 1 159 ? 0.169  -0.210  1.667   0.54 32.07 ?  159 ASN   A OD1  1 
ATOM   3548 N ND2  A ASN   A 1 159 ? 1.131  1.275   0.769   0.46 27.88 ?  159 ASN   A ND2  1 
ATOM   3549 N ND2  B ASN   A 1 159 ? 0.845  1.465   0.336   0.54 31.49 ?  159 ASN   A ND2  1 
ATOM   3550 H H    A ASN   A 1 159 ? 3.657  -0.251  2.746   0.46 27.97 ?  159 ASN   A H    1 
ATOM   3551 H H    B ASN   A 1 159 ? 3.504  0.146   2.248   0.54 28.75 ?  159 ASN   A H    1 
ATOM   3552 H HA   A ASN   A 1 159 ? 2.083  -2.240  2.159   0.46 28.05 ?  159 ASN   A HA   1 
ATOM   3553 H HA   B ASN   A 1 159 ? 1.968  -1.940  1.868   0.54 29.84 ?  159 ASN   A HA   1 
ATOM   3554 H HB2  A ASN   A 1 159 ? 3.108  -0.190  0.527   0.46 30.28 ?  159 ASN   A HB2  1 
ATOM   3555 H HB2  B ASN   A 1 159 ? 2.819  0.020   0.039   0.54 33.37 ?  159 ASN   A HB2  1 
ATOM   3556 H HB3  A ASN   A 1 159 ? 2.114  -1.285  -0.055  0.46 30.28 ?  159 ASN   A HB3  1 
ATOM   3557 H HB3  B ASN   A 1 159 ? 1.819  -1.143  -0.381  0.54 33.37 ?  159 ASN   A HB3  1 
ATOM   3558 H HD21 A ASN   A 1 159 ? 0.477  1.782   1.008   0.46 33.47 ?  159 ASN   A HD21 1 
ATOM   3559 H HD21 B ASN   A 1 159 ? 0.199  1.972   0.587   0.54 37.80 ?  159 ASN   A HD21 1 
ATOM   3560 H HD22 A ASN   A 1 159 ? 1.736  1.582   0.243   0.46 33.47 ?  159 ASN   A HD22 1 
ATOM   3561 H HD22 B ASN   A 1 159 ? 1.416  1.744   -0.241  0.54 37.80 ?  159 ASN   A HD22 1 
ATOM   3562 N N    A LEU   A 1 160 ? 5.052  -2.579  1.026   0.46 22.04 ?  160 LEU   A N    1 
ATOM   3563 N N    B LEU   A 1 160 ? 4.912  -2.251  0.743   0.54 21.97 ?  160 LEU   A N    1 
ATOM   3564 C CA   A LEU   A 1 160 ? 5.969  -3.569  0.469   0.46 21.04 ?  160 LEU   A CA   1 
ATOM   3565 C CA   B LEU   A 1 160 ? 5.845  -3.265  0.273   0.54 21.74 ?  160 LEU   A CA   1 
ATOM   3566 C C    A LEU   A 1 160 ? 6.143  -4.754  1.412   0.46 20.69 ?  160 LEU   A C    1 
ATOM   3567 C C    B LEU   A 1 160 ? 6.015  -4.370  1.308   0.54 20.89 ?  160 LEU   A C    1 
ATOM   3568 O O    A LEU   A 1 160 ? 6.167  -5.910  0.973   0.46 21.19 ?  160 LEU   A O    1 
ATOM   3569 O O    B LEU   A 1 160 ? 5.984  -5.558  0.970   0.54 21.20 ?  160 LEU   A O    1 
ATOM   3570 C CB   A LEU   A 1 160 ? 7.319  -2.914  0.182   0.46 20.26 ?  160 LEU   A CB   1 
ATOM   3571 C CB   B LEU   A 1 160 ? 7.191  -2.628  -0.061  0.54 22.16 ?  160 LEU   A CB   1 
ATOM   3572 C CG   A LEU   A 1 160 ? 8.442  -3.870  -0.213  0.46 20.69 ?  160 LEU   A CG   1 
ATOM   3573 C CG   B LEU   A 1 160 ? 8.238  -3.631  -0.533  0.54 23.16 ?  160 LEU   A CG   1 
ATOM   3574 C CD1  A LEU   A 1 160 ? 8.057  -4.643  -1.460  0.46 20.89 ?  160 LEU   A CD1  1 
ATOM   3575 C CD1  B LEU   A 1 160 ? 7.701  -4.425  -1.710  0.54 23.61 ?  160 LEU   A CD1  1 
ATOM   3576 C CD2  A LEU   A 1 160 ? 9.735  -3.102  -0.428  0.46 20.39 ?  160 LEU   A CD2  1 
ATOM   3577 C CD2  B LEU   A 1 160 ? 9.527  -2.924  -0.903  0.54 23.16 ?  160 LEU   A CD2  1 
ATOM   3578 H H    A LEU   A 1 160 ? 5.417  -1.829  1.238   0.46 26.46 ?  160 LEU   A H    1 
ATOM   3579 H H    B LEU   A 1 160 ? 5.272  -1.493  0.934   0.54 26.38 ?  160 LEU   A H    1 
ATOM   3580 H HA   A LEU   A 1 160 ? 5.611  -3.896  -0.369  0.46 25.26 ?  160 LEU   A HA   1 
ATOM   3581 H HA   B LEU   A 1 160 ? 5.488  -3.661  -0.533  0.54 26.10 ?  160 LEU   A HA   1 
ATOM   3582 H HB2  A LEU   A 1 160 ? 7.212  -2.271  -0.541  0.46 24.32 ?  160 LEU   A HB2  1 
ATOM   3583 H HB2  B LEU   A 1 160 ? 7.069  -1.966  -0.766  0.54 26.60 ?  160 LEU   A HB2  1 
ATOM   3584 H HB3  A LEU   A 1 160 ? 7.610  -2.455  0.984   0.46 24.32 ?  160 LEU   A HB3  1 
ATOM   3585 H HB3  B LEU   A 1 160 ? 7.539  -2.199  0.735   0.54 26.60 ?  160 LEU   A HB3  1 
ATOM   3586 H HG   A LEU   A 1 160 ? 8.595  -4.505  0.504   0.46 24.84 ?  160 LEU   A HG   1 
ATOM   3587 H HG   B LEU   A 1 160 ? 8.436  -4.251  0.186   0.54 27.80 ?  160 LEU   A HG   1 
ATOM   3588 H HD11 A LEU   A 1 160 ? 8.819  -5.163  -1.756  0.46 25.08 ?  160 LEU   A HD11 1 
ATOM   3589 H HD11 B LEU   A 1 160 ? 8.415  -4.965  -2.070  0.54 28.34 ?  160 LEU   A HD11 1 
ATOM   3590 H HD12 A LEU   A 1 160 ? 7.315  -5.232  -1.249  0.46 25.08 ?  160 LEU   A HD12 1 
ATOM   3591 H HD12 B LEU   A 1 160 ? 6.981  -5.001  -1.405  0.54 28.34 ?  160 LEU   A HD12 1 
ATOM   3592 H HD13 A LEU   A 1 160 ? 7.795  -4.014  -2.151  0.46 25.08 ?  160 LEU   A HD13 1 
ATOM   3593 H HD13 B LEU   A 1 160 ? 7.372  -3.809  -2.383  0.54 28.34 ?  160 LEU   A HD13 1 
ATOM   3594 H HD21 A LEU   A 1 160 ? 10.436 -3.725  -0.676  0.46 24.48 ?  160 LEU   A HD21 1 
ATOM   3595 H HD21 B LEU   A 1 160 ? 10.175 -3.582  -1.196  0.54 27.80 ?  160 LEU   A HD21 1 
ATOM   3596 H HD22 A LEU   A 1 160 ? 9.603  -2.453  -1.138  0.46 24.48 ?  160 LEU   A HD22 1 
ATOM   3597 H HD22 B LEU   A 1 160 ? 9.345  -2.294  -1.619  0.54 27.80 ?  160 LEU   A HD22 1 
ATOM   3598 H HD23 A LEU   A 1 160 ? 9.974  -2.646  0.395   0.46 24.48 ?  160 LEU   A HD23 1 
ATOM   3599 H HD23 B LEU   A 1 160 ? 9.861  -2.451  -0.125  0.54 27.80 ?  160 LEU   A HD23 1 
ATOM   3600 N N    A TYR   A 1 161 ? 6.281  -4.481  2.710   0.46 19.47 ?  161 TYR   A N    1 
ATOM   3601 N N    B TYR   A 1 161 ? 6.204  -3.999  2.576   0.54 19.91 ?  161 TYR   A N    1 
ATOM   3602 C CA   A TYR   A 1 161 ? 6.425  -5.546  3.697   0.46 19.37 ?  161 TYR   A CA   1 
ATOM   3603 C CA   B TYR   A 1 161 ? 6.301  -5.002  3.634   0.54 19.73 ?  161 TYR   A CA   1 
ATOM   3604 C C    A TYR   A 1 161 ? 5.274  -6.543  3.609   0.46 19.65 ?  161 TYR   A C    1 
ATOM   3605 C C    B TYR   A 1 161 ? 5.083  -5.918  3.626   0.54 20.20 ?  161 TYR   A C    1 
ATOM   3606 O O    A TYR   A 1 161 ? 5.488  -7.761  3.594   0.46 19.89 ?  161 TYR   A O    1 
ATOM   3607 O O    B TYR   A 1 161 ? 5.210  -7.146  3.689   0.54 20.21 ?  161 TYR   A O    1 
ATOM   3608 C CB   A TYR   A 1 161 ? 6.488  -4.928  5.094   0.46 19.83 ?  161 TYR   A CB   1 
ATOM   3609 C CB   B TYR   A 1 161 ? 6.438  -4.322  4.999   0.54 18.90 ?  161 TYR   A CB   1 
ATOM   3610 C CG   A TYR   A 1 161 ? 6.388  -5.939  6.205   0.46 19.78 ?  161 TYR   A CG   1 
ATOM   3611 C CG   B TYR   A 1 161 ? 6.407  -5.307  6.150   0.54 18.13 ?  161 TYR   A CG   1 
ATOM   3612 C CD1  A TYR   A 1 161 ? 7.510  -6.634  6.636   0.46 19.08 ?  161 TYR   A CD1  1 
ATOM   3613 C CD1  B TYR   A 1 161 ? 7.562  -5.967  6.556   0.54 18.35 ?  161 TYR   A CD1  1 
ATOM   3614 C CD2  A TYR   A 1 161 ? 5.174  -6.202  6.820   0.46 19.47 ?  161 TYR   A CD2  1 
ATOM   3615 C CD2  B TYR   A 1 161 ? 5.223  -5.591  6.823   0.54 18.43 ?  161 TYR   A CD2  1 
ATOM   3616 C CE1  A TYR   A 1 161 ? 7.424  -7.567  7.645   0.46 18.90 ?  161 TYR   A CE1  1 
ATOM   3617 C CE1  B TYR   A 1 161 ? 7.545  -6.871  7.598   0.54 18.27 ?  161 TYR   A CE1  1 
ATOM   3618 C CE2  A TYR   A 1 161 ? 5.077  -7.132  7.830   0.46 18.87 ?  161 TYR   A CE2  1 
ATOM   3619 C CE2  B TYR   A 1 161 ? 5.195  -6.502  7.869   0.54 18.88 ?  161 TYR   A CE2  1 
ATOM   3620 C CZ   A TYR   A 1 161 ? 6.204  -7.810  8.241   0.46 19.60 ?  161 TYR   A CZ   1 
ATOM   3621 C CZ   B TYR   A 1 161 ? 6.357  -7.136  8.253   0.54 18.32 ?  161 TYR   A CZ   1 
ATOM   3622 O OH   A TYR   A 1 161 ? 6.109  -8.735  9.250   0.46 21.00 ?  161 TYR   A OH   1 
ATOM   3623 O OH   B TYR   A 1 161 ? 6.323  -8.041  9.291   0.54 19.25 ?  161 TYR   A OH   1 
ATOM   3624 H H    A TYR   A 1 161 ? 6.292  -3.693  3.041   0.46 23.38 ?  161 TYR   A H    1 
ATOM   3625 H H    B TYR   A 1 161 ? 6.272  -3.184  2.844   0.54 23.91 ?  161 TYR   A H    1 
ATOM   3626 H HA   A TYR   A 1 161 ? 7.253  -6.026  3.538   0.46 23.26 ?  161 TYR   A HA   1 
ATOM   3627 H HA   B TYR   A 1 161 ? 7.095  -5.541  3.490   0.54 23.69 ?  161 TYR   A HA   1 
ATOM   3628 H HB2  A TYR   A 1 161 ? 7.335  -4.461  5.190   0.46 23.81 ?  161 TYR   A HB2  1 
ATOM   3629 H HB2  B TYR   A 1 161 ? 7.285  -3.845  5.035   0.54 22.69 ?  161 TYR   A HB2  1 
ATOM   3630 H HB3  A TYR   A 1 161 ? 5.755  -4.302  5.194   0.46 23.81 ?  161 TYR   A HB3  1 
ATOM   3631 H HB3  B TYR   A 1 161 ? 5.705  -3.698  5.117   0.54 22.69 ?  161 TYR   A HB3  1 
ATOM   3632 H HD1  A TYR   A 1 161 ? 8.333  -6.471  6.233   0.46 22.91 ?  161 TYR   A HD1  1 
ATOM   3633 H HD1  B TYR   A 1 161 ? 8.364  -5.788  6.120   0.54 22.03 ?  161 TYR   A HD1  1 
ATOM   3634 H HD2  A TYR   A 1 161 ? 4.411  -5.747  6.544   0.46 23.37 ?  161 TYR   A HD2  1 
ATOM   3635 H HD2  B TYR   A 1 161 ? 4.437  -5.162  6.570   0.54 22.14 ?  161 TYR   A HD2  1 
ATOM   3636 H HE1  A TYR   A 1 161 ? 8.185  -8.026  7.923   0.46 22.69 ?  161 TYR   A HE1  1 
ATOM   3637 H HE1  B TYR   A 1 161 ? 8.329  -7.297  7.863   0.54 21.94 ?  161 TYR   A HE1  1 
ATOM   3638 H HE2  A TYR   A 1 161 ? 4.256  -7.302  8.236   0.46 22.66 ?  161 TYR   A HE2  1 
ATOM   3639 H HE2  B TYR   A 1 161 ? 4.398  -6.674  8.317   0.54 22.67 ?  161 TYR   A HE2  1 
ATOM   3640 H HH   A TYR   A 1 161 ? 5.313  -8.786  9.517   0.46 25.21 ?  161 TYR   A HH   1 
ATOM   3641 H HH   B TYR   A 1 161 ? 5.543  -8.096  9.603   0.54 23.11 ?  161 TYR   A HH   1 
ATOM   3642 N N    A ASP   A 1 162 ? 4.038  -6.038  3.567   0.46 19.63 ?  162 ASP   A N    1 
ATOM   3643 N N    B ASP   A 1 162 ? 3.888  -5.325  3.574   0.54 21.23 ?  162 ASP   A N    1 
ATOM   3644 C CA   A ASP   A 1 162 ? 2.878  -6.923  3.472   0.46 20.22 ?  162 ASP   A CA   1 
ATOM   3645 C CA   B ASP   A 1 162 ? 2.658  -6.114  3.584   0.54 22.82 ?  162 ASP   A CA   1 
ATOM   3646 C C    A ASP   A 1 162 ? 2.941  -7.772  2.209   0.46 20.29 ?  162 ASP   A C    1 
ATOM   3647 C C    B ASP   A 1 162 ? 2.623  -7.116  2.438   0.54 22.84 ?  162 ASP   A C    1 
ATOM   3648 O O    A ASP   A 1 162 ? 2.589  -8.958  2.227   0.46 20.11 ?  162 ASP   A O    1 
ATOM   3649 O O    B ASP   A 1 162 ? 2.160  -8.250  2.609   0.54 23.40 ?  162 ASP   A O    1 
ATOM   3650 C CB   A ASP   A 1 162 ? 1.582  -6.107  3.481   0.46 21.00 ?  162 ASP   A CB   1 
ATOM   3651 C CB   B ASP   A 1 162 ? 1.447  -5.189  3.506   0.54 24.57 ?  162 ASP   A CB   1 
ATOM   3652 C CG   A ASP   A 1 162 ? 1.236  -5.547  4.852   0.46 22.26 ?  162 ASP   A CG   1 
ATOM   3653 C CG   B ASP   A 1 162 ? 1.221  -4.422  4.793   0.54 25.60 ?  162 ASP   A CG   1 
ATOM   3654 O OD1  A ASP   A 1 162 ? 1.854  -5.960  5.856   0.46 22.76 ?  162 ASP   A OD1  1 
ATOM   3655 O OD1  B ASP   A 1 162 ? 1.814  -4.811  5.825   0.54 26.28 ?  162 ASP   A OD1  1 
ATOM   3656 O OD2  A ASP   A 1 162 ? 0.326  -4.692  4.919   0.46 22.82 -1 162 ASP   A OD2  1 
ATOM   3657 O OD2  B ASP   A 1 162 ? 0.451  -3.438  4.779   0.54 25.67 -1 162 ASP   A OD2  1 
ATOM   3658 H H    A ASP   A 1 162 ? 3.847  -5.203  3.596   0.46 23.57 ?  162 ASP   A H    1 
ATOM   3659 H H    B ASP   A 1 162 ? 3.769  -4.472  3.554   0.54 25.49 ?  162 ASP   A H    1 
ATOM   3660 H HA   A ASP   A 1 162 ? 2.864  -7.522  4.233   0.46 24.28 ?  162 ASP   A HA   1 
ATOM   3661 H HA   B ASP   A 1 162 ? 2.610  -6.606  4.417   0.54 27.40 ?  162 ASP   A HA   1 
ATOM   3662 H HB2  A ASP   A 1 162 ? 1.670  -5.366  2.862   0.46 25.21 ?  162 ASP   A HB2  1 
ATOM   3663 H HB2  B ASP   A 1 162 ? 1.584  -4.552  2.784   0.54 29.50 ?  162 ASP   A HB2  1 
ATOM   3664 H HB3  A ASP   A 1 162 ? 0.845  -6.678  3.212   0.46 25.21 ?  162 ASP   A HB3  1 
ATOM   3665 H HB3  B ASP   A 1 162 ? 0.659  -5.727  3.322   0.54 29.50 ?  162 ASP   A HB3  1 
ATOM   3666 N N    A LYS   A 1 163 ? 3.385  -7.177  1.100   0.46 21.05 ?  163 LYS   A N    1 
ATOM   3667 N N    B LYS   A 1 163 ? 3.084  -6.714  1.253   0.54 22.99 ?  163 LYS   A N    1 
ATOM   3668 C CA   A LYS   A 1 163 ? 3.494  -7.920  -0.150  0.46 21.60 ?  163 LYS   A CA   1 
ATOM   3669 C CA   B LYS   A 1 163 ? 3.116  -7.656  0.142   0.54 24.13 ?  163 LYS   A CA   1 
ATOM   3670 C C    A LYS   A 1 163 ? 4.576  -8.990  -0.062  0.46 20.12 ?  163 LYS   A C    1 
ATOM   3671 C C    B LYS   A 1 163 ? 4.197  -8.710  0.346   0.54 22.54 ?  163 LYS   A C    1 
ATOM   3672 O O    A LYS   A 1 163 ? 4.395  -10.108 -0.560  0.46 19.51 ?  163 LYS   A O    1 
ATOM   3673 O O    B LYS   A 1 163 ? 3.998  -9.884  0.011   0.54 22.71 ?  163 LYS   A O    1 
ATOM   3674 C CB   A LYS   A 1 163 ? 3.769  -6.950  -1.300  0.46 23.59 ?  163 LYS   A CB   1 
ATOM   3675 C CB   B LYS   A 1 163 ? 3.320  -6.920  -1.180  0.54 27.42 ?  163 LYS   A CB   1 
ATOM   3676 C CG   A LYS   A 1 163 ? 3.692  -7.593  -2.667  0.46 26.07 ?  163 LYS   A CG   1 
ATOM   3677 C CG   B LYS   A 1 163 ? 3.441  -7.856  -2.375  0.54 30.15 ?  163 LYS   A CG   1 
ATOM   3678 C CD   A LYS   A 1 163 ? 4.101  -6.637  -3.768  0.46 28.99 ?  163 LYS   A CD   1 
ATOM   3679 C CD   B LYS   A 1 163 ? 4.343  -7.292  -3.448  0.54 32.64 ?  163 LYS   A CD   1 
ATOM   3680 C CE   A LYS   A 1 163 ? 4.020  -7.320  -5.124  0.46 31.19 ?  163 LYS   A CE   1 
ATOM   3681 C CE   B LYS   A 1 163 ? 3.545  -6.857  -4.659  0.54 34.51 ?  163 LYS   A CE   1 
ATOM   3682 N NZ   A LYS   A 1 163 ? 4.759  -6.573  -6.176  0.46 32.49 ?  163 LYS   A NZ   1 
ATOM   3683 N NZ   B LYS   A 1 163 ? 4.443  -6.463  -5.776  0.54 35.54 ?  163 LYS   A NZ   1 
ATOM   3684 H H    A LYS   A 1 163 ? 3.638  -6.358  1.049   0.46 25.27 ?  163 LYS   A H    1 
ATOM   3685 H H    B LYS   A 1 163 ? 3.379  -5.924  1.070   0.54 27.60 ?  163 LYS   A H    1 
ATOM   3686 H HA   A LYS   A 1 163 ? 2.658  -8.367  -0.329  0.46 25.94 ?  163 LYS   A HA   1 
ATOM   3687 H HA   B LYS   A 1 163 ? 2.272  -8.116  0.097   0.54 28.97 ?  163 LYS   A HA   1 
ATOM   3688 H HB2  A LYS   A 1 163 ? 3.108  -6.238  -1.272  0.46 28.33 ?  163 LYS   A HB2  1 
ATOM   3689 H HB2  B LYS   A 1 163 ? 2.553  -6.342  -1.339  0.54 32.92 ?  163 LYS   A HB2  1 
ATOM   3690 H HB3  A LYS   A 1 163 ? 4.658  -6.576  -1.198  0.46 28.33 ?  163 LYS   A HB3  1 
ATOM   3691 H HB3  B LYS   A 1 163 ? 4.126  -6.386  -1.125  0.54 32.92 ?  163 LYS   A HB3  1 
ATOM   3692 H HG2  A LYS   A 1 163 ? 4.289  -8.357  -2.694  0.46 31.30 ?  163 LYS   A HG2  1 
ATOM   3693 H HG2  B LYS   A 1 163 ? 3.804  -8.715  -2.107  0.54 36.19 ?  163 LYS   A HG2  1 
ATOM   3694 H HG3  A LYS   A 1 163 ? 2.779  -7.875  -2.835  0.46 31.30 ?  163 LYS   A HG3  1 
ATOM   3695 H HG3  B LYS   A 1 163 ? 2.561  -7.982  -2.758  0.54 36.19 ?  163 LYS   A HG3  1 
ATOM   3696 H HD2  A LYS   A 1 163 ? 3.503  -5.874  -3.773  0.46 34.81 ?  163 LYS   A HD2  1 
ATOM   3697 H HD2  B LYS   A 1 163 ? 4.824  -6.521  -3.106  0.54 39.18 ?  163 LYS   A HD2  1 
ATOM   3698 H HD3  A LYS   A 1 163 ? 5.017  -6.349  -3.621  0.46 34.81 ?  163 LYS   A HD3  1 
ATOM   3699 H HD3  B LYS   A 1 163 ? 4.970  -7.978  -3.724  0.54 39.18 ?  163 LYS   A HD3  1 
ATOM   3700 H HE2  A LYS   A 1 163 ? 4.392  -8.213  -5.061  0.46 37.44 ?  163 LYS   A HE2  1 
ATOM   3701 H HE2  B LYS   A 1 163 ? 2.991  -7.594  -4.958  0.54 41.43 ?  163 LYS   A HE2  1 
ATOM   3702 H HE3  A LYS   A 1 163 ? 3.092  -7.372  -5.390  0.46 37.44 ?  163 LYS   A HE3  1 
ATOM   3703 H HE3  B LYS   A 1 163 ? 2.996  -6.094  -4.423  0.54 41.43 ?  163 LYS   A HE3  1 
ATOM   3704 H HZ1  A LYS   A 1 163 ? 4.692  -7.001  -6.953  0.46 39.00 ?  163 LYS   A HZ1  1 
ATOM   3705 H HZ1  B LYS   A 1 163 ? 3.961  -6.212  -6.479  0.54 42.67 ?  163 LYS   A HZ1  1 
ATOM   3706 H HZ2  A LYS   A 1 163 ? 4.415  -5.757  -6.263  0.46 39.00 ?  163 LYS   A HZ2  1 
ATOM   3707 H HZ2  B LYS   A 1 163 ? 4.964  -5.787  -5.523  0.54 42.67 ?  163 LYS   A HZ2  1 
ATOM   3708 H HZ3  A LYS   A 1 163 ? 5.618  -6.505  -5.955  0.46 39.00 ?  163 LYS   A HZ3  1 
ATOM   3709 H HZ3  B LYS   A 1 163 ? 4.958  -7.152  -6.009  0.54 42.67 ?  163 LYS   A HZ3  1 
ATOM   3710 N N    A LEU   A 1 164 ? 5.709  -8.663  0.566   0.46 18.34 ?  164 LEU   A N    1 
ATOM   3711 N N    B LEU   A 1 164 ? 5.352  -8.312  0.882   0.54 20.76 ?  164 LEU   A N    1 
ATOM   3712 C CA   A LEU   A 1 164 ? 6.785  -9.636  0.740   0.46 17.66 ?  164 LEU   A CA   1 
ATOM   3713 C CA   B LEU   A 1 164 ? 6.437  -9.270  1.068   0.54 20.38 ?  164 LEU   A CA   1 
ATOM   3714 C C    A LEU   A 1 164 ? 6.323  -10.820 1.578   0.46 17.54 ?  164 LEU   A C    1 
ATOM   3715 C C    B LEU   A 1 164 ? 6.041  -10.388 2.028   0.54 20.38 ?  164 LEU   A C    1 
ATOM   3716 O O    A LEU   A 1 164 ? 6.582  -11.979 1.238   0.46 17.84 ?  164 LEU   A O    1 
ATOM   3717 O O    B LEU   A 1 164 ? 6.418  -11.547 1.823   0.54 20.10 ?  164 LEU   A O    1 
ATOM   3718 C CB   A LEU   A 1 164 ? 7.976  -8.959  1.419   0.46 17.33 ?  164 LEU   A CB   1 
ATOM   3719 C CB   B LEU   A 1 164 ? 7.694  -8.548  1.558   0.54 19.79 ?  164 LEU   A CB   1 
ATOM   3720 C CG   A LEU   A 1 164 ? 8.776  -7.969  0.574   0.46 17.09 ?  164 LEU   A CG   1 
ATOM   3721 C CG   B LEU   A 1 164 ? 8.398  -7.649  0.538   0.54 19.85 ?  164 LEU   A CG   1 
ATOM   3722 C CD1  A LEU   A 1 164 ? 9.636  -7.065  1.457   0.46 16.89 ?  164 LEU   A CD1  1 
ATOM   3723 C CD1  B LEU   A 1 164 ? 9.579  -6.926  1.176   0.54 20.34 ?  164 LEU   A CD1  1 
ATOM   3724 C CD2  A LEU   A 1 164 ? 9.632  -8.734  -0.420  0.46 16.81 ?  164 LEU   A CD2  1 
ATOM   3725 C CD2  B LEU   A 1 164 ? 8.851  -8.452  -0.671  0.54 20.20 ?  164 LEU   A CD2  1 
ATOM   3726 H H    A LEU   A 1 164 ? 5.882  -7.886  0.898   0.46 22.02 ?  164 LEU   A H    1 
ATOM   3727 H H    B LEU   A 1 164 ? 5.531  -7.508  1.138   0.54 24.93 ?  164 LEU   A H    1 
ATOM   3728 H HA   A LEU   A 1 164 ? 7.077  -9.964  -0.128  0.46 21.20 ?  164 LEU   A HA   1 
ATOM   3729 H HA   B LEU   A 1 164 ? 6.649  -9.674  0.212   0.54 24.47 ?  164 LEU   A HA   1 
ATOM   3730 H HB2  A LEU   A 1 164 ? 7.653  -8.476  2.193   0.46 20.81 ?  164 LEU   A HB2  1 
ATOM   3731 H HB2  B LEU   A 1 164 ? 7.455  -7.986  2.311   0.54 23.76 ?  164 LEU   A HB2  1 
ATOM   3732 H HB3  A LEU   A 1 164 ? 8.597  -9.650  1.709   0.46 20.81 ?  164 LEU   A HB3  1 
ATOM   3733 H HB3  B LEU   A 1 164 ? 8.341  -9.212  1.844   0.54 23.76 ?  164 LEU   A HB3  1 
ATOM   3734 H HG   A LEU   A 1 164 ? 8.164  -7.408  0.075   0.46 20.53 ?  164 LEU   A HG   1 
ATOM   3735 H HG   B LEU   A 1 164 ? 7.776  -6.975  0.225   0.54 23.84 ?  164 LEU   A HG   1 
ATOM   3736 H HD11 A LEU   A 1 164 ? 10.134 -6.450  0.895   0.46 20.29 ?  164 LEU   A HD11 1 
ATOM   3737 H HD11 B LEU   A 1 164 ? 10.003 -6.361  0.511   0.54 24.42 ?  164 LEU   A HD11 1 
ATOM   3738 H HD12 A LEU   A 1 164 ? 9.058  -6.566  2.057   0.46 20.29 ?  164 LEU   A HD12 1 
ATOM   3739 H HD12 B LEU   A 1 164 ? 9.256  -6.384  1.912   0.54 24.42 ?  164 LEU   A HD12 1 
ATOM   3740 H HD13 A LEU   A 1 164 ? 10.250 -7.613  1.972   0.46 20.29 ?  164 LEU   A HD13 1 
ATOM   3741 H HD13 B LEU   A 1 164 ? 10.213 -7.585  1.503   0.54 24.42 ?  164 LEU   A HD13 1 
ATOM   3742 H HD21 A LEU   A 1 164 ? 10.163 -8.104  -0.935  0.46 20.19 ?  164 LEU   A HD21 1 
ATOM   3743 H HD21 B LEU   A 1 164 ? 9.465  -7.917  -1.197  0.54 24.25 ?  164 LEU   A HD21 1 
ATOM   3744 H HD22 A LEU   A 1 164 ? 10.220 -9.338  0.063   0.46 20.19 ?  164 LEU   A HD22 1 
ATOM   3745 H HD22 B LEU   A 1 164 ? 9.290  -9.260  -0.366  0.54 24.25 ?  164 LEU   A HD22 1 
ATOM   3746 H HD23 A LEU   A 1 164 ? 9.056  -9.240  -1.014  0.46 20.19 ?  164 LEU   A HD23 1 
ATOM   3747 H HD23 B LEU   A 1 164 ? 8.073  -8.681  -1.206  0.54 24.25 ?  164 LEU   A HD23 1 
ATOM   3748 N N    A VAL   A 1 165 ? 5.660  -10.539 2.700   0.46 17.00 ?  165 VAL   A N    1 
ATOM   3749 N N    B VAL   A 1 165 ? 5.285  -10.064 3.084   0.54 19.97 ?  165 VAL   A N    1 
ATOM   3750 C CA   A VAL   A 1 165 ? 5.189  -11.599 3.584   0.46 17.28 ?  165 VAL   A CA   1 
ATOM   3751 C CA   B VAL   A 1 165 ? 4.904  -11.067 4.083   0.54 20.90 ?  165 VAL   A CA   1 
ATOM   3752 C C    A VAL   A 1 165 ? 4.115  -12.424 2.891   0.46 17.76 ?  165 VAL   A C    1 
ATOM   3753 C C    B VAL   A 1 165 ? 3.690  -11.886 3.677   0.54 21.20 ?  165 VAL   A C    1 
ATOM   3754 O O    A VAL   A 1 165 ? 4.203  -13.655 2.826   0.46 17.49 ?  165 VAL   A O    1 
ATOM   3755 O O    B VAL   A 1 165 ? 3.264  -12.768 4.442   0.54 20.81 ?  165 VAL   A O    1 
ATOM   3756 C CB   A VAL   A 1 165 ? 4.679  -10.989 4.902   0.46 18.09 ?  165 VAL   A CB   1 
ATOM   3757 C CB   B VAL   A 1 165 ? 4.681  -10.465 5.486   0.54 21.35 ?  165 VAL   A CB   1 
ATOM   3758 C CG1  A VAL   A 1 165 ? 3.942  -12.027 5.731   0.46 17.40 ?  165 VAL   A CG1  1 
ATOM   3759 C CG1  B VAL   A 1 165 ? 5.972  -9.848  6.006   0.54 22.31 ?  165 VAL   A CG1  1 
ATOM   3760 C CG2  A VAL   A 1 165 ? 5.835  -10.384 5.689   0.46 19.01 ?  165 VAL   A CG2  1 
ATOM   3761 C CG2  B VAL   A 1 165 ? 3.539  -9.446  5.479   0.54 20.69 ?  165 VAL   A CG2  1 
ATOM   3762 H H    A VAL   A 1 165 ? 5.480  -9.748  2.967   0.46 20.41 ?  165 VAL   A H    1 
ATOM   3763 H H    B VAL   A 1 165 ? 4.996  -9.269  3.241   0.54 23.97 ?  165 VAL   A H    1 
ATOM   3764 H HA   A VAL   A 1 165 ? 5.929  -12.190 3.794   0.46 20.75 ?  165 VAL   A HA   1 
ATOM   3765 H HA   B VAL   A 1 165 ? 5.646  -11.681 4.166   0.54 25.10 ?  165 VAL   A HA   1 
ATOM   3766 H HB   A VAL   A 1 165 ? 4.057  -10.275 4.695   0.46 21.72 ?  165 VAL   A HB   1 
ATOM   3767 H HB   B VAL   A 1 165 ? 4.434  -11.179 6.092   0.54 25.64 ?  165 VAL   A HB   1 
ATOM   3768 H HG11 A VAL   A 1 165 ? 3.875  -11.708 6.643   0.46 20.90 ?  165 VAL   A HG11 1 
ATOM   3769 H HG11 B VAL   A 1 165 ? 5.833  -9.545  6.917   0.54 26.79 ?  165 VAL   A HG11 1 
ATOM   3770 H HG12 A VAL   A 1 165 ? 3.052  -12.152 5.361   0.46 20.90 ?  165 VAL   A HG12 1 
ATOM   3771 H HG12 B VAL   A 1 165 ? 6.673  -10.519 5.986   0.54 26.79 ?  165 VAL   A HG12 1 
ATOM   3772 H HG13 A VAL   A 1 165 ? 4.434  -12.860 5.704   0.46 20.90 ?  165 VAL   A HG13 1 
ATOM   3773 H HG13 B VAL   A 1 165 ? 6.216  -9.099  5.441   0.54 26.79 ?  165 VAL   A HG13 1 
ATOM   3774 H HG21 A VAL   A 1 165 ? 5.493  -10.012 6.517   0.46 22.83 ?  165 VAL   A HG21 1 
ATOM   3775 H HG21 B VAL   A 1 165 ? 3.463  -9.051  6.363   0.54 24.84 ?  165 VAL   A HG21 1 
ATOM   3776 H HG22 A VAL   A 1 165 ? 6.484  -11.079 5.882   0.46 22.83 ?  165 VAL   A HG22 1 
ATOM   3777 H HG22 B VAL   A 1 165 ? 3.731  -8.755  4.826   0.54 24.84 ?  165 VAL   A HG22 1 
ATOM   3778 H HG23 A VAL   A 1 165 ? 6.248  -9.685  5.157   0.46 22.83 ?  165 VAL   A HG23 1 
ATOM   3779 H HG23 B VAL   A 1 165 ? 2.712  -9.898  5.249   0.54 24.84 ?  165 VAL   A HG23 1 
ATOM   3780 N N    A SER   A 1 166 ? 3.095  -11.750 2.352   0.46 18.50 ?  166 SER   A N    1 
ATOM   3781 N N    B SER   A 1 166 ? 3.112  -11.624 2.507   0.54 21.39 ?  166 SER   A N    1 
ATOM   3782 C CA   A SER   A 1 166 ? 1.976  -12.446 1.728   0.46 19.26 ?  166 SER   A CA   1 
ATOM   3783 C CA   B SER   A 1 166 ? 2.036  -12.445 1.969   0.54 22.13 ?  166 SER   A CA   1 
ATOM   3784 C C    A SER   A 1 166 ? 2.419  -13.332 0.576   0.46 19.49 ?  166 SER   A C    1 
ATOM   3785 C C    B SER   A 1 166 ? 2.428  -13.181 0.692   0.54 22.70 ?  166 SER   A C    1 
ATOM   3786 O O    A SER   A 1 166 ? 1.805  -14.379 0.335   0.46 20.66 ?  166 SER   A O    1 
ATOM   3787 O O    B SER   A 1 166 ? 1.555  -13.763 0.036   0.54 22.40 ?  166 SER   A O    1 
ATOM   3788 C CB   A SER   A 1 166 ? 0.950  -11.433 1.211   0.46 20.91 ?  166 SER   A CB   1 
ATOM   3789 C CB   B SER   A 1 166 ? 0.783  -11.599 1.730   0.54 23.97 ?  166 SER   A CB   1 
ATOM   3790 O OG   A SER   A 1 166 ? 0.418  -10.660 2.271   0.46 23.43 ?  166 SER   A OG   1 
ATOM   3791 O OG   B SER   A 1 166 ? 0.108  -11.344 2.949   0.54 27.24 ?  166 SER   A OG   1 
ATOM   3792 H H    A SER   A 1 166 ? 3.031  -10.897 2.331   0.46 22.21 ?  166 SER   A H    1 
ATOM   3793 H H    B SER   A 1 166 ? 3.324  -10.956 2.005   0.54 25.68 ?  166 SER   A H    1 
ATOM   3794 H HA   A SER   A 1 166 ? 1.535  -13.008 2.383   0.46 23.13 ?  166 SER   A HA   1 
ATOM   3795 H HA   B SER   A 1 166 ? 1.805  -13.114 2.625   0.54 26.57 ?  166 SER   A HA   1 
ATOM   3796 H HB2  A SER   A 1 166 ? 1.384  -10.847 0.568   0.46 25.10 ?  166 SER   A HB2  1 
ATOM   3797 H HB2  B SER   A 1 166 ? 1.041  -10.758 1.315   0.54 28.78 ?  166 SER   A HB2  1 
ATOM   3798 H HB3  A SER   A 1 166 ? 0.223  -11.910 0.776   0.46 25.10 ?  166 SER   A HB3  1 
ATOM   3799 H HB3  B SER   A 1 166 ? 0.178  -12.082 1.149   0.54 28.78 ?  166 SER   A HB3  1 
ATOM   3800 H HG   A SER   A 1 166 ? 1.036  -10.226 2.643   0.46 28.12 ?  166 SER   A HG   1 
ATOM   3801 H HG   B SER   A 1 166 ? -0.561 -10.858 2.812   0.54 32.70 ?  166 SER   A HG   1 
ATOM   3802 N N    A SER   A 1 167 ? 3.447  -12.921 -0.170  0.46 19.89 ?  167 SER   A N    1 
ATOM   3803 N N    B SER   A 1 167 ? 3.707  -13.179 0.323   0.54 24.66 ?  167 SER   A N    1 
ATOM   3804 C CA   A SER   A 1 167 ? 3.894  -13.667 -1.339  0.46 19.58 ?  167 SER   A CA   1 
ATOM   3805 C CA   B SER   A 1 167 ? 4.172  -13.874 -0.868  0.54 26.46 ?  167 SER   A CA   1 
ATOM   3806 C C    A SER   A 1 167 ? 5.067  -14.598 -1.047  0.46 19.45 ?  167 SER   A C    1 
ATOM   3807 C C    B SER   A 1 167 ? 4.911  -15.146 -0.472  0.54 27.65 ?  167 SER   A C    1 
ATOM   3808 O O    A SER   A 1 167 ? 5.584  -15.227 -1.976  0.46 20.57 ?  167 SER   A O    1 
ATOM   3809 O O    B SER   A 1 167 ? 5.345  -15.308 0.672   0.54 26.75 ?  167 SER   A O    1 
ATOM   3810 C CB   A SER   A 1 167 ? 4.276  -12.708 -2.476  0.46 20.16 ?  167 SER   A CB   1 
ATOM   3811 C CB   B SER   A 1 167 ? 5.113  -12.992 -1.698  0.54 27.50 ?  167 SER   A CB   1 
ATOM   3812 O OG   A SER   A 1 167 ? 5.385  -11.899 -2.118  0.46 20.58 ?  167 SER   A OG   1 
ATOM   3813 O OG   B SER   A 1 167 ? 4.792  -11.615 -1.591  0.54 28.07 ?  167 SER   A OG   1 
ATOM   3814 H H    A SER   A 1 167 ? 3.888  -12.192 -0.027  0.46 23.88 ?  167 SER   A H    1 
ATOM   3815 H H    B SER   A 1 167 ? 4.335  -12.771 0.755   0.54 29.60 ?  167 SER   A H    1 
ATOM   3816 H HA   A SER   A 1 167 ? 3.148  -14.204 -1.657  0.46 23.51 ?  167 SER   A HA   1 
ATOM   3817 H HA   B SER   A 1 167 ? 3.414  -14.116 -1.421  0.54 31.77 ?  167 SER   A HA   1 
ATOM   3818 H HB2  A SER   A 1 167 ? 4.505  -13.231 -3.263  0.46 24.20 ?  167 SER   A HB2  1 
ATOM   3819 H HB2  B SER   A 1 167 ? 6.013  -13.140 -1.388  0.54 33.02 ?  167 SER   A HB2  1 
ATOM   3820 H HB3  A SER   A 1 167 ? 3.519  -12.131 -2.676  0.46 24.20 ?  167 SER   A HB3  1 
ATOM   3821 H HB3  B SER   A 1 167 ? 5.043  -13.255 -2.628  0.54 33.02 ?  167 SER   A HB3  1 
ATOM   3822 H HG   A SER   A 1 167 ? 5.199  -11.453 -1.432  0.46 24.71 ?  167 SER   A HG   1 
ATOM   3823 H HG   B SER   A 1 167 ? 4.904  -11.352 -0.802  0.54 33.70 ?  167 SER   A HG   1 
ATOM   3824 N N    A PHE   A 1 168 ? 5.510  -14.698 0.204   0.46 19.28 ?  168 PHE   A N    1 
ATOM   3825 N N    B PHE   A 1 168 ? 5.043  -16.059 -1.431  0.54 30.16 ?  168 PHE   A N    1 
ATOM   3826 C CA   A PHE   A 1 168 ? 6.701  -15.486 0.499   0.46 18.89 ?  168 PHE   A CA   1 
ATOM   3827 C CA   B PHE   A 1 168 ? 5.867  -17.235 -1.192  0.54 33.62 ?  168 PHE   A CA   1 
ATOM   3828 C C    A PHE   A 1 168 ? 6.393  -16.972 0.414   0.46 19.33 ?  168 PHE   A C    1 
ATOM   3829 C C    B PHE   A 1 168 ? 7.341  -16.891 -1.382  0.54 35.26 ?  168 PHE   A C    1 
ATOM   3830 O O    A PHE   A 1 168 ? 5.410  -17.448 0.988   0.46 21.52 ?  168 PHE   A O    1 
ATOM   3831 O O    B PHE   A 1 168 ? 7.700  -15.918 -2.050  0.54 35.06 ?  168 PHE   A O    1 
ATOM   3832 C CB   A PHE   A 1 168 ? 7.238  -15.167 1.892   0.46 18.48 ?  168 PHE   A CB   1 
ATOM   3833 C CB   B PHE   A 1 168 ? 5.465  -18.414 -2.091  0.54 35.19 ?  168 PHE   A CB   1 
ATOM   3834 C CG   A PHE   A 1 168 ? 8.497  -15.922 2.227   0.46 18.06 ?  168 PHE   A CG   1 
ATOM   3835 C CG   B PHE   A 1 168 ? 5.900  -18.288 -3.539  0.54 36.80 ?  168 PHE   A CG   1 
ATOM   3836 C CD1  A PHE   A 1 168 ? 9.695  -15.568 1.638   0.46 18.09 ?  168 PHE   A CD1  1 
ATOM   3837 C CD1  B PHE   A 1 168 ? 7.207  -18.565 -3.923  0.54 37.48 ?  168 PHE   A CD1  1 
ATOM   3838 C CD2  A PHE   A 1 168 ? 8.482  -16.991 3.115   0.46 17.06 ?  168 PHE   A CD2  1 
ATOM   3839 C CD2  B PHE   A 1 168 ? 4.986  -17.941 -4.521  0.54 37.23 ?  168 PHE   A CD2  1 
ATOM   3840 C CE1  A PHE   A 1 168 ? 10.861 -16.258 1.932   0.46 17.93 ?  168 PHE   A CE1  1 
ATOM   3841 C CE1  B PHE   A 1 168 ? 7.597  -18.463 -5.248  0.54 37.65 ?  168 PHE   A CE1  1 
ATOM   3842 C CE2  A PHE   A 1 168 ? 9.651  -17.684 3.414   0.46 17.14 ?  168 PHE   A CE2  1 
ATOM   3843 C CE2  B PHE   A 1 168 ? 5.370  -17.842 -5.849  0.54 37.63 ?  168 PHE   A CE2  1 
ATOM   3844 C CZ   A PHE   A 1 168 ? 10.838 -17.316 2.817   0.46 17.70 ?  168 PHE   A CZ   1 
ATOM   3845 C CZ   B PHE   A 1 168 ? 6.678  -18.104 -6.212  0.54 37.84 ?  168 PHE   A CZ   1 
ATOM   3846 H H    A PHE   A 1 168 ? 5.146  -14.316 0.884   0.46 23.15 ?  168 PHE   A H    1 
ATOM   3847 H H    B PHE   A 1 168 ? 4.671  -16.023 -2.206  0.54 36.20 ?  168 PHE   A H    1 
ATOM   3848 H HA   A PHE   A 1 168 ? 7.385  -15.280 -0.150  0.46 22.68 ?  168 PHE   A HA   1 
ATOM   3849 H HA   B PHE   A 1 168 ? 5.741  -17.512 -0.272  0.54 40.35 ?  168 PHE   A HA   1 
ATOM   3850 H HB2  A PHE   A 1 168 ? 7.431  -14.218 1.942   0.46 22.19 ?  168 PHE   A HB2  1 
ATOM   3851 H HB2  B PHE   A 1 168 ? 5.868  -19.222 -1.733  0.54 42.24 ?  168 PHE   A HB2  1 
ATOM   3852 H HB3  A PHE   A 1 168 ? 6.560  -15.399 2.550   0.46 22.19 ?  168 PHE   A HB3  1 
ATOM   3853 H HB3  B PHE   A 1 168 ? 4.502  -18.497 -2.079  0.54 42.24 ?  168 PHE   A HB3  1 
ATOM   3854 H HD1  A PHE   A 1 168 ? 9.722  -14.855 1.042   0.46 21.72 ?  168 PHE   A HD1  1 
ATOM   3855 H HD1  B PHE   A 1 168 ? 7.835  -18.805 -3.281  0.54 44.99 ?  168 PHE   A HD1  1 
ATOM   3856 H HD2  A PHE   A 1 168 ? 7.678  -17.244 3.518   0.46 20.49 ?  168 PHE   A HD2  1 
ATOM   3857 H HD2  B PHE   A 1 168 ? 4.106  -17.764 -4.284  0.54 44.70 ?  168 PHE   A HD2  1 
ATOM   3858 H HE1  A PHE   A 1 168 ? 11.664 -16.008 1.534   0.46 21.53 ?  168 PHE   A HE1  1 
ATOM   3859 H HE1  B PHE   A 1 168 ? 8.478  -18.642 -5.490  0.54 45.20 ?  168 PHE   A HE1  1 
ATOM   3860 H HE2  A PHE   A 1 168 ? 9.626  -18.398 4.010   0.46 20.59 ?  168 PHE   A HE2  1 
ATOM   3861 H HE2  B PHE   A 1 168 ? 4.747  -17.601 -6.497  0.54 45.17 ?  168 PHE   A HE2  1 
ATOM   3862 H HZ   A PHE   A 1 168 ? 11.621 -17.778 3.017   0.46 21.26 ?  168 PHE   A HZ   1 
ATOM   3863 H HZ   B PHE   A 1 168 ? 6.937  -18.038 -7.104  0.54 45.42 ?  168 PHE   A HZ   1 
ATOM   3864 N N    A LEU   A 1 169 ? 7.253  -17.714 -0.275  0.46 20.22 ?  169 LEU   A N    1 
ATOM   3865 N N    B LEU   A 1 169 ? 8.197  -17.708 -0.781  0.54 36.82 ?  169 LEU   A N    1 
ATOM   3866 C CA   A LEU   A 1 169 ? 7.034  -19.141 -0.446  0.46 22.44 ?  169 LEU   A CA   1 
ATOM   3867 C CA   B LEU   A 1 169 ? 9.637  -17.502 -0.885  0.54 37.73 ?  169 LEU   A CA   1 
ATOM   3868 C C    A LEU   A 1 169 ? 7.890  -19.935 0.520   0.46 23.21 ?  169 LEU   A C    1 
ATOM   3869 C C    B LEU   A 1 169 ? 10.285 -18.722 -1.521  0.54 39.00 ?  169 LEU   A C    1 
ATOM   3870 O O    A LEU   A 1 169 ? 7.368  -20.462 1.500   0.46 24.33 ?  169 LEU   A O    1 
ATOM   3871 O O    B LEU   A 1 169 ? 11.508 -18.837 -1.573  0.54 39.54 ?  169 LEU   A O    1 
ATOM   3872 C CB   A LEU   A 1 169 ? 7.317  -19.565 -1.887  0.46 23.77 ?  169 LEU   A CB   1 
ATOM   3873 C CB   B LEU   A 1 169 ? 10.258 -17.222 0.486   0.54 37.65 ?  169 LEU   A CB   1 
ATOM   3874 C CG   A LEU   A 1 169 ? 6.981  -21.018 -2.237  0.46 25.35 ?  169 LEU   A CG   1 
ATOM   3875 C CG   B LEU   A 1 169 ? 9.538  -17.797 1.704   0.54 37.46 ?  169 LEU   A CG   1 
ATOM   3876 C CD1  A LEU   A 1 169 ? 5.553  -21.363 -1.845  0.46 26.24 ?  169 LEU   A CD1  1 
ATOM   3877 C CD1  B LEU   A 1 169 ? 10.540 -18.366 2.683   0.54 37.38 ?  169 LEU   A CD1  1 
ATOM   3878 C CD2  A LEU   A 1 169 ? 7.199  -21.270 -3.720  0.46 25.71 ?  169 LEU   A CD2  1 
ATOM   3879 C CD2  B LEU   A 1 169 ? 8.704  -16.714 2.359   0.54 37.35 ?  169 LEU   A CD2  1 
ATOM   3880 O OXT  A LEU   A 1 169 ? 9.103  -20.056 0.349   0.46 23.52 -1 169 LEU   A OXT  1 
ATOM   3881 O OXT  B LEU   A 1 169 ? 9.588  -19.621 -1.994  0.54 39.48 -1 169 LEU   A OXT  1 
ATOM   3882 H H    A LEU   A 1 169 ? 7.966  -17.414 -0.647  0.46 24.27 ?  169 LEU   A H    1 
ATOM   3883 H H    B LEU   A 1 169 ? 7.973  -18.398 -0.315  0.54 44.20 ?  169 LEU   A H    1 
ATOM   3884 H HA   A LEU   A 1 169 ? 6.112  -19.346 -0.241  0.46 26.94 ?  169 LEU   A HA   1 
ATOM   3885 H HA   B LEU   A 1 169 ? 9.808  -16.728 -1.445  0.54 45.29 ?  169 LEU   A HA   1 
ATOM   3886 H HB2  A LEU   A 1 169 ? 6.797  -19.000 -2.475  0.46 28.54 ?  169 LEU   A HB2  1 
ATOM   3887 H HB2  B LEU   A 1 169 ? 11.164 -17.574 0.496   0.54 45.20 ?  169 LEU   A HB2  1 
ATOM   3888 H HB3  A LEU   A 1 169 ? 8.261  -19.438 -2.064  0.46 28.54 ?  169 LEU   A HB3  1 
ATOM   3889 H HB3  B LEU   A 1 169 ? 10.296 -16.261 0.602   0.54 45.20 ?  169 LEU   A HB3  1 
ATOM   3890 H HG   A LEU   A 1 169 ? 7.576  -21.609 -1.747  0.46 30.43 ?  169 LEU   A HG   1 
ATOM   3891 H HG   B LEU   A 1 169 ? 8.948  -18.517 1.430   0.54 44.96 ?  169 LEU   A HG   1 
ATOM   3892 H HD11 A LEU   A 1 169 ? 5.309  -22.208 -2.250  0.46 31.50 ?  169 LEU   A HD11 1 
ATOM   3893 H HD11 B LEU   A 1 169 ? 10.065 -18.696 3.460   0.54 44.88 ?  169 LEU   A HD11 1 
ATOM   3894 H HD12 A LEU   A 1 169 ? 5.498  -21.432 -0.878  0.46 31.50 ?  169 LEU   A HD12 1 
ATOM   3895 H HD12 B LEU   A 1 169 ? 11.021 -19.092 2.255   0.54 44.88 ?  169 LEU   A HD12 1 
ATOM   3896 H HD13 A LEU   A 1 169 ? 4.962  -20.661 -2.161  0.46 31.50 ?  169 LEU   A HD13 1 
ATOM   3897 H HD13 B LEU   A 1 169 ? 11.157 -17.666 2.942   0.54 44.88 ?  169 LEU   A HD13 1 
ATOM   3898 H HD21 A LEU   A 1 169 ? 6.987  -22.196 -3.919  0.46 30.86 ?  169 LEU   A HD21 1 
ATOM   3899 H HD21 B LEU   A 1 169 ? 8.267  -17.084 3.139   0.54 44.83 ?  169 LEU   A HD21 1 
ATOM   3900 H HD22 A LEU   A 1 169 ? 6.617  -20.682 -4.228  0.46 30.86 ?  169 LEU   A HD22 1 
ATOM   3901 H HD22 B LEU   A 1 169 ? 9.287  -15.984 2.622   0.54 44.83 ?  169 LEU   A HD22 1 
ATOM   3902 H HD23 A LEU   A 1 169 ? 8.125  -21.088 -3.940  0.46 30.86 ?  169 LEU   A HD23 1 
ATOM   3903 H HD23 B LEU   A 1 169 ? 8.042  -16.396 1.725   0.54 44.83 ?  169 LEU   A HD23 1 
ATOM   3904 N N    A SER   B 1 1   ? 50.803 -9.294  -23.748 0.46 30.98 ?  1   SER   B N    1 
ATOM   3905 N N    B SER   B 1 1   ? 50.735 -9.242  -23.874 0.54 28.97 ?  1   SER   B N    1 
ATOM   3906 C CA   A SER   B 1 1   ? 51.304 -10.358 -22.854 0.46 31.18 ?  1   SER   B CA   1 
ATOM   3907 C CA   B SER   B 1 1   ? 51.151 -10.215 -22.849 0.54 28.83 ?  1   SER   B CA   1 
ATOM   3908 C C    A SER   B 1 1   ? 50.223 -11.393 -22.586 0.46 30.89 ?  1   SER   B C    1 
ATOM   3909 C C    B SER   B 1 1   ? 50.043 -11.214 -22.564 0.54 26.43 ?  1   SER   B C    1 
ATOM   3910 O O    A SER   B 1 1   ? 49.033 -11.166 -22.829 0.46 30.96 ?  1   SER   B O    1 
ATOM   3911 O O    B SER   B 1 1   ? 48.868 -11.026 -22.928 0.54 25.53 ?  1   SER   B O    1 
ATOM   3912 C CB   A SER   B 1 1   ? 51.788 -9.771  -21.532 0.46 31.13 ?  1   SER   B CB   1 
ATOM   3913 C CB   B SER   B 1 1   ? 51.551 -9.515  -21.555 0.54 29.94 ?  1   SER   B CB   1 
ATOM   3914 O OG   A SER   B 1 1   ? 50.707 -9.566  -20.645 0.46 33.10 ?  1   SER   B OG   1 
ATOM   3915 O OG   B SER   B 1 1   ? 50.437 -9.426  -20.685 0.54 32.69 ?  1   SER   B OG   1 
ATOM   3916 H H1   A SER   B 1 1   ? 50.663 -9.636  -24.555 0.46 37.18 ?  1   SER   B H1   1 
ATOM   3917 H H1   B SER   B 1 1   ? 51.456 -8.817  -24.173 0.54 34.78 ?  1   SER   B H1   1 
ATOM   3918 H H2   A SER   B 1 1   ? 50.046 -8.971  -23.420 0.46 37.18 ?  1   SER   B H2   1 
ATOM   3919 H H2   B SER   B 1 1   ? 50.342 -9.675  -24.538 0.54 34.78 ?  1   SER   B H2   1 
ATOM   3920 H H3   A SER   B 1 1   ? 51.412 -8.648  -23.796 0.46 37.18 ?  1   SER   B H3   1 
ATOM   3921 H H3   B SER   B 1 1   ? 50.173 -8.662  -23.510 0.54 34.78 ?  1   SER   B H3   1 
ATOM   3922 H HA   A SER   B 1 1   ? 52.049 -10.791 -23.288 0.46 37.43 ?  1   SER   B HA   1 
ATOM   3923 H HA   B SER   B 1 1   ? 51.919 -10.698 -23.180 0.54 34.61 ?  1   SER   B HA   1 
ATOM   3924 H HB2  A SER   B 1 1   ? 52.409 -10.393 -21.127 0.46 37.38 ?  1   SER   B HB2  1 
ATOM   3925 H HB2  B SER   B 1 1   ? 52.262 -10.024 -21.131 0.54 35.94 ?  1   SER   B HB2  1 
ATOM   3926 H HB3  A SER   B 1 1   ? 52.226 -8.922  -21.701 0.46 37.38 ?  1   SER   B HB3  1 
ATOM   3927 H HB3  B SER   B 1 1   ? 51.862 -8.619  -21.757 0.54 35.94 ?  1   SER   B HB3  1 
ATOM   3928 H HG   A SER   B 1 1   ? 50.904 -8.965  -20.090 0.46 39.73 ?  1   SER   B HG   1 
ATOM   3929 H HG   B SER   B 1 1   ? 50.554 -8.798  -20.140 0.54 39.24 ?  1   SER   B HG   1 
ATOM   3930 N N    A MET   B 1 2   ? 50.657 -12.530 -22.062 0.46 30.77 ?  2   MET   B N    1 
ATOM   3931 N N    B MET   B 1 2   ? 50.441 -12.280 -21.885 0.54 25.58 ?  2   MET   B N    1 
ATOM   3932 C CA   A MET   B 1 2   ? 49.820 -13.710 -21.898 0.46 30.52 ?  2   MET   B CA   1 
ATOM   3933 C CA   B MET   B 1 2   ? 49.635 -13.482 -21.735 0.54 25.69 ?  2   MET   B CA   1 
ATOM   3934 C C    A MET   B 1 2   ? 49.581 -13.928 -20.409 0.46 28.21 ?  2   MET   B C    1 
ATOM   3935 C C    B MET   B 1 2   ? 49.402 -13.695 -20.246 0.54 24.18 ?  2   MET   B C    1 
ATOM   3936 O O    A MET   B 1 2   ? 50.520 -14.214 -19.659 0.46 29.15 ?  2   MET   B O    1 
ATOM   3937 O O    B MET   B 1 2   ? 50.337 -14.026 -19.509 0.54 25.27 ?  2   MET   B O    1 
ATOM   3938 C CB   A MET   B 1 2   ? 50.515 -14.913 -22.524 0.46 33.61 ?  2   MET   B CB   1 
ATOM   3939 C CB   B MET   B 1 2   ? 50.393 -14.654 -22.347 0.54 29.85 ?  2   MET   B CB   1 
ATOM   3940 C CG   A MET   B 1 2   ? 49.651 -16.156 -22.626 0.46 36.93 ?  2   MET   B CG   1 
ATOM   3941 C CG   B MET   B 1 2   ? 49.555 -15.872 -22.705 0.54 33.23 ?  2   MET   B CG   1 
ATOM   3942 S SD   A MET   B 1 2   ? 50.471 -17.465 -23.554 0.46 40.15 ?  2   MET   B SD   1 
ATOM   3943 S SD   B MET   B 1 2   ? 50.504 -17.020 -23.719 0.54 36.86 ?  2   MET   B SD   1 
ATOM   3944 C CE   A MET   B 1 2   ? 51.021 -16.522 -24.976 0.46 39.73 ?  2   MET   B CE   1 
ATOM   3945 C CE   B MET   B 1 2   ? 51.362 -15.887 -24.788 0.54 36.26 ?  2   MET   B CE   1 
ATOM   3946 H H    A MET   B 1 2   ? 51.463 -12.643 -21.786 0.46 36.93 ?  2   MET   B H    1 
ATOM   3947 H H    B MET   B 1 2   ? 51.206 -12.342 -21.493 0.54 30.71 ?  2   MET   B H    1 
ATOM   3948 H HA   A MET   B 1 2   ? 48.974 -13.578 -22.353 0.46 36.64 ?  2   MET   B HA   1 
ATOM   3949 H HA   B MET   B 1 2   ? 48.793 -13.389 -22.210 0.54 30.84 ?  2   MET   B HA   1 
ATOM   3950 H HB2  A MET   B 1 2   ? 50.793 -14.650 -23.413 0.46 40.35 ?  2   MET   B HB2  1 
ATOM   3951 H HB2  B MET   B 1 2   ? 50.804 -14.304 -23.147 0.54 35.83 ?  2   MET   B HB2  1 
ATOM   3952 H HB3  A MET   B 1 2   ? 51.294 -15.144 -21.994 0.46 40.35 ?  2   MET   B HB3  1 
ATOM   3953 H HB3  B MET   B 1 2   ? 51.082 -14.960 -21.738 0.54 35.83 ?  2   MET   B HB3  1 
ATOM   3954 H HG2  A MET   B 1 2   ? 49.463 -16.485 -21.732 0.46 44.33 ?  2   MET   B HG2  1 
ATOM   3955 H HG2  B MET   B 1 2   ? 49.282 -16.334 -21.892 0.54 39.89 ?  2   MET   B HG2  1 
ATOM   3956 H HG3  A MET   B 1 2   ? 48.828 -15.936 -23.087 0.46 44.33 ?  2   MET   B HG3  1 
ATOM   3957 H HG3  B MET   B 1 2   ? 48.778 -15.607 -23.214 0.54 39.89 ?  2   MET   B HG3  1 
ATOM   3958 H HE1  A MET   B 1 2   ? 51.187 -17.129 -25.705 0.46 47.69 ?  2   MET   B HE1  1 
ATOM   3959 H HE1  B MET   B 1 2   ? 51.672 -16.378 -25.546 0.54 43.53 ?  2   MET   B HE1  1 
ATOM   3960 H HE2  A MET   B 1 2   ? 50.320 -15.892 -25.217 0.46 47.69 ?  2   MET   B HE2  1 
ATOM   3961 H HE2  B MET   B 1 2   ? 50.742 -15.192 -25.065 0.54 43.53 ?  2   MET   B HE2  1 
ATOM   3962 H HE3  A MET   B 1 2   ? 51.834 -16.033 -24.755 0.46 47.69 ?  2   MET   B HE3  1 
ATOM   3963 H HE3  B MET   B 1 2   ? 52.113 -15.499 -24.304 0.54 43.53 ?  2   MET   B HE3  1 
ATOM   3964 N N    A VAL   B 1 3   ? 48.327 -13.782 -19.986 0.46 25.67 ?  3   VAL   B N    1 
ATOM   3965 N N    B VAL   B 1 3   ? 48.174 -13.460 -19.802 0.54 22.67 ?  3   VAL   B N    1 
ATOM   3966 C CA   A VAL   B 1 3   ? 47.921 -14.012 -18.608 0.46 23.71 ?  3   VAL   B CA   1 
ATOM   3967 C CA   B VAL   B 1 3   ? 47.758 -13.762 -18.439 0.54 22.05 ?  3   VAL   B CA   1 
ATOM   3968 C C    A VAL   B 1 3   ? 46.682 -14.899 -18.622 0.46 20.91 ?  3   VAL   B C    1 
ATOM   3969 C C    B VAL   B 1 3   ? 46.532 -14.664 -18.491 0.54 20.45 ?  3   VAL   B C    1 
ATOM   3970 O O    A VAL   B 1 3   ? 46.002 -15.038 -19.641 0.46 21.06 ?  3   VAL   B O    1 
ATOM   3971 O O    B VAL   B 1 3   ? 45.738 -14.617 -19.436 0.54 21.02 ?  3   VAL   B O    1 
ATOM   3972 C CB   A VAL   B 1 3   ? 47.644 -12.693 -17.850 0.46 25.20 ?  3   VAL   B CB   1 
ATOM   3973 C CB   B VAL   B 1 3   ? 47.486 -12.491 -17.598 0.54 23.21 ?  3   VAL   B CB   1 
ATOM   3974 C CG1  A VAL   B 1 3   ? 48.917 -11.852 -17.741 0.46 26.00 ?  3   VAL   B CG1  1 
ATOM   3975 C CG1  B VAL   B 1 3   ? 48.767 -11.677 -17.427 0.54 23.68 ?  3   VAL   B CG1  1 
ATOM   3976 C CG2  A VAL   B 1 3   ? 46.530 -11.903 -18.532 0.46 25.57 ?  3   VAL   B CG2  1 
ATOM   3977 C CG2  B VAL   B 1 3   ? 46.381 -11.645 -18.226 0.54 23.61 ?  3   VAL   B CG2  1 
ATOM   3978 H H    A VAL   B 1 3   ? 47.678 -13.543 -20.500 0.46 30.82 ?  3   VAL   B H    1 
ATOM   3979 H H    B VAL   B 1 3   ? 47.553 -13.113 -20.287 0.54 27.22 ?  3   VAL   B H    1 
ATOM   3980 H HA   A VAL   B 1 3   ? 48.628 -14.484 -18.144 0.46 28.47 ?  3   VAL   B HA   1 
ATOM   3981 H HA   B VAL   B 1 3   ? 48.458 -14.257 -18.000 0.54 26.47 ?  3   VAL   B HA   1 
ATOM   3982 H HB   A VAL   B 1 3   ? 47.352 -12.906 -16.951 0.46 30.25 ?  3   VAL   B HB   1 
ATOM   3983 H HB   B VAL   B 1 3   ? 47.190 -12.758 -16.716 0.54 27.87 ?  3   VAL   B HB   1 
ATOM   3984 H HG11 A VAL   B 1 3   ? 48.716 -11.037 -17.254 0.46 31.21 ?  3   VAL   B HG11 1 
ATOM   3985 H HG11 B VAL   B 1 3   ? 48.573 -10.891 -16.892 0.54 28.43 ?  3   VAL   B HG11 1 
ATOM   3986 H HG12 A VAL   B 1 3   ? 49.593 -12.361 -17.268 0.46 31.21 ?  3   VAL   B HG12 1 
ATOM   3987 H HG12 B VAL   B 1 3   ? 49.431 -12.226 -16.981 0.54 28.43 ?  3   VAL   B HG12 1 
ATOM   3988 H HG13 A VAL   B 1 3   ? 49.230 -11.635 -18.633 0.46 31.21 ?  3   VAL   B HG13 1 
ATOM   3989 H HG13 B VAL   B 1 3   ? 49.091 -11.410 -18.302 0.54 28.43 ?  3   VAL   B HG13 1 
ATOM   3990 H HG21 A VAL   B 1 3   ? 46.458 -11.033 -18.108 0.46 30.70 ?  3   VAL   B HG21 1 
ATOM   3991 H HG21 B VAL   B 1 3   ? 46.310 -10.808 -17.739 0.54 28.35 ?  3   VAL   B HG21 1 
ATOM   3992 H HG22 A VAL   B 1 3   ? 46.746 -11.796 -19.471 0.46 30.70 ?  3   VAL   B HG22 1 
ATOM   3993 H HG22 B VAL   B 1 3   ? 46.604 -11.470 -19.153 0.54 28.35 ?  3   VAL   B HG22 1 
ATOM   3994 H HG23 A VAL   B 1 3   ? 45.694 -12.386 -18.436 0.46 30.70 ?  3   VAL   B HG23 1 
ATOM   3995 H HG23 B VAL   B 1 3   ? 45.543 -12.130 -18.172 0.54 28.35 ?  3   VAL   B HG23 1 
ATOM   3996 N N    . ASN   B 1 4   ? 46.390 -15.503 -17.468 1.00 20.17 ?  4   ASN   B N    1 
ATOM   3997 C CA   . ASN   B 1 4   ? 45.245 -16.410 -17.349 1.00 19.33 ?  4   ASN   B CA   1 
ATOM   3998 C C    . ASN   B 1 4   ? 45.185 -17.386 -18.523 1.00 18.93 ?  4   ASN   B C    1 
ATOM   3999 O O    . ASN   B 1 4   ? 44.122 -17.643 -19.088 1.00 20.45 ?  4   ASN   B O    1 
ATOM   4000 C CB   . ASN   B 1 4   ? 43.928 -15.643 -17.197 1.00 19.16 ?  4   ASN   B CB   1 
ATOM   4001 C CG   . ASN   B 1 4   ? 43.870 -14.841 -15.908 1.00 17.46 ?  4   ASN   B CG   1 
ATOM   4002 O OD1  . ASN   B 1 4   ? 44.149 -15.358 -14.825 1.00 17.15 ?  4   ASN   B OD1  1 
ATOM   4003 N ND2  . ASN   B 1 4   ? 43.535 -13.557 -16.024 1.00 18.64 ?  4   ASN   B ND2  1 
ATOM   4004 H H    A ASN   B 1 4   ? 46.837 -15.397 -16.745 0.46 24.22 ?  4   ASN   B H    1 
ATOM   4005 H H    B ASN   B 1 4   ? 46.959 -15.571 -16.832 0.54 24.22 ?  4   ASN   B H    1 
ATOM   4006 H HA   . ASN   B 1 4   ? 45.368 -16.931 -16.542 1.00 23.21 ?  4   ASN   B HA   1 
ATOM   4007 H HB2  . ASN   B 1 4   ? 43.824 -15.026 -17.937 1.00 23.00 ?  4   ASN   B HB2  1 
ATOM   4008 H HB3  . ASN   B 1 4   ? 43.194 -16.276 -17.186 1.00 23.00 ?  4   ASN   B HB3  1 
ATOM   4009 H HD21 . ASN   B 1 4   ? 43.490 -13.058 -15.321 1.00 22.38 ?  4   ASN   B HD21 1 
ATOM   4010 H HD22 . ASN   B 1 4   ? 43.353 -13.222 -16.795 1.00 22.38 ?  4   ASN   B HD22 1 
ATOM   4011 N N    . SER   B 1 5   ? 46.340 -17.932 -18.907 1.00 19.82 ?  5   SER   B N    1 
ATOM   4012 C CA   . SER   B 1 5   ? 46.413 -18.849 -20.044 1.00 22.80 ?  5   SER   B CA   1 
ATOM   4013 C C    . SER   B 1 5   ? 46.418 -20.272 -19.500 1.00 24.15 ?  5   SER   B C    1 
ATOM   4014 O O    . SER   B 1 5   ? 47.452 -20.930 -19.416 1.00 26.80 ?  5   SER   B O    1 
ATOM   4015 C CB   . SER   B 1 5   ? 47.635 -18.553 -20.904 1.00 26.50 ?  5   SER   B CB   1 
ATOM   4016 O OG   . SER   B 1 5   ? 48.815 -18.641 -20.129 1.00 30.93 ?  5   SER   B OG   1 
ATOM   4017 H H    . SER   B 1 5   ? 47.099 -17.797 -18.518 1.00 23.80 ?  5   SER   B H    1 
ATOM   4018 H HA   . SER   B 1 5   ? 45.625 -18.746 -20.589 1.00 27.38 ?  5   SER   B HA   1 
ATOM   4019 H HB2  . SER   B 1 5   ? 47.671 -19.194 -21.634 1.00 31.81 ?  5   SER   B HB2  1 
ATOM   4020 H HB3  . SER   B 1 5   ? 47.550 -17.654 -21.261 1.00 31.81 ?  5   SER   B HB3  1 
ATOM   4021 H HG   . SER   B 1 5   ? 48.915 -19.421 -19.843 1.00 37.13 ?  5   SER   B HG   1 
ATOM   4022 N N    . PHE   B 1 6   ? 45.229 -20.741 -19.116 1.00 24.79 ?  6   PHE   B N    1 
ATOM   4023 C CA   . PHE   B 1 6   ? 45.059 -22.079 -18.564 1.00 23.94 ?  6   PHE   B CA   1 
ATOM   4024 C C    . PHE   B 1 6   ? 45.013 -23.086 -19.704 1.00 27.52 ?  6   PHE   B C    1 
ATOM   4025 O O    . PHE   B 1 6   ? 44.327 -22.864 -20.703 1.00 30.28 ?  6   PHE   B O    1 
ATOM   4026 C CB   . PHE   B 1 6   ? 43.765 -22.145 -17.751 1.00 22.06 ?  6   PHE   B CB   1 
ATOM   4027 C CG   . PHE   B 1 6   ? 43.762 -21.259 -16.531 1.00 20.24 ?  6   PHE   B CG   1 
ATOM   4028 C CD1  . PHE   B 1 6   ? 44.250 -21.721 -15.324 1.00 18.65 ?  6   PHE   B CD1  1 
ATOM   4029 C CD2  . PHE   B 1 6   ? 43.288 -19.960 -16.599 1.00 18.67 ?  6   PHE   B CD2  1 
ATOM   4030 C CE1  . PHE   B 1 6   ? 44.239 -20.914 -14.195 1.00 18.26 ?  6   PHE   B CE1  1 
ATOM   4031 C CE2  . PHE   B 1 6   ? 43.295 -19.139 -15.481 1.00 19.67 ?  6   PHE   B CE2  1 
ATOM   4032 C CZ   . PHE   B 1 6   ? 43.768 -19.610 -14.283 1.00 18.72 ?  6   PHE   B CZ   1 
ATOM   4033 H H    . PHE   B 1 6   ? 44.495 -20.300 -19.179 1.00 29.77 ?  6   PHE   B H    1 
ATOM   4034 H HA   . PHE   B 1 6   ? 45.799 -22.302 -17.988 1.00 28.74 ?  6   PHE   B HA   1 
ATOM   4035 H HB2  . PHE   B 1 6   ? 43.021 -21.873 -18.316 1.00 26.48 ?  6   PHE   B HB2  1 
ATOM   4036 H HB3  . PHE   B 1 6   ? 43.623 -23.058 -17.450 1.00 26.48 ?  6   PHE   B HB3  1 
ATOM   4037 H HD1  . PHE   B 1 6   ? 44.570 -22.591 -15.261 1.00 22.39 ?  6   PHE   B HD1  1 
ATOM   4038 H HD2  . PHE   B 1 6   ? 42.959 -19.638 -17.407 1.00 22.42 ?  6   PHE   B HD2  1 
ATOM   4039 H HE1  . PHE   B 1 6   ? 44.574 -21.231 -13.387 1.00 21.92 ?  6   PHE   B HE1  1 
ATOM   4040 H HE2  . PHE   B 1 6   ? 42.960 -18.272 -15.541 1.00 23.61 ?  6   PHE   B HE2  1 
ATOM   4041 H HZ   . PHE   B 1 6   ? 43.766 -19.067 -13.529 1.00 22.48 ?  6   PHE   B HZ   1 
ATOM   4042 N N    A SER   B 1 7   ? 45.744 -24.190 -19.557 0.46 28.30 ?  7   SER   B N    1 
ATOM   4043 N N    B SER   B 1 7   ? 45.752 -24.185 -19.555 0.54 28.13 ?  7   SER   B N    1 
ATOM   4044 C CA   A SER   B 1 7   ? 45.826 -25.199 -20.603 0.46 30.14 ?  7   SER   B CA   1 
ATOM   4045 C CA   B SER   B 1 7   ? 45.875 -25.188 -20.603 0.54 30.08 ?  7   SER   B CA   1 
ATOM   4046 C C    A SER   B 1 7   ? 45.776 -26.591 -19.993 0.46 29.06 ?  7   SER   B C    1 
ATOM   4047 C C    B SER   B 1 7   ? 45.832 -26.579 -19.991 0.54 28.86 ?  7   SER   B C    1 
ATOM   4048 O O    A SER   B 1 7   ? 46.345 -26.832 -18.925 0.46 29.33 ?  7   SER   B O    1 
ATOM   4049 O O    B SER   B 1 7   ? 46.430 -26.823 -18.940 0.54 29.11 ?  7   SER   B O    1 
ATOM   4050 C CB   A SER   B 1 7   ? 47.118 -25.045 -21.415 0.46 32.82 ?  7   SER   B CB   1 
ATOM   4051 C CB   B SER   B 1 7   ? 47.190 -25.012 -21.371 0.54 33.04 ?  7   SER   B CB   1 
ATOM   4052 O OG   A SER   B 1 7   ? 47.129 -25.922 -22.528 0.46 34.79 ?  7   SER   B OG   1 
ATOM   4053 O OG   B SER   B 1 7   ? 47.204 -25.799 -22.548 0.54 35.22 ?  7   SER   B OG   1 
ATOM   4054 H H    A SER   B 1 7   ? 46.209 -24.374 -18.857 0.46 33.98 ?  7   SER   B H    1 
ATOM   4055 H H    B SER   B 1 7   ? 46.203 -24.370 -18.845 0.54 33.77 ?  7   SER   B H    1 
ATOM   4056 H HA   A SER   B 1 7   ? 45.074 -25.108 -21.205 0.46 36.18 ?  7   SER   B HA   1 
ATOM   4057 H HA   B SER   B 1 7   ? 45.140 -25.108 -21.227 0.54 36.12 ?  7   SER   B HA   1 
ATOM   4058 H HB2  A SER   B 1 7   ? 47.183 -24.130 -21.732 0.46 39.40 ?  7   SER   B HB2  1 
ATOM   4059 H HB2  B SER   B 1 7   ? 47.288 -24.078 -21.615 0.54 39.66 ?  7   SER   B HB2  1 
ATOM   4060 H HB3  A SER   B 1 7   ? 47.877 -25.252 -20.846 0.46 39.40 ?  7   SER   B HB3  1 
ATOM   4061 H HB3  B SER   B 1 7   ? 47.928 -25.283 -20.802 0.54 39.66 ?  7   SER   B HB3  1 
ATOM   4062 H HG   A SER   B 1 7   ? 47.841 -25.823 -22.965 0.46 41.77 ?  7   SER   B HG   1 
ATOM   4063 H HG   B SER   B 1 7   ? 47.930 -25.690 -22.959 0.54 42.28 ?  7   SER   B HG   1 
ATOM   4064 N N    A GLY   B 1 8   ? 45.091 -27.503 -20.682 0.46 29.06 ?  8   GLY   B N    1 
ATOM   4065 N N    B GLY   B 1 8   ? 45.124 -27.489 -20.660 0.54 29.14 ?  8   GLY   B N    1 
ATOM   4066 C CA   A GLY   B 1 8   ? 45.059 -28.893 -20.278 0.46 28.62 ?  8   GLY   B CA   1 
ATOM   4067 C CA   B GLY   B 1 8   ? 45.089 -28.875 -20.244 0.54 28.81 ?  8   GLY   B CA   1 
ATOM   4068 C C    A GLY   B 1 8   ? 44.078 -29.226 -19.183 0.46 27.29 ?  8   GLY   B C    1 
ATOM   4069 C C    B GLY   B 1 8   ? 44.124 -29.189 -19.129 0.54 27.43 ?  8   GLY   B C    1 
ATOM   4070 O O    A GLY   B 1 8   ? 44.188 -30.298 -18.577 0.46 27.96 ?  8   GLY   B O    1 
ATOM   4071 O O    B GLY   B 1 8   ? 44.293 -30.212 -18.455 0.54 28.31 ?  8   GLY   B O    1 
ATOM   4072 H H    A GLY   B 1 8   ? 44.634 -27.335 -21.390 0.46 34.89 ?  8   GLY   B H    1 
ATOM   4073 H H    B GLY   B 1 8   ? 44.651 -27.321 -21.357 0.54 34.98 ?  8   GLY   B H    1 
ATOM   4074 H HA2  A GLY   B 1 8   ? 44.838 -29.440 -21.049 0.46 34.36 ?  8   GLY   B HA2  1 
ATOM   4075 H HA2  B GLY   B 1 8   ? 44.851 -29.428 -21.005 0.54 34.59 ?  8   GLY   B HA2  1 
ATOM   4076 H HA3  A GLY   B 1 8   ? 45.938 -29.153 -19.968 0.46 34.36 ?  8   GLY   B HA3  1 
ATOM   4077 H HA3  B GLY   B 1 8   ? 45.971 -29.139 -19.946 0.54 34.59 ?  8   GLY   B HA3  1 
ATOM   4078 N N    . TYR   B 1 9   ? 43.109 -28.354 -18.913 1.00 26.22 ?  9   TYR   B N    1 
ATOM   4079 C CA   . TYR   B 1 9   ? 42.129 -28.599 -17.866 1.00 23.10 ?  9   TYR   B CA   1 
ATOM   4080 C C    . TYR   B 1 9   ? 40.942 -29.381 -18.398 1.00 23.29 ?  9   TYR   B C    1 
ATOM   4081 O O    . TYR   B 1 9   ? 40.525 -29.230 -19.552 1.00 25.78 ?  9   TYR   B O    1 
ATOM   4082 C CB   . TYR   B 1 9   ? 41.621 -27.300 -17.241 1.00 22.60 ?  9   TYR   B CB   1 
ATOM   4083 C CG   . TYR   B 1 9   ? 42.635 -26.678 -16.315 1.00 22.00 ?  9   TYR   B CG   1 
ATOM   4084 C CD1  . TYR   B 1 9   ? 43.742 -26.020 -16.827 1.00 22.59 ?  9   TYR   B CD1  1 
ATOM   4085 C CD2  . TYR   B 1 9   ? 42.506 -26.771 -14.935 1.00 21.91 ?  9   TYR   B CD2  1 
ATOM   4086 C CE1  . TYR   B 1 9   ? 44.699 -25.468 -16.000 1.00 23.03 ?  9   TYR   B CE1  1 
ATOM   4087 C CE2  . TYR   B 1 9   ? 43.463 -26.215 -14.090 1.00 22.02 ?  9   TYR   B CE2  1 
ATOM   4088 C CZ   . TYR   B 1 9   ? 44.555 -25.558 -14.633 1.00 22.76 ?  9   TYR   B CZ   1 
ATOM   4089 O OH   . TYR   B 1 9   ? 45.523 -25.000 -13.826 1.00 22.79 ?  9   TYR   B OH   1 
ATOM   4090 H H    A TYR   B 1 9   ? 42.988 -27.615 -19.333 0.46 31.47 ?  9   TYR   B H    1 
ATOM   4091 H H    B TYR   B 1 9   ? 42.957 -27.642 -19.370 0.54 31.47 ?  9   TYR   B H    1 
ATOM   4092 H HA   . TYR   B 1 9   ? 42.531 -29.123 -17.163 1.00 27.74 ?  9   TYR   B HA   1 
ATOM   4093 H HB2  . TYR   B 1 9   ? 41.413 -26.656 -17.941 1.00 27.14 ?  9   TYR   B HB2  1 
ATOM   4094 H HB3  . TYR   B 1 9   ? 40.828 -27.496 -16.723 1.00 27.14 ?  9   TYR   B HB3  1 
ATOM   4095 H HD1  . TYR   B 1 9   ? 43.845 -25.959 -17.751 1.00 27.12 ?  9   TYR   B HD1  1 
ATOM   4096 H HD2  . TYR   B 1 9   ? 41.770 -27.217 -14.573 1.00 26.30 ?  9   TYR   B HD2  1 
ATOM   4097 H HE1  . TYR   B 1 9   ? 45.432 -25.033 -16.364 1.00 27.65 ?  9   TYR   B HE1  1 
ATOM   4098 H HE2  . TYR   B 1 9   ? 43.366 -26.286 -13.165 1.00 26.44 ?  9   TYR   B HE2  1 
ATOM   4099 H HH   . TYR   B 1 9   ? 46.104 -24.621 -14.299 1.00 27.36 ?  9   TYR   B HH   1 
ATOM   4100 N N    . LEU   B 1 10  ? 40.406 -30.232 -17.532 1.00 21.02 ?  10  LEU   B N    1 
ATOM   4101 C CA   . LEU   B 1 10  ? 39.195 -30.984 -17.807 1.00 20.56 ?  10  LEU   B CA   1 
ATOM   4102 C C    . LEU   B 1 10  ? 38.003 -30.217 -17.256 1.00 19.99 ?  10  LEU   B C    1 
ATOM   4103 O O    . LEU   B 1 10  ? 38.006 -29.801 -16.094 1.00 19.79 ?  10  LEU   B O    1 
ATOM   4104 C CB   . LEU   B 1 10  ? 39.294 -32.346 -17.128 1.00 21.71 ?  10  LEU   B CB   1 
ATOM   4105 C CG   . LEU   B 1 10  ? 38.117 -33.275 -17.389 1.00 23.45 ?  10  LEU   B CG   1 
ATOM   4106 C CD1  . LEU   B 1 10  ? 38.193 -33.812 -18.809 1.00 25.27 ?  10  LEU   B CD1  1 
ATOM   4107 C CD2  . LEU   B 1 10  ? 38.108 -34.406 -16.381 1.00 25.36 ?  10  LEU   B CD2  1 
ATOM   4108 H H    . LEU   B 1 10  ? 40.729 -30.397 -16.748 1.00 25.24 ?  10  LEU   B H    1 
ATOM   4109 H HA   . LEU   B 1 10  ? 39.082 -31.111 -18.764 1.00 24.69 ?  10  LEU   B HA   1 
ATOM   4110 H HB2  . LEU   B 1 10  ? 40.093 -32.794 -17.446 1.00 26.07 ?  10  LEU   B HB2  1 
ATOM   4111 H HB3  . LEU   B 1 10  ? 39.355 -32.212 -16.170 1.00 26.07 ?  10  LEU   B HB3  1 
ATOM   4112 H HG   . LEU   B 1 10  ? 37.283 -32.782 -17.294 1.00 28.15 ?  10  LEU   B HG   1 
ATOM   4113 H HD11 . LEU   B 1 10  ? 37.464 -34.436 -18.949 1.00 30.34 ?  10  LEU   B HD11 1 
ATOM   4114 H HD12 . LEU   B 1 10  ? 38.117 -33.071 -19.431 1.00 30.34 ?  10  LEU   B HD12 1 
ATOM   4115 H HD13 . LEU   B 1 10  ? 39.043 -34.261 -18.928 1.00 30.34 ?  10  LEU   B HD13 1 
ATOM   4116 H HD21 . LEU   B 1 10  ? 37.357 -34.987 -16.572 1.00 30.45 ?  10  LEU   B HD21 1 
ATOM   4117 H HD22 . LEU   B 1 10  ? 38.939 -34.895 -16.459 1.00 30.45 ?  10  LEU   B HD22 1 
ATOM   4118 H HD23 . LEU   B 1 10  ? 38.022 -34.030 -15.492 1.00 30.45 ?  10  LEU   B HD23 1 
ATOM   4119 N N    . LYS   B 1 11  ? 36.988 -30.028 -18.090 1.00 21.66 ?  11  LYS   B N    1 
ATOM   4120 C CA   . LYS   B 1 11  ? 35.788 -29.321 -17.668 1.00 23.80 ?  11  LYS   B CA   1 
ATOM   4121 C C    . LYS   B 1 11  ? 34.914 -30.250 -16.828 1.00 22.91 ?  11  LYS   B C    1 
ATOM   4122 O O    . LYS   B 1 11  ? 34.528 -31.335 -17.288 1.00 25.47 ?  11  LYS   B O    1 
ATOM   4123 C CB   . LYS   B 1 11  ? 35.027 -28.839 -18.902 1.00 28.18 ?  11  LYS   B CB   1 
ATOM   4124 C CG   . LYS   B 1 11  ? 33.855 -27.925 -18.620 1.00 32.10 ?  11  LYS   B CG   1 
ATOM   4125 C CD   . LYS   B 1 11  ? 33.128 -27.590 -19.918 1.00 35.64 ?  11  LYS   B CD   1 
ATOM   4126 C CE   . LYS   B 1 11  ? 32.124 -26.465 -19.735 1.00 38.41 ?  11  LYS   B CE   1 
ATOM   4127 N NZ   . LYS   B 1 11  ? 32.785 -25.140 -19.587 1.00 40.13 ?  11  LYS   B NZ   1 
ATOM   4128 H H    . LYS   B 1 11  ? 36.972 -30.292 -18.913 1.00 26.00 ?  11  LYS   B H    1 
ATOM   4129 H HA   . LYS   B 1 11  ? 36.036 -28.548 -17.134 1.00 28.57 ?  11  LYS   B HA   1 
ATOM   4130 H HB2  . LYS   B 1 11  ? 35.642 -28.356 -19.477 1.00 33.84 ?  11  LYS   B HB2  1 
ATOM   4131 H HB3  . LYS   B 1 11  ? 34.685 -29.615 -19.374 1.00 33.84 ?  11  LYS   B HB3  1 
ATOM   4132 H HG2  . LYS   B 1 11  ? 33.232 -28.369 -18.025 1.00 38.53 ?  11  LYS   B HG2  1 
ATOM   4133 H HG3  . LYS   B 1 11  ? 34.175 -27.099 -18.225 1.00 38.53 ?  11  LYS   B HG3  1 
ATOM   4134 H HD2  . LYS   B 1 11  ? 33.778 -27.312 -20.583 1.00 42.78 ?  11  LYS   B HD2  1 
ATOM   4135 H HD3  . LYS   B 1 11  ? 32.650 -28.376 -20.226 1.00 42.78 ?  11  LYS   B HD3  1 
ATOM   4136 H HE2  . LYS   B 1 11  ? 31.542 -26.427 -20.511 1.00 46.11 ?  11  LYS   B HE2  1 
ATOM   4137 H HE3  . LYS   B 1 11  ? 31.603 -26.639 -18.937 1.00 46.11 ?  11  LYS   B HE3  1 
ATOM   4138 H HZ1  . LYS   B 1 11  ? 32.173 -24.503 -19.484 1.00 48.17 ?  11  LYS   B HZ1  1 
ATOM   4139 H HZ2  . LYS   B 1 11  ? 33.321 -25.145 -18.877 1.00 48.17 ?  11  LYS   B HZ2  1 
ATOM   4140 H HZ3  . LYS   B 1 11  ? 33.270 -24.960 -20.313 1.00 48.17 ?  11  LYS   B HZ3  1 
ATOM   4141 N N    . LEU   B 1 12  ? 34.594 -29.823 -15.604 1.00 20.84 ?  12  LEU   B N    1 
ATOM   4142 C CA   . LEU   B 1 12  ? 33.635 -30.529 -14.754 1.00 20.06 ?  12  LEU   B CA   1 
ATOM   4143 C C    . LEU   B 1 12  ? 32.237 -29.934 -14.835 1.00 20.34 ?  12  LEU   B C    1 
ATOM   4144 O O    . LEU   B 1 12  ? 31.262 -30.667 -14.991 1.00 21.26 ?  12  LEU   B O    1 
ATOM   4145 C CB   . LEU   B 1 12  ? 34.100 -30.538 -13.293 1.00 19.65 ?  12  LEU   B CB   1 
ATOM   4146 C CG   . LEU   B 1 12  ? 35.438 -31.226 -13.015 1.00 19.84 ?  12  LEU   B CG   1 
ATOM   4147 C CD1  . LEU   B 1 12  ? 35.776 -31.151 -11.535 1.00 20.01 ?  12  LEU   B CD1  1 
ATOM   4148 C CD2  . LEU   B 1 12  ? 35.427 -32.679 -13.498 1.00 20.91 ?  12  LEU   B CD2  1 
ATOM   4149 H H    . LEU   B 1 12  ? 34.927 -29.119 -15.240 1.00 25.03 ?  12  LEU   B H    1 
ATOM   4150 H HA   . LEU   B 1 12  ? 33.572 -31.446 -15.051 1.00 24.08 ?  12  LEU   B HA   1 
ATOM   4151 H HB2  . LEU   B 1 12  ? 34.172 -29.622 -12.985 1.00 23.60 ?  12  LEU   B HB2  1 
ATOM   4152 H HB3  . LEU   B 1 12  ? 33.425 -31.000 -12.763 1.00 23.60 ?  12  LEU   B HB3  1 
ATOM   4153 H HG   . LEU   B 1 12  ? 36.133 -30.754 -13.500 1.00 23.82 ?  12  LEU   B HG   1 
ATOM   4154 H HD11 . LEU   B 1 12  ? 36.632 -31.589 -11.386 1.00 24.02 ?  12  LEU   B HD11 1 
ATOM   4155 H HD12 . LEU   B 1 12  ? 35.834 -30.220 -11.269 1.00 24.02 ?  12  LEU   B HD12 1 
ATOM   4156 H HD13 . LEU   B 1 12  ? 35.084 -31.599 -11.029 1.00 24.02 ?  12  LEU   B HD13 1 
ATOM   4157 H HD21 . LEU   B 1 12  ? 36.234 -33.120 -13.191 1.00 25.10 ?  12  LEU   B HD21 1 
ATOM   4158 H HD22 . LEU   B 1 12  ? 34.647 -33.126 -13.136 1.00 25.10 ?  12  LEU   B HD22 1 
ATOM   4159 H HD23 . LEU   B 1 12  ? 35.393 -32.689 -14.468 1.00 25.10 ?  12  LEU   B HD23 1 
ATOM   4160 N N    . THR   B 1 13  ? 32.126 -28.617 -14.691 1.00 20.72 ?  13  THR   B N    1 
ATOM   4161 C CA   . THR   B 1 13  ? 30.894 -27.874 -14.908 1.00 20.78 ?  13  THR   B CA   1 
ATOM   4162 C C    . THR   B 1 13  ? 31.223 -26.674 -15.791 1.00 23.06 ?  13  THR   B C    1 
ATOM   4163 O O    . THR   B 1 13  ? 32.370 -26.471 -16.203 1.00 23.69 ?  13  THR   B O    1 
ATOM   4164 C CB   . THR   B 1 13  ? 30.286 -27.390 -13.585 1.00 20.64 ?  13  THR   B CB   1 
ATOM   4165 O OG1  . THR   B 1 13  ? 31.110 -26.347 -13.052 1.00 20.50 ?  13  THR   B OG1  1 
ATOM   4166 C CG2  . THR   B 1 13  ? 30.196 -28.522 -12.566 1.00 20.67 ?  13  THR   B CG2  1 
ATOM   4167 H H    . THR   B 1 13  ? 32.787 -28.105 -14.464 1.00 24.88 ?  13  THR   B H    1 
ATOM   4168 H HA   . THR   B 1 13  ? 30.250 -28.431 -15.358 1.00 24.95 ?  13  THR   B HA   1 
ATOM   4169 H HB   . THR   B 1 13  ? 29.389 -27.049 -13.741 1.00 24.79 ?  13  THR   B HB   1 
ATOM   4170 H HG1  . THR   B 1 13  ? 30.775 -25.590 -13.235 1.00 24.61 ?  13  THR   B HG1  1 
ATOM   4171 H HG21 . THR   B 1 13  ? 29.708 -28.227 -11.778 1.00 24.81 ?  13  THR   B HG21 1 
ATOM   4172 H HG22 . THR   B 1 13  ? 29.732 -29.281 -12.953 1.00 24.81 ?  13  THR   B HG22 1 
ATOM   4173 H HG23 . THR   B 1 13  ? 31.085 -28.800 -12.296 1.00 24.81 ?  13  THR   B HG23 1 
ATOM   4174 N N    A ASP   B 1 14  ? 30.204 -25.859 -16.063 0.46 23.85 ?  14  ASP   B N    1 
ATOM   4175 N N    B ASP   B 1 14  ? 30.212 -25.849 -16.068 0.54 23.79 ?  14  ASP   B N    1 
ATOM   4176 C CA   A ASP   B 1 14  ? 30.409 -24.692 -16.911 0.46 25.56 ?  14  ASP   B CA   1 
ATOM   4177 C CA   B ASP   B 1 14  ? 30.424 -24.691 -16.933 0.54 25.62 ?  14  ASP   B CA   1 
ATOM   4178 C C    A ASP   B 1 14  ? 31.523 -23.798 -16.383 0.46 23.57 ?  14  ASP   B C    1 
ATOM   4179 C C    B ASP   B 1 14  ? 31.423 -23.693 -16.364 0.54 23.95 ?  14  ASP   B C    1 
ATOM   4180 O O    A ASP   B 1 14  ? 32.230 -23.168 -17.177 0.46 24.08 ?  14  ASP   B O    1 
ATOM   4181 O O    B ASP   B 1 14  ? 31.900 -22.834 -17.111 0.54 25.11 ?  14  ASP   B O    1 
ATOM   4182 C CB   A ASP   B 1 14  ? 29.103 -23.908 -17.057 0.46 29.01 ?  14  ASP   B CB   1 
ATOM   4183 C CB   B ASP   B 1 14  ? 29.110 -23.961 -17.203 0.54 29.04 ?  14  ASP   B CB   1 
ATOM   4184 C CG   A ASP   B 1 14  ? 28.117 -24.574 -17.991 0.46 32.00 ?  14  ASP   B CG   1 
ATOM   4185 C CG   B ASP   B 1 14  ? 28.285 -24.634 -18.278 0.54 32.35 ?  14  ASP   B CG   1 
ATOM   4186 O OD1  A ASP   B 1 14  ? 28.435 -25.639 -18.568 0.46 32.69 ?  14  ASP   B OD1  1 
ATOM   4187 O OD1  B ASP   B 1 14  ? 28.885 -25.226 -19.202 0.54 33.44 ?  14  ASP   B OD1  1 
ATOM   4188 O OD2  A ASP   B 1 14  ? 27.011 -24.021 -18.139 0.46 33.71 -1 14  ASP   B OD2  1 
ATOM   4189 O OD2  B ASP   B 1 14  ? 27.043 -24.576 -18.201 0.54 33.78 -1 14  ASP   B OD2  1 
ATOM   4190 H H    A ASP   B 1 14  ? 29.403 -25.952 -15.764 0.46 28.64 ?  14  ASP   B H    1 
ATOM   4191 H H    B ASP   B 1 14  ? 29.407 -25.941 -15.778 0.54 28.56 ?  14  ASP   B H    1 
ATOM   4192 H HA   A ASP   B 1 14  ? 30.677 -24.980 -17.792 0.46 30.68 ?  14  ASP   B HA   1 
ATOM   4193 H HA   B ASP   B 1 14  ? 30.765 -25.001 -17.784 0.54 30.76 ?  14  ASP   B HA   1 
ATOM   4194 H HB2  A ASP   B 1 14  ? 28.659 -23.847 -16.201 0.46 34.83 ?  14  ASP   B HB2  1 
ATOM   4195 H HB2  B ASP   B 1 14  ? 28.592 -23.926 -16.383 0.54 34.86 ?  14  ASP   B HB2  1 
ATOM   4196 H HB3  A ASP   B 1 14  ? 29.289 -23.022 -17.404 0.46 34.83 ?  14  ASP   B HB3  1 
ATOM   4197 H HB3  B ASP   B 1 14  ? 29.310 -23.057 -17.503 0.54 34.86 ?  14  ASP   B HB3  1 
ATOM   4198 N N    . ASN   B 1 15  ? 31.722 -23.751 -15.062 1.00 21.40 ?  15  ASN   B N    1 
ATOM   4199 C CA   . ASN   B 1 15  ? 32.688 -22.828 -14.464 1.00 19.04 ?  15  ASN   B CA   1 
ATOM   4200 C C    . ASN   B 1 15  ? 33.791 -23.478 -13.636 1.00 17.85 ?  15  ASN   B C    1 
ATOM   4201 O O    . ASN   B 1 15  ? 34.628 -22.749 -13.096 1.00 17.83 ?  15  ASN   B O    1 
ATOM   4202 C CB   . ASN   B 1 15  ? 31.975 -21.773 -13.602 1.00 19.01 ?  15  ASN   B CB   1 
ATOM   4203 C CG   . ASN   B 1 15  ? 31.349 -22.370 -12.359 1.00 17.87 ?  15  ASN   B CG   1 
ATOM   4204 O OD1  . ASN   B 1 15  ? 30.408 -23.170 -12.445 1.00 20.19 ?  15  ASN   B OD1  1 
ATOM   4205 N ND2  . ASN   B 1 15  ? 31.860 -22.008 -11.203 1.00 17.36 ?  15  ASN   B ND2  1 
ATOM   4206 H H    A ASN   B 1 15  ? 31.313 -24.254 -14.492 0.46 25.70 ?  15  ASN   B H    1 
ATOM   4207 H H    B ASN   B 1 15  ? 31.346 -24.286 -14.500 0.54 25.70 ?  15  ASN   B H    1 
ATOM   4208 H HA   . ASN   B 1 15  ? 33.128 -22.345 -15.175 1.00 22.86 ?  15  ASN   B HA   1 
ATOM   4209 H HB2  . ASN   B 1 15  ? 32.627 -21.100 -13.321 1.00 22.83 ?  15  ASN   B HB2  1 
ATOM   4210 H HB3  . ASN   B 1 15  ? 31.277 -21.343 -14.125 1.00 22.83 ?  15  ASN   B HB3  1 
ATOM   4211 H HD21 . ASN   B 1 15  ? 31.528 -22.321 -10.472 1.00 20.84 ?  15  ASN   B HD21 1 
ATOM   4212 H HD22 . ASN   B 1 15  ? 32.520 -21.455 -11.169 1.00 20.84 ?  15  ASN   B HD22 1 
ATOM   4213 N N    . VAL   B 1 16  ? 33.829 -24.804 -13.514 1.00 17.41 ?  16  VAL   B N    1 
ATOM   4214 C CA   . VAL   B 1 16  ? 34.821 -25.498 -12.692 1.00 16.98 ?  16  VAL   B CA   1 
ATOM   4215 C C    . VAL   B 1 16  ? 35.614 -26.446 -13.578 1.00 17.38 ?  16  VAL   B C    1 
ATOM   4216 O O    . VAL   B 1 16  ? 35.033 -27.323 -14.236 1.00 17.88 ?  16  VAL   B O    1 
ATOM   4217 C CB   . VAL   B 1 16  ? 34.183 -26.246 -11.510 1.00 17.38 ?  16  VAL   B CB   1 
ATOM   4218 C CG1  . VAL   B 1 16  ? 35.239 -27.000 -10.699 1.00 16.76 ?  16  VAL   B CG1  1 
ATOM   4219 C CG2  . VAL   B 1 16  ? 33.392 -25.286 -10.639 1.00 17.32 ?  16  VAL   B CG2  1 
ATOM   4220 H H    . VAL   B 1 16  ? 33.274 -25.340 -13.908 1.00 20.91 ?  16  VAL   B H    1 
ATOM   4221 H HA   . VAL   B 1 16  ? 35.437 -24.846 -12.333 1.00 20.40 ?  16  VAL   B HA   1 
ATOM   4222 H HB   . VAL   B 1 16  ? 33.558 -26.903 -11.861 1.00 20.88 ?  16  VAL   B HB   1 
ATOM   4223 H HG11 . VAL   B 1 16  ? 34.838 -27.302 -9.867  1.00 20.13 ?  16  VAL   B HG11 1 
ATOM   4224 H HG12 . VAL   B 1 16  ? 35.552 -27.761 -11.209 1.00 20.13 ?  16  VAL   B HG12 1 
ATOM   4225 H HG13 . VAL   B 1 16  ? 35.976 -26.399 -10.507 1.00 20.13 ?  16  VAL   B HG13 1 
ATOM   4226 H HG21 . VAL   B 1 16  ? 33.044 -25.766 -9.872  1.00 20.80 ?  16  VAL   B HG21 1 
ATOM   4227 H HG22 . VAL   B 1 16  ? 33.975 -24.570 -10.346 1.00 20.80 ?  16  VAL   B HG22 1 
ATOM   4228 H HG23 . VAL   B 1 16  ? 32.655 -24.918 -11.158 1.00 20.80 ?  16  VAL   B HG23 1 
ATOM   4229 N N    . TYR   B 1 17  ? 36.941 -26.285 -13.561 1.00 17.86 ?  17  TYR   B N    1 
ATOM   4230 C CA   . TYR   B 1 17  ? 37.891 -27.040 -14.368 1.00 17.24 ?  17  TYR   B CA   1 
ATOM   4231 C C    . TYR   B 1 17  ? 38.945 -27.640 -13.448 1.00 16.56 ?  17  TYR   B C    1 
ATOM   4232 O O    . TYR   B 1 17  ? 39.217 -27.102 -12.371 1.00 17.30 ?  17  TYR   B O    1 
ATOM   4233 C CB   . TYR   B 1 17  ? 38.595 -26.131 -15.382 1.00 19.59 ?  17  TYR   B CB   1 
ATOM   4234 C CG   . TYR   B 1 17  ? 37.660 -25.370 -16.290 1.00 23.44 ?  17  TYR   B CG   1 
ATOM   4235 C CD1  . TYR   B 1 17  ? 37.088 -24.171 -15.886 1.00 24.70 ?  17  TYR   B CD1  1 
ATOM   4236 C CD2  . TYR   B 1 17  ? 37.358 -25.843 -17.560 1.00 26.08 ?  17  TYR   B CD2  1 
ATOM   4237 C CE1  . TYR   B 1 17  ? 36.228 -23.469 -16.716 1.00 27.08 ?  17  TYR   B CE1  1 
ATOM   4238 C CE2  . TYR   B 1 17  ? 36.506 -25.149 -18.399 1.00 28.21 ?  17  TYR   B CE2  1 
ATOM   4239 C CZ   . TYR   B 1 17  ? 35.945 -23.962 -17.970 1.00 28.64 ?  17  TYR   B CZ   1 
ATOM   4240 O OH   . TYR   B 1 17  ? 35.102 -23.263 -18.800 1.00 29.84 ?  17  TYR   B OH   1 
ATOM   4241 H H    . TYR   B 1 17  ? 37.334 -25.716 -13.051 1.00 21.44 ?  17  TYR   B H    1 
ATOM   4242 H HA   . TYR   B 1 17  ? 37.433 -27.758 -14.844 1.00 20.71 ?  17  TYR   B HA   1 
ATOM   4243 H HB2  . TYR   B 1 17  ? 39.141 -25.489 -14.905 1.00 23.52 ?  17  TYR   B HB2  1 
ATOM   4244 H HB3  . TYR   B 1 17  ? 39.151 -26.681 -15.950 1.00 23.52 ?  17  TYR   B HB3  1 
ATOM   4245 H HD1  . TYR   B 1 17  ? 37.280 -23.837 -15.038 1.00 29.65 ?  17  TYR   B HD1  1 
ATOM   4246 H HD2  . TYR   B 1 17  ? 37.731 -26.642 -17.851 1.00 31.31 ?  17  TYR   B HD2  1 
ATOM   4247 H HE1  . TYR   B 1 17  ? 35.851 -22.665 -16.432 1.00 32.51 ?  17  TYR   B HE1  1 
ATOM   4248 H HE2  . TYR   B 1 17  ? 36.306 -25.478 -19.247 1.00 33.87 ?  17  TYR   B HE2  1 
ATOM   4249 H HH   . TYR   B 1 17  ? 35.004 -23.667 -19.530 1.00 35.82 ?  17  TYR   B HH   1 
ATOM   4250 N N    . ILE   B 1 18  ? 39.568 -28.744 -13.878 1.00 16.78 ?  18  ILE   B N    1 
ATOM   4251 C CA   . ILE   B 1 18  ? 40.493 -29.458 -13.009 1.00 16.48 ?  18  ILE   B CA   1 
ATOM   4252 C C    . ILE   B 1 18  ? 41.662 -30.006 -13.819 1.00 17.05 ?  18  ILE   B C    1 
ATOM   4253 O O    . ILE   B 1 18  ? 41.514 -30.405 -14.978 1.00 18.76 ?  18  ILE   B O    1 
ATOM   4254 C CB   . ILE   B 1 18  ? 39.741 -30.556 -12.205 1.00 17.09 ?  18  ILE   B CB   1 
ATOM   4255 C CG1  . ILE   B 1 18  ? 40.617 -31.131 -11.088 1.00 17.52 ?  18  ILE   B CG1  1 
ATOM   4256 C CG2  . ILE   B 1 18  ? 39.198 -31.673 -13.132 1.00 17.21 ?  18  ILE   B CG2  1 
ATOM   4257 C CD1  . ILE   B 1 18  ? 39.820 -31.914 -10.046 1.00 18.90 ?  18  ILE   B CD1  1 
ATOM   4258 H H    . ILE   B 1 18  ? 39.488 -29.088 -14.665 1.00 20.15 ?  18  ILE   B H    1 
ATOM   4259 H HA   . ILE   B 1 18  ? 40.858 -28.834 -12.360 1.00 19.79 ?  18  ILE   B HA   1 
ATOM   4260 H HB   . ILE   B 1 18  ? 38.975 -30.138 -11.780 1.00 20.53 ?  18  ILE   B HB   1 
ATOM   4261 H HG12 . ILE   B 1 18  ? 41.267 -31.739 -11.477 1.00 21.04 ?  18  ILE   B HG12 1 
ATOM   4262 H HG13 . ILE   B 1 18  ? 41.068 -30.407 -10.635 1.00 21.04 ?  18  ILE   B HG13 1 
ATOM   4263 H HG21 . ILE   B 1 18  ? 38.641 -32.281 -12.611 1.00 20.67 ?  18  ILE   B HG21 1 
ATOM   4264 H HG22 . ILE   B 1 18  ? 38.660 -31.269 -13.835 1.00 20.67 ?  18  ILE   B HG22 1 
ATOM   4265 H HG23 . ILE   B 1 18  ? 39.937 -32.160 -13.521 1.00 20.67 ?  18  ILE   B HG23 1 
ATOM   4266 H HD11 . ILE   B 1 18  ? 40.424 -32.213 -9.346  1.00 22.69 ?  18  ILE   B HD11 1 
ATOM   4267 H HD12 . ILE   B 1 18  ? 39.141 -31.333 -9.668  1.00 22.69 ?  18  ILE   B HD12 1 
ATOM   4268 H HD13 . ILE   B 1 18  ? 39.402 -32.679 -10.470 1.00 22.69 ?  18  ILE   B HD13 1 
ATOM   4269 N N    . LYS   B 1 19  ? 42.836 -30.038 -13.187 1.00 17.61 ?  19  LYS   B N    1 
ATOM   4270 C CA   . LYS   B 1 19  ? 44.049 -30.506 -13.837 1.00 17.89 ?  19  LYS   B CA   1 
ATOM   4271 C C    . LYS   B 1 19  ? 44.933 -31.194 -12.809 1.00 18.49 ?  19  LYS   B C    1 
ATOM   4272 O O    . LYS   B 1 19  ? 45.008 -30.762 -11.654 1.00 17.49 ?  19  LYS   B O    1 
ATOM   4273 C CB   . LYS   B 1 19  ? 44.816 -29.328 -14.445 1.00 19.66 ?  19  LYS   B CB   1 
ATOM   4274 C CG   . LYS   B 1 19  ? 46.032 -29.730 -15.257 1.00 21.53 ?  19  LYS   B CG   1 
ATOM   4275 C CD   . LYS   B 1 19  ? 46.738 -28.490 -15.785 1.00 23.24 ?  19  LYS   B CD   1 
ATOM   4276 C CE   . LYS   B 1 19  ? 47.878 -28.834 -16.718 1.00 25.89 ?  19  LYS   B CE   1 
ATOM   4277 N NZ   . LYS   B 1 19  ? 48.459 -27.604 -17.324 1.00 27.27 ?  19  LYS   B NZ   1 
ATOM   4278 H H    . LYS   B 1 19  ? 42.949 -29.801 -12.370 1.00 21.15 ?  19  LYS   B H    1 
ATOM   4279 H HA   . LYS   B 1 19  ? 43.825 -31.135 -14.545 1.00 21.48 ?  19  LYS   B HA   1 
ATOM   4280 H HB2  . LYS   B 1 19  ? 44.218 -28.837 -15.034 1.00 23.60 ?  19  LYS   B HB2  1 
ATOM   4281 H HB3  . LYS   B 1 19  ? 45.113 -28.745 -13.725 1.00 23.60 ?  19  LYS   B HB3  1 
ATOM   4282 H HG2  . LYS   B 1 19  ? 46.647 -30.224 -14.697 1.00 25.85 ?  19  LYS   B HG2  1 
ATOM   4283 H HG3  . LYS   B 1 19  ? 45.748 -30.269 -16.013 1.00 25.85 ?  19  LYS   B HG3  1 
ATOM   4284 H HD2  . LYS   B 1 19  ? 46.104 -27.940 -16.272 1.00 27.90 ?  19  LYS   B HD2  1 
ATOM   4285 H HD3  . LYS   B 1 19  ? 47.104 -27.988 -15.035 1.00 27.90 ?  19  LYS   B HD3  1 
ATOM   4286 H HE2  . LYS   B 1 19  ? 48.575 -29.293 -16.221 1.00 31.08 ?  19  LYS   B HE2  1 
ATOM   4287 H HE3  . LYS   B 1 19  ? 47.545 -29.404 -17.432 1.00 31.08 ?  19  LYS   B HE3  1 
ATOM   4288 H HZ1  . LYS   B 1 19  ? 49.108 -27.820 -17.893 1.00 32.74 ?  19  LYS   B HZ1  1 
ATOM   4289 H HZ2  . LYS   B 1 19  ? 47.827 -27.155 -17.765 1.00 32.74 ?  19  LYS   B HZ2  1 
ATOM   4290 H HZ3  . LYS   B 1 19  ? 48.794 -27.080 -16.688 1.00 32.74 ?  19  LYS   B HZ3  1 
ATOM   4291 N N    . ASN   B 1 20  ? 45.627 -32.242 -13.243 1.00 20.06 ?  20  ASN   B N    1 
ATOM   4292 C CA   . ASN   B 1 20  ? 46.639 -32.879 -12.407 1.00 21.01 ?  20  ASN   B CA   1 
ATOM   4293 C C    . ASN   B 1 20  ? 47.917 -32.069 -12.581 1.00 21.74 ?  20  ASN   B C    1 
ATOM   4294 O O    . ASN   B 1 20  ? 48.570 -32.149 -13.625 1.00 23.97 ?  20  ASN   B O    1 
ATOM   4295 C CB   . ASN   B 1 20  ? 46.805 -34.336 -12.835 1.00 22.68 ?  20  ASN   B CB   1 
ATOM   4296 C CG   . ASN   B 1 20  ? 47.967 -35.043 -12.152 1.00 24.17 ?  20  ASN   B CG   1 
ATOM   4297 O OD1  . ASN   B 1 20  ? 48.614 -35.909 -12.758 1.00 27.83 ?  20  ASN   B OD1  1 
ATOM   4298 N ND2  . ASN   B 1 20  ? 48.212 -34.720 -10.887 1.00 23.14 ?  20  ASN   B ND2  1 
ATOM   4299 H H    . ASN   B 1 20  ? 45.541 -32.593 -14.025 1.00 24.09 ?  20  ASN   B H    1 
ATOM   4300 H HA   . ASN   B 1 20  ? 46.354 -32.847 -11.482 1.00 25.23 ?  20  ASN   B HA   1 
ATOM   4301 H HB2  . ASN   B 1 20  ? 45.994 -34.818 -12.617 1.00 27.23 ?  20  ASN   B HB2  1 
ATOM   4302 H HB3  . ASN   B 1 20  ? 46.960 -34.363 -13.791 1.00 27.23 ?  20  ASN   B HB3  1 
ATOM   4303 H HD21 . ASN   B 1 20  ? 48.862 -35.092 -10.467 1.00 27.78 ?  20  ASN   B HD21 1 
ATOM   4304 H HD22 . ASN   B 1 20  ? 47.734 -34.121 -10.488 1.00 27.78 ?  20  ASN   B HD22 1 
ATOM   4305 N N    . ALA   B 1 21  ? 48.263 -31.254 -11.579 1.00 20.88 ?  21  ALA   B N    1 
ATOM   4306 C CA   . ALA   B 1 21  ? 49.386 -30.346 -11.740 1.00 21.27 ?  21  ALA   B CA   1 
ATOM   4307 C C    . ALA   B 1 21  ? 49.840 -29.822 -10.389 1.00 19.02 ?  21  ALA   B C    1 
ATOM   4308 O O    . ALA   B 1 21  ? 49.101 -29.844 -9.405  1.00 19.02 ?  21  ALA   B O    1 
ATOM   4309 C CB   . ALA   B 1 21  ? 49.019 -29.176 -12.652 1.00 23.09 ?  21  ALA   B CB   1 
ATOM   4310 H H    . ALA   B 1 21  ? 47.855 -31.205 -10.806 1.00 25.07 ?  21  ALA   B H    1 
ATOM   4311 H HA   . ALA   B 1 21  ? 50.121 -30.834 -12.134 1.00 25.54 ?  21  ALA   B HA   1 
ATOM   4312 H HB1  . ALA   B 1 21  ? 49.815 -28.656 -12.810 1.00 27.72 ?  21  ALA   B HB1  1 
ATOM   4313 H HB2  . ALA   B 1 21  ? 48.680 -29.537 -13.484 1.00 27.72 ?  21  ALA   B HB2  1 
ATOM   4314 H HB3  . ALA   B 1 21  ? 48.338 -28.643 -12.218 1.00 27.72 ?  21  ALA   B HB3  1 
ATOM   4315 N N    . ASP   B 1 22  ? 51.096 -29.374 -10.375 1.00 18.48 ?  22  ASP   B N    1 
ATOM   4316 C CA   . ASP   B 1 22  ? 51.713 -28.667 -9.255  1.00 18.61 ?  22  ASP   B CA   1 
ATOM   4317 C C    . ASP   B 1 22  ? 51.299 -27.200 -9.344  1.00 18.03 ?  22  ASP   B C    1 
ATOM   4318 O O    . ASP   B 1 22  ? 51.596 -26.537 -10.338 1.00 18.09 ?  22  ASP   B O    1 
ATOM   4319 C CB   . ASP   B 1 22  ? 53.232 -28.837 -9.401  1.00 19.77 ?  22  ASP   B CB   1 
ATOM   4320 C CG   . ASP   B 1 22  ? 54.052 -28.045 -8.386  1.00 21.50 ?  22  ASP   B CG   1 
ATOM   4321 O OD1  . ASP   B 1 22  ? 53.681 -26.927 -7.995  1.00 21.24 ?  22  ASP   B OD1  1 
ATOM   4322 O OD2  . ASP   B 1 22  ? 55.136 -28.541 -8.000  1.00 24.46 -1 22  ASP   B OD2  1 
ATOM   4323 H H    . ASP   B 1 22  ? 51.639 -29.465 -11.042 1.00 22.19 ?  22  ASP   B H    1 
ATOM   4324 H HA   . ASP   B 1 22  ? 51.421 -29.041 -8.409  1.00 22.35 ?  22  ASP   B HA   1 
ATOM   4325 H HB2  . ASP   B 1 22  ? 53.454 -29.770 -9.295  1.00 23.74 ?  22  ASP   B HB2  1 
ATOM   4326 H HB3  . ASP   B 1 22  ? 53.494 -28.531 -10.285 1.00 23.74 ?  22  ASP   B HB3  1 
ATOM   4327 N N    . ILE   B 1 23  ? 50.589 -26.700 -8.322  1.00 17.36 ?  23  ILE   B N    1 
ATOM   4328 C CA   . ILE   B 1 23  ? 49.988 -25.366 -8.396  1.00 16.43 ?  23  ILE   B CA   1 
ATOM   4329 C C    . ILE   B 1 23  ? 51.034 -24.272 -8.554  1.00 15.41 ?  23  ILE   B C    1 
ATOM   4330 O O    . ILE   B 1 23  ? 50.756 -23.243 -9.175  1.00 15.48 ?  23  ILE   B O    1 
ATOM   4331 C CB   . ILE   B 1 23  ? 49.055 -25.124 -7.191  1.00 17.06 ?  23  ILE   B CB   1 
ATOM   4332 C CG1  . ILE   B 1 23  ? 48.224 -23.857 -7.403  1.00 17.52 ?  23  ILE   B CG1  1 
ATOM   4333 C CG2  . ILE   B 1 23  ? 49.835 -25.069 -5.892  1.00 17.96 ?  23  ILE   B CG2  1 
ATOM   4334 C CD1  . ILE   B 1 23  ? 47.081 -23.688 -6.412  1.00 17.86 ?  23  ILE   B CD1  1 
ATOM   4335 H H    . ILE   B 1 23  ? 50.459 -27.109 -7.576  1.00 20.85 ?  23  ILE   B H    1 
ATOM   4336 H HA   . ILE   B 1 23  ? 49.432 -25.340 -9.187  1.00 19.74 ?  23  ILE   B HA   1 
ATOM   4337 H HB   . ILE   B 1 23  ? 48.441 -25.874 -7.137  1.00 20.49 ?  23  ILE   B HB   1 
ATOM   4338 H HG12 . ILE   B 1 23  ? 48.806 -23.083 -7.317  1.00 21.04 ?  23  ILE   B HG12 1 
ATOM   4339 H HG13 . ILE   B 1 23  ? 47.842 -23.876 -8.296  1.00 21.04 ?  23  ILE   B HG13 1 
ATOM   4340 H HG21 . ILE   B 1 23  ? 49.216 -25.052 -5.147  1.00 21.56 ?  23  ILE   B HG21 1 
ATOM   4341 H HG22 . ILE   B 1 23  ? 50.405 -25.854 -5.829  1.00 21.56 ?  23  ILE   B HG22 1 
ATOM   4342 H HG23 . ILE   B 1 23  ? 50.384 -24.267 -5.883  1.00 21.56 ?  23  ILE   B HG23 1 
ATOM   4343 H HD11 . ILE   B 1 23  ? 46.580 -22.893 -6.646  1.00 21.45 ?  23  ILE   B HD11 1 
ATOM   4344 H HD12 . ILE   B 1 23  ? 46.510 -24.469 -6.464  1.00 21.45 ?  23  ILE   B HD12 1 
ATOM   4345 H HD13 . ILE   B 1 23  ? 47.451 -23.602 -5.522  1.00 21.45 ?  23  ILE   B HD13 1 
ATOM   4346 N N    . VAL   B 1 24  ? 52.239 -24.468 -8.009  1.00 16.03 ?  24  VAL   B N    1 
ATOM   4347 C CA   . VAL   B 1 24  ? 53.305 -23.483 -8.183  1.00 15.84 ?  24  VAL   B CA   1 
ATOM   4348 C C    . VAL   B 1 24  ? 53.759 -23.445 -9.634  1.00 17.32 ?  24  VAL   B C    1 
ATOM   4349 O O    . VAL   B 1 24  ? 53.893 -22.371 -10.238 1.00 17.68 ?  24  VAL   B O    1 
ATOM   4350 C CB   . VAL   B 1 24  ? 54.482 -23.795 -7.236  1.00 16.41 ?  24  VAL   B CB   1 
ATOM   4351 C CG1  . VAL   B 1 24  ? 55.685 -22.913 -7.566  1.00 17.80 ?  24  VAL   B CG1  1 
ATOM   4352 C CG2  . VAL   B 1 24  ? 54.073 -23.601 -5.793  1.00 17.21 ?  24  VAL   B CG2  1 
ATOM   4353 H H    . VAL   B 1 24  ? 52.463 -25.157 -7.552  1.00 19.25 ?  24  VAL   B H    1 
ATOM   4354 H HA   . VAL   B 1 24  ? 52.963 -22.605 -7.958  1.00 19.03 ?  24  VAL   B HA   1 
ATOM   4355 H HB   . VAL   B 1 24  ? 54.746 -24.721 -7.352  1.00 19.71 ?  24  VAL   B HB   1 
ATOM   4356 H HG11 . VAL   B 1 24  ? 56.274 -22.890 -6.795  1.00 21.37 ?  24  VAL   B HG11 1 
ATOM   4357 H HG12 . VAL   B 1 24  ? 56.150 -23.285 -8.327  1.00 21.37 ?  24  VAL   B HG12 1 
ATOM   4358 H HG13 . VAL   B 1 24  ? 55.372 -22.016 -7.767  1.00 21.37 ?  24  VAL   B HG13 1 
ATOM   4359 H HG21 . VAL   B 1 24  ? 54.801 -23.882 -5.221  1.00 20.67 ?  24  VAL   B HG21 1 
ATOM   4360 H HG22 . VAL   B 1 24  ? 53.882 -22.659 -5.649  1.00 20.67 ?  24  VAL   B HG22 1 
ATOM   4361 H HG23 . VAL   B 1 24  ? 53.282 -24.130 -5.615  1.00 20.67 ?  24  VAL   B HG23 1 
ATOM   4362 N N    . GLU   B 1 25  ? 54.033 -24.618 -10.210 1.00 18.41 ?  25  GLU   B N    1 
ATOM   4363 C CA   . GLU   B 1 25  ? 54.420 -24.662 -11.613 1.00 20.14 ?  25  GLU   B CA   1 
ATOM   4364 C C    . GLU   B 1 25  ? 53.309 -24.118 -12.494 1.00 17.65 ?  25  GLU   B C    1 
ATOM   4365 O O    . GLU   B 1 25  ? 53.572 -23.396 -13.461 1.00 18.71 ?  25  GLU   B O    1 
ATOM   4366 C CB   . GLU   B 1 25  ? 54.810 -26.087 -12.007 1.00 25.63 ?  25  GLU   B CB   1 
ATOM   4367 C CG   . GLU   B 1 25  ? 56.112 -26.532 -11.349 1.00 32.29 ?  25  GLU   B CG   1 
ATOM   4368 C CD   . GLU   B 1 25  ? 57.235 -25.501 -11.483 1.00 38.70 ?  25  GLU   B CD   1 
ATOM   4369 O OE1  . GLU   B 1 25  ? 57.664 -25.222 -12.625 1.00 41.14 ?  25  GLU   B OE1  1 
ATOM   4370 O OE2  . GLU   B 1 25  ? 57.675 -24.950 -10.444 1.00 40.08 -1 25  GLU   B OE2  1 
ATOM   4371 H H    . GLU   B 1 25  ? 54.006 -25.382 -9.818  1.00 22.10 ?  25  GLU   B H    1 
ATOM   4372 H HA   . GLU   B 1 25  ? 55.183 -24.083 -11.746 1.00 24.18 ?  25  GLU   B HA   1 
ATOM   4373 H HB2  . GLU   B 1 25  ? 54.108 -26.699 -11.724 1.00 30.76 ?  25  GLU   B HB2  1 
ATOM   4374 H HB3  . GLU   B 1 25  ? 54.922 -26.135 -12.969 1.00 30.76 ?  25  GLU   B HB3  1 
ATOM   4375 H HG2  . GLU   B 1 25  ? 55.960 -26.661 -10.405 1.00 38.76 ?  25  GLU   B HG2  1 
ATOM   4376 H HG3  . GLU   B 1 25  ? 56.407 -27.357 -11.763 1.00 38.76 ?  25  GLU   B HG3  1 
ATOM   4377 N N    A GLU   B 1 26  ? 52.059 -24.447 -12.167 0.46 16.39 ?  26  GLU   B N    1 
ATOM   4378 N N    B GLU   B 1 26  ? 52.058 -24.446 -12.164 0.54 16.90 ?  26  GLU   B N    1 
ATOM   4379 C CA   A GLU   B 1 26  ? 50.931 -23.923 -12.928 0.46 16.69 ?  26  GLU   B CA   1 
ATOM   4380 C CA   B GLU   B 1 26  ? 50.925 -23.931 -12.925 0.54 17.95 ?  26  GLU   B CA   1 
ATOM   4381 C C    A GLU   B 1 26  ? 50.892 -22.406 -12.862 0.46 16.70 ?  26  GLU   B C    1 
ATOM   4382 C C    B GLU   B 1 26  ? 50.863 -22.414 -12.855 0.54 17.15 ?  26  GLU   B C    1 
ATOM   4383 O O    A GLU   B 1 26  ? 50.714 -21.733 -13.882 0.46 17.59 ?  26  GLU   B O    1 
ATOM   4384 O O    B GLU   B 1 26  ? 50.631 -21.749 -13.870 0.54 17.89 ?  26  GLU   B O    1 
ATOM   4385 C CB   A GLU   B 1 26  ? 49.622 -24.494 -12.388 0.46 17.53 ?  26  GLU   B CB   1 
ATOM   4386 C CB   B GLU   B 1 26  ? 49.621 -24.519 -12.386 0.54 20.17 ?  26  GLU   B CB   1 
ATOM   4387 C CG   A GLU   B 1 26  ? 49.267 -25.868 -12.916 0.46 18.82 ?  26  GLU   B CG   1 
ATOM   4388 C CG   B GLU   B 1 26  ? 49.065 -25.705 -13.161 0.54 23.23 ?  26  GLU   B CG   1 
ATOM   4389 C CD   A GLU   B 1 26  ? 49.122 -25.916 -14.435 0.46 18.83 ?  26  GLU   B CD   1 
ATOM   4390 C CD   B GLU   B 1 26  ? 48.754 -25.367 -14.610 0.54 24.35 ?  26  GLU   B CD   1 
ATOM   4391 O OE1  A GLU   B 1 26  ? 48.266 -25.191 -14.992 0.46 19.18 ?  26  GLU   B OE1  1 
ATOM   4392 O OE1  B GLU   B 1 26  ? 47.737 -24.700 -14.890 0.54 25.86 ?  26  GLU   B OE1  1 
ATOM   4393 O OE2  A GLU   B 1 26  ? 49.866 -26.688 -15.069 0.46 19.36 -1 26  GLU   B OE2  1 
ATOM   4394 O OE2  B GLU   B 1 26  ? 49.538 -25.783 -15.475 0.54 23.71 -1 26  GLU   B OE2  1 
ATOM   4395 H H    A GLU   B 1 26  ? 51.840 -24.960 -11.512 0.46 19.68 ?  26  GLU   B H    1 
ATOM   4396 H H    B GLU   B 1 26  ? 51.843 -24.956 -11.506 0.54 20.29 ?  26  GLU   B H    1 
ATOM   4397 H HA   A GLU   B 1 26  ? 51.020 -24.183 -13.856 0.46 20.04 ?  26  GLU   B HA   1 
ATOM   4398 H HA   B GLU   B 1 26  ? 51.020 -24.189 -13.854 0.54 21.56 ?  26  GLU   B HA   1 
ATOM   4399 H HB2  A GLU   B 1 26  ? 49.688 -24.558 -11.419 0.46 21.05 ?  26  GLU   B HB2  1 
ATOM   4400 H HB2  B GLU   B 1 26  ? 49.766 -24.814 -11.475 0.54 24.22 ?  26  GLU   B HB2  1 
ATOM   4401 H HB3  A GLU   B 1 26  ? 48.898 -23.890 -12.620 0.46 21.05 ?  26  GLU   B HB3  1 
ATOM   4402 H HB3  B GLU   B 1 26  ? 48.943 -23.826 -12.398 0.54 24.22 ?  26  GLU   B HB3  1 
ATOM   4403 H HG2  A GLU   B 1 26  ? 49.973 -26.473 -12.671 0.46 22.60 ?  26  GLU   B HG2  1 
ATOM   4404 H HG2  B GLU   B 1 26  ? 49.713 -26.426 -13.145 0.54 27.89 ?  26  GLU   B HG2  1 
ATOM   4405 H HG3  A GLU   B 1 26  ? 48.428 -26.141 -12.508 0.46 22.60 ?  26  GLU   B HG3  1 
ATOM   4406 H HG3  B GLU   B 1 26  ? 48.237 -25.998 -12.745 0.54 27.89 ?  26  GLU   B HG3  1 
ATOM   4407 N N    . ALA   B 1 27  ? 51.045 -21.851 -11.661 1.00 16.75 ?  27  ALA   B N    1 
ATOM   4408 C CA   . ALA   B 1 27  ? 50.991 -20.403 -11.521 1.00 16.03 ?  27  ALA   B CA   1 
ATOM   4409 C C    . ALA   B 1 27  ? 52.060 -19.743 -12.377 1.00 17.03 ?  27  ALA   B C    1 
ATOM   4410 O O    . ALA   B 1 27  ? 51.796 -18.744 -13.059 1.00 18.29 ?  27  ALA   B O    1 
ATOM   4411 C CB   . ALA   B 1 27  ? 51.125 -20.012 -10.050 1.00 16.38 ?  27  ALA   B CB   1 
ATOM   4412 H H    A ALA   B 1 27  ? 51.189 -22.281 -10.930 0.46 20.12 ?  27  ALA   B H    1 
ATOM   4413 H H    B ALA   B 1 27  ? 51.200 -22.279 -10.931 0.54 20.12 ?  27  ALA   B H    1 
ATOM   4414 H HA   . ALA   B 1 27  ? 50.130 -20.089 -11.833 1.00 19.25 ?  27  ALA   B HA   1 
ATOM   4415 H HB1  . ALA   B 1 27  ? 51.077 -19.041 -9.978  1.00 19.67 ?  27  ALA   B HB1  1 
ATOM   4416 H HB2  . ALA   B 1 27  ? 50.391 -20.409 -9.552  1.00 19.67 ?  27  ALA   B HB2  1 
ATOM   4417 H HB3  . ALA   B 1 27  ? 51.970 -20.327 -9.710  1.00 19.67 ?  27  ALA   B HB3  1 
ATOM   4418 N N    . LYS   B 1 28  ? 53.272 -20.296 -12.375 1.00 18.84 ?  28  LYS   B N    1 
ATOM   4419 C CA   . LYS   B 1 28  ? 54.347 -19.677 -13.144 1.00 21.04 ?  28  LYS   B CA   1 
ATOM   4420 C C    . LYS   B 1 28  ? 54.088 -19.753 -14.645 1.00 21.92 ?  28  LYS   B C    1 
ATOM   4421 O O    . LYS   B 1 28  ? 54.473 -18.841 -15.386 1.00 24.45 ?  28  LYS   B O    1 
ATOM   4422 C CB   . LYS   B 1 28  ? 55.705 -20.275 -12.748 1.00 24.96 ?  28  LYS   B CB   1 
ATOM   4423 C CG   . LYS   B 1 28  ? 56.090 -19.950 -11.300 1.00 28.45 ?  28  LYS   B CG   1 
ATOM   4424 C CD   . LYS   B 1 28  ? 57.520 -20.351 -10.945 1.00 33.56 ?  28  LYS   B CD   1 
ATOM   4425 C CE   . LYS   B 1 28  ? 57.637 -21.827 -10.665 1.00 37.42 ?  28  LYS   B CE   1 
ATOM   4426 N NZ   . LYS   B 1 28  ? 58.989 -22.162 -10.125 1.00 40.23 ?  28  LYS   B NZ   1 
ATOM   4427 H H    . LYS   B 1 28  ? 53.495 -21.005 -11.946 1.00 22.63 ?  28  LYS   B H    1 
ATOM   4428 H HA   . LYS   B 1 28  ? 54.383 -18.736 -12.913 1.00 25.27 ?  28  LYS   B HA   1 
ATOM   4429 H HB2  . LYS   B 1 28  ? 55.668 -21.240 -12.834 1.00 29.97 ?  28  LYS   B HB2  1 
ATOM   4430 H HB3  . LYS   B 1 28  ? 56.396 -19.915 -13.327 1.00 29.97 ?  28  LYS   B HB3  1 
ATOM   4431 H HG2  . LYS   B 1 28  ? 56.005 -18.992 -11.164 1.00 34.15 ?  28  LYS   B HG2  1 
ATOM   4432 H HG3  . LYS   B 1 28  ? 55.489 -20.421 -10.704 1.00 34.15 ?  28  LYS   B HG3  1 
ATOM   4433 H HD2  . LYS   B 1 28  ? 58.104 -20.134 -11.689 1.00 40.29 ?  28  LYS   B HD2  1 
ATOM   4434 H HD3  . LYS   B 1 28  ? 57.796 -19.865 -10.152 1.00 40.29 ?  28  LYS   B HD3  1 
ATOM   4435 H HE2  . LYS   B 1 28  ? 56.974 -22.084 -10.006 1.00 44.91 ?  28  LYS   B HE2  1 
ATOM   4436 H HE3  . LYS   B 1 28  ? 57.506 -22.324 -11.487 1.00 44.91 ?  28  LYS   B HE3  1 
ATOM   4437 H HZ1  . LYS   B 1 28  ? 59.044 -23.034 -9.964  1.00 48.29 ?  28  LYS   B HZ1  1 
ATOM   4438 H HZ2  . LYS   B 1 28  ? 59.615 -21.935 -10.715 1.00 48.29 ?  28  LYS   B HZ2  1 
ATOM   4439 H HZ3  . LYS   B 1 28  ? 59.131 -21.717 -9.367  1.00 48.29 ?  28  LYS   B HZ3  1 
ATOM   4440 N N    . LYS   B 1 29  ? 53.392 -20.795 -15.107 1.00 23.35 ?  29  LYS   B N    1 
ATOM   4441 C CA   . LYS   B 1 29  ? 53.084 -20.925 -16.529 1.00 26.57 ?  29  LYS   B CA   1 
ATOM   4442 C C    . LYS   B 1 29  ? 51.844 -20.122 -16.934 1.00 25.00 ?  29  LYS   B C    1 
ATOM   4443 O O    . LYS   B 1 29  ? 51.855 -19.449 -17.972 1.00 26.68 ?  29  LYS   B O    1 
ATOM   4444 C CB   . LYS   B 1 29  ? 52.896 -22.400 -16.882 1.00 33.38 ?  29  LYS   B CB   1 
ATOM   4445 C CG   . LYS   B 1 29  ? 52.833 -22.669 -18.373 1.00 39.60 ?  29  LYS   B CG   1 
ATOM   4446 C CD   . LYS   B 1 29  ? 53.039 -24.143 -18.684 1.00 44.53 ?  29  LYS   B CD   1 
ATOM   4447 C CE   . LYS   B 1 29  ? 51.879 -24.987 -18.188 1.00 48.15 ?  29  LYS   B CE   1 
ATOM   4448 N NZ   . LYS   B 1 29  ? 52.092 -26.434 -18.476 1.00 50.16 ?  29  LYS   B NZ   1 
ATOM   4449 H H    . LYS   B 1 29  ? 53.095 -21.437 -14.618 1.00 28.04 ?  29  LYS   B H    1 
ATOM   4450 H HA   . LYS   B 1 29  ? 53.832 -20.592 -17.042 1.00 31.89 ?  29  LYS   B HA   1 
ATOM   4451 H HB2  . LYS   B 1 29  ? 53.645 -22.906 -16.522 1.00 40.07 ?  29  LYS   B HB2  1 
ATOM   4452 H HB3  . LYS   B 1 29  ? 52.069 -22.717 -16.488 1.00 40.07 ?  29  LYS   B HB3  1 
ATOM   4453 H HG2  . LYS   B 1 29  ? 51.961 -22.408 -18.707 1.00 47.53 ?  29  LYS   B HG2  1 
ATOM   4454 H HG3  . LYS   B 1 29  ? 53.530 -22.164 -18.820 1.00 47.53 ?  29  LYS   B HG3  1 
ATOM   4455 H HD2  . LYS   B 1 29  ? 53.112 -24.260 -19.644 1.00 53.45 ?  29  LYS   B HD2  1 
ATOM   4456 H HD3  . LYS   B 1 29  ? 53.849 -24.452 -18.247 1.00 53.45 ?  29  LYS   B HD3  1 
ATOM   4457 H HE2  . LYS   B 1 29  ? 51.790 -24.879 -17.228 1.00 57.79 ?  29  LYS   B HE2  1 
ATOM   4458 H HE3  . LYS   B 1 29  ? 51.065 -24.704 -18.634 1.00 57.79 ?  29  LYS   B HE3  1 
ATOM   4459 H HZ1  . LYS   B 1 29  ? 51.401 -26.908 -18.177 1.00 60.21 ?  29  LYS   B HZ1  1 
ATOM   4460 H HZ2  . LYS   B 1 29  ? 52.172 -26.561 -19.353 1.00 60.21 ?  29  LYS   B HZ2  1 
ATOM   4461 H HZ3  . LYS   B 1 29  ? 52.833 -26.718 -18.074 1.00 60.21 ?  29  LYS   B HZ3  1 
ATOM   4462 N N    . VAL   B 1 30  ? 50.770 -20.198 -16.142 1.00 23.17 ?  30  VAL   B N    1 
ATOM   4463 C CA   . VAL   B 1 30  ? 49.484 -19.579 -16.487 1.00 22.82 ?  30  VAL   B CA   1 
ATOM   4464 C C    . VAL   B 1 30  ? 49.507 -18.071 -16.291 1.00 22.46 ?  30  VAL   B C    1 
ATOM   4465 O O    . VAL   B 1 30  ? 48.794 -17.331 -16.991 1.00 23.25 ?  30  VAL   B O    1 
ATOM   4466 C CB   . VAL   B 1 30  ? 48.385 -20.194 -15.598 1.00 23.22 ?  30  VAL   B CB   1 
ATOM   4467 C CG1  . VAL   B 1 30  ? 47.097 -19.401 -15.702 1.00 24.19 ?  30  VAL   B CG1  1 
ATOM   4468 C CG2  . VAL   B 1 30  ? 48.153 -21.652 -15.958 1.00 24.82 ?  30  VAL   B CG2  1 
ATOM   4469 H H    . VAL   B 1 30  ? 50.753 -20.633 -15.395 1.00 27.82 ?  30  VAL   B H    1 
ATOM   4470 H HA   . VAL   B 1 30  ? 49.268 -19.784 -17.413 1.00 27.40 ?  30  VAL   B HA   1 
ATOM   4471 H HB   . VAL   B 1 30  ? 48.677 -20.166 -14.672 1.00 27.88 ?  30  VAL   B HB   1 
ATOM   4472 H HG11 . VAL   B 1 30  ? 46.359 -19.982 -15.449 1.00 29.04 ?  30  VAL   B HG11 1 
ATOM   4473 H HG12 . VAL   B 1 30  ? 47.138 -18.645 -15.103 1.00 29.04 ?  30  VAL   B HG12 1 
ATOM   4474 H HG13 . VAL   B 1 30  ? 46.978 -19.111 -16.616 1.00 29.04 ?  30  VAL   B HG13 1 
ATOM   4475 H HG21 . VAL   B 1 30  ? 47.464 -22.016 -15.375 1.00 29.79 ?  30  VAL   B HG21 1 
ATOM   4476 H HG22 . VAL   B 1 30  ? 47.858 -21.704 -16.882 1.00 29.79 ?  30  VAL   B HG22 1 
ATOM   4477 H HG23 . VAL   B 1 30  ? 48.976 -22.144 -15.843 1.00 29.79 ?  30  VAL   B HG23 1 
ATOM   4478 N N    A LYS   B 1 31  ? 50.311 -17.594 -15.349 0.46 21.94 ?  31  LYS   B N    1 
ATOM   4479 N N    B LYS   B 1 31  ? 50.281 -17.594 -15.328 0.54 21.88 ?  31  LYS   B N    1 
ATOM   4480 C CA   A LYS   B 1 31  ? 50.328 -16.193 -14.953 0.46 22.74 ?  31  LYS   B CA   1 
ATOM   4481 C CA   B LYS   B 1 31  ? 50.322 -16.187 -14.958 0.54 22.74 ?  31  LYS   B CA   1 
ATOM   4482 C C    A LYS   B 1 31  ? 48.922 -15.700 -14.595 0.46 20.53 ?  31  LYS   B C    1 
ATOM   4483 C C    B LYS   B 1 31  ? 48.922 -15.701 -14.598 0.54 20.64 ?  31  LYS   B C    1 
ATOM   4484 O O    A LYS   B 1 31  ? 48.401 -14.777 -15.225 0.46 20.97 ?  31  LYS   B O    1 
ATOM   4485 O O    B LYS   B 1 31  ? 48.400 -14.773 -15.229 0.54 21.17 ?  31  LYS   B O    1 
ATOM   4486 C CB   A LYS   B 1 31  ? 50.965 -15.321 -16.026 0.46 25.64 ?  31  LYS   B CB   1 
ATOM   4487 C CB   B LYS   B 1 31  ? 50.967 -15.369 -16.079 0.54 25.71 ?  31  LYS   B CB   1 
ATOM   4488 C CG   A LYS   B 1 31  ? 52.390 -15.754 -16.373 0.46 28.61 ?  31  LYS   B CG   1 
ATOM   4489 C CG   B LYS   B 1 31  ? 52.344 -15.911 -16.474 0.54 28.80 ?  31  LYS   B CG   1 
ATOM   4490 C CD   A LYS   B 1 31  ? 52.950 -14.953 -17.533 0.46 30.93 ?  31  LYS   B CD   1 
ATOM   4491 C CD   B LYS   B 1 31  ? 52.920 -15.209 -17.687 0.54 31.08 ?  31  LYS   B CD   1 
ATOM   4492 C CE   A LYS   B 1 31  ? 54.398 -15.308 -17.794 0.46 32.62 ?  31  LYS   B CE   1 
ATOM   4493 C CE   B LYS   B 1 31  ? 54.401 -15.498 -17.817 0.54 32.78 ?  31  LYS   B CE   1 
ATOM   4494 N NZ   A LYS   B 1 31  ? 55.258 -14.949 -16.633 0.46 33.44 ?  31  LYS   B NZ   1 
ATOM   4495 N NZ   B LYS   B 1 31  ? 55.149 -15.065 -16.601 0.54 33.49 ?  31  LYS   B NZ   1 
ATOM   4496 H H    A LYS   B 1 31  ? 50.872 -18.084 -14.918 0.46 26.34 ?  31  LYS   B H    1 
ATOM   4497 H H    B LYS   B 1 31  ? 50.807 -18.089 -14.863 0.54 26.26 ?  31  LYS   B H    1 
ATOM   4498 H HA   A LYS   B 1 31  ? 50.866 -16.122 -14.160 0.46 27.30 ?  31  LYS   B HA   1 
ATOM   4499 H HA   B LYS   B 1 31  ? 50.876 -16.104 -14.176 0.54 27.30 ?  31  LYS   B HA   1 
ATOM   4500 H HB2  A LYS   B 1 31  ? 50.431 -15.367 -16.832 0.46 30.79 ?  31  LYS   B HB2  1 
ATOM   4501 H HB2  B LYS   B 1 31  ? 50.399 -15.387 -16.863 0.54 30.86 ?  31  LYS   B HB2  1 
ATOM   4502 H HB3  A LYS   B 1 31  ? 50.999 -14.410 -15.699 0.46 30.79 ?  31  LYS   B HB3  1 
ATOM   4503 H HB3  B LYS   B 1 31  ? 51.082 -14.455 -15.771 0.54 30.86 ?  31  LYS   B HB3  1 
ATOM   4504 H HG2  A LYS   B 1 31  ? 52.960 -15.617 -15.600 0.46 34.35 ?  31  LYS   B HG2  1 
ATOM   4505 H HG2  B LYS   B 1 31  ? 52.952 -15.788 -15.730 0.54 34.57 ?  31  LYS   B HG2  1 
ATOM   4506 H HG3  A LYS   B 1 31  ? 52.388 -16.692 -16.624 0.46 34.35 ?  31  LYS   B HG3  1 
ATOM   4507 H HG3  B LYS   B 1 31  ? 52.268 -16.854 -16.688 0.54 34.57 ?  31  LYS   B HG3  1 
ATOM   4508 H HD2  A LYS   B 1 31  ? 52.437 -15.149 -18.332 0.46 37.13 ?  31  LYS   B HD2  1 
ATOM   4509 H HD2  B LYS   B 1 31  ? 52.471 -15.531 -18.487 0.54 37.31 ?  31  LYS   B HD2  1 
ATOM   4510 H HD3  A LYS   B 1 31  ? 52.898 -14.008 -17.321 0.46 37.13 ?  31  LYS   B HD3  1 
ATOM   4511 H HD3  B LYS   B 1 31  ? 52.797 -14.252 -17.593 0.54 37.31 ?  31  LYS   B HD3  1 
ATOM   4512 H HE2  A LYS   B 1 31  ? 54.474 -16.264 -17.945 0.46 39.16 ?  31  LYS   B HE2  1 
ATOM   4513 H HE2  B LYS   B 1 31  ? 54.535 -16.452 -17.930 0.54 39.35 ?  31  LYS   B HE2  1 
ATOM   4514 H HE3  A LYS   B 1 31  ? 54.714 -14.819 -18.570 0.46 39.16 ?  31  LYS   B HE3  1 
ATOM   4515 H HE3  B LYS   B 1 31  ? 54.757 -15.016 -18.579 0.54 39.35 ?  31  LYS   B HE3  1 
ATOM   4516 H HZ1  A LYS   B 1 31  ? 56.113 -15.096 -16.829 0.46 40.14 ?  31  LYS   B HZ1  1 
ATOM   4517 H HZ1  B LYS   B 1 31  ? 56.023 -15.049 -16.770 0.54 40.20 ?  31  LYS   B HZ1  1 
ATOM   4518 H HZ2  A LYS   B 1 31  ? 55.151 -14.089 -16.431 0.46 40.14 ?  31  LYS   B HZ2  1 
ATOM   4519 H HZ2  B LYS   B 1 31  ? 54.887 -14.249 -16.358 0.54 40.20 ?  31  LYS   B HZ2  1 
ATOM   4520 H HZ3  A LYS   B 1 31  ? 55.036 -15.441 -15.925 0.46 40.14 ?  31  LYS   B HZ3  1 
ATOM   4521 H HZ3  B LYS   B 1 31  ? 54.995 -15.628 -15.929 0.54 40.20 ?  31  LYS   B HZ3  1 
ATOM   4522 N N    . PRO   B 1 32  ? 48.289 -16.303 -13.589 1.00 17.61 ?  32  PRO   B N    1 
ATOM   4523 C CA   . PRO   B 1 32  ? 46.904 -15.945 -13.266 1.00 16.19 ?  32  PRO   B CA   1 
ATOM   4524 C C    . PRO   B 1 32  ? 46.818 -14.597 -12.570 1.00 16.27 ?  32  PRO   B C    1 
ATOM   4525 O O    . PRO   B 1 32  ? 47.744 -14.169 -11.877 1.00 17.72 ?  32  PRO   B O    1 
ATOM   4526 C CB   . PRO   B 1 32  ? 46.483 -17.058 -12.301 1.00 16.21 ?  32  PRO   B CB   1 
ATOM   4527 C CG   . PRO   B 1 32  ? 47.773 -17.417 -11.595 1.00 17.71 ?  32  PRO   B CG   1 
ATOM   4528 C CD   . PRO   B 1 32  ? 48.855 -17.264 -12.621 1.00 17.55 ?  32  PRO   B CD   1 
ATOM   4529 H HA   . PRO   B 1 32  ? 46.344 -15.951 -14.057 1.00 19.44 ?  32  PRO   B HA   1 
ATOM   4530 H HB2  . PRO   B 1 32  ? 45.825 -16.724 -11.671 1.00 19.47 ?  32  PRO   B HB2  1 
ATOM   4531 H HB3  . PRO   B 1 32  ? 46.137 -17.815 -12.799 1.00 19.47 ?  32  PRO   B HB3  1 
ATOM   4532 H HG2  . PRO   B 1 32  ? 47.925 -16.809 -10.851 1.00 21.26 ?  32  PRO   B HG2  1 
ATOM   4533 H HG3  . PRO   B 1 32  ? 47.738 -18.334 -11.280 1.00 21.26 ?  32  PRO   B HG3  1 
ATOM   4534 H HD2  . PRO   B 1 32  ? 49.659 -16.898 -12.211 1.00 21.08 ?  32  PRO   B HD2  1 
ATOM   4535 H HD3  . PRO   B 1 32  ? 49.033 -18.111 -13.052 1.00 21.08 ?  32  PRO   B HD3  1 
ATOM   4536 N N    . THR   B 1 33  ? 45.672 -13.935 -12.741 1.00 16.56 ?  33  THR   B N    1 
ATOM   4537 C CA   . THR   B 1 33  ? 45.379 -12.757 -11.937 1.00 15.96 ?  33  THR   B CA   1 
ATOM   4538 C C    . THR   B 1 33  ? 45.339 -13.098 -10.455 1.00 16.15 ?  33  THR   B C    1 
ATOM   4539 O O    . THR   B 1 33  ? 45.820 -12.325 -9.617  1.00 16.94 ?  33  THR   B O    1 
ATOM   4540 C CB   . THR   B 1 33  ? 44.060 -12.135 -12.391 1.00 16.94 ?  33  THR   B CB   1 
ATOM   4541 O OG1  . THR   B 1 33  ? 44.132 -11.856 -13.791 1.00 16.81 ?  33  THR   B OG1  1 
ATOM   4542 C CG2  . THR   B 1 33  ? 43.773 -10.841 -11.624 1.00 18.24 ?  33  THR   B CG2  1 
ATOM   4543 H H    . THR   B 1 33  ? 45.052 -14.151 -13.296 1.00 19.89 ?  33  THR   B H    1 
ATOM   4544 H HA   . THR   B 1 33  ? 46.074 -12.102 -12.065 1.00 19.17 ?  33  THR   B HA   1 
ATOM   4545 H HB   . THR   B 1 33  ? 43.327 -12.751 -12.216 1.00 20.34 ?  33  THR   B HB   1 
ATOM   4546 H HG1  . THR   B 1 33  ? 43.410 -11.499 -14.050 1.00 20.18 ?  33  THR   B HG1  1 
ATOM   4547 H HG21 . THR   B 1 33  ? 43.021 -10.377 -12.023 1.00 21.91 ?  33  THR   B HG21 1 
ATOM   4548 H HG22 . THR   B 1 33  ? 43.562 -11.040 -10.696 1.00 21.91 ?  33  THR   B HG22 1 
ATOM   4549 H HG23 . THR   B 1 33  ? 44.551 -10.263 -11.652 1.00 21.91 ?  33  THR   B HG23 1 
ATOM   4550 N N    . VAL   B 1 34  ? 44.791 -14.266 -10.111 1.00 15.38 ?  34  VAL   B N    1 
ATOM   4551 C CA   . VAL   B 1 34  ? 44.595 -14.672 -8.721  1.00 14.81 ?  34  VAL   B CA   1 
ATOM   4552 C C    . VAL   B 1 34  ? 45.020 -16.124 -8.554  1.00 14.08 ?  34  VAL   B C    1 
ATOM   4553 O O    . VAL   B 1 34  ? 44.500 -17.009 -9.244  1.00 14.28 ?  34  VAL   B O    1 
ATOM   4554 C CB   . VAL   B 1 34  ? 43.125 -14.533 -8.272  1.00 15.89 ?  34  VAL   B CB   1 
ATOM   4555 C CG1  . VAL   B 1 34  ? 42.977 -14.998 -6.835  1.00 15.95 ?  34  VAL   B CG1  1 
ATOM   4556 C CG2  . VAL   B 1 34  ? 42.632 -13.090 -8.432  1.00 17.55 ?  34  VAL   B CG2  1 
ATOM   4557 H H    . VAL   B 1 34  ? 44.518 -14.861 -10.674 1.00 18.47 ?  34  VAL   B H    1 
ATOM   4558 H HA   . VAL   B 1 34  ? 45.138 -14.127 -8.138  1.00 17.78 ?  34  VAL   B HA   1 
ATOM   4559 H HB   . VAL   B 1 34  ? 42.564 -15.101 -8.823  1.00 19.08 ?  34  VAL   B HB   1 
ATOM   4560 H HG11 . VAL   B 1 34  ? 42.133 -14.665 -6.474  1.00 19.15 ?  34  VAL   B HG11 1 
ATOM   4561 H HG12 . VAL   B 1 34  ? 42.975 -15.970 -6.804  1.00 19.15 ?  34  VAL   B HG12 1 
ATOM   4562 H HG13 . VAL   B 1 34  ? 43.712 -14.652 -6.305  1.00 19.15 ?  34  VAL   B HG13 1 
ATOM   4563 H HG21 . VAL   B 1 34  ? 41.715 -13.027 -8.119  1.00 21.08 ?  34  VAL   B HG21 1 
ATOM   4564 H HG22 . VAL   B 1 34  ? 43.199 -12.501 -7.907  1.00 21.08 ?  34  VAL   B HG22 1 
ATOM   4565 H HG23 . VAL   B 1 34  ? 42.678 -12.842 -9.368  1.00 21.08 ?  34  VAL   B HG23 1 
ATOM   4566 N N    . VAL   B 1 35  ? 45.928 -16.376 -7.616  1.00 13.57 ?  35  VAL   B N    1 
ATOM   4567 C CA   . VAL   B 1 35  ? 46.168 -17.726 -7.106  1.00 13.41 ?  35  VAL   B CA   1 
ATOM   4568 C C    . VAL   B 1 35  ? 45.639 -17.786 -5.683  1.00 12.73 ?  35  VAL   B C    1 
ATOM   4569 O O    . VAL   B 1 35  ? 45.854 -16.853 -4.900  1.00 12.95 ?  35  VAL   B O    1 
ATOM   4570 C CB   . VAL   B 1 35  ? 47.650 -18.151 -7.193  1.00 13.53 ?  35  VAL   B CB   1 
ATOM   4571 C CG1  . VAL   B 1 35  ? 48.579 -17.326 -6.291  1.00 15.14 ?  35  VAL   B CG1  1 
ATOM   4572 C CG2  . VAL   B 1 35  ? 47.761 -19.652 -6.876  1.00 13.98 ?  35  VAL   B CG2  1 
ATOM   4573 H H    . VAL   B 1 35  ? 46.420 -15.772 -7.244  1.00 16.30 ?  35  VAL   B H    1 
ATOM   4574 H HA   . VAL   B 1 35  ? 45.650 -18.351 -7.631  1.00 16.11 ?  35  VAL   B HA   1 
ATOM   4575 H HB   . VAL   B 1 35  ? 47.947 -18.036 -8.112  1.00 16.25 ?  35  VAL   B HB   1 
ATOM   4576 H HG11 . VAL   B 1 35  ? 49.498 -17.592 -6.465  1.00 18.19 ?  35  VAL   B HG11 1 
ATOM   4577 H HG12 . VAL   B 1 35  ? 48.458 -16.392 -6.492  1.00 18.19 ?  35  VAL   B HG12 1 
ATOM   4578 H HG13 . VAL   B 1 35  ? 48.355 -17.506 -5.364  1.00 18.19 ?  35  VAL   B HG13 1 
ATOM   4579 H HG21 . VAL   B 1 35  ? 48.673 -19.944 -7.003  1.00 16.79 ?  35  VAL   B HG21 1 
ATOM   4580 H HG22 . VAL   B 1 35  ? 47.487 -19.806 -5.955  1.00 16.79 ?  35  VAL   B HG22 1 
ATOM   4581 H HG23 . VAL   B 1 35  ? 47.170 -20.152 -7.474  1.00 16.79 ?  35  VAL   B HG23 1 
ATOM   4582 N N    . VAL   B 1 36  ? 44.910 -18.862 -5.362  1.00 13.03 ?  36  VAL   B N    1 
ATOM   4583 C CA   . VAL   B 1 36  ? 44.367 -19.046 -4.027  1.00 12.32 ?  36  VAL   B CA   1 
ATOM   4584 C C    . VAL   B 1 36  ? 45.369 -19.799 -3.169  1.00 12.70 ?  36  VAL   B C    1 
ATOM   4585 O O    . VAL   B 1 36  ? 45.913 -20.833 -3.585  1.00 13.22 ?  36  VAL   B O    1 
ATOM   4586 C CB   . VAL   B 1 36  ? 43.032 -19.805 -4.092  1.00 12.90 ?  36  VAL   B CB   1 
ATOM   4587 C CG1  . VAL   B 1 36  ? 42.531 -20.140 -2.695  1.00 14.37 ?  36  VAL   B CG1  1 
ATOM   4588 C CG2  . VAL   B 1 36  ? 42.014 -18.984 -4.858  1.00 13.59 ?  36  VAL   B CG2  1 
ATOM   4589 H H    . VAL   B 1 36  ? 44.735 -19.511 -5.897  1.00 15.66 ?  36  VAL   B H    1 
ATOM   4590 H HA   . VAL   B 1 36  ? 44.202 -18.182 -3.617  1.00 14.80 ?  36  VAL   B HA   1 
ATOM   4591 H HB   . VAL   B 1 36  ? 43.168 -20.646 -4.565  1.00 15.50 ?  36  VAL   B HB   1 
ATOM   4592 H HG11 . VAL   B 1 36  ? 41.591 -20.378 -2.745  1.00 17.25 ?  36  VAL   B HG11 1 
ATOM   4593 H HG12 . VAL   B 1 36  ? 43.038 -20.887 -2.337  1.00 17.25 ?  36  VAL   B HG12 1 
ATOM   4594 H HG13 . VAL   B 1 36  ? 42.642 -19.362 -2.125  1.00 17.25 ?  36  VAL   B HG13 1 
ATOM   4595 H HG21 . VAL   B 1 36  ? 41.168 -19.459 -4.861  1.00 16.32 ?  36  VAL   B HG21 1 
ATOM   4596 H HG22 . VAL   B 1 36  ? 41.915 -18.128 -4.423  1.00 16.32 ?  36  VAL   B HG22 1 
ATOM   4597 H HG23 . VAL   B 1 36  ? 42.330 -18.866 -5.766  1.00 16.32 ?  36  VAL   B HG23 1 
ATOM   4598 N N    . ASN   B 1 37  ? 45.580 -19.309 -1.950  1.00 12.70 ?  37  ASN   B N    1 
ATOM   4599 C CA   . ASN   B 1 37  ? 46.342 -20.031 -0.947  1.00 12.52 ?  37  ASN   B CA   1 
ATOM   4600 C C    . ASN   B 1 37  ? 45.407 -20.704 0.047   1.00 13.41 ?  37  ASN   B C    1 
ATOM   4601 O O    . ASN   B 1 37  ? 44.393 -20.129 0.449   1.00 13.11 ?  37  ASN   B O    1 
ATOM   4602 C CB   . ASN   B 1 37  ? 47.284 -19.085 -0.205  1.00 13.27 ?  37  ASN   B CB   1 
ATOM   4603 C CG   . ASN   B 1 37  ? 48.128 -19.794 0.816   1.00 13.23 ?  37  ASN   B CG   1 
ATOM   4604 O OD1  . ASN   B 1 37  ? 48.481 -20.968 0.644   1.00 14.54 ?  37  ASN   B OD1  1 
ATOM   4605 N ND2  . ASN   B 1 37  ? 48.466 -19.096 1.888   1.00 12.86 ?  37  ASN   B ND2  1 
ATOM   4606 H H    . ASN   B 1 37  ? 45.287 -18.545 -1.672  1.00 15.25 ?  37  ASN   B H    1 
ATOM   4607 H HA   . ASN   B 1 37  ? 46.879 -20.717 -1.377  1.00 15.04 ?  37  ASN   B HA   1 
ATOM   4608 H HB2  . ASN   B 1 37  ? 47.890 -18.672 -0.845  1.00 15.94 ?  37  ASN   B HB2  1 
ATOM   4609 H HB3  . ASN   B 1 37  ? 46.770 -18.407 0.251   1.00 15.94 ?  37  ASN   B HB3  1 
ATOM   4610 H HD21 . ASN   B 1 37  ? 48.958 -19.447 2.504   1.00 15.45 ?  37  ASN   B HD21 1 
ATOM   4611 H HD22 . ASN   B 1 37  ? 48.215 -18.277 1.973   1.00 15.45 ?  37  ASN   B HD22 1 
ATOM   4612 N N    . ALA   B 1 38  ? 45.755 -21.938 0.417   1.00 13.46 ?  38  ALA   B N    1 
ATOM   4613 C CA   . ALA   B 1 38  ? 45.103 -22.675 1.498   1.00 13.31 ?  38  ALA   B CA   1 
ATOM   4614 C C    . ALA   B 1 38  ? 45.688 -22.173 2.818   1.00 13.35 ?  38  ALA   B C    1 
ATOM   4615 O O    . ALA   B 1 38  ? 46.581 -22.783 3.420   1.00 14.37 ?  38  ALA   B O    1 
ATOM   4616 C CB   . ALA   B 1 38  ? 45.340 -24.169 1.320   1.00 14.77 ?  38  ALA   B CB   1 
ATOM   4617 H H    . ALA   B 1 38  ? 46.406 -22.377 0.055   1.00 16.16 ?  38  ALA   B H    1 
ATOM   4618 H HA   . ALA   B 1 38  ? 44.149 -22.497 1.487   1.00 15.99 ?  38  ALA   B HA   1 
ATOM   4619 H HB1  . ALA   B 1 38  ? 44.892 -24.647 2.042   1.00 17.74 ?  38  ALA   B HB1  1 
ATOM   4620 H HB2  . ALA   B 1 38  ? 44.968 -24.447 0.467   1.00 17.74 ?  38  ALA   B HB2  1 
ATOM   4621 H HB3  . ALA   B 1 38  ? 46.289 -24.347 1.346   1.00 17.74 ?  38  ALA   B HB3  1 
ATOM   4622 N N    . ALA   B 1 39  ? 45.156 -21.037 3.274   1.00 13.55 ?  39  ALA   B N    1 
ATOM   4623 C CA   . ALA   B 1 39  ? 45.711 -20.313 4.405   1.00 13.69 ?  39  ALA   B CA   1 
ATOM   4624 C C    . ALA   B 1 39  ? 45.089 -20.742 5.734   1.00 13.35 ?  39  ALA   B C    1 
ATOM   4625 O O    . ALA   B 1 39  ? 44.048 -21.410 5.787   1.00 14.90 ?  39  ALA   B O    1 
ATOM   4626 C CB   . ALA   B 1 39  ? 45.490 -18.814 4.211   1.00 13.77 ?  39  ALA   B CB   1 
ATOM   4627 H H    . ALA   B 1 39  ? 44.452 -20.668 2.946   1.00 16.28 ?  39  ALA   B H    1 
ATOM   4628 H HA   . ALA   B 1 39  ? 46.663 -20.474 4.455   1.00 16.44 ?  39  ALA   B HA   1 
ATOM   4629 H HB1  . ALA   B 1 39  ? 45.866 -18.334 4.970   1.00 16.54 ?  39  ALA   B HB1  1 
ATOM   4630 H HB2  . ALA   B 1 39  ? 45.933 -18.533 3.395   1.00 16.54 ?  39  ALA   B HB2  1 
ATOM   4631 H HB3  . ALA   B 1 39  ? 44.539 -18.635 4.150   1.00 16.54 ?  39  ALA   B HB3  1 
ATOM   4632 N N    . ASN   B 1 40  ? 45.737 -20.326 6.823   1.00 13.71 ?  40  ASN   B N    1 
ATOM   4633 C CA   . ASN   B 1 40  ? 45.172 -20.363 8.166   1.00 14.05 ?  40  ASN   B CA   1 
ATOM   4634 C C    . ASN   B 1 40  ? 44.998 -18.933 8.683   1.00 14.63 ?  40  ASN   B C    1 
ATOM   4635 O O    . ASN   B 1 40  ? 45.416 -17.962 8.045   1.00 15.06 ?  40  ASN   B O    1 
ATOM   4636 C CB   . ASN   B 1 40  ? 46.018 -21.233 9.111   1.00 15.91 ?  40  ASN   B CB   1 
ATOM   4637 C CG   . ASN   B 1 40  ? 47.471 -20.820 9.139   1.00 16.76 ?  40  ASN   B CG   1 
ATOM   4638 O OD1  . ASN   B 1 40  ? 47.797 -19.638 9.201   1.00 19.11 ?  40  ASN   B OD1  1 
ATOM   4639 N ND2  . ASN   B 1 40  ? 48.361 -21.794 9.086   1.00 17.43 ?  40  ASN   B ND2  1 
ATOM   4640 H H    . ASN   B 1 40  ? 46.537 -20.009 6.809   1.00 16.46 ?  40  ASN   B H    1 
ATOM   4641 H HA   . ASN   B 1 40  ? 44.284 -20.763 8.114   1.00 16.88 ?  40  ASN   B HA   1 
ATOM   4642 H HB2  . ASN   B 1 40  ? 45.654 -21.159 10.011  1.00 19.11 ?  40  ASN   B HB2  1 
ATOM   4643 H HB3  . ASN   B 1 40  ? 45.968 -22.156 8.814   1.00 19.11 ?  40  ASN   B HB3  1 
ATOM   4644 H HD21 . ASN   B 1 40  ? 49.205 -21.608 9.108   1.00 20.94 ?  40  ASN   B HD21 1 
ATOM   4645 H HD22 . ASN   B 1 40  ? 48.107 -22.611 9.037   1.00 20.94 ?  40  ASN   B HD22 1 
ATOM   4646 N N    . VAL   B 1 41  ? 44.352 -18.803 9.847   1.00 15.36 ?  41  VAL   B N    1 
ATOM   4647 C CA   . VAL   B 1 41  ? 43.896 -17.481 10.293  1.00 15.85 ?  41  VAL   B CA   1 
ATOM   4648 C C    . VAL   B 1 41  ? 45.050 -16.530 10.586  1.00 16.05 ?  41  VAL   B C    1 
ATOM   4649 O O    . VAL   B 1 41  ? 44.873 -15.311 10.490  1.00 17.23 ?  41  VAL   B O    1 
ATOM   4650 C CB   . VAL   B 1 41  ? 42.914 -17.550 11.481  1.00 17.25 ?  41  VAL   B CB   1 
ATOM   4651 C CG1  . VAL   B 1 41  ? 41.613 -18.230 11.071  1.00 17.91 ?  41  VAL   B CG1  1 
ATOM   4652 C CG2  . VAL   B 1 41  ? 43.548 -18.242 12.679  1.00 18.70 ?  41  VAL   B CG2  1 
ATOM   4653 H H    . VAL   B 1 41  ? 44.168 -19.448 10.383  1.00 18.44 ?  41  VAL   B H    1 
ATOM   4654 H HA   . VAL   B 1 41  ? 43.404 -17.082 9.561   1.00 19.04 ?  41  VAL   B HA   1 
ATOM   4655 H HB   . VAL   B 1 41  ? 42.691 -16.646 11.751  1.00 20.72 ?  41  VAL   B HB   1 
ATOM   4656 H HG11 . VAL   B 1 41  ? 41.004 -18.231 11.827  1.00 21.50 ?  41  VAL   B HG11 1 
ATOM   4657 H HG12 . VAL   B 1 41  ? 41.219 -17.742 10.331  1.00 21.50 ?  41  VAL   B HG12 1 
ATOM   4658 H HG13 . VAL   B 1 41  ? 41.805 -19.142 10.801  1.00 21.50 ?  41  VAL   B HG13 1 
ATOM   4659 H HG21 . VAL   B 1 41  ? 42.906 -18.265 13.408  1.00 22.46 ?  41  VAL   B HG21 1 
ATOM   4660 H HG22 . VAL   B 1 41  ? 43.791 -19.150 12.430  1.00 22.46 ?  41  VAL   B HG22 1 
ATOM   4661 H HG23 . VAL   B 1 41  ? 44.337 -17.751 12.949  1.00 22.46 ?  41  VAL   B HG23 1 
ATOM   4662 N N    . TYR   B 1 42  ? 46.215 -17.044 10.984  1.00 16.71 ?  42  TYR   B N    1 
ATOM   4663 C CA   . TYR   B 1 42  ? 47.373 -16.193 11.249  1.00 16.44 ?  42  TYR   B CA   1 
ATOM   4664 C C    . TYR   B 1 42  ? 48.328 -16.113 10.059  1.00 15.87 ?  42  TYR   B C    1 
ATOM   4665 O O    . TYR   B 1 42  ? 49.417 -15.539 10.183  1.00 17.40 ?  42  TYR   B O    1 
ATOM   4666 C CB   . TYR   B 1 42  ? 48.073 -16.596 12.556  1.00 19.16 ?  42  TYR   B CB   1 
ATOM   4667 C CG   . TYR   B 1 42  ? 47.448 -15.936 13.781  1.00 19.59 ?  42  TYR   B CG   1 
ATOM   4668 C CD1  . TYR   B 1 42  ? 47.648 -14.580 14.039  1.00 18.67 ?  42  TYR   B CD1  1 
ATOM   4669 C CD2  . TYR   B 1 42  ? 46.647 -16.648 14.661  1.00 21.64 ?  42  TYR   B CD2  1 
ATOM   4670 C CE1  . TYR   B 1 42  ? 47.076 -13.969 15.138  1.00 19.37 ?  42  TYR   B CE1  1 
ATOM   4671 C CE2  . TYR   B 1 42  ? 46.077 -16.043 15.764  1.00 21.62 ?  42  TYR   B CE2  1 
ATOM   4672 C CZ   . TYR   B 1 42  ? 46.291 -14.702 15.999  1.00 21.02 ?  42  TYR   B CZ   1 
ATOM   4673 O OH   . TYR   B 1 42  ? 45.719 -14.095 17.097  1.00 24.71 ?  42  TYR   B OH   1 
ATOM   4674 H H    . TYR   B 1 42  ? 46.362 -17.891 11.101  1.00 20.07 ?  42  TYR   B H    1 
ATOM   4675 H HA   . TYR   B 1 42  ? 47.040 -15.299 11.387  1.00 19.74 ?  42  TYR   B HA   1 
ATOM   4676 H HB2  . TYR   B 1 42  ? 48.015 -17.556 12.669  1.00 23.01 ?  42  TYR   B HB2  1 
ATOM   4677 H HB3  . TYR   B 1 42  ? 49.005 -16.323 12.508  1.00 23.01 ?  42  TYR   B HB3  1 
ATOM   4678 H HD1  . TYR   B 1 42  ? 48.179 -14.075 13.459  1.00 22.42 ?  42  TYR   B HD1  1 
ATOM   4679 H HD2  . TYR   B 1 42  ? 46.495 -17.554 14.501  1.00 25.98 ?  42  TYR   B HD2  1 
ATOM   4680 H HE1  . TYR   B 1 42  ? 47.221 -13.061 15.295  1.00 23.25 ?  42  TYR   B HE1  1 
ATOM   4681 H HE2  . TYR   B 1 42  ? 45.538 -16.540 16.338  1.00 25.96 ?  42  TYR   B HE2  1 
ATOM   4682 H HH   . TYR   B 1 42  ? 45.931 -13.281 17.109  1.00 29.67 ?  42  TYR   B HH   1 
ATOM   4683 N N    . LEU   B 1 43  ? 47.931 -16.647 8.906   1.00 15.08 ?  43  LEU   B N    1 
ATOM   4684 C CA   . LEU   B 1 43  ? 48.729 -16.575 7.689   1.00 14.84 ?  43  LEU   B CA   1 
ATOM   4685 C C    . LEU   B 1 43  ? 50.146 -17.086 7.932   1.00 15.14 ?  43  LEU   B C    1 
ATOM   4686 O O    . LEU   B 1 43  ? 51.123 -16.506 7.460   1.00 15.74 ?  43  LEU   B O    1 
ATOM   4687 C CB   . LEU   B 1 43  ? 48.748 -15.167 7.093   1.00 15.66 ?  43  LEU   B CB   1 
ATOM   4688 C CG   . LEU   B 1 43  ? 47.407 -14.561 6.670   1.00 15.08 ?  43  LEU   B CG   1 
ATOM   4689 C CD1  . LEU   B 1 43  ? 47.690 -13.164 6.082   1.00 16.04 ?  43  LEU   B CD1  1 
ATOM   4690 C CD2  . LEU   B 1 43  ? 46.641 -15.443 5.691   1.00 15.90 ?  43  LEU   B CD2  1 
ATOM   4691 H H    . LEU   B 1 43  ? 47.195 -17.077 8.806   1.00 18.11 ?  43  LEU   B H    1 
ATOM   4692 H HA   . LEU   B 1 43  ? 48.317 -17.157 7.030   1.00 17.82 ?  43  LEU   B HA   1 
ATOM   4693 H HB2  . LEU   B 1 43  ? 49.141 -14.566 7.747   1.00 18.80 ?  43  LEU   B HB2  1 
ATOM   4694 H HB3  . LEU   B 1 43  ? 49.312 -15.185 6.303   1.00 18.80 ?  43  LEU   B HB3  1 
ATOM   4695 H HG   . LEU   B 1 43  ? 46.863 -14.435 7.457   1.00 18.11 ?  43  LEU   B HG   1 
ATOM   4696 H HD11 . LEU   B 1 43  ? 46.849 -12.758 5.809   1.00 19.26 ?  43  LEU   B HD11 1 
ATOM   4697 H HD12 . LEU   B 1 43  ? 48.113 -12.608 6.761   1.00 19.26 ?  43  LEU   B HD12 1 
ATOM   4698 H HD13 . LEU   B 1 43  ? 48.278 -13.247 5.316   1.00 19.26 ?  43  LEU   B HD13 1 
ATOM   4699 H HD21 . LEU   B 1 43  ? 45.844 -14.970 5.396   1.00 19.10 ?  43  LEU   B HD21 1 
ATOM   4700 H HD22 . LEU   B 1 43  ? 47.205 -15.640 4.926   1.00 19.10 ?  43  LEU   B HD22 1 
ATOM   4701 H HD23 . LEU   B 1 43  ? 46.389 -16.264 6.137   1.00 19.10 ?  43  LEU   B HD23 1 
ATOM   4702 N N    . LYS   B 1 44  ? 50.251 -18.207 8.653   1.00 15.36 ?  44  LYS   B N    1 
ATOM   4703 C CA   . LYS   B 1 44  ? 51.518 -18.883 8.901   1.00 15.56 ?  44  LYS   B CA   1 
ATOM   4704 C C    . LYS   B 1 44  ? 51.640 -20.003 7.878   1.00 15.08 ?  44  LYS   B C    1 
ATOM   4705 O O    . LYS   B 1 44  ? 50.936 -21.015 7.965   1.00 16.38 ?  44  LYS   B O    1 
ATOM   4706 C CB   . LYS   B 1 44  ? 51.582 -19.404 10.337  1.00 17.58 ?  44  LYS   B CB   1 
ATOM   4707 C CG   . LYS   B 1 44  ? 51.760 -18.288 11.367  1.00 20.95 ?  44  LYS   B CG   1 
ATOM   4708 C CD   . LYS   B 1 44  ? 52.968 -17.412 10.993  1.00 24.57 ?  44  LYS   B CD   1 
ATOM   4709 C CE   . LYS   B 1 44  ? 53.436 -16.512 12.112  1.00 27.97 ?  44  LYS   B CE   1 
ATOM   4710 N NZ   . LYS   B 1 44  ? 54.635 -15.715 11.727  1.00 29.27 ?  44  LYS   B NZ   1 
ATOM   4711 H H    . LYS   B 1 44  ? 49.578 -18.611 9.012   1.00 18.44 ?  44  LYS   B H    1 
ATOM   4712 H HA   . LYS   B 1 44  ? 52.248 -18.269 8.742   1.00 18.69 ?  44  LYS   B HA   1 
ATOM   4713 H HB2  . LYS   B 1 44  ? 50.753 -19.868 10.542  1.00 21.11 ?  44  LYS   B HB2  1 
ATOM   4714 H HB3  . LYS   B 1 44  ? 52.330 -20.013 10.422  1.00 21.11 ?  44  LYS   B HB3  1 
ATOM   4715 H HG2  . LYS   B 1 44  ? 50.969 -17.731 11.388  1.00 25.15 ?  44  LYS   B HG2  1 
ATOM   4716 H HG3  . LYS   B 1 44  ? 51.925 -18.678 12.244  1.00 25.15 ?  44  LYS   B HG3  1 
ATOM   4717 H HD2  . LYS   B 1 44  ? 53.705 -17.994 10.731  1.00 29.50 ?  44  LYS   B HD2  1 
ATOM   4718 H HD3  . LYS   B 1 44  ? 52.719 -16.845 10.245  1.00 29.50 ?  44  LYS   B HD3  1 
ATOM   4719 H HE2  . LYS   B 1 44  ? 52.727 -15.891 12.320  1.00 33.58 ?  44  LYS   B HE2  1 
ATOM   4720 H HE3  . LYS   B 1 44  ? 53.659 -17.053 12.886  1.00 33.58 ?  44  LYS   B HE3  1 
ATOM   4721 H HZ1  . LYS   B 1 44  ? 54.882 -15.193 12.404  1.00 35.14 ?  44  LYS   B HZ1  1 
ATOM   4722 H HZ2  . LYS   B 1 44  ? 55.310 -16.256 11.517  1.00 35.14 ?  44  LYS   B HZ2  1 
ATOM   4723 H HZ3  . LYS   B 1 44  ? 54.447 -15.203 11.022  1.00 35.14 ?  44  LYS   B HZ3  1 
ATOM   4724 N N    . HIS   B 1 45  ? 52.494 -19.789 6.880   1.00 14.88 ?  45  HIS   B N    1 
ATOM   4725 C CA   . HIS   B 1 45  ? 52.535 -20.617 5.673   1.00 14.51 ?  45  HIS   B CA   1 
ATOM   4726 C C    . HIS   B 1 45  ? 53.552 -21.745 5.836   1.00 17.01 ?  45  HIS   B C    1 
ATOM   4727 O O    . HIS   B 1 45  ? 54.612 -21.768 5.218   1.00 19.55 ?  45  HIS   B O    1 
ATOM   4728 C CB   . HIS   B 1 45  ? 52.853 -19.761 4.461   1.00 15.04 ?  45  HIS   B CB   1 
ATOM   4729 C CG   . HIS   B 1 45  ? 51.969 -18.569 4.343   1.00 14.87 ?  45  HIS   B CG   1 
ATOM   4730 N ND1  . HIS   B 1 45  ? 50.590 -18.666 4.326   1.00 14.94 ?  45  HIS   B ND1  1 
ATOM   4731 C CD2  . HIS   B 1 45  ? 52.268 -17.251 4.252   1.00 15.29 ?  45  HIS   B CD2  1 
ATOM   4732 C CE1  . HIS   B 1 45  ? 50.085 -17.451 4.218   1.00 14.25 ?  45  HIS   B CE1  1 
ATOM   4733 N NE2  . HIS   B 1 45  ? 51.077 -16.574 4.173   1.00 14.55 ?  45  HIS   B NE2  1 
ATOM   4734 H H    . HIS   B 1 45  ? 53.077 -19.151 6.876   1.00 17.88 ?  45  HIS   B H    1 
ATOM   4735 H HA   . HIS   B 1 45  ? 51.656 -21.012 5.538   1.00 17.43 ?  45  HIS   B HA   1 
ATOM   4736 H HB2  . HIS   B 1 45  ? 53.765 -19.447 4.525   1.00 18.06 ?  45  HIS   B HB2  1 
ATOM   4737 H HB3  . HIS   B 1 45  ? 52.738 -20.295 3.658   1.00 18.06 ?  45  HIS   B HB3  1 
ATOM   4738 H HD2  . HIS   B 1 45  ? 53.123 -16.880 4.246   1.00 18.36 ?  45  HIS   B HD2  1 
ATOM   4739 H HE1  . HIS   B 1 45  ? 49.180 -17.238 4.178   1.00 17.11 ?  45  HIS   B HE1  1 
ATOM   4740 H HE2  . HIS   B 1 45  ? 50.993 -15.721 4.108   1.00 17.47 ?  45  HIS   B HE2  1 
ATOM   4741 N N    . GLY   B 1 46  ? 53.182 -22.719 6.662   1.00 18.08 ?  46  GLY   B N    1 
ATOM   4742 C CA   . GLY   B 1 46  ? 54.121 -23.757 7.036   1.00 20.83 ?  46  GLY   B CA   1 
ATOM   4743 C C    . GLY   B 1 46  ? 54.162 -24.961 6.115   1.00 22.28 ?  46  GLY   B C    1 
ATOM   4744 O O    . GLY   B 1 46  ? 55.231 -25.359 5.644   1.00 25.75 ?  46  GLY   B O    1 
ATOM   4745 H H    . GLY   B 1 46  ? 52.404 -22.781 7.036   1.00 21.71 ?  46  GLY   B H    1 
ATOM   4746 H HA2  . GLY   B 1 46  ? 55.013 -23.376 7.071   1.00 25.01 ?  46  GLY   B HA2  1 
ATOM   4747 H HA3  . GLY   B 1 46  ? 53.900 -24.077 7.926   1.00 25.01 ?  46  GLY   B HA3  1 
ATOM   4748 N N    . GLY   B 1 47  ? 53.009 -25.559 5.839   1.00 20.83 ?  47  GLY   B N    1 
ATOM   4749 C CA   . GLY   B 1 47  ? 52.956 -26.852 5.184   1.00 19.30 ?  47  GLY   B CA   1 
ATOM   4750 C C    . GLY   B 1 47  ? 52.027 -26.834 3.987   1.00 16.87 ?  47  GLY   B C    1 
ATOM   4751 O O    . GLY   B 1 47  ? 51.372 -25.834 3.706   1.00 15.88 ?  47  GLY   B O    1 
ATOM   4752 H H    . GLY   B 1 47  ? 52.234 -25.236 6.036   1.00 25.01 ?  47  GLY   B H    1 
ATOM   4753 H HA2  . GLY   B 1 47  ? 53.843 -27.103 4.881   1.00 23.17 ?  47  GLY   B HA2  1 
ATOM   4754 H HA3  . GLY   B 1 47  ? 52.644 -27.522 5.812   1.00 23.17 ?  47  GLY   B HA3  1 
ATOM   4755 N N    . GLY   B 1 48  ? 51.988 -27.964 3.292   1.00 15.89 ?  48  GLY   B N    1 
ATOM   4756 C CA   . GLY   B 1 48  ? 51.066 -28.128 2.187   1.00 15.97 ?  48  GLY   B CA   1 
ATOM   4757 C C    . GLY   B 1 48  ? 51.199 -27.024 1.157   1.00 14.75 ?  48  GLY   B C    1 
ATOM   4758 O O    . GLY   B 1 48  ? 52.294 -26.552 0.845   1.00 14.80 ?  48  GLY   B O    1 
ATOM   4759 H H    . GLY   B 1 48  ? 52.491 -28.642 3.443   1.00 19.09 ?  48  GLY   B H    1 
ATOM   4760 H HA2  . GLY   B 1 48  ? 51.233 -28.983 1.752   1.00 19.18 ?  48  GLY   B HA2  1 
ATOM   4761 H HA3  . GLY   B 1 48  ? 50.154 -28.130 2.519   1.00 19.18 ?  48  GLY   B HA3  1 
ATOM   4762 N N    . VAL   B 1 49  ? 50.055 -26.600 0.618   1.00 14.91 ?  49  VAL   B N    1 
ATOM   4763 C CA   . VAL   B 1 49  ? 50.026 -25.582 -0.429  1.00 14.54 ?  49  VAL   B CA   1 
ATOM   4764 C C    . VAL   B 1 49  ? 50.674 -24.288 0.051   1.00 13.48 ?  49  VAL   B C    1 
ATOM   4765 O O    . VAL   B 1 49  ? 51.467 -23.669 -0.670  1.00 14.26 ?  49  VAL   B O    1 
ATOM   4766 C CB   . VAL   B 1 49  ? 48.576 -25.349 -0.899  1.00 16.04 ?  49  VAL   B CB   1 
ATOM   4767 C CG1  . VAL   B 1 49  ? 48.469 -24.080 -1.761  1.00 16.36 ?  49  VAL   B CG1  1 
ATOM   4768 C CG2  . VAL   B 1 49  ? 48.062 -26.581 -1.660  1.00 18.20 ?  49  VAL   B CG2  1 
ATOM   4769 H H    . VAL   B 1 49  ? 49.281 -26.893 0.841   1.00 17.90 ?  49  VAL   B H    1 
ATOM   4770 H HA   . VAL   B 1 49  ? 50.537 -25.896 -1.190  1.00 17.47 ?  49  VAL   B HA   1 
ATOM   4771 H HB   . VAL   B 1 49  ? 48.013 -25.230 -0.122  1.00 19.26 ?  49  VAL   B HB   1 
ATOM   4772 H HG11 . VAL   B 1 49  ? 47.632 -24.103 -2.250  1.00 19.65 ?  49  VAL   B HG11 1 
ATOM   4773 H HG12 . VAL   B 1 49  ? 48.490 -23.302 -1.181  1.00 19.65 ?  49  VAL   B HG12 1 
ATOM   4774 H HG13 . VAL   B 1 49  ? 49.214 -24.054 -2.381  1.00 19.65 ?  49  VAL   B HG13 1 
ATOM   4775 H HG21 . VAL   B 1 49  ? 47.151 -26.416 -1.948  1.00 21.86 ?  49  VAL   B HG21 1 
ATOM   4776 H HG22 . VAL   B 1 49  ? 48.630 -26.735 -2.433  1.00 21.86 ?  49  VAL   B HG22 1 
ATOM   4777 H HG23 . VAL   B 1 49  ? 48.090 -27.351 -1.071  1.00 21.86 ?  49  VAL   B HG23 1 
ATOM   4778 N N    . ALA   B 1 50  ? 50.326 -23.841 1.260   1.00 13.78 ?  50  ALA   B N    1 
ATOM   4779 C CA   . ALA   B 1 50  ? 50.843 -22.555 1.733   1.00 13.66 ?  50  ALA   B CA   1 
ATOM   4780 C C    . ALA   B 1 50  ? 52.368 -22.576 1.838   1.00 14.04 ?  50  ALA   B C    1 
ATOM   4781 O O    . ALA   B 1 50  ? 53.046 -21.612 1.456   1.00 13.81 ?  50  ALA   B O    1 
ATOM   4782 C CB   . ALA   B 1 50  ? 50.214 -22.196 3.075   1.00 13.96 ?  50  ALA   B CB   1 
ATOM   4783 H H    . ALA   B 1 50  ? 49.796 -24.240 1.806   1.00 16.55 ?  50  ALA   B H    1 
ATOM   4784 H HA   . ALA   B 1 50  ? 50.604 -21.861 1.101   1.00 16.40 ?  50  ALA   B HA   1 
ATOM   4785 H HB1  . ALA   B 1 50  ? 50.568 -21.340 3.375   1.00 16.77 ?  50  ALA   B HB1  1 
ATOM   4786 H HB2  . ALA   B 1 50  ? 49.250 -22.126 2.966   1.00 16.77 ?  50  ALA   B HB2  1 
ATOM   4787 H HB3  . ALA   B 1 50  ? 50.424 -22.883 3.722   1.00 16.77 ?  50  ALA   B HB3  1 
ATOM   4788 N N    . GLY   B 1 51  ? 52.929 -23.660 2.363   1.00 14.54 ?  51  GLY   B N    1 
ATOM   4789 C CA   . GLY   B 1 51  ? 54.377 -23.743 2.442   1.00 14.83 ?  51  GLY   B CA   1 
ATOM   4790 C C    . GLY   B 1 51  ? 55.025 -23.720 1.072   1.00 14.62 ?  51  GLY   B C    1 
ATOM   4791 O O    . GLY   B 1 51  ? 56.073 -23.091 0.880   1.00 16.12 ?  51  GLY   B O    1 
ATOM   4792 H H    . GLY   B 1 51  ? 52.507 -24.344 2.670   1.00 17.46 ?  51  GLY   B H    1 
ATOM   4793 H HA2  . GLY   B 1 51  ? 54.721 -22.992 2.951   1.00 17.81 ?  51  GLY   B HA2  1 
ATOM   4794 H HA3  . GLY   B 1 51  ? 54.634 -24.563 2.891   1.00 17.81 ?  51  GLY   B HA3  1 
ATOM   4795 N N    . ALA   B 1 52  ? 54.415 -24.404 0.098   1.00 14.29 ?  52  ALA   B N    1 
ATOM   4796 C CA   . ALA   B 1 52  ? 54.966 -24.420 -1.254  1.00 14.48 ?  52  ALA   B CA   1 
ATOM   4797 C C    . ALA   B 1 52  ? 54.883 -23.041 -1.908  1.00 13.92 ?  52  ALA   B C    1 
ATOM   4798 O O    . ALA   B 1 52  ? 55.847 -22.588 -2.542  1.00 15.12 ?  52  ALA   B O    1 
ATOM   4799 C CB   . ALA   B 1 52  ? 54.240 -25.464 -2.100  1.00 15.48 ?  52  ALA   B CB   1 
ATOM   4800 H H    . ALA   B 1 52  ? 53.699 -24.871 0.200   1.00 17.16 ?  52  ALA   B H    1 
ATOM   4801 H HA   . ALA   B 1 52  ? 55.899 -24.678 -1.211  1.00 17.39 ?  52  ALA   B HA   1 
ATOM   4802 H HB1  . ALA   B 1 52  ? 54.611 -25.463 -2.997  1.00 18.59 ?  52  ALA   B HB1  1 
ATOM   4803 H HB2  . ALA   B 1 52  ? 54.356 -26.342 -1.698  1.00 18.59 ?  52  ALA   B HB2  1 
ATOM   4804 H HB3  . ALA   B 1 52  ? 53.294 -25.245 -2.136  1.00 18.59 ?  52  ALA   B HB3  1 
ATOM   4805 N N    . LEU   B 1 53  ? 53.750 -22.350 -1.770  1.00 14.00 ?  53  LEU   B N    1 
ATOM   4806 C CA   . LEU   B 1 53  ? 53.628 -21.022 -2.357  1.00 14.44 ?  53  LEU   B CA   1 
ATOM   4807 C C    . LEU   B 1 53  ? 54.627 -20.072 -1.720  1.00 13.88 ?  53  LEU   B C    1 
ATOM   4808 O O    . LEU   B 1 53  ? 55.335 -19.334 -2.418  1.00 14.81 ?  53  LEU   B O    1 
ATOM   4809 C CB   . LEU   B 1 53  ? 52.199 -20.483 -2.198  1.00 14.73 ?  53  LEU   B CB   1 
ATOM   4810 C CG   . LEU   B 1 53  ? 51.066 -21.204 -2.945  1.00 15.14 ?  53  LEU   B CG   1 
ATOM   4811 C CD1  . LEU   B 1 53  ? 49.733 -20.566 -2.620  1.00 16.25 ?  53  LEU   B CD1  1 
ATOM   4812 C CD2  . LEU   B 1 53  ? 51.290 -21.222 -4.456  1.00 16.88 ?  53  LEU   B CD2  1 
ATOM   4813 H H    . LEU   B 1 53  ? 53.051 -22.629 -1.349  1.00 16.82 ?  53  LEU   B H    1 
ATOM   4814 H HA   . LEU   B 1 53  ? 53.829 -21.075 -3.303  1.00 17.34 ?  53  LEU   B HA   1 
ATOM   4815 H HB2  . LEU   B 1 53  ? 51.971 -20.508 -1.256  1.00 17.70 ?  53  LEU   B HB2  1 
ATOM   4816 H HB3  . LEU   B 1 53  ? 52.191 -19.562 -2.501  1.00 17.70 ?  53  LEU   B HB3  1 
ATOM   4817 H HG   . LEU   B 1 53  ? 51.026 -22.120 -2.639  1.00 18.18 ?  53  LEU   B HG   1 
ATOM   4818 H HD11 . LEU   B 1 53  ? 49.032 -21.033 -3.100  1.00 19.52 ?  53  LEU   B HD11 1 
ATOM   4819 H HD12 . LEU   B 1 53  ? 49.575 -20.626 -1.664  1.00 19.52 ?  53  LEU   B HD12 1 
ATOM   4820 H HD13 . LEU   B 1 53  ? 49.752 -19.632 -2.891  1.00 19.52 ?  53  LEU   B HD13 1 
ATOM   4821 H HD21 . LEU   B 1 53  ? 50.601 -21.760 -4.868  1.00 20.27 ?  53  LEU   B HD21 1 
ATOM   4822 H HD22 . LEU   B 1 53  ? 51.245 -20.313 -4.791  1.00 20.27 ?  53  LEU   B HD22 1 
ATOM   4823 H HD23 . LEU   B 1 53  ? 52.163 -21.602 -4.640  1.00 20.27 ?  53  LEU   B HD23 1 
ATOM   4824 N N    . ASN   B 1 54  ? 54.715 -20.090 -0.392  1.00 14.13 ?  54  ASN   B N    1 
ATOM   4825 C CA   . ASN   B 1 54  ? 55.636 -19.180 0.273   1.00 14.33 ?  54  ASN   B CA   1 
ATOM   4826 C C    . ASN   B 1 54  ? 57.075 -19.460 -0.136  1.00 14.45 ?  54  ASN   B C    1 
ATOM   4827 O O    . ASN   B 1 54  ? 57.854 -18.521 -0.377  1.00 15.52 ?  54  ASN   B O    1 
ATOM   4828 C CB   . ASN   B 1 54  ? 55.482 -19.258 1.784   1.00 15.15 ?  54  ASN   B CB   1 
ATOM   4829 C CG   . ASN   B 1 54  ? 56.467 -18.368 2.490   1.00 15.82 ?  54  ASN   B CG   1 
ATOM   4830 O OD1  . ASN   B 1 54  ? 56.498 -17.156 2.249   1.00 16.06 ?  54  ASN   B OD1  1 
ATOM   4831 N ND2  . ASN   B 1 54  ? 57.287 -18.957 3.354   1.00 17.88 ?  54  ASN   B ND2  1 
ATOM   4832 H H    . ASN   B 1 54  ? 54.258 -20.597 0.133   1.00 16.98 ?  54  ASN   B H    1 
ATOM   4833 H HA   . ASN   B 1 54  ? 55.426 -18.271 0.004   1.00 17.21 ?  54  ASN   B HA   1 
ATOM   4834 H HB2  . ASN   B 1 54  ? 54.585 -18.972 2.031   1.00 18.20 ?  54  ASN   B HB2  1 
ATOM   4835 H HB3  . ASN   B 1 54  ? 55.631 -20.170 2.076   1.00 18.20 ?  54  ASN   B HB3  1 
ATOM   4836 H HD21 . ASN   B 1 54  ? 57.873 -18.500 3.789   1.00 21.47 ?  54  ASN   B HD21 1 
ATOM   4837 H HD22 . ASN   B 1 54  ? 57.231 -19.810 3.487   1.00 21.47 ?  54  ASN   B HD22 1 
ATOM   4838 N N    . LYS   B 1 55  ? 57.460 -20.741 -0.192  1.00 15.12 ?  55  LYS   B N    1 
ATOM   4839 C CA   . LYS   B 1 55  ? 58.818 -21.089 -0.597  1.00 16.40 ?  55  LYS   B CA   1 
ATOM   4840 C C    . LYS   B 1 55  ? 59.120 -20.561 -1.992  1.00 16.24 ?  55  LYS   B C    1 
ATOM   4841 O O    . LYS   B 1 55  ? 60.220 -20.050 -2.246  1.00 16.70 ?  55  LYS   B O    1 
ATOM   4842 C CB   . LYS   B 1 55  ? 59.016 -22.608 -0.543  1.00 18.16 ?  55  LYS   B CB   1 
ATOM   4843 C CG   . LYS   B 1 55  ? 60.423 -23.059 -0.913  1.00 23.26 ?  55  LYS   B CG   1 
ATOM   4844 C CD   . LYS   B 1 55  ? 60.615 -24.561 -0.745  1.00 26.93 ?  55  LYS   B CD   1 
ATOM   4845 C CE   . LYS   B 1 55  ? 60.611 -24.974 0.725   1.00 30.80 ?  55  LYS   B CE   1 
ATOM   4846 N NZ   . LYS   B 1 55  ? 61.122 -26.350 0.921   1.00 33.53 ?  55  LYS   B NZ   1 
ATOM   4847 H H    . LYS   B 1 55  ? 56.953 -21.416 -0.004  1.00 18.15 ?  55  LYS   B H    1 
ATOM   4848 H HA   . LYS   B 1 55  ? 59.444 -20.686 0.018   1.00 19.70 ?  55  LYS   B HA   1 
ATOM   4849 H HB2  . LYS   B 1 55  ? 58.829 -22.917 0.358   1.00 21.80 ?  55  LYS   B HB2  1 
ATOM   4850 H HB3  . LYS   B 1 55  ? 58.397 -23.029 -1.166  1.00 21.80 ?  55  LYS   B HB3  1 
ATOM   4851 H HG2  . LYS   B 1 55  ? 60.596 -22.837 -1.841  1.00 27.92 ?  55  LYS   B HG2  1 
ATOM   4852 H HG3  . LYS   B 1 55  ? 61.060 -22.607 -0.338  1.00 27.92 ?  55  LYS   B HG3  1 
ATOM   4853 H HD2  . LYS   B 1 55  ? 59.893 -25.032 -1.192  1.00 32.33 ?  55  LYS   B HD2  1 
ATOM   4854 H HD3  . LYS   B 1 55  ? 61.469 -24.823 -1.127  1.00 32.33 ?  55  LYS   B HD3  1 
ATOM   4855 H HE2  . LYS   B 1 55  ? 61.176 -24.361 1.224   1.00 36.98 ?  55  LYS   B HE2  1 
ATOM   4856 H HE3  . LYS   B 1 55  ? 59.700 -24.931 1.061   1.00 36.98 ?  55  LYS   B HE3  1 
ATOM   4857 H HZ1  . LYS   B 1 55  ? 61.064 -26.574 1.781   1.00 40.26 ?  55  LYS   B HZ1  1 
ATOM   4858 H HZ2  . LYS   B 1 55  ? 60.638 -26.922 0.441   1.00 40.26 ?  55  LYS   B HZ2  1 
ATOM   4859 H HZ3  . LYS   B 1 55  ? 61.970 -26.398 0.664   1.00 40.26 ?  55  LYS   B HZ3  1 
ATOM   4860 N N    . ALA   B 1 56  ? 58.151 -20.655 -2.906  1.00 14.90 ?  56  ALA   B N    1 
ATOM   4861 C CA   . ALA   B 1 56  ? 58.372 -20.159 -4.256  1.00 15.95 ?  56  ALA   B CA   1 
ATOM   4862 C C    . ALA   B 1 56  ? 58.651 -18.662 -4.263  1.00 15.86 ?  56  ALA   B C    1 
ATOM   4863 O O    . ALA   B 1 56  ? 59.367 -18.177 -5.148  1.00 17.25 ?  56  ALA   B O    1 
ATOM   4864 C CB   . ALA   B 1 56  ? 57.183 -20.502 -5.154  1.00 16.59 ?  56  ALA   B CB   1 
ATOM   4865 H H    . ALA   B 1 56  ? 57.363 -20.979 -2.770  1.00 17.89 ?  56  ALA   B H    1 
ATOM   4866 H HA   . ALA   B 1 56  ? 59.155 -20.594 -4.621  1.00 19.16 ?  56  ALA   B HA   1 
ATOM   4867 H HB1  . ALA   B 1 56  ? 57.362 -20.172 -6.053  1.00 19.92 ?  56  ALA   B HB1  1 
ATOM   4868 H HB2  . ALA   B 1 56  ? 57.079 -21.467 -5.176  1.00 19.92 ?  56  ALA   B HB2  1 
ATOM   4869 H HB3  . ALA   B 1 56  ? 56.386 -20.087 -4.802  1.00 19.92 ?  56  ALA   B HB3  1 
ATOM   4870 N N    . THR   B 1 57  ? 58.098 -17.918 -3.303  1.00 16.16 ?  57  THR   B N    1 
ATOM   4871 C CA   . THR   B 1 57  ? 58.343 -16.484 -3.209  1.00 16.69 ?  57  THR   B CA   1 
ATOM   4872 C C    . THR   B 1 57  ? 59.573 -16.156 -2.384  1.00 18.03 ?  57  THR   B C    1 
ATOM   4873 O O    . THR   B 1 57  ? 59.805 -14.978 -2.071  1.00 17.90 ?  57  THR   B O    1 
ATOM   4874 C CB   . THR   B 1 57  ? 57.143 -15.743 -2.592  1.00 15.83 ?  57  THR   B CB   1 
ATOM   4875 O OG1  . THR   B 1 57  ? 57.105 -15.955 -1.175  1.00 16.45 ?  57  THR   B OG1  1 
ATOM   4876 C CG2  . THR   B 1 57  ? 55.842 -16.159 -3.244  1.00 15.96 ?  57  THR   B CG2  1 
ATOM   4877 H H    . THR   B 1 57  ? 57.561 -18.220 -2.699  1.00 19.41 ?  57  THR   B H    1 
ATOM   4878 H HA   . THR   B 1 57  ? 58.474 -16.129 -4.103  1.00 20.04 ?  57  THR   B HA   1 
ATOM   4879 H HB   . THR   B 1 57  ? 57.251 -14.789 -2.755  1.00 19.00 ?  57  THR   B HB   1 
ATOM   4880 H HG1  . THR   B 1 57  ? 57.007 -16.776 -1.012  1.00 19.76 ?  57  THR   B HG1  1 
ATOM   4881 H HG21 . THR   B 1 57  ? 55.115 -15.603 -2.936  1.00 19.16 ?  57  THR   B HG21 1 
ATOM   4882 H HG22 . THR   B 1 57  ? 55.914 -16.079 -4.212  1.00 19.16 ?  57  THR   B HG22 1 
ATOM   4883 H HG23 . THR   B 1 57  ? 55.644 -17.086 -3.028  1.00 19.16 ?  57  THR   B HG23 1 
ATOM   4884 N N    . ASN   B 1 58  ? 60.366 -17.158 -2.022  1.00 17.93 ?  58  ASN   B N    1 
ATOM   4885 C CA   . ASN   B 1 58  ? 61.568 -16.930 -1.223  1.00 21.14 ?  58  ASN   B CA   1 
ATOM   4886 C C    . ASN   B 1 58  ? 61.228 -16.216 0.084   1.00 18.63 ?  58  ASN   B C    1 
ATOM   4887 O O    . ASN   B 1 58  ? 61.952 -15.330 0.542   1.00 19.54 ?  58  ASN   B O    1 
ATOM   4888 C CB   . ASN   B 1 58  ? 62.644 -16.174 -2.012  1.00 30.97 ?  58  ASN   B CB   1 
ATOM   4889 C CG   . ASN   B 1 58  ? 64.022 -16.305 -1.390  1.00 42.57 ?  58  ASN   B CG   1 
ATOM   4890 O OD1  . ASN   B 1 58  ? 64.340 -17.318 -0.764  1.00 45.77 ?  58  ASN   B OD1  1 
ATOM   4891 N ND2  . ASN   B 1 58  ? 64.850 -15.278 -1.559  1.00 51.09 ?  58  ASN   B ND2  1 
ATOM   4892 H H    . ASN   B 1 58  ? 60.237 -17.986 -2.229  1.00 21.52 ?  58  ASN   B H    1 
ATOM   4893 H HA   . ASN   B 1 58  ? 61.945 -17.795 -0.997  1.00 25.38 ?  58  ASN   B HA   1 
ATOM   4894 H HB2  . ASN   B 1 58  ? 62.691 -16.528 -2.917  1.00 37.17 ?  58  ASN   B HB2  1 
ATOM   4895 H HB3  . ASN   B 1 58  ? 62.420 -15.231 -2.039  1.00 37.17 ?  58  ASN   B HB3  1 
ATOM   4896 H HD21 . ASN   B 1 58  ? 65.644 -15.304 -1.227  1.00 61.32 ?  58  ASN   B HD21 1 
ATOM   4897 H HD22 . ASN   B 1 58  ? 64.594 -14.586 -2.001  1.00 61.32 ?  58  ASN   B HD22 1 
ATOM   4898 N N    . ASN   B 1 59  ? 60.117 -16.618 0.700   1.00 17.56 ?  59  ASN   B N    1 
ATOM   4899 C CA   . ASN   B 1 59  ? 59.629 -16.116 1.984   1.00 17.05 ?  59  ASN   B CA   1 
ATOM   4900 C C    . ASN   B 1 59  ? 59.041 -14.709 1.917   1.00 16.50 ?  59  ASN   B C    1 
ATOM   4901 O O    . ASN   B 1 59  ? 58.623 -14.189 2.952   1.00 17.04 ?  59  ASN   B O    1 
ATOM   4902 C CB   . ASN   B 1 59  ? 60.692 -16.174 3.094   1.00 17.47 ?  59  ASN   B CB   1 
ATOM   4903 C CG   . ASN   B 1 59  ? 60.099 -16.351 4.477   1.00 19.36 ?  59  ASN   B CG   1 
ATOM   4904 O OD1  . ASN   B 1 59  ? 59.282 -17.250 4.706   1.00 19.19 ?  59  ASN   B OD1  1 
ATOM   4905 N ND2  . ASN   B 1 59  ? 60.524 -15.502 5.422   1.00 20.89 ?  59  ASN   B ND2  1 
ATOM   4906 H H    . ASN   B 1 59  ? 59.589 -17.218 0.368   1.00 21.09 ?  59  ASN   B H    1 
ATOM   4907 H HA   . ASN   B 1 59  ? 58.919 -16.707 2.271   1.00 20.47 ?  59  ASN   B HA   1 
ATOM   4908 H HB2  . ASN   B 1 59  ? 61.294 -16.925 2.934   1.00 20.98 ?  59  ASN   B HB2  1 
ATOM   4909 H HB3  . ASN   B 1 59  ? 61.202 -15.348 3.099   1.00 20.98 ?  59  ASN   B HB3  1 
ATOM   4910 H HD21 . ASN   B 1 59  ? 60.217 -15.558 6.227   1.00 25.09 ?  59  ASN   B HD21 1 
ATOM   4911 H HD22 . ASN   B 1 59  ? 61.088 -14.885 5.224   1.00 25.09 ?  59  ASN   B HD22 1 
ATOM   4912 N N    . ALA   B 1 60  ? 58.987 -14.077 0.743   1.00 16.51 ?  60  ALA   B N    1 
ATOM   4913 C CA   . ALA   B 1 60  ? 58.395 -12.743 0.671   1.00 17.18 ?  60  ALA   B CA   1 
ATOM   4914 C C    . ALA   B 1 60  ? 56.927 -12.764 1.079   1.00 15.57 ?  60  ALA   B C    1 
ATOM   4915 O O    . ALA   B 1 60  ? 56.431 -11.809 1.689   1.00 15.76 ?  60  ALA   B O    1 
ATOM   4916 C CB   . ALA   B 1 60  ? 58.557 -12.159 -0.733  1.00 18.88 ?  60  ALA   B CB   1 
ATOM   4917 H H    . ALA   B 1 60  ? 59.278 -14.401 -0.004  1.00 19.83 ?  60  ALA   B H    1 
ATOM   4918 H HA   . ALA   B 1 60  ? 58.870 -12.171 1.287   1.00 20.63 ?  60  ALA   B HA   1 
ATOM   4919 H HB1  . ALA   B 1 60  ? 58.161 -11.277 -0.750  1.00 22.67 ?  60  ALA   B HB1  1 
ATOM   4920 H HB2  . ALA   B 1 60  ? 59.505 -12.102 -0.946  1.00 22.67 ?  60  ALA   B HB2  1 
ATOM   4921 H HB3  . ALA   B 1 60  ? 58.113 -12.738 -1.372  1.00 22.67 ?  60  ALA   B HB3  1 
ATOM   4922 N N    . MET   B 1 61  ? 56.216 -13.844 0.758   1.00 15.15 ?  61  MET   B N    1 
ATOM   4923 C CA   . MET   B 1 61  ? 54.819 -13.952 1.154   1.00 14.42 ?  61  MET   B CA   1 
ATOM   4924 C C    . MET   B 1 61  ? 54.670 -13.950 2.673   1.00 15.30 ?  61  MET   B C    1 
ATOM   4925 O O    . MET   B 1 61  ? 53.766 -13.301 3.221   1.00 15.11 ?  61  MET   B O    1 
ATOM   4926 C CB   . MET   B 1 61  ? 54.230 -15.225 0.542   1.00 15.18 ?  61  MET   B CB   1 
ATOM   4927 C CG   . MET   B 1 61  ? 52.771 -15.492 0.895   1.00 14.23 ?  61  MET   B CG   1 
ATOM   4928 S SD   . MET   B 1 61  ? 52.147 -17.027 0.169   1.00 14.97 ?  61  MET   B SD   1 
ATOM   4929 C CE   . MET   B 1 61  ? 51.900 -16.481 -1.511  1.00 15.61 ?  61  MET   B CE   1 
ATOM   4930 H H    . MET   B 1 61  ? 56.515 -14.528 0.318   1.00 18.19 ?  61  MET   B H    1 
ATOM   4931 H HA   . MET   B 1 61  ? 54.329 -13.199 0.790   1.00 17.32 ?  61  MET   B HA   1 
ATOM   4932 H HB2  . MET   B 1 61  ? 54.289 -15.164 -0.425  1.00 18.23 ?  61  MET   B HB2  1 
ATOM   4933 H HB3  . MET   B 1 61  ? 54.746 -15.987 0.851   1.00 18.23 ?  61  MET   B HB3  1 
ATOM   4934 H HG2  . MET   B 1 61  ? 52.674 -15.566 1.858   1.00 17.09 ?  61  MET   B HG2  1 
ATOM   4935 H HG3  . MET   B 1 61  ? 52.220 -14.761 0.565   1.00 17.09 ?  61  MET   B HG3  1 
ATOM   4936 H HE1  . MET   B 1 61  ? 51.545 -17.217 -2.037  1.00 18.74 ?  61  MET   B HE1  1 
ATOM   4937 H HE2  . MET   B 1 61  ? 51.264 -15.742 -1.518  1.00 18.74 ?  61  MET   B HE2  1 
ATOM   4938 H HE3  . MET   B 1 61  ? 52.745 -16.187 -1.882  1.00 18.74 ?  61  MET   B HE3  1 
ATOM   4939 N N    . GLN   B 1 62  ? 55.539 -14.679 3.372   1.00 15.06 ?  62  GLN   B N    1 
ATOM   4940 C CA   . GLN   B 1 62  ? 55.448 -14.742 4.829   1.00 15.44 ?  62  GLN   B CA   1 
ATOM   4941 C C    . GLN   B 1 62  ? 55.730 -13.386 5.465   1.00 15.57 ?  62  GLN   B C    1 
ATOM   4942 O O    . GLN   B 1 62  ? 55.032 -12.970 6.400   1.00 16.20 ?  62  GLN   B O    1 
ATOM   4943 C CB   . GLN   B 1 62  ? 56.408 -15.798 5.382   1.00 16.26 ?  62  GLN   B CB   1 
ATOM   4944 C CG   . GLN   B 1 62  ? 56.179 -16.064 6.854   1.00 16.08 ?  62  GLN   B CG   1 
ATOM   4945 C CD   . GLN   B 1 62  ? 54.806 -16.659 7.107   1.00 16.51 ?  62  GLN   B CD   1 
ATOM   4946 O OE1  . GLN   B 1 62  ? 54.547 -17.809 6.753   1.00 16.43 ?  62  GLN   B OE1  1 
ATOM   4947 N NE2  . GLN   B 1 62  ? 53.908 -15.873 7.701   1.00 16.52 ?  62  GLN   B NE2  1 
ATOM   4948 H H    . GLN   B 1 62  ? 56.178 -15.149 3.033   1.00 18.09 ?  62  GLN   B H    1 
ATOM   4949 H HA   . GLN   B 1 62  ? 54.542 -15.003 5.070   1.00 18.54 ?  62  GLN   B HA   1 
ATOM   4950 H HB2  . GLN   B 1 62  ? 56.285 -16.629 4.900   1.00 19.53 ?  62  GLN   B HB2  1 
ATOM   4951 H HB3  . GLN   B 1 62  ? 57.321 -15.480 5.269   1.00 19.53 ?  62  GLN   B HB3  1 
ATOM   4952 H HG2  . GLN   B 1 62  ? 56.848 -16.697 7.168   1.00 19.31 ?  62  GLN   B HG2  1 
ATOM   4953 H HG3  . GLN   B 1 62  ? 56.251 -15.233 7.349   1.00 19.31 ?  62  GLN   B HG3  1 
ATOM   4954 H HE21 . GLN   B 1 62  ? 54.131 -15.071 7.934   1.00 19.84 ?  62  GLN   B HE21 1 
ATOM   4955 H HE22 . GLN   B 1 62  ? 53.122 -16.166 7.870   1.00 19.84 ?  62  GLN   B HE22 1 
ATOM   4956 N N    . VAL   B 1 63  ? 56.757 -12.682 4.985   1.00 16.09 ?  63  VAL   B N    1 
ATOM   4957 C CA   . VAL   B 1 63  ? 57.058 -11.359 5.530   1.00 16.99 ?  63  VAL   B CA   1 
ATOM   4958 C C    . VAL   B 1 63  ? 55.867 -10.426 5.338   1.00 16.04 ?  63  VAL   B C    1 
ATOM   4959 O O    . VAL   B 1 63  ? 55.439 -9.734  6.272   1.00 17.05 ?  63  VAL   B O    1 
ATOM   4960 C CB   . VAL   B 1 63  ? 58.355 -10.808 4.908   1.00 18.43 ?  63  VAL   B CB   1 
ATOM   4961 C CG1  . VAL   B 1 63  ? 58.593 -9.362  5.335   1.00 19.20 ?  63  VAL   B CG1  1 
ATOM   4962 C CG2  . VAL   B 1 63  ? 59.544 -11.680 5.311   1.00 19.02 ?  63  VAL   B CG2  1 
ATOM   4963 H H    . VAL   B 1 63  ? 57.281 -12.945 4.352   1.00 19.32 ?  63  VAL   B H    1 
ATOM   4964 H HA   . VAL   B 1 63  ? 57.212 -11.448 6.480   1.00 20.40 ?  63  VAL   B HA   1 
ATOM   4965 H HB   . VAL   B 1 63  ? 58.291 -10.831 3.941   1.00 22.13 ?  63  VAL   B HB   1 
ATOM   4966 H HG11 . VAL   B 1 63  ? 59.512 -9.110  5.122   1.00 23.06 ?  63  VAL   B HG11 1 
ATOM   4967 H HG12 . VAL   B 1 63  ? 57.982 -8.780  4.859   1.00 23.06 ?  63  VAL   B HG12 1 
ATOM   4968 H HG13 . VAL   B 1 63  ? 58.453 -9.281  6.292   1.00 23.06 ?  63  VAL   B HG13 1 
ATOM   4969 H HG21 . VAL   B 1 63  ? 60.359 -11.308 4.929   1.00 22.83 ?  63  VAL   B HG21 1 
ATOM   4970 H HG22 . VAL   B 1 63  ? 59.616 -11.689 6.281   1.00 22.83 ?  63  VAL   B HG22 1 
ATOM   4971 H HG23 . VAL   B 1 63  ? 59.408 -12.579 4.981   1.00 22.83 ?  63  VAL   B HG23 1 
ATOM   4972 N N    . GLU   B 1 64  ? 55.305 -10.411 4.128   1.00 15.04 ?  64  GLU   B N    1 
ATOM   4973 C CA   . GLU   B 1 64  ? 54.139 -9.580  3.847   1.00 15.18 ?  64  GLU   B CA   1 
ATOM   4974 C C    . GLU   B 1 64  ? 52.955 -9.989  4.716   1.00 14.70 ?  64  GLU   B C    1 
ATOM   4975 O O    . GLU   B 1 64  ? 52.216 -9.134  5.225   1.00 15.09 ?  64  GLU   B O    1 
ATOM   4976 C CB   . GLU   B 1 64  ? 53.792 -9.719  2.365   1.00 15.61 ?  64  GLU   B CB   1 
ATOM   4977 C CG   . GLU   B 1 64  ? 52.537 -8.963  1.910   1.00 15.83 ?  64  GLU   B CG   1 
ATOM   4978 C CD   . GLU   B 1 64  ? 51.980 -9.494  0.604   1.00 16.27 ?  64  GLU   B CD   1 
ATOM   4979 O OE1  . GLU   B 1 64  ? 52.154 -10.706 0.312   1.00 17.18 ?  64  GLU   B OE1  1 
ATOM   4980 O OE2  . GLU   B 1 64  ? 51.324 -8.703  -0.114  1.00 17.37 -1 64  GLU   B OE2  1 
ATOM   4981 H H    . GLU   B 1 64  ? 55.596 -10.866 3.447   1.00 18.07 ?  64  GLU   B H    1 
ATOM   4982 H HA   . GLU   B 1 64  ? 54.359 -8.648  4.025   1.00 18.24 ?  64  GLU   B HA   1 
ATOM   4983 H HB2  . GLU   B 1 64  ? 54.539 -9.380  1.835   1.00 18.75 ?  64  GLU   B HB2  1 
ATOM   4984 H HB3  . GLU   B 1 64  ? 53.658 -10.654 2.168   1.00 18.75 ?  64  GLU   B HB3  1 
ATOM   4985 H HG2  . GLU   B 1 64  ? 51.845 -9.040  2.587   1.00 19.01 ?  64  GLU   B HG2  1 
ATOM   4986 H HG3  . GLU   B 1 64  ? 52.763 -8.023  1.783   1.00 19.01 ?  64  GLU   B HG3  1 
ATOM   4987 N N    . SER   B 1 65  ? 52.783 -11.296 4.914   1.00 14.64 ?  65  SER   B N    1 
ATOM   4988 C CA   . SER   B 1 65  ? 51.675 -11.804 5.715   1.00 15.12 ?  65  SER   B CA   1 
ATOM   4989 C C    . SER   B 1 65  ? 51.800 -11.398 7.179   1.00 15.64 ?  65  SER   B C    1 
ATOM   4990 O O    . SER   B 1 65  ? 50.800 -11.005 7.805   1.00 15.73 ?  65  SER   B O    1 
ATOM   4991 C CB   . SER   B 1 65  ? 51.596 -13.320 5.582   1.00 15.32 ?  65  SER   B CB   1 
ATOM   4992 O OG   . SER   B 1 65  ? 51.215 -13.699 4.271   1.00 15.19 ?  65  SER   B OG   1 
ATOM   4993 H H    . SER   B 1 65  ? 53.296 -11.910 4.589   1.00 17.58 ?  65  SER   B H    1 
ATOM   4994 H HA   . SER   B 1 65  ? 50.847 -11.428 5.372   1.00 18.16 ?  65  SER   B HA   1 
ATOM   4995 H HB2  . SER   B 1 65  ? 52.462 -13.698 5.787   1.00 18.40 ?  65  SER   B HB2  1 
ATOM   4996 H HB3  . SER   B 1 65  ? 50.933 -13.650 6.211   1.00 18.40 ?  65  SER   B HB3  1 
ATOM   4997 H HG   . SER   B 1 65  ? 51.783 -13.421 3.715   1.00 18.24 ?  65  SER   B HG   1 
ATOM   4998 N N    . ASP   B 1 66  ? 53.012 -11.478 7.745   1.00 15.21 ?  66  ASP   B N    1 
ATOM   4999 C CA   . ASP   B 1 66  ? 53.195 -11.095 9.141   1.00 15.42 ?  66  ASP   B CA   1 
ATOM   5000 C C    . ASP   B 1 66  ? 52.883 -9.617  9.344   1.00 16.20 ?  66  ASP   B C    1 
ATOM   5001 O O    . ASP   B 1 66  ? 52.315 -9.226  10.371  1.00 16.92 ?  66  ASP   B O    1 
ATOM   5002 C CB   . ASP   B 1 66  ? 54.623 -11.405 9.594   1.00 17.40 ?  66  ASP   B CB   1 
ATOM   5003 C CG   . ASP   B 1 66  ? 54.893 -12.901 9.739   1.00 19.13 ?  66  ASP   B CG   1 
ATOM   5004 O OD1  . ASP   B 1 66  ? 53.938 -13.706 9.695   1.00 19.91 ?  66  ASP   B OD1  1 
ATOM   5005 O OD2  . ASP   B 1 66  ? 56.074 -13.254 9.913   1.00 22.62 -1 66  ASP   B OD2  1 
ATOM   5006 H H    . ASP   B 1 66  ? 53.729 -11.755 7.346   1.00 18.27 ?  66  ASP   B H    1 
ATOM   5007 H HA   . ASP   B 1 66  ? 52.590 -11.608 9.695   1.00 18.51 ?  66  ASP   B HA   1 
ATOM   5008 H HB2  . ASP   B 1 66  ? 55.253 -11.060 8.943   1.00 20.90 ?  66  ASP   B HB2  1 
ATOM   5009 H HB3  . ASP   B 1 66  ? 54.783 -10.997 10.460  1.00 20.90 ?  66  ASP   B HB3  1 
ATOM   5010 N N    . ASP   B 1 67  ? 53.251 -8.782  8.374   1.00 16.25 ?  67  ASP   B N    1 
ATOM   5011 C CA   . ASP   B 1 67  ? 52.919 -7.365  8.465   1.00 16.39 ?  67  ASP   B CA   1 
ATOM   5012 C C    . ASP   B 1 67  ? 51.410 -7.143  8.393   1.00 17.16 ?  67  ASP   B C    1 
ATOM   5013 O O    . ASP   B 1 67  ? 50.862 -6.331  9.149   1.00 17.10 ?  67  ASP   B O    1 
ATOM   5014 C CB   . ASP   B 1 67  ? 53.631 -6.598  7.363   1.00 17.78 ?  67  ASP   B CB   1 
ATOM   5015 C CG   . ASP   B 1 67  ? 53.199 -5.169  7.306   1.00 19.68 ?  67  ASP   B CG   1 
ATOM   5016 O OD1  . ASP   B 1 67  ? 53.690 -4.367  8.137   1.00 20.66 ?  67  ASP   B OD1  1 
ATOM   5017 O OD2  . ASP   B 1 67  ? 52.360 -4.846  6.448   1.00 20.91 -1 67  ASP   B OD2  1 
ATOM   5018 H H    . ASP   B 1 67  ? 53.701 -9.005  7.675   1.00 19.52 ?  67  ASP   B H    1 
ATOM   5019 H HA   . ASP   B 1 67  ? 53.234 -7.021  9.318   1.00 19.68 ?  67  ASP   B HA   1 
ATOM   5020 H HB2  . ASP   B 1 67  ? 54.588 -6.623  7.521   1.00 21.35 ?  67  ASP   B HB2  1 
ATOM   5021 H HB3  . ASP   B 1 67  ? 53.424 -7.007  6.507   1.00 21.35 ?  67  ASP   B HB3  1 
ATOM   5022 N N    . TYR   B 1 68  ? 50.720 -7.880  7.513   1.00 16.56 ?  68  TYR   B N    1 
ATOM   5023 C CA   . TYR   B 1 68  ? 49.266 -7.785  7.435   1.00 16.80 ?  68  TYR   B CA   1 
ATOM   5024 C C    . TYR   B 1 68  ? 48.628 -8.141  8.772   1.00 16.49 ?  68  TYR   B C    1 
ATOM   5025 O O    . TYR   B 1 68  ? 47.699 -7.463  9.231   1.00 17.16 ?  68  TYR   B O    1 
ATOM   5026 C CB   . TYR   B 1 68  ? 48.746 -8.725  6.346   1.00 17.68 ?  68  TYR   B CB   1 
ATOM   5027 C CG   . TYR   B 1 68  ? 47.237 -8.863  6.382   1.00 19.01 ?  68  TYR   B CG   1 
ATOM   5028 C CD1  . TYR   B 1 68  ? 46.622 -9.809  7.199   1.00 19.76 ?  68  TYR   B CD1  1 
ATOM   5029 C CD2  . TYR   B 1 68  ? 46.426 -8.026  5.636   1.00 20.46 ?  68  TYR   B CD2  1 
ATOM   5030 C CE1  . TYR   B 1 68  ? 45.252 -9.917  7.271   1.00 21.90 ?  68  TYR   B CE1  1 
ATOM   5031 C CE2  . TYR   B 1 68  ? 45.040 -8.139  5.693   1.00 21.93 ?  68  TYR   B CE2  1 
ATOM   5032 C CZ   . TYR   B 1 68  ? 44.471 -9.078  6.520   1.00 22.36 ?  68  TYR   B CZ   1 
ATOM   5033 O OH   . TYR   B 1 68  ? 43.102 -9.189  6.595   1.00 24.35 ?  68  TYR   B OH   1 
ATOM   5034 H H    . TYR   B 1 68  ? 51.066 -8.448  6.966   1.00 19.89 ?  68  TYR   B H    1 
ATOM   5035 H HA   . TYR   B 1 68  ? 49.016 -6.874  7.208   1.00 20.17 ?  68  TYR   B HA   1 
ATOM   5036 H HB2  . TYR   B 1 68  ? 48.993 -8.372  5.480   1.00 21.23 ?  68  TYR   B HB2  1 
ATOM   5037 H HB3  . TYR   B 1 68  ? 49.133 -9.603  6.476   1.00 21.23 ?  68  TYR   B HB3  1 
ATOM   5038 H HD1  . TYR   B 1 68  ? 47.154 -10.379 7.716   1.00 23.73 ?  68  TYR   B HD1  1 
ATOM   5039 H HD2  . TYR   B 1 68  ? 46.815 -7.379  5.094   1.00 24.56 ?  68  TYR   B HD2  1 
ATOM   5040 H HE1  . TYR   B 1 68  ? 44.860 -10.568 7.813   1.00 26.29 ?  68  TYR   B HE1  1 
ATOM   5041 H HE2  . TYR   B 1 68  ? 44.499 -7.572  5.192   1.00 26.33 ?  68  TYR   B HE2  1 
ATOM   5042 H HH   . TYR   B 1 68  ? 42.731 -8.640  6.077   1.00 29.24 ?  68  TYR   B HH   1 
ATOM   5043 N N    . ILE   B 1 69  ? 49.109 -9.211  9.405   1.00 16.18 ?  69  ILE   B N    1 
ATOM   5044 C CA   . ILE   B 1 69  ? 48.544 -9.647  10.680  1.00 17.57 ?  69  ILE   B CA   1 
ATOM   5045 C C    . ILE   B 1 69  ? 48.806 -8.612  11.767  1.00 17.08 ?  69  ILE   B C    1 
ATOM   5046 O O    . ILE   B 1 69  ? 47.944 -8.343  12.613  1.00 17.06 ?  69  ILE   B O    1 
ATOM   5047 C CB   . ILE   B 1 69  ? 49.116 -11.027 11.056  1.00 18.59 ?  69  ILE   B CB   1 
ATOM   5048 C CG1  . ILE   B 1 69  ? 48.583 -12.117 10.117  1.00 19.43 ?  69  ILE   B CG1  1 
ATOM   5049 C CG2  . ILE   B 1 69  ? 48.820 -11.355 12.507  1.00 19.48 ?  69  ILE   B CG2  1 
ATOM   5050 C CD1  . ILE   B 1 69  ? 47.095 -12.418 10.259  1.00 19.98 ?  69  ILE   B CD1  1 
ATOM   5051 H H    . ILE   B 1 69  ? 49.754 -9.696  9.118   1.00 19.43 ?  69  ILE   B H    1 
ATOM   5052 H HA   . ILE   B 1 69  ? 47.584 -9.735  10.585  1.00 21.10 ?  69  ILE   B HA   1 
ATOM   5053 H HB   . ILE   B 1 69  ? 50.076 -10.993 10.951  1.00 22.32 ?  69  ILE   B HB   1 
ATOM   5054 H HG12 . ILE   B 1 69  ? 48.736 -11.840 9.200   1.00 23.33 ?  69  ILE   B HG12 1 
ATOM   5055 H HG13 . ILE   B 1 69  ? 49.063 -12.942 10.292  1.00 23.33 ?  69  ILE   B HG13 1 
ATOM   5056 H HG21 . ILE   B 1 69  ? 48.935 -12.309 12.640  1.00 23.40 ?  69  ILE   B HG21 1 
ATOM   5057 H HG22 . ILE   B 1 69  ? 49.434 -10.867 13.074  1.00 23.40 ?  69  ILE   B HG22 1 
ATOM   5058 H HG23 . ILE   B 1 69  ? 47.904 -11.104 12.707  1.00 23.40 ?  69  ILE   B HG23 1 
ATOM   5059 H HD11 . ILE   B 1 69  ? 46.857 -13.131 9.644   1.00 23.99 ?  69  ILE   B HD11 1 
ATOM   5060 H HD12 . ILE   B 1 69  ? 46.910 -12.698 11.170  1.00 23.99 ?  69  ILE   B HD12 1 
ATOM   5061 H HD13 . ILE   B 1 69  ? 46.585 -11.621 10.048  1.00 23.99 ?  69  ILE   B HD13 1 
ATOM   5062 N N    . ALA   B 1 70  ? 49.999 -8.017  11.778  1.00 17.17 ?  70  ALA   B N    1 
ATOM   5063 C CA   . ALA   B 1 70  ? 50.284 -6.996  12.777  1.00 16.38 ?  70  ALA   B CA   1 
ATOM   5064 C C    . ALA   B 1 70  ? 49.297 -5.842  12.674  1.00 16.48 ?  70  ALA   B C    1 
ATOM   5065 O O    . ALA   B 1 70  ? 48.852 -5.302  13.690  1.00 17.75 ?  70  ALA   B O    1 
ATOM   5066 C CB   . ALA   B 1 70  ? 51.714 -6.492  12.615  1.00 16.67 ?  70  ALA   B CB   1 
ATOM   5067 H H    . ALA   B 1 70  ? 50.641 -8.193  11.236  1.00 20.62 ?  70  ALA   B H    1 
ATOM   5068 H HA   . ALA   B 1 70  ? 50.209 -7.383  13.665  1.00 19.67 ?  70  ALA   B HA   1 
ATOM   5069 H HB1  . ALA   B 1 70  ? 51.900 -5.829  13.304  1.00 20.02 ?  70  ALA   B HB1  1 
ATOM   5070 H HB2  . ALA   B 1 70  ? 52.332 -7.237  12.711  1.00 20.02 ?  70  ALA   B HB2  1 
ATOM   5071 H HB3  . ALA   B 1 70  ? 51.818 -6.091  11.739  1.00 20.02 ?  70  ALA   B HB3  1 
ATOM   5072 N N    . THR   B 1 71  ? 48.933 -5.466  11.450  1.00 17.60 ?  71  THR   B N    1 
ATOM   5073 C CA   . THR   B 1 71  ? 48.039 -4.333  11.236  1.00 19.12 ?  71  THR   B CA   1 
ATOM   5074 C C    . THR   B 1 71  ? 46.573 -4.700  11.452  1.00 18.96 ?  71  THR   B C    1 
ATOM   5075 O O    . THR   B 1 71  ? 45.798 -3.891  11.982  1.00 19.65 ?  71  THR   B O    1 
ATOM   5076 C CB   . THR   B 1 71  ? 48.263 -3.774  9.827   1.00 20.91 ?  71  THR   B CB   1 
ATOM   5077 O OG1  . THR   B 1 71  ? 49.593 -3.245  9.731   1.00 22.81 ?  71  THR   B OG1  1 
ATOM   5078 C CG2  . THR   B 1 71  ? 47.260 -2.675  9.505   1.00 21.28 ?  71  THR   B CG2  1 
ATOM   5079 H H    . THR   B 1 71  ? 49.188 -5.858  10.729  1.00 21.13 ?  71  THR   B H    1 
ATOM   5080 H HA   . THR   B 1 71  ? 48.269 -3.635  11.869  1.00 22.96 ?  71  THR   B HA   1 
ATOM   5081 H HB   . THR   B 1 71  ? 48.161 -4.486  9.177   1.00 25.11 ?  71  THR   B HB   1 
ATOM   5082 H HG1  . THR   B 1 71  ? 49.728 -2.928  8.962   1.00 27.38 ?  71  THR   B HG1  1 
ATOM   5083 H HG21 . THR   B 1 71  ? 47.562 -2.168  8.735   1.00 25.56 ?  71  THR   B HG21 1 
ATOM   5084 H HG22 . THR   B 1 71  ? 46.395 -3.061  9.308   1.00 25.56 ?  71  THR   B HG22 1 
ATOM   5085 H HG23 . THR   B 1 71  ? 47.176 -2.072  10.262  1.00 25.56 ?  71  THR   B HG23 1 
ATOM   5086 N N    . ASN   B 1 72  ? 46.171 -5.905  11.055  1.00 18.56 ?  72  ASN   B N    1 
ATOM   5087 C CA   . ASN   B 1 72  ? 44.764 -6.249  10.927  1.00 18.97 ?  72  ASN   B CA   1 
ATOM   5088 C C    . ASN   B 1 72  ? 44.288 -7.343  11.874  1.00 19.60 ?  72  ASN   B C    1 
ATOM   5089 O O    . ASN   B 1 72  ? 43.068 -7.511  12.030  1.00 21.82 ?  72  ASN   B O    1 
ATOM   5090 C CB   . ASN   B 1 72  ? 44.441 -6.654  9.478   1.00 19.79 ?  72  ASN   B CB   1 
ATOM   5091 C CG   . ASN   B 1 72  ? 44.724 -5.546  8.491   1.00 20.69 ?  72  ASN   B CG   1 
ATOM   5092 O OD1  . ASN   B 1 72  ? 45.725 -5.570  7.761   1.00 22.44 ?  72  ASN   B OD1  1 
ATOM   5093 N ND2  . ASN   B 1 72  ? 43.852 -4.556  8.472   1.00 22.73 ?  72  ASN   B ND2  1 
ATOM   5094 H H    . ASN   B 1 72  ? 46.709 -6.555  10.850  1.00 22.29 ?  72  ASN   B H    1 
ATOM   5095 H HA   . ASN   B 1 72  ? 44.248 -5.459  11.124  1.00 22.78 ?  72  ASN   B HA   1 
ATOM   5096 H HB2  . ASN   B 1 72  ? 44.988 -7.417  9.231   1.00 23.76 ?  72  ASN   B HB2  1 
ATOM   5097 H HB3  . ASN   B 1 72  ? 43.505 -6.876  9.414   1.00 23.76 ?  72  ASN   B HB3  1 
ATOM   5098 H HD21 . ASN   B 1 72  ? 43.958 -3.893  7.929   1.00 27.29 ?  72  ASN   B HD21 1 
ATOM   5099 H HD22 . ASN   B 1 72  ? 43.165 -4.572  8.992   1.00 27.29 ?  72  ASN   B HD22 1 
ATOM   5100 N N    . GLY   B 1 73  ? 45.191 -8.089  12.512  1.00 19.75 ?  73  GLY   B N    1 
ATOM   5101 C CA   . GLY   B 1 73  ? 44.792 -9.243  13.282  1.00 19.04 ?  73  GLY   B CA   1 
ATOM   5102 C C    . GLY   B 1 73  ? 44.419 -10.430 12.416  1.00 17.99 ?  73  GLY   B C    1 
ATOM   5103 O O    . GLY   B 1 73  ? 44.410 -10.354 11.186  1.00 17.77 ?  73  GLY   B O    1 
ATOM   5104 H H    . GLY   B 1 73  ? 46.041 -7.942  12.509  1.00 23.71 ?  73  GLY   B H    1 
ATOM   5105 H HA2  . GLY   B 1 73  ? 45.519 -9.505  13.866  1.00 22.86 ?  73  GLY   B HA2  1 
ATOM   5106 H HA3  . GLY   B 1 73  ? 44.026 -9.010  13.834  1.00 22.86 ?  73  GLY   B HA3  1 
ATOM   5107 N N    . PRO   B 1 74  ? 44.092 -11.549 13.059  1.00 17.44 ?  74  PRO   B N    1 
ATOM   5108 C CA   . PRO   B 1 74  ? 43.826 -12.785 12.317  1.00 16.85 ?  74  PRO   B CA   1 
ATOM   5109 C C    . PRO   B 1 74  ? 42.539 -12.731 11.511  1.00 16.30 ?  74  PRO   B C    1 
ATOM   5110 O O    . PRO   B 1 74  ? 41.604 -11.979 11.819  1.00 17.77 ?  74  PRO   B O    1 
ATOM   5111 C CB   . PRO   B 1 74  ? 43.728 -13.838 13.428  1.00 17.55 ?  74  PRO   B CB   1 
ATOM   5112 C CG   . PRO   B 1 74  ? 43.338 -13.074 14.649  1.00 19.88 ?  74  PRO   B CG   1 
ATOM   5113 C CD   . PRO   B 1 74  ? 44.031 -11.755 14.515  1.00 18.63 ?  74  PRO   B CD   1 
ATOM   5114 H HA   . PRO   B 1 74  ? 44.574 -12.994 11.731  1.00 20.24 ?  74  PRO   B HA   1 
ATOM   5115 H HB2  . PRO   B 1 74  ? 43.045 -14.491 13.196  1.00 21.07 ?  74  PRO   B HB2  1 
ATOM   5116 H HB3  . PRO   B 1 74  ? 44.588 -14.271 13.546  1.00 21.07 ?  74  PRO   B HB3  1 
ATOM   5117 H HG2  . PRO   B 1 74  ? 42.376 -12.952 14.670  1.00 23.87 ?  74  PRO   B HG2  1 
ATOM   5118 H HG3  . PRO   B 1 74  ? 43.644 -13.540 15.441  1.00 23.87 ?  74  PRO   B HG3  1 
ATOM   5119 H HD2  . PRO   B 1 74  ? 43.509 -11.052 14.941  1.00 22.37 ?  74  PRO   B HD2  1 
ATOM   5120 H HD3  . PRO   B 1 74  ? 44.927 -11.800 14.884  1.00 22.37 ?  74  PRO   B HD3  1 
ATOM   5121 N N    . LEU   B 1 75  ? 42.512 -13.548 10.461  1.00 15.80 ?  75  LEU   B N    1 
ATOM   5122 C CA   . LEU   B 1 75  ? 41.305 -13.777 9.692   1.00 15.77 ?  75  LEU   B CA   1 
ATOM   5123 C C    . LEU   B 1 75  ? 40.329 -14.619 10.502  1.00 16.58 ?  75  LEU   B C    1 
ATOM   5124 O O    . LEU   B 1 75  ? 40.660 -15.166 11.553  1.00 17.67 ?  75  LEU   B O    1 
ATOM   5125 C CB   . LEU   B 1 75  ? 41.633 -14.500 8.387   1.00 15.71 ?  75  LEU   B CB   1 
ATOM   5126 C CG   . LEU   B 1 75  ? 42.462 -13.720 7.359   1.00 17.62 ?  75  LEU   B CG   1 
ATOM   5127 C CD1  . LEU   B 1 75  ? 42.623 -14.513 6.073   1.00 19.30 ?  75  LEU   B CD1  1 
ATOM   5128 C CD2  . LEU   B 1 75  ? 41.863 -12.374 7.068   1.00 22.34 ?  75  LEU   B CD2  1 
ATOM   5129 H H    . LEU   B 1 75  ? 43.199 -13.992 10.174  1.00 18.97 ?  75  LEU   B H    1 
ATOM   5130 H HA   . LEU   B 1 75  ? 40.886 -12.929 9.483   1.00 18.94 ?  75  LEU   B HA   1 
ATOM   5131 H HB2  . LEU   B 1 75  ? 42.130 -15.310 8.602   1.00 18.86 ?  75  LEU   B HB2  1 
ATOM   5132 H HB3  . LEU   B 1 75  ? 40.799 -14.748 7.955   1.00 18.86 ?  75  LEU   B HB3  1 
ATOM   5133 H HG   . LEU   B 1 75  ? 43.348 -13.574 7.728   1.00 21.16 ?  75  LEU   B HG   1 
ATOM   5134 H HD11 . LEU   B 1 75  ? 43.164 -13.999 5.449   1.00 23.17 ?  75  LEU   B HD11 1 
ATOM   5135 H HD12 . LEU   B 1 75  ? 43.064 -15.356 6.270   1.00 23.17 ?  75  LEU   B HD12 1 
ATOM   5136 H HD13 . LEU   B 1 75  ? 41.748 -14.680 5.689   1.00 23.17 ?  75  LEU   B HD13 1 
ATOM   5137 H HD21 . LEU   B 1 75  ? 42.307 -11.988 6.299   1.00 26.82 ?  75  LEU   B HD21 1 
ATOM   5138 H HD22 . LEU   B 1 75  ? 40.916 -12.483 6.888   1.00 26.82 ?  75  LEU   B HD22 1 
ATOM   5139 H HD23 . LEU   B 1 75  ? 41.984 -11.798 7.843   1.00 26.82 ?  75  LEU   B HD23 1 
ATOM   5140 N N    . LYS   B 1 76  ? 39.106 -14.719 9.988   1.00 18.48 ?  76  LYS   B N    1 
ATOM   5141 C CA   . LYS   B 1 76  ? 38.120 -15.668 10.480  1.00 19.70 ?  76  LYS   B CA   1 
ATOM   5142 C C    . LYS   B 1 76  ? 38.203 -16.941 9.648   1.00 17.45 ?  76  LYS   B C    1 
ATOM   5143 O O    . LYS   B 1 76  ? 38.473 -16.888 8.451   1.00 16.88 ?  76  LYS   B O    1 
ATOM   5144 C CB   . LYS   B 1 76  ? 36.706 -15.096 10.291  1.00 21.74 ?  76  LYS   B CB   1 
ATOM   5145 C CG   . LYS   B 1 76  ? 36.431 -13.715 10.894  1.00 23.97 ?  76  LYS   B CG   1 
ATOM   5146 C CD   . LYS   B 1 76  ? 34.995 -13.236 10.592  1.00 25.41 ?  76  LYS   B CD   1 
ATOM   5147 C CE   . LYS   B 1 76  ? 34.717 -11.856 11.183  1.00 27.81 ?  76  LYS   B CE   1 
ATOM   5148 N NZ   . LYS   B 1 76  ? 33.436 -11.229 10.746  1.00 27.66 ?  76  LYS   B NZ   1 
ATOM   5149 H H    . LYS   B 1 76  ? 38.821 -14.233 9.339   1.00 22.19 ?  76  LYS   B H    1 
ATOM   5150 H HA   . LYS   B 1 76  ? 38.272 -15.878 11.415  1.00 23.65 ?  76  LYS   B HA   1 
ATOM   5151 H HB2  . LYS   B 1 76  ? 36.532 -15.036 9.338   1.00 26.11 ?  76  LYS   B HB2  1 
ATOM   5152 H HB3  . LYS   B 1 76  ? 36.076 -15.715 10.692  1.00 26.11 ?  76  LYS   B HB3  1 
ATOM   5153 H HG2  . LYS   B 1 76  ? 36.550 -13.760 11.856  1.00 28.78 ?  76  LYS   B HG2  1 
ATOM   5154 H HG3  . LYS   B 1 76  ? 37.058 -13.075 10.512  1.00 28.78 ?  76  LYS   B HG3  1 
ATOM   5155 H HD2  . LYS   B 1 76  ? 34.876 -13.192 9.630   1.00 30.50 ?  76  LYS   B HD2  1 
ATOM   5156 H HD3  . LYS   B 1 76  ? 34.369 -13.869 10.978  1.00 30.50 ?  76  LYS   B HD3  1 
ATOM   5157 H HE2  . LYS   B 1 76  ? 34.695 -11.935 12.148  1.00 33.38 ?  76  LYS   B HE2  1 
ATOM   5158 H HE3  . LYS   B 1 76  ? 35.441 -11.262 10.922  1.00 33.38 ?  76  LYS   B HE3  1 
ATOM   5159 H HZ1  . LYS   B 1 76  ? 33.343 -10.427 11.128  1.00 33.21 ?  76  LYS   B HZ1  1 
ATOM   5160 H HZ2  . LYS   B 1 76  ? 33.429 -11.124 9.861   1.00 33.21 ?  76  LYS   B HZ2  1 
ATOM   5161 H HZ3  . LYS   B 1 76  ? 32.747 -11.739 10.981  1.00 33.21 ?  76  LYS   B HZ3  1 
ATOM   5162 N N    . VAL   B 1 77  ? 37.949 -18.093 10.279  1.00 18.14 ?  77  VAL   B N    1 
ATOM   5163 C CA   . VAL   B 1 77  ? 37.735 -19.302 9.490   1.00 18.13 ?  77  VAL   B CA   1 
ATOM   5164 C C    . VAL   B 1 77  ? 36.540 -19.065 8.576   1.00 16.98 ?  77  VAL   B C    1 
ATOM   5165 O O    . VAL   B 1 77  ? 35.474 -18.623 9.023   1.00 16.23 ?  77  VAL   B O    1 
ATOM   5166 C CB   . VAL   B 1 77  ? 37.529 -20.528 10.390  1.00 20.26 ?  77  VAL   B CB   1 
ATOM   5167 C CG1  . VAL   B 1 77  ? 37.275 -21.764 9.533   1.00 21.51 ?  77  VAL   B CG1  1 
ATOM   5168 C CG2  . VAL   B 1 77  ? 38.743 -20.744 11.292  1.00 21.95 ?  77  VAL   B CG2  1 
ATOM   5169 H H    . VAL   B 1 77  ? 37.902 -18.195 11.130  1.00 21.78 ?  77  VAL   B H    1 
ATOM   5170 H HA   . VAL   B 1 77  ? 38.512 -19.460 8.934   1.00 21.77 ?  77  VAL   B HA   1 
ATOM   5171 H HB   . VAL   B 1 77  ? 36.752 -20.386 10.953  1.00 24.33 ?  77  VAL   B HB   1 
ATOM   5172 H HG11 . VAL   B 1 77  ? 37.335 -22.552 10.094  1.00 25.83 ?  77  VAL   B HG11 1 
ATOM   5173 H HG12 . VAL   B 1 77  ? 36.386 -21.704 9.144   1.00 25.83 ?  77  VAL   B HG12 1 
ATOM   5174 H HG13 . VAL   B 1 77  ? 37.942 -21.804 8.832   1.00 25.83 ?  77  VAL   B HG13 1 
ATOM   5175 H HG21 . VAL   B 1 77  ? 38.609 -21.553 11.808  1.00 26.35 ?  77  VAL   B HG21 1 
ATOM   5176 H HG22 . VAL   B 1 77  ? 39.533 -20.825 10.740  1.00 26.35 ?  77  VAL   B HG22 1 
ATOM   5177 H HG23 . VAL   B 1 77  ? 38.828 -19.982 11.888  1.00 26.35 ?  77  VAL   B HG23 1 
ATOM   5178 N N    . GLY   B 1 78  ? 36.715 -19.353 7.285   1.00 16.07 ?  78  GLY   B N    1 
ATOM   5179 C CA   . GLY   B 1 78  ? 35.734 -19.033 6.273   1.00 16.06 ?  78  GLY   B CA   1 
ATOM   5180 C C    . GLY   B 1 78  ? 35.983 -17.724 5.559   1.00 15.75 ?  78  GLY   B C    1 
ATOM   5181 O O    . GLY   B 1 78  ? 35.309 -17.447 4.565   1.00 15.67 ?  78  GLY   B O    1 
ATOM   5182 H H    . GLY   B 1 78  ? 37.408 -19.763 6.977   1.00 19.30 ?  78  GLY   B H    1 
ATOM   5183 H HA2  . GLY   B 1 78  ? 35.713 -19.743 5.617   1.00 19.29 ?  78  GLY   B HA2  1 
ATOM   5184 H HA3  . GLY   B 1 78  ? 34.854 -18.989 6.694   1.00 19.29 ?  78  GLY   B HA3  1 
ATOM   5185 N N    . GLY   B 1 79  ? 36.938 -16.922 6.033   1.00 15.60 ?  79  GLY   B N    1 
ATOM   5186 C CA   . GLY   B 1 79  ? 37.239 -15.635 5.441   1.00 15.53 ?  79  GLY   B CA   1 
ATOM   5187 C C    . GLY   B 1 79  ? 38.483 -15.652 4.562   1.00 14.81 ?  79  GLY   B C    1 
ATOM   5188 O O    . GLY   B 1 79  ? 39.115 -16.677 4.334   1.00 15.52 ?  79  GLY   B O    1 
ATOM   5189 H H    . GLY   B 1 79  ? 37.440 -17.116 6.702   1.00 18.73 ?  79  GLY   B H    1 
ATOM   5190 H HA2  . GLY   B 1 79  ? 36.488 -15.349 4.893   1.00 18.66 ?  79  GLY   B HA2  1 
ATOM   5191 H HA3  . GLY   B 1 79  ? 37.373 -14.983 6.140   1.00 18.66 ?  79  GLY   B HA3  1 
ATOM   5192 N N    . SER   B 1 80  ? 38.853 -14.466 4.083   1.00 15.08 ?  80  SER   B N    1 
ATOM   5193 C CA   . SER   B 1 80  ? 39.969 -14.334 3.154   1.00 14.67 ?  80  SER   B CA   1 
ATOM   5194 C C    . SER   B 1 80  ? 40.549 -12.924 3.211   1.00 14.75 ?  80  SER   B C    1 
ATOM   5195 O O    . SER   B 1 80  ? 39.932 -11.993 3.734   1.00 15.82 ?  80  SER   B O    1 
ATOM   5196 C CB   . SER   B 1 80  ? 39.532 -14.643 1.721   1.00 14.58 ?  80  SER   B CB   1 
ATOM   5197 O OG   . SER   B 1 80  ? 38.689 -13.612 1.215   1.00 15.36 ?  80  SER   B OG   1 
ATOM   5198 H H    . SER   B 1 80  ? 38.483 -13.719 4.292   1.00 18.11 ?  80  SER   B H    1 
ATOM   5199 H HA   . SER   B 1 80  ? 40.663 -14.955 3.409   1.00 17.62 ?  80  SER   B HA   1 
ATOM   5200 H HB2  . SER   B 1 80  ? 40.318 -14.695 1.152   1.00 17.51 ?  80  SER   B HB2  1 
ATOM   5201 H HB3  . SER   B 1 80  ? 39.055 -15.482 1.709   1.00 17.51 ?  80  SER   B HB3  1 
ATOM   5202 H HG   . SER   B 1 80  ? 37.985 -13.556 1.688   1.00 18.45 ?  80  SER   B HG   1 
ATOM   5203 N N    . CYS   B 1 81  ? 41.736 -12.774 2.625   1.00 14.31 ?  81  CYS   B N    1 
ATOM   5204 C CA   . CYS   B 1 81  ? 42.282 -11.461 2.309   1.00 13.94 ?  81  CYS   B CA   1 
ATOM   5205 C C    . CYS   B 1 81  ? 43.056 -11.555 1.007   1.00 14.04 ?  81  CYS   B C    1 
ATOM   5206 O O    . CYS   B 1 81  ? 43.572 -12.615 0.644   1.00 14.60 ?  81  CYS   B O    1 
ATOM   5207 C CB   . CYS   B 1 81  ? 43.169 -10.906 3.419   1.00 15.07 ?  81  CYS   B CB   1 
ATOM   5208 S SG   . CYS   B 1 81  ? 44.689 -11.854 3.694   1.00 15.63 ?  81  CYS   B SG   1 
ATOM   5209 H H    . CYS   B 1 81  ? 42.251 -13.424 2.401   1.00 17.18 ?  81  CYS   B H    1 
ATOM   5210 H HA   . CYS   B 1 81  ? 41.545 -10.837 2.174   1.00 16.75 ?  81  CYS   B HA   1 
ATOM   5211 H HB2  . CYS   B 1 81  ? 43.429 -9.996  3.190   1.00 18.10 ?  81  CYS   B HB2  1 
ATOM   5212 H HB3  . CYS   B 1 81  ? 42.663 -10.895 4.250   1.00 18.10 ?  81  CYS   B HB3  1 
ATOM   5213 H HG   . CYS   B 1 81  ? 45.308 -11.340 4.595   1.00 18.77 ?  81  CYS   B HG   1 
ATOM   5214 N N    . VAL   B 1 82  ? 43.152 -10.426 0.315   1.00 13.59 ?  82  VAL   B N    1 
ATOM   5215 C CA   . VAL   B 1 82  ? 43.914 -10.307 -0.925  1.00 13.63 ?  82  VAL   B CA   1 
ATOM   5216 C C    . VAL   B 1 82  ? 45.255 -9.661  -0.602  1.00 14.41 ?  82  VAL   B C    1 
ATOM   5217 O O    . VAL   B 1 82  ? 45.298 -8.549  -0.057  1.00 15.40 ?  82  VAL   B O    1 
ATOM   5218 C CB   . VAL   B 1 82  ? 43.156 -9.462  -1.962  1.00 14.89 ?  82  VAL   B CB   1 
ATOM   5219 C CG1  . VAL   B 1 82  ? 43.972 -9.329  -3.237  1.00 16.60 ?  82  VAL   B CG1  1 
ATOM   5220 C CG2  . VAL   B 1 82  ? 41.782 -10.052 -2.249  1.00 16.23 ?  82  VAL   B CG2  1 
ATOM   5221 H H    . VAL   B 1 82  ? 42.778 -9.684  0.548   1.00 16.32 ?  82  VAL   B H    1 
ATOM   5222 H HA   . VAL   B 1 82  ? 44.077 -11.189 -1.296  1.00 16.38 ?  82  VAL   B HA   1 
ATOM   5223 H HB   . VAL   B 1 82  ? 43.036 -8.569  -1.603  1.00 17.89 ?  82  VAL   B HB   1 
ATOM   5224 H HG11 . VAL   B 1 82  ? 43.405 -8.969  -3.936  1.00 19.93 ?  82  VAL   B HG11 1 
ATOM   5225 H HG12 . VAL   B 1 82  ? 44.722 -8.733  -3.081  1.00 19.93 ?  82  VAL   B HG12 1 
ATOM   5226 H HG13 . VAL   B 1 82  ? 44.297 -10.207 -3.497  1.00 19.93 ?  82  VAL   B HG13 1 
ATOM   5227 H HG21 . VAL   B 1 82  ? 41.351 -9.523  -2.942  1.00 19.49 ?  82  VAL   B HG21 1 
ATOM   5228 H HG22 . VAL   B 1 82  ? 41.884 -10.967 -2.548  1.00 19.49 ?  82  VAL   B HG22 1 
ATOM   5229 H HG23 . VAL   B 1 82  ? 41.250 -10.024 -1.438  1.00 19.49 ?  82  VAL   B HG23 1 
ATOM   5230 N N    . LEU   B 1 83  ? 46.343 -10.348 -0.949  1.00 14.27 ?  83  LEU   B N    1 
ATOM   5231 C CA   . LEU   B 1 83  ? 47.699 -9.821  -0.830  1.00 14.13 ?  83  LEU   B CA   1 
ATOM   5232 C C    . LEU   B 1 83  ? 48.408 -9.977  -2.178  1.00 14.03 ?  83  LEU   B C    1 
ATOM   5233 O O    . LEU   B 1 83  ? 47.804 -10.393 -3.172  1.00 14.30 ?  83  LEU   B O    1 
ATOM   5234 C CB   . LEU   B 1 83  ? 48.453 -10.495 0.325   1.00 15.48 ?  83  LEU   B CB   1 
ATOM   5235 C CG   . LEU   B 1 83  ? 47.941 -10.130 1.723   1.00 16.16 ?  83  LEU   B CG   1 
ATOM   5236 C CD1  . LEU   B 1 83  ? 48.540 -11.018 2.790   1.00 16.20 ?  83  LEU   B CD1  1 
ATOM   5237 C CD2  . LEU   B 1 83  ? 48.192 -8.663  2.074   1.00 16.69 ?  83  LEU   B CD2  1 
ATOM   5238 H H    . LEU   B 1 83  ? 46.319 -11.148 -1.269  1.00 17.14 ?  83  LEU   B H    1 
ATOM   5239 H HA   . LEU   B 1 83  ? 47.646 -8.873  -0.635  1.00 16.97 ?  83  LEU   B HA   1 
ATOM   5240 H HB2  . LEU   B 1 83  ? 48.380 -11.454 0.227   1.00 18.59 ?  83  LEU   B HB2  1 
ATOM   5241 H HB3  . LEU   B 1 83  ? 49.387 -10.232 0.280   1.00 18.59 ?  83  LEU   B HB3  1 
ATOM   5242 H HG   . LEU   B 1 83  ? 46.981 -10.269 1.739   1.00 19.41 ?  83  LEU   B HG   1 
ATOM   5243 H HD11 . LEU   B 1 83  ? 48.184 -10.762 3.655   1.00 19.45 ?  83  LEU   B HD11 1 
ATOM   5244 H HD12 . LEU   B 1 83  ? 48.301 -11.944 2.599   1.00 19.45 ?  83  LEU   B HD12 1 
ATOM   5245 H HD13 . LEU   B 1 83  ? 49.503 -10.921 2.783   1.00 19.45 ?  83  LEU   B HD13 1 
ATOM   5246 H HD21 . LEU   B 1 83  ? 47.938 -8.506  3.001   1.00 20.05 ?  83  LEU   B HD21 1 
ATOM   5247 H HD22 . LEU   B 1 83  ? 49.132 -8.458  1.953   1.00 20.05 ?  83  LEU   B HD22 1 
ATOM   5248 H HD23 . LEU   B 1 83  ? 47.655 -8.096  1.492   1.00 20.05 ?  83  LEU   B HD23 1 
ATOM   5249 N N    . SER   B 1 84  ? 49.687 -9.601  -2.236  1.00 14.74 ?  84  SER   B N    1 
ATOM   5250 C CA   . SER   B 1 84  ? 50.414 -9.721  -3.488  1.00 14.65 ?  84  SER   B CA   1 
ATOM   5251 C C    . SER   B 1 84  ? 50.569 -11.183 -3.908  1.00 13.96 ?  84  SER   B C    1 
ATOM   5252 O O    . SER   B 1 84  ? 50.692 -12.081 -3.082  1.00 13.96 ?  84  SER   B O    1 
ATOM   5253 C CB   . SER   B 1 84  ? 51.807 -9.105  -3.346  1.00 17.39 ?  84  SER   B CB   1 
ATOM   5254 O OG   . SER   B 1 84  ? 52.553 -9.329  -4.523  1.00 19.46 ?  84  SER   B OG   1 
ATOM   5255 H H    . SER   B 1 84  ? 50.137 -9.268  -1.583  1.00 17.70 ?  84  SER   B H    1 
ATOM   5256 H HA   . SER   B 1 84  ? 49.938 -9.256  -4.190  1.00 17.60 ?  84  SER   B HA   1 
ATOM   5257 H HB2  . SER   B 1 84  ? 51.717 -8.148  -3.196  1.00 20.88 ?  84  SER   B HB2  1 
ATOM   5258 H HB3  . SER   B 1 84  ? 52.268 -9.516  -2.600  1.00 20.88 ?  84  SER   B HB3  1 
ATOM   5259 H HG   . SER   B 1 84  ? 53.326 -8.969  -4.446  1.00 23.37 ?  84  SER   B HG   1 
ATOM   5260 N N    . GLY   B 1 85  ? 50.626 -11.403 -5.218  1.00 14.63 ?  85  GLY   B N    1 
ATOM   5261 C CA   . GLY   B 1 85  ? 50.971 -12.698 -5.757  1.00 15.30 ?  85  GLY   B CA   1 
ATOM   5262 C C    . GLY   B 1 85  ? 52.438 -12.895 -6.062  1.00 14.75 ?  85  GLY   B C    1 
ATOM   5263 O O    . GLY   B 1 85  ? 52.810 -13.982 -6.515  1.00 15.59 ?  85  GLY   B O    1 
ATOM   5264 H H    . GLY   B 1 85  ? 50.453 -10.821 -5.810  1.00 17.57 ?  85  GLY   B H    1 
ATOM   5265 H HA2  . GLY   B 1 85  ? 50.699 -13.393 -5.128  1.00 18.37 ?  85  GLY   B HA2  1 
ATOM   5266 H HA3  . GLY   B 1 85  ? 50.476 -12.842 -6.577  1.00 18.37 ?  85  GLY   B HA3  1 
ATOM   5267 N N    . HIS   B 1 86  ? 53.289 -11.892 -5.831  1.00 14.64 ?  86  HIS   B N    1 
ATOM   5268 C CA   . HIS   B 1 86  ? 54.752 -12.054 -5.905  1.00 15.29 ?  86  HIS   B CA   1 
ATOM   5269 C C    . HIS   B 1 86  ? 55.123 -12.563 -7.295  1.00 15.84 ?  86  HIS   B C    1 
ATOM   5270 O O    . HIS   B 1 86  ? 54.741 -11.935 -8.296  1.00 17.06 ?  86  HIS   B O    1 
ATOM   5271 C CB   . HIS   B 1 86  ? 55.255 -12.892 -4.730  1.00 15.63 ?  86  HIS   B CB   1 
ATOM   5272 C CG   . HIS   B 1 86  ? 54.932 -12.297 -3.407  1.00 14.89 ?  86  HIS   B CG   1 
ATOM   5273 N ND1  . HIS   B 1 86  ? 55.742 -11.363 -2.798  1.00 17.23 ?  86  HIS   B ND1  1 
ATOM   5274 C CD2  . HIS   B 1 86  ? 53.863 -12.460 -2.594  1.00 15.60 ?  86  HIS   B CD2  1 
ATOM   5275 C CE1  . HIS   B 1 86  ? 55.180 -10.974 -1.667  1.00 17.34 ?  86  HIS   B CE1  1 
ATOM   5276 N NE2  . HIS   B 1 86  ? 54.038 -11.624 -1.522  1.00 16.26 ?  86  HIS   B NE2  1 
ATOM   5277 H H    . HIS   B 1 86  ? 53.039 -11.093 -5.644  1.00 17.58 ?  86  HIS   B H    1 
ATOM   5278 H HA   . HIS   B 1 86  ? 55.155 -11.177 -5.809  1.00 18.36 ?  86  HIS   B HA   1 
ATOM   5279 H HB2  . HIS   B 1 86  ? 54.848 -13.773 -4.773  1.00 18.77 ?  86  HIS   B HB2  1 
ATOM   5280 H HB3  . HIS   B 1 86  ? 56.221 -12.974 -4.788  1.00 18.77 ?  86  HIS   B HB3  1 
ATOM   5281 H HD2  . HIS   B 1 86  ? 53.130 -13.021 -2.745  1.00 18.74 ?  86  HIS   B HD2  1 
ATOM   5282 H HE1  . HIS   B 1 86  ? 55.530 -10.362 -1.065  1.00 20.82 ?  86  HIS   B HE1  1 
ATOM   5283 H HE2  . HIS   B 1 86  ? 53.494 -11.553 -0.850  1.00 19.53 ?  86  HIS   B HE2  1 
ATOM   5284 N N    . ASN   B 1 87  ? 55.896 -13.641 -7.408  1.00 16.14 ?  87  ASN   B N    1 
ATOM   5285 C CA   . ASN   B 1 87  ? 56.272 -14.215 -8.691  1.00 16.48 ?  87  ASN   B CA   1 
ATOM   5286 C C    . ASN   B 1 87  ? 55.288 -15.260 -9.184  1.00 16.25 ?  87  ASN   B C    1 
ATOM   5287 O O    . ASN   B 1 87  ? 55.599 -15.968 -10.145 1.00 18.14 ?  87  ASN   B O    1 
ATOM   5288 C CB   . ASN   B 1 87  ? 57.662 -14.847 -8.585  1.00 18.52 ?  87  ASN   B CB   1 
ATOM   5289 C CG   . ASN   B 1 87  ? 57.727 -15.960 -7.542  1.00 19.48 ?  87  ASN   B CG   1 
ATOM   5290 O OD1  . ASN   B 1 87  ? 57.112 -15.871 -6.472  1.00 18.08 ?  87  ASN   B OD1  1 
ATOM   5291 N ND2  . ASN   B 1 87  ? 58.466 -17.032 -7.863  1.00 23.05 ?  87  ASN   B ND2  1 
ATOM   5292 H H    . ASN   B 1 87  ? 56.231 -14.064 -6.735  1.00 19.38 ?  87  ASN   B H    1 
ATOM   5293 H HA   . ASN   B 1 87  ? 56.318 -13.511 -9.350  1.00 19.79 ?  87  ASN   B HA   1 
ATOM   5294 H HB2  . ASN   B 1 87  ? 57.903 -15.228 -9.451  1.00 22.24 ?  87  ASN   B HB2  1 
ATOM   5295 H HB3  . ASN   B 1 87  ? 58.306 -14.165 -8.340  1.00 22.24 ?  87  ASN   B HB3  1 
ATOM   5296 H HD21 . ASN   B 1 87  ? 58.536 -17.685 -7.311  1.00 27.67 ?  87  ASN   B HD21 1 
ATOM   5297 H HD22 . ASN   B 1 87  ? 58.881 -17.063 -8.620  1.00 27.67 ?  87  ASN   B HD22 1 
ATOM   5298 N N    . LEU   B 1 88  ? 54.120 -15.371 -8.551  1.00 15.14 ?  88  LEU   B N    1 
ATOM   5299 C CA   . LEU   B 1 88  ? 53.142 -16.403 -8.883  1.00 15.44 ?  88  LEU   B CA   1 
ATOM   5300 C C    . LEU   B 1 88  ? 51.917 -15.888 -9.614  1.00 15.27 ?  88  LEU   B C    1 
ATOM   5301 O O    . LEU   B 1 88  ? 51.328 -16.627 -10.409 1.00 16.26 ?  88  LEU   B O    1 
ATOM   5302 C CB   . LEU   B 1 88  ? 52.656 -17.089 -7.605  1.00 16.93 ?  88  LEU   B CB   1 
ATOM   5303 C CG   . LEU   B 1 88  ? 53.780 -17.702 -6.787  1.00 19.14 ?  88  LEU   B CG   1 
ATOM   5304 C CD1  . LEU   B 1 88  ? 53.277 -18.146 -5.424  1.00 20.50 ?  88  LEU   B CD1  1 
ATOM   5305 C CD2  . LEU   B 1 88  ? 54.410 -18.853 -7.546  1.00 23.76 ?  88  LEU   B CD2  1 
ATOM   5306 H H    . LEU   B 1 88  ? 53.871 -14.857 -7.895  1.00 18.19 ?  88  LEU   B H    1 
ATOM   5307 H HA   . LEU   B 1 88  ? 53.562 -17.069 -9.437  1.00 18.54 ?  88  LEU   B HA   1 
ATOM   5308 H HB2  . LEU   B 1 88  ? 52.200 -16.446 -7.040  1.00 20.33 ?  88  LEU   B HB2  1 
ATOM   5309 H HB3  . LEU   B 1 88  ? 52.040 -17.807 -7.842  1.00 20.33 ?  88  LEU   B HB3  1 
ATOM   5310 H HG   . LEU   B 1 88  ? 54.466 -17.035 -6.641  1.00 22.99 ?  88  LEU   B HG   1 
ATOM   5311 H HD11 . LEU   B 1 88  ? 53.968 -18.668 -4.980  1.00 24.62 ?  88  LEU   B HD11 1 
ATOM   5312 H HD12 . LEU   B 1 88  ? 53.062 -17.365 -4.893  1.00 24.62 ?  88  LEU   B HD12 1 
ATOM   5313 H HD13 . LEU   B 1 88  ? 52.483 -18.693 -5.544  1.00 24.62 ?  88  LEU   B HD13 1 
ATOM   5314 H HD21 . LEU   B 1 88  ? 55.019 -19.325 -6.958  1.00 28.53 ?  88  LEU   B HD21 1 
ATOM   5315 H HD22 . LEU   B 1 88  ? 53.711 -19.451 -7.851  1.00 28.53 ?  88  LEU   B HD22 1 
ATOM   5316 H HD23 . LEU   B 1 88  ? 54.896 -18.498 -8.308  1.00 28.53 ?  88  LEU   B HD23 1 
ATOM   5317 N N    . ALA   B 1 89  ? 51.508 -14.655 -9.349  1.00 14.76 ?  89  ALA   B N    1 
ATOM   5318 C CA   . ALA   B 1 89  ? 50.218 -14.159 -9.811  1.00 14.37 ?  89  ALA   B CA   1 
ATOM   5319 C C    . ALA   B 1 89  ? 50.191 -12.667 -9.533  1.00 15.17 ?  89  ALA   B C    1 
ATOM   5320 O O    . ALA   B 1 89  ? 51.012 -12.149 -8.777  1.00 15.72 ?  89  ALA   B O    1 
ATOM   5321 C CB   . ALA   B 1 89  ? 49.078 -14.831 -9.053  1.00 14.20 ?  89  ALA   B CB   1 
ATOM   5322 H H    . ALA   B 1 89  ? 51.958 -14.073 -8.897  1.00 17.72 ?  89  ALA   B H    1 
ATOM   5323 H HA   . ALA   B 1 89  ? 50.115 -14.312 -10.764 1.00 17.26 ?  89  ALA   B HA   1 
ATOM   5324 H HB1  . ALA   B 1 89  ? 48.232 -14.498 -9.395  1.00 17.06 ?  89  ALA   B HB1  1 
ATOM   5325 H HB2  . ALA   B 1 89  ? 49.133 -15.790 -9.190  1.00 17.06 ?  89  ALA   B HB2  1 
ATOM   5326 H HB3  . ALA   B 1 89  ? 49.160 -14.624 -8.112  1.00 17.06 ?  89  ALA   B HB3  1 
ATOM   5327 N N    . LYS   B 1 90  ? 49.208 -11.978 -10.102 1.00 15.67 ?  90  LYS   B N    1 
ATOM   5328 C CA   . LYS   B 1 90  ? 49.013 -10.592 -9.689  1.00 15.60 ?  90  LYS   B CA   1 
ATOM   5329 C C    . LYS   B 1 90  ? 48.695 -10.523 -8.197  1.00 15.74 ?  90  LYS   B C    1 
ATOM   5330 O O    . LYS   B 1 90  ? 49.337 -9.780  -7.442  1.00 16.76 ?  90  LYS   B O    1 
ATOM   5331 C CB   . LYS   B 1 90  ? 47.921 -9.927  -10.526 1.00 17.28 ?  90  LYS   B CB   1 
ATOM   5332 C CG   . LYS   B 1 90  ? 47.657 -8.470  -10.151 1.00 17.63 ?  90  LYS   B CG   1 
ATOM   5333 C CD   . LYS   B 1 90  ? 48.859 -7.591  -10.292 1.00 22.09 ?  90  LYS   B CD   1 
ATOM   5334 C CE   . LYS   B 1 90  ? 48.459 -6.147  -10.047 1.00 24.69 ?  90  LYS   B CE   1 
ATOM   5335 N NZ   . LYS   B 1 90  ? 49.674 -5.308  -9.920  1.00 24.13 ?  90  LYS   B NZ   1 
ATOM   5336 H H    . LYS   B 1 90  ? 48.664 -12.271 -10.702 1.00 18.82 ?  90  LYS   B H    1 
ATOM   5337 H HA   . LYS   B 1 90  ? 49.834 -10.102 -9.836  1.00 18.73 ?  90  LYS   B HA   1 
ATOM   5338 H HB2  . LYS   B 1 90  ? 48.187 -9.945  -11.461 1.00 20.75 ?  90  LYS   B HB2  1 
ATOM   5339 H HB3  . LYS   B 1 90  ? 47.091 -10.419 -10.415 1.00 20.75 ?  90  LYS   B HB3  1 
ATOM   5340 H HG2  . LYS   B 1 90  ? 46.958 -8.123  -10.733 1.00 21.17 ?  90  LYS   B HG2  1 
ATOM   5341 H HG3  . LYS   B 1 90  ? 47.354 -8.434  -9.228  1.00 21.17 ?  90  LYS   B HG3  1 
ATOM   5342 H HD2  . LYS   B 1 90  ? 49.525 -7.841  -9.632  1.00 26.52 ?  90  LYS   B HD2  1 
ATOM   5343 H HD3  . LYS   B 1 90  ? 49.217 -7.667  -11.188 1.00 26.52 ?  90  LYS   B HD3  1 
ATOM   5344 H HE2  . LYS   B 1 90  ? 47.936 -5.816  -10.797 1.00 29.64 ?  90  LYS   B HE2  1 
ATOM   5345 H HE3  . LYS   B 1 90  ? 47.950 -6.076  -9.223  1.00 29.64 ?  90  LYS   B HE3  1 
ATOM   5346 H HZ1  . LYS   B 1 90  ? 49.450 -4.458  -9.778  1.00 28.97 ?  90  LYS   B HZ1  1 
ATOM   5347 H HZ2  . LYS   B 1 90  ? 50.170 -5.593  -9.237  1.00 28.97 ?  90  LYS   B HZ2  1 
ATOM   5348 H HZ3  . LYS   B 1 90  ? 50.158 -5.357  -10.667 1.00 28.97 ?  90  LYS   B HZ3  1 
ATOM   5349 N N    . HIS   B 1 91  ? 47.728 -11.317 -7.746  1.00 14.06 ?  91  HIS   B N    1 
ATOM   5350 C CA   . HIS   B 1 91  ? 47.287 -11.327 -6.363  1.00 14.65 ?  91  HIS   B CA   1 
ATOM   5351 C C    . HIS   B 1 91  ? 47.280 -12.755 -5.847  1.00 13.57 ?  91  HIS   B C    1 
ATOM   5352 O O    . HIS   B 1 91  ? 47.040 -13.703 -6.608  1.00 13.70 ?  91  HIS   B O    1 
ATOM   5353 C CB   . HIS   B 1 91  ? 45.828 -10.860 -6.236  1.00 16.03 ?  91  HIS   B CB   1 
ATOM   5354 C CG   . HIS   B 1 91  ? 45.593 -9.468  -6.710  1.00 18.72 ?  91  HIS   B CG   1 
ATOM   5355 N ND1  . HIS   B 1 91  ? 46.158 -8.370  -6.098  1.00 22.37 ?  91  HIS   B ND1  1 
ATOM   5356 C CD2  . HIS   B 1 91  ? 44.831 -8.989  -7.718  1.00 21.61 ?  91  HIS   B CD2  1 
ATOM   5357 C CE1  . HIS   B 1 91  ? 45.769 -7.273  -6.723  1.00 23.39 ?  91  HIS   B CE1  1 
ATOM   5358 N NE2  . HIS   B 1 91  ? 44.958 -7.621  -7.706  1.00 23.41 ?  91  HIS   B NE2  1 
ATOM   5359 H H    . HIS   B 1 91  ? 47.298 -11.883 -8.240  1.00 16.88 ?  91  HIS   B H    1 
ATOM   5360 H HA   . HIS   B 1 91  ? 47.860 -10.777 -5.808  1.00 17.60 ?  91  HIS   B HA   1 
ATOM   5361 H HB2  . HIS   B 1 91  ? 45.261 -11.447 -6.759  1.00 19.25 ?  91  HIS   B HB2  1 
ATOM   5362 H HB3  . HIS   B 1 91  ? 45.566 -10.900 -5.300  1.00 19.25 ?  91  HIS   B HB3  1 
ATOM   5363 H HD1  . HIS   B 1 91  ? 46.691 -8.392  -5.421  1.00 26.86 ?  91  HIS   B HD1  1 
ATOM   5364 H HD2  . HIS   B 1 91  ? 44.325 -9.483  -8.316  1.00 25.94 ?  91  HIS   B HD2  1 
ATOM   5365 H HE1  . HIS   B 1 91  ? 46.021 -6.400  -6.503  1.00 28.09 ?  91  HIS   B HE1  1 
ATOM   5366 N N    . CYS   B 1 92  ? 47.471 -12.897 -4.543  1.00 13.54 ?  92  CYS   B N    1 
ATOM   5367 C CA   . CYS   B 1 92  ? 47.160 -14.136 -3.836  1.00 12.92 ?  92  CYS   B CA   1 
ATOM   5368 C C    . CYS   B 1 92  ? 45.942 -13.909 -2.950  1.00 12.72 ?  92  CYS   B C    1 
ATOM   5369 O O    . CYS   B 1 92  ? 45.930 -12.998 -2.114  1.00 13.55 ?  92  CYS   B O    1 
ATOM   5370 C CB   . CYS   B 1 92  ? 48.337 -14.583 -2.978  1.00 13.36 ?  92  CYS   B CB   1 
ATOM   5371 S SG   . CYS   B 1 92  ? 47.978 -16.128 -2.067  1.00 14.09 ?  92  CYS   B SG   1 
ATOM   5372 H H    . CYS   B 1 92  ? 47.799 -12.283 -4.039  1.00 16.26 ?  92  CYS   B H    1 
ATOM   5373 H HA   . CYS   B 1 92  ? 46.962 -14.837 -4.483  1.00 15.52 ?  92  CYS   B HA   1 
ATOM   5374 H HB2  . CYS   B 1 92  ? 49.108 -14.737 -3.545  1.00 16.04 ?  92  CYS   B HB2  1 
ATOM   5375 H HB3  . CYS   B 1 92  ? 48.532 -13.893 -2.327  1.00 16.04 ?  92  CYS   B HB3  1 
ATOM   5376 H HG   . CYS   B 1 92  ? 48.952 -16.431 -1.436  1.00 16.93 ?  92  CYS   B HG   1 
ATOM   5377 N N    . LEU   B 1 93  ? 44.907 -14.715 -3.156  1.00 12.58 ?  93  LEU   B N    1 
ATOM   5378 C CA   . LEU   B 1 93  ? 43.733 -14.718 -2.297  1.00 13.16 ?  93  LEU   B CA   1 
ATOM   5379 C C    . LEU   B 1 93  ? 43.946 -15.781 -1.229  1.00 12.32 ?  93  LEU   B C    1 
ATOM   5380 O O    . LEU   B 1 93  ? 43.895 -16.978 -1.522  1.00 13.47 ?  93  LEU   B O    1 
ATOM   5381 C CB   . LEU   B 1 93  ? 42.474 -15.006 -3.109  1.00 13.23 ?  93  LEU   B CB   1 
ATOM   5382 C CG   . LEU   B 1 93  ? 41.169 -15.041 -2.302  1.00 14.45 ?  93  LEU   B CG   1 
ATOM   5383 C CD1  . LEU   B 1 93  ? 40.782 -13.666 -1.804  1.00 14.99 ?  93  LEU   B CD1  1 
ATOM   5384 C CD2  . LEU   B 1 93  ? 40.034 -15.649 -3.106  1.00 14.36 ?  93  LEU   B CD2  1 
ATOM   5385 H H    . LEU   B 1 93  ? 44.862 -15.282 -3.811  1.00 15.11 ?  93  LEU   B H    1 
ATOM   5386 H HA   . LEU   B 1 93  ? 43.645 -13.848 -1.876  1.00 15.80 ?  93  LEU   B HA   1 
ATOM   5387 H HB2  . LEU   B 1 93  ? 42.380 -14.312 -3.786  1.00 15.89 ?  93  LEU   B HB2  1 
ATOM   5388 H HB3  . LEU   B 1 93  ? 42.582 -15.864 -3.544  1.00 15.89 ?  93  LEU   B HB3  1 
ATOM   5389 H HG   . LEU   B 1 93  ? 41.310 -15.607 -1.528  1.00 17.35 ?  93  LEU   B HG   1 
ATOM   5390 H HD11 . LEU   B 1 93  ? 39.940 -13.737 -1.327  1.00 18.00 ?  93  LEU   B HD11 1 
ATOM   5391 H HD12 . LEU   B 1 93  ? 41.473 -13.337 -1.215  1.00 18.00 ?  93  LEU   B HD12 1 
ATOM   5392 H HD13 . LEU   B 1 93  ? 40.680 -13.074 -2.567  1.00 18.00 ?  93  LEU   B HD13 1 
ATOM   5393 H HD21 . LEU   B 1 93  ? 39.231 -15.658 -2.560  1.00 17.24 ?  93  LEU   B HD21 1 
ATOM   5394 H HD22 . LEU   B 1 93  ? 39.884 -15.116 -3.903  1.00 17.24 ?  93  LEU   B HD22 1 
ATOM   5395 H HD23 . LEU   B 1 93  ? 40.268 -16.559 -3.359  1.00 17.24 ?  93  LEU   B HD23 1 
ATOM   5396 N N    . HIS   B 1 94  ? 44.226 -15.346 -0.006  1.00 12.57 ?  94  HIS   B N    1 
ATOM   5397 C CA   . HIS   B 1 94  ? 44.457 -16.248 1.119   1.00 12.29 ?  94  HIS   B CA   1 
ATOM   5398 C C    . HIS   B 1 94  ? 43.091 -16.592 1.706   1.00 13.50 ?  94  HIS   B C    1 
ATOM   5399 O O    . HIS   B 1 94  ? 42.427 -15.723 2.275   1.00 14.66 ?  94  HIS   B O    1 
ATOM   5400 C CB   . HIS   B 1 94  ? 45.331 -15.567 2.173   1.00 13.59 ?  94  HIS   B CB   1 
ATOM   5401 C CG   . HIS   B 1 94  ? 46.718 -15.255 1.702   1.00 13.49 ?  94  HIS   B CG   1 
ATOM   5402 N ND1  . HIS   B 1 94  ? 47.743 -16.169 1.782   1.00 13.69 ?  94  HIS   B ND1  1 
ATOM   5403 C CD2  . HIS   B 1 94  ? 47.241 -14.143 1.126   1.00 13.55 ?  94  HIS   B CD2  1 
ATOM   5404 C CE1  . HIS   B 1 94  ? 48.844 -15.621 1.295   1.00 13.56 ?  94  HIS   B CE1  1 
ATOM   5405 N NE2  . HIS   B 1 94  ? 48.564 -14.402 0.873   1.00 13.79 ?  94  HIS   B NE2  1 
ATOM   5406 H H    . HIS   B 1 94  ? 44.292 -14.507 0.201   1.00 15.10 ?  94  HIS   B H    1 
ATOM   5407 H HA   . HIS   B 1 94  ? 44.892 -17.059 0.808   1.00 14.77 ?  94  HIS   B HA   1 
ATOM   5408 H HB2  . HIS   B 1 94  ? 44.911 -14.736 2.434   1.00 16.32 ?  94  HIS   B HB2  1 
ATOM   5409 H HB3  . HIS   B 1 94  ? 45.407 -16.157 2.936   1.00 16.32 ?  94  HIS   B HB3  1 
ATOM   5410 H HD2  . HIS   B 1 94  ? 46.792 -13.350 0.932   1.00 16.28 ?  94  HIS   B HD2  1 
ATOM   5411 H HE1  . HIS   B 1 94  ? 49.676 -16.040 1.232   1.00 16.29 ?  94  HIS   B HE1  1 
ATOM   5412 H HE2  . HIS   B 1 94  ? 49.131 -13.851 0.521   1.00 16.56 ?  94  HIS   B HE2  1 
ATOM   5413 N N    . VAL   B 1 95  ? 42.650 -17.842 1.548   1.00 12.84 ?  95  VAL   B N    1 
ATOM   5414 C CA   . VAL   B 1 95  ? 41.321 -18.286 1.986   1.00 13.17 ?  95  VAL   B CA   1 
ATOM   5415 C C    . VAL   B 1 95  ? 41.480 -19.323 3.092   1.00 13.18 ?  95  VAL   B C    1 
ATOM   5416 O O    . VAL   B 1 95  ? 42.263 -20.269 2.946   1.00 13.84 ?  95  VAL   B O    1 
ATOM   5417 C CB   . VAL   B 1 95  ? 40.499 -18.884 0.827   1.00 12.97 ?  95  VAL   B CB   1 
ATOM   5418 C CG1  . VAL   B 1 95  ? 39.124 -19.344 1.324   1.00 14.81 ?  95  VAL   B CG1  1 
ATOM   5419 C CG2  . VAL   B 1 95  ? 40.336 -17.887 -0.301  1.00 13.81 ?  95  VAL   B CG2  1 
ATOM   5420 H H    . VAL   B 1 95  ? 43.107 -18.465 1.170   1.00 15.42 ?  95  VAL   B H    1 
ATOM   5421 H HA   . VAL   B 1 95  ? 40.830 -17.528 2.346   1.00 15.82 ?  95  VAL   B HA   1 
ATOM   5422 H HB   . VAL   B 1 95  ? 40.966 -19.660 0.481   1.00 15.57 ?  95  VAL   B HB   1 
ATOM   5423 H HG11 . VAL   B 1 95  ? 38.559 -19.531 0.556   1.00 17.79 ?  95  VAL   B HG11 1 
ATOM   5424 H HG12 . VAL   B 1 95  ? 39.226 -20.148 1.858   1.00 17.79 ?  95  VAL   B HG12 1 
ATOM   5425 H HG13 . VAL   B 1 95  ? 38.727 -18.639 1.859   1.00 17.79 ?  95  VAL   B HG13 1 
ATOM   5426 H HG21 . VAL   B 1 95  ? 39.750 -18.267 -0.971  1.00 16.59 ?  95  VAL   B HG21 1 
ATOM   5427 H HG22 . VAL   B 1 95  ? 39.945 -17.073 0.058   1.00 16.59 ?  95  VAL   B HG22 1 
ATOM   5428 H HG23 . VAL   B 1 95  ? 41.205 -17.700 -0.679  1.00 16.59 ?  95  VAL   B HG23 1 
ATOM   5429 N N    . VAL   B 1 96  ? 40.732 -19.160 4.186   1.00 13.63 ?  96  VAL   B N    1 
ATOM   5430 C CA   . VAL   B 1 96  ? 40.820 -20.056 5.338   1.00 14.38 ?  96  VAL   B CA   1 
ATOM   5431 C C    . VAL   B 1 96  ? 39.635 -21.019 5.294   1.00 15.15 ?  96  VAL   B C    1 
ATOM   5432 O O    . VAL   B 1 96  ? 38.506 -20.658 5.653   1.00 15.47 ?  96  VAL   B O    1 
ATOM   5433 C CB   . VAL   B 1 96  ? 40.876 -19.298 6.666   1.00 15.05 ?  96  VAL   B CB   1 
ATOM   5434 C CG1  . VAL   B 1 96  ? 41.068 -20.276 7.815   1.00 16.28 ?  96  VAL   B CG1  1 
ATOM   5435 C CG2  . VAL   B 1 96  ? 41.982 -18.255 6.653   1.00 15.24 ?  96  VAL   B CG2  1 
ATOM   5436 H H    . VAL   B 1 96  ? 40.156 -18.523 4.282   1.00 16.37 ?  96  VAL   B H    1 
ATOM   5437 H HA   . VAL   B 1 96  ? 41.634 -20.580 5.263   1.00 17.27 ?  96  VAL   B HA   1 
ATOM   5438 H HB   . VAL   B 1 96  ? 40.032 -18.842 6.802   1.00 18.08 ?  96  VAL   B HB   1 
ATOM   5439 H HG11 . VAL   B 1 96  ? 41.256 -19.775 8.627   1.00 19.55 ?  96  VAL   B HG11 1 
ATOM   5440 H HG12 . VAL   B 1 96  ? 40.262 -20.799 7.930   1.00 19.55 ?  96  VAL   B HG12 1 
ATOM   5441 H HG13 . VAL   B 1 96  ? 41.818 -20.860 7.612   1.00 19.55 ?  96  VAL   B HG13 1 
ATOM   5442 H HG21 . VAL   B 1 96  ? 42.034 -17.834 7.528   1.00 18.30 ?  96  VAL   B HG21 1 
ATOM   5443 H HG22 . VAL   B 1 96  ? 42.822 -18.676 6.436   1.00 18.30 ?  96  VAL   B HG22 1 
ATOM   5444 H HG23 . VAL   B 1 96  ? 41.770 -17.576 5.983   1.00 18.30 ?  96  VAL   B HG23 1 
ATOM   5445 N N    . GLY   B 1 97  ? 39.888 -22.258 4.866   1.00 14.45 ?  97  GLY   B N    1 
ATOM   5446 C CA   . GLY   B 1 97  ? 38.920 -23.319 5.014   1.00 15.46 ?  97  GLY   B CA   1 
ATOM   5447 C C    . GLY   B 1 97  ? 39.047 -23.912 6.399   1.00 16.72 ?  97  GLY   B C    1 
ATOM   5448 O O    . GLY   B 1 97  ? 40.090 -23.782 7.057   1.00 16.67 ?  97  GLY   B O    1 
ATOM   5449 H H    . GLY   B 1 97  ? 40.628 -22.497 4.486   1.00 17.35 ?  97  GLY   B H    1 
ATOM   5450 H HA2  . GLY   B 1 97  ? 38.028 -22.961 4.894   1.00 18.57 ?  97  GLY   B HA2  1 
ATOM   5451 H HA3  . GLY   B 1 97  ? 39.080 -24.005 4.345   1.00 18.57 ?  97  GLY   B HA3  1 
ATOM   5452 N N    . PRO   B 1 98  ? 38.005 -24.596 6.867   1.00 16.59 ?  98  PRO   B N    1 
ATOM   5453 C CA   . PRO   B 1 98  ? 38.106 -25.277 8.162   1.00 18.30 ?  98  PRO   B CA   1 
ATOM   5454 C C    . PRO   B 1 98  ? 39.123 -26.409 8.123   1.00 17.47 ?  98  PRO   B C    1 
ATOM   5455 O O    . PRO   B 1 98  ? 39.228 -27.153 7.146   1.00 17.92 ?  98  PRO   B O    1 
ATOM   5456 C CB   . PRO   B 1 98  ? 36.686 -25.803 8.393   1.00 18.37 ?  98  PRO   B CB   1 
ATOM   5457 C CG   . PRO   B 1 98  ? 36.123 -25.977 7.036   1.00 18.16 ?  98  PRO   B CG   1 
ATOM   5458 C CD   . PRO   B 1 98  ? 36.678 -24.803 6.255   1.00 17.29 ?  98  PRO   B CD   1 
ATOM   5459 H HA   . PRO   B 1 98  ? 38.347 -24.644 8.856   1.00 21.97 ?  98  PRO   B HA   1 
ATOM   5460 H HB2  . PRO   B 1 98  ? 36.731 -26.652 8.866   1.00 22.06 ?  98  PRO   B HB2  1 
ATOM   5461 H HB3  . PRO   B 1 98  ? 36.178 -25.154 8.899   1.00 22.06 ?  98  PRO   B HB3  1 
ATOM   5462 H HG2  . PRO   B 1 98  ? 36.428 -26.826 6.662   1.00 21.81 ?  98  PRO   B HG2  1 
ATOM   5463 H HG3  . PRO   B 1 98  ? 35.155 -25.951 7.078   1.00 21.81 ?  98  PRO   B HG3  1 
ATOM   5464 H HD2  . PRO   B 1 98  ? 36.763 -25.030 5.314   1.00 20.76 ?  98  PRO   B HD2  1 
ATOM   5465 H HD3  . PRO   B 1 98  ? 36.127 -24.018 6.385   1.00 20.76 ?  98  PRO   B HD3  1 
ATOM   5466 N N    . ASN   B 1 99  ? 39.881 -26.530 9.205   1.00 18.89 ?  99  ASN   B N    1 
ATOM   5467 C CA   . ASN   B 1 99  ? 40.860 -27.602 9.372   1.00 20.09 ?  99  ASN   B CA   1 
ATOM   5468 C C    . ASN   B 1 99  ? 40.229 -28.672 10.262  1.00 23.21 ?  99  ASN   B C    1 
ATOM   5469 O O    . ASN   B 1 99  ? 40.181 -28.526 11.486  1.00 25.05 ?  99  ASN   B O    1 
ATOM   5470 C CB   . ASN   B 1 99  ? 42.138 -27.034 9.975   1.00 20.21 ?  99  ASN   B CB   1 
ATOM   5471 C CG   . ASN   B 1 99  ? 43.266 -28.044 10.000  1.00 20.84 ?  99  ASN   B CG   1 
ATOM   5472 O OD1  . ASN   B 1 99  ? 43.034 -29.225 10.180  1.00 21.66 ?  99  ASN   B OD1  1 
ATOM   5473 N ND2  . ASN   B 1 99  ? 44.488 -27.582 9.812   1.00 21.19 ?  99  ASN   B ND2  1 
ATOM   5474 H H    . ASN   B 1 99  ? 39.848 -25.988 9.870   1.00 22.69 ?  99  ASN   B H    1 
ATOM   5475 H HA   . ASN   B 1 99  ? 41.065 -28.000 8.515   1.00 24.12 ?  99  ASN   B HA   1 
ATOM   5476 H HB2  . ASN   B 1 99  ? 42.424 -26.277 9.450   1.00 24.27 ?  99  ASN   B HB2  1 
ATOM   5477 H HB3  . ASN   B 1 99  ? 41.953 -26.757 10.890  1.00 24.27 ?  99  ASN   B HB3  1 
ATOM   5478 H HD21 . ASN   B 1 99  ? 45.157 -28.119 9.823   1.00 25.45 ?  99  ASN   B HD21 1 
ATOM   5479 H HD22 . ASN   B 1 99  ? 44.606 -26.742 9.684   1.00 25.45 ?  99  ASN   B HD22 1 
ATOM   5480 N N    A VAL   B 1 100 ? 39.721 -29.739 9.637   0.46 25.05 ?  100 VAL   B N    1 
ATOM   5481 N N    B VAL   B 1 100 ? 39.741 -29.748 9.635   0.54 24.96 ?  100 VAL   B N    1 
ATOM   5482 C CA   A VAL   B 1 100 ? 39.096 -30.822 10.396  0.46 27.65 ?  100 VAL   B CA   1 
ATOM   5483 C CA   B VAL   B 1 100 ? 39.100 -30.835 10.374  0.54 27.67 ?  100 VAL   B CA   1 
ATOM   5484 C C    A VAL   B 1 100 ? 40.105 -31.490 11.319  0.46 28.31 ?  100 VAL   B C    1 
ATOM   5485 C C    B VAL   B 1 100 ? 40.096 -31.526 11.292  0.54 28.24 ?  100 VAL   B C    1 
ATOM   5486 O O    A VAL   B 1 100 ? 39.744 -31.968 12.400  0.46 29.17 ?  100 VAL   B O    1 
ATOM   5487 O O    B VAL   B 1 100 ? 39.717 -32.062 12.339  0.54 28.90 ?  100 VAL   B O    1 
ATOM   5488 C CB   A VAL   B 1 100 ? 38.418 -31.829 9.443   0.46 29.88 ?  100 VAL   B CB   1 
ATOM   5489 C CB   B VAL   B 1 100 ? 38.430 -31.822 9.394   0.54 30.16 ?  100 VAL   B CB   1 
ATOM   5490 C CG1  A VAL   B 1 100 ? 37.915 -33.047 10.210  0.46 30.94 ?  100 VAL   B CG1  1 
ATOM   5491 C CG1  B VAL   B 1 100 ? 37.908 -33.048 10.130  0.54 31.44 ?  100 VAL   B CG1  1 
ATOM   5492 C CG2  A VAL   B 1 100 ? 37.269 -31.159 8.701   0.46 30.50 ?  100 VAL   B CG2  1 
ATOM   5493 C CG2  B VAL   B 1 100 ? 37.299 -31.133 8.641   0.54 30.76 ?  100 VAL   B CG2  1 
ATOM   5494 H H    A VAL   B 1 100 ? 39.712 -29.847 8.783   0.46 30.08 ?  100 VAL   B H    1 
ATOM   5495 H H    B VAL   B 1 100 ? 39.758 -29.863 8.782   0.54 29.97 ?  100 VAL   B H    1 
ATOM   5496 H HA   A VAL   B 1 100 ? 38.394 -30.443 10.951  0.46 33.19 ?  100 VAL   B HA   1 
ATOM   5497 H HA   B VAL   B 1 100 ? 38.396 -30.461 10.927  0.54 33.22 ?  100 VAL   B HA   1 
ATOM   5498 H HB   A VAL   B 1 100 ? 39.065 -32.135 8.787   0.46 35.87 ?  100 VAL   B HB   1 
ATOM   5499 H HB   B VAL   B 1 100 ? 39.087 -32.119 8.744   0.54 36.21 ?  100 VAL   B HB   1 
ATOM   5500 H HG11 A VAL   B 1 100 ? 37.313 -33.552 9.639   0.46 37.14 ?  100 VAL   B HG11 1 
ATOM   5501 H HG11 B VAL   B 1 100 ? 37.314 -33.540 9.540   0.54 37.74 ?  100 VAL   B HG11 1 
ATOM   5502 H HG12 A VAL   B 1 100 ? 38.670 -33.601 10.462  0.46 37.14 ?  100 VAL   B HG12 1 
ATOM   5503 H HG12 B VAL   B 1 100 ? 38.657 -33.610 10.384  0.54 37.74 ?  100 VAL   B HG12 1 
ATOM   5504 H HG13 A VAL   B 1 100 ? 37.442 -32.748 11.002  0.46 37.14 ?  100 VAL   B HG13 1 
ATOM   5505 H HG13 B VAL   B 1 100 ? 37.424 -32.761 10.919  0.54 37.74 ?  100 VAL   B HG13 1 
ATOM   5506 H HG21 A VAL   B 1 100 ? 36.846 -31.810 8.118   0.46 36.62 ?  100 VAL   B HG21 1 
ATOM   5507 H HG21 B VAL   B 1 100 ? 36.880 -31.775 8.046   0.54 36.93 ?  100 VAL   B HG21 1 
ATOM   5508 H HG22 A VAL   B 1 100 ? 36.626 -30.829 9.348   0.46 36.62 ?  100 VAL   B HG22 1 
ATOM   5509 H HG22 B VAL   B 1 100 ? 36.650 -30.803 9.282   0.54 36.93 ?  100 VAL   B HG22 1 
ATOM   5510 H HG23 A VAL   B 1 100 ? 37.619 -30.424 8.176   0.46 36.62 ?  100 VAL   B HG23 1 
ATOM   5511 H HG23 B VAL   B 1 100 ? 37.664 -30.396 8.128   0.54 36.93 ?  100 VAL   B HG23 1 
ATOM   5512 N N    . ASN   B 1 101 ? 41.378 -31.543 10.914  1.00 27.93 ?  101 ASN   B N    1 
ATOM   5513 C CA   . ASN   B 1 101 ? 42.406 -32.106 11.788  1.00 29.45 ?  101 ASN   B CA   1 
ATOM   5514 C C    . ASN   B 1 101 ? 42.603 -31.282 13.054  1.00 32.58 ?  101 ASN   B C    1 
ATOM   5515 O O    . ASN   B 1 101 ? 43.187 -31.788 14.019  1.00 34.09 ?  101 ASN   B O    1 
ATOM   5516 C CB   . ASN   B 1 101 ? 43.734 -32.259 11.037  1.00 29.67 ?  101 ASN   B CB   1 
ATOM   5517 C CG   . ASN   B 1 101 ? 43.712 -33.406 10.038  1.00 29.72 ?  101 ASN   B CG   1 
ATOM   5518 O OD1  . ASN   B 1 101 ? 43.005 -34.389 10.228  1.00 30.89 ?  101 ASN   B OD1  1 
ATOM   5519 N ND2  . ASN   B 1 101 ? 44.484 -33.279 8.967   1.00 29.03 ?  101 ASN   B ND2  1 
ATOM   5520 H H    A ASN   B 1 101 ? 41.659 -31.276 10.149  0.46 33.53 ?  101 ASN   B H    1 
ATOM   5521 H H    B ASN   B 1 101 ? 41.667 -31.250 10.161  0.54 33.53 ?  101 ASN   B H    1 
ATOM   5522 H HA   . ASN   B 1 101 ? 42.126 -32.986 12.069  1.00 35.36 ?  101 ASN   B HA   1 
ATOM   5523 H HB2  . ASN   B 1 101 ? 43.924 -31.443 10.549  1.00 35.62 ?  101 ASN   B HB2  1 
ATOM   5524 H HB3  . ASN   B 1 101 ? 44.442 -32.433 11.677  1.00 35.62 ?  101 ASN   B HB3  1 
ATOM   5525 H HD21 . ASN   B 1 101 ? 44.504 -33.907 8.377   1.00 34.85 ?  101 ASN   B HD21 1 
ATOM   5526 H HD22 . ASN   B 1 101 ? 44.970 -32.579 8.865   1.00 34.85 ?  101 ASN   B HD22 1 
ATOM   5527 N N    . LYS   B 1 102 ? 42.133 -30.031 13.067  1.00 34.58 ?  102 LYS   B N    1 
ATOM   5528 C CA   . LYS   B 1 102 ? 42.088 -29.195 14.262  1.00 36.33 ?  102 LYS   B CA   1 
ATOM   5529 C C    . LYS   B 1 102 ? 40.696 -29.142 14.878  1.00 35.42 ?  102 LYS   B C    1 
ATOM   5530 O O    . LYS   B 1 102 ? 40.452 -28.318 15.763  1.00 36.47 ?  102 LYS   B O    1 
ATOM   5531 C CB   . LYS   B 1 102 ? 42.524 -27.764 13.937  1.00 40.37 ?  102 LYS   B CB   1 
ATOM   5532 C CG   . LYS   B 1 102 ? 43.961 -27.588 13.487  1.00 44.52 ?  102 LYS   B CG   1 
ATOM   5533 C CD   . LYS   B 1 102 ? 44.162 -26.154 13.009  1.00 48.17 ?  102 LYS   B CD   1 
ATOM   5534 C CE   . LYS   B 1 102 ? 45.622 -25.813 12.762  1.00 50.80 ?  102 LYS   B CE   1 
ATOM   5535 N NZ   . LYS   B 1 102 ? 45.774 -24.388 12.326  1.00 52.17 ?  102 LYS   B NZ   1 
ATOM   5536 H H    . LYS   B 1 102 ? 41.813 -29.633 12.374  1.00 41.51 ?  102 LYS   B H    1 
ATOM   5537 H HA   . LYS   B 1 102 ? 42.700 -29.549 14.925  1.00 43.61 ?  102 LYS   B HA   1 
ATOM   5538 H HB2  . LYS   B 1 102 ? 41.956 -27.424 13.230  1.00 48.46 ?  102 LYS   B HB2  1 
ATOM   5539 H HB3  . LYS   B 1 102 ? 42.405 -27.218 14.733  1.00 48.46 ?  102 LYS   B HB3  1 
ATOM   5540 H HG2  . LYS   B 1 102 ? 44.561 -27.755 14.230  1.00 53.44 ?  102 LYS   B HG2  1 
ATOM   5541 H HG3  . LYS   B 1 102 ? 44.149 -28.191 12.751  1.00 53.44 ?  102 LYS   B HG3  1 
ATOM   5542 H HD2  . LYS   B 1 102 ? 43.680 -26.028 12.177  1.00 57.82 ?  102 LYS   B HD2  1 
ATOM   5543 H HD3  . LYS   B 1 102 ? 43.821 -25.546 13.684  1.00 57.82 ?  102 LYS   B HD3  1 
ATOM   5544 H HE2  . LYS   B 1 102 ? 46.125 -25.936 13.582  1.00 60.98 ?  102 LYS   B HE2  1 
ATOM   5545 H HE3  . LYS   B 1 102 ? 45.973 -26.385 12.062  1.00 60.98 ?  102 LYS   B HE3  1 
ATOM   5546 H HZ1  . LYS   B 1 102 ? 46.632 -24.202 12.185  1.00 62.62 ?  102 LYS   B HZ1  1 
ATOM   5547 H HZ2  . LYS   B 1 102 ? 45.320 -24.250 11.572  1.00 62.62 ?  102 LYS   B HZ2  1 
ATOM   5548 H HZ3  . LYS   B 1 102 ? 45.459 -23.842 12.955  1.00 62.62 ?  102 LYS   B HZ3  1 
ATOM   5549 N N    . GLY   B 1 103 ? 39.775 -29.982 14.416  1.00 34.27 ?  103 GLY   B N    1 
ATOM   5550 C CA   . GLY   B 1 103 ? 38.435 -30.027 14.963  1.00 33.82 ?  103 GLY   B CA   1 
ATOM   5551 C C    . GLY   B 1 103 ? 37.512 -28.915 14.522  1.00 32.21 ?  103 GLY   B C    1 
ATOM   5552 O O    . GLY   B 1 103 ? 36.444 -28.748 15.123  1.00 33.33 ?  103 GLY   B O    1 
ATOM   5553 H H    . GLY   B 1 103 ? 39.909 -30.543 13.783  1.00 41.14 ?  103 GLY   B H    1 
ATOM   5554 H HA2  . GLY   B 1 103 ? 38.024 -30.870 14.714  1.00 40.60 ?  103 GLY   B HA2  1 
ATOM   5555 H HA3  . GLY   B 1 103 ? 38.487 -29.997 15.931  1.00 40.60 ?  103 GLY   B HA3  1 
ATOM   5556 N N    A GLU   B 1 104 ? 37.893 -28.136 13.512  0.46 31.04 ?  104 GLU   B N    1 
ATOM   5557 N N    B GLU   B 1 104 ? 37.869 -28.164 13.483  0.54 30.11 ?  104 GLU   B N    1 
ATOM   5558 C CA   A GLU   B 1 104 ? 37.065 -27.029 13.065  0.46 29.82 ?  104 GLU   B CA   1 
ATOM   5559 C CA   B GLU   B 1 104 ? 37.020 -27.080 13.016  0.54 27.96 ?  104 GLU   B CA   1 
ATOM   5560 C C    A GLU   B 1 104 ? 35.874 -27.542 12.257  0.46 30.41 ?  104 GLU   B C    1 
ATOM   5561 C C    B GLU   B 1 104 ? 35.853 -27.621 12.191  0.54 28.39 ?  104 GLU   B C    1 
ATOM   5562 O O    A GLU   B 1 104 ? 35.903 -28.629 11.672  0.46 30.76 ?  104 GLU   B O    1 
ATOM   5563 O O    B GLU   B 1 104 ? 35.910 -28.714 11.620  0.54 29.13 ?  104 GLU   B O    1 
ATOM   5564 C CB   A GLU   B 1 104 ? 37.900 -26.032 12.260  0.46 28.86 ?  104 GLU   B CB   1 
ATOM   5565 C CB   B GLU   B 1 104 ? 37.848 -26.067 12.225  0.54 26.49 ?  104 GLU   B CB   1 
ATOM   5566 C CG   A GLU   B 1 104 ? 38.998 -25.393 13.100  0.46 28.12 ?  104 GLU   B CG   1 
ATOM   5567 C CG   B GLU   B 1 104 ? 38.957 -25.472 13.075  0.54 25.28 ?  104 GLU   B CG   1 
ATOM   5568 C CD   A GLU   B 1 104 ? 39.945 -24.511 12.308  0.46 27.35 ?  104 GLU   B CD   1 
ATOM   5569 C CD   B GLU   B 1 104 ? 39.919 -24.581 12.314  0.54 23.91 ?  104 GLU   B CD   1 
ATOM   5570 O OE1  A GLU   B 1 104 ? 39.959 -24.579 11.060  0.46 26.10 ?  104 GLU   B OE1  1 
ATOM   5571 O OE1  B GLU   B 1 104 ? 39.940 -24.595 11.063  0.54 22.56 ?  104 GLU   B OE1  1 
ATOM   5572 O OE2  A GLU   B 1 104 ? 40.690 -23.745 12.952  0.46 27.86 -1 104 GLU   B OE2  1 
ATOM   5573 O OE2  B GLU   B 1 104 ? 40.673 -23.859 12.994  0.54 23.78 -1 104 GLU   B OE2  1 
ATOM   5574 H H    A GLU   B 1 104 ? 38.631 -28.225 13.077  0.46 37.26 ?  104 GLU   B H    1 
ATOM   5575 H H    B GLU   B 1 104 ? 38.599 -28.259 13.038  0.54 36.15 ?  104 GLU   B H    1 
ATOM   5576 H HA   A GLU   B 1 104 ? 36.719 -26.563 13.843  0.46 35.80 ?  104 GLU   B HA   1 
ATOM   5577 H HA   B GLU   B 1 104 ? 36.651 -26.619 13.786  0.54 33.57 ?  104 GLU   B HA   1 
ATOM   5578 H HB2  A GLU   B 1 104 ? 38.319 -26.491 11.517  0.46 34.65 ?  104 GLU   B HB2  1 
ATOM   5579 H HB2  B GLU   B 1 104 ? 38.252 -26.507 11.462  0.54 31.80 ?  104 GLU   B HB2  1 
ATOM   5580 H HB3  A GLU   B 1 104 ? 37.323 -25.323 11.931  0.46 34.65 ?  104 GLU   B HB3  1 
ATOM   5581 H HB3  B GLU   B 1 104 ? 37.272 -25.343 11.929  0.54 31.80 ?  104 GLU   B HB3  1 
ATOM   5582 H HG2  A GLU   B 1 104 ? 38.588 -24.844 13.788  0.46 33.76 ?  104 GLU   B HG2  1 
ATOM   5583 H HG2  B GLU   B 1 104 ? 38.559 -24.936 13.780  0.54 30.35 ?  104 GLU   B HG2  1 
ATOM   5584 H HG3  A GLU   B 1 104 ? 39.526 -26.093 13.512  0.46 33.76 ?  104 GLU   B HG3  1 
ATOM   5585 H HG3  B GLU   B 1 104 ? 39.475 -26.192 13.468  0.54 30.35 ?  104 GLU   B HG3  1 
ATOM   5586 N N    A ASP   B 1 105 ? 34.814 -26.738 12.239  0.46 30.54 ?  105 ASP   B N    1 
ATOM   5587 N N    B ASP   B 1 105 ? 34.780 -26.833 12.142  0.54 27.83 ?  105 ASP   B N    1 
ATOM   5588 C CA   A ASP   B 1 105 ? 33.533 -27.175 11.698  0.46 31.66 ?  105 ASP   B CA   1 
ATOM   5589 C CA   B ASP   B 1 105 ? 33.504 -27.292 11.605  0.54 28.71 ?  105 ASP   B CA   1 
ATOM   5590 C C    A ASP   B 1 105 ? 33.590 -27.234 10.175  0.46 30.18 ?  105 ASP   B C    1 
ATOM   5591 C C    B ASP   B 1 105 ? 33.557 -27.327 10.081  0.54 27.50 ?  105 ASP   B C    1 
ATOM   5592 O O    A ASP   B 1 105 ? 33.787 -26.211 9.512   0.46 30.08 ?  105 ASP   B O    1 
ATOM   5593 O O    B ASP   B 1 105 ? 33.713 -26.286 9.434   0.54 27.41 ?  105 ASP   B O    1 
ATOM   5594 C CB   A ASP   B 1 105 ? 32.435 -26.217 12.155  0.46 33.74 ?  105 ASP   B CB   1 
ATOM   5595 C CB   B ASP   B 1 105 ? 32.382 -26.366 12.077  0.54 30.24 ?  105 ASP   B CB   1 
ATOM   5596 C CG   A ASP   B 1 105 ? 31.061 -26.629 11.672  0.46 35.86 ?  105 ASP   B CG   1 
ATOM   5597 C CG   B ASP   B 1 105 ? 30.998 -26.947 11.832  0.54 31.44 ?  105 ASP   B CG   1 
ATOM   5598 O OD1  A ASP   B 1 105 ? 30.907 -27.775 11.197  0.46 36.47 ?  105 ASP   B OD1  1 
ATOM   5599 O OD1  B ASP   B 1 105 ? 30.848 -27.797 10.926  0.54 32.18 ?  105 ASP   B OD1  1 
ATOM   5600 O OD2  A ASP   B 1 105 ? 30.135 -25.796 11.753  0.46 37.00 -1 105 ASP   B OD2  1 
ATOM   5601 O OD2  B ASP   B 1 105 ? 30.054 -26.554 12.550  0.54 31.77 -1 105 ASP   B OD2  1 
ATOM   5602 H H    A ASP   B 1 105 ? 34.812 -25.929 12.532  0.46 36.66 ?  105 ASP   B H    1 
ATOM   5603 H H    B ASP   B 1 105 ? 34.769 -26.018 12.412  0.54 33.41 ?  105 ASP   B H    1 
ATOM   5604 H HA   A ASP   B 1 105 ? 33.328 -28.061 12.032  0.46 38.01 ?  105 ASP   B HA   1 
ATOM   5605 H HA   B ASP   B 1 105 ? 33.318 -28.186 11.926  0.54 34.47 ?  105 ASP   B HA   1 
ATOM   5606 H HB2  A ASP   B 1 105 ? 32.439 -26.175 13.128  0.46 40.51 ?  105 ASP   B HB2  1 
ATOM   5607 H HB2  B ASP   B 1 105 ? 32.481 -26.213 13.030  0.54 36.30 ?  105 ASP   B HB2  1 
ATOM   5608 H HB3  A ASP   B 1 105 ? 32.604 -25.339 11.787  0.46 40.51 ?  105 ASP   B HB3  1 
ATOM   5609 H HB3  B ASP   B 1 105 ? 32.450 -25.520 11.601  0.54 36.30 ?  105 ASP   B HB3  1 
ATOM   5610 N N    A ILE   B 1 106 ? 33.395 -28.436 9.625   0.46 29.44 ?  106 ILE   B N    1 
ATOM   5611 N N    B ILE   B 1 106 ? 33.394 -28.526 9.512   0.54 27.17 ?  106 ILE   B N    1 
ATOM   5612 C CA   A ILE   B 1 106 ? 33.386 -28.627 8.179   0.46 28.22 ?  106 ILE   B CA   1 
ATOM   5613 C CA   B ILE   B 1 106 ? 33.363 -28.690 8.063   0.54 26.14 ?  106 ILE   B CA   1 
ATOM   5614 C C    A ILE   B 1 106 ? 32.283 -27.822 7.505   0.46 26.72 ?  106 ILE   B C    1 
ATOM   5615 C C    B ILE   B 1 106 ? 32.265 -27.853 7.422   0.54 24.62 ?  106 ILE   B C    1 
ATOM   5616 O O    A ILE   B 1 106 ? 32.372 -27.539 6.306   0.46 25.97 ?  106 ILE   B O    1 
ATOM   5617 O O    B ILE   B 1 106 ? 32.339 -27.551 6.227   0.54 23.48 ?  106 ILE   B O    1 
ATOM   5618 C CB   A ILE   B 1 106 ? 33.279 -30.135 7.849   0.46 29.20 ?  106 ILE   B CB   1 
ATOM   5619 C CB   B ILE   B 1 106 ? 33.228 -30.191 7.708   0.54 27.63 ?  106 ILE   B CB   1 
ATOM   5620 C CG1  A ILE   B 1 106 ? 33.550 -30.394 6.365   0.46 29.24 ?  106 ILE   B CG1  1 
ATOM   5621 C CG1  B ILE   B 1 106 ? 33.537 -30.436 6.230   0.54 28.11 ?  106 ILE   B CG1  1 
ATOM   5622 C CG2  A ILE   B 1 106 ? 31.908 -30.674 8.240   0.46 29.98 ?  106 ILE   B CG2  1 
ATOM   5623 C CG2  B ILE   B 1 106 ? 31.833 -30.705 8.049   0.54 28.66 ?  106 ILE   B CG2  1 
ATOM   5624 C CD1  A ILE   B 1 106 ? 34.917 -29.936 5.909   0.46 29.11 ?  106 ILE   B CD1  1 
ATOM   5625 C CD1  B ILE   B 1 106 ? 34.917 -29.979 5.816   0.54 28.20 ?  106 ILE   B CD1  1 
ATOM   5626 H H    A ILE   B 1 106 ? 33.271 -29.157 10.072  0.46 35.35 ?  106 ILE   B H    1 
ATOM   5627 H H    B ILE   B 1 106 ? 33.302 -29.260 9.947   0.54 32.62 ?  106 ILE   B H    1 
ATOM   5628 H HA   A ILE   B 1 106 ? 34.226 -28.307 7.829   0.46 33.88 ?  106 ILE   B HA   1 
ATOM   5629 H HA   B ILE   B 1 106 ? 34.199 -28.374 7.707   0.54 31.38 ?  106 ILE   B HA   1 
ATOM   5630 H HB   A ILE   B 1 106 ? 33.947 -30.606 8.366   0.46 35.05 ?  106 ILE   B HB   1 
ATOM   5631 H HB   B ILE   B 1 106 ? 33.868 -30.686 8.238   0.54 33.18 ?  106 ILE   B HB   1 
ATOM   5632 H HG12 A ILE   B 1 106 ? 33.489 -31.349 6.197   0.46 35.10 ?  106 ILE   B HG12 1 
ATOM   5633 H HG12 B ILE   B 1 106 ? 33.477 -31.389 6.050   0.54 33.74 ?  106 ILE   B HG12 1 
ATOM   5634 H HG13 A ILE   B 1 106 ? 32.888 -29.926 5.834   0.46 35.10 ?  106 ILE   B HG13 1 
ATOM   5635 H HG13 B ILE   B 1 106 ? 32.891 -29.960 5.687   0.54 33.74 ?  106 ILE   B HG13 1 
ATOM   5636 H HG21 A ILE   B 1 106 ? 31.923 -31.643 8.183   0.46 35.99 ?  106 ILE   B HG21 1 
ATOM   5637 H HG21 B ILE   B 1 106 ? 31.836 -31.675 8.008   0.54 34.41 ?  106 ILE   B HG21 1 
ATOM   5638 H HG22 A ILE   B 1 106 ? 31.709 -30.401 9.149   0.46 35.99 ?  106 ILE   B HG22 1 
ATOM   5639 H HG22 B ILE   B 1 106 ? 31.601 -30.414 8.944   0.54 34.41 ?  106 ILE   B HG22 1 
ATOM   5640 H HG23 A ILE   B 1 106 ? 31.240 -30.319 7.634   0.46 35.99 ?  106 ILE   B HG23 1 
ATOM   5641 H HG23 B ILE   B 1 106 ? 31.196 -30.350 7.410   0.54 34.41 ?  106 ILE   B HG23 1 
ATOM   5642 H HD11 A ILE   B 1 106 ? 35.124 -30.355 5.060   0.46 34.95 ?  106 ILE   B HD11 1 
ATOM   5643 H HD11 B ILE   B 1 106 ? 35.158 -30.415 4.985   0.54 33.86 ?  106 ILE   B HD11 1 
ATOM   5644 H HD12 A ILE   B 1 106 ? 34.911 -28.971 5.808   0.46 34.95 ?  106 ILE   B HD12 1 
ATOM   5645 H HD12 B ILE   B 1 106 ? 34.908 -29.016 5.693   0.54 33.86 ?  106 ILE   B HD12 1 
ATOM   5646 H HD13 A ILE   B 1 106 ? 35.575 -30.196 6.574   0.46 34.95 ?  106 ILE   B HD13 1 
ATOM   5647 H HD13 B ILE   B 1 106 ? 35.551 -30.219 6.511   0.54 33.86 ?  106 ILE   B HD13 1 
ATOM   5648 N N    A GLN   B 1 107 ? 31.237 -27.448 8.245   0.46 27.17 ?  107 GLN   B N    1 
ATOM   5649 N N    B GLN   B 1 107 ? 31.240 -27.472 8.186   0.54 25.75 ?  107 GLN   B N    1 
ATOM   5650 C CA   A GLN   B 1 107 ? 30.159 -26.661 7.656   0.46 27.30 ?  107 GLN   B CA   1 
ATOM   5651 C CA   B GLN   B 1 107 ? 30.156 -26.670 7.630   0.54 26.42 ?  107 GLN   B CA   1 
ATOM   5652 C C    A GLN   B 1 107 ? 30.653 -25.325 7.117   0.46 25.00 ?  107 GLN   B C    1 
ATOM   5653 C C    B GLN   B 1 107 ? 30.630 -25.304 7.144   0.54 24.69 ?  107 GLN   B C    1 
ATOM   5654 O O    A GLN   B 1 107 ? 30.026 -24.766 6.211   0.46 25.20 ?  107 GLN   B O    1 
ATOM   5655 O O    B GLN   B 1 107 ? 29.962 -24.699 6.299   0.54 25.05 ?  107 GLN   B O    1 
ATOM   5656 C CB   A GLN   B 1 107 ? 29.048 -26.437 8.689   0.46 30.75 ?  107 GLN   B CB   1 
ATOM   5657 C CB   B GLN   B 1 107 ? 29.034 -26.522 8.664   0.54 30.21 ?  107 GLN   B CB   1 
ATOM   5658 C CG   A GLN   B 1 107 ? 27.729 -25.914 8.112   0.46 34.17 ?  107 GLN   B CG   1 
ATOM   5659 C CG   B GLN   B 1 107 ? 27.716 -25.984 8.107   0.54 34.29 ?  107 GLN   B CG   1 
ATOM   5660 C CD   A GLN   B 1 107 ? 27.695 -24.401 7.970   0.46 36.93 ?  107 GLN   B CD   1 
ATOM   5661 C CD   B GLN   B 1 107 ? 27.613 -24.472 8.188   0.54 37.33 ?  107 GLN   B CD   1 
ATOM   5662 O OE1  A GLN   B 1 107 ? 28.540 -23.692 8.520   0.46 38.14 ?  107 GLN   B OE1  1 
ATOM   5663 O OE1  B GLN   B 1 107 ? 28.458 -23.810 8.794   0.54 38.49 ?  107 GLN   B OE1  1 
ATOM   5664 N NE2  A GLN   B 1 107 ? 26.710 -23.900 7.229   0.46 37.94 ?  107 GLN   B NE2  1 
ATOM   5665 N NE2  B GLN   B 1 107 ? 26.567 -23.916 7.580   0.54 38.46 ?  107 GLN   B NE2  1 
ATOM   5666 H H    A GLN   B 1 107 ? 31.132 -27.627 9.077   0.46 32.62 ?  107 GLN   B H    1 
ATOM   5667 H H    B GLN   B 1 107 ? 31.147 -27.662 9.018   0.54 30.92 ?  107 GLN   B H    1 
ATOM   5668 H HA   A GLN   B 1 107 ? 29.774 -27.157 6.917   0.46 32.77 ?  107 GLN   B HA   1 
ATOM   5669 H HA   B GLN   B 1 107 ? 29.784 -27.137 6.867   0.54 31.72 ?  107 GLN   B HA   1 
ATOM   5670 H HB2  A GLN   B 1 107 ? 28.858 -27.279 9.125   0.46 36.91 ?  107 GLN   B HB2  1 
ATOM   5671 H HB2  B GLN   B 1 107 ? 28.849 -27.391 9.045   0.54 36.26 ?  107 GLN   B HB2  1 
ATOM   5672 H HB3  A GLN   B 1 107 ? 29.357 -25.792 9.345   0.46 36.91 ?  107 GLN   B HB3  1 
ATOM   5673 H HB3  B GLN   B 1 107 ? 29.327 -25.916 9.362   0.54 36.26 ?  107 GLN   B HB3  1 
ATOM   5674 H HG2  A GLN   B 1 107 ? 27.592 -26.295 7.232   0.46 41.02 ?  107 GLN   B HG2  1 
ATOM   5675 H HG2  B GLN   B 1 107 ? 27.637 -26.238 7.174   0.54 41.16 ?  107 GLN   B HG2  1 
ATOM   5676 H HG3  A GLN   B 1 107 ? 27.000 -26.176 8.701   0.46 41.02 ?  107 GLN   B HG3  1 
ATOM   5677 H HG3  B GLN   B 1 107 ? 26.978 -26.364 8.614   0.54 41.16 ?  107 GLN   B HG3  1 
ATOM   5678 H HE21 A GLN   B 1 107 ? 26.138 -24.426 6.858   0.46 45.54 ?  107 GLN   B HE21 1 
ATOM   5679 H HE21 B GLN   B 1 107 ? 25.997 -24.410 7.165   0.54 46.17 ?  107 GLN   B HE21 1 
ATOM   5680 H HE22 A GLN   B 1 107 ? 26.641 -23.049 7.119   0.46 45.54 ?  107 GLN   B HE22 1 
ATOM   5681 H HE22 B GLN   B 1 107 ? 26.461 -23.063 7.599   0.54 46.17 ?  107 GLN   B HE22 1 
ATOM   5682 N N    . LEU   B 1 108 ? 31.766 -24.807 7.644   1.00 22.65 ?  108 LEU   B N    1 
ATOM   5683 C CA   . LEU   B 1 108 ? 32.298 -23.513 7.214   1.00 20.87 ?  108 LEU   B CA   1 
ATOM   5684 C C    . LEU   B 1 108 ? 32.948 -23.550 5.840   1.00 18.76 ?  108 LEU   B C    1 
ATOM   5685 O O    . LEU   B 1 108 ? 33.376 -22.498 5.344   1.00 17.87 ?  108 LEU   B O    1 
ATOM   5686 C CB   . LEU   B 1 108 ? 33.303 -22.988 8.239   1.00 21.14 ?  108 LEU   B CB   1 
ATOM   5687 C CG   . LEU   B 1 108 ? 32.695 -22.564 9.573   1.00 23.42 ?  108 LEU   B CG   1 
ATOM   5688 C CD1  . LEU   B 1 108 ? 33.737 -22.544 10.674  1.00 22.81 ?  108 LEU   B CD1  1 
ATOM   5689 C CD2  . LEU   B 1 108 ? 32.039 -21.198 9.443   1.00 25.43 ?  108 LEU   B CD2  1 
ATOM   5690 H H    A LEU   B 1 108 ? 32.221 -25.188 8.265   0.46 27.20 ?  108 LEU   B H    1 
ATOM   5691 H H    B LEU   B 1 108 ? 32.237 -25.202 8.244   0.54 27.20 ?  108 LEU   B H    1 
ATOM   5692 H HA   . LEU   B 1 108 ? 31.566 -22.881 7.175   1.00 25.06 ?  108 LEU   B HA   1 
ATOM   5693 H HB2  . LEU   B 1 108 ? 33.950 -23.680 8.427   1.00 25.38 ?  108 LEU   B HB2  1 
ATOM   5694 H HB3  . LEU   B 1 108 ? 33.747 -22.212 7.867   1.00 25.38 ?  108 LEU   B HB3  1 
ATOM   5695 H HG   . LEU   B 1 108 ? 32.005 -23.197 9.830   1.00 28.12 ?  108 LEU   B HG   1 
ATOM   5696 H HD11 . LEU   B 1 108 ? 33.318 -22.274 11.509  1.00 27.39 ?  108 LEU   B HD11 1 
ATOM   5697 H HD12 . LEU   B 1 108 ? 34.113 -23.434 10.770  1.00 27.39 ?  108 LEU   B HD12 1 
ATOM   5698 H HD13 . LEU   B 1 108 ? 34.436 -21.914 10.440  1.00 27.39 ?  108 LEU   B HD13 1 
ATOM   5699 H HD21 . LEU   B 1 108 ? 31.673 -20.936 10.303  1.00 30.53 ?  108 LEU   B HD21 1 
ATOM   5700 H HD22 . LEU   B 1 108 ? 32.706 -20.554 9.158   1.00 30.53 ?  108 LEU   B HD22 1 
ATOM   5701 H HD23 . LEU   B 1 108 ? 31.328 -21.251 8.785   1.00 30.53 ?  108 LEU   B HD23 1 
ATOM   5702 N N    . LEU   B 1 109 ? 33.032 -24.721 5.214   1.00 18.28 ?  109 LEU   B N    1 
ATOM   5703 C CA   . LEU   B 1 109 ? 33.663 -24.827 3.906   1.00 16.88 ?  109 LEU   B CA   1 
ATOM   5704 C C    . LEU   B 1 109 ? 32.894 -24.065 2.834   1.00 16.32 ?  109 LEU   B C    1 
ATOM   5705 O O    . LEU   B 1 109 ? 33.508 -23.480 1.932   1.00 16.22 ?  109 LEU   B O    1 
ATOM   5706 C CB   . LEU   B 1 109 ? 33.826 -26.312 3.544   1.00 18.02 ?  109 LEU   B CB   1 
ATOM   5707 C CG   . LEU   B 1 109 ? 34.571 -26.663 2.258   1.00 16.93 ?  109 LEU   B CG   1 
ATOM   5708 C CD1  . LEU   B 1 109 ? 35.947 -26.017 2.229   1.00 17.04 ?  109 LEU   B CD1  1 
ATOM   5709 C CD2  . LEU   B 1 109 ? 34.697 -28.176 2.132   1.00 17.74 ?  109 LEU   B CD2  1 
ATOM   5710 H H    . LEU   B 1 109 ? 32.743 -25.467 5.531   1.00 21.95 ?  109 LEU   B H    1 
ATOM   5711 H HA   . LEU   B 1 109 ? 34.549 -24.439 3.959   1.00 20.28 ?  109 LEU   B HA   1 
ATOM   5712 H HB2  . LEU   B 1 109 ? 34.306 -26.745 4.265   1.00 21.64 ?  109 LEU   B HB2  1 
ATOM   5713 H HB3  . LEU   B 1 109 ? 32.943 -26.701 3.470   1.00 21.64 ?  109 LEU   B HB3  1 
ATOM   5714 H HG   . LEU   B 1 109 ? 34.063 -26.346 1.491   1.00 20.33 ?  109 LEU   B HG   1 
ATOM   5715 H HD11 . LEU   B 1 109 ? 36.435 -26.353 1.457   1.00 20.46 ?  109 LEU   B HD11 1 
ATOM   5716 H HD12 . LEU   B 1 109 ? 35.844 -25.061 2.168   1.00 20.46 ?  109 LEU   B HD12 1 
ATOM   5717 H HD13 . LEU   B 1 109 ? 36.420 -26.257 3.042   1.00 20.46 ?  109 LEU   B HD13 1 
ATOM   5718 H HD21 . LEU   B 1 109 ? 35.271 -28.387 1.379   1.00 21.30 ?  109 LEU   B HD21 1 
ATOM   5719 H HD22 . LEU   B 1 109 ? 35.083 -28.530 2.950   1.00 21.30 ?  109 LEU   B HD22 1 
ATOM   5720 H HD23 . LEU   B 1 109 ? 33.815 -28.562 1.993   1.00 21.30 ?  109 LEU   B HD23 1 
ATOM   5721 N N    . LYS   B 1 110 ? 31.563 -24.009 2.929   1.00 15.92 ?  110 LYS   B N    1 
ATOM   5722 C CA   . LYS   B 1 110 ? 30.814 -23.237 1.941   1.00 16.34 ?  110 LYS   B CA   1 
ATOM   5723 C C    . LYS   B 1 110 ? 31.156 -21.751 2.024   1.00 15.23 ?  110 LYS   B C    1 
ATOM   5724 O O    . LYS   B 1 110 ? 31.409 -21.110 1.001   1.00 15.20 ?  110 LYS   B O    1 
ATOM   5725 C CB   . LYS   B 1 110 ? 29.306 -23.479 2.088   1.00 17.57 ?  110 LYS   B CB   1 
ATOM   5726 C CG   . LYS   B 1 110 ? 28.505 -22.877 0.939   1.00 18.18 ?  110 LYS   B CG   1 
ATOM   5727 C CD   . LYS   B 1 110 ? 27.014 -23.265 0.995   1.00 17.81 ?  110 LYS   B CD   1 
ATOM   5728 C CE   . LYS   B 1 110 ? 26.266 -22.729 -0.224  1.00 19.15 ?  110 LYS   B CE   1 
ATOM   5729 N NZ   . LYS   B 1 110 ? 26.630 -23.426 -1.487  1.00 18.82 ?  110 LYS   B NZ   1 
ATOM   5730 H H    . LYS   B 1 110 ? 31.086 -24.387 3.541   1.00 19.12 ?  110 LYS   B H    1 
ATOM   5731 H HA   . LYS   B 1 110 ? 31.070 -23.546 1.060   1.00 19.62 ?  110 LYS   B HA   1 
ATOM   5732 H HB2  . LYS   B 1 110 ? 29.140 -24.438 2.101   1.00 21.09 ?  110 LYS   B HB2  1 
ATOM   5733 H HB3  . LYS   B 1 110 ? 28.998 -23.079 2.915   1.00 21.09 ?  110 LYS   B HB3  1 
ATOM   5734 H HG2  . LYS   B 1 110 ? 28.560 -21.910 0.982   1.00 21.84 ?  110 LYS   B HG2  1 
ATOM   5735 H HG3  . LYS   B 1 110 ? 28.862 -23.195 0.097   1.00 21.84 ?  110 LYS   B HG3  1 
ATOM   5736 H HD2  . LYS   B 1 110 ? 26.926 -24.232 1.006   1.00 21.39 ?  110 LYS   B HD2  1 
ATOM   5737 H HD3  . LYS   B 1 110 ? 26.605 -22.883 1.791   1.00 21.39 ?  110 LYS   B HD3  1 
ATOM   5738 H HE2  . LYS   B 1 110 ? 25.313 -22.842 -0.091  1.00 22.99 ?  110 LYS   B HE2  1 
ATOM   5739 H HE3  . LYS   B 1 110 ? 26.477 -21.789 -0.334  1.00 22.99 ?  110 LYS   B HE3  1 
ATOM   5740 H HZ1  . LYS   B 1 110 ? 26.171 -23.075 -2.166  1.00 22.59 ?  110 LYS   B HZ1  1 
ATOM   5741 H HZ2  . LYS   B 1 110 ? 27.499 -23.326 -1.646  1.00 22.59 ?  110 LYS   B HZ2  1 
ATOM   5742 H HZ3  . LYS   B 1 110 ? 26.440 -24.288 -1.422  1.00 22.59 ?  110 LYS   B HZ3  1 
ATOM   5743 N N    . SER   B 1 111 ? 31.172 -21.195 3.238   1.00 16.86 ?  111 SER   B N    1 
ATOM   5744 C CA   . SER   B 1 111 ? 31.574 -19.798 3.407   1.00 16.17 ?  111 SER   B CA   1 
ATOM   5745 C C    . SER   B 1 111 ? 32.956 -19.547 2.813   1.00 15.22 ?  111 SER   B C    1 
ATOM   5746 O O    . SER   B 1 111 ? 33.180 -18.532 2.141   1.00 16.01 ?  111 SER   B O    1 
ATOM   5747 C CB   . SER   B 1 111 ? 31.562 -19.411 4.887   1.00 17.10 ?  111 SER   B CB   1 
ATOM   5748 O OG   . SER   B 1 111 ? 30.256 -19.421 5.424   1.00 19.15 ?  111 SER   B OG   1 
ATOM   5749 H H    . SER   B 1 111 ? 30.949 -21.594 3.964   1.00 20.25 ?  111 SER   B H    1 
ATOM   5750 H HA   . SER   B 1 111 ? 30.941 -19.224 2.946   1.00 19.42 ?  111 SER   B HA   1 
ATOM   5751 H HB2  . SER   B 1 111 ? 32.108 -20.042 5.379   1.00 20.53 ?  111 SER   B HB2  1 
ATOM   5752 H HB3  . SER   B 1 111 ? 31.933 -18.517 4.979   1.00 20.53 ?  111 SER   B HB3  1 
ATOM   5753 H HG   . SER   B 1 111 ? 29.961 -20.202 5.460   1.00 22.99 ?  111 SER   B HG   1 
ATOM   5754 N N    . ALA   B 1 112 ? 33.895 -20.466 3.046   1.00 15.26 ?  112 ALA   B N    1 
ATOM   5755 C CA   . ALA   B 1 112 ? 35.242 -20.300 2.501   1.00 14.87 ?  112 ALA   B CA   1 
ATOM   5756 C C    . ALA   B 1 112 ? 35.209 -20.225 0.979   1.00 14.59 ?  112 ALA   B C    1 
ATOM   5757 O O    . ALA   B 1 112 ? 35.842 -19.348 0.377   1.00 15.02 ?  112 ALA   B O    1 
ATOM   5758 C CB   . ALA   B 1 112 ? 36.151 -21.432 2.982   1.00 15.37 ?  112 ALA   B CB   1 
ATOM   5759 H H    . ALA   B 1 112 ? 33.781 -21.185 3.502   1.00 18.33 ?  112 ALA   B H    1 
ATOM   5760 H HA   . ALA   B 1 112 ? 35.607 -19.463 2.829   1.00 17.85 ?  112 ALA   B HA   1 
ATOM   5761 H HB1  . ALA   B 1 112 ? 37.042 -21.295 2.615   1.00 18.46 ?  112 ALA   B HB1  1 
ATOM   5762 H HB2  . ALA   B 1 112 ? 36.191 -21.414 3.951   1.00 18.46 ?  112 ALA   B HB2  1 
ATOM   5763 H HB3  . ALA   B 1 112 ? 35.794 -22.277 2.678   1.00 18.46 ?  112 ALA   B HB3  1 
ATOM   5764 N N    . TYR   B 1 113 ? 34.473 -21.133 0.330   1.00 14.19 ?  113 TYR   B N    1 
ATOM   5765 C CA   . TYR   B 1 113 ? 34.398 -21.099 -1.129  1.00 13.95 ?  113 TYR   B CA   1 
ATOM   5766 C C    . TYR   B 1 113 ? 33.685 -19.849 -1.650  1.00 13.99 ?  113 TYR   B C    1 
ATOM   5767 O O    . TYR   B 1 113 ? 33.952 -19.411 -2.776  1.00 14.28 ?  113 TYR   B O    1 
ATOM   5768 C CB   . TYR   B 1 113 ? 33.713 -22.360 -1.673  1.00 14.13 ?  113 TYR   B CB   1 
ATOM   5769 C CG   . TYR   B 1 113 ? 34.671 -23.501 -1.936  1.00 14.98 ?  113 TYR   B CG   1 
ATOM   5770 C CD1  . TYR   B 1 113 ? 35.652 -23.395 -2.908  1.00 14.77 ?  113 TYR   B CD1  1 
ATOM   5771 C CD2  . TYR   B 1 113 ? 34.582 -24.680 -1.221  1.00 15.64 ?  113 TYR   B CD2  1 
ATOM   5772 C CE1  . TYR   B 1 113 ? 36.536 -24.424 -3.151  1.00 15.80 ?  113 TYR   B CE1  1 
ATOM   5773 C CE2  . TYR   B 1 113 ? 35.456 -25.733 -1.458  1.00 15.64 ?  113 TYR   B CE2  1 
ATOM   5774 C CZ   . TYR   B 1 113 ? 36.430 -25.603 -2.428  1.00 14.89 ?  113 TYR   B CZ   1 
ATOM   5775 O OH   . TYR   B 1 113 ? 37.318 -26.626 -2.706  1.00 16.39 ?  113 TYR   B OH   1 
ATOM   5776 H H    . TYR   B 1 113 ? 34.017 -21.767 0.705   1.00 17.04 ?  113 TYR   B H    1 
ATOM   5777 H HA   . TYR   B 1 113 ? 35.298 -21.080 -1.471  1.00 16.75 ?  113 TYR   B HA   1 
ATOM   5778 H HB2  . TYR   B 1 113 ? 33.053 -22.666 -1.027  1.00 16.97 ?  113 TYR   B HB2  1 
ATOM   5779 H HB3  . TYR   B 1 113 ? 33.266 -22.136 -2.508  1.00 16.97 ?  113 TYR   B HB3  1 
ATOM   5780 H HD1  . TYR   B 1 113 ? 35.724 -22.599 -3.398  1.00 17.74 ?  113 TYR   B HD1  1 
ATOM   5781 H HD2  . TYR   B 1 113 ? 33.917 -24.767 -0.574  1.00 18.79 ?  113 TYR   B HD2  1 
ATOM   5782 H HE1  . TYR   B 1 113 ? 37.182 -24.333 -3.811  1.00 18.98 ?  113 TYR   B HE1  1 
ATOM   5783 H HE2  . TYR   B 1 113 ? 35.373 -26.524 -0.975  1.00 18.79 ?  113 TYR   B HE2  1 
ATOM   5784 H HH   . TYR   B 1 113 ? 37.143 -27.287 -2.212  1.00 19.68 ?  113 TYR   B HH   1 
ATOM   5785 N N    . GLU   B 1 114 ? 32.768 -19.258 -0.868  1.00 14.08 ?  114 GLU   B N    1 
ATOM   5786 C CA   . GLU   B 1 114 ? 32.092 -18.046 -1.326  1.00 13.84 ?  114 GLU   B CA   1 
ATOM   5787 C C    . GLU   B 1 114 ? 33.083 -16.925 -1.633  1.00 14.11 ?  114 GLU   B C    1 
ATOM   5788 O O    . GLU   B 1 114 ? 32.803 -16.065 -2.473  1.00 14.94 ?  114 GLU   B O    1 
ATOM   5789 C CB   . GLU   B 1 114 ? 31.037 -17.610 -0.306  1.00 15.14 ?  114 GLU   B CB   1 
ATOM   5790 C CG   . GLU   B 1 114 ? 29.783 -18.493 -0.403  1.00 15.33 ?  114 GLU   B CG   1 
ATOM   5791 C CD   . GLU   B 1 114 ? 28.776 -18.315 0.716   1.00 15.37 ?  114 GLU   B CD   1 
ATOM   5792 O OE1  . GLU   B 1 114 ? 29.074 -17.705 1.762   1.00 14.86 ?  114 GLU   B OE1  1 
ATOM   5793 O OE2  . GLU   B 1 114 ? 27.666 -18.862 0.556   1.00 15.91 -1 114 GLU   B OE2  1 
ATOM   5794 H H    . GLU   B 1 114 ? 32.527 -19.536 -0.086  1.00 16.91 ?  114 GLU   B H    1 
ATOM   5795 H HA   . GLU   B 1 114 ? 31.629 -18.251 -2.149  1.00 16.62 ?  114 GLU   B HA   1 
ATOM   5796 H HB2  . GLU   B 1 114 ? 31.402 -17.690 0.591   1.00 18.18 ?  114 GLU   B HB2  1 
ATOM   5797 H HB3  . GLU   B 1 114 ? 30.781 -16.691 -0.483  1.00 18.18 ?  114 GLU   B HB3  1 
ATOM   5798 H HG2  . GLU   B 1 114 ? 29.328 -18.292 -1.234  1.00 18.41 ?  114 GLU   B HG2  1 
ATOM   5799 H HG3  . GLU   B 1 114 ? 30.060 -19.423 -0.399  1.00 18.41 ?  114 GLU   B HG3  1 
ATOM   5800 N N    . ASN   B 1 115 ? 34.244 -16.917 -0.977  1.00 13.43 ?  115 ASN   B N    1 
ATOM   5801 C CA   . ASN   B 1 115 ? 35.246 -15.897 -1.285  1.00 13.27 ?  115 ASN   B CA   1 
ATOM   5802 C C    . ASN   B 1 115 ? 35.643 -15.919 -2.760  1.00 13.48 ?  115 ASN   B C    1 
ATOM   5803 O O    . ASN   B 1 115 ? 36.019 -14.880 -3.329  1.00 14.12 ?  115 ASN   B O    1 
ATOM   5804 C CB   . ASN   B 1 115 ? 36.479 -16.067 -0.389  1.00 14.53 ?  115 ASN   B CB   1 
ATOM   5805 C CG   . ASN   B 1 115 ? 36.192 -15.784 1.066   1.00 14.66 ?  115 ASN   B CG   1 
ATOM   5806 O OD1  . ASN   B 1 115 ? 36.174 -14.635 1.490   1.00 16.88 ?  115 ASN   B OD1  1 
ATOM   5807 N ND2  . ASN   B 1 115 ? 36.005 -16.837 1.854   1.00 15.50 ?  115 ASN   B ND2  1 
ATOM   5808 H H    . ASN   B 1 115 ? 34.471 -17.468 -0.350  1.00 16.13 ?  115 ASN   B H    1 
ATOM   5809 H HA   . ASN   B 1 115 ? 34.871 -15.022 -1.095  1.00 15.94 ?  115 ASN   B HA   1 
ATOM   5810 H HB2  . ASN   B 1 115 ? 36.801 -16.977 -0.454  1.00 17.46 ?  115 ASN   B HB2  1 
ATOM   5811 H HB3  . ASN   B 1 115 ? 37.170 -15.448 -0.677  1.00 17.46 ?  115 ASN   B HB3  1 
ATOM   5812 H HD21 . ASN   B 1 115 ? 35.846 -16.722 2.691   1.00 18.62 ?  115 ASN   B HD21 1 
ATOM   5813 H HD22 . ASN   B 1 115 ? 36.034 -17.629 1.524   1.00 18.62 ?  115 ASN   B HD22 1 
ATOM   5814 N N    . PHE   B 1 116 ? 35.620 -17.099 -3.391  1.00 13.51 ?  116 PHE   B N    1 
ATOM   5815 C CA   . PHE   B 1 116 ? 36.030 -17.194 -4.782  1.00 13.75 ?  116 PHE   B CA   1 
ATOM   5816 C C    . PHE   B 1 116 ? 35.133 -16.373 -5.696  1.00 13.47 ?  116 PHE   B C    1 
ATOM   5817 O O    . PHE   B 1 116 ? 35.578 -15.935 -6.766  1.00 13.77 ?  116 PHE   B O    1 
ATOM   5818 C CB   . PHE   B 1 116 ? 35.995 -18.649 -5.292  1.00 13.45 ?  116 PHE   B CB   1 
ATOM   5819 C CG   . PHE   B 1 116 ? 37.071 -19.592 -4.749  1.00 13.58 ?  116 PHE   B CG   1 
ATOM   5820 C CD1  . PHE   B 1 116 ? 37.715 -19.403 -3.535  1.00 13.97 ?  116 PHE   B CD1  1 
ATOM   5821 C CD2  . PHE   B 1 116 ? 37.374 -20.734 -5.479  1.00 13.12 ?  116 PHE   B CD2  1 
ATOM   5822 C CE1  . PHE   B 1 116 ? 38.657 -20.320 -3.076  1.00 14.40 ?  116 PHE   B CE1  1 
ATOM   5823 C CE2  . PHE   B 1 116 ? 38.305 -21.657 -5.025  1.00 14.08 ?  116 PHE   B CE2  1 
ATOM   5824 C CZ   . PHE   B 1 116 ? 38.939 -21.452 -3.825  1.00 14.02 ?  116 PHE   B CZ   1 
ATOM   5825 H H    . PHE   B 1 116 ? 35.379 -17.849 -3.031  1.00 16.23 ?  116 PHE   B H    1 
ATOM   5826 H HA   . PHE   B 1 116 ? 36.938 -16.864 -4.870  1.00 16.51 ?  116 PHE   B HA   1 
ATOM   5827 H HB2  . PHE   B 1 116 ? 35.132 -19.033 -5.069  1.00 16.16 ?  116 PHE   B HB2  1 
ATOM   5828 H HB3  . PHE   B 1 116 ? 36.092 -18.633 -6.261  1.00 16.16 ?  116 PHE   B HB3  1 
ATOM   5829 H HD1  . PHE   B 1 116 ? 37.520 -18.655 -3.022  1.00 16.77 ?  116 PHE   B HD1  1 
ATOM   5830 H HD2  . PHE   B 1 116 ? 36.938 -20.891 -6.289  1.00 15.76 ?  116 PHE   B HD2  1 
ATOM   5831 H HE1  . PHE   B 1 116 ? 39.091 -20.182 -2.263  1.00 17.29 ?  116 PHE   B HE1  1 
ATOM   5832 H HE2  . PHE   B 1 116 ? 38.499 -22.411 -5.538  1.00 16.91 ?  116 PHE   B HE2  1 
ATOM   5833 H HZ   . PHE   B 1 116 ? 39.578 -22.060 -3.525  1.00 16.84 ?  116 PHE   B HZ   1 
ATOM   5834 N N    . ASN   B 1 117 ? 33.863 -16.162 -5.307  1.00 13.36 ?  117 ASN   B N    1 
ATOM   5835 C CA   . ASN   B 1 117 ? 32.923 -15.461 -6.182  1.00 13.95 ?  117 ASN   B CA   1 
ATOM   5836 C C    . ASN   B 1 117 ? 33.242 -13.987 -6.339  1.00 14.61 ?  117 ASN   B C    1 
ATOM   5837 O O    . ASN   B 1 117 ? 32.648 -13.335 -7.200  1.00 16.03 ?  117 ASN   B O    1 
ATOM   5838 C CB   . ASN   B 1 117 ? 31.495 -15.673 -5.693  1.00 14.63 ?  117 ASN   B CB   1 
ATOM   5839 C CG   . ASN   B 1 117 ? 31.033 -17.091 -5.923  1.00 14.28 ?  117 ASN   B CG   1 
ATOM   5840 O OD1  . ASN   B 1 117 ? 31.379 -17.691 -6.939  1.00 15.27 ?  117 ASN   B OD1  1 
ATOM   5841 N ND2  . ASN   B 1 117 ? 30.314 -17.648 -4.967  1.00 14.12 ?  117 ASN   B ND2  1 
ATOM   5842 H H    . ASN   B 1 117 ? 33.532 -16.412 -4.549  1.00 16.05 ?  117 ASN   B H    1 
ATOM   5843 H HA   . ASN   B 1 117 ? 32.981 -15.865 -7.060  1.00 16.76 ?  117 ASN   B HA   1 
ATOM   5844 H HB2  . ASN   B 1 117 ? 31.444 -15.488 -4.739  1.00 17.57 ?  117 ASN   B HB2  1 
ATOM   5845 H HB3  . ASN   B 1 117 ? 30.896 -15.077 -6.175  1.00 17.57 ?  117 ASN   B HB3  1 
ATOM   5846 H HD21 . ASN   B 1 117 ? 30.023 -18.457 -5.052  1.00 16.96 ?  117 ASN   B HD21 1 
ATOM   5847 H HD22 . ASN   B 1 117 ? 30.090 -17.196 -4.263  1.00 16.96 ?  117 ASN   B HD22 1 
ATOM   5848 N N    . GLN   B 1 118 ? 34.176 -13.459 -5.558  1.00 14.28 ?  118 GLN   B N    1 
ATOM   5849 C CA   . GLN   B 1 118 ? 34.603 -12.074 -5.703  1.00 14.46 ?  118 GLN   B CA   1 
ATOM   5850 C C    . GLN   B 1 118 ? 35.676 -11.892 -6.773  1.00 15.28 ?  118 GLN   B C    1 
ATOM   5851 O O    . GLN   B 1 118 ? 36.147 -10.769 -6.967  1.00 16.58 ?  118 GLN   B O    1 
ATOM   5852 C CB   . GLN   B 1 118 ? 35.089 -11.533 -4.348  1.00 14.79 ?  118 GLN   B CB   1 
ATOM   5853 C CG   . GLN   B 1 118 ? 34.011 -11.585 -3.272  1.00 15.62 ?  118 GLN   B CG   1 
ATOM   5854 C CD   . GLN   B 1 118 ? 32.847 -10.661 -3.589  1.00 15.76 ?  118 GLN   B CD   1 
ATOM   5855 O OE1  . GLN   B 1 118 ? 33.045 -9.512  -3.998  1.00 16.73 ?  118 GLN   B OE1  1 
ATOM   5856 N NE2  . GLN   B 1 118 ? 31.628 -11.153 -3.412  1.00 15.67 ?  118 GLN   B NE2  1 
ATOM   5857 H H    . GLN   B 1 118 ? 34.583 -13.881 -4.929  1.00 17.15 ?  118 GLN   B H    1 
ATOM   5858 H HA   . GLN   B 1 118 ? 33.836 -11.540 -5.968  1.00 17.36 ?  118 GLN   B HA   1 
ATOM   5859 H HB2  . GLN   B 1 118 ? 35.842 -12.060 -4.044  1.00 17.76 ?  118 GLN   B HB2  1 
ATOM   5860 H HB3  . GLN   B 1 118 ? 35.351 -10.604 -4.447  1.00 17.76 ?  118 GLN   B HB3  1 
ATOM   5861 H HG2  . GLN   B 1 118 ? 33.678 -12.502 -3.208  1.00 18.76 ?  118 GLN   B HG2  1 
ATOM   5862 H HG3  . GLN   B 1 118 ? 34.400 -11.322 -2.423  1.00 18.76 ?  118 GLN   B HG3  1 
ATOM   5863 H HE21 . GLN   B 1 118 ? 31.529 -11.961 -3.114  1.00 18.82 ?  118 GLN   B HE21 1 
ATOM   5864 H HE22 . GLN   B 1 118 ? 30.942 -10.670 -3.571  1.00 18.82 ?  118 GLN   B HE22 1 
ATOM   5865 N N    . HIS   B 1 119 ? 36.051 -12.948 -7.492  1.00 14.81 ?  119 HIS   B N    1 
ATOM   5866 C CA   . HIS   B 1 119 ? 37.080 -12.893 -8.520  1.00 14.14 ?  119 HIS   B CA   1 
ATOM   5867 C C    . HIS   B 1 119 ? 36.579 -13.639 -9.739  1.00 15.28 ?  119 HIS   B C    1 
ATOM   5868 O O    . HIS   B 1 119 ? 36.060 -14.750 -9.617  1.00 15.83 ?  119 HIS   B O    1 
ATOM   5869 C CB   . HIS   B 1 119 ? 38.359 -13.517 -7.982  1.00 15.40 ?  119 HIS   B CB   1 
ATOM   5870 C CG   . HIS   B 1 119 ? 38.835 -12.832 -6.747  1.00 16.16 ?  119 HIS   B CG   1 
ATOM   5871 N ND1  . HIS   B 1 119 ? 39.625 -11.700 -6.789  1.00 17.65 ?  119 HIS   B ND1  1 
ATOM   5872 C CD2  . HIS   B 1 119 ? 38.543 -13.041 -5.442  1.00 17.81 ?  119 HIS   B CD2  1 
ATOM   5873 C CE1  . HIS   B 1 119 ? 39.832 -11.272 -5.559  1.00 19.17 ?  119 HIS   B CE1  1 
ATOM   5874 N NE2  . HIS   B 1 119 ? 39.184 -12.063 -4.724  1.00 19.54 ?  119 HIS   B NE2  1 
ATOM   5875 H H    . HIS   B 1 119 ? 35.709 -13.732 -7.404  1.00 17.78 ?  119 HIS   B H    1 
ATOM   5876 H HA   . HIS   B 1 119 ? 37.259 -11.964 -8.766  1.00 16.98 ?  119 HIS   B HA   1 
ATOM   5877 H HB2  . HIS   B 1 119 ? 38.198 -14.448 -7.772  1.00 18.50 ?  119 HIS   B HB2  1 
ATOM   5878 H HB3  . HIS   B 1 119 ? 39.060 -13.445 -8.655  1.00 18.50 ?  119 HIS   B HB3  1 
ATOM   5879 H HD2  . HIS   B 1 119 ? 38.012 -13.725 -5.098  1.00 21.39 ?  119 HIS   B HD2  1 
ATOM   5880 H HE1  . HIS   B 1 119 ? 40.362 -10.550 -5.315  1.00 23.02 ?  119 HIS   B HE1  1 
ATOM   5881 H HE2  . HIS   B 1 119 ? 39.184 -11.994 -3.865  1.00 23.46 ?  119 HIS   B HE2  1 
ATOM   5882 N N    A GLU   B 1 120 ? 36.743 -13.033 -10.915 0.46 16.07 ?  120 GLU   B N    1 
ATOM   5883 N N    B GLU   B 1 120 ? 36.748 -13.041 -10.918 0.54 15.75 ?  120 GLU   B N    1 
ATOM   5884 C CA   A GLU   B 1 120 ? 36.148 -13.610 -12.115 0.46 17.17 ?  120 GLU   B CA   1 
ATOM   5885 C CA   B GLU   B 1 120 ? 36.136 -13.622 -12.107 0.54 16.68 ?  120 GLU   B CA   1 
ATOM   5886 C C    A GLU   B 1 120 ? 36.822 -14.913 -12.525 0.46 16.04 ?  120 GLU   B C    1 
ATOM   5887 C C    B GLU   B 1 120 ? 36.826 -14.909 -12.544 0.54 15.85 ?  120 GLU   B C    1 
ATOM   5888 O O    A GLU   B 1 120 ? 36.159 -15.788 -13.091 0.46 15.85 ?  120 GLU   B O    1 
ATOM   5889 O O    B GLU   B 1 120 ? 36.178 -15.764 -13.156 0.54 15.63 ?  120 GLU   B O    1 
ATOM   5890 C CB   A GLU   B 1 120 ? 36.168 -12.601 -13.263 0.46 21.13 ?  120 GLU   B CB   1 
ATOM   5891 C CB   B GLU   B 1 120 ? 36.097 -12.604 -13.249 0.54 20.49 ?  120 GLU   B CB   1 
ATOM   5892 C CG   A GLU   B 1 120 ? 35.204 -11.438 -13.073 0.46 25.91 ?  120 GLU   B CG   1 
ATOM   5893 C CG   B GLU   B 1 120 ? 35.175 -11.422 -12.975 0.54 25.61 ?  120 GLU   B CG   1 
ATOM   5894 C CD   A GLU   B 1 120 ? 35.110 -10.548 -14.293 0.46 30.82 ?  120 GLU   B CD   1 
ATOM   5895 C CD   B GLU   B 1 120 ? 35.000 -10.494 -14.160 0.54 30.92 ?  120 GLU   B CD   1 
ATOM   5896 O OE1  A GLU   B 1 120 ? 36.162 -10.261 -14.906 0.46 32.77 ?  120 GLU   B OE1  1 
ATOM   5897 O OE1  B GLU   B 1 120 ? 35.946 -10.359 -14.965 0.54 32.98 ?  120 GLU   B OE1  1 
ATOM   5898 O OE2  A GLU   B 1 120 ? 33.981 -10.143 -14.640 0.46 33.47 -1 120 GLU   B OE2  1 
ATOM   5899 O OE2  B GLU   B 1 120 ? 33.909 -9.896  -14.279 0.54 34.05 -1 120 GLU   B OE2  1 
ATOM   5900 H H    A GLU   B 1 120 ? 37.187 -12.306 -11.044 0.46 19.29 ?  120 GLU   B H    1 
ATOM   5901 H H    B GLU   B 1 120 ? 37.202 -12.321 -11.055 0.54 18.92 ?  120 GLU   B H    1 
ATOM   5902 H HA   A GLU   B 1 120 ? 35.222 -13.816 -11.924 0.46 20.62 ?  120 GLU   B HA   1 
ATOM   5903 H HA   B GLU   B 1 120 ? 35.220 -13.850 -11.891 0.54 20.03 ?  120 GLU   B HA   1 
ATOM   5904 H HB2  A GLU   B 1 120 ? 37.060 -12.233 -13.344 0.46 25.37 ?  120 GLU   B HB2  1 
ATOM   5905 H HB2  B GLU   B 1 120 ? 36.990 -12.260 -13.391 0.54 24.60 ?  120 GLU   B HB2  1 
ATOM   5906 H HB3  A GLU   B 1 120 ? 35.923 -13.056 -14.084 0.46 25.37 ?  120 GLU   B HB3  1 
ATOM   5907 H HB3  B GLU   B 1 120 ? 35.782 -13.051 -14.050 0.54 24.60 ?  120 GLU   B HB3  1 
ATOM   5908 H HG2  A GLU   B 1 120 ? 34.315 -11.786 -12.897 0.46 31.11 ?  120 GLU   B HG2  1 
ATOM   5909 H HG2  B GLU   B 1 120 ? 34.294 -11.755 -12.745 0.54 30.75 ?  120 GLU   B HG2  1 
ATOM   5910 H HG3  A GLU   B 1 120 ? 35.502 -10.895 -12.328 0.46 31.11 ?  120 GLU   B HG3  1 
ATOM   5911 H HG3  B GLU   B 1 120 ? 35.537 -10.902 -12.245 0.54 30.75 ?  120 GLU   B HG3  1 
ATOM   5912 N N    . VAL   B 1 121 ? 38.123 -15.053 -12.273 1.00 15.44 ?  121 VAL   B N    1 
ATOM   5913 C CA   . VAL   B 1 121 ? 38.866 -16.266 -12.616 1.00 14.91 ?  121 VAL   B CA   1 
ATOM   5914 C C    . VAL   B 1 121 ? 39.979 -16.463 -11.596 1.00 15.05 ?  121 VAL   B C    1 
ATOM   5915 O O    . VAL   B 1 121 ? 40.659 -15.503 -11.215 1.00 15.41 ?  121 VAL   B O    1 
ATOM   5916 C CB   . VAL   B 1 121 ? 39.400 -16.219 -14.067 1.00 16.62 ?  121 VAL   B CB   1 
ATOM   5917 C CG1  . VAL   B 1 121 ? 40.261 -14.978 -14.307 1.00 18.82 ?  121 VAL   B CG1  1 
ATOM   5918 C CG2  . VAL   B 1 121 ? 40.157 -17.500 -14.413 1.00 18.50 ?  121 VAL   B CG2  1 
ATOM   5919 H H    A VAL   B 1 121 ? 38.610 -14.443 -11.905 0.46 18.55 ?  121 VAL   B H    1 
ATOM   5920 H H    B VAL   B 1 121 ? 38.607 -14.445 -11.898 0.54 18.55 ?  121 VAL   B H    1 
ATOM   5921 H HA   . VAL   B 1 121 ? 38.264 -17.020 -12.546 1.00 17.91 ?  121 VAL   B HA   1 
ATOM   5922 H HB   . VAL   B 1 121 ? 38.635 -16.165 -14.669 1.00 19.95 ?  121 VAL   B HB   1 
ATOM   5923 H HG11 . VAL   B 1 121 ? 40.577 -14.988 -15.223 1.00 22.60 ?  121 VAL   B HG11 1 
ATOM   5924 H HG12 . VAL   B 1 121 ? 39.721 -14.185 -14.153 1.00 22.60 ?  121 VAL   B HG12 1 
ATOM   5925 H HG13 . VAL   B 1 121 ? 41.010 -14.993 -13.695 1.00 22.60 ?  121 VAL   B HG13 1 
ATOM   5926 H HG21 . VAL   B 1 121 ? 40.359 -17.495 -15.365 1.00 22.21 ?  121 VAL   B HG21 1 
ATOM   5927 H HG22 . VAL   B 1 121 ? 40.982 -17.524 -13.904 1.00 22.21 ?  121 VAL   B HG22 1 
ATOM   5928 H HG23 . VAL   B 1 121 ? 39.606 -18.264 -14.197 1.00 22.21 ?  121 VAL   B HG23 1 
ATOM   5929 N N    . LEU   B 1 122 ? 40.166 -17.713 -11.146 1.00 14.95 ?  122 LEU   B N    1 
ATOM   5930 C CA   . LEU   B 1 122 ? 41.153 -18.067 -10.124 1.00 14.11 ?  122 LEU   B CA   1 
ATOM   5931 C C    . LEU   B 1 122 ? 41.819 -19.392 -10.456 1.00 13.76 ?  122 LEU   B C    1 
ATOM   5932 O O    . LEU   B 1 122 ? 41.156 -20.312 -10.952 1.00 14.90 ?  122 LEU   B O    1 
ATOM   5933 C CB   . LEU   B 1 122 ? 40.503 -18.295 -8.739  1.00 16.55 ?  122 LEU   B CB   1 
ATOM   5934 C CG   . LEU   B 1 122 ? 39.458 -17.285 -8.257  1.00 16.31 ?  122 LEU   B CG   1 
ATOM   5935 C CD1  . LEU   B 1 122 ? 38.061 -17.693 -8.733  1.00 17.23 ?  122 LEU   B CD1  1 
ATOM   5936 C CD2  . LEU   B 1 122 ? 39.496 -17.148 -6.747  1.00 15.45 ?  122 LEU   B CD2  1 
ATOM   5937 H H    . LEU   B 1 122 ? 39.727 -18.397 -11.424 1.00 17.95 ?  122 LEU   B H    1 
ATOM   5938 H HA   . LEU   B 1 122 ? 41.837 -17.383 -10.036 1.00 16.95 ?  122 LEU   B HA   1 
ATOM   5939 H HB2  . LEU   B 1 122 ? 40.063 -19.160 -8.755  1.00 19.88 ?  122 LEU   B HB2  1 
ATOM   5940 H HB3  . LEU   B 1 122 ? 41.202 -18.309 -8.070  1.00 19.88 ?  122 LEU   B HB3  1 
ATOM   5941 H HG   . LEU   B 1 122 ? 39.661 -16.416 -8.642  1.00 19.59 ?  122 LEU   B HG   1 
ATOM   5942 H HD11 . LEU   B 1 122 ? 37.412 -17.050 -8.400  1.00 20.68 ?  122 LEU   B HD11 1 
ATOM   5943 H HD12 . LEU   B 1 122 ? 38.042 -17.701 -9.704  1.00 20.68 ?  122 LEU   B HD12 1 
ATOM   5944 H HD13 . LEU   B 1 122 ? 37.853 -18.576 -8.392  1.00 20.68 ?  122 LEU   B HD13 1 
ATOM   5945 H HD21 . LEU   B 1 122 ? 38.813 -16.523 -6.463  1.00 18.56 ?  122 LEU   B HD21 1 
ATOM   5946 H HD22 . LEU   B 1 122 ? 39.340 -18.017 -6.344  1.00 18.56 ?  122 LEU   B HD22 1 
ATOM   5947 H HD23 . LEU   B 1 122 ? 40.374 -16.819 -6.480  1.00 18.56 ?  122 LEU   B HD23 1 
ATOM   5948 N N    . LEU   B 1 123 ? 43.110 -19.499 -10.123 1.00 13.39 ?  123 LEU   B N    1 
ATOM   5949 C CA   . LEU   B 1 123 ? 43.810 -20.773 -9.986  1.00 13.73 ?  123 LEU   B CA   1 
ATOM   5950 C C    . LEU   B 1 123 ? 43.767 -21.151 -8.512  1.00 13.28 ?  123 LEU   B C    1 
ATOM   5951 O O    . LEU   B 1 123 ? 44.124 -20.333 -7.659  1.00 13.82 ?  123 LEU   B O    1 
ATOM   5952 C CB   . LEU   B 1 123 ? 45.269 -20.582 -10.414 1.00 14.32 ?  123 LEU   B CB   1 
ATOM   5953 C CG   . LEU   B 1 123 ? 46.207 -21.776 -10.206 1.00 14.81 ?  123 LEU   B CG   1 
ATOM   5954 C CD1  . LEU   B 1 123 ? 45.755 -22.984 -11.033 1.00 15.12 ?  123 LEU   B CD1  1 
ATOM   5955 C CD2  . LEU   B 1 123 ? 47.623 -21.382 -10.562 1.00 15.82 ?  123 LEU   B CD2  1 
ATOM   5956 H H    . LEU   B 1 123 ? 43.622 -18.827 -9.970  1.00 16.08 ?  123 LEU   B H    1 
ATOM   5957 H HA   . LEU   B 1 123 ? 43.401 -21.466 -10.524 1.00 16.49 ?  123 LEU   B HA   1 
ATOM   5958 H HB2  . LEU   B 1 123 ? 45.287 -20.367 -11.359 1.00 17.20 ?  123 LEU   B HB2  1 
ATOM   5959 H HB3  . LEU   B 1 123 ? 45.640 -19.834 -9.912  1.00 17.20 ?  123 LEU   B HB3  1 
ATOM   5960 H HG   . LEU   B 1 123 ? 46.197 -22.026 -9.267  1.00 17.79 ?  123 LEU   B HG   1 
ATOM   5961 H HD11 . LEU   B 1 123 ? 46.397 -23.696 -10.917 1.00 18.15 ?  123 LEU   B HD11 1 
ATOM   5962 H HD12 . LEU   B 1 123 ? 44.881 -23.262 -10.725 1.00 18.15 ?  123 LEU   B HD12 1 
ATOM   5963 H HD13 . LEU   B 1 123 ? 45.712 -22.719 -11.966 1.00 18.15 ?  123 LEU   B HD13 1 
ATOM   5964 H HD21 . LEU   B 1 123 ? 48.207 -22.143 -10.425 1.00 19.00 ?  123 LEU   B HD21 1 
ATOM   5965 H HD22 . LEU   B 1 123 ? 47.650 -21.106 -11.493 1.00 19.00 ?  123 LEU   B HD22 1 
ATOM   5966 H HD23 . LEU   B 1 123 ? 47.903 -20.644 -9.994  1.00 19.00 ?  123 LEU   B HD23 1 
ATOM   5967 N N    . ALA   B 1 124 ? 43.340 -22.383 -8.197  1.00 13.45 ?  124 ALA   B N    1 
ATOM   5968 C CA   . ALA   B 1 124 ? 43.084 -22.702 -6.799  1.00 14.06 ?  124 ALA   B CA   1 
ATOM   5969 C C    . ALA   B 1 124 ? 43.356 -24.157 -6.462  1.00 13.07 ?  124 ALA   B C    1 
ATOM   5970 O O    . ALA   B 1 124 ? 43.241 -25.033 -7.328  1.00 13.84 ?  124 ALA   B O    1 
ATOM   5971 C CB   . ALA   B 1 124 ? 41.631 -22.383 -6.439  1.00 14.26 ?  124 ALA   B CB   1 
ATOM   5972 H H    . ALA   B 1 124 ? 43.207 -23.031 -8.755  1.00 16.15 ?  124 ALA   B H    1 
ATOM   5973 H HA   . ALA   B 1 124 ? 43.649 -22.136 -6.254  1.00 16.89 ?  124 ALA   B HA   1 
ATOM   5974 H HB1  . ALA   B 1 124 ? 41.476 -22.595 -5.508  1.00 17.13 ?  124 ALA   B HB1  1 
ATOM   5975 H HB2  . ALA   B 1 124 ? 41.458 -21.438 -6.596  1.00 17.13 ?  124 ALA   B HB2  1 
ATOM   5976 H HB3  . ALA   B 1 124 ? 41.039 -22.916 -7.001  1.00 17.13 ?  124 ALA   B HB3  1 
ATOM   5977 N N    . PRO   B 1 125 ? 43.661 -24.442 -5.199  1.00 13.23 ?  125 PRO   B N    1 
ATOM   5978 C CA   . PRO   B 1 125 ? 43.601 -25.806 -4.672  1.00 14.72 ?  125 PRO   B CA   1 
ATOM   5979 C C    . PRO   B 1 125 ? 42.205 -26.072 -4.110  1.00 15.13 ?  125 PRO   B C    1 
ATOM   5980 O O    . PRO   B 1 125 ? 41.407 -25.161 -3.905  1.00 14.98 ?  125 PRO   B O    1 
ATOM   5981 C CB   . PRO   B 1 125 ? 44.603 -25.721 -3.519  1.00 15.52 ?  125 PRO   B CB   1 
ATOM   5982 C CG   . PRO   B 1 125 ? 44.303 -24.332 -2.937  1.00 15.27 ?  125 PRO   B CG   1 
ATOM   5983 C CD   . PRO   B 1 125 ? 43.989 -23.466 -4.141  1.00 13.34 ?  125 PRO   B CD   1 
ATOM   5984 H HA   . PRO   B 1 125 ? 43.868 -26.467 -5.326  1.00 17.68 ?  125 PRO   B HA   1 
ATOM   5985 H HB2  . PRO   B 1 125 ? 44.433 -26.412 -2.867  1.00 18.64 ?  125 PRO   B HB2  1 
ATOM   5986 H HB3  . PRO   B 1 125 ? 45.515 -25.760 -3.854  1.00 18.64 ?  125 PRO   B HB3  1 
ATOM   5987 H HG2  . PRO   B 1 125 ? 43.537 -24.382 -2.342  1.00 18.34 ?  125 PRO   B HG2  1 
ATOM   5988 H HG3  . PRO   B 1 125 ? 45.081 -23.994 -2.462  1.00 18.34 ?  125 PRO   B HG3  1 
ATOM   5989 H HD2  . PRO   B 1 125 ? 43.228 -22.881 -3.961  1.00 16.03 ?  125 PRO   B HD2  1 
ATOM   5990 H HD3  . PRO   B 1 125 ? 44.770 -22.935 -4.399  1.00 16.03 ?  125 PRO   B HD3  1 
ATOM   5991 N N    . LEU   B 1 126 ? 41.932 -27.346 -3.836  1.00 15.04 ?  126 LEU   B N    1 
ATOM   5992 C CA   . LEU   B 1 126 ? 40.715 -27.723 -3.123  1.00 15.90 ?  126 LEU   B CA   1 
ATOM   5993 C C    . LEU   B 1 126 ? 40.825 -27.318 -1.661  1.00 15.27 ?  126 LEU   B C    1 
ATOM   5994 O O    . LEU   B 1 126 ? 41.717 -27.775 -0.942  1.00 17.12 ?  126 LEU   B O    1 
ATOM   5995 C CB   . LEU   B 1 126 ? 40.460 -29.225 -3.232  1.00 17.02 ?  126 LEU   B CB   1 
ATOM   5996 C CG   . LEU   B 1 126 ? 39.936 -29.715 -4.579  1.00 17.36 ?  126 LEU   B CG   1 
ATOM   5997 C CD1  . LEU   B 1 126 ? 40.003 -31.234 -4.649  1.00 19.59 ?  126 LEU   B CD1  1 
ATOM   5998 C CD2  . LEU   B 1 126 ? 38.505 -29.231 -4.828  1.00 17.95 ?  126 LEU   B CD2  1 
ATOM   5999 H H    . LEU   B 1 126 ? 42.446 -28.007 -4.034  1.00 18.06 ?  126 LEU   B H    1 
ATOM   6000 H HA   . LEU   B 1 126 ? 39.964 -27.255 -3.507  1.00 19.10 ?  126 LEU   B HA   1 
ATOM   6001 H HB2  . LEU   B 1 126 ? 41.292 -29.692 -3.055  1.00 20.44 ?  126 LEU   B HB2  1 
ATOM   6002 H HB3  . LEU   B 1 126 ? 39.804 -29.472 -2.558  1.00 20.44 ?  126 LEU   B HB3  1 
ATOM   6003 H HG   . LEU   B 1 126 ? 40.503 -29.347 -5.281  1.00 20.84 ?  126 LEU   B HG   1 
ATOM   6004 H HD11 . LEU   B 1 126 ? 39.664 -31.522 -5.509  1.00 23.52 ?  126 LEU   B HD11 1 
ATOM   6005 H HD12 . LEU   B 1 126 ? 40.924 -31.515 -4.540  1.00 23.52 ?  126 LEU   B HD12 1 
ATOM   6006 H HD13 . LEU   B 1 126 ? 39.457 -31.603 -3.936  1.00 23.52 ?  126 LEU   B HD13 1 
ATOM   6007 H HD21 . LEU   B 1 126 ? 38.177 -29.631 -5.647  1.00 21.56 ?  126 LEU   B HD21 1 
ATOM   6008 H HD22 . LEU   B 1 126 ? 37.947 -29.496 -4.081  1.00 21.56 ?  126 LEU   B HD22 1 
ATOM   6009 H HD23 . LEU   B 1 126 ? 38.501 -28.261 -4.911  1.00 21.56 ?  126 LEU   B HD23 1 
ATOM   6010 N N    . LEU   B 1 127 ? 39.896 -26.489 -1.208  1.00 15.43 ?  127 LEU   B N    1 
ATOM   6011 C CA   . LEU   B 1 127 ? 39.946 -25.990 0.155   1.00 15.52 ?  127 LEU   B CA   1 
ATOM   6012 C C    . LEU   B 1 127 ? 39.676 -27.109 1.152   1.00 15.65 ?  127 LEU   B C    1 
ATOM   6013 O O    . LEU   B 1 127 ? 38.849 -28.002 0.927   1.00 16.21 ?  127 LEU   B O    1 
ATOM   6014 C CB   . LEU   B 1 127 ? 38.916 -24.876 0.358   1.00 16.16 ?  127 LEU   B CB   1 
ATOM   6015 C CG   . LEU   B 1 127 ? 39.107 -23.612 -0.469  1.00 16.10 ?  127 LEU   B CG   1 
ATOM   6016 C CD1  . LEU   B 1 127 ? 37.991 -22.643 -0.136  1.00 17.23 ?  127 LEU   B CD1  1 
ATOM   6017 C CD2  . LEU   B 1 127 ? 40.462 -22.977 -0.207  1.00 17.32 ?  127 LEU   B CD2  1 
ATOM   6018 H H    . LEU   B 1 127 ? 39.243 -26.180 -1.674  1.00 18.53 ?  127 LEU   B H    1 
ATOM   6019 H HA   . LEU   B 1 127 ? 40.830 -25.618 0.334   1.00 18.64 ?  127 LEU   B HA   1 
ATOM   6020 H HB2  . LEU   B 1 127 ? 38.041 -25.236 0.139   1.00 19.40 ?  127 LEU   B HB2  1 
ATOM   6021 H HB3  . LEU   B 1 127 ? 38.930 -24.616 1.291   1.00 19.40 ?  127 LEU   B HB3  1 
ATOM   6022 H HG   . LEU   B 1 127 ? 39.037 -23.821 -1.411  1.00 19.33 ?  127 LEU   B HG   1 
ATOM   6023 H HD11 . LEU   B 1 127 ? 38.109 -21.830 -0.658  1.00 20.68 ?  127 LEU   B HD11 1 
ATOM   6024 H HD12 . LEU   B 1 127 ? 37.139 -23.049 -0.349  1.00 20.68 ?  127 LEU   B HD12 1 
ATOM   6025 H HD13 . LEU   B 1 127 ? 38.030 -22.428 0.811   1.00 20.68 ?  127 LEU   B HD13 1 
ATOM   6026 H HD21 . LEU   B 1 127 ? 40.495 -22.105 -0.637  1.00 20.80 ?  127 LEU   B HD21 1 
ATOM   6027 H HD22 . LEU   B 1 127 ? 40.584 -22.874 0.750   1.00 20.80 ?  127 LEU   B HD22 1 
ATOM   6028 H HD23 . LEU   B 1 127 ? 41.151 -23.551 -0.571  1.00 20.80 ?  127 LEU   B HD23 1 
ATOM   6029 N N    . SER   B 1 128 ? 40.359 -27.017 2.285   1.00 15.66 ?  128 SER   B N    1 
ATOM   6030 C CA   . SER   B 1 128 ? 40.261 -27.926 3.413   1.00 16.15 ?  128 SER   B CA   1 
ATOM   6031 C C    . SER   B 1 128 ? 40.768 -29.329 3.094   1.00 16.55 ?  128 SER   B C    1 
ATOM   6032 O O    . SER   B 1 128 ? 40.656 -30.210 3.939   1.00 19.10 ?  128 SER   B O    1 
ATOM   6033 C CB   . SER   B 1 128 ? 38.859 -27.949 4.043   1.00 17.00 ?  128 SER   B CB   1 
ATOM   6034 O OG   . SER   B 1 128 ? 38.540 -26.670 4.596   1.00 17.45 ?  128 SER   B OG   1 
ATOM   6035 H H    . SER   B 1 128 ? 40.925 -26.377 2.435   1.00 18.80 ?  128 SER   B H    1 
ATOM   6036 H HA   . SER   B 1 128 ? 40.848 -27.587 4.096   1.00 19.39 ?  128 SER   B HA   1 
ATOM   6037 H HB2  . SER   B 1 128 ? 38.204 -28.177 3.366   1.00 20.41 ?  128 SER   B HB2  1 
ATOM   6038 H HB3  . SER   B 1 128 ? 38.843 -28.615 4.754   1.00 20.41 ?  128 SER   B HB3  1 
ATOM   6039 H HG   . SER   B 1 128 ? 39.111 -26.470 5.181   1.00 20.96 ?  128 SER   B HG   1 
ATOM   6040 N N    . ALA   B 1 129 ? 41.370 -29.546 1.925   1.00 18.14 ?  129 ALA   B N    1 
ATOM   6041 C CA   . ALA   B 1 129 ? 41.900 -30.854 1.563   1.00 19.80 ?  129 ALA   B CA   1 
ATOM   6042 C C    . ALA   B 1 129 ? 43.289 -31.049 2.158   1.00 18.44 ?  129 ALA   B C    1 
ATOM   6043 O O    . ALA   B 1 129 ? 43.843 -30.166 2.823   1.00 17.83 ?  129 ALA   B O    1 
ATOM   6044 C CB   . ALA   B 1 129 ? 41.942 -31.013 0.046   1.00 22.01 ?  129 ALA   B CB   1 
ATOM   6045 H H    . ALA   B 1 129 ? 41.498 -28.945 1.321   1.00 21.78 ?  129 ALA   B H    1 
ATOM   6046 H HA   . ALA   B 1 129 ? 41.322 -31.544 1.921   1.00 23.78 ?  129 ALA   B HA   1 
ATOM   6047 H HB1  . ALA   B 1 129 ? 42.285 -31.894 -0.174  1.00 26.43 ?  129 ALA   B HB1  1 
ATOM   6048 H HB2  . ALA   B 1 129 ? 41.044 -30.910 -0.305  1.00 26.43 ?  129 ALA   B HB2  1 
ATOM   6049 H HB3  . ALA   B 1 129 ? 42.523 -30.331 -0.327  1.00 26.43 ?  129 ALA   B HB3  1 
ATOM   6050 N N    . GLY   B 1 130 ? 43.856 -32.230 1.913   1.00 18.58 ?  130 GLY   B N    1 
ATOM   6051 C CA   . GLY   B 1 130 ? 45.245 -32.476 2.277   1.00 18.73 ?  130 GLY   B CA   1 
ATOM   6052 C C    . GLY   B 1 130 ? 45.454 -32.371 3.771   1.00 18.83 ?  130 GLY   B C    1 
ATOM   6053 O O    . GLY   B 1 130 ? 44.745 -33.003 4.565   1.00 20.86 ?  130 GLY   B O    1 
ATOM   6054 H H    . GLY   B 1 130 ? 43.464 -32.898 1.535   1.00 22.31 ?  130 GLY   B H    1 
ATOM   6055 H HA2  . GLY   B 1 130 ? 45.505 -33.366 1.994   1.00 22.49 ?  130 GLY   B HA2  1 
ATOM   6056 H HA3  . GLY   B 1 130 ? 45.817 -31.829 1.838   1.00 22.49 ?  130 GLY   B HA3  1 
ATOM   6057 N N    . ILE   B 1 131 ? 46.420 -31.539 4.170   1.00 19.65 ?  131 ILE   B N    1 
ATOM   6058 C CA   . ILE   B 1 131 ? 46.758 -31.393 5.575   1.00 20.35 ?  131 ILE   B CA   1 
ATOM   6059 C C    . ILE   B 1 131 ? 45.626 -30.803 6.402   1.00 19.35 ?  131 ILE   B C    1 
ATOM   6060 O O    . ILE   B 1 131 ? 45.681 -30.870 7.628   1.00 20.97 ?  131 ILE   B O    1 
ATOM   6061 C CB   . ILE   B 1 131 ? 48.077 -30.602 5.783   1.00 22.17 ?  131 ILE   B CB   1 
ATOM   6062 C CG1  . ILE   B 1 131 ? 47.930 -29.126 5.374   1.00 22.26 ?  131 ILE   B CG1  1 
ATOM   6063 C CG2  . ILE   B 1 131 ? 49.232 -31.260 5.023   1.00 23.93 ?  131 ILE   B CG2  1 
ATOM   6064 C CD1  . ILE   B 1 131 ? 49.141 -28.261 5.756   1.00 23.55 ?  131 ILE   B CD1  1 
ATOM   6065 H H    . ILE   B 1 131 ? 46.899 -31.057 3.641   1.00 23.59 ?  131 ILE   B H    1 
ATOM   6066 H HA   . ILE   B 1 131 ? 46.918 -32.275 5.933   1.00 24.44 ?  131 ILE   B HA   1 
ATOM   6067 H HB   . ILE   B 1 131 ? 48.294 -30.624 6.729   1.00 26.61 ?  131 ILE   B HB   1 
ATOM   6068 H HG12 . ILE   B 1 131 ? 47.825 -29.074 4.412   1.00 26.73 ?  131 ILE   B HG12 1 
ATOM   6069 H HG13 . ILE   B 1 131 ? 47.154 -28.744 5.812   1.00 26.73 ?  131 ILE   B HG13 1 
ATOM   6070 H HG21 . ILE   B 1 131 ? 50.063 -30.835 5.281   1.00 28.73 ?  131 ILE   B HG21 1 
ATOM   6071 H HG22 . ILE   B 1 131 ? 49.254 -32.201 5.246   1.00 28.73 ?  131 ILE   B HG22 1 
ATOM   6072 H HG23 . ILE   B 1 131 ? 49.082 -31.147 4.071   1.00 28.73 ?  131 ILE   B HG23 1 
ATOM   6073 H HD11 . ILE   B 1 131 ? 48.940 -27.332 5.559   1.00 28.27 ?  131 ILE   B HD11 1 
ATOM   6074 H HD12 . ILE   B 1 131 ? 49.317 -28.366 6.705   1.00 28.27 ?  131 ILE   B HD12 1 
ATOM   6075 H HD13 . ILE   B 1 131 ? 49.911 -28.549 5.243   1.00 28.27 ?  131 ILE   B HD13 1 
ATOM   6076 N N    . PHE   B 1 132 ? 44.599 -30.227 5.767   1.00 17.96 ?  132 PHE   B N    1 
ATOM   6077 C CA   . PHE   B 1 132 ? 43.433 -29.728 6.493   1.00 18.81 ?  132 PHE   B CA   1 
ATOM   6078 C C    . PHE   B 1 132 ? 42.415 -30.824 6.820   1.00 20.41 ?  132 PHE   B C    1 
ATOM   6079 O O    . PHE   B 1 132 ? 41.496 -30.574 7.605   1.00 22.29 ?  132 PHE   B O    1 
ATOM   6080 C CB   . PHE   B 1 132 ? 42.754 -28.591 5.716   1.00 18.19 ?  132 PHE   B CB   1 
ATOM   6081 C CG   . PHE   B 1 132 ? 43.459 -27.252 5.824   1.00 17.65 ?  132 PHE   B CG   1 
ATOM   6082 C CD1  . PHE   B 1 132 ? 44.758 -27.075 5.357   1.00 19.54 ?  132 PHE   B CD1  1 
ATOM   6083 C CD2  . PHE   B 1 132 ? 42.797 -26.161 6.363   1.00 16.59 ?  132 PHE   B CD2  1 
ATOM   6084 C CE1  . PHE   B 1 132 ? 45.383 -25.835 5.452   1.00 20.28 ?  132 PHE   B CE1  1 
ATOM   6085 C CE2  . PHE   B 1 132 ? 43.409 -24.918 6.445   1.00 17.96 ?  132 PHE   B CE2  1 
ATOM   6086 C CZ   . PHE   B 1 132 ? 44.704 -24.757 5.996   1.00 19.72 ?  132 PHE   B CZ   1 
ATOM   6087 H H    . PHE   B 1 132 ? 44.548 -30.130 4.914   1.00 21.56 ?  132 PHE   B H    1 
ATOM   6088 H HA   . PHE   B 1 132 ? 43.740 -29.362 7.334   1.00 22.59 ?  132 PHE   B HA   1 
ATOM   6089 H HB2  . PHE   B 1 132 ? 42.728 -28.834 4.782   1.00 21.84 ?  132 PHE   B HB2  1 
ATOM   6090 H HB3  . PHE   B 1 132 ? 41.849 -28.482 6.055   1.00 21.84 ?  132 PHE   B HB3  1 
ATOM   6091 H HD1  . PHE   B 1 132 ? 45.215 -27.804 4.993   1.00 23.46 ?  132 PHE   B HD1  1 
ATOM   6092 H HD2  . PHE   B 1 132 ? 41.925 -26.260 6.671   1.00 19.92 ?  132 PHE   B HD2  1 
ATOM   6093 H HE1  . PHE   B 1 132 ? 46.253 -25.730 5.146   1.00 24.35 ?  132 PHE   B HE1  1 
ATOM   6094 H HE2  . PHE   B 1 132 ? 42.953 -24.199 6.823   1.00 21.57 ?  132 PHE   B HE2  1 
ATOM   6095 H HZ   . PHE   B 1 132 ? 45.118 -23.924 6.065   1.00 23.68 ?  132 PHE   B HZ   1 
ATOM   6096 N N    . GLY   B 1 133 ? 42.533 -32.024 6.237   1.00 20.05 ?  133 GLY   B N    1 
ATOM   6097 C CA   . GLY   B 1 133 ? 41.820 -33.189 6.739   1.00 20.41 ?  133 GLY   B CA   1 
ATOM   6098 C C    . GLY   B 1 133 ? 40.426 -33.450 6.200   1.00 20.72 ?  133 GLY   B C    1 
ATOM   6099 O O    . GLY   B 1 133 ? 39.832 -34.462 6.574   1.00 23.59 ?  133 GLY   B O    1 
ATOM   6100 H H    . GLY   B 1 133 ? 43.019 -32.182 5.545   1.00 24.07 ?  133 GLY   B H    1 
ATOM   6101 H HA2  . GLY   B 1 133 ? 42.362 -33.977 6.565   1.00 24.50 ?  133 GLY   B HA2  1 
ATOM   6102 H HA3  . GLY   B 1 133 ? 41.741 -33.104 7.705   1.00 24.50 ?  133 GLY   B HA3  1 
ATOM   6103 N N    . ALA   B 1 134 ? 39.872 -32.589 5.358   1.00 19.88 ?  134 ALA   B N    1 
ATOM   6104 C CA   . ALA   B 1 134 ? 38.545 -32.859 4.823   1.00 19.44 ?  134 ALA   B CA   1 
ATOM   6105 C C    . ALA   B 1 134 ? 38.617 -33.859 3.674   1.00 19.67 ?  134 ALA   B C    1 
ATOM   6106 O O    . ALA   B 1 134 ? 39.669 -34.073 3.066   1.00 20.98 ?  134 ALA   B O    1 
ATOM   6107 C CB   . ALA   B 1 134 ? 37.893 -31.568 4.333   1.00 19.07 ?  134 ALA   B CB   1 
ATOM   6108 H H    . ALA   B 1 134 ? 40.230 -31.853 5.103   1.00 23.87 ?  134 ALA   B H    1 
ATOM   6109 H HA   . ALA   B 1 134 ? 37.990 -33.235 5.528   1.00 23.34 ?  134 ALA   B HA   1 
ATOM   6110 H HB1  . ALA   B 1 134 ? 37.005 -31.772 4.009   1.00 22.89 ?  134 ALA   B HB1  1 
ATOM   6111 H HB2  . ALA   B 1 134 ? 37.848 -30.941 5.069   1.00 22.89 ?  134 ALA   B HB2  1 
ATOM   6112 H HB3  . ALA   B 1 134 ? 38.434 -31.201 3.615   1.00 22.89 ?  134 ALA   B HB3  1 
ATOM   6113 N N    . ASP   B 1 135 ? 37.481 -34.477 3.383   1.00 20.56 ?  135 ASP   B N    1 
ATOM   6114 C CA   . ASP   B 1 135 ? 37.387 -35.376 2.242   1.00 21.35 ?  135 ASP   B CA   1 
ATOM   6115 C C    . ASP   B 1 135 ? 37.493 -34.531 0.980   1.00 19.63 ?  135 ASP   B C    1 
ATOM   6116 O O    . ASP   B 1 135 ? 36.646 -33.649 0.764   1.00 19.56 ?  135 ASP   B O    1 
ATOM   6117 C CB   . ASP   B 1 135 ? 36.044 -36.112 2.298   1.00 22.80 ?  135 ASP   B CB   1 
ATOM   6118 C CG   . ASP   B 1 135 ? 35.848 -37.098 1.159   1.00 25.12 ?  135 ASP   B CG   1 
ATOM   6119 O OD1  . ASP   B 1 135 ? 36.702 -37.184 0.250   1.00 25.16 ?  135 ASP   B OD1  1 
ATOM   6120 O OD2  . ASP   B 1 135 ? 34.813 -37.802 1.184   1.00 27.99 -1 135 ASP   B OD2  1 
ATOM   6121 H H    . ASP   B 1 135 ? 36.753 -34.401 3.836   1.00 24.69 ?  135 ASP   B H    1 
ATOM   6122 H HA   . ASP   B 1 135 ? 38.103 -36.035 2.278   1.00 25.63 ?  135 ASP   B HA   1 
ATOM   6123 H HB2  . ASP   B 1 135 ? 35.986 -36.607 3.131   1.00 27.37 ?  135 ASP   B HB2  1 
ATOM   6124 H HB3  . ASP   B 1 135 ? 35.329 -35.464 2.246   1.00 27.37 ?  135 ASP   B HB3  1 
ATOM   6125 N N    . PRO   B 1 136 ? 38.510 -34.730 0.140   1.00 20.66 ?  136 PRO   B N    1 
ATOM   6126 C CA   . PRO   B 1 136 ? 38.595 -33.924 -1.087  1.00 19.72 ?  136 PRO   B CA   1 
ATOM   6127 C C    . PRO   B 1 136 ? 37.393 -34.086 -2.003  1.00 18.27 ?  136 PRO   B C    1 
ATOM   6128 O O    . PRO   B 1 136 ? 37.063 -33.140 -2.733  1.00 17.88 ?  136 PRO   B O    1 
ATOM   6129 C CB   . PRO   B 1 136 ? 39.905 -34.397 -1.736  1.00 20.49 ?  136 PRO   B CB   1 
ATOM   6130 C CG   . PRO   B 1 136 ? 40.120 -35.784 -1.180  1.00 22.37 ?  136 PRO   B CG   1 
ATOM   6131 C CD   . PRO   B 1 136 ? 39.598 -35.724 0.229   1.00 21.82 ?  136 PRO   B CD   1 
ATOM   6132 H HA   . PRO   B 1 136 ? 38.677 -32.991 -0.856  1.00 23.68 ?  136 PRO   B HA   1 
ATOM   6133 H HB2  . PRO   B 1 136 ? 39.801 -34.424 -2.700  1.00 24.60 ?  136 PRO   B HB2  1 
ATOM   6134 H HB3  . PRO   B 1 136 ? 40.625 -33.804 -1.480  1.00 24.60 ?  136 PRO   B HB3  1 
ATOM   6135 H HG2  . PRO   B 1 136 ? 39.619 -36.433 -1.701  1.00 26.86 ?  136 PRO   B HG2  1 
ATOM   6136 H HG3  . PRO   B 1 136 ? 41.067 -35.998 -1.185  1.00 26.86 ?  136 PRO   B HG3  1 
ATOM   6137 H HD2  . PRO   B 1 136 ? 39.255 -36.590 0.501   1.00 26.20 ?  136 PRO   B HD2  1 
ATOM   6138 H HD3  . PRO   B 1 136 ? 40.289 -35.409 0.837   1.00 26.20 ?  136 PRO   B HD3  1 
ATOM   6139 N N    . ILE   B 1 137 ? 36.721 -35.246 -1.978  1.00 18.73 ?  137 ILE   B N    1 
ATOM   6140 C CA   . ILE   B 1 137 ? 35.515 -35.420 -2.781  1.00 19.41 ?  137 ILE   B CA   1 
ATOM   6141 C C    . ILE   B 1 137 ? 34.436 -34.456 -2.318  1.00 18.81 ?  137 ILE   B C    1 
ATOM   6142 O O    . ILE   B 1 137 ? 33.734 -33.841 -3.133  1.00 18.24 ?  137 ILE   B O    1 
ATOM   6143 C CB   . ILE   B 1 137 ? 35.043 -36.889 -2.718  1.00 21.42 ?  137 ILE   B CB   1 
ATOM   6144 C CG1  . ILE   B 1 137 ? 36.066 -37.797 -3.415  1.00 24.20 ?  137 ILE   B CG1  1 
ATOM   6145 C CG2  . ILE   B 1 137 ? 33.657 -37.062 -3.351  1.00 22.43 ?  137 ILE   B CG2  1 
ATOM   6146 C CD1  . ILE   B 1 137 ? 35.747 -39.289 -3.343  1.00 27.35 ?  137 ILE   B CD1  1 
ATOM   6147 H H    . ILE   B 1 137 ? 36.939 -35.942 -1.514  1.00 22.49 ?  137 ILE   B H    1 
ATOM   6148 H HA   . ILE   B 1 137 ? 35.715 -35.219 -3.707  1.00 23.30 ?  137 ILE   B HA   1 
ATOM   6149 H HB   . ILE   B 1 137 ? 34.981 -37.157 -1.788  1.00 25.72 ?  137 ILE   B HB   1 
ATOM   6150 H HG12 . ILE   B 1 137 ? 36.111 -37.553 -4.352  1.00 29.06 ?  137 ILE   B HG12 1 
ATOM   6151 H HG13 . ILE   B 1 137 ? 36.931 -37.664 -2.999  1.00 29.06 ?  137 ILE   B HG13 1 
ATOM   6152 H HG21 . ILE   B 1 137 ? 33.404 -37.999 -3.321  1.00 26.93 ?  137 ILE   B HG21 1 
ATOM   6153 H HG22 . ILE   B 1 137 ? 33.010 -36.542 -2.856  1.00 26.93 ?  137 ILE   B HG22 1 
ATOM   6154 H HG23 . ILE   B 1 137 ? 33.694 -36.762 -4.272  1.00 26.93 ?  137 ILE   B HG23 1 
ATOM   6155 H HD11 . ILE   B 1 137 ? 36.450 -39.769 -3.802  1.00 32.83 ?  137 ILE   B HD11 1 
ATOM   6156 H HD12 . ILE   B 1 137 ? 35.705 -39.562 -2.413  1.00 32.83 ?  137 ILE   B HD12 1 
ATOM   6157 H HD13 . ILE   B 1 137 ? 34.898 -39.462 -3.780  1.00 32.83 ?  137 ILE   B HD13 1 
ATOM   6158 N N    . HIS   B 1 138 ? 34.302 -34.297 -1.000  1.00 18.96 ?  138 HIS   B N    1 
ATOM   6159 C CA   . HIS   B 1 138 ? 33.364 -33.321 -0.464  1.00 19.38 ?  138 HIS   B CA   1 
ATOM   6160 C C    . HIS   B 1 138 ? 33.785 -31.898 -0.802  1.00 18.43 ?  138 HIS   B C    1 
ATOM   6161 O O    . HIS   B 1 138 ? 32.939 -31.056 -1.113  1.00 18.84 ?  138 HIS   B O    1 
ATOM   6162 C CB   . HIS   B 1 138 ? 33.252 -33.482 1.045   1.00 20.57 ?  138 HIS   B CB   1 
ATOM   6163 C CG   . HIS   B 1 138 ? 32.316 -32.505 1.669   1.00 21.47 ?  138 HIS   B CG   1 
ATOM   6164 N ND1  . HIS   B 1 138 ? 30.973 -32.453 1.351   1.00 23.76 ?  138 HIS   B ND1  1 
ATOM   6165 C CD2  . HIS   B 1 138 ? 32.534 -31.513 2.564   1.00 22.59 ?  138 HIS   B CD2  1 
ATOM   6166 C CE1  . HIS   B 1 138 ? 30.406 -31.475 2.034   1.00 24.41 ?  138 HIS   B CE1  1 
ATOM   6167 N NE2  . HIS   B 1 138 ? 31.329 -30.895 2.783   1.00 23.25 ?  138 HIS   B NE2  1 
ATOM   6168 H H    . HIS   B 1 138 ? 34.743 -34.739 -0.405  1.00 22.77 ?  138 HIS   B H    1 
ATOM   6169 H HA   . HIS   B 1 138 ? 32.487 -33.483 -0.844  1.00 23.27 ?  138 HIS   B HA   1 
ATOM   6170 H HB2  . HIS   B 1 138 ? 32.928 -34.372 1.250   1.00 24.70 ?  138 HIS   B HB2  1 
ATOM   6171 H HB3  . HIS   B 1 138 ? 34.129 -33.351 1.443   1.00 24.70 ?  138 HIS   B HB3  1 
ATOM   6172 H HD2  . HIS   B 1 138 ? 33.343 -31.299 2.972   1.00 27.12 ?  138 HIS   B HD2  1 
ATOM   6173 H HE1  . HIS   B 1 138 ? 29.505 -31.241 2.001   1.00 29.31 ?  138 HIS   B HE1  1 
ATOM   6174 H HE2  . HIS   B 1 138 ? 31.191 -30.234 3.321   1.00 27.92 ?  138 HIS   B HE2  1 
ATOM   6175 N N    . SER   B 1 139 ? 35.081 -31.598 -0.727  1.00 17.92 ?  139 SER   B N    1 
ATOM   6176 C CA   . SER   B 1 139 ? 35.524 -30.251 -1.060  1.00 17.13 ?  139 SER   B CA   1 
ATOM   6177 C C    . SER   B 1 139 ? 35.168 -29.904 -2.496  1.00 16.07 ?  139 SER   B C    1 
ATOM   6178 O O    . SER   B 1 139 ? 34.727 -28.787 -2.780  1.00 16.41 ?  139 SER   B O    1 
ATOM   6179 C CB   . SER   B 1 139 ? 37.028 -30.110 -0.822  1.00 16.83 ?  139 SER   B CB   1 
ATOM   6180 O OG   . SER   B 1 139 ? 37.435 -28.773 -1.085  1.00 16.81 ?  139 SER   B OG   1 
ATOM   6181 H H    . SER   B 1 139 ? 35.697 -32.140 -0.480  1.00 21.52 ?  139 SER   B H    1 
ATOM   6182 H HA   . SER   B 1 139 ? 35.075 -29.617 -0.486  1.00 20.57 ?  139 SER   B HA   1 
ATOM   6183 H HB2  . SER   B 1 139 ? 37.228 -30.332 0.104   1.00 20.21 ?  139 SER   B HB2  1 
ATOM   6184 H HB3  . SER   B 1 139 ? 37.507 -30.712 -1.416  1.00 20.21 ?  139 SER   B HB3  1 
ATOM   6185 H HG   . SER   B 1 139 ? 38.261 -28.685 -0.951  1.00 20.19 ?  139 SER   B HG   1 
ATOM   6186 N N    . LEU   B 1 140 ? 35.355 -30.849 -3.419  1.00 15.78 ?  140 LEU   B N    1 
ATOM   6187 C CA   . LEU   B 1 140 ? 34.992 -30.608 -4.808  1.00 16.27 ?  140 LEU   B CA   1 
ATOM   6188 C C    . LEU   B 1 140 ? 33.493 -30.377 -4.940  1.00 16.33 ?  140 LEU   B C    1 
ATOM   6189 O O    . LEU   B 1 140 ? 33.059 -29.463 -5.650  1.00 16.53 ?  140 LEU   B O    1 
ATOM   6190 C CB   . LEU   B 1 140 ? 35.469 -31.765 -5.691  1.00 16.01 ?  140 LEU   B CB   1 
ATOM   6191 C CG   . LEU   B 1 140 ? 35.136 -31.670 -7.173  1.00 17.10 ?  140 LEU   B CG   1 
ATOM   6192 C CD1  . LEU   B 1 140 ? 35.728 -30.409 -7.776  1.00 18.54 ?  140 LEU   B CD1  1 
ATOM   6193 C CD2  . LEU   B 1 140 ? 35.637 -32.910 -7.902  1.00 17.94 ?  140 LEU   B CD2  1 
ATOM   6194 H H    . LEU   B 1 140 ? 35.677 -31.636 -3.268  1.00 18.95 ?  140 LEU   B H    1 
ATOM   6195 H HA   . LEU   B 1 140 ? 35.445 -29.808 -5.112  1.00 19.54 ?  140 LEU   B HA   1 
ATOM   6196 H HB2  . LEU   B 1 140 ? 36.437 -31.828 -5.624  1.00 19.23 ?  140 LEU   B HB2  1 
ATOM   6197 H HB3  . LEU   B 1 140 ? 35.075 -32.589 -5.365  1.00 19.23 ?  140 LEU   B HB3  1 
ATOM   6198 H HG   . LEU   B 1 140 ? 34.174 -31.632 -7.281  1.00 20.53 ?  140 LEU   B HG   1 
ATOM   6199 H HD11 . LEU   B 1 140 ? 35.609 -30.432 -8.737  1.00 22.27 ?  140 LEU   B HD11 1 
ATOM   6200 H HD12 . LEU   B 1 140 ? 35.280 -29.639 -7.401  1.00 22.27 ?  140 LEU   B HD12 1 
ATOM   6201 H HD13 . LEU   B 1 140 ? 36.678 -30.377 -7.563  1.00 22.27 ?  140 LEU   B HD13 1 
ATOM   6202 H HD21 . LEU   B 1 140 ? 35.410 -32.832 -8.844  1.00 21.55 ?  140 LEU   B HD21 1 
ATOM   6203 H HD22 . LEU   B 1 140 ? 36.595 -32.975 -7.794  1.00 21.55 ?  140 LEU   B HD22 1 
ATOM   6204 H HD23 . LEU   B 1 140 ? 35.203 -33.693 -7.524  1.00 21.55 ?  140 LEU   B HD23 1 
ATOM   6205 N N    . ARG   B 1 141 ? 32.692 -31.182 -4.235  1.00 16.18 ?  141 ARG   B N    1 
ATOM   6206 C CA   . ARG   B 1 141 ? 31.241 -30.998 -4.204  1.00 17.47 ?  141 ARG   B CA   1 
ATOM   6207 C C    . ARG   B 1 141 ? 30.866 -29.581 -3.789  1.00 17.03 ?  141 ARG   B C    1 
ATOM   6208 O O    . ARG   B 1 141 ? 30.071 -28.903 -4.463  1.00 17.53 ?  141 ARG   B O    1 
ATOM   6209 C CB   . ARG   B 1 141 ? 30.662 -32.011 -3.210  1.00 19.23 ?  141 ARG   B CB   1 
ATOM   6210 C CG   . ARG   B 1 141 ? 29.194 -31.881 -2.896  1.00 21.69 ?  141 ARG   B CG   1 
ATOM   6211 C CD   . ARG   B 1 141 ? 28.413 -32.529 -3.960  1.00 22.59 ?  141 ARG   B CD   1 
ATOM   6212 N NE   . ARG   B 1 141 ? 28.139 -31.641 -5.078  1.00 23.47 ?  141 ARG   B NE   1 
ATOM   6213 C CZ   . ARG   B 1 141 ? 28.128 -32.023 -6.348  1.00 22.75 ?  141 ARG   B CZ   1 
ATOM   6214 N NH1  . ARG   B 1 141 ? 28.589 -33.209 -6.719  1.00 22.13 ?  141 ARG   B NH1  1 
ATOM   6215 N NH2  . ARG   B 1 141 ? 27.644 -31.194 -7.268  1.00 23.05 ?  141 ARG   B NH2  1 
ATOM   6216 H H    . ARG   B 1 141 ? 32.973 -31.831 -3.749  1.00 19.43 ?  141 ARG   B H    1 
ATOM   6217 H HA   . ARG   B 1 141 ? 30.874 -31.165 -5.080  1.00 20.98 ?  141 ARG   B HA   1 
ATOM   6218 H HB2  . ARG   B 1 141 ? 30.819 -32.901 -3.564  1.00 23.09 ?  141 ARG   B HB2  1 
ATOM   6219 H HB3  . ARG   B 1 141 ? 31.141 -31.920 -2.374  1.00 23.09 ?  141 ARG   B HB3  1 
ATOM   6220 H HG2  . ARG   B 1 141 ? 29.005 -32.322 -2.055  1.00 26.04 ?  141 ARG   B HG2  1 
ATOM   6221 H HG3  . ARG   B 1 141 ? 28.936 -30.941 -2.844  1.00 26.04 ?  141 ARG   B HG3  1 
ATOM   6222 H HD2  . ARG   B 1 141 ? 28.904 -33.303 -4.283  1.00 27.12 ?  141 ARG   B HD2  1 
ATOM   6223 H HD3  . ARG   B 1 141 ? 27.567 -32.813 -3.594  1.00 27.12 ?  141 ARG   B HD3  1 
ATOM   6224 H HE   . ARG   B 1 141 ? 28.037 -30.803 -4.909  1.00 28.18 ?  141 ARG   B HE   1 
ATOM   6225 H HH11 . ARG   B 1 141 ? 28.892 -33.766 -6.136  1.00 26.57 ?  141 ARG   B HH11 1 
ATOM   6226 H HH12 . ARG   B 1 141 ? 28.571 -33.433 -7.547  1.00 26.57 ?  141 ARG   B HH12 1 
ATOM   6227 H HH21 . ARG   B 1 141 ? 27.354 -30.417 -7.038  1.00 27.67 ?  141 ARG   B HH21 1 
ATOM   6228 H HH22 . ARG   B 1 141 ? 27.646 -31.423 -8.097  1.00 27.67 ?  141 ARG   B HH22 1 
ATOM   6229 N N    . VAL   B 1 142 ? 31.399 -29.126 -2.654  1.00 16.22 ?  142 VAL   B N    1 
ATOM   6230 C CA   . VAL   B 1 142 ? 31.065 -27.788 -2.178  1.00 16.36 ?  142 VAL   B CA   1 
ATOM   6231 C C    . VAL   B 1 142 ? 31.551 -26.738 -3.166  1.00 15.93 ?  142 VAL   B C    1 
ATOM   6232 O O    . VAL   B 1 142 ? 30.864 -25.750 -3.419  1.00 16.81 ?  142 VAL   B O    1 
ATOM   6233 C CB   . VAL   B 1 142 ? 31.598 -27.549 -0.751  1.00 17.53 ?  142 VAL   B CB   1 
ATOM   6234 C CG1  . VAL   B 1 142 ? 31.290 -26.118 -0.303  1.00 17.99 ?  142 VAL   B CG1  1 
ATOM   6235 C CG2  . VAL   B 1 142 ? 30.990 -28.552 0.232   1.00 17.65 ?  142 VAL   B CG2  1 
ATOM   6236 H H    . VAL   B 1 142 ? 31.936 -29.568 -2.138  1.00 19.48 ?  142 VAL   B H    1 
ATOM   6237 H HA   . VAL   B 1 142 ? 30.103 -27.713 -2.132  1.00 19.65 ?  142 VAL   B HA   1 
ATOM   6238 H HB   . VAL   B 1 142 ? 32.562 -27.665 -0.743  1.00 21.05 ?  142 VAL   B HB   1 
ATOM   6239 H HG11 . VAL   B 1 142 ? 31.451 -26.041 0.649   1.00 21.60 ?  142 VAL   B HG11 1 
ATOM   6240 H HG12 . VAL   B 1 142 ? 31.862 -25.501 -0.786  1.00 21.60 ?  142 VAL   B HG12 1 
ATOM   6241 H HG13 . VAL   B 1 142 ? 30.357 -25.922 -0.495  1.00 21.60 ?  142 VAL   B HG13 1 
ATOM   6242 H HG21 . VAL   B 1 142 ? 31.316 -28.363 1.128   1.00 21.19 ?  142 VAL   B HG21 1 
ATOM   6243 H HG22 . VAL   B 1 142 ? 30.022 -28.473 0.213   1.00 21.19 ?  142 VAL   B HG22 1 
ATOM   6244 H HG23 . VAL   B 1 142 ? 31.250 -29.452 -0.026  1.00 21.19 ?  142 VAL   B HG23 1 
ATOM   6245 N N    . CYS   B 1 143 ? 32.725 -26.951 -3.758  1.00 15.73 ?  143 CYS   B N    1 
ATOM   6246 C CA   . CYS   B 1 143 ? 33.237 -26.017 -4.762  1.00 16.33 ?  143 CYS   B CA   1 
ATOM   6247 C C    . CYS   B 1 143 ? 32.241 -25.863 -5.909  1.00 15.35 ?  143 CYS   B C    1 
ATOM   6248 O O    . CYS   B 1 143 ? 31.828 -24.752 -6.258  1.00 15.99 ?  143 CYS   B O    1 
ATOM   6249 C CB   . CYS   B 1 143 ? 34.592 -26.510 -5.288  1.00 16.58 ?  143 CYS   B CB   1 
ATOM   6250 S SG   . CYS   B 1 143 ? 35.349 -25.405 -6.511  1.00 16.72 ?  143 CYS   B SG   1 
ATOM   6251 H H    . CYS   B 1 143 ? 33.249 -27.614 -3.588  1.00 18.89 ?  143 CYS   B H    1 
ATOM   6252 H HA   . CYS   B 1 143 ? 33.374 -25.149 -4.353  1.00 19.61 ?  143 CYS   B HA   1 
ATOM   6253 H HB2  . CYS   B 1 143 ? 35.211 -26.605 -4.547  1.00 19.92 ?  143 CYS   B HB2  1 
ATOM   6254 H HB3  . CYS   B 1 143 ? 34.466 -27.377 -5.712  1.00 19.92 ?  143 CYS   B HB3  1 
ATOM   6255 H HG   . CYS   B 1 143 ? 36.416 -25.838 -6.842  1.00 20.08 ?  143 CYS   B HG   1 
ATOM   6256 N N    . VAL   B 1 144 ? 31.828 -26.980 -6.499  1.00 16.31 ?  144 VAL   B N    1 
ATOM   6257 C CA   . VAL   B 1 144 ? 30.924 -26.926 -7.642  1.00 17.48 ?  144 VAL   B CA   1 
ATOM   6258 C C    . VAL   B 1 144 ? 29.578 -26.313 -7.269  1.00 17.25 ?  144 VAL   B C    1 
ATOM   6259 O O    . VAL   B 1 144 ? 28.953 -25.621 -8.084  1.00 18.55 ?  144 VAL   B O    1 
ATOM   6260 C CB   . VAL   B 1 144 ? 30.758 -28.360 -8.181  1.00 20.13 ?  144 VAL   B CB   1 
ATOM   6261 C CG1  . VAL   B 1 144 ? 29.477 -28.515 -8.988  1.00 23.01 ?  144 VAL   B CG1  1 
ATOM   6262 C CG2  . VAL   B 1 144 ? 32.005 -28.788 -8.973  1.00 19.53 ?  144 VAL   B CG2  1 
ATOM   6263 H H    . VAL   B 1 144 ? 32.068 -27.773 -6.269  1.00 19.59 ?  144 VAL   B H    1 
ATOM   6264 H HA   . VAL   B 1 144 ? 31.314 -26.386 -8.341  1.00 20.99 ?  144 VAL   B HA   1 
ATOM   6265 H HB   . VAL   B 1 144 ? 30.690 -28.963 -7.422  1.00 24.17 ?  144 VAL   B HB   1 
ATOM   6266 H HG11 . VAL   B 1 144 ? 29.550 -29.317 -9.530  1.00 27.62 ?  144 VAL   B HG11 1 
ATOM   6267 H HG12 . VAL   B 1 144 ? 28.731 -28.597 -8.378  1.00 27.62 ?  144 VAL   B HG12 1 
ATOM   6268 H HG13 . VAL   B 1 144 ? 29.370 -27.741 -9.557  1.00 27.62 ?  144 VAL   B HG13 1 
ATOM   6269 H HG21 . VAL   B 1 144 ? 31.879 -29.692 -9.296  1.00 23.45 ?  144 VAL   B HG21 1 
ATOM   6270 H HG22 . VAL   B 1 144 ? 32.122 -28.181 -9.722  1.00 23.45 ?  144 VAL   B HG22 1 
ATOM   6271 H HG23 . VAL   B 1 144 ? 32.778 -28.746 -8.390  1.00 23.45 ?  144 VAL   B HG23 1 
ATOM   6272 N N    . ASP   B 1 145 ? 29.112 -26.543 -6.046  1.00 17.69 ?  145 ASP   B N    1 
ATOM   6273 C CA   . ASP   B 1 145 ? 27.801 -26.064 -5.625  1.00 17.94 ?  145 ASP   B CA   1 
ATOM   6274 C C    . ASP   B 1 145 ? 27.833 -24.644 -5.077  1.00 18.11 ?  145 ASP   B C    1 
ATOM   6275 O O    . ASP   B 1 145 ? 26.776 -24.107 -4.737  1.00 19.09 ?  145 ASP   B O    1 
ATOM   6276 C CB   . ASP   B 1 145 ? 27.210 -26.984 -4.549  1.00 20.44 ?  145 ASP   B CB   1 
ATOM   6277 C CG   . ASP   B 1 145 ? 26.853 -28.373 -5.065  1.00 22.16 ?  145 ASP   B CG   1 
ATOM   6278 O OD1  . ASP   B 1 145 ? 26.743 -28.579 -6.293  1.00 22.48 ?  145 ASP   B OD1  1 
ATOM   6279 O OD2  . ASP   B 1 145 ? 26.666 -29.261 -4.210  1.00 23.98 -1 145 ASP   B OD2  1 
ATOM   6280 H H    . ASP   B 1 145 ? 29.539 -26.970 -5.435  1.00 21.24 ?  145 ASP   B H    1 
ATOM   6281 H HA   . ASP   B 1 145 ? 27.203 -26.070 -6.390  1.00 21.54 ?  145 ASP   B HA   1 
ATOM   6282 H HB2  . ASP   B 1 145 ? 27.854 -27.097 -3.842  1.00 24.54 ?  145 ASP   B HB2  1 
ATOM   6283 H HB3  . ASP   B 1 145 ? 26.396 -26.581 -4.205  1.00 24.54 ?  145 ASP   B HB3  1 
ATOM   6284 N N    . THR   B 1 146 ? 29.003 -24.031 -4.962  1.00 16.69 ?  146 THR   B N    1 
ATOM   6285 C CA   . THR   B 1 146 ? 29.143 -22.704 -4.362  1.00 16.65 ?  146 THR   B CA   1 
ATOM   6286 C C    . THR   B 1 146 ? 29.785 -21.690 -5.291  1.00 16.18 ?  146 THR   B C    1 
ATOM   6287 O O    . THR   B 1 146 ? 29.329 -20.539 -5.358  1.00 16.63 ?  146 THR   B O    1 
ATOM   6288 C CB   . THR   B 1 146 ? 29.981 -22.804 -3.078  1.00 16.60 ?  146 THR   B CB   1 
ATOM   6289 O OG1  . THR   B 1 146 ? 29.405 -23.778 -2.200  1.00 16.87 ?  146 THR   B OG1  1 
ATOM   6290 C CG2  . THR   B 1 146 ? 30.085 -21.441 -2.365  1.00 16.87 ?  146 THR   B CG2  1 
ATOM   6291 H H    . THR   B 1 146 ? 29.751 -24.362 -5.231  1.00 20.05 ?  146 THR   B H    1 
ATOM   6292 H HA   . THR   B 1 146 ? 28.274 -22.361 -4.124  1.00 19.99 ?  146 THR   B HA   1 
ATOM   6293 H HB   . THR   B 1 146 ? 30.882 -23.086 -3.307  1.00 19.94 ?  146 THR   B HB   1 
ATOM   6294 H HG1  . THR   B 1 146 ? 29.404 -24.536 -2.562  1.00 20.26 ?  146 THR   B HG1  1 
ATOM   6295 H HG21 . THR   B 1 146 ? 30.450 -21.560 -1.473  1.00 20.26 ?  146 THR   B HG21 1 
ATOM   6296 H HG22 . THR   B 1 146 ? 30.676 -20.849 -2.864  1.00 20.26 ?  146 THR   B HG22 1 
ATOM   6297 H HG23 . THR   B 1 146 ? 29.212 -21.033 -2.298  1.00 20.26 ?  146 THR   B HG23 1 
ATOM   6298 N N    . VAL   B 1 147 ? 30.850 -22.071 -5.984  1.00 15.70 ?  147 VAL   B N    1 
ATOM   6299 C CA   . VAL   B 1 147 ? 31.582 -21.133 -6.825  1.00 15.81 ?  147 VAL   B CA   1 
ATOM   6300 C C    . VAL   B 1 147 ? 30.850 -20.999 -8.146  1.00 16.23 ?  147 VAL   B C    1 
ATOM   6301 O O    . VAL   B 1 147 ? 30.469 -22.005 -8.761  1.00 16.53 ?  147 VAL   B O    1 
ATOM   6302 C CB   . VAL   B 1 147 ? 33.028 -21.600 -7.046  1.00 15.96 ?  147 VAL   B CB   1 
ATOM   6303 C CG1  . VAL   B 1 147 ? 33.782 -20.574 -7.906  1.00 16.29 ?  147 VAL   B CG1  1 
ATOM   6304 C CG2  . VAL   B 1 147 ? 33.744 -21.773 -5.720  1.00 16.06 ?  147 VAL   B CG2  1 
ATOM   6305 H H    . VAL   B 1 147 ? 31.173 -22.869 -5.991  1.00 18.86 ?  147 VAL   B H    1 
ATOM   6306 H HA   . VAL   B 1 147 ? 31.612 -20.261 -6.398  1.00 18.98 ?  147 VAL   B HA   1 
ATOM   6307 H HB   . VAL   B 1 147 ? 33.034 -22.452 -7.516  1.00 19.17 ?  147 VAL   B HB   1 
ATOM   6308 H HG11 . VAL   B 1 147 ? 34.731 -20.773 -7.896  1.00 19.56 ?  147 VAL   B HG11 1 
ATOM   6309 H HG12 . VAL   B 1 147 ? 33.450 -20.602 -8.818  1.00 19.56 ?  147 VAL   B HG12 1 
ATOM   6310 H HG13 . VAL   B 1 147 ? 33.636 -19.681 -7.536  1.00 19.56 ?  147 VAL   B HG13 1 
ATOM   6311 H HG21 . VAL   B 1 147 ? 34.675 -22.001 -5.889  1.00 19.28 ?  147 VAL   B HG21 1 
ATOM   6312 H HG22 . VAL   B 1 147 ? 33.700 -20.934 -5.230  1.00 19.28 ?  147 VAL   B HG22 1 
ATOM   6313 H HG23 . VAL   B 1 147 ? 33.316 -22.476 -5.216  1.00 19.28 ?  147 VAL   B HG23 1 
ATOM   6314 N N    . ARG   B 1 148 ? 30.626 -19.748 -8.566  1.00 15.09 ?  148 ARG   B N    1 
ATOM   6315 C CA   . ARG   B 1 148 ? 29.997 -19.444 -9.841  1.00 15.26 ?  148 ARG   B CA   1 
ATOM   6316 C C    . ARG   B 1 148 ? 30.948 -18.778 -10.824 1.00 14.84 ?  148 ARG   B C    1 
ATOM   6317 O O    . ARG   B 1 148 ? 30.660 -18.771 -12.023 1.00 17.18 ?  148 ARG   B O    1 
ATOM   6318 C CB   . ARG   B 1 148 ? 28.753 -18.559 -9.636  1.00 15.03 ?  148 ARG   B CB   1 
ATOM   6319 C CG   . ARG   B 1 148 ? 27.684 -19.243 -8.801  1.00 16.14 ?  148 ARG   B CG   1 
ATOM   6320 C CD   . ARG   B 1 148 ? 26.490 -18.343 -8.527  1.00 17.57 ?  148 ARG   B CD   1 
ATOM   6321 N NE   . ARG   B 1 148 ? 26.891 -17.138 -7.806  1.00 18.40 ?  148 ARG   B NE   1 
ATOM   6322 C CZ   . ARG   B 1 148 ? 27.191 -17.096 -6.515  1.00 17.34 ?  148 ARG   B CZ   1 
ATOM   6323 N NH1  . ARG   B 1 148 ? 27.131 -18.178 -5.749  1.00 17.26 ?  148 ARG   B NH1  1 
ATOM   6324 N NH2  . ARG   B 1 148 ? 27.593 -15.947 -5.981  1.00 17.10 ?  148 ARG   B NH2  1 
ATOM   6325 H H    . ARG   B 1 148 ? 30.847 -19.037 -8.116  1.00 18.12 ?  148 ARG   B H    1 
ATOM   6326 H HA   . ARG   B 1 148 ? 29.699 -20.269 -10.240 1.00 18.33 ?  148 ARG   B HA   1 
ATOM   6327 H HB2  . ARG   B 1 148 ? 29.012 -17.738 -9.187  1.00 18.05 ?  148 ARG   B HB2  1 
ATOM   6328 H HB3  . ARG   B 1 148 ? 28.365 -18.349 -10.505 1.00 18.05 ?  148 ARG   B HB3  1 
ATOM   6329 H HG2  . ARG   B 1 148 ? 27.375 -20.027 -9.275  1.00 19.38 ?  148 ARG   B HG2  1 
ATOM   6330 H HG3  . ARG   B 1 148 ? 28.077 -19.498 -7.951  1.00 19.38 ?  148 ARG   B HG3  1 
ATOM   6331 H HD2  . ARG   B 1 148 ? 26.094 -18.072 -9.369  1.00 21.10 ?  148 ARG   B HD2  1 
ATOM   6332 H HD3  . ARG   B 1 148 ? 25.848 -18.822 -7.986  1.00 21.10 ?  148 ARG   B HD3  1 
ATOM   6333 H HE   . ARG   B 1 148 ? 26.941 -16.402 -8.248  1.00 22.10 ?  148 ARG   B HE   1 
ATOM   6334 H HH11 . ARG   B 1 148 ? 26.874 -18.929 -6.079  1.00 20.72 ?  148 ARG   B HH11 1 
ATOM   6335 H HH12 . ARG   B 1 148 ? 27.330 -18.125 -4.912  1.00 20.72 ?  148 ARG   B HH12 1 
ATOM   6336 H HH21 . ARG   B 1 148 ? 27.645 -15.239 -6.465  1.00 20.54 ?  148 ARG   B HH21 1 
ATOM   6337 H HH22 . ARG   B 1 148 ? 27.794 -15.905 -5.142  1.00 20.54 ?  148 ARG   B HH22 1 
ATOM   6338 N N    . THR   B 1 149 ? 32.060 -18.219 -10.349 1.00 15.67 ?  149 THR   B N    1 
ATOM   6339 C CA   . THR   B 1 149 ? 33.102 -17.655 -11.193 1.00 15.70 ?  149 THR   B CA   1 
ATOM   6340 C C    . THR   B 1 149 ? 33.990 -18.799 -11.701 1.00 15.46 ?  149 THR   B C    1 
ATOM   6341 O O    . THR   B 1 149 ? 33.797 -19.970 -11.353 1.00 15.55 ?  149 THR   B O    1 
ATOM   6342 C CB   . THR   B 1 149 ? 33.872 -16.600 -10.401 1.00 15.50 ?  149 THR   B CB   1 
ATOM   6343 O OG1  . THR   B 1 149 ? 34.339 -17.202 -9.186  1.00 15.91 ?  149 THR   B OG1  1 
ATOM   6344 C CG2  . THR   B 1 149 ? 32.975 -15.409 -10.100 1.00 16.11 ?  149 THR   B CG2  1 
ATOM   6345 H H    . THR   B 1 149 ? 32.230 -18.150 -9.511  1.00 18.82 ?  149 THR   B H    1 
ATOM   6346 H HA   . THR   B 1 149 ? 32.693 -17.216 -11.953 1.00 18.86 ?  149 THR   B HA   1 
ATOM   6347 H HB   . THR   B 1 149 ? 34.632 -16.298 -10.911 1.00 18.61 ?  149 THR   B HB   1 
ATOM   6348 H HG1  . THR   B 1 149 ? 34.756 -16.635 -8.717  1.00 19.10 ?  149 THR   B HG1  1 
ATOM   6349 H HG21 . THR   B 1 149 ? 33.469 -14.734 -9.614  1.00 19.35 ?  149 THR   B HG21 1 
ATOM   6350 H HG22 . THR   B 1 149 ? 32.647 -15.029 -10.929 1.00 19.35 ?  149 THR   B HG22 1 
ATOM   6351 H HG23 . THR   B 1 149 ? 32.214 -15.691 -9.562  1.00 19.35 ?  149 THR   B HG23 1 
ATOM   6352 N N    . ASN   B 1 150 ? 34.941 -18.482 -12.572 1.00 15.40 ?  150 ASN   B N    1 
ATOM   6353 C CA   . ASN   B 1 150 ? 35.714 -19.526 -13.243 1.00 15.82 ?  150 ASN   B CA   1 
ATOM   6354 C C    . ASN   B 1 150 ? 36.883 -19.966 -12.370 1.00 15.79 ?  150 ASN   B C    1 
ATOM   6355 O O    . ASN   B 1 150 ? 37.818 -19.197 -12.129 1.00 16.05 ?  150 ASN   B O    1 
ATOM   6356 C CB   . ASN   B 1 150 ? 36.192 -19.039 -14.602 1.00 17.43 ?  150 ASN   B CB   1 
ATOM   6357 C CG   . ASN   B 1 150 ? 35.043 -18.790 -15.547 1.00 20.40 ?  150 ASN   B CG   1 
ATOM   6358 O OD1  . ASN   B 1 150 ? 34.129 -19.608 -15.650 1.00 21.95 ?  150 ASN   B OD1  1 
ATOM   6359 N ND2  . ASN   B 1 150 ? 35.055 -17.645 -16.207 1.00 23.35 ?  150 ASN   B ND2  1 
ATOM   6360 H H    . ASN   B 1 150 ? 35.158 -17.679 -12.798 1.00 18.50 ?  150 ASN   B H    1 
ATOM   6361 H HA   . ASN   B 1 150 ? 35.139 -20.297 -13.391 1.00 19.00 ?  150 ASN   B HA   1 
ATOM   6362 H HB2  . ASN   B 1 150 ? 36.676 -18.210 -14.496 1.00 20.93 ?  150 ASN   B HB2  1 
ATOM   6363 H HB3  . ASN   B 1 150 ? 36.769 -19.716 -14.999 1.00 20.93 ?  150 ASN   B HB3  1 
ATOM   6364 H HD21 . ASN   B 1 150 ? 34.426 -17.456 -16.762 1.00 28.04 ?  150 ASN   B HD21 1 
ATOM   6365 H HD22 . ASN   B 1 150 ? 35.708 -17.091 -16.096 1.00 28.04 ?  150 ASN   B HD22 1 
ATOM   6366 N N    . VAL   B 1 151 ? 36.844 -21.210 -11.902 1.00 14.97 ?  151 VAL   B N    1 
ATOM   6367 C CA   . VAL   B 1 151 ? 37.874 -21.737 -11.019 1.00 15.19 ?  151 VAL   B CA   1 
ATOM   6368 C C    . VAL   B 1 151 ? 38.585 -22.903 -11.696 1.00 14.67 ?  151 VAL   B C    1 
ATOM   6369 O O    . VAL   B 1 151 ? 37.941 -23.842 -12.199 1.00 15.76 ?  151 VAL   B O    1 
ATOM   6370 C CB   . VAL   B 1 151 ? 37.320 -22.083 -9.621  1.00 16.96 ?  151 VAL   B CB   1 
ATOM   6371 C CG1  . VAL   B 1 151 ? 36.178 -23.073 -9.704  1.00 19.29 ?  151 VAL   B CG1  1 
ATOM   6372 C CG2  . VAL   B 1 151 ? 38.437 -22.579 -8.708  1.00 16.26 ?  151 VAL   B CG2  1 
ATOM   6373 H H    . VAL   B 1 151 ? 36.214 -21.773 -12.079 1.00 17.98 ?  151 VAL   B H    1 
ATOM   6374 H HA   . VAL   B 1 151 ? 38.535 -21.041 -10.887 1.00 18.24 ?  151 VAL   B HA   1 
ATOM   6375 H HB   . VAL   B 1 151 ? 36.965 -21.264 -9.223  1.00 20.36 ?  151 VAL   B HB   1 
ATOM   6376 H HG11 . VAL   B 1 151 ? 35.864 -23.273 -8.806  1.00 23.16 ?  151 VAL   B HG11 1 
ATOM   6377 H HG12 . VAL   B 1 151 ? 35.455 -22.686 -10.224 1.00 23.16 ?  151 VAL   B HG12 1 
ATOM   6378 H HG13 . VAL   B 1 151 ? 36.494 -23.885 -10.130 1.00 23.16 ?  151 VAL   B HG13 1 
ATOM   6379 H HG21 . VAL   B 1 151 ? 38.096 -22.656 -7.801  1.00 19.53 ?  151 VAL   B HG21 1 
ATOM   6380 H HG22 . VAL   B 1 151 ? 38.743 -23.441 -9.020  1.00 19.53 ?  151 VAL   B HG22 1 
ATOM   6381 H HG23 . VAL   B 1 151 ? 39.170 -21.939 -8.725  1.00 19.53 ?  151 VAL   B HG23 1 
ATOM   6382 N N    . TYR   B 1 152 ? 39.913 -22.816 -11.717 1.00 14.96 ?  152 TYR   B N    1 
ATOM   6383 C CA   . TYR   B 1 152 ? 40.807 -23.814 -12.283 1.00 14.47 ?  152 TYR   B CA   1 
ATOM   6384 C C    . TYR   B 1 152 ? 41.527 -24.477 -11.113 1.00 13.99 ?  152 TYR   B C    1 
ATOM   6385 O O    . TYR   B 1 152 ? 42.388 -23.861 -10.474 1.00 14.71 ?  152 TYR   B O    1 
ATOM   6386 C CB   . TYR   B 1 152 ? 41.789 -23.128 -13.238 1.00 15.78 ?  152 TYR   B CB   1 
ATOM   6387 C CG   . TYR   B 1 152 ? 41.106 -22.660 -14.505 1.00 16.05 ?  152 TYR   B CG   1 
ATOM   6388 C CD1  . TYR   B 1 152 ? 40.404 -21.454 -14.553 1.00 16.96 ?  152 TYR   B CD1  1 
ATOM   6389 C CD2  . TYR   B 1 152 ? 41.117 -23.449 -15.644 1.00 17.06 ?  152 TYR   B CD2  1 
ATOM   6390 C CE1  . TYR   B 1 152 ? 39.759 -21.050 -15.707 1.00 18.24 ?  152 TYR   B CE1  1 
ATOM   6391 C CE2  . TYR   B 1 152 ? 40.475 -23.058 -16.798 1.00 18.40 ?  152 TYR   B CE2  1 
ATOM   6392 C CZ   . TYR   B 1 152 ? 39.797 -21.856 -16.827 1.00 17.70 ?  152 TYR   B CZ   1 
ATOM   6393 O OH   . TYR   B 1 152 ? 39.160 -21.473 -17.981 1.00 21.26 ?  152 TYR   B OH   1 
ATOM   6394 H H    . TYR   B 1 152 ? 40.345 -22.145 -11.378 1.00 17.97 ?  152 TYR   B H    1 
ATOM   6395 H HA   . TYR   B 1 152 ? 40.297 -24.480 -12.764 1.00 17.37 ?  152 TYR   B HA   1 
ATOM   6396 H HB2  . TYR   B 1 152 ? 42.177 -22.358 -12.794 1.00 18.95 ?  152 TYR   B HB2  1 
ATOM   6397 H HB3  . TYR   B 1 152 ? 42.486 -23.758 -13.480 1.00 18.95 ?  152 TYR   B HB3  1 
ATOM   6398 H HD1  . TYR   B 1 152 ? 40.373 -20.911 -13.794 1.00 20.36 ?  152 TYR   B HD1  1 
ATOM   6399 H HD2  . TYR   B 1 152 ? 41.575 -24.263 -15.625 1.00 20.48 ?  152 TYR   B HD2  1 
ATOM   6400 H HE1  . TYR   B 1 152 ? 39.298 -20.238 -15.730 1.00 21.90 ?  152 TYR   B HE1  1 
ATOM   6401 H HE2  . TYR   B 1 152 ? 40.503 -23.592 -17.558 1.00 22.09 ?  152 TYR   B HE2  1 
ATOM   6402 H HH   . TYR   B 1 152 ? 38.785 -20.719 -17.873 1.00 25.53 ?  152 TYR   B HH   1 
ATOM   6403 N N    . LEU   B 1 153 ? 41.165 -25.730 -10.833 1.00 14.08 ?  153 LEU   B N    1 
ATOM   6404 C CA   . LEU   B 1 153 ? 41.689 -26.476 -9.699  1.00 13.96 ?  153 LEU   B CA   1 
ATOM   6405 C C    . LEU   B 1 153 ? 42.922 -27.281 -10.096 1.00 14.30 ?  153 LEU   B C    1 
ATOM   6406 O O    . LEU   B 1 153 ? 42.908 -27.999 -11.101 1.00 15.68 ?  153 LEU   B O    1 
ATOM   6407 C CB   . LEU   B 1 153 ? 40.615 -27.436 -9.194  1.00 14.33 ?  153 LEU   B CB   1 
ATOM   6408 C CG   . LEU   B 1 153 ? 39.355 -26.781 -8.617  1.00 15.33 ?  153 LEU   B CG   1 
ATOM   6409 C CD1  . LEU   B 1 153 ? 38.251 -27.811 -8.462  1.00 17.20 ?  153 LEU   B CD1  1 
ATOM   6410 C CD2  . LEU   B 1 153 ? 39.649 -26.126 -7.281  1.00 16.39 ?  153 LEU   B CD2  1 
ATOM   6411 H H    . LEU   B 1 153 ? 40.594 -26.174 -11.301 1.00 16.91 ?  153 LEU   B H    1 
ATOM   6412 H HA   . LEU   B 1 153 ? 41.911 -25.858 -8.982  1.00 16.77 ?  153 LEU   B HA   1 
ATOM   6413 H HB2  . LEU   B 1 153 ? 40.332 -27.998 -9.933  1.00 17.21 ?  153 LEU   B HB2  1 
ATOM   6414 H HB3  . LEU   B 1 153 ? 40.997 -27.987 -8.495  1.00 17.21 ?  153 LEU   B HB3  1 
ATOM   6415 H HG   . LEU   B 1 153 ? 39.047 -26.091 -9.228  1.00 18.41 ?  153 LEU   B HG   1 
ATOM   6416 H HD11 . LEU   B 1 153 ? 37.449 -27.368 -8.139  1.00 20.65 ?  153 LEU   B HD11 1 
ATOM   6417 H HD12 . LEU   B 1 153 ? 38.076 -28.219 -9.324  1.00 20.65 ?  153 LEU   B HD12 1 
ATOM   6418 H HD13 . LEU   B 1 153 ? 38.534 -28.485 -7.826  1.00 20.65 ?  153 LEU   B HD13 1 
ATOM   6419 H HD21 . LEU   B 1 153 ? 38.831 -25.765 -6.914  1.00 19.69 ?  153 LEU   B HD21 1 
ATOM   6420 H HD22 . LEU   B 1 153 ? 40.016 -26.797 -6.676  1.00 19.69 ?  153 LEU   B HD22 1 
ATOM   6421 H HD23 . LEU   B 1 153 ? 40.300 -25.416 -7.409  1.00 19.69 ?  153 LEU   B HD23 1 
ATOM   6422 N N    . ALA   B 1 154 ? 43.980 -27.155 -9.298  1.00 14.89 ?  154 ALA   B N    1 
ATOM   6423 C CA   . ALA   B 1 154 ? 45.201 -27.933 -9.476  1.00 15.98 ?  154 ALA   B CA   1 
ATOM   6424 C C    . ALA   B 1 154 ? 45.275 -29.005 -8.396  1.00 16.60 ?  154 ALA   B C    1 
ATOM   6425 O O    . ALA   B 1 154 ? 45.228 -28.694 -7.197  1.00 18.95 ?  154 ALA   B O    1 
ATOM   6426 C CB   . ALA   B 1 154 ? 46.417 -27.021 -9.396  1.00 17.05 ?  154 ALA   B CB   1 
ATOM   6427 H H    . ALA   B 1 154 ? 44.011 -26.610 -8.631  1.00 17.88 ?  154 ALA   B H    1 
ATOM   6428 H HA   . ALA   B 1 154 ? 45.190 -28.357 -10.347 1.00 19.19 ?  154 ALA   B HA   1 
ATOM   6429 H HB1  . ALA   B 1 154 ? 47.220 -27.550 -9.514  1.00 20.47 ?  154 ALA   B HB1  1 
ATOM   6430 H HB2  . ALA   B 1 154 ? 46.360 -26.345 -10.092 1.00 20.47 ?  154 ALA   B HB2  1 
ATOM   6431 H HB3  . ALA   B 1 154 ? 46.434 -26.588 -8.524  1.00 20.47 ?  154 ALA   B HB3  1 
ATOM   6432 N N    . VAL   B 1 155 ? 45.377 -30.260 -8.822  1.00 15.18 ?  155 VAL   B N    1 
ATOM   6433 C CA   . VAL   B 1 155 ? 45.497 -31.399 -7.919  1.00 15.79 ?  155 VAL   B CA   1 
ATOM   6434 C C    . VAL   B 1 155 ? 46.838 -32.066 -8.192  1.00 15.23 ?  155 VAL   B C    1 
ATOM   6435 O O    . VAL   B 1 155 ? 47.077 -32.564 -9.299  1.00 17.34 ?  155 VAL   B O    1 
ATOM   6436 C CB   . VAL   B 1 155 ? 44.342 -32.394 -8.096  1.00 16.45 ?  155 VAL   B CB   1 
ATOM   6437 C CG1  . VAL   B 1 155 ? 44.543 -33.574 -7.161  1.00 17.52 ?  155 VAL   B CG1  1 
ATOM   6438 C CG2  . VAL   B 1 155 ? 42.996 -31.703 -7.834  1.00 18.39 ?  155 VAL   B CG2  1 
ATOM   6439 H H    . VAL   B 1 155 ? 45.385 -30.484 -9.659  1.00 18.24 ?  155 VAL   B H    1 
ATOM   6440 H HA   . VAL   B 1 155 ? 45.494 -31.085 -7.006  1.00 18.97 ?  155 VAL   B HA   1 
ATOM   6441 H HB   . VAL   B 1 155 ? 44.335 -32.721 -9.008  1.00 19.75 ?  155 VAL   B HB   1 
ATOM   6442 H HG11 . VAL   B 1 155 ? 43.718 -34.082 -7.100  1.00 21.04 ?  155 VAL   B HG11 1 
ATOM   6443 H HG12 . VAL   B 1 155 ? 45.251 -34.144 -7.510  1.00 21.04 ?  155 VAL   B HG12 1 
ATOM   6444 H HG13 . VAL   B 1 155 ? 44.792 -33.248 -6.279  1.00 21.04 ?  155 VAL   B HG13 1 
ATOM   6445 H HG21 . VAL   B 1 155 ? 42.284 -32.360 -7.905  1.00 22.08 ?  155 VAL   B HG21 1 
ATOM   6446 H HG22 . VAL   B 1 155 ? 43.004 -31.324 -6.939  1.00 22.08 ?  155 VAL   B HG22 1 
ATOM   6447 H HG23 . VAL   B 1 155 ? 42.864 -31.001 -8.489  1.00 22.08 ?  155 VAL   B HG23 1 
ATOM   6448 N N    . PHE   B 1 156 ? 47.699 -32.093 -7.176  1.00 16.39 ?  156 PHE   B N    1 
ATOM   6449 C CA   . PHE   B 1 156 ? 49.075 -32.558 -7.362  1.00 16.85 ?  156 PHE   B CA   1 
ATOM   6450 C C    . PHE   B 1 156 ? 49.168 -34.062 -7.626  1.00 17.89 ?  156 PHE   B C    1 
ATOM   6451 O O    . PHE   B 1 156 ? 49.878 -34.504 -8.541  1.00 20.79 ?  156 PHE   B O    1 
ATOM   6452 C CB   . PHE   B 1 156 ? 49.897 -32.186 -6.133  1.00 17.26 ?  156 PHE   B CB   1 
ATOM   6453 C CG   . PHE   B 1 156 ? 51.331 -32.645 -6.204  1.00 18.09 ?  156 PHE   B CG   1 
ATOM   6454 C CD1  . PHE   B 1 156 ? 52.178 -32.145 -7.173  1.00 20.19 ?  156 PHE   B CD1  1 
ATOM   6455 C CD2  . PHE   B 1 156 ? 51.829 -33.578 -5.311  1.00 18.93 ?  156 PHE   B CD2  1 
ATOM   6456 C CE1  . PHE   B 1 156 ? 53.512 -32.545 -7.248  1.00 21.46 ?  156 PHE   B CE1  1 
ATOM   6457 C CE2  . PHE   B 1 156 ? 53.151 -33.994 -5.388  1.00 19.95 ?  156 PHE   B CE2  1 
ATOM   6458 C CZ   . PHE   B 1 156 ? 53.988 -33.469 -6.363  1.00 20.91 ?  156 PHE   B CZ   1 
ATOM   6459 H H    . PHE   B 1 156 ? 47.510 -31.843 -6.376  1.00 19.68 ?  156 PHE   B H    1 
ATOM   6460 H HA   . PHE   B 1 156 ? 49.457 -32.098 -8.122  1.00 20.24 ?  156 PHE   B HA   1 
ATOM   6461 H HB2  . PHE   B 1 156 ? 49.896 -31.220 -6.040  1.00 20.73 ?  156 PHE   B HB2  1 
ATOM   6462 H HB3  . PHE   B 1 156 ? 49.492 -32.591 -5.348  1.00 20.73 ?  156 PHE   B HB3  1 
ATOM   6463 H HD1  . PHE   B 1 156 ? 51.853 -31.509 -7.780  1.00 24.25 ?  156 PHE   B HD1  1 
ATOM   6464 H HD2  . PHE   B 1 156 ? 51.269 -33.931 -4.654  1.00 22.73 ?  156 PHE   B HD2  1 
ATOM   6465 H HE1  . PHE   B 1 156 ? 54.065 -32.200 -7.910  1.00 25.77 ?  156 PHE   B HE1  1 
ATOM   6466 H HE2  . PHE   B 1 156 ? 53.485 -34.625 -4.783  1.00 23.96 ?  156 PHE   B HE2  1 
ATOM   6467 H HZ   . PHE   B 1 156 ? 54.876 -33.752 -6.416  1.00 25.10 ?  156 PHE   B HZ   1 
ATOM   6468 N N    . ASP   B 1 157 ? 48.517 -34.868 -6.802  1.00 18.66 ?  157 ASP   B N    1 
ATOM   6469 C CA   . ASP   B 1 157 ? 48.650 -36.318 -6.893  1.00 20.42 ?  157 ASP   B CA   1 
ATOM   6470 C C    . ASP   B 1 157 ? 47.743 -36.871 -7.989  1.00 20.63 ?  157 ASP   B C    1 
ATOM   6471 O O    . ASP   B 1 157 ? 46.515 -36.760 -7.892  1.00 19.51 ?  157 ASP   B O    1 
ATOM   6472 C CB   . ASP   B 1 157 ? 48.271 -36.925 -5.552  1.00 21.97 ?  157 ASP   B CB   1 
ATOM   6473 C CG   . ASP   B 1 157 ? 48.437 -38.439 -5.524  1.00 24.58 ?  157 ASP   B CG   1 
ATOM   6474 O OD1  . ASP   B 1 157 ? 48.805 -39.042 -6.562  1.00 25.40 ?  157 ASP   B OD1  1 
ATOM   6475 O OD2  . ASP   B 1 157 ? 48.226 -39.016 -4.445  1.00 26.87 -1 157 ASP   B OD2  1 
ATOM   6476 H H    . ASP   B 1 157 ? 47.995 -34.596 -6.170  1.00 22.41 ?  157 ASP   B H    1 
ATOM   6477 H HA   . ASP   B 1 157 ? 49.571 -36.548 -7.095  1.00 24.52 ?  157 ASP   B HA   1 
ATOM   6478 H HB2  . ASP   B 1 157 ? 48.832 -36.537 -4.865  1.00 26.38 ?  157 ASP   B HB2  1 
ATOM   6479 H HB3  . ASP   B 1 157 ? 47.338 -36.716 -5.370  1.00 26.38 ?  157 ASP   B HB3  1 
ATOM   6480 N N    . LYS   B 1 158 ? 48.349 -37.492 -9.011  1.00 22.82 ?  158 LYS   B N    1 
ATOM   6481 C CA   . LYS   B 1 158 ? 47.587 -38.125 -10.092 1.00 23.74 ?  158 LYS   B CA   1 
ATOM   6482 C C    . LYS   B 1 158 ? 46.525 -39.095 -9.569  1.00 23.27 ?  158 LYS   B C    1 
ATOM   6483 O O    . LYS   B 1 158 ? 45.422 -39.182 -10.125 1.00 24.15 ?  158 LYS   B O    1 
ATOM   6484 C CB   . LYS   B 1 158 ? 48.548 -38.840 -11.050 1.00 26.68 ?  158 LYS   B CB   1 
ATOM   6485 C CG   . LYS   B 1 158 ? 47.881 -39.745 -12.080 1.00 29.37 ?  158 LYS   B CG   1 
ATOM   6486 C CD   . LYS   B 1 158 ? 47.015 -38.977 -13.072 1.00 31.24 ?  158 LYS   B CD   1 
ATOM   6487 C CE   . LYS   B 1 158 ? 46.429 -39.909 -14.128 1.00 33.28 ?  158 LYS   B CE   1 
ATOM   6488 N NZ   . LYS   B 1 158 ? 45.301 -39.290 -14.895 1.00 33.56 ?  158 LYS   B NZ   1 
ATOM   6489 H H    . LYS   B 1 158 ? 49.203 -37.550 -9.103  1.00 27.40 ?  158 LYS   B H    1 
ATOM   6490 H HA   . LYS   B 1 158 ? 47.133 -37.434 -10.601 1.00 28.50 ?  158 LYS   B HA   1 
ATOM   6491 H HB2  . LYS   B 1 158 ? 49.056 -38.170 -11.541 1.00 32.03 ?  158 LYS   B HB2  1 
ATOM   6492 H HB3  . LYS   B 1 158 ? 49.157 -39.386 -10.530 1.00 32.03 ?  158 LYS   B HB3  1 
ATOM   6493 H HG2  . LYS   B 1 158 ? 48.571 -40.204 -12.586 1.00 35.26 ?  158 LYS   B HG2  1 
ATOM   6494 H HG3  . LYS   B 1 158 ? 47.322 -40.402 -11.633 1.00 35.26 ?  158 LYS   B HG3  1 
ATOM   6495 H HD2  . LYS   B 1 158 ? 46.285 -38.549 -12.600 1.00 37.50 ?  158 LYS   B HD2  1 
ATOM   6496 H HD3  . LYS   B 1 158 ? 47.560 -38.311 -13.524 1.00 37.50 ?  158 LYS   B HD3  1 
ATOM   6497 H HE2  . LYS   B 1 158 ? 47.122 -40.149 -14.760 1.00 39.95 ?  158 LYS   B HE2  1 
ATOM   6498 H HE3  . LYS   B 1 158 ? 46.090 -40.708 -13.693 1.00 39.95 ?  158 LYS   B HE3  1 
ATOM   6499 H HZ1  . LYS   B 1 158 ? 44.990 -39.866 -15.498 1.00 40.28 ?  158 LYS   B HZ1  1 
ATOM   6500 H HZ2  . LYS   B 1 158 ? 44.644 -39.063 -14.343 1.00 40.28 ?  158 LYS   B HZ2  1 
ATOM   6501 H HZ3  . LYS   B 1 158 ? 45.590 -38.560 -15.318 1.00 40.28 ?  158 LYS   B HZ3  1 
ATOM   6502 N N    A ASN   B 1 159 ? 46.838 -39.839 -8.506  0.46 22.32 ?  159 ASN   B N    1 
ATOM   6503 N N    B ASN   B 1 159 ? 46.832 -39.829 -8.497  0.54 22.63 ?  159 ASN   B N    1 
ATOM   6504 C CA   A ASN   B 1 159 ? 45.878 -40.812 -7.992  0.46 23.03 ?  159 ASN   B CA   1 
ATOM   6505 C CA   B ASN   B 1 159 ? 45.878 -40.814 -7.994  0.54 23.72 ?  159 ASN   B CA   1 
ATOM   6506 C C    A ASN   B 1 159 ? 44.670 -40.127 -7.351  0.46 22.04 ?  159 ASN   B C    1 
ATOM   6507 C C    B ASN   B 1 159 ? 44.678 -40.147 -7.320  0.54 22.35 ?  159 ASN   B C    1 
ATOM   6508 O O    A ASN   B 1 159 ? 43.535 -40.602 -7.489  0.46 22.02 ?  159 ASN   B O    1 
ATOM   6509 O O    B ASN   B 1 159 ? 43.556 -40.662 -7.405  0.54 22.13 ?  159 ASN   B O    1 
ATOM   6510 C CB   A ASN   B 1 159 ? 46.580 -41.759 -7.023  0.46 24.41 ?  159 ASN   B CB   1 
ATOM   6511 C CB   B ASN   B 1 159 ? 46.592 -41.781 -7.055  0.54 25.77 ?  159 ASN   B CB   1 
ATOM   6512 C CG   A ASN   B 1 159 ? 47.564 -42.673 -7.727  0.46 25.33 ?  159 ASN   B CG   1 
ATOM   6513 C CG   B ASN   B 1 159 ? 47.675 -42.585 -7.765  0.54 27.43 ?  159 ASN   B CG   1 
ATOM   6514 O OD1  A ASN   B 1 159 ? 47.266 -43.211 -8.800  0.46 25.05 ?  159 ASN   B OD1  1 
ATOM   6515 O OD1  B ASN   B 1 159 ? 47.497 -43.017 -8.907  0.54 28.06 ?  159 ASN   B OD1  1 
ATOM   6516 N ND2  A ASN   B 1 159 ? 48.747 -42.847 -7.138  0.46 25.70 ?  159 ASN   B ND2  1 
ATOM   6517 N ND2  B ASN   B 1 159 ? 48.803 -42.785 -7.093  0.54 27.94 ?  159 ASN   B ND2  1 
ATOM   6518 H H    A ASN   B 1 159 ? 47.588 -39.799 -8.084  0.46 26.80 ?  159 ASN   B H    1 
ATOM   6519 H H    B ASN   B 1 159 ? 47.565 -39.765 -8.052  0.54 27.17 ?  159 ASN   B H    1 
ATOM   6520 H HA   A ASN   B 1 159 ? 45.563 -41.346 -8.737  0.46 27.65 ?  159 ASN   B HA   1 
ATOM   6521 H HA   B ASN   B 1 159 ? 45.550 -41.327 -8.747  0.54 28.48 ?  159 ASN   B HA   1 
ATOM   6522 H HB2  A ASN   B 1 159 ? 47.072 -41.245 -6.364  0.46 29.30 ?  159 ASN   B HB2  1 
ATOM   6523 H HB2  B ASN   B 1 159 ? 47.015 -41.283 -6.340  0.54 30.94 ?  159 ASN   B HB2  1 
ATOM   6524 H HB3  A ASN   B 1 159 ? 45.923 -42.320 -6.591  0.46 29.30 ?  159 ASN   B HB3  1 
ATOM   6525 H HB3  B ASN   B 1 159 ? 45.946 -42.405 -6.691  0.54 30.94 ?  159 ASN   B HB3  1 
ATOM   6526 H HD21 A ASN   B 1 159 ? 49.345 -43.354 -7.500  0.46 30.86 ?  159 ASN   B HD21 1 
ATOM   6527 H HD21 B ASN   B 1 159 ? 49.443 -43.238 -7.450  0.54 33.54 ?  159 ASN   B HD21 1 
ATOM   6528 H HD22 A ASN   B 1 159 ? 48.918 -42.461 -6.387  0.46 30.86 ?  159 ASN   B HD22 1 
ATOM   6529 H HD22 B ASN   B 1 159 ? 48.891 -42.474 -6.297  0.54 33.54 ?  159 ASN   B HD22 1 
ATOM   6530 N N    . LEU   B 1 160 ? 44.884 -39.010 -6.653  1.00 21.77 ?  160 LEU   B N    1 
ATOM   6531 C CA   . LEU   B 1 160 ? 43.751 -38.270 -6.108  1.00 19.86 ?  160 LEU   B CA   1 
ATOM   6532 C C    . LEU   B 1 160 ? 42.967 -37.593 -7.226  1.00 19.06 ?  160 LEU   B C    1 
ATOM   6533 O O    . LEU   B 1 160 ? 41.730 -37.608 -7.223  1.00 19.45 ?  160 LEU   B O    1 
ATOM   6534 C CB   . LEU   B 1 160 ? 44.216 -37.250 -5.064  1.00 19.41 ?  160 LEU   B CB   1 
ATOM   6535 C CG   . LEU   B 1 160 ? 43.093 -36.309 -4.575  1.00 19.12 ?  160 LEU   B CG   1 
ATOM   6536 C CD1  . LEU   B 1 160 ? 41.934 -37.101 -3.980  1.00 20.79 ?  160 LEU   B CD1  1 
ATOM   6537 C CD2  . LEU   B 1 160 ? 43.636 -35.314 -3.559  1.00 18.99 ?  160 LEU   B CD2  1 
ATOM   6538 H H    A LEU   B 1 160 ? 45.659 -38.665 -6.495  0.46 26.14 ?  160 LEU   B H    1 
ATOM   6539 H H    B LEU   B 1 160 ? 45.658 -38.656 -6.512  0.54 26.14 ?  160 LEU   B H    1 
ATOM   6540 H HA   . LEU   B 1 160 ? 43.160 -38.900 -5.671  1.00 23.84 ?  160 LEU   B HA   1 
ATOM   6541 H HB2  . LEU   B 1 160 ? 44.562 -37.730 -4.295  1.00 23.30 ?  160 LEU   B HB2  1 
ATOM   6542 H HB3  . LEU   B 1 160 ? 44.916 -36.703 -5.453  1.00 23.30 ?  160 LEU   B HB3  1 
ATOM   6543 H HG   . LEU   B 1 160 ? 42.752 -35.805 -5.328  1.00 22.96 ?  160 LEU   B HG   1 
ATOM   6544 H HD11 . LEU   B 1 160 ? 41.297 -36.486 -3.593  1.00 24.96 ?  160 LEU   B HD11 1 
ATOM   6545 H HD12 . LEU   B 1 160 ? 41.505 -37.620 -4.683  1.00 24.96 ?  160 LEU   B HD12 1 
ATOM   6546 H HD13 . LEU   B 1 160 ? 42.276 -37.701 -3.295  1.00 24.96 ?  160 LEU   B HD13 1 
ATOM   6547 H HD21 . LEU   B 1 160 ? 42.916 -34.722 -3.286  1.00 22.81 ?  160 LEU   B HD21 1 
ATOM   6548 H HD22 . LEU   B 1 160 ? 43.976 -35.797 -2.792  1.00 22.81 ?  160 LEU   B HD22 1 
ATOM   6549 H HD23 . LEU   B 1 160 ? 44.347 -34.799 -3.972  1.00 22.81 ?  160 LEU   B HD23 1 
ATOM   6550 N N    . TYR   B 1 161 ? 43.668 -37.029 -8.211  1.00 19.76 ?  161 TYR   B N    1 
ATOM   6551 C CA   . TYR   B 1 161 ? 43.000 -36.465 -9.380  1.00 19.98 ?  161 TYR   B CA   1 
ATOM   6552 C C    . TYR   B 1 161 ? 42.065 -37.494 -10.004 1.00 19.46 ?  161 TYR   B C    1 
ATOM   6553 O O    . TYR   B 1 161 ? 40.905 -37.201 -10.300 1.00 19.16 ?  161 TYR   B O    1 
ATOM   6554 C CB   . TYR   B 1 161 ? 44.053 -35.993 -10.395 1.00 20.79 ?  161 TYR   B CB   1 
ATOM   6555 C CG   . TYR   B 1 161 ? 43.480 -35.533 -11.717 1.00 21.45 ?  161 TYR   B CG   1 
ATOM   6556 C CD1  . TYR   B 1 161 ? 43.068 -34.212 -11.895 1.00 21.35 ?  161 TYR   B CD1  1 
ATOM   6557 C CD2  . TYR   B 1 161 ? 43.338 -36.414 -12.786 1.00 21.89 ?  161 TYR   B CD2  1 
ATOM   6558 C CE1  . TYR   B 1 161 ? 42.538 -33.788 -13.096 1.00 21.96 ?  161 TYR   B CE1  1 
ATOM   6559 C CE2  . TYR   B 1 161 ? 42.797 -35.999 -13.990 1.00 22.06 ?  161 TYR   B CE2  1 
ATOM   6560 C CZ   . TYR   B 1 161 ? 42.406 -34.682 -14.140 1.00 21.60 ?  161 TYR   B CZ   1 
ATOM   6561 O OH   . TYR   B 1 161 ? 41.870 -34.250 -15.333 1.00 23.80 ?  161 TYR   B OH   1 
ATOM   6562 H H    . TYR   B 1 161 ? 44.520 -36.959 -8.226  1.00 23.73 ?  161 TYR   B H    1 
ATOM   6563 H HA   . TYR   B 1 161 ? 42.470 -35.699 -9.115  1.00 23.99 ?  161 TYR   B HA   1 
ATOM   6564 H HB2  . TYR   B 1 161 ? 44.541 -35.244 -10.011 1.00 24.96 ?  161 TYR   B HB2  1 
ATOM   6565 H HB3  . TYR   B 1 161 ? 44.663 -36.720 -10.580 1.00 24.96 ?  161 TYR   B HB3  1 
ATOM   6566 H HD1  . TYR   B 1 161 ? 43.155 -33.597 -11.197 1.00 25.64 ?  161 TYR   B HD1  1 
ATOM   6567 H HD2  . TYR   B 1 161 ? 43.598 -37.298 -12.686 1.00 26.28 ?  161 TYR   B HD2  1 
ATOM   6568 H HE1  . TYR   B 1 161 ? 42.269 -32.899 -13.201 1.00 26.37 ?  161 TYR   B HE1  1 
ATOM   6569 H HE2  . TYR   B 1 161 ? 42.708 -36.600 -14.696 1.00 26.49 ?  161 TYR   B HE2  1 
ATOM   6570 H HH   . TYR   B 1 161 ? 41.840 -34.886 -15.886 1.00 28.57 ?  161 TYR   B HH   1 
ATOM   6571 N N    A ASP   B 1 162 ? 42.555 -38.723 -10.179 0.46 19.99 ?  162 ASP   B N    1 
ATOM   6572 N N    B ASP   B 1 162 ? 42.568 -38.711 -10.220 0.54 20.09 ?  162 ASP   B N    1 
ATOM   6573 C CA   A ASP   B 1 162 ? 41.744 -39.770 -10.794 0.46 20.49 ?  162 ASP   B CA   1 
ATOM   6574 C CA   B ASP   B 1 162 ? 41.763 -39.748 -10.858 0.54 20.55 ?  162 ASP   B CA   1 
ATOM   6575 C C    A ASP   B 1 162 ? 40.522 -40.097 -9.944  0.46 20.41 ?  162 ASP   B C    1 
ATOM   6576 C C    B ASP   B 1 162 ? 40.546 -40.102 -10.012 0.54 20.21 ?  162 ASP   B C    1 
ATOM   6577 O O    A ASP   B 1 162 ? 39.419 -40.290 -10.474 0.46 21.09 ?  162 ASP   B O    1 
ATOM   6578 O O    B ASP   B 1 162 ? 39.453 -40.339 -10.546 0.54 20.78 ?  162 ASP   B O    1 
ATOM   6579 C CB   A ASP   B 1 162 ? 42.596 -41.025 -11.016 0.46 21.50 ?  162 ASP   B CB   1 
ATOM   6580 C CB   B ASP   B 1 162 ? 42.618 -40.994 -11.106 0.54 21.76 ?  162 ASP   B CB   1 
ATOM   6581 C CG   A ASP   B 1 162 ? 43.541 -40.898 -12.202 0.46 22.75 ?  162 ASP   B CG   1 
ATOM   6582 C CG   B ASP   B 1 162 ? 43.607 -40.815 -12.251 0.54 23.17 ?  162 ASP   B CG   1 
ATOM   6583 O OD1  A ASP   B 1 162 ? 43.489 -39.871 -12.912 0.46 23.50 ?  162 ASP   B OD1  1 
ATOM   6584 O OD1  B ASP   B 1 162 ? 43.379 -39.948 -13.121 0.54 23.61 ?  162 ASP   B OD1  1 
ATOM   6585 O OD2  A ASP   B 1 162 ? 44.330 -41.842 -12.431 0.46 23.50 -1 162 ASP   B OD2  1 
ATOM   6586 O OD2  B ASP   B 1 162 ? 44.610 -41.560 -12.286 0.54 24.43 -1 162 ASP   B OD2  1 
ATOM   6587 H H    A ASP   B 1 162 ? 43.345 -38.973 -9.950  0.46 24.00 ?  162 ASP   B H    1 
ATOM   6588 H H    B ASP   B 1 162 ? 43.368 -38.955 -10.013 0.54 24.12 ?  162 ASP   B H    1 
ATOM   6589 H HA   A ASP   B 1 162 ? 41.435 -39.468 -11.658 0.46 24.60 ?  162 ASP   B HA   1 
ATOM   6590 H HA   B ASP   B 1 162 ? 41.454 -39.429 -11.718 0.54 24.68 ?  162 ASP   B HA   1 
ATOM   6591 H HB2  A ASP   B 1 162 ? 43.137 -41.192 -10.226 0.46 25.81 ?  162 ASP   B HB2  1 
ATOM   6592 H HB2  B ASP   B 1 162 ? 43.139 -41.194 -10.309 0.54 26.12 ?  162 ASP   B HB2  1 
ATOM   6593 H HB3  A ASP   B 1 162 ? 42.019 -41.782 -11.190 0.46 25.81 ?  162 ASP   B HB3  1 
ATOM   6594 H HB3  B ASP   B 1 162 ? 42.042 -41.746 -11.318 0.54 26.12 ?  162 ASP   B HB3  1 
ATOM   6595 N N    A LYS   B 1 163 ? 40.694 -40.165 -8.622  0.46 20.00 ?  163 LYS   B N    1 
ATOM   6596 N N    B LYS   B 1 163 ? 40.720 -40.165 -8.691  0.54 19.50 ?  163 LYS   B N    1 
ATOM   6597 C CA   A LYS   B 1 163 ? 39.561 -40.441 -7.747  0.46 20.56 ?  163 LYS   B CA   1 
ATOM   6598 C CA   B LYS   B 1 163 ? 39.592 -40.432 -7.805  0.54 19.91 ?  163 LYS   B CA   1 
ATOM   6599 C C    A LYS   B 1 163 ? 38.529 -39.321 -7.795  0.46 19.28 ?  163 LYS   B C    1 
ATOM   6600 C C    B LYS   B 1 163 ? 38.539 -39.333 -7.904  0.54 18.74 ?  163 LYS   B C    1 
ATOM   6601 O O    A LYS   B 1 163 ? 37.323 -39.583 -7.679  0.46 19.57 ?  163 LYS   B O    1 
ATOM   6602 O O    B LYS   B 1 163 ? 37.330 -39.613 -7.940  0.54 18.88 ?  163 LYS   B O    1 
ATOM   6603 C CB   A LYS   B 1 163 ? 40.035 -40.633 -6.308  0.46 22.66 ?  163 LYS   B CB   1 
ATOM   6604 C CB   B LYS   B 1 163 ? 40.089 -40.562 -6.366  0.54 21.82 ?  163 LYS   B CB   1 
ATOM   6605 C CG   A LYS   B 1 163 ? 38.945 -41.168 -5.405  0.46 26.07 ?  163 LYS   B CG   1 
ATOM   6606 C CG   B LYS   B 1 163 ? 39.035 -41.072 -5.411  0.54 25.55 ?  163 LYS   B CG   1 
ATOM   6607 C CD   A LYS   B 1 163 ? 39.335 -41.168 -3.943  0.46 28.81 ?  163 LYS   B CD   1 
ATOM   6608 C CD   B LYS   B 1 163 ? 39.587 -41.359 -4.024  0.54 28.90 ?  163 LYS   B CD   1 
ATOM   6609 C CE   A LYS   B 1 163 ? 38.257 -41.847 -3.111  0.46 30.58 ?  163 LYS   B CE   1 
ATOM   6610 C CE   B LYS   B 1 163 ? 38.544 -42.075 -3.176  0.54 31.17 ?  163 LYS   B CE   1 
ATOM   6611 N NZ   A LYS   B 1 163 ? 38.326 -41.467 -1.675  0.46 31.57 ?  163 LYS   B NZ   1 
ATOM   6612 N NZ   B LYS   B 1 163 ? 38.675 -41.760 -1.726  0.54 32.36 ?  163 LYS   B NZ   1 
ATOM   6613 H H    A LYS   B 1 163 ? 41.447 -40.060 -8.219  0.46 24.02 ?  163 LYS   B H    1 
ATOM   6614 H H    B LYS   B 1 163 ? 41.480 -40.074 -8.293  0.54 23.41 ?  163 LYS   B H    1 
ATOM   6615 H HA   A LYS   B 1 163 ? 39.134 -41.269 -8.033  0.46 24.69 ?  163 LYS   B HA   1 
ATOM   6616 H HA   B LYS   B 1 163 ? 39.185 -41.280 -8.061  0.54 23.91 ?  163 LYS   B HA   1 
ATOM   6617 H HB2  A LYS   B 1 163 ? 40.773 -41.270 -6.296  0.46 27.21 ?  163 LYS   B HB2  1 
ATOM   6618 H HB2  B LYS   B 1 163 ? 40.837 -41.189 -6.343  0.54 26.20 ?  163 LYS   B HB2  1 
ATOM   6619 H HB3  A LYS   B 1 163 ? 40.330 -39.782 -5.955  0.46 27.21 ?  163 LYS   B HB3  1 
ATOM   6620 H HB3  B LYS   B 1 163 ? 40.380 -39.696 -6.055  0.54 26.20 ?  163 LYS   B HB3  1 
ATOM   6621 H HG2  A LYS   B 1 163 ? 38.154 -40.616 -5.500  0.46 31.29 ?  163 LYS   B HG2  1 
ATOM   6622 H HG2  B LYS   B 1 163 ? 38.337 -40.407 -5.323  0.54 30.68 ?  163 LYS   B HG2  1 
ATOM   6623 H HG3  A LYS   B 1 163 ? 38.743 -42.083 -5.660  0.46 31.29 ?  163 LYS   B HG3  1 
ATOM   6624 H HG3  B LYS   B 1 163 ? 38.662 -41.901 -5.758  0.54 30.68 ?  163 LYS   B HG3  1 
ATOM   6625 H HD2  A LYS   B 1 163 ? 40.165 -41.659 -3.829  0.46 34.58 ?  163 LYS   B HD2  1 
ATOM   6626 H HD2  B LYS   B 1 163 ? 40.368 -41.929 -4.096  0.54 34.69 ?  163 LYS   B HD2  1 
ATOM   6627 H HD3  A LYS   B 1 163 ? 39.434 -40.255 -3.634  0.46 34.58 ?  163 LYS   B HD3  1 
ATOM   6628 H HD3  B LYS   B 1 163 ? 39.814 -40.523 -3.588  0.54 34.69 ?  163 LYS   B HD3  1 
ATOM   6629 H HE2  A LYS   B 1 163 ? 37.383 -41.606 -3.453  0.46 36.71 ?  163 LYS   B HE2  1 
ATOM   6630 H HE2  B LYS   B 1 163 ? 37.658 -41.802 -3.465  0.54 37.42 ?  163 LYS   B HE2  1 
ATOM   6631 H HE3  A LYS   B 1 163 ? 38.376 -42.807 -3.171  0.46 36.71 ?  163 LYS   B HE3  1 
ATOM   6632 H HE3  B LYS   B 1 163 ? 38.648 -43.033 -3.286  0.54 37.42 ?  163 LYS   B HE3  1 
ATOM   6633 H HZ1  A LYS   B 1 163 ? 37.683 -41.881 -1.221  0.46 37.90 ?  163 LYS   B HZ1  1 
ATOM   6634 H HZ1  B LYS   B 1 163 ? 38.050 -42.193 -1.263  0.54 38.85 ?  163 LYS   B HZ1  1 
ATOM   6635 H HZ2  A LYS   B 1 163 ? 39.116 -41.703 -1.339  0.46 37.90 ?  163 LYS   B HZ2  1 
ATOM   6636 H HZ2  B LYS   B 1 163 ? 39.477 -42.006 -1.432  0.54 38.85 ?  163 LYS   B HZ2  1 
ATOM   6637 H HZ3  A LYS   B 1 163 ? 38.225 -40.588 -1.588  0.46 37.90 ?  163 LYS   B HZ3  1 
ATOM   6638 H HZ3  B LYS   B 1 163 ? 38.575 -40.884 -1.595  0.54 38.85 ?  163 LYS   B HZ3  1 
ATOM   6639 N N    . LEU   B 1 164 ? 38.986 -38.077 -7.945  1.00 18.82 ?  164 LEU   B N    1 
ATOM   6640 C CA   . LEU   B 1 164 ? 38.075 -36.942 -7.992  1.00 17.77 ?  164 LEU   B CA   1 
ATOM   6641 C C    . LEU   B 1 164 ? 37.297 -36.924 -9.299  1.00 18.15 ?  164 LEU   B C    1 
ATOM   6642 O O    . LEU   B 1 164 ? 36.073 -36.725 -9.301  1.00 19.15 ?  164 LEU   B O    1 
ATOM   6643 C CB   . LEU   B 1 164 ? 38.883 -35.654 -7.832  1.00 16.11 ?  164 LEU   B CB   1 
ATOM   6644 C CG   . LEU   B 1 164 ? 39.396 -35.347 -6.431  1.00 17.36 ?  164 LEU   B CG   1 
ATOM   6645 C CD1  . LEU   B 1 164 ? 40.478 -34.282 -6.515  1.00 17.44 ?  164 LEU   B CD1  1 
ATOM   6646 C CD2  . LEU   B 1 164 ? 38.273 -34.898 -5.506  1.00 19.56 ?  164 LEU   B CD2  1 
ATOM   6647 H H    A LEU   B 1 164 ? 39.826 -37.872 -8.017  0.46 22.60 ?  164 LEU   B H    1 
ATOM   6648 H H    B LEU   B 1 164 ? 39.826 -37.861 -7.947  0.54 22.60 ?  164 LEU   B H    1 
ATOM   6649 H HA   . LEU   B 1 164 ? 37.448 -37.010 -7.264  1.00 21.33 ?  164 LEU   B HA   1 
ATOM   6650 H HB2  . LEU   B 1 164 ? 39.662 -35.709 -8.416  1.00 19.35 ?  164 LEU   B HB2  1 
ATOM   6651 H HB3  . LEU   B 1 164 ? 38.328 -34.914 -8.110  1.00 19.35 ?  164 LEU   B HB3  1 
ATOM   6652 H HG   . LEU   B 1 164 ? 39.790 -36.150 -6.056  1.00 20.85 ?  164 LEU   B HG   1 
ATOM   6653 H HD11 . LEU   B 1 164 ? 40.786 -34.071 -5.619  1.00 20.95 ?  164 LEU   B HD11 1 
ATOM   6654 H HD12 . LEU   B 1 164 ? 41.216 -34.616 -7.048  1.00 20.95 ?  164 LEU   B HD12 1 
ATOM   6655 H HD13 . LEU   B 1 164 ? 40.107 -33.484 -6.930  1.00 20.95 ?  164 LEU   B HD13 1 
ATOM   6656 H HD21 . LEU   B 1 164 ? 38.654 -34.681 -4.638  1.00 23.49 ?  164 LEU   B HD21 1 
ATOM   6657 H HD22 . LEU   B 1 164 ? 37.849 -34.113 -5.884  1.00 23.49 ?  164 LEU   B HD22 1 
ATOM   6658 H HD23 . LEU   B 1 164 ? 37.630 -35.615 -5.414  1.00 23.49 ?  164 LEU   B HD23 1 
ATOM   6659 N N    A VAL   B 1 165 ? 37.985 -37.109 -10.426 0.46 19.33 ?  165 VAL   B N    1 
ATOM   6660 N N    B VAL   B 1 165 ? 37.993 -37.133 -10.420 0.54 19.55 ?  165 VAL   B N    1 
ATOM   6661 C CA   A VAL   B 1 165 ? 37.305 -37.055 -11.716 0.46 20.61 ?  165 VAL   B CA   1 
ATOM   6662 C CA   B VAL   B 1 165 ? 37.354 -37.084 -11.730 0.54 20.96 ?  165 VAL   B CA   1 
ATOM   6663 C C    A VAL   B 1 165 ? 36.365 -38.243 -11.870 0.46 22.32 ?  165 VAL   B C    1 
ATOM   6664 C C    B VAL   B 1 165 ? 36.439 -38.286 -11.927 0.54 22.74 ?  165 VAL   B C    1 
ATOM   6665 O O    A VAL   B 1 165 ? 35.189 -38.089 -12.222 0.46 23.31 ?  165 VAL   B O    1 
ATOM   6666 O O    B VAL   B 1 165 ? 35.313 -38.155 -12.421 0.54 23.61 ?  165 VAL   B O    1 
ATOM   6667 C CB   A VAL   B 1 165 ? 38.328 -36.981 -12.865 0.46 21.45 ?  165 VAL   B CB   1 
ATOM   6668 C CB   B VAL   B 1 165 ? 38.427 -36.988 -12.833 0.54 22.13 ?  165 VAL   B CB   1 
ATOM   6669 C CG1  A VAL   B 1 165 ? 37.623 -37.088 -14.203 0.46 22.74 ?  165 VAL   B CG1  1 
ATOM   6670 C CG1  B VAL   B 1 165 ? 37.799 -37.093 -14.205 0.54 23.31 ?  165 VAL   B CG1  1 
ATOM   6671 C CG2  A VAL   B 1 165 ? 39.143 -35.689 -12.778 0.46 21.50 ?  165 VAL   B CG2  1 
ATOM   6672 C CG2  B VAL   B 1 165 ? 39.227 -35.689 -12.698 0.54 22.09 ?  165 VAL   B CG2  1 
ATOM   6673 H H    A VAL   B 1 165 ? 38.837 -37.266 -10.476 0.46 23.21 ?  165 VAL   B H    1 
ATOM   6674 H H    B VAL   B 1 165 ? 38.843 -37.302 -10.452 0.54 23.47 ?  165 VAL   B H    1 
ATOM   6675 H HA   A VAL   B 1 165 ? 36.772 -36.249 -11.751 0.46 24.74 ?  165 VAL   B HA   1 
ATOM   6676 H HA   B VAL   B 1 165 ? 36.813 -36.283 -11.786 0.54 25.17 ?  165 VAL   B HA   1 
ATOM   6677 H HB   A VAL   B 1 165 ? 38.946 -37.725 -12.792 0.46 25.75 ?  165 VAL   B HB   1 
ATOM   6678 H HB   B VAL   B 1 165 ? 39.050 -37.725 -12.737 0.54 26.57 ?  165 VAL   B HB   1 
ATOM   6679 H HG11 A VAL   B 1 165 ? 38.222 -36.783 -14.901 0.46 27.30 ?  165 VAL   B HG11 1 
ATOM   6680 H HG11 B VAL   B 1 165 ? 38.442 -36.809 -14.872 0.54 27.99 ?  165 VAL   B HG11 1 
ATOM   6681 H HG12 A VAL   B 1 165 ? 37.386 -38.016 -14.360 0.46 27.30 ?  165 VAL   B HG12 1 
ATOM   6682 H HG12 B VAL   B 1 165 ? 37.548 -38.018 -14.366 0.54 27.99 ?  165 VAL   B HG12 1 
ATOM   6683 H HG13 A VAL   B 1 165 ? 36.826 -36.539 -14.185 0.46 27.30 ?  165 VAL   B HG13 1 
ATOM   6684 H HG13 B VAL   B 1 165 ? 37.015 -36.526 -14.237 0.54 27.99 ?  165 VAL   B HG13 1 
ATOM   6685 H HG21 A VAL   B 1 165 ? 39.765 -35.655 -13.524 0.46 25.82 ?  165 VAL   B HG21 1 
ATOM   6686 H HG21 B VAL   B 1 165 ? 39.878 -35.641 -13.418 0.54 26.52 ?  165 VAL   B HG21 1 
ATOM   6687 H HG22 A VAL   B 1 165 ? 38.540 -34.931 -12.818 0.46 25.82 ?  165 VAL   B HG22 1 
ATOM   6688 H HG22 B VAL   B 1 165 ? 38.619 -34.936 -12.753 0.54 26.52 ?  165 VAL   B HG22 1 
ATOM   6689 H HG23 A VAL   B 1 165 ? 39.633 -35.679 -11.941 0.46 25.82 ?  165 VAL   B HG23 1 
ATOM   6690 H HG23 B VAL   B 1 165 ? 39.683 -35.686 -11.842 0.54 26.52 ?  165 VAL   B HG23 1 
ATOM   6691 N N    A SER   B 1 166 ? 36.872 -39.446 -11.596 0.46 22.99 ?  166 SER   B N    1 
ATOM   6692 N N    B SER   B 1 166 ? 36.910 -39.476 -11.545 0.54 23.31 ?  166 SER   B N    1 
ATOM   6693 C CA   A SER   B 1 166 ? 36.098 -40.649 -11.871 0.46 23.85 ?  166 SER   B CA   1 
ATOM   6694 C CA   B SER   B 1 166 ? 36.153 -40.690 -11.826 0.54 24.14 ?  166 SER   B CA   1 
ATOM   6695 C C    A SER   B 1 166 ? 34.844 -40.720 -11.012 0.46 24.25 ?  166 SER   B C    1 
ATOM   6696 C C    B SER   B 1 166 ? 34.891 -40.778 -10.981 0.54 24.57 ?  166 SER   B C    1 
ATOM   6697 O O    A SER   B 1 166 ? 33.838 -41.279 -11.447 0.46 25.44 ?  166 SER   B O    1 
ATOM   6698 O O    B SER   B 1 166 ? 33.930 -41.427 -11.392 0.54 26.13 ?  166 SER   B O    1 
ATOM   6699 C CB   A SER   B 1 166 ? 36.967 -41.900 -11.705 0.46 24.35 ?  166 SER   B CB   1 
ATOM   6700 C CB   B SER   B 1 166 ? 37.026 -41.933 -11.630 0.54 24.81 ?  166 SER   B CB   1 
ATOM   6701 O OG   A SER   B 1 166 ? 37.358 -42.090 -10.356 0.46 24.32 ?  166 SER   B OG   1 
ATOM   6702 O OG   B SER   B 1 166 ? 37.385 -42.109 -10.269 0.54 24.76 ?  166 SER   B OG   1 
ATOM   6703 H H    A SER   B 1 166 ? 37.649 -39.590 -11.259 0.46 27.60 ?  166 SER   B H    1 
ATOM   6704 H H    B SER   B 1 166 ? 37.654 -39.603 -11.137 0.54 27.99 ?  166 SER   B H    1 
ATOM   6705 H HA   A SER   B 1 166 ? 35.805 -40.626 -12.795 0.46 28.63 ?  166 SER   B HA   1 
ATOM   6706 H HA   B SER   B 1 166 ? 35.876 -40.678 -12.756 0.54 28.98 ?  166 SER   B HA   1 
ATOM   6707 H HB2  A SER   B 1 166 ? 36.468 -42.675 -12.006 0.46 29.23 ?  166 SER   B HB2  1 
ATOM   6708 H HB2  B SER   B 1 166 ? 36.534 -42.713 -11.933 0.54 29.79 ?  166 SER   B HB2  1 
ATOM   6709 H HB3  A SER   B 1 166 ? 37.768 -41.798 -12.251 0.46 29.23 ?  166 SER   B HB3  1 
ATOM   6710 H HB3  B SER   B 1 166 ? 37.836 -41.832 -12.156 0.54 29.79 ?  166 SER   B HB3  1 
ATOM   6711 H HG   A SER   B 1 166 ? 37.790 -41.425 -10.091 0.46 29.20 ?  166 SER   B HG   1 
ATOM   6712 H HG   B SER   B 1 166 ? 37.805 -41.439 -10.000 0.54 29.73 ?  166 SER   B HG   1 
ATOM   6713 N N    . SER   B 1 167 ? 34.865 -40.144 -9.811  1.00 23.02 ?  167 SER   B N    1 
ATOM   6714 C CA   . SER   B 1 167 ? 33.710 -40.185 -8.920  1.00 23.24 ?  167 SER   B CA   1 
ATOM   6715 C C    . SER   B 1 167 ? 32.814 -38.952 -9.019  1.00 22.17 ?  167 SER   B C    1 
ATOM   6716 O O    . SER   B 1 167 ? 31.731 -38.944 -8.419  1.00 22.64 ?  167 SER   B O    1 
ATOM   6717 C CB   . SER   B 1 167 ? 34.155 -40.364 -7.462  1.00 23.37 ?  167 SER   B CB   1 
ATOM   6718 O OG   . SER   B 1 167 ? 34.841 -39.206 -7.002  1.00 23.71 ?  167 SER   B OG   1 
ATOM   6719 H H    A SER   B 1 167 ? 35.537 -39.716 -9.496  0.46 27.64 ?  167 SER   B H    1 
ATOM   6720 H H    B SER   B 1 167 ? 35.518 -39.681 -9.508  0.54 27.64 ?  167 SER   B H    1 
ATOM   6721 H HA   . SER   B 1 167 ? 33.170 -40.959 -9.156  1.00 27.91 ?  167 SER   B HA   1 
ATOM   6722 H HB2  . SER   B 1 167 ? 33.367 -40.515 -6.914  1.00 28.05 ?  167 SER   B HB2  1 
ATOM   6723 H HB3  . SER   B 1 167 ? 34.748 -41.131 -7.407  1.00 28.05 ?  167 SER   B HB3  1 
ATOM   6724 H HG   . SER   B 1 167 ? 35.513 -39.066 -7.486  1.00 28.47 ?  167 SER   B HG   1 
ATOM   6725 N N    . PHE   B 1 168 ? 33.204 -37.926 -9.777  1.00 21.84 ?  168 PHE   B N    1 
ATOM   6726 C CA   . PHE   B 1 168 ? 32.365 -36.733 -9.877  1.00 20.72 ?  168 PHE   B CA   1 
ATOM   6727 C C    . PHE   B 1 168 ? 31.064 -37.020 -10.630 1.00 18.75 ?  168 PHE   B C    1 
ATOM   6728 O O    . PHE   B 1 168 ? 30.008 -36.432 -10.311 1.00 19.62 ?  168 PHE   B O    1 
ATOM   6729 C CB   . PHE   B 1 168 ? 33.143 -35.597 -10.542 1.00 22.02 ?  168 PHE   B CB   1 
ATOM   6730 C CG   . PHE   B 1 168 ? 32.335 -34.362 -10.711 1.00 22.27 ?  168 PHE   B CG   1 
ATOM   6731 C CD1  . PHE   B 1 168 ? 31.979 -33.607 -9.605  1.00 24.40 ?  168 PHE   B CD1  1 
ATOM   6732 C CD2  . PHE   B 1 168 ? 31.899 -33.963 -11.960 1.00 21.93 ?  168 PHE   B CD2  1 
ATOM   6733 C CE1  . PHE   B 1 168 ? 31.209 -32.480 -9.739  1.00 24.86 ?  168 PHE   B CE1  1 
ATOM   6734 C CE2  . PHE   B 1 168 ? 31.154 -32.806 -12.109 1.00 23.57 ?  168 PHE   B CE2  1 
ATOM   6735 C CZ   . PHE   B 1 168 ? 30.798 -32.068 -10.995 1.00 23.98 ?  168 PHE   B CZ   1 
ATOM   6736 H H    . PHE   B 1 168 ? 33.938 -37.891 -10.232 1.00 26.23 ?  168 PHE   B H    1 
ATOM   6737 H HA   . PHE   B 1 168 ? 32.127 -36.448 -8.986  1.00 24.88 ?  168 PHE   B HA   1 
ATOM   6738 H HB2  . PHE   B 1 168 ? 33.912 -35.381 -9.993  1.00 26.44 ?  168 PHE   B HB2  1 
ATOM   6739 H HB3  . PHE   B 1 168 ? 33.434 -35.883 -11.422 1.00 26.44 ?  168 PHE   B HB3  1 
ATOM   6740 H HD1  . PHE   B 1 168 ? 32.249 -33.887 -8.761  1.00 29.30 ?  168 PHE   B HD1  1 
ATOM   6741 H HD2  . PHE   B 1 168 ? 32.147 -34.455 -12.710 1.00 26.33 ?  168 PHE   B HD2  1 
ATOM   6742 H HE1  . PHE   B 1 168 ? 30.975 -31.984 -8.989  1.00 29.85 ?  168 PHE   B HE1  1 
ATOM   6743 H HE2  . PHE   B 1 168 ? 30.870 -32.545 -12.955 1.00 28.30 ?  168 PHE   B HE2  1 
ATOM   6744 H HZ   . PHE   B 1 168 ? 30.281 -31.304 -11.093 1.00 28.79 ?  168 PHE   B HZ   1 
ATOM   6745 N N    A LEU   B 1 169 ? 31.114 -37.891 -11.633 0.46 19.29 ?  169 LEU   B N    1 
ATOM   6746 N N    B LEU   B 1 169 ? 31.122 -37.891 -11.633 0.54 19.11 ?  169 LEU   B N    1 
ATOM   6747 C CA   A LEU   B 1 169 ? 29.932 -38.206 -12.428 0.46 21.27 ?  169 LEU   B CA   1 
ATOM   6748 C CA   B LEU   B 1 169 ? 29.965 -38.200 -12.461 0.54 21.25 ?  169 LEU   B CA   1 
ATOM   6749 C C    A LEU   B 1 169 ? 29.928 -39.652 -12.896 0.46 23.41 ?  169 LEU   B C    1 
ATOM   6750 C C    B LEU   B 1 169 ? 30.018 -39.621 -12.995 0.54 23.62 ?  169 LEU   B C    1 
ATOM   6751 O O    A LEU   B 1 169 ? 28.972 -40.096 -13.534 0.46 24.66 ?  169 LEU   B O    1 
ATOM   6752 O O    B LEU   B 1 169 ? 29.228 -39.987 -13.867 0.54 24.70 ?  169 LEU   B O    1 
ATOM   6753 C CB   A LEU   B 1 169 ? 29.843 -37.287 -13.645 0.46 23.22 ?  169 LEU   B CB   1 
ATOM   6754 C CB   B LEU   B 1 169 ? 29.901 -37.247 -13.648 0.54 23.53 ?  169 LEU   B CB   1 
ATOM   6755 C CG   A LEU   B 1 169 ? 28.601 -36.394 -13.709 0.46 26.19 ?  169 LEU   B CG   1 
ATOM   6756 C CG   B LEU   B 1 169 ? 28.616 -36.435 -13.815 0.54 26.81 ?  169 LEU   B CG   1 
ATOM   6757 C CD1  A LEU   B 1 169 ? 28.581 -35.605 -15.005 0.46 27.14 ?  169 LEU   B CD1  1 
ATOM   6758 C CD1  B LEU   B 1 169 ? 28.578 -35.860 -15.210 0.54 27.75 ?  169 LEU   B CD1  1 
ATOM   6759 C CD2  A LEU   B 1 169 ? 27.329 -37.213 -13.560 0.46 26.82 ?  169 LEU   B CD2  1 
ATOM   6760 C CD2  B LEU   B 1 169 ? 27.373 -37.267 -13.540 0.54 27.71 ?  169 LEU   B CD2  1 
ATOM   6761 O OXT  A LEU   B 1 169 ? 30.872 -40.399 -12.659 0.46 24.27 -1 169 LEU   B OXT  1 
ATOM   6762 O OXT  B LEU   B 1 169 ? 30.851 -40.423 -12.589 0.54 24.78 -1 169 LEU   B OXT  1 
ATOM   6763 H H    A LEU   B 1 169 ? 31.823 -38.320 -11.877 0.46 23.17 ?  169 LEU   B H    1 
ATOM   6764 H H    B LEU   B 1 169 ? 31.833 -38.326 -11.860 0.54 22.95 ?  169 LEU   B H    1 
ATOM   6765 H HA   A LEU   B 1 169 ? 29.148 -38.071 -11.884 0.46 25.54 ?  169 LEU   B HA   1 
ATOM   6766 H HA   B LEU   B 1 169 ? 29.166 -38.106 -11.929 0.54 25.51 ?  169 LEU   B HA   1 
ATOM   6767 H HB2  A LEU   B 1 169 ? 30.617 -36.705 -13.645 0.46 27.88 ?  169 LEU   B HB2  1 
ATOM   6768 H HB2  B LEU   B 1 169 ? 30.630 -36.614 -13.568 0.54 28.25 ?  169 LEU   B HB2  1 
ATOM   6769 H HB3  A LEU   B 1 169 ? 29.847 -37.831 -14.449 0.46 27.88 ?  169 LEU   B HB3  1 
ATOM   6770 H HB3  B LEU   B 1 169 ? 30.016 -37.763 -14.463 0.54 28.25 ?  169 LEU   B HB3  1 
ATOM   6771 H HG   A LEU   B 1 169 ? 28.633 -35.760 -12.976 0.46 31.44 ?  169 LEU   B HG   1 
ATOM   6772 H HG   B LEU   B 1 169 ? 28.628 -35.696 -13.186 0.54 32.19 ?  169 LEU   B HG   1 
ATOM   6773 H HD11 A LEU   B 1 169 ? 27.798 -35.034 -15.014 0.46 32.59 ?  169 LEU   B HD11 1 
ATOM   6774 H HD11 B LEU   B 1 169 ? 27.785 -35.311 -15.301 0.54 33.31 ?  169 LEU   B HD11 1 
ATOM   6775 H HD12 A LEU   B 1 169 ? 29.386 -35.067 -15.057 0.46 32.59 ?  169 LEU   B HD12 1 
ATOM   6776 H HD12 B LEU   B 1 169 ? 29.373 -35.322 -15.349 0.54 33.31 ?  169 LEU   B HD12 1 
ATOM   6777 H HD13 A LEU   B 1 169 ? 28.548 -36.226 -15.750 0.46 32.59 ?  169 LEU   B HD13 1 
ATOM   6778 H HD13 B LEU   B 1 169 ? 28.555 -36.589 -15.849 0.54 33.31 ?  169 LEU   B HD13 1 
ATOM   6779 H HD21 A LEU   B 1 169 ? 26.585 -36.716 -13.929 0.46 32.20 ?  169 LEU   B HD21 1 
ATOM   6780 H HD21 B LEU   B 1 169 ? 26.616 -36.862 -13.987 0.54 33.26 ?  169 LEU   B HD21 1 
ATOM   6781 H HD22 A LEU   B 1 169 ? 27.438 -38.052 -14.037 0.46 32.20 ?  169 LEU   B HD22 1 
ATOM   6782 H HD22 B LEU   B 1 169 ? 27.515 -38.167 -13.877 0.54 33.26 ?  169 LEU   B HD22 1 
ATOM   6783 H HD23 A LEU   B 1 169 ? 27.177 -37.388 -12.618 0.46 32.20 ?  169 LEU   B HD23 1 
ATOM   6784 H HD23 B LEU   B 1 169 ? 27.218 -37.295 -12.583 0.54 33.26 ?  169 LEU   B HD23 1 
HETATM 6785 N N2   B A1BAX C 2 .   ? 15.178 1.568   6.330   0.54 15.01 ?  201 A1BAX A N2   1 
HETATM 6786 C C3   B A1BAX C 2 .   ? 15.666 4.903   5.234   0.54 14.96 ?  201 A1BAX A C3   1 
HETATM 6787 C C6   B A1BAX C 2 .   ? 14.985 1.711   3.529   0.54 15.15 ?  201 A1BAX A C6   1 
HETATM 6788 C C9   B A1BAX C 2 .   ? 13.223 -1.242  0.237   0.54 17.77 ?  201 A1BAX A C9   1 
HETATM 6789 C C12  B A1BAX C 2 .   ? 11.924 1.377   -0.018  0.54 18.99 ?  201 A1BAX A C12  1 
HETATM 6790 C C14  B A1BAX C 2 .   ? 11.715 1.064   -2.508  0.54 20.40 ?  201 A1BAX A C14  1 
HETATM 6791 C C1   B A1BAX C 2 .   ? 15.505 5.070   2.740   0.54 17.41 ?  201 A1BAX A C1   1 
HETATM 6792 C C10  B A1BAX C 2 .   ? 12.987 -0.600  -1.115  0.54 19.19 ?  201 A1BAX A C10  1 
HETATM 6793 C C11  B A1BAX C 2 .   ? 11.804 0.361   -1.153  0.54 19.47 ?  201 A1BAX A C11  1 
HETATM 6794 C C13  B A1BAX C 2 .   ? 12.143 0.727   1.346   0.54 17.75 ?  201 A1BAX A C13  1 
HETATM 6795 C C15  B A1BAX C 2 .   ? 15.247 2.903   4.234   0.54 14.42 ?  201 A1BAX A C15  1 
HETATM 6796 C C2   B A1BAX C 2 .   ? 15.468 4.311   3.994   0.54 15.09 ?  201 A1BAX A C2   1 
HETATM 6797 C C4   B A1BAX C 2 .   ? 15.325 2.735   5.642   0.54 15.12 ?  201 A1BAX A C4   1 
HETATM 6798 C C5   B A1BAX C 2 .   ? 14.941 0.530   5.525   0.54 13.94 ?  201 A1BAX A C5   1 
HETATM 6799 C C7   B A1BAX C 2 .   ? 14.722 0.498   1.363   0.54 16.64 ?  201 A1BAX A C7   1 
HETATM 6800 C C8   B A1BAX C 2 .   ? 13.329 -0.252  1.403   0.54 16.57 ?  201 A1BAX A C8   1 
HETATM 6801 N N1   B A1BAX C 2 .   ? 15.577 3.949   6.228   0.54 15.88 ?  201 A1BAX A N1   1 
HETATM 6802 N N3   B A1BAX C 2 .   ? 14.841 0.523   4.178   0.54 14.31 ?  201 A1BAX A N3   1 
HETATM 6803 N N4   B A1BAX C 2 .   ? 14.880 1.707   2.140   0.54 16.40 ?  201 A1BAX A N4   1 
HETATM 6804 O O1   B A1BAX C 2 .   ? 13.270 -0.960  2.625   0.54 16.35 ?  201 A1BAX A O1   1 
HETATM 6805 H H5   B A1BAX C 2 .   ? 15.855 5.946   5.484   0.54 17.97 ?  201 A1BAX A H5   1 
HETATM 6806 H H12  B A1BAX C 2 .   ? 14.123 -1.886  0.188   0.54 21.34 ?  201 A1BAX A H12  1 
HETATM 6807 H H11  B A1BAX C 2 .   ? 12.401 -1.958  0.445   0.54 21.34 ?  201 A1BAX A H11  1 
HETATM 6808 H H15  B A1BAX C 2 .   ? 11.000 1.978   0.027   0.54 22.80 ?  201 A1BAX A H15  1 
HETATM 6809 H H16  B A1BAX C 2 .   ? 12.719 2.112   -0.235  0.54 22.80 ?  201 A1BAX A H16  1 
HETATM 6810 H H20  B A1BAX C 2 .   ? 11.235 0.448   -3.280  0.54 24.50 ?  201 A1BAX A H20  1 
HETATM 6811 H H21  B A1BAX C 2 .   ? 12.694 1.349   -2.921  0.54 24.50 ?  201 A1BAX A H21  1 
HETATM 6812 H H19  B A1BAX C 2 .   ? 11.130 1.991   -2.463  0.54 24.50 ?  201 A1BAX A H19  1 
HETATM 6813 H H2   B A1BAX C 2 .   ? 15.582 4.453   1.842   0.54 20.90 ?  201 A1BAX A H2   1 
HETATM 6814 H H3   B A1BAX C 2 .   ? 16.333 5.785   2.720   0.54 20.90 ?  201 A1BAX A H3   1 
HETATM 6815 H H4   B A1BAX C 2 .   ? 14.590 5.679   2.605   0.54 20.90 ?  201 A1BAX A H4   1 
HETATM 6816 H H14  B A1BAX C 2 .   ? 13.915 -0.091  -1.459  0.54 23.04 ?  201 A1BAX A H14  1 
HETATM 6817 H H13  B A1BAX C 2 .   ? 12.819 -1.386  -1.861  0.54 23.04 ?  201 A1BAX A H13  1 
HETATM 6818 H H1   B A1BAX C 2 .   ? 10.856 -0.222  -1.022  0.54 23.38 ?  201 A1BAX A H1   1 
HETATM 6819 H H18  B A1BAX C 2 .   ? 11.211 0.195   1.637   0.54 21.32 ?  201 A1BAX A H18  1 
HETATM 6820 H H17  B A1BAX C 2 .   ? 12.256 1.504   2.123   0.54 21.32 ?  201 A1BAX A H17  1 
HETATM 6821 H H7   B A1BAX C 2 .   ? 14.816 -0.424  6.074   0.54 16.75 ?  201 A1BAX A H7   1 
HETATM 6822 H H9   B A1BAX C 2 .   ? 14.893 0.828   0.311   0.54 19.98 ?  201 A1BAX A H9   1 
HETATM 6823 H H10  B A1BAX C 2 .   ? 15.534 -0.228  1.573   0.54 19.98 ?  201 A1BAX A H10  1 
HETATM 6824 H H6   B A1BAX C 2 .   ? 15.675 4.097   7.240   0.54 19.07 ?  201 A1BAX A H6   1 
HETATM 6825 H H8   B A1BAX C 2 .   ? 14.914 2.603   1.698   0.54 19.69 ?  201 A1BAX A H8   1 
HETATM 6826 H H22  B A1BAX C 2 .   ? 12.396 -1.313  2.730   0.54 19.63 ?  201 A1BAX A H22  1 
HETATM 6827 O O    . HOH   D 3 .   ? 11.977 0.639   14.882  1.00 45.52 ?  301 HOH   A O    1 
HETATM 6828 O O    . HOH   D 3 .   ? 14.631 -4.446  20.560  1.00 49.06 ?  302 HOH   A O    1 
HETATM 6829 O O    . HOH   D 3 .   ? 34.449 -1.771  12.476  1.00 47.86 ?  303 HOH   A O    1 
HETATM 6830 O O    . HOH   D 3 .   ? 11.572 -10.508 -10.130 1.00 51.98 ?  304 HOH   A O    1 
HETATM 6831 O O    . HOH   D 3 .   ? 23.843 -15.759 -9.280  1.00 43.36 ?  305 HOH   A O    1 
HETATM 6832 O O    . HOH   D 3 .   ? 29.009 0.360   -9.850  1.00 22.10 ?  306 HOH   A O    1 
HETATM 6833 O O    A HOH   D 3 .   ? 4.705  4.077   0.537   0.46 24.97 ?  307 HOH   A O    1 
HETATM 6834 O O    . HOH   D 3 .   ? 25.801 -0.885  -7.575  1.00 22.88 ?  308 HOH   A O    1 
HETATM 6835 O O    . HOH   D 3 .   ? 0.762  -4.138  -0.119  1.00 33.89 ?  309 HOH   A O    1 
HETATM 6836 O O    . HOH   D 3 .   ? 22.799 12.609  1.628   1.00 19.12 ?  310 HOH   A O    1 
HETATM 6837 O O    . HOH   D 3 .   ? 7.978  -12.471 -0.818  1.00 34.24 ?  311 HOH   A O    1 
HETATM 6838 O O    . HOH   D 3 .   ? 18.935 -21.837 6.944   1.00 41.00 ?  312 HOH   A O    1 
HETATM 6839 O O    . HOH   D 3 .   ? 14.317 -4.528  -11.945 1.00 40.84 ?  313 HOH   A O    1 
HETATM 6840 O O    . HOH   D 3 .   ? 28.231 -6.121  19.519  1.00 45.30 ?  314 HOH   A O    1 
HETATM 6841 O O    . HOH   D 3 .   ? 14.954 -12.088 18.612  1.00 48.19 ?  315 HOH   A O    1 
HETATM 6842 O O    . HOH   D 3 .   ? 16.985 -17.992 14.768  1.00 34.26 ?  316 HOH   A O    1 
HETATM 6843 O O    . HOH   D 3 .   ? -0.806 -8.390  2.098   1.00 54.51 ?  317 HOH   A O    1 
HETATM 6844 O O    . HOH   D 3 .   ? 14.675 -13.878 16.549  1.00 33.51 ?  318 HOH   A O    1 
HETATM 6845 O O    . HOH   D 3 .   ? 42.573 10.553  5.204   1.00 22.95 ?  319 HOH   A O    1 
HETATM 6846 O O    B HOH   D 3 .   ? 8.433  4.010   0.811   0.54 27.22 ?  320 HOH   A O    1 
HETATM 6847 O O    . HOH   D 3 .   ? 21.321 -2.234  -2.394  1.00 24.40 ?  321 HOH   A O    1 
HETATM 6848 O O    . HOH   D 3 .   ? 9.072  -10.099 19.152  1.00 50.63 ?  322 HOH   A O    1 
HETATM 6849 O O    . HOH   D 3 .   ? 26.985 11.531  1.602   1.00 21.31 ?  323 HOH   A O    1 
HETATM 6850 O O    A HOH   D 3 .   ? 3.559  -9.269  9.695   0.46 34.76 ?  324 HOH   A O    1 
HETATM 6851 O O    . HOH   D 3 .   ? 16.883 -19.028 4.906   1.00 22.16 ?  325 HOH   A O    1 
HETATM 6852 O O    . HOH   D 3 .   ? 13.509 -15.153 -7.614  1.00 34.29 ?  326 HOH   A O    1 
HETATM 6853 O O    . HOH   D 3 .   ? 15.143 4.228   17.623  1.00 39.04 ?  327 HOH   A O    1 
HETATM 6854 O O    . HOH   D 3 .   ? 17.068 -17.697 -5.087  1.00 34.35 ?  328 HOH   A O    1 
HETATM 6855 O O    . HOH   D 3 .   ? 9.901  -21.217 5.606   1.00 27.03 ?  329 HOH   A O    1 
HETATM 6856 O O    B HOH   D 3 .   ? 14.740 -3.486  3.347   0.54 24.66 ?  330 HOH   A O    1 
HETATM 6857 O O    . HOH   D 3 .   ? 30.204 -13.303 -8.600  1.00 23.63 ?  331 HOH   A O    1 
HETATM 6858 O O    B HOH   D 3 .   ? 3.685  -15.403 -3.646  0.54 34.56 ?  332 HOH   A O    1 
HETATM 6859 O O    . HOH   D 3 .   ? 34.027 -1.078  -8.983  1.00 29.41 ?  333 HOH   A O    1 
HETATM 6860 O O    . HOH   D 3 .   ? 31.819 8.226   14.804  1.00 27.85 ?  334 HOH   A O    1 
HETATM 6861 O O    A HOH   D 3 .   ? 28.232 -0.162  -13.385 0.46 28.58 ?  335 HOH   A O    1 
HETATM 6862 O O    A HOH   D 3 .   ? 14.271 0.722   6.739   0.46 25.21 ?  336 HOH   A O    1 
HETATM 6863 O O    . HOH   D 3 .   ? 42.541 4.283   5.325   1.00 31.99 ?  337 HOH   A O    1 
HETATM 6864 O O    . HOH   D 3 .   ? 37.560 2.714   10.132  1.00 31.43 ?  338 HOH   A O    1 
HETATM 6865 O O    . HOH   D 3 .   ? 30.917 -18.059 7.849   1.00 23.69 ?  339 HOH   A O    1 
HETATM 6866 O O    . HOH   D 3 .   ? 38.328 10.159  7.127   1.00 28.57 ?  340 HOH   A O    1 
HETATM 6867 O O    . HOH   D 3 .   ? 13.344 -1.467  -6.555  1.00 26.17 ?  341 HOH   A O    1 
HETATM 6868 O O    . HOH   D 3 .   ? 22.526 -11.839 21.816  1.00 54.68 ?  342 HOH   A O    1 
HETATM 6869 O O    . HOH   D 3 .   ? 39.728 -0.988  -5.192  1.00 23.38 ?  343 HOH   A O    1 
HETATM 6870 O O    A HOH   D 3 .   ? -0.491 -2.906  3.040   0.46 29.44 ?  344 HOH   A O    1 
HETATM 6871 O O    . HOH   D 3 .   ? 28.543 -10.577 -14.018 1.00 48.38 ?  345 HOH   A O    1 
HETATM 6872 O O    . HOH   D 3 .   ? 19.872 -12.505 -8.826  1.00 29.13 ?  346 HOH   A O    1 
HETATM 6873 O O    . HOH   D 3 .   ? 21.347 10.395  14.933  1.00 40.35 ?  347 HOH   A O    1 
HETATM 6874 O O    . HOH   D 3 .   ? 35.703 -12.632 6.845   1.00 19.26 ?  348 HOH   A O    1 
HETATM 6875 O O    . HOH   D 3 .   ? 20.532 -19.620 -5.083  1.00 31.26 ?  349 HOH   A O    1 
HETATM 6876 O O    . HOH   D 3 .   ? 10.261 -22.144 -1.178  1.00 58.01 ?  350 HOH   A O    1 
HETATM 6877 O O    . HOH   D 3 .   ? 37.338 12.047  4.972   1.00 38.44 ?  351 HOH   A O    1 
HETATM 6878 O O    . HOH   D 3 .   ? 24.348 3.692   -1.844  1.00 21.31 ?  352 HOH   A O    1 
HETATM 6879 O O    . HOH   D 3 .   ? 44.379 7.121   6.443   1.00 29.66 ?  353 HOH   A O    1 
HETATM 6880 O O    A HOH   D 3 .   ? 14.620 -3.519  3.051   0.46 14.78 ?  354 HOH   A O    1 
HETATM 6881 O O    . HOH   D 3 .   ? 18.600 9.648   8.868   1.00 25.80 ?  355 HOH   A O    1 
HETATM 6882 O O    . HOH   D 3 .   ? 24.039 -2.005  -2.207  1.00 13.65 ?  356 HOH   A O    1 
HETATM 6883 O O    . HOH   D 3 .   ? 31.007 -13.885 -2.516  1.00 16.29 ?  357 HOH   A O    1 
HETATM 6884 O O    . HOH   D 3 .   ? 38.573 5.019   6.929   1.00 18.82 ?  358 HOH   A O    1 
HETATM 6885 O O    . HOH   D 3 .   ? 22.202 -19.169 11.463  1.00 42.30 ?  359 HOH   A O    1 
HETATM 6886 O O    . HOH   D 3 .   ? 5.236  3.099   4.709   1.00 42.99 ?  360 HOH   A O    1 
HETATM 6887 O O    . HOH   D 3 .   ? 37.204 -2.914  9.624   1.00 46.18 ?  361 HOH   A O    1 
HETATM 6888 O O    . HOH   D 3 .   ? 27.404 -10.402 14.038  1.00 21.70 ?  362 HOH   A O    1 
HETATM 6889 O O    A HOH   D 3 .   ? 6.911  -7.972  11.811  0.46 20.10 ?  363 HOH   A O    1 
HETATM 6890 O O    . HOH   D 3 .   ? 13.938 -22.882 7.389   1.00 23.55 ?  364 HOH   A O    1 
HETATM 6891 O O    . HOH   D 3 .   ? 31.893 -9.290  -6.693  1.00 25.38 ?  365 HOH   A O    1 
HETATM 6892 O O    . HOH   D 3 .   ? 18.865 -0.671  -1.713  1.00 25.47 ?  366 HOH   A O    1 
HETATM 6893 O O    . HOH   D 3 .   ? 37.563 -2.049  5.906   1.00 29.14 ?  367 HOH   A O    1 
HETATM 6894 O O    . HOH   D 3 .   ? 14.381 -21.121 -4.359  1.00 36.41 ?  368 HOH   A O    1 
HETATM 6895 O O    A HOH   D 3 .   ? 15.115 -21.429 14.176  0.46 17.93 ?  369 HOH   A O    1 
HETATM 6896 O O    . HOH   D 3 .   ? 27.435 13.924  2.725   1.00 37.75 ?  370 HOH   A O    1 
HETATM 6897 O O    . HOH   D 3 .   ? 30.815 3.163   8.187   1.00 14.78 ?  371 HOH   A O    1 
HETATM 6898 O O    . HOH   D 3 .   ? 36.349 -4.981  -0.543  1.00 41.67 ?  372 HOH   A O    1 
HETATM 6899 O O    B HOH   D 3 .   ? 6.417  -13.980 3.182   0.54 38.89 ?  373 HOH   A O    1 
HETATM 6900 O O    . HOH   D 3 .   ? 18.661 -19.415 13.598  1.00 45.98 ?  374 HOH   A O    1 
HETATM 6901 O O    . HOH   D 3 .   ? 22.161 5.612   18.837  1.00 40.00 ?  375 HOH   A O    1 
HETATM 6902 O O    . HOH   D 3 .   ? 44.066 8.485   -3.068  1.00 31.32 ?  376 HOH   A O    1 
HETATM 6903 O O    . HOH   D 3 .   ? 33.467 -16.909 8.079   1.00 22.26 ?  377 HOH   A O    1 
HETATM 6904 O O    . HOH   D 3 .   ? 27.431 -6.316  -14.185 1.00 37.42 ?  378 HOH   A O    1 
HETATM 6905 O O    . HOH   D 3 .   ? 33.638 -7.111  4.283   1.00 20.00 ?  379 HOH   A O    1 
HETATM 6906 O O    A HOH   D 3 .   ? 24.594 2.109   -7.044  0.46 19.05 ?  380 HOH   A O    1 
HETATM 6907 O O    . HOH   D 3 .   ? 8.284  -21.437 3.965   1.00 50.40 ?  381 HOH   A O    1 
HETATM 6908 O O    . HOH   D 3 .   ? 16.399 -21.909 0.933   1.00 38.53 ?  382 HOH   A O    1 
HETATM 6909 O O    . HOH   D 3 .   ? 21.312 3.153   -0.304  1.00 17.32 ?  383 HOH   A O    1 
HETATM 6910 O O    . HOH   D 3 .   ? 43.412 7.853   2.712   1.00 25.54 ?  384 HOH   A O    1 
HETATM 6911 O O    . HOH   D 3 .   ? 23.532 11.497  4.048   1.00 16.30 ?  385 HOH   A O    1 
HETATM 6912 O O    . HOH   D 3 .   ? 21.766 -21.826 8.494   1.00 37.11 ?  386 HOH   A O    1 
HETATM 6913 O O    . HOH   D 3 .   ? 31.802 -7.272  -9.892  1.00 24.54 ?  387 HOH   A O    1 
HETATM 6914 O O    . HOH   D 3 .   ? 24.156 -7.618  14.410  1.00 20.71 ?  388 HOH   A O    1 
HETATM 6915 O O    . HOH   D 3 .   ? 31.051 6.138   -12.334 1.00 29.18 ?  389 HOH   A O    1 
HETATM 6916 O O    . HOH   D 3 .   ? 10.943 1.958   12.534  1.00 29.96 ?  390 HOH   A O    1 
HETATM 6917 O O    . HOH   D 3 .   ? 13.859 -4.664  17.290  1.00 32.12 ?  391 HOH   A O    1 
HETATM 6918 O O    A HOH   D 3 .   ? 17.489 -1.597  0.392   0.46 21.00 ?  392 HOH   A O    1 
HETATM 6919 O O    . HOH   D 3 .   ? 32.749 -9.173  5.957   1.00 21.59 ?  393 HOH   A O    1 
HETATM 6920 O O    . HOH   D 3 .   ? 30.663 1.990   16.667  1.00 23.82 ?  394 HOH   A O    1 
HETATM 6921 O O    . HOH   D 3 .   ? 38.135 -1.337  -1.936  1.00 20.53 ?  395 HOH   A O    1 
HETATM 6922 O O    . HOH   D 3 .   ? 20.495 -19.899 2.788   1.00 24.04 ?  396 HOH   A O    1 
HETATM 6923 O O    . HOH   D 3 .   ? 27.293 2.518   18.688  1.00 32.75 ?  397 HOH   A O    1 
HETATM 6924 O O    . HOH   D 3 .   ? 26.979 4.227   -0.742  1.00 15.41 ?  398 HOH   A O    1 
HETATM 6925 O O    B HOH   D 3 .   ? 4.586  3.446   0.255   0.54 20.01 ?  399 HOH   A O    1 
HETATM 6926 O O    . HOH   D 3 .   ? 29.682 -2.009  -12.885 1.00 50.52 ?  400 HOH   A O    1 
HETATM 6927 O O    B HOH   D 3 .   ? 5.290  -14.208 5.876   0.54 30.03 ?  401 HOH   A O    1 
HETATM 6928 O O    A HOH   D 3 .   ? 6.723  -3.193  12.835  0.46 31.20 ?  402 HOH   A O    1 
HETATM 6929 O O    . HOH   D 3 .   ? 30.006 -9.993  13.005  1.00 24.92 ?  403 HOH   A O    1 
HETATM 6930 O O    . HOH   D 3 .   ? 9.083  -11.960 17.203  1.00 48.13 ?  404 HOH   A O    1 
HETATM 6931 O O    . HOH   D 3 .   ? 24.068 4.157   -4.903  1.00 28.91 ?  405 HOH   A O    1 
HETATM 6932 O O    . HOH   D 3 .   ? 23.854 -20.177 -1.322  1.00 20.04 ?  406 HOH   A O    1 
HETATM 6933 O O    . HOH   D 3 .   ? 22.643 8.309   18.197  1.00 46.83 ?  407 HOH   A O    1 
HETATM 6934 O O    . HOH   D 3 .   ? 32.721 -4.255  -9.875  1.00 33.13 ?  408 HOH   A O    1 
HETATM 6935 O O    A HOH   D 3 .   ? 15.792 -0.807  5.216   0.46 32.96 ?  409 HOH   A O    1 
HETATM 6936 O O    A HOH   D 3 .   ? 6.438  -5.416  11.132  0.46 20.93 ?  410 HOH   A O    1 
HETATM 6937 O O    A HOH   D 3 .   ? 14.489 -0.359  -12.095 0.46 22.52 ?  411 HOH   A O    1 
HETATM 6938 O O    . HOH   D 3 .   ? 16.152 16.717  8.464   1.00 44.93 ?  412 HOH   A O    1 
HETATM 6939 O O    A HOH   D 3 .   ? 18.576 -2.406  -16.385 0.46 28.02 ?  413 HOH   A O    1 
HETATM 6940 O O    . HOH   D 3 .   ? 40.878 -8.331  -6.572  1.00 41.00 ?  414 HOH   A O    1 
HETATM 6941 O O    . HOH   D 3 .   ? 15.073 -8.002  -9.815  1.00 39.40 ?  415 HOH   A O    1 
HETATM 6942 O O    . HOH   D 3 .   ? 44.869 -0.596  3.024   1.00 42.32 ?  416 HOH   A O    1 
HETATM 6943 O O    . HOH   D 3 .   ? 30.263 -12.799 13.478  1.00 22.86 ?  417 HOH   A O    1 
HETATM 6944 O O    A HOH   D 3 .   ? 20.118 4.624   -7.615  0.46 18.54 ?  418 HOH   A O    1 
HETATM 6945 O O    . HOH   D 3 .   ? 24.650 -17.423 12.703  1.00 29.91 ?  419 HOH   A O    1 
HETATM 6946 O O    . HOH   D 3 .   ? 21.683 -13.833 -8.207  1.00 53.76 ?  420 HOH   A O    1 
HETATM 6947 O O    . HOH   D 3 .   ? 32.447 -10.583 3.216   1.00 34.50 ?  421 HOH   A O    1 
HETATM 6948 O O    A HOH   D 3 .   ? 11.063 -0.237  1.874   0.46 30.98 ?  422 HOH   A O    1 
HETATM 6949 O O    . HOH   D 3 .   ? 27.937 0.888   -7.257  1.00 16.72 ?  423 HOH   A O    1 
HETATM 6950 O O    . HOH   D 3 .   ? 35.011 -5.218  -3.056  1.00 19.60 ?  424 HOH   A O    1 
HETATM 6951 O O    . HOH   D 3 .   ? 36.683 -5.022  5.350   1.00 28.07 ?  425 HOH   A O    1 
HETATM 6952 O O    A HOH   D 3 .   ? 7.696  -6.204  -6.554  0.46 35.96 ?  426 HOH   A O    1 
HETATM 6953 O O    A HOH   D 3 .   ? 16.037 7.085   2.910   0.46 20.16 ?  427 HOH   A O    1 
HETATM 6954 O O    . HOH   D 3 .   ? 10.320 -13.592 -1.708  1.00 26.05 ?  428 HOH   A O    1 
HETATM 6955 O O    . HOH   D 3 .   ? 41.650 1.654   4.983   1.00 40.95 ?  429 HOH   A O    1 
HETATM 6956 O O    . HOH   D 3 .   ? 23.276 7.571   -3.195  1.00 37.80 ?  430 HOH   A O    1 
HETATM 6957 O O    . HOH   D 3 .   ? 21.131 -9.018  21.313  1.00 58.77 ?  431 HOH   A O    1 
HETATM 6958 O O    A HOH   D 3 .   ? 18.869 2.141   -0.813  0.46 12.89 ?  432 HOH   A O    1 
HETATM 6959 O O    . HOH   D 3 .   ? 14.505 -24.679 11.493  1.00 47.67 ?  433 HOH   A O    1 
HETATM 6960 O O    A HOH   D 3 .   ? 18.461 4.905   -15.099 0.46 49.70 ?  434 HOH   A O    1 
HETATM 6961 O O    . HOH   D 3 .   ? 19.503 -10.515 23.919  1.00 91.86 ?  435 HOH   A O    1 
HETATM 6962 O O    . HOH   D 3 .   ? 27.087 -3.041  19.381  1.00 43.00 ?  436 HOH   A O    1 
HETATM 6963 O O    . HOH   D 3 .   ? 23.283 -20.849 1.328   1.00 22.11 ?  437 HOH   A O    1 
HETATM 6964 O O    A HOH   D 3 .   ? 16.268 3.062   -1.508  0.46 14.50 ?  438 HOH   A O    1 
HETATM 6965 O O    . HOH   D 3 .   ? 11.738 -10.597 16.920  1.00 33.87 ?  439 HOH   A O    1 
HETATM 6966 O O    A HOH   D 3 .   ? 15.850 2.409   24.722  0.46 35.77 ?  440 HOH   A O    1 
HETATM 6967 O O    . HOH   D 3 .   ? 23.580 -7.924  17.114  1.00 28.18 ?  441 HOH   A O    1 
HETATM 6968 O O    . HOH   D 3 .   ? 16.106 -14.129 20.117  1.00 60.23 ?  442 HOH   A O    1 
HETATM 6969 O O    B HOH   D 3 .   ? 17.714 3.930   -3.033  0.54 39.32 ?  443 HOH   A O    1 
HETATM 6970 O O    . HOH   D 3 .   ? 15.450 11.800  7.903   1.00 52.25 ?  444 HOH   A O    1 
HETATM 6971 O O    . HOH   D 3 .   ? 31.292 -12.774 0.066   1.00 22.79 ?  445 HOH   A O    1 
HETATM 6972 O O    A HOH   D 3 .   ? 9.333  -16.190 -1.991  0.46 30.22 ?  446 HOH   A O    1 
HETATM 6973 O O    B HOH   D 3 .   ? 3.461  2.432   2.408   0.54 21.57 ?  447 HOH   A O    1 
HETATM 6974 O O    B HOH   D 3 .   ? 15.744 3.008   -0.559  0.54 25.45 ?  448 HOH   A O    1 
HETATM 6975 O O    . HOH   D 3 .   ? 30.682 14.837  2.717   1.00 21.96 ?  449 HOH   A O    1 
HETATM 6976 O O    . HOH   D 3 .   ? 34.417 -8.094  -0.644  1.00 33.29 ?  450 HOH   A O    1 
HETATM 6977 O O    . HOH   D 3 .   ? 21.394 -14.635 17.910  1.00 62.14 ?  451 HOH   A O    1 
HETATM 6978 O O    . HOH   D 3 .   ? 37.628 -8.745  -3.307  1.00 25.80 ?  452 HOH   A O    1 
HETATM 6979 O O    . HOH   D 3 .   ? 20.615 -17.586 24.900  1.00 68.07 ?  453 HOH   A O    1 
HETATM 6980 O O    . HOH   D 3 .   ? 18.379 -15.903 16.370  1.00 45.89 ?  454 HOH   A O    1 
HETATM 6981 O O    A HOH   D 3 .   ? 14.022 -0.200  3.404   0.46 22.77 ?  455 HOH   A O    1 
HETATM 6982 O O    . HOH   D 3 .   ? -1.687 -4.777  7.465   1.00 58.49 ?  456 HOH   A O    1 
HETATM 6983 O O    B HOH   D 3 .   ? 18.257 1.868   -0.459  0.54 21.27 ?  457 HOH   A O    1 
HETATM 6984 O O    . HOH   D 3 .   ? 29.775 -15.886 10.714  1.00 36.98 ?  458 HOH   A O    1 
HETATM 6985 O O    . HOH   D 3 .   ? 25.434 8.285   -4.818  1.00 37.93 ?  459 HOH   A O    1 
HETATM 6986 O O    . HOH   D 3 .   ? 27.861 7.023   -6.642  1.00 44.80 ?  460 HOH   A O    1 
HETATM 6987 O O    . HOH   D 3 .   ? 32.327 -15.913 10.852  1.00 40.60 ?  461 HOH   A O    1 
HETATM 6988 O O    . HOH   D 3 .   ? 24.782 5.834   20.768  1.00 57.14 ?  462 HOH   A O    1 
HETATM 6989 O O    . HOH   D 3 .   ? 19.783 -17.243 -5.064  1.00 34.03 ?  463 HOH   A O    1 
HETATM 6990 O O    . HOH   D 3 .   ? 23.031 -22.352 -3.307  1.00 39.05 ?  464 HOH   A O    1 
HETATM 6991 O O    . HOH   D 3 .   ? 24.612 14.760  7.719   1.00 42.85 ?  465 HOH   A O    1 
HETATM 6992 O O    . HOH   D 3 .   ? 18.850 11.150  11.078  1.00 36.78 ?  466 HOH   A O    1 
HETATM 6993 O O    . HOH   D 3 .   ? 15.745 -21.381 3.795   1.00 30.66 ?  467 HOH   A O    1 
HETATM 6994 O O    B HOH   D 3 .   ? 15.681 5.408   -1.973  0.54 24.91 ?  468 HOH   A O    1 
HETATM 6995 O O    A HOH   D 3 .   ? 11.120 -14.740 -6.150  0.46 32.52 ?  469 HOH   A O    1 
HETATM 6996 O O    . HOH   D 3 .   ? 12.323 1.766   17.230  1.00 47.50 ?  470 HOH   A O    1 
HETATM 6997 O O    B HOH   D 3 .   ? 1.491  3.963   3.217   0.54 32.27 ?  471 HOH   A O    1 
HETATM 6998 O O    . HOH   D 3 .   ? 27.365 -11.234 16.527  1.00 40.35 ?  472 HOH   A O    1 
HETATM 6999 O O    . HOH   D 3 .   ? 39.560 -6.999  -3.380  1.00 46.76 ?  473 HOH   A O    1 
HETATM 7000 O O    A HOH   D 3 .   ? 21.986 5.348   -5.905  0.46 28.38 ?  474 HOH   A O    1 
HETATM 7001 O O    . HOH   D 3 .   ? 25.754 10.930  -3.810  1.00 41.78 ?  475 HOH   A O    1 
HETATM 7002 O O    . HOH   D 3 .   ? 26.953 11.912  -1.645  1.00 42.16 ?  476 HOH   A O    1 
HETATM 7003 O O    . HOH   D 3 .   ? 22.995 11.763  -4.138  1.00 26.12 ?  477 HOH   A O    1 
HETATM 7004 O O    . HOH   D 3 .   ? 15.618 -16.926 -7.037  1.00 40.41 ?  478 HOH   A O    1 
HETATM 7005 O O    . HOH   D 3 .   ? 23.455 13.826  5.461   1.00 23.41 ?  479 HOH   A O    1 
HETATM 7006 O O    . HOH   D 3 .   ? 13.978 -10.136 -10.922 1.00 38.42 ?  480 HOH   A O    1 
HETATM 7007 O O    . HOH   D 3 .   ? 28.608 -4.760  -12.432 1.00 39.88 ?  481 HOH   A O    1 
HETATM 7008 O O    . HOH   D 3 .   ? 18.029 -16.174 -8.968  1.00 48.65 ?  482 HOH   A O    1 
HETATM 7009 O O    . HOH   D 3 .   ? 12.009 -12.948 16.733  1.00 69.06 ?  483 HOH   A O    1 
HETATM 7010 O O    . HOH   D 3 .   ? 29.014 8.992   17.523  1.00 43.46 ?  484 HOH   A O    1 
HETATM 7011 O O    . HOH   D 3 .   ? 16.898 -20.425 16.048  1.00 38.23 ?  485 HOH   A O    1 
HETATM 7012 O O    . HOH   D 3 .   ? 17.464 -18.677 19.791  1.00 56.87 ?  486 HOH   A O    1 
HETATM 7013 O O    . HOH   D 3 .   ? 28.496 -7.974  -15.462 1.00 53.75 ?  487 HOH   A O    1 
HETATM 7014 O O    . HOH   D 3 .   ? 41.020 -4.021  -0.356  1.00 42.25 ?  488 HOH   A O    1 
HETATM 7015 O O    . HOH   D 3 .   ? 30.674 0.775   19.276  1.00 44.70 ?  489 HOH   A O    1 
HETATM 7016 O O    . HOH   D 3 .   ? 35.447 7.444   12.167  1.00 40.91 ?  490 HOH   A O    1 
HETATM 7017 O O    . HOH   D 3 .   ? 23.222 -12.612 19.368  1.00 53.20 ?  491 HOH   A O    1 
HETATM 7018 O O    . HOH   D 3 .   ? 39.220 2.433   7.221   1.00 37.96 ?  492 HOH   A O    1 
HETATM 7019 O O    . HOH   D 3 .   ? 13.877 -25.091 8.901   1.00 36.74 ?  493 HOH   A O    1 
HETATM 7020 O O    . HOH   D 3 .   ? 41.824 9.378   -4.098  1.00 34.62 ?  494 HOH   A O    1 
HETATM 7021 O O    . HOH   D 3 .   ? 44.592 10.481  -1.511  1.00 32.02 ?  495 HOH   A O    1 
HETATM 7022 O O    . HOH   D 3 .   ? 25.742 -18.925 -11.897 1.00 41.63 ?  496 HOH   A O    1 
HETATM 7023 O O    . HOH   D 3 .   ? 19.983 -22.214 4.205   1.00 35.03 ?  497 HOH   A O    1 
HETATM 7024 O O    . HOH   D 3 .   ? 20.424 -15.869 -7.470  1.00 34.65 ?  498 HOH   A O    1 
HETATM 7025 O O    . HOH   D 3 .   ? 16.197 -23.322 5.838   1.00 41.06 ?  499 HOH   A O    1 
HETATM 7026 O O    . HOH   D 3 .   ? 18.504 -23.082 1.882   1.00 49.52 ?  500 HOH   A O    1 
HETATM 7027 O O    . HOH   D 3 .   ? 31.678 -0.655  -10.542 1.00 27.76 ?  501 HOH   A O    1 
HETATM 7028 O O    . HOH   D 3 .   ? 40.526 -0.257  -7.892  1.00 38.92 ?  502 HOH   A O    1 
HETATM 7029 O O    B HOH   D 3 .   ? 13.823 7.689   4.476   0.54 25.86 ?  503 HOH   A O    1 
HETATM 7030 O O    . HOH   D 3 .   ? 15.993 -6.731  -11.976 1.00 49.06 ?  504 HOH   A O    1 
HETATM 7031 O O    . HOH   D 3 .   ? 8.185  -2.889  -5.887  1.00 60.36 ?  505 HOH   A O    1 
HETATM 7032 O O    . HOH   D 3 .   ? 37.360 -6.624  7.473   1.00 29.07 ?  506 HOH   A O    1 
HETATM 7033 O O    . HOH   D 3 .   ? 30.810 -5.891  -11.949 1.00 50.44 ?  507 HOH   A O    1 
HETATM 7034 O O    . HOH   D 3 .   ? 30.742 5.746   -14.767 1.00 40.12 ?  508 HOH   A O    1 
HETATM 7035 O O    . HOH   D 3 .   ? 39.521 -0.001  6.564   1.00 32.91 ?  509 HOH   A O    1 
HETATM 7036 O O    . HOH   D 3 .   ? 38.042 13.897  6.792   1.00 57.45 ?  510 HOH   A O    1 
HETATM 7037 O O    . HOH   D 3 .   ? 23.087 -23.781 1.640   1.00 36.72 ?  511 HOH   A O    1 
HETATM 7038 O O    B HOH   D 3 .   ? 4.981  6.088   1.162   0.54 25.82 ?  512 HOH   A O    1 
HETATM 7039 O O    . HOH   D 3 .   ? 28.948 14.404  0.759   1.00 55.22 ?  513 HOH   A O    1 
HETATM 7040 O O    . HOH   D 3 .   ? 17.195 -6.735  -14.295 1.00 47.12 ?  514 HOH   A O    1 
HETATM 7041 O O    . HOH   D 3 .   ? 21.916 -23.951 4.400   1.00 30.94 ?  515 HOH   A O    1 
HETATM 7042 O O    . HOH   D 3 .   ? 36.445 -6.477  10.189  1.00 54.49 ?  516 HOH   A O    1 
HETATM 7043 O O    B HOH   D 3 .   ? 7.456  6.868   2.138   0.54 39.23 ?  517 HOH   A O    1 
HETATM 7044 O O    B HOH   D 3 .   ? 8.509  0.234   -4.938  0.54 42.29 ?  518 HOH   A O    1 
HETATM 7045 O O    A HOH   D 3 .   ? 14.874 8.791   4.802   0.46 30.40 ?  519 HOH   A O    1 
HETATM 7046 O O    . HOH   D 3 .   ? 24.070 8.957   -7.264  1.00 45.68 ?  520 HOH   A O    1 
HETATM 7047 O O    B HOH   D 3 .   ? 2.985  6.289   2.826   0.54 37.78 ?  521 HOH   A O    1 
HETATM 7048 O O    . HOH   D 3 .   ? 15.773 -12.084 27.368  1.00 48.52 ?  522 HOH   A O    1 
HETATM 7049 O O    . HOH   D 3 .   ? 16.362 -21.172 18.744  1.00 45.36 ?  523 HOH   A O    1 
HETATM 7050 O O    . HOH   D 3 .   ? 14.819 -22.873 19.810  1.00 40.86 ?  524 HOH   A O    1 
HETATM 7051 O O    . HOH   E 3 .   ? 29.762 -22.399 5.531   1.00 24.08 ?  201 HOH   B O    1 
HETATM 7052 O O    . HOH   E 3 .   ? 52.842 -13.576 -20.306 1.00 35.03 ?  202 HOH   B O    1 
HETATM 7053 O O    . HOH   E 3 .   ? 49.264 -22.640 -19.774 1.00 56.37 ?  203 HOH   B O    1 
HETATM 7054 O O    . HOH   E 3 .   ? 41.346 -7.762  5.492   1.00 43.23 ?  204 HOH   B O    1 
HETATM 7055 O O    . HOH   E 3 .   ? 47.298 -7.419  -4.059  1.00 44.67 ?  205 HOH   B O    1 
HETATM 7056 O O    . HOH   E 3 .   ? 41.779 -36.077 -17.104 1.00 34.85 ?  206 HOH   B O    1 
HETATM 7057 O O    . HOH   E 3 .   ? 54.435 -9.437  -8.787  1.00 24.52 ?  207 HOH   B O    1 
HETATM 7058 O O    . HOH   E 3 .   ? 59.179 -18.673 6.865   1.00 40.75 ?  208 HOH   B O    1 
HETATM 7059 O O    . HOH   E 3 .   ? 50.124 -3.338  7.194   1.00 35.75 ?  209 HOH   B O    1 
HETATM 7060 O O    . HOH   E 3 .   ? 48.187 -6.986  15.549  1.00 33.84 ?  210 HOH   B O    1 
HETATM 7061 O O    . HOH   E 3 .   ? 41.524 -39.262 -14.809 1.00 26.51 ?  211 HOH   B O    1 
HETATM 7062 O O    . HOH   E 3 .   ? 56.276 -19.704 7.208   1.00 36.68 ?  212 HOH   B O    1 
HETATM 7063 O O    . HOH   E 3 .   ? 55.547 -16.699 -14.359 1.00 38.38 ?  213 HOH   B O    1 
HETATM 7064 O O    . HOH   E 3 .   ? 38.069 -39.416 -0.086  1.00 41.67 ?  214 HOH   B O    1 
HETATM 7065 O O    . HOH   E 3 .   ? 58.180 -12.874 8.397   1.00 37.24 ?  215 HOH   B O    1 
HETATM 7066 O O    . HOH   E 3 .   ? 37.086 -19.862 -18.050 1.00 37.82 ?  216 HOH   B O    1 
HETATM 7067 O O    . HOH   E 3 .   ? 30.197 -41.053 -8.068  1.00 20.33 ?  217 HOH   B O    1 
HETATM 7068 O O    . HOH   E 3 .   ? 27.914 -42.065 -14.963 1.00 37.79 ?  218 HOH   B O    1 
HETATM 7069 O O    . HOH   E 3 .   ? 45.015 -34.908 6.937   1.00 46.42 ?  219 HOH   B O    1 
HETATM 7070 O O    . HOH   E 3 .   ? 50.666 -6.151  0.235   1.00 31.10 ?  220 HOH   B O    1 
HETATM 7071 O O    . HOH   E 3 .   ? 32.849 -43.862 -11.268 1.00 23.27 ?  221 HOH   B O    1 
HETATM 7072 O O    . HOH   E 3 .   ? 57.703 -24.518 5.092   1.00 40.26 ?  222 HOH   B O    1 
HETATM 7073 O O    . HOH   E 3 .   ? 26.421 -19.299 -1.772  1.00 16.26 ?  223 HOH   B O    1 
HETATM 7074 O O    . HOH   E 3 .   ? 30.641 -42.180 -10.577 1.00 31.02 ?  224 HOH   B O    1 
HETATM 7075 O O    . HOH   E 3 .   ? 36.024 -43.298 -8.270  1.00 40.05 ?  225 HOH   B O    1 
HETATM 7076 O O    . HOH   E 3 .   ? 44.416 -7.242  2.130   1.00 38.41 ?  226 HOH   B O    1 
HETATM 7077 O O    . HOH   E 3 .   ? 34.487 -36.381 -7.145  1.00 23.23 ?  227 HOH   B O    1 
HETATM 7078 O O    . HOH   E 3 .   ? 27.503 -29.219 -1.640  1.00 39.04 ?  228 HOH   B O    1 
HETATM 7079 O O    . HOH   E 3 .   ? 35.012 -8.021  -2.879  1.00 22.45 ?  229 HOH   B O    1 
HETATM 7080 O O    . HOH   E 3 .   ? 28.382 -19.729 -13.147 1.00 29.38 ?  230 HOH   B O    1 
HETATM 7081 O O    . HOH   E 3 .   ? 38.961 -11.819 12.420  1.00 41.86 ?  231 HOH   B O    1 
HETATM 7082 O O    . HOH   E 3 .   ? 50.675 -12.973 -0.517  1.00 14.08 ?  232 HOH   B O    1 
HETATM 7083 O O    . HOH   E 3 .   ? 44.421 -27.697 -0.696  1.00 24.54 ?  233 HOH   B O    1 
HETATM 7084 O O    . HOH   E 3 .   ? 34.164 -18.460 11.398  1.00 27.00 ?  234 HOH   B O    1 
HETATM 7085 O O    . HOH   E 3 .   ? 56.639 -30.779 -7.648  1.00 33.91 ?  235 HOH   B O    1 
HETATM 7086 O O    . HOH   E 3 .   ? 30.753 -28.682 4.324   1.00 29.28 ?  236 HOH   B O    1 
HETATM 7087 O O    . HOH   E 3 .   ? 29.743 -26.249 3.944   1.00 33.17 ?  237 HOH   B O    1 
HETATM 7088 O O    . HOH   E 3 .   ? 57.193 -26.813 -7.530  1.00 48.36 ?  238 HOH   B O    1 
HETATM 7089 O O    . HOH   E 3 .   ? 39.270 -10.858 6.134   1.00 29.08 ?  239 HOH   B O    1 
HETATM 7090 O O    . HOH   E 3 .   ? 51.648 -6.493  4.376   1.00 24.03 ?  240 HOH   B O    1 
HETATM 7091 O O    . HOH   E 3 .   ? 34.743 -24.573 13.922  1.00 32.32 ?  241 HOH   B O    1 
HETATM 7092 O O    . HOH   E 3 .   ? 29.669 -25.246 -10.809 1.00 19.90 ?  242 HOH   B O    1 
HETATM 7093 O O    . HOH   E 3 .   ? 57.550 -24.347 -3.793  1.00 24.10 ?  243 HOH   B O    1 
HETATM 7094 O O    . HOH   E 3 .   ? 42.500 -25.345 2.716   1.00 17.54 ?  244 HOH   B O    1 
HETATM 7095 O O    . HOH   E 3 .   ? 57.434 -16.328 -12.166 1.00 21.38 ?  245 HOH   B O    1 
HETATM 7096 O O    . HOH   E 3 .   ? 43.058 -43.283 -8.087  1.00 31.87 ?  246 HOH   B O    1 
HETATM 7097 O O    . HOH   E 3 .   ? 41.329 -9.557  13.105  1.00 24.89 ?  247 HOH   B O    1 
HETATM 7098 O O    . HOH   E 3 .   ? 41.829 -23.447 9.371   1.00 21.55 ?  248 HOH   B O    1 
HETATM 7099 O O    . HOH   E 3 .   ? 39.384 -11.072 0.379   1.00 20.12 ?  249 HOH   B O    1 
HETATM 7100 O O    . HOH   E 3 .   ? 40.275 -12.780 -11.513 1.00 18.42 ?  250 HOH   B O    1 
HETATM 7101 O O    . HOH   E 3 .   ? 50.931 -39.902 -8.111  1.00 34.30 ?  251 HOH   B O    1 
HETATM 7102 O O    . HOH   E 3 .   ? 49.839 -24.799 5.767   1.00 36.99 ?  252 HOH   B O    1 
HETATM 7103 O O    . HOH   E 3 .   ? 42.597 -22.850 3.897   1.00 14.43 ?  253 HOH   B O    1 
HETATM 7104 O O    . HOH   E 3 .   ? 48.108 -24.515 -17.675 1.00 35.72 ?  254 HOH   B O    1 
HETATM 7105 O O    . HOH   E 3 .   ? 43.175 -32.447 -16.997 1.00 26.62 ?  255 HOH   B O    1 
HETATM 7106 O O    . HOH   E 3 .   ? 30.797 -15.714 2.653   1.00 16.49 ?  256 HOH   B O    1 
HETATM 7107 O O    . HOH   E 3 .   ? 46.347 -1.519  13.324  1.00 34.84 ?  257 HOH   B O    1 
HETATM 7108 O O    . HOH   E 3 .   ? 40.601 -15.923 14.228  1.00 29.89 ?  258 HOH   B O    1 
HETATM 7109 O O    . HOH   E 3 .   ? 44.926 -43.587 -10.336 1.00 30.76 ?  259 HOH   B O    1 
HETATM 7110 O O    . HOH   E 3 .   ? 51.486 -13.825 11.028  1.00 28.69 ?  260 HOH   B O    1 
HETATM 7111 O O    . HOH   E 3 .   ? 38.394 -11.108 -2.220  1.00 21.52 ?  261 HOH   B O    1 
HETATM 7112 O O    . HOH   E 3 .   ? 58.097 -10.626 -4.110  1.00 24.54 ?  262 HOH   B O    1 
HETATM 7113 O O    . HOH   E 3 .   ? 47.927 -22.727 5.872   1.00 21.68 ?  263 HOH   B O    1 
HETATM 7114 O O    . HOH   E 3 .   ? 27.135 -31.912 -9.924  1.00 23.17 ?  264 HOH   B O    1 
HETATM 7115 O O    . HOH   E 3 .   ? 43.272 -15.804 -12.183 1.00 16.82 ?  265 HOH   B O    1 
HETATM 7116 O O    . HOH   E 3 .   ? 34.923 -33.479 -19.051 1.00 34.09 ?  266 HOH   B O    1 
HETATM 7117 O O    . HOH   E 3 .   ? 25.328 -25.894 -1.210  1.00 35.47 ?  267 HOH   B O    1 
HETATM 7118 O O    . HOH   E 3 .   ? 59.756 -15.299 8.117   1.00 38.65 ?  268 HOH   B O    1 
HETATM 7119 O O    . HOH   E 3 .   ? 46.613 -31.214 -4.737  1.00 24.28 ?  269 HOH   B O    1 
HETATM 7120 O O    . HOH   E 3 .   ? 28.267 -34.417 -9.399  1.00 21.72 ?  270 HOH   B O    1 
HETATM 7121 O O    . HOH   E 3 .   ? 49.743 -0.481  10.257  1.00 33.67 ?  271 HOH   B O    1 
HETATM 7122 O O    . HOH   E 3 .   ? 56.140 -23.527 -14.613 1.00 30.03 ?  272 HOH   B O    1 
HETATM 7123 O O    . HOH   E 3 .   ? 48.343 -36.562 -15.489 1.00 54.68 ?  273 HOH   B O    1 
HETATM 7124 O O    . HOH   E 3 .   ? 47.068 -34.004 -4.539  1.00 20.61 ?  274 HOH   B O    1 
HETATM 7125 O O    . HOH   E 3 .   ? 38.331 -9.422  -13.305 1.00 32.99 ?  275 HOH   B O    1 
HETATM 7126 O O    . HOH   E 3 .   ? 57.474 -9.202  1.388   1.00 22.78 ?  276 HOH   B O    1 
HETATM 7127 O O    . HOH   E 3 .   ? 34.366 -12.779 2.621   1.00 23.57 ?  277 HOH   B O    1 
HETATM 7128 O O    . HOH   E 3 .   ? 52.666 -10.339 12.947  1.00 27.50 ?  278 HOH   B O    1 
HETATM 7129 O O    . HOH   E 3 .   ? 42.266 -9.848  9.411   1.00 24.48 ?  279 HOH   B O    1 
HETATM 7130 O O    . HOH   E 3 .   ? 43.498 -15.436 18.235  1.00 35.71 ?  280 HOH   B O    1 
HETATM 7131 O O    . HOH   E 3 .   ? 51.642 -6.045  -8.016  1.00 58.65 ?  281 HOH   B O    1 
HETATM 7132 O O    . HOH   E 3 .   ? 45.943 -40.375 -3.444  1.00 35.27 ?  282 HOH   B O    1 
HETATM 7133 O O    . HOH   E 3 .   ? 42.350 -34.667 3.807   1.00 30.52 ?  283 HOH   B O    1 
HETATM 7134 O O    . HOH   E 3 .   ? 56.928 -8.591  8.413   1.00 22.10 ?  284 HOH   B O    1 
HETATM 7135 O O    . HOH   E 3 .   ? 28.447 -30.961 -14.667 1.00 34.28 ?  285 HOH   B O    1 
HETATM 7136 O O    . HOH   E 3 .   ? 29.605 -34.193 -0.443  1.00 40.07 ?  286 HOH   B O    1 
HETATM 7137 O O    . HOH   E 3 .   ? 33.479 -15.362 -13.977 1.00 24.51 ?  287 HOH   B O    1 
HETATM 7138 O O    . HOH   E 3 .   ? 49.249 -28.688 -6.767  1.00 18.13 ?  288 HOH   B O    1 
HETATM 7139 O O    . HOH   E 3 .   ? 37.306 -35.624 7.243   1.00 38.23 ?  289 HOH   B O    1 
HETATM 7140 O O    . HOH   E 3 .   ? 46.797 -29.559 9.914   1.00 31.68 ?  290 HOH   B O    1 
HETATM 7141 O O    . HOH   E 3 .   ? 42.873 -20.400 -20.810 1.00 39.47 ?  291 HOH   B O    1 
HETATM 7142 O O    . HOH   E 3 .   ? 37.465 -18.050 13.102  1.00 31.79 ?  292 HOH   B O    1 
HETATM 7143 O O    . HOH   E 3 .   ? 48.650 -20.004 5.963   1.00 16.74 ?  293 HOH   B O    1 
HETATM 7144 O O    . HOH   E 3 .   ? 42.926 -43.593 -14.222 1.00 42.01 ?  294 HOH   B O    1 
HETATM 7145 O O    . HOH   E 3 .   ? 41.098 -5.481  11.527  1.00 58.27 ?  295 HOH   B O    1 
HETATM 7146 O O    . HOH   E 3 .   ? 48.360 -25.028 3.191   1.00 16.25 ?  296 HOH   B O    1 
HETATM 7147 O O    . HOH   E 3 .   ? 27.487 -26.689 -15.616 1.00 35.39 ?  297 HOH   B O    1 
HETATM 7148 O O    . HOH   E 3 .   ? 31.743 -17.867 -14.531 1.00 32.96 ?  298 HOH   B O    1 
HETATM 7149 O O    . HOH   E 3 .   ? 27.855 -22.923 -7.969  1.00 20.61 ?  299 HOH   B O    1 
HETATM 7150 O O    . HOH   E 3 .   ? 53.539 -12.687 -22.221 1.00 34.19 ?  300 HOH   B O    1 
HETATM 7151 O O    . HOH   E 3 .   ? 36.675 -12.760 -1.476  1.00 31.40 ?  301 HOH   B O    1 
HETATM 7152 O O    . HOH   E 3 .   ? 45.358 -33.436 -15.871 1.00 25.35 ?  302 HOH   B O    1 
HETATM 7153 O O    . HOH   E 3 .   ? 25.896 -21.435 -3.473  1.00 18.18 ?  303 HOH   B O    1 
HETATM 7154 O O    . HOH   E 3 .   ? 51.228 -37.640 -9.396  1.00 31.45 ?  304 HOH   B O    1 
HETATM 7155 O O    . HOH   E 3 .   ? 52.540 -35.673 -8.392  1.00 31.40 ?  305 HOH   B O    1 
HETATM 7156 O O    . HOH   E 3 .   ? 43.891 -29.335 -4.677  1.00 30.97 ?  306 HOH   B O    1 
HETATM 7157 O O    . HOH   E 3 .   ? 41.148 -24.340 15.834  1.00 50.34 ?  307 HOH   B O    1 
HETATM 7158 O O    . HOH   E 3 .   ? 42.640 -12.297 -18.501 1.00 35.63 ?  308 HOH   B O    1 
HETATM 7159 O O    . HOH   E 3 .   ? 42.229 -9.964  -14.943 1.00 39.33 ?  309 HOH   B O    1 
HETATM 7160 O O    . HOH   E 3 .   ? 62.644 -13.595 4.748   1.00 31.58 ?  310 HOH   B O    1 
HETATM 7161 O O    . HOH   E 3 .   ? 57.592 -22.104 3.183   1.00 32.45 ?  311 HOH   B O    1 
HETATM 7162 O O    . HOH   E 3 .   ? 51.280 -32.921 -10.578 1.00 39.65 ?  312 HOH   B O    1 
HETATM 7163 O O    . HOH   E 3 .   ? 53.510 -30.141 4.547   1.00 20.81 ?  313 HOH   B O    1 
HETATM 7164 O O    . HOH   E 3 .   ? 44.597 -27.422 2.077   1.00 18.76 ?  314 HOH   B O    1 
HETATM 7165 O O    . HOH   E 3 .   ? 44.124 -1.742  7.643   1.00 49.67 ?  315 HOH   B O    1 
HETATM 7166 O O    . HOH   E 3 .   ? 43.124 -21.346 10.705  1.00 19.06 ?  316 HOH   B O    1 
HETATM 7167 O O    . HOH   E 3 .   ? 57.001 -12.062 12.453  1.00 41.94 ?  317 HOH   B O    1 
HETATM 7168 O O    . HOH   E 3 .   ? 44.593 -24.579 9.621   1.00 22.18 ?  318 HOH   B O    1 
HETATM 7169 O O    . HOH   E 3 .   ? 37.788 -10.270 -10.761 1.00 19.36 ?  319 HOH   B O    1 
HETATM 7170 O O    . HOH   E 3 .   ? 32.759 -34.615 -5.819  1.00 19.65 ?  320 HOH   B O    1 
HETATM 7171 O O    . HOH   E 3 .   ? 48.014 -32.721 -16.476 1.00 46.04 ?  321 HOH   B O    1 
HETATM 7172 O O    . HOH   E 3 .   ? 27.706 -14.776 -9.395  1.00 38.49 ?  322 HOH   B O    1 
HETATM 7173 O O    . HOH   E 3 .   ? 34.927 -33.501 4.529   1.00 31.03 ?  323 HOH   B O    1 
HETATM 7174 O O    . HOH   E 3 .   ? 41.653 -8.092  1.371   1.00 27.11 ?  324 HOH   B O    1 
HETATM 7175 O O    . HOH   E 3 .   ? 52.440 -29.234 -13.029 1.00 26.86 ?  325 HOH   B O    1 
HETATM 7176 O O    . HOH   E 3 .   ? 40.176 -10.850 -9.592  1.00 20.20 ?  326 HOH   B O    1 
HETATM 7177 O O    . HOH   E 3 .   ? 37.213 -30.567 -21.015 1.00 37.31 ?  327 HOH   B O    1 
HETATM 7178 O O    . HOH   E 3 .   ? 59.980 -17.205 -10.432 1.00 38.61 ?  328 HOH   B O    1 
HETATM 7179 O O    . HOH   E 3 .   ? 53.192 -16.122 -12.720 1.00 32.52 ?  329 HOH   B O    1 
HETATM 7180 O O    . HOH   E 3 .   ? 26.282 -21.023 -6.194  1.00 19.00 ?  330 HOH   B O    1 
HETATM 7181 O O    . HOH   E 3 .   ? 33.460 -31.095 11.068  1.00 40.26 ?  331 HOH   B O    1 
HETATM 7182 O O    . HOH   E 3 .   ? 38.336 -12.688 7.904   1.00 21.85 ?  332 HOH   B O    1 
HETATM 7183 O O    . HOH   E 3 .   ? 62.875 -20.073 -0.824  1.00 42.06 ?  333 HOH   B O    1 
HETATM 7184 O O    . HOH   E 3 .   ? 36.676 -12.389 4.324   1.00 20.63 ?  334 HOH   B O    1 
HETATM 7185 O O    . HOH   E 3 .   ? 43.128 -34.593 0.168   1.00 23.47 ?  335 HOH   B O    1 
HETATM 7186 O O    . HOH   E 3 .   ? 47.191 -24.476 8.260   1.00 32.69 ?  336 HOH   B O    1 
HETATM 7187 O O    . HOH   E 3 .   ? 39.462 -23.521 -20.261 1.00 38.37 ?  337 HOH   B O    1 
HETATM 7188 O O    . HOH   E 3 .   ? 48.557 -11.958 -13.932 1.00 30.05 ?  338 HOH   B O    1 
HETATM 7189 O O    . HOH   E 3 .   ? 36.893 -15.134 -16.531 1.00 43.93 ?  339 HOH   B O    1 
HETATM 7190 O O    . HOH   E 3 .   ? 47.401 -27.408 2.084   1.00 17.96 ?  340 HOH   B O    1 
HETATM 7191 O O    . HOH   E 3 .   ? 46.813 -19.870 12.290  1.00 33.47 ?  341 HOH   B O    1 
HETATM 7192 O O    . HOH   E 3 .   ? 28.851 -43.078 -12.317 1.00 46.82 ?  342 HOH   B O    1 
HETATM 7193 O O    . HOH   E 3 .   ? 36.990 -45.271 -9.771  1.00 39.01 ?  343 HOH   B O    1 
HETATM 7194 O O    . HOH   E 3 .   ? 45.706 -36.294 -16.047 1.00 37.37 ?  344 HOH   B O    1 
HETATM 7195 O O    . HOH   E 3 .   ? 32.949 -14.670 1.074   1.00 20.90 ?  345 HOH   B O    1 
HETATM 7196 O O    . HOH   E 3 .   ? 33.704 -9.376  -8.803  1.00 35.01 ?  346 HOH   B O    1 
HETATM 7197 O O    . HOH   E 3 .   ? 39.704 -44.387 -11.124 1.00 37.77 ?  347 HOH   B O    1 
HETATM 7198 O O    . HOH   E 3 .   ? 38.537 -12.253 -16.236 1.00 47.64 ?  348 HOH   B O    1 
HETATM 7199 O O    . HOH   E 3 .   ? 38.520 -22.216 15.037  1.00 46.59 ?  349 HOH   B O    1 
HETATM 7200 O O    . HOH   E 3 .   ? 40.366 -43.514 -9.049  1.00 31.34 ?  350 HOH   B O    1 
HETATM 7201 O O    . HOH   E 3 .   ? 62.486 -20.010 -4.767  1.00 53.09 ?  351 HOH   B O    1 
HETATM 7202 O O    . HOH   E 3 .   ? 34.499 -10.252 7.647   1.00 27.42 ?  352 HOH   B O    1 
HETATM 7203 O O    . HOH   E 3 .   ? 36.070 -8.595  -9.630  1.00 37.51 ?  353 HOH   B O    1 
HETATM 7204 O O    . HOH   E 3 .   ? 55.582 -8.272  10.904  1.00 29.39 ?  354 HOH   B O    1 
HETATM 7205 O O    . HOH   E 3 .   ? 27.640 -26.645 -0.502  1.00 34.81 ?  355 HOH   B O    1 
HETATM 7206 O O    . HOH   E 3 .   ? 23.154 -23.567 6.788   1.00 44.71 ?  356 HOH   B O    1 
HETATM 7207 O O    . HOH   E 3 .   ? 56.461 -7.235  3.008   1.00 30.77 ?  357 HOH   B O    1 
HETATM 7208 O O    . HOH   E 3 .   ? 34.065 -7.717  11.438  1.00 45.87 ?  358 HOH   B O    1 
HETATM 7209 O O    . HOH   E 3 .   ? 44.085 -37.333 -17.747 1.00 37.71 ?  359 HOH   B O    1 
HETATM 7210 O O    . HOH   E 3 .   ? 43.092 -12.749 -21.197 1.00 47.10 ?  360 HOH   B O    1 
HETATM 7211 O O    . HOH   E 3 .   ? 61.429 -19.929 1.782   1.00 36.43 ?  361 HOH   B O    1 
HETATM 7212 O O    . HOH   E 3 .   ? 27.070 -25.999 -11.277 1.00 37.95 ?  362 HOH   B O    1 
HETATM 7213 O O    . HOH   E 3 .   ? 56.951 -21.505 -16.294 1.00 42.22 ?  363 HOH   B O    1 
HETATM 7214 O O    . HOH   E 3 .   ? 40.162 -8.817  9.942   1.00 42.66 ?  364 HOH   B O    1 
HETATM 7215 O O    . HOH   E 3 .   ? 48.134 -26.594 8.962   1.00 47.96 ?  365 HOH   B O    1 
HETATM 7216 O O    . HOH   E 3 .   ? 54.281 -5.757  3.005   1.00 39.20 ?  366 HOH   B O    1 
HETATM 7217 O O    . HOH   E 3 .   ? 40.058 -11.363 -13.945 1.00 33.46 ?  367 HOH   B O    1 
HETATM 7218 O O    . HOH   E 3 .   ? 32.578 -23.546 14.178  1.00 45.46 ?  368 HOH   B O    1 
HETATM 7219 O O    . HOH   E 3 .   ? 41.779 -10.098 -17.484 1.00 57.87 ?  369 HOH   B O    1 
HETATM 7220 O O    . HOH   E 3 .   ? 39.862 -6.909  7.815   1.00 48.09 ?  370 HOH   B O    1 
HETATM 7221 O O    . HOH   E 3 .   ? 62.920 -12.437 6.879   1.00 44.19 ?  371 HOH   B O    1 
HETATM 7222 O O    . HOH   E 3 .   ? 56.088 -7.833  -0.618  1.00 35.18 ?  372 HOH   B O    1 
HETATM 7223 O O    . HOH   E 3 .   ? 58.996 -10.324 9.242   1.00 43.79 ?  373 HOH   B O    1 
HETATM 7224 O O    . HOH   E 3 .   ? 36.121 -8.590  8.888   1.00 36.41 ?  374 HOH   B O    1 
HETATM 7225 O O    . HOH   E 3 .   ? 51.982 -12.857 13.341  1.00 32.80 ?  375 HOH   B O    1 
HETATM 7226 O O    . HOH   E 3 .   ? 42.682 -17.323 -23.116 1.00 55.52 ?  376 HOH   B O    1 
HETATM 7227 O O    . HOH   E 3 .   ? 44.092 -5.644  -3.491  1.00 49.02 ?  377 HOH   B O    1 
HETATM 7228 O O    . HOH   E 3 .   ? 37.974 -10.508 9.982   1.00 33.49 ?  378 HOH   B O    1 
HETATM 7229 O O    . HOH   E 3 .   ? 36.452 -22.688 13.347  1.00 28.48 ?  379 HOH   B O    1 
HETATM 7230 O O    . HOH   E 3 .   ? 39.705 -14.015 15.694  1.00 54.99 ?  380 HOH   B O    1 
HETATM 7231 O O    . HOH   E 3 .   ? 52.856 -29.868 7.186   1.00 25.43 ?  381 HOH   B O    1 
HETATM 7232 O O    . HOH   E 3 .   ? 40.210 -7.607  3.200   1.00 41.62 ?  382 HOH   B O    1 
HETATM 7233 O O    . HOH   E 3 .   ? 41.766 -6.636  -4.796  1.00 51.80 ?  383 HOH   B O    1 
HETATM 7234 O O    . HOH   E 3 .   ? 60.377 -22.243 2.842   1.00 43.02 ?  384 HOH   B O    1 
HETATM 7235 O O    . HOH   E 3 .   ? 35.275 -20.296 13.260  1.00 36.94 ?  385 HOH   B O    1 
HETATM 7236 O O    . HOH   E 3 .   ? 40.878 -9.748  15.755  1.00 57.12 ?  386 HOH   B O    1 
HETATM 7237 O O    . HOH   E 3 .   ? 46.759 -5.354  2.906   1.00 42.19 ?  387 HOH   B O    1 
HETATM 7238 O O    . HOH   E 3 .   ? 35.341 -33.689 7.381   1.00 43.49 ?  388 HOH   B O    1 
HETATM 7239 O O    . HOH   E 3 .   ? 23.880 -20.896 -7.624  1.00 30.60 ?  389 HOH   B O    1 
HETATM 7240 O O    . HOH   E 3 .   ? 40.739 -6.571  -0.925  1.00 27.92 ?  390 HOH   B O    1 
HETATM 7241 O O    . HOH   E 3 .   ? 44.052 -31.707 -3.725  1.00 38.11 ?  391 HOH   B O    1 
HETATM 7242 O O    . HOH   E 3 .   ? 26.638 -28.044 -13.546 1.00 37.26 ?  392 HOH   B O    1 
HETATM 7243 O O    . HOH   E 3 .   ? 27.719 -27.013 2.220   1.00 33.78 ?  393 HOH   B O    1 
HETATM 7244 O O    . HOH   E 3 .   ? 24.590 -20.632 -10.446 1.00 40.95 ?  394 HOH   B O    1 
HETATM 7245 O O    . HOH   E 3 .   ? 34.246 -33.416 9.658   1.00 39.05 ?  395 HOH   B O    1 
HETATM 7246 O O    . HOH   E 3 .   ? 50.625 -30.782 8.703   1.00 30.14 ?  396 HOH   B O    1 
HETATM 7247 O O    . HOH   E 3 .   ? 26.802 -30.711 -12.522 1.00 31.09 ?  397 HOH   B O    1 
HETATM 7248 O O    . HOH   E 3 .   ? 45.638 -20.187 15.318  1.00 66.36 ?  398 HOH   B O    1 
HETATM 7249 O O    . HOH   E 3 .   ? 57.638 -6.543  -2.330  1.00 39.14 ?  399 HOH   B O    1 
HETATM 7250 O O    . HOH   E 3 .   ? 40.887 -11.845 -22.328 1.00 47.35 ?  400 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   ? 0.8420 0.8569 0.9100 -0.0054 -0.0204 0.0690  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.8432 0.8582 0.9164 -0.0058 -0.0203 0.0720  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.8382 0.8535 0.9022 -0.0067 -0.0207 0.0711  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.8393 0.8546 0.9075 -0.0071 -0.0207 0.0741  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.8182 0.8398 0.8740 -0.0138 -0.0223 0.0782  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.8190 0.8407 0.8778 -0.0140 -0.0223 0.0800  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.8219 0.8439 0.8864 -0.0121 -0.0236 0.0787  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.8232 0.8453 0.8917 -0.0125 -0.0236 0.0807  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.8510 0.8614 0.9142 -0.0027 -0.0193 0.0676  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.8523 0.8625 0.9195 -0.0033 -0.0197 0.0716  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.8556 0.8637 0.9176 -0.0012 -0.0191 0.0669  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.8569 0.8648 0.9229 -0.0019 -0.0194 0.0713  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.8549 0.8635 0.9181 -0.0016 -0.0192 0.0666  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.8562 0.8646 0.9232 -0.0024 -0.0195 0.0710  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.7908 0.8191 0.8204 -0.0238 -0.0225 0.0846  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.7322 0.7737 0.7021 -0.0454 -0.0237 0.0928  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.6537 0.7234 0.6196 -0.0696 -0.0158 0.0613  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.6570 0.7234 0.6136 -0.0691 -0.0204 0.0679  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.7479 0.7772 0.6562 -0.0450 -0.0320 0.1329  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.7590 0.7788 0.6095 -0.0470 -0.0422 0.1715  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.7655 0.7792 0.5847 -0.0487 -0.0478 0.1868  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.7612 0.7797 0.5997 -0.0467 -0.0447 0.1873  4   ASN   A ND2 
46   N N   A SER   A 5   ? 0.6110 0.6955 0.5784 -0.0846 -0.0080 0.0427  5   SER   A N   
47   N N   B SER   A 5   ? 0.6104 0.6955 0.5744 -0.0856 -0.0098 0.0428  5   SER   A N   
48   C CA  A SER   A 5   ? 0.5666 0.6679 0.5392 -0.0993 0.0029  0.0263  5   SER   A CA  
49   C CA  B SER   A 5   ? 0.5656 0.6680 0.5328 -0.1007 -0.0002 0.0264  5   SER   A CA  
50   C C   A SER   A 5   ? 0.5154 0.6315 0.4798 -0.1131 0.0174  0.0182  5   SER   A C   
51   C C   B SER   A 5   ? 0.5148 0.6315 0.4753 -0.1139 0.0162  0.0180  5   SER   A C   
52   O O   A SER   A 5   ? 0.5158 0.6317 0.4702 -0.1113 0.0157  0.0118  5   SER   A O   
53   O O   B SER   A 5   ? 0.5150 0.6315 0.4624 -0.1119 0.0152  0.0117  5   SER   A O   
54   C CB  A SER   A 5   ? 0.5729 0.6744 0.5589 -0.1007 -0.0004 0.0195  5   SER   A CB  
55   C CB  B SER   A 5   ? 0.5714 0.6749 0.5498 -0.1029 -0.0071 0.0189  5   SER   A CB  
56   O OG  A SER   A 5   ? 0.5762 0.6776 0.5708 -0.1030 -0.0030 0.0162  5   SER   A OG  
57   O OG  B SER   A 5   ? 0.5740 0.6781 0.5588 -0.1059 -0.0129 0.0149  5   SER   A OG  
68   N N   . PHE   A 6   ? 0.4645 0.5951 0.4213 -0.1278 0.0340  0.0227  6   PHE   A N   
69   C CA  . PHE   A 6   ? 0.3765 0.5184 0.3272 -0.1485 0.0573  0.0405  6   PHE   A CA  
70   C C   . PHE   A 6   ? 0.3460 0.4921 0.3277 -0.1610 0.0737  0.0371  6   PHE   A C   
71   O O   . PHE   A 6   ? 0.3555 0.5068 0.3811 -0.1530 0.0563  0.0580  6   PHE   A O   
72   C CB  . PHE   A 6   ? 0.3386 0.4725 0.2741 -0.1426 0.0341  0.0553  6   PHE   A CB  
73   C CG  . PHE   A 6   ? 0.3060 0.4260 0.2403 -0.1406 0.0086  0.0441  6   PHE   A CG  
74   C CD1 . PHE   A 6   ? 0.2930 0.4100 0.2448 -0.1288 -0.0039 0.0327  6   PHE   A CD1 
75   C CD2 . PHE   A 6   ? 0.3131 0.4080 0.2663 -0.1287 0.0036  0.0450  6   PHE   A CD2 
76   C CE1 . PHE   A 6   ? 0.2877 0.3931 0.2426 -0.1280 0.0045  0.0370  6   PHE   A CE1 
77   C CE2 . PHE   A 6   ? 0.3093 0.3965 0.2726 -0.1207 0.0025  0.0417  6   PHE   A CE2 
78   C CZ  . PHE   A 6   ? 0.2992 0.3869 0.2512 -0.1263 -0.0167 0.0354  6   PHE   A CZ  
89   N N   A SER   A 7   ? 0.3197 0.4719 0.3003 -0.1562 0.0891  0.0276  7   SER   A N   
90   N N   B SER   A 7   ? 0.3316 0.4738 0.3055 -0.1627 0.0773  0.0156  7   SER   A N   
91   C CA  A SER   A 7   ? 0.3098 0.4610 0.3071 -0.1308 0.0892  0.0120  7   SER   A CA  
92   C CA  B SER   A 7   ? 0.3363 0.4660 0.3249 -0.1412 0.0668  -0.0057 7   SER   A CA  
93   C C   A SER   A 7   ? 0.2885 0.4377 0.2767 -0.1165 0.0827  0.0148  7   SER   A C   
94   C C   B SER   A 7   ? 0.3129 0.4449 0.2969 -0.1355 0.0771  -0.0033 7   SER   A C   
95   O O   A SER   A 7   ? 0.3026 0.4390 0.2528 -0.1106 0.0635  0.0105  7   SER   A O   
96   O O   B SER   A 7   ? 0.3119 0.4459 0.2789 -0.1410 0.0779  -0.0051 7   SER   A O   
97   C CB  A SER   A 7   ? 0.3183 0.4704 0.3182 -0.1185 0.1110  0.0102  7   SER   A CB  
98   C CB  B SER   A 7   ? 0.3541 0.4745 0.3459 -0.1332 0.0602  -0.0176 7   SER   A CB  
99   O OG  A SER   A 7   ? 0.3346 0.4746 0.3323 -0.1130 0.1130  0.0110  7   SER   A OG  
100  O OG  B SER   A 7   ? 0.3731 0.4778 0.3665 -0.1294 0.0459  -0.0179 7   SER   A OG  
111  N N   A GLY   A 8   ? 0.2637 0.4195 0.2709 -0.1001 0.0778  0.0091  8   GLY   A N   
112  N N   B GLY   A 8   ? 0.2989 0.4310 0.3025 -0.1154 0.0723  -0.0119 8   GLY   A N   
113  C CA  A GLY   A 8   ? 0.2427 0.3968 0.2700 -0.0772 0.0878  0.0112  8   GLY   A CA  
114  C CA  B GLY   A 8   ? 0.2867 0.4118 0.3050 -0.0882 0.0671  -0.0047 8   GLY   A CA  
115  C C   A GLY   A 8   ? 0.2197 0.3695 0.2610 -0.0574 0.0742  0.0027  8   GLY   A C   
116  C C   B GLY   A 8   ? 0.2650 0.3902 0.2902 -0.0680 0.0537  -0.0034 8   GLY   A C   
117  O O   A GLY   A 8   ? 0.2058 0.3765 0.2592 -0.0448 0.0722  -0.0070 8   GLY   A O   
118  O O   B GLY   A 8   ? 0.2598 0.3956 0.2910 -0.0584 0.0518  -0.0056 8   GLY   A O   
125  N N   A TYR   A 9   ? 0.1966 0.3348 0.2585 -0.0530 0.0734  0.0142  9   TYR   A N   
126  N N   B TYR   A 9   ? 0.2376 0.3623 0.2771 -0.0584 0.0461  0.0130  9   TYR   A N   
127  C CA  A TYR   A 9   ? 0.1881 0.2979 0.2536 -0.0476 0.0514  0.0269  9   TYR   A CA  
128  C CA  B TYR   A 9   ? 0.2180 0.3311 0.2633 -0.0491 0.0323  0.0335  9   TYR   A CA  
129  C C   A TYR   A 9   ? 0.1932 0.2738 0.2432 -0.0427 0.0408  0.0403  9   TYR   A C   
130  C C   B TYR   A 9   ? 0.2102 0.3104 0.2585 -0.0443 0.0312  0.0318  9   TYR   A C   
131  O O   A TYR   A 9   ? 0.1929 0.2977 0.2423 -0.0342 0.0404  0.0376  9   TYR   A O   
132  O O   B TYR   A 9   ? 0.2035 0.3235 0.2808 -0.0496 0.0114  0.0165  9   TYR   A O   
133  C CB  A TYR   A 9   ? 0.1775 0.2894 0.2594 -0.0373 0.0418  0.0165  9   TYR   A CB  
134  C CB  B TYR   A 9   ? 0.2019 0.3244 0.2423 -0.0462 0.0120  0.0480  9   TYR   A CB  
135  C CG  A TYR   A 9   ? 0.1796 0.2728 0.2555 -0.0239 0.0445  0.0134  9   TYR   A CG  
136  C CG  B TYR   A 9   ? 0.2082 0.3245 0.2239 -0.0426 0.0213  0.0564  9   TYR   A CG  
137  C CD1 A TYR   A 9   ? 0.1799 0.2698 0.2628 -0.0171 0.0381  0.0048  9   TYR   A CD1 
138  C CD1 B TYR   A 9   ? 0.2176 0.3285 0.2315 -0.0357 0.0212  0.0586  9   TYR   A CD1 
139  C CD2 A TYR   A 9   ? 0.1670 0.2641 0.2617 -0.0199 0.0401  0.0205  9   TYR   A CD2 
140  C CD2 B TYR   A 9   ? 0.2021 0.3219 0.2043 -0.0304 0.0149  0.0680  9   TYR   A CD2 
141  C CE1 A TYR   A 9   ? 0.1785 0.2595 0.2813 -0.0125 0.0276  0.0074  9   TYR   A CE1 
142  C CE1 B TYR   A 9   ? 0.2158 0.3256 0.2185 -0.0287 0.0259  0.0603  9   TYR   A CE1 
143  C CE2 A TYR   A 9   ? 0.1656 0.2547 0.2776 -0.0139 0.0404  0.0119  9   TYR   A CE2 
144  C CE2 B TYR   A 9   ? 0.2011 0.3185 0.2236 -0.0294 0.0176  0.0617  9   TYR   A CE2 
145  C CZ  A TYR   A 9   ? 0.1736 0.2480 0.2962 -0.0139 0.0375  0.0179  9   TYR   A CZ  
146  C CZ  B TYR   A 9   ? 0.2033 0.3251 0.2227 -0.0284 0.0304  0.0556  9   TYR   A CZ  
147  O OH  A TYR   A 9   ? 0.1950 0.2396 0.3286 -0.0131 0.0449  0.0254  9   TYR   A OH  
148  O OH  B TYR   A 9   ? 0.1844 0.3235 0.2107 -0.0377 0.0341  0.0453  9   TYR   A OH  
167  N N   A LEU   A 10  ? 0.1926 0.2369 0.2379 -0.0402 0.0270  0.0305  10  LEU   A N   
168  N N   B LEU   A 10  ? 0.1984 0.2790 0.2282 -0.0398 0.0377  0.0243  10  LEU   A N   
169  C CA  A LEU   A 10  ? 0.1815 0.2142 0.2316 -0.0315 0.0134  0.0356  10  LEU   A CA  
170  C CA  B LEU   A 10  ? 0.2197 0.2587 0.2199 -0.0265 0.0340  0.0263  10  LEU   A CA  
171  C C   A LEU   A 10  ? 0.1543 0.1941 0.2228 -0.0285 0.0130  0.0392  10  LEU   A C   
172  C C   B LEU   A 10  ? 0.2212 0.2391 0.2321 -0.0411 0.0273  0.0101  10  LEU   A C   
173  O O   A LEU   A 10  ? 0.1481 0.1798 0.1937 -0.0263 0.0312  0.0452  10  LEU   A O   
174  O O   B LEU   A 10  ? 0.2232 0.2359 0.2298 -0.0441 0.0297  0.0029  10  LEU   A O   
175  C CB  A LEU   A 10  ? 0.1894 0.2132 0.2384 -0.0303 0.0019  0.0505  10  LEU   A CB  
176  C CB  B LEU   A 10  ? 0.2309 0.2556 0.2187 -0.0240 0.0389  0.0166  10  LEU   A CB  
177  C CG  A LEU   A 10  ? 0.1969 0.2221 0.2953 -0.0142 -0.0325 0.0518  10  LEU   A CG  
178  C CG  B LEU   A 10  ? 0.2409 0.2530 0.2301 -0.0184 0.0369  -0.0034 10  LEU   A CG  
179  C CD1 A LEU   A 10  ? 0.2174 0.2276 0.3260 -0.0134 -0.0285 0.0556  10  LEU   A CD1 
180  C CD1 B LEU   A 10  ? 0.2369 0.2486 0.2052 -0.0198 0.0321  -0.0036 10  LEU   A CD1 
181  C CD2 A LEU   A 10  ? 0.2187 0.2380 0.3227 -0.0190 -0.0094 0.0348  10  LEU   A CD2 
182  C CD2 B LEU   A 10  ? 0.2246 0.2460 0.2419 -0.0054 0.0108  -0.0233 10  LEU   A CD2 
205  N N   A LYS   A 11  ? 0.1496 0.1877 0.2149 -0.0215 0.0060  0.0474  11  LYS   A N   
206  N N   B LYS   A 11  ? 0.2251 0.2319 0.2431 -0.0379 0.0210  0.0098  11  LYS   A N   
207  C CA  A LYS   A 11  ? 0.1541 0.1778 0.2277 -0.0156 0.0046  0.0450  11  LYS   A CA  
208  C CA  B LYS   A 11  ? 0.2188 0.2265 0.2039 -0.0406 0.0482  0.0167  11  LYS   A CA  
209  C C   A LYS   A 11  ? 0.1601 0.1804 0.2169 -0.0238 0.0072  0.0320  11  LYS   A C   
210  C C   B LYS   A 11  ? 0.2206 0.2274 0.2089 -0.0538 0.0471  0.0290  11  LYS   A C   
211  O O   A LYS   A 11  ? 0.1542 0.1947 0.2530 -0.0484 0.0080  0.0240  11  LYS   A O   
212  O O   B LYS   A 11  ? 0.2313 0.2168 0.2215 -0.0616 0.0346  0.0313  11  LYS   A O   
213  C CB  A LYS   A 11  ? 0.1388 0.1622 0.2093 -0.0177 0.0083  0.0510  11  LYS   A CB  
214  C CB  B LYS   A 11  ? 0.2367 0.2263 0.2115 -0.0271 0.0164  -0.0021 11  LYS   A CB  
215  C CG  A LYS   A 11  ? 0.1569 0.1639 0.2099 -0.0112 0.0072  0.0337  11  LYS   A CG  
216  C CG  B LYS   A 11  ? 0.2362 0.2234 0.2000 -0.0243 0.0075  0.0048  11  LYS   A CG  
217  C CD  A LYS   A 11  ? 0.1670 0.1750 0.2159 -0.0170 0.0067  0.0285  11  LYS   A CD  
218  C CD  B LYS   A 11  ? 0.2462 0.2238 0.1941 -0.0098 0.0042  0.0052  11  LYS   A CD  
219  C CE  A LYS   A 11  ? 0.1724 0.1817 0.2290 -0.0181 0.0073  0.0151  11  LYS   A CE  
220  C CE  B LYS   A 11  ? 0.2566 0.2341 0.2126 -0.0044 0.0050  0.0070  11  LYS   A CE  
221  N NZ  A LYS   A 11  ? 0.1656 0.1637 0.2033 -0.0157 0.0022  0.0217  11  LYS   A NZ  
222  N NZ  B LYS   A 11  ? 0.2665 0.2367 0.2218 -0.0089 0.0017  0.0041  11  LYS   A NZ  
249  N N   A LEU   A 12  ? 0.1497 0.1752 0.1832 -0.0206 0.0032  0.0255  12  LEU   A N   
250  N N   B LEU   A 12  ? 0.2182 0.2431 0.2159 -0.0495 0.0210  0.0366  12  LEU   A N   
251  C CA  A LEU   A 12  ? 0.1532 0.1800 0.1826 -0.0219 0.0075  0.0365  12  LEU   A CA  
252  C CA  B LEU   A 12  ? 0.2335 0.2514 0.1982 -0.0458 0.0089  0.0305  12  LEU   A CA  
253  C C   A LEU   A 12  ? 0.1560 0.1582 0.2007 -0.0453 0.0280  0.0370  12  LEU   A C   
254  C C   B LEU   A 12  ? 0.2445 0.2445 0.2010 -0.0523 0.0115  -0.0003 12  LEU   A C   
255  O O   A LEU   A 12  ? 0.1587 0.1503 0.2424 -0.0325 0.0144  0.0366  12  LEU   A O   
256  O O   B LEU   A 12  ? 0.2627 0.2476 0.2078 -0.0494 0.0167  -0.0200 12  LEU   A O   
257  C CB  A LEU   A 12  ? 0.1673 0.1824 0.1746 -0.0079 0.0004  0.0380  12  LEU   A CB  
258  C CB  B LEU   A 12  ? 0.2371 0.2707 0.2228 -0.0488 -0.0114 0.0319  12  LEU   A CB  
259  C CG  A LEU   A 12  ? 0.1667 0.1872 0.1828 -0.0031 0.0112  0.0319  12  LEU   A CG  
260  C CG  B LEU   A 12  ? 0.2250 0.2772 0.2566 -0.0538 -0.0058 0.0351  12  LEU   A CG  
261  C CD1 A LEU   A 12  ? 0.1736 0.1903 0.1752 0.0011  0.0322  0.0398  12  LEU   A CD1 
262  C CD1 B LEU   A 12  ? 0.2274 0.2780 0.2791 -0.0484 0.0009  0.0368  12  LEU   A CD1 
263  C CD2 A LEU   A 12  ? 0.1784 0.1967 0.2164 -0.0059 -0.0013 0.0305  12  LEU   A CD2 
264  C CD2 B LEU   A 12  ? 0.2299 0.2795 0.2876 -0.0540 -0.0124 0.0304  12  LEU   A CD2 
287  N N   A THR   A 13  ? 0.1643 0.1523 0.2102 -0.0458 -0.0011 0.0146  13  THR   A N   
288  N N   B THR   A 13  ? 0.2506 0.2453 0.2146 -0.0427 0.0128  -0.0032 13  THR   A N   
289  C CA  A THR   A 13  ? 0.1586 0.1742 0.2192 -0.0298 0.0085  0.0111  13  THR   A CA  
290  C CA  B THR   A 13  ? 0.2526 0.2386 0.2186 -0.0670 0.0223  0.0187  13  THR   A CA  
291  C C   A THR   A 13  ? 0.1564 0.1750 0.2313 -0.0296 0.0058  0.0219  13  THR   A C   
292  C C   B THR   A 13  ? 0.2542 0.2385 0.2151 -0.0618 0.0392  0.0186  13  THR   A C   
293  O O   A THR   A 13  ? 0.1455 0.1693 0.2352 -0.0212 -0.0099 0.0113  13  THR   A O   
294  O O   B THR   A 13  ? 0.2589 0.2466 0.2175 -0.0501 0.0396  0.0342  13  THR   A O   
295  C CB  A THR   A 13  ? 0.1690 0.1941 0.2442 -0.0163 0.0027  0.0113  13  THR   A CB  
296  C CB  B THR   A 13  ? 0.2498 0.2386 0.1959 -0.0621 0.0160  0.0088  13  THR   A CB  
297  O OG1 A THR   A 13  ? 0.1665 0.1908 0.2542 -0.0088 0.0078  0.0190  13  THR   A OG1 
298  O OG1 B THR   A 13  ? 0.2408 0.2427 0.2371 -0.0708 0.0224  0.0175  13  THR   A OG1 
299  C CG2 A THR   A 13  ? 0.1727 0.1918 0.2620 -0.0113 -0.0064 -0.0028 13  THR   A CG2 
300  C CG2 B THR   A 13  ? 0.2476 0.2483 0.1747 -0.0660 0.0146  0.0017  13  THR   A CG2 
315  N N   A ASP   A 14  ? 0.1582 0.1801 0.2370 -0.0213 0.0199  0.0344  14  ASP   A N   
316  N N   B ASP   A 14  ? 0.2616 0.2375 0.2266 -0.0659 0.0349  0.0151  14  ASP   A N   
317  C CA  A ASP   A 14  ? 0.1664 0.1986 0.2546 -0.0192 0.0140  0.0414  14  ASP   A CA  
318  C CA  B ASP   A 14  ? 0.2768 0.2434 0.2564 -0.0515 0.0202  0.0496  14  ASP   A CA  
319  C C   A ASP   A 14  ? 0.1606 0.1751 0.2413 -0.0194 0.0113  0.0435  14  ASP   A C   
320  C C   B ASP   A 14  ? 0.2596 0.2198 0.2417 -0.0493 -0.0005 0.0408  14  ASP   A C   
321  O O   A ASP   A 14  ? 0.1620 0.1725 0.2367 -0.0116 0.0123  0.0541  14  ASP   A O   
322  O O   B ASP   A 14  ? 0.2704 0.2217 0.2718 -0.0577 -0.0004 0.0301  14  ASP   A O   
323  C CB  A ASP   A 14  ? 0.1830 0.2433 0.2976 -0.0135 0.0108  0.0573  14  ASP   A CB  
324  C CB  B ASP   A 14  ? 0.3080 0.2747 0.3150 -0.0431 0.0035  0.0628  14  ASP   A CB  
325  C CG  A ASP   A 14  ? 0.1928 0.2825 0.3375 -0.0101 0.0004  0.0617  14  ASP   A CG  
326  C CG  B ASP   A 14  ? 0.3325 0.3192 0.3755 -0.0317 0.0026  0.0682  14  ASP   A CG  
327  O OD1 A ASP   A 14  ? 0.1927 0.2883 0.3530 0.0080  -0.0306 0.0790  14  ASP   A OD1 
328  O OD1 B ASP   A 14  ? 0.3571 0.3369 0.3951 -0.0057 -0.0078 0.0810  14  ASP   A OD1 
329  O OD2 A ASP   A 14  ? 0.2051 0.3108 0.3528 -0.0103 -0.0077 0.0402  14  ASP   A OD2 
330  O OD2 B ASP   A 14  ? 0.3350 0.3396 0.4008 -0.0501 0.0111  0.0682  14  ASP   A OD2 
339  N N   A ASN   A 15  ? 0.1586 0.1694 0.2402 -0.0272 0.0080  0.0231  15  ASN   A N   
340  N N   B ASN   A 15  ? 0.2313 0.2006 0.2219 -0.0352 0.0077  0.0429  15  ASN   A N   
341  C CA  A ASN   A 15  ? 0.1547 0.1717 0.2259 -0.0119 -0.0055 0.0181  15  ASN   A CA  
342  C CA  B ASN   A 15  ? 0.2272 0.1986 0.2219 -0.0234 0.0180  0.0418  15  ASN   A CA  
343  C C   A ASN   A 15  ? 0.1662 0.1719 0.2325 -0.0069 -0.0071 0.0030  15  ASN   A C   
344  C C   B ASN   A 15  ? 0.2147 0.1928 0.2144 -0.0151 0.0202  0.0320  15  ASN   A C   
345  O O   A ASN   A 15  ? 0.1674 0.1697 0.2699 -0.0033 -0.0137 -0.0096 15  ASN   A O   
346  O O   B ASN   A 15  ? 0.2047 0.2002 0.2237 -0.0079 0.0125  0.0180  15  ASN   A O   
347  C CB  A ASN   A 15  ? 0.1490 0.1794 0.2068 -0.0025 -0.0154 0.0065  15  ASN   A CB  
348  C CB  B ASN   A 15  ? 0.2326 0.2052 0.2280 -0.0228 0.0239  0.0417  15  ASN   A CB  
349  C CG  A ASN   A 15  ? 0.1553 0.1814 0.2301 -0.0189 -0.0026 -0.0155 15  ASN   A CG  
350  C CG  B ASN   A 15  ? 0.2305 0.2115 0.2469 -0.0274 0.0300  0.0238  15  ASN   A CG  
351  O OD1 A ASN   A 15  ? 0.1611 0.1868 0.2661 -0.0245 0.0061  -0.0162 15  ASN   A OD1 
352  O OD1 B ASN   A 15  ? 0.2258 0.2096 0.2414 -0.0389 0.0519  0.0202  15  ASN   A OD1 
353  N ND2 A ASN   A 15  ? 0.1589 0.1867 0.2163 -0.0311 0.0030  -0.0121 15  ASN   A ND2 
354  N ND2 B ASN   A 15  ? 0.2291 0.2167 0.2464 -0.0246 0.0292  0.0238  15  ASN   A ND2 
367  N N   A VAL   A 16  ? 0.1685 0.1627 0.2134 -0.0049 0.0023  0.0046  16  VAL   A N   
368  N N   B VAL   A 16  ? 0.2133 0.1864 0.2157 -0.0184 0.0095  0.0256  16  VAL   A N   
369  C CA  A VAL   A 16  ? 0.1692 0.1577 0.2211 -0.0081 0.0089  0.0154  16  VAL   A CA  
370  C CA  B VAL   A 16  ? 0.2169 0.1897 0.2074 -0.0087 0.0143  0.0282  16  VAL   A CA  
371  C C   A VAL   A 16  ? 0.1665 0.1522 0.2046 -0.0235 0.0169  0.0152  16  VAL   A C   
372  C C   B VAL   A 16  ? 0.2158 0.1938 0.2146 -0.0195 0.0098  0.0243  16  VAL   A C   
373  O O   A VAL   A 16  ? 0.1477 0.1519 0.2064 -0.0139 0.0131  0.0103  16  VAL   A O   
374  O O   B VAL   A 16  ? 0.2183 0.1899 0.2243 -0.0429 0.0200  0.0303  16  VAL   A O   
375  C CB  A VAL   A 16  ? 0.1777 0.1546 0.2439 0.0109  0.0223  0.0226  16  VAL   A CB  
376  C CB  B VAL   A 16  ? 0.2269 0.1930 0.1970 0.0077  0.0065  0.0418  16  VAL   A CB  
377  C CG1 A VAL   A 16  ? 0.1915 0.1537 0.2433 0.0052  0.0207  0.0305  16  VAL   A CG1 
378  C CG1 B VAL   A 16  ? 0.2371 0.1949 0.1997 0.0197  0.0237  0.0431  16  VAL   A CG1 
379  C CG2 A VAL   A 16  ? 0.1811 0.1574 0.2681 0.0124  0.0474  0.0162  16  VAL   A CG2 
380  C CG2 B VAL   A 16  ? 0.2255 0.2027 0.2214 -0.0009 0.0105  0.0223  16  VAL   A CG2 
399  N N   A TYR   A 17  ? 0.1658 0.1526 0.1850 -0.0319 0.0389  0.0192  17  TYR   A N   
400  N N   B TYR   A 17  ? 0.2256 0.1926 0.2101 -0.0122 0.0043  0.0276  17  TYR   A N   
401  C CA  A TYR   A 17  ? 0.1623 0.1687 0.1737 -0.0228 0.0269  0.0353  17  TYR   A CA  
402  C CA  B TYR   A 17  ? 0.2327 0.1930 0.2151 -0.0137 -0.0006 0.0138  17  TYR   A CA  
403  C C   A TYR   A 17  ? 0.1660 0.1724 0.2042 -0.0129 0.0303  0.0245  17  TYR   A C   
404  C C   B TYR   A 17  ? 0.1988 0.1974 0.1985 -0.0197 0.0161  0.0110  17  TYR   A C   
405  O O   A TYR   A 17  ? 0.1670 0.1716 0.1963 -0.0135 0.0449  0.0281  17  TYR   A O   
406  O O   B TYR   A 17  ? 0.1800 0.1941 0.2211 -0.0277 0.0231  0.0235  17  TYR   A O   
407  C CB  A TYR   A 17  ? 0.1685 0.1640 0.1653 -0.0189 0.0123  0.0391  17  TYR   A CB  
408  C CB  B TYR   A 17  ? 0.2731 0.1860 0.2396 -0.0060 -0.0056 0.0223  17  TYR   A CB  
409  C CG  A TYR   A 17  ? 0.1801 0.1610 0.1569 -0.0317 -0.0003 0.0286  17  TYR   A CG  
410  C CG  B TYR   A 17  ? 0.2964 0.1999 0.2667 0.0018  -0.0097 0.0355  17  TYR   A CG  
411  C CD1 A TYR   A 17  ? 0.1900 0.1796 0.1813 -0.0270 -0.0037 0.0269  17  TYR   A CD1 
412  C CD1 B TYR   A 17  ? 0.3032 0.2197 0.2750 0.0082  -0.0071 0.0427  17  TYR   A CD1 
413  C CD2 A TYR   A 17  ? 0.1931 0.1731 0.1585 -0.0264 -0.0110 0.0420  17  TYR   A CD2 
414  C CD2 B TYR   A 17  ? 0.3089 0.1961 0.2609 -0.0075 -0.0136 0.0302  17  TYR   A CD2 
415  C CE1 A TYR   A 17  ? 0.2030 0.1829 0.1693 -0.0263 -0.0151 0.0378  17  TYR   A CE1 
416  C CE1 B TYR   A 17  ? 0.3143 0.2245 0.2625 -0.0034 -0.0090 0.0312  17  TYR   A CE1 
417  C CE2 A TYR   A 17  ? 0.2140 0.1810 0.1738 -0.0266 -0.0164 0.0383  17  TYR   A CE2 
418  C CE2 B TYR   A 17  ? 0.3129 0.1988 0.2474 -0.0116 -0.0168 0.0139  17  TYR   A CE2 
419  C CZ  A TYR   A 17  ? 0.2242 0.1783 0.1666 -0.0288 -0.0224 0.0395  17  TYR   A CZ  
420  C CZ  B TYR   A 17  ? 0.3194 0.2162 0.2399 -0.0132 -0.0199 0.0294  17  TYR   A CZ  
421  O OH  A TYR   A 17  ? 0.2525 0.1848 0.1583 -0.0252 -0.0092 0.0204  17  TYR   A OH  
422  O OH  B TYR   A 17  ? 0.3305 0.2297 0.2295 -0.0205 -0.0252 0.0299  17  TYR   A OH  
441  N N   A ILE   A 18  ? 0.1740 0.1670 0.2305 -0.0205 0.0420  0.0306  18  ILE   A N   
442  N N   B ILE   A 18  ? 0.1839 0.2010 0.1620 -0.0271 0.0273  0.0090  18  ILE   A N   
443  C CA  A ILE   A 18  ? 0.1838 0.1772 0.2217 -0.0183 0.0471  0.0128  18  ILE   A CA  
444  C CA  B ILE   A 18  ? 0.1861 0.2104 0.1668 -0.0258 0.0102  0.0140  18  ILE   A CA  
445  C C   A ILE   A 18  ? 0.1886 0.1775 0.2443 -0.0138 0.0562  0.0149  18  ILE   A C   
446  C C   B ILE   A 18  ? 0.1863 0.2153 0.1884 -0.0214 0.0165  0.0142  18  ILE   A C   
447  O O   A ILE   A 18  ? 0.1887 0.1758 0.2416 -0.0163 0.0681  0.0214  18  ILE   A O   
448  O O   B ILE   A 18  ? 0.1862 0.2135 0.2160 -0.0209 0.0282  0.0108  18  ILE   A O   
449  C CB  A ILE   A 18  ? 0.1783 0.1901 0.1955 -0.0136 0.0287  0.0140  18  ILE   A CB  
450  C CB  B ILE   A 18  ? 0.1977 0.2188 0.1782 -0.0222 0.0039  0.0246  18  ILE   A CB  
451  C CG1 A ILE   A 18  ? 0.2009 0.2116 0.2097 -0.0192 0.0085  0.0196  18  ILE   A CG1 
452  C CG1 B ILE   A 18  ? 0.2253 0.2294 0.2023 -0.0212 -0.0039 0.0263  18  ILE   A CG1 
453  C CG2 A ILE   A 18  ? 0.1706 0.1877 0.1956 -0.0049 0.0243  0.0035  18  ILE   A CG2 
454  C CG2 B ILE   A 18  ? 0.1974 0.2255 0.2225 -0.0262 0.0044  0.0138  18  ILE   A CG2 
455  C CD1 A ILE   A 18  ? 0.2160 0.2264 0.2340 -0.0206 0.0028  0.0208  18  ILE   A CD1 
456  C CD1 B ILE   A 18  ? 0.2335 0.2380 0.2140 -0.0335 -0.0260 0.0148  18  ILE   A CD1 
479  N N   A LYS   A 19  ? 0.1990 0.1824 0.2707 -0.0075 0.0649  0.0185  19  LYS   A N   
480  N N   B LYS   A 19  ? 0.1847 0.2129 0.1753 -0.0259 0.0233  0.0138  19  LYS   A N   
481  C CA  A LYS   A 19  ? 0.2119 0.1981 0.2698 -0.0020 0.0650  0.0237  19  LYS   A CA  
482  C CA  B LYS   A 19  ? 0.1896 0.2237 0.1578 -0.0263 0.0291  0.0163  19  LYS   A CA  
483  C C   A LYS   A 19  ? 0.2063 0.2050 0.2829 0.0064  0.0583  0.0271  19  LYS   A C   
484  C C   B LYS   A 19  ? 0.1863 0.2286 0.1761 -0.0135 0.0415  0.0294  19  LYS   A C   
485  O O   A LYS   A 19  ? 0.1920 0.2131 0.2991 0.0040  0.0649  0.0313  19  LYS   A O   
486  O O   B LYS   A 19  ? 0.1821 0.2160 0.1971 -0.0234 0.0390  0.0269  19  LYS   A O   
487  C CB  A LYS   A 19  ? 0.2235 0.2161 0.2629 0.0094  0.0610  0.0206  19  LYS   A CB  
488  C CB  B LYS   A 19  ? 0.2062 0.2244 0.1358 -0.0308 0.0330  0.0021  19  LYS   A CB  
489  C CG  A LYS   A 19  ? 0.2352 0.2240 0.2678 0.0131  0.0600  0.0091  19  LYS   A CG  
490  C CG  B LYS   A 19  ? 0.2308 0.2466 0.1698 -0.0316 0.0408  -0.0176 19  LYS   A CG  
491  C CD  A LYS   A 19  ? 0.2412 0.2352 0.2780 0.0200  0.0676  0.0007  19  LYS   A CD  
492  C CD  B LYS   A 19  ? 0.2497 0.2587 0.1921 -0.0300 0.0545  -0.0364 19  LYS   A CD  
493  C CE  A LYS   A 19  ? 0.2486 0.2444 0.2854 0.0167  0.0810  0.0006  19  LYS   A CE  
494  C CE  B LYS   A 19  ? 0.2578 0.2742 0.2252 -0.0355 0.0492  -0.0333 19  LYS   A CE  
495  N NZ  A LYS   A 19  ? 0.2427 0.2510 0.2855 0.0107  0.0950  -0.0017 19  LYS   A NZ  
496  N NZ  B LYS   A 19  ? 0.2684 0.2809 0.2575 -0.0419 0.0419  -0.0322 19  LYS   A NZ  
523  N N   A ASN   A 20  ? 0.2133 0.2150 0.3257 0.0049  0.0480  0.0282  20  ASN   A N   
524  N N   B ASN   A 20  ? 0.1820 0.2328 0.1736 -0.0020 0.0420  0.0317  20  ASN   A N   
525  C CA  A ASN   A 20  ? 0.2173 0.2321 0.3330 0.0135  0.0475  0.0184  20  ASN   A CA  
526  C CA  B ASN   A 20  ? 0.1769 0.2370 0.2246 0.0034  0.0472  0.0318  20  ASN   A CA  
527  C C   A ASN   A 20  ? 0.2140 0.2338 0.3309 0.0032  0.0669  0.0076  20  ASN   A C   
528  C C   B ASN   A 20  ? 0.1950 0.2466 0.2501 -0.0073 0.0475  0.0302  20  ASN   A C   
529  O O   A ASN   A 20  ? 0.2272 0.2226 0.3352 -0.0042 0.0629  0.0121  20  ASN   A O   
530  O O   B ASN   A 20  ? 0.1935 0.2427 0.2671 -0.0042 0.0307  0.0330  20  ASN   A O   
531  C CB  A ASN   A 20  ? 0.2272 0.2477 0.3344 0.0160  0.0367  0.0205  20  ASN   A CB  
532  C CB  B ASN   A 20  ? 0.1656 0.2365 0.2582 0.0071  0.0567  0.0303  20  ASN   A CB  
533  C CG  A ASN   A 20  ? 0.2360 0.2490 0.3430 0.0303  0.0312  0.0241  20  ASN   A CG  
534  C CG  B ASN   A 20  ? 0.1696 0.2343 0.2697 0.0082  0.0518  0.0391  20  ASN   A CG  
535  O OD1 A ASN   A 20  ? 0.2463 0.2488 0.3664 0.0395  0.0310  0.0289  20  ASN   A OD1 
536  O OD1 B ASN   A 20  ? 0.1636 0.2439 0.2681 0.0145  0.0378  0.0678  20  ASN   A OD1 
537  N ND2 A ASN   A 20  ? 0.2522 0.2433 0.3534 0.0324  0.0084  0.0408  20  ASN   A ND2 
538  N ND2 B ASN   A 20  ? 0.1825 0.2176 0.2921 0.0197  0.0352  0.0416  20  ASN   A ND2 
551  N N   A ALA   A 21  ? 0.2015 0.2445 0.3214 0.0036  0.0729  -0.0201 21  ALA   A N   
552  N N   B ALA   A 21  ? 0.2231 0.2581 0.2880 -0.0347 0.0220  0.0154  21  ALA   A N   
553  C CA  A ALA   A 21  ? 0.2064 0.2482 0.2770 -0.0036 0.0659  -0.0242 21  ALA   A CA  
554  C CA  B ALA   A 21  ? 0.2403 0.2667 0.2971 -0.0342 0.0215  0.0284  21  ALA   A CA  
555  C C   A ALA   A 21  ? 0.2100 0.2473 0.2633 -0.0076 0.0538  -0.0228 21  ALA   A C   
556  C C   B ALA   A 21  ? 0.2350 0.2652 0.2784 -0.0327 0.0348  0.0270  21  ALA   A C   
557  O O   A ALA   A 21  ? 0.2058 0.2517 0.2694 -0.0089 0.0568  -0.0198 21  ALA   A O   
558  O O   B ALA   A 21  ? 0.2344 0.2674 0.2760 -0.0343 0.0350  0.0366  21  ALA   A O   
559  C CB  A ALA   A 21  ? 0.2099 0.2561 0.2876 -0.0254 0.0512  -0.0307 21  ALA   A CB  
560  C CB  B ALA   A 21  ? 0.2467 0.2731 0.3408 -0.0254 0.0112  0.0240  21  ALA   A CB  
571  N N   A ASP   A 22  ? 0.2070 0.2389 0.2623 -0.0145 0.0476  -0.0154 22  ASP   A N   
572  N N   B ASP   A 22  ? 0.2257 0.2636 0.2835 -0.0365 0.0476  0.0048  22  ASP   A N   
573  C CA  A ASP   A 22  ? 0.2044 0.2278 0.2458 -0.0075 0.0261  0.0027  22  ASP   A CA  
574  C CA  B ASP   A 22  ? 0.2166 0.2578 0.2727 -0.0315 0.0482  0.0114  22  ASP   A CA  
575  C C   A ASP   A 22  ? 0.2028 0.2185 0.2109 -0.0118 0.0218  0.0151  22  ASP   A C   
576  C C   B ASP   A 22  ? 0.2093 0.2430 0.2169 -0.0329 0.0534  0.0107  22  ASP   A C   
577  O O   A ASP   A 22  ? 0.2017 0.2059 0.2115 -0.0089 0.0115  0.0252  22  ASP   A O   
578  O O   B ASP   A 22  ? 0.2171 0.2502 0.2366 -0.0359 0.0674  0.0215  22  ASP   A O   
579  C CB  A ASP   A 22  ? 0.2110 0.2231 0.2689 0.0053  0.0104  -0.0076 22  ASP   A CB  
580  C CB  B ASP   A 22  ? 0.2068 0.2675 0.3064 -0.0168 0.0588  -0.0077 22  ASP   A CB  
581  C CG  A ASP   A 22  ? 0.2186 0.2170 0.2873 0.0218  0.0100  -0.0074 22  ASP   A CG  
582  C CG  B ASP   A 22  ? 0.2081 0.2762 0.3374 -0.0098 0.0685  -0.0146 22  ASP   A CG  
583  O OD1 A ASP   A 22  ? 0.2173 0.2007 0.2810 0.0222  -0.0138 0.0003  22  ASP   A OD1 
584  O OD1 B ASP   A 22  ? 0.2096 0.2840 0.3401 -0.0116 0.0612  -0.0019 22  ASP   A OD1 
585  O OD2 A ASP   A 22  ? 0.2263 0.2329 0.3303 0.0445  0.0282  -0.0243 22  ASP   A OD2 
586  O OD2 B ASP   A 22  ? 0.2182 0.2955 0.3793 -0.0046 0.0821  -0.0222 22  ASP   A OD2 
595  N N   A ILE   A 23  ? 0.2088 0.2204 0.1965 -0.0085 0.0115  0.0207  23  ILE   A N   
596  N N   B ILE   A 23  ? 0.2085 0.2271 0.1897 -0.0280 0.0276  -0.0037 23  ILE   A N   
597  C CA  A ILE   A 23  ? 0.2164 0.2232 0.1761 -0.0024 0.0247  0.0273  23  ILE   A CA  
598  C CA  B ILE   A 23  ? 0.2040 0.2344 0.1893 -0.0195 0.0224  -0.0046 23  ILE   A CA  
599  C C   A ILE   A 23  ? 0.2153 0.2248 0.1660 -0.0110 0.0469  0.0511  23  ILE   A C   
600  C C   B ILE   A 23  ? 0.1986 0.2401 0.1887 -0.0316 0.0438  -0.0110 23  ILE   A C   
601  O O   A ILE   A 23  ? 0.2232 0.2353 0.1856 -0.0189 0.0419  0.0502  23  ILE   A O   
602  O O   B ILE   A 23  ? 0.2077 0.2281 0.1938 -0.0352 0.0409  -0.0209 23  ILE   A O   
603  C CB  A ILE   A 23  ? 0.2215 0.2223 0.1410 0.0086  0.0158  0.0283  23  ILE   A CB  
604  C CB  B ILE   A 23  ? 0.1927 0.2180 0.1792 -0.0068 0.0214  0.0068  23  ILE   A CB  
605  C CG1 A ILE   A 23  ? 0.2297 0.2260 0.1769 0.0034  0.0050  0.0161  23  ILE   A CG1 
606  C CG1 B ILE   A 23  ? 0.1791 0.2091 0.1757 -0.0038 0.0131  0.0084  23  ILE   A CG1 
607  C CG2 A ILE   A 23  ? 0.2191 0.2316 0.1320 0.0246  0.0038  0.0441  23  ILE   A CG2 
608  C CG2 B ILE   A 23  ? 0.1943 0.2377 0.2012 -0.0086 0.0242  0.0001  23  ILE   A CG2 
609  C CD1 A ILE   A 23  ? 0.2355 0.2253 0.1816 0.0088  -0.0159 0.0115  23  ILE   A CD1 
610  C CD1 B ILE   A 23  ? 0.1781 0.2061 0.1762 -0.0044 -0.0082 -0.0188 23  ILE   A CD1 
633  N N   A VAL   A 24  ? 0.2222 0.2226 0.1772 -0.0149 0.0562  0.0406  24  VAL   A N   
634  N N   B VAL   A 24  ? 0.2054 0.2584 0.1966 -0.0368 0.0483  -0.0167 24  VAL   A N   
635  C CA  A VAL   A 24  ? 0.2305 0.2284 0.2074 -0.0152 0.0271  0.0284  24  VAL   A CA  
636  C CA  B VAL   A 24  ? 0.2194 0.2702 0.2228 -0.0326 0.0243  -0.0091 24  VAL   A CA  
637  C C   A VAL   A 24  ? 0.2387 0.2416 0.2261 -0.0233 0.0247  0.0174  24  VAL   A C   
638  C C   B VAL   A 24  ? 0.2296 0.2922 0.2278 -0.0414 0.0266  -0.0199 24  VAL   A C   
639  O O   A VAL   A 24  ? 0.2481 0.2293 0.2292 -0.0345 0.0342  0.0277  24  VAL   A O   
640  O O   B VAL   A 24  ? 0.2339 0.2933 0.2345 -0.0470 0.0496  -0.0191 24  VAL   A O   
641  C CB  A VAL   A 24  ? 0.2400 0.2352 0.2240 -0.0152 0.0325  0.0231  24  VAL   A CB  
642  C CB  B VAL   A 24  ? 0.2342 0.2788 0.2555 -0.0277 0.0254  0.0142  24  VAL   A CB  
643  C CG1 A VAL   A 24  ? 0.2483 0.2448 0.2475 -0.0085 0.0311  0.0042  24  VAL   A CG1 
644  C CG1 B VAL   A 24  ? 0.2492 0.2946 0.2838 -0.0187 0.0175  0.0073  24  VAL   A CG1 
645  C CG2 A VAL   A 24  ? 0.2585 0.2447 0.2404 -0.0090 0.0384  0.0402  24  VAL   A CG2 
646  C CG2 B VAL   A 24  ? 0.2561 0.2844 0.2798 -0.0195 0.0344  0.0319  24  VAL   A CG2 
665  N N   A GLU   A 25  ? 0.2424 0.2709 0.2267 -0.0100 0.0339  -0.0066 25  GLU   A N   
666  N N   B GLU   A 25  ? 0.2397 0.3140 0.2135 -0.0422 0.0464  -0.0321 25  GLU   A N   
667  C CA  A GLU   A 25  ? 0.2533 0.2915 0.2403 0.0015  0.0397  -0.0178 25  GLU   A CA  
668  C CA  B GLU   A 25  ? 0.2538 0.3277 0.2305 -0.0385 0.0566  -0.0304 25  GLU   A CA  
669  C C   A GLU   A 25  ? 0.2463 0.3018 0.2316 -0.0051 0.0449  -0.0128 25  GLU   A C   
670  C C   B GLU   A 25  ? 0.2443 0.3325 0.2166 -0.0509 0.0587  -0.0134 25  GLU   A C   
671  O O   A GLU   A 25  ? 0.2497 0.3054 0.2523 0.0058  0.0466  -0.0210 25  GLU   A O   
672  O O   B GLU   A 25  ? 0.2507 0.3412 0.2423 -0.0465 0.0601  -0.0193 25  GLU   A O   
673  C CB  A GLU   A 25  ? 0.2805 0.3108 0.2880 0.0039  0.0488  -0.0138 25  GLU   A CB  
674  C CB  B GLU   A 25  ? 0.2825 0.3434 0.2725 -0.0387 0.0811  -0.0215 25  GLU   A CB  
675  C CG  A GLU   A 25  ? 0.3133 0.3280 0.3517 -0.0045 0.0480  -0.0134 25  GLU   A CG  
676  C CG  B GLU   A 25  ? 0.3200 0.3622 0.3426 -0.0452 0.0848  -0.0121 25  GLU   A CG  
677  C CD  A GLU   A 25  ? 0.3365 0.3401 0.4026 -0.0179 0.0461  0.0002  25  GLU   A CD  
678  C CD  B GLU   A 25  ? 0.3461 0.3813 0.4050 -0.0541 0.0811  -0.0005 25  GLU   A CD  
679  O OE1 A GLU   A 25  ? 0.3436 0.3427 0.4050 -0.0198 0.0408  0.0021  25  GLU   A OE1 
680  O OE1 B GLU   A 25  ? 0.3558 0.3924 0.4169 -0.0495 0.0799  -0.0074 25  GLU   A OE1 
681  O OE2 A GLU   A 25  ? 0.3459 0.3494 0.4317 -0.0272 0.0430  0.0016  25  GLU   A OE2 
682  O OE2 B GLU   A 25  ? 0.3592 0.3887 0.4407 -0.0593 0.0837  0.0078  25  GLU   A OE2 
695  N N   A GLU   A 26  ? 0.2402 0.3054 0.2255 -0.0225 0.0582  -0.0144 26  GLU   A N   
696  N N   B GLU   A 26  ? 0.2345 0.3270 0.2058 -0.0653 0.0693  -0.0056 26  GLU   A N   
697  C CA  A GLU   A 26  ? 0.2510 0.3087 0.2196 -0.0387 0.0526  -0.0167 26  GLU   A CA  
698  C CA  B GLU   A 26  ? 0.2462 0.3238 0.1960 -0.0718 0.0602  0.0002  26  GLU   A CA  
699  C C   A GLU   A 26  ? 0.2482 0.2959 0.1950 -0.0456 0.0393  -0.0026 26  GLU   A C   
700  C C   B GLU   A 26  ? 0.2468 0.3087 0.1881 -0.0669 0.0481  -0.0021 26  GLU   A C   
701  O O   A GLU   A 26  ? 0.2578 0.2762 0.1872 -0.0553 0.0300  0.0119  26  GLU   A O   
702  O O   B GLU   A 26  ? 0.2548 0.2994 0.1908 -0.0896 0.0437  -0.0036 26  GLU   A O   
703  C CB  A GLU   A 26  ? 0.2674 0.3244 0.2486 -0.0445 0.0534  -0.0310 26  GLU   A CB  
704  C CB  B GLU   A 26  ? 0.2576 0.3345 0.2040 -0.0819 0.0472  0.0077  26  GLU   A CB  
705  C CG  A GLU   A 26  ? 0.2768 0.3464 0.2915 -0.0568 0.0782  -0.0403 26  GLU   A CG  
706  C CG  B GLU   A 26  ? 0.2709 0.3510 0.2462 -0.0943 0.0484  0.0132  26  GLU   A CG  
707  C CD  A GLU   A 26  ? 0.2675 0.3594 0.3057 -0.0647 0.1067  -0.0495 26  GLU   A CD  
708  C CD  B GLU   A 26  ? 0.2658 0.3583 0.2405 -0.1038 0.0507  0.0236  26  GLU   A CD  
709  O OE1 A GLU   A 26  ? 0.2548 0.3655 0.2924 -0.0621 0.1419  -0.0887 26  GLU   A OE1 
710  O OE1 B GLU   A 26  ? 0.2647 0.3672 0.2105 -0.1040 0.0567  0.0147  26  GLU   A OE1 
711  O OE2 A GLU   A 26  ? 0.2743 0.3705 0.3258 -0.0654 0.1120  -0.0346 26  GLU   A OE2 
712  O OE2 B GLU   A 26  ? 0.2712 0.3572 0.2795 -0.1021 0.0401  0.0489  26  GLU   A OE2 
725  N N   . ALA   A 27  ? 0.2264 0.2942 0.1942 -0.0581 0.0435  0.0122  27  ALA   A N   
726  C CA  . ALA   A 27  ? 0.2254 0.3130 0.1681 -0.0531 0.0392  0.0124  27  ALA   A CA  
727  C C   . ALA   A 27  ? 0.2619 0.3415 0.2067 -0.0722 0.0452  -0.0080 27  ALA   A C   
728  O O   . ALA   A 27  ? 0.2699 0.3360 0.2095 -0.0776 0.0363  0.0054  27  ALA   A O   
729  C CB  . ALA   A 27  ? 0.2134 0.3071 0.1745 -0.0509 0.0151  0.0091  27  ALA   A CB  
736  N N   A LYS   A 28  ? 0.2926 0.3589 0.2249 -0.0686 0.0413  -0.0187 28  LYS   A N   
737  N N   B LYS   A 28  ? 0.2881 0.3540 0.2158 -0.0724 0.0397  -0.0229 28  LYS   A N   
738  C CA  A LYS   A 28  ? 0.3315 0.3876 0.2596 -0.0561 0.0362  -0.0379 28  LYS   A CA  
739  C CA  B LYS   A 28  ? 0.3247 0.3811 0.2443 -0.0608 0.0344  -0.0453 28  LYS   A CA  
740  C C   A LYS   A 28  ? 0.3465 0.4068 0.2447 -0.0647 0.0447  -0.0276 28  LYS   A C   
741  C C   B LYS   A 28  ? 0.3400 0.4028 0.2257 -0.0668 0.0456  -0.0341 28  LYS   A C   
742  O O   A LYS   A 28  ? 0.3500 0.4115 0.2771 -0.0637 0.0385  -0.0248 28  LYS   A O   
743  O O   B LYS   A 28  ? 0.3439 0.4087 0.2704 -0.0649 0.0382  -0.0301 28  LYS   A O   
744  C CB  A LYS   A 28  ? 0.3557 0.4007 0.3148 -0.0408 0.0286  -0.0510 28  LYS   A CB  
745  C CB  B LYS   A 28  ? 0.3476 0.3919 0.2974 -0.0493 0.0272  -0.0558 28  LYS   A CB  
746  C CG  A LYS   A 28  ? 0.3800 0.4105 0.3670 -0.0301 0.0301  -0.0586 28  LYS   A CG  
747  C CG  B LYS   A 28  ? 0.3725 0.4010 0.3498 -0.0420 0.0330  -0.0608 28  LYS   A CG  
748  C CD  A LYS   A 28  ? 0.4009 0.4246 0.4260 -0.0218 0.0227  -0.0620 28  LYS   A CD  
749  C CD  B LYS   A 28  ? 0.3968 0.4176 0.4185 -0.0344 0.0265  -0.0609 28  LYS   A CD  
750  C CE  A LYS   A 28  ? 0.4110 0.4313 0.4624 -0.0198 0.0200  -0.0653 28  LYS   A CE  
751  C CE  B LYS   A 28  ? 0.4107 0.4258 0.4597 -0.0346 0.0253  -0.0631 28  LYS   A CE  
752  N NZ  A LYS   A 28  ? 0.4179 0.4351 0.4864 -0.0175 0.0177  -0.0702 28  LYS   A NZ  
753  N NZ  B LYS   A 28  ? 0.4189 0.4308 0.4858 -0.0321 0.0240  -0.0676 28  LYS   A NZ  
780  N N   A LYS   A 29  ? 0.3568 0.4206 0.2344 -0.0767 0.0689  -0.0104 29  LYS   A N   
781  N N   B LYS   A 29  ? 0.3490 0.4174 0.2097 -0.0783 0.0778  -0.0138 29  LYS   A N   
782  C CA  A LYS   A 29  ? 0.3748 0.4414 0.2568 -0.0810 0.0802  0.0003  29  LYS   A CA  
783  C CA  B LYS   A 29  ? 0.3672 0.4415 0.2353 -0.0812 0.0918  -0.0022 29  LYS   A CA  
784  C C   A LYS   A 29  ? 0.3793 0.4365 0.2222 -0.0883 0.0705  0.0162  29  LYS   A C   
785  C C   B LYS   A 29  ? 0.3738 0.4380 0.2062 -0.0877 0.0772  0.0152  29  LYS   A C   
786  O O   A LYS   A 29  ? 0.3903 0.4480 0.2433 -0.0844 0.0621  0.0035  29  LYS   A O   
787  O O   B LYS   A 29  ? 0.3809 0.4527 0.2279 -0.0836 0.0748  0.0027  29  LYS   A O   
788  C CB  A LYS   A 29  ? 0.3888 0.4667 0.3274 -0.0707 0.0988  0.0024  29  LYS   A CB  
789  C CB  B LYS   A 29  ? 0.3800 0.4688 0.3058 -0.0682 0.1156  -0.0004 29  LYS   A CB  
790  C CG  A LYS   A 29  ? 0.4069 0.4898 0.4009 -0.0574 0.1059  0.0024  29  LYS   A CG  
791  C CG  B LYS   A 29  ? 0.3990 0.4940 0.3859 -0.0507 0.1225  -0.0016 29  LYS   A CG  
792  C CD  A LYS   A 29  ? 0.4244 0.5094 0.4658 -0.0486 0.1061  -0.0022 29  LYS   A CD  
793  C CD  B LYS   A 29  ? 0.4168 0.5146 0.4556 -0.0382 0.1211  -0.0066 29  LYS   A CD  
794  C CE  A LYS   A 29  ? 0.4357 0.5217 0.5060 -0.0422 0.1110  -0.0055 29  LYS   A CE  
795  C CE  B LYS   A 29  ? 0.4269 0.5273 0.4976 -0.0298 0.1250  -0.0107 29  LYS   A CE  
796  N NZ  A LYS   A 29  ? 0.4425 0.5304 0.5294 -0.0369 0.1092  -0.0055 29  LYS   A NZ  
797  N NZ  B LYS   A 29  ? 0.4345 0.5363 0.5252 -0.0239 0.1206  -0.0087 29  LYS   A NZ  
824  N N   . VAL   A 30  ? 0.3716 0.4204 0.2180 -0.0973 0.0694  0.0292  30  VAL   A N   
825  C CA  . VAL   A 30  ? 0.3674 0.3914 0.2120 -0.1141 0.0344  0.0503  30  VAL   A CA  
826  C C   . VAL   A 30  ? 0.3795 0.3765 0.1819 -0.1068 0.0177  0.0321  30  VAL   A C   
827  O O   . VAL   A 30  ? 0.3933 0.3681 0.1683 -0.1076 0.0155  0.0307  30  VAL   A O   
828  C CB  . VAL   A 30  ? 0.3587 0.3839 0.2550 -0.1354 0.0016  0.0673  30  VAL   A CB  
829  C CG1 . VAL   A 30  ? 0.3664 0.3910 0.2939 -0.1299 -0.0118 0.0787  30  VAL   A CG1 
830  C CG2 . VAL   A 30  ? 0.3522 0.3804 0.3066 -0.1478 -0.0031 0.0660  30  VAL   A CG2 
841  N N   A LYS   A 31  ? 0.3688 0.3672 0.1833 -0.1132 0.0105  0.0283  31  LYS   A N   
842  N N   B LYS   A 31  ? 0.3673 0.3663 0.1698 -0.1136 0.0115  0.0298  31  LYS   A N   
843  C CA  A LYS   A 31  ? 0.3734 0.3702 0.2080 -0.1079 -0.0153 0.0299  31  LYS   A CA  
844  C CA  B LYS   A 31  ? 0.3754 0.3707 0.1883 -0.1063 -0.0193 0.0324  31  LYS   A CA  
845  C C   A LYS   A 31  ? 0.3468 0.3543 0.1726 -0.1029 -0.0271 0.0479  31  LYS   A C   
846  C C   B LYS   A 31  ? 0.3473 0.3553 0.1551 -0.1010 -0.0339 0.0544  31  LYS   A C   
847  O O   A LYS   A 31  ? 0.3576 0.3595 0.1801 -0.0983 -0.0311 0.0548  31  LYS   A O   
848  O O   B LYS   A 31  ? 0.3590 0.3613 0.1584 -0.0945 -0.0405 0.0647  31  LYS   A O   
849  C CB  A LYS   A 31  ? 0.4083 0.3935 0.3131 -0.1010 -0.0272 0.0148  31  LYS   A CB  
850  C CB  B LYS   A 31  ? 0.4143 0.3959 0.2959 -0.0969 -0.0311 0.0159  31  LYS   A CB  
851  C CG  A LYS   A 31  ? 0.4426 0.4201 0.4380 -0.0910 -0.0446 -0.0017 31  LYS   A CG  
852  C CG  B LYS   A 31  ? 0.4506 0.4254 0.4263 -0.0849 -0.0489 -0.0015 31  LYS   A CG  
853  C CD  A LYS   A 31  ? 0.4700 0.4421 0.5342 -0.0807 -0.0563 -0.0180 31  LYS   A CD  
854  C CD  B LYS   A 31  ? 0.4804 0.4504 0.5272 -0.0717 -0.0603 -0.0192 31  LYS   A CD  
855  C CE  A LYS   A 31  ? 0.4891 0.4571 0.5994 -0.0733 -0.0630 -0.0320 31  LYS   A CE  
856  C CE  B LYS   A 31  ? 0.5026 0.4674 0.5954 -0.0615 -0.0654 -0.0317 31  LYS   A CE  
857  N NZ  A LYS   A 31  ? 0.5000 0.4605 0.6357 -0.0664 -0.0667 -0.0403 31  LYS   A NZ  
858  N NZ  B LYS   A 31  ? 0.5149 0.4708 0.6326 -0.0525 -0.0687 -0.0398 31  LYS   A NZ  
885  N N   . PRO   A 32  ? 0.3149 0.3281 0.1537 -0.1041 -0.0165 0.0405  32  PRO   A N   
886  C CA  . PRO   A 32  ? 0.3043 0.3138 0.1775 -0.0909 -0.0317 0.0468  32  PRO   A CA  
887  C C   . PRO   A 32  ? 0.2992 0.2994 0.1927 -0.0797 -0.0373 0.0518  32  PRO   A C   
888  O O   . PRO   A 32  ? 0.2993 0.2760 0.1943 -0.0768 -0.0617 0.0486  32  PRO   A O   
889  C CB  . PRO   A 32  ? 0.2875 0.3123 0.1713 -0.0906 -0.0325 0.0455  32  PRO   A CB  
890  C CG  . PRO   A 32  ? 0.2848 0.3207 0.1585 -0.0884 -0.0426 0.0297  32  PRO   A CG  
891  C CD  . PRO   A 32  ? 0.2885 0.3266 0.1276 -0.1002 -0.0390 0.0288  32  PRO   A CD  
899  N N   . THR   A 33  ? 0.3048 0.2981 0.1773 -0.0676 -0.0276 0.0621  33  THR   A N   
900  C CA  . THR   A 33  ? 0.3065 0.3054 0.1796 -0.0555 -0.0386 0.0654  33  THR   A CA  
901  C C   . THR   A 33  ? 0.2783 0.2794 0.1730 -0.0565 -0.0470 0.0538  33  THR   A C   
902  O O   . THR   A 33  ? 0.2770 0.2766 0.1720 -0.0679 -0.0531 0.0500  33  THR   A O   
903  C CB  . THR   A 33  ? 0.3292 0.3248 0.2046 -0.0428 -0.0422 0.0833  33  THR   A CB  
904  O OG1 . THR   A 33  ? 0.3515 0.3498 0.2315 -0.0190 -0.0196 0.0954  33  THR   A OG1 
905  C CG2 . THR   A 33  ? 0.3356 0.3290 0.2504 -0.0304 -0.0633 0.0820  33  THR   A CG2 
913  N N   . VAL   A 34  ? 0.2498 0.2649 0.1625 -0.0496 -0.0452 0.0461  34  VAL   A N   
914  C CA  . VAL   A 34  ? 0.2334 0.2455 0.1301 -0.0492 -0.0288 0.0334  34  VAL   A CA  
915  C C   . VAL   A 34  ? 0.2147 0.2310 0.1513 -0.0462 -0.0271 0.0303  34  VAL   A C   
916  O O   . VAL   A 34  ? 0.2122 0.2297 0.1847 -0.0478 -0.0177 0.0282  34  VAL   A O   
917  C CB  . VAL   A 34  ? 0.2321 0.2371 0.1688 -0.0585 -0.0105 0.0189  34  VAL   A CB  
918  C CG1 . VAL   A 34  ? 0.2354 0.2332 0.1662 -0.0520 0.0052  0.0001  34  VAL   A CG1 
919  C CG2 . VAL   A 34  ? 0.2498 0.2515 0.2162 -0.0408 -0.0299 0.0142  34  VAL   A CG2 
929  N N   . VAL   A 35  ? 0.1914 0.2192 0.1519 -0.0388 -0.0285 0.0325  35  VAL   A N   
930  C CA  . VAL   A 35  ? 0.1822 0.2097 0.1469 -0.0357 -0.0002 0.0273  35  VAL   A CA  
931  C C   . VAL   A 35  ? 0.1744 0.2042 0.1556 -0.0349 -0.0011 0.0149  35  VAL   A C   
932  O O   . VAL   A 35  ? 0.1838 0.2140 0.1367 -0.0408 0.0075  0.0049  35  VAL   A O   
933  C CB  . VAL   A 35  ? 0.1983 0.2219 0.1571 -0.0314 0.0079  0.0085  35  VAL   A CB  
934  C CG1 . VAL   A 35  ? 0.2235 0.2283 0.1642 -0.0393 0.0065  0.0082  35  VAL   A CG1 
935  C CG2 . VAL   A 35  ? 0.2061 0.2329 0.1808 -0.0263 0.0043  0.0143  35  VAL   A CG2 
945  N N   . VAL   A 36  ? 0.1623 0.1923 0.1497 -0.0297 0.0072  0.0139  36  VAL   A N   
946  C CA  . VAL   A 36  ? 0.1535 0.1849 0.1358 -0.0166 0.0008  0.0099  36  VAL   A CA  
947  C C   . VAL   A 36  ? 0.1584 0.1852 0.1636 -0.0210 0.0071  0.0224  36  VAL   A C   
948  O O   . VAL   A 36  ? 0.1719 0.1903 0.1561 -0.0202 0.0116  0.0124  36  VAL   A O   
949  C CB  . VAL   A 36  ? 0.1536 0.1722 0.1689 -0.0168 -0.0041 0.0022  36  VAL   A CB  
950  C CG1 . VAL   A 36  ? 0.1667 0.1659 0.1761 -0.0071 -0.0020 0.0029  36  VAL   A CG1 
951  C CG2 . VAL   A 36  ? 0.1642 0.1801 0.1975 -0.0197 -0.0192 0.0254  36  VAL   A CG2 
961  N N   . ASN   A 37  ? 0.1676 0.1649 0.1407 -0.0085 -0.0055 0.0198  37  ASN   A N   
962  C CA  . ASN   A 37  ? 0.1535 0.1602 0.1536 -0.0052 0.0034  0.0158  37  ASN   A CA  
963  C C   . ASN   A 37  ? 0.1584 0.1544 0.1508 -0.0184 0.0126  0.0139  37  ASN   A C   
964  O O   . ASN   A 37  ? 0.1810 0.1634 0.1471 0.0051  -0.0001 0.0031  37  ASN   A O   
965  C CB  . ASN   A 37  ? 0.1442 0.1514 0.1742 -0.0064 0.0015  0.0145  37  ASN   A CB  
966  C CG  . ASN   A 37  ? 0.1662 0.1658 0.1674 -0.0001 0.0100  0.0015  37  ASN   A CG  
967  O OD1 . ASN   A 37  ? 0.1618 0.1653 0.1846 -0.0083 0.0067  0.0051  37  ASN   A OD1 
968  N ND2 . ASN   A 37  ? 0.1653 0.1727 0.1695 0.0009  0.0047  0.0390  37  ASN   A ND2 
975  N N   A ALA   A 38  ? 0.1578 0.1630 0.1368 -0.0019 0.0152  0.0031  38  ALA   A N   
976  N N   B ALA   A 38  ? 0.1624 0.1697 0.1567 -0.0058 0.0124  0.0120  38  ALA   A N   
977  C CA  A ALA   A 38  ? 0.1599 0.1550 0.1319 0.0031  0.0073  -0.0063 38  ALA   A CA  
978  C CA  B ALA   A 38  ? 0.1700 0.1691 0.1785 -0.0077 0.0018  0.0178  38  ALA   A CA  
979  C C   A ALA   A 38  ? 0.1558 0.1545 0.1495 0.0092  -0.0036 -0.0067 38  ALA   A C   
980  C C   B ALA   A 38  ? 0.1658 0.1725 0.1947 -0.0069 -0.0113 0.0162  38  ALA   A C   
981  O O   A ALA   A 38  ? 0.1481 0.1438 0.1442 0.0013  0.0057  -0.0194 38  ALA   A O   
982  O O   B ALA   A 38  ? 0.1553 0.1640 0.2045 -0.0159 -0.0069 0.0286  38  ALA   A O   
983  C CB  A ALA   A 38  ? 0.1583 0.1756 0.1331 -0.0191 0.0033  0.0184  38  ALA   A CB  
984  C CB  B ALA   A 38  ? 0.1725 0.1795 0.1833 -0.0247 -0.0057 0.0263  38  ALA   A CB  
995  N N   A ALA   A 39  ? 0.1520 0.1517 0.1176 0.0230  -0.0010 -0.0060 39  ALA   A N   
996  N N   B ALA   A 39  ? 0.1582 0.1802 0.1964 -0.0071 0.0116  0.0289  39  ALA   A N   
997  C CA  A ALA   A 39  ? 0.1579 0.1538 0.1412 0.0244  0.0066  0.0016  39  ALA   A CA  
998  C CA  B ALA   A 39  ? 0.1560 0.1751 0.1727 -0.0011 0.0013  0.0286  39  ALA   A CA  
999  C C   A ALA   A 39  ? 0.1690 0.1534 0.1257 -0.0005 -0.0007 -0.0041 39  ALA   A C   
1000 C C   B ALA   A 39  ? 0.1561 0.1644 0.1628 0.0040  -0.0046 0.0146  39  ALA   A C   
1001 O O   A ALA   A 39  ? 0.1805 0.1615 0.1293 -0.0215 0.0110  -0.0099 39  ALA   A O   
1002 O O   B ALA   A 39  ? 0.1657 0.1671 0.1797 0.0070  -0.0140 0.0257  39  ALA   A O   
1003 C CB  A ALA   A 39  ? 0.1527 0.1572 0.1669 0.0357  -0.0001 0.0026  39  ALA   A CB  
1004 C CB  B ALA   A 39  ? 0.1684 0.1853 0.1750 -0.0093 0.0019  0.0160  39  ALA   A CB  
1015 N N   A ASN   A 40  ? 0.1773 0.1586 0.1607 -0.0085 0.0215  -0.0014 40  ASN   A N   
1016 N N   B ASN   A 40  ? 0.1642 0.1598 0.1647 -0.0077 0.0241  0.0069  40  ASN   A N   
1017 C CA  A ASN   A 40  ? 0.1901 0.1644 0.1637 -0.0016 0.0091  -0.0064 40  ASN   A CA  
1018 C CA  B ASN   A 40  ? 0.1787 0.1668 0.1580 -0.0063 0.0196  0.0150  40  ASN   A CA  
1019 C C   A ASN   A 40  ? 0.1840 0.1544 0.1598 -0.0031 0.0117  -0.0085 40  ASN   A C   
1020 C C   B ASN   A 40  ? 0.1773 0.1529 0.1505 -0.0108 0.0191  0.0045  40  ASN   A C   
1021 O O   A ASN   A 40  ? 0.1739 0.1551 0.1762 -0.0059 0.0124  0.0048  40  ASN   A O   
1022 O O   B ASN   A 40  ? 0.1616 0.1529 0.1589 -0.0208 0.0216  0.0197  40  ASN   A O   
1023 C CB  A ASN   A 40  ? 0.2036 0.1538 0.1549 0.0027  -0.0007 -0.0245 40  ASN   A CB  
1024 C CB  B ASN   A 40  ? 0.1803 0.1615 0.1507 -0.0115 0.0156  0.0059  40  ASN   A CB  
1025 C CG  A ASN   A 40  ? 0.2254 0.1524 0.2051 0.0162  -0.0144 -0.0105 40  ASN   A CG  
1026 C CG  B ASN   A 40  ? 0.1863 0.1707 0.1958 -0.0149 0.0212  0.0172  40  ASN   A CG  
1027 O OD1 A ASN   A 40  ? 0.2369 0.1473 0.2190 0.0287  -0.0321 -0.0004 40  ASN   A OD1 
1028 O OD1 B ASN   A 40  ? 0.1896 0.1740 0.1926 -0.0184 0.0280  0.0262  40  ASN   A OD1 
1029 N ND2 A ASN   A 40  ? 0.2317 0.1600 0.2114 0.0227  -0.0236 -0.0284 40  ASN   A ND2 
1030 N ND2 B ASN   A 40  ? 0.1919 0.1815 0.1995 -0.0042 0.0179  -0.0022 40  ASN   A ND2 
1043 N N   . VAL   A 41  ? 0.1856 0.1585 0.1635 -0.0012 0.0205  -0.0009 41  VAL   A N   
1044 C CA  . VAL   A 41  ? 0.1861 0.1655 0.1806 0.0013  0.0348  0.0127  41  VAL   A CA  
1045 C C   . VAL   A 41  ? 0.1796 0.1722 0.1825 0.0108  0.0382  0.0127  41  VAL   A C   
1046 O O   . VAL   A 41  ? 0.1863 0.1629 0.2035 0.0026  0.0354  -0.0007 41  VAL   A O   
1047 C CB  . VAL   A 41  ? 0.2120 0.1722 0.1681 -0.0071 0.0523  0.0072  41  VAL   A CB  
1048 C CG1 . VAL   A 41  ? 0.2144 0.1785 0.1946 -0.0127 0.0546  -0.0036 41  VAL   A CG1 
1049 C CG2 . VAL   A 41  ? 0.2401 0.1865 0.1861 -0.0280 0.0463  -0.0111 41  VAL   A CG2 
1060 N N   . TYR   A 42  ? 0.1583 0.1664 0.2076 0.0005  0.0315  0.0248  42  TYR   A N   
1061 C CA  . TYR   A 42  ? 0.1613 0.1648 0.1861 -0.0126 0.0320  0.0313  42  TYR   A CA  
1062 C C   . TYR   A 42  ? 0.1621 0.1504 0.1708 -0.0019 0.0379  0.0279  42  TYR   A C   
1063 O O   . TYR   A 42  ? 0.1742 0.1565 0.1805 -0.0163 0.0191  0.0053  42  TYR   A O   
1064 C CB  . TYR   A 42  ? 0.1930 0.1833 0.1771 -0.0025 0.0317  0.0474  42  TYR   A CB  
1065 C CG  . TYR   A 42  ? 0.2146 0.1793 0.1666 0.0017  0.0242  0.0467  42  TYR   A CG  
1066 C CD1 . TYR   A 42  ? 0.2241 0.1861 0.2022 -0.0155 0.0287  0.0340  42  TYR   A CD1 
1067 C CD2 . TYR   A 42  ? 0.2279 0.1987 0.1961 0.0057  0.0391  0.0299  42  TYR   A CD2 
1068 C CE1 . TYR   A 42  ? 0.2468 0.1936 0.2325 -0.0176 0.0509  0.0150  42  TYR   A CE1 
1069 C CE2 . TYR   A 42  ? 0.2514 0.1884 0.2120 -0.0153 0.0414  0.0468  42  TYR   A CE2 
1070 C CZ  . TYR   A 42  ? 0.2705 0.1973 0.2101 -0.0192 0.0553  0.0150  42  TYR   A CZ  
1071 O OH  . TYR   A 42  ? 0.2899 0.2229 0.2233 -0.0301 0.0394  0.0027  42  TYR   A OH  
1081 N N   . LEU   A 43  ? 0.1546 0.1515 0.1833 -0.0092 0.0296  0.0005  43  LEU   A N   
1082 C CA  . LEU   A 43  ? 0.1665 0.1500 0.1629 -0.0116 0.0170  0.0053  43  LEU   A CA  
1083 C C   . LEU   A 43  ? 0.1656 0.1482 0.1739 -0.0009 0.0152  0.0080  43  LEU   A C   
1084 O O   . LEU   A 43  ? 0.1757 0.1605 0.2006 0.0041  0.0022  -0.0022 43  LEU   A O   
1085 C CB  . LEU   A 43  ? 0.1751 0.1556 0.2054 -0.0054 0.0151  0.0198  43  LEU   A CB  
1086 C CG  . LEU   A 43  ? 0.1716 0.1539 0.2001 0.0006  0.0067  0.0121  43  LEU   A CG  
1087 C CD1 . LEU   A 43  ? 0.1791 0.1731 0.2165 -0.0032 -0.0067 0.0272  43  LEU   A CD1 
1088 C CD2 . LEU   A 43  ? 0.1832 0.1649 0.1799 -0.0096 0.0043  0.0359  43  LEU   A CD2 
1100 N N   A LYS   A 44  ? 0.1759 0.1539 0.1772 0.0009  0.0190  0.0066  44  LYS   A N   
1101 N N   B LYS   A 44  ? 0.1737 0.1548 0.1735 0.0046  0.0169  0.0000  44  LYS   A N   
1102 C CA  A LYS   A 44  ? 0.1897 0.1590 0.1919 -0.0032 0.0262  0.0133  44  LYS   A CA  
1103 C CA  B LYS   A 44  ? 0.1849 0.1622 0.1891 0.0042  0.0228  0.0019  44  LYS   A CA  
1104 C C   A LYS   A 44  ? 0.1806 0.1537 0.1765 0.0037  0.0104  -0.0026 44  LYS   A C   
1105 C C   B LYS   A 44  ? 0.1751 0.1582 0.1711 0.0154  0.0030  -0.0098 44  LYS   A C   
1106 O O   A LYS   A 44  ? 0.1918 0.1680 0.1838 -0.0098 0.0032  -0.0076 44  LYS   A O   
1107 O O   B LYS   A 44  ? 0.1910 0.1674 0.2021 0.0103  -0.0018 -0.0038 44  LYS   A O   
1108 C CB  A LYS   A 44  ? 0.2122 0.1699 0.2367 -0.0072 0.0314  0.0284  44  LYS   A CB  
1109 C CB  B LYS   A 44  ? 0.2092 0.1752 0.2353 0.0005  0.0264  0.0095  44  LYS   A CB  
1110 C CG  A LYS   A 44  ? 0.2404 0.2153 0.2992 -0.0050 0.0355  0.0146  44  LYS   A CG  
1111 C CG  B LYS   A 44  ? 0.2389 0.2290 0.3014 0.0043  0.0285  -0.0119 44  LYS   A CG  
1112 C CD  A LYS   A 44  ? 0.2773 0.2630 0.3737 -0.0140 0.0328  0.0282  44  LYS   A CD  
1113 C CD  B LYS   A 44  ? 0.2781 0.2844 0.3838 -0.0047 0.0203  0.0017  44  LYS   A CD  
1114 C CE  A LYS   A 44  ? 0.3007 0.2951 0.4148 -0.0206 0.0415  0.0305  44  LYS   A CE  
1115 C CE  B LYS   A 44  ? 0.3028 0.3141 0.4279 -0.0083 0.0241  -0.0008 44  LYS   A CE  
1116 N NZ  A LYS   A 44  ? 0.3065 0.3115 0.4212 -0.0357 0.0513  0.0332  44  LYS   A NZ  
1117 N NZ  B LYS   A 44  ? 0.3066 0.3185 0.4286 -0.0177 0.0234  0.0011  44  LYS   A NZ  
1144 N N   A HIS   A 45  ? 0.1686 0.1433 0.1929 0.0043  0.0140  0.0178  45  HIS   A N   
1145 N N   B HIS   A 45  ? 0.1629 0.1580 0.1901 0.0089  0.0017  0.0026  45  HIS   A N   
1146 C CA  A HIS   A 45  ? 0.1675 0.1368 0.1885 0.0161  0.0172  0.0179  45  HIS   A CA  
1147 C CA  B HIS   A 45  ? 0.1616 0.1679 0.1879 0.0079  0.0102  0.0006  45  HIS   A CA  
1148 C C   A HIS   A 45  ? 0.1676 0.1465 0.1895 0.0111  0.0054  0.0241  45  HIS   A C   
1149 C C   B HIS   A 45  ? 0.1667 0.1896 0.2176 0.0048  -0.0068 -0.0142 45  HIS   A C   
1150 O O   A HIS   A 45  ? 0.1733 0.1416 0.2321 0.0093  0.0137  0.0062  45  HIS   A O   
1151 O O   B HIS   A 45  ? 0.1929 0.1997 0.2620 0.0036  -0.0010 -0.0241 45  HIS   A O   
1152 C CB  A HIS   A 45  ? 0.1853 0.1339 0.1713 0.0066  0.0104  0.0027  45  HIS   A CB  
1153 C CB  B HIS   A 45  ? 0.1667 0.1651 0.1491 -0.0041 0.0163  -0.0061 45  HIS   A CB  
1154 C CG  A HIS   A 45  ? 0.1786 0.1298 0.1678 -0.0007 0.0123  0.0106  45  HIS   A CG  
1155 C CG  B HIS   A 45  ? 0.1513 0.1729 0.1549 -0.0087 0.0225  0.0065  45  HIS   A CG  
1156 N ND1 A HIS   A 45  ? 0.1736 0.1323 0.1625 -0.0014 0.0166  -0.0001 45  HIS   A ND1 
1157 N ND1 B HIS   A 45  ? 0.1401 0.1832 0.1698 -0.0086 0.0086  0.0211  45  HIS   A ND1 
1158 C CD2 A HIS   A 45  ? 0.1809 0.1341 0.1764 -0.0143 -0.0046 0.0073  45  HIS   A CD2 
1159 C CD2 B HIS   A 45  ? 0.1477 0.1770 0.1811 -0.0195 0.0100  -0.0002 45  HIS   A CD2 
1160 C CE1 A HIS   A 45  ? 0.1727 0.1406 0.1659 -0.0048 -0.0012 0.0042  45  HIS   A CE1 
1161 C CE1 B HIS   A 45  ? 0.1317 0.1790 0.1854 -0.0095 -0.0069 0.0100  45  HIS   A CE1 
1162 N NE2 A HIS   A 45  ? 0.1768 0.1473 0.1669 -0.0057 0.0050  0.0157  45  HIS   A NE2 
1163 N NE2 B HIS   A 45  ? 0.1412 0.1845 0.1838 -0.0099 0.0114  0.0107  45  HIS   A NE2 
1178 N N   A GLY   A 46  ? 0.1762 0.1640 0.1933 0.0120  -0.0265 0.0198  46  GLY   A N   
1179 N N   B GLY   A 46  ? 0.1694 0.2002 0.2278 0.0178  -0.0145 0.0057  46  GLY   A N   
1180 C CA  A GLY   A 46  ? 0.1893 0.1694 0.2010 0.0143  -0.0445 0.0335  46  GLY   A CA  
1181 C CA  B GLY   A 46  ? 0.1747 0.2074 0.2177 0.0179  0.0008  0.0264  46  GLY   A CA  
1182 C C   A GLY   A 46  ? 0.1936 0.1699 0.2127 0.0224  -0.0480 0.0198  46  GLY   A C   
1183 C C   B GLY   A 46  ? 0.1786 0.2060 0.1945 0.0231  -0.0018 0.0123  46  GLY   A C   
1184 O O   A GLY   A 46  ? 0.1948 0.1640 0.2185 0.0236  -0.0608 0.0089  46  GLY   A O   
1185 O O   B GLY   A 46  ? 0.1896 0.2238 0.1965 0.0126  0.0018  0.0018  46  GLY   A O   
1192 N N   A GLY   A 47  ? 0.1944 0.1816 0.2279 0.0175  -0.0389 0.0131  47  GLY   A N   
1193 N N   B GLY   A 47  ? 0.1862 0.1971 0.1923 0.0246  -0.0055 -0.0010 47  GLY   A N   
1194 C CA  A GLY   A 47  ? 0.1905 0.1857 0.2010 0.0215  -0.0485 0.0148  47  GLY   A CA  
1195 C CA  B GLY   A 47  ? 0.1895 0.2002 0.1780 0.0125  -0.0256 -0.0097 47  GLY   A CA  
1196 C C   A GLY   A 47  ? 0.1917 0.1833 0.1844 0.0177  -0.0366 0.0214  47  GLY   A C   
1197 C C   B GLY   A 47  ? 0.1919 0.2003 0.1775 0.0097  -0.0020 -0.0322 47  GLY   A C   
1198 O O   A GLY   A 47  ? 0.1881 0.1678 0.1880 0.0283  -0.0433 0.0212  47  GLY   A O   
1199 O O   B GLY   A 47  ? 0.1878 0.2051 0.1875 0.0129  -0.0007 -0.0241 47  GLY   A O   
1206 N N   A GLY   A 48  ? 0.1816 0.1921 0.1687 0.0167  -0.0206 0.0327  48  GLY   A N   
1207 N N   B GLY   A 48  ? 0.1793 0.2034 0.1679 0.0010  -0.0089 -0.0246 48  GLY   A N   
1208 C CA  A GLY   A 48  ? 0.1885 0.1846 0.1846 0.0012  -0.0167 0.0155  48  GLY   A CA  
1209 C CA  B GLY   A 48  ? 0.1837 0.1934 0.1614 -0.0042 -0.0058 -0.0155 48  GLY   A CA  
1210 C C   A GLY   A 48  ? 0.1809 0.1790 0.1828 0.0045  -0.0202 0.0023  48  GLY   A C   
1211 C C   B GLY   A 48  ? 0.1760 0.1874 0.1704 0.0112  -0.0022 -0.0157 48  GLY   A C   
1212 O O   A GLY   A 48  ? 0.1911 0.1766 0.1779 0.0093  -0.0152 0.0018  48  GLY   A O   
1213 O O   B GLY   A 48  ? 0.1694 0.1987 0.1815 0.0152  -0.0167 -0.0156 48  GLY   A O   
1220 N N   A VAL   A 49  ? 0.1730 0.1704 0.1937 -0.0068 -0.0263 -0.0050 49  VAL   A N   
1221 N N   B VAL   A 49  ? 0.1742 0.1671 0.1623 0.0064  -0.0079 -0.0286 49  VAL   A N   
1222 C CA  A VAL   A 49  ? 0.1825 0.1848 0.1799 -0.0117 -0.0159 0.0139  49  VAL   A CA  
1223 C CA  B VAL   A 49  ? 0.1635 0.1760 0.1473 0.0032  -0.0051 -0.0079 49  VAL   A CA  
1224 C C   A VAL   A 49  ? 0.1809 0.1640 0.1422 -0.0050 0.0043  0.0224  49  VAL   A C   
1225 C C   B VAL   A 49  ? 0.1650 0.1743 0.1255 0.0048  0.0082  -0.0161 49  VAL   A C   
1226 O O   A VAL   A 49  ? 0.1789 0.1589 0.1465 -0.0142 0.0061  0.0022  49  VAL   A O   
1227 O O   B VAL   A 49  ? 0.1695 0.1779 0.1268 0.0040  0.0231  -0.0045 49  VAL   A O   
1228 C CB  A VAL   A 49  ? 0.1961 0.2057 0.2393 -0.0251 -0.0227 -0.0029 49  VAL   A CB  
1229 C CB  B VAL   A 49  ? 0.1485 0.1794 0.1848 -0.0026 -0.0143 -0.0042 49  VAL   A CB  
1230 C CG1 A VAL   A 49  ? 0.1906 0.2116 0.2490 -0.0389 -0.0260 -0.0080 49  VAL   A CG1 
1231 C CG1 B VAL   A 49  ? 0.1335 0.1760 0.1809 0.0001  0.0102  0.0275  49  VAL   A CG1 
1232 C CG2 A VAL   A 49  ? 0.2079 0.2184 0.2642 -0.0308 -0.0264 0.0068  49  VAL   A CG2 
1233 C CG2 B VAL   A 49  ? 0.1773 0.1922 0.1827 -0.0102 -0.0343 -0.0040 49  VAL   A CG2 
1252 N N   A ALA   A 50  ? 0.1781 0.1599 0.1092 -0.0013 -0.0072 0.0379  50  ALA   A N   
1253 N N   B ALA   A 50  ? 0.1582 0.1691 0.1780 0.0054  -0.0164 -0.0229 50  ALA   A N   
1254 C CA  A ALA   A 50  ? 0.1755 0.1584 0.1212 -0.0077 0.0089  0.0394  50  ALA   A CA  
1255 C CA  B ALA   A 50  ? 0.1589 0.1532 0.1824 0.0057  -0.0171 -0.0276 50  ALA   A CA  
1256 C C   A ALA   A 50  ? 0.1706 0.1721 0.1137 -0.0105 -0.0018 0.0255  50  ALA   A C   
1257 C C   B ALA   A 50  ? 0.1627 0.1462 0.1929 0.0062  -0.0194 -0.0293 50  ALA   A C   
1258 O O   A ALA   A 50  ? 0.1639 0.1799 0.1224 -0.0201 0.0180  0.0232  50  ALA   A O   
1259 O O   B ALA   A 50  ? 0.1684 0.1409 0.2045 0.0159  -0.0221 -0.0285 50  ALA   A O   
1260 C CB  A ALA   A 50  ? 0.1781 0.1618 0.1373 0.0046  0.0002  0.0355  50  ALA   A CB  
1261 C CB  B ALA   A 50  ? 0.1705 0.1559 0.1867 0.0075  0.0029  -0.0226 50  ALA   A CB  
1272 N N   A GLY   A 51  ? 0.1575 0.1787 0.1108 -0.0013 -0.0126 0.0272  51  GLY   A N   
1273 N N   B GLY   A 51  ? 0.1523 0.1537 0.1859 0.0081  -0.0329 -0.0300 51  GLY   A N   
1274 C CA  A GLY   A 51  ? 0.1653 0.1773 0.1562 -0.0060 -0.0020 0.0173  51  GLY   A CA  
1275 C CA  B GLY   A 51  ? 0.1577 0.1447 0.1817 0.0110  -0.0171 -0.0196 51  GLY   A CA  
1276 C C   A GLY   A 51  ? 0.1647 0.1720 0.1558 -0.0006 -0.0007 0.0111  51  GLY   A C   
1277 C C   B GLY   A 51  ? 0.1795 0.1529 0.1638 0.0190  -0.0082 -0.0197 51  GLY   A C   
1278 O O   A GLY   A 51  ? 0.1607 0.1854 0.1673 -0.0109 -0.0016 -0.0043 51  GLY   A O   
1279 O O   B GLY   A 51  ? 0.1923 0.1697 0.1454 0.0132  0.0048  -0.0207 51  GLY   A O   
1286 N N   A ALA   A 52  ? 0.1608 0.1748 0.1705 -0.0043 0.0033  0.0093  52  ALA   A N   
1287 N N   B ALA   A 52  ? 0.1747 0.1634 0.1700 0.0128  0.0057  -0.0237 52  ALA   A N   
1288 C CA  A ALA   A 52  ? 0.1507 0.1671 0.1923 -0.0052 0.0016  0.0088  52  ALA   A CA  
1289 C CA  B ALA   A 52  ? 0.1599 0.1649 0.1829 0.0101  0.0071  -0.0239 52  ALA   A CA  
1290 C C   A ALA   A 52  ? 0.1574 0.1664 0.1837 -0.0080 0.0184  0.0047  52  ALA   A C   
1291 C C   B ALA   A 52  ? 0.1558 0.1619 0.1584 0.0012  0.0091  -0.0259 52  ALA   A C   
1292 O O   A ALA   A 52  ? 0.1677 0.1604 0.2114 0.0127  0.0101  -0.0000 52  ALA   A O   
1293 O O   B ALA   A 52  ? 0.1714 0.1689 0.1794 0.0004  0.0041  -0.0219 52  ALA   A O   
1294 C CB  A ALA   A 52  ? 0.1398 0.1756 0.2004 -0.0012 -0.0190 0.0217  52  ALA   A CB  
1295 C CB  B ALA   A 52  ? 0.1601 0.1825 0.2210 0.0092  0.0032  -0.0142 52  ALA   A CB  
1306 N N   A LEU   A 53  ? 0.1734 0.1717 0.1582 -0.0150 0.0195  0.0290  53  LEU   A N   
1307 N N   B LEU   A 53  ? 0.1652 0.1690 0.1267 0.0052  -0.0129 -0.0119 53  LEU   A N   
1308 C CA  A LEU   A 53  ? 0.1715 0.1865 0.1580 -0.0111 0.0116  0.0231  53  LEU   A CA  
1309 C CA  B LEU   A 53  ? 0.1664 0.1804 0.1153 0.0056  -0.0118 -0.0033 53  LEU   A CA  
1310 C C   A LEU   A 53  ? 0.1872 0.1887 0.1790 0.0046  0.0046  0.0098  53  LEU   A C   
1311 C C   B LEU   A 53  ? 0.1801 0.1754 0.1119 0.0020  0.0234  -0.0095 53  LEU   A C   
1312 O O   A LEU   A 53  ? 0.2034 0.1974 0.2097 -0.0043 -0.0041 0.0064  53  LEU   A O   
1313 O O   B LEU   A 53  ? 0.1866 0.1784 0.1170 -0.0244 0.0289  -0.0020 53  LEU   A O   
1314 C CB  A LEU   A 53  ? 0.1514 0.1936 0.1777 -0.0194 0.0209  0.0060  53  LEU   A CB  
1315 C CB  B LEU   A 53  ? 0.1548 0.1808 0.1447 -0.0009 -0.0186 -0.0064 53  LEU   A CB  
1316 C CG  A LEU   A 53  ? 0.1556 0.1952 0.1649 -0.0062 0.0111  0.0014  53  LEU   A CG  
1317 C CG  B LEU   A 53  ? 0.1488 0.1885 0.1451 -0.0002 -0.0129 0.0024  53  LEU   A CG  
1318 C CD1 A LEU   A 53  ? 0.1440 0.2117 0.1479 0.0186  0.0107  0.0160  53  LEU   A CD1 
1319 C CD1 B LEU   A 53  ? 0.1527 0.1964 0.1467 0.0013  -0.0114 0.0037  53  LEU   A CD1 
1320 C CD2 A LEU   A 53  ? 0.1628 0.1933 0.1790 0.0092  -0.0013 0.0096  53  LEU   A CD2 
1321 C CD2 B LEU   A 53  ? 0.1556 0.1925 0.1452 -0.0141 -0.0101 0.0137  53  LEU   A CD2 
1344 N N   A ASN   A 54  ? 0.1823 0.1819 0.1698 0.0020  -0.0158 0.0156  54  ASN   A N   
1345 N N   B ASN   A 54  ? 0.1659 0.1648 0.1482 -0.0086 0.0162  0.0001  54  ASN   A N   
1346 C CA  A ASN   A 54  ? 0.1720 0.1816 0.1805 -0.0043 -0.0129 0.0145  54  ASN   A CA  
1347 C CA  B ASN   A 54  ? 0.1517 0.1667 0.1654 -0.0193 0.0213  -0.0110 54  ASN   A CA  
1348 C C   A ASN   A 54  ? 0.1775 0.1838 0.1759 0.0037  -0.0024 0.0085  54  ASN   A C   
1349 C C   B ASN   A 54  ? 0.1687 0.1743 0.1609 -0.0063 0.0048  -0.0056 54  ASN   A C   
1350 O O   A ASN   A 54  ? 0.1786 0.1923 0.1957 0.0042  0.0092  0.0017  54  ASN   A O   
1351 O O   B ASN   A 54  ? 0.1714 0.1749 0.1762 -0.0049 0.0042  -0.0184 54  ASN   A O   
1352 C CB  A ASN   A 54  ? 0.1713 0.1799 0.2021 -0.0064 -0.0310 0.0210  54  ASN   A CB  
1353 C CB  B ASN   A 54  ? 0.1521 0.1634 0.1834 -0.0140 0.0227  -0.0225 54  ASN   A CB  
1354 C CG  A ASN   A 54  ? 0.1830 0.1858 0.2090 -0.0042 -0.0445 0.0241  54  ASN   A CG  
1355 C CG  B ASN   A 54  ? 0.1638 0.1666 0.1865 -0.0125 0.0243  -0.0292 54  ASN   A CG  
1356 O OD1 A ASN   A 54  ? 0.1875 0.1881 0.2201 0.0050  -0.0447 0.0333  54  ASN   A OD1 
1357 O OD1 B ASN   A 54  ? 0.1595 0.1618 0.1689 -0.0203 0.0544  -0.0383 54  ASN   A OD1 
1358 N ND2 A ASN   A 54  ? 0.1939 0.1958 0.2221 -0.0134 -0.0376 0.0501  54  ASN   A ND2 
1359 N ND2 B ASN   A 54  ? 0.1811 0.1812 0.2017 -0.0246 0.0095  0.0016  54  ASN   A ND2 
1372 N N   . LYS   A 55  ? 0.1805 0.1841 0.1769 0.0084  0.0128  -0.0176 55  LYS   A N   
1373 C CA  . LYS   A 55  ? 0.1819 0.2069 0.1550 0.0130  -0.0057 -0.0163 55  LYS   A CA  
1374 C C   . LYS   A 55  ? 0.1846 0.2060 0.1417 -0.0025 -0.0120 -0.0292 55  LYS   A C   
1375 O O   . LYS   A 55  ? 0.1913 0.2136 0.1590 0.0028  0.0019  -0.0288 55  LYS   A O   
1376 C CB  . LYS   A 55  ? 0.1813 0.2019 0.1996 0.0223  -0.0050 -0.0081 55  LYS   A CB  
1377 C CG  . LYS   A 55  ? 0.2242 0.2364 0.2126 0.0416  -0.0237 -0.0189 55  LYS   A CG  
1378 C CD  . LYS   A 55  ? 0.2496 0.2693 0.2404 0.0591  -0.0281 -0.0342 55  LYS   A CD  
1379 C CE  . LYS   A 55  ? 0.2663 0.3042 0.2543 0.0714  -0.0538 -0.0333 55  LYS   A CE  
1380 N NZ  . LYS   A 55  ? 0.2798 0.3335 0.2591 0.0794  -0.0632 -0.0215 55  LYS   A NZ  
1395 N N   . ALA   A 56  ? 0.1834 0.2198 0.1822 -0.0141 0.0116  -0.0108 56  ALA   A N   
1396 C CA  . ALA   A 56  ? 0.1788 0.2386 0.1833 -0.0256 0.0197  -0.0207 56  ALA   A CA  
1397 C C   . ALA   A 56  ? 0.1932 0.2455 0.1521 -0.0184 0.0184  -0.0386 56  ALA   A C   
1398 O O   . ALA   A 56  ? 0.1933 0.2781 0.1638 -0.0175 0.0212  -0.0353 56  ALA   A O   
1399 C CB  . ALA   A 56  ? 0.1729 0.2531 0.2074 -0.0263 0.0067  -0.0231 56  ALA   A CB  
1405 N N   . THR   A 57  ? 0.1765 0.2219 0.1733 -0.0197 0.0266  -0.0211 57  THR   A N   
1406 C CA  . THR   A 57  ? 0.1845 0.2021 0.1778 -0.0199 0.0052  -0.0085 57  THR   A CA  
1407 C C   . THR   A 57  ? 0.1876 0.2064 0.1695 -0.0129 -0.0029 -0.0207 57  THR   A C   
1408 O O   . THR   A 57  ? 0.1904 0.2092 0.1789 -0.0118 -0.0048 -0.0325 57  THR   A O   
1409 C CB  . THR   A 57  ? 0.1796 0.2015 0.1557 -0.0175 0.0114  -0.0114 57  THR   A CB  
1410 O OG1 . THR   A 57  ? 0.1776 0.2058 0.1635 -0.0158 0.0023  -0.0197 57  THR   A OG1 
1411 C CG2 . THR   A 57  ? 0.1893 0.2138 0.1506 -0.0149 -0.0002 0.0034  57  THR   A CG2 
1419 N N   . ASN   A 58  ? 0.1901 0.2072 0.1827 -0.0122 0.0199  -0.0388 58  ASN   A N   
1420 C CA  . ASN   A 58  ? 0.2048 0.1995 0.1997 -0.0130 0.0284  -0.0477 58  ASN   A CA  
1421 C C   . ASN   A 58  ? 0.2029 0.1832 0.1857 -0.0026 0.0015  -0.0328 58  ASN   A C   
1422 O O   . ASN   A 58  ? 0.2057 0.1758 0.2054 -0.0181 -0.0111 -0.0360 58  ASN   A O   
1423 C CB  . ASN   A 58  ? 0.2659 0.2161 0.2433 -0.0228 0.0672  -0.0619 58  ASN   A CB  
1424 C CG  . ASN   A 58  ? 0.3214 0.2474 0.3254 -0.0260 0.0563  -0.0223 58  ASN   A CG  
1425 O OD1 . ASN   A 58  ? 0.3499 0.2227 0.3898 0.0128  0.0991  -0.0095 58  ASN   A OD1 
1426 N ND2 . ASN   A 58  ? 0.3404 0.2690 0.3410 -0.0217 0.0347  -0.0214 58  ASN   A ND2 
1433 N N   . ASN   A 59  ? 0.1881 0.1798 0.1745 -0.0036 -0.0051 -0.0350 59  ASN   A N   
1434 C CA  . ASN   A 59  ? 0.2029 0.1704 0.1653 0.0144  0.0019  -0.0049 59  ASN   A CA  
1435 C C   . ASN   A 59  ? 0.1915 0.1677 0.1713 -0.0086 -0.0008 0.0006  59  ASN   A C   
1436 O O   . ASN   A 59  ? 0.1826 0.1772 0.1763 -0.0120 0.0128  0.0042  59  ASN   A O   
1437 C CB  . ASN   A 59  ? 0.2129 0.1629 0.1623 -0.0006 -0.0288 -0.0012 59  ASN   A CB  
1438 C CG  . ASN   A 59  ? 0.2023 0.1686 0.1925 0.0007  -0.0168 0.0096  59  ASN   A CG  
1439 O OD1 . ASN   A 59  ? 0.1947 0.1691 0.1980 -0.0061 -0.0083 0.0043  59  ASN   A OD1 
1440 N ND2 . ASN   A 59  ? 0.2167 0.1638 0.2174 -0.0059 -0.0100 0.0054  59  ASN   A ND2 
1447 N N   . ALA   A 60  ? 0.1629 0.1725 0.1935 0.0050  0.0016  -0.0033 60  ALA   A N   
1448 C CA  . ALA   A 60  ? 0.1697 0.1783 0.1748 0.0001  -0.0056 0.0034  60  ALA   A CA  
1449 C C   . ALA   A 60  ? 0.1730 0.1728 0.1690 -0.0102 0.0184  -0.0084 60  ALA   A C   
1450 O O   . ALA   A 60  ? 0.1596 0.1724 0.2064 -0.0083 0.0066  -0.0059 60  ALA   A O   
1451 C CB  . ALA   A 60  ? 0.1931 0.1751 0.1790 -0.0156 0.0005  -0.0235 60  ALA   A CB  
1457 N N   . MET   A 61  ? 0.1667 0.1509 0.1990 -0.0040 0.0017  -0.0148 61  MET   A N   
1458 C CA  . MET   A 61  ? 0.1646 0.1559 0.1802 -0.0117 0.0079  0.0073  61  MET   A CA  
1459 C C   . MET   A 61  ? 0.1669 0.1662 0.1770 -0.0116 -0.0083 -0.0014 61  MET   A C   
1460 O O   . MET   A 61  ? 0.1712 0.1576 0.1835 -0.0070 0.0137  -0.0036 61  MET   A O   
1461 C CB  . MET   A 61  ? 0.1792 0.1692 0.1700 -0.0099 0.0122  0.0001  61  MET   A CB  
1462 C CG  . MET   A 61  ? 0.1821 0.1831 0.1599 -0.0065 0.0073  -0.0039 61  MET   A CG  
1463 S SD  . MET   A 61  ? 0.1698 0.1731 0.2172 -0.0206 0.0030  -0.0095 61  MET   A SD  
1464 C CE  . MET   A 61  ? 0.2000 0.1874 0.2518 -0.0040 0.0157  -0.0394 61  MET   A CE  
1474 N N   . GLN   A 62  ? 0.1577 0.1622 0.1848 -0.0068 -0.0061 0.0122  62  GLN   A N   
1475 C CA  . GLN   A 62  ? 0.1773 0.1474 0.1868 -0.0134 0.0051  0.0062  62  GLN   A CA  
1476 C C   . GLN   A 62  ? 0.1803 0.1396 0.1914 -0.0054 0.0052  -0.0009 62  GLN   A C   
1477 O O   . GLN   A 62  ? 0.1720 0.1705 0.1777 -0.0012 0.0144  -0.0037 62  GLN   A O   
1478 C CB  . GLN   A 62  ? 0.1779 0.1464 0.1881 -0.0061 -0.0044 -0.0014 62  GLN   A CB  
1479 C CG  . GLN   A 62  ? 0.1759 0.1478 0.1830 0.0069  0.0098  0.0154  62  GLN   A CG  
1480 C CD  . GLN   A 62  ? 0.1869 0.1574 0.1529 -0.0020 0.0208  -0.0003 62  GLN   A CD  
1481 O OE1 . GLN   A 62  ? 0.1821 0.1696 0.1790 -0.0023 0.0087  -0.0065 62  GLN   A OE1 
1482 N NE2 . GLN   A 62  ? 0.1791 0.1667 0.1866 -0.0051 0.0070  0.0005  62  GLN   A NE2 
1491 N N   . VAL   A 63  ? 0.1805 0.1549 0.1941 -0.0208 0.0173  -0.0120 63  VAL   A N   
1492 C CA  . VAL   A 63  ? 0.1759 0.1642 0.2039 -0.0217 0.0096  -0.0200 63  VAL   A CA  
1493 C C   . VAL   A 63  ? 0.1812 0.1689 0.1961 -0.0147 0.0186  -0.0251 63  VAL   A C   
1494 O O   . VAL   A 63  ? 0.1737 0.1683 0.2065 -0.0168 0.0051  -0.0078 63  VAL   A O   
1495 C CB  . VAL   A 63  ? 0.1879 0.1755 0.2477 -0.0185 0.0058  -0.0439 63  VAL   A CB  
1496 C CG1 . VAL   A 63  ? 0.1948 0.2078 0.2802 -0.0155 -0.0075 -0.0732 63  VAL   A CG1 
1497 C CG2 . VAL   A 63  ? 0.2060 0.1668 0.2736 -0.0163 0.0099  -0.0378 63  VAL   A CG2 
1507 N N   . GLU   A 64  ? 0.1693 0.1641 0.1970 -0.0124 -0.0032 -0.0131 64  GLU   A N   
1508 C CA  . GLU   A 64  ? 0.1621 0.1648 0.1986 -0.0090 -0.0081 -0.0031 64  GLU   A CA  
1509 C C   . GLU   A 64  ? 0.1674 0.1637 0.1822 -0.0066 -0.0049 0.0123  64  GLU   A C   
1510 O O   . GLU   A 64  ? 0.1681 0.1641 0.1979 -0.0053 0.0061  0.0071  64  GLU   A O   
1511 C CB  . GLU   A 64  ? 0.1707 0.1682 0.2006 -0.0173 0.0102  -0.0153 64  GLU   A CB  
1512 C CG  . GLU   A 64  ? 0.1713 0.1768 0.1881 -0.0182 0.0184  -0.0010 64  GLU   A CG  
1513 C CD  . GLU   A 64  ? 0.1951 0.1854 0.2021 -0.0205 0.0193  -0.0059 64  GLU   A CD  
1514 O OE1 . GLU   A 64  ? 0.1866 0.1950 0.2214 -0.0158 0.0234  -0.0023 64  GLU   A OE1 
1515 O OE2 . GLU   A 64  ? 0.2142 0.1770 0.1961 -0.0287 0.0019  -0.0022 64  GLU   A OE2 
1522 N N   . SER   A 65  ? 0.1642 0.1688 0.1712 -0.0079 0.0003  0.0124  65  SER   A N   
1523 C CA  . SER   A 65  ? 0.1644 0.1658 0.1654 -0.0054 0.0113  0.0022  65  SER   A CA  
1524 C C   . SER   A 65  ? 0.1755 0.1669 0.1685 -0.0055 0.0055  0.0011  65  SER   A C   
1525 O O   . SER   A 65  ? 0.1799 0.1718 0.2048 -0.0103 0.0284  -0.0189 65  SER   A O   
1526 C CB  . SER   A 65  ? 0.1605 0.1601 0.1853 -0.0106 0.0026  0.0121  65  SER   A CB  
1527 O OG  . SER   A 65  ? 0.1587 0.1724 0.1820 -0.0108 0.0004  0.0127  65  SER   A OG  
1533 N N   . ASP   A 66  ? 0.1625 0.1503 0.1850 -0.0005 0.0187  0.0133  66  ASP   A N   
1534 C CA  . ASP   A 66  ? 0.1747 0.1694 0.1958 0.0017  0.0053  0.0001  66  ASP   A CA  
1535 C C   . ASP   A 66  ? 0.1580 0.1622 0.2014 0.0052  0.0111  0.0093  66  ASP   A C   
1536 O O   . ASP   A 66  ? 0.1635 0.1753 0.2395 0.0045  0.0409  0.0062  66  ASP   A O   
1537 C CB  . ASP   A 66  ? 0.1833 0.1804 0.2347 0.0076  0.0038  0.0293  66  ASP   A CB  
1538 C CG  . ASP   A 66  ? 0.1939 0.2019 0.2733 -0.0072 0.0138  0.0426  66  ASP   A CG  
1539 O OD1 . ASP   A 66  ? 0.1989 0.2212 0.2681 -0.0069 0.0053  0.0594  66  ASP   A OD1 
1540 O OD2 . ASP   A 66  ? 0.2087 0.2209 0.3443 0.0104  -0.0001 0.0153  66  ASP   A OD2 
1545 N N   . ASP   A 67  ? 0.1523 0.1634 0.2323 -0.0031 -0.0095 0.0187  67  ASP   A N   
1546 C CA  . ASP   A 67  ? 0.1712 0.1927 0.2494 0.0049  -0.0070 0.0204  67  ASP   A CA  
1547 C C   . ASP   A 67  ? 0.1593 0.1909 0.2257 0.0036  0.0106  0.0227  67  ASP   A C   
1548 O O   . ASP   A 67  ? 0.1604 0.1900 0.2495 0.0039  0.0209  0.0385  67  ASP   A O   
1549 C CB  . ASP   A 67  ? 0.1887 0.1862 0.2720 -0.0107 -0.0259 0.0258  67  ASP   A CB  
1550 C CG  . ASP   A 67  ? 0.1880 0.1946 0.2943 -0.0169 -0.0422 0.0264  67  ASP   A CG  
1551 O OD1 . ASP   A 67  ? 0.1907 0.2116 0.3836 -0.0312 -0.0354 0.0363  67  ASP   A OD1 
1552 O OD2 . ASP   A 67  ? 0.1759 0.2113 0.2743 0.0052  -0.0070 0.0314  67  ASP   A OD2 
1557 N N   . TYR   A 68  ? 0.1645 0.1729 0.2230 0.0129  0.0179  0.0318  68  TYR   A N   
1558 C CA  . TYR   A 68  ? 0.1816 0.1756 0.2081 0.0158  0.0206  0.0247  68  TYR   A CA  
1559 C C   . TYR   A 68  ? 0.1794 0.1583 0.1944 0.0019  0.0274  0.0139  68  TYR   A C   
1560 O O   . TYR   A 68  ? 0.1817 0.1701 0.2317 0.0132  0.0378  0.0119  68  TYR   A O   
1561 C CB  . TYR   A 68  ? 0.1758 0.1820 0.2142 -0.0028 0.0404  0.0153  68  TYR   A CB  
1562 C CG  . TYR   A 68  ? 0.1748 0.1785 0.2416 0.0131  0.0405  0.0117  68  TYR   A CG  
1563 C CD1 . TYR   A 68  ? 0.2008 0.1806 0.2935 -0.0160 0.0530  -0.0073 68  TYR   A CD1 
1564 C CD2 . TYR   A 68  ? 0.1966 0.1956 0.2726 0.0140  0.0629  0.0075  68  TYR   A CD2 
1565 C CE1 . TYR   A 68  ? 0.2094 0.2038 0.3427 -0.0238 0.0581  -0.0165 68  TYR   A CE1 
1566 C CE2 . TYR   A 68  ? 0.2087 0.1782 0.3199 -0.0021 0.0842  -0.0211 68  TYR   A CE2 
1567 C CZ  . TYR   A 68  ? 0.2089 0.1870 0.3478 -0.0209 0.0532  -0.0197 68  TYR   A CZ  
1568 O OH  . TYR   A 68  ? 0.2388 0.2077 0.3899 -0.0225 0.0501  -0.0590 68  TYR   A OH  
1578 N N   . ILE   A 69  ? 0.1647 0.1527 0.2061 -0.0053 0.0251  0.0285  69  ILE   A N   
1579 C CA  . ILE   A 69  ? 0.1721 0.1618 0.2134 -0.0005 0.0254  0.0121  69  ILE   A CA  
1580 C C   . ILE   A 69  ? 0.1828 0.1586 0.2105 0.0093  0.0407  0.0200  69  ILE   A C   
1581 O O   . ILE   A 69  ? 0.1818 0.1782 0.1936 0.0080  0.0260  0.0197  69  ILE   A O   
1582 C CB  . ILE   A 69  ? 0.1834 0.1761 0.2067 0.0048  0.0116  0.0006  69  ILE   A CB  
1583 C CG1 . ILE   A 69  ? 0.1815 0.1805 0.2353 0.0014  0.0210  -0.0019 69  ILE   A CG1 
1584 C CG2 . ILE   A 69  ? 0.1988 0.1928 0.2396 0.0079  0.0023  -0.0105 69  ILE   A CG2 
1585 C CD1 . ILE   A 69  ? 0.1826 0.1999 0.2509 -0.0026 0.0139  -0.0097 69  ILE   A CD1 
1597 N N   . ALA   A 70  ? 0.1899 0.1725 0.2212 -0.0096 0.0255  0.0234  70  ALA   A N   
1598 C CA  . ALA   A 70  ? 0.1871 0.1808 0.2412 -0.0204 0.0329  0.0258  70  ALA   A CA  
1599 C C   . ALA   A 70  ? 0.1935 0.1995 0.2512 -0.0121 0.0446  0.0239  70  ALA   A C   
1600 O O   . ALA   A 70  ? 0.2057 0.2337 0.2820 0.0099  0.0611  0.0539  70  ALA   A O   
1601 C CB  . ALA   A 70  ? 0.1883 0.1765 0.2720 -0.0263 0.0239  0.0247  70  ALA   A CB  
1607 N N   . THR   A 71  ? 0.1819 0.1820 0.2187 0.0015  0.0380  0.0238  71  THR   A N   
1608 C CA  . THR   A 71  ? 0.1975 0.2022 0.2597 0.0113  0.0367  0.0209  71  THR   A CA  
1609 C C   . THR   A 71  ? 0.1886 0.2006 0.2790 0.0165  0.0487  0.0126  71  THR   A C   
1610 O O   . THR   A 71  ? 0.1837 0.2260 0.3416 0.0032  0.0375  -0.0129 71  THR   A O   
1611 C CB  . THR   A 71  ? 0.2337 0.2251 0.2828 0.0166  -0.0130 0.0356  71  THR   A CB  
1612 O OG1 . THR   A 71  ? 0.2613 0.2486 0.2998 0.0182  -0.0342 0.0194  71  THR   A OG1 
1613 C CG2 . THR   A 71  ? 0.2476 0.2557 0.3069 0.0211  -0.0221 0.0504  71  THR   A CG2 
1621 N N   . ASN   A 72  ? 0.1885 0.1862 0.2536 0.0166  0.0382  0.0162  72  ASN   A N   
1622 C CA  . ASN   A 72  ? 0.1921 0.1828 0.2531 0.0211  0.0536  0.0316  72  ASN   A CA  
1623 C C   . ASN   A 72  ? 0.2025 0.1973 0.2394 0.0093  0.0636  0.0099  72  ASN   A C   
1624 O O   . ASN   A 72  ? 0.2204 0.1950 0.2529 0.0037  0.0492  0.0015  72  ASN   A O   
1625 C CB  . ASN   A 72  ? 0.2100 0.1923 0.2533 0.0278  0.0672  0.0401  72  ASN   A CB  
1626 C CG  . ASN   A 72  ? 0.2455 0.2140 0.2457 0.0302  0.0563  0.0495  72  ASN   A CG  
1627 O OD1 . ASN   A 72  ? 0.2639 0.2579 0.2648 0.0313  0.0573  0.0386  72  ASN   A OD1 
1628 N ND2 . ASN   A 72  ? 0.2666 0.2014 0.2473 0.0569  0.0221  0.0267  72  ASN   A ND2 
1635 N N   . GLY   A 73  ? 0.1990 0.1913 0.1948 0.0094  0.0566  0.0051  73  GLY   A N   
1636 C CA  . GLY   A 73  ? 0.1977 0.1741 0.2172 0.0023  0.0380  0.0044  73  GLY   A CA  
1637 C C   . GLY   A 73  ? 0.1971 0.1598 0.2187 0.0048  0.0395  0.0311  73  GLY   A C   
1638 O O   . GLY   A 73  ? 0.2046 0.1739 0.2189 0.0159  0.0291  0.0312  73  GLY   A O   
1642 N N   . PRO   A 74  ? 0.1956 0.1830 0.2111 -0.0047 0.0597  0.0030  74  PRO   A N   
1643 C CA  . PRO   A 74  ? 0.1917 0.1732 0.2249 -0.0010 0.0417  0.0064  74  PRO   A CA  
1644 C C   . PRO   A 74  ? 0.1994 0.1431 0.2285 -0.0046 0.0302  0.0084  74  PRO   A C   
1645 O O   . PRO   A 74  ? 0.2042 0.1570 0.2441 -0.0005 0.0297  -0.0087 74  PRO   A O   
1646 C CB  . PRO   A 74  ? 0.2117 0.2140 0.2431 0.0091  0.0390  0.0426  74  PRO   A CB  
1647 C CG  . PRO   A 74  ? 0.2448 0.2647 0.2984 -0.0171 0.0154  0.0184  74  PRO   A CG  
1648 C CD  . PRO   A 74  ? 0.2142 0.2307 0.2328 -0.0119 0.0336  -0.0041 74  PRO   A CD  
1656 N N   . LEU   A 75  ? 0.2051 0.1468 0.2020 -0.0090 0.0316  -0.0028 75  LEU   A N   
1657 C CA  . LEU   A 75  ? 0.2096 0.1554 0.1708 -0.0037 0.0127  0.0046  75  LEU   A CA  
1658 C C   . LEU   A 75  ? 0.2177 0.1625 0.1735 -0.0008 0.0269  0.0091  75  LEU   A C   
1659 O O   . LEU   A 75  ? 0.2354 0.1700 0.2009 0.0004  0.0006  0.0102  75  LEU   A O   
1660 C CB  . LEU   A 75  ? 0.2107 0.1692 0.1604 0.0055  0.0149  0.0295  75  LEU   A CB  
1661 C CG  . LEU   A 75  ? 0.2203 0.2026 0.1789 -0.0183 0.0353  0.0186  75  LEU   A CG  
1662 C CD1 . LEU   A 75  ? 0.2368 0.2531 0.1944 -0.0305 0.0246  -0.0176 75  LEU   A CD1 
1663 C CD2 . LEU   A 75  ? 0.2646 0.2302 0.2645 0.0073  0.0286  0.0281  75  LEU   A CD2 
1675 N N   . LYS   A 76  ? 0.2211 0.1538 0.1986 -0.0043 0.0212  -0.0098 76  LYS   A N   
1676 C CA  . LYS   A 76  ? 0.2000 0.1793 0.2093 -0.0116 0.0156  -0.0035 76  LYS   A CA  
1677 C C   . LYS   A 76  ? 0.1906 0.1595 0.1679 0.0067  0.0152  0.0085  76  LYS   A C   
1678 O O   . LYS   A 76  ? 0.2043 0.1586 0.1631 -0.0054 0.0062  0.0088  76  LYS   A O   
1679 C CB  . LYS   A 76  ? 0.2069 0.2077 0.2534 -0.0059 0.0267  -0.0485 76  LYS   A CB  
1680 C CG  . LYS   A 76  ? 0.2231 0.1994 0.3205 0.0043  0.0058  -0.0337 76  LYS   A CG  
1681 C CD  . LYS   A 76  ? 0.2335 0.1913 0.3832 0.0086  -0.0062 -0.0289 76  LYS   A CD  
1682 C CE  . LYS   A 76  ? 0.2625 0.2187 0.4434 0.0028  -0.0039 -0.0464 76  LYS   A CE  
1683 N NZ  . LYS   A 76  ? 0.2719 0.2156 0.4887 -0.0168 -0.0144 -0.0674 76  LYS   A NZ  
1697 N N   . VAL   A 77  ? 0.2022 0.1750 0.1713 -0.0055 0.0253  0.0171  77  VAL   A N   
1698 C CA  . VAL   A 77  ? 0.2024 0.1673 0.1653 0.0094  0.0198  0.0167  77  VAL   A CA  
1699 C C   . VAL   A 77  ? 0.2103 0.1559 0.1803 0.0048  0.0220  0.0095  77  VAL   A C   
1700 O O   . VAL   A 77  ? 0.2232 0.1676 0.1681 0.0108  0.0253  -0.0081 77  VAL   A O   
1701 C CB  . VAL   A 77  ? 0.2309 0.1876 0.1880 0.0074  -0.0024 0.0239  77  VAL   A CB  
1702 C CG1 . VAL   A 77  ? 0.2454 0.2031 0.2280 -0.0048 -0.0211 0.0102  77  VAL   A CG1 
1703 C CG2 . VAL   A 77  ? 0.2443 0.2036 0.2393 0.0029  -0.0116 0.0282  77  VAL   A CG2 
1713 N N   . GLY   A 78  ? 0.1940 0.1515 0.1730 0.0081  0.0187  0.0137  78  GLY   A N   
1714 C CA  . GLY   A 78  ? 0.2007 0.1681 0.1732 0.0017  0.0242  0.0024  78  GLY   A CA  
1715 C C   . GLY   A 78  ? 0.1919 0.1639 0.1637 0.0024  0.0159  0.0204  78  GLY   A C   
1716 O O   . GLY   A 78  ? 0.1985 0.1610 0.1929 -0.0068 0.0143  0.0171  78  GLY   A O   
1720 N N   . GLY   A 79  ? 0.1945 0.1640 0.1695 -0.0021 0.0091  0.0189  79  GLY   A N   
1721 C CA  . GLY   A 79  ? 0.1884 0.1678 0.1738 -0.0057 0.0090  0.0123  79  GLY   A CA  
1722 C C   . GLY   A 79  ? 0.1610 0.1553 0.1745 -0.0046 0.0010  0.0079  79  GLY   A C   
1723 O O   . GLY   A 79  ? 0.1705 0.1669 0.1949 0.0183  0.0004  0.0201  79  GLY   A O   
1727 N N   . SER   A 80  ? 0.1521 0.1657 0.1962 0.0085  0.0148  -0.0072 80  SER   A N   
1728 C CA  . SER   A 80  ? 0.1625 0.1533 0.1770 -0.0065 -0.0021 0.0037  80  SER   A CA  
1729 C C   . SER   A 80  ? 0.1723 0.1652 0.1739 -0.0132 0.0001  0.0131  80  SER   A C   
1730 O O   . SER   A 80  ? 0.1758 0.1987 0.1998 0.0023  0.0013  0.0051  80  SER   A O   
1731 C CB  . SER   A 80  ? 0.1801 0.1534 0.1949 -0.0012 0.0113  0.0064  80  SER   A CB  
1732 O OG  . SER   A 80  ? 0.2028 0.1669 0.2426 -0.0046 -0.0111 0.0265  80  SER   A OG  
1738 N N   . CYS   A 81  ? 0.1702 0.1484 0.1795 -0.0134 -0.0117 0.0193  81  CYS   A N   
1739 C CA  . CYS   A 81  ? 0.1563 0.1783 0.1853 -0.0119 -0.0123 0.0267  81  CYS   A CA  
1740 C C   . CYS   A 81  ? 0.1593 0.1723 0.1628 -0.0050 -0.0045 0.0310  81  CYS   A C   
1741 O O   . CYS   A 81  ? 0.1597 0.1979 0.1880 0.0031  0.0013  0.0294  81  CYS   A O   
1742 C CB  . CYS   A 81  ? 0.1752 0.1868 0.2077 -0.0220 -0.0141 0.0426  81  CYS   A CB  
1743 S SG  . CYS   A 81  ? 0.1831 0.1617 0.2057 -0.0151 0.0016  0.0132  81  CYS   A SG  
1749 N N   . VAL   A 82  ? 0.1777 0.1641 0.1631 -0.0031 -0.0129 0.0159  82  VAL   A N   
1750 C CA  . VAL   A 82  ? 0.1702 0.1808 0.1627 -0.0129 -0.0055 0.0196  82  VAL   A CA  
1751 C C   . VAL   A 82  ? 0.1776 0.1868 0.1908 -0.0152 -0.0112 0.0263  82  VAL   A C   
1752 O O   . VAL   A 82  ? 0.1696 0.1927 0.2231 -0.0084 -0.0039 0.0037  82  VAL   A O   
1753 C CB  . VAL   A 82  ? 0.2083 0.1913 0.1969 -0.0119 -0.0050 0.0378  82  VAL   A CB  
1754 C CG1 . VAL   A 82  ? 0.2292 0.2003 0.2406 -0.0149 -0.0190 0.0409  82  VAL   A CG1 
1755 C CG2 . VAL   A 82  ? 0.2141 0.1932 0.2148 -0.0148 0.0005  0.0365  82  VAL   A CG2 
1765 N N   . LEU   A 83  ? 0.1764 0.1726 0.1659 -0.0209 -0.0114 0.0164  83  LEU   A N   
1766 C CA  . LEU   A 83  ? 0.1716 0.1866 0.1619 -0.0176 -0.0069 0.0164  83  LEU   A CA  
1767 C C   . LEU   A 83  ? 0.1771 0.1871 0.1640 -0.0197 -0.0185 0.0177  83  LEU   A C   
1768 O O   . LEU   A 83  ? 0.1848 0.2002 0.1743 -0.0287 -0.0055 0.0275  83  LEU   A O   
1769 C CB  . LEU   A 83  ? 0.1863 0.1947 0.1568 -0.0223 -0.0126 0.0294  83  LEU   A CB  
1770 C CG  . LEU   A 83  ? 0.2017 0.1959 0.1568 -0.0212 -0.0067 0.0150  83  LEU   A CG  
1771 C CD1 . LEU   A 83  ? 0.2184 0.2106 0.1589 -0.0441 -0.0113 0.0287  83  LEU   A CD1 
1772 C CD2 . LEU   A 83  ? 0.2087 0.2118 0.1954 -0.0197 0.0010  0.0225  83  LEU   A CD2 
1784 N N   . SER   A 84  ? 0.1891 0.1990 0.1655 -0.0251 -0.0295 0.0138  84  SER   A N   
1785 C CA  . SER   A 84  ? 0.2044 0.2061 0.1438 -0.0193 -0.0367 0.0112  84  SER   A CA  
1786 C C   . SER   A 84  ? 0.2050 0.2015 0.1621 -0.0222 -0.0103 0.0102  84  SER   A C   
1787 O O   . SER   A 84  ? 0.1885 0.2160 0.1694 -0.0160 -0.0027 0.0042  84  SER   A O   
1788 C CB  . SER   A 84  ? 0.2165 0.2227 0.1553 -0.0305 -0.0111 -0.0005 84  SER   A CB  
1789 O OG  . SER   A 84  ? 0.2153 0.2452 0.1823 -0.0312 -0.0197 -0.0279 84  SER   A OG  
1795 N N   . GLY   A 85  ? 0.2112 0.2082 0.1597 -0.0319 -0.0127 -0.0003 85  GLY   A N   
1796 C CA  . GLY   A 85  ? 0.2264 0.2310 0.1748 -0.0383 -0.0064 -0.0221 85  GLY   A CA  
1797 C C   . GLY   A 85  ? 0.2205 0.2314 0.1470 -0.0264 -0.0151 -0.0124 85  GLY   A C   
1798 O O   . GLY   A 85  ? 0.2126 0.2405 0.1844 -0.0370 0.0096  -0.0146 85  GLY   A O   
1802 N N   . HIS   A 86  ? 0.2129 0.2171 0.1430 -0.0287 -0.0033 -0.0016 86  HIS   A N   
1803 C CA  . HIS   A 86  ? 0.2317 0.2293 0.1404 -0.0271 -0.0036 0.0006  86  HIS   A CA  
1804 C C   . HIS   A 86  ? 0.2451 0.2426 0.1389 -0.0322 0.0043  0.0197  86  HIS   A C   
1805 O O   . HIS   A 86  ? 0.2688 0.2606 0.1386 -0.0259 0.0108  0.0068  86  HIS   A O   
1806 C CB  . HIS   A 86  ? 0.2165 0.2249 0.1429 -0.0110 0.0206  0.0103  86  HIS   A CB  
1807 C CG  . HIS   A 86  ? 0.2092 0.2254 0.1595 -0.0140 0.0144  0.0109  86  HIS   A CG  
1808 N ND1 . HIS   A 86  ? 0.2208 0.2299 0.2222 -0.0335 0.0029  0.0067  86  HIS   A ND1 
1809 C CD2 . HIS   A 86  ? 0.2210 0.2088 0.1577 -0.0056 0.0200  0.0073  86  HIS   A CD2 
1810 C CE1 . HIS   A 86  ? 0.2046 0.2231 0.2249 -0.0219 0.0293  0.0110  86  HIS   A CE1 
1811 N NE2 . HIS   A 86  ? 0.2134 0.2041 0.1988 -0.0060 0.0300  0.0353  86  HIS   A NE2 
1819 N N   . ASN   A 87  ? 0.2541 0.2511 0.1748 -0.0159 0.0269  -0.0084 87  ASN   A N   
1820 C CA  . ASN   A 87  ? 0.2740 0.2790 0.1885 -0.0040 0.0545  -0.0130 87  ASN   A CA  
1821 C C   . ASN   A 87  ? 0.2763 0.3030 0.2130 -0.0233 0.0566  -0.0001 87  ASN   A C   
1822 O O   . ASN   A 87  ? 0.3293 0.3460 0.2721 -0.0340 0.1095  -0.0124 87  ASN   A O   
1823 C CB  . ASN   A 87  ? 0.3065 0.2939 0.2047 0.0040  0.0659  -0.0207 87  ASN   A CB  
1824 C CG  . ASN   A 87  ? 0.3169 0.3046 0.2044 0.0061  0.0770  0.0012  87  ASN   A CG  
1825 O OD1 . ASN   A 87  ? 0.3410 0.3112 0.2041 0.0331  0.0628  0.0069  87  ASN   A OD1 
1826 N ND2 . ASN   A 87  ? 0.3218 0.3251 0.1956 0.0027  0.0815  -0.0000 87  ASN   A ND2 
1833 N N   A LEU   A 88  ? 0.2581 0.2858 0.2041 -0.0328 0.0303  0.0080  88  LEU   A N   
1834 N N   B LEU   A 88  ? 0.2569 0.2888 0.2023 -0.0308 0.0297  -0.0002 88  LEU   A N   
1835 C CA  A LEU   A 88  ? 0.2393 0.2828 0.2222 -0.0438 0.0319  0.0328  88  LEU   A CA  
1836 C CA  B LEU   A 88  ? 0.2367 0.2903 0.2230 -0.0404 0.0356  0.0209  88  LEU   A CA  
1837 C C   A LEU   A 88  ? 0.2325 0.2871 0.2215 -0.0438 0.0328  0.0426  88  LEU   A C   
1838 C C   B LEU   A 88  ? 0.2319 0.2918 0.2222 -0.0417 0.0370  0.0391  88  LEU   A C   
1839 O O   A LEU   A 88  ? 0.2383 0.2899 0.2451 -0.0420 0.0311  0.0561  88  LEU   A O   
1840 O O   B LEU   A 88  ? 0.2398 0.2957 0.2438 -0.0372 0.0369  0.0546  88  LEU   A O   
1841 C CB  A LEU   A 88  ? 0.2321 0.2753 0.2218 -0.0484 0.0044  0.0515  88  LEU   A CB  
1842 C CB  B LEU   A 88  ? 0.2268 0.2893 0.2224 -0.0426 0.0064  0.0272  88  LEU   A CB  
1843 C CG  A LEU   A 88  ? 0.2455 0.2799 0.2521 -0.0442 0.0016  0.0556  88  LEU   A CG  
1844 C CG  B LEU   A 88  ? 0.2386 0.2989 0.2521 -0.0333 0.0023  0.0254  88  LEU   A CG  
1845 C CD1 A LEU   A 88  ? 0.2612 0.2849 0.2592 -0.0419 -0.0138 0.0243  88  LEU   A CD1 
1846 C CD1 B LEU   A 88  ? 0.2538 0.3079 0.2572 -0.0260 -0.0071 0.0003  88  LEU   A CD1 
1847 C CD2 A LEU   A 88  ? 0.2489 0.2816 0.2935 -0.0393 0.0060  0.0580  88  LEU   A CD2 
1848 C CD2 B LEU   A 88  ? 0.2408 0.2995 0.2933 -0.0280 -0.0008 0.0203  88  LEU   A CD2 
1871 N N   . ALA   A 89  ? 0.2243 0.2785 0.1925 -0.0339 0.0181  0.0207  89  ALA   A N   
1872 C CA  . ALA   A 89  ? 0.2407 0.2781 0.1791 -0.0305 -0.0013 0.0327  89  ALA   A CA  
1873 C C   . ALA   A 89  ? 0.2484 0.2805 0.1803 -0.0273 -0.0049 0.0249  89  ALA   A C   
1874 O O   . ALA   A 89  ? 0.2443 0.2671 0.2162 -0.0431 -0.0130 -0.0057 89  ALA   A O   
1875 C CB  . ALA   A 89  ? 0.2343 0.2711 0.1715 -0.0317 -0.0177 0.0365  89  ALA   A CB  
1882 N N   . LYS   A 90  ? 0.2491 0.2896 0.1825 -0.0390 -0.0144 0.0258  90  LYS   A N   
1883 C CA  . LYS   A 90  ? 0.2598 0.3007 0.1919 -0.0264 -0.0369 0.0263  90  LYS   A CA  
1884 C C   . LYS   A 90  ? 0.2384 0.2726 0.1653 -0.0342 -0.0318 0.0147  90  LYS   A C   
1885 O O   . LYS   A 90  ? 0.2405 0.2865 0.1870 -0.0539 -0.0448 0.0304  90  LYS   A O   
1886 C CB  . LYS   A 90  ? 0.2916 0.3355 0.2149 -0.0312 -0.0612 0.0388  90  LYS   A CB  
1887 C CG  . LYS   A 90  ? 0.3486 0.3769 0.3302 -0.0270 -0.0545 0.0486  90  LYS   A CG  
1888 C CD  . LYS   A 90  ? 0.3987 0.4213 0.4476 -0.0308 -0.0479 0.0454  90  LYS   A CD  
1889 C CE  . LYS   A 90  ? 0.4342 0.4529 0.5390 -0.0287 -0.0416 0.0244  90  LYS   A CE  
1890 N NZ  . LYS   A 90  ? 0.4566 0.4632 0.6006 -0.0335 -0.0361 0.0087  90  LYS   A NZ  
1904 N N   . HIS   A 91  ? 0.2181 0.2501 0.1283 -0.0279 -0.0407 0.0211  91  HIS   A N   
1905 C CA  . HIS   A 91  ? 0.2194 0.2466 0.1327 -0.0306 -0.0485 0.0198  91  HIS   A CA  
1906 C C   . HIS   A 91  ? 0.2071 0.2204 0.1154 -0.0299 -0.0209 0.0247  91  HIS   A C   
1907 O O   . HIS   A 91  ? 0.1877 0.2210 0.1707 -0.0316 -0.0113 0.0163  91  HIS   A O   
1908 C CB  . HIS   A 91  ? 0.2442 0.2904 0.2052 -0.0119 -0.0449 0.0115  91  HIS   A CB  
1909 C CG  . HIS   A 91  ? 0.2965 0.3386 0.2987 0.0001  -0.0655 0.0020  91  HIS   A CG  
1910 N ND1 . HIS   A 91  ? 0.3096 0.3599 0.3551 0.0047  -0.0944 -0.0257 91  HIS   A ND1 
1911 C CD2 . HIS   A 91  ? 0.3203 0.3545 0.3455 0.0196  -0.0827 0.0050  91  HIS   A CD2 
1912 C CE1 . HIS   A 91  ? 0.3231 0.3718 0.3844 0.0120  -0.1012 -0.0102 91  HIS   A CE1 
1913 N NE2 . HIS   A 91  ? 0.3315 0.3731 0.3804 0.0266  -0.0968 0.0014  91  HIS   A NE2 
1921 N N   . CYS   A 92  ? 0.1978 0.2045 0.1365 -0.0377 -0.0110 0.0146  92  CYS   A N   
1922 C CA  . CYS   A 92  ? 0.1759 0.1953 0.1683 -0.0311 -0.0065 0.0043  92  CYS   A CA  
1923 C C   . CYS   A 92  ? 0.1733 0.1832 0.1732 -0.0258 0.0009  0.0074  92  CYS   A C   
1924 O O   . CYS   A 92  ? 0.1861 0.1880 0.1640 -0.0316 0.0056  -0.0009 92  CYS   A O   
1925 C CB  . CYS   A 92  ? 0.1756 0.1915 0.1775 -0.0202 0.0021  0.0039  92  CYS   A CB  
1926 S SG  . CYS   A 92  ? 0.1817 0.1846 0.1665 -0.0207 -0.0006 0.0154  92  CYS   A SG  
1932 N N   . LEU   A 93  ? 0.1788 0.1697 0.1618 -0.0193 0.0042  0.0111  93  LEU   A N   
1933 C CA  . LEU   A 93  ? 0.1558 0.1588 0.1558 -0.0223 -0.0010 0.0218  93  LEU   A CA  
1934 C C   . LEU   A 93  ? 0.1632 0.1504 0.1628 -0.0091 -0.0072 0.0149  93  LEU   A C   
1935 O O   . LEU   A 93  ? 0.1586 0.1711 0.1606 -0.0041 0.0023  0.0111  93  LEU   A O   
1936 C CB  . LEU   A 93  ? 0.1745 0.1719 0.1765 -0.0110 -0.0126 0.0257  93  LEU   A CB  
1937 C CG  . LEU   A 93  ? 0.1766 0.1770 0.1622 -0.0230 0.0019  0.0089  93  LEU   A CG  
1938 C CD1 . LEU   A 93  ? 0.1772 0.1872 0.2000 -0.0055 0.0188  0.0082  93  LEU   A CD1 
1939 C CD2 . LEU   A 93  ? 0.1821 0.1659 0.2047 -0.0228 -0.0127 -0.0043 93  LEU   A CD2 
1951 N N   . HIS   A 94  ? 0.1571 0.1526 0.1711 -0.0212 0.0073  0.0223  94  HIS   A N   
1952 C CA  . HIS   A 94  ? 0.1624 0.1628 0.1532 -0.0209 0.0022  0.0254  94  HIS   A CA  
1953 C C   . HIS   A 94  ? 0.1653 0.1505 0.1581 -0.0111 -0.0074 0.0095  94  HIS   A C   
1954 O O   . HIS   A 94  ? 0.1623 0.1592 0.2099 -0.0034 0.0019  -0.0017 94  HIS   A O   
1955 C CB  . HIS   A 94  ? 0.1634 0.1627 0.1411 -0.0058 -0.0038 0.0180  94  HIS   A CB  
1956 C CG  . HIS   A 94  ? 0.1588 0.1660 0.1401 -0.0101 -0.0038 0.0074  94  HIS   A CG  
1957 N ND1 . HIS   A 94  ? 0.1614 0.1556 0.1635 -0.0119 -0.0086 0.0041  94  HIS   A ND1 
1958 C CD2 . HIS   A 94  ? 0.1599 0.1640 0.1644 -0.0119 -0.0023 0.0015  94  HIS   A CD2 
1959 C CE1 . HIS   A 94  ? 0.1559 0.1543 0.1811 -0.0131 -0.0139 0.0060  94  HIS   A CE1 
1960 N NE2 . HIS   A 94  ? 0.1705 0.1584 0.1630 -0.0131 -0.0091 0.0004  94  HIS   A NE2 
1968 N N   . VAL   A 95  ? 0.1574 0.1580 0.1449 -0.0072 0.0043  -0.0068 95  VAL   A N   
1969 C CA  . VAL   A 95  ? 0.1651 0.1590 0.1480 -0.0087 0.0118  0.0017  95  VAL   A CA  
1970 C C   . VAL   A 95  ? 0.1702 0.1443 0.1543 -0.0153 -0.0020 0.0063  95  VAL   A C   
1971 O O   . VAL   A 95  ? 0.1678 0.1631 0.1527 0.0091  -0.0014 0.0061  95  VAL   A O   
1972 C CB  . VAL   A 95  ? 0.1728 0.1601 0.1557 -0.0162 0.0024  0.0084  95  VAL   A CB  
1973 C CG1 . VAL   A 95  ? 0.1788 0.1603 0.1690 -0.0250 0.0009  0.0055  95  VAL   A CG1 
1974 C CG2 . VAL   A 95  ? 0.1698 0.1581 0.1521 -0.0247 0.0040  0.0285  95  VAL   A CG2 
1984 N N   . VAL   A 96  ? 0.1658 0.1559 0.1327 -0.0022 0.0034  0.0031  96  VAL   A N   
1985 C CA  . VAL   A 96  ? 0.1715 0.1553 0.1350 -0.0006 0.0112  0.0078  96  VAL   A CA  
1986 C C   . VAL   A 96  ? 0.1714 0.1684 0.1597 0.0033  0.0108  0.0111  96  VAL   A C   
1987 O O   . VAL   A 96  ? 0.1817 0.1698 0.1621 -0.0032 0.0301  -0.0101 96  VAL   A O   
1988 C CB  . VAL   A 96  ? 0.1786 0.1576 0.1388 -0.0079 0.0125  0.0103  96  VAL   A CB  
1989 C CG1 . VAL   A 96  ? 0.1963 0.1586 0.1395 -0.0139 0.0239  0.0151  96  VAL   A CG1 
1990 C CG2 . VAL   A 96  ? 0.1715 0.1643 0.1790 -0.0014 0.0211  0.0166  96  VAL   A CG2 
2000 N N   A GLY   A 97  ? 0.1829 0.1679 0.1575 0.0036  0.0066  0.0085  97  GLY   A N   
2001 N N   B GLY   A 97  ? 0.1757 0.1672 0.1462 0.0041  -0.0006 0.0128  97  GLY   A N   
2002 C CA  A GLY   A 97  ? 0.1913 0.1776 0.1643 -0.0042 -0.0047 0.0050  97  GLY   A CA  
2003 C CA  B GLY   A 97  ? 0.1775 0.1793 0.1486 -0.0024 -0.0166 0.0132  97  GLY   A CA  
2004 C C   A GLY   A 97  ? 0.1909 0.1796 0.1579 -0.0018 -0.0059 -0.0060 97  GLY   A C   
2005 C C   B GLY   A 97  ? 0.1699 0.1840 0.1314 0.0016  -0.0223 0.0153  97  GLY   A C   
2006 O O   A GLY   A 97  ? 0.1891 0.1672 0.1969 -0.0027 0.0147  -0.0188 97  GLY   A O   
2007 O O   B GLY   A 97  ? 0.1736 0.1859 0.1790 -0.0172 -0.0000 0.0251  97  GLY   A O   
2014 N N   A PRO   A 98  ? 0.1890 0.1730 0.1513 -0.0023 -0.0100 -0.0128 98  PRO   A N   
2015 N N   B PRO   A 98  ? 0.1882 0.1845 0.1318 -0.0007 -0.0073 0.0264  98  PRO   A N   
2016 C CA  A PRO   A 98  ? 0.1798 0.1857 0.1429 -0.0014 0.0020  -0.0140 98  PRO   A CA  
2017 C CA  B PRO   A 98  ? 0.2069 0.1985 0.1215 0.0093  0.0084  0.0084  98  PRO   A CA  
2018 C C   A PRO   A 98  ? 0.1798 0.1910 0.1458 -0.0079 0.0005  0.0049  98  PRO   A C   
2019 C C   B PRO   A 98  ? 0.2260 0.2165 0.1322 0.0069  0.0184  0.0202  98  PRO   A C   
2020 O O   A PRO   A 98  ? 0.1643 0.1866 0.1686 -0.0047 0.0064  0.0122  98  PRO   A O   
2021 O O   B PRO   A 98  ? 0.2172 0.2226 0.1939 0.0043  0.0289  0.0350  98  PRO   A O   
2022 C CB  A PRO   A 98  ? 0.1799 0.2007 0.1431 0.0119  -0.0016 -0.0295 98  PRO   A CB  
2023 C CB  B PRO   A 98  ? 0.2138 0.1984 0.1330 0.0238  0.0078  0.0156  98  PRO   A CB  
2024 C CG  A PRO   A 98  ? 0.1819 0.1918 0.1610 0.0159  -0.0027 -0.0344 98  PRO   A CG  
2025 C CG  B PRO   A 98  ? 0.2084 0.1967 0.1379 0.0142  0.0055  0.0074  98  PRO   A CG  
2026 C CD  A PRO   A 98  ? 0.1904 0.1773 0.1573 0.0021  -0.0092 -0.0242 98  PRO   A CD  
2027 C CD  B PRO   A 98  ? 0.1981 0.1834 0.1309 -0.0020 -0.0080 0.0249  98  PRO   A CD  
2042 N N   A ASN   A 99  ? 0.1856 0.2011 0.1411 -0.0138 0.0066  0.0216  99  ASN   A N   
2043 N N   B ASN   A 99  ? 0.2459 0.2246 0.1374 0.0163  0.0050  0.0303  99  ASN   A N   
2044 C CA  A ASN   A 99  ? 0.2099 0.2211 0.1283 -0.0084 0.0044  0.0282  99  ASN   A CA  
2045 C CA  B ASN   A 99  ? 0.2727 0.2223 0.1823 0.0246  0.0076  0.0256  99  ASN   A CA  
2046 C C   A ASN   A 99  ? 0.2450 0.2501 0.1574 -0.0133 0.0065  0.0371  99  ASN   A C   
2047 C C   B ASN   A 99  ? 0.2837 0.2258 0.1822 0.0295  0.0019  0.0497  99  ASN   A C   
2048 O O   A ASN   A 99  ? 0.2603 0.2729 0.1787 -0.0001 0.0205  0.0068  99  ASN   A O   
2049 O O   B ASN   A 99  ? 0.2798 0.2139 0.1740 0.0358  -0.0119 0.0476  99  ASN   A O   
2050 C CB  A ASN   A 99  ? 0.2107 0.2138 0.1104 -0.0019 -0.0262 0.0383  99  ASN   A CB  
2051 C CB  B ASN   A 99  ? 0.2819 0.2105 0.2113 0.0319  0.0155  0.0228  99  ASN   A CB  
2052 C CG  A ASN   A 99  ? 0.2101 0.2221 0.1237 0.0055  -0.0347 0.0218  99  ASN   A CG  
2053 C CG  B ASN   A 99  ? 0.2980 0.2069 0.2390 0.0248  0.0131  0.0324  99  ASN   A CG  
2054 O OD1 A ASN   A 99  ? 0.2262 0.2252 0.1547 0.0084  -0.0295 0.0154  99  ASN   A OD1 
2055 O OD1 B ASN   A 99  ? 0.2894 0.2167 0.2278 0.0430  0.0110  0.0360  99  ASN   A OD1 
2056 N ND2 A ASN   A 99  ? 0.2081 0.2197 0.1770 -0.0009 -0.0262 0.0360  99  ASN   A ND2 
2057 N ND2 B ASN   A 99  ? 0.3180 0.2129 0.3261 0.0134  -0.0117 0.0267  99  ASN   A ND2 
2070 N N   A VAL   A 100 ? 0.2597 0.2561 0.1410 -0.0258 -0.0154 0.0436  100 VAL   A N   
2071 N N   B VAL   A 100 ? 0.3086 0.2603 0.2236 0.0165  -0.0069 0.0547  100 VAL   A N   
2072 C CA  A VAL   A 100 ? 0.2799 0.2744 0.1570 -0.0300 -0.0250 0.0460  100 VAL   A CA  
2073 C CA  B VAL   A 100 ? 0.3477 0.2930 0.2664 0.0285  -0.0246 0.0593  100 VAL   A CA  
2074 C C   A VAL   A 100 ? 0.2990 0.3033 0.1577 -0.0357 -0.0385 0.0667  100 VAL   A C   
2075 C C   B VAL   A 100 ? 0.3750 0.3086 0.2867 0.0472  -0.0387 0.0595  100 VAL   A C   
2076 O O   A VAL   A 100 ? 0.3082 0.3161 0.1660 -0.0384 -0.0368 0.0869  100 VAL   A O   
2077 O O   B VAL   A 100 ? 0.3897 0.3169 0.3126 0.0415  -0.0334 0.0454  100 VAL   A O   
2078 C CB  A VAL   A 100 ? 0.2877 0.2635 0.1959 -0.0349 -0.0455 0.0292  100 VAL   A CB  
2079 C CB  B VAL   A 100 ? 0.3566 0.3141 0.3249 0.0168  -0.0258 0.0442  100 VAL   A CB  
2080 C CG1 A VAL   A 100 ? 0.2876 0.2768 0.2192 -0.0271 -0.0344 0.0463  100 VAL   A CG1 
2081 C CG1 B VAL   A 100 ? 0.3650 0.3282 0.3472 0.0075  -0.0266 0.0350  100 VAL   A CG1 
2082 C CG2 A VAL   A 100 ? 0.2958 0.2524 0.2042 -0.0329 -0.0505 0.0257  100 VAL   A CG2 
2083 C CG2 B VAL   A 100 ? 0.3634 0.3256 0.3649 0.0109  -0.0181 0.0491  100 VAL   A CG2 
2102 N N   A ASN   A 101 ? 0.3053 0.3119 0.1726 -0.0441 -0.0380 0.0887  101 ASN   A N   
2103 N N   B ASN   A 101 ? 0.3902 0.3239 0.2813 0.0561  -0.0415 0.0588  101 ASN   A N   
2104 C CA  A ASN   A 101 ? 0.3126 0.3309 0.2072 -0.0383 -0.0447 0.0939  101 ASN   A CA  
2105 C CA  B ASN   A 101 ? 0.4002 0.3338 0.2857 0.0667  -0.0500 0.0811  101 ASN   A CA  
2106 C C   A ASN   A 101 ? 0.3256 0.3580 0.2300 -0.0464 -0.0149 0.1059  101 ASN   A C   
2107 C C   B ASN   A 101 ? 0.4149 0.3476 0.3128 0.0634  -0.0271 0.1003  101 ASN   A C   
2108 O O   A ASN   A 101 ? 0.3414 0.3661 0.2653 -0.0415 -0.0097 0.0936  101 ASN   A O   
2109 O O   B ASN   A 101 ? 0.4191 0.3479 0.3462 0.0692  -0.0083 0.1130  101 ASN   A O   
2110 C CB  A ASN   A 101 ? 0.3025 0.3220 0.2021 -0.0326 -0.0564 0.0879  101 ASN   A CB  
2111 C CB  B ASN   A 101 ? 0.4052 0.3345 0.2877 0.0674  -0.0442 0.0746  101 ASN   A CB  
2112 C CG  A ASN   A 101 ? 0.2984 0.3198 0.2007 -0.0220 -0.0628 0.0651  101 ASN   A CG  
2113 C CG  B ASN   A 101 ? 0.4096 0.3291 0.3082 0.0679  -0.0405 0.0714  101 ASN   A CG  
2114 O OD1 A ASN   A 101 ? 0.2882 0.3258 0.1938 -0.0070 -0.0587 0.0445  101 ASN   A OD1 
2115 O OD1 B ASN   A 101 ? 0.4149 0.3405 0.3316 0.0631  -0.0595 0.0634  101 ASN   A OD1 
2116 N ND2 A ASN   A 101 ? 0.3025 0.3131 0.1925 -0.0287 -0.0692 0.0638  101 ASN   A ND2 
2117 N ND2 B ASN   A 101 ? 0.4052 0.3203 0.3155 0.0742  -0.0282 0.0852  101 ASN   A ND2 
2130 N N   A LYS   A 102 ? 0.3202 0.3800 0.2469 -0.0598 0.0160  0.1012  102 LYS   A N   
2131 N N   B LYS   A 102 ? 0.4213 0.3677 0.3395 0.0503  -0.0196 0.0724  102 LYS   A N   
2132 C CA  A LYS   A 102 ? 0.3210 0.3981 0.2496 -0.0710 0.0155  0.0928  102 LYS   A CA  
2133 C CA  B LYS   A 102 ? 0.4368 0.3897 0.3361 0.0330  -0.0039 0.0616  102 LYS   A CA  
2134 C C   A LYS   A 102 ? 0.3394 0.4217 0.2634 -0.0623 0.0029  0.0703  102 LYS   A C   
2135 C C   B LYS   A 102 ? 0.4314 0.3766 0.2977 0.0245  -0.0120 0.0670  102 LYS   A C   
2136 O O   A LYS   A 102 ? 0.3449 0.4346 0.2931 -0.0579 0.0028  0.0497  102 LYS   A O   
2137 O O   B LYS   A 102 ? 0.4370 0.3757 0.3234 0.0111  -0.0186 0.0657  102 LYS   A O   
2138 C CB  A LYS   A 102 ? 0.3218 0.4001 0.2621 -0.0862 0.0129  0.0893  102 LYS   A CB  
2139 C CB  B LYS   A 102 ? 0.4580 0.4223 0.4086 0.0185  0.0035  0.0299  102 LYS   A CB  
2140 C CG  A LYS   A 102 ? 0.3165 0.4006 0.2731 -0.1035 0.0093  0.0848  102 LYS   A CG  
2141 C CG  B LYS   A 102 ? 0.4730 0.4467 0.4664 0.0118  0.0062  0.0124  102 LYS   A CG  
2142 C CD  A LYS   A 102 ? 0.3175 0.4061 0.2983 -0.1069 0.0106  0.0650  102 LYS   A CD  
2143 C CD  B LYS   A 102 ? 0.4835 0.4690 0.5128 0.0064  0.0004  0.0053  102 LYS   A CD  
2144 C CE  A LYS   A 102 ? 0.3197 0.4072 0.3151 -0.1044 0.0117  0.0418  102 LYS   A CE  
2145 C CE  B LYS   A 102 ? 0.4910 0.4837 0.5454 -0.0037 -0.0078 0.0010  102 LYS   A CE  
2146 N NZ  A LYS   A 102 ? 0.3228 0.4103 0.3093 -0.1061 0.0180  0.0253  102 LYS   A NZ  
2147 N NZ  B LYS   A 102 ? 0.4975 0.4947 0.5656 -0.0088 -0.0110 -0.0002 102 LYS   A NZ  
2174 N N   A GLY   A 103 ? 0.3433 0.4316 0.2671 -0.0556 -0.0049 0.0499  103 GLY   A N   
2175 N N   B GLY   A 103 ? 0.4195 0.3669 0.2507 0.0294  -0.0212 0.0529  103 GLY   A N   
2176 C CA  A GLY   A 103 ? 0.3527 0.4385 0.2793 -0.0445 -0.0061 0.0308  103 GLY   A CA  
2177 C CA  B GLY   A 103 ? 0.4054 0.3518 0.2413 0.0297  -0.0249 0.0540  103 GLY   A CA  
2178 C C   A GLY   A 103 ? 0.3530 0.4421 0.2898 -0.0363 0.0085  0.0224  103 GLY   A C   
2179 C C   B GLY   A 103 ? 0.3826 0.3359 0.2128 0.0233  -0.0262 0.0509  103 GLY   A C   
2180 O O   A GLY   A 103 ? 0.3685 0.4490 0.3090 -0.0312 0.0029  0.0136  103 GLY   A O   
2181 O O   B GLY   A 103 ? 0.3929 0.3350 0.2177 0.0257  -0.0338 0.0347  103 GLY   A O   
2188 N N   A GLU   A 104 ? 0.3338 0.4341 0.2558 -0.0430 0.0315  0.0194  104 GLU   A N   
2189 N N   B GLU   A 104 ? 0.3489 0.3172 0.1837 0.0225  -0.0285 0.0672  104 GLU   A N   
2190 C CA  A GLU   A 104 ? 0.3110 0.4223 0.2308 -0.0551 0.0441  0.0177  104 GLU   A CA  
2191 C CA  B GLU   A 104 ? 0.3200 0.2922 0.1629 0.0090  -0.0268 0.0588  104 GLU   A CA  
2192 C C   A GLU   A 104 ? 0.3090 0.4294 0.2290 -0.0572 0.0460  0.0002  104 GLU   A C   
2193 C C   B GLU   A 104 ? 0.3205 0.2783 0.1537 0.0071  -0.0298 0.0447  104 GLU   A C   
2194 O O   A GLU   A 104 ? 0.3007 0.4307 0.2475 -0.0640 0.0436  -0.0178 104 GLU   A O   
2195 O O   B GLU   A 104 ? 0.3273 0.2709 0.2066 0.0054  -0.0241 0.0153  104 GLU   A O   
2196 C CB  A GLU   A 104 ? 0.2851 0.4035 0.2100 -0.0676 0.0488  0.0336  104 GLU   A CB  
2197 C CB  B GLU   A 104 ? 0.2912 0.2853 0.1745 -0.0061 -0.0130 0.0704  104 GLU   A CB  
2198 C CG  A GLU   A 104 ? 0.2733 0.3883 0.2120 -0.0617 0.0298  0.0303  104 GLU   A CG  
2199 C CG  B GLU   A 104 ? 0.2872 0.2894 0.2048 -0.0130 -0.0167 0.0796  104 GLU   A CG  
2200 C CD  A GLU   A 104 ? 0.2606 0.3731 0.2003 -0.0530 0.0262  0.0382  104 GLU   A CD  
2201 C CD  B GLU   A 104 ? 0.2888 0.2901 0.1993 -0.0220 -0.0217 0.0849  104 GLU   A CD  
2202 O OE1 A GLU   A 104 ? 0.2524 0.3665 0.1841 -0.0494 0.0180  0.0421  104 GLU   A OE1 
2203 O OE1 B GLU   A 104 ? 0.2954 0.2790 0.1919 -0.0219 -0.0251 0.0709  104 GLU   A OE1 
2204 O OE2 A GLU   A 104 ? 0.2655 0.3672 0.1978 -0.0374 0.0352  0.0421  104 GLU   A OE2 
2205 O OE2 B GLU   A 104 ? 0.2914 0.3025 0.2177 -0.0328 -0.0138 0.0908  104 GLU   A OE2 
2218 N N   A ASP   A 105 ? 0.3207 0.4364 0.2387 -0.0460 0.0434  -0.0220 105 ASP   A N   
2219 N N   B ASP   A 105 ? 0.3285 0.2745 0.1794 0.0037  -0.0293 0.0406  105 ASP   A N   
2220 C CA  A ASP   A 105 ? 0.3300 0.4393 0.2518 -0.0361 0.0420  -0.0424 105 ASP   A CA  
2221 C CA  B ASP   A 105 ? 0.3348 0.2823 0.2208 0.0064  -0.0071 0.0236  105 ASP   A CA  
2222 C C   A ASP   A 105 ? 0.3063 0.4214 0.2179 -0.0474 0.0288  -0.0684 105 ASP   A C   
2223 C C   B ASP   A 105 ? 0.3180 0.2695 0.2032 -0.0120 0.0066  0.0219  105 ASP   A C   
2224 O O   A ASP   A 105 ? 0.3005 0.4239 0.1999 -0.0521 0.0179  -0.0905 105 ASP   A O   
2225 O O   B ASP   A 105 ? 0.3012 0.2515 0.1734 -0.0036 0.0118  0.0088  105 ASP   A O   
2226 C CB  A ASP   A 105 ? 0.3560 0.4553 0.3019 -0.0180 0.0533  -0.0400 105 ASP   A CB  
2227 C CB  B ASP   A 105 ? 0.3459 0.2944 0.2735 0.0237  -0.0038 0.0076  105 ASP   A CB  
2228 C CG  A ASP   A 105 ? 0.3849 0.4699 0.3488 -0.0049 0.0557  -0.0390 105 ASP   A CG  
2229 C CG  B ASP   A 105 ? 0.3588 0.3029 0.3247 0.0490  0.0014  -0.0136 105 ASP   A CG  
2230 O OD1 A ASP   A 105 ? 0.3942 0.4750 0.3487 -0.0028 0.0469  -0.0536 105 ASP   A OD1 
2231 O OD1 B ASP   A 105 ? 0.3626 0.3021 0.3093 0.0444  -0.0134 -0.0245 105 ASP   A OD1 
2232 O OD2 A ASP   A 105 ? 0.4019 0.4761 0.3846 0.0029  0.0609  -0.0272 105 ASP   A OD2 
2233 O OD2 B ASP   A 105 ? 0.3641 0.3111 0.3748 0.0636  -0.0023 -0.0082 105 ASP   A OD2 
2242 N N   A ILE   A 106 ? 0.2900 0.3998 0.2217 -0.0503 0.0104  -0.0783 106 ILE   A N   
2243 N N   B ILE   A 106 ? 0.3240 0.2884 0.2257 -0.0218 -0.0088 0.0331  106 ILE   A N   
2244 C CA  A ILE   A 106 ? 0.2592 0.3738 0.2331 -0.0589 -0.0251 -0.1041 106 ILE   A CA  
2245 C CA  B ILE   A 106 ? 0.3325 0.2883 0.2681 -0.0348 -0.0202 0.0334  106 ILE   A CA  
2246 C C   A ILE   A 106 ? 0.2457 0.3490 0.2434 -0.0644 -0.0318 -0.1315 106 ILE   A C   
2247 C C   B ILE   A 106 ? 0.3326 0.2699 0.2668 -0.0384 -0.0077 0.0522  106 ILE   A C   
2248 O O   A ILE   A 106 ? 0.2256 0.3348 0.2655 -0.0694 -0.0305 -0.1304 106 ILE   A O   
2249 O O   B ILE   A 106 ? 0.3219 0.2593 0.2780 -0.0426 0.0036  0.0620  106 ILE   A O   
2250 C CB  A ILE   A 106 ? 0.2596 0.3784 0.2523 -0.0534 -0.0563 -0.0774 106 ILE   A CB  
2251 C CB  B ILE   A 106 ? 0.3437 0.3073 0.3024 -0.0429 -0.0377 0.0149  106 ILE   A CB  
2252 C CG1 A ILE   A 106 ? 0.2637 0.3764 0.2825 -0.0427 -0.0639 -0.0546 106 ILE   A CG1 
2253 C CG1 B ILE   A 106 ? 0.3387 0.3175 0.3237 -0.0417 -0.0478 0.0053  106 ILE   A CG1 
2254 C CG2 A ILE   A 106 ? 0.2633 0.3828 0.2628 -0.0531 -0.0750 -0.0780 106 ILE   A CG2 
2255 C CG2 B ILE   A 106 ? 0.3528 0.3107 0.3213 -0.0399 -0.0430 0.0088  106 ILE   A CG2 
2256 C CD1 A ILE   A 106 ? 0.2732 0.3767 0.2968 -0.0343 -0.0671 -0.0394 106 ILE   A CD1 
2257 C CD1 B ILE   A 106 ? 0.3320 0.3218 0.3416 -0.0476 -0.0517 -0.0027 106 ILE   A CD1 
2280 N N   A GLN   A 107 ? 0.2636 0.3365 0.2701 -0.0562 -0.0153 -0.1470 107 GLN   A N   
2281 N N   B GLN   A 107 ? 0.3441 0.2618 0.2717 -0.0374 -0.0048 0.0438  107 GLN   A N   
2282 C CA  A GLN   A 107 ? 0.2835 0.3190 0.3411 -0.0395 0.0104  -0.1314 107 GLN   A CA  
2283 C CA  B GLN   A 107 ? 0.3586 0.2768 0.3294 -0.0345 0.0046  0.0389  107 GLN   A CA  
2284 C C   A GLN   A 107 ? 0.2539 0.2785 0.3381 -0.0278 0.0336  -0.0930 107 GLN   A C   
2285 C C   B GLN   A 107 ? 0.3318 0.2481 0.3015 -0.0279 0.0120  0.0369  107 GLN   A C   
2286 O O   A GLN   A 107 ? 0.2545 0.2695 0.4089 -0.0168 0.0419  -0.0907 107 GLN   A O   
2287 O O   B GLN   A 107 ? 0.3374 0.2453 0.3214 -0.0271 0.0085  0.0406  107 GLN   A O   
2288 C CB  A GLN   A 107 ? 0.3266 0.3480 0.4211 -0.0403 -0.0024 -0.1249 107 GLN   A CB  
2289 C CB  B GLN   A 107 ? 0.3968 0.3204 0.4080 -0.0434 -0.0044 0.0348  107 GLN   A CB  
2290 C CG  A GLN   A 107 ? 0.3710 0.3816 0.5090 -0.0414 -0.0132 -0.1041 107 GLN   A CG  
2291 C CG  B GLN   A 107 ? 0.4300 0.3672 0.4926 -0.0474 -0.0171 0.0393  107 GLN   A CG  
2292 C CD  A GLN   A 107 ? 0.4052 0.4051 0.5814 -0.0386 -0.0158 -0.0823 107 GLN   A CD  
2293 C CD  B GLN   A 107 ? 0.4562 0.4089 0.5721 -0.0491 -0.0245 0.0421  107 GLN   A CD  
2294 O OE1 A GLN   A 107 ? 0.4167 0.4200 0.6209 -0.0322 -0.0179 -0.0753 107 GLN   A OE1 
2295 O OE1 B GLN   A 107 ? 0.4673 0.4196 0.5938 -0.0477 -0.0261 0.0510  107 GLN   A OE1 
2296 N NE2 A GLN   A 107 ? 0.4163 0.4140 0.6013 -0.0404 -0.0157 -0.0808 107 GLN   A NE2 
2297 N NE2 B GLN   A 107 ? 0.4613 0.4179 0.5995 -0.0541 -0.0278 0.0394  107 GLN   A NE2 
2314 N N   A LEU   A 108 ? 0.2241 0.2404 0.2664 -0.0253 0.0388  -0.0951 108 LEU   A N   
2315 N N   B LEU   A 108 ? 0.2983 0.2296 0.2529 -0.0226 0.0169  0.0109  108 LEU   A N   
2316 C CA  A LEU   A 108 ? 0.2126 0.2167 0.2263 -0.0181 0.0300  -0.0404 108 LEU   A CA  
2317 C CA  B LEU   A 108 ? 0.2661 0.2139 0.2276 -0.0120 0.0232  0.0229  108 LEU   A CA  
2318 C C   A LEU   A 108 ? 0.2051 0.1962 0.2155 -0.0096 0.0189  -0.0046 108 LEU   A C   
2319 C C   B LEU   A 108 ? 0.2348 0.1970 0.2175 -0.0048 0.0144  0.0365  108 LEU   A C   
2320 O O   A LEU   A 108 ? 0.1830 0.1868 0.2237 0.0003  0.0179  -0.0253 108 LEU   A O   
2321 O O   B LEU   A 108 ? 0.2223 0.1962 0.2386 0.0093  0.0121  0.0408  108 LEU   A O   
2322 C CB  A LEU   A 108 ? 0.2220 0.2253 0.2071 -0.0304 0.0402  -0.0411 108 LEU   A CB  
2323 C CB  B LEU   A 108 ? 0.2763 0.2275 0.2109 -0.0160 0.0455  0.0095  108 LEU   A CB  
2324 C CG  A LEU   A 108 ? 0.2338 0.2510 0.2365 -0.0385 0.0362  -0.0369 108 LEU   A CG  
2325 C CG  B LEU   A 108 ? 0.2883 0.2543 0.2427 -0.0170 0.0523  0.0019  108 LEU   A CG  
2326 C CD1 A LEU   A 108 ? 0.2485 0.2568 0.2489 -0.0467 0.0437  -0.0258 108 LEU   A CD1 
2327 C CD1 B LEU   A 108 ? 0.3012 0.2579 0.2483 -0.0193 0.0657  0.0046  108 LEU   A CD1 
2328 C CD2 A LEU   A 108 ? 0.2405 0.2734 0.2821 -0.0326 0.0368  -0.0262 108 LEU   A CD2 
2329 C CD2 B LEU   A 108 ? 0.2946 0.2783 0.2910 -0.0144 0.0542  0.0062  108 LEU   A CD2 
2352 N N   . LEU   A 109 ? 0.2110 0.1887 0.2036 -0.0025 0.0063  0.0088  109 LEU   A N   
2353 C CA  . LEU   A 109 ? 0.2048 0.1893 0.1861 0.0032  -0.0115 0.0126  109 LEU   A CA  
2354 C C   . LEU   A 109 ? 0.1831 0.1944 0.1776 -0.0001 -0.0010 -0.0097 109 LEU   A C   
2355 O O   . LEU   A 109 ? 0.1901 0.1790 0.1869 -0.0036 -0.0090 -0.0006 109 LEU   A O   
2356 C CB  . LEU   A 109 ? 0.2108 0.2099 0.2165 0.0169  -0.0171 0.0190  109 LEU   A CB  
2357 C CG  . LEU   A 109 ? 0.2030 0.2175 0.2369 0.0104  -0.0051 0.0150  109 LEU   A CG  
2358 C CD1 . LEU   A 109 ? 0.2064 0.2027 0.2296 0.0028  -0.0074 -0.0136 109 LEU   A CD1 
2359 C CD2 . LEU   A 109 ? 0.1905 0.2340 0.2728 -0.0013 -0.0340 0.0227  109 LEU   A CD2 
2372 N N   . LYS   A 110 ? 0.1755 0.1885 0.1935 0.0071  -0.0263 -0.0010 110 LYS   A N   
2373 C CA  . LYS   A 110 ? 0.1686 0.1667 0.2085 0.0001  -0.0245 -0.0057 110 LYS   A CA  
2374 C C   . LYS   A 110 ? 0.1796 0.1419 0.2116 -0.0108 -0.0095 0.0150  110 LYS   A C   
2375 O O   . LYS   A 110 ? 0.1710 0.1479 0.2287 -0.0060 -0.0180 0.0156  110 LYS   A O   
2376 C CB  . LYS   A 110 ? 0.1928 0.1803 0.2365 -0.0042 -0.0306 -0.0015 110 LYS   A CB  
2377 C CG  . LYS   A 110 ? 0.2014 0.1793 0.2600 -0.0024 -0.0287 -0.0074 110 LYS   A CG  
2378 C CD  . LYS   A 110 ? 0.1955 0.1863 0.2705 -0.0197 -0.0078 -0.0096 110 LYS   A CD  
2379 C CE  . LYS   A 110 ? 0.1962 0.1988 0.2737 -0.0295 -0.0020 0.0039  110 LYS   A CE  
2380 N NZ  . LYS   A 110 ? 0.2039 0.2029 0.3008 -0.0345 -0.0098 -0.0048 110 LYS   A NZ  
2394 N N   . SER   A 111 ? 0.1846 0.1531 0.2183 -0.0081 -0.0078 0.0178  111 SER   A N   
2395 C CA  . SER   A 111 ? 0.1763 0.1597 0.1968 -0.0051 0.0043  0.0026  111 SER   A CA  
2396 C C   . SER   A 111 ? 0.1787 0.1605 0.1909 -0.0040 0.0008  0.0122  111 SER   A C   
2397 O O   . SER   A 111 ? 0.1866 0.1603 0.2004 -0.0075 0.0024  0.0109  111 SER   A O   
2398 C CB  . SER   A 111 ? 0.1870 0.1900 0.2016 0.0005  0.0291  -0.0185 111 SER   A CB  
2399 O OG  . SER   A 111 ? 0.2230 0.2054 0.2268 0.0073  0.0168  -0.0233 111 SER   A OG  
2405 N N   . ALA   A 112 ? 0.1648 0.1378 0.2197 -0.0029 0.0008  0.0118  112 ALA   A N   
2406 C CA  . ALA   A 112 ? 0.1775 0.1390 0.2175 -0.0058 0.0085  0.0110  112 ALA   A CA  
2407 C C   . ALA   A 112 ? 0.1702 0.1264 0.2042 0.0035  -0.0012 0.0148  112 ALA   A C   
2408 O O   . ALA   A 112 ? 0.1832 0.1507 0.1767 -0.0092 0.0101  0.0117  112 ALA   A O   
2409 C CB  . ALA   A 112 ? 0.1863 0.1440 0.2303 -0.0083 0.0068  0.0107  112 ALA   A CB  
2415 N N   . TYR   A 113 ? 0.1588 0.1514 0.2096 -0.0095 -0.0036 0.0257  113 TYR   A N   
2416 C CA  . TYR   A 113 ? 0.1710 0.1417 0.1895 -0.0144 0.0082  0.0266  113 TYR   A CA  
2417 C C   . TYR   A 113 ? 0.1713 0.1461 0.1766 -0.0189 0.0084  0.0293  113 TYR   A C   
2418 O O   . TYR   A 113 ? 0.1703 0.1489 0.1865 -0.0081 0.0055  0.0214  113 TYR   A O   
2419 C CB  . TYR   A 113 ? 0.1745 0.1655 0.2118 -0.0211 -0.0096 0.0311  113 TYR   A CB  
2420 C CG  . TYR   A 113 ? 0.1723 0.1784 0.1673 -0.0191 -0.0081 0.0262  113 TYR   A CG  
2421 C CD1 . TYR   A 113 ? 0.1706 0.2060 0.1851 -0.0001 -0.0060 0.0149  113 TYR   A CD1 
2422 C CD2 . TYR   A 113 ? 0.1725 0.1925 0.1957 -0.0219 -0.0002 0.0319  113 TYR   A CD2 
2423 C CE1 . TYR   A 113 ? 0.1782 0.2164 0.1687 -0.0051 0.0037  0.0124  113 TYR   A CE1 
2424 C CE2 . TYR   A 113 ? 0.1828 0.2013 0.2031 -0.0101 -0.0154 0.0202  113 TYR   A CE2 
2425 C CZ  . TYR   A 113 ? 0.1738 0.2207 0.1724 0.0012  -0.0015 0.0161  113 TYR   A CZ  
2426 O OH  . TYR   A 113 ? 0.1753 0.2305 0.2061 0.0035  0.0005  0.0115  113 TYR   A OH  
2436 N N   . GLU   A 114 ? 0.1625 0.1508 0.1766 -0.0117 0.0014  0.0173  114 GLU   A N   
2437 C CA  . GLU   A 114 ? 0.1736 0.1475 0.1746 -0.0064 -0.0007 0.0227  114 GLU   A CA  
2438 C C   . GLU   A 114 ? 0.1560 0.1627 0.1728 -0.0040 -0.0151 0.0086  114 GLU   A C   
2439 O O   . GLU   A 114 ? 0.1687 0.1631 0.1859 -0.0122 -0.0131 0.0223  114 GLU   A O   
2440 C CB  . GLU   A 114 ? 0.1722 0.1553 0.1793 -0.0100 -0.0139 0.0107  114 GLU   A CB  
2441 C CG  . GLU   A 114 ? 0.1787 0.1589 0.2146 -0.0140 -0.0085 -0.0023 114 GLU   A CG  
2442 C CD  . GLU   A 114 ? 0.1842 0.1447 0.2288 -0.0159 -0.0219 0.0025  114 GLU   A CD  
2443 O OE1 . GLU   A 114 ? 0.1855 0.1403 0.2356 -0.0139 0.0006  -0.0021 114 GLU   A OE1 
2444 O OE2 . GLU   A 114 ? 0.2166 0.1531 0.2677 -0.0191 -0.0224 -0.0138 114 GLU   A OE2 
2451 N N   . ASN   A 115 ? 0.1588 0.1568 0.1888 -0.0152 0.0008  0.0133  115 ASN   A N   
2452 C CA  . ASN   A 115 ? 0.1630 0.1538 0.1960 -0.0100 0.0012  0.0097  115 ASN   A CA  
2453 C C   . ASN   A 115 ? 0.1676 0.1590 0.1963 -0.0197 -0.0155 0.0189  115 ASN   A C   
2454 O O   . ASN   A 115 ? 0.1660 0.1689 0.1957 -0.0224 -0.0063 0.0252  115 ASN   A O   
2455 C CB  . ASN   A 115 ? 0.1785 0.1575 0.1801 -0.0155 -0.0072 0.0175  115 ASN   A CB  
2456 C CG  . ASN   A 115 ? 0.1690 0.1740 0.1926 -0.0226 -0.0063 -0.0030 115 ASN   A CG  
2457 O OD1 . ASN   A 115 ? 0.1869 0.2863 0.2071 -0.0197 0.0097  0.0259  115 ASN   A OD1 
2458 N ND2 . ASN   A 115 ? 0.1676 0.1730 0.2153 -0.0281 0.0121  -0.0090 115 ASN   A ND2 
2465 N N   . PHE   A 116 ? 0.1608 0.1718 0.2051 -0.0201 -0.0065 0.0245  116 PHE   A N   
2466 C CA  . PHE   A 116 ? 0.1728 0.1855 0.1848 -0.0066 0.0134  0.0315  116 PHE   A CA  
2467 C C   . PHE   A 116 ? 0.1699 0.1808 0.1832 -0.0149 0.0143  0.0275  116 PHE   A C   
2468 O O   . PHE   A 116 ? 0.1757 0.1800 0.2011 -0.0059 -0.0034 0.0413  116 PHE   A O   
2469 C CB  . PHE   A 116 ? 0.1652 0.1771 0.1918 -0.0075 0.0139  0.0312  116 PHE   A CB  
2470 C CG  . PHE   A 116 ? 0.1667 0.1729 0.1770 -0.0070 0.0094  0.0322  116 PHE   A CG  
2471 C CD1 . PHE   A 116 ? 0.1826 0.1513 0.1830 -0.0134 0.0088  0.0017  116 PHE   A CD1 
2472 C CD2 . PHE   A 116 ? 0.1836 0.1842 0.2020 -0.0086 -0.0017 0.0268  116 PHE   A CD2 
2473 C CE1 . PHE   A 116 ? 0.1737 0.1436 0.1941 -0.0257 -0.0059 0.0071  116 PHE   A CE1 
2474 C CE2 . PHE   A 116 ? 0.1736 0.1819 0.2305 -0.0083 -0.0018 0.0261  116 PHE   A CE2 
2475 C CZ  . PHE   A 116 ? 0.1766 0.1502 0.2215 -0.0016 -0.0126 0.0338  116 PHE   A CZ  
2485 N N   . ASN   A 117 ? 0.1694 0.1628 0.1893 -0.0137 -0.0007 0.0262  117 ASN   A N   
2486 C CA  . ASN   A 117 ? 0.1786 0.1751 0.2006 -0.0091 0.0036  0.0275  117 ASN   A CA  
2487 C C   . ASN   A 117 ? 0.1781 0.1808 0.2138 -0.0067 -0.0107 0.0481  117 ASN   A C   
2488 O O   . ASN   A 117 ? 0.1870 0.1778 0.2570 -0.0036 -0.0096 0.0581  117 ASN   A O   
2489 C CB  . ASN   A 117 ? 0.1911 0.1717 0.1972 -0.0152 -0.0016 0.0277  117 ASN   A CB  
2490 C CG  . ASN   A 117 ? 0.1849 0.1741 0.2213 -0.0057 0.0014  0.0212  117 ASN   A CG  
2491 O OD1 . ASN   A 117 ? 0.1866 0.1912 0.2185 -0.0259 0.0008  0.0231  117 ASN   A OD1 
2492 N ND2 . ASN   A 117 ? 0.1790 0.1504 0.2427 -0.0150 -0.0052 0.0254  117 ASN   A ND2 
2499 N N   . GLN   A 118 ? 0.1742 0.1823 0.2373 -0.0269 -0.0213 0.0398  118 GLN   A N   
2500 C CA  . GLN   A 118 ? 0.1901 0.1897 0.2284 -0.0284 -0.0353 0.0441  118 GLN   A CA  
2501 C C   . GLN   A 118 ? 0.1933 0.1818 0.2372 -0.0291 -0.0306 0.0394  118 GLN   A C   
2502 O O   . GLN   A 118 ? 0.1986 0.2183 0.2553 -0.0193 -0.0323 0.0222  118 GLN   A O   
2503 C CB  . GLN   A 118 ? 0.1882 0.1878 0.2346 -0.0179 -0.0222 0.0360  118 GLN   A CB  
2504 C CG  . GLN   A 118 ? 0.1728 0.1912 0.2365 -0.0153 -0.0247 0.0378  118 GLN   A CG  
2505 C CD  . GLN   A 118 ? 0.1700 0.1945 0.2465 -0.0086 -0.0251 0.0253  118 GLN   A CD  
2506 O OE1 . GLN   A 118 ? 0.1776 0.2137 0.2585 0.0077  -0.0273 0.0106  118 GLN   A OE1 
2507 N NE2 . GLN   A 118 ? 0.1732 0.1878 0.2368 -0.0035 -0.0218 0.0168  118 GLN   A NE2 
2516 N N   . HIS   A 119 ? 0.1779 0.1783 0.2311 -0.0200 -0.0131 0.0359  119 HIS   A N   
2517 C CA  . HIS   A 119 ? 0.1904 0.1984 0.2258 -0.0255 -0.0207 0.0353  119 HIS   A CA  
2518 C C   . HIS   A 119 ? 0.2190 0.2062 0.1830 -0.0353 -0.0250 0.0465  119 HIS   A C   
2519 O O   . HIS   A 119 ? 0.2219 0.2140 0.1942 -0.0479 -0.0465 0.0537  119 HIS   A O   
2520 C CB  . HIS   A 119 ? 0.1912 0.2038 0.2324 -0.0195 0.0222  0.0461  119 HIS   A CB  
2521 C CG  . HIS   A 119 ? 0.1941 0.2037 0.2741 -0.0176 0.0092  0.0397  119 HIS   A CG  
2522 N ND1 . HIS   A 119 ? 0.2010 0.2138 0.3400 -0.0291 0.0023  0.0232  119 HIS   A ND1 
2523 C CD2 . HIS   A 119 ? 0.2009 0.2064 0.2887 0.0055  0.0190  0.0390  119 HIS   A CD2 
2524 C CE1 . HIS   A 119 ? 0.2038 0.2077 0.3514 -0.0338 0.0199  0.0483  119 HIS   A CE1 
2525 N NE2 . HIS   A 119 ? 0.2159 0.2119 0.3397 -0.0117 0.0414  0.0690  119 HIS   A NE2 
2533 N N   . GLU   A 120 ? 0.2324 0.2386 0.2017 -0.0425 -0.0316 0.0710  120 GLU   A N   
2534 C CA  . GLU   A 120 ? 0.2580 0.2885 0.2407 -0.0459 -0.0329 0.1009  120 GLU   A CA  
2535 C C   . GLU   A 120 ? 0.2229 0.2762 0.2413 -0.0557 -0.0152 0.1001  120 GLU   A C   
2536 O O   . GLU   A 120 ? 0.2238 0.2804 0.2578 -0.0526 -0.0338 0.1105  120 GLU   A O   
2537 C CB  . GLU   A 120 ? 0.3428 0.3621 0.2916 -0.0228 -0.0352 0.1430  120 GLU   A CB  
2538 C CG  . GLU   A 120 ? 0.4386 0.4485 0.4186 -0.0089 -0.0398 0.1363  120 GLU   A CG  
2539 C CD  . GLU   A 120 ? 0.5078 0.5058 0.5517 0.0045  -0.0385 0.1291  120 GLU   A CD  
2540 O OE1 . GLU   A 120 ? 0.5432 0.5355 0.5757 0.0095  -0.0399 0.1226  120 GLU   A OE1 
2541 O OE2 . GLU   A 120 ? 0.5496 0.5496 0.6218 0.0073  -0.0402 0.1235  120 GLU   A OE2 
2548 N N   . VAL   A 121 ? 0.2157 0.2780 0.2094 -0.0461 -0.0036 0.0861  121 VAL   A N   
2549 C CA  . VAL   A 121 ? 0.2178 0.2905 0.2111 -0.0507 0.0033  0.0947  121 VAL   A CA  
2550 C C   . VAL   A 121 ? 0.2039 0.2652 0.1931 -0.0403 -0.0018 0.0759  121 VAL   A C   
2551 O O   . VAL   A 121 ? 0.2094 0.2583 0.1950 -0.0508 -0.0136 0.0597  121 VAL   A O   
2552 C CB  . VAL   A 121 ? 0.2708 0.3368 0.2309 -0.0273 0.0153  0.1038  121 VAL   A CB  
2553 C CG1 . VAL   A 121 ? 0.2805 0.3579 0.2258 -0.0118 0.0137  0.1048  121 VAL   A CG1 
2554 C CG2 . VAL   A 121 ? 0.2919 0.3509 0.2919 -0.0461 0.0168  0.0927  121 VAL   A CG2 
2564 N N   . LEU   A 122 ? 0.2011 0.2427 0.1734 -0.0405 -0.0070 0.0500  122 LEU   A N   
2565 C CA  . LEU   A 122 ? 0.2170 0.2150 0.1716 -0.0407 0.0084  0.0374  122 LEU   A CA  
2566 C C   . LEU   A 122 ? 0.2049 0.2041 0.1640 -0.0487 -0.0028 0.0416  122 LEU   A C   
2567 O O   . LEU   A 122 ? 0.2073 0.2113 0.2061 -0.0562 -0.0243 0.0395  122 LEU   A O   
2568 C CB  . LEU   A 122 ? 0.2342 0.2088 0.2209 -0.0341 0.0086  0.0421  122 LEU   A CB  
2569 C CG  . LEU   A 122 ? 0.2276 0.2145 0.2204 -0.0319 0.0239  0.0226  122 LEU   A CG  
2570 C CD1 . LEU   A 122 ? 0.2511 0.2022 0.2221 -0.0400 0.0350  0.0167  122 LEU   A CD1 
2571 C CD2 . LEU   A 122 ? 0.2283 0.2090 0.1890 -0.0362 0.0186  0.0240  122 LEU   A CD2 
2583 N N   A LEU   A 123 ? 0.1888 0.2036 0.1848 -0.0466 0.0039  0.0420  123 LEU   A N   
2584 N N   B LEU   A 123 ? 0.2049 0.1966 0.1850 -0.0464 -0.0076 0.0250  123 LEU   A N   
2585 C CA  A LEU   A 123 ? 0.1797 0.2150 0.1833 -0.0352 0.0128  0.0489  123 LEU   A CA  
2586 C CA  B LEU   A 123 ? 0.2098 0.2024 0.1702 -0.0360 -0.0036 0.0160  123 LEU   A CA  
2587 C C   A LEU   A 123 ? 0.1659 0.2077 0.1918 -0.0302 0.0076  0.0430  123 LEU   A C   
2588 C C   B LEU   A 123 ? 0.2034 0.1850 0.1407 -0.0317 -0.0099 0.0097  123 LEU   A C   
2589 O O   A LEU   A 123 ? 0.1512 0.2065 0.2094 -0.0340 0.0174  0.0341  123 LEU   A O   
2590 O O   B LEU   A 123 ? 0.1954 0.1913 0.1491 -0.0252 -0.0047 0.0111  123 LEU   A O   
2591 C CB  A LEU   A 123 ? 0.1796 0.2141 0.1689 -0.0265 0.0276  0.0574  123 LEU   A CB  
2592 C CB  B LEU   A 123 ? 0.2133 0.2053 0.1831 -0.0304 0.0043  0.0139  123 LEU   A CB  
2593 C CG  A LEU   A 123 ? 0.1892 0.2262 0.1886 -0.0190 0.0218  0.0318  123 LEU   A CG  
2594 C CG  B LEU   A 123 ? 0.2252 0.2144 0.1956 -0.0265 0.0030  0.0050  123 LEU   A CG  
2595 C CD1 A LEU   A 123 ? 0.1943 0.2323 0.2196 -0.0266 0.0256  0.0131  123 LEU   A CD1 
2596 C CD1 B LEU   A 123 ? 0.2283 0.2141 0.2250 -0.0381 0.0040  -0.0101 123 LEU   A CD1 
2597 C CD2 A LEU   A 123 ? 0.1945 0.2357 0.1778 -0.0196 0.0016  0.0276  123 LEU   A CD2 
2598 C CD2 B LEU   A 123 ? 0.2345 0.2267 0.1993 -0.0273 -0.0101 -0.0009 123 LEU   A CD2 
2621 N N   A ALA   A 124 ? 0.1569 0.2025 0.1897 -0.0364 0.0115  0.0464  124 ALA   A N   
2622 N N   B ALA   A 124 ? 0.1880 0.1759 0.1414 -0.0288 -0.0089 0.0148  124 ALA   A N   
2623 C CA  A ALA   A 124 ? 0.1645 0.2012 0.1911 -0.0359 0.0061  0.0401  124 ALA   A CA  
2624 C CA  B ALA   A 124 ? 0.1859 0.1749 0.1475 -0.0125 -0.0046 0.0193  124 ALA   A CA  
2625 C C   A ALA   A 124 ? 0.1647 0.1909 0.1761 -0.0332 0.0051  0.0246  124 ALA   A C   
2626 C C   B ALA   A 124 ? 0.1801 0.1831 0.1514 -0.0095 0.0183  -0.0036 124 ALA   A C   
2627 O O   A ALA   A 124 ? 0.1656 0.1894 0.1805 -0.0278 0.0042  0.0259  124 ALA   A O   
2628 O O   B ALA   A 124 ? 0.1823 0.1979 0.1690 -0.0095 0.0313  0.0021  124 ALA   A O   
2629 C CB  A ALA   A 124 ? 0.1700 0.2059 0.2053 -0.0436 -0.0002 0.0314  124 ALA   A CB  
2630 C CB  B ALA   A 124 ? 0.1846 0.1626 0.1468 -0.0074 -0.0118 0.0245  124 ALA   A CB  
2641 N N   A PRO   A 125 ? 0.1620 0.1781 0.1711 -0.0307 0.0055  0.0346  125 PRO   A N   
2642 N N   B PRO   A 125 ? 0.1851 0.1866 0.1591 -0.0103 0.0057  -0.0003 125 PRO   A N   
2643 C CA  A PRO   A 125 ? 0.1744 0.1825 0.1659 -0.0199 0.0080  0.0389  125 PRO   A CA  
2644 C CA  B PRO   A 125 ? 0.2045 0.1934 0.1659 -0.0027 -0.0099 0.0003  125 PRO   A CA  
2645 C C   A PRO   A 125 ? 0.1670 0.1734 0.1668 -0.0127 0.0131  0.0315  125 PRO   A C   
2646 C C   B PRO   A 125 ? 0.2040 0.1947 0.1505 -0.0025 -0.0134 -0.0044 125 PRO   A C   
2647 O O   A PRO   A 125 ? 0.1664 0.1630 0.2207 -0.0089 0.0200  0.0424  125 PRO   A O   
2648 O O   B PRO   A 125 ? 0.1979 0.1863 0.1707 -0.0053 -0.0127 -0.0093 125 PRO   A O   
2649 C CB  A PRO   A 125 ? 0.1695 0.1852 0.1682 -0.0182 0.0185  0.0347  125 PRO   A CB  
2650 C CB  B PRO   A 125 ? 0.2070 0.1877 0.1896 0.0042  0.0013  -0.0040 125 PRO   A CB  
2651 C CG  A PRO   A 125 ? 0.1645 0.1715 0.1681 -0.0164 0.0214  0.0401  125 PRO   A CG  
2652 C CG  B PRO   A 125 ? 0.2082 0.1863 0.1836 -0.0052 0.0124  0.0075  125 PRO   A CG  
2653 C CD  A PRO   A 125 ? 0.1578 0.1679 0.1690 -0.0317 0.0107  0.0371  125 PRO   A CD  
2654 C CD  B PRO   A 125 ? 0.1941 0.1822 0.1746 -0.0159 0.0057  -0.0010 125 PRO   A CD  
2669 N N   A LEU   A 126 ? 0.1512 0.1721 0.1817 -0.0142 0.0251  0.0369  126 LEU   A N   
2670 N N   B LEU   A 126 ? 0.2059 0.2190 0.1552 -0.0031 0.0089  -0.0054 126 LEU   A N   
2671 C CA  A LEU   A 126 ? 0.1518 0.1736 0.1875 -0.0130 0.0219  0.0288  126 LEU   A CA  
2672 C CA  B LEU   A 126 ? 0.1945 0.2048 0.1561 -0.0043 0.0104  0.0078  126 LEU   A CA  
2673 C C   A LEU   A 126 ? 0.1770 0.1636 0.1803 -0.0031 -0.0065 0.0087  126 LEU   A C   
2674 C C   B LEU   A 126 ? 0.2014 0.2096 0.1887 0.0112  0.0205  0.0197  126 LEU   A C   
2675 O O   A LEU   A 126 ? 0.1852 0.1501 0.2061 -0.0220 -0.0167 -0.0034 126 LEU   A O   
2676 O O   B LEU   A 126 ? 0.2278 0.2048 0.2353 0.0162  0.0472  0.0308  126 LEU   A O   
2677 C CB  A LEU   A 126 ? 0.1485 0.1740 0.2108 -0.0131 0.0078  0.0270  126 LEU   A CB  
2678 C CB  B LEU   A 126 ? 0.1987 0.2175 0.1648 -0.0190 -0.0015 0.0030  126 LEU   A CB  
2679 C CG  A LEU   A 126 ? 0.1462 0.1782 0.2345 -0.0017 0.0095  0.0413  126 LEU   A CG  
2680 C CG  B LEU   A 126 ? 0.1996 0.2237 0.1994 -0.0166 0.0061  0.0141  126 LEU   A CG  
2681 C CD1 A LEU   A 126 ? 0.1374 0.1913 0.2555 -0.0021 -0.0034 0.0505  126 LEU   A CD1 
2682 C CD1 B LEU   A 126 ? 0.1957 0.2222 0.2420 -0.0294 -0.0045 0.0134  126 LEU   A CD1 
2683 C CD2 A LEU   A 126 ? 0.1645 0.1723 0.2312 0.0035  0.0142  0.0488  126 LEU   A CD2 
2684 C CD2 B LEU   A 126 ? 0.2135 0.2306 0.2331 -0.0144 0.0044  0.0204  126 LEU   A CD2 
2707 N N   A LEU   A 127 ? 0.1694 0.1771 0.1667 -0.0032 -0.0105 0.0132  127 LEU   A N   
2708 N N   B LEU   A 127 ? 0.1740 0.2218 0.1641 0.0092  0.0162  0.0154  127 LEU   A N   
2709 C CA  A LEU   A 127 ? 0.1737 0.1635 0.1688 -0.0027 -0.0164 0.0199  127 LEU   A CA  
2710 C CA  B LEU   A 127 ? 0.1726 0.2164 0.1840 0.0049  0.0156  0.0192  127 LEU   A CA  
2711 C C   A LEU   A 127 ? 0.1659 0.1597 0.1684 -0.0059 -0.0163 0.0023  127 LEU   A C   
2712 C C   B LEU   A 127 ? 0.1651 0.2244 0.1812 -0.0026 0.0158  0.0135  127 LEU   A C   
2713 O O   A LEU   A 127 ? 0.1791 0.1480 0.2004 0.0020  -0.0163 0.0036  127 LEU   A O   
2714 O O   B LEU   A 127 ? 0.1835 0.2349 0.1640 0.0002  0.0152  0.0310  127 LEU   A O   
2715 C CB  A LEU   A 127 ? 0.1802 0.1723 0.1747 0.0122  -0.0023 0.0345  127 LEU   A CB  
2716 C CB  B LEU   A 127 ? 0.1711 0.2241 0.1990 0.0042  0.0157  0.0136  127 LEU   A CB  
2717 C CG  A LEU   A 127 ? 0.1881 0.1830 0.1723 0.0085  0.0019  0.0237  127 LEU   A CG  
2718 C CG  B LEU   A 127 ? 0.1820 0.2310 0.2085 0.0109  -0.0046 0.0154  127 LEU   A CG  
2719 C CD1 A LEU   A 127 ? 0.1861 0.1722 0.1931 -0.0017 0.0044  0.0237  127 LEU   A CD1 
2720 C CD1 B LEU   A 127 ? 0.1750 0.2363 0.2537 0.0253  0.0007  0.0258  127 LEU   A CD1 
2721 C CD2 A LEU   A 127 ? 0.1976 0.1848 0.1566 0.0179  -0.0079 0.0320  127 LEU   A CD2 
2722 C CD2 B LEU   A 127 ? 0.2010 0.2417 0.2118 0.0172  -0.0283 -0.0038 127 LEU   A CD2 
2745 N N   A SER   A 128 ? 0.1657 0.1680 0.1437 -0.0038 -0.0163 -0.0059 128 SER   A N   
2746 N N   B SER   A 128 ? 0.1695 0.2374 0.2069 -0.0124 0.0067  0.0269  128 SER   A N   
2747 C CA  A SER   A 128 ? 0.1755 0.1633 0.1431 0.0003  0.0013  0.0081  128 SER   A CA  
2748 C CA  B SER   A 128 ? 0.1826 0.2616 0.2113 -0.0032 -0.0107 0.0377  128 SER   A CA  
2749 C C   A SER   A 128 ? 0.1715 0.1605 0.1359 -0.0013 0.0073  0.0164  128 SER   A C   
2750 C C   B SER   A 128 ? 0.2058 0.2937 0.2483 0.0123  -0.0375 0.0344  128 SER   A C   
2751 O O   A SER   A 128 ? 0.1885 0.1752 0.1345 -0.0023 0.0277  0.0020  128 SER   A O   
2752 O O   B SER   A 128 ? 0.2070 0.3011 0.2691 0.0176  -0.0582 0.0171  128 SER   A O   
2753 C CB  A SER   A 128 ? 0.1912 0.1810 0.1462 0.0045  0.0089  0.0039  128 SER   A CB  
2754 C CB  B SER   A 128 ? 0.1821 0.2600 0.1850 0.0020  -0.0048 0.0398  128 SER   A CB  
2755 O OG  A SER   A 128 ? 0.1976 0.1900 0.1745 -0.0059 0.0133  0.0119  128 SER   A OG  
2756 O OG  B SER   A 128 ? 0.1675 0.2519 0.1607 0.0015  -0.0020 0.0276  128 SER   A OG  
2767 N N   A ALA   A 129 ? 0.1588 0.1596 0.1513 -0.0026 0.0113  0.0424  129 ALA   A N   
2768 N N   B ALA   A 129 ? 0.2312 0.3234 0.2693 0.0328  -0.0379 0.0356  129 ALA   A N   
2769 C CA  A ALA   A 129 ? 0.1420 0.1605 0.1603 0.0061  0.0044  0.0452  129 ALA   A CA  
2770 C CA  B ALA   A 129 ? 0.2577 0.3465 0.3044 0.0462  -0.0379 0.0210  129 ALA   A CA  
2771 C C   A ALA   A 129 ? 0.1590 0.1669 0.1540 0.0002  0.0015  0.0112  129 ALA   A C   
2772 C C   B ALA   A 129 ? 0.2696 0.3499 0.3119 0.0552  -0.0364 0.0153  129 ALA   A C   
2773 O O   A ALA   A 129 ? 0.1608 0.1707 0.1825 -0.0159 -0.0227 0.0464  129 ALA   A O   
2774 O O   B ALA   A 129 ? 0.2870 0.3570 0.3484 0.0568  -0.0342 0.0098  129 ALA   A O   
2775 C CB  A ALA   A 129 ? 0.1312 0.1863 0.1965 0.0097  0.0076  0.0536  129 ALA   A CB  
2776 C CB  B ALA   A 129 ? 0.2681 0.3527 0.3119 0.0473  -0.0378 0.0170  129 ALA   A CB  
2787 N N   A GLY   A 130 ? 0.1738 0.1761 0.1676 -0.0013 0.0027  -0.0089 130 GLY   A N   
2788 N N   B GLY   A 130 ? 0.2704 0.3511 0.2964 0.0558  -0.0171 0.0002  130 GLY   A N   
2789 C CA  A GLY   A 130 ? 0.1869 0.1739 0.1640 0.0049  0.0122  -0.0144 130 GLY   A CA  
2790 C CA  B GLY   A 130 ? 0.2771 0.3490 0.2842 0.0588  -0.0117 0.0039  130 GLY   A CA  
2791 C C   A GLY   A 130 ? 0.1824 0.1522 0.1543 0.0124  0.0062  -0.0054 130 GLY   A C   
2792 C C   B GLY   A 130 ? 0.2783 0.3440 0.2600 0.0545  -0.0184 0.0040  130 GLY   A C   
2793 O O   A GLY   A 130 ? 0.1877 0.1487 0.1523 0.0124  0.0071  0.0111  130 GLY   A O   
2794 O O   B GLY   A 130 ? 0.2716 0.3491 0.2287 0.0486  -0.0162 -0.0206 130 GLY   A O   
2801 N N   A ILE   A 131 ? 0.1818 0.1451 0.1776 0.0025  0.0082  0.0144  131 ILE   A N   
2802 N N   B ILE   A 131 ? 0.2855 0.3356 0.2909 0.0467  -0.0394 -0.0013 131 ILE   A N   
2803 C CA  A ILE   A 131 ? 0.1942 0.1609 0.1679 -0.0065 0.0063  -0.0045 131 ILE   A CA  
2804 C CA  B ILE   A 131 ? 0.2996 0.3298 0.3350 0.0379  -0.0350 -0.0035 131 ILE   A CA  
2805 C C   A ILE   A 131 ? 0.1817 0.1566 0.1507 -0.0014 0.0076  0.0204  131 ILE   A C   
2806 C C   B ILE   A 131 ? 0.2990 0.3153 0.3142 0.0366  -0.0431 0.0131  131 ILE   A C   
2807 O O   A ILE   A 131 ? 0.1915 0.1558 0.1581 0.0125  -0.0053 0.0461  131 ILE   A O   
2808 O O   B ILE   A 131 ? 0.3081 0.3223 0.3267 0.0351  -0.0272 0.0384  131 ILE   A O   
2809 C CB  A ILE   A 131 ? 0.2110 0.1703 0.1991 -0.0154 -0.0107 -0.0083 131 ILE   A CB  
2810 C CB  B ILE   A 131 ? 0.3203 0.3420 0.4006 0.0274  -0.0261 -0.0139 131 ILE   A CB  
2811 C CG1 A ILE   A 131 ? 0.2081 0.2042 0.2132 -0.0183 -0.0071 -0.0236 131 ILE   A CG1 
2812 C CG1 B ILE   A 131 ? 0.3357 0.3565 0.4314 0.0148  -0.0200 -0.0163 131 ILE   A CG1 
2813 C CG2 A ILE   A 131 ? 0.2275 0.1460 0.2159 -0.0243 -0.0062 -0.0054 131 ILE   A CG2 
2814 C CG2 B ILE   A 131 ? 0.3258 0.3415 0.4174 0.0277  -0.0290 -0.0142 131 ILE   A CG2 
2815 C CD1 A ILE   A 131 ? 0.2103 0.2204 0.2178 -0.0168 -0.0129 -0.0273 131 ILE   A CD1 
2816 C CD1 B ILE   A 131 ? 0.3453 0.3654 0.4523 0.0134  -0.0186 -0.0120 131 ILE   A CD1 
2839 N N   A PHE   A 132 ? 0.1751 0.1595 0.1249 0.0029  0.0088  0.0301  132 PHE   A N   
2840 N N   B PHE   A 132 ? 0.2849 0.2941 0.2932 0.0316  -0.0589 0.0094  132 PHE   A N   
2841 C CA  A PHE   A 132 ? 0.1848 0.1639 0.1314 -0.0109 -0.0101 0.0074  132 PHE   A CA  
2842 C CA  B PHE   A 132 ? 0.2734 0.2719 0.3107 0.0213  -0.0600 0.0079  132 PHE   A CA  
2843 C C   A PHE   A 132 ? 0.1980 0.1821 0.1414 -0.0094 -0.0225 0.0015  132 PHE   A C   
2844 C C   B PHE   A 132 ? 0.2725 0.2541 0.2792 0.0075  -0.0564 0.0073  132 PHE   A C   
2845 O O   A PHE   A 132 ? 0.2166 0.1869 0.1515 -0.0095 -0.0189 -0.0057 132 PHE   A O   
2846 O O   B PHE   A 132 ? 0.2762 0.2562 0.2618 -0.0046 -0.0601 -0.0114 132 PHE   A O   
2847 C CB  A PHE   A 132 ? 0.1801 0.1481 0.1252 -0.0205 -0.0159 0.0128  132 PHE   A CB  
2848 C CB  B PHE   A 132 ? 0.2637 0.2734 0.3590 0.0190  -0.0822 0.0058  132 PHE   A CB  
2849 C CG  A PHE   A 132 ? 0.1793 0.1463 0.1316 -0.0062 -0.0343 0.0095  132 PHE   A CG  
2850 C CG  B PHE   A 132 ? 0.2753 0.2780 0.4136 0.0172  -0.0775 0.0149  132 PHE   A CG  
2851 C CD1 A PHE   A 132 ? 0.1714 0.1602 0.1565 0.0009  -0.0387 -0.0163 132 PHE   A CD1 
2852 C CD1 B PHE   A 132 ? 0.2850 0.2865 0.4344 0.0165  -0.0670 0.0206  132 PHE   A CD1 
2853 C CD2 A PHE   A 132 ? 0.1871 0.1551 0.1480 -0.0116 -0.0439 0.0120  132 PHE   A CD2 
2854 C CD2 B PHE   A 132 ? 0.2751 0.2818 0.4249 0.0208  -0.0780 0.0208  132 PHE   A CD2 
2855 C CE1 A PHE   A 132 ? 0.1797 0.1614 0.1544 0.0042  -0.0324 -0.0239 132 PHE   A CE1 
2856 C CE1 B PHE   A 132 ? 0.2880 0.2869 0.4414 0.0180  -0.0680 0.0148  132 PHE   A CE1 
2857 C CE2 A PHE   A 132 ? 0.1781 0.1588 0.1274 0.0042  -0.0433 0.0006  132 PHE   A CE2 
2858 C CE2 B PHE   A 132 ? 0.2805 0.2900 0.4436 0.0169  -0.0815 0.0168  132 PHE   A CE2 
2859 C CZ  A PHE   A 132 ? 0.1707 0.1552 0.1337 -0.0059 -0.0365 -0.0043 132 PHE   A CZ  
2860 C CZ  B PHE   A 132 ? 0.2788 0.2923 0.4415 0.0134  -0.0854 0.0125  132 PHE   A CZ  
2879 N N   A GLY   A 133 ? 0.2049 0.1897 0.1414 -0.0109 -0.0376 -0.0066 133 GLY   A N   
2880 N N   B GLY   A 133 ? 0.2686 0.2369 0.2571 0.0177  -0.0614 0.0204  133 GLY   A N   
2881 C CA  A GLY   A 133 ? 0.2179 0.2055 0.1491 -0.0081 -0.0283 -0.0128 133 GLY   A CA  
2882 C CA  B GLY   A 133 ? 0.2688 0.2386 0.2420 0.0068  -0.0521 0.0191  133 GLY   A CA  
2883 C C   A GLY   A 133 ? 0.2243 0.2150 0.1884 -0.0073 -0.0286 -0.0216 133 GLY   A C   
2884 C C   B GLY   A 133 ? 0.2598 0.2483 0.2374 -0.0079 -0.0479 0.0285  133 GLY   A C   
2885 O O   A GLY   A 133 ? 0.2307 0.2254 0.2245 -0.0169 -0.0339 -0.0311 133 GLY   A O   
2886 O O   B GLY   A 133 ? 0.2646 0.2668 0.2633 -0.0113 -0.0469 0.0328  133 GLY   A O   
2893 N N   A ALA   A 134 ? 0.2288 0.2075 0.1774 -0.0036 -0.0199 -0.0345 134 ALA   A N   
2894 N N   B ALA   A 134 ? 0.2474 0.2348 0.2095 -0.0218 -0.0376 0.0468  134 ALA   A N   
2895 C CA  A ALA   A 134 ? 0.2415 0.2104 0.2101 0.0083  -0.0230 -0.0311 134 ALA   A CA  
2896 C CA  B ALA   A 134 ? 0.2491 0.2343 0.2150 -0.0325 -0.0451 0.0606  134 ALA   A CA  
2897 C C   A ALA   A 134 ? 0.2381 0.2161 0.2108 0.0090  -0.0247 -0.0166 134 ALA   A C   
2898 C C   B ALA   A 134 ? 0.2428 0.2439 0.2300 -0.0363 -0.0353 0.0419  134 ALA   A C   
2899 O O   A ALA   A 134 ? 0.2502 0.2212 0.2395 0.0273  -0.0184 -0.0077 134 ALA   A O   
2900 O O   B ALA   A 134 ? 0.2468 0.2559 0.2556 -0.0370 -0.0234 0.0479  134 ALA   A O   
2901 C CB  A ALA   A 134 ? 0.2564 0.2113 0.2433 0.0071  -0.0316 -0.0341 134 ALA   A CB  
2902 C CB  B ALA   A 134 ? 0.2618 0.2293 0.2451 -0.0381 -0.0484 0.0610  134 ALA   A CB  
2913 N N   A ASP   A 135 ? 0.2321 0.2346 0.2166 -0.0043 -0.0279 0.0164  135 ASP   A N   
2914 N N   B ASP   A 135 ? 0.2458 0.2565 0.2335 -0.0373 -0.0373 0.0465  135 ASP   A N   
2915 C CA  A ASP   A 135 ? 0.2096 0.2468 0.2276 -0.0080 -0.0450 0.0466  135 ASP   A CA  
2916 C CA  B ASP   A 135 ? 0.2390 0.2668 0.2524 -0.0389 -0.0506 0.0448  135 ASP   A CA  
2917 C C   A ASP   A 135 ? 0.1845 0.2534 0.2280 -0.0031 -0.0391 0.0594  135 ASP   A C   
2918 C C   B ASP   A 135 ? 0.2189 0.2548 0.2521 -0.0364 -0.0545 0.0413  135 ASP   A C   
2919 O O   A ASP   A 135 ? 0.1909 0.2549 0.2516 0.0005  -0.0398 0.0777  135 ASP   A O   
2920 O O   B ASP   A 135 ? 0.2184 0.2421 0.2819 -0.0275 -0.0512 0.0576  135 ASP   A O   
2921 C CB  A ASP   A 135 ? 0.2294 0.2635 0.2679 -0.0304 -0.0600 0.0430  135 ASP   A CB  
2922 C CB  B ASP   A 135 ? 0.2572 0.2977 0.3030 -0.0408 -0.0612 0.0328  135 ASP   A CB  
2923 C CG  A ASP   A 135 ? 0.2395 0.2772 0.3211 -0.0482 -0.0692 0.0428  135 ASP   A CG  
2924 C CG  B ASP   A 135 ? 0.2744 0.3306 0.3755 -0.0413 -0.0502 0.0234  135 ASP   A CG  
2925 O OD1 A ASP   A 135 ? 0.2249 0.2737 0.2839 -0.0533 -0.0907 0.0822  135 ASP   A OD1 
2926 O OD1 B ASP   A 135 ? 0.2866 0.3518 0.4203 -0.0447 -0.0309 0.0191  135 ASP   A OD1 
2927 O OD2 A ASP   A 135 ? 0.2730 0.2966 0.3907 -0.0428 -0.0269 0.0415  135 ASP   A OD2 
2928 O OD2 B ASP   A 135 ? 0.2736 0.3448 0.3965 -0.0430 -0.0726 0.0343  135 ASP   A OD2 
2937 N N   A PRO   A 136 ? 0.1599 0.2508 0.2413 0.0125  -0.0294 0.0705  136 PRO   A N   
2938 N N   B PRO   A 136 ? 0.2193 0.2567 0.2673 -0.0268 -0.0234 0.0406  136 PRO   A N   
2939 C CA  A PRO   A 136 ? 0.1542 0.2587 0.2439 0.0053  -0.0247 0.0527  136 PRO   A CA  
2940 C CA  B PRO   A 136 ? 0.2224 0.2607 0.2788 -0.0277 -0.0112 0.0168  136 PRO   A CA  
2941 C C   A PRO   A 136 ? 0.1375 0.2626 0.2262 0.0077  -0.0331 0.0441  136 PRO   A C   
2942 C C   B PRO   A 136 ? 0.2195 0.2642 0.2677 -0.0200 -0.0063 0.0143  136 PRO   A C   
2943 O O   A PRO   A 136 ? 0.1346 0.2638 0.1805 0.0178  -0.0142 0.0493  136 PRO   A O   
2944 O O   B PRO   A 136 ? 0.2134 0.2549 0.2320 -0.0153 0.0014  0.0240  136 PRO   A O   
2945 C CB  A PRO   A 136 ? 0.1539 0.2650 0.2721 0.0133  -0.0083 0.0493  136 PRO   A CB  
2946 C CB  B PRO   A 136 ? 0.2390 0.2657 0.3001 -0.0232 -0.0099 0.0266  136 PRO   A CB  
2947 C CG  A PRO   A 136 ? 0.1723 0.2740 0.2932 0.0338  -0.0179 0.0472  136 PRO   A CG  
2948 C CG  B PRO   A 136 ? 0.2479 0.2857 0.3295 -0.0224 -0.0033 0.0274  136 PRO   A CG  
2949 C CD  A PRO   A 136 ? 0.1707 0.2637 0.2826 0.0310  -0.0163 0.0630  136 PRO   A CD  
2950 C CD  B PRO   A 136 ? 0.2387 0.2760 0.2968 -0.0173 -0.0007 0.0413  136 PRO   A CD  
2965 N N   A ILE   A 137 ? 0.1417 0.2624 0.2303 -0.0068 -0.0493 0.0522  137 ILE   A N   
2966 N N   B ILE   A 137 ? 0.2289 0.2722 0.2724 -0.0255 -0.0030 0.0206  137 ILE   A N   
2967 C CA  A ILE   A 137 ? 0.1519 0.2585 0.2329 -0.0074 -0.0466 0.0619  137 ILE   A CA  
2968 C CA  B ILE   A 137 ? 0.2381 0.2763 0.2799 -0.0239 -0.0061 0.0235  137 ILE   A CA  
2969 C C   A ILE   A 137 ? 0.1580 0.2588 0.2196 -0.0090 -0.0383 0.0497  137 ILE   A C   
2970 C C   B ILE   A 137 ? 0.2303 0.2614 0.2503 -0.0252 -0.0081 0.0168  137 ILE   A C   
2971 O O   A ILE   A 137 ? 0.1541 0.2652 0.1997 -0.0132 -0.0348 0.0455  137 ILE   A O   
2972 O O   B ILE   A 137 ? 0.2210 0.2635 0.2422 -0.0364 -0.0093 0.0332  137 ILE   A O   
2973 C CB  A ILE   A 137 ? 0.1656 0.2638 0.2812 -0.0156 -0.0465 0.0649  137 ILE   A CB  
2974 C CB  B ILE   A 137 ? 0.2622 0.3004 0.3425 -0.0271 -0.0071 0.0230  137 ILE   A CB  
2975 C CG1 A ILE   A 137 ? 0.1901 0.2824 0.3109 -0.0175 -0.0503 0.0820  137 ILE   A CG1 
2976 C CG1 B ILE   A 137 ? 0.2812 0.3302 0.3707 -0.0259 0.0032  0.0264  137 ILE   A CG1 
2977 C CG2 A ILE   A 137 ? 0.1538 0.2665 0.2574 -0.0221 -0.0400 0.0675  137 ILE   A CG2 
2978 C CG2 B ILE   A 137 ? 0.2674 0.3094 0.3612 -0.0287 -0.0087 0.0229  137 ILE   A CG2 
2979 C CD1 A ILE   A 137 ? 0.2098 0.2992 0.3590 -0.0200 -0.0340 0.0766  137 ILE   A CD1 
2980 C CD1 B ILE   A 137 ? 0.2934 0.3478 0.3952 -0.0236 0.0115  0.0279  137 ILE   A CD1 
3003 N N   A HIS   A 138 ? 0.1756 0.2611 0.2120 -0.0113 -0.0225 0.0476  138 HIS   A N   
3004 N N   B HIS   A 138 ? 0.2348 0.2488 0.2267 -0.0233 -0.0015 0.0043  138 HIS   A N   
3005 C CA  A HIS   A 138 ? 0.1820 0.2629 0.1905 -0.0160 -0.0182 0.0487  138 HIS   A CA  
3006 C CA  B HIS   A 138 ? 0.2350 0.2397 0.1863 -0.0217 -0.0069 0.0044  138 HIS   A CA  
3007 C C   A HIS   A 138 ? 0.1659 0.2481 0.1988 -0.0127 -0.0178 0.0478  138 HIS   A C   
3008 C C   B HIS   A 138 ? 0.2165 0.2256 0.1745 -0.0065 -0.0060 0.0249  138 HIS   A C   
3009 O O   A HIS   A 138 ? 0.1678 0.2549 0.2198 -0.0168 -0.0213 0.0319  138 HIS   A O   
3010 O O   B HIS   A 138 ? 0.2183 0.2127 0.1825 -0.0189 0.0021  0.0215  138 HIS   A O   
3011 C CB  A HIS   A 138 ? 0.1993 0.2836 0.1954 -0.0152 -0.0352 0.0476  138 HIS   A CB  
3012 C CB  B HIS   A 138 ? 0.2541 0.2506 0.2159 -0.0210 -0.0227 -0.0230 138 HIS   A CB  
3013 C CG  A HIS   A 138 ? 0.2071 0.2886 0.2024 -0.0217 -0.0310 0.0492  138 HIS   A CG  
3014 C CG  B HIS   A 138 ? 0.2643 0.2539 0.2530 -0.0148 -0.0258 -0.0403 138 HIS   A CG  
3015 N ND1 A HIS   A 138 ? 0.2155 0.2975 0.2276 -0.0284 -0.0218 0.0480  138 HIS   A ND1 
3016 N ND1 B HIS   A 138 ? 0.2709 0.2543 0.2894 -0.0220 -0.0243 -0.0432 138 HIS   A ND1 
3017 C CD2 A HIS   A 138 ? 0.2102 0.2884 0.1979 -0.0249 -0.0266 0.0589  138 HIS   A CD2 
3018 C CD2 B HIS   A 138 ? 0.2717 0.2574 0.2727 -0.0086 -0.0223 -0.0313 138 HIS   A CD2 
3019 C CE1 A HIS   A 138 ? 0.2182 0.2958 0.2152 -0.0216 -0.0314 0.0454  138 HIS   A CE1 
3020 C CE1 B HIS   A 138 ? 0.2734 0.2533 0.2848 -0.0157 -0.0149 -0.0524 138 HIS   A CE1 
3021 N NE2 A HIS   A 138 ? 0.2226 0.2916 0.2006 -0.0242 -0.0204 0.0544  138 HIS   A NE2 
3022 N NE2 B HIS   A 138 ? 0.2778 0.2547 0.2846 -0.0111 -0.0147 -0.0477 138 HIS   A NE2 
3037 N N   A SER   A 139 ? 0.1605 0.2308 0.2172 -0.0169 -0.0158 0.0558  139 SER   A N   
3038 N N   B SER   A 139 ? 0.2070 0.2157 0.1901 -0.0109 -0.0017 0.0401  139 SER   A N   
3039 C CA  A SER   A 139 ? 0.1654 0.2142 0.2310 -0.0120 -0.0190 0.0541  139 SER   A CA  
3040 C CA  B SER   A 139 ? 0.2069 0.2013 0.1909 -0.0026 -0.0091 0.0296  139 SER   A CA  
3041 C C   A SER   A 139 ? 0.1765 0.2074 0.2356 -0.0213 -0.0197 0.0481  139 SER   A C   
3042 C C   B SER   A 139 ? 0.2050 0.1960 0.1647 -0.0100 0.0100  0.0284  139 SER   A C   
3043 O O   A SER   A 139 ? 0.1751 0.2008 0.2465 -0.0273 -0.0279 0.0464  139 SER   A O   
3044 O O   B SER   A 139 ? 0.1953 0.1916 0.1709 -0.0150 -0.0081 0.0233  139 SER   A O   
3045 C CB  A SER   A 139 ? 0.1560 0.1968 0.2250 -0.0041 -0.0204 0.0572  139 SER   A CB  
3046 C CB  B SER   A 139 ? 0.2092 0.1899 0.1663 0.0058  -0.0159 0.0351  139 SER   A CB  
3047 O OG  A SER   A 139 ? 0.1536 0.1880 0.2399 -0.0038 -0.0263 0.0553  139 SER   A OG  
3048 O OG  B SER   A 139 ? 0.2247 0.2096 0.1712 0.0122  -0.0300 0.0192  139 SER   A OG  
3059 N N   A LEU   A 140 ? 0.1646 0.2005 0.2224 -0.0263 -0.0264 0.0437  140 LEU   A N   
3060 N N   B LEU   A 140 ? 0.1981 0.1983 0.1675 -0.0154 0.0195  0.0298  140 LEU   A N   
3061 C CA  A LEU   A 140 ? 0.1585 0.1821 0.2045 -0.0161 -0.0306 0.0275  140 LEU   A CA  
3062 C CA  B LEU   A 140 ? 0.1893 0.1823 0.1929 -0.0010 0.0236  0.0209  140 LEU   A CA  
3063 C C   A LEU   A 140 ? 0.1550 0.1877 0.1972 -0.0086 -0.0070 0.0259  140 LEU   A C   
3064 C C   B LEU   A 140 ? 0.1933 0.1898 0.1909 -0.0067 0.0174  0.0264  140 LEU   A C   
3065 O O   A LEU   A 140 ? 0.1560 0.1678 0.2164 -0.0041 -0.0029 0.0415  140 LEU   A O   
3066 O O   B LEU   A 140 ? 0.1864 0.1967 0.1999 0.0052  0.0119  0.0079  140 LEU   A O   
3067 C CB  A LEU   A 140 ? 0.1631 0.1722 0.2207 -0.0078 -0.0160 0.0312  140 LEU   A CB  
3068 C CB  B LEU   A 140 ? 0.1738 0.1716 0.2197 0.0046  0.0312  0.0279  140 LEU   A CB  
3069 C CG  A LEU   A 140 ? 0.1641 0.1680 0.2290 -0.0141 -0.0095 0.0297  140 LEU   A CG  
3070 C CG  B LEU   A 140 ? 0.1767 0.1605 0.2441 -0.0000 0.0111  0.0350  140 LEU   A CG  
3071 C CD1 A LEU   A 140 ? 0.1548 0.1618 0.2650 0.0059  -0.0198 0.0190  140 LEU   A CD1 
3072 C CD1 B LEU   A 140 ? 0.1794 0.1690 0.2436 -0.0099 0.0056  0.0292  140 LEU   A CD1 
3073 C CD2 A LEU   A 140 ? 0.1687 0.1625 0.2252 -0.0066 -0.0229 0.0197  140 LEU   A CD2 
3074 C CD2 B LEU   A 140 ? 0.1772 0.1683 0.2553 -0.0086 0.0068  0.0574  140 LEU   A CD2 
3097 N N   A ARG   A 141 ? 0.1494 0.2018 0.2051 -0.0142 -0.0192 0.0166  141 ARG   A N   
3098 N N   B ARG   A 141 ? 0.1966 0.1924 0.2118 -0.0275 0.0043  0.0315  141 ARG   A N   
3099 C CA  A ARG   A 141 ? 0.1645 0.2163 0.2237 -0.0270 -0.0371 0.0066  141 ARG   A CA  
3100 C CA  B ARG   A 141 ? 0.2111 0.2232 0.2352 -0.0228 0.0096  0.0205  141 ARG   A CA  
3101 C C   A ARG   A 141 ? 0.1615 0.2093 0.2238 -0.0281 -0.0346 0.0123  141 ARG   A C   
3102 C C   B ARG   A 141 ? 0.2033 0.2175 0.2263 -0.0101 0.0067  0.0241  141 ARG   A C   
3103 O O   A ARG   A 141 ? 0.1554 0.2091 0.2477 -0.0248 -0.0165 0.0117  141 ARG   A O   
3104 O O   B ARG   A 141 ? 0.2055 0.2181 0.2361 -0.0236 0.0149  0.0311  141 ARG   A O   
3105 C CB  A ARG   A 141 ? 0.1814 0.2464 0.2519 -0.0257 -0.0457 -0.0115 141 ARG   A CB  
3106 C CB  B ARG   A 141 ? 0.2352 0.2589 0.2644 -0.0099 0.0200  0.0192  141 ARG   A CB  
3107 C CG  A ARG   A 141 ? 0.1912 0.2646 0.2648 -0.0398 -0.0208 -0.0101 141 ARG   A CG  
3108 C CG  B ARG   A 141 ? 0.2725 0.2983 0.3288 -0.0084 0.0109  0.0108  141 ARG   A CG  
3109 C CD  A ARG   A 141 ? 0.2057 0.2867 0.2828 -0.0484 -0.0150 -0.0183 141 ARG   A CD  
3110 C CD  B ARG   A 141 ? 0.2965 0.3251 0.3741 -0.0104 0.0124  0.0229  141 ARG   A CD  
3111 N NE  A ARG   A 141 ? 0.2020 0.3040 0.3035 -0.0345 0.0026  -0.0112 141 ARG   A NE  
3112 N NE  B ARG   A 141 ? 0.3193 0.3477 0.4096 -0.0159 0.0114  0.0208  141 ARG   A NE  
3113 C CZ  A ARG   A 141 ? 0.1883 0.3170 0.2973 -0.0338 0.0061  -0.0152 141 ARG   A CZ  
3114 C CZ  B ARG   A 141 ? 0.3430 0.3724 0.4312 -0.0194 0.0146  0.0159  141 ARG   A CZ  
3115 N NH1 A ARG   A 141 ? 0.1843 0.3170 0.2950 -0.0336 0.0220  -0.0421 141 ARG   A NH1 
3116 N NH1 B ARG   A 141 ? 0.3579 0.3801 0.4375 -0.0192 0.0077  0.0157  141 ARG   A NH1 
3117 N NH2 A ARG   A 141 ? 0.1839 0.3224 0.2849 -0.0308 -0.0098 0.0028  141 ARG   A NH2 
3118 N NH2 B ARG   A 141 ? 0.3505 0.3813 0.4393 -0.0202 0.0096  0.0098  141 ARG   A NH2 
3145 N N   A VAL   A 142 ? 0.1562 0.2093 0.2007 -0.0276 -0.0334 0.0184  142 VAL   A N   
3146 N N   B VAL   A 142 ? 0.1941 0.2105 0.2106 -0.0095 -0.0024 0.0335  142 VAL   A N   
3147 C CA  A VAL   A 142 ? 0.1598 0.2152 0.2052 -0.0192 -0.0059 0.0086  142 VAL   A CA  
3148 C CA  B VAL   A 142 ? 0.1866 0.2068 0.2064 -0.0058 -0.0046 0.0381  142 VAL   A CA  
3149 C C   A VAL   A 142 ? 0.1704 0.2112 0.1952 -0.0199 -0.0076 0.0151  142 VAL   A C   
3150 C C   B VAL   A 142 ? 0.1791 0.2065 0.2075 -0.0182 -0.0078 0.0206  142 VAL   A C   
3151 O O   A VAL   A 142 ? 0.1800 0.2088 0.1845 -0.0079 -0.0168 0.0291  142 VAL   A O   
3152 O O   B VAL   A 142 ? 0.1859 0.1993 0.2401 -0.0108 -0.0130 0.0257  142 VAL   A O   
3153 C CB  A VAL   A 142 ? 0.1658 0.2129 0.2131 -0.0131 -0.0054 0.0051  142 VAL   A CB  
3154 C CB  B VAL   A 142 ? 0.2017 0.2139 0.2040 -0.0071 -0.0001 0.0386  142 VAL   A CB  
3155 C CG1 A VAL   A 142 ? 0.1562 0.2082 0.2149 -0.0245 -0.0015 -0.0072 142 VAL   A CG1 
3156 C CG1 B VAL   A 142 ? 0.1978 0.2160 0.2122 -0.0232 -0.0017 0.0343  142 VAL   A CG1 
3157 C CG2 A VAL   A 142 ? 0.1846 0.2226 0.2305 -0.0152 0.0077  0.0060  142 VAL   A CG2 
3158 C CG2 B VAL   A 142 ? 0.2238 0.2121 0.1980 -0.0001 0.0047  0.0526  142 VAL   A CG2 
3177 N N   . CYS   A 143 ? 0.1754 0.2061 0.2054 -0.0225 -0.0114 0.0212  143 CYS   A N   
3178 C CA  . CYS   A 143 ? 0.1893 0.2233 0.1770 -0.0282 0.0055  0.0186  143 CYS   A CA  
3179 C C   . CYS   A 143 ? 0.2021 0.2282 0.2056 -0.0330 -0.0071 0.0406  143 CYS   A C   
3180 O O   . CYS   A 143 ? 0.1873 0.2074 0.2167 -0.0170 -0.0190 0.0419  143 CYS   A O   
3181 C CB  . CYS   A 143 ? 0.1968 0.2316 0.2091 -0.0064 0.0161  0.0212  143 CYS   A CB  
3182 S SG  . CYS   A 143 ? 0.2035 0.2341 0.2072 -0.0028 0.0039  0.0255  143 CYS   A SG  
3189 N N   . VAL   A 144 ? 0.1995 0.2249 0.2355 -0.0403 -0.0077 0.0436  144 VAL   A N   
3190 C CA  . VAL   A 144 ? 0.2080 0.2380 0.2804 -0.0410 -0.0001 0.0370  144 VAL   A CA  
3191 C C   . VAL   A 144 ? 0.1988 0.2232 0.2647 -0.0425 -0.0512 0.0456  144 VAL   A C   
3192 O O   . VAL   A 144 ? 0.2134 0.2374 0.2740 -0.0467 -0.0292 0.0664  144 VAL   A O   
3193 C CB  . VAL   A 144 ? 0.2311 0.2713 0.3246 -0.0352 0.0452  0.0532  144 VAL   A CB  
3194 C CG1 . VAL   A 144 ? 0.2511 0.2923 0.3757 -0.0403 0.0400  0.0263  144 VAL   A CG1 
3195 C CG2 . VAL   A 144 ? 0.2337 0.2925 0.3399 -0.0358 0.0523  0.0490  144 VAL   A CG2 
3205 N N   . ASP   A 145 ? 0.2056 0.2167 0.2975 -0.0417 -0.0387 0.0326  145 ASP   A N   
3206 C CA  . ASP   A 145 ? 0.2055 0.2316 0.3071 -0.0413 -0.0376 0.0295  145 ASP   A CA  
3207 C C   . ASP   A 145 ? 0.2035 0.2162 0.2948 -0.0477 -0.0288 0.0228  145 ASP   A C   
3208 O O   . ASP   A 145 ? 0.2261 0.2134 0.3253 -0.0419 -0.0077 -0.0025 145 ASP   A O   
3209 C CB  . ASP   A 145 ? 0.2306 0.2567 0.3285 -0.0573 -0.0559 0.0295  145 ASP   A CB  
3210 C CG  . ASP   A 145 ? 0.2519 0.2966 0.3410 -0.0673 -0.0542 0.0317  145 ASP   A CG  
3211 O OD1 . ASP   A 145 ? 0.2518 0.3116 0.3502 -0.0772 -0.0195 0.0343  145 ASP   A OD1 
3212 O OD2 . ASP   A 145 ? 0.2596 0.3173 0.3523 -0.0792 -0.0830 0.0167  145 ASP   A OD2 
3217 N N   . THR   A 146 ? 0.1968 0.1944 0.2591 -0.0494 -0.0183 0.0149  146 THR   A N   
3218 C CA  . THR   A 146 ? 0.1865 0.1894 0.2291 -0.0420 -0.0093 0.0174  146 THR   A CA  
3219 C C   . THR   A 146 ? 0.1902 0.1843 0.2318 -0.0292 -0.0084 0.0167  146 THR   A C   
3220 O O   . THR   A 146 ? 0.2040 0.1921 0.2563 -0.0128 -0.0205 0.0320  146 THR   A O   
3221 C CB  . THR   A 146 ? 0.1874 0.1847 0.2097 -0.0215 -0.0040 0.0074  146 THR   A CB  
3222 O OG1 . THR   A 146 ? 0.1820 0.2021 0.2395 -0.0147 -0.0093 -0.0005 146 THR   A OG1 
3223 C CG2 . THR   A 146 ? 0.1888 0.1930 0.2263 -0.0220 0.0011  0.0232  146 THR   A CG2 
3231 N N   . VAL   A 147 ? 0.1748 0.1794 0.2165 -0.0184 -0.0097 0.0279  147 VAL   A N   
3232 C CA  . VAL   A 147 ? 0.1784 0.1953 0.2092 -0.0098 -0.0043 0.0289  147 VAL   A CA  
3233 C C   . VAL   A 147 ? 0.1901 0.1992 0.2338 -0.0250 -0.0014 0.0380  147 VAL   A C   
3234 O O   . VAL   A 147 ? 0.1925 0.1993 0.2593 -0.0355 -0.0196 0.0508  147 VAL   A O   
3235 C CB  . VAL   A 147 ? 0.1806 0.2033 0.2028 -0.0149 0.0054  0.0451  147 VAL   A CB  
3236 C CG1 . VAL   A 147 ? 0.2217 0.2147 0.2117 -0.0032 0.0111  0.0533  147 VAL   A CG1 
3237 C CG2 . VAL   A 147 ? 0.1983 0.2047 0.2025 -0.0206 -0.0017 0.0360  147 VAL   A CG2 
3247 N N   . ARG   A 148 ? 0.1909 0.1995 0.2274 -0.0283 -0.0065 0.0608  148 ARG   A N   
3248 C CA  . ARG   A 148 ? 0.1970 0.2064 0.2501 -0.0282 -0.0134 0.0718  148 ARG   A CA  
3249 C C   . ARG   A 148 ? 0.2133 0.2049 0.2617 -0.0376 -0.0111 0.0687  148 ARG   A C   
3250 O O   . ARG   A 148 ? 0.2427 0.2225 0.2720 -0.0366 0.0009  0.0703  148 ARG   A O   
3251 C CB  . ARG   A 148 ? 0.1936 0.2127 0.2700 -0.0325 0.0153  0.0598  148 ARG   A CB  
3252 C CG  . ARG   A 148 ? 0.1932 0.2132 0.2895 -0.0225 0.0036  0.0601  148 ARG   A CG  
3253 C CD  . ARG   A 148 ? 0.2135 0.1880 0.3153 -0.0224 0.0159  0.0660  148 ARG   A CD  
3254 N NE  . ARG   A 148 ? 0.2048 0.1915 0.3293 -0.0117 0.0154  0.0560  148 ARG   A NE  
3255 C CZ  . ARG   A 148 ? 0.2091 0.1752 0.2851 -0.0106 0.0035  0.0593  148 ARG   A CZ  
3256 N NH1 . ARG   A 148 ? 0.1950 0.1797 0.2951 -0.0141 0.0052  0.0274  148 ARG   A NH1 
3257 N NH2 . ARG   A 148 ? 0.2068 0.2036 0.2816 0.0064  0.0007  0.0539  148 ARG   A NH2 
3271 N N   . THR   A 149 ? 0.2171 0.2088 0.2497 -0.0433 -0.0345 0.0589  149 THR   A N   
3272 C CA  . THR   A 149 ? 0.2089 0.2042 0.2433 -0.0387 -0.0424 0.0654  149 THR   A CA  
3273 C C   . THR   A 149 ? 0.2056 0.2175 0.2297 -0.0391 -0.0176 0.0784  149 THR   A C   
3274 O O   . THR   A 149 ? 0.2055 0.2243 0.2510 -0.0394 -0.0282 0.0716  149 THR   A O   
3275 C CB  . THR   A 149 ? 0.2117 0.2169 0.2595 -0.0425 -0.0272 0.0557  149 THR   A CB  
3276 O OG1 . THR   A 149 ? 0.2284 0.2005 0.2637 -0.0516 -0.0219 0.0582  149 THR   A OG1 
3277 C CG2 . THR   A 149 ? 0.2206 0.2412 0.2729 -0.0381 -0.0179 0.0339  149 THR   A CG2 
3285 N N   . ASN   A 150 ? 0.2032 0.2336 0.2359 -0.0455 -0.0022 0.0769  150 ASN   A N   
3286 C CA  . ASN   A 150 ? 0.2039 0.2540 0.2402 -0.0404 -0.0211 0.0691  150 ASN   A CA  
3287 C C   . ASN   A 150 ? 0.1965 0.2472 0.2521 -0.0525 -0.0236 0.0575  150 ASN   A C   
3288 O O   . ASN   A 150 ? 0.2110 0.2442 0.2720 -0.0473 -0.0420 0.0544  150 ASN   A O   
3289 C CB  . ASN   A 150 ? 0.2497 0.2890 0.2757 -0.0465 -0.0081 0.0918  150 ASN   A CB  
3290 C CG  . ASN   A 150 ? 0.3126 0.3231 0.3729 -0.0299 -0.0139 0.0887  150 ASN   A CG  
3291 O OD1 . ASN   A 150 ? 0.3343 0.3297 0.4068 -0.0384 0.0010  0.1265  150 ASN   A OD1 
3292 N ND2 . ASN   A 150 ? 0.3582 0.3486 0.4175 -0.0160 -0.0161 0.0753  150 ASN   A ND2 
3299 N N   . VAL   A 151 ? 0.1976 0.2346 0.2367 -0.0455 -0.0181 0.0628  151 VAL   A N   
3300 C CA  . VAL   A 151 ? 0.2230 0.2217 0.2360 -0.0317 0.0001  0.0729  151 VAL   A CA  
3301 C C   . VAL   A 151 ? 0.2077 0.2059 0.2277 -0.0546 0.0075  0.0631  151 VAL   A C   
3302 O O   . VAL   A 151 ? 0.2094 0.2232 0.2927 -0.0495 0.0037  0.0761  151 VAL   A O   
3303 C CB  . VAL   A 151 ? 0.2512 0.2421 0.2190 -0.0305 -0.0119 0.0839  151 VAL   A CB  
3304 C CG1 . VAL   A 151 ? 0.2398 0.2711 0.2781 -0.0415 -0.0226 0.0682  151 VAL   A CG1 
3305 C CG2 . VAL   A 151 ? 0.2857 0.2353 0.2244 -0.0180 0.0086  0.0685  151 VAL   A CG2 
3315 N N   . TYR   A 152 ? 0.2043 0.2276 0.2156 -0.0351 0.0015  0.0458  152 TYR   A N   
3316 C CA  . TYR   A 152 ? 0.2046 0.2390 0.1931 -0.0525 -0.0106 0.0456  152 TYR   A CA  
3317 C C   . TYR   A 152 ? 0.1821 0.2285 0.1828 -0.0472 0.0041  0.0510  152 TYR   A C   
3318 O O   . TYR   A 152 ? 0.1904 0.2217 0.2127 -0.0468 0.0020  0.0407  152 TYR   A O   
3319 C CB  . TYR   A 152 ? 0.2285 0.2475 0.2059 -0.0601 0.0008  0.0666  152 TYR   A CB  
3320 C CG  . TYR   A 152 ? 0.2331 0.2889 0.2270 -0.0562 0.0015  0.0899  152 TYR   A CG  
3321 C CD1 . TYR   A 152 ? 0.2516 0.3155 0.2601 -0.0387 0.0010  0.1072  152 TYR   A CD1 
3322 C CD2 . TYR   A 152 ? 0.2292 0.3087 0.2186 -0.0646 0.0039  0.0687  152 TYR   A CD2 
3323 C CE1 . TYR   A 152 ? 0.2818 0.3382 0.2670 -0.0257 0.0152  0.1211  152 TYR   A CE1 
3324 C CE2 . TYR   A 152 ? 0.2735 0.3357 0.2507 -0.0546 0.0014  0.0837  152 TYR   A CE2 
3325 C CZ  . TYR   A 152 ? 0.2983 0.3423 0.2581 -0.0471 0.0211  0.1366  152 TYR   A CZ  
3326 O OH  . TYR   A 152 ? 0.3432 0.3713 0.3384 -0.0283 0.0296  0.1634  152 TYR   A OH  
3336 N N   A LEU   A 153 ? 0.1743 0.2220 0.1851 -0.0435 0.0100  0.0528  153 LEU   A N   
3337 N N   B LEU   A 153 ? 0.1838 0.2270 0.1746 -0.0487 0.0018  0.0351  153 LEU   A N   
3338 C CA  A LEU   A 153 ? 0.1660 0.2049 0.1944 -0.0274 0.0076  0.0506  153 LEU   A CA  
3339 C CA  B LEU   A 153 ? 0.1753 0.2177 0.1528 -0.0377 0.0101  0.0270  153 LEU   A CA  
3340 C C   A LEU   A 153 ? 0.1638 0.2092 0.2123 -0.0214 0.0293  0.0378  153 LEU   A C   
3341 C C   B LEU   A 153 ? 0.1776 0.2317 0.1818 -0.0304 0.0201  0.0138  153 LEU   A C   
3342 O O   A LEU   A 153 ? 0.1746 0.2095 0.2235 -0.0274 0.0278  0.0368  153 LEU   A O   
3343 O O   B LEU   A 153 ? 0.1896 0.2381 0.1530 -0.0350 0.0244  0.0030  153 LEU   A O   
3344 C CB  A LEU   A 153 ? 0.1567 0.1961 0.2241 -0.0246 0.0019  0.0433  153 LEU   A CB  
3345 C CB  B LEU   A 153 ? 0.1530 0.2129 0.1491 -0.0221 0.0227  0.0191  153 LEU   A CB  
3346 C CG  A LEU   A 153 ? 0.1582 0.1852 0.2450 -0.0177 0.0016  0.0363  153 LEU   A CG  
3347 C CG  B LEU   A 153 ? 0.1633 0.2029 0.1684 -0.0040 0.0267  0.0266  153 LEU   A CG  
3348 C CD1 A LEU   A 153 ? 0.1562 0.1791 0.2457 -0.0165 -0.0163 0.0441  153 LEU   A CD1 
3349 C CD1 B LEU   A 153 ? 0.1794 0.2062 0.1637 -0.0039 0.0247  0.0114  153 LEU   A CD1 
3350 C CD2 A LEU   A 153 ? 0.1675 0.1847 0.2470 -0.0104 0.0097  0.0287  153 LEU   A CD2 
3351 C CD2 B LEU   A 153 ? 0.1503 0.2037 0.1917 0.0195  0.0289  0.0223  153 LEU   A CD2 
3374 N N   A ALA   A 154 ? 0.1703 0.2066 0.2137 -0.0073 0.0262  0.0347  154 ALA   A N   
3375 N N   B ALA   A 154 ? 0.1832 0.2272 0.1867 -0.0211 0.0386  0.0138  154 ALA   A N   
3376 C CA  A ALA   A 154 ? 0.1827 0.2024 0.2019 -0.0015 0.0171  0.0189  154 ALA   A CA  
3377 C CA  B ALA   A 154 ? 0.1972 0.2291 0.1978 -0.0214 0.0278  0.0037  154 ALA   A CA  
3378 C C   A ALA   A 154 ? 0.1765 0.2042 0.1917 -0.0006 0.0129  0.0207  154 ALA   A C   
3379 C C   B ALA   A 154 ? 0.1969 0.2383 0.1914 -0.0232 0.0237  0.0081  154 ALA   A C   
3380 O O   A ALA   A 154 ? 0.1798 0.1950 0.1993 -0.0005 0.0118  0.0334  154 ALA   A O   
3381 O O   B ALA   A 154 ? 0.1980 0.2291 0.1980 -0.0341 0.0104  0.0110  154 ALA   A O   
3382 C CB  A ALA   A 154 ? 0.1959 0.1976 0.2187 0.0076  0.0053  0.0058  154 ALA   A CB  
3383 C CB  B ALA   A 154 ? 0.2064 0.2310 0.2219 -0.0262 0.0186  -0.0011 154 ALA   A CB  
3394 N N   A VAL   A 155 ? 0.1816 0.2149 0.1880 0.0039  -0.0003 0.0346  155 VAL   A N   
3395 N N   B VAL   A 155 ? 0.2106 0.2580 0.2061 -0.0169 0.0296  0.0238  155 VAL   A N   
3396 C CA  A VAL   A 155 ? 0.1801 0.2237 0.2137 -0.0063 -0.0094 0.0300  155 VAL   A CA  
3397 C CA  B VAL   A 155 ? 0.2137 0.2719 0.2226 -0.0173 0.0335  0.0329  155 VAL   A CA  
3398 C C   A VAL   A 155 ? 0.1917 0.2332 0.2466 -0.0035 -0.0164 0.0272  155 VAL   A C   
3399 C C   B VAL   A 155 ? 0.2374 0.2827 0.2582 -0.0086 0.0456  0.0464  155 VAL   A C   
3400 O O   A VAL   A 155 ? 0.1699 0.2330 0.2547 -0.0031 -0.0254 0.0135  155 VAL   A O   
3401 O O   B VAL   A 155 ? 0.2226 0.2913 0.2564 0.0013  0.0541  0.0566  155 VAL   A O   
3402 C CB  A VAL   A 155 ? 0.1780 0.2220 0.2282 -0.0048 -0.0137 0.0264  155 VAL   A CB  
3403 C CB  B VAL   A 155 ? 0.2031 0.2767 0.2177 -0.0152 0.0211  0.0257  155 VAL   A CB  
3404 C CG1 A VAL   A 155 ? 0.1803 0.2377 0.2448 -0.0123 -0.0197 0.0352  155 VAL   A CG1 
3405 C CG1 B VAL   A 155 ? 0.2085 0.2905 0.2342 -0.0238 0.0080  0.0286  155 VAL   A CG1 
3406 C CG2 A VAL   A 155 ? 0.1954 0.2167 0.2630 0.0033  0.0002  0.0222  155 VAL   A CG2 
3407 C CG2 B VAL   A 155 ? 0.2112 0.2787 0.2445 -0.0117 0.0345  0.0131  155 VAL   A CG2 
3426 N N   A PHE   A 156 ? 0.1996 0.2400 0.2694 0.0008  -0.0131 0.0379  156 PHE   A N   
3427 N N   B PHE   A 156 ? 0.2564 0.2847 0.3088 -0.0108 0.0487  0.0349  156 PHE   A N   
3428 C CA  A PHE   A 156 ? 0.2008 0.2478 0.2842 -0.0048 -0.0021 0.0596  156 PHE   A CA  
3429 C CA  B PHE   A 156 ? 0.2736 0.2994 0.3633 -0.0125 0.0541  0.0331  156 PHE   A CA  
3430 C C   A PHE   A 156 ? 0.2020 0.2560 0.2841 0.0041  0.0062  0.0476  156 PHE   A C   
3431 C C   B PHE   A 156 ? 0.2916 0.3101 0.3937 -0.0002 0.0417  0.0474  156 PHE   A C   
3432 O O   A PHE   A 156 ? 0.1888 0.2433 0.2838 0.0116  -0.0085 0.0233  156 PHE   A O   
3433 O O   B PHE   A 156 ? 0.3167 0.3151 0.4443 -0.0002 0.0318  0.0541  156 PHE   A O   
3434 C CB  A PHE   A 156 ? 0.2096 0.2521 0.3030 -0.0015 -0.0061 0.0765  156 PHE   A CB  
3435 C CB  B PHE   A 156 ? 0.2779 0.3093 0.3943 -0.0252 0.0765  0.0074  156 PHE   A CB  
3436 C CG  A PHE   A 156 ? 0.2484 0.2639 0.3098 0.0265  -0.0279 0.0824  156 PHE   A CG  
3437 C CG  B PHE   A 156 ? 0.3019 0.3242 0.4394 -0.0251 0.0795  -0.0189 156 PHE   A CG  
3438 C CD1 A PHE   A 156 ? 0.2700 0.2755 0.3225 0.0506  -0.0283 0.0816  156 PHE   A CD1 
3439 C CD1 B PHE   A 156 ? 0.3126 0.3307 0.4650 -0.0246 0.0891  -0.0338 156 PHE   A CD1 
3440 C CD2 A PHE   A 156 ? 0.2649 0.2640 0.3152 0.0302  -0.0428 0.0959  156 PHE   A CD2 
3441 C CD2 B PHE   A 156 ? 0.2995 0.3253 0.4409 -0.0366 0.0913  -0.0342 156 PHE   A CD2 
3442 C CE1 A PHE   A 156 ? 0.2840 0.2803 0.3392 0.0570  -0.0148 0.0726  156 PHE   A CE1 
3443 C CE1 B PHE   A 156 ? 0.3157 0.3332 0.4756 -0.0241 0.0980  -0.0481 156 PHE   A CE1 
3444 C CE2 A PHE   A 156 ? 0.2774 0.2713 0.3242 0.0428  -0.0360 0.0912  156 PHE   A CE2 
3445 C CE2 B PHE   A 156 ? 0.3059 0.3310 0.4608 -0.0348 0.0985  -0.0413 156 PHE   A CE2 
3446 C CZ  A PHE   A 156 ? 0.2789 0.2640 0.3279 0.0619  -0.0091 0.0882  156 PHE   A CZ  
3447 C CZ  B PHE   A 156 ? 0.3167 0.3354 0.4703 -0.0215 0.1013  -0.0626 156 PHE   A CZ  
3466 N N   A ASP   A 157 ? 0.2091 0.2650 0.2781 0.0120  -0.0013 0.0525  157 ASP   A N   
3467 N N   B ASP   A 157 ? 0.2678 0.3130 0.3528 0.0106  0.0288  0.0506  157 ASP   A N   
3468 C CA  A ASP   A 157 ? 0.2210 0.2860 0.3021 0.0195  -0.0002 0.0593  157 ASP   A CA  
3469 C CA  B ASP   A 157 ? 0.2502 0.3237 0.3202 0.0096  0.0281  0.0610  157 ASP   A CA  
3470 C C   A ASP   A 157 ? 0.2078 0.2992 0.2957 0.0321  0.0018  0.0687  157 ASP   A C   
3471 C C   B ASP   A 157 ? 0.2389 0.3404 0.2887 0.0232  0.0263  0.0626  157 ASP   A C   
3472 O O   A ASP   A 157 ? 0.2027 0.2924 0.2838 0.0311  -0.0160 0.0709  157 ASP   A O   
3473 O O   B ASP   A 157 ? 0.2273 0.3413 0.2842 0.0204  0.0167  0.0586  157 ASP   A O   
3474 C CB  A ASP   A 157 ? 0.2344 0.2928 0.3322 0.0332  -0.0094 0.0674  157 ASP   A CB  
3475 C CB  B ASP   A 157 ? 0.2344 0.3189 0.3173 0.0090  0.0305  0.0760  157 ASP   A CB  
3476 C CG  A ASP   A 157 ? 0.2525 0.2973 0.3897 0.0401  -0.0221 0.0671  157 ASP   A CG  
3477 C CG  B ASP   A 157 ? 0.2122 0.3095 0.3303 0.0029  0.0317  0.0907  157 ASP   A CG  
3478 O OD1 A ASP   A 157 ? 0.2648 0.3037 0.4270 0.0300  -0.0268 0.0521  157 ASP   A OD1 
3479 O OD1 B ASP   A 157 ? 0.2144 0.3022 0.3816 -0.0061 0.0131  0.0944  157 ASP   A OD1 
3480 O OD2 A ASP   A 157 ? 0.2548 0.2964 0.4214 0.0473  -0.0246 0.0734  157 ASP   A OD2 
3481 O OD2 B ASP   A 157 ? 0.2117 0.3179 0.3372 0.0090  0.0168  0.0857  157 ASP   A OD2 
3490 N N   A LYS   A 158 ? 0.2149 0.3161 0.3092 0.0401  0.0209  0.0662  158 LYS   A N   
3491 N N   B LYS   A 158 ? 0.2478 0.3531 0.2968 0.0302  0.0338  0.0586  158 LYS   A N   
3492 C CA  A LYS   A 158 ? 0.2159 0.3366 0.3329 0.0356  0.0409  0.0493  158 LYS   A CA  
3493 C CA  B LYS   A 158 ? 0.2618 0.3649 0.3028 0.0261  0.0254  0.0686  158 LYS   A CA  
3494 C C   A LYS   A 158 ? 0.2093 0.3449 0.3287 0.0329  0.0464  0.0612  158 LYS   A C   
3495 C C   B LYS   A 158 ? 0.2500 0.3574 0.2861 0.0218  0.0261  0.0801  158 LYS   A C   
3496 O O   A LYS   A 158 ? 0.2043 0.3536 0.3120 0.0171  0.0587  0.0670  158 LYS   A O   
3497 O O   B LYS   A 158 ? 0.2343 0.3470 0.2636 0.0199  0.0373  0.0777  158 LYS   A O   
3498 C CB  A LYS   A 158 ? 0.2372 0.3478 0.3602 0.0313  0.0586  0.0281  158 LYS   A CB  
3499 C CB  B LYS   A 158 ? 0.2826 0.3857 0.3526 0.0270  0.0122  0.0595  158 LYS   A CB  
3500 C CG  A LYS   A 158 ? 0.2588 0.3587 0.3812 0.0322  0.0789  0.0154  158 LYS   A CG  
3501 C CG  B LYS   A 158 ? 0.3148 0.4101 0.4075 0.0267  0.0031  0.0423  158 LYS   A CG  
3502 C CD  A LYS   A 158 ? 0.2833 0.3740 0.3945 0.0314  0.1018  0.0125  158 LYS   A CD  
3503 C CD  B LYS   A 158 ? 0.3504 0.4356 0.4709 0.0279  0.0004  0.0247  158 LYS   A CD  
3504 C CE  A LYS   A 158 ? 0.3102 0.3757 0.3931 0.0238  0.1178  0.0305  158 LYS   A CE  
3505 C CE  B LYS   A 158 ? 0.3713 0.4496 0.5177 0.0264  -0.0066 0.0127  158 LYS   A CE  
3506 N NZ  A LYS   A 158 ? 0.3182 0.3731 0.3787 0.0125  0.1341  0.0467  158 LYS   A NZ  
3507 N NZ  B LYS   A 158 ? 0.3742 0.4563 0.5447 0.0274  -0.0105 0.0040  158 LYS   A NZ  
3534 N N   A ASN   A 159 ? 0.2027 0.3396 0.3428 0.0420  0.0337  0.0572  159 ASN   A N   
3535 N N   B ASN   A 159 ? 0.2490 0.3555 0.3055 0.0187  0.0091  0.0833  159 ASN   A N   
3536 C CA  A ASN   A 159 ? 0.2079 0.3312 0.3484 0.0319  0.0174  0.0601  159 ASN   A CA  
3537 C CA  B ASN   A 159 ? 0.2577 0.3623 0.3245 0.0052  0.0040  0.0741  159 ASN   A CA  
3538 C C   A ASN   A 159 ? 0.2063 0.3259 0.3101 0.0206  0.0211  0.0681  159 ASN   A C   
3539 C C   B ASN   A 159 ? 0.2478 0.3485 0.2876 -0.0122 0.0097  0.0645  159 ASN   A C   
3540 O O   A ASN   A 159 ? 0.1940 0.3265 0.2724 0.0246  0.0003  0.0704  159 ASN   A O   
3541 O O   B ASN   A 159 ? 0.2392 0.3452 0.2683 -0.0249 -0.0035 0.0435  159 ASN   A O   
3542 C CB  A ASN   A 159 ? 0.2239 0.3357 0.3986 0.0269  -0.0038 0.0605  159 ASN   A CB  
3543 C CB  B ASN   A 159 ? 0.2778 0.3811 0.3973 0.0131  -0.0079 0.0839  159 ASN   A CB  
3544 C CG  A ASN   A 159 ? 0.2407 0.3452 0.4481 0.0221  -0.0044 0.0575  159 ASN   A CG  
3545 C CG  B ASN   A 159 ? 0.2954 0.3962 0.4707 0.0172  -0.0143 0.0865  159 ASN   A CG  
3546 O OD1 A ASN   A 159 ? 0.2438 0.3482 0.4595 0.0258  0.0047  0.0719  159 ASN   A OD1 
3547 O OD1 B ASN   A 159 ? 0.3037 0.4069 0.5081 0.0214  -0.0067 0.0793  159 ASN   A OD1 
3548 N ND2 A ASN   A 159 ? 0.2452 0.3491 0.4652 0.0134  -0.0188 0.0433  159 ASN   A ND2 
3549 N ND2 B ASN   A 159 ? 0.3007 0.4024 0.4933 0.0114  -0.0341 0.0819  159 ASN   A ND2 
3562 N N   A LEU   A 160 ? 0.2060 0.3079 0.3236 0.0085  0.0281  0.0650  160 LEU   A N   
3563 N N   B LEU   A 160 ? 0.2386 0.3269 0.2694 -0.0147 0.0088  0.0745  160 LEU   A N   
3564 C CA  A LEU   A 160 ? 0.2100 0.2912 0.2982 0.0057  0.0402  0.0779  160 LEU   A CA  
3565 C CA  B LEU   A 160 ? 0.2493 0.3165 0.2601 -0.0163 0.0290  0.0710  160 LEU   A CA  
3566 C C   A LEU   A 160 ? 0.1952 0.2900 0.3009 0.0061  0.0311  0.0761  160 LEU   A C   
3567 C C   B LEU   A 160 ? 0.2447 0.2976 0.2515 -0.0366 0.0294  0.0768  160 LEU   A C   
3568 O O   A LEU   A 160 ? 0.1866 0.2926 0.3257 0.0121  0.0271  0.0858  160 LEU   A O   
3569 O O   B LEU   A 160 ? 0.2444 0.2952 0.2658 -0.0482 0.0218  0.0769  160 LEU   A O   
3570 C CB  A LEU   A 160 ? 0.2171 0.2793 0.2733 0.0003  0.0438  0.0847  160 LEU   A CB  
3571 C CB  B LEU   A 160 ? 0.2553 0.3166 0.2701 -0.0041 0.0378  0.0683  160 LEU   A CB  
3572 C CG  A LEU   A 160 ? 0.2198 0.2799 0.2862 -0.0077 0.0313  0.0520  160 LEU   A CG  
3573 C CG  B LEU   A 160 ? 0.2578 0.3185 0.3035 0.0059  0.0211  0.0455  160 LEU   A CG  
3574 C CD1 A LEU   A 160 ? 0.2178 0.2832 0.2926 -0.0058 0.0339  0.0278  160 LEU   A CD1 
3575 C CD1 B LEU   A 160 ? 0.2553 0.3185 0.3231 0.0099  0.0202  0.0282  160 LEU   A CD1 
3576 C CD2 A LEU   A 160 ? 0.2216 0.2757 0.2775 -0.0152 0.0340  0.0507  160 LEU   A CD2 
3577 C CD2 B LEU   A 160 ? 0.2596 0.3187 0.3015 0.0118  0.0190  0.0502  160 LEU   A CD2 
3600 N N   A TYR   A 161 ? 0.1887 0.2750 0.2761 -0.0010 0.0307  0.0668  161 TYR   A N   
3601 N N   B TYR   A 161 ? 0.2406 0.2750 0.2411 -0.0452 0.0437  0.0670  161 TYR   A N   
3602 C CA  A TYR   A 161 ? 0.1868 0.2598 0.2895 -0.0145 0.0343  0.0706  161 TYR   A CA  
3603 C CA  B TYR   A 161 ? 0.2397 0.2680 0.2419 -0.0427 0.0316  0.0608  161 TYR   A CA  
3604 C C   A TYR   A 161 ? 0.1714 0.2665 0.3088 -0.0186 0.0411  0.0642  161 TYR   A C   
3605 C C   B TYR   A 161 ? 0.2455 0.2820 0.2399 -0.0473 0.0174  0.0790  161 TYR   A C   
3606 O O   A TYR   A 161 ? 0.1720 0.2715 0.3125 -0.0225 0.0431  0.0691  161 TYR   A O   
3607 O O   B TYR   A 161 ? 0.2409 0.2823 0.2445 -0.0394 0.0095  0.0674  161 TYR   A O   
3608 C CB  A TYR   A 161 ? 0.2023 0.2558 0.2953 -0.0164 0.0339  0.0686  161 TYR   A CB  
3609 C CB  B TYR   A 161 ? 0.2342 0.2524 0.2314 -0.0288 0.0353  0.0531  161 TYR   A CB  
3610 C CG  A TYR   A 161 ? 0.2143 0.2520 0.2852 -0.0140 0.0173  0.0614  161 TYR   A CG  
3611 C CG  B TYR   A 161 ? 0.2255 0.2347 0.2288 -0.0254 0.0395  0.0423  161 TYR   A CG  
3612 C CD1 A TYR   A 161 ? 0.2064 0.2445 0.2741 -0.0120 0.0058  0.0695  161 TYR   A CD1 
3613 C CD1 B TYR   A 161 ? 0.2143 0.2329 0.2499 -0.0281 0.0536  0.0371  161 TYR   A CD1 
3614 C CD2 A TYR   A 161 ? 0.2158 0.2455 0.2783 -0.0078 0.0070  0.0622  161 TYR   A CD2 
3615 C CD2 B TYR   A 161 ? 0.2249 0.2322 0.2433 -0.0230 0.0500  0.0454  161 TYR   A CD2 
3616 C CE1 A TYR   A 161 ? 0.2072 0.2327 0.2781 -0.0128 0.0061  0.0723  161 TYR   A CE1 
3617 C CE1 B TYR   A 161 ? 0.2147 0.2409 0.2386 -0.0243 0.0723  0.0355  161 TYR   A CE1 
3618 C CE2 A TYR   A 161 ? 0.2155 0.2287 0.2728 -0.0128 -0.0038 0.0744  161 TYR   A CE2 
3619 C CE2 B TYR   A 161 ? 0.2283 0.2439 0.2451 -0.0180 0.0492  0.0505  161 TYR   A CE2 
3620 C CZ  A TYR   A 161 ? 0.2204 0.2316 0.2927 -0.0151 -0.0015 0.0729  161 TYR   A CZ  
3621 C CZ  B TYR   A 161 ? 0.2277 0.2403 0.2281 -0.0227 0.0582  0.0588  161 TYR   A CZ  
3622 O OH  A TYR   A 161 ? 0.2358 0.2247 0.3375 -0.0293 -0.0184 0.0875  161 TYR   A OH  
3623 O OH  B TYR   A 161 ? 0.2318 0.2482 0.2514 -0.0226 0.0335  0.0717  161 TYR   A OH  
3642 N N   A ASP   A 162 ? 0.1526 0.2673 0.3260 -0.0088 0.0468  0.0760  162 ASP   A N   
3643 N N   B ASP   A 162 ? 0.2464 0.2954 0.2648 -0.0707 0.0278  0.0858  162 ASP   A N   
3644 C CA  A ASP   A 162 ? 0.1523 0.2856 0.3305 -0.0104 0.0596  0.0610  162 ASP   A CA  
3645 C CA  B ASP   A 162 ? 0.2607 0.3130 0.2934 -0.0585 0.0234  0.0794  162 ASP   A CA  
3646 C C   A ASP   A 162 ? 0.1487 0.3073 0.3148 -0.0000 0.0475  0.0521  162 ASP   A C   
3647 C C   B ASP   A 162 ? 0.2769 0.3077 0.2832 -0.0558 0.0073  0.0720  162 ASP   A C   
3648 O O   A ASP   A 162 ? 0.1420 0.3133 0.3088 0.0045  0.0549  0.0465  162 ASP   A O   
3649 O O   B ASP   A 162 ? 0.2909 0.3151 0.2831 -0.0474 -0.0079 0.0771  162 ASP   A O   
3650 C CB  A ASP   A 162 ? 0.1583 0.2886 0.3509 -0.0151 0.0715  0.0508  162 ASP   A CB  
3651 C CB  B ASP   A 162 ? 0.2626 0.3348 0.3361 -0.0463 0.0401  0.0778  162 ASP   A CB  
3652 C CG  A ASP   A 162 ? 0.1760 0.2975 0.3724 -0.0139 0.0648  0.0447  162 ASP   A CG  
3653 C CG  B ASP   A 162 ? 0.2682 0.3506 0.3536 -0.0307 0.0539  0.0737  162 ASP   A CG  
3654 O OD1 A ASP   A 162 ? 0.1815 0.3070 0.3763 -0.0104 0.0705  0.0484  162 ASP   A OD1 
3655 O OD1 B ASP   A 162 ? 0.2734 0.3568 0.3685 -0.0150 0.0566  0.0701  162 ASP   A OD1 
3656 O OD2 A ASP   A 162 ? 0.1864 0.2998 0.3808 -0.0137 0.0731  0.0399  162 ASP   A OD2 
3657 O OD2 B ASP   A 162 ? 0.2662 0.3573 0.3517 -0.0322 0.0666  0.0707  162 ASP   A OD2 
3666 N N   A LYS   A 163 ? 0.1662 0.3222 0.3114 0.0143  0.0149  0.0478  163 LYS   A N   
3667 N N   B LYS   A 163 ? 0.2874 0.3083 0.2778 -0.0487 -0.0002 0.0533  163 LYS   A N   
3668 C CA  A LYS   A 163 ? 0.1792 0.3358 0.3059 0.0116  -0.0054 0.0398  163 LYS   A CA  
3669 C CA  B LYS   A 163 ? 0.2995 0.3186 0.2988 -0.0466 0.0014  0.0435  163 LYS   A CA  
3670 C C   A LYS   A 163 ? 0.1742 0.3265 0.2638 -0.0026 0.0105  0.0229  163 LYS   A C   
3671 C C   B LYS   A 163 ? 0.2879 0.2956 0.2729 -0.0410 0.0050  0.0342  163 LYS   A C   
3672 O O   A LYS   A 163 ? 0.1604 0.3211 0.2599 -0.0070 0.0138  0.0121  163 LYS   A O   
3673 O O   B LYS   A 163 ? 0.2852 0.2974 0.2802 -0.0379 0.0076  0.0218  163 LYS   A O   
3674 C CB  A LYS   A 163 ? 0.2020 0.3536 0.3409 0.0325  -0.0265 0.0471  163 LYS   A CB  
3675 C CB  B LYS   A 163 ? 0.3265 0.3540 0.3612 -0.0411 -0.0060 0.0504  163 LYS   A CB  
3676 C CG  A LYS   A 163 ? 0.2386 0.3722 0.3798 0.0307  -0.0258 0.0466  163 LYS   A CG  
3677 C CG  B LYS   A 163 ? 0.3452 0.3823 0.4180 -0.0429 -0.0135 0.0582  163 LYS   A CG  
3678 C CD  A LYS   A 163 ? 0.2797 0.3911 0.4308 0.0324  -0.0249 0.0343  163 LYS   A CD  
3679 C CD  B LYS   A 163 ? 0.3615 0.4067 0.4718 -0.0415 -0.0154 0.0646  163 LYS   A CD  
3680 C CE  A LYS   A 163 ? 0.3070 0.4041 0.4737 0.0231  -0.0198 0.0300  163 LYS   A CE  
3681 C CE  B LYS   A 163 ? 0.3669 0.4267 0.5177 -0.0447 -0.0134 0.0611  163 LYS   A CE  
3682 N NZ  A LYS   A 163 ? 0.3204 0.4135 0.5005 0.0153  -0.0149 0.0256  163 LYS   A NZ  
3683 N NZ  B LYS   A 163 ? 0.3741 0.4387 0.5376 -0.0516 -0.0048 0.0615  163 LYS   A NZ  
3710 N N   A LEU   A 164 ? 0.1628 0.3113 0.2226 -0.0077 0.0061  0.0170  164 LEU   A N   
3711 N N   B LEU   A 164 ? 0.2741 0.2699 0.2449 -0.0332 -0.0035 0.0410  164 LEU   A N   
3712 C CA  A LEU   A 164 ? 0.1732 0.2929 0.2047 -0.0184 0.0333  0.0231  164 LEU   A CA  
3713 C CA  B LEU   A 164 ? 0.2774 0.2509 0.2461 -0.0272 0.0056  0.0455  164 LEU   A CA  
3714 C C   A LEU   A 164 ? 0.1824 0.2902 0.1938 -0.0179 0.0282  0.0233  164 LEU   A C   
3715 C C   B LEU   A 164 ? 0.2825 0.2477 0.2440 -0.0289 0.0048  0.0479  164 LEU   A C   
3716 O O   A LEU   A 164 ? 0.1970 0.2929 0.1879 -0.0189 0.0224  -0.0078 164 LEU   A O   
3717 O O   B LEU   A 164 ? 0.2852 0.2303 0.2483 -0.0457 0.0111  0.0475  164 LEU   A O   
3718 C CB  A LEU   A 164 ? 0.1643 0.2773 0.2167 -0.0311 0.0431  0.0243  164 LEU   A CB  
3719 C CB  B LEU   A 164 ? 0.2635 0.2399 0.2486 -0.0246 0.0219  0.0359  164 LEU   A CB  
3720 C CG  A LEU   A 164 ? 0.1614 0.2655 0.2225 -0.0241 0.0289  0.0376  164 LEU   A CG  
3721 C CG  B LEU   A 164 ? 0.2629 0.2324 0.2589 -0.0299 0.0273  0.0446  164 LEU   A CG  
3722 C CD1 A LEU   A 164 ? 0.1516 0.2677 0.2225 -0.0221 0.0354  0.0271  164 LEU   A CD1 
3723 C CD1 B LEU   A 164 ? 0.2585 0.2336 0.2806 -0.0337 0.0363  0.0565  164 LEU   A CD1 
3724 C CD2 A LEU   A 164 ? 0.1491 0.2629 0.2268 -0.0263 0.0290  0.0441  164 LEU   A CD2 
3725 C CD2 B LEU   A 164 ? 0.2662 0.2338 0.2674 -0.0316 0.0269  0.0398  164 LEU   A CD2 
3748 N N   A VAL   A 165 ? 0.1662 0.2808 0.1988 -0.0245 0.0286  0.0385  165 VAL   A N   
3749 N N   B VAL   A 165 ? 0.2721 0.2501 0.2364 -0.0242 0.0030  0.0524  165 VAL   A N   
3750 C CA  A VAL   A 165 ? 0.1692 0.2726 0.2148 -0.0210 0.0231  0.0468  165 VAL   A CA  
3751 C CA  B VAL   A 165 ? 0.2747 0.2603 0.2592 -0.0217 0.0109  0.0504  165 VAL   A CA  
3752 C C   A VAL   A 165 ? 0.1679 0.2816 0.2253 -0.0209 0.0121  0.0502  165 VAL   A C   
3753 C C   B VAL   A 165 ? 0.2680 0.2672 0.2704 -0.0286 0.0362  0.0428  165 VAL   A C   
3754 O O   A VAL   A 165 ? 0.1741 0.2751 0.2153 -0.0240 0.0149  0.0532  165 VAL   A O   
3755 O O   B VAL   A 165 ? 0.2737 0.2644 0.2526 -0.0244 0.0396  0.0240  165 VAL   A O   
3756 C CB  A VAL   A 165 ? 0.1859 0.2732 0.2281 -0.0178 0.0227  0.0445  165 VAL   A CB  
3757 C CB  B VAL   A 165 ? 0.2830 0.2555 0.2729 -0.0061 0.0087  0.0517  165 VAL   A CB  
3758 C CG1 A VAL   A 165 ? 0.1833 0.2747 0.2032 -0.0127 0.0137  0.0391  165 VAL   A CG1 
3759 C CG1 B VAL   A 165 ? 0.2927 0.2550 0.3000 -0.0099 -0.0025 0.0431  165 VAL   A CG1 
3760 C CG2 A VAL   A 165 ? 0.1993 0.2725 0.2505 -0.0132 0.0072  0.0385  165 VAL   A CG2 
3761 C CG2 B VAL   A 165 ? 0.2822 0.2479 0.2560 0.0063  0.0158  0.0624  165 VAL   A CG2 
3780 N N   A SER   A 166 ? 0.1623 0.2860 0.2544 -0.0164 -0.0137 0.0487  166 SER   A N   
3781 N N   B SER   A 166 ? 0.2527 0.2711 0.2888 -0.0289 0.0272  0.0605  166 SER   A N   
3782 C CA  A SER   A 166 ? 0.1592 0.3026 0.2700 -0.0138 -0.0159 0.0390  166 SER   A CA  
3783 C CA  B SER   A 166 ? 0.2486 0.2952 0.2972 -0.0305 0.0288  0.0700  166 SER   A CA  
3784 C C   A SER   A 166 ? 0.1555 0.3036 0.2815 -0.0011 -0.0022 0.0352  166 SER   A C   
3785 C C   B SER   A 166 ? 0.2460 0.3196 0.2970 -0.0330 0.0099  0.0629  166 SER   A C   
3786 O O   A SER   A 166 ? 0.1706 0.3086 0.3057 0.0014  0.0124  0.0178  166 SER   A O   
3787 O O   B SER   A 166 ? 0.2447 0.3256 0.2807 -0.0252 -0.0058 0.0578  166 SER   A O   
3788 C CB  A SER   A 166 ? 0.1798 0.3226 0.2920 -0.0082 -0.0288 0.0191  166 SER   A CB  
3789 C CB  B SER   A 166 ? 0.2659 0.3010 0.3440 -0.0161 0.0414  0.0685  166 SER   A CB  
3790 O OG  A SER   A 166 ? 0.2308 0.3435 0.3158 -0.0293 -0.0244 0.0419  166 SER   A OG  
3791 O OG  B SER   A 166 ? 0.2929 0.3151 0.4268 -0.0098 0.0371  0.0434  166 SER   A OG  
3802 N N   A SER   A 167 ? 0.1655 0.3050 0.2851 0.0160  0.0013  0.0425  167 SER   A N   
3803 N N   B SER   A 167 ? 0.2604 0.3443 0.3321 -0.0381 0.0144  0.0662  167 SER   A N   
3804 C CA  A SER   A 167 ? 0.1758 0.3017 0.2664 0.0160  0.0039  0.0378  167 SER   A CA  
3805 C CA  B SER   A 167 ? 0.2833 0.3666 0.3556 -0.0409 0.0182  0.0650  167 SER   A CA  
3806 C C   A SER   A 167 ? 0.1822 0.3020 0.2549 0.0175  0.0179  0.0331  167 SER   A C   
3807 C C   B SER   A 167 ? 0.2891 0.3899 0.3714 -0.0367 0.0087  0.0551  167 SER   A C   
3808 O O   A SER   A 167 ? 0.2072 0.3024 0.2720 0.0179  -0.0009 0.0362  167 SER   A O   
3809 O O   B SER   A 167 ? 0.2774 0.3692 0.3700 -0.0504 0.0265  0.0541  167 SER   A O   
3810 C CB  A SER   A 167 ? 0.1794 0.3074 0.2790 0.0115  -0.0065 0.0391  167 SER   A CB  
3811 C CB  B SER   A 167 ? 0.3015 0.3713 0.3720 -0.0331 0.0192  0.0732  167 SER   A CB  
3812 O OG  A SER   A 167 ? 0.1770 0.3146 0.2902 0.0018  0.0083  0.0489  167 SER   A OG  
3813 O OG  B SER   A 167 ? 0.3103 0.3790 0.3774 -0.0292 0.0127  0.0741  167 SER   A OG  
3824 N N   A PHE   A 168 ? 0.1790 0.3081 0.2454 0.0268  0.0429  0.0216  168 PHE   A N   
3825 N N   B PHE   A 168 ? 0.3220 0.4325 0.3914 -0.0137 -0.0126 0.0365  168 PHE   A N   
3826 C CA  A PHE   A 168 ? 0.1714 0.3131 0.2331 0.0150  0.0314  0.0106  168 PHE   A CA  
3827 C CA  B PHE   A 168 ? 0.3613 0.4774 0.4385 0.0049  -0.0268 0.0166  168 PHE   A CA  
3828 C C   A PHE   A 168 ? 0.1738 0.3147 0.2461 0.0063  0.0431  -0.0025 168 PHE   A C   
3829 C C   B PHE   A 168 ? 0.3704 0.4947 0.4748 0.0215  -0.0405 0.0095  168 PHE   A C   
3830 O O   A PHE   A 168 ? 0.1978 0.3100 0.3099 -0.0162 0.0560  0.0119  168 PHE   A O   
3831 O O   B PHE   A 168 ? 0.3612 0.4961 0.4748 0.0276  -0.0471 0.0154  168 PHE   A O   
3832 C CB  A PHE   A 168 ? 0.1724 0.3119 0.2178 0.0126  0.0037  0.0134  168 PHE   A CB  
3833 C CB  B PHE   A 168 ? 0.3862 0.5040 0.4467 0.0037  -0.0228 0.0140  168 PHE   A CB  
3834 C CG  A PHE   A 168 ? 0.1718 0.3078 0.2067 0.0094  -0.0215 0.0269  168 PHE   A CG  
3835 C CG  B PHE   A 168 ? 0.4083 0.5300 0.4597 0.0031  -0.0187 0.0094  168 PHE   A CG  
3836 C CD1 A PHE   A 168 ? 0.1780 0.3075 0.2018 0.0063  -0.0246 0.0303  168 PHE   A CD1 
3837 C CD1 B PHE   A 168 ? 0.4174 0.5424 0.4643 -0.0007 -0.0129 0.0065  168 PHE   A CD1 
3838 C CD2 A PHE   A 168 ? 0.1546 0.3034 0.1901 0.0010  -0.0136 0.0323  168 PHE   A CD2 
3839 C CD2 B PHE   A 168 ? 0.4145 0.5396 0.4607 0.0024  -0.0139 0.0118  168 PHE   A CD2 
3840 C CE1 A PHE   A 168 ? 0.1774 0.3059 0.1979 0.0051  -0.0232 0.0250  168 PHE   A CE1 
3841 C CE1 B PHE   A 168 ? 0.4220 0.5490 0.4597 0.0002  -0.0116 0.0071  168 PHE   A CE1 
3842 C CE2 A PHE   A 168 ? 0.1725 0.2970 0.1819 0.0068  -0.0018 0.0342  168 PHE   A CE2 
3843 C CE2 B PHE   A 168 ? 0.4206 0.5471 0.4621 0.0038  -0.0095 0.0077  168 PHE   A CE2 
3844 C CZ  A PHE   A 168 ? 0.1793 0.3016 0.1917 0.0078  -0.0136 0.0242  168 PHE   A CZ  
3845 C CZ  B PHE   A 168 ? 0.4236 0.5510 0.4630 0.0031  -0.0092 0.0082  168 PHE   A CZ  
3864 N N   A LEU   A 169 ? 0.1800 0.3238 0.2643 0.0045  0.0427  -0.0288 169 LEU   A N   
3865 N N   B LEU   A 169 ? 0.3901 0.5086 0.5004 0.0276  -0.0427 -0.0149 169 LEU   A N   
3866 C CA  A LEU   A 169 ? 0.2109 0.3371 0.3045 0.0134  0.0297  -0.0252 169 LEU   A CA  
3867 C CA  B LEU   A 169 ? 0.4025 0.5213 0.5098 0.0377  -0.0353 -0.0312 169 LEU   A CA  
3868 C C   A LEU   A 169 ? 0.2148 0.3386 0.3284 0.0053  0.0217  -0.0052 169 LEU   A C   
3869 C C   B LEU   A 169 ? 0.4111 0.5279 0.5429 0.0424  -0.0285 -0.0510 169 LEU   A C   
3870 O O   A LEU   A 169 ? 0.2212 0.3407 0.3625 -0.0052 0.0141  -0.0067 169 LEU   A O   
3871 O O   B LEU   A 169 ? 0.4092 0.5330 0.5600 0.0435  -0.0229 -0.0633 169 LEU   A O   
3872 C CB  A LEU   A 169 ? 0.2356 0.3470 0.3206 0.0285  0.0193  -0.0371 169 LEU   A CB  
3873 C CB  B LEU   A 169 ? 0.4156 0.5290 0.4861 0.0364  -0.0334 -0.0341 169 LEU   A CB  
3874 C CG  A LEU   A 169 ? 0.2603 0.3597 0.3431 0.0200  -0.0000 -0.0512 169 LEU   A CG  
3875 C CG  B LEU   A 169 ? 0.4234 0.5350 0.4649 0.0348  -0.0354 -0.0430 169 LEU   A CG  
3876 C CD1 A LEU   A 169 ? 0.2738 0.3592 0.3640 0.0167  -0.0055 -0.0562 169 LEU   A CD1 
3877 C CD1 B LEU   A 169 ? 0.4286 0.5367 0.4551 0.0325  -0.0390 -0.0408 169 LEU   A CD1 
3878 C CD2 A LEU   A 169 ? 0.2659 0.3702 0.3405 0.0163  0.0076  -0.0524 169 LEU   A CD2 
3879 C CD2 B LEU   A 169 ? 0.4234 0.5377 0.4580 0.0358  -0.0330 -0.0484 169 LEU   A CD2 
3880 O OXT A LEU   A 169 ? 0.2049 0.3499 0.3387 0.0034  0.0123  0.0130  169 LEU   A OXT 
3881 O OXT B LEU   A 169 ? 0.4137 0.5280 0.5584 0.0453  -0.0334 -0.0604 169 LEU   A OXT 
3904 N N   A SER   B 1   ? 0.4179 0.3642 0.3949 -0.0646 -0.1138 0.0403  1   SER   B N   
3905 N N   B SER   B 1   ? 0.3794 0.3609 0.3606 -0.1114 -0.0798 0.0585  1   SER   B N   
3906 C CA  A SER   B 1   ? 0.4147 0.3732 0.3969 -0.0735 -0.1090 0.0329  1   SER   B CA  
3907 C CA  B SER   B 1   ? 0.3663 0.3653 0.3637 -0.1217 -0.0801 0.0639  1   SER   B CA  
3908 C C   A SER   B 1   ? 0.3989 0.3828 0.3920 -0.0704 -0.0989 0.0451  1   SER   B C   
3909 C C   B SER   B 1   ? 0.3244 0.3596 0.3203 -0.1235 -0.0918 0.0817  1   SER   B C   
3910 O O   A SER   B 1   ? 0.4088 0.3839 0.3838 -0.0638 -0.0871 0.0420  1   SER   B O   
3911 O O   B SER   B 1   ? 0.3336 0.3603 0.2763 -0.1102 -0.0883 0.0797  1   SER   B O   
3912 C CB  A SER   B 1   ? 0.4195 0.3672 0.3963 -0.0798 -0.1155 0.0114  1   SER   B CB  
3913 C CB  B SER   B 1   ? 0.3838 0.3691 0.3847 -0.1234 -0.0695 0.0496  1   SER   B CB  
3914 O OG  A SER   B 1   ? 0.4373 0.3745 0.4457 -0.0774 -0.0996 0.0075  1   SER   B OG  
3915 O OG  B SER   B 1   ? 0.4064 0.3847 0.4509 -0.1178 -0.0595 0.0410  1   SER   B OG  
3930 N N   A MET   B 2   ? 0.3836 0.3887 0.3967 -0.0662 -0.0902 0.0674  2   MET   B N   
3931 N N   B MET   B 2   ? 0.2951 0.3503 0.3264 -0.1271 -0.0860 0.1229  2   MET   B N   
3932 C CA  A MET   B 2   ? 0.3701 0.3884 0.4013 -0.0563 -0.0805 0.0816  2   MET   B CA  
3933 C CA  B MET   B 2   ? 0.2955 0.3508 0.3299 -0.1087 -0.0871 0.1451  2   MET   B CA  
3934 C C   A MET   B 2   ? 0.3357 0.3698 0.3665 -0.0558 -0.0804 0.1050  2   MET   B C   
3935 C C   B MET   B 2   ? 0.2717 0.3398 0.3075 -0.0893 -0.0909 0.1591  2   MET   B C   
3936 O O   A MET   B 2   ? 0.3345 0.3834 0.3898 -0.0489 -0.0847 0.1079  2   MET   B O   
3937 O O   B MET   B 2   ? 0.2674 0.3611 0.3317 -0.0808 -0.0936 0.1516  2   MET   B O   
3938 C CB  A MET   B 2   ? 0.3948 0.4116 0.4706 -0.0388 -0.0613 0.0601  2   MET   B CB  
3939 C CB  B MET   B 2   ? 0.3342 0.3823 0.4175 -0.0847 -0.0822 0.1193  2   MET   B CB  
3940 C CG  A MET   B 2   ? 0.4178 0.4356 0.5496 -0.0224 -0.0411 0.0481  2   MET   B CG  
3941 C CG  B MET   B 2   ? 0.3612 0.4080 0.4935 -0.0645 -0.0682 0.1138  2   MET   B CG  
3942 S SD  A MET   B 2   ? 0.4439 0.4558 0.6259 -0.0086 -0.0216 0.0395  2   MET   B SD  
3943 S SD  B MET   B 2   ? 0.3957 0.4357 0.5691 -0.0477 -0.0523 0.1028  2   MET   B SD  
3944 C CE  A MET   B 2   ? 0.4431 0.4562 0.6101 -0.0093 -0.0137 0.0479  2   MET   B CE  
3945 C CE  B MET   B 2   ? 0.3901 0.4359 0.5519 -0.0573 -0.0481 0.0997  2   MET   B CE  
3964 N N   A VAL   B 3   ? 0.3023 0.3338 0.3392 -0.0671 -0.0712 0.1136  3   VAL   B N   
3965 N N   B VAL   B 3   ? 0.2480 0.3119 0.3016 -0.0918 -0.0735 0.1576  3   VAL   B N   
3966 C CA  A VAL   B 3   ? 0.2762 0.2961 0.3285 -0.0733 -0.0718 0.1032  3   VAL   B CA  
3967 C CA  B VAL   B 3   ? 0.2420 0.2909 0.3049 -0.0752 -0.0736 0.1190  3   VAL   B CA  
3968 C C   A VAL   B 3   ? 0.2459 0.2664 0.2822 -0.0719 -0.0709 0.0996  3   VAL   B C   
3969 C C   B VAL   B 3   ? 0.2312 0.2783 0.2674 -0.0601 -0.0706 0.1068  3   VAL   B C   
3970 O O   A VAL   B 3   ? 0.2396 0.2553 0.3051 -0.0716 -0.0772 0.0990  3   VAL   B O   
3971 O O   B VAL   B 3   ? 0.2267 0.2896 0.2822 -0.0335 -0.0918 0.1046  3   VAL   B O   
3972 C CB  A VAL   B 3   ? 0.2886 0.2947 0.3740 -0.0763 -0.0681 0.0879  3   VAL   B CB  
3973 C CB  B VAL   B 3   ? 0.2583 0.2822 0.3415 -0.0675 -0.0669 0.1034  3   VAL   B CB  
3974 C CG1 A VAL   B 3   ? 0.3011 0.2863 0.4004 -0.0743 -0.0659 0.0819  3   VAL   B CG1 
3975 C CG1 B VAL   B 3   ? 0.2719 0.2708 0.3571 -0.0639 -0.0580 0.1044  3   VAL   B CG1 
3976 C CG2 A VAL   B 3   ? 0.2921 0.2962 0.3833 -0.0791 -0.0610 0.0905  3   VAL   B CG2 
3977 C CG2 B VAL   B 3   ? 0.2638 0.2753 0.3582 -0.0677 -0.0611 0.1084  3   VAL   B CG2 
3996 N N   . ASN   B 4   ? 0.2358 0.2603 0.2704 -0.0622 -0.0551 0.0794  4   ASN   B N   
3997 C CA  . ASN   B 4   ? 0.2330 0.2588 0.2426 -0.0599 -0.0617 0.0530  4   ASN   B CA  
3998 C C   . ASN   B 4   ? 0.2397 0.2659 0.2136 -0.0551 -0.0704 0.0413  4   ASN   B C   
3999 O O   . ASN   B 4   ? 0.2503 0.2709 0.2557 -0.0537 -0.0687 0.0254  4   ASN   B O   
4000 C CB  . ASN   B 4   ? 0.2509 0.2491 0.2279 -0.0454 -0.0735 0.0587  4   ASN   B CB  
4001 C CG  . ASN   B 4   ? 0.2400 0.2235 0.2000 -0.0526 -0.0785 0.0385  4   ASN   B CG  
4002 O OD1 . ASN   B 4   ? 0.2403 0.2059 0.2054 -0.0494 -0.0762 0.0353  4   ASN   B OD1 
4003 N ND2 . ASN   B 4   ? 0.2552 0.2300 0.2229 -0.0227 -0.0530 0.0382  4   ASN   B ND2 
4011 N N   . SER   B 5   ? 0.2580 0.2730 0.2220 -0.0634 -0.0340 0.0403  5   SER   B N   
4012 C CA  . SER   B 5   ? 0.2885 0.3135 0.2644 -0.0512 -0.0009 0.0408  5   SER   B CA  
4013 C C   . SER   B 5   ? 0.3024 0.3096 0.3056 -0.0704 0.0077  0.0392  5   SER   B C   
4014 O O   . SER   B 5   ? 0.3254 0.2969 0.3961 -0.0548 0.0493  0.0199  5   SER   B O   
4015 C CB  . SER   B 5   ? 0.3159 0.3472 0.3438 -0.0339 0.0117  0.0614  5   SER   B CB  
4016 O OG  . SER   B 5   ? 0.3543 0.3897 0.4310 -0.0174 0.0248  0.0698  5   SER   B OG  
4022 N N   . PHE   B 6   ? 0.3259 0.3334 0.2827 -0.0718 0.0193  0.0439  6   PHE   B N   
4023 C CA  . PHE   B 6   ? 0.3309 0.3375 0.2412 -0.1011 0.0199  0.0255  6   PHE   B CA  
4024 C C   . PHE   B 6   ? 0.3872 0.3758 0.2824 -0.1074 0.0320  -0.0303 6   PHE   B C   
4025 O O   . PHE   B 6   ? 0.3954 0.4337 0.3213 -0.0997 -0.0030 -0.0469 6   PHE   B O   
4026 C CB  . PHE   B 6   ? 0.2946 0.3119 0.2315 -0.0905 0.0067  0.0301  6   PHE   B CB  
4027 C CG  . PHE   B 6   ? 0.2621 0.2750 0.2318 -0.0908 -0.0087 0.0205  6   PHE   B CG  
4028 C CD1 . PHE   B 6   ? 0.2578 0.2508 0.2000 -0.0833 -0.0296 0.0126  6   PHE   B CD1 
4029 C CD2 . PHE   B 6   ? 0.2402 0.2723 0.1969 -0.0712 -0.0081 0.0445  6   PHE   B CD2 
4030 C CE1 . PHE   B 6   ? 0.2582 0.2339 0.2015 -0.0617 -0.0284 0.0158  6   PHE   B CE1 
4031 C CE2 . PHE   B 6   ? 0.2433 0.2666 0.2373 -0.0611 -0.0034 0.0388  6   PHE   B CE2 
4032 C CZ  . PHE   B 6   ? 0.2519 0.2349 0.2246 -0.0618 -0.0210 0.0218  6   PHE   B CZ  
4042 N N   A SER   B 7   ? 0.4144 0.3653 0.2956 -0.1184 0.0478  -0.0544 7   SER   B N   
4043 N N   B SER   B 7   ? 0.4184 0.3630 0.2874 -0.1236 0.0472  -0.0587 7   SER   B N   
4044 C CA  A SER   B 7   ? 0.4380 0.3740 0.3332 -0.1173 0.0686  -0.0644 7   SER   B CA  
4045 C CA  B SER   B 7   ? 0.4449 0.3729 0.3252 -0.1248 0.0693  -0.0680 7   SER   B CA  
4046 C C   A SER   B 7   ? 0.4336 0.3522 0.3184 -0.1255 0.0864  -0.0760 7   SER   B C   
4047 C C   B SER   B 7   ? 0.4385 0.3504 0.3074 -0.1355 0.0871  -0.0782 7   SER   B C   
4048 O O   A SER   B 7   ? 0.4359 0.3513 0.3270 -0.1297 0.0960  -0.0734 7   SER   B O   
4049 O O   B SER   B 7   ? 0.4398 0.3497 0.3167 -0.1421 0.1016  -0.0682 7   SER   B O   
4050 C CB  A SER   B 7   ? 0.4574 0.3912 0.3983 -0.1124 0.0795  -0.0632 7   SER   B CB  
4051 C CB  B SER   B 7   ? 0.4679 0.3897 0.3978 -0.1202 0.0818  -0.0698 7   SER   B CB  
4052 O OG  A SER   B 7   ? 0.4693 0.3987 0.4541 -0.1102 0.0805  -0.0526 7   SER   B OG  
4053 O OG  B SER   B 7   ? 0.4828 0.3937 0.4616 -0.1204 0.0830  -0.0617 7   SER   B OG  
4064 N N   A GLY   B 8   ? 0.4323 0.3379 0.3340 -0.1197 0.0915  -0.0728 8   GLY   B N   
4065 N N   B GLY   B 8   ? 0.4371 0.3381 0.3319 -0.1267 0.0885  -0.0751 8   GLY   B N   
4066 C CA  A GLY   B 8   ? 0.4245 0.3260 0.3369 -0.1145 0.0966  -0.0753 8   GLY   B CA  
4067 C CA  B GLY   B 8   ? 0.4277 0.3282 0.3389 -0.1189 0.0922  -0.0782 8   GLY   B CA  
4068 C C   A GLY   B 8   ? 0.4135 0.3050 0.3186 -0.1130 0.1012  -0.0624 8   GLY   B C   
4069 C C   B GLY   B 8   ? 0.4146 0.3076 0.3199 -0.1159 0.0946  -0.0650 8   GLY   B C   
4070 O O   A GLY   B 8   ? 0.4211 0.3072 0.3338 -0.1120 0.1054  -0.0633 8   GLY   B O   
4071 O O   B GLY   B 8   ? 0.4246 0.3154 0.3358 -0.1106 0.0897  -0.0746 8   GLY   B O   
4078 N N   . TYR   B 9   ? 0.4024 0.2894 0.3042 -0.1028 0.0895  -0.0622 9   TYR   B N   
4079 C CA  . TYR   B 9   ? 0.3688 0.2510 0.2579 -0.0776 0.0583  -0.0543 9   TYR   B CA  
4080 C C   . TYR   B 9   ? 0.3574 0.2582 0.2693 -0.0653 0.0199  -0.0540 9   TYR   B C   
4081 O O   . TYR   B 9   ? 0.3858 0.2771 0.3165 -0.0675 0.0250  -0.0228 9   TYR   B O   
4082 C CB  . TYR   B 9   ? 0.3531 0.2163 0.2895 -0.0614 0.0529  -0.0564 9   TYR   B CB  
4083 C CG  . TYR   B 9   ? 0.3384 0.1953 0.3021 -0.0613 0.0354  -0.0581 9   TYR   B CG  
4084 C CD1 . TYR   B 9   ? 0.3359 0.2092 0.3132 -0.0782 0.0352  -0.0491 9   TYR   B CD1 
4085 C CD2 . TYR   B 9   ? 0.3201 0.1933 0.3190 -0.0527 0.0159  -0.0550 9   TYR   B CD2 
4086 C CE1 . TYR   B 9   ? 0.3240 0.2302 0.3209 -0.0881 0.0392  -0.0450 9   TYR   B CE1 
4087 C CE2 . TYR   B 9   ? 0.3098 0.2005 0.3264 -0.0650 0.0179  -0.0276 9   TYR   B CE2 
4088 C CZ  . TYR   B 9   ? 0.3135 0.2262 0.3251 -0.0793 0.0345  -0.0608 9   TYR   B CZ  
4089 O OH  . TYR   B 9   ? 0.2957 0.2397 0.3305 -0.0911 0.0415  -0.0570 9   TYR   B OH  
4100 N N   . LEU   B 10  ? 0.3186 0.2281 0.2518 -0.0749 0.0070  -0.0500 10  LEU   B N   
4101 C CA  . LEU   B 10  ? 0.3151 0.2246 0.2416 -0.0728 -0.0115 -0.0199 10  LEU   B CA  
4102 C C   . LEU   B 10  ? 0.3023 0.2235 0.2336 -0.0777 -0.0462 -0.0259 10  LEU   B C   
4103 O O   . LEU   B 10  ? 0.2878 0.2337 0.2304 -0.0575 -0.0538 -0.0170 10  LEU   B O   
4104 C CB  . LEU   B 10  ? 0.3362 0.2251 0.2638 -0.0618 -0.0315 0.0008  10  LEU   B CB  
4105 C CG  . LEU   B 10  ? 0.3629 0.2335 0.2945 -0.0592 -0.0558 -0.0078 10  LEU   B CG  
4106 C CD1 . LEU   B 10  ? 0.3838 0.2574 0.3190 -0.0497 -0.0549 -0.0191 10  LEU   B CD1 
4107 C CD2 . LEU   B 10  ? 0.3721 0.2468 0.3447 -0.0631 -0.0366 0.0155  10  LEU   B CD2 
4119 N N   . LYS   B 11  ? 0.3254 0.2583 0.2391 -0.0595 -0.0551 -0.0340 11  LYS   B N   
4120 C CA  . LYS   B 11  ? 0.3359 0.2904 0.2780 -0.0497 -0.0694 -0.0495 11  LYS   B CA  
4121 C C   . LYS   B 11  ? 0.3184 0.2599 0.2923 -0.0703 -0.0606 -0.0672 11  LYS   B C   
4122 O O   . LYS   B 11  ? 0.3431 0.2762 0.3485 -0.0856 -0.0560 -0.0831 11  LYS   B O   
4123 C CB  . LYS   B 11  ? 0.3729 0.3528 0.3451 -0.0161 -0.0668 -0.0346 11  LYS   B CB  
4124 C CG  . LYS   B 11  ? 0.4056 0.3886 0.4253 0.0048  -0.0628 -0.0277 11  LYS   B CG  
4125 C CD  . LYS   B 11  ? 0.4331 0.4180 0.5032 0.0117  -0.0576 -0.0349 11  LYS   B CD  
4126 C CE  . LYS   B 11  ? 0.4549 0.4394 0.5650 0.0134  -0.0484 -0.0406 11  LYS   B CE  
4127 N NZ  . LYS   B 11  ? 0.4666 0.4556 0.6024 0.0151  -0.0472 -0.0417 11  LYS   B NZ  
4141 N N   . LEU   B 12  ? 0.2686 0.2346 0.2887 -0.0675 -0.0650 -0.0551 12  LEU   B N   
4142 C CA  . LEU   B 12  ? 0.2614 0.2011 0.2996 -0.0597 -0.0589 -0.0539 12  LEU   B CA  
4143 C C   . LEU   B 12  ? 0.2590 0.2129 0.3008 -0.0631 -0.0609 -0.0635 12  LEU   B C   
4144 O O   . LEU   B 12  ? 0.2673 0.2184 0.3219 -0.0689 -0.0590 -0.0485 12  LEU   B O   
4145 C CB  . LEU   B 12  ? 0.2702 0.1878 0.2887 -0.0405 -0.0457 -0.0375 12  LEU   B CB  
4146 C CG  . LEU   B 12  ? 0.2635 0.1922 0.2982 -0.0409 -0.0300 -0.0298 12  LEU   B CG  
4147 C CD1 . LEU   B 12  ? 0.2702 0.1941 0.2959 -0.0330 -0.0363 0.0006  12  LEU   B CD1 
4148 C CD2 . LEU   B 12  ? 0.2716 0.1986 0.3243 -0.0268 -0.0129 -0.0510 12  LEU   B CD2 
4160 N N   . THR   B 13  ? 0.2531 0.2174 0.3168 -0.0568 -0.0615 -0.0702 13  THR   B N   
4161 C CA  . THR   B 13  ? 0.2582 0.2347 0.2968 -0.0550 -0.0841 -0.0408 13  THR   B CA  
4162 C C   . THR   B 13  ? 0.2996 0.2507 0.3259 -0.0676 -0.0897 -0.0255 13  THR   B C   
4163 O O   . THR   B 13  ? 0.3214 0.2469 0.3318 -0.0678 -0.0578 -0.0091 13  THR   B O   
4164 C CB  . THR   B 13  ? 0.2313 0.2417 0.3114 -0.0403 -0.0803 -0.0125 13  THR   B CB  
4165 O OG1 . THR   B 13  ? 0.2230 0.2292 0.3265 -0.0434 -0.0776 -0.0252 13  THR   B OG1 
4166 C CG2 . THR   B 13  ? 0.2359 0.2368 0.3125 -0.0513 -0.0573 0.0089  13  THR   B CG2 
4174 N N   A ASP   B 14  ? 0.3078 0.2664 0.3321 -0.0794 -0.1124 -0.0101 14  ASP   B N   
4175 N N   B ASP   B 14  ? 0.3093 0.2723 0.3222 -0.0690 -0.1112 0.0033  14  ASP   B N   
4176 C CA  A ASP   B 14  ? 0.3214 0.2806 0.3690 -0.0891 -0.1095 0.0057  14  ASP   B CA  
4177 C CA  B ASP   B 14  ? 0.3251 0.2915 0.3569 -0.0696 -0.1021 0.0268  14  ASP   B CA  
4178 C C   A ASP   B 14  ? 0.3119 0.2575 0.3262 -0.0848 -0.1119 0.0042  14  ASP   B C   
4179 C C   B ASP   B 14  ? 0.3104 0.2698 0.3296 -0.0690 -0.1023 0.0221  14  ASP   B C   
4180 O O   A ASP   B 14  ? 0.3357 0.2672 0.3120 -0.0846 -0.1095 0.0112  14  ASP   B O   
4181 O O   B ASP   B 14  ? 0.3280 0.2891 0.3369 -0.0614 -0.0901 0.0429  14  ASP   B O   
4182 C CB  A ASP   B 14  ? 0.3401 0.3152 0.4469 -0.0940 -0.1213 0.0052  14  ASP   B CB  
4183 C CB  B ASP   B 14  ? 0.3514 0.3288 0.4231 -0.0591 -0.1098 0.0321  14  ASP   B CB  
4184 C CG  A ASP   B 14  ? 0.3622 0.3353 0.5185 -0.0973 -0.1186 -0.0074 14  ASP   B CG  
4185 C CG  B ASP   B 14  ? 0.3800 0.3630 0.4861 -0.0439 -0.1045 0.0254  14  ASP   B CG  
4186 O OD1 A ASP   B 14  ? 0.3756 0.3329 0.5337 -0.1138 -0.1123 -0.0154 14  ASP   B OD1 
4187 O OD1 B ASP   B 14  ? 0.3919 0.3834 0.4952 -0.0440 -0.0973 0.0216  14  ASP   B OD1 
4188 O OD2 A ASP   B 14  ? 0.3661 0.3515 0.5633 -0.0937 -0.1206 -0.0040 14  ASP   B OD2 
4189 O OD2 B ASP   B 14  ? 0.3875 0.3708 0.5251 -0.0377 -0.1027 0.0301  14  ASP   B OD2 
4198 N N   . ASN   B 15  ? 0.2753 0.2318 0.3060 -0.0698 -0.1196 0.0147  15  ASN   B N   
4199 C CA  . ASN   B 15  ? 0.2349 0.2054 0.2832 -0.0453 -0.0967 0.0116  15  ASN   B CA  
4200 C C   . ASN   B 15  ? 0.2295 0.1863 0.2623 -0.0298 -0.0663 0.0177  15  ASN   B C   
4201 O O   . ASN   B 15  ? 0.2146 0.1876 0.2751 -0.0323 -0.0739 -0.0131 15  ASN   B O   
4202 C CB  . ASN   B 15  ? 0.2281 0.1987 0.2957 -0.0276 -0.0765 0.0035  15  ASN   B CB  
4203 C CG  . ASN   B 15  ? 0.2021 0.1958 0.2813 -0.0272 -0.0539 0.0122  15  ASN   B CG  
4204 O OD1 . ASN   B 15  ? 0.2248 0.2200 0.3225 -0.0550 -0.0574 0.0095  15  ASN   B OD1 
4205 N ND2 . ASN   B 15  ? 0.1943 0.1688 0.2963 -0.0125 -0.0175 -0.0158 15  ASN   B ND2 
4213 N N   . VAL   B 16  ? 0.2235 0.1731 0.2649 -0.0394 -0.0648 0.0042  16  VAL   B N   
4214 C CA  . VAL   B 16  ? 0.2246 0.1772 0.2435 -0.0246 -0.0576 -0.0064 16  VAL   B CA  
4215 C C   . VAL   B 16  ? 0.2296 0.1754 0.2555 -0.0374 -0.0580 -0.0020 16  VAL   B C   
4216 O O   . VAL   B 16  ? 0.2319 0.1942 0.2534 -0.0318 -0.0455 -0.0371 16  VAL   B O   
4217 C CB  . VAL   B 16  ? 0.2177 0.1866 0.2562 -0.0060 -0.0487 -0.0175 16  VAL   B CB  
4218 C CG1 . VAL   B 16  ? 0.2112 0.1791 0.2467 0.0015  -0.0321 -0.0199 16  VAL   B CG1 
4219 C CG2 . VAL   B 16  ? 0.2108 0.1868 0.2606 0.0023  -0.0412 -0.0422 16  VAL   B CG2 
4229 N N   . TYR   B 17  ? 0.2333 0.1951 0.2501 -0.0367 -0.0509 -0.0084 17  TYR   B N   
4230 C CA  . TYR   B 17  ? 0.2318 0.2076 0.2159 -0.0434 -0.0303 -0.0055 17  TYR   B CA  
4231 C C   . TYR   B 17  ? 0.2211 0.1781 0.2300 -0.0475 -0.0362 -0.0275 17  TYR   B C   
4232 O O   . TYR   B 17  ? 0.2133 0.1884 0.2555 -0.0362 -0.0504 -0.0327 17  TYR   B O   
4233 C CB  . TYR   B 17  ? 0.2542 0.2564 0.2337 -0.0342 -0.0492 0.0481  17  TYR   B CB  
4234 C CG  . TYR   B 17  ? 0.2912 0.3124 0.2870 -0.0213 -0.0587 0.0633  17  TYR   B CG  
4235 C CD1 . TYR   B 17  ? 0.3066 0.3261 0.3057 -0.0076 -0.0796 0.0837  17  TYR   B CD1 
4236 C CD2 . TYR   B 17  ? 0.3231 0.3456 0.3223 -0.0096 -0.0597 0.0601  17  TYR   B CD2 
4237 C CE1 . TYR   B 17  ? 0.3367 0.3677 0.3245 0.0082  -0.0799 0.0644  17  TYR   B CE1 
4238 C CE2 . TYR   B 17  ? 0.3482 0.3784 0.3452 0.0113  -0.0776 0.0580  17  TYR   B CE2 
4239 C CZ  . TYR   B 17  ? 0.3559 0.3837 0.3486 0.0175  -0.0900 0.0608  17  TYR   B CZ  
4240 O OH  . TYR   B 17  ? 0.3798 0.3901 0.3639 0.0290  -0.0965 0.0685  17  TYR   B OH  
4250 N N   . ILE   B 18  ? 0.2315 0.1898 0.2161 -0.0482 -0.0284 -0.0234 18  ILE   B N   
4251 C CA  . ILE   B 18  ? 0.2388 0.1847 0.2025 -0.0432 -0.0231 -0.0246 18  ILE   B CA  
4252 C C   . ILE   B 18  ? 0.2555 0.1781 0.2142 -0.0578 -0.0167 -0.0428 18  ILE   B C   
4253 O O   . ILE   B 18  ? 0.2695 0.1846 0.2588 -0.0403 -0.0353 -0.0479 18  ILE   B O   
4254 C CB  . ILE   B 18  ? 0.2393 0.1952 0.2150 -0.0494 -0.0375 -0.0142 18  ILE   B CB  
4255 C CG1 . ILE   B 18  ? 0.2346 0.2040 0.2272 -0.0531 -0.0482 -0.0007 18  ILE   B CG1 
4256 C CG2 . ILE   B 18  ? 0.2273 0.1999 0.2268 -0.0467 -0.0429 -0.0020 18  ILE   B CG2 
4257 C CD1 . ILE   B 18  ? 0.2379 0.2308 0.2494 -0.0386 -0.0397 0.0346  18  ILE   B CD1 
4269 N N   . LYS   B 19  ? 0.2505 0.1790 0.2397 -0.0374 0.0148  -0.0382 19  LYS   B N   
4270 C CA  . LYS   B 19  ? 0.2476 0.1930 0.2391 -0.0401 0.0242  -0.0379 19  LYS   B CA  
4271 C C   . LYS   B 19  ? 0.2446 0.1825 0.2754 -0.0338 0.0251  -0.0591 19  LYS   B C   
4272 O O   . LYS   B 19  ? 0.2235 0.1781 0.2629 -0.0129 0.0188  -0.0445 19  LYS   B O   
4273 C CB  . LYS   B 19  ? 0.2521 0.2235 0.2713 -0.0377 0.0318  -0.0316 19  LYS   B CB  
4274 C CG  . LYS   B 19  ? 0.2818 0.2415 0.2948 -0.0388 0.0313  -0.0275 19  LYS   B CG  
4275 C CD  . LYS   B 19  ? 0.3077 0.2699 0.3053 -0.0678 0.0413  -0.0149 19  LYS   B CD  
4276 C CE  . LYS   B 19  ? 0.3365 0.2996 0.3476 -0.0782 0.0434  -0.0243 19  LYS   B CE  
4277 N NZ  . LYS   B 19  ? 0.3594 0.3293 0.3473 -0.0746 0.0685  -0.0158 19  LYS   B NZ  
4291 N N   . ASN   B 20  ? 0.2570 0.1977 0.3076 -0.0291 0.0265  -0.0668 20  ASN   B N   
4292 C CA  . ASN   B 20  ? 0.2417 0.2107 0.3458 -0.0214 0.0313  -0.0863 20  ASN   B CA  
4293 C C   . ASN   B 20  ? 0.2360 0.2464 0.3435 -0.0239 0.0457  -0.0918 20  ASN   B C   
4294 O O   . ASN   B 20  ? 0.2520 0.2858 0.3729 -0.0467 0.0650  -0.0927 20  ASN   B O   
4295 C CB  . ASN   B 20  ? 0.2669 0.2094 0.3854 0.0058  0.0211  -0.0826 20  ASN   B CB  
4296 C CG  . ASN   B 20  ? 0.2927 0.2122 0.4135 0.0369  0.0308  -0.1003 20  ASN   B CG  
4297 O OD1 . ASN   B 20  ? 0.3440 0.2495 0.4641 0.0566  0.0319  -0.1020 20  ASN   B OD1 
4298 N ND2 . ASN   B 20  ? 0.2638 0.2092 0.4063 0.0400  0.0194  -0.0727 20  ASN   B ND2 
4305 N N   . ALA   B 21  ? 0.2293 0.2183 0.3456 -0.0324 0.0444  -0.0677 21  ALA   B N   
4306 C CA  . ALA   B 21  ? 0.2451 0.2154 0.3476 -0.0238 0.0387  -0.0560 21  ALA   B CA  
4307 C C   . ALA   B 21  ? 0.2422 0.1873 0.2930 -0.0175 0.0568  -0.0472 21  ALA   B C   
4308 O O   . ALA   B 21  ? 0.2483 0.1929 0.2813 -0.0284 0.0441  -0.0335 21  ALA   B O   
4309 C CB  . ALA   B 21  ? 0.2698 0.2422 0.3652 -0.0449 0.0293  -0.0374 21  ALA   B CB  
4315 N N   . ASP   B 22  ? 0.2226 0.1815 0.2981 -0.0264 0.0314  -0.0279 22  ASP   B N   
4316 C CA  . ASP   B 22  ? 0.2283 0.1885 0.2903 -0.0061 0.0081  -0.0131 22  ASP   B CA  
4317 C C   . ASP   B 22  ? 0.2281 0.1813 0.2754 -0.0159 -0.0063 -0.0110 22  ASP   B C   
4318 O O   . ASP   B 22  ? 0.2331 0.1776 0.2766 -0.0052 -0.0021 0.0014  22  ASP   B O   
4319 C CB  . ASP   B 22  ? 0.2345 0.2022 0.3145 -0.0086 0.0124  -0.0113 22  ASP   B CB  
4320 C CG  . ASP   B 22  ? 0.2368 0.2180 0.3621 0.0071  -0.0133 -0.0069 22  ASP   B CG  
4321 O OD1 . ASP   B 22  ? 0.2464 0.1955 0.3651 0.0080  -0.0257 -0.0023 22  ASP   B OD1 
4322 O OD2 . ASP   B 22  ? 0.2517 0.2527 0.4249 0.0197  -0.0398 -0.0093 22  ASP   B OD2 
4327 N N   . ILE   B 23  ? 0.2287 0.1821 0.2489 -0.0068 -0.0275 0.0224  23  ILE   B N   
4328 C CA  . ILE   B 23  ? 0.2086 0.1843 0.2316 -0.0127 -0.0216 0.0077  23  ILE   B CA  
4329 C C   . ILE   B 23  ? 0.1990 0.1847 0.2016 -0.0088 -0.0360 0.0211  23  ILE   B C   
4330 O O   . ILE   B 23  ? 0.1941 0.1764 0.2176 -0.0096 -0.0239 0.0082  23  ILE   B O   
4331 C CB  . ILE   B 23  ? 0.2129 0.1880 0.2473 -0.0138 -0.0131 0.0163  23  ILE   B CB  
4332 C CG1 . ILE   B 23  ? 0.2145 0.1992 0.2521 -0.0219 0.0041  0.0247  23  ILE   B CG1 
4333 C CG2 . ILE   B 23  ? 0.2180 0.2076 0.2567 -0.0264 -0.0028 0.0108  23  ILE   B CG2 
4334 C CD1 . ILE   B 23  ? 0.2181 0.1960 0.2646 -0.0101 -0.0082 0.0383  23  ILE   B CD1 
4346 N N   . VAL   B 24  ? 0.2069 0.1833 0.2189 -0.0198 -0.0294 0.0048  24  VAL   B N   
4347 C CA  . VAL   B 24  ? 0.1884 0.1766 0.2369 -0.0157 -0.0231 -0.0005 24  VAL   B CA  
4348 C C   . VAL   B 24  ? 0.1992 0.1879 0.2709 -0.0140 -0.0292 0.0091  24  VAL   B C   
4349 O O   . VAL   B 24  ? 0.2064 0.1977 0.2678 -0.0253 -0.0223 0.0130  24  VAL   B O   
4350 C CB  . VAL   B 24  ? 0.1918 0.1953 0.2364 -0.0084 -0.0123 0.0074  24  VAL   B CB  
4351 C CG1 . VAL   B 24  ? 0.1987 0.1974 0.2801 -0.0058 -0.0290 0.0145  24  VAL   B CG1 
4352 C CG2 . VAL   B 24  ? 0.1788 0.2248 0.2503 -0.0069 0.0039  0.0153  24  VAL   B CG2 
4362 N N   . GLU   B 25  ? 0.2124 0.2044 0.2825 -0.0171 -0.0117 0.0058  25  GLU   B N   
4363 C CA  . GLU   B 25  ? 0.2445 0.2294 0.2913 -0.0122 -0.0032 -0.0048 25  GLU   B CA  
4364 C C   . GLU   B 25  ? 0.2380 0.2043 0.2283 -0.0242 -0.0064 -0.0016 25  GLU   B C   
4365 O O   . GLU   B 25  ? 0.2322 0.2079 0.2708 -0.0209 -0.0026 0.0035  25  GLU   B O   
4366 C CB  . GLU   B 25  ? 0.2931 0.2993 0.3813 0.0039  -0.0124 0.0134  25  GLU   B CB  
4367 C CG  . GLU   B 25  ? 0.3489 0.3661 0.5119 0.0206  -0.0006 0.0055  25  GLU   B CG  
4368 C CD  . GLU   B 25  ? 0.4167 0.4376 0.6163 0.0209  0.0049  0.0017  25  GLU   B CD  
4369 O OE1 . GLU   B 25  ? 0.4433 0.4700 0.6498 0.0272  0.0152  0.0029  25  GLU   B OE1 
4370 O OE2 . GLU   B 25  ? 0.4320 0.4484 0.6425 0.0237  0.0079  -0.0109 25  GLU   B OE2 
4377 N N   A GLU   B 26  ? 0.2277 0.1948 0.2003 -0.0311 -0.0031 -0.0058 26  GLU   B N   
4378 N N   B GLU   B 26  ? 0.2217 0.2022 0.2181 -0.0359 0.0079  0.0103  26  GLU   B N   
4379 C CA  A GLU   B 26  ? 0.2341 0.2002 0.1998 -0.0262 -0.0100 -0.0088 26  GLU   B CA  
4380 C CA  B GLU   B 26  ? 0.2253 0.2180 0.2388 -0.0318 0.0087  0.0200  26  GLU   B CA  
4381 C C   A GLU   B 26  ? 0.2179 0.2078 0.2086 -0.0207 -0.0115 0.0154  26  GLU   B C   
4382 C C   B GLU   B 26  ? 0.2119 0.2180 0.2217 -0.0260 -0.0033 0.0328  26  GLU   B C   
4383 O O   A GLU   B 26  ? 0.2338 0.2230 0.2114 -0.0182 -0.0163 0.0155  26  GLU   B O   
4384 O O   B GLU   B 26  ? 0.2260 0.2352 0.2185 -0.0288 -0.0124 0.0372  26  GLU   B O   
4385 C CB  A GLU   B 26  ? 0.2596 0.2034 0.2030 -0.0326 -0.0076 -0.0136 26  GLU   B CB  
4386 C CB  B GLU   B 26  ? 0.2457 0.2389 0.2818 -0.0396 0.0264  0.0296  26  GLU   B CB  
4387 C CG  A GLU   B 26  ? 0.2882 0.2133 0.2137 -0.0223 -0.0123 -0.0195 26  GLU   B CG  
4388 C CG  B GLU   B 26  ? 0.2707 0.2685 0.3434 -0.0278 0.0345  0.0307  26  GLU   B CG  
4389 C CD  A GLU   B 26  ? 0.3087 0.2046 0.2021 -0.0378 -0.0060 -0.0517 26  GLU   B CD  
4390 C CD  B GLU   B 26  ? 0.2735 0.2681 0.3835 -0.0265 0.0521  0.0477  26  GLU   B CD  
4391 O OE1 A GLU   B 26  ? 0.3248 0.1953 0.2087 -0.0325 0.0312  -0.0627 26  GLU   B OE1 
4392 O OE1 B GLU   B 26  ? 0.2802 0.2627 0.4398 -0.0228 0.1080  0.0404  26  GLU   B OE1 
4393 O OE2 A GLU   B 26  ? 0.3101 0.2142 0.2111 -0.0548 -0.0136 -0.0147 26  GLU   B OE2 
4394 O OE2 B GLU   B 26  ? 0.2589 0.2675 0.3745 -0.0175 0.0529  0.0315  26  GLU   B OE2 
4407 N N   . ALA   B 27  ? 0.1951 0.2057 0.2358 -0.0284 -0.0067 0.0227  27  ALA   B N   
4408 C CA  . ALA   B 27  ? 0.2020 0.1973 0.2097 -0.0278 -0.0184 0.0252  27  ALA   B CA  
4409 C C   . ALA   B 27  ? 0.2056 0.2023 0.2393 -0.0163 -0.0028 0.0393  27  ALA   B C   
4410 O O   . ALA   B 27  ? 0.2072 0.2042 0.2836 -0.0040 -0.0074 0.0544  27  ALA   B O   
4411 C CB  . ALA   B 27  ? 0.2247 0.1632 0.2345 -0.0353 0.0000  0.0212  27  ALA   B CB  
4418 N N   . LYS   B 28  ? 0.2011 0.2115 0.3034 -0.0170 0.0011  0.0645  28  LYS   B N   
4419 C CA  . LYS   B 28  ? 0.2069 0.2491 0.3437 -0.0044 0.0553  0.0938  28  LYS   B CA  
4420 C C   . LYS   B 28  ? 0.2313 0.2707 0.3308 -0.0047 0.0735  0.0919  28  LYS   B C   
4421 O O   . LYS   B 28  ? 0.2689 0.2928 0.3674 -0.0024 0.0623  0.1043  28  LYS   B O   
4422 C CB  . LYS   B 28  ? 0.2417 0.2876 0.4192 0.0047  0.0806  0.1141  28  LYS   B CB  
4423 C CG  . LYS   B 28  ? 0.2697 0.3507 0.4605 0.0146  0.0800  0.1299  28  LYS   B CG  
4424 C CD  . LYS   B 28  ? 0.3189 0.4284 0.5279 0.0252  0.0928  0.1359  28  LYS   B CD  
4425 C CE  . LYS   B 28  ? 0.3547 0.4835 0.5833 0.0398  0.0910  0.1492  28  LYS   B CE  
4426 N NZ  . LYS   B 28  ? 0.3920 0.5283 0.6082 0.0532  0.0916  0.1637  28  LYS   B NZ  
4440 N N   . LYS   B 29  ? 0.2537 0.2954 0.3382 0.0101  0.0674  0.0786  29  LYS   B N   
4441 C CA  . LYS   B 29  ? 0.3091 0.3478 0.3525 0.0227  0.0610  0.0815  29  LYS   B CA  
4442 C C   . LYS   B 29  ? 0.2974 0.3437 0.3086 0.0168  0.0220  0.0927  29  LYS   B C   
4443 O O   . LYS   B 29  ? 0.3122 0.3831 0.3183 0.0216  0.0288  0.0957  29  LYS   B O   
4444 C CB  . LYS   B 29  ? 0.3976 0.4184 0.4522 0.0279  0.0596  0.0632  29  LYS   B CB  
4445 C CG  . LYS   B 29  ? 0.4691 0.4699 0.5655 0.0254  0.0606  0.0530  29  LYS   B CG  
4446 C CD  . LYS   B 29  ? 0.5258 0.5119 0.6543 0.0184  0.0723  0.0457  29  LYS   B CD  
4447 C CE  . LYS   B 29  ? 0.5711 0.5477 0.7106 0.0113  0.0884  0.0431  29  LYS   B CE  
4448 N NZ  . LYS   B 29  ? 0.5963 0.5700 0.7396 0.0083  0.0964  0.0416  29  LYS   B NZ  
4462 N N   . VAL   B 30  ? 0.2701 0.3183 0.2921 0.0019  0.0105  0.0853  30  VAL   B N   
4463 C CA  . VAL   B 30  ? 0.2468 0.3025 0.3178 -0.0119 -0.0046 0.0913  30  VAL   B CA  
4464 C C   . VAL   B 30  ? 0.2251 0.3044 0.3238 -0.0145 -0.0023 0.1222  30  VAL   B C   
4465 O O   . VAL   B 30  ? 0.2358 0.3292 0.3184 -0.0078 0.0059  0.1285  30  VAL   B O   
4466 C CB  . VAL   B 30  ? 0.2429 0.2874 0.3521 -0.0356 -0.0291 0.0807  30  VAL   B CB  
4467 C CG1 . VAL   B 30  ? 0.2596 0.3032 0.3564 -0.0291 -0.0406 0.0577  30  VAL   B CG1 
4468 C CG2 . VAL   B 30  ? 0.2615 0.2947 0.3866 -0.0464 -0.0414 0.0467  30  VAL   B CG2 
4478 N N   A LYS   B 31  ? 0.2088 0.2786 0.3462 -0.0311 0.0060  0.1290  31  LYS   B N   
4479 N N   B LYS   B 31  ? 0.2035 0.2796 0.3480 -0.0327 0.0104  0.1261  31  LYS   B N   
4480 C CA  A LYS   B 31  ? 0.2068 0.2759 0.3812 -0.0335 0.0013  0.1213  31  LYS   B CA  
4481 C CA  B LYS   B 31  ? 0.2009 0.2797 0.3834 -0.0371 0.0067  0.1180  31  LYS   B CA  
4482 C C   A LYS   B 31  ? 0.2009 0.2405 0.3388 -0.0326 -0.0370 0.1001  31  LYS   B C   
4483 C C   B LYS   B 31  ? 0.1980 0.2426 0.3437 -0.0352 -0.0355 0.0980  31  LYS   B C   
4484 O O   A LYS   B 31  ? 0.2028 0.2514 0.3426 -0.0402 -0.0451 0.1187  31  LYS   B O   
4485 O O   B LYS   B 31  ? 0.2000 0.2545 0.3500 -0.0469 -0.0438 0.1176  31  LYS   B O   
4486 C CB  A LYS   B 31  ? 0.2186 0.3159 0.4399 -0.0236 0.0171  0.1379  31  LYS   B CB  
4487 C CB  B LYS   B 31  ? 0.2119 0.3266 0.4383 -0.0269 0.0219  0.1305  31  LYS   B CB  
4488 C CG  A LYS   B 31  ? 0.2476 0.3539 0.4856 -0.0174 0.0260  0.1290  31  LYS   B CG  
4489 C CG  B LYS   B 31  ? 0.2450 0.3713 0.4777 -0.0187 0.0276  0.1149  31  LYS   B CG  
4490 C CD  A LYS   B 31  ? 0.2722 0.3884 0.5146 -0.0063 0.0192  0.1071  31  LYS   B CD  
4491 C CD  B LYS   B 31  ? 0.2655 0.4135 0.5017 -0.0129 0.0182  0.0914  31  LYS   B CD  
4492 C CE  A LYS   B 31  ? 0.2922 0.4100 0.5374 0.0053  0.0122  0.0902  31  LYS   B CE  
4493 C CE  B LYS   B 31  ? 0.2838 0.4379 0.5239 -0.0089 0.0131  0.0761  31  LYS   B CE  
4494 N NZ  A LYS   B 31  ? 0.3081 0.4195 0.5430 0.0199  -0.0012 0.0737  31  LYS   B NZ  
4495 N NZ  B LYS   B 31  ? 0.3001 0.4475 0.5247 0.0050  -0.0050 0.0597  31  LYS   B NZ  
4522 N N   . PRO   B 32  ? 0.1911 0.1995 0.2786 -0.0405 -0.0508 0.0706  32  PRO   B N   
4523 C CA  . PRO   B 32  ? 0.2031 0.1950 0.2169 -0.0364 -0.0515 0.0362  32  PRO   B CA  
4524 C C   . PRO   B 32  ? 0.2174 0.1828 0.2179 -0.0410 -0.0701 0.0285  32  PRO   B C   
4525 O O   . PRO   B 32  ? 0.2386 0.1738 0.2611 -0.0530 -0.0919 0.0324  32  PRO   B O   
4526 C CB  . PRO   B 32  ? 0.2130 0.1999 0.2031 -0.0460 -0.0413 0.0264  32  PRO   B CB  
4527 C CG  . PRO   B 32  ? 0.2405 0.1796 0.2527 -0.0378 -0.0623 0.0343  32  PRO   B CG  
4528 C CD  . PRO   B 32  ? 0.2207 0.1850 0.2612 -0.0338 -0.0811 0.0406  32  PRO   B CD  
4536 N N   . THR   B 33  ? 0.2259 0.1731 0.2301 -0.0361 -0.0773 0.0254  33  THR   B N   
4537 C CA  . THR   B 33  ? 0.2320 0.1721 0.2023 -0.0317 -0.0650 0.0188  33  THR   B CA  
4538 C C   . THR   B 33  ? 0.2366 0.1725 0.2047 -0.0318 -0.0663 0.0270  33  THR   B C   
4539 O O   . THR   B 33  ? 0.2622 0.1870 0.1946 -0.0295 -0.0616 0.0197  33  THR   B O   
4540 C CB  . THR   B 33  ? 0.2503 0.1811 0.2123 -0.0138 -0.0697 0.0340  33  THR   B CB  
4541 O OG1 . THR   B 33  ? 0.2406 0.1886 0.2093 -0.0236 -0.0585 0.0381  33  THR   B OG1 
4542 C CG2 . THR   B 33  ? 0.2692 0.1805 0.2434 -0.0109 -0.0648 0.0475  33  THR   B CG2 
4550 N N   . VAL   B 34  ? 0.2304 0.1520 0.2019 -0.0302 -0.0615 0.0160  34  VAL   B N   
4551 C CA  . VAL   B 34  ? 0.2126 0.1638 0.1861 -0.0240 -0.0494 0.0126  34  VAL   B CA  
4552 C C   . VAL   B 34  ? 0.1950 0.1731 0.1668 -0.0358 -0.0425 0.0069  34  VAL   B C   
4553 O O   . VAL   B 34  ? 0.2074 0.1656 0.1696 -0.0359 -0.0427 0.0124  34  VAL   B O   
4554 C CB  . VAL   B 34  ? 0.2186 0.1766 0.2085 -0.0019 -0.0428 0.0013  34  VAL   B CB  
4555 C CG1 . VAL   B 34  ? 0.2041 0.1874 0.2146 -0.0061 -0.0282 -0.0087 34  VAL   B CG1 
4556 C CG2 . VAL   B 34  ? 0.2335 0.1809 0.2525 -0.0029 -0.0185 0.0091  34  VAL   B CG2 
4566 N N   . VAL   B 35  ? 0.1872 0.1620 0.1666 -0.0311 -0.0379 0.0067  35  VAL   B N   
4567 C CA  . VAL   B 35  ? 0.1831 0.1582 0.1683 -0.0250 -0.0196 0.0062  35  VAL   B CA  
4568 C C   . VAL   B 35  ? 0.1777 0.1412 0.1649 -0.0252 -0.0253 0.0053  35  VAL   B C   
4569 O O   . VAL   B 35  ? 0.1810 0.1443 0.1668 -0.0294 -0.0092 -0.0046 35  VAL   B O   
4570 C CB  . VAL   B 35  ? 0.1710 0.1787 0.1643 -0.0210 -0.0187 -0.0010 35  VAL   B CB  
4571 C CG1 . VAL   B 35  ? 0.1789 0.2017 0.1949 -0.0236 -0.0112 0.0040  35  VAL   B CG1 
4572 C CG2 . VAL   B 35  ? 0.1736 0.1742 0.1835 -0.0084 -0.0161 -0.0003 35  VAL   B CG2 
4582 N N   . VAL   B 36  ? 0.1718 0.1522 0.1712 -0.0236 -0.0288 0.0119  36  VAL   B N   
4583 C CA  . VAL   B 36  ? 0.1720 0.1403 0.1559 -0.0195 -0.0275 0.0065  36  VAL   B CA  
4584 C C   . VAL   B 36  ? 0.1717 0.1482 0.1626 -0.0196 -0.0233 0.0092  36  VAL   B C   
4585 O O   . VAL   B 36  ? 0.1704 0.1661 0.1659 -0.0235 -0.0110 0.0014  36  VAL   B O   
4586 C CB  . VAL   B 36  ? 0.1564 0.1514 0.1825 -0.0176 -0.0094 0.0015  36  VAL   B CB  
4587 C CG1 . VAL   B 36  ? 0.1707 0.1726 0.2026 -0.0399 -0.0276 -0.0043 36  VAL   B CG1 
4588 C CG2 . VAL   B 36  ? 0.1807 0.1580 0.1777 -0.0157 -0.0276 0.0179  36  VAL   B CG2 
4598 N N   . ASN   B 37  ? 0.1655 0.1545 0.1623 -0.0132 -0.0179 0.0197  37  ASN   B N   
4599 C CA  . ASN   B 37  ? 0.1638 0.1532 0.1586 -0.0200 -0.0356 0.0131  37  ASN   B CA  
4600 C C   . ASN   B 37  ? 0.1747 0.1496 0.1852 -0.0106 -0.0316 0.0065  37  ASN   B C   
4601 O O   . ASN   B 37  ? 0.1769 0.1588 0.1623 -0.0057 -0.0157 0.0039  37  ASN   B O   
4602 C CB  . ASN   B 37  ? 0.1697 0.1622 0.1723 -0.0189 -0.0247 0.0061  37  ASN   B CB  
4603 C CG  . ASN   B 37  ? 0.1678 0.1624 0.1723 -0.0194 -0.0335 -0.0037 37  ASN   B CG  
4604 O OD1 . ASN   B 37  ? 0.1820 0.1670 0.2035 -0.0087 -0.0231 -0.0015 37  ASN   B OD1 
4605 N ND2 . ASN   B 37  ? 0.1784 0.1540 0.1564 -0.0165 -0.0399 0.0104  37  ASN   B ND2 
4612 N N   . ALA   B 38  ? 0.1905 0.1411 0.1796 -0.0048 -0.0221 0.0115  38  ALA   B N   
4613 C CA  . ALA   B 38  ? 0.1748 0.1535 0.1775 -0.0035 -0.0193 0.0069  38  ALA   B CA  
4614 C C   . ALA   B 38  ? 0.1845 0.1438 0.1790 -0.0071 -0.0220 0.0192  38  ALA   B C   
4615 O O   . ALA   B 38  ? 0.2054 0.1623 0.1784 -0.0090 -0.0145 0.0196  38  ALA   B O   
4616 C CB  . ALA   B 38  ? 0.2041 0.1690 0.1880 -0.0017 0.0021  0.0075  38  ALA   B CB  
4622 N N   . ALA   B 39  ? 0.1949 0.1546 0.1655 0.0079  -0.0179 0.0201  39  ALA   B N   
4623 C CA  . ALA   B 39  ? 0.1997 0.1580 0.1623 0.0079  -0.0188 0.0074  39  ALA   B CA  
4624 C C   . ALA   B 39  ? 0.2001 0.1624 0.1445 0.0102  -0.0143 -0.0131 39  ALA   B C   
4625 O O   . ALA   B 39  ? 0.2035 0.1749 0.1879 -0.0062 -0.0306 0.0094  39  ALA   B O   
4626 C CB  . ALA   B 39  ? 0.2110 0.1748 0.1375 -0.0026 -0.0192 0.0016  39  ALA   B CB  
4632 N N   . ASN   B 40  ? 0.2024 0.1950 0.1233 -0.0080 -0.0243 0.0001  40  ASN   B N   
4633 C CA  . ASN   B 40  ? 0.2041 0.1913 0.1386 -0.0052 -0.0160 0.0029  40  ASN   B CA  
4634 C C   . ASN   B 40  ? 0.2100 0.1924 0.1534 -0.0008 -0.0281 0.0088  40  ASN   B C   
4635 O O   . ASN   B 40  ? 0.2254 0.1922 0.1546 -0.0047 -0.0254 0.0086  40  ASN   B O   
4636 C CB  . ASN   B 40  ? 0.2274 0.1874 0.1898 0.0108  -0.0232 0.0130  40  ASN   B CB  
4637 C CG  . ASN   B 40  ? 0.2316 0.1912 0.2138 -0.0048 -0.0421 0.0232  40  ASN   B CG  
4638 O OD1 . ASN   B 40  ? 0.2303 0.1853 0.3105 -0.0068 -0.0491 0.0179  40  ASN   B OD1 
4639 N ND2 . ASN   B 40  ? 0.2285 0.1958 0.2381 0.0012  -0.0203 0.0386  40  ASN   B ND2 
4646 N N   . VAL   B 41  ? 0.2220 0.1979 0.1636 0.0223  -0.0074 0.0004  41  VAL   B N   
4647 C CA  . VAL   B 41  ? 0.2269 0.2205 0.1549 0.0045  -0.0230 -0.0095 41  VAL   B CA  
4648 C C   . VAL   B 41  ? 0.2142 0.2274 0.1681 0.0052  -0.0218 -0.0114 41  VAL   B C   
4649 O O   . VAL   B 41  ? 0.2274 0.2271 0.2000 -0.0036 -0.0194 -0.0090 41  VAL   B O   
4650 C CB  . VAL   B 41  ? 0.2329 0.2384 0.1843 -0.0038 -0.0093 -0.0139 41  VAL   B CB  
4651 C CG1 . VAL   B 41  ? 0.2263 0.2370 0.2171 -0.0165 0.0152  -0.0058 41  VAL   B CG1 
4652 C CG2 . VAL   B 41  ? 0.2525 0.2555 0.2025 -0.0192 -0.0125 -0.0048 41  VAL   B CG2 
4662 N N   . TYR   B 42  ? 0.2196 0.2237 0.1917 0.0095  -0.0282 0.0047  42  TYR   B N   
4663 C CA  . TYR   B 42  ? 0.2313 0.2260 0.1673 0.0118  -0.0395 -0.0056 42  TYR   B CA  
4664 C C   . TYR   B 42  ? 0.2221 0.1983 0.1825 0.0078  -0.0266 -0.0138 42  TYR   B C   
4665 O O   . TYR   B 42  ? 0.2154 0.2185 0.2273 0.0129  -0.0269 -0.0191 42  TYR   B O   
4666 C CB  . TYR   B 42  ? 0.2588 0.2621 0.2072 0.0177  -0.0436 -0.0033 42  TYR   B CB  
4667 C CG  . TYR   B 42  ? 0.2585 0.2810 0.2048 0.0025  -0.0326 0.0127  42  TYR   B CG  
4668 C CD1 . TYR   B 42  ? 0.2507 0.2680 0.1907 0.0047  -0.0398 0.0090  42  TYR   B CD1 
4669 C CD2 . TYR   B 42  ? 0.2860 0.3036 0.2327 -0.0041 -0.0266 0.0149  42  TYR   B CD2 
4670 C CE1 . TYR   B 42  ? 0.2744 0.2921 0.1694 -0.0013 -0.0308 0.0139  42  TYR   B CE1 
4671 C CE2 . TYR   B 42  ? 0.2959 0.3111 0.2147 0.0026  -0.0090 0.0487  42  TYR   B CE2 
4672 C CZ  . TYR   B 42  ? 0.3084 0.3202 0.1702 0.0235  0.0022  0.0259  42  TYR   B CZ  
4673 O OH  . TYR   B 42  ? 0.3470 0.3543 0.2376 0.0540  0.0214  0.0489  42  TYR   B OH  
4683 N N   . LEU   B 43  ? 0.2106 0.1857 0.1767 -0.0070 -0.0230 -0.0197 43  LEU   B N   
4684 C CA  . LEU   B 43  ? 0.2136 0.1862 0.1639 -0.0092 -0.0306 0.0033  43  LEU   B CA  
4685 C C   . LEU   B 43  ? 0.2170 0.1860 0.1721 -0.0084 -0.0287 0.0002  43  LEU   B C   
4686 O O   . LEU   B 43  ? 0.2068 0.1903 0.2007 -0.0057 -0.0402 0.0018  43  LEU   B O   
4687 C CB  . LEU   B 43  ? 0.2180 0.1848 0.1922 -0.0007 -0.0387 -0.0010 43  LEU   B CB  
4688 C CG  . LEU   B 43  ? 0.2099 0.1791 0.1840 0.0008  -0.0453 -0.0109 43  LEU   B CG  
4689 C CD1 . LEU   B 43  ? 0.2162 0.1743 0.2189 0.0002  -0.0462 -0.0165 43  LEU   B CD1 
4690 C CD2 . LEU   B 43  ? 0.2118 0.1862 0.2062 -0.0058 -0.0364 -0.0110 43  LEU   B CD2 
4702 N N   . LYS   B 44  ? 0.2164 0.1856 0.1815 0.0013  -0.0345 -0.0073 44  LYS   B N   
4703 C CA  . LYS   B 44  ? 0.2327 0.1925 0.1661 -0.0057 -0.0530 0.0105  44  LYS   B CA  
4704 C C   . LYS   B 44  ? 0.2256 0.1812 0.1661 -0.0024 -0.0390 -0.0005 44  LYS   B C   
4705 O O   . LYS   B 44  ? 0.2276 0.1886 0.2063 -0.0059 -0.0190 0.0025  44  LYS   B O   
4706 C CB  . LYS   B 44  ? 0.2561 0.2213 0.1906 0.0014  -0.0597 0.0137  44  LYS   B CB  
4707 C CG  . LYS   B 44  ? 0.2934 0.2608 0.2418 -0.0052 -0.0826 0.0197  44  LYS   B CG  
4708 C CD  . LYS   B 44  ? 0.3346 0.2905 0.3086 -0.0242 -0.0818 0.0027  44  LYS   B CD  
4709 C CE  . LYS   B 44  ? 0.3752 0.3236 0.3640 -0.0352 -0.0806 0.0097  44  LYS   B CE  
4710 N NZ  . LYS   B 44  ? 0.3891 0.3332 0.3900 -0.0302 -0.0960 0.0176  44  LYS   B NZ  
4724 N N   . HIS   B 45  ? 0.2158 0.1873 0.1624 -0.0062 -0.0314 0.0164  45  HIS   B N   
4725 C CA  . HIS   B 45  ? 0.2070 0.1684 0.1759 0.0033  -0.0175 0.0082  45  HIS   B CA  
4726 C C   . HIS   B 45  ? 0.2350 0.1990 0.2122 0.0028  -0.0468 -0.0104 45  HIS   B C   
4727 O O   . HIS   B 45  ? 0.2609 0.2191 0.2626 0.0273  -0.0047 -0.0105 45  HIS   B O   
4728 C CB  . HIS   B 45  ? 0.1914 0.1758 0.2041 0.0042  -0.0140 -0.0110 45  HIS   B CB  
4729 C CG  . HIS   B 45  ? 0.1916 0.1800 0.1935 -0.0113 -0.0089 0.0002  45  HIS   B CG  
4730 N ND1 . HIS   B 45  ? 0.2007 0.1746 0.1922 -0.0095 -0.0235 -0.0116 45  HIS   B ND1 
4731 C CD2 . HIS   B 45  ? 0.1903 0.2017 0.1888 -0.0282 -0.0271 0.0087  45  HIS   B CD2 
4732 C CE1 . HIS   B 45  ? 0.1819 0.1616 0.1977 -0.0003 -0.0430 -0.0085 45  HIS   B CE1 
4733 N NE2 . HIS   B 45  ? 0.1939 0.1861 0.1728 -0.0049 -0.0235 -0.0014 45  HIS   B NE2 
4741 N N   . GLY   B 46  ? 0.2630 0.2059 0.2183 0.0183  -0.0756 0.0129  46  GLY   B N   
4742 C CA  . GLY   B 46  ? 0.2782 0.2230 0.2901 0.0173  -0.0830 0.0015  46  GLY   B CA  
4743 C C   . GLY   B 46  ? 0.2752 0.2315 0.3397 0.0202  -0.0626 0.0075  46  GLY   B C   
4744 O O   . GLY   B 46  ? 0.2830 0.2480 0.4474 0.0351  -0.0141 -0.0200 46  GLY   B O   
4748 N N   . GLY   B 47  ? 0.2623 0.2405 0.2887 -0.0103 -0.0562 0.0102  47  GLY   B N   
4749 C CA  . GLY   B 47  ? 0.2515 0.2225 0.2593 0.0059  -0.0335 0.0063  47  GLY   B CA  
4750 C C   . GLY   B 47  ? 0.2201 0.1981 0.2228 0.0017  -0.0047 0.0055  47  GLY   B C   
4751 O O   . GLY   B 47  ? 0.2215 0.1588 0.2231 0.0037  -0.0168 0.0140  47  GLY   B O   
4755 N N   . GLY   B 48  ? 0.2002 0.1903 0.2134 -0.0030 -0.0301 0.0202  48  GLY   B N   
4756 C CA  . GLY   B 48  ? 0.2003 0.1817 0.2247 -0.0117 -0.0079 0.0058  48  GLY   B CA  
4757 C C   . GLY   B 48  ? 0.1944 0.1665 0.1995 0.0012  -0.0045 0.0022  48  GLY   B C   
4758 O O   . GLY   B 48  ? 0.1782 0.1646 0.2197 0.0033  -0.0181 -0.0006 48  GLY   B O   
4762 N N   . VAL   B 49  ? 0.1896 0.1729 0.2040 0.0115  -0.0213 0.0039  49  VAL   B N   
4763 C CA  . VAL   B 49  ? 0.1925 0.1913 0.1687 0.0035  -0.0282 -0.0031 49  VAL   B CA  
4764 C C   . VAL   B 49  ? 0.1775 0.1723 0.1623 0.0079  -0.0179 -0.0014 49  VAL   B C   
4765 O O   . VAL   B 49  ? 0.1872 0.1834 0.1714 0.0073  -0.0086 0.0163  49  VAL   B O   
4766 C CB  . VAL   B 49  ? 0.2004 0.2103 0.1987 -0.0112 -0.0497 0.0014  49  VAL   B CB  
4767 C CG1 . VAL   B 49  ? 0.2066 0.2197 0.1954 -0.0032 -0.0454 0.0086  49  VAL   B CG1 
4768 C CG2 . VAL   B 49  ? 0.2166 0.2330 0.2420 -0.0307 -0.0578 -0.0128 49  VAL   B CG2 
4778 N N   . ALA   B 50  ? 0.1776 0.1609 0.1850 -0.0015 -0.0159 0.0069  50  ALA   B N   
4779 C CA  . ALA   B 50  ? 0.1785 0.1605 0.1798 0.0045  -0.0107 0.0140  50  ALA   B CA  
4780 C C   . ALA   B 50  ? 0.1760 0.1656 0.1919 -0.0042 -0.0232 0.0124  50  ALA   B C   
4781 O O   . ALA   B 50  ? 0.1827 0.1677 0.1745 -0.0016 -0.0168 0.0004  50  ALA   B O   
4782 C CB  . ALA   B 50  ? 0.1896 0.1667 0.1742 0.0055  -0.0246 0.0144  50  ALA   B CB  
4788 N N   . GLY   B 51  ? 0.1748 0.1751 0.2026 -0.0074 -0.0287 0.0192  51  GLY   B N   
4789 C CA  . GLY   B 51  ? 0.1821 0.1716 0.2098 0.0142  -0.0342 0.0198  51  GLY   B CA  
4790 C C   . GLY   B 51  ? 0.1844 0.1660 0.2053 0.0192  -0.0179 0.0164  51  GLY   B C   
4791 O O   . GLY   B 51  ? 0.1845 0.1933 0.2345 0.0027  -0.0127 0.0068  51  GLY   B O   
4795 N N   . ALA   B 52  ? 0.1763 0.1673 0.1992 0.0066  -0.0090 0.0111  52  ALA   B N   
4796 C CA  . ALA   B 52  ? 0.1738 0.1799 0.1965 0.0160  -0.0083 -0.0034 52  ALA   B CA  
4797 C C   . ALA   B 52  ? 0.1771 0.1777 0.1741 0.0135  -0.0182 0.0030  52  ALA   B C   
4798 O O   . ALA   B 52  ? 0.1876 0.1760 0.2109 0.0062  -0.0099 -0.0001 52  ALA   B O   
4799 C CB  . ALA   B 52  ? 0.2005 0.1816 0.2062 0.0082  -0.0023 -0.0133 52  ALA   B CB  
4805 N N   . LEU   B 53  ? 0.1691 0.1645 0.1985 0.0093  -0.0165 0.0138  53  LEU   B N   
4806 C CA  . LEU   B 53  ? 0.1780 0.1846 0.1858 0.0099  -0.0190 0.0143  53  LEU   B CA  
4807 C C   . LEU   B 53  ? 0.1701 0.1859 0.1715 0.0083  -0.0197 0.0086  53  LEU   B C   
4808 O O   . LEU   B 53  ? 0.1812 0.1865 0.1951 -0.0157 -0.0136 0.0070  53  LEU   B O   
4809 C CB  . LEU   B 53  ? 0.1863 0.1769 0.1966 -0.0004 -0.0260 0.0193  53  LEU   B CB  
4810 C CG  . LEU   B 53  ? 0.1897 0.1993 0.1861 0.0015  -0.0242 0.0195  53  LEU   B CG  
4811 C CD1 . LEU   B 53  ? 0.1951 0.2325 0.1900 0.0218  -0.0219 0.0059  53  LEU   B CD1 
4812 C CD2 . LEU   B 53  ? 0.2021 0.2188 0.2203 -0.0106 -0.0294 -0.0192 53  LEU   B CD2 
4824 N N   . ASN   B 54  ? 0.1840 0.1696 0.1834 -0.0035 -0.0191 0.0103  54  ASN   B N   
4825 C CA  . ASN   B 54  ? 0.1812 0.1868 0.1766 0.0055  -0.0170 -0.0008 54  ASN   B CA  
4826 C C   . ASN   B 54  ? 0.1686 0.1822 0.1983 0.0031  -0.0203 0.0073  54  ASN   B C   
4827 O O   . ASN   B 54  ? 0.1756 0.1965 0.2173 -0.0121 0.0012  0.0013  54  ASN   B O   
4828 C CB  . ASN   B 54  ? 0.1747 0.2001 0.2009 0.0001  -0.0114 0.0054  54  ASN   B CB  
4829 C CG  . ASN   B 54  ? 0.1879 0.2101 0.2030 -0.0030 -0.0245 -0.0066 54  ASN   B CG  
4830 O OD1 . ASN   B 54  ? 0.1865 0.2070 0.2168 -0.0120 -0.0299 -0.0136 54  ASN   B OD1 
4831 N ND2 . ASN   B 54  ? 0.2072 0.2327 0.2393 -0.0024 -0.0492 0.0022  54  ASN   B ND2 
4838 N N   . LYS   B 55  ? 0.1763 0.1838 0.2142 0.0121  -0.0091 0.0084  55  LYS   B N   
4839 C CA  . LYS   B 55  ? 0.1932 0.1928 0.2372 0.0157  -0.0235 0.0056  55  LYS   B CA  
4840 C C   . LYS   B 55  ? 0.1879 0.1989 0.2303 0.0131  -0.0203 -0.0113 55  LYS   B C   
4841 O O   . LYS   B 55  ? 0.1820 0.2111 0.2414 0.0106  -0.0123 -0.0093 55  LYS   B O   
4842 C CB  . LYS   B 55  ? 0.2113 0.2089 0.2696 0.0282  -0.0080 0.0176  55  LYS   B CB  
4843 C CG  . LYS   B 55  ? 0.2594 0.2537 0.3706 0.0162  0.0268  0.0235  55  LYS   B CG  
4844 C CD  . LYS   B 55  ? 0.2983 0.2837 0.4411 0.0356  0.0707  0.0331  55  LYS   B CD  
4845 C CE  . LYS   B 55  ? 0.3369 0.3104 0.5231 0.0340  0.0948  0.0461  55  LYS   B CE  
4846 N NZ  . LYS   B 55  ? 0.3551 0.3417 0.5774 0.0203  0.0642  0.0730  55  LYS   B NZ  
4860 N N   . ALA   B 56  ? 0.1737 0.2034 0.1891 0.0016  -0.0228 -0.0090 56  ALA   B N   
4861 C CA  . ALA   B 56  ? 0.1938 0.2116 0.2007 0.0048  -0.0142 -0.0178 56  ALA   B CA  
4862 C C   . ALA   B 56  ? 0.1925 0.2099 0.2000 0.0025  0.0002  -0.0141 56  ALA   B C   
4863 O O   . ALA   B 56  ? 0.2077 0.2209 0.2267 -0.0022 0.0136  0.0198  56  ALA   B O   
4864 C CB  . ALA   B 56  ? 0.1987 0.2340 0.1975 -0.0097 -0.0265 -0.0043 56  ALA   B CB  
4870 N N   . THR   B 57  ? 0.2115 0.2038 0.1989 -0.0080 0.0137  -0.0082 57  THR   B N   
4871 C CA  . THR   B 57  ? 0.2204 0.1891 0.2245 -0.0038 -0.0051 -0.0073 57  THR   B CA  
4872 C C   . THR   B 57  ? 0.2106 0.2158 0.2588 -0.0116 0.0018  0.0044  57  THR   B C   
4873 O O   . THR   B 57  ? 0.1990 0.2177 0.2634 -0.0165 -0.0010 -0.0013 57  THR   B O   
4874 C CB  . THR   B 57  ? 0.2202 0.1796 0.2015 -0.0105 -0.0119 0.0167  57  THR   B CB  
4875 O OG1 . THR   B 57  ? 0.2124 0.1802 0.2325 -0.0118 -0.0050 0.0034  57  THR   B OG1 
4876 C CG2 . THR   B 57  ? 0.2177 0.1773 0.2112 -0.0068 -0.0208 -0.0025 57  THR   B CG2 
4884 N N   . ASN   B 58  ? 0.1859 0.2306 0.2646 -0.0305 0.0018  0.0003  58  ASN   B N   
4885 C CA  . ASN   B 58  ? 0.2068 0.2957 0.3007 -0.0507 0.0203  0.0187  58  ASN   B CA  
4886 C C   . ASN   B 58  ? 0.1780 0.2648 0.2649 -0.0328 -0.0192 0.0054  58  ASN   B C   
4887 O O   . ASN   B 58  ? 0.1814 0.2795 0.2814 -0.0356 -0.0089 -0.0270 58  ASN   B O   
4888 C CB  . ASN   B 58  ? 0.3320 0.4059 0.4387 -0.0653 0.0444  0.0347  58  ASN   B CB  
4889 C CG  . ASN   B 58  ? 0.4856 0.5156 0.6163 -0.0653 0.0633  0.0566  58  ASN   B CG  
4890 O OD1 . ASN   B 58  ? 0.5325 0.5341 0.6724 -0.0658 0.0669  0.0632  58  ASN   B OD1 
4891 N ND2 . ASN   B 58  ? 0.6262 0.6262 0.6888 -0.0654 0.0705  0.0614  58  ASN   B ND2 
4898 N N   . ASN   B 59  ? 0.1781 0.2426 0.2466 -0.0120 -0.0348 0.0155  59  ASN   B N   
4899 C CA  . ASN   B 59  ? 0.1910 0.2315 0.2254 -0.0106 -0.0355 0.0055  59  ASN   B CA  
4900 C C   . ASN   B 59  ? 0.1749 0.2159 0.2363 -0.0266 -0.0274 -0.0117 59  ASN   B C   
4901 O O   . ASN   B 59  ? 0.1874 0.2266 0.2332 -0.0220 -0.0085 -0.0127 59  ASN   B O   
4902 C CB  . ASN   B 59  ? 0.1929 0.2468 0.2240 -0.0148 -0.0396 0.0051  59  ASN   B CB  
4903 C CG  . ASN   B 59  ? 0.2182 0.2589 0.2583 -0.0183 -0.0705 0.0027  59  ASN   B CG  
4904 O OD1 . ASN   B 59  ? 0.2315 0.2638 0.2338 -0.0170 -0.0478 0.0289  59  ASN   B OD1 
4905 N ND2 . ASN   B 59  ? 0.2226 0.2624 0.3090 -0.0158 -0.0840 0.0065  59  ASN   B ND2 
4912 N N   . ALA   B 60  ? 0.1734 0.2066 0.2474 -0.0159 -0.0223 0.0179  60  ALA   B N   
4913 C CA  . ALA   B 60  ? 0.1852 0.2103 0.2571 -0.0234 -0.0235 0.0073  60  ALA   B CA  
4914 C C   . ALA   B 60  ? 0.1905 0.1909 0.2103 -0.0148 -0.0121 -0.0053 60  ALA   B C   
4915 O O   . ALA   B 60  ? 0.1919 0.1957 0.2113 -0.0169 -0.0060 -0.0078 60  ALA   B O   
4916 C CB  . ALA   B 60  ? 0.1978 0.2126 0.3070 -0.0203 -0.0007 0.0072  60  ALA   B CB  
4922 N N   . MET   B 61  ? 0.1818 0.1715 0.2223 -0.0209 -0.0109 0.0050  61  MET   B N   
4923 C CA  . MET   B 61  ? 0.1847 0.1685 0.1948 -0.0146 -0.0175 -0.0000 61  MET   B CA  
4924 C C   . MET   B 61  ? 0.1929 0.1718 0.2167 -0.0116 -0.0300 0.0103  61  MET   B C   
4925 O O   . MET   B 61  ? 0.1925 0.1792 0.2023 -0.0059 -0.0305 -0.0140 61  MET   B O   
4926 C CB  . MET   B 61  ? 0.1838 0.1854 0.2075 -0.0128 -0.0172 0.0031  61  MET   B CB  
4927 C CG  . MET   B 61  ? 0.1792 0.1837 0.1778 -0.0153 -0.0072 -0.0076 61  MET   B CG  
4928 S SD  . MET   B 61  ? 0.1798 0.1774 0.2116 -0.0110 -0.0165 -0.0103 61  MET   B SD  
4929 C CE  . MET   B 61  ? 0.1976 0.1822 0.2133 -0.0189 -0.0208 -0.0348 61  MET   B CE  
4939 N N   . GLN   B 62  ? 0.1753 0.1830 0.2139 -0.0079 -0.0348 0.0207  62  GLN   B N   
4940 C CA  . GLN   B 62  ? 0.1912 0.1864 0.2089 -0.0083 -0.0428 0.0039  62  GLN   B CA  
4941 C C   . GLN   B 62  ? 0.1876 0.1910 0.2128 -0.0042 -0.0417 0.0054  62  GLN   B C   
4942 O O   . GLN   B 62  ? 0.2124 0.1980 0.2053 -0.0011 -0.0448 -0.0136 62  GLN   B O   
4943 C CB  . GLN   B 62  ? 0.2090 0.2011 0.2077 -0.0069 -0.0633 0.0098  62  GLN   B CB  
4944 C CG  . GLN   B 62  ? 0.2096 0.1980 0.2033 -0.0074 -0.0683 -0.0093 62  GLN   B CG  
4945 C CD  . GLN   B 62  ? 0.2128 0.1849 0.2295 0.0045  -0.0518 -0.0107 62  GLN   B CD  
4946 O OE1 . GLN   B 62  ? 0.2054 0.1777 0.2413 0.0030  -0.0432 -0.0092 62  GLN   B OE1 
4947 N NE2 . GLN   B 62  ? 0.2127 0.1871 0.2280 0.0003  -0.0393 -0.0295 62  GLN   B NE2 
4956 N N   . VAL   B 63  ? 0.1916 0.1908 0.2289 -0.0197 -0.0291 -0.0169 63  VAL   B N   
4957 C CA  . VAL   B 63  ? 0.2138 0.1846 0.2472 -0.0145 -0.0389 -0.0152 63  VAL   B CA  
4958 C C   . VAL   B 63  ? 0.2134 0.1790 0.2172 -0.0153 -0.0527 -0.0245 63  VAL   B C   
4959 O O   . VAL   B 63  ? 0.2280 0.1811 0.2387 -0.0251 -0.0541 -0.0177 63  VAL   B O   
4960 C CB  . VAL   B 63  ? 0.2158 0.1993 0.2853 -0.0232 -0.0222 -0.0155 63  VAL   B CB  
4961 C CG1 . VAL   B 63  ? 0.2137 0.2033 0.3125 -0.0374 -0.0076 -0.0237 63  VAL   B CG1 
4962 C CG2 . VAL   B 63  ? 0.2082 0.2305 0.2838 -0.0132 -0.0320 -0.0326 63  VAL   B CG2 
4972 N N   . GLU   B 64  ? 0.1925 0.1805 0.1985 -0.0141 -0.0382 -0.0133 64  GLU   B N   
4973 C CA  . GLU   B 64  ? 0.1950 0.1761 0.2059 -0.0192 -0.0462 0.0024  64  GLU   B CA  
4974 C C   . GLU   B 64  ? 0.1905 0.1622 0.2058 0.0041  -0.0548 -0.0089 64  GLU   B C   
4975 O O   . GLU   B 64  ? 0.2078 0.1629 0.2024 -0.0091 -0.0459 -0.0172 64  GLU   B O   
4976 C CB  . GLU   B 64  ? 0.1983 0.1964 0.1985 -0.0203 -0.0459 0.0084  64  GLU   B CB  
4977 C CG  . GLU   B 64  ? 0.2010 0.1879 0.2126 -0.0179 -0.0496 -0.0174 64  GLU   B CG  
4978 C CD  . GLU   B 64  ? 0.1907 0.2006 0.2270 -0.0202 -0.0513 -0.0195 64  GLU   B CD  
4979 O OE1 . GLU   B 64  ? 0.2101 0.2039 0.2389 -0.0300 -0.0307 -0.0260 64  GLU   B OE1 
4980 O OE2 . GLU   B 64  ? 0.1972 0.2093 0.2536 -0.0405 -0.0666 -0.0095 64  GLU   B OE2 
4987 N N   . SER   B 65  ? 0.1983 0.1751 0.1829 -0.0119 -0.0386 -0.0099 65  SER   B N   
4988 C CA  . SER   B 65  ? 0.1980 0.1736 0.2029 0.0035  -0.0335 -0.0110 65  SER   B CA  
4989 C C   . SER   B 65  ? 0.2004 0.1912 0.2027 -0.0012 -0.0407 -0.0229 65  SER   B C   
4990 O O   . SER   B 65  ? 0.1932 0.1833 0.2211 -0.0157 -0.0338 -0.0196 65  SER   B O   
4991 C CB  . SER   B 65  ? 0.2076 0.1683 0.2063 0.0004  -0.0428 0.0016  65  SER   B CB  
4992 O OG  . SER   B 65  ? 0.2069 0.1688 0.2016 -0.0060 -0.0402 -0.0168 65  SER   B OG  
4998 N N   . ASP   B 66  ? 0.2017 0.1885 0.1878 -0.0148 -0.0444 -0.0119 66  ASP   B N   
4999 C CA  . ASP   B 66  ? 0.2199 0.1894 0.1763 -0.0148 -0.0527 -0.0103 66  ASP   B CA  
5000 C C   . ASP   B 66  ? 0.2300 0.1963 0.1892 -0.0185 -0.0420 -0.0212 66  ASP   B C   
5001 O O   . ASP   B 66  ? 0.2399 0.2010 0.2019 -0.0080 -0.0388 -0.0173 66  ASP   B O   
5002 C CB  . ASP   B 66  ? 0.2381 0.2010 0.2221 -0.0031 -0.0760 -0.0367 66  ASP   B CB  
5003 C CG  . ASP   B 66  ? 0.2628 0.2182 0.2457 0.0020  -0.0966 -0.0136 66  ASP   B CG  
5004 O OD1 . ASP   B 66  ? 0.2786 0.2191 0.2588 0.0019  -0.0794 -0.0059 66  ASP   B OD1 
5005 O OD2 . ASP   B 66  ? 0.2998 0.2400 0.3198 0.0222  -0.0863 -0.0134 66  ASP   B OD2 
5010 N N   . ASP   B 67  ? 0.2228 0.1866 0.2081 -0.0057 -0.0464 -0.0283 67  ASP   B N   
5011 C CA  . ASP   B 67  ? 0.2305 0.1886 0.2037 -0.0063 -0.0360 -0.0161 67  ASP   B CA  
5012 C C   . ASP   B 67  ? 0.2275 0.1931 0.2315 0.0013  -0.0453 -0.0304 67  ASP   B C   
5013 O O   . ASP   B 67  ? 0.2182 0.1985 0.2330 -0.0057 -0.0395 -0.0245 67  ASP   B O   
5014 C CB  . ASP   B 67  ? 0.2520 0.1989 0.2245 -0.0209 -0.0446 -0.0160 67  ASP   B CB  
5015 C CG  . ASP   B 67  ? 0.2906 0.2053 0.2519 -0.0181 -0.0796 -0.0147 67  ASP   B CG  
5016 O OD1 . ASP   B 67  ? 0.3258 0.1931 0.2662 -0.0111 -0.0755 0.0071  67  ASP   B OD1 
5017 O OD2 . ASP   B 67  ? 0.3013 0.2134 0.2798 -0.0035 -0.0851 -0.0188 67  ASP   B OD2 
5022 N N   . TYR   B 68  ? 0.2221 0.1780 0.2291 0.0042  -0.0499 -0.0320 68  TYR   B N   
5023 C CA  . TYR   B 68  ? 0.2234 0.1954 0.2194 0.0019  -0.0458 -0.0345 68  TYR   B CA  
5024 C C   . TYR   B 68  ? 0.2211 0.1932 0.2125 0.0018  -0.0407 -0.0301 68  TYR   B C   
5025 O O   . TYR   B 68  ? 0.2242 0.1980 0.2297 0.0081  -0.0492 -0.0457 68  TYR   B O   
5026 C CB  . TYR   B 68  ? 0.2179 0.2276 0.2262 0.0013  -0.0488 -0.0535 68  TYR   B CB  
5027 C CG  . TYR   B 68  ? 0.2209 0.2647 0.2367 0.0176  -0.0384 -0.0743 68  TYR   B CG  
5028 C CD1 . TYR   B 68  ? 0.2104 0.2793 0.2613 0.0018  -0.0378 -0.0843 68  TYR   B CD1 
5029 C CD2 . TYR   B 68  ? 0.2205 0.2903 0.2665 0.0243  -0.0583 -0.0740 68  TYR   B CD2 
5030 C CE1 . TYR   B 68  ? 0.2213 0.2978 0.3129 0.0052  -0.0454 -0.1070 68  TYR   B CE1 
5031 C CE2 . TYR   B 68  ? 0.2210 0.3034 0.3088 0.0186  -0.0484 -0.0998 68  TYR   B CE2 
5032 C CZ  . TYR   B 68  ? 0.2228 0.3088 0.3181 0.0062  -0.0583 -0.1147 68  TYR   B CZ  
5033 O OH  . TYR   B 68  ? 0.2272 0.3355 0.3627 -0.0085 -0.0329 -0.1138 68  TYR   B OH  
5043 N N   . ILE   B 69  ? 0.2100 0.1890 0.2158 -0.0051 -0.0471 -0.0211 69  ILE   B N   
5044 C CA  . ILE   B 69  ? 0.2244 0.2048 0.2384 -0.0120 -0.0492 -0.0178 69  ILE   B CA  
5045 C C   . ILE   B 69  ? 0.2147 0.2012 0.2330 0.0076  -0.0631 -0.0247 69  ILE   B C   
5046 O O   . ILE   B 69  ? 0.2124 0.2095 0.2262 0.0132  -0.0404 -0.0262 69  ILE   B O   
5047 C CB  . ILE   B 69  ? 0.2317 0.2040 0.2706 -0.0075 -0.0067 -0.0164 69  ILE   B CB  
5048 C CG1 . ILE   B 69  ? 0.2361 0.2195 0.2826 -0.0253 0.0134  -0.0454 69  ILE   B CG1 
5049 C CG2 . ILE   B 69  ? 0.2567 0.2070 0.2767 -0.0054 -0.0074 -0.0275 69  ILE   B CG2 
5050 C CD1 . ILE   B 69  ? 0.2333 0.2169 0.3089 -0.0353 0.0249  -0.0557 69  ILE   B CD1 
5062 N N   . ALA   B 70  ? 0.2233 0.1914 0.2378 0.0064  -0.0583 -0.0382 70  ALA   B N   
5063 C CA  . ALA   B 70  ? 0.2204 0.1913 0.2105 -0.0009 -0.0408 -0.0378 70  ALA   B CA  
5064 C C   . ALA   B 70  ? 0.2270 0.1887 0.2104 -0.0080 -0.0476 -0.0410 70  ALA   B C   
5065 O O   . ALA   B 70  ? 0.2492 0.1915 0.2339 -0.0006 -0.0544 -0.0457 70  ALA   B O   
5066 C CB  . ALA   B 70  ? 0.2180 0.2174 0.1981 -0.0017 -0.0483 -0.0263 70  ALA   B CB  
5072 N N   . THR   B 71  ? 0.2501 0.1955 0.2230 0.0005  -0.0632 -0.0416 71  THR   B N   
5073 C CA  . THR   B 71  ? 0.2618 0.2028 0.2619 0.0032  -0.0676 -0.0501 71  THR   B CA  
5074 C C   . THR   B 71  ? 0.2497 0.2026 0.2678 0.0207  -0.0661 -0.0493 71  THR   B C   
5075 O O   . THR   B 71  ? 0.2583 0.2020 0.2865 0.0216  -0.0615 -0.0605 71  THR   B O   
5076 C CB  . THR   B 71  ? 0.2775 0.2196 0.2974 0.0063  -0.0805 -0.0343 71  THR   B CB  
5077 O OG1 . THR   B 71  ? 0.2939 0.2438 0.3288 -0.0167 -0.1045 -0.0135 71  THR   B OG1 
5078 C CG2 . THR   B 71  ? 0.2960 0.2020 0.3107 -0.0018 -0.0649 -0.0065 71  THR   B CG2 
5086 N N   . ASN   B 72  ? 0.2287 0.2140 0.2627 0.0199  -0.0793 -0.0559 72  ASN   B N   
5087 C CA  . ASN   B 72  ? 0.2288 0.2206 0.2715 0.0135  -0.0761 -0.0822 72  ASN   B CA  
5088 C C   . ASN   B 72  ? 0.2295 0.2281 0.2872 -0.0065 -0.0578 -0.0765 72  ASN   B C   
5089 O O   . ASN   B 72  ? 0.2377 0.2506 0.3407 -0.0033 -0.0066 -0.0821 72  ASN   B O   
5090 C CB  . ASN   B 72  ? 0.2265 0.2489 0.2764 0.0143  -0.0663 -0.0655 72  ASN   B CB  
5091 C CG  . ASN   B 72  ? 0.2420 0.2637 0.2802 0.0332  -0.0612 -0.0427 72  ASN   B CG  
5092 O OD1 . ASN   B 72  ? 0.2827 0.2753 0.2944 0.0233  -0.0585 -0.0449 72  ASN   B OD1 
5093 N ND2 . ASN   B 72  ? 0.2508 0.2848 0.3278 0.0461  -0.0665 -0.0023 72  ASN   B ND2 
5100 N N   . GLY   B 73  ? 0.2333 0.2273 0.2896 -0.0156 -0.0535 -0.0727 73  GLY   B N   
5101 C CA  . GLY   B 73  ? 0.2254 0.2400 0.2582 -0.0261 -0.0509 -0.0639 73  GLY   B CA  
5102 C C   . GLY   B 73  ? 0.2158 0.2439 0.2236 -0.0145 -0.0489 -0.0483 73  GLY   B C   
5103 O O   . GLY   B 73  ? 0.2124 0.2376 0.2252 -0.0043 -0.0427 -0.0476 73  GLY   B O   
5107 N N   . PRO   B 74  ? 0.2273 0.2582 0.1772 -0.0079 -0.0418 -0.0453 74  PRO   B N   
5108 C CA  . PRO   B 74  ? 0.2245 0.2535 0.1623 -0.0013 -0.0316 -0.0296 74  PRO   B CA  
5109 C C   . PRO   B 74  ? 0.2142 0.2262 0.1790 -0.0037 -0.0255 -0.0343 74  PRO   B C   
5110 O O   . PRO   B 74  ? 0.2154 0.2292 0.2307 -0.0135 -0.0161 -0.0390 74  PRO   B O   
5111 C CB  . PRO   B 74  ? 0.2429 0.2686 0.1552 0.0028  -0.0295 -0.0261 74  PRO   B CB  
5112 C CG  . PRO   B 74  ? 0.2716 0.2843 0.1994 0.0030  -0.0239 -0.0270 74  PRO   B CG  
5113 C CD  . PRO   B 74  ? 0.2636 0.2681 0.1763 0.0091  -0.0146 -0.0384 74  PRO   B CD  
5121 N N   . LEU   B 75  ? 0.2175 0.2165 0.1661 0.0148  -0.0362 -0.0263 75  LEU   B N   
5122 C CA  . LEU   B 75  ? 0.2213 0.2125 0.1654 -0.0081 -0.0340 -0.0074 75  LEU   B CA  
5123 C C   . LEU   B 75  ? 0.2259 0.2355 0.1686 -0.0035 -0.0102 -0.0113 75  LEU   B C   
5124 O O   . LEU   B 75  ? 0.2253 0.2478 0.1983 -0.0094 -0.0068 -0.0111 75  LEU   B O   
5125 C CB  . LEU   B 75  ? 0.2111 0.2218 0.1639 -0.0176 -0.0485 0.0202  75  LEU   B CB  
5126 C CG  . LEU   B 75  ? 0.2488 0.2388 0.1820 -0.0345 -0.0341 0.0135  75  LEU   B CG  
5127 C CD1 . LEU   B 75  ? 0.2819 0.2553 0.1959 -0.0542 0.0118  0.0066  75  LEU   B CD1 
5128 C CD2 . LEU   B 75  ? 0.2897 0.2709 0.2881 -0.0247 -0.0292 0.0339  75  LEU   B CD2 
5140 N N   . LYS   B 76  ? 0.2282 0.2640 0.2099 -0.0141 -0.0147 0.0055  76  LYS   B N   
5141 C CA  . LYS   B 76  ? 0.2367 0.2632 0.2486 -0.0128 0.0215  -0.0029 76  LYS   B CA  
5142 C C   . LYS   B 76  ? 0.2205 0.2438 0.1988 -0.0158 -0.0010 0.0133  76  LYS   B C   
5143 O O   . LYS   B 76  ? 0.2239 0.2183 0.1992 -0.0180 -0.0081 0.0180  76  LYS   B O   
5144 C CB  . LYS   B 76  ? 0.2461 0.2784 0.3016 -0.0199 0.0450  -0.0449 76  LYS   B CB  
5145 C CG  . LYS   B 76  ? 0.2506 0.3131 0.3472 -0.0087 0.0186  -0.0669 76  LYS   B CG  
5146 C CD  . LYS   B 76  ? 0.2376 0.3340 0.3937 0.0024  0.0283  -0.0854 76  LYS   B CD  
5147 C CE  . LYS   B 76  ? 0.2406 0.3655 0.4505 0.0014  0.0091  -0.0827 76  LYS   B CE  
5148 N NZ  . LYS   B 76  ? 0.2266 0.3732 0.4511 -0.0124 -0.0265 -0.1124 76  LYS   B NZ  
5162 N N   . VAL   B 77  ? 0.2178 0.2654 0.2061 -0.0027 0.0009  0.0223  77  VAL   B N   
5163 C CA  . VAL   B 77  ? 0.2189 0.2519 0.2181 -0.0065 -0.0038 0.0569  77  VAL   B CA  
5164 C C   . VAL   B 77  ? 0.1960 0.2237 0.2255 0.0013  0.0096  0.0430  77  VAL   B C   
5165 O O   . VAL   B 77  ? 0.1995 0.2230 0.1941 0.0118  0.0052  0.0340  77  VAL   B O   
5166 C CB  . VAL   B 77  ? 0.2382 0.2596 0.2720 -0.0047 -0.0040 0.0598  77  VAL   B CB  
5167 C CG1 . VAL   B 77  ? 0.2582 0.2485 0.3106 -0.0036 0.0145  0.0787  77  VAL   B CG1 
5168 C CG2 . VAL   B 77  ? 0.2548 0.2832 0.2959 -0.0064 -0.0205 0.0623  77  VAL   B CG2 
5178 N N   . GLY   B 78  ? 0.1946 0.2083 0.2077 0.0104  0.0098  0.0293  78  GLY   B N   
5179 C CA  . GLY   B 78  ? 0.2133 0.2144 0.1825 0.0174  0.0088  0.0509  78  GLY   B CA  
5180 C C   . GLY   B 78  ? 0.2045 0.2064 0.1876 0.0090  0.0042  0.0326  78  GLY   B C   
5181 O O   . GLY   B 78  ? 0.1963 0.1867 0.2123 -0.0042 -0.0019 0.0307  78  GLY   B O   
5185 N N   . GLY   B 79  ? 0.1944 0.2049 0.1933 -0.0043 0.0034  0.0276  79  GLY   B N   
5186 C CA  . GLY   B 79  ? 0.1958 0.1983 0.1961 0.0010  0.0050  0.0222  79  GLY   B CA  
5187 C C   . GLY   B 79  ? 0.1844 0.1991 0.1791 -0.0002 0.0027  0.0084  79  GLY   B C   
5188 O O   . GLY   B 79  ? 0.1911 0.1864 0.2120 0.0014  -0.0055 0.0162  79  GLY   B O   
5192 N N   . SER   B 80  ? 0.1807 0.1837 0.2086 -0.0030 -0.0038 0.0035  80  SER   B N   
5193 C CA  . SER   B 80  ? 0.1756 0.1739 0.2079 -0.0049 -0.0190 0.0090  80  SER   B CA  
5194 C C   . SER   B 80  ? 0.1706 0.1755 0.2141 0.0041  -0.0254 0.0032  80  SER   B C   
5195 O O   . SER   B 80  ? 0.1893 0.1732 0.2387 0.0178  -0.0240 0.0051  80  SER   B O   
5196 C CB  . SER   B 80  ? 0.1760 0.1740 0.2042 -0.0032 -0.0218 0.0304  80  SER   B CB  
5197 O OG  . SER   B 80  ? 0.1778 0.1859 0.2199 -0.0105 -0.0145 0.0142  80  SER   B OG  
5203 N N   . CYS   B 81  ? 0.1696 0.1704 0.2036 -0.0022 -0.0243 0.0017  81  CYS   B N   
5204 C CA  . CYS   B 81  ? 0.1799 0.1659 0.1840 -0.0002 -0.0283 -0.0019 81  CYS   B CA  
5205 C C   . CYS   B 81  ? 0.1877 0.1632 0.1824 0.0095  -0.0270 0.0116  81  CYS   B C   
5206 O O   . CYS   B 81  ? 0.2065 0.1543 0.1938 0.0128  -0.0098 0.0096  81  CYS   B O   
5207 C CB  . CYS   B 81  ? 0.1951 0.1715 0.2059 0.0065  -0.0168 0.0090  81  CYS   B CB  
5208 S SG  . CYS   B 81  ? 0.1961 0.1903 0.2076 -0.0125 -0.0424 -0.0082 81  CYS   B SG  
5214 N N   . VAL   B 82  ? 0.1852 0.1574 0.1737 -0.0066 -0.0268 0.0139  82  VAL   B N   
5215 C CA  . VAL   B 82  ? 0.1909 0.1619 0.1652 -0.0197 -0.0189 0.0140  82  VAL   B CA  
5216 C C   . VAL   B 82  ? 0.1999 0.1579 0.1899 -0.0094 -0.0369 -0.0043 82  VAL   B C   
5217 O O   . VAL   B 82  ? 0.2011 0.1631 0.2209 -0.0091 -0.0388 -0.0233 82  VAL   B O   
5218 C CB  . VAL   B 82  ? 0.1954 0.1723 0.1981 -0.0016 -0.0248 0.0081  82  VAL   B CB  
5219 C CG1 . VAL   B 82  ? 0.2111 0.2010 0.2185 0.0120  -0.0313 0.0168  82  VAL   B CG1 
5220 C CG2 . VAL   B 82  ? 0.2046 0.1920 0.2199 -0.0159 -0.0341 0.0077  82  VAL   B CG2 
5230 N N   . LEU   B 83  ? 0.1897 0.1594 0.1932 -0.0199 -0.0311 0.0073  83  LEU   B N   
5231 C CA  . LEU   B 83  ? 0.1825 0.1513 0.2031 -0.0185 -0.0261 0.0086  83  LEU   B CA  
5232 C C   . LEU   B 83  ? 0.1894 0.1521 0.1915 -0.0239 -0.0386 0.0162  83  LEU   B C   
5233 O O   . LEU   B 83  ? 0.1933 0.1598 0.1900 -0.0128 -0.0404 0.0227  83  LEU   B O   
5234 C CB  . LEU   B 83  ? 0.2027 0.1631 0.2225 -0.0207 -0.0387 -0.0083 83  LEU   B CB  
5235 C CG  . LEU   B 83  ? 0.2235 0.1745 0.2161 -0.0259 -0.0278 -0.0091 83  LEU   B CG  
5236 C CD1 . LEU   B 83  ? 0.2373 0.1639 0.2143 -0.0056 -0.0268 -0.0063 83  LEU   B CD1 
5237 C CD2 . LEU   B 83  ? 0.2301 0.1787 0.2256 -0.0223 -0.0455 -0.0114 83  LEU   B CD2 
5249 N N   . SER   B 84  ? 0.2107 0.1507 0.1986 -0.0347 -0.0296 -0.0033 84  SER   B N   
5250 C CA  . SER   B 84  ? 0.2041 0.1731 0.1795 -0.0305 -0.0173 0.0200  84  SER   B CA  
5251 C C   . SER   B 84  ? 0.1879 0.2043 0.1381 -0.0197 -0.0359 0.0294  84  SER   B C   
5252 O O   . SER   B 84  ? 0.1923 0.1899 0.1481 -0.0229 -0.0264 -0.0002 84  SER   B O   
5253 C CB  . SER   B 84  ? 0.2205 0.1886 0.2516 -0.0378 0.0086  0.0077  84  SER   B CB  
5254 O OG  . SER   B 84  ? 0.2152 0.2061 0.3181 -0.0440 -0.0049 0.0147  84  SER   B OG  
5260 N N   . GLY   B 85  ? 0.1824 0.2201 0.1535 -0.0267 -0.0308 0.0388  85  GLY   B N   
5261 C CA  . GLY   B 85  ? 0.1930 0.2175 0.1708 -0.0326 0.0016  -0.0009 85  GLY   B CA  
5262 C C   . GLY   B 85  ? 0.1872 0.1886 0.1847 -0.0385 -0.0181 0.0001  85  GLY   B C   
5263 O O   . GLY   B 85  ? 0.2007 0.2046 0.1870 -0.0547 -0.0042 -0.0176 85  GLY   B O   
5267 N N   . HIS   B 86  ? 0.1867 0.1783 0.1911 -0.0320 -0.0357 0.0137  86  HIS   B N   
5268 C CA  . HIS   B 86  ? 0.1896 0.1935 0.1977 -0.0385 -0.0423 0.0159  86  HIS   B CA  
5269 C C   . HIS   B 86  ? 0.1888 0.2177 0.1953 -0.0444 -0.0344 0.0427  86  HIS   B C   
5270 O O   . HIS   B 86  ? 0.1951 0.2337 0.2194 -0.0432 -0.0166 0.0459  86  HIS   B O   
5271 C CB  . HIS   B 86  ? 0.2014 0.1923 0.2000 -0.0295 -0.0378 0.0044  86  HIS   B CB  
5272 C CG  . HIS   B 86  ? 0.1995 0.1978 0.1685 -0.0178 -0.0598 0.0022  86  HIS   B CG  
5273 N ND1 . HIS   B 86  ? 0.2043 0.2307 0.2195 -0.0321 -0.0493 0.0065  86  HIS   B ND1 
5274 C CD2 . HIS   B 86  ? 0.1998 0.1907 0.2023 -0.0197 -0.0411 -0.0016 86  HIS   B CD2 
5275 C CE1 . HIS   B 86  ? 0.2214 0.2183 0.2191 -0.0197 -0.0258 -0.0167 86  HIS   B CE1 
5276 N NE2 . HIS   B 86  ? 0.1987 0.2063 0.2129 -0.0092 -0.0225 -0.0098 86  HIS   B NE2 
5284 N N   . ASN   B 87  ? 0.1956 0.2128 0.2049 -0.0385 -0.0127 0.0339  87  ASN   B N   
5285 C CA  . ASN   B 87  ? 0.2034 0.2269 0.1958 -0.0274 -0.0142 0.0376  87  ASN   B CA  
5286 C C   . ASN   B 87  ? 0.2266 0.2090 0.1819 -0.0298 0.0065  0.0246  87  ASN   B C   
5287 O O   . ASN   B 87  ? 0.2487 0.2221 0.2183 -0.0311 0.0250  0.0146  87  ASN   B O   
5288 C CB  . ASN   B 87  ? 0.2082 0.2615 0.2340 -0.0151 -0.0199 0.0125  87  ASN   B CB  
5289 C CG  . ASN   B 87  ? 0.2303 0.2816 0.2283 0.0208  -0.0006 0.0367  87  ASN   B CG  
5290 O OD1 . ASN   B 87  ? 0.2251 0.2559 0.2058 0.0205  0.0243  0.0460  87  ASN   B OD1 
5291 N ND2 . ASN   B 87  ? 0.2710 0.3050 0.2997 0.0254  0.0121  0.0412  87  ASN   B ND2 
5298 N N   . LEU   B 88  ? 0.1997 0.1942 0.1814 -0.0400 0.0017  0.0121  88  LEU   B N   
5299 C CA  . LEU   B 88  ? 0.2061 0.1944 0.1860 -0.0378 -0.0234 0.0023  88  LEU   B CA  
5300 C C   . LEU   B 88  ? 0.2038 0.1936 0.1828 -0.0355 -0.0270 0.0021  88  LEU   B C   
5301 O O   . LEU   B 88  ? 0.2215 0.1952 0.2011 -0.0169 -0.0405 -0.0030 88  LEU   B O   
5302 C CB  . LEU   B 88  ? 0.2395 0.2030 0.2007 -0.0330 -0.0295 0.0271  88  LEU   B CB  
5303 C CG  . LEU   B 88  ? 0.2789 0.2387 0.2097 -0.0365 -0.0625 0.0525  88  LEU   B CG  
5304 C CD1 . LEU   B 88  ? 0.2916 0.2803 0.2071 -0.0515 -0.0486 0.0596  88  LEU   B CD1 
5305 C CD2 . LEU   B 88  ? 0.3277 0.2773 0.2977 0.0028  -0.0783 0.0287  88  LEU   B CD2 
5317 N N   . ALA   B 89  ? 0.2030 0.1856 0.1721 -0.0456 0.0026  0.0096  89  ALA   B N   
5318 C CA  . ALA   B 89  ? 0.1993 0.1762 0.1705 -0.0367 -0.0135 0.0146  89  ALA   B CA  
5319 C C   . ALA   B 89  ? 0.2107 0.1719 0.1938 -0.0382 -0.0011 0.0071  89  ALA   B C   
5320 O O   . ALA   B 89  ? 0.1891 0.1889 0.2194 -0.0487 -0.0081 -0.0163 89  ALA   B O   
5321 C CB  . ALA   B 89  ? 0.1795 0.1847 0.1754 -0.0390 -0.0217 0.0255  89  ALA   B CB  
5327 N N   . LYS   B 90  ? 0.2442 0.1611 0.1900 -0.0446 -0.0110 0.0138  90  LYS   B N   
5328 C CA  . LYS   B 90  ? 0.2526 0.1675 0.1725 -0.0439 -0.0160 0.0157  90  LYS   B CA  
5329 C C   . LYS   B 90  ? 0.2432 0.1730 0.1817 -0.0342 -0.0210 -0.0015 90  LYS   B C   
5330 O O   . LYS   B 90  ? 0.2583 0.1826 0.1957 -0.0545 -0.0191 -0.0099 90  LYS   B O   
5331 C CB  . LYS   B 90  ? 0.2772 0.1797 0.1995 -0.0472 -0.0112 0.0242  90  LYS   B CB  
5332 C CG  . LYS   B 90  ? 0.2857 0.1943 0.1898 -0.0368 0.0046  0.0065  90  LYS   B CG  
5333 C CD  . LYS   B 90  ? 0.3250 0.2313 0.2830 -0.0270 0.0377  -0.0205 90  LYS   B CD  
5334 C CE  . LYS   B 90  ? 0.3280 0.2624 0.3477 -0.0419 0.0671  -0.0247 90  LYS   B CE  
5335 N NZ  . LYS   B 90  ? 0.3202 0.2702 0.3265 -0.0705 0.1000  -0.0301 90  LYS   B NZ  
5349 N N   . HIS   B 91  ? 0.2159 0.1557 0.1625 -0.0254 -0.0345 0.0266  91  HIS   B N   
5350 C CA  . HIS   B 91  ? 0.2112 0.1620 0.1835 -0.0270 -0.0277 0.0103  91  HIS   B CA  
5351 C C   . HIS   B 91  ? 0.2033 0.1710 0.1412 -0.0264 -0.0285 0.0066  91  HIS   B C   
5352 O O   . HIS   B 91  ? 0.2114 0.1706 0.1387 -0.0251 -0.0350 0.0053  91  HIS   B O   
5353 C CB  . HIS   B 91  ? 0.2287 0.1744 0.2060 0.0016  -0.0337 0.0251  91  HIS   B CB  
5354 C CG  . HIS   B 91  ? 0.2574 0.1910 0.2629 0.0037  0.0052  0.0248  91  HIS   B CG  
5355 N ND1 . HIS   B 91  ? 0.2997 0.1989 0.3513 0.0073  0.0088  0.0265  91  HIS   B ND1 
5356 C CD2 . HIS   B 91  ? 0.2733 0.2142 0.3334 0.0141  0.0162  0.0475  91  HIS   B CD2 
5357 C CE1 . HIS   B 91  ? 0.3114 0.2054 0.3720 0.0228  0.0180  0.0191  91  HIS   B CE1 
5358 N NE2 . HIS   B 91  ? 0.2933 0.2167 0.3794 0.0371  0.0271  0.0565  91  HIS   B NE2 
5366 N N   . CYS   B 92  ? 0.1867 0.1664 0.1613 -0.0382 -0.0437 0.0012  92  CYS   B N   
5367 C CA  . CYS   B 92  ? 0.1961 0.1588 0.1362 -0.0292 -0.0345 0.0088  92  CYS   B CA  
5368 C C   . CYS   B 92  ? 0.1915 0.1508 0.1411 -0.0146 -0.0231 -0.0045 92  CYS   B C   
5369 O O   . CYS   B 92  ? 0.1927 0.1510 0.1710 -0.0148 -0.0162 0.0056  92  CYS   B O   
5370 C CB  . CYS   B 92  ? 0.1963 0.1578 0.1535 -0.0194 -0.0322 0.0027  92  CYS   B CB  
5371 S SG  . CYS   B 92  ? 0.1786 0.1678 0.1891 -0.0200 -0.0281 0.0064  92  CYS   B SG  
5377 N N   . LEU   B 93  ? 0.1733 0.1545 0.1500 -0.0207 -0.0251 -0.0002 93  LEU   B N   
5378 C CA  . LEU   B 93  ? 0.1736 0.1571 0.1692 -0.0088 -0.0405 0.0023  93  LEU   B CA  
5379 C C   . LEU   B 93  ? 0.1673 0.1517 0.1491 -0.0042 -0.0277 0.0091  93  LEU   B C   
5380 O O   . LEU   B 93  ? 0.1753 0.1396 0.1969 -0.0100 -0.0261 -0.0018 93  LEU   B O   
5381 C CB  . LEU   B 93  ? 0.1741 0.1563 0.1724 -0.0035 -0.0344 0.0107  93  LEU   B CB  
5382 C CG  . LEU   B 93  ? 0.1744 0.1760 0.1985 -0.0060 -0.0388 0.0095  93  LEU   B CG  
5383 C CD1 . LEU   B 93  ? 0.1859 0.1867 0.1969 0.0033  -0.0338 0.0007  93  LEU   B CD1 
5384 C CD2 . LEU   B 93  ? 0.1659 0.1678 0.2119 0.0012  -0.0365 0.0047  93  LEU   B CD2 
5396 N N   . HIS   B 94  ? 0.1821 0.1522 0.1434 -0.0128 -0.0234 0.0075  94  HIS   B N   
5397 C CA  . HIS   B 94  ? 0.1710 0.1486 0.1475 -0.0003 -0.0073 0.0007  94  HIS   B CA  
5398 C C   . HIS   B 94  ? 0.1677 0.1565 0.1887 -0.0089 -0.0074 0.0101  94  HIS   B C   
5399 O O   . HIS   B 94  ? 0.1760 0.1705 0.2107 -0.0137 0.0116  -0.0006 94  HIS   B O   
5400 C CB  . HIS   B 94  ? 0.1727 0.1612 0.1824 -0.0083 -0.0087 0.0082  94  HIS   B CB  
5401 C CG  . HIS   B 94  ? 0.1727 0.1522 0.1878 -0.0129 -0.0306 0.0116  94  HIS   B CG  
5402 N ND1 . HIS   B 94  ? 0.1788 0.1513 0.1899 -0.0093 -0.0356 0.0053  94  HIS   B ND1 
5403 C CD2 . HIS   B 94  ? 0.1790 0.1497 0.1862 -0.0044 -0.0393 0.0006  94  HIS   B CD2 
5404 C CE1 . HIS   B 94  ? 0.1710 0.1490 0.1953 -0.0034 -0.0368 0.0075  94  HIS   B CE1 
5405 N NE2 . HIS   B 94  ? 0.1701 0.1669 0.1868 -0.0133 -0.0379 -0.0007 94  HIS   B NE2 
5413 N N   . VAL   B 95  ? 0.1645 0.1405 0.1828 -0.0138 -0.0089 0.0036  95  VAL   B N   
5414 C CA  . VAL   B 95  ? 0.1757 0.1541 0.1707 -0.0062 -0.0086 0.0205  95  VAL   B CA  
5415 C C   . VAL   B 95  ? 0.1710 0.1585 0.1713 -0.0177 -0.0016 0.0180  95  VAL   B C   
5416 O O   . VAL   B 95  ? 0.1644 0.1741 0.1872 -0.0011 -0.0111 0.0248  95  VAL   B O   
5417 C CB  . VAL   B 95  ? 0.1758 0.1557 0.1612 -0.0081 -0.0271 -0.0085 95  VAL   B CB  
5418 C CG1 . VAL   B 95  ? 0.1821 0.1763 0.2043 -0.0134 -0.0114 0.0209  95  VAL   B CG1 
5419 C CG2 . VAL   B 95  ? 0.1947 0.1610 0.1690 0.0016  -0.0307 0.0198  95  VAL   B CG2 
5429 N N   . VAL   B 96  ? 0.1777 0.1735 0.1668 0.0035  -0.0015 0.0329  96  VAL   B N   
5430 C CA  . VAL   B 96  ? 0.1913 0.1891 0.1660 -0.0006 -0.0018 0.0315  96  VAL   B CA  
5431 C C   . VAL   B 96  ? 0.2002 0.1784 0.1968 0.0053  -0.0118 0.0214  96  VAL   B C   
5432 O O   . VAL   B 96  ? 0.1952 0.1885 0.2040 -0.0012 0.0062  0.0099  96  VAL   B O   
5433 C CB  . VAL   B 96  ? 0.1967 0.1945 0.1806 0.0092  0.0020  0.0039  96  VAL   B CB  
5434 C CG1 . VAL   B 96  ? 0.2101 0.2077 0.2008 0.0133  -0.0062 -0.0075 96  VAL   B CG1 
5435 C CG2 . VAL   B 96  ? 0.2053 0.2047 0.1689 0.0015  0.0084  -0.0060 96  VAL   B CG2 
5445 N N   . GLY   B 97  ? 0.1939 0.1756 0.1795 -0.0079 -0.0151 0.0328  97  GLY   B N   
5446 C CA  . GLY   B 97  ? 0.2106 0.1871 0.1897 -0.0025 0.0071  0.0330  97  GLY   B CA  
5447 C C   . GLY   B 97  ? 0.2231 0.1965 0.2156 -0.0032 0.0031  0.0246  97  GLY   B C   
5448 O O   . GLY   B 97  ? 0.2273 0.1995 0.2067 -0.0058 -0.0053 0.0147  97  GLY   B O   
5452 N N   . PRO   B 98  ? 0.2316 0.1929 0.2058 -0.0050 0.0140  0.0241  98  PRO   B N   
5453 C CA  . PRO   B 98  ? 0.2558 0.1995 0.2398 -0.0001 0.0150  0.0253  98  PRO   B CA  
5454 C C   . PRO   B 98  ? 0.2628 0.2016 0.1992 0.0101  0.0185  0.0334  98  PRO   B C   
5455 O O   . PRO   B 98  ? 0.2440 0.2120 0.2250 0.0184  0.0201  0.0528  98  PRO   B O   
5456 C CB  . PRO   B 98  ? 0.2462 0.2155 0.2362 0.0127  0.0259  0.0372  98  PRO   B CB  
5457 C CG  . PRO   B 98  ? 0.2292 0.2048 0.2561 -0.0041 0.0275  0.0577  98  PRO   B CG  
5458 C CD  . PRO   B 98  ? 0.2213 0.1892 0.2464 -0.0052 0.0125  0.0333  98  PRO   B CD  
5466 N N   . ASN   B 99  ? 0.2692 0.2267 0.2220 0.0322  0.0134  0.0204  99  ASN   B N   
5467 C CA  . ASN   B 99  ? 0.2921 0.2422 0.2289 0.0437  0.0177  0.0561  99  ASN   B CA  
5468 C C   . ASN   B 99  ? 0.3249 0.2911 0.2657 0.0519  0.0324  0.1085  99  ASN   B C   
5469 O O   . ASN   B 99  ? 0.3442 0.3100 0.2976 0.0589  0.0330  0.1072  99  ASN   B O   
5470 C CB  . ASN   B 99  ? 0.2988 0.2392 0.2299 0.0510  0.0063  0.0394  99  ASN   B CB  
5471 C CG  . ASN   B 99  ? 0.3077 0.2465 0.2375 0.0467  0.0099  0.0337  99  ASN   B CG  
5472 O OD1 . ASN   B 99  ? 0.3166 0.2402 0.2663 0.0454  0.0166  0.0616  99  ASN   B OD1 
5473 N ND2 . ASN   B 99  ? 0.3051 0.2508 0.2494 0.0432  -0.0058 0.0344  99  ASN   B ND2 
5480 N N   A VAL   B 100 ? 0.3485 0.3041 0.2994 0.0402  0.0432  0.1241  100 VAL   B N   
5481 N N   B VAL   B 100 ? 0.3470 0.3024 0.2991 0.0385  0.0432  0.1253  100 VAL   B N   
5482 C CA  A VAL   B 100 ? 0.3780 0.3284 0.3441 0.0288  0.0509  0.1297  100 VAL   B CA  
5483 C CA  B VAL   B 100 ? 0.3771 0.3273 0.3470 0.0250  0.0510  0.1288  100 VAL   B CA  
5484 C C   A VAL   B 100 ? 0.3933 0.3393 0.3431 0.0385  0.0567  0.1409  100 VAL   B C   
5485 C C   B VAL   B 100 ? 0.3926 0.3375 0.3428 0.0354  0.0567  0.1377  100 VAL   B C   
5486 O O   A VAL   B 100 ? 0.4016 0.3491 0.3578 0.0347  0.0632  0.1467  100 VAL   B O   
5487 O O   B VAL   B 100 ? 0.4007 0.3452 0.3521 0.0302  0.0624  0.1379  100 VAL   B O   
5488 C CB  A VAL   B 100 ? 0.3906 0.3403 0.4044 0.0063  0.0522  0.1370  100 VAL   B CB  
5489 C CB  B VAL   B 100 ? 0.3899 0.3403 0.4158 -0.0004 0.0520  0.1383  100 VAL   B CB  
5490 C CG1 A VAL   B 100 ? 0.3978 0.3459 0.4319 0.0032  0.0507  0.1315  100 VAL   B CG1 
5491 C CG1 B VAL   B 100 ? 0.3980 0.3471 0.4495 -0.0033 0.0509  0.1315  100 VAL   B CG1 
5492 C CG2 A VAL   B 100 ? 0.3921 0.3454 0.4215 -0.0048 0.0572  0.1382  100 VAL   B CG2 
5493 C CG2 B VAL   B 100 ? 0.3907 0.3450 0.4331 -0.0131 0.0575  0.1421  100 VAL   B CG2 
5512 N N   . ASN   B 101 ? 0.3999 0.3390 0.3224 0.0546  0.0555  0.1416  101 ASN   B N   
5513 C CA  . ASN   B 101 ? 0.4399 0.3538 0.3254 0.0736  0.0376  0.1492  101 ASN   B CA  
5514 C C   . ASN   B 101 ? 0.4942 0.3947 0.3490 0.0752  0.0197  0.1435  101 ASN   B C   
5515 O O   . ASN   B 101 ? 0.5062 0.4036 0.3857 0.0894  0.0284  0.1104  101 ASN   B O   
5516 C CB  . ASN   B 101 ? 0.4348 0.3354 0.3573 0.0810  0.0543  0.1301  101 ASN   B CB  
5517 C CG  . ASN   B 101 ? 0.4278 0.3262 0.3752 0.0865  0.0602  0.1244  101 ASN   B CG  
5518 O OD1 . ASN   B 101 ? 0.4404 0.3176 0.4156 0.0760  0.0813  0.1169  101 ASN   B OD1 
5519 N ND2 . ASN   B 101 ? 0.4135 0.3209 0.3687 0.0951  0.0633  0.1072  101 ASN   B ND2 
5527 N N   . LYS   B 102 ? 0.5278 0.4260 0.3600 0.0604  0.0077  0.1397  102 LYS   B N   
5528 C CA  . LYS   B 102 ? 0.5611 0.4572 0.3619 0.0416  0.0002  0.1287  102 LYS   B CA  
5529 C C   . LYS   B 102 ? 0.5495 0.4503 0.3461 0.0462  0.0078  0.1278  102 LYS   B C   
5530 O O   . LYS   B 102 ? 0.5614 0.4621 0.3624 0.0460  -0.0074 0.1130  102 LYS   B O   
5531 C CB  . LYS   B 102 ? 0.6025 0.5020 0.4293 0.0241  0.0035  0.0873  102 LYS   B CB  
5532 C CG  . LYS   B 102 ? 0.6392 0.5479 0.5045 0.0138  0.0097  0.0434  102 LYS   B CG  
5533 C CD  . LYS   B 102 ? 0.6744 0.5797 0.5762 0.0045  0.0185  0.0145  102 LYS   B CD  
5534 C CE  . LYS   B 102 ? 0.6954 0.5998 0.6351 -0.0020 0.0264  -0.0050 102 LYS   B CE  
5535 N NZ  . LYS   B 102 ? 0.7012 0.6138 0.6673 -0.0043 0.0265  -0.0162 102 LYS   B NZ  
5549 N N   . GLY   B 103 ? 0.5218 0.4339 0.3464 0.0422  0.0365  0.1220  103 GLY   B N   
5550 C CA  . GLY   B 103 ? 0.4962 0.4177 0.3712 0.0435  0.0650  0.0978  103 GLY   B CA  
5551 C C   . GLY   B 103 ? 0.4633 0.3920 0.3684 0.0357  0.0850  0.0888  103 GLY   B C   
5552 O O   . GLY   B 103 ? 0.4686 0.4039 0.3939 0.0367  0.0887  0.0664  103 GLY   B O   
5556 N N   A GLU   B 104 ? 0.4446 0.3769 0.3579 0.0316  0.0891  0.0767  104 GLU   B N   
5557 N N   B GLU   B 104 ? 0.4351 0.3610 0.3480 0.0245  0.0948  0.0829  104 GLU   B N   
5558 C CA  A GLU   B 104 ? 0.4232 0.3696 0.3401 0.0402  0.0851  0.0518  104 GLU   B CA  
5559 C CA  B GLU   B 104 ? 0.4041 0.3379 0.3204 0.0295  0.0922  0.0595  104 GLU   B CA  
5560 C C   A GLU   B 104 ? 0.4244 0.3722 0.3587 0.0281  0.1097  0.0436  104 GLU   B C   
5561 C C   B GLU   B 104 ? 0.4050 0.3382 0.3356 0.0167  0.1192  0.0573  104 GLU   B C   
5562 O O   A GLU   B 104 ? 0.4198 0.3726 0.3763 0.0331  0.1106  0.0395  104 GLU   B O   
5563 O O   B GLU   B 104 ? 0.4010 0.3368 0.3689 0.0251  0.1173  0.0472  104 GLU   B O   
5564 C CB  A GLU   B 104 ? 0.4091 0.3582 0.3294 0.0539  0.0494  0.0267  104 GLU   B CB  
5565 C CB  B GLU   B 104 ? 0.3836 0.3152 0.3076 0.0386  0.0480  0.0272  104 GLU   B CB  
5566 C CG  A GLU   B 104 ? 0.3983 0.3527 0.3175 0.0636  0.0144  -0.0012 104 GLU   B CG  
5567 C CG  B GLU   B 104 ? 0.3690 0.3021 0.2894 0.0431  0.0037  -0.0070 104 GLU   B CG  
5568 C CD  A GLU   B 104 ? 0.3922 0.3484 0.2985 0.0680  -0.0153 -0.0136 104 GLU   B CD  
5569 C CD  B GLU   B 104 ? 0.3614 0.2886 0.2586 0.0407  -0.0299 -0.0182 104 GLU   B CD  
5570 O OE1 A GLU   B 104 ? 0.3793 0.3426 0.2699 0.0778  -0.0040 -0.0221 104 GLU   B OE1 
5571 O OE1 B GLU   B 104 ? 0.3433 0.2803 0.2335 0.0486  -0.0119 -0.0301 104 GLU   B OE1 
5572 O OE2 A GLU   B 104 ? 0.3970 0.3539 0.3078 0.0620  -0.0482 -0.0218 104 GLU   B OE2 
5573 O OE2 B GLU   B 104 ? 0.3666 0.2873 0.2495 0.0279  -0.0774 -0.0258 104 GLU   B OE2 
5586 N N   A ASP   B 105 ? 0.4218 0.3767 0.3619 0.0158  0.1338  0.0390  105 ASP   B N   
5587 N N   B ASP   B 105 ? 0.3982 0.3402 0.3191 -0.0009 0.1487  0.0648  105 ASP   B N   
5588 C CA  A ASP   B 105 ? 0.4320 0.3851 0.3858 0.0075  0.1476  0.0258  105 ASP   B CA  
5589 C CA  B ASP   B 105 ? 0.4102 0.3486 0.3322 -0.0084 0.1646  0.0541  105 ASP   B CA  
5590 C C   A ASP   B 105 ? 0.4196 0.3606 0.3667 -0.0005 0.1520  0.0185  105 ASP   B C   
5591 C C   B ASP   B 105 ? 0.3973 0.3241 0.3235 -0.0174 0.1656  0.0435  105 ASP   B C   
5592 O O   A ASP   B 105 ? 0.4149 0.3550 0.3729 0.0068  0.1563  0.0170  105 ASP   B O   
5593 O O   B ASP   B 105 ? 0.3894 0.3169 0.3350 -0.0111 0.1616  0.0422  105 ASP   B O   
5594 C CB  A ASP   B 105 ? 0.4456 0.4086 0.4279 0.0089  0.1571  0.0132  105 ASP   B CB  
5595 C CB  B ASP   B 105 ? 0.4229 0.3718 0.3544 -0.0059 0.1791  0.0446  105 ASP   B CB  
5596 C CG  A ASP   B 105 ? 0.4575 0.4265 0.4785 0.0065  0.1648  0.0057  105 ASP   B CG  
5597 C CG  B ASP   B 105 ? 0.4341 0.3880 0.3724 -0.0087 0.1954  0.0434  105 ASP   B CG  
5598 O OD1 A ASP   B 105 ? 0.4598 0.4349 0.4910 0.0012  0.1672  0.0067  105 ASP   B OD1 
5599 O OD1 B ASP   B 105 ? 0.4338 0.3948 0.3942 -0.0177 0.1948  0.0347  105 ASP   B OD1 
5600 O OD2 A ASP   B 105 ? 0.4620 0.4324 0.5115 0.0089  0.1621  0.0014  105 ASP   B OD2 
5601 O OD2 B ASP   B 105 ? 0.4345 0.3933 0.3794 -0.0074 0.2031  0.0519  105 ASP   B OD2 
5610 N N   A ILE   B 106 ? 0.4139 0.3397 0.3651 -0.0038 0.1349  0.0180  106 ILE   B N   
5611 N N   B ILE   B 106 ? 0.3954 0.3064 0.3307 -0.0155 0.1424  0.0358  106 ILE   B N   
5612 C CA  A ILE   B 106 ? 0.3950 0.3161 0.3612 -0.0175 0.1331  0.0200  106 ILE   B CA  
5613 C CA  B ILE   B 106 ? 0.3760 0.2850 0.3321 -0.0291 0.1458  0.0322  106 ILE   B CA  
5614 C C   A ILE   B 106 ? 0.3668 0.3030 0.3456 -0.0204 0.1208  0.0100  106 ILE   B C   
5615 C C   B ILE   B 106 ? 0.3449 0.2785 0.3120 -0.0287 0.1382  0.0152  106 ILE   B C   
5616 O O   A ILE   B 106 ? 0.3596 0.2895 0.3375 -0.0245 0.1122  0.0075  106 ILE   B O   
5617 O O   B ILE   B 106 ? 0.3347 0.2633 0.2942 -0.0324 0.1192  0.0063  106 ILE   B O   
5618 C CB  A ILE   B 106 ? 0.4107 0.3087 0.3899 -0.0229 0.1282  0.0256  106 ILE   B CB  
5619 C CB  B ILE   B 106 ? 0.3983 0.2789 0.3728 -0.0359 0.1346  0.0358  106 ILE   B CB  
5620 C CG1 A ILE   B 106 ? 0.4144 0.3020 0.3945 -0.0210 0.1257  0.0223  106 ILE   B CG1 
5621 C CG1 B ILE   B 106 ? 0.4055 0.2753 0.3870 -0.0289 0.1254  0.0276  106 ILE   B CG1 
5622 C CG2 A ILE   B 106 ? 0.4168 0.3144 0.4078 -0.0258 0.1291  0.0246  106 ILE   B CG2 
5623 C CG2 B ILE   B 106 ? 0.4062 0.2876 0.3951 -0.0412 0.1340  0.0334  106 ILE   B CG2 
5624 C CD1 A ILE   B 106 ? 0.4177 0.2951 0.3935 -0.0182 0.1245  0.0232  106 ILE   B CD1 
5625 C CD1 B ILE   B 106 ? 0.4108 0.2695 0.3913 -0.0237 0.1222  0.0294  106 ILE   B CD1 
5648 N N   A GLN   B 107 ? 0.3484 0.3160 0.3680 -0.0221 0.1107  0.0112  107 GLN   B N   
5649 N N   B GLN   B 107 ? 0.3300 0.3021 0.3464 -0.0267 0.1348  0.0156  107 GLN   B N   
5650 C CA  A GLN   B 107 ? 0.3305 0.3215 0.3852 -0.0136 0.0937  0.0162  107 GLN   B CA  
5651 C CA  B GLN   B 107 ? 0.3152 0.3151 0.3735 -0.0147 0.1177  0.0228  107 GLN   B CA  
5652 C C   A GLN   B 107 ? 0.2995 0.2976 0.3529 0.0017  0.0667  0.0096  107 GLN   B C   
5653 C C   B GLN   B 107 ? 0.2905 0.2972 0.3502 0.0028  0.0777  0.0127  107 GLN   B C   
5654 O O   A GLN   B 107 ? 0.2907 0.3023 0.3644 0.0045  0.0328  -0.0135 107 GLN   B O   
5655 O O   B GLN   B 107 ? 0.2773 0.3065 0.3680 0.0109  0.0438  -0.0130 107 GLN   B O   
5656 C CB  A GLN   B 107 ? 0.3551 0.3599 0.4532 -0.0156 0.0868  0.0189  107 GLN   B CB  
5657 C CB  B GLN   B 107 ? 0.3426 0.3590 0.4461 -0.0131 0.1138  0.0247  107 GLN   B CB  
5658 C CG  A GLN   B 107 ? 0.3831 0.3911 0.5242 -0.0101 0.0657  0.0235  107 GLN   B CG  
5659 C CG  B GLN   B 107 ? 0.3777 0.3998 0.5253 -0.0036 0.0896  0.0274  107 GLN   B CG  
5660 C CD  A GLN   B 107 ? 0.4042 0.4168 0.5823 -0.0115 0.0478  0.0300  107 GLN   B CD  
5661 C CD  B GLN   B 107 ? 0.4033 0.4288 0.5861 -0.0024 0.0716  0.0344  107 GLN   B CD  
5662 O OE1 A GLN   B 107 ? 0.4119 0.4310 0.6062 -0.0109 0.0516  0.0225  107 GLN   B OE1 
5663 O OE1 B GLN   B 107 ? 0.4130 0.4428 0.6067 -0.0025 0.0763  0.0299  107 GLN   B OE1 
5664 N NE2 A GLN   B 107 ? 0.4144 0.4226 0.6044 -0.0070 0.0346  0.0422  107 GLN   B NE2 
5665 N NE2 B GLN   B 107 ? 0.4134 0.4382 0.6098 0.0047  0.0621  0.0445  107 GLN   B NE2 
5682 N N   . LEU   B 108 ? 0.2726 0.2733 0.3148 0.0179  0.0786  0.0228  108 LEU   B N   
5683 C CA  . LEU   B 108 ? 0.2625 0.2619 0.2685 0.0174  0.0522  0.0366  108 LEU   B CA  
5684 C C   . LEU   B 108 ? 0.2194 0.2314 0.2620 0.0137  0.0310  0.0437  108 LEU   B C   
5685 O O   . LEU   B 108 ? 0.2235 0.2146 0.2409 0.0145  0.0153  0.0407  108 LEU   B O   
5686 C CB  . LEU   B 108 ? 0.2682 0.2764 0.2586 -0.0013 0.0540  0.0609  108 LEU   B CB  
5687 C CG  . LEU   B 108 ? 0.3026 0.3224 0.2649 0.0010  0.0588  0.0272  108 LEU   B CG  
5688 C CD1 . LEU   B 108 ? 0.2987 0.3362 0.2318 -0.0116 0.0711  0.0203  108 LEU   B CD1 
5689 C CD2 . LEU   B 108 ? 0.3308 0.3476 0.2879 0.0131  0.0395  0.0034  108 LEU   B CD2 
5702 N N   . LEU   B 109 ? 0.2057 0.2145 0.2742 0.0166  0.0262  0.0357  109 LEU   B N   
5703 C CA  . LEU   B 109 ? 0.1977 0.1824 0.2614 0.0040  0.0197  0.0439  109 LEU   B CA  
5704 C C   . LEU   B 109 ? 0.1912 0.1669 0.2618 -0.0090 0.0211  0.0207  109 LEU   B C   
5705 O O   . LEU   B 109 ? 0.1850 0.1598 0.2715 0.0075  0.0208  0.0423  109 LEU   B O   
5706 C CB  . LEU   B 109 ? 0.2129 0.1766 0.2953 0.0089  0.0116  0.0400  109 LEU   B CB  
5707 C CG  . LEU   B 109 ? 0.1994 0.1668 0.2771 -0.0021 0.0178  0.0370  109 LEU   B CG  
5708 C CD1 . LEU   B 109 ? 0.1905 0.2012 0.2557 -0.0095 0.0278  0.0283  109 LEU   B CD1 
5709 C CD2 . LEU   B 109 ? 0.2180 0.1543 0.3018 -0.0079 0.0217  0.0382  109 LEU   B CD2 
5721 N N   . LYS   B 110 ? 0.1862 0.1617 0.2571 -0.0115 0.0143  0.0377  110 LYS   B N   
5722 C CA  . LYS   B 110 ? 0.1876 0.1555 0.2777 -0.0086 -0.0001 0.0398  110 LYS   B CA  
5723 C C   . LYS   B 110 ? 0.1743 0.1455 0.2588 -0.0128 -0.0062 0.0298  110 LYS   B C   
5724 O O   . LYS   B 110 ? 0.1739 0.1625 0.2410 -0.0159 -0.0027 0.0249  110 LYS   B O   
5725 C CB  . LYS   B 110 ? 0.1861 0.1673 0.3140 -0.0120 0.0117  0.0167  110 LYS   B CB  
5726 C CG  . LYS   B 110 ? 0.1850 0.1665 0.3395 -0.0090 -0.0258 0.0159  110 LYS   B CG  
5727 C CD  . LYS   B 110 ? 0.1839 0.1595 0.3334 -0.0152 -0.0066 0.0450  110 LYS   B CD  
5728 C CE  . LYS   B 110 ? 0.1722 0.1900 0.3653 -0.0050 -0.0113 0.0120  110 LYS   B CE  
5729 N NZ  . LYS   B 110 ? 0.1808 0.1974 0.3368 -0.0098 -0.0225 0.0306  110 LYS   B NZ  
5743 N N   . SER   B 111 ? 0.1858 0.1706 0.2843 -0.0088 0.0170  0.0136  111 SER   B N   
5744 C CA  . SER   B 111 ? 0.1939 0.1736 0.2470 0.0039  0.0250  0.0174  111 SER   B CA  
5745 C C   . SER   B 111 ? 0.1857 0.1578 0.2348 -0.0079 0.0069  0.0122  111 SER   B C   
5746 O O   . SER   B 111 ? 0.1767 0.1663 0.2652 -0.0131 -0.0170 0.0033  111 SER   B O   
5747 C CB  . SER   B 111 ? 0.1946 0.1959 0.2592 -0.0052 0.0214  0.0330  111 SER   B CB  
5748 O OG  . SER   B 111 ? 0.2191 0.2142 0.2942 -0.0049 0.0318  0.0363  111 SER   B OG  
5754 N N   . ALA   B 112 ? 0.1844 0.1597 0.2357 -0.0041 0.0086  0.0139  112 ALA   B N   
5755 C CA  . ALA   B 112 ? 0.1790 0.1673 0.2186 -0.0040 -0.0159 0.0096  112 ALA   B CA  
5756 C C   . ALA   B 112 ? 0.1667 0.1671 0.2206 0.0042  -0.0090 -0.0010 112 ALA   B C   
5757 O O   . ALA   B 112 ? 0.1571 0.1720 0.2415 -0.0125 -0.0025 -0.0085 112 ALA   B O   
5758 C CB  . ALA   B 112 ? 0.1871 0.1689 0.2278 -0.0022 -0.0232 0.0119  112 ALA   B CB  
5764 N N   . TYR   B 113 ? 0.1653 0.1573 0.2166 -0.0041 -0.0047 -0.0071 113 TYR   B N   
5765 C CA  . TYR   B 113 ? 0.1691 0.1575 0.2034 -0.0055 0.0025  -0.0138 113 TYR   B CA  
5766 C C   . TYR   B 113 ? 0.1638 0.1661 0.2016 -0.0156 0.0005  -0.0066 113 TYR   B C   
5767 O O   . TYR   B 113 ? 0.1685 0.1681 0.2058 -0.0138 -0.0081 -0.0027 113 TYR   B O   
5768 C CB  . TYR   B 113 ? 0.1718 0.1489 0.2162 -0.0030 0.0181  -0.0052 113 TYR   B CB  
5769 C CG  . TYR   B 113 ? 0.1781 0.1604 0.2306 -0.0072 -0.0002 -0.0054 113 TYR   B CG  
5770 C CD1 . TYR   B 113 ? 0.1736 0.1517 0.2359 -0.0072 0.0048  0.0073  113 TYR   B CD1 
5771 C CD2 . TYR   B 113 ? 0.1745 0.1616 0.2583 -0.0143 -0.0075 0.0176  113 TYR   B CD2 
5772 C CE1 . TYR   B 113 ? 0.1880 0.1614 0.2510 -0.0077 0.0127  -0.0004 113 TYR   B CE1 
5773 C CE2 . TYR   B 113 ? 0.1774 0.1493 0.2677 -0.0023 -0.0062 0.0307  113 TYR   B CE2 
5774 C CZ  . TYR   B 113 ? 0.1726 0.1457 0.2475 -0.0010 -0.0007 0.0088  113 TYR   B CZ  
5775 O OH  . TYR   B 113 ? 0.1859 0.1476 0.2891 0.0137  0.0089  0.0173  113 TYR   B OH  
5785 N N   . GLU   B 114 ? 0.1734 0.1494 0.2122 -0.0081 -0.0104 0.0079  114 GLU   B N   
5786 C CA  . GLU   B 114 ? 0.1570 0.1470 0.2217 0.0095  -0.0133 0.0024  114 GLU   B CA  
5787 C C   . GLU   B 114 ? 0.1599 0.1550 0.2210 0.0031  -0.0163 0.0070  114 GLU   B C   
5788 O O   . GLU   B 114 ? 0.1688 0.1514 0.2472 0.0093  -0.0309 0.0099  114 GLU   B O   
5789 C CB  . GLU   B 114 ? 0.1572 0.1686 0.2495 -0.0055 -0.0083 -0.0082 114 GLU   B CB  
5790 C CG  . GLU   B 114 ? 0.1666 0.1600 0.2557 -0.0092 -0.0116 0.0054  114 GLU   B CG  
5791 C CD  . GLU   B 114 ? 0.1712 0.1581 0.2545 -0.0222 -0.0147 0.0040  114 GLU   B CD  
5792 O OE1 . GLU   B 114 ? 0.1575 0.1621 0.2449 -0.0125 -0.0102 0.0085  114 GLU   B OE1 
5793 O OE2 . GLU   B 114 ? 0.1706 0.1831 0.2508 -0.0319 -0.0196 0.0109  114 GLU   B OE2 
5800 N N   . ASN   B 115 ? 0.1633 0.1586 0.1883 0.0028  -0.0156 0.0078  115 ASN   B N   
5801 C CA  . ASN   B 115 ? 0.1629 0.1657 0.1758 -0.0114 -0.0082 0.0011  115 ASN   B CA  
5802 C C   . ASN   B 115 ? 0.1662 0.1753 0.1709 -0.0162 -0.0152 0.0016  115 ASN   B C   
5803 O O   . ASN   B 115 ? 0.1779 0.1614 0.1972 -0.0241 -0.0086 0.0110  115 ASN   B O   
5804 C CB  . ASN   B 115 ? 0.1741 0.1813 0.1968 -0.0180 -0.0282 0.0193  115 ASN   B CB  
5805 C CG  . ASN   B 115 ? 0.1866 0.1930 0.1776 -0.0028 -0.0268 0.0151  115 ASN   B CG  
5806 O OD1 . ASN   B 115 ? 0.2297 0.2025 0.2091 -0.0040 0.0037  0.0026  115 ASN   B OD1 
5807 N ND2 . ASN   B 115 ? 0.1920 0.2027 0.1943 -0.0141 -0.0023 0.0089  115 ASN   B ND2 
5814 N N   . PHE   B 116 ? 0.1653 0.1627 0.1854 0.0007  -0.0204 -0.0238 116 PHE   B N   
5815 C CA  . PHE   B 116 ? 0.1664 0.1533 0.2026 -0.0046 -0.0230 -0.0060 116 PHE   B CA  
5816 C C   . PHE   B 116 ? 0.1739 0.1379 0.1999 -0.0262 -0.0254 0.0079  116 PHE   B C   
5817 O O   . PHE   B 116 ? 0.1693 0.1558 0.1980 -0.0118 -0.0218 0.0043  116 PHE   B O   
5818 C CB  . PHE   B 116 ? 0.1723 0.1454 0.1933 0.0003  -0.0338 0.0027  116 PHE   B CB  
5819 C CG  . PHE   B 116 ? 0.1608 0.1561 0.1988 -0.0047 -0.0251 0.0130  116 PHE   B CG  
5820 C CD1 . PHE   B 116 ? 0.1605 0.1589 0.2112 -0.0022 -0.0170 0.0052  116 PHE   B CD1 
5821 C CD2 . PHE   B 116 ? 0.1518 0.1637 0.1830 -0.0009 -0.0226 -0.0014 116 PHE   B CD2 
5822 C CE1 . PHE   B 116 ? 0.1670 0.1615 0.2185 -0.0104 -0.0296 0.0008  116 PHE   B CE1 
5823 C CE2 . PHE   B 116 ? 0.1515 0.1670 0.2165 -0.0194 -0.0157 0.0185  116 PHE   B CE2 
5824 C CZ  . PHE   B 116 ? 0.1365 0.1719 0.2244 -0.0067 -0.0400 0.0060  116 PHE   B CZ  
5834 N N   . ASN   B 117 ? 0.1694 0.1527 0.1857 -0.0185 -0.0256 0.0183  117 ASN   B N   
5835 C CA  . ASN   B 117 ? 0.1830 0.1529 0.1942 -0.0116 -0.0230 0.0096  117 ASN   B CA  
5836 C C   . ASN   B 117 ? 0.1847 0.1445 0.2261 -0.0120 -0.0221 0.0000  117 ASN   B C   
5837 O O   . ASN   B 117 ? 0.1883 0.1625 0.2584 -0.0138 -0.0517 0.0140  117 ASN   B O   
5838 C CB  . ASN   B 117 ? 0.1901 0.1604 0.2055 -0.0274 -0.0213 -0.0032 117 ASN   B CB  
5839 C CG  . ASN   B 117 ? 0.1813 0.1523 0.2092 -0.0003 -0.0344 0.0025  117 ASN   B CG  
5840 O OD1 . ASN   B 117 ? 0.1970 0.1426 0.2405 -0.0070 -0.0264 -0.0081 117 ASN   B OD1 
5841 N ND2 . ASN   B 117 ? 0.1734 0.1516 0.2114 -0.0135 -0.0162 0.0063  117 ASN   B ND2 
5848 N N   . GLN   B 118 ? 0.1691 0.1447 0.2287 -0.0090 -0.0252 -0.0132 118 GLN   B N   
5849 C CA  . GLN   B 118 ? 0.1922 0.1446 0.2124 -0.0035 -0.0266 -0.0007 118 GLN   B CA  
5850 C C   . GLN   B 118 ? 0.1771 0.1538 0.2495 0.0063  -0.0313 0.0200  118 GLN   B C   
5851 O O   . GLN   B 118 ? 0.2085 0.1515 0.2700 -0.0034 -0.0164 0.0103  118 GLN   B O   
5852 C CB  . GLN   B 118 ? 0.1988 0.1478 0.2155 0.0071  -0.0212 -0.0056 118 GLN   B CB  
5853 C CG  . GLN   B 118 ? 0.2038 0.1490 0.2408 0.0065  -0.0308 -0.0059 118 GLN   B CG  
5854 C CD  . GLN   B 118 ? 0.2050 0.1486 0.2454 -0.0023 -0.0369 -0.0261 118 GLN   B CD  
5855 O OE1 . GLN   B 118 ? 0.2019 0.1597 0.2743 0.0120  -0.0015 0.0013  118 GLN   B OE1 
5856 N NE2 . GLN   B 118 ? 0.2181 0.1367 0.2407 -0.0086 -0.0345 0.0005  118 GLN   B NE2 
5865 N N   . HIS   B 119 ? 0.1815 0.1595 0.2216 -0.0032 -0.0294 0.0060  119 HIS   B N   
5866 C CA  . HIS   B 119 ? 0.1958 0.1591 0.1824 -0.0031 -0.0457 0.0119  119 HIS   B CA  
5867 C C   . HIS   B 119 ? 0.2059 0.1677 0.2070 -0.0075 -0.0516 0.0092  119 HIS   B C   
5868 O O   . HIS   B 119 ? 0.2055 0.1668 0.2293 -0.0347 -0.0373 0.0070  119 HIS   B O   
5869 C CB  . HIS   B 119 ? 0.2012 0.1793 0.2047 -0.0134 -0.0391 0.0035  119 HIS   B CB  
5870 C CG  . HIS   B 119 ? 0.2030 0.1910 0.2199 0.0016  -0.0650 -0.0086 119 HIS   B CG  
5871 N ND1 . HIS   B 119 ? 0.2157 0.2027 0.2523 -0.0056 -0.0563 -0.0330 119 HIS   B ND1 
5872 C CD2 . HIS   B 119 ? 0.2054 0.2112 0.2601 0.0340  -0.0722 -0.0165 119 HIS   B CD2 
5873 C CE1 . HIS   B 119 ? 0.2392 0.2151 0.2741 0.0030  -0.0777 -0.0438 119 HIS   B CE1 
5874 N NE2 . HIS   B 119 ? 0.2345 0.2348 0.2730 0.0237  -0.0722 -0.0291 119 HIS   B NE2 
5882 N N   A GLU   B 120 ? 0.2272 0.1780 0.2052 -0.0132 -0.0511 0.0187  120 GLU   B N   
5883 N N   B GLU   B 120 ? 0.2286 0.1707 0.1993 -0.0142 -0.0550 0.0215  120 GLU   B N   
5884 C CA  A GLU   B 120 ? 0.2421 0.1969 0.2135 -0.0099 -0.0538 0.0263  120 GLU   B CA  
5885 C CA  B GLU   B 120 ? 0.2436 0.1874 0.2027 -0.0096 -0.0616 0.0300  120 GLU   B CA  
5886 C C   A GLU   B 120 ? 0.2177 0.1907 0.2010 -0.0116 -0.0482 0.0136  120 GLU   B C   
5887 C C   B GLU   B 120 ? 0.2180 0.1854 0.1987 -0.0139 -0.0533 0.0167  120 GLU   B C   
5888 O O   A GLU   B 120 ? 0.2130 0.1871 0.2019 -0.0103 -0.0433 0.0148  120 GLU   B O   
5889 O O   B GLU   B 120 ? 0.2143 0.1774 0.2021 -0.0192 -0.0463 0.0241  120 GLU   B O   
5890 C CB  A GLU   B 120 ? 0.2987 0.2251 0.2790 0.0119  -0.0795 0.0385  120 GLU   B CB  
5891 C CB  B GLU   B 120 ? 0.3041 0.2111 0.2632 0.0175  -0.0966 0.0442  120 GLU   B CB  
5892 C CG  A GLU   B 120 ? 0.3467 0.2854 0.3524 0.0203  -0.0844 0.0418  120 GLU   B CG  
5893 C CG  B GLU   B 120 ? 0.3582 0.2775 0.3375 0.0309  -0.1061 0.0461  120 GLU   B CG  
5894 C CD  A GLU   B 120 ? 0.3847 0.3470 0.4393 0.0164  -0.0802 0.0481  120 GLU   B CD  
5895 C CD  B GLU   B 120 ? 0.3991 0.3492 0.4264 0.0282  -0.1041 0.0514  120 GLU   B CD  
5896 O OE1 A GLU   B 120 ? 0.4036 0.3690 0.4727 0.0050  -0.0741 0.0643  120 GLU   B OE1 
5897 O OE1 B GLU   B 120 ? 0.4175 0.3751 0.4606 0.0123  -0.0936 0.0684  120 GLU   B OE1 
5898 O OE2 A GLU   B 120 ? 0.4080 0.3723 0.4914 0.0186  -0.0780 0.0359  120 GLU   B OE2 
5899 O OE2 B GLU   B 120 ? 0.4271 0.3791 0.4875 0.0271  -0.1029 0.0356  120 GLU   B OE2 
5912 N N   . VAL   B 121 ? 0.2048 0.1799 0.2020 -0.0186 -0.0354 0.0107  121 VAL   B N   
5913 C CA  . VAL   B 121 ? 0.1979 0.1940 0.1746 -0.0053 -0.0300 0.0132  121 VAL   B CA  
5914 C C   . VAL   B 121 ? 0.1883 0.1900 0.1935 -0.0190 -0.0386 0.0358  121 VAL   B C   
5915 O O   . VAL   B 121 ? 0.1979 0.1667 0.2209 -0.0256 -0.0383 0.0106  121 VAL   B O   
5916 C CB  . VAL   B 121 ? 0.2007 0.2231 0.2075 -0.0031 -0.0215 0.0146  121 VAL   B CB  
5917 C CG1 . VAL   B 121 ? 0.2119 0.2462 0.2571 -0.0198 -0.0038 0.0073  121 VAL   B CG1 
5918 C CG2 . VAL   B 121 ? 0.2330 0.2521 0.2176 0.0073  -0.0106 -0.0074 121 VAL   B CG2 
5929 N N   . LEU   B 122 ? 0.1867 0.1840 0.1971 -0.0093 -0.0369 0.0260  122 LEU   B N   
5930 C CA  . LEU   B 122 ? 0.1775 0.1880 0.1707 -0.0197 -0.0381 0.0254  122 LEU   B CA  
5931 C C   . LEU   B 122 ? 0.1831 0.1727 0.1672 -0.0322 -0.0326 0.0095  122 LEU   B C   
5932 O O   . LEU   B 122 ? 0.1890 0.1753 0.2017 -0.0306 -0.0429 -0.0045 122 LEU   B O   
5933 C CB  . LEU   B 122 ? 0.2081 0.1876 0.2333 -0.0009 -0.0498 0.0116  122 LEU   B CB  
5934 C CG  . LEU   B 122 ? 0.1900 0.2019 0.2280 -0.0177 -0.0327 -0.0124 122 LEU   B CG  
5935 C CD1 . LEU   B 122 ? 0.2010 0.2240 0.2294 -0.0193 -0.0289 -0.0146 122 LEU   B CD1 
5936 C CD2 . LEU   B 122 ? 0.1855 0.2060 0.1957 -0.0000 -0.0274 -0.0137 122 LEU   B CD2 
5948 N N   . LEU   B 123 ? 0.1943 0.1489 0.1655 -0.0314 -0.0369 0.0110  123 LEU   B N   
5949 C CA  . LEU   B 123 ? 0.1960 0.1465 0.1793 -0.0274 -0.0336 0.0213  123 LEU   B CA  
5950 C C   . LEU   B 123 ? 0.1880 0.1476 0.1688 -0.0170 -0.0249 0.0129  123 LEU   B C   
5951 O O   . LEU   B 123 ? 0.1990 0.1591 0.1670 -0.0285 -0.0245 -0.0074 123 LEU   B O   
5952 C CB  . LEU   B 123 ? 0.1964 0.1532 0.1945 -0.0286 -0.0330 0.0175  123 LEU   B CB  
5953 C CG  . LEU   B 123 ? 0.1932 0.1666 0.2031 -0.0195 -0.0216 0.0123  123 LEU   B CG  
5954 C CD1 . LEU   B 123 ? 0.1983 0.1804 0.1956 -0.0186 -0.0230 -0.0077 123 LEU   B CD1 
5955 C CD2 . LEU   B 123 ? 0.1943 0.1770 0.2300 -0.0220 0.0023  0.0057  123 LEU   B CD2 
5967 N N   . ALA   B 124 ? 0.1898 0.1566 0.1645 -0.0207 -0.0152 0.0059  124 ALA   B N   
5968 C CA  . ALA   B 124 ? 0.1789 0.1622 0.1932 -0.0179 -0.0308 0.0023  124 ALA   B CA  
5969 C C   . ALA   B 124 ? 0.1719 0.1616 0.1633 -0.0203 -0.0235 0.0010  124 ALA   B C   
5970 O O   . ALA   B 124 ? 0.1803 0.1656 0.1798 -0.0167 -0.0216 0.0038  124 ALA   B O   
5971 C CB  . ALA   B 124 ? 0.1835 0.1684 0.1899 0.0019  -0.0098 -0.0158 124 ALA   B CB  
5977 N N   . PRO   B 125 ? 0.1723 0.1544 0.1760 -0.0307 -0.0381 0.0110  125 PRO   B N   
5978 C CA  . PRO   B 125 ? 0.1872 0.1603 0.2117 -0.0296 -0.0385 0.0285  125 PRO   B CA  
5979 C C   . PRO   B 125 ? 0.1795 0.1498 0.2455 -0.0302 -0.0321 0.0265  125 PRO   B C   
5980 O O   . PRO   B 125 ? 0.1819 0.1594 0.2280 -0.0177 -0.0288 0.0291  125 PRO   B O   
5981 C CB  . PRO   B 125 ? 0.1840 0.1974 0.2082 -0.0365 -0.0378 0.0291  125 PRO   B CB  
5982 C CG  . PRO   B 125 ? 0.1994 0.1918 0.1891 -0.0471 -0.0336 0.0135  125 PRO   B CG  
5983 C CD  . PRO   B 125 ? 0.1737 0.1734 0.1599 -0.0421 -0.0309 0.0170  125 PRO   B CD  
5991 N N   . LEU   B 126 ? 0.1834 0.1448 0.2432 -0.0266 -0.0074 0.0186  126 LEU   B N   
5992 C CA  . LEU   B 126 ? 0.1902 0.1596 0.2544 -0.0235 -0.0143 0.0131  126 LEU   B CA  
5993 C C   . LEU   B 126 ? 0.1834 0.1660 0.2310 -0.0150 -0.0112 0.0225  126 LEU   B C   
5994 O O   . LEU   B 126 ? 0.1933 0.2134 0.2440 0.0154  -0.0241 0.0053  126 LEU   B O   
5995 C CB  . LEU   B 126 ? 0.2069 0.1627 0.2771 -0.0139 -0.0078 0.0080  126 LEU   B CB  
5996 C CG  . LEU   B 126 ? 0.2233 0.1619 0.2742 -0.0297 0.0085  -0.0146 126 LEU   B CG  
5997 C CD1 . LEU   B 126 ? 0.2402 0.1835 0.3205 -0.0307 0.0054  -0.0241 126 LEU   B CD1 
5998 C CD2 . LEU   B 126 ? 0.2173 0.1863 0.2785 -0.0304 -0.0011 -0.0240 126 LEU   B CD2 
6010 N N   . LEU   B 127 ? 0.1834 0.1556 0.2472 -0.0066 0.0017  0.0123  127 LEU   B N   
6011 C CA  . LEU   B 127 ? 0.1917 0.1558 0.2422 -0.0095 -0.0059 0.0297  127 LEU   B CA  
6012 C C   . LEU   B 127 ? 0.1782 0.1563 0.2602 -0.0084 -0.0078 0.0268  127 LEU   B C   
6013 O O   . LEU   B 127 ? 0.1780 0.1671 0.2709 -0.0165 -0.0093 0.0125  127 LEU   B O   
6014 C CB  . LEU   B 127 ? 0.2004 0.1525 0.2610 -0.0174 0.0060  0.0221  127 LEU   B CB  
6015 C CG  . LEU   B 127 ? 0.2152 0.1512 0.2452 -0.0104 0.0125  0.0194  127 LEU   B CG  
6016 C CD1 . LEU   B 127 ? 0.2202 0.1568 0.2775 0.0058  -0.0022 -0.0024 127 LEU   B CD1 
6017 C CD2 . LEU   B 127 ? 0.2273 0.1782 0.2525 -0.0301 0.0136  0.0246  127 LEU   B CD2 
6029 N N   . SER   B 128 ? 0.1728 0.1761 0.2460 0.0081  -0.0127 0.0253  128 SER   B N   
6030 C CA  . SER   B 128 ? 0.1879 0.1727 0.2529 0.0062  -0.0310 0.0276  128 SER   B CA  
6031 C C   . SER   B 128 ? 0.2028 0.1590 0.2671 -0.0068 -0.0338 0.0208  128 SER   B C   
6032 O O   . SER   B 128 ? 0.2201 0.1730 0.3326 0.0001  -0.0352 0.0437  128 SER   B O   
6033 C CB  . SER   B 128 ? 0.2018 0.1857 0.2583 0.0036  -0.0113 0.0414  128 SER   B CB  
6034 O OG  . SER   B 128 ? 0.2088 0.1916 0.2628 0.0022  -0.0004 0.0425  128 SER   B OG  
6040 N N   . ALA   B 129 ? 0.2178 0.1760 0.2955 0.0271  -0.0232 -0.0047 129 ALA   B N   
6041 C CA  . ALA   B 129 ? 0.2361 0.1987 0.3176 0.0251  -0.0149 -0.0170 129 ALA   B CA  
6042 C C   . ALA   B 129 ? 0.2186 0.1885 0.2935 0.0154  -0.0045 -0.0010 129 ALA   B C   
6043 O O   . ALA   B 129 ? 0.2026 0.1760 0.2988 0.0184  -0.0200 0.0214  129 ALA   B O   
6044 C CB  . ALA   B 129 ? 0.2613 0.2207 0.3544 0.0228  -0.0074 -0.0297 129 ALA   B CB  
6050 N N   . GLY   B 130 ? 0.2281 0.1892 0.2885 0.0178  -0.0099 -0.0021 130 GLY   B N   
6051 C CA  . GLY   B 130 ? 0.2222 0.1991 0.2903 0.0048  0.0106  0.0274  130 GLY   B CA  
6052 C C   . GLY   B 130 ? 0.2248 0.2035 0.2871 0.0105  -0.0041 0.0214  130 GLY   B C   
6053 O O   . GLY   B 130 ? 0.2373 0.2267 0.3287 0.0151  0.0032  0.0224  130 GLY   B O   
6057 N N   . ILE   B 131 ? 0.2224 0.2196 0.3046 0.0236  -0.0027 0.0045  131 ILE   B N   
6058 C CA  . ILE   B 131 ? 0.2484 0.2247 0.3002 0.0264  -0.0151 0.0289  131 ILE   B CA  
6059 C C   . ILE   B 131 ? 0.2563 0.2209 0.2578 0.0208  -0.0094 0.0369  131 ILE   B C   
6060 O O   . ILE   B 131 ? 0.2877 0.2381 0.2710 0.0269  -0.0311 0.0375  131 ILE   B O   
6061 C CB  . ILE   B 131 ? 0.2444 0.2498 0.3480 0.0166  -0.0234 0.0328  131 ILE   B CB  
6062 C CG1 . ILE   B 131 ? 0.2150 0.2661 0.3648 -0.0220 0.0011  0.0297  131 ILE   B CG1 
6063 C CG2 . ILE   B 131 ? 0.2663 0.2686 0.3743 0.0425  -0.0408 0.0251  131 ILE   B CG2 
6064 C CD1 . ILE   B 131 ? 0.2224 0.2944 0.3779 -0.0205 -0.0013 0.0356  131 ILE   B CD1 
6076 N N   . PHE   B 132 ? 0.2357 0.1982 0.2483 0.0246  -0.0022 0.0366  132 PHE   B N   
6077 C CA  . PHE   B 132 ? 0.2382 0.2101 0.2666 0.0234  0.0166  0.0185  132 PHE   B CA  
6078 C C   . PHE   B 132 ? 0.2588 0.2240 0.2927 0.0246  0.0224  0.0325  132 PHE   B C   
6079 O O   . PHE   B 132 ? 0.2716 0.2446 0.3309 0.0112  0.0463  0.0455  132 PHE   B O   
6080 C CB  . PHE   B 132 ? 0.2218 0.2157 0.2536 0.0092  0.0165  0.0183  132 PHE   B CB  
6081 C CG  . PHE   B 132 ? 0.2228 0.2211 0.2268 0.0059  0.0096  0.0137  132 PHE   B CG  
6082 C CD1 . PHE   B 132 ? 0.2391 0.2119 0.2915 -0.0074 0.0200  0.0118  132 PHE   B CD1 
6083 C CD2 . PHE   B 132 ? 0.2259 0.2052 0.1991 0.0092  0.0124  0.0317  132 PHE   B CD2 
6084 C CE1 . PHE   B 132 ? 0.2389 0.2122 0.3194 -0.0072 0.0226  0.0122  132 PHE   B CE1 
6085 C CE2 . PHE   B 132 ? 0.2365 0.2073 0.2385 0.0171  -0.0016 0.0436  132 PHE   B CE2 
6086 C CZ  . PHE   B 132 ? 0.2440 0.2122 0.2932 0.0044  -0.0045 0.0295  132 PHE   B CZ  
6096 N N   . GLY   B 133 ? 0.2574 0.2166 0.2878 0.0016  -0.0009 0.0565  133 GLY   B N   
6097 C CA  . GLY   B 133 ? 0.2564 0.2289 0.2901 -0.0192 -0.0030 0.0703  133 GLY   B CA  
6098 C C   . GLY   B 133 ? 0.2700 0.2277 0.2895 -0.0292 0.0109  0.0636  133 GLY   B C   
6099 O O   . GLY   B 133 ? 0.3049 0.2390 0.3523 -0.0521 0.0254  0.0688  133 GLY   B O   
6103 N N   . ALA   B 134 ? 0.2598 0.2254 0.2699 -0.0215 0.0032  0.0424  134 ALA   B N   
6104 C CA  . ALA   B 134 ? 0.2493 0.2297 0.2594 -0.0099 0.0239  0.0289  134 ALA   B CA  
6105 C C   . ALA   B 134 ? 0.2569 0.2107 0.2799 -0.0155 0.0249  0.0484  134 ALA   B C   
6106 O O   . ALA   B 134 ? 0.2633 0.2433 0.2906 -0.0013 0.0189  0.0474  134 ALA   B O   
6107 C CB  . ALA   B 134 ? 0.2429 0.2379 0.2436 -0.0054 0.0113  0.0045  134 ALA   B CB  
6113 N N   . ASP   B 135 ? 0.2742 0.2013 0.3059 -0.0154 0.0131  0.0422  135 ASP   B N   
6114 C CA  . ASP   B 135 ? 0.2897 0.1929 0.3285 -0.0086 0.0103  0.0458  135 ASP   B CA  
6115 C C   . ASP   B 135 ? 0.2610 0.1661 0.3187 -0.0049 -0.0043 0.0244  135 ASP   B C   
6116 O O   . ASP   B 135 ? 0.2431 0.1695 0.3306 0.0006  0.0002  0.0261  135 ASP   B O   
6117 C CB  . ASP   B 135 ? 0.3218 0.2103 0.3341 -0.0353 0.0148  0.0477  135 ASP   B CB  
6118 C CG  . ASP   B 135 ? 0.3556 0.2167 0.3823 -0.0597 0.0012  0.0474  135 ASP   B CG  
6119 O OD1 . ASP   B 135 ? 0.3727 0.2001 0.3830 -0.0468 -0.0250 0.0445  135 ASP   B OD1 
6120 O OD2 . ASP   B 135 ? 0.3814 0.2594 0.4226 -0.0752 -0.0032 0.0174  135 ASP   B OD2 
6125 N N   . PRO   B 136 ? 0.2603 0.1897 0.3349 0.0318  -0.0376 0.0278  136 PRO   B N   
6126 C CA  . PRO   B 136 ? 0.2429 0.1808 0.3257 0.0202  -0.0368 0.0080  136 PRO   B CA  
6127 C C   . PRO   B 136 ? 0.2218 0.1590 0.3133 0.0057  -0.0241 0.0084  136 PRO   B C   
6128 O O   . PRO   B 136 ? 0.2087 0.1627 0.3080 0.0102  -0.0148 0.0010  136 PRO   B O   
6129 C CB  . PRO   B 136 ? 0.2469 0.1912 0.3404 0.0381  -0.0327 -0.0055 136 PRO   B CB  
6130 C CG  . PRO   B 136 ? 0.2697 0.2115 0.3687 0.0338  -0.0184 -0.0014 136 PRO   B CG  
6131 C CD  . PRO   B 136 ? 0.2724 0.2069 0.3500 0.0527  -0.0154 0.0207  136 PRO   B CD  
6139 N N   . ILE   B 137 ? 0.2360 0.1553 0.3204 0.0052  -0.0256 0.0070  137 ILE   B N   
6140 C CA  . ILE   B 137 ? 0.2438 0.1580 0.3356 -0.0137 -0.0335 0.0129  137 ILE   B CA  
6141 C C   . ILE   B 137 ? 0.2222 0.1626 0.3300 -0.0239 -0.0055 0.0236  137 ILE   B C   
6142 O O   . ILE   B 137 ? 0.2028 0.1702 0.3200 -0.0167 0.0183  0.0063  137 ILE   B O   
6143 C CB  . ILE   B 137 ? 0.2693 0.1597 0.3850 -0.0124 -0.0341 -0.0057 137 ILE   B CB  
6144 C CG1 . ILE   B 137 ? 0.3040 0.1811 0.4346 -0.0018 -0.0388 -0.0120 137 ILE   B CG1 
6145 C CG2 . ILE   B 137 ? 0.2711 0.1639 0.4173 -0.0337 -0.0327 0.0082  137 ILE   B CG2 
6146 C CD1 . ILE   B 137 ? 0.3330 0.2105 0.4956 0.0055  -0.0315 0.0033  137 ILE   B CD1 
6158 N N   . HIS   B 138 ? 0.2179 0.1596 0.3430 -0.0134 0.0056  0.0291  138 HIS   B N   
6159 C CA  . HIS   B 138 ? 0.2235 0.1736 0.3391 -0.0088 0.0070  0.0393  138 HIS   B CA  
6160 C C   . HIS   B 138 ? 0.2169 0.1677 0.3155 -0.0185 -0.0153 0.0544  138 HIS   B C   
6161 O O   . HIS   B 138 ? 0.2071 0.1807 0.3282 -0.0060 -0.0028 0.0483  138 HIS   B O   
6162 C CB  . HIS   B 138 ? 0.2466 0.1901 0.3448 -0.0140 0.0372  0.0290  138 HIS   B CB  
6163 C CG  . HIS   B 138 ? 0.2687 0.2095 0.3377 -0.0094 0.0601  0.0516  138 HIS   B CG  
6164 N ND1 . HIS   B 138 ? 0.2808 0.2283 0.3935 -0.0102 0.0746  0.0468  138 HIS   B ND1 
6165 C CD2 . HIS   B 138 ? 0.3039 0.2241 0.3303 -0.0136 0.0634  0.0635  138 HIS   B CD2 
6166 C CE1 . HIS   B 138 ? 0.2938 0.2388 0.3949 -0.0140 0.0854  0.0339  138 HIS   B CE1 
6167 N NE2 . HIS   B 138 ? 0.3049 0.2306 0.3480 -0.0112 0.0891  0.0449  138 HIS   B NE2 
6175 N N   . SER   B 139 ? 0.2122 0.1570 0.3116 -0.0080 -0.0153 0.0377  139 SER   B N   
6176 C CA  . SER   B 139 ? 0.2023 0.1597 0.2889 -0.0112 -0.0108 0.0248  139 SER   B CA  
6177 C C   . SER   B 139 ? 0.1760 0.1577 0.2769 -0.0083 -0.0074 0.0136  139 SER   B C   
6178 O O   . SER   B 139 ? 0.1933 0.1558 0.2744 -0.0092 -0.0211 0.0269  139 SER   B O   
6179 C CB  . SER   B 139 ? 0.2114 0.1647 0.2633 -0.0084 -0.0268 0.0050  139 SER   B CB  
6180 O OG  . SER   B 139 ? 0.2099 0.1441 0.2849 -0.0079 -0.0211 0.0399  139 SER   B OG  
6186 N N   . LEU   B 140 ? 0.1835 0.1383 0.2776 -0.0066 -0.0050 0.0076  140 LEU   B N   
6187 C CA  . LEU   B 140 ? 0.1797 0.1491 0.2895 0.0051  -0.0111 -0.0004 140 LEU   B CA  
6188 C C   . LEU   B 140 ? 0.1840 0.1302 0.3062 -0.0069 -0.0194 0.0001  140 LEU   B C   
6189 O O   . LEU   B 140 ? 0.1813 0.1545 0.2923 -0.0033 -0.0192 0.0164  140 LEU   B O   
6190 C CB  . LEU   B 140 ? 0.1706 0.1585 0.2793 -0.0139 -0.0057 0.0071  140 LEU   B CB  
6191 C CG  . LEU   B 140 ? 0.1863 0.1745 0.2887 -0.0104 -0.0159 0.0052  140 LEU   B CG  
6192 C CD1 . LEU   B 140 ? 0.1915 0.1877 0.3254 -0.0189 0.0154  0.0157  140 LEU   B CD1 
6193 C CD2 . LEU   B 140 ? 0.2022 0.1986 0.2810 0.0025  -0.0278 -0.0062 140 LEU   B CD2 
6205 N N   . ARG   B 141 ? 0.1843 0.1361 0.2942 -0.0091 -0.0197 0.0033  141 ARG   B N   
6206 C CA  . ARG   B 141 ? 0.1842 0.1455 0.3343 -0.0252 -0.0120 0.0030  141 ARG   B CA  
6207 C C   . ARG   B 141 ? 0.1649 0.1573 0.3248 -0.0090 -0.0033 0.0149  141 ARG   B C   
6208 O O   . ARG   B 141 ? 0.1586 0.1608 0.3468 -0.0196 -0.0293 -0.0047 141 ARG   B O   
6209 C CB  . ARG   B 141 ? 0.1961 0.1667 0.3678 -0.0281 0.0023  -0.0157 141 ARG   B CB  
6210 C CG  . ARG   B 141 ? 0.2424 0.2032 0.3784 -0.0177 0.0112  -0.0001 141 ARG   B CG  
6211 C CD  . ARG   B 141 ? 0.2840 0.2036 0.3707 -0.0134 -0.0046 -0.0149 141 ARG   B CD  
6212 N NE  . ARG   B 141 ? 0.3037 0.2094 0.3786 -0.0384 0.0043  -0.0301 141 ARG   B NE  
6213 C CZ  . ARG   B 141 ? 0.3148 0.1983 0.3512 -0.0442 0.0151  -0.0312 141 ARG   B CZ  
6214 N NH1 . ARG   B 141 ? 0.3250 0.1807 0.3351 -0.0479 0.0069  -0.0249 141 ARG   B NH1 
6215 N NH2 . ARG   B 141 ? 0.3201 0.1976 0.3580 -0.0311 -0.0100 -0.0366 141 ARG   B NH2 
6229 N N   . VAL   B 142 ? 0.1749 0.1502 0.2912 0.0047  -0.0047 0.0036  142 VAL   B N   
6230 C CA  . VAL   B 142 ? 0.1744 0.1466 0.3008 -0.0057 -0.0094 0.0015  142 VAL   B CA  
6231 C C   . VAL   B 142 ? 0.1745 0.1498 0.2811 -0.0049 -0.0207 0.0063  142 VAL   B C   
6232 O O   . VAL   B 142 ? 0.1828 0.1542 0.3018 0.0052  -0.0144 0.0083  142 VAL   B O   
6233 C CB  . VAL   B 142 ? 0.1918 0.1690 0.3053 -0.0053 -0.0003 0.0192  142 VAL   B CB  
6234 C CG1 . VAL   B 142 ? 0.1991 0.1649 0.3195 0.0092  0.0241  0.0206  142 VAL   B CG1 
6235 C CG2 . VAL   B 142 ? 0.1945 0.1655 0.3106 0.0011  -0.0006 0.0182  142 VAL   B CG2 
6245 N N   . CYS   B 143 ? 0.1635 0.1681 0.2660 -0.0105 -0.0113 0.0019  143 CYS   B N   
6246 C CA  . CYS   B 143 ? 0.1669 0.1713 0.2822 -0.0062 -0.0131 -0.0130 143 CYS   B CA  
6247 C C   . CYS   B 143 ? 0.1641 0.1578 0.2613 -0.0131 -0.0241 -0.0081 143 CYS   B C   
6248 O O   . CYS   B 143 ? 0.1742 0.1569 0.2764 -0.0043 -0.0310 -0.0132 143 CYS   B O   
6249 C CB  . CYS   B 143 ? 0.1787 0.1730 0.2785 0.0036  -0.0169 0.0063  143 CYS   B CB  
6250 S SG  . CYS   B 143 ? 0.1779 0.1793 0.2779 -0.0059 -0.0084 0.0105  143 CYS   B SG  
6256 N N   . VAL   B 144 ? 0.1769 0.1549 0.2880 -0.0217 -0.0127 -0.0284 144 VAL   B N   
6257 C CA  . VAL   B 144 ? 0.1877 0.1670 0.3096 -0.0200 -0.0191 -0.0386 144 VAL   B CA  
6258 C C   . VAL   B 144 ? 0.1649 0.1550 0.3355 -0.0122 -0.0211 -0.0023 144 VAL   B C   
6259 O O   . VAL   B 144 ? 0.1848 0.1794 0.3407 0.0008  -0.0420 0.0205  144 VAL   B O   
6260 C CB  . VAL   B 144 ? 0.2048 0.1906 0.3694 -0.0115 -0.0282 -0.0441 144 VAL   B CB  
6261 C CG1 . VAL   B 144 ? 0.2281 0.2388 0.4073 -0.0200 -0.0263 -0.0346 144 VAL   B CG1 
6262 C CG2 . VAL   B 144 ? 0.2120 0.1776 0.3525 -0.0065 -0.0367 -0.0328 144 VAL   B CG2 
6272 N N   . ASP   B 145 ? 0.1762 0.1612 0.3348 0.0030  -0.0040 -0.0393 145 ASP   B N   
6273 C CA  . ASP   B 145 ? 0.1824 0.1597 0.3395 -0.0040 -0.0122 -0.0212 145 ASP   B CA  
6274 C C   . ASP   B 145 ? 0.1850 0.1619 0.3411 -0.0123 0.0065  -0.0187 145 ASP   B C   
6275 O O   . ASP   B 145 ? 0.1820 0.1793 0.3640 -0.0145 0.0078  -0.0332 145 ASP   B O   
6276 C CB  . ASP   B 145 ? 0.1966 0.1756 0.4043 -0.0107 -0.0027 -0.0061 145 ASP   B CB  
6277 C CG  . ASP   B 145 ? 0.2102 0.1773 0.4546 -0.0077 0.0135  -0.0058 145 ASP   B CG  
6278 O OD1 . ASP   B 145 ? 0.2019 0.1739 0.4783 -0.0183 -0.0292 -0.0304 145 ASP   B OD1 
6279 O OD2 . ASP   B 145 ? 0.2423 0.1850 0.4837 -0.0127 0.0378  0.0132  145 ASP   B OD2 
6284 N N   . THR   B 146 ? 0.1690 0.1646 0.3007 -0.0188 -0.0095 -0.0188 146 THR   B N   
6285 C CA  . THR   B 146 ? 0.1843 0.1725 0.2757 -0.0127 -0.0067 -0.0117 146 THR   B CA  
6286 C C   . THR   B 146 ? 0.1759 0.1649 0.2739 -0.0029 -0.0246 0.0024  146 THR   B C   
6287 O O   . THR   B 146 ? 0.1719 0.1600 0.2999 -0.0052 -0.0201 0.0034  146 THR   B O   
6288 C CB  . THR   B 146 ? 0.1841 0.1796 0.2670 -0.0103 0.0056  -0.0099 146 THR   B CB  
6289 O OG1 . THR   B 146 ? 0.1830 0.1648 0.2931 -0.0134 -0.0048 0.0209  146 THR   B OG1 
6290 C CG2 . THR   B 146 ? 0.2130 0.1774 0.2507 0.0030  -0.0101 -0.0448 146 THR   B CG2 
6298 N N   . VAL   B 147 ? 0.1691 0.1613 0.2662 -0.0010 -0.0160 0.0054  147 VAL   B N   
6299 C CA  . VAL   B 147 ? 0.1720 0.1632 0.2654 -0.0014 -0.0220 0.0130  147 VAL   B CA  
6300 C C   . VAL   B 147 ? 0.1836 0.1692 0.2640 -0.0091 -0.0249 -0.0094 147 VAL   B C   
6301 O O   . VAL   B 147 ? 0.1833 0.1760 0.2687 -0.0202 -0.0334 -0.0116 147 VAL   B O   
6302 C CB  . VAL   B 147 ? 0.1740 0.1687 0.2639 -0.0019 -0.0187 0.0153  147 VAL   B CB  
6303 C CG1 . VAL   B 147 ? 0.1769 0.1811 0.2608 -0.0200 -0.0062 0.0102  147 VAL   B CG1 
6304 C CG2 . VAL   B 147 ? 0.1764 0.1754 0.2584 -0.0026 -0.0271 0.0144  147 VAL   B CG2 
6314 N N   . ARG   B 148 ? 0.1722 0.1578 0.2433 -0.0025 -0.0333 -0.0057 148 ARG   B N   
6315 C CA  . ARG   B 148 ? 0.1733 0.1678 0.2387 -0.0108 -0.0360 -0.0032 148 ARG   B CA  
6316 C C   . ARG   B 148 ? 0.1795 0.1654 0.2190 -0.0152 -0.0329 -0.0112 148 ARG   B C   
6317 O O   . ARG   B 148 ? 0.2099 0.2061 0.2366 -0.0306 -0.0500 -0.0058 148 ARG   B O   
6318 C CB  . ARG   B 148 ? 0.1709 0.1701 0.2301 -0.0064 -0.0374 -0.0035 148 ARG   B CB  
6319 C CG  . ARG   B 148 ? 0.1704 0.1830 0.2598 -0.0045 -0.0360 -0.0231 148 ARG   B CG  
6320 C CD  . ARG   B 148 ? 0.1811 0.2092 0.2774 0.0076  -0.0480 -0.0277 148 ARG   B CD  
6321 N NE  . ARG   B 148 ? 0.2065 0.2151 0.2777 0.0065  -0.0541 -0.0384 148 ARG   B NE  
6322 C CZ  . ARG   B 148 ? 0.1992 0.2119 0.2478 0.0068  -0.0361 -0.0230 148 ARG   B CZ  
6323 N NH1 . ARG   B 148 ? 0.1777 0.1989 0.2791 0.0003  -0.0116 -0.0281 148 ARG   B NH1 
6324 N NH2 . ARG   B 148 ? 0.2257 0.1956 0.2285 0.0137  -0.0463 -0.0200 148 ARG   B NH2 
6338 N N   . THR   B 149 ? 0.1876 0.1654 0.2425 -0.0169 -0.0401 -0.0109 149 THR   B N   
6339 C CA  . THR   B 149 ? 0.1874 0.1714 0.2378 -0.0118 -0.0440 -0.0101 149 THR   B CA  
6340 C C   . THR   B 149 ? 0.1965 0.1744 0.2165 -0.0078 -0.0303 0.0011  149 THR   B C   
6341 O O   . THR   B 149 ? 0.1997 0.1647 0.2265 -0.0168 -0.0263 -0.0034 149 THR   B O   
6342 C CB  . THR   B 149 ? 0.1864 0.1699 0.2325 -0.0160 -0.0436 0.0014  149 THR   B CB  
6343 O OG1 . THR   B 149 ? 0.1903 0.1785 0.2356 -0.0235 -0.0375 -0.0030 149 THR   B OG1 
6344 C CG2 . THR   B 149 ? 0.2073 0.1737 0.2312 -0.0076 -0.0244 0.0133  149 THR   B CG2 
6352 N N   . ASN   B 150 ? 0.2087 0.1717 0.2048 -0.0107 -0.0530 0.0116  150 ASN   B N   
6353 C CA  . ASN   B 150 ? 0.2156 0.1754 0.2102 -0.0131 -0.0439 0.0024  150 ASN   B CA  
6354 C C   . ASN   B 150 ? 0.2045 0.1803 0.2151 -0.0144 -0.0520 0.0013  150 ASN   B C   
6355 O O   . ASN   B 150 ? 0.2121 0.1720 0.2259 -0.0269 -0.0643 -0.0123 150 ASN   B O   
6356 C CB  . ASN   B 150 ? 0.2284 0.2065 0.2273 -0.0273 -0.0647 0.0157  150 ASN   B CB  
6357 C CG  . ASN   B 150 ? 0.2587 0.2520 0.2645 -0.0283 -0.0695 0.0369  150 ASN   B CG  
6358 O OD1 . ASN   B 150 ? 0.2663 0.2710 0.2969 -0.0443 -0.0666 0.0396  150 ASN   B OD1 
6359 N ND2 . ASN   B 150 ? 0.2811 0.2882 0.3179 -0.0132 -0.0524 0.0882  150 ASN   B ND2 
6366 N N   . VAL   B 151 ? 0.1905 0.1852 0.1933 -0.0170 -0.0515 -0.0048 151 VAL   B N   
6367 C CA  . VAL   B 151 ? 0.1927 0.1860 0.1983 -0.0217 -0.0350 0.0015  151 VAL   B CA  
6368 C C   . VAL   B 151 ? 0.1839 0.1733 0.2002 -0.0333 -0.0505 -0.0101 151 VAL   B C   
6369 O O   . VAL   B 151 ? 0.2002 0.1733 0.2253 -0.0249 -0.0389 -0.0057 151 VAL   B O   
6370 C CB  . VAL   B 151 ? 0.2153 0.1988 0.2302 -0.0162 -0.0425 0.0049  151 VAL   B CB  
6371 C CG1 . VAL   B 151 ? 0.2266 0.2069 0.2993 -0.0177 -0.0453 -0.0121 151 VAL   B CG1 
6372 C CG2 . VAL   B 151 ? 0.2149 0.2067 0.1962 0.0157  -0.0413 0.0093  151 VAL   B CG2 
6382 N N   . TYR   B 152 ? 0.1890 0.1627 0.2169 -0.0198 -0.0491 -0.0109 152 TYR   B N   
6383 C CA  . TYR   B 152 ? 0.1923 0.1599 0.1975 -0.0345 -0.0298 -0.0178 152 TYR   B CA  
6384 C C   . TYR   B 152 ? 0.1875 0.1547 0.1894 -0.0252 -0.0245 -0.0030 152 TYR   B C   
6385 O O   . TYR   B 152 ? 0.1990 0.1575 0.2025 -0.0364 -0.0231 0.0021  152 TYR   B O   
6386 C CB  . TYR   B 152 ? 0.2051 0.1956 0.1989 -0.0272 -0.0325 -0.0001 152 TYR   B CB  
6387 C CG  . TYR   B 152 ? 0.2131 0.2077 0.1889 -0.0333 -0.0479 -0.0068 152 TYR   B CG  
6388 C CD1 . TYR   B 152 ? 0.2268 0.2183 0.1991 -0.0252 -0.0600 -0.0078 152 TYR   B CD1 
6389 C CD2 . TYR   B 152 ? 0.2303 0.2169 0.2008 -0.0436 -0.0416 -0.0107 152 TYR   B CD2 
6390 C CE1 . TYR   B 152 ? 0.2486 0.2311 0.2134 -0.0247 -0.0472 0.0131  152 TYR   B CE1 
6391 C CE2 . TYR   B 152 ? 0.2481 0.2386 0.2122 -0.0438 -0.0543 -0.0118 152 TYR   B CE2 
6392 C CZ  . TYR   B 152 ? 0.2467 0.2432 0.1826 -0.0365 -0.0759 0.0291  152 TYR   B CZ  
6393 O OH  . TYR   B 152 ? 0.2835 0.2840 0.2402 -0.0286 -0.0686 0.0340  152 TYR   B OH  
6403 N N   . LEU   B 153 ? 0.1921 0.1543 0.1884 -0.0244 -0.0310 -0.0058 153 LEU   B N   
6404 C CA  . LEU   B 153 ? 0.1996 0.1527 0.1783 -0.0176 -0.0242 -0.0105 153 LEU   B CA  
6405 C C   . LEU   B 153 ? 0.2054 0.1611 0.1768 -0.0270 -0.0237 -0.0271 153 LEU   B C   
6406 O O   . LEU   B 153 ? 0.2056 0.1867 0.2034 -0.0234 -0.0160 -0.0385 153 LEU   B O   
6407 C CB  . LEU   B 153 ? 0.1955 0.1457 0.2032 -0.0356 -0.0116 0.0013  153 LEU   B CB  
6408 C CG  . LEU   B 153 ? 0.1852 0.1628 0.2344 -0.0252 -0.0265 0.0009  153 LEU   B CG  
6409 C CD1 . LEU   B 153 ? 0.1997 0.1832 0.2705 -0.0182 -0.0210 -0.0022 153 LEU   B CD1 
6410 C CD2 . LEU   B 153 ? 0.1847 0.1972 0.2410 -0.0334 -0.0194 0.0156  153 LEU   B CD2 
6422 N N   . ALA   B 154 ? 0.2020 0.1482 0.2155 -0.0137 -0.0341 -0.0087 154 ALA   B N   
6423 C CA  . ALA   B 154 ? 0.2218 0.1602 0.2252 -0.0006 -0.0300 -0.0124 154 ALA   B CA  
6424 C C   . ALA   B 154 ? 0.2270 0.1755 0.2281 0.0121  -0.0308 -0.0225 154 ALA   B C   
6425 O O   . ALA   B 154 ? 0.2690 0.1752 0.2758 0.0139  -0.0314 -0.0220 154 ALA   B O   
6426 C CB  . ALA   B 154 ? 0.2225 0.1694 0.2560 -0.0032 -0.0339 -0.0103 154 ALA   B CB  
6432 N N   . VAL   B 155 ? 0.1771 0.1640 0.2359 0.0047  -0.0107 -0.0068 155 VAL   B N   
6433 C CA  . VAL   B 155 ? 0.1737 0.1705 0.2560 0.0045  -0.0229 -0.0099 155 VAL   B CA  
6434 C C   . VAL   B 155 ? 0.1633 0.1655 0.2500 0.0000  -0.0119 -0.0154 155 VAL   B C   
6435 O O   . VAL   B 155 ? 0.1840 0.1763 0.2987 -0.0019 -0.0309 -0.0287 155 VAL   B O   
6436 C CB  . VAL   B 155 ? 0.1745 0.1728 0.2776 0.0003  -0.0431 0.0012  155 VAL   B CB  
6437 C CG1 . VAL   B 155 ? 0.1873 0.1792 0.2992 -0.0091 -0.0358 0.0172  155 VAL   B CG1 
6438 C CG2 . VAL   B 155 ? 0.1886 0.1901 0.3200 -0.0018 -0.0216 0.0327  155 VAL   B CG2 
6448 N N   . PHE   B 156 ? 0.1673 0.1823 0.2732 0.0034  -0.0119 -0.0195 156 PHE   B N   
6449 C CA  . PHE   B 156 ? 0.1588 0.1825 0.2990 0.0135  -0.0247 -0.0270 156 PHE   B CA  
6450 C C   . PHE   B 156 ? 0.1615 0.1925 0.3258 0.0192  -0.0235 -0.0462 156 PHE   B C   
6451 O O   . PHE   B 156 ? 0.1925 0.1991 0.3985 0.0204  -0.0059 -0.0389 156 PHE   B O   
6452 C CB  . PHE   B 156 ? 0.1745 0.1721 0.3093 -0.0015 -0.0373 -0.0132 156 PHE   B CB  
6453 C CG  . PHE   B 156 ? 0.1699 0.1938 0.3235 -0.0054 -0.0287 0.0147  156 PHE   B CG  
6454 C CD1 . PHE   B 156 ? 0.1785 0.2224 0.3662 0.0000  0.0020  0.0587  156 PHE   B CD1 
6455 C CD2 . PHE   B 156 ? 0.1885 0.2090 0.3217 0.0128  -0.0247 0.0223  156 PHE   B CD2 
6456 C CE1 . PHE   B 156 ? 0.1892 0.2429 0.3834 -0.0016 -0.0086 0.0524  156 PHE   B CE1 
6457 C CE2 . PHE   B 156 ? 0.1931 0.2202 0.3449 0.0076  -0.0283 0.0167  156 PHE   B CE2 
6458 C CZ  . PHE   B 156 ? 0.1882 0.2322 0.3741 0.0016  -0.0242 0.0478  156 PHE   B CZ  
6468 N N   . ASP   B 157 ? 0.1731 0.1764 0.3595 0.0206  -0.0415 -0.0053 157 ASP   B N   
6469 C CA  . ASP   B 157 ? 0.1798 0.1839 0.4123 0.0127  -0.0360 -0.0110 157 ASP   B CA  
6470 C C   . ASP   B 157 ? 0.1839 0.1793 0.4206 -0.0026 -0.0119 -0.0332 157 ASP   B C   
6471 O O   . ASP   B 157 ? 0.1673 0.1764 0.3975 0.0005  -0.0185 -0.0182 157 ASP   B O   
6472 C CB  . ASP   B 157 ? 0.2024 0.2063 0.4261 0.0050  -0.0419 0.0094  157 ASP   B CB  
6473 C CG  . ASP   B 157 ? 0.2551 0.2233 0.4556 -0.0075 -0.0309 0.0033  157 ASP   B CG  
6474 O OD1 . ASP   B 157 ? 0.2726 0.2197 0.4726 0.0199  -0.0348 -0.0019 157 ASP   B OD1 
6475 O OD2 . ASP   B 157 ? 0.2824 0.2416 0.4971 -0.0146 -0.0221 0.0007  157 ASP   B OD2 
6480 N N   . LYS   B 158 ? 0.2010 0.2165 0.4495 -0.0013 -0.0159 -0.0631 158 LYS   B N   
6481 C CA  . LYS   B 158 ? 0.2070 0.2431 0.4519 -0.0037 0.0019  -0.0871 158 LYS   B CA  
6482 C C   . LYS   B 158 ? 0.2077 0.2120 0.4643 0.0067  -0.0150 -0.0753 158 LYS   B C   
6483 O O   . LYS   B 158 ? 0.2069 0.2122 0.4986 0.0095  -0.0062 -0.1008 158 LYS   B O   
6484 C CB  . LYS   B 158 ? 0.2448 0.3058 0.4632 -0.0015 0.0107  -0.1062 158 LYS   B CB  
6485 C CG  . LYS   B 158 ? 0.2821 0.3522 0.4818 -0.0082 0.0143  -0.1203 158 LYS   B CG  
6486 C CD  . LYS   B 158 ? 0.3027 0.4004 0.4837 -0.0123 0.0266  -0.1360 158 LYS   B CD  
6487 C CE  . LYS   B 158 ? 0.3210 0.4440 0.4995 -0.0138 0.0329  -0.1372 158 LYS   B CE  
6488 N NZ  . LYS   B 158 ? 0.3069 0.4674 0.5007 -0.0285 0.0442  -0.1341 158 LYS   B NZ  
6502 N N   A ASN   B 159 ? 0.1912 0.1939 0.4629 0.0133  -0.0160 -0.0625 159 ASN   B N   
6503 N N   B ASN   B 159 ? 0.1926 0.1996 0.4677 0.0012  -0.0143 -0.0520 159 ASN   B N   
6504 C CA  A ASN   B 159 ? 0.2082 0.1977 0.4691 0.0251  -0.0221 -0.0575 159 ASN   B CA  
6505 C CA  B ASN   B 159 ? 0.2122 0.2107 0.4783 0.0047  -0.0184 -0.0384 159 ASN   B CA  
6506 C C   A ASN   B 159 ? 0.1995 0.1769 0.4610 0.0211  -0.0437 -0.0456 159 ASN   B C   
6507 C C   B ASN   B 159 ? 0.1959 0.1869 0.4665 0.0050  -0.0486 -0.0337 159 ASN   B C   
6508 O O   A ASN   B 159 ? 0.2058 0.1663 0.4644 0.0098  -0.0507 -0.0438 159 ASN   B O   
6509 O O   B ASN   B 159 ? 0.1932 0.1798 0.4678 -0.0158 -0.0697 -0.0265 159 ASN   B O   
6510 C CB  A ASN   B 159 ? 0.2315 0.2134 0.4824 0.0374  -0.0306 -0.0488 159 ASN   B CB  
6511 C CB  B ASN   B 159 ? 0.2475 0.2355 0.4961 0.0026  -0.0180 -0.0109 159 ASN   B CB  
6512 C CG  A ASN   B 159 ? 0.2470 0.2269 0.4885 0.0481  -0.0461 -0.0598 159 ASN   B CG  
6513 C CG  B ASN   B 159 ? 0.2738 0.2602 0.5083 -0.0000 -0.0288 -0.0051 159 ASN   B CG  
6514 O OD1 A ASN   B 159 ? 0.2542 0.2150 0.4827 0.0593  -0.0542 -0.0722 159 ASN   B OD1 
6515 O OD1 B ASN   B 159 ? 0.2898 0.2663 0.5101 0.0028  -0.0312 0.0013  159 ASN   B OD1 
6516 N ND2 A ASN   B 159 ? 0.2436 0.2425 0.4904 0.0475  -0.0525 -0.0545 159 ASN   B ND2 
6517 N ND2 B ASN   B 159 ? 0.2748 0.2719 0.5147 -0.0043 -0.0348 0.0004  159 ASN   B ND2 
6530 N N   . LEU   B 160 ? 0.1947 0.1834 0.4490 0.0060  -0.0516 -0.0391 160 LEU   B N   
6531 C CA  . LEU   B 160 ? 0.1969 0.1690 0.3885 0.0055  -0.0383 -0.0203 160 LEU   B CA  
6532 C C   . LEU   B 160 ? 0.1848 0.1647 0.3746 -0.0078 -0.0252 -0.0233 160 LEU   B C   
6533 O O   . LEU   B 160 ? 0.1701 0.1825 0.3862 -0.0063 -0.0267 -0.0285 160 LEU   B O   
6534 C CB  . LEU   B 160 ? 0.1940 0.1818 0.3615 0.0025  -0.0412 -0.0116 160 LEU   B CB  
6535 C CG  . LEU   B 160 ? 0.1901 0.1994 0.3372 0.0097  -0.0413 0.0093  160 LEU   B CG  
6536 C CD1 . LEU   B 160 ? 0.2023 0.2211 0.3664 0.0057  -0.0144 0.0226  160 LEU   B CD1 
6537 C CD2 . LEU   B 160 ? 0.1917 0.2049 0.3251 0.0210  -0.0268 -0.0118 160 LEU   B CD2 
6550 N N   . TYR   B 161 ? 0.1821 0.1643 0.4046 -0.0014 -0.0098 -0.0358 161 TYR   B N   
6551 C CA  . TYR   B 161 ? 0.1821 0.1777 0.3994 -0.0225 -0.0046 -0.0482 161 TYR   B CA  
6552 C C   . TYR   B 161 ? 0.1916 0.1770 0.3707 -0.0150 -0.0024 -0.0398 161 TYR   B C   
6553 O O   . TYR   B 161 ? 0.2027 0.1922 0.3331 -0.0156 -0.0193 -0.0258 161 TYR   B O   
6554 C CB  . TYR   B 161 ? 0.1956 0.1861 0.4082 -0.0205 0.0014  -0.0449 161 TYR   B CB  
6555 C CG  . TYR   B 161 ? 0.2360 0.1973 0.3817 -0.0250 0.0066  -0.0508 161 TYR   B CG  
6556 C CD1 . TYR   B 161 ? 0.2324 0.1923 0.3866 -0.0272 0.0189  -0.0562 161 TYR   B CD1 
6557 C CD2 . TYR   B 161 ? 0.2655 0.2099 0.3562 -0.0113 -0.0004 -0.0512 161 TYR   B CD2 
6558 C CE1 . TYR   B 161 ? 0.2542 0.2158 0.3644 -0.0385 0.0260  -0.0628 161 TYR   B CE1 
6559 C CE2 . TYR   B 161 ? 0.2739 0.2240 0.3401 -0.0197 0.0149  -0.0525 161 TYR   B CE2 
6560 C CZ  . TYR   B 161 ? 0.2710 0.2234 0.3262 -0.0410 0.0030  -0.0554 161 TYR   B CZ  
6561 O OH  . TYR   B 161 ? 0.3134 0.2581 0.3328 -0.0410 0.0062  -0.0637 161 TYR   B OH  
6571 N N   A ASP   B 162 ? 0.1954 0.1828 0.3812 -0.0106 -0.0032 -0.0606 162 ASP   B N   
6572 N N   B ASP   B 162 ? 0.1972 0.1785 0.3875 -0.0157 0.0041  -0.0670 162 ASP   B N   
6573 C CA  A ASP   B 162 ? 0.1961 0.1927 0.3895 -0.0024 -0.0175 -0.0596 162 ASP   B CA  
6574 C CA  B ASP   B 162 ? 0.1985 0.1841 0.3983 -0.0116 0.0013  -0.0638 162 ASP   B CA  
6575 C C   A ASP   B 162 ? 0.1962 0.1840 0.3952 -0.0054 -0.0417 -0.0355 162 ASP   B C   
6576 C C   B ASP   B 162 ? 0.1990 0.1664 0.4026 -0.0202 -0.0230 -0.0496 162 ASP   B C   
6577 O O   A ASP   B 162 ? 0.1974 0.1905 0.4134 -0.0081 -0.0601 -0.0312 162 ASP   B O   
6578 O O   B ASP   B 162 ? 0.2039 0.1768 0.4088 -0.0259 -0.0426 -0.0536 162 ASP   B O   
6579 C CB  A ASP   B 162 ? 0.2116 0.2028 0.4024 0.0089  -0.0208 -0.0829 162 ASP   B CB  
6580 C CB  B ASP   B 162 ? 0.2191 0.1960 0.4115 0.0018  0.0043  -0.0744 162 ASP   B CB  
6581 C CG  A ASP   B 162 ? 0.2206 0.2167 0.4271 0.0105  -0.0245 -0.0991 162 ASP   B CG  
6582 C CG  B ASP   B 162 ? 0.2323 0.2126 0.4355 0.0067  0.0068  -0.0709 162 ASP   B CG  
6583 O OD1 A ASP   B 162 ? 0.2348 0.2330 0.4251 -0.0046 -0.0280 -0.0967 162 ASP   B OD1 
6584 O OD1 B ASP   B 162 ? 0.2396 0.2337 0.4239 -0.0084 0.0094  -0.0698 162 ASP   B OD1 
6585 O OD2 A ASP   B 162 ? 0.2227 0.2238 0.4465 0.0181  -0.0366 -0.1191 162 ASP   B OD2 
6586 O OD2 B ASP   B 162 ? 0.2471 0.2228 0.4583 0.0167  -0.0007 -0.0668 162 ASP   B OD2 
6595 N N   A LYS   B 163 ? 0.1998 0.1700 0.3903 -0.0057 -0.0606 -0.0132 163 LYS   B N   
6596 N N   B LYS   B 163 ? 0.2008 0.1411 0.3990 -0.0243 -0.0460 -0.0271 163 LYS   B N   
6597 C CA  A LYS   B 163 ? 0.2095 0.1835 0.3882 -0.0091 -0.0440 0.0059  163 LYS   B CA  
6598 C CA  B LYS   B 163 ? 0.2056 0.1588 0.3923 -0.0237 -0.0277 -0.0027 163 LYS   B CA  
6599 C C   A LYS   B 163 ? 0.1826 0.1751 0.3747 -0.0221 -0.0332 0.0088  163 LYS   B C   
6600 C C   B LYS   B 163 ? 0.1755 0.1649 0.3717 -0.0344 -0.0174 -0.0049 163 LYS   B C   
6601 O O   A LYS   B 163 ? 0.1838 0.1778 0.3818 -0.0212 -0.0320 0.0279  163 LYS   B O   
6602 O O   B LYS   B 163 ? 0.1725 0.1742 0.3707 -0.0378 -0.0116 -0.0032 163 LYS   B O   
6603 C CB  A LYS   B 163 ? 0.2423 0.2130 0.4059 0.0095  -0.0547 0.0115  163 LYS   B CB  
6604 C CB  B LYS   B 163 ? 0.2400 0.1818 0.4074 0.0011  -0.0435 0.0100  163 LYS   B CB  
6605 C CG  A LYS   B 163 ? 0.2943 0.2664 0.4297 0.0100  -0.0430 0.0142  163 LYS   B CG  
6606 C CG  B LYS   B 163 ? 0.2999 0.2432 0.4278 0.0005  -0.0303 0.0172  163 LYS   B CG  
6607 C CD  A LYS   B 163 ? 0.3338 0.3053 0.4553 0.0014  -0.0359 0.0073  163 LYS   B CD  
6608 C CD  B LYS   B 163 ? 0.3480 0.2928 0.4572 -0.0078 -0.0223 0.0101  163 LYS   B CD  
6609 C CE  A LYS   B 163 ? 0.3606 0.3293 0.4719 0.0016  -0.0225 0.0049  163 LYS   B CE  
6610 C CE  B LYS   B 163 ? 0.3826 0.3236 0.4780 -0.0115 -0.0113 0.0076  163 LYS   B CE  
6611 N NZ  A LYS   B 163 ? 0.3792 0.3363 0.4841 0.0020  -0.0196 -0.0035 163 LYS   B NZ  
6612 N NZ  B LYS   B 163 ? 0.4049 0.3347 0.4901 -0.0134 -0.0139 0.0033  163 LYS   B NZ  
6639 N N   . LEU   B 164 ? 0.1697 0.1704 0.3751 -0.0210 -0.0300 0.0011  164 LEU   B N   
6640 C CA  . LEU   B 164 ? 0.1717 0.1710 0.3322 -0.0121 -0.0350 0.0128  164 LEU   B CA  
6641 C C   . LEU   B 164 ? 0.1886 0.1765 0.3246 -0.0088 -0.0468 0.0191  164 LEU   B C   
6642 O O   . LEU   B 164 ? 0.1740 0.1918 0.3620 -0.0215 -0.0437 -0.0012 164 LEU   B O   
6643 C CB  . LEU   B 164 ? 0.1645 0.1677 0.2800 -0.0057 -0.0258 0.0116  164 LEU   B CB  
6644 C CG  . LEU   B 164 ? 0.1838 0.1776 0.2984 -0.0088 -0.0212 -0.0016 164 LEU   B CG  
6645 C CD1 . LEU   B 164 ? 0.1985 0.1652 0.2991 -0.0227 -0.0330 -0.0120 164 LEU   B CD1 
6646 C CD2 . LEU   B 164 ? 0.2124 0.2056 0.3252 -0.0134 -0.0097 -0.0140 164 LEU   B CD2 
6659 N N   A VAL   B 165 ? 0.2175 0.1777 0.3392 -0.0096 -0.0549 0.0041  165 VAL   B N   
6660 N N   B VAL   B 165 ? 0.2217 0.1785 0.3424 -0.0196 -0.0536 0.0082  165 VAL   B N   
6661 C CA  A VAL   B 165 ? 0.2412 0.1913 0.3505 -0.0126 -0.0685 -0.0110 165 VAL   B CA  
6662 C CA  B VAL   B 165 ? 0.2479 0.1932 0.3554 -0.0300 -0.0665 -0.0038 165 VAL   B CA  
6663 C C   A VAL   B 165 ? 0.2562 0.2164 0.3757 -0.0221 -0.0913 -0.0152 165 VAL   B C   
6664 C C   B VAL   B 165 ? 0.2648 0.2212 0.3782 -0.0344 -0.0881 -0.0128 165 VAL   B C   
6665 O O   A VAL   B 165 ? 0.2738 0.2242 0.3878 -0.0231 -0.0958 -0.0166 165 VAL   B O   
6666 O O   B VAL   B 165 ? 0.2843 0.2262 0.3867 -0.0322 -0.0823 -0.0171 165 VAL   B O   
6667 C CB  A VAL   B 165 ? 0.2621 0.2019 0.3509 0.0022  -0.0548 -0.0360 165 VAL   B CB  
6668 C CB  B VAL   B 165 ? 0.2731 0.2076 0.3601 -0.0217 -0.0496 -0.0271 165 VAL   B CB  
6669 C CG1 A VAL   B 165 ? 0.2888 0.2083 0.3670 0.0019  -0.0408 -0.0382 165 VAL   B CG1 
6670 C CG1 B VAL   B 165 ? 0.2985 0.2126 0.3746 -0.0264 -0.0428 -0.0250 165 VAL   B CG1 
6671 C CG2 A VAL   B 165 ? 0.2614 0.2010 0.3546 0.0049  -0.0564 -0.0358 165 VAL   B CG2 
6672 C CG2 B VAL   B 165 ? 0.2720 0.2054 0.3617 -0.0216 -0.0525 -0.0299 165 VAL   B CG2 
6691 N N   A SER   B 166 ? 0.2609 0.2174 0.3952 -0.0266 -0.0986 -0.0272 166 SER   B N   
6692 N N   B SER   B 166 ? 0.2631 0.2253 0.3973 -0.0333 -0.1057 -0.0275 166 SER   B N   
6693 C CA  A SER   B 166 ? 0.2660 0.2144 0.4257 -0.0347 -0.0964 -0.0299 166 SER   B CA  
6694 C CA  B SER   B 166 ? 0.2632 0.2227 0.4313 -0.0366 -0.1061 -0.0327 166 SER   B CA  
6695 C C   A SER   B 166 ? 0.2565 0.2071 0.4578 -0.0413 -0.0805 -0.0028 166 SER   B C   
6696 C C   B SER   B 166 ? 0.2515 0.2181 0.4641 -0.0376 -0.0839 -0.0055 166 SER   B C   
6697 O O   A SER   B 166 ? 0.2642 0.2066 0.4960 -0.0617 -0.0885 -0.0247 166 SER   B O   
6698 O O   B SER   B 166 ? 0.2524 0.2350 0.5055 -0.0531 -0.0958 -0.0290 166 SER   B O   
6699 C CB  A SER   B 166 ? 0.2772 0.2154 0.4325 -0.0224 -0.0853 -0.0478 166 SER   B CB  
6700 C CB  B SER   B 166 ? 0.2736 0.2218 0.4473 -0.0267 -0.0916 -0.0530 166 SER   B CB  
6701 O OG  A SER   B 166 ? 0.2750 0.2041 0.4451 -0.0084 -0.0831 -0.0366 166 SER   B OG  
6702 O OG  B SER   B 166 ? 0.2666 0.2083 0.4660 -0.0152 -0.0914 -0.0446 166 SER   B OG  
6713 N N   . SER   B 167 ? 0.2402 0.2055 0.4291 -0.0450 -0.0973 0.0334  167 SER   B N   
6714 C CA  . SER   B 167 ? 0.2331 0.2240 0.4260 -0.0200 -0.0650 0.0487  167 SER   B CA  
6715 C C   . SER   B 167 ? 0.2213 0.2145 0.4066 -0.0438 -0.0537 0.0680  167 SER   B C   
6716 O O   . SER   B 167 ? 0.2227 0.2314 0.4060 -0.0531 -0.0499 0.0603  167 SER   B O   
6717 C CB  . SER   B 167 ? 0.2042 0.2355 0.4482 -0.0439 -0.0441 0.0360  167 SER   B CB  
6718 O OG  . SER   B 167 ? 0.2203 0.2339 0.4468 -0.0371 -0.0203 0.0277  167 SER   B OG  
6725 N N   . PHE   B 168 ? 0.2137 0.2091 0.4071 -0.0419 -0.0493 0.0731  168 PHE   B N   
6726 C CA  . PHE   B 168 ? 0.2177 0.2018 0.3679 -0.0547 -0.0566 0.0353  168 PHE   B CA  
6727 C C   . PHE   B 168 ? 0.2072 0.1979 0.3073 -0.0239 -0.0111 0.0096  168 PHE   B C   
6728 O O   . PHE   B 168 ? 0.2268 0.1792 0.3394 -0.0094 -0.0126 -0.0071 168 PHE   B O   
6729 C CB  . PHE   B 168 ? 0.2269 0.2196 0.3901 -0.0632 -0.0740 0.0640  168 PHE   B CB  
6730 C CG  . PHE   B 168 ? 0.2609 0.2043 0.3808 -0.0529 -0.0703 0.0382  168 PHE   B CG  
6731 C CD1 . PHE   B 168 ? 0.2893 0.2174 0.4204 -0.0524 -0.0771 0.0271  168 PHE   B CD1 
6732 C CD2 . PHE   B 168 ? 0.2472 0.1943 0.3917 -0.0415 -0.0757 0.0284  168 PHE   B CD2 
6733 C CE1 . PHE   B 168 ? 0.3007 0.2319 0.4120 -0.0426 -0.0735 0.0348  168 PHE   B CE1 
6734 C CE2 . PHE   B 168 ? 0.2788 0.2037 0.4132 -0.0474 -0.0666 0.0331  168 PHE   B CE2 
6735 C CZ  . PHE   B 168 ? 0.2876 0.2174 0.4063 -0.0420 -0.0812 0.0563  168 PHE   B CZ  
6745 N N   A LEU   B 169 ? 0.2228 0.2149 0.2954 -0.0054 -0.0129 0.0028  169 LEU   B N   
6746 N N   B LEU   B 169 ? 0.2284 0.2094 0.2885 0.0029  -0.0067 0.0070  169 LEU   B N   
6747 C CA  A LEU   B 169 ? 0.2485 0.2436 0.3162 0.0022  -0.0081 -0.0277 169 LEU   B CA  
6748 C CA  B LEU   B 169 ? 0.2614 0.2365 0.3093 0.0162  0.0077  -0.0262 169 LEU   B CA  
6749 C C   A LEU   B 169 ? 0.2621 0.2643 0.3631 0.0076  -0.0057 -0.0492 169 LEU   B C   
6750 C C   B LEU   B 169 ? 0.2859 0.2565 0.3549 0.0261  0.0169  -0.0465 169 LEU   B C   
6751 O O   A LEU   B 169 ? 0.2703 0.2707 0.3961 -0.0126 -0.0082 -0.0763 169 LEU   B O   
6752 O O   B LEU   B 169 ? 0.3030 0.2661 0.3694 0.0096  0.0225  -0.0717 169 LEU   B O   
6753 C CB  A LEU   B 169 ? 0.2824 0.2789 0.3211 -0.0013 -0.0208 -0.0040 169 LEU   B CB  
6754 C CB  B LEU   B 169 ? 0.2978 0.2770 0.3191 0.0081  -0.0124 0.0012  169 LEU   B CB  
6755 C CG  A LEU   B 169 ? 0.3248 0.3101 0.3602 0.0060  -0.0218 0.0107  169 LEU   B CG  
6756 C CG  B LEU   B 169 ? 0.3432 0.3124 0.3633 0.0134  -0.0153 0.0153  169 LEU   B CG  
6757 C CD1 A LEU   B 169 ? 0.3365 0.3260 0.3688 0.0011  -0.0341 0.0284  169 LEU   B CD1 
6758 C CD1 B LEU   B 169 ? 0.3576 0.3314 0.3652 0.0082  -0.0262 0.0265  169 LEU   B CD1 
6759 C CD2 A LEU   B 169 ? 0.3269 0.3198 0.3725 0.0153  -0.0069 -0.0006 169 LEU   B CD2 
6760 C CD2 B LEU   B 169 ? 0.3459 0.3247 0.3822 0.0206  -0.0016 0.0034  169 LEU   B CD2 
6761 O OXT A LEU   B 169 ? 0.2743 0.2768 0.3710 0.0319  0.0066  -0.0361 169 LEU   B OXT 
6762 O OXT B LEU   B 169 ? 0.2985 0.2680 0.3750 0.0558  0.0299  -0.0370 169 LEU   B OXT 
6785 N N2  B A1BAX C .   ? 0.1922 0.2098 0.1682 -0.0351 0.0101  0.0034  201 A1BAX A N2  
6786 C C3  B A1BAX C .   ? 0.1654 0.2021 0.2010 -0.0214 0.0193  0.0097  201 A1BAX A C3  
6787 C C6  B A1BAX C .   ? 0.2004 0.2217 0.1536 -0.0234 0.0050  0.0122  201 A1BAX A C6  
6788 C C9  B A1BAX C .   ? 0.2680 0.2304 0.1767 -0.0370 0.0097  0.0099  201 A1BAX A C9  
6789 C C12 B A1BAX C .   ? 0.2693 0.2427 0.2096 -0.0347 -0.0079 0.0241  201 A1BAX A C12 
6790 C C14 B A1BAX C .   ? 0.3042 0.2600 0.2109 -0.0167 -0.0163 0.0439  201 A1BAX A C14 
6791 C C1  B A1BAX C .   ? 0.1993 0.2243 0.2378 -0.0048 0.0317  -0.0022 201 A1BAX A C1  
6792 C C10 B A1BAX C .   ? 0.2823 0.2342 0.2126 -0.0350 0.0002  0.0214  201 A1BAX A C10 
6793 C C11 B A1BAX C .   ? 0.2860 0.2469 0.2070 -0.0258 -0.0104 0.0310  201 A1BAX A C11 
6794 C C13 B A1BAX C .   ? 0.2483 0.2301 0.1961 -0.0458 -0.0244 0.0150  201 A1BAX A C13 
6795 C C15 B A1BAX C .   ? 0.1857 0.2062 0.1559 -0.0260 0.0074  0.0009  201 A1BAX A C15 
6796 C C2  B A1BAX C .   ? 0.1819 0.2038 0.1877 -0.0220 0.0364  0.0209  201 A1BAX A C2  
6797 C C4  B A1BAX C .   ? 0.1863 0.2020 0.1862 -0.0193 0.0011  0.0097  201 A1BAX A C4  
6798 C C5  B A1BAX C .   ? 0.2034 0.2087 0.1177 -0.0331 0.0108  0.0114  201 A1BAX A C5  
6799 C C7  B A1BAX C .   ? 0.2230 0.2434 0.1657 -0.0433 0.0072  0.0038  201 A1BAX A C7  
6800 C C8  B A1BAX C .   ? 0.2366 0.2305 0.1625 -0.0418 -0.0037 0.0083  201 A1BAX A C8  
6801 N N1  B A1BAX C .   ? 0.1828 0.1961 0.2244 -0.0146 -0.0103 -0.0169 201 A1BAX A N1  
6802 N N3  B A1BAX C .   ? 0.2010 0.2118 0.1308 -0.0373 -0.0121 0.0021  201 A1BAX A N3  
6803 N N4  B A1BAX C .   ? 0.2075 0.2316 0.1840 -0.0419 -0.0017 0.0088  201 A1BAX A N4  
6804 O O1  B A1BAX C .   ? 0.2299 0.2327 0.1586 -0.0274 -0.0074 0.0040  201 A1BAX A O1  
6827 O O   . HOH   D .   ? 0.6125 0.4946 0.6224 -0.0950 0.1587  -0.1001 301 HOH   A O   
6828 O O   . HOH   D .   ? 0.4686 0.8537 0.5416 -0.1559 -0.0224 0.0806  302 HOH   A O   
6829 O O   . HOH   D .   ? 0.7864 0.6484 0.3837 0.2602  -0.1469 0.0725  303 HOH   A O   
6830 O O   . HOH   D .   ? 0.6892 0.6915 0.5942 -0.1233 -0.1647 0.0347  304 HOH   A O   
6831 O O   . HOH   D .   ? 0.7681 0.3982 0.4812 0.2016  -0.0958 -0.0023 305 HOH   A O   
6832 O O   . HOH   D .   ? 0.3186 0.3276 0.1934 -0.0160 0.0447  0.0380  306 HOH   A O   
6833 O O   A HOH   D .   ? 0.3891 0.1581 0.4016 -0.0143 -0.0005 0.0535  307 HOH   A O   
6834 O O   . HOH   D .   ? 0.2719 0.2880 0.3093 -0.0576 -0.0576 0.1057  308 HOH   A O   
6835 O O   . HOH   D .   ? 0.3736 0.4988 0.4151 -0.0181 -0.0720 0.0113  309 HOH   A O   
6836 O O   . HOH   D .   ? 0.2533 0.2152 0.2581 0.0230  -0.0169 0.0015  310 HOH   A O   
6837 O O   . HOH   D .   ? 0.2059 0.7573 0.3378 0.0269  0.0376  0.0657  311 HOH   A O   
6838 O O   . HOH   D .   ? 0.6000 0.3216 0.6363 -0.0039 0.0753  -0.0372 312 HOH   A O   
6839 O O   . HOH   D .   ? 0.5990 0.5550 0.3978 -0.0633 -0.1161 0.0610  313 HOH   A O   
6840 O O   . HOH   D .   ? 0.6744 0.6321 0.4146 -0.0548 -0.0373 0.1159  314 HOH   A O   
6841 O O   . HOH   D .   ? 0.7105 0.5255 0.5949 -0.1171 0.1770  0.1504  315 HOH   A O   
6842 O O   . HOH   D .   ? 0.4276 0.3405 0.5334 -0.0609 -0.1563 0.1803  316 HOH   A O   
6843 O O   . HOH   D .   ? 0.8735 0.5236 0.6741 -0.0438 -0.0157 -0.0672 317 HOH   A O   
6844 O O   . HOH   D .   ? 0.4543 0.3700 0.4488 -0.1554 0.0423  0.0752  318 HOH   A O   
6845 O O   . HOH   D .   ? 0.2573 0.2415 0.3732 -0.0581 0.0144  -0.0034 319 HOH   A O   
6846 O O   B HOH   D .   ? 0.2901 0.2812 0.4628 -0.0198 -0.1560 0.1422  320 HOH   A O   
6847 O O   . HOH   D .   ? 0.2178 0.2792 0.4301 0.0231  -0.0863 -0.1209 321 HOH   A O   
6848 O O   . HOH   D .   ? 0.7162 0.6618 0.5460 -0.0939 0.1647  0.2796  322 HOH   A O   
6849 O O   . HOH   D .   ? 0.2922 0.2391 0.2786 0.0633  -0.0401 -0.0122 323 HOH   A O   
6850 O O   A HOH   D .   ? 0.4397 0.4246 0.4566 -0.0186 0.1555  0.0420  324 HOH   A O   
6851 O O   . HOH   D .   ? 0.2530 0.2730 0.3158 -0.0770 -0.0276 0.0776  325 HOH   A O   
6852 O O   . HOH   D .   ? 0.3832 0.4525 0.4671 -0.1697 -0.0298 -0.0303 326 HOH   A O   
6853 O O   . HOH   D .   ? 0.5214 0.5048 0.4572 0.0934  0.0478  -0.1338 327 HOH   A O   
6854 O O   . HOH   D .   ? 0.3652 0.5105 0.4293 -0.0965 0.0168  0.0240  328 HOH   A O   
6855 O O   . HOH   D .   ? 0.3454 0.3810 0.3007 -0.0914 0.0286  -0.0571 329 HOH   A O   
6856 O O   B HOH   D .   ? 0.2675 0.3135 0.3562 -0.0060 0.0334  0.0312  330 HOH   A O   
6857 O O   . HOH   D .   ? 0.2539 0.3034 0.3404 0.0478  -0.0378 -0.0073 331 HOH   A O   
6858 O O   B HOH   D .   ? 0.4809 0.4037 0.4285 -0.1613 -0.0320 0.0091  332 HOH   A O   
6859 O O   . HOH   D .   ? 0.3710 0.4825 0.2638 0.0213  0.0445  0.0086  333 HOH   A O   
6860 O O   . HOH   D .   ? 0.3495 0.4092 0.2994 -0.0638 -0.0434 -0.0678 334 HOH   A O   
6861 O O   A HOH   D .   ? 0.4287 0.4179 0.2395 -0.1687 0.0479  0.0517  335 HOH   A O   
6862 O O   A HOH   D .   ? 0.2945 0.3404 0.3227 0.1093  -0.0269 -0.0125 336 HOH   A O   
6863 O O   . HOH   D .   ? 0.3695 0.3848 0.4612 0.1110  0.0982  0.0820  337 HOH   A O   
6864 O O   . HOH   D .   ? 0.2722 0.4988 0.4230 0.0407  -0.0447 0.1424  338 HOH   A O   
6865 O O   . HOH   D .   ? 0.3296 0.2497 0.3206 0.0257  0.0092  0.0251  339 HOH   A O   
6866 O O   . HOH   D .   ? 0.4130 0.3259 0.3467 0.0229  -0.0450 -0.0359 340 HOH   A O   
6867 O O   . HOH   D .   ? 0.3148 0.2351 0.4446 -0.0031 -0.0386 -0.0494 341 HOH   A O   
6868 O O   . HOH   D .   ? 0.6072 0.6869 0.7837 -0.1452 -0.1170 0.2544  342 HOH   A O   
6869 O O   . HOH   D .   ? 0.2374 0.2274 0.4236 0.0064  0.0862  -0.0151 343 HOH   A O   
6870 O O   A HOH   D .   ? 0.3095 0.3876 0.4214 0.0167  0.0338  -0.0118 344 HOH   A O   
6871 O O   . HOH   D .   ? 0.6134 0.7620 0.4626 0.2777  0.0043  -0.0098 345 HOH   A O   
6872 O O   . HOH   D .   ? 0.2684 0.3583 0.4802 -0.0656 0.0367  -0.0520 346 HOH   A O   
6873 O O   . HOH   D .   ? 0.3775 0.7844 0.3712 0.1319  0.0520  -0.1308 347 HOH   A O   
6874 O O   . HOH   D .   ? 0.1911 0.2209 0.3200 0.0056  -0.0036 0.0298  348 HOH   A O   
6875 O O   . HOH   D .   ? 0.3047 0.3540 0.5291 -0.0220 -0.1545 -0.0519 349 HOH   A O   
6876 O O   . HOH   D .   ? 0.6926 0.8816 0.6298 -0.0766 0.0880  0.1109  350 HOH   A O   
6877 O O   . HOH   D .   ? 0.6467 0.3010 0.5129 -0.1819 0.2235  -0.0631 351 HOH   A O   
6878 O O   . HOH   D .   ? 0.2941 0.2520 0.2634 -0.0317 0.0395  -0.0038 352 HOH   A O   
6879 O O   . HOH   D .   ? 0.2918 0.4342 0.4009 0.1203  -0.0657 0.0047  353 HOH   A O   
6880 O O   A HOH   D .   ? 0.1424 0.2590 0.1602 0.0480  0.0301  0.0466  354 HOH   A O   
6881 O O   . HOH   D .   ? 0.2469 0.3665 0.3668 0.0470  0.0552  -0.0778 355 HOH   A O   
6882 O O   . HOH   D .   ? 0.1792 0.1603 0.1790 -0.0047 0.0009  0.0026  356 HOH   A O   
6883 O O   . HOH   D .   ? 0.1979 0.1609 0.2602 -0.0048 0.0051  0.0034  357 HOH   A O   
6884 O O   . HOH   D .   ? 0.1999 0.2656 0.2497 -0.0049 -0.0239 0.0525  358 HOH   A O   
6885 O O   . HOH   D .   ? 0.7548 0.4826 0.3700 0.0242  -0.0095 0.1620  359 HOH   A O   
6886 O O   . HOH   D .   ? 0.5156 0.6141 0.5037 0.2663  -0.0280 -0.1451 360 HOH   A O   
6887 O O   . HOH   D .   ? 0.4046 0.7025 0.6478 0.0129  -0.1829 0.1011  361 HOH   A O   
6888 O O   . HOH   D .   ? 0.2666 0.2714 0.2865 -0.0637 -0.0774 0.0567  362 HOH   A O   
6889 O O   A HOH   D .   ? 0.1879 0.3213 0.2545 0.0236  0.0490  0.0907  363 HOH   A O   
6890 O O   . HOH   D .   ? 0.3049 0.2690 0.3210 -0.0280 -0.0273 0.0048  364 HOH   A O   
6891 O O   . HOH   D .   ? 0.4289 0.2406 0.2948 0.1157  0.0509  0.0368  365 HOH   A O   
6892 O O   . HOH   D .   ? 0.2873 0.3048 0.3757 0.0559  -0.0965 -0.0750 366 HOH   A O   
6893 O O   . HOH   D .   ? 0.3135 0.3267 0.4668 -0.0348 0.1414  -0.0415 367 HOH   A O   
6894 O O   . HOH   D .   ? 0.3311 0.4630 0.5893 -0.0618 -0.1180 -0.1168 368 HOH   A O   
6895 O O   A HOH   D .   ? 0.2341 0.2341 0.2129 -0.0507 -0.0236 0.0489  369 HOH   A O   
6896 O O   . HOH   D .   ? 0.6061 0.2704 0.5579 0.0719  -0.0637 0.0072  370 HOH   A O   
6897 O O   . HOH   D .   ? 0.1778 0.1982 0.1855 -0.0057 -0.0031 -0.0023 371 HOH   A O   
6898 O O   . HOH   D .   ? 0.6718 0.4027 0.5089 0.1434  0.1675  0.0444  372 HOH   A O   
6899 O O   B HOH   D .   ? 0.4046 0.6845 0.3884 -0.1047 -0.0468 0.2333  373 HOH   A O   
6900 O O   . HOH   D .   ? 0.7691 0.3960 0.5819 -0.1384 -0.1523 0.1818  374 HOH   A O   
6901 O O   . HOH   D .   ? 0.4898 0.5095 0.5206 -0.0490 0.1666  -0.1280 375 HOH   A O   
6902 O O   . HOH   D .   ? 0.2962 0.5146 0.3794 0.0425  0.0926  0.2366  376 HOH   A O   
6903 O O   . HOH   D .   ? 0.2352 0.3038 0.3068 0.0296  0.0162  0.0935  377 HOH   A O   
6904 O O   . HOH   D .   ? 0.3791 0.6849 0.3577 -0.1174 0.0150  0.0815  378 HOH   A O   
6905 O O   . HOH   D .   ? 0.2594 0.2376 0.2630 -0.0553 -0.0105 0.0133  379 HOH   A O   
6906 O O   A HOH   D .   ? 0.2104 0.2182 0.2950 -0.0136 -0.0184 0.0525  380 HOH   A O   
6907 O O   . HOH   D .   ? 0.6849 0.4483 0.7819 0.0825  -0.1896 0.0642  381 HOH   A O   
6908 O O   . HOH   D .   ? 0.5523 0.3125 0.5993 -0.1194 0.0057  0.0027  382 HOH   A O   
6909 O O   . HOH   D .   ? 0.1966 0.2282 0.2332 0.0075  -0.0223 -0.0439 383 HOH   A O   
6910 O O   . HOH   D .   ? 0.2923 0.3560 0.3219 0.0165  0.0303  0.0196  384 HOH   A O   
6911 O O   . HOH   D .   ? 0.1880 0.1911 0.2403 0.0028  0.0093  0.0174  385 HOH   A O   
6912 O O   . HOH   D .   ? 0.5272 0.3589 0.5240 -0.1983 0.0765  0.0455  386 HOH   A O   
6913 O O   . HOH   D .   ? 0.3609 0.3152 0.2564 0.0695  0.0817  0.0077  387 HOH   A O   
6914 O O   . HOH   D .   ? 0.2947 0.2641 0.2279 -0.0726 -0.0010 0.0522  388 HOH   A O   
6915 O O   . HOH   D .   ? 0.4881 0.2978 0.3227 -0.0934 0.0188  -0.0012 389 HOH   A O   
6916 O O   . HOH   D .   ? 0.2949 0.5229 0.3206 -0.0476 0.0696  -0.0550 390 HOH   A O   
6917 O O   . HOH   D .   ? 0.3472 0.5079 0.3651 -0.2018 0.0817  -0.0335 391 HOH   A O   
6918 O O   A HOH   D .   ? 0.3856 0.1827 0.2298 0.0396  -0.0172 -0.0191 392 HOH   A O   
6919 O O   . HOH   D .   ? 0.2443 0.2196 0.3564 0.0087  0.0696  0.0713  393 HOH   A O   
6920 O O   . HOH   D .   ? 0.3378 0.2986 0.2686 -0.0980 -0.0708 0.0587  394 HOH   A O   
6921 O O   . HOH   D .   ? 0.2630 0.2209 0.2960 -0.0451 -0.0164 0.0502  395 HOH   A O   
6922 O O   . HOH   D .   ? 0.3158 0.2386 0.3588 -0.0220 -0.0558 0.0534  396 HOH   A O   
6923 O O   . HOH   D .   ? 0.5939 0.4274 0.2232 -0.0582 0.0574  0.0696  397 HOH   A O   
6924 O O   . HOH   D .   ? 0.2093 0.1816 0.1946 -0.0217 -0.0015 0.0075  398 HOH   A O   
6925 O O   B HOH   D .   ? 0.3024 0.1597 0.2983 -0.0288 -0.0071 0.0070  399 HOH   A O   
6926 O O   . HOH   D .   ? 0.5972 0.7589 0.5634 -0.1353 0.1186  -0.0136 400 HOH   A O   
6927 O O   B HOH   D .   ? 0.4896 0.3742 0.2773 0.0980  -0.0455 -0.0181 401 HOH   A O   
6928 O O   A HOH   D .   ? 0.2904 0.4989 0.3963 -0.1665 0.1316  -0.0638 402 HOH   A O   
6929 O O   . HOH   D .   ? 0.2409 0.3099 0.3960 -0.0213 -0.0132 0.0450  403 HOH   A O   
6930 O O   . HOH   D .   ? 0.6865 0.4780 0.6644 -0.1220 -0.1201 0.1216  404 HOH   A O   
6931 O O   . HOH   D .   ? 0.2724 0.3721 0.4540 -0.0351 -0.0215 -0.0721 405 HOH   A O   
6932 O O   . HOH   D .   ? 0.1955 0.2347 0.3314 -0.0020 -0.0251 0.0281  406 HOH   A O   
6933 O O   . HOH   D .   ? 0.5887 0.7789 0.4116 0.0622  0.2752  -0.0045 407 HOH   A O   
6934 O O   . HOH   D .   ? 0.3435 0.6795 0.2356 -0.0242 0.0835  0.0625  408 HOH   A O   
6935 O O   A HOH   D .   ? 0.5336 0.2572 0.4617 -0.1475 0.0262  -0.0234 409 HOH   A O   
6936 O O   A HOH   D .   ? 0.1605 0.3502 0.2847 -0.0506 0.0577  0.0137  410 HOH   A O   
6937 O O   A HOH   D .   ? 0.2687 0.3890 0.1978 0.0423  -0.0331 0.0028  411 HOH   A O   
6938 O O   . HOH   D .   ? 0.5255 0.6231 0.5585 0.1307  -0.1256 -0.1683 412 HOH   A O   
6939 O O   A HOH   D .   ? 0.4675 0.3157 0.2815 -0.1314 0.0386  0.0362  413 HOH   A O   
6940 O O   . HOH   D .   ? 0.2762 0.4251 0.8564 -0.0222 0.0316  0.0019  414 HOH   A O   
6941 O O   . HOH   D .   ? 0.6806 0.4204 0.3960 0.0465  -0.1433 -0.0488 415 HOH   A O   
6942 O O   . HOH   D .   ? 0.6245 0.4847 0.4986 0.0875  -0.1549 0.1363  416 HOH   A O   
6943 O O   . HOH   D .   ? 0.2404 0.3294 0.2985 -0.0439 -0.0617 0.0637  417 HOH   A O   
6944 O O   A HOH   D .   ? 0.2330 0.1940 0.2773 -0.0194 -0.0300 0.0523  418 HOH   A O   
6945 O O   . HOH   D .   ? 0.4211 0.3824 0.3331 -0.0266 -0.0253 0.1216  419 HOH   A O   
6946 O O   . HOH   D .   ? 0.5705 0.7769 0.6951 0.2249  0.1643  0.0394  420 HOH   A O   
6947 O O   . HOH   D .   ? 0.4756 0.2421 0.5930 -0.0890 -0.2796 0.0960  421 HOH   A O   
6948 O O   A HOH   D .   ? 0.4363 0.3176 0.4232 0.0776  0.1377  0.0695  422 HOH   A O   
6949 O O   . HOH   D .   ? 0.2511 0.1927 0.1915 -0.0004 0.0272  0.0289  423 HOH   A O   
6950 O O   . HOH   D .   ? 0.3583 0.1518 0.2348 0.0087  -0.0599 0.0121  424 HOH   A O   
6951 O O   . HOH   D .   ? 0.3012 0.4568 0.3086 0.1726  0.0008  0.0644  425 HOH   A O   
6952 O O   A HOH   D .   ? 0.2664 0.6096 0.4903 -0.0163 -0.0086 0.1416  426 HOH   A O   
6953 O O   A HOH   D .   ? 0.2141 0.2593 0.2925 0.0334  -0.0553 -0.0111 427 HOH   A O   
6954 O O   . HOH   D .   ? 0.2495 0.3500 0.3903 -0.0039 -0.0344 0.0475  428 HOH   A O   
6955 O O   . HOH   D .   ? 0.4627 0.7075 0.3857 -0.1252 -0.0807 0.1884  429 HOH   A O   
6956 O O   . HOH   D .   ? 0.3366 0.4530 0.6467 -0.0696 0.1692  -0.2222 430 HOH   A O   
6957 O O   . HOH   D .   ? 0.6861 0.6977 0.8491 -0.1557 0.1011  -0.1409 431 HOH   A O   
6958 O O   A HOH   D .   ? 0.1730 0.1576 0.1593 -0.0296 0.0006  -0.0148 432 HOH   A O   
6959 O O   . HOH   D .   ? 0.7035 0.4238 0.6839 0.2276  0.1804  -0.0618 433 HOH   A O   
6960 O O   A HOH   D .   ? 0.7950 0.7141 0.3791 0.2964  -0.1291 0.0800  434 HOH   A O   
6961 O O   . HOH   D .   ? 1.2109 1.3862 0.8931 0.0313  -0.1245 0.0563  435 HOH   A O   
6962 O O   . HOH   D .   ? 0.6377 0.5685 0.4274 -0.0766 -0.2136 0.0780  436 HOH   A O   
6963 O O   . HOH   D .   ? 0.2746 0.2343 0.3310 0.0038  -0.0022 0.0026  437 HOH   A O   
6964 O O   A HOH   D .   ? 0.2247 0.1542 0.1719 -0.0106 -0.0125 -0.0114 438 HOH   A O   
6965 O O   . HOH   D .   ? 0.4560 0.5377 0.2932 -0.0393 -0.0361 0.0341  439 HOH   A O   
6966 O O   A HOH   D .   ? 0.4521 0.5432 0.3639 -0.0040 0.0876  -0.0078 440 HOH   A O   
6967 O O   . HOH   D .   ? 0.4885 0.3444 0.2380 -0.1062 0.0099  0.0265  441 HOH   A O   
6968 O O   . HOH   D .   ? 0.8351 0.7318 0.7215 -0.1124 -0.0703 -0.0818 442 HOH   A O   
6969 O O   B HOH   D .   ? 0.6445 0.4362 0.4134 0.1913  -0.0024 -0.0609 443 HOH   A O   
6970 O O   . HOH   D .   ? 0.5410 0.8529 0.5913 -0.0155 -0.0959 0.3180  444 HOH   A O   
6971 O O   . HOH   D .   ? 0.2603 0.3172 0.2886 0.0180  -0.0512 -0.0271 445 HOH   A O   
6972 O O   A HOH   D .   ? 0.3108 0.3320 0.5054 -0.0777 0.1101  0.0344  446 HOH   A O   
6973 O O   B HOH   D .   ? 0.2944 0.2318 0.2932 -0.0219 0.0583  -0.0118 447 HOH   A O   
6974 O O   B HOH   D .   ? 0.2967 0.3149 0.3555 -0.1244 -0.0739 0.1707  448 HOH   A O   
6975 O O   . HOH   D .   ? 0.2919 0.2067 0.3358 0.0154  0.0061  0.0099  449 HOH   A O   
6976 O O   . HOH   D .   ? 0.5276 0.3982 0.3392 0.2571  -0.0802 -0.0426 450 HOH   A O   
6977 O O   . HOH   D .   ? 0.6893 0.7857 0.8860 -0.0042 -0.0452 0.2059  451 HOH   A O   
6978 O O   . HOH   D .   ? 0.2101 0.2887 0.4814 -0.0251 -0.0683 0.1148  452 HOH   A O   
6979 O O   . HOH   D .   ? 0.9605 0.7773 0.8485 0.0091  -0.1146 -0.0819 453 HOH   A O   
6980 O O   . HOH   D .   ? 0.5392 0.5843 0.6201 -0.1627 -0.0140 -0.1027 454 HOH   A O   
6981 O O   A HOH   D .   ? 0.3599 0.2356 0.2698 0.0542  0.0211  0.0427  455 HOH   A O   
6982 O O   . HOH   D .   ? 0.9118 0.7212 0.5892 -0.0717 0.2376  0.2757  456 HOH   A O   
6983 O O   B HOH   D .   ? 0.2711 0.2532 0.2840 -0.1210 -0.1140 0.0630  457 HOH   A O   
6984 O O   . HOH   D .   ? 0.5564 0.3512 0.4976 0.0309  0.0326  0.1264  458 HOH   A O   
6985 O O   . HOH   D .   ? 0.3814 0.4557 0.6041 0.0986  0.0104  0.2589  459 HOH   A O   
6986 O O   . HOH   D .   ? 0.4865 0.5793 0.6366 0.1795  0.0772  0.2123  460 HOH   A O   
6987 O O   . HOH   D .   ? 0.5191 0.4574 0.5660 0.0007  -0.0334 0.1682  461 HOH   A O   
6988 O O   . HOH   D .   ? 0.7907 0.8741 0.5063 0.0293  -0.0872 -0.0572 462 HOH   A O   
6989 O O   . HOH   D .   ? 0.3923 0.3683 0.5324 -0.1011 0.0910  -0.1656 463 HOH   A O   
6990 O O   . HOH   D .   ? 0.3291 0.5244 0.6300 -0.1349 0.0088  -0.1758 464 HOH   A O   
6991 O O   . HOH   D .   ? 0.4887 0.5051 0.6342 0.0165  0.0142  0.1187  465 HOH   A O   
6992 O O   . HOH   D .   ? 0.3950 0.5609 0.4415 0.0985  -0.0108 -0.2001 466 HOH   A O   
6993 O O   . HOH   D .   ? 0.3450 0.3873 0.4325 -0.1302 0.0611  -0.0276 467 HOH   A O   
6994 O O   B HOH   D .   ? 0.2492 0.3505 0.3469 -0.0251 -0.0071 0.1215  468 HOH   A O   
6995 O O   A HOH   D .   ? 0.4075 0.4904 0.3376 -0.0571 0.0166  0.0437  469 HOH   A O   
6996 O O   . HOH   D .   ? 0.6328 0.6254 0.5465 -0.0467 0.0958  0.0314  470 HOH   A O   
6997 O O   B HOH   D .   ? 0.3700 0.3687 0.4872 0.1011  -0.0275 -0.0445 471 HOH   A O   
6998 O O   . HOH   D .   ? 0.4821 0.6698 0.3813 -0.1561 -0.1528 0.2090  472 HOH   A O   
6999 O O   . HOH   D .   ? 0.6827 0.3364 0.7578 -0.1697 -0.1680 0.1658  473 HOH   A O   
7000 O O   A HOH   D .   ? 0.2909 0.3264 0.4609 0.0914  -0.1212 -0.0420 474 HOH   A O   
7001 O O   . HOH   D .   ? 0.5257 0.5205 0.5411 0.1337  0.1738  0.1000  475 HOH   A O   
7002 O O   . HOH   D .   ? 0.4083 0.4785 0.7152 -0.1483 0.1268  -0.1152 476 HOH   A O   
7003 O O   . HOH   D .   ? 0.3403 0.3749 0.2774 0.0780  -0.0107 -0.0394 477 HOH   A O   
7004 O O   . HOH   D .   ? 0.6006 0.5500 0.3846 -0.0084 -0.0621 -0.0552 478 HOH   A O   
7005 O O   . HOH   D .   ? 0.3246 0.2339 0.3312 0.0354  -0.0816 -0.0328 479 HOH   A O   
7006 O O   . HOH   D .   ? 0.4902 0.5748 0.3948 -0.0093 -0.0386 -0.0102 480 HOH   A O   
7007 O O   . HOH   D .   ? 0.5718 0.5154 0.4282 -0.0765 0.1118  0.0271  481 HOH   A O   
7008 O O   . HOH   D .   ? 0.6076 0.5827 0.6580 -0.0246 -0.0659 -0.0522 482 HOH   A O   
7009 O O   . HOH   D .   ? 1.0312 0.9220 0.6709 -0.0650 0.1264  0.1678  483 HOH   A O   
7010 O O   . HOH   D .   ? 0.5030 0.4979 0.6505 -0.2608 0.0177  -0.0726 484 HOH   A O   
7011 O O   . HOH   D .   ? 0.6352 0.3922 0.4253 -0.1014 -0.1200 0.0460  485 HOH   A O   
7012 O O   . HOH   D .   ? 0.7293 0.6926 0.7390 -0.0959 0.1136  0.0083  486 HOH   A O   
7013 O O   . HOH   D .   ? 0.6416 0.7016 0.6992 0.0027  0.2065  -0.1084 487 HOH   A O   
7014 O O   . HOH   D .   ? 0.6184 0.4404 0.5466 0.0106  0.0480  -0.0984 488 HOH   A O   
7015 O O   . HOH   D .   ? 0.9216 0.4260 0.3507 -0.0383 -0.1405 0.0333  489 HOH   A O   
7016 O O   . HOH   D .   ? 0.6439 0.4190 0.4915 -0.2194 -0.0651 0.1623  490 HOH   A O   
7017 O O   . HOH   D .   ? 0.7552 0.6999 0.5661 -0.0928 0.0796  0.0796  491 HOH   A O   
7018 O O   . HOH   D .   ? 0.3293 0.2686 0.8443 -0.0179 -0.2133 0.0610  492 HOH   A O   
7019 O O   . HOH   D .   ? 0.4803 0.3205 0.5950 -0.1059 0.0578  0.0330  493 HOH   A O   
7020 O O   . HOH   D .   ? 0.3183 0.5871 0.4101 0.0866  0.1053  0.2664  494 HOH   A O   
7021 O O   . HOH   D .   ? 0.3322 0.3608 0.5236 -0.0564 0.1282  0.0486  495 HOH   A O   
7022 O O   . HOH   D .   ? 0.4996 0.6308 0.4515 -0.0097 -0.0552 -0.0446 496 HOH   A O   
7023 O O   . HOH   D .   ? 0.3454 0.3059 0.6796 -0.0201 0.0145  0.1839  497 HOH   A O   
7024 O O   . HOH   D .   ? 0.3757 0.5667 0.3742 0.0139  0.0002  -0.1090 498 HOH   A O   
7025 O O   . HOH   D .   ? 0.3539 0.5222 0.6842 -0.1470 0.0874  -0.0867 499 HOH   A O   
7026 O O   . HOH   D .   ? 0.6169 0.5583 0.7063 0.0834  -0.1098 0.0528  500 HOH   A O   
7027 O O   . HOH   D .   ? 0.4311 0.3137 0.3099 -0.0653 0.1004  -0.0348 501 HOH   A O   
7028 O O   . HOH   D .   ? 0.5418 0.4029 0.5339 -0.0436 0.2407  0.0776  502 HOH   A O   
7029 O O   B HOH   D .   ? 0.3711 0.3646 0.2467 0.0711  -0.0528 0.0814  503 HOH   A O   
7030 O O   . HOH   D .   ? 0.7634 0.5043 0.5963 -0.1061 -0.1051 -0.0234 504 HOH   A O   
7031 O O   . HOH   D .   ? 0.8101 0.8624 0.6211 0.1852  -0.1419 0.1000  505 HOH   A O   
7032 O O   . HOH   D .   ? 0.3050 0.4120 0.3876 0.0641  -0.0835 0.0678  506 HOH   A O   
7033 O O   . HOH   D .   ? 0.4287 0.8888 0.5989 -0.1337 -0.0262 0.2867  507 HOH   A O   
7034 O O   . HOH   D .   ? 0.7942 0.2589 0.4712 -0.0523 0.0420  0.0241  508 HOH   A O   
7035 O O   . HOH   D .   ? 0.3167 0.4637 0.4702 0.0446  -0.0592 -0.0257 509 HOH   A O   
7036 O O   . HOH   D .   ? 0.8432 0.5779 0.7616 0.2587  -0.1093 -0.0650 510 HOH   A O   
7037 O O   . HOH   D .   ? 0.5537 0.3214 0.5203 -0.1607 0.0100  0.0134  511 HOH   A O   
7038 O O   B HOH   D .   ? 0.3495 0.3019 0.3296 0.0563  -0.1269 0.0726  512 HOH   A O   
7039 O O   . HOH   D .   ? 0.6895 0.8369 0.5717 0.1125  0.0535  0.2115  513 HOH   A O   
7040 O O   . HOH   D .   ? 0.5688 0.7727 0.4487 -0.0573 -0.0299 -0.1734 514 HOH   A O   
7041 O O   . HOH   D .   ? 0.3090 0.3295 0.5371 -0.0172 -0.0045 0.1016  515 HOH   A O   
7042 O O   . HOH   D .   ? 0.7205 0.8169 0.5331 0.4080  0.0197  0.1054  516 HOH   A O   
7043 O O   B HOH   D .   ? 0.7198 0.4487 0.3220 -0.0206 0.0948  0.0736  517 HOH   A O   
7044 O O   B HOH   D .   ? 0.6772 0.4743 0.4553 0.3130  -0.0319 0.0103  518 HOH   A O   
7045 O O   A HOH   D .   ? 0.3111 0.5570 0.2869 0.1255  0.0708  0.0086  519 HOH   A O   
7046 O O   . HOH   D .   ? 0.3678 0.7591 0.6086 0.0966  0.0939  -0.1113 520 HOH   A O   
7047 O O   B HOH   D .   ? 0.5774 0.3810 0.4772 0.0961  0.1619  0.1574  521 HOH   A O   
7048 O O   . HOH   D .   ? 0.5056 0.7725 0.5654 -0.0821 -0.0127 0.0898  522 HOH   A O   
7049 O O   . HOH   D .   ? 0.6501 0.6261 0.4475 0.1894  -0.0830 0.1761  523 HOH   A O   
7050 O O   . HOH   D .   ? 0.2930 0.5956 0.6639 0.0176  -0.0074 0.3320  524 HOH   A O   
7051 O O   . HOH   E .   ? 0.2684 0.3003 0.3462 -0.0133 0.0619  0.0558  201 HOH   B O   
7052 O O   . HOH   E .   ? 0.3464 0.4408 0.5439 -0.0390 0.0063  -0.1433 202 HOH   B O   
7053 O O   . HOH   E .   ? 0.7626 0.5830 0.7960 0.2565  0.0136  0.0579  203 HOH   B O   
7054 O O   . HOH   E .   ? 0.5234 0.6957 0.4233 0.3088  -0.1283 -0.0091 204 HOH   B O   
7055 O O   . HOH   E .   ? 0.5565 0.4117 0.7290 -0.0207 -0.1584 0.2782  205 HOH   B O   
7056 O O   . HOH   E .   ? 0.5015 0.3287 0.4941 -0.0298 0.0227  -0.1633 206 HOH   B O   
7057 O O   . HOH   E .   ? 0.2313 0.3179 0.3822 0.0044  0.0024  -0.0162 207 HOH   B O   
7058 O O   . HOH   E .   ? 0.3952 0.6981 0.4552 0.0194  -0.0196 0.3170  208 HOH   B O   
7059 O O   . HOH   E .   ? 0.4466 0.5146 0.3970 0.2121  0.0237  0.0944  209 HOH   B O   
7060 O O   . HOH   E .   ? 0.4517 0.5662 0.2678 0.0751  -0.0685 -0.1033 210 HOH   B O   
7061 O O   . HOH   E .   ? 0.2574 0.2516 0.4982 -0.0273 -0.0212 -0.0886 211 HOH   B O   
7062 O O   . HOH   E .   ? 0.3015 0.2960 0.7964 0.0569  -0.0814 0.0852  212 HOH   B O   
7063 O O   . HOH   E .   ? 0.7178 0.3301 0.4105 -0.2125 0.0208  -0.0003 213 HOH   B O   
7064 O O   . HOH   E .   ? 0.6961 0.3441 0.5430 0.0969  0.0629  0.0104  214 HOH   B O   
7065 O O   . HOH   E .   ? 0.5003 0.4953 0.4194 -0.0231 -0.1133 0.1098  215 HOH   B O   
7066 O O   . HOH   E .   ? 0.4042 0.6248 0.4081 0.1260  -0.0459 0.0069  216 HOH   B O   
7067 O O   . HOH   E .   ? 0.1745 0.2485 0.3494 -0.0092 -0.0038 0.0342  217 HOH   B O   
7068 O O   . HOH   E .   ? 0.2523 0.6174 0.5662 -0.0419 0.1014  -0.2491 218 HOH   B O   
7069 O O   . HOH   E .   ? 0.7173 0.6590 0.3873 0.0770  0.0815  0.0111  219 HOH   B O   
7070 O O   . HOH   E .   ? 0.5913 0.2435 0.3470 -0.0050 -0.0843 0.0345  220 HOH   B O   
7071 O O   . HOH   E .   ? 0.2576 0.2560 0.3704 -0.0511 0.0246  -0.0575 221 HOH   B O   
7072 O O   . HOH   E .   ? 0.3794 0.5325 0.6180 0.1883  0.0682  -0.0615 222 HOH   B O   
7073 O O   . HOH   E .   ? 0.1973 0.1790 0.2415 -0.0251 -0.0296 -0.0058 223 HOH   B O   
7074 O O   . HOH   E .   ? 0.4186 0.3932 0.3666 0.0270  -0.0645 -0.0842 224 HOH   B O   
7075 O O   . HOH   E .   ? 0.3259 0.2935 0.9023 -0.0473 0.1065  -0.0186 225 HOH   B O   
7076 O O   . HOH   E .   ? 0.5918 0.4330 0.4346 -0.0343 0.1375  -0.1681 226 HOH   B O   
7077 O O   . HOH   E .   ? 0.2180 0.2596 0.4049 -0.0201 -0.0398 0.0173  227 HOH   B O   
7078 O O   . HOH   E .   ? 0.3679 0.3447 0.7709 -0.0345 0.0265  -0.0160 228 HOH   B O   
7079 O O   . HOH   E .   ? 0.2764 0.1530 0.4238 0.0038  -0.0964 0.0085  229 HOH   B O   
7080 O O   . HOH   E .   ? 0.3062 0.4029 0.4071 -0.0375 -0.1163 -0.0402 230 HOH   B O   
7081 O O   . HOH   E .   ? 0.3182 0.5285 0.7439 0.0347  0.0762  -0.0614 231 HOH   B O   
7082 O O   . HOH   E .   ? 0.1929 0.1646 0.1775 -0.0208 -0.0240 -0.0011 232 HOH   B O   
7083 O O   . HOH   E .   ? 0.2578 0.4191 0.2555 -0.0553 -0.0355 0.0531  233 HOH   B O   
7084 O O   . HOH   E .   ? 0.3753 0.3707 0.2799 0.0395  0.0686  0.0301  234 HOH   B O   
7085 O O   . HOH   E .   ? 0.3883 0.3939 0.5063 0.1340  -0.0731 0.0233  235 HOH   B O   
7086 O O   . HOH   E .   ? 0.3975 0.2512 0.4640 -0.0082 0.1474  -0.0045 236 HOH   B O   
7087 O O   . HOH   E .   ? 0.3528 0.2622 0.6453 0.0426  0.2111  0.1474  237 HOH   B O   
7088 O O   . HOH   E .   ? 0.5762 0.4441 0.8173 -0.1196 -0.1959 -0.0836 238 HOH   B O   
7089 O O   . HOH   E .   ? 0.3276 0.4134 0.3641 -0.0669 0.0128  -0.0767 239 HOH   B O   
7090 O O   . HOH   E .   ? 0.4172 0.2129 0.2830 0.0272  -0.1072 -0.0264 240 HOH   B O   
7091 O O   . HOH   E .   ? 0.6150 0.2931 0.3199 -0.0059 -0.0152 -0.0245 241 HOH   B O   
7092 O O   . HOH   E .   ? 0.2080 0.1900 0.3582 -0.0275 -0.0181 0.0083  242 HOH   B O   
7093 O O   . HOH   E .   ? 0.3372 0.2768 0.3017 0.0908  0.0530  0.0073  243 HOH   B O   
7094 O O   . HOH   E .   ? 0.1867 0.1803 0.2995 -0.0025 -0.0162 -0.0125 244 HOH   B O   
7095 O O   . HOH   E .   ? 0.2646 0.2282 0.3195 -0.0178 0.0757  -0.0076 245 HOH   B O   
7096 O O   . HOH   E .   ? 0.3590 0.2136 0.6382 -0.0270 -0.1343 -0.0092 246 HOH   B O   
7097 O O   . HOH   E .   ? 0.2968 0.2831 0.3658 0.0281  0.0018  -0.0793 247 HOH   B O   
7098 O O   . HOH   E .   ? 0.3058 0.2627 0.2503 0.0048  -0.0560 -0.0040 248 HOH   B O   
7099 O O   . HOH   E .   ? 0.2902 0.2338 0.2405 -0.0547 -0.0539 0.0186  249 HOH   B O   
7100 O O   . HOH   E .   ? 0.2579 0.1928 0.2491 -0.0375 -0.0639 0.0292  250 HOH   B O   
7101 O O   . HOH   E .   ? 0.2813 0.3690 0.6530 0.1085  -0.0831 -0.0871 251 HOH   B O   
7102 O O   . HOH   E .   ? 0.5853 0.4780 0.3423 0.2711  0.0648  0.1029  252 HOH   B O   
7103 O O   . HOH   E .   ? 0.1768 0.1646 0.2067 -0.0133 -0.0259 0.0039  253 HOH   B O   
7104 O O   . HOH   E .   ? 0.5781 0.3111 0.4678 -0.1450 -0.0032 -0.0854 254 HOH   B O   
7105 O O   . HOH   E .   ? 0.3210 0.2880 0.4023 -0.0463 0.0299  -0.0867 255 HOH   B O   
7106 O O   . HOH   E .   ? 0.1774 0.2311 0.2181 -0.0329 -0.0103 0.0194  256 HOH   B O   
7107 O O   . HOH   E .   ? 0.3975 0.4067 0.5197 0.0639  -0.0828 -0.2301 257 HOH   B O   
7108 O O   . HOH   E .   ? 0.4453 0.3886 0.3019 0.0204  0.0611  0.0358  258 HOH   B O   
7109 O O   . HOH   E .   ? 0.3876 0.2909 0.4901 0.0681  -0.0669 -0.0748 259 HOH   B O   
7110 O O   . HOH   E .   ? 0.3041 0.4201 0.3658 -0.1035 -0.0357 0.0047  260 HOH   B O   
7111 O O   . HOH   E .   ? 0.2609 0.2559 0.3007 0.0596  -0.0866 -0.0704 261 HOH   B O   
7112 O O   . HOH   E .   ? 0.2701 0.4024 0.2601 -0.0758 0.0179  0.0381  262 HOH   B O   
7113 O O   . HOH   E .   ? 0.2876 0.2731 0.2630 0.0015  -0.0294 -0.0152 263 HOH   B O   
7114 O O   . HOH   E .   ? 0.2575 0.2230 0.3997 -0.0039 -0.0333 -0.0309 264 HOH   B O   
7115 O O   . HOH   E .   ? 0.2400 0.2060 0.1931 -0.0507 -0.0633 0.0084  265 HOH   B O   
7116 O O   . HOH   E .   ? 0.3837 0.2778 0.6337 0.0157  -0.0488 -0.0635 266 HOH   B O   
7117 O O   . HOH   E .   ? 0.5615 0.3315 0.4547 -0.2199 -0.0413 0.0322  267 HOH   B O   
7118 O O   . HOH   E .   ? 0.2807 0.8663 0.3217 0.0917  -0.0665 -0.1029 268 HOH   B O   
7119 O O   . HOH   E .   ? 0.3211 0.3522 0.2492 0.1166  -0.0467 -0.0597 269 HOH   B O   
7120 O O   . HOH   E .   ? 0.2127 0.1825 0.4299 -0.0102 -0.0439 -0.0434 270 HOH   B O   
7121 O O   . HOH   E .   ? 0.4739 0.3131 0.4921 -0.0374 -0.0862 -0.0405 271 HOH   B O   
7122 O O   . HOH   E .   ? 0.3366 0.3577 0.4466 -0.0159 0.0890  0.0243  272 HOH   B O   
7123 O O   . HOH   E .   ? 0.8136 0.6657 0.5982 0.2719  -0.0168 -0.1838 273 HOH   B O   
7124 O O   . HOH   E .   ? 0.2087 0.2440 0.3306 0.0074  -0.0048 0.0185  274 HOH   B O   
7125 O O   . HOH   E .   ? 0.5797 0.3028 0.3712 0.0344  0.0083  0.1216  275 HOH   B O   
7126 O O   . HOH   E .   ? 0.2857 0.2337 0.3462 -0.0515 -0.0267 -0.0154 276 HOH   B O   
7127 O O   . HOH   E .   ? 0.2827 0.2630 0.3499 -0.0268 0.0099  -0.0537 277 HOH   B O   
7128 O O   . HOH   E .   ? 0.4609 0.3128 0.2712 0.0380  -0.1073 -0.0287 278 HOH   B O   
7129 O O   . HOH   E .   ? 0.3158 0.3087 0.3057 -0.0589 -0.1058 0.0252  279 HOH   B O   
7130 O O   . HOH   E .   ? 0.5196 0.5685 0.2688 0.1082  -0.0759 -0.0220 280 HOH   B O   
7131 O O   . HOH   E .   ? 0.7089 0.8200 0.6997 0.3996  -0.0990 -0.0599 281 HOH   B O   
7132 O O   . HOH   E .   ? 0.3254 0.3492 0.6654 -0.0383 -0.0876 0.1449  282 HOH   B O   
7133 O O   . HOH   E .   ? 0.3146 0.3243 0.5207 0.0358  0.0574  0.1078  283 HOH   B O   
7134 O O   . HOH   E .   ? 0.3045 0.2763 0.2590 -0.0731 -0.0589 -0.0372 284 HOH   B O   
7135 O O   . HOH   E .   ? 0.2367 0.5592 0.5066 -0.0174 -0.0225 -0.1616 285 HOH   B O   
7136 O O   . HOH   E .   ? 0.4210 0.4997 0.6020 -0.1978 -0.0017 0.1717  286 HOH   B O   
7137 O O   . HOH   E .   ? 0.3025 0.2981 0.3306 0.0398  -0.0928 0.0012  287 HOH   B O   
7138 O O   . HOH   E .   ? 0.2246 0.2001 0.2640 -0.0323 -0.0338 0.0237  288 HOH   B O   
7139 O O   . HOH   E .   ? 0.5307 0.3871 0.5347 -0.1335 -0.0053 0.1449  289 HOH   B O   
7140 O O   . HOH   E .   ? 0.3861 0.4000 0.4175 0.1158  -0.0238 -0.0587 290 HOH   B O   
7141 O O   . HOH   E .   ? 0.5479 0.6291 0.3226 0.0299  -0.0953 0.1324  291 HOH   B O   
7142 O O   . HOH   E .   ? 0.4424 0.5283 0.2370 -0.0093 0.0400  0.0503  292 HOH   B O   
7143 O O   . HOH   E .   ? 0.2047 0.2266 0.2049 -0.0206 -0.0320 0.0143  293 HOH   B O   
7144 O O   . HOH   E .   ? 0.5598 0.3846 0.6518 0.0504  -0.1148 -0.1659 294 HOH   B O   
7145 O O   . HOH   E .   ? 0.3804 0.9799 0.8538 0.2561  -0.0466 -0.1337 295 HOH   B O   
7146 O O   . HOH   E .   ? 0.2017 0.1839 0.2317 -0.0068 -0.0203 -0.0034 296 HOH   B O   
7147 O O   . HOH   E .   ? 0.3059 0.5078 0.5309 -0.0610 -0.1129 0.0678  297 HOH   B O   
7148 O O   . HOH   E .   ? 0.3553 0.5345 0.3625 -0.0648 -0.1317 0.1093  298 HOH   B O   
7149 O O   . HOH   E .   ? 0.2021 0.1861 0.3950 -0.0250 -0.0152 -0.0111 299 HOH   B O   
7150 O O   . HOH   E .   ? 0.2923 0.5246 0.4821 -0.0778 -0.0325 0.0830  300 HOH   B O   
7151 O O   . HOH   E .   ? 0.4817 0.2340 0.4774 -0.1039 -0.2665 0.1000  301 HOH   B O   
7152 O O   . HOH   E .   ? 0.3579 0.2881 0.3170 -0.0397 0.0193  -0.1163 302 HOH   B O   
7153 O O   . HOH   E .   ? 0.1848 0.1700 0.3358 0.0081  0.0000  -0.0135 303 HOH   B O   
7154 O O   . HOH   E .   ? 0.2066 0.3794 0.6090 0.0337  -0.0301 -0.1423 304 HOH   B O   
7155 O O   . HOH   E .   ? 0.2349 0.3126 0.6455 0.0680  -0.0066 -0.0389 305 HOH   B O   
7156 O O   . HOH   E .   ? 0.4174 0.2093 0.5502 0.0844  0.2001  0.0715  306 HOH   B O   
7157 O O   . HOH   E .   ? 0.7087 0.6470 0.5571 -0.1145 -0.0427 0.1622  307 HOH   B O   
7158 O O   . HOH   E .   ? 0.5521 0.5050 0.2967 0.2160  -0.0997 0.0298  308 HOH   B O   
7159 O O   . HOH   E .   ? 0.3968 0.7301 0.3674 0.2208  0.0105  0.0770  309 HOH   B O   
7160 O O   . HOH   E .   ? 0.2632 0.3411 0.5955 -0.0299 -0.0412 0.0071  310 HOH   B O   
7161 O O   . HOH   E .   ? 0.3229 0.3851 0.5248 -0.0595 -0.1733 0.1402  311 HOH   B O   
7162 O O   . HOH   E .   ? 0.3541 0.3964 0.7561 -0.0073 -0.0741 0.1672  312 HOH   B O   
7163 O O   . HOH   E .   ? 0.2238 0.2056 0.3615 0.0270  -0.0862 0.0217  313 HOH   B O   
7164 O O   . HOH   E .   ? 0.2018 0.2073 0.3038 0.0037  -0.0188 0.0238  314 HOH   B O   
7165 O O   . HOH   E .   ? 0.6145 0.5444 0.7283 0.0474  -0.1410 0.2390  315 HOH   B O   
7166 O O   . HOH   E .   ? 0.2516 0.2213 0.2514 -0.0103 0.0075  0.0240  316 HOH   B O   
7167 O O   . HOH   E .   ? 0.4822 0.5938 0.5176 0.0174  -0.1748 -0.0136 317 HOH   B O   
7168 O O   . HOH   E .   ? 0.3200 0.2694 0.2534 0.0249  -0.0252 0.0107  318 HOH   B O   
7169 O O   . HOH   E .   ? 0.2810 0.1717 0.2830 -0.0003 -0.0187 0.0288  319 HOH   B O   
7170 O O   . HOH   E .   ? 0.1939 0.2121 0.3405 -0.0294 -0.0281 0.0235  320 HOH   B O   
7171 O O   . HOH   E .   ? 0.6797 0.4851 0.5846 0.1011  0.0821  -0.1220 321 HOH   B O   
7172 O O   . HOH   E .   ? 0.7565 0.3303 0.3758 -0.0089 -0.0872 -0.0381 322 HOH   B O   
7173 O O   . HOH   E .   ? 0.3701 0.3973 0.4114 -0.1103 0.1240  -0.0418 323 HOH   B O   
7174 O O   . HOH   E .   ? 0.4472 0.2256 0.3574 0.1331  0.0718  0.0577  324 HOH   B O   
7175 O O   . HOH   E .   ? 0.3140 0.3001 0.4066 -0.0332 0.0932  -0.0855 325 HOH   B O   
7176 O O   . HOH   E .   ? 0.2624 0.2133 0.2920 -0.0427 -0.0208 -0.0055 326 HOH   B O   
7177 O O   . HOH   E .   ? 0.5519 0.5561 0.3096 0.0493  -0.0993 -0.1183 327 HOH   B O   
7178 O O   . HOH   E .   ? 0.4808 0.3526 0.6336 0.0768  0.2224  0.2203  328 HOH   B O   
7179 O O   . HOH   E .   ? 0.5535 0.3643 0.3178 -0.1852 0.1253  -0.0264 329 HOH   B O   
7180 O O   . HOH   E .   ? 0.1997 0.2017 0.3206 -0.0168 -0.0383 0.0030  330 HOH   B O   
7181 O O   . HOH   E .   ? 0.7166 0.4116 0.4016 0.0006  0.1230  0.1665  331 HOH   B O   
7182 O O   . HOH   E .   ? 0.2253 0.3073 0.2976 -0.0398 -0.0472 0.0825  332 HOH   B O   
7183 O O   . HOH   E .   ? 0.4872 0.4461 0.6647 0.0574  -0.0590 0.0370  333 HOH   B O   
7184 O O   . HOH   E .   ? 0.2424 0.2103 0.3314 0.0325  0.0391  -0.0004 334 HOH   B O   
7185 O O   . HOH   E .   ? 0.2083 0.3022 0.3811 0.0206  -0.0151 -0.0860 335 HOH   B O   
7186 O O   . HOH   E .   ? 0.3063 0.2558 0.6799 -0.0414 -0.0660 0.0780  336 HOH   B O   
7187 O O   . HOH   E .   ? 0.5405 0.5664 0.3511 -0.0938 -0.0486 0.0102  337 HOH   B O   
7188 O O   . HOH   E .   ? 0.2646 0.2665 0.6107 -0.0666 -0.0338 0.1391  338 HOH   B O   
7189 O O   . HOH   E .   ? 0.4868 0.6915 0.4908 -0.0769 -0.0843 0.2394  339 HOH   B O   
7190 O O   . HOH   E .   ? 0.2045 0.1702 0.3075 0.0008  -0.0307 0.0178  340 HOH   B O   
7191 O O   . HOH   E .   ? 0.4912 0.3432 0.4371 0.0434  -0.1446 -0.0821 341 HOH   B O   
7192 O O   . HOH   E .   ? 0.3079 0.7838 0.6872 -0.1286 -0.1694 0.1081  342 HOH   B O   
7193 O O   . HOH   E .   ? 0.4057 0.6069 0.4695 -0.0709 -0.1140 -0.0807 343 HOH   B O   
7194 O O   . HOH   E .   ? 0.5376 0.4035 0.4788 0.0271  0.0244  -0.1651 344 HOH   B O   
7195 O O   . HOH   E .   ? 0.2610 0.2215 0.3116 -0.0027 0.0366  -0.0018 345 HOH   B O   
7196 O O   . HOH   E .   ? 0.2575 0.6195 0.4531 0.1257  -0.0556 -0.1114 346 HOH   B O   
7197 O O   . HOH   E .   ? 0.4196 0.4716 0.5439 0.0028  -0.1517 0.0127  347 HOH   B O   
7198 O O   . HOH   E .   ? 0.8091 0.6943 0.3068 0.0319  -0.0503 0.1851  348 HOH   B O   
7199 O O   . HOH   E .   ? 0.5041 0.6905 0.5756 -0.0723 -0.0530 0.2419  349 HOH   B O   
7200 O O   . HOH   E .   ? 0.3175 0.2773 0.5961 -0.0284 -0.0965 -0.1090 350 HOH   B O   
7201 O O   . HOH   E .   ? 0.5571 0.6705 0.7897 0.0405  -0.0294 -0.1235 351 HOH   B O   
7202 O O   . HOH   E .   ? 0.3462 0.2502 0.4457 0.0350  -0.1278 -0.0679 352 HOH   B O   
7203 O O   . HOH   E .   ? 0.5246 0.4452 0.4556 0.0741  0.1412  -0.1111 353 HOH   B O   
7204 O O   . HOH   E .   ? 0.4924 0.2339 0.3903 -0.0804 0.0266  -0.0901 354 HOH   B O   
7205 O O   . HOH   E .   ? 0.2915 0.3709 0.6602 -0.0214 -0.0171 0.0400  355 HOH   B O   
7206 O O   . HOH   E .   ? 0.5480 0.5110 0.6398 -0.1344 0.0372  0.1786  356 HOH   B O   
7207 O O   . HOH   E .   ? 0.3853 0.3023 0.4814 -0.0663 -0.0391 -0.0367 357 HOH   B O   
7208 O O   . HOH   E .   ? 0.5979 0.5941 0.5510 0.2253  -0.1374 0.1665  358 HOH   B O   
7209 O O   . HOH   E .   ? 0.4284 0.4413 0.5630 -0.1567 0.0393  -0.0347 359 HOH   B O   
7210 O O   . HOH   E .   ? 0.5411 0.6245 0.6240 0.0040  -0.0499 -0.0274 360 HOH   B O   
7211 O O   . HOH   E .   ? 0.4901 0.3388 0.5553 -0.0092 -0.2188 0.0321  361 HOH   B O   
7212 O O   . HOH   E .   ? 0.2542 0.4348 0.7529 -0.0635 -0.1264 0.0146  362 HOH   B O   
7213 O O   . HOH   E .   ? 0.4971 0.4599 0.6471 -0.0020 0.1276  0.1238  363 HOH   B O   
7214 O O   . HOH   E .   ? 0.4812 0.7095 0.4302 0.2073  0.0082  0.0865  364 HOH   B O   
7215 O O   . HOH   E .   ? 0.5914 0.6962 0.5348 -0.0402 -0.0481 -0.1571 365 HOH   B O   
7216 O O   . HOH   E .   ? 0.5845 0.3581 0.5467 -0.1600 -0.1141 0.0360  366 HOH   B O   
7217 O O   . HOH   E .   ? 0.6605 0.2642 0.3467 0.0018  -0.0048 0.0316  367 HOH   B O   
7218 O O   . HOH   E .   ? 0.6977 0.5051 0.5244 0.1379  0.0376  0.1170  368 HOH   B O   
7219 O O   . HOH   E .   ? 0.8594 0.8030 0.5365 0.2805  -0.1181 0.0588  369 HOH   B O   
7220 O O   . HOH   E .   ? 0.5750 0.5792 0.6732 0.3121  0.1933  0.1264  370 HOH   B O   
7221 O O   . HOH   E .   ? 0.5359 0.5764 0.5666 -0.1008 -0.0525 0.0263  371 HOH   B O   
7222 O O   . HOH   E .   ? 0.6545 0.3780 0.3040 -0.1545 -0.0738 -0.0372 372 HOH   B O   
7223 O O   . HOH   E .   ? 0.5846 0.6230 0.4561 0.0715  -0.1666 0.1189  373 HOH   B O   
7224 O O   . HOH   E .   ? 0.3738 0.3482 0.6615 -0.0149 -0.1370 -0.0603 374 HOH   B O   
7225 O O   . HOH   E .   ? 0.3946 0.4802 0.3713 0.0658  -0.0884 -0.0773 375 HOH   B O   
7226 O O   . HOH   E .   ? 0.6802 0.8891 0.5401 -0.1820 0.0775  -0.1373 376 HOH   B O   
7227 O O   . HOH   E .   ? 0.7994 0.4914 0.5716 -0.0208 -0.0846 0.0356  377 HOH   B O   
7228 O O   . HOH   E .   ? 0.3027 0.5399 0.4300 -0.0118 -0.0275 -0.0170 378 HOH   B O   
7229 O O   . HOH   E .   ? 0.3575 0.4015 0.3231 0.0310  -0.0101 -0.0175 379 HOH   B O   
7230 O O   . HOH   E .   ? 0.6173 0.7773 0.6948 0.0013  0.2015  0.2171  380 HOH   B O   
7231 O O   . HOH   E .   ? 0.3339 0.2966 0.3358 0.0112  0.0490  0.0348  381 HOH   B O   
7232 O O   . HOH   E .   ? 0.4319 0.5120 0.6377 0.1492  -0.0125 0.0541  382 HOH   B O   
7233 O O   . HOH   E .   ? 0.5131 0.7223 0.7326 0.1144  0.1339  0.3421  383 HOH   B O   
7234 O O   . HOH   E .   ? 0.3121 0.7113 0.6112 0.1157  0.0440  0.2597  384 HOH   B O   
7235 O O   . HOH   E .   ? 0.5323 0.4482 0.4232 -0.0352 -0.0390 0.0247  385 HOH   B O   
7236 O O   . HOH   E .   ? 0.8124 0.7531 0.6050 0.3180  0.0672  0.0275  386 HOH   B O   
7237 O O   . HOH   E .   ? 0.7283 0.3586 0.5160 0.0205  0.0067  -0.0831 387 HOH   B O   
7238 O O   . HOH   E .   ? 0.5366 0.5112 0.6047 0.0363  0.0582  0.0296  388 HOH   B O   
7239 O O   . HOH   E .   ? 0.2968 0.3963 0.4695 -0.0271 -0.1162 -0.0291 389 HOH   B O   
7240 O O   . HOH   E .   ? 0.3826 0.2809 0.3972 0.0933  -0.0244 -0.0211 390 HOH   B O   
7241 O O   . HOH   E .   ? 0.5361 0.4135 0.4983 -0.0138 0.0663  0.0579  391 HOH   B O   
7242 O O   . HOH   E .   ? 0.2820 0.3071 0.8265 -0.0546 -0.1466 0.1395  392 HOH   B O   
7243 O O   . HOH   E .   ? 0.4170 0.2522 0.6144 0.0280  0.0906  0.0989  393 HOH   B O   
7244 O O   . HOH   E .   ? 0.3571 0.6727 0.5261 0.0813  -0.0680 -0.1398 394 HOH   B O   
7245 O O   . HOH   E .   ? 0.4519 0.5152 0.5167 -0.0677 0.0568  0.1186  395 HOH   B O   
7246 O O   . HOH   E .   ? 0.3704 0.3350 0.4398 -0.0004 0.0389  -0.0063 396 HOH   B O   
7247 O O   . HOH   E .   ? 0.2605 0.2799 0.6408 -0.0346 -0.1276 0.0203  397 HOH   B O   
7248 O O   . HOH   E .   ? 0.7523 0.8295 0.9395 0.1787  -0.1353 0.3776  398 HOH   B O   
7249 O O   . HOH   E .   ? 0.6139 0.4427 0.4304 -0.2599 -0.0423 0.1467  399 HOH   B O   
7250 O O   . HOH   E .   ? 0.6577 0.7400 0.4016 0.2589  0.0735  0.0752  400 HOH   B O   
# 
